LOCUS       WP_391985730             240 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Streptomyces flaveolus].
ACCESSION   WP_391985730
VERSION     WP_391985730.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 240)
  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 240)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         1..240
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25031
     Region          3..231
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 mirvaavgdi hmgldsqgll rpafetlpdc adllllagdl trhgtpeear vvarevrglp
       61 vpvvavlgnh dhhdeqpekv tailqdagvt vlegeatvve cagnrvgiag tkgfgggfvg
      121 rsagefgepv mkefvrttrr sadslhaalk glddrgcavr valthfspva dtlageppei
      181 hpflgsylla eaidtagadl avhghahlgt ehgmtsggvr vrnvaqpvir rafnvyqlga
//
LOCUS       WP_391986277             432 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces flaveolus].
ACCESSION   WP_391986277
VERSION     WP_391986277.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         1..432
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=48731
     Region          67..331
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 msdqkvknif vlgldeanlp tlqavpgada lrfhplltve elqggevslp ditekaqqvl
       61 dafdgsidai vgywdfpvst lvpilgeryg trttslesvv kcehkywsrl eqqkvtdchp
      121 rfgrvdlead pprppgdlrf pmwlkpalsy sselafgvkd eeqfrravde irkgisrvgr
      181 pfervldrid vppemdgvgg rvclaeeslt giqvavegyv hegevtvygt ldsidypdsp
      241 cflrhqypsm lppqvitrlh dvtervmrri gfdsatfsve yfydpgsqei nlleinprhs
      301 qshaelfqyv dgvpnhhpml alalgddprm phrqgpyama akwyyrwftd gvvrnvpspe
      361 diarieretp gvrihvlpee gqrlsdlsqq dsysyevahi ftggddeedm rrkydhcvaa
      421 lglafdephd gq
//
LOCUS       WP_391986574             321 aa            linear   BCT 20-JAN-2025
DEFINITION  quinone oxidoreductase family protein [Streptomyces flaveolus].
ACCESSION   WP_391986574
VERSION     WP_391986574.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 321)
  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 321)
  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 321)
  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   4  (residues 1 to 321)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         1..321
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=32964
     Region          5..301
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 meyamlaarl htwnavpdla etapvgppgd gevtveveaa avthldltvm tgtfahrpal
       61 pftpgtagvg tvveggaall grrvlvrggg iglerdgtwa ervavpagav reiprdadaa
      121 laatcyspmt tawaaveavg riaegervlv tgaagavgsl cvqlaaraga hvvavvrned
      181 aagavpdaah evlvrpvaee vagkggadvl ldtvggdtvp afleamrpgg rvvligyvag
      241 ttlrvelpal mardvtllpm nmvrrhvpae vfdrllrdlt egrltlrtta lpfariaeav
      301 etrrggggrg tlavlmgdpr r
//
LOCUS       WP_391987142             421 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            flaveolus].
ACCESSION   WP_391987142
VERSION     WP_391987142.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 421)
  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 421)
  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 421)
  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 11448557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         1..421
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45465
     Region          <10..72
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
ORIGIN      
        1 mqgneslnsa mqesgltqae ladkvnahlt caghegtvsd rtvrnwltgk trwphprqre
       61 aleavfscta gelgfsppar rrrtsnpaed pvrrrnflta asgttaavav pfvgappqvg
      121 tsdvlrlrsg ldalmalddt rggheglera altgaaeale kqklgatqri rlrlfsvaad
      181 ytataawsal darqsdraya llgkalylag maqdpvvklr vwnsyamlah qrgehtqavd
      241 saqaaqatsi tkrdpffasl ahtrtaighs nlgdrqaair slghaqealg kaepdqprps
      301 wmafygpael tamtaivrdr tgdaaeaeaa shkalgsipk qfrrnralat arlalaqlhq
      361 rdidqacata ssvfelmkgs plpgrmrsll gdyyrdlitl apdaavarew gdryraewrr
      421 a
//
LOCUS       WP_391987501             414 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces californicus].
ACCESSION   WP_391987501
VERSION     WP_391987501.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 414)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..414
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43524
     Region          74..255
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          261..388
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mngqpisgas agasgkrrgg tglsalmlga llmlvtacgg sadagdkkdp argtkkgdtt
       61 asqavvtiap kdgadavats galkigaeqg klttvkvadp kgnevegeia adgaswtper
      121 hlaaatkytv havakdsegr esakdttftt lvpantfigq ytpedgstvg vgmpvsinft
      181 rgitdpdave raikvtaepa veieghwfgn drldfrpeky wasgtkvtve lnldgvegrp
      241 gvygkqtktv kftigrsqvs tvdasakrmk vvrdgkqikd ipisagapat ttyngqmvis
      301 eklkvtrmng dtvgfggeyd ikdvphamrl stsgtflhgn ywgassifgn tntshgcvgl
      361 rdvrggydnq tpaawfydks ligdvvivkn shdkviqpdn glngwnmdwa ewkk
//
LOCUS       WP_391987559             516 aa            linear   BCT 20-JAN-2025
DEFINITION  sodium:solute symporter family protein [Streptomyces californicus].
ACCESSION   WP_391987559
VERSION     WP_391987559.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Henriquez,T., Wirtz,L., Su,D. and Jung,H.
  TITLE     Prokaryotic Solute/Sodium Symporters: Versatile Functions and
            Mechanisms of a Transporter Family
  JOURNAL   Int J Mol Sci 22 (4), 1880 (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Wright,E.M. and Turk,E.
  TITLE     The sodium/glucose cotransport family SLC5
  JOURNAL   Pflugers Arch 447 (5), 510-518 (2004)
   PUBMED   12748858
  REMARK    Erratum:[Pflugers Arch. 2004 Feb;447(5):813-5]
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Jung,H.
  TITLE     The sodium/substrate symporter family: structural and functional
            features
  JOURNAL   FEBS Lett 529 (1), 73-77 (2002)
   PUBMED   12354616
REFERENCE   4  (residues 1 to 516)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001756
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..516
                     /product="sodium:solute symporter family protein"
                     /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=53906
     Region          37..450
                     /region_name="PutP"
                     /note="Na+/proline symporter [Amino acid transport and
                     metabolism]; COG0591"
                     /db_xref="CDD:440356"
ORIGIN      
        1 mnaavatsvf gvfmvatval gllalrgrgg gggglaewsv ggrslgpvfi wvlmagegyt
       61 sfsylgaagw gynygapvly vvaymscgya igyvvgpmlw syarrhglvg itdmvahrfg
      121 rpwlgavvav latvfllpyi qlqitgmgvv lstisygtvs lnwayflafa vttgfvvvsg
      181 lrgsawvsvl kdvlviatlg flalyvplhy fdgygafldr lvtekadwlt fpghggggsg
      241 gsglgelwfi sttflnaltv vifpttvagy lgarnadalr rnamylpayn vllfvpmllg
      301 laalfvvpgl agaesnlalf klvvdslpaw avgvigvaaa lssivpmavf mlvigtmwgr
      361 svlsllprfa erqktaaqvv vvvagslall ltytapntlv rlslisyegm aqllpmvlla
      421 lvwrrltfrg afsglvvgva vvcalvfsgn dpvggvnagl valaanlava lavtfaggrd
      481 adprpdaevl ahdptdedee kevllpadpg psdhrv
//
LOCUS       WP_391987695             275 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            californicus].
ACCESSION   WP_391987695
VERSION     WP_391987695.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (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
REFERENCE   4  (residues 1 to 275)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..275
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30502
     Region          15..68
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          89..263
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mvnrkrldsd dpdrdfgvql rlardargwt qdelasrmgc sgthisavet grrsptprfs
       61 rsadralgtg dkfsrmvqam kepalldgfp eyvkyearav elrlyevgii pgllqtpeya
      121 rvladsavrr gsitpdqaee rvaflakrqa alvrpnppml fvtmdescir rpvggsavmn
      181 aqldrliefa elpntvlqva pyeigerrtf dlpvniltlp drsvvcyaes qtqghldres
      241 sfvlpiltey hqlqgaslsq tasvvkicel rkgtp
//
LOCUS       WP_391987782             462 aa            linear   BCT 20-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Streptomyces californicus].
ACCESSION   WP_391987782
VERSION     WP_391987782.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            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 10481000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..462
                     /product="FAD-binding oxidoreductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47821
     Region          19..152
                     /region_name="FAD_binding_4"
                     /note="FAD binding domain; pfam01565"
                     /db_xref="CDD:426326"
     Region          <426..460
                     /region_name="ALO"
                     /note="D-arabinono-1,4-lactone oxidase; cl21623"
                     /db_xref="CDD:451334"
ORIGIN      
        1 msvdtvsltg wgrtspttav rfrprtyeea aavvrgrgpr gvvarglgrs pgdaaqnagg
       61 svldltglar igavdpaagv vrcdagvsle rllrvllpqg llppvvpgtg rltvggaias
      121 dlpgpdhrrs gsfarhvsal elltadgevr tvlpgtalfd atagglgltg vilgatlrlr
      181 rvgsalmsvs teragdldel larftaggdr mpyasawidl margrstgrg iltrgehapp
      241 parpahagrt rllsragagr grssapgpls glfealpplp gallgpgpaa lynaaryrva
      301 prarageprp ssaffhgpda fpephalygr gglvryrftv gygqeetlhr vvrriaarrs
      361 pavravlhrf gaagpgllsf aapgwclald lpaalpglgr fldgvdeeva aaggrvclaa
      421 dsrtrpetaa amypglaefr elrarldpag afrsdlsrrl gl
//
LOCUS       WP_391987948             135 aa            linear   BCT 20-JAN-2025
DEFINITION  TOBE domain-containing protein [Streptomyces californicus].
ACCESSION   WP_391987948
VERSION     WP_391987948.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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 10007583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..135
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13787
     Region          1..128
                     /region_name="MopI"
                     /note="Molybdopterin-binding protein MopI [Coenzyme
                     transport and metabolism]; COG3585"
                     /db_xref="CDD:442804"
ORIGIN      
        1 mptysigqaa ellavspetv rrwadagdlv mvrsgsgsrl idgvslagfa sargrglhpv
       61 pgdvltsvrn sfagivtavr adgvmaqvei qsgphrlvsl issdsveelg ldvgvpatar
      121 vkstnvhidr saggr
//
LOCUS       WP_391988329             295 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            californicus].
ACCESSION   WP_391988329
VERSION     WP_391988329.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 295)
  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 295)
  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 295)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..295
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33200
     Region          38..90
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          112..290
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mthgtdgtgt igqgtskgsg argraasepe sqyslkvfge vvkafrkrar ltqeefaplv
       61 rysvetiasi eqgrrfppld fveraeavld afgvieaaak hltrkrglas wfqqwaqlel
      121 salslhtyec rmipgllqsp nymrasfanr lppltdeqie vrlaarqerq qllrsrpnta
      181 fsfileehlf lrnlggdevt relidhilel selrnvtvqi mevarqhhag ldgpmqllet
      241 pkhqwlgyle gqehgelitd ptvismfqmr casmrsqart aedtrslmqr mrgat
//
LOCUS       WP_391988917             234 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Streptomyces californicus].
ACCESSION   WP_391988917
VERSION     WP_391988917.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 234)
  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 10007985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..234
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24648
     Region          34..224
                     /region_name="COG3786"
                     /note="L,D-peptidoglycan transpeptidase YkuD,
                     ErfK/YbiS/YcfS/YnhG family [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443000"
ORIGIN      
        1 mrrplvtaav llalagslga apatgvpplp erladtgggs qlitaealda asttgtvtww
       61 errggrwaqa gsaparfgen glaegatreq gtsttptgly dlpyafgved apagttypyr
      121 kvtddswwcq dnasaaynrw veprpdhcra deaehlvsyg tqyaralvig fnyerpvrhr
      181 gagiflhvng rgatagcvsv padamaqila waepgrrphi avgtssgpta itry
//
LOCUS       WP_391989008             429 aa            linear   BCT 20-JAN-2025
DEFINITION  M20 metallopeptidase family protein [Streptomyces californicus].
ACCESSION   WP_391989008
VERSION     WP_391989008.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Lindner,H.A., Lunin,V.V., Alary,A., Hecker,R., Cygler,M. and
            Menard,R.
  TITLE     Essential roles of zinc ligation and enzyme dimerization for
            catalysis in the aminoacylase-1/M20 family
  JOURNAL   J Biol Chem 278 (45), 44496-44504 (2003)
   PUBMED   12933810
REFERENCE   2  (residues 1 to 429)
  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 11444961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..429
                     /product="M20 metallopeptidase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45579
     Region          9..421
                     /region_name="AbgB"
                     /note="Metal-dependent
                     amidase/aminoacylase/carboxypeptidase [General function
                     prediction only]; COG1473"
                     /db_xref="CDD:441082"
ORIGIN      
        1 msgdpihaef deraeaveqq viewrhhlhr npelsnrevd taklvtdhlt slnldevrtg
       61 isghgvvgvl rggkpgdrvv alradidalp vkedsgesfa stvvdqdypg gpfpvahacg
      121 hdghtamllg aatvlagvre qlpgtvlfvf qpaeegapag essgakqmid egachdpept
      181 mafgmhlgpl ptgyvgyrvg nqfgassmik ivltgqqvhg stpwmgidpm paagaitvgv
      241 gqlyrqvsaf dpitvtighv edvgrfnivp gtvtlwgtir csveedmadi qkrlttlaqq
      301 taaaynctae vdylqdvpav hnrkewtdav lpairdviga ekvfetpatl gyddvsefvn
      361 kyggvylmlg aqdgelnddg avvptsggrg lvpnhnprfy vdddalvqgv rlhcqvaygh
      421 ltgtiapak
//
LOCUS       WP_391989083             320 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Streptomyces californicus].
ACCESSION   WP_391989083
VERSION     WP_391989083.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..320
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=33340
     Region          14..318
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mtlrdpapat plarparlrp gsrvavvaps gpvpadrlee gvailrdwgl dpvvaphvls
       61 ahpeldhlag adedraadlr aawcdpsvea vfcarggyga hrmvdlldwa airaagpkvf
      121 vgysditvlh eafalragfa tlhgpmvate tflkdeptre hlratlfepd tvltlgldta
      181 rtlvpgraeg vlyggcvsll aadagtpggr tharggllai edtgeepyrl dgiltrllrs
      241 galtgvagva cgswqlcgpy ekirpvladr lgalgipvve elgfghgpts ltiplgvpav
      301 ldapadggrc tltvrtpalr
//
LOCUS       WP_391989246             504 aa            linear   BCT 20-JAN-2025
DEFINITION  type I restriction-modification system subunit M [Streptomyces
            californicus].
ACCESSION   WP_391989246
VERSION     WP_391989246.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 504)
  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   2  (residues 1 to 504)
  AUTHORS   Youell,J. and Firman,K.
  TITLE     Mechanistic insight into Type I restriction endonucleases
  JOURNAL   Front Biosci (Landmark Ed) 17 (6), 2122-2139 (2012)
   PUBMED   22652768
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Sistla,S. and Rao,D.N.
  TITLE     S-Adenosyl-L-methionine-dependent restriction enzymes
  JOURNAL   Crit Rev Biochem Mol Biol 39 (1), 1-19 (2004)
   PUBMED   15121719
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Murray,N.E.
  TITLE     Type I restriction systems: sophisticated molecular machines (a
            legacy of Bertani and Weigle)
  JOURNAL   Microbiol Mol Biol Rev 64 (2), 412-434 (2000)
   PUBMED   10839821
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114514
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..504
                     /product="type I restriction-modification system subunit
                     M"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=55368
     Region          8..135
                     /region_name="HsdM_N"
                     /note="HsdM N-terminal domain; pfam12161"
                     /db_xref="CDD:463478"
     Region          148..396
                     /region_name="HsdM"
                     /note="Type I restriction-modification system, DNA
                     methylase subunit [Defense mechanisms]; COG0286"
                     /db_xref="CDD:440055"
ORIGIN      
        1 mtitqhelea rlwdaanalr gpvdpadfkt yvfpmlfwkw isdtwvhehd aafneygddl
       61 ddeieadfhr felpegtlws evtekvtnlg aeiakafqri emanprslag vfgdaswgnk
      121 eripesallg liqafnkirl dpstvshdll gagyeyllkn fadesgkkag efftprevvn
      181 llvgilqpep gesvydpscg sggmlvatin qlresgkdhr tlraygqein lttasiarmn
      241 lflheiedfd ikrgdtlrap afkapsgavr qfdtvianpp fslanwgadr wssdpraicg
      301 vppakngdya fvqhmvssmt pgfgrvgvvm phgvlfrggt eanirqglie kdlleavvgl
      361 ppnlfystsi pacllifrdq kpverkehvl fidgsarfvk gkkqnrmsed dvraltdayq
      421 tgnapgsegg anvrlvpfge ieqngfdlni gryikvaaee tadlgaalva yadarqhrmn
      481 teaamferla aagvdlsmfg vpse
//
LOCUS       WP_391990016             289 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Streptomyces
            californicus].
ACCESSION   WP_391990016
VERSION     WP_391990016.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 289)
  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 289)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..289
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29746
     Region          2..289
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mpiaatgdli aeadarqrav aafnvitleh aeavaegaea agspvilqis enavayhrgr
       61 paplaraaae vaaqaavpvs lhldhvqste llhraadcgf ssamfdaarl pyaenlaatr
      121 aavvwaherg iwleaelgqv ggkngeppld ahapgartdp eearsfvaat gvdalavavg
      181 tshamtsrda vidhallsgl reavpvplvl hgssgasdee lsravaggir kvnigtalni
      241 amtgairerl ardersvdpr ryladgrdam aatvtrmisl lpsgcahaa
//
LOCUS       WP_391990239             553 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein, partial [Streptomyces
            californicus].
ACCESSION   WP_391990239
VERSION     WP_391990239.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 553)
  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 553)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..>553
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          273..450
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 mvrvpfraaa drvrrrlgrt arpssrsrta artpaaapgd laaagrgpgr hpylralgml
       61 vvvvlgawlg llavgsirtp vgpmdttmtl rpsltggski nvsplgalel dshiaplrld
      121 vdvdrldper sqalvdqper fsnlqdevtr dvaagtrela vrscvavvsg aaalglvvyr
      181 rprralaagg laltllaasg vsayatwnpk svlepkfsgl lssapslvgd arsivtefdi
      241 yqrelarlvt nvtklydats tlpvyqpdpg tirvlhvsdi hlnpaawhii aslveqyeid
      301 vivdsgdtmd hgsaaengfl dpirdlgapy vwvrgnhdsr vtqeylekfr nvrvlddgaa
      361 vnvgglriag tgdasftpdr tgpgsnkeaa rlegmrlata lrdqeragtp adiavahdpn
      421 taretdgtvp lvlsghyhrr ineqlklgtr lkvegstggg glravqnekp ekvhasvlym
      481 drstrrlqaw deitlgglgl ttaevsrhlp eenlkkdapg sptpgpaapp pggppppppp
      541 rraggppppp pnt
//
LOCUS       WP_391990379             297 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptomyces bobili].
ACCESSION   WP_391990379
VERSION     WP_391990379.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bobili
  ORGANISM  Streptomyces bobili
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 297)
  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 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   3  (residues 1 to 297)
  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   4  (residues 1 to 297)
  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 297)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Streptomyces bobili"
                     /db_xref="taxon:67280"
     Protein         1..297
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31945
     Region          21..174
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          203..283
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mhleelrtll arharpdwtt aidgvlisrv drpdppapsm sgtvlaviaq gakrlalgdr
       61 vyaygagqyl vasvdlpvtg qftqaapdqp algfgltlep savaelllqa gpgdtprpag
      121 gtpsgiavsd appalldavv rllrlldepn dravlaplvk reilwrlitg eqgatvrhlg
      181 ladsglshva ravrwirehy aepfrvedva rlagmsvsaf yrnfqavtam spiqfqkqir
      241 lqearlllat hpgdvtgvgh rvgydnpsqf sreyrrqfga ppsrdaarlr stegvlp
//
LOCUS       WP_391990984             209 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces bobili].
ACCESSION   WP_391990984
VERSION     WP_391990984.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bobili
  ORGANISM  Streptomyces bobili
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Streptomyces bobili"
                     /db_xref="taxon:67280"
     Protein         1..209
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22515
     Region          2..209
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 mnsrerilgr vrraladvqg edapierayl rvhgdpsiee ttdllaenla dyraivhrct
       61 adelaatlag mlaargsqtv lvppgldpsw ladadvdqvp drpestpyel dridsvvtac
      121 alaiaetgti vldgspdqgr rritlvpdhh icvvrvpqqv vssvpqamer ldparpltwi
      181 sgpsatsdie ldrvegvhgp rtlevilvg
//
LOCUS       WP_391991079             283 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces bobili].
ACCESSION   WP_391991079
VERSION     WP_391991079.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bobili
  ORGANISM  Streptomyces bobili
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 283)
  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 283)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Streptomyces bobili"
                     /db_xref="taxon:67280"
     Protein         1..283
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31642
     Region          24..77
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          100..278
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mtdssdvtac eyerepdpsd slrtfgavvq alrehvglsr vefaalvqfs khtvesvelg
       61 rrmpdesfve raeealgntg alrkaarflt rgeaglaawf rrwarlekva vslctyecrl
      121 vpgllqsegy mralceqdip plsdddlett vrarmgrqll lrerpnttfd fiveeavfmr
      181 rlggvdvtrd lidhvleaig prnvtlqimp ansehhacma gpiqlletpe gswrgysegq
      241 engrliadpk qvsrlhmrya rlrsqalppk dsvgllqrir gal
//
LOCUS       WP_391991187             229 aa            linear   BCT 20-JAN-2025
DEFINITION  4'-phosphopantetheinyl transferase family protein [Streptomyces
            bobili].
ACCESSION   WP_391991187
VERSION     WP_391991187.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bobili
  ORGANISM  Streptomyces bobili
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459479
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Streptomyces bobili"
                     /db_xref="taxon:67280"
     Protein         1..229
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=24415
     Region          29..226
                     /region_name="EntD"
                     /note="4'-phosphopantetheinyl transferase EntD
                     (siderophore biosynthesis) [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2977"
                     /db_xref="CDD:442216"
ORIGIN      
        1 mieellpatv iaveahgedg vrefgdgply pqeealvara vakrrreftl vrscarrame
       61 klgvppqavl pgergaptwp aglagsmthc dgyaaaalvr agdlaslgid aephqplpdg
      121 vlsaialpae rerlrrlaad rpdvhwdrll fsakesvyka wfpltrkwld fseadieidd
      181 gpagaaqgtl rarllvpgpv vdgcrlghfe ggwtvgrglv ataitvphg
//
LOCUS       WP_391991294             307 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Streptomyces bobili].
ACCESSION   WP_391991294
VERSION     WP_391991294.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bobili
  ORGANISM  Streptomyces bobili
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces bobili"
                     /db_xref="taxon:67280"
     Protein         1..307
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32094
     Region          4..305
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mkgllrpsrl apgarvavva psgpvveerl qagldllrgw dldpfaaphv ldrhgelgyl
       61 agtdaeraad lqrawcdprv davicarggy gaqrvvdlld wdamraagpk vflgfsdstt
      121 lheafavrlg lvtlygpvaa gidfvknara qehlratlfa petvrtltsd gtalapgrar
      181 gvtlggclal latgygtpht rpgargglll ledvgerpyt vdraltqllr tgwldgvagi
      241 algswaqcgp yeelrpvlad rlgglgvpvv eelgfghcdg altvpfgvta eldadagtlt
      301 ldapalr
//
LOCUS       WP_391991551             296 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces bobili].
ACCESSION   WP_391991551
VERSION     WP_391991551.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bobili
  ORGANISM  Streptomyces bobili
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 296)
  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 296)
  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 296)
  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 10611723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces bobili"
                     /db_xref="taxon:67280"
     Protein         1..296
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30532
     Region          14..74
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Region          196..279
                     /region_name="DUF2690"
                     /note="Protein of unknown function (DUF2690); pfam10901"
                     /db_xref="CDD:402475"
ORIGIN      
        1 mprwkdlpdg ldprvgefvt rlrrtvdgdg sslaaladgt gygrtswery lngrllapkg
       61 avialaevtg tdpaplitlw elaerawsrs elrhdnatea vhlsrartvt apapapapap
      121 ealaadpppg pgrrptrrpt mflagalgvv tvavgafflt dggpaernrt aaapptpsat
      181 pprslppgvl cagadctgkd peetgcsdgd vttaasitvg ttlvevrhsd tcaaawgriv
      241 ravqgdtvqv tvgqvrqsgg vttvgdtiay tpmvavkepg emracvelas gergct
//
LOCUS       WP_391991861             414 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces bobili].
ACCESSION   WP_391991861
VERSION     WP_391991861.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bobili
  ORGANISM  Streptomyces bobili
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 414)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Streptomyces bobili"
                     /db_xref="taxon:67280"
     Protein         1..414
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43498
     Region          75..256
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          262..388
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mnvrpisgas vdgrsrgrdk rlalivggll lavtacgggg nsgsektkdd kgagataaas
       61 gqseavvsia pkdgakavdt sgalkvtaak gkltevvvkd adgtkvdgti aadgtgwtps
      121 thlaaatkyq vhavakdaeg rtaaedasft tltpentfvg tftpedgskv gvgmpfsvrf
      181 trgitapddv ekaikittvp avdvqghwfg ndrldfrpek ywkagtkvtv elnldgvegr
      241 kgvygkqskk vsftigrdqv sivdakkrtm qvtqegkvvk tipvttgkpg yatwngqmvi
      301 sekftvtrmn gdtvgydgey dikdvphamr ltdsgtfvhg nywggdafgn ynashgcigl
      361 rdvrggydsg vpaawffdhs mvgdvvvvkn stdptveasn glngwnipwa ewtk
//
LOCUS       WP_391991935             238 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces bobili].
ACCESSION   WP_391991935
VERSION     WP_391991935.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bobili
  ORGANISM  Streptomyces bobili
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616714
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Streptomyces bobili"
                     /db_xref="taxon:67280"
     Protein         1..238
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24594
     Region          7..238
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 mtraetfral hrgrlpddpl vlpgpwdaas araladagfp alaipsagva aslgyadget
       61 paeemfaava riaravdvpv sadvedgygl ppkelverll eagavgcnle dsdesglkda
      121 hahadrlaev rsaaagrlfl naridtflrg esdpartier aalyvdagad cvypigapva
      181 vlpllrsgtr vpvnvfarig egpspaelge lgatrvtfgp gvqrrataav teiaallr
//
LOCUS       WP_391991940             357 aa            linear   BCT 20-JAN-2025
DEFINITION  BMP family lipoprotein [Streptomyces bobili].
ACCESSION   WP_391991940
VERSION     WP_391991940.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bobili
  ORGANISM  Streptomyces bobili
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Yousief,S.W., Bahey-El-Din,M. and Zaghloul,T.I.
  TITLE     Immunization with the basic membrane protein (BMP) family ABC
            transporter elicits protection against Enterococcus faecium in a
            murine infection model
  JOURNAL   Microbes Infect 22 (3), 127-136 (2020)
   PUBMED   31585177
REFERENCE   2  (residues 1 to 357)
  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   3  (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   4  (residues 1 to 357)
  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   5  (residues 1 to 357)
  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 11448319
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Streptomyces bobili"
                     /db_xref="taxon:67280"
     Protein         1..357
                     /product="BMP family lipoprotein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /calculated_mol_wt=36680
     Region          50..354
                     /region_name="Med"
                     /note="Lipoprotein Med, regulator of KinD/Spo0A, PBP1-ABC
                     superfamily, includes NupN [Signal transduction
                     mechanisms]; COG1744"
                     /db_xref="CDD:441350"
ORIGIN      
        1 msrrtgfvra aasvavvala aagcgessts skpsekesgk esatysgkgi glaydiggkg
       61 dqsfndaaya gfekadkefg iggrdvepqd gesdadkvqr ltqlaqsgyn pvigvgyiya
      121 pavkevaakf pdttfgiidd eqvvaknvad mvfseeqasy lagvaaakas kkahigfigg
      181 vdiplihkfe agyvqgaksv npaikiesqy ltetpqeggf sspdkgkaga sgqieagadv
      241 iyhaaglsgq gviseaagkk vwaigvdsdq ysqtslaayk dyilgsalkn vggavydlak
      301 svyegkplsg vvrgslsndg vgfadtnpky kamtdvvaav dkakkdivdg kitvntk
//
LOCUS       WP_391992269             291 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces bobili].
ACCESSION   WP_391992269
VERSION     WP_391992269.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bobili
  ORGANISM  Streptomyces bobili
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415139
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Streptomyces bobili"
                     /db_xref="taxon:67280"
     Protein         1..291
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=31593
     Region          1..260
                     /region_name="LysX"
                     /note="Glutathione synthase, LysX or RimK-type ligase,
                     ATP-grasp superfamily [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism,
                     Translation, ribosomal structure and biogenesis, Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0189"
                     /db_xref="CDD:439959"
ORIGIN      
        1 mprialvtyd pgpepskdrd lpvllralee agagaeavcw ddadvdwasy dlalirstwd
       61 yswraaefta waercakatr lanpaavvrw ntdkrylgel aaagipvvpt rylgpgepad
      121 lpddheyvvk ptsgagarya arytpdqhdt avrhlarmhe egltamvqpy vrgidtgger
      181 alqffggsll hasrkravla sgtafdadkv ahpglepwlp taaeldvaer alaavpdape
      241 llyarvdlvd gddgrprvme lelvepnlfl flhpesvprv vevilaaava r
//
LOCUS       WP_391992453             470 aa            linear   BCT 20-JAN-2025
DEFINITION  alpha,alpha-trehalose-phosphate synthase (UDP-forming)
            [Streptomyces bobili].
ACCESSION   WP_391992453
VERSION     WP_391992453.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bobili
  ORGANISM  Streptomyces bobili
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 470)
  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 470)
  AUTHORS   Eastmond,P.J. and Graham,I.A.
  TITLE     Trehalose metabolism: a regulatory role for trehalose-6-phosphate?
  JOURNAL   Curr Opin Plant Biol 6 (3), 231-235 (2003)
   PUBMED   12753972
REFERENCE   3  (residues 1 to 470)
  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   4  (residues 1 to 470)
  AUTHORS   Elbein,A.D., Pan,Y.T., Pastuszak,I. and Carroll,D.
  TITLE     New insights on trehalose: a multifunctional molecule
  JOURNAL   Glycobiology 13 (4), 17R-27R (2003)
   PUBMED   12626396
REFERENCE   5  (residues 1 to 470)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 929-939 (1997)
   PUBMED   9334165
  REMARK    Erratum:[Biochem J 1998 Feb 1;329(Pt 3):719]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Streptomyces bobili"
                     /db_xref="taxon:67280"
     Protein         1..470
                     /product="alpha,alpha-trehalose-phosphate synthase
                     (UDP-forming)"
                     /EC_number="2.4.1.15"
                     /GO_function="GO:0003825 - alpha,alpha-trehalose-phosphate
                     synthase (UDP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0005992 - trehalose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51743
     Region          11..470
                     /region_name="OtsA"
                     /note="Trehalose-6-phosphate synthase, GT20 family
                     [Carbohydrate transport and metabolism]; COG0380"
                     /db_xref="CDD:440149"
ORIGIN      
        1 mastrgaaae gaqvlvasnr gpvsyqvred gslharrggg glvsglsaig pdagalwvcs
       61 altdgdreav rrgvgedgvr mlavpadvha dayngiansv lwfihhllyq tplepvfdae
      121 frrqwasyet ynrafaeala eeaaegaavl vqdyhlclvp gmlrelrpdl righfshtpw
      181 apvdyfallp tdiraqllrg mlgadrlgfl trrwadafta cstefvgglg gteigvhglg
      241 adadflrars hendveeriv alreeigegr kaivrvdrte lsknivrgll ayrqllddrp
      301 ewrervvhva faypsrqdla vyrdytaevq rvareinery gtpgwtpvvl hvkddfarsl
      361 aayrladval vnpvrdgmnl vakevpivsd qgcalvlsre agaywelged aivvnpydil
      421 etaralheal tmapeervar akrlkeaata lpparwfleq lqalqslhrd
//
LOCUS       WP_391992608             406 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces bobili].
ACCESSION   WP_391992608
VERSION     WP_391992608.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bobili
  ORGANISM  Streptomyces bobili
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 406)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Streptomyces bobili"
                     /db_xref="taxon:67280"
     Protein         1..406
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=42445
     Region          71..242
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          248..376
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mttpnktarr tlgacaalvv galtltacgg sanaedkngk gggdsakvrt akilisaeng
       61 stgasinstg vkvsegrltt vkmkvagteq fvagslaadg sswkpkeqle rgtkyeisat
      121 amggngrmvm adsvfttvsa ansfigtytp dngttvgvgm pvsftfdkai edkkavqshi
      181 tvstssgqkv vghwfgsqrl dfrpeeywka gskvtmkidl dgvkgangah gvqkktvtft
      241 igrsqvstvd vgtqtmsvvr dgaplksvpi ssgsaqhtty ngqmvitekf tqtrmnsrtv
      301 glggeydipd vphamrltqs gtfihgnywy nkgnppfgre gtshgcvgla dargaqgdtp
      361 akwfydnsli gdvvivknsp dktvapdngl ngwnlgwsew iagsav
//
LOCUS       WP_391992808             284 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Streptomyces bobili].
ACCESSION   WP_391992808
VERSION     WP_391992808.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bobili
  ORGANISM  Streptomyces bobili
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 284)
  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 284)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces bobili"
                     /db_xref="taxon:67280"
     Protein         1..284
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29217
     Region          23..276
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mpltttgdlv traraartav vafniitleh ieavitgaes agvpvvlqvs enavkfrhgr
       61 llplaraava aaeraavpva lhldhvrsha llqeaadagf ssvmydashl pyadnlastr
      121 aaadrahaqg lwieaelgei ggkggeaprd ahapgartdp aearafvtds rvdalavavg
      181 sahamttrta aldhgllrrl rasvdvplvl hgssgvpdge lraavaggia kvnigtalnl
      241 amtgairdyl aahpdavdsr gylavgream ayaverissm lipa
//
LOCUS       WP_391992928             241 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Streptomyces bobili].
ACCESSION   WP_391992928
VERSION     WP_391992928.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bobili
  ORGANISM  Streptomyces bobili
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 241)
  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 241)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Streptomyces bobili"
                     /db_xref="taxon:67280"
     Protein         1..241
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25356
     Region          3..231
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 mirvaavgdi hmgpdsqgll rpafdtldec adllllagdl trhgtpeear vvgrevrglp
       61 vpvvavlgnh dhhdeqpekv tgilqeagvt vlegegtvve cagtrvgvag tkgfcggfvg
      121 rsagefgepl mkefvrytrr sadalhgale dlgrdgcdlr ialthfspva dtlageplei
      181 ypflgsylla eaidtagadl svhghahmgt ehgmtaggvr vrnvaqpvir rafsvyrlha
      241 a
//
LOCUS       WP_391993083             825 aa            linear   BCT 20-JAN-2025
DEFINITION  GcvT family protein [Streptomyces bobili].
ACCESSION   WP_391993083
VERSION     WP_391993083.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bobili
  ORGANISM  Streptomyces bobili
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Stauffer,L.T., Ghrist,A. and Stauffer,G.V.
  TITLE     The Escherichia coli gcvT gene encoding the T-protein of the
            glycine cleavage enzyme system
  JOURNAL   DNA Seq 3 (6), 339-346 (1993)
   PUBMED   8219277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Streptomyces bobili"
                     /db_xref="taxon:67280"
     Protein         1..825
                     /product="GcvT family protein"
                     /calculated_mol_wt=90566
     Region          15..400
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
     Region          386..441
                     /region_name="FAO_M"
                     /note="FAD dependent oxidoreductase central domain;
                     pfam16350"
                     /db_xref="CDD:465100"
     Region          436..824
                     /region_name="GcvT"
                     /note="Glycine cleavage system protein T
                     (aminomethyltransferase) [Amino acid transport and
                     metabolism]; COG0404"
                     /db_xref="CDD:440173"
ORIGIN      
        1 msstpenrpr ttsstprvvv igagivgcsl adeltargwt dvtvleqgpl papggstsha
       61 pglvfqtsps rtlsefakyt vqkfgslrid gvpcfnqvgg lelattperl adlhrragya
      121 aawgirgkiv gtarckelwp lldesivlgg fhtpddglar allaaraqme raaqrgarfl
      181 drhtvtgier egghvtavvt drgtfpadhv vsaagfwgpv igrmagidvp lqplahqyvk
      241 tkalpelgdh aeeasrpilr fqdrdlyfre htdrigigsy ahrplpvdpf avppydeara
      301 rdmdmpssyp lteedwapsw edcrrlvpal rdsdieegfn gvfsftpdgm pvlgesrqlr
      361 gfwlaeavwv thsagvakav aewmvdgrps ldvhecdltr feeaqrspay vrargsqqfa
      421 evydvlhplq pmeqprplrv spfharqeql gafflegggw erphwyeana plvdglgpge
      481 ppvrdawsar ywspvaaaea katrekvaly dmtplrrlev tgpgalafld rmtsnnlrkk
      541 pgavtytlll detggirsdl tvarlaadrf qiganspadl drlvrhapdd vqvrditsgt
      601 ccvgvwgpla rdlvqpltrd dfshegfgyf raketyvghv pvtamrlsyv gelgwelytt
      661 adlglrlwdt lweagrdlgv iaagrsafns lrlekgyraw gtdmtdehdp yeagvgfavr
      721 mdkagfvgre alenrtesnr rltplllddp ahvvlgkepv hvdgapagyv tsasygytlg
      781 rciayawlpv lpagaavhie yfgekvpatv aeeplfdpkm trirr
//
LOCUS       WP_391993160             238 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Streptomyces bobili].
ACCESSION   WP_391993160
VERSION     WP_391993160.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bobili
  ORGANISM  Streptomyces bobili
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 238)
  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 10007985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Streptomyces bobili"
                     /db_xref="taxon:67280"
     Protein         1..238
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=25374
     Region          42..228
                     /region_name="COG3786"
                     /note="L,D-peptidoglycan transpeptidase YkuD,
                     ErfK/YbiS/YcfS/YnhG family [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443000"
ORIGIN      
        1 mrrpalatal vcasllllga apetggptpp pplparmtdt gggtqlitav apdtgattgr
       61 ltwwdlrggr wlragsapar fganglvega vrrqgtsttp tglydlpfaf gieapprgta
      121 yayrpvrads wwcqdnasrs ynrwteprpa dcraaesehl ityrtqyaha lvigfnyrkp
      181 vrdrgagifl hvngrgatag cvsvpadamr rvlawarpaq rphlaigtag grtaitry
//
LOCUS       WP_391993481             405 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces bobili].
ACCESSION   WP_391993481
VERSION     WP_391993481.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bobili
  ORGANISM  Streptomyces bobili
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 405)
  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 405)
  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 405)
  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 11448557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Streptomyces bobili"
                     /db_xref="taxon:67280"
     Protein         1..405
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43938
     Region          6..65
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
ORIGIN      
        1 mraelttgqr vararrrmgw dqgqlaaavd rsvswvskie tgrlpldrms vlgqlaevlg
       61 vevteltgqp yrhdtaelds ghasvpglrl alqqatmpgg agmiaaatlp tlsdltlrve
      121 aaeklrqdak ftalgdvlpq ilrdlvvlcd vaggtdvpra eglmlrashm arvssnllgh
      181 hdlgwsavqr elvaaeraes pvlraaarwd lcgvwlhage lgaardmark alddlephma
      241 asnetvralw gamhlraava wsrlwdrsea ethltearri aadvsedgnv fqtqfnavnt
      301 eihsvevsle lgrprdvlsr adlvaveria sgerqshfwv csavgqmmng kpesaaeail
      361 kadriapqhv rnrpiarnlv adlrstdrhs naaeirrlaa smklg
//
LOCUS       WP_391993290             309 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Streptomyces bobili].
ACCESSION   WP_391993290
VERSION     WP_391993290.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bobili
  ORGANISM  Streptomyces bobili
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Streptomyces bobili"
                     /db_xref="taxon:67280"
     Protein         1..309
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33260
     Region          7..303
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mrgvtgrlml ldtaslyfra yfgvpdsvka pdgtpvnavr glldfidrlv kdhrpdelva
       61 cmdadwrpqw rvdlipsyka hrvaqehevg pdeeevpdtl spqvplieav ldalgiarvg
      121 vagyeaddvi gtftarakgp vdivtgdrdl yqlvddargv rvlyplkgvg tlqttdeawl
      181 rekygvdgrg yadlallrgd psdglpgvpg igektaakll tefgdlagil aavddpkakl
      241 tpsqrkrlde arpylavapt vvkvaddvpl pevstalprt prepatveal aerwglggsl
      301 rrllttlgt
//
LOCUS       WP_391994246             735 aa            linear   BCT 20-JAN-2025
DEFINITION  caspase family protein [Streptomyces bobili].
ACCESSION   WP_391994246
VERSION     WP_391994246.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bobili
  ORGANISM  Streptomyces bobili
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 735)
  AUTHORS   Van Opdenbosch,N. and Lamkanfi,M.
  TITLE     Caspases in Cell Death, Inflammation, and Disease
  JOURNAL   Immunity 50 (6), 1352-1364 (2019)
   PUBMED   31216460
REFERENCE   2  (residues 1 to 735)
  AUTHORS   Tsiatsiani,L., Van Breusegem,F., Gallois,P., Zavialov,A., Lam,E.
            and Bozhkov,P.V.
  TITLE     Metacaspases
  JOURNAL   Cell Death Differ 18 (8), 1279-1288 (2011)
   PUBMED   21597462
REFERENCE   3  (residues 1 to 735)
  AUTHORS   Zhang,J.H., Zhang,Y. and Herman,B.
  TITLE     Caspases, apoptosis and aging
  JOURNAL   Ageing Res Rev 2 (4), 357-366 (2003)
   PUBMED   14522240
REFERENCE   4  (residues 1 to 735)
  AUTHORS   Salvesen,G.S.
  TITLE     Caspases and apoptosis
  JOURNAL   Essays Biochem 38, 9-19 (2002)
   PUBMED   12463158
REFERENCE   5  (residues 1 to 735)
  AUTHORS   Villa,P., Kaufmann,S.H. and Earnshaw,W.C.
  TITLE     Caspases and caspase inhibitors
  JOURNAL   Trends Biochem Sci 22 (10), 388-393 (1997)
   PUBMED   9357314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..735
                     /organism="Streptomyces bobili"
                     /db_xref="taxon:67280"
     Protein         1..735
                     /product="caspase family protein"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=80971
     Region          8..224
                     /region_name="COG4249"
                     /note="Uncharacterized conserved protein, contains caspase
                     domain [General function prediction only]"
                     /db_xref="CDD:443391"
ORIGIN      
        1 mglpdpdatr vvligaeeyq nfpdlpavrn nltrlaelfr spdvgglpag hcvtvrnpad
       61 yeevldavhe aaseatdtlv vyyaghgmrs pdgllhlalg hseqgrklyk svaygylraa
      121 vlestalrkv vildccysga aleghmggad efadqtaieg tcvmtasaat qaamapmgar
      181 ytaftgelvk aisegvpdvl gpldmnslym hvrrelkskg mpvplqragg qghaialfrn
      241 kwrrpqeept laalreewfr eiqegllwhv rnvpalgkgr lrtdfgeprl igsllvaria
      301 aqlargesta qicdmlavsp lftapgpdrd elieliaevq srferdglat tvavldglgl
      361 lpwspestnm llleywtaqr grtvfrtrve relrelwdst dmrvheelsa lpsspleayp
      421 dvwerlkdep dlrvgnvgam vlgergggdr awdrwistrt wsilkarhlv rlggdlarcq
      481 aaqralghfl dqappgdefi gvleraekif qeqlghialt vegmsaieye llrersrdeh
      541 fqdgclatfq qhllgryrsf tpfpehvtth gtwgplpwws ialhdereql aaqellargg
      601 mqmsvtaksr dadelvvtcq epgpgpshit arigfdllda vhacelllla crqsvtvdfl
      661 tehidewddh evnlmgtlsv giggetgail adistralrr llpgasgsef hdeaipalek
      721 llnssrlpqi crhpr
//
LOCUS       WP_391994330             310 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces bobili].
ACCESSION   WP_391994330
VERSION     WP_391994330.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bobili
  ORGANISM  Streptomyces bobili
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 310)
  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 310)
  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 310)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces bobili"
                     /db_xref="taxon:67280"
     Protein         1..310
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34689
     Region          2..60
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          80..256
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 maalfgsrvr rlrtaagltq aelgqkthvv stritqiera sgakptlelt raldavlgad
       61 nllvdlwpyv yreafpdwsr rfmelaerat dvreyaahvv pgllqteeya ravlrvgltl
      121 ssdaqlderl aarmgrqvrl tgpdrpelwv vldeavlrrp igghtvmraq ferlldaaea
      181 rhvtvqvlpf dqgehdamgg sltiltlaeg eqvaytegah ygqliedpae vsrfevtydr
      241 lraealppim sldmirsvme gynrgdrrdr ganvpsrsgr rrlaqeqlqq pggrqlrrgg
      301 prlprrrprs
//
LOCUS       WP_391994361             403 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces bobili].
ACCESSION   WP_391994361
VERSION     WP_391994361.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bobili
  ORGANISM  Streptomyces bobili
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  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 403)
  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
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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   5  (residues 1 to 403)
  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   6  (residues 1 to 403)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 403)
  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 20283677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces bobili"
                     /db_xref="taxon:67280"
     Protein         1..403
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40041
     Region          42..98
                     /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            45..46
                     /site_type="active"
                     /note="putative switch regulator [active]"
                     /db_xref="CDD:238044"
     Site            order(64..66,75)
                     /site_type="other"
                     /note="non-specific DNA interactions [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            75..81
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            order(76..77,81)
                     /site_type="other"
                     /note="sequence specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238044"
     Site            76..77
                     /site_type="other"
                     /note="putative cAMP binding site [chemical binding]"
                     /db_xref="CDD:238044"
     Region          112..394
                     /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 mgrvnrtngg gtvsgkdgga rvvaggaasg vaggalganl lavrshnaal vldllrtagp
       61 dgisrlelae rtgltpqavs kitarlreeg laaeagrras tggkprtvlr lvpgaahavg
      121 vhldrdalri vltdldgsvv gerrgpldlg agaeavlgav eggvgevvgr argqaragrp
      181 vaarllgvgv alpgpldhth gvlhrvtgfp ewdgfplrda larrlglpvv vdkdtnaaal
      241 glavggergs faylhlgtgl gaglviggrv hrgahtgage fghqvvqldg ppcpcgnrgc
      301 vealclaaid rgdpaeaarv lgtaaanlag lldidqillg grtitttpdp fvrgvaavla
      361 araaregspe pavpvrlapg gsasvaegaa hlllgpvfgr tdv
//
LOCUS       WP_391994515             288 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces bobili].
ACCESSION   WP_391994515
VERSION     WP_391994515.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bobili
  ORGANISM  Streptomyces bobili
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   3  (residues 1 to 288)
  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 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 16111081
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces bobili"
                     /db_xref="taxon:67280"
     Protein         1..288
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32098
     Region          35..83
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(36,40,65)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(39,64)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(46..47,58,61,65..66)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          104..282
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mgateqgpqq vgdgeepqsd deestavlrt vgkvikmcre rqgmtqaelg aairyseeqv
       61 ssvergrrap kpafleaadt vleaggliag lqkdveeary pkkvrdlkkl eaqaveicay
      121 anhhihgllq tpeyaealya mrrptytvee idrhvaarma rksvfervpt pllsfvqeev
      181 tlrrplggrm vlrrqlehll eigtlrhvei qvmptdredh agmggslqll klmdgktvgh
      241 seaqlhsyli sgtrdiqvme mrhgmiraqa ltpresltfi ekvlgeet
//
LOCUS       WP_391995050             341 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Streptomyces bobili].
ACCESSION   WP_391995050
VERSION     WP_391995050.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bobili
  ORGANISM  Streptomyces bobili
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Streptomyces bobili"
                     /db_xref="taxon:67280"
     Protein         1..341
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36720
     Region          10..329
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mtltalpqpl rpralrpgdl vvvaslsgpl havyepdleq avvvlermgf rvrraplleg
       61 grhrwwsaar paeiaeelna llrdpevrai iahdggqtal gyldlidfea itadpkpilg
      121 fsdisllhlv lyartglvgf htdlatpglg ghwqrataar raeleklyst lltgtepiga
      181 lpatptwecw ragrtegrli ggvinrivln qvtpyalple wfdgavlfwe eagglaayvw
      241 sylqvlrhag ildrisgmvv gipdgidgld spdasptlre ivldvlgdrd ipvlgnvefg
      301 hagpnlpmpv girvaldaqq rtlsllepav hpltltgnpg a
//
LOCUS       WP_391995343            1430 aa            linear   BCT 20-JAN-2025
DEFINITION  Rne/Rng family ribonuclease [Streptomyces californicus].
ACCESSION   WP_391995343
VERSION     WP_391995343.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1430)
  AUTHORS   Kime,L., Jourdan,S.S. and McDowall,K.J.
  TITLE     Identifying and characterizing substrates of the RNase E/G family
            of enzymes
  JOURNAL   Methods Enzymol 447, 215-241 (2008)
   PUBMED   19161846
REFERENCE   2  (residues 1 to 1430)
  AUTHORS   Callaghan,A.J., Marcaida,M.J., Stead,J.A., McDowall,K.J.,
            Scott,W.G. and Luisi,B.F.
  TITLE     Structure of Escherichia coli RNase E catalytic domain and
            implications for RNA turnover
  JOURNAL   Nature 437 (7062), 1187-1191 (2005)
   PUBMED   16237448
REFERENCE   3  (residues 1 to 1430)
  AUTHORS   Li,Z., Pandit,S. and Deutscher,M.P.
  TITLE     RNase G (CafA protein) and RNase E are both required for the 5'
            maturation of 16S ribosomal RNA
  JOURNAL   EMBO J 18 (10), 2878-2885 (1999)
   PUBMED   10329633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1430
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..1430
                     /product="Rne/Rng family ribonuclease"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=150099
     Region          <49..>155
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          674..1075
                     /region_name="CafA"
                     /note="Ribonuclease G or E [Translation, ribosomal
                     structure and biogenesis]; COG1530"
                     /db_xref="CDD:441139"
ORIGIN      
        1 mpqpnepgtt gnneentpgd klpprrrrra asrpagppgg aapaaedvtp aipadasaap
       61 avddtpgeta aeaappartr rravrkstap agappqaeta epapdaetap vaeaparpva
      121 deepaapapr arrravrkat apagspeaae vveapvevaa epetepeeea vaavetpeea
      181 paprrrrasr katspagapq saeeavvvve paadapaeep aaavaepaap rgrtrrrasa
      241 pagapqaaap vsepeqvraa epaapaavea etaeeapapr grrrasrkas apagspqpae
      301 aaaavgsads adsadsadsa dsadvaeepv esgeslpaav aeelaaetde veeaaprgrr
      361 rrrataaags peftakteep trrsrratrp avavfqapvf aepmfqtpet aaaaaaaags
      421 aspydeadev eeqtgseqsa apaeaapqgg srrrrrrrge sdaaeqaapv etpaveapea
      481 eaeadehddd adeygdrpsr rrrrggrrrr rgeahdtdde ntddapartg aeetraedeq
      541 dggrgqaqet adesdeddda sasgsssssr rrrrrrrrsg daaadadhgt sddpertvvk
      601 vreprkkeer epgtgfdevq sikgstrmea kkqrrregre qgrrrvpiit eaeflarrea
      661 vervmvvrqn gertqigvle dnvlvehyvn keqstsyvgn vylgkvqnvl psmeaafvdi
      721 gkgrnavlya gevnfealgm ahgprrieta lksgqsvlvq vtkdpighkg arltsqvslp
      781 grylvyvpeg smtgisrklp dtersrlkti lkkivpedag vivrtaaega sedelrrdve
      841 rlqqqwadiq kkakgtsssn aptllygepd mtvrvvrdif nedfskvivs gdeawetihg
      901 yvshvapdlt erlsrwtsev dvfatyride qlmkaldrkv ylpsggslvi dkteamvvvd
      961 vntgkftgqg gnleetvtrn nleaaeeivr qlrlrdlggi vvvdfidmvl esnrdlvlrr
     1021 lleclgrdrt khqvaevtsl glvqmtrkrv gqgllesfse tcvhcngrgv ivhmeqptsp
     1081 ggggggkksk krrggagqdh dhghdhgsed hasaetsete aveteaelaa evaapvavep
     1141 avreddefyg spaeaeaaat rgrgrrrasr kasapagapk aeapaaeptp eptpepvvea
     1201 paaetsvaea pvaeapeapa eaapqgrtrr ratrkatapa gapkqaeaae pvqpaepaad
     1261 pvavedpvve paaaetpave apaepapeae apvaapprar rrvtrkvtap agsptggdda
     1321 avvvvdtase akapeaddra pegtpesgvt dsesaeaapa kktarktaak kapakkaaak
     1381 ktaakktaak kttaktaakk atkktvaaeq qpspsvnast gssegeasag
//
LOCUS       WP_391995563             268 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Streptomyces californicus].
ACCESSION   WP_391995563
VERSION     WP_391995563.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 268)
  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 268)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..268
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29345
     Region          17..258
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 mrgsepddgg aatrstrihv vsdvhgntea laragdgada liclgdlvlf ldyadhsrgi
       61 fpdlfgvena drivalrtar rydearafgr elwagrdrna eilgavrrqy aelfaafptp
      121 tyatygnvdv pdlwpeytrp gttvldgerv eiggrvfgfv ggglrtpmnt pyeisdeeya
      181 akvealgevd vlcshippev peltydtvar rfergspall eairatrpry alfghvhqpl
      241 vrrmrigate cvnvghfast gtpwalsw
//
LOCUS       WP_391995814             446 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            californicus].
ACCESSION   WP_391995814
VERSION     WP_391995814.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 446)
  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 446)
  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 446)
  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 11448557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..446
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=48406
     Region          <14..70
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
ORIGIN      
        1 msdpmalhpl tyvregkgwg kaelarrmre rgaelgvpla tnrttvwkwe qgqapdadaq
       61 rvladllgvp edhvrtaawp rwlpawesta lvapwtpagt vkvfadlvrs ghmdrrgfls
      121 itgvaltgva anwaaapeaf asaidgdrvt damvatiear vdtlrtlddq mggarlldqa
      181 tsdlalitsl ldhgrytdai ehrlyvtaar vsylagwmay dkglrslgqr yyvgalrsah
      241 sakddgfgaf ilaemgvhis dsgdtaarvk lidtaignap salppaatsy lylhqaeals
      301 rdtqheaagk slnraydlwg ahfegdrpdw lgwygeaqlk stegkimlrs gfperatsal
      361 aiaidqavpr dravrsgrla tarlaardla galdaanvgl ellenhvrsd rahvrltkfs
      421 rylephsavp svrefrdrly alpava
//
LOCUS       WP_391995839             390 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            californicus].
ACCESSION   WP_391995839
VERSION     WP_391995839.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 390)
  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 390)
  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 390)
  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 11448557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..390
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=42078
     Region          96..162
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
ORIGIN      
        1 msrradsdet ratarpgprd ggrpdqpgrg grpgrddrdd rgrtaaadar pdqpgadaas
       61 asasaepvrt eeahitaart gralttsalh aaatgadtfp avlrealgrr glslervser
      121 lkargitisq atlsswqrgr sqperarslr avdvleeild lpagtlrsll gprrprgrtt
      181 ppgaegaalq ilgedsvvek algarfrhfn qetsslmvhd ivrigesgtm sgfsttnvlr
      241 agragadral fvlsfddeaa epvdirvtcg rlaeatylkg lkslvleihf grklakldtt
      301 vvsyavevsp sltrathyer wsrtnlheyl qqvyfhpgal pvdchryvre kvgappraqr
      361 riplgaahdv hvltsrckpg vhgvaweygp
//
LOCUS       WP_391996246             538 aa            linear   BCT 20-JAN-2025
DEFINITION  peptide ABC transporter substrate-binding protein [Streptomyces
            californicus].
ACCESSION   WP_391996246
VERSION     WP_391996246.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 538)
  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 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   3  (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   4  (residues 1 to 538)
  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 538)
  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 11467924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..538
                     /product="peptide 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=58922
     Region          23..525
                     /region_name="OppA"
                     /note="ABC-type oligopeptide transport system, periplasmic
                     component [Amino acid transport and metabolism]; COG4166"
                     /db_xref="CDD:443327"
ORIGIN      
        1 mrgaksakwv agaavialaa tacgggdsdg gkentsgqpa gyvsidvgep qkplmpadtn
       61 esngsyviqs lftqlldfdd kgeivltnae svetedsktw tvklkagwkf hngeavtaqs
      121 yidawnwyan vknaqqnafw fsdikgyadv hpekgdpksd kmsglkavdd ttftieltdk
      181 vpyfnyklgy atfaplpkvf yddpkafgqk pigngpytfe kwthkkliqv kawpeyqgpn
      241 kaankgiqfk nystveaayq dvisgnldmi rqvgprdlpk yktdlgdgai dqpyaaiqtl
      301 vpafysksfk didpkvlqgl smaidrdtit ktvlngtrip atsftppqvk gnqtldsdil
      361 kynpakakel ikagggvpen kftiqynadg ghkewvtavc esirnatgve ctgdakpdfp
      421 tdleardnde vkgfyrggwv adypvnvnfl kelyhskaes nngrfndkev dalmakgdka
      481 dsleesvaay qevekklvek mpaiplwyya ingghgknvd nvkvdfhgdl eltgvttk
//
LOCUS       WP_391996278             982 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces californicus].
ACCESSION   WP_391996278
VERSION     WP_391996278.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 982)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 982)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..982
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..982
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=103474
     Region          704..973
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mqppkaadas dagerpqgas etparsdlpv asappagsgp pvtsasaadp gsavpvvpga
       61 ghgplrpdgp tvsgtghlag stlasadaah sdrvsgdepl lparvhrpsd lmrlligvla
      121 iavlftiaaf aqgtttgled diskgteqap dlliklaglv ssiavllvpv afaierlikr
      181 dglriadgvl aavlahgvtl atdlwvsqaa prtiqdaltq qattggltdp vhgylapvia
      241 ymtavgmarr prwrvvlwvv llldafamlv ggyttpfsii ltvligwtva ygtlyavgsp
      301 nvrptgqhlm aglrhvgfhp vaamraddvp dkdnadqgdr grrylvtled gppldvtvvd
      361 reqqaqgffy rawrrltlrt ltqrrsiqsl rqaleqeall ayaaiaagan apkliatsel
      421 gpdavmlvye higgrsldqm edeeitddlv rgawrqveal qsrriahrrl tgdailvdrs
      481 grafvtdlrg geiaagdlvl rmdvaqlltt lglrvgaers vagalavlgp davadclpll
      541 qpialsrstr atlrriarer sqrerdavle asraakqara rdaaeaapee raglgadaaa
      601 epskalskad akadakadak aerktlrnek qaekraidda leeareedll aqirrqvlli
      661 rpqapvepvr lerikartlf sfiagaiaay flisqvtqad ftvveqarwg wvaaalgfsa
      721 lsyvaaamsl lgfvpervsf lktvqaqvag sfvkivapaa vggvalntrf lqragvrpgl
      781 avasvgasql fglgahimll alfgyltgte ktpdsltpsr tviaglltva vlvlvvtaip
      841 flrkfvvtrv rslfagvvpr mldvvqrpqk lltgiggmll ltglfvlcld asirafsgpd
      901 vpqlsyasia vvflagnalg saaptpggmg avegaltlgl iavglpkeva apavllyrvm
      961 tlwlpvlpgw lafnqltrkg el
//
LOCUS       WP_391996488             393 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces californicus].
ACCESSION   WP_391996488
VERSION     WP_391996488.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 393)
  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 393)
  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
REFERENCE   3  (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   4  (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   5  (residues 1 to 393)
  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   6  (residues 1 to 393)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (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 20170230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..393
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39944
     Region          <10..>74
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          77..384
                     /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 mtarpgnahq aqllrllrdg gpnsraqlgd qvelsrskla vevdrlletg lvvadglaas
       61 rggrrshnir lapelrflgv digatsidva vtnaelevlg hlnhpmdvre gpvavfeqvl
      121 slaaklrasg laegfdgagi gvpgpvrfpe gvpvappimp gwdgfpvrea lsqelgcpvm
      181 vdndvnlmam geqhagvars vgdylcvkig tgigcgivvg gevyrgttgs agdighirvd
      241 pdgracacgn kgcleahfsg aalardaeda aregrspela arlaaagrlt aadvaaaaaa
      301 gdaaaldlir eggnrlgqvi aslvsffnpg lvvigggvtg lghnllasvr tqvykqslpl
      361 atgnlpivlg elgptagvig aarlisdhlf spa
//
LOCUS       WP_391996537             374 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            californicus].
ACCESSION   WP_391996537
VERSION     WP_391996537.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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   4  (residues 1 to 374)
  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 374)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..374
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39923
     Region          16..351
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 mtatqapeaa vksadeavfs vrnlwkvfgp kadrvpggeh aalppaelre atgctaavrd
       61 vsfdvrkgev fvvmglsgsg kstlvrcltr lieptsgtla idgedvlamd rsrlrelrrh
      121 raamvfqhfg llphrtvvdn vaygleiqgl skserrskaa elvakvglag medrrpsqls
      181 ggqqqrvgla ralavdpsvl lfdepfsald plirremqde vvrlhreegr tmvfithdls
      241 ealrlgtria lmrdggivql gtpeeivgsp addyvrefvr dvpreqvltv atamrpalag
      301 esergpavrp datvaeaiea vsrsgdpaar vmdagrlvgv vdraclldvv agtaepavaa
      361 papdapdgpr evta
//
LOCUS       WP_391997048             550 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Streptomyces californicus].
ACCESSION   WP_391997048
VERSION     WP_391997048.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 550)
  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 550)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..550
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=58119
     Region          273..450
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 mvrvpfraaa drvrcrlgri arpssrsrta artpaaapgd laaagrgpgr hpclralgml
       61 avvvlgawlg llavgsirtp vgpmdttmtl rpsltggski nvsplgalel dshiaplrld
      121 vdvdrldper sqalvdqper fsslqdevtr dvaagtrela vrscvavvsg aaalglvvyr
      181 rprralaagg laltllaasg vsayatwnpk svlepkfsgl lssapslvgd arsivtefdi
      241 yqrelarlvt nvtklydats tlpvyqpdpg tirvlhvsdi hlnpaawhii aslveqyeid
      301 vivdsgdtmd hgsaaengfl dpirdlgapy vwvrgnhdsr vtqeylekfg nvrvlddgaa
      361 vnvgglriag tgdasftpdr tgpgsnkeaa rlegmrlata lrdqeragtp adiavahdpn
      421 taretdgtvp lvlsghyhrr ineqlklgtr lkvegstggg glravqnekp ekvhasvlym
      481 drstrrlqaw deitlgglgl ttaevsrhlp eenlkkdapg sptpspssps ssaspapspg
      541 rssgrptpap
//
LOCUS       WP_391997685             386 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces californicus].
ACCESSION   WP_391997685
VERSION     WP_391997685.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 386)
  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 386)
  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
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 386)
  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   5  (residues 1 to 386)
  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   6  (residues 1 to 386)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 386)
  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 20283677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..386
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39907
     Region          20..62
                     /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"
     Region          78..365
                     /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 mkirasdgsr lrrinlaatl ralrgepavg ltelaarael srptveglve dllglgwvse
       61 vppesgrmgr prrlfrfrae aghvlgidvg ssgaravvcd lngevrgrst vraeasfgre
      121 krlagmrsaa healsyagvp aahvmavcvg ttgvvtatgt vrlcvslpdw tgldlaaeag
      181 rdfdapvlve ndcnlaalae rwvgvaqhad dvvfvlsgtr tgagmlirge lhrggrgaag
      241 eigalplvgw hrapshlaaf pglppsapag evaglvfaaa rsgdpaarwa veqfahdlae
      301 giaalvlsvd pdlvvlgggv srsadvlmep lrrhldplcl eppalaisgl gdqavvtgav
      361 rhalnhvdar lydvdaplpa ssrpgp
//
LOCUS       WP_391997700             284 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces
            californicus].
ACCESSION   WP_391997700
VERSION     WP_391997700.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789410
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..284
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30628
     Region          4..283
                     /region_name="PrpB"
                     /note="2-Methylisocitrate lyase and related enzymes, PEP
                     mutase family [Carbohydrate transport and metabolism];
                     COG2513"
                     /db_xref="CDD:442003"
ORIGIN      
        1 mpqrpttrlr rliggdgihv apgaydglsa rlveesgsel lyasggaiar sfgvpdigll
       61 slsevvarie qmvevtslpv iadadtgfgn avnavrtlal yeragvagmh iedqtfpkrc
      121 ghlddkslvs tdemvrkvra vheartdpdf vlvartdaia tegldaaver ahayaeagad
      181 vifveapetv eqieriaerv pqpklinmfh ggktpvvpre rlrelgyrlv ivpsdlqrav
      241 itavrrtlea inrdgdsgav redlasfadr ervvrtaeyl algs
//
LOCUS       WP_391998144             295 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            californicus].
ACCESSION   WP_391998144
VERSION     WP_391998144.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 295)
  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 295)
  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 295)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..295
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33220
     Region          38..90
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          112..290
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mthgtdgigt igqgtskgsg argraasepe sqyslkvfge vvkafrkrar ltqeefaplv
       61 rysvetiasi eqgrrfpppd fveraeavld afgvieaaak hltrkrglas wfqqwaqlel
      121 salslhtyec rmipgllqtp ayartlftdq lppltdeqie vrlaarqerq qllrnrpnta
      181 fsfileehlf lrnlggdevt relldhllel sdlrnvtiqi mevvrpkhag lhgpmqllet
      241 pqhqwfgyle gqehgelvtd pkvistfqmr casmrsqart aedtrslmkr mrgat
//
LOCUS       WP_391998507             253 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces
            californicus].
ACCESSION   WP_391998507
VERSION     WP_391998507.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616714
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..253
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26805
     Region          13..248
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 mdsrttvera qrlkqlhadh qplvlptvwd awsartavaa gfpaltigsh pladsrgaed
       61 qegqtfeevl aavrpiiaav dvpvsvdlea gygqkpadli aglievggvg lnvedtvhse
      121 ggrvrttqeh aayvaglraa adeagvpvwi ngrtdlfaha edpaavldea ierlralvqa
      181 gadsvypvki qdndelltav taavsvpvns tahpvkhdle rfrrlgvgri tygpllqmal
      241 tdamkdmlgp wap
//
LOCUS       WP_391998556             415 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            californicus].
ACCESSION   WP_391998556
VERSION     WP_391998556.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces californicus
  ORGANISM  Streptomyces californicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  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 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   3  (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   4  (residues 1 to 415)
  AUTHORS   Igarashi,K., Ito,K. and Kashiwagi,K.
  TITLE     Polyamine uptake systems in Escherichia coli
  JOURNAL   Res Microbiol 152 (3-4), 271-278 (2001)
   PUBMED   11421274
REFERENCE   5  (residues 1 to 415)
  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   6  (residues 1 to 415)
  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 11430824
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces californicus"
                     /db_xref="taxon:67351"
     Protein         1..415
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0019808 - polyamine binding [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:0015846 - polyamine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45385
     Region          28..413
                     /region_name="PotD"
                     /note="Spermidine/putrescine-binding periplasmic protein
                     [Amino acid transport and metabolism]; COG0687"
                     /db_xref="CDD:440451"
ORIGIN      
        1 merheterlt svqlaamrrs lsngrgaltr rsllrasgmg alalggistl gacgippagr
       61 tegsaasddh sakekevhfs nwteymdvse deksrptlqa ftertgikvk ytedindnve
      121 ffgkikpqla agqdtgrdli cvtdwlaari irlgwaqkld hanlphafan vsaqfrtpdw
      181 dpgraysfpw tgiptviayn kkatggrkvd svtqllddpk lkgrvsflse mrdtvgmtll
      241 dqgkdpgkfs dadfdgaigr lqkavdkkqi rrftgndyta dlskgdiaac vawagdiiql
      301 qadnpdieya ipaagyitss dsllvpahar hktnaeklid yyyeppvaaq laayinyvcp
      361 vdgvreelak idesmasntl ilpdkemaak srsfrslstk eetayeekfa kliga
//
LOCUS       WP_391999514             361 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            sp. NPDC014995].
ACCESSION   WP_391999514
VERSION     WP_391999514.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014995
  ORGANISM  Streptomyces sp. NPDC014995
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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   4  (residues 1 to 361)
  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 361)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Streptomyces sp. NPDC014995"
                     /db_xref="taxon:3364936"
     Protein         1..361
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39610
     Region          20..355
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 mttqtevpqr rgtpqdsgpt pvisvrrlwk vfgpkadrvp dseelcgltr relmdrtgct
       61 aavrdvhfdv spgevfvvmg lsgsgkstlv rcltrliept ageivfeged irqaddkrlr
      121 dlrrrkfsmv fqhfgllphr rvvdnvafgl eirgmgkaer teraqevvel vglagyensy
      181 pdqlsggmqq rvglaralag dpdvlffdep fsaldplirr dmqnevirlh hevgktmvfi
      241 thdlsealkl gdrilimrdg kmvqcgtgde lvgapaddyv refvkdvprg dvltlrwimr
      301 ppadgdpldg pelgpdvvvk eatravlaad kpvkvvengk llgivgdeei lavvagqegg
      361 a
//
LOCUS       WP_391999591             574 aa            linear   BCT 20-JAN-2025
DEFINITION  SWIM zinc finger family protein [Streptomyces fradiae].
ACCESSION   WP_391999591
VERSION     WP_391999591.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces fradiae
  ORGANISM  Streptomyces fradiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Hassan,I.U., Rehman,H.M., Liu,Z., Zhou,L., Samma,M.K., Wang,C.,
            Rong,Z., Qi,X., Cai,D. and Zhao,H.
  TITLE     Genome-wide identification and spatiotemporal expression profiling
            of zinc finger SWIM domain-containing protein family genes
  JOURNAL   Zool Res 44 (3), 663-674 (2023)
   PUBMED   37161653
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     SWIM, a novel Zn-chelating domain present in bacteria, archaea and
            eukaryotes
  JOURNAL   Trends Biochem Sci 27 (8), 384-386 (2002)
   PUBMED   12151216
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Streptomyces fradiae"
                     /db_xref="taxon:1906"
     Protein         1..574
                     /product="SWIM zinc finger family protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62896
     Region          4..518
                     /region_name="SWIM"
                     /note="Uncharacterized protein, contains SWIM-type Zn
                     finger domain [Function unknown]; COG4715"
                     /db_xref="CDD:443750"
ORIGIN      
        1 mgglteaklr alaggrsfer glgyvdevsg vefrdgwira svrgteryev elllgggrkl
       61 agtcdcpygq egnfckhlva lgltviaqea dlprlrkaar drtrgleawl tglsrddlia
      121 lvreeaaddr slrrrlelra asahgdvagi rshirelldi gpfvqygyve yadvrayadq
      181 agqavaairs ltasgraada talaqeaigl lasvvegvdd sdgrlgqvga dladahheac
      241 raarpdpeel ahwlvthvld eaadltdfdp ldygdvlger gtaalrryaa eawqanrtgw
      301 aekrlmqrla ksgrdidtvi avhaadlapd ghthllvare ldaagrtpea lewaergire
      361 aedlagvdta lvdhladryt rtdrladavt lrrdhfaarr tlltyqqlrv aavaadrwlt
      421 ereealellr adveqagayd grvlvdvlld dkdldaawqa ahehgahdgq wltladqsrp
      481 trpadalpvh lrlaarlare tgnrayeqlv slllsvrdch hrlgtpddft tyvadlraaq
      541 krkrnlmrlm ddcglrlakp vmltsstrln vvyg
//
LOCUS       WP_391999893             540 aa            linear   BCT 20-JAN-2025
DEFINITION  peptide ABC transporter substrate-binding protein [Streptomyces sp.
            NPDC014995].
ACCESSION   WP_391999893
VERSION     WP_391999893.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014995
  ORGANISM  Streptomyces sp. NPDC014995
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 540)
  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 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   3  (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
REFERENCE   4  (residues 1 to 540)
  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 540)
  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 11467924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Streptomyces sp. NPDC014995"
                     /db_xref="taxon:3364936"
     Protein         1..540
                     /product="peptide 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=59323
     Region          24..535
                     /region_name="OppA"
                     /note="ABC-type oligopeptide transport system, periplasmic
                     component [Amino acid transport and metabolism]; COG4166"
                     /db_xref="CDD:443327"
ORIGIN      
        1 mrgvtqvtrv acaaavtlaa tacgggvgad tgavlssswg dpqnplepan tnevqggkvl
       61 dmifrslkry nprtgraedm laerietsds rnftitvkdg wtfsngekvt aksfvdawny
      121 gaslknnqkn ayffeyiegy trthpddggk qsaetlsglr vvdertftvr lrqkfstfpd
      181 tlgypafapl prafftdhag wlrkpvgngp yriesytkgs qmelrtwedy pgpdkaangg
      241 vtlkvytdnn taytdlmagn ldlvddvpat qlknvandlg drylntpagi iqtlafphyd
      301 krwnragsek vrtglsrain reqitrtifh ntrtpatdwa spvlgteggy kkglcgdacv
      361 ydpaearrli eeggglpggq vkitynadtg shkqwvdavc nsinnalgkd kacvgnpvgt
      421 fadfrgqitd rkmtgpfrag wqmdypliqn fvqplyytna ssndgkwssk efdrlvdean
      481 aesdtaaave kfqqaervvr dqmaaiplwy qngsagyser lsdvrlnpfs vpvyneikvs
//
LOCUS       WP_392000465             237 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Streptomyces sp.
            NPDC014995].
ACCESSION   WP_392000465
VERSION     WP_392000465.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014995
  ORGANISM  Streptomyces sp. NPDC014995
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 237)
  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 11440233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Streptomyces sp. NPDC014995"
                     /db_xref="taxon:3364936"
     Protein         1..237
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25786
     Region          3..230
                     /region_name="GCD1"
                     /note="NDP-sugar pyrophosphorylase, includes eIF-2Bgamma,
                     eIF-2Bepsilon, and LPS biosynthesis protein s
                     [Translation, ribosomal structure and biogenesis, Cell
                     wall/membrane/envelope biogenesis]; COG1208"
                     /db_xref="CDD:440821"
ORIGIN      
        1 mhavilaggk gvrlrpytta lpkplvpigd qhaileivlr qlatagftsc tiaighlgei
       61 irayvgdgsq wglavdyate dsplgtmgpl lnlrdrlpet flvmngdvlt dldyadvlrr
      121 hresgaplti atyarkvhid fgvlttsdgk vvaftekpsv dyrvsmgvyg lsrstlegyt
      181 pglplgfdel vldllraqep phayefdgyw ldigrpddyd ranaefttrk slllkga
//
LOCUS       WP_392000476             327 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces fradiae].
ACCESSION   WP_392000476
VERSION     WP_392000476.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces fradiae
  ORGANISM  Streptomyces fradiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415139
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces fradiae"
                     /db_xref="taxon:1906"
     Protein         1..327
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=36269
     Region          <114..308
                     /region_name="LysX"
                     /note="Glutathione synthase, LysX or RimK-type ligase,
                     ATP-grasp superfamily [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism,
                     Translation, ribosomal structure and biogenesis, Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0189"
                     /db_xref="CDD:439959"
ORIGIN      
        1 miltvslkdd lhalavrhea lsrgcrdfhi vecdqisghe slswtvdgds pttlrtsdgr
       61 lvrledasvv wwrrvrasqq daasrenrse rnlvdndcrg altgilstaf ggewishpea
      121 tdrasdklyq lavarraglr vpktlvtqsr devarfreqv griivkpvvg tsgpllftqy
      181 lddpsalpaa syeacpavyq eyvegdrhir lncfgdrmya arlttdlldw radltmpisp
      241 wpvpddlarr vratlralgl rmgavdlklt pegepvwlev npqgqflfle pllgipltry
      301 fvdfllaaee tasapaagrr pveraaa
//
LOCUS       WP_392001598             421 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC014995].
ACCESSION   WP_392001598
VERSION     WP_392001598.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014995
  ORGANISM  Streptomyces sp. NPDC014995
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 421)
  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 421)
  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
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 421)
  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   5  (residues 1 to 421)
  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   6  (residues 1 to 421)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 421)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 421)
  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 20283677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Streptomyces sp. NPDC014995"
                     /db_xref="taxon:3364936"
     Protein         1..421
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41549
     Region          40..96
                     /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            43..44
                     /site_type="active"
                     /note="putative switch regulator [active]"
                     /db_xref="CDD:238041"
     Site            order(62..64,73)
                     /site_type="other"
                     /note="non-specific DNA interactions [nucleotide binding]"
                     /db_xref="CDD:238041"
     Site            73..79
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238041"
     Site            order(74..75,79)
                     /site_type="other"
                     /note="sequence specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238041"
     Site            74..75
                     /site_type="other"
                     /note="putative cAMP binding site [chemical binding]"
                     /db_xref="CDD:238041"
     Region          110..>345
                     /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 mtsgpasgtr ggpasgttgg patgttggpv rgmaganlla vrshntalvl dllrtagqdg
       61 isrlelaert gltpqavski tarlreegfa aeagrrastg gkprtvlrlv paaghavgvh
      121 ldrdelrvvl teldgrvvge rcvpldlgag adavvgavvr eaegavgeal tggavgeapa
      181 gsavggalae gavgdmlkgc rtllgvgval pgpldhthgv lkrvtgfpew dgfplrdtla
      241 rrlgvpvvvd kdtnaaalgl avggergsfa ylhlgtglga glviggsvhr girtgagefg
      301 hqvlqldgpp cpcgnrgcve alclaaiarg dvaeaarvlg taaanlagll didllllggr
      361 titatpdpfv dgvttvlaar ahregapega vpvrlapgga ravaegaaql llgpvfgrgn
      421 g
//
LOCUS       WP_392001709             235 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease H family protein [Streptomyces sp. NPDC014995].
ACCESSION   WP_392001709
VERSION     WP_392001709.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014995
  ORGANISM  Streptomyces sp. NPDC014995
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 235)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Streptomyces sp. NPDC014995"
                     /db_xref="taxon:3364936"
     Protein         1..235
                     /product="ribonuclease H family protein"
                     /EC_number="3.1.26.4"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=24674
     Region          8..149
                     /region_name="RNase_HI_prokaryote_like"
                     /note="RNase HI family found mainly in prokaryotes;
                     cd09278"
                     /db_xref="CDD:260010"
     Site            order(14..17,49..51,54,76,126,146)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260010"
ORIGIN      
        1 mivcmrervv aacdgaskgn pgpagwawvi sddseaparw eagplgratn nvaeltaler
       61 llaavdpdvp leirmdsqya mkavttwlpg wkrngwktsa gkpvanqelv vridelldgr
      121 tvdfryvpah qvdgdrlndf adraasqaas vqqpagsalg spepppspdt ppaagarrrt
      181 aggtsprrsg gssartikak fpgrcvcgrp yaagepiakn dqgwghpecr taaag
//
LOCUS       WP_392002105             374 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            fradiae].
ACCESSION   WP_392002105
VERSION     WP_392002105.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces fradiae
  ORGANISM  Streptomyces fradiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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   4  (residues 1 to 374)
  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 374)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Streptomyces fradiae"
                     /db_xref="taxon:1906"
     Protein         1..374
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39224
     Region          27..363
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 msadattapa aagtgsapgt asadpgtpvf avrdlwkvfg pkaervpgda aladlppael
       61 rartgctaav rgvsfdvhkg esfvvmglsg sgkstlvrcl trlieptsgt leidgddvla
      121 mdrarlrelr rrraamvfqh fgllphrsvl dnvaygleiq gvgraerrer aagfvakvgl
      181 aglehrrpgq lsggqqqrvg laralavdpe vllfdepfsa ldplirrdmq eevvrlhree
      241 grtmvfithd lgealrvgdr ialmrdgrvv qlgtpeeivg apaddyvrdf vrdvpreqvv
      301 tvrtamrpvt addaahgpav ppgatvaeai taaahgggap vrvvqdgrcl gvvdpqtllg
      361 vvagvaapgg raaa
//
LOCUS       WP_392002203             239 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces fradiae].
ACCESSION   WP_392002203
VERSION     WP_392002203.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces fradiae
  ORGANISM  Streptomyces fradiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616714
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Streptomyces fradiae"
                     /db_xref="taxon:1906"
     Protein         1..239
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24352
     Region          2..232
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 mfralhhgra pgdplvlpgp wdaasarvla eagfpalatp sagvaaslgy adgrtpagem
       61 faavarivra vdvpvsadle ggyglparel aarvldigva gvnledgdad glrdagahar
      121 wlaefraavg gevflnarvd tyvrgagdva etvrrarlya aagadgvypl kappevlpvl
      181 raevdvplna laapggpapa elgrlgasrv tygphlhrra tralrdiaaa lredgtvtg
//
LOCUS       WP_392002273             421 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces fradiae].
ACCESSION   WP_392002273
VERSION     WP_392002273.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces fradiae
  ORGANISM  Streptomyces fradiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 421)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Streptomyces fradiae"
                     /db_xref="taxon:1906"
     Protein         1..421
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=45245
     Region          67..253
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          260..390
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 matrtaaira tavrstaart airsavvwav avaalagcga ggvleglggk agwgrdeais
       61 vtphdgardv ppdgrlevrv pegrlesvrv rgardaeaae vpgtvapdgr swqprpgtrl
      121 alaaryavda vavdgdgrrt vrrtefatrv pdrrfvayfa pedratvgtg mivtfrfnrp
      181 vrdraavera irvtadppve vvghwfgaer ldvrparywr pgtrvtvelr lrdveaapgv
      241 ygvqrlttrf tvgrsqvsrv daaahtmevr rdgrllatvp itagapkttt yngrmvvtel
      301 hevtrmngat vgftdadgks eydikdvpha mrltesgtfl hgnywaersv fgasnvshgc
      361 vglrdvkggs adspagwffd rtlvgdvvev vnsrdrtvap gnglsgwnms warwkagsal
      421 r
//
LOCUS       WP_392002391             414 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC014995].
ACCESSION   WP_392002391
VERSION     WP_392002391.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014995
  ORGANISM  Streptomyces sp. NPDC014995
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 414)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Streptomyces sp. NPDC014995"
                     /db_xref="taxon:3364936"
     Protein         1..414
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=45113
     Region          61..246
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          252..383
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mrhvqrrarr agaalaavmt wagllagaag ctgddaggld rvlgkppape dvirvtpadg
       61 skevrpeqgl rvrvpdgrle svkvvkaqda qetpvpgris adglswrphd nrlalaaryt
      121 vdavavdgdg rrsarhttft thvpeerfig yiapenrstv gtgmivsmkf nreienraav
      181 eravqvtarp aveirphwfg ndrldfrprd ywrpgtkvtv alrfrdvega pgvfglqskt
      241 fsftigrhqv svvdaarhtm kvrrdgdlia tvpitagapk tttyngkmvv temheltrmn
      301 gatvgftkkn gkaeydvpdv phamrltdsg tflhgsywas advfgrrnis hgcvglrdir
      361 ggssetpagw ffdrsligdv ievvnskdkq vapdnglggw nmdweewteg savn
//
LOCUS       WP_392002678             475 aa            linear   BCT 20-JAN-2025
DEFINITION  alpha,alpha-trehalose-phosphate synthase (UDP-forming)
            [Streptomyces sp. NPDC014995].
ACCESSION   WP_392002678
VERSION     WP_392002678.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014995
  ORGANISM  Streptomyces sp. NPDC014995
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 475)
  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 475)
  AUTHORS   Eastmond,P.J. and Graham,I.A.
  TITLE     Trehalose metabolism: a regulatory role for trehalose-6-phosphate?
  JOURNAL   Curr Opin Plant Biol 6 (3), 231-235 (2003)
   PUBMED   12753972
REFERENCE   3  (residues 1 to 475)
  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   4  (residues 1 to 475)
  AUTHORS   Elbein,A.D., Pan,Y.T., Pastuszak,I. and Carroll,D.
  TITLE     New insights on trehalose: a multifunctional molecule
  JOURNAL   Glycobiology 13 (4), 17R-27R (2003)
   PUBMED   12626396
REFERENCE   5  (residues 1 to 475)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 929-939 (1997)
   PUBMED   9334165
  REMARK    Erratum:[Biochem J 1998 Feb 1;329(Pt 3):719]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Streptomyces sp. NPDC014995"
                     /db_xref="taxon:3364936"
     Protein         1..475
                     /product="alpha,alpha-trehalose-phosphate synthase
                     (UDP-forming)"
                     /EC_number="2.4.1.15"
                     /GO_function="GO:0003825 - alpha,alpha-trehalose-phosphate
                     synthase (UDP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0005992 - trehalose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51949
     Region          11..475
                     /region_name="OtsA"
                     /note="Trehalose-6-phosphate synthase, GT20 family
                     [Carbohydrate transport and metabolism]; COG0380"
                     /db_xref="CDD:440149"
ORIGIN      
        1 mastdgaaaq gaqvlvasnr gpvsyavged gslharrggg glvsglsaig pdagalwvcs
       61 altegdreav rrgvgeagvr mlpipadvha dayngiansv lwfihhllyq tptepvfdae
      121 frrewasyet ynrafaeala eeaaegaavl vqdyhlclvp gmlrelrpdl righfshtpw
      181 apvdyfgllp ddiraqllrg mlgadrlgfl trrwadafta ccteftgglg rtevgvhglg
      241 adadflrars hepdveerlp alreeigtap dgsarraivr vdrtelskni vrgllayeqf
      301 lddhpewrer vvhvafayps rqdlavyrdy taevqrvave inerfgtpdw tpvvlhvkdd
      361 farslaayrl advalvnpir dgmnlvakev pvvsdrgcal vlsreagayw elgddaivvn
      421 pydvletara lhealsmgpe eraertkrlv asatalppaq wfleqlqalr eiqps
//
LOCUS       WP_392002841             285 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces fradiae].
ACCESSION   WP_392002841
VERSION     WP_392002841.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces fradiae
  ORGANISM  Streptomyces fradiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 285)
  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 285)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptomyces fradiae"
                     /db_xref="taxon:1906"
     Protein         1..285
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32208
     Region          19..81
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          102..280
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mteerrpegp tnsgehdgdd agtevlrsfg rqlkifrtla glsqaelggr lgysealvas
       61 veqgrripke hlvekadevl eargvlaark eevarvryps ffrdaarvea qavelhaydt
      121 hvvkgllqtq dyaravftrr rplldeetie qrvaarmarq eifsrwpvpl msfvmeeavl
      181 rrpiggrsvl rgqlehlmlm gekrsvelqv mpldredhag lsgpftlmet mdgrrvayve
      241 vqnvsrlhid rkpvreieaq ygiiraqalt presmafiek llgel
//
LOCUS       WP_392002922             131 aa            linear   BCT 20-JAN-2025
DEFINITION  TOBE domain-containing protein [Streptomyces sp. NPDC014995].
ACCESSION   WP_392002922
VERSION     WP_392002922.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014995
  ORGANISM  Streptomyces sp. NPDC014995
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 131)
  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 10007583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Streptomyces sp. NPDC014995"
                     /db_xref="taxon:3364936"
     Protein         1..131
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13761
     Region          1..128
                     /region_name="MopI"
                     /note="Molybdopterin-binding protein MopI [Coenzyme
                     transport and metabolism]; COG3585"
                     /db_xref="CDD:442804"
ORIGIN      
        1 mqsytigqaa rllgvspdta rrwadagrva thrdetgrrl idgrdlaafs velagsgste
       61 egtshtsarn afpgivtaik lgdvaaqvdi qagphrlvsl ltreaveelg levgmeatar
      121 vkstnvhidr s
//
LOCUS       WP_392003548             249 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces fradiae].
ACCESSION   WP_392003548
VERSION     WP_392003548.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces fradiae
  ORGANISM  Streptomyces fradiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Streptomyces fradiae"
                     /db_xref="taxon:1906"
     Protein         1..249
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=28021
     Region          <3..162
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mfvkpldesg svgarrldda aelhawaeea gsrrfevdef lrgtlyhvdt avqdgeivha
       61 eanaylhpcy eyvngrvcas htlpddhpar psllefnrrv ldaladkprn gayhheiyqr
      121 pdgslvflei aarapaalvp stsrirwgld ieeahfrlqr geglpgsrte gphaawvyfp
      181 kaegrvsrld rarlrsdhhw qwnvevgqtt sapqdirdfa asvllwnddf dtlrrdlevl
      241 dshtavitd
//
LOCUS       WP_392003634             399 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC014995].
ACCESSION   WP_392003634
VERSION     WP_392003634.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014995
  ORGANISM  Streptomyces sp. NPDC014995
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 399)
  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   5  (residues 1 to 399)
  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   6  (residues 1 to 399)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 399)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Streptomyces sp. NPDC014995"
                     /db_xref="taxon:3364936"
     Protein         1..399
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40631
     Region          14..77
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          77..379
                     /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 metpgsqssl hranlervvr avrlagsltq aeiarttgls aatvsnivre lkdggtvevt
       61 ptsaggrrar svslsgdagi vigvdfghth lrvavgnlah qvlaeesepl dvdasstqgf
      121 draeqlvnrl leatgvdrtk iagvglgvpg pidvesgtlg ssailpgwig trpaeelrgr
      181 lgvavhvdnd anlgalgemv wgsgrgvrdl ayikvasgvg aglvidgkiy rgpggtagei
      241 ghitldesgp vcrcgnrgcl etftaaryvl pllqsshgtd ltmegvvrla rdgdpgcrrv
      301 iadvgrhvgs gvanlcnlln psrvvlggdl aeagelvlgp iresvgryai psaarqlsvl
      361 pgalggraev lgalalalse mgdstlldgt lpaaapaft
//
LOCUS       WP_392003821             281 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC014995].
ACCESSION   WP_392003821
VERSION     WP_392003821.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014995
  ORGANISM  Streptomyces sp. NPDC014995
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 281)
  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 281)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces sp. NPDC014995"
                     /db_xref="taxon:3364936"
     Protein         1..281
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31642
     Region          20..71
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          98..276
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mneaadetgw dvqpgdeiaq vvetvgrllr lhreaagmrv adlaqtlryg edmirkierg
       61 vriprpefle kadevvearg alkefkedmr karypkkvrg ladlegkave llmygnhnih
      121 gllqteeymr allstwrpay spdelermva armarkalfe rspgpelsfv qeqvtlerpv
      181 gdtmvlrrql ehmleiarlp fvelqvmpth ranhpgtggr iqvlkfsdgt algrtdgdfg
      241 grpvsdprql rvldlrygii raqaltpges lafieqalgr l
//
LOCUS       WP_392004568             161 aa            linear   BCT 20-JAN-2025
DEFINITION  SRPBCC family protein [Streptomyces sp. NPDC014995].
ACCESSION   WP_392004568
VERSION     WP_392004568.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014995
  ORGANISM  Streptomyces sp. NPDC014995
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 161)
  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 10008053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Streptomyces sp. NPDC014995"
                     /db_xref="taxon:3364936"
     Protein         1..161
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=17862
     Region          11..156
                     /region_name="YndB"
                     /note="Chalcone/flavanone-binding protein YndB,
                     AHSA1/START/SRPBCC domain [Lipid transport and
                     metabolism]; COG3832"
                     /db_xref="CDD:443044"
ORIGIN      
        1 msvtsvdkdf dsltltltad faapaekvwq lwadprrler wwgpptypat vehhdltpgg
       61 evtyfmtgpe gdkhrgwwrv tsvapptsle ftdgfadeeg tpsptmpttt vsvrltrrgd
      121 gtrmeirsaf atreqmeqlv tmgmeeglkq avgqmddlla d
//
LOCUS       WP_392004414             707 aa            linear   BCT 20-JAN-2025
DEFINITION  DNA gyrase/topoisomerase IV subunit B [Streptomyces sp.
            NPDC014995].
ACCESSION   WP_392004414
VERSION     WP_392004414.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014995
  ORGANISM  Streptomyces sp. NPDC014995
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Tari,L.W., Trzoss,M., Bensen,D.C., Li,X., Chen,Z., Lam,T.,
            Zhang,J., Creighton,C.J., Cunningham,M.L., Kwan,B., Stidham,M.,
            Shaw,K.J., Lightstone,F.C., Wong,S.E., Nguyen,T.B., Nix,J. and
            Finn,J.
  TITLE     Pyrrolopyrimidine inhibitors of DNA gyrase B (GyrB) and
            topoisomerase IV (ParE). Part I: Structure guided discovery and
            optimization of dual targeting agents with potent, broad-spectrum
            enzymatic activity
  JOURNAL   Bioorg Med Chem Lett 23 (5), 1529-1536 (2013)
   PUBMED   23352267
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Gadelle,D., Filee,J., Buhler,C. and Forterre,P.
  TITLE     Phylogenomics of type II DNA topoisomerases
  JOURNAL   Bioessays 25 (3), 232-242 (2003)
   PUBMED   12596227
REFERENCE   3  (residues 1 to 707)
  AUTHORS   Wang,J.C.
  TITLE     Cellular roles of DNA topoisomerases: a molecular perspective
  JOURNAL   Nat Rev Mol Cell Biol 3 (6), 430-440 (2002)
   PUBMED   12042765
REFERENCE   4  (residues 1 to 707)
  AUTHORS   Champoux,J.J.
  TITLE     DNA topoisomerases: structure, function, and mechanism
  JOURNAL   Annu Rev Biochem 70, 369-413 (2001)
   PUBMED   11395412
REFERENCE   5  (residues 1 to 707)
  AUTHORS   Roca,J.
  TITLE     The mechanisms of DNA topoisomerases
  JOURNAL   Trends Biochem Sci 20 (4), 156-160 (1995)
   PUBMED   7770916
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Streptomyces sp. NPDC014995"
                     /db_xref="taxon:3364936"
     Protein         1..707
                     /product="DNA gyrase/topoisomerase IV subunit B"
                     /EC_number="5.6.2.2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003918 - DNA topoisomerase type II
                     (double strand cut, ATP-hydrolyzing) activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006265 - DNA topological change [Evidence
                     IEA]"
                     /calculated_mol_wt=77115
     Region          21..701
                     /region_name="GyrB"
                     /note="DNA gyrase/topoisomerase IV, subunit B
                     [Replication, recombination and repair]; COG0187"
                     /db_xref="CDD:439957"
ORIGIN      
        1 mtaetsvpst allagadrdg snytarhllv legleavrkr pgmyigstds rglmhclwei
       61 idnsvdealg gycdhievvl hddgsvevrd ngrgipvdve pktglsgiev vmtklhaggk
      121 fgggsyaasg glhgvgasvv nalsarldve vdrgghthai sfrrgvpgaf aadgpdakfe
      181 sksglrkakk iprtrtgtrv rywadrqifl kdaklslenl hqrarqtafl vpgltivvrd
      241 eyglgeggsk geesfrfdgg isefceylat dkpvcdvlrf tgqgtfketv pvlddhgqmt
      301 ptevtrelgv dvalrwgtgy dttlrsfvni iatpkggthv agfeqavvkt lnevlrakkl
      361 lrvaeddivk ddalegltav vtvrlaepqf egqtkevlgt saarrivntv iskelkaflt
      421 stkrdaaaqa rvvmekavaa artriaarqh kdaqrrktal essslpakla dcrsddvdrs
      481 elfivegdsa lgtaklarns efqallpirg kilnvqkssv tdmlknaecg aiiqvigags
      541 grtfdidaar ygkiimmtda dvdgshirtl lltlfhrymr pmvesgrvfa avpplhrvel
      601 vqpkkgqdky vytysdrelr dklmefqskg irykdsiqry kglgemdadq laettmdprh
      661 rtlrrinlsd leaaeqvfdl lmgndvaprk efisssaatl drsrida
//
LOCUS       WP_392004682             404 aa            linear   BCT 20-JAN-2025
DEFINITION  threonine synthase [Streptomyces bacillaris].
ACCESSION   WP_392004682
VERSION     WP_392004682.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 404)
  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 404)
  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   3  (residues 1 to 404)
  AUTHORS   Parsot,C.
  TITLE     Evolution of biosynthetic pathways: a common ancestor for threonine
            synthase, threonine dehydratase and D-serine dehydratase
  JOURNAL   EMBO J 5 (11), 3013-3019 (1986)
   PUBMED   3098560
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423064
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..404
                     /product="threonine synthase"
                     /EC_number="4.2.3.1"
                     /GO_function="GO:0004795 - threonine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009088 - threonine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42439
     Region          83..399
                     /region_name="ThrC"
                     /note="Threonine synthase [Amino acid transport and
                     metabolism]; COG0498"
                     /db_xref="CDD:440264"
ORIGIN      
        1 mttislatgq rslgdpdisy plwpplthgc prtssdamsy pleidydytr vtsdfvtgqg
       61 rprsgldrwa pllpplaapg lgeggtplia igdgvyvkde srnptwshkd rlnritvsaa
      121 vavgapgvvv assgnhgasa aayaaraglr cvvlgsselp pavasflsay gavvlpveta
      181 rrwplteriv eefgfhpvsn ltpfhtghaf gaegyktvay eiaadivdpg avfvptgyge
      241 llfgiwkgft elhrlgllsr vprlfscepa aggplaaalr qglsatrvev adteaygiac
      301 pvnsyrgvra itgsggralt vddeamhraq aelagqglwv elssaaglag lrtlpddeti
      361 egpvvcvtts sgfkdtrvgd hrltpvdpsw esvrarlrae girs
//
LOCUS       WP_392004862            1402 aa            linear   BCT 20-JAN-2025
DEFINITION  Rne/Rng family ribonuclease [Streptomyces sp. NPDC014995].
ACCESSION   WP_392004862
VERSION     WP_392004862.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014995
  ORGANISM  Streptomyces sp. NPDC014995
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1402)
  AUTHORS   Kime,L., Jourdan,S.S. and McDowall,K.J.
  TITLE     Identifying and characterizing substrates of the RNase E/G family
            of enzymes
  JOURNAL   Methods Enzymol 447, 215-241 (2008)
   PUBMED   19161846
REFERENCE   2  (residues 1 to 1402)
  AUTHORS   Callaghan,A.J., Marcaida,M.J., Stead,J.A., McDowall,K.J.,
            Scott,W.G. and Luisi,B.F.
  TITLE     Structure of Escherichia coli RNase E catalytic domain and
            implications for RNA turnover
  JOURNAL   Nature 437 (7062), 1187-1191 (2005)
   PUBMED   16237448
REFERENCE   3  (residues 1 to 1402)
  AUTHORS   Li,Z., Pandit,S. and Deutscher,M.P.
  TITLE     RNase G (CafA protein) and RNase E are both required for the 5'
            maturation of 16S ribosomal RNA
  JOURNAL   EMBO J 18 (10), 2878-2885 (1999)
   PUBMED   10329633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1402
                     /organism="Streptomyces sp. NPDC014995"
                     /db_xref="taxon:3364936"
     Protein         1..1402
                     /product="Rne/Rng family ribonuclease"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=147794
     Region          <126..262
                     /region_name="rne"
                     /note="ribonuclease E; Reviewed; PRK10811"
                     /db_xref="CDD:236766"
     Region          638..1036
                     /region_name="CafA"
                     /note="Ribonuclease G or E [Translation, ribosomal
                     structure and biogenesis]; COG1530"
                     /db_xref="CDD:441139"
     Region          <1144..1287
                     /region_name="rne"
                     /note="ribonuclease E; Reviewed; PRK10811"
                     /db_xref="CDD:236766"
ORIGIN      
        1 mleptettes vtdsdsntps dtlpprrrrr aasrpagppa asadtpaetv apaipaaapa
       61 adlvtddsde ektdetaeaa gtpaaavdea vesaaepasa rprrratrra tapvgapapa
      121 eaaetvvpvt aaetpepvae vasaeditsv eesaavveda aprrsrrrat rrvsapaaag
      181 dtavaaveta eepvqepsve epvaeaasar prrratrrva apsgapkaae aeaetaevae
      241 epvtvqaeas aeaptetpaa eeaaprrtrr ratrrvaapa epaeaaeape aevpaaaevk
      301 apeapeaeaa kvseparape aaevpaaqad edaaprrgrr rvarkaavgf separpagee
      361 aeaprrparp avavfqppvf teprfqtpqr aaaeaaavga epvepepvea vepveelpee
      421 qtgarrrrrr rgagqgeeta eaavpavaed qaepeeadea edvvegddes eesgsrrrrr
      481 rggrrrrrge avegeageae aeelaaeqae qdaedtaeqe eedaeeghad etggstagsr
      541 rrrrrrrrag dgaaeaepde gdpertvvkv reprkaseps devqsikgst rleakkqrrr
      601 egreqgrrrv piiteaefla rreavervmv vrqngdrtqi gvledgvlve hyvnkeqsts
      661 yvgnvylgkv qnvlpsmeaa fidigkgrna vlyagevnfe algmangprr iesalksgqs
      721 vlvqvtkdpi ghkgarltsq vslpgrylvy vpegsmtgis rklpdtersr lktilkkivp
      781 edagvivrta aegasedelr rdverlqaqw ediqkkaksg naptllygep dmtvrvvrdi
      841 fnedftkvvv sgddawstih gyvshvapdl aerlsrwtse vdvfstyrid eqlakaldrk
      901 vwlpsggslv idrteamvvi dvntgkftgq ggnleetvtr nnleaaeeiv rqlrlrdlgg
      961 iividfidmv lesnrdlvlr rlleclgrdr tkhqvaevts lglvqmtrkr vgqgllesfs
     1021 etcvhcngrg vivhldqpss anggkrkkrg rggdgqaheh eavaaetaea vvavaaeaes
     1081 eaevaaeaaa plaleapdfa pdeelyssva eaeaaatrgr grrrasrras apagaprggs
     1141 rkavadeapm eaptaqdvtv eeeaerpvqp aeavaaqaep vavedpvvea aaaeapvvee
     1201 aapkgrtrrr atrkvsapag spagaeaavv tvaesapaev aaerpaepeg taeaeavaep
     1261 vvesaaparp rrravrkata ptapeetavv vvpsaaaeaa aepaaeapaq aaaenpaeap
     1321 adaeageepa eaapakkaaa rktakkatak kaattkktaa kktvakktaa kkttakkaak
     1381 ttakktaaaq qsvpsvsatt ed
//
LOCUS       WP_392004954             403 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC014995].
ACCESSION   WP_392004954
VERSION     WP_392004954.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014995
  ORGANISM  Streptomyces sp. NPDC014995
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  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 403)
  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
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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   5  (residues 1 to 403)
  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   6  (residues 1 to 403)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 403)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces sp. NPDC014995"
                     /db_xref="taxon:3364936"
     Protein         1..403
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41255
     Region          1..>61
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          81..391
                     /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 magtagapgt prvlramndr aaldlllahg plsrtrigrl tglskptasq llarleaagl
       61 vlatgttegg pgpnaqlyev npaaahaagl dvtpervlaa vadvtgrtvg thevptpgrk
      121 gtgavvrqvt ealdgavkaa gltrddvrrl vvatpgafdp gtgrlryash lpgwhsptll
      181 ddlaaalpmp veyendvnlv avaeqrlgaa rghddfvllw neaglgaalv lggrlhrgwt
      241 ggagevgflp vpgaplvrqv transggyqe lagsqaiprl arqlgitdip sgphaeaaaa
      301 lvrraatedt vphglllrty atrlatglas lvsvldpelv vlggaaltag gealralvqa
      361 eleelaasrp klvvgqvter pvlrgalesa laatrdevfd tsr
//
LOCUS       WP_392005858             289 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Streptomyces bacillaris].
ACCESSION   WP_392005858
VERSION     WP_392005858.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 289)
  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 289)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..289
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29837
     Region          23..284
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mpiaatgeli aeaaarrgav aafnvitleh aeaivegaea arapvilqis enavkyhggr
       61 lrplaraahe taraaavpva lhldhvhspe llhqaaecgf ssamfdaarl pyaenlaatr
      121 aaavwahgeg lrleaelgqv ggkngeppld ahapgartdp dealafvtat gvdalavavg
      181 tshamtsrda ridhdllarl rdavpvplvl hgssgasdee laravaggia kvnigtalni
      241 amtgairerl ardergvdpr pylaqgrdam artvtrmmav lssapvkpv
//
LOCUS       WP_392006216             245 aa            linear   BCT 20-JAN-2025
DEFINITION  4'-phosphopantetheinyl transferase family protein [Streptomyces
            bacillaris].
ACCESSION   WP_392006216
VERSION     WP_392006216.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459479
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..245
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=26349
     Region          25..232
                     /region_name="EntD"
                     /note="4'-phosphopantetheinyl transferase EntD
                     (siderophore biosynthesis) [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2977"
                     /db_xref="CDD:442216"
ORIGIN      
        1 mierllpayv scaatrevsv adgnlfpeee eliaravpkr rndfatarac arramgrlgl
       61 epvavlhgkr gmplwpegiv gslthcegyr aaalaragdv lslgidaeph aplpdgvael
      121 vvlpsererf aaaggeagdi hwdrllfsak esvfktwypl tlteldfeea dltfhreape
      181 gregeqagvg ssgravegtf sarllrtdpa vppvlegrwr iedgivatal llrpdrqega
      241 apqsp
//
LOCUS       WP_392006392             284 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces
            bacillaris].
ACCESSION   WP_392006392
VERSION     WP_392006392.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789410
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..284
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30528
     Region          6..283
                     /region_name="PrpB"
                     /note="2-Methylisocitrate lyase and related enzymes, PEP
                     mutase family [Carbohydrate transport and metabolism];
                     COG2513"
                     /db_xref="CDD:442003"
ORIGIN      
        1 mskrsttrlr qmiesdgihv apgaydglsa rlveesgsel lyasggaiar scgvpdigll
       61 sltevaarig qmvdvtslpv iadadtgfgn avnavrtlal yerigvagmh iedqtfpkrc
      121 ghlddkslvs tdemvrkiqa vgkartdpdf vliartdaia tegldaaier ahayveagad
      181 vifveapesv eqieriaari pqpklinmfh ggktplvpke rlrelgyrli iipsdlqrav
      241 itavrrtlea inrdgdsgav hedmasfaer erivrtadyl aigs
//
LOCUS       WP_392006530             273 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptomyces sp.
            NPDC014995].
ACCESSION   WP_392006530
VERSION     WP_392006530.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014995
  ORGANISM  Streptomyces sp. NPDC014995
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 273)
  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 273)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 273)
  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   4  (residues 1 to 273)
  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 273)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Streptomyces sp. NPDC014995"
                     /db_xref="taxon:3364936"
     Protein         1..273
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29591
     Region          15..252
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <140..251
                     /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 mtlrldeapt vvdagigvhg vstahdvfrl pdlwqlhlyh yvgalslgqs vhpirpghvs
       61 lvppntevhf hyrgrsehfy vhlrlhdggt arvvpvmqda aaesthladl lrhavtampt
      121 saprataevw talwriaelp rgegagrrhp fvaaaqayve ehlagplsvp dvaravgish
      181 thltrvfrae tgltvvsyir hrrlqrarhl llsstlsita vaaavgiadl qafnkacrre
      241 lgasprdvra aaptglgdrg phespietar qcr
//
LOCUS       WP_392007096             432 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces bacillaris].
ACCESSION   WP_392007096
VERSION     WP_392007096.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..432
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=47242
     Region          66..322
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mfdlarahan gdryllllgs dillrergiv salrtypgpv igmsetpaaq nanrffdhvl
       61 radyyderqa leavqqfere tglrpgavvp iiemtvhvsv avarhyglpr lsdaclakvr
      121 dkhtmkaafe aagvpcarhr lfgtleelhr aareldfplv lkprdfagnv gtvrvngpde
      181 ldeayvycrd slleiaplyg fedgrfqaee fvtsthevsv evanhrgert vvavtdkska
      241 gapyfsergq lvpsadsgne elrrvalaac aaldidhgla hvevlvdgdr lsvvevaarp
      301 ggdgimdlid rvygfspydl hfgsytdtld glpavtaept gmgataflka ppgtitevkp
      361 vhdltpeevg lyitaqvgdv srpltsylar dgvlecferg qsdqrafrak adelarqrte
      421 qiftveaehd rs
//
LOCUS       WP_392006726             319 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Streptomyces bacillaris].
ACCESSION   WP_392006726
VERSION     WP_392006726.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..319
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=33108
     Region          13..317
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mtavpssaap larpprlrpg arvavvapsg pvpadrleag lgvlrgwgle pvvmphvhdv
       61 hpdldhlagt dadraadlra awcdpsvdav fcarggygah rmvdlldwaa iraagpkvfv
      121 gysditalhe afalragyat lhgpmvater fledaptreh lratlfepeq vrtlgldtaa
      181 alvpgrargi lyggcvslla aaigtphars darggllaie dtgeepyrld giltrllrsg
      241 slaglagvvc gswqecgpye kvravladrf gplgipviee lgfghgptal tvplgvpavl
      301 dapadggrct ltvevpall
//
LOCUS       WP_392007116             244 aa            linear   BCT 20-JAN-2025
DEFINITION  TerD family protein [Streptomyces bacillaris].
ACCESSION   WP_392007116
VERSION     WP_392007116.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            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 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..244
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=27320
     Region          <13..241
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mgffdglwpa raaqfdagng tssaitlskr natvslskqg alsgnlrvnl swrmrtsdie
       61 grsrqsgrlr rplklfqpev vqahtqgvvn vdldlgcmye ladgtkgvvq plgnligdln
      121 sppyirlsgd drfgapsget vyvnldqrdq fkrllffvyi ydrtpafdrt hakitlypgn
      181 gprieielde rapqarscav ftvenvkdel ivrrevkfvy gfqseldrly gygmqwgrgy
      241 ksrt
//
LOCUS       WP_392007186             355 aa            linear   BCT 20-JAN-2025
DEFINITION  heme/hemin ABC transporter substrate-binding protein [Streptomyces
            bacillaris].
ACCESSION   WP_392007186
VERSION     WP_392007186.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Naoe,Y., Nakamura,N., Rahman,M.M., Tosha,T., Nagatoishi,S.,
            Tsumoto,K., Shiro,Y. and Sugimoto,H.
  TITLE     Structural basis for binding and transfer of heme in bacterial
            heme-acquisition systems
  JOURNAL   Proteins 85 (12), 2217-2230 (2017)
   PUBMED   28913898
REFERENCE   2  (residues 1 to 355)
  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   3  (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   4  (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   5  (residues 1 to 355)
  AUTHORS   Ho,W.W., Li,H., Eakanunkul,S., Tong,Y., Wilks,A., Guo,M. and
            Poulos,T.L.
  TITLE     Holo- and apo-bound structures of bacterial periplasmic
            heme-binding proteins
  JOURNAL   J Biol Chem 282 (49), 35796-35802 (2007)
   PUBMED   17925389
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..355
                     /product="heme/hemin 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=36100
     Region          84..352
                     /region_name="ChuT"
                     /note="ABC-type hemin transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG4558"
                     /db_xref="CDD:443619"
ORIGIN      
        1 mrisqdhgph qgqdagrpar gragaaltvl valallltgc ggggndsask pakgaadadr
       61 veplaaapap klpvtvdsad gkkvtidstd rivpltgsls eivftlgfgk qvvarditat
      121 feqaeklpvv trahdvsaes vlslkptvvl adtttgpaea idqirsagip llvvepakgl
      181 gdvgrridtv aealgvpaag telkertear iaavqktipd hadgkkprva flylrgsasv
      241 yllggaesga sslleaagav dagktsglkk dftaitseal akaapdaill mtkgfdsvgg
      301 mdglvkipgi aetpagmdrr vvtiddgvll nygprtdrvl adiveqlyak ggkgq
//
LOCUS       WP_392007239             336 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            bacillaris].
ACCESSION   WP_392007239
VERSION     WP_392007239.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 336)
  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 336)
  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 336)
  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 11448557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..336
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=38593
     Region          26..81
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
ORIGIN      
        1 mltdhhagag rsmdaqgeev tvdqaaedfa aevarwrevr gmskralara mgfdpsyvsh
       61 vesgrhkpse dfarladeal kagksiwrrw rtyekarvrt slmpsspsap hrpeqpyatd
      121 salvvqhdaa slqydgrsyr ltmrrllrnt gtepvtryli risvdrypgd peqsnahyra
      181 hpltwdeldl tatcrgekmr wqakhdrdaf kevwllfene hgrfplypge svwieyaytv
      241 ghekwgnwfq ravrlpteql evqlvfpaal dpvvwgtets mtaeasplrt ppirgdageq
      301 rtftwitttp alharyrlew rfraqpepds dqgefr
//
LOCUS       WP_392007263             269 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Streptomyces bacillaris].
ACCESSION   WP_392007263
VERSION     WP_392007263.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..269
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29604
     Region          18..259
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 mrgsetdgsa agprrstrih vvsdvhgnae dlaragegad aliclgdlvl fldyrdhsrg
       61 ifpalfgqen asrivalrta rrfeearafg relwagrdrh seilgavrqq yaelfaafpt
      121 ptyatygnvd vphlwpeyar pgttvldger veiggrvfgf vgggltspmn tpyeisdeey
      181 aakvealgpv dvlcshippe ipeltydtva rrfergsral leairttrpr yalfghvhqp
      241 lvrrmrigdt ecvnvghfas tgtpwaltw
//
LOCUS       WP_392007344             279 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            bacillaris].
ACCESSION   WP_392007344
VERSION     WP_392007344.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 279)
  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 279)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..279
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31171
     Region          17..71
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          93..273
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 manikqlnpa sspqaafgar irrfreergw tqdvlapkig yssqhisave tvrkpptlrf
       61 srksdhafgt tgtpesfere ymemrngsll egfpeyvgye graveirlfe vglipgllqt
      121 pdyaravayg dvergsitye qadqrvefla rrqealvrsq ppmvfvvmde sclhqavggs
      181 evmnaqlrrl eemsarpnwi iqvapfslge rrafdlpvyl ltmadrsiva yaesqaqgyv
      241 eretsvvapm fttyhqlqge slsktasaak isklrkgtp
//
LOCUS       WP_392007453             422 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces bacillaris].
ACCESSION   WP_392007453
VERSION     WP_392007453.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..422
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=45567
     Region          56..314
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 msdhivvlhr wrdrhahyen yldhrahrvt yvttelalds vpggaaaart vpatddldav
       61 wravtelrth fgvpervval negdldtaal vrerlgcagq tsgelarfrd kltmnrvtaa
      121 agipapafad apdeaavltf aqrhswpvvv kprrgtasrg vvrldseadl pllrtsppep
      181 rlvqefcadp ifhidglwtg eelgpwrasr yvntcvdftq gealgsvevd dpellgplga
      241 ftgrvaaalg pepwvfhlea fvgtsadgsp sirfleagyr vggaeipfvw revhgidlag
      301 aaadvqlgrr pelpvpeewr tggwllvpsp vpapcrvtaw dlpdpptpge gpytavipav
      361 gqvvprvggy ehvgarfrfr gassgdveka ilrtaaqfrl ecaperearg vrgaravcgl
      421 dr
//
LOCUS       WP_392007949             282 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            omiyaensis].
ACCESSION   WP_392007949
VERSION     WP_392007949.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces omiyaensis
  ORGANISM  Streptomyces omiyaensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 282)
  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 282)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces omiyaensis"
                     /db_xref="taxon:68247"
     Protein         1..282
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31033
     Region          17..68
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          90..264
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mvnirnldps aspldyygse lrrlreeagl nqaqlgsilf ctaslvgqie takkvptref
       61 serldaalmt gglftrlvgl vlksqlptwf qayaeleaka tyistyqsqm vygllqtegy
      121 aravlatglp dnledlvaar lerqrivsra nppliwvvld eaallrpmgg cavmrtqldr
      181 llsfadqrwv rvqvlpfaag ehasligsfn llrfdddpdv vytedliagh ttanpetvke
      241 aalryaglqa salsvedsae lilrvmeery gdqrgsepra la
//
LOCUS       WP_392008120             324 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            bacillaris].
ACCESSION   WP_392008120
VERSION     WP_392008120.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 324)
  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 324)
  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 324)
  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 18542080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..324
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35753
     Region          18..71
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
     Region          94..266
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mragkqsgtk rvtswqliga qlrllrkrag ltqaalaeqv rvgedtiasi eqgrrslqld
       61 laikldelle tkgvlqvave kipreeryqa lvkdfveyer davsllsyet qlipgllqte
      121 ayarlvfdcn yppveqelie krmaerlgrq kilerrpspv lhfileenil harlgapevm
      181 reqllhlrrc mdlpfvtiqi mpwnapghag lggpltllet sdhdqlayvs ghlharvyde
      241 padvsalmqr ygmlrsqals veksvrllda llaallgesc paqhtrppva ppsagsrpvk
      301 akataatask spptpppsts atpr
//
LOCUS       WP_392008337             402 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces omiyaensis].
ACCESSION   WP_392008337
VERSION     WP_392008337.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces omiyaensis
  ORGANISM  Streptomyces omiyaensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 402)
  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 402)
  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
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 402)
  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   5  (residues 1 to 402)
  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   6  (residues 1 to 402)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 402)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 402)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Streptomyces omiyaensis"
                     /db_xref="taxon:68247"
     Protein         1..402
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41546
     Region          18..>62
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          81..390
                     /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 magtqgtpgt prvlramndr aaldlllehg tlsrtrigkl tglskptasq llarleaagl
       61 vratgttegr pgpsaqlyal dpgagyaagl dvnqhriraa vaditgavtg eyelrtggrt
      121 gdgvvrqvtg aldgavkaag ltradvrrlv igtpgafdpa tgrlryashl pgwhsptlle
      181 elaavlpmpf eyendvnlva vaeralgaar ghedfvllwn eeglgaalvl ggrlhrgftg
      241 gagevgflpv pgtplvrqvt kansggfqel agvqsvpgia raagidtpdr pyvpvasgll
      301 araaetpdeg pyaelldrya ervatglasl vavldpelvv lsgdvlvagg eplrarvqae
      361 ladlaasrpr lvltavphep vlrgalesal attrdevfdt sr
//
LOCUS       WP_392008426             403 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC015140].
ACCESSION   WP_392008426
VERSION     WP_392008426.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015140
  ORGANISM  Streptomyces sp. NPDC015140
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  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 403)
  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
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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   5  (residues 1 to 403)
  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   6  (residues 1 to 403)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 403)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces sp. NPDC015140"
                     /db_xref="taxon:3364943"
     Protein         1..403
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41554
     Region          1..>61
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          81..391
                     /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 magtagtpgt prvlramndr aaldlllehg plsrtrigkl tglskptasq llarleaagl
       61 vlaggttegr pgpgaqlyev npaaayaagl dvtpdrvlaa vadvtgrtvg rfelptpgrr
      121 pvapvvqqvt daldgavkaa glaradvhrl vigtpgafdp gtgrlryash lpgwhsptll
      181 delaaalpmp veyendvnla avaeqrlgaa rghedfvllw nqeglgaalv lggrlhrgwt
      241 ggagevgflp vpgaplvrkv srtgsggfqe lagsqalpgl arelgltglp pgpyheaaaa
      301 lvaraaeadd ephrrllqty atrlatglas lvsvldpelv vlsgtslaag getlrdlvqd
      361 eleelaasrp rlvvgevtdh pvlrgalesa lattrdevfd tsr
//
LOCUS       WP_392008496            1315 aa            linear   BCT 20-JAN-2025
DEFINITION  Rne/Rng family ribonuclease [Streptomyces sp. NPDC015140].
ACCESSION   WP_392008496
VERSION     WP_392008496.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015140
  ORGANISM  Streptomyces sp. NPDC015140
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1315)
  AUTHORS   Kime,L., Jourdan,S.S. and McDowall,K.J.
  TITLE     Identifying and characterizing substrates of the RNase E/G family
            of enzymes
  JOURNAL   Methods Enzymol 447, 215-241 (2008)
   PUBMED   19161846
REFERENCE   2  (residues 1 to 1315)
  AUTHORS   Callaghan,A.J., Marcaida,M.J., Stead,J.A., McDowall,K.J.,
            Scott,W.G. and Luisi,B.F.
  TITLE     Structure of Escherichia coli RNase E catalytic domain and
            implications for RNA turnover
  JOURNAL   Nature 437 (7062), 1187-1191 (2005)
   PUBMED   16237448
REFERENCE   3  (residues 1 to 1315)
  AUTHORS   Li,Z., Pandit,S. and Deutscher,M.P.
  TITLE     RNase G (CafA protein) and RNase E are both required for the 5'
            maturation of 16S ribosomal RNA
  JOURNAL   EMBO J 18 (10), 2878-2885 (1999)
   PUBMED   10329633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1315
                     /organism="Streptomyces sp. NPDC015140"
                     /db_xref="taxon:3364943"
     Protein         1..1315
                     /product="Rne/Rng family ribonuclease"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=138568
     Region          <323..434
                     /region_name="MSCRAMM_ClfA"
                     /note="MSCRAMM family adhesin clumping factor ClfA;
                     NF033609"
                     /db_xref="CDD:468110"
     Region          555..958
                     /region_name="CafA"
                     /note="Ribonuclease G or E [Translation, ribosomal
                     structure and biogenesis]; COG1530"
                     /db_xref="CDD:441139"
ORIGIN      
        1 mlepteptes sttstdsesn tpsdtlpprr rrraasrpag ppsggsdapa etvapaevta
       61 atdeaeetee teaaqaaapa peaaparprr ravrrasapa gtptsteaae tvvaapsgae
      121 apvaepvaea gevtedpapr rsrrratrsv ttpaepaaae taeatpaapa aadaaaaaap
      181 aagteaedaa pkgrtrrrat rrvtapaeap aeaaaevrep tpepvreaap eaakdaepae
      241 daaprrarrr strkaaggfa apaqtaasdd adapkrpsrp avavfqapvf aepqfqtper
      301 aaaeaaaeaa gaapakpaev aeeqseeqsa gsrrrrrrrg aaeegtedrt paaaqeeret
      361 dtradsdadt eadadsdesg edhddadgse dsgsrrrrrr ggrrrrrgds adgdlndges
      421 eqtadqaeqd gadtaeqaee daeesaesag dgggssssrr rrrrrrragd gsgdgdastd
      481 dpertvvkvr eprpprekse psdevqsikg strleakkqr rregreqgrr rvpiiteaef
      541 larreaverv mvvrqhgert qigvledgvl vehyvnkeqa tsyvgnvylg kvqnvlpsme
      601 aafidigkgr navlyagevn fealgmangp rriesalksg qsvlvqvtkd pighkgarlt
      661 sqvslpgryl vyvpegsmtg isrklpdter srlktilkki vpedagvivr taaegasede
      721 lrrdverlqa qwediqkkak sgnaptllyg epdmtvrvvr difnedfsqv vvsgddawqt
      781 ihgyvshvap dladrlskwt sevdvfatyr ideqlakald rkvwlpsggs lvidrteami
      841 vvdvntgkft gqggnleetv trnnleaaee ivrqlrlrdl ggiividfid mvlesnrdlv
      901 lrrlleclgr drtkhqvaev tslglvqmtr krvgqglles fsetcvhcng rgvivhldqp
      961 taaggggggs krrkraraga dqpheheava gvetgptaeq eadtesesev aaevaepval
     1021 papdftadee lyssaaeaea aatrgrgrrr asrrasapag apkagkgeae raegptaqdv
     1081 tvqeeverpv rresatevla epaavedava gghvtapaea papaaeeaap kgrtrrratr
     1141 kvsapagspa gaeaavvtvp etapapqaeq apqapaeapa epaaeeaapa rprrravrks
     1201 taptaseeaa vmvvpsagpe eeraeqaapd tetaeeaapa kkaaarktak katakkaatk
     1261 ktaakkttta kkatakkaak tttakkttak ktaskktaaa aqqapssvta atdeg
//
LOCUS       WP_392009097             424 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC015140].
ACCESSION   WP_392009097
VERSION     WP_392009097.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015140
  ORGANISM  Streptomyces sp. NPDC015140
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 424)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Streptomyces sp. NPDC015140"
                     /db_xref="taxon:3364943"
     Protein         1..424
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=44674
     Region          59..234
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          253..372
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 msdtvhfqar grtvvgctll vmalgagvta ctdddnplsa spydaagqis fngpkdagkk
       61 adpdkplevv aegadgritd vtamdasgry vagelsadga rwhstsplaa nasytvrvst
      121 edgdgapgrk vltfetgkpg akktlgitfg pkagaygvgq pvtaelsqpv rdkaqraive
      181 ralkvdstpa vegawhwvdd kklhyrpkef wpahatiqvr stldgikvgd rmwggaakpl
      241 kittddrvva vtdaaahtlt vfqdgkeikq ipvttgkpgf dtrngvkvvl gkeafvrmrs
      301 ttvgiaegss esydlpvhfa trvtwsgeyv haapwsvgsq gsanvshgcv gmstanaewf
      361 fkavqegdlv evvnsggemm epfgngfgdw nldwnkwrtg saltggggsa snnqetarlr
      421 ptvv
//
LOCUS       WP_392009380             235 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Streptomyces bacillaris].
ACCESSION   WP_392009380
VERSION     WP_392009380.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 235)
  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 10007985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..235
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=25131
     Region          35..225
                     /region_name="COG3786"
                     /note="L,D-peptidoglycan transpeptidase YkuD,
                     ErfK/YbiS/YcfS/YnhG family [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443000"
ORIGIN      
        1 mrrplltlav llalatgslg aapadtpppl pyrladtggg sqlitaeapd tgsttgtvtw
       61 werrggrwte kgsaparfga nglaegasre qgtsttptgl ydlpyafgie dapagtrypy
      121 rkvnddswwc qdnasraynr wveprpdhcr adeaeqlvty gtqyaralvi gfnydrpvrg
      181 rgagiflhvn grgatagcvs vpaeamaeil awvrperrph iavgtssgpt aitry
//
LOCUS       WP_392009594             302 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Streptomyces bacillaris].
ACCESSION   WP_392009594
VERSION     WP_392009594.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..302
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32515
     Region          1..296
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mlldtaslyf rayfgvpdsv rapdgtpvna arglldfiar lvqdhrpdel vacwdndwrp
       61 qwrvdlipty kahrvaeetp agqtdeeeip dtlspqvpii edvldalgia rvgvtpyead
      121 dvigtltara tgpvdivtgd rdlyqlvdda rqvrvlyplk gvgtlqltde awlrekygvd
      181 gagyvdlall rgdpsdglpg vpgigektaa klldaygdla gimaavgdpk akltpsqrkr
      241 ldeardyvav apkvvrvaad vplpdfdpal preprdpaal ealagqwglg galqrllttl
      301 ra
//
LOCUS       WP_392009724             543 aa            linear   BCT 20-JAN-2025
DEFINITION  peptide ABC transporter substrate-binding protein [Streptomyces
            omiyaensis].
ACCESSION   WP_392009724
VERSION     WP_392009724.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces omiyaensis
  ORGANISM  Streptomyces omiyaensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 543)
  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 543)
  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 543)
  AUTHORS   ter Beek,J., 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 543)
  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 543)
  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 11467924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Streptomyces omiyaensis"
                     /db_xref="taxon:68247"
     Protein         1..543
                     /product="peptide 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=58538
     Region          27..530
                     /region_name="OppA"
                     /note="ABC-type oligopeptide transport system, periplasmic
                     component [Amino acid transport and metabolism]; COG4166"
                     /db_xref="CDD:443327"
ORIGIN      
        1 mskhtmnpsr stalaaaavl tvvasatacg sgeptkpkna pgkpggaysv altepdhllp
       61 grttssyslq vlqglfdppa aldpgngsvk plaavswstt dntvwtikfr sgttfhngek
      121 vtaasfadaw naaaygpnaw danyyfaqie gydalnpsee gakpsartls glkvldettl
      181 qvtlkapfgq fpmllsfpaf aplpkaatan pdaadvapig ngpyridgaw ernqkirlak
      241 fadyrgprkp madrvdfkiy tsretaftel qagnvdvltt vpaansaqak rlfgerfsir
      301 psgtmdylgl pvkdprfadp rlrkalsmai drkgitqaiy ngvykpatsl vgdmipghrt
      361 dacgptcayd paaakrlfea aggfdgplel hfsnadptye qwmtsianql kdnlgiqdvt
      421 frkmapadls allnegknkg pfrqnwvidy psiqnyldgl yypgnrsgws deqfdalvak
      481 gnaaqgaeai aayqkaedia lrelpyiplw nwqdqsawsd riddvvidpy aaglhldrvt
      541 vsd
//
LOCUS       WP_392009958             466 aa            linear   BCT 20-JAN-2025
DEFINITION  alpha,alpha-trehalose-phosphate synthase (UDP-forming)
            [Streptomyces bacillaris].
ACCESSION   WP_392009958
VERSION     WP_392009958.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 466)
  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 466)
  AUTHORS   Eastmond,P.J. and Graham,I.A.
  TITLE     Trehalose metabolism: a regulatory role for trehalose-6-phosphate?
  JOURNAL   Curr Opin Plant Biol 6 (3), 231-235 (2003)
   PUBMED   12753972
REFERENCE   3  (residues 1 to 466)
  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   4  (residues 1 to 466)
  AUTHORS   Elbein,A.D., Pan,Y.T., Pastuszak,I. and Carroll,D.
  TITLE     New insights on trehalose: a multifunctional molecule
  JOURNAL   Glycobiology 13 (4), 17R-27R (2003)
   PUBMED   12626396
REFERENCE   5  (residues 1 to 466)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 929-939 (1997)
   PUBMED   9334165
  REMARK    Erratum:[Biochem J 1998 Feb 1;329(Pt 3):719]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..466
                     /product="alpha,alpha-trehalose-phosphate synthase
                     (UDP-forming)"
                     /EC_number="2.4.1.15"
                     /GO_function="GO:0003825 - alpha,alpha-trehalose-phosphate
                     synthase (UDP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0005992 - trehalose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51113
     Region          13..465
                     /region_name="OtsA"
                     /note="Trehalose-6-phosphate synthase, GT20 family
                     [Carbohydrate transport and metabolism]; COG0380"
                     /db_xref="CDD:440149"
ORIGIN      
        1 mvtehgeata pstaqvlvas nrgpitytlg edgtldakrg ggglvsglsa vddklwvcaa
       61 lgdgdreavr rgvgepgvrm ldidaevhad ayngiansvl wfvhhllyqt pvepvfdaef
      121 rrqwasyety nrafaqalae eagegaavlv qdyhlalvpg mlrelrpdlr ighfshtpwa
      181 pvdyfrllpd digeqllrgi lgadraaflt rrwadafigc cteilggtgr trigvhglga
      241 dadflrrrsr eadvdermaa lreqvgenrk tivrvdrtel sknivrglha yrallethpe
      301 wrervvhvaf aypsrqdlav yrdytaavqs lateingayg teswtpvvlh vkddfarsla
      361 ayrladvalv npirdgmnlv akevpvvsdh gcalvlsrea gayeelgeda ivvnpydvtg
      421 taealheals mgaeertgrt krlaeaatal ppqrwfldql ealrqe
//
LOCUS       WP_392010074             439 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015140].
ACCESSION   WP_392010074
VERSION     WP_392010074.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015140
  ORGANISM  Streptomyces sp. NPDC015140
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 439)
  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 439)
  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 439)
  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 10611723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Streptomyces sp. NPDC015140"
                     /db_xref="taxon:3364943"
     Protein         1..439
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43666
     Region          17..73
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(23,27,52)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(26,51)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(33..34,45,48,52..53)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          <120..265
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          337..420
                     /region_name="DUF2690"
                     /note="Protein of unknown function (DUF2690); pfam10901"
                     /db_xref="CDD:402475"
ORIGIN      
        1 mprwkalpee ldpqikeftg qlrrlvdrsd lsvasvadat gysktswery lngrllapkg
       61 aiialaevtg tnplhlttmw elaerawsrs emrhdmtmea irisqaraal gdlgtasgkt
      121 agpghggrns rgsrsgrhgg gasatsgvag pagvaptlgp tvpaqptaad spdaaagpvr
      181 gggttgspsv pfsgdpspgg atdgnswgla gyrgpaptgd rtarpghrag sgeaatamgp
      241 aatpgpaape grspsagyge pphggpgsrg rsngggsrrm ttfvagvvgv lvviagaffl
      301 lndggdkkne gtkpspsptv sseqqlppgv kcsgdactgk dpeamgcggd lvttaatatv
      361 gttavevrys ktcgtawarv tqaaqgdkvq vsaegrnqqt gtvsgvgdtv aytpmvavks
      421 aaaaeacvtt asgvqgcte
//
LOCUS       WP_392010743             438 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces bacillaris].
ACCESSION   WP_392010743
VERSION     WP_392010743.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..438
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=48872
     Region          49..332
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mpddsrknif vigmdeanrr tleavpdadr hrlhplltie elqegqvtvd ellararavl
       61 daheggidai vgywdfpvst lvpllseeyr tvstslesvv kcehkywsrl eqrkvtdayp
      121 rfgmvdlesd dprppeglrf pmwvkpalay sselafgvad laefrsavae iregiarvgk
      181 pfeaildlle lppemagvgg evclaeeamt giqvavegyv hrgevtvygv ldsinypgss
      241 sflrhqypst lpapvirrlh evsertmrqi gmdratfsie yfydpktadi rlleinprhs
      301 qshaemfqfv dgvpnhhrmf rlvlggdpav ppgggryrva akwyyrwfge grvhrvptae
      361 dlaaiereip gvhidmvpae gqrlstvhgq dsysyevahi ftggddeddl rrkfdacvaa
      421 lgltfdetep ggrgrngs
//
LOCUS       WP_392010518             934 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces sp. NPDC015140].
ACCESSION   WP_392010518
VERSION     WP_392010518.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015140
  ORGANISM  Streptomyces sp. NPDC015140
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 934)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 934)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..934
                     /organism="Streptomyces sp. NPDC015140"
                     /db_xref="taxon:3364943"
     Protein         1..934
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=99074
     Region          658..933
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mkqqgvhped aegtsdassr pdtadgsggk sarraaagrs ataadpddva hidevegdep
       61 llparvhrps dlmrllvgvl avavllavaa fahgttsgle qdinkgtgqa pdllikiagl
      121 assiaillvp vafaierlik rdglriadgv laavlahgvt latdlwvaka apgsiqealt
      181 qpspgdihal tdpvhgylap viaymtavgm srrprwravl wivllldafs mlvtgyttpf
      241 siiltvligw tvaygtlyav gspnvrptgr tlmaglrhvg frpvtaaree apadsvetgd
      301 rgrryfvtle dghpldvtvv dreqqaqgff yrawrnltlr gfatrsslps lrqaleqeal
      361 layaaigaga napkliatse lgpdavmlvy ehtggrtlds lpdeeitdel lrgtweqvqa
      421 lqsrriahrr lvgdailvdr sgaviltdlr igeiaagdll lrmdisqllv tlglrvgaer
      481 avasavgvlg pdavadclpm lqpialsrst ratlrrlare raerereavl essrqaklar
      541 aeaaagedag dtpeksvqlt ktedtgktek tdksdkkaar aeqraekrav eealeearee
      601 dlltlirhav lrirpqapve parlervrpr tlisfiagai gayflltqlt hiefgplisn
      661 aewgwvaaav lfsaasyiaa amallgfvpe rvpflrtvaa qvagsfvkiv apaavggval
      721 ntrflqragv rpglavasvg asqlfglgch ilmlmafgyl tgtektpsls psrtviagll
      781 tvavlvlvvt svpflrkfvv trvrslfagv vprmldvlqr pqklitgigg mllltacfvm
      841 cldasirafg ddstsislas vavvflagna lgsaaptpgg vgaveatltv gliavglpke
      901 vaapavllyr lltlwlpvlp gwlmfnhltr keal
//
LOCUS       WP_392010956             458 aa            linear   BCT 20-JAN-2025
DEFINITION  SWIM zinc finger family protein [Streptomyces bacillaris].
ACCESSION   WP_392010956
VERSION     WP_392010956.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Hassan,I.U., Rehman,H.M., Liu,Z., Zhou,L., Samma,M.K., Wang,C.,
            Rong,Z., Qi,X., Cai,D. and Zhao,H.
  TITLE     Genome-wide identification and spatiotemporal expression profiling
            of zinc finger SWIM domain-containing protein family genes
  JOURNAL   Zool Res 44 (3), 663-674 (2023)
   PUBMED   37161653
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     SWIM, a novel Zn-chelating domain present in bacteria, archaea and
            eukaryotes
  JOURNAL   Trends Biochem Sci 27 (8), 384-386 (2002)
   PUBMED   12151216
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10516955
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..458
                     /product="SWIM zinc finger family protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48064
     Region          412..444
                     /region_name="SWIM"
                     /note="SWIM zinc finger; pfam04434"
                     /db_xref="CDD:309540"
ORIGIN      
        1 mtrsvqalay arpsalessq ggaslgleta ggltprgaea hprffagfls apriaargll
       61 avadvaaary yqrtlassld pvvtgngdrl rfesfsgccg vyarldvlqe glegertghg
      121 ttnvdvnnpl rdalsritad dplhlrvgpe elavttvdgp lvekkvplpd rwlrgfaeaq
      181 vasagfdlra elsaaqavaf lrslprrsgn aargaqwvva sgsalrpttr pvpgavclpg
      241 perlvalerv lrhatalrvy gpavadgapv asawevvlpg mrltltlspd aargfsgegg
      301 vlealatdea aadaelvsvl laweptiepa slaeqsglsv ervraaltrl gtagrvgydl
      361 adaayfhrel pydadraerh nprlvaarel agagavsldg avasvasgdr ryqvresdgr
      421 ltctcqwwad yrgkrgpckh alavtmvrrg atvaggvr
//
LOCUS       WP_392011416             131 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TOBE domain-containing protein [unclassified
            Streptomyces].
ACCESSION   WP_392011416
VERSION     WP_392011416.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 131)
  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 10007583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..131
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13768
     Region          1..128
                     /region_name="MopI"
                     /note="Molybdopterin-binding protein MopI [Coenzyme
                     transport and metabolism]; COG3585"
                     /db_xref="CDD:442804"
ORIGIN      
        1 mqaytigqaa rllgvspdta rrwadagrvt thrdeggkrl idgkdlaafs velaqsgsge
       61 edasytsvrn afpgivtaik lgdvaaqvei qagphrlvsl ltreaveelg levgmeatar
      121 vkstnvhvdr a
//
LOCUS       WP_392011753             430 aa            linear   BCT 20-JAN-2025
DEFINITION  M20 metallopeptidase family protein [Streptomyces omiyaensis].
ACCESSION   WP_392011753
VERSION     WP_392011753.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces omiyaensis
  ORGANISM  Streptomyces omiyaensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Lindner,H.A., Lunin,V.V., Alary,A., Hecker,R., Cygler,M. and
            Menard,R.
  TITLE     Essential roles of zinc ligation and enzyme dimerization for
            catalysis in the aminoacylase-1/M20 family
  JOURNAL   J Biol Chem 278 (45), 44496-44504 (2003)
   PUBMED   12933810
REFERENCE   2  (residues 1 to 430)
  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 11444961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Streptomyces omiyaensis"
                     /db_xref="taxon:68247"
     Protein         1..430
                     /product="M20 metallopeptidase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45213
     Region          9..423
                     /region_name="AbgB"
                     /note="Metal-dependent
                     amidase/aminoacylase/carboxypeptidase [General function
                     prediction only]; COG1473"
                     /db_xref="CDD:441082"
ORIGIN      
        1 mtadpvhael drlseeaaaq viawrrhlhr npelsnreeg tarlvaehlr qlgldevrtg
       61 iaghgvvgvl rgtaagggrv aalradtdal pvkdlcgtdf asrvvdadyp ggpfpvshac
      121 ghdchtamlm gaatvlagvr drlpgtvllv fqpaeegppv tetggalamv dagafadpvp
      181 tmafgmhvtp ypkgyvgyrv gnqygasvlv ritvtgrqvh gstpwqgvdp mpavgavltg
      241 igqlyrqvsa fdpvtvtigh vedvgrfnii getvtlwgtv rcavegdmpa vrdrlrrlae
      301 hsaaaygata eveylqpvpp vhntgpwvaa alptlrrvag gervtetgat lgyddvselv
      361 srfgglyvml gvqdatlgen glpvpeeggr glvtnhnprf yadddtlvtg vrlhahvayd
      421 hlagtllpae
//
LOCUS       WP_392011695             574 aa            linear   BCT 20-JAN-2025
DEFINITION  complex I subunit 4 family protein [Streptomyces bacillaris].
ACCESSION   WP_392011695
VERSION     WP_392011695.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 574)
  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 574)
  AUTHORS   Galemou Yoga,E., Angerer,H., Parey,K. and Zickermann,V.
  TITLE     Respiratory complex I - Mechanistic insights and advances in
            structure determination
  JOURNAL   Biochim Biophys Acta Bioenerg 1861 (3), 148153 (2020)
   PUBMED   31935361
REFERENCE   3  (residues 1 to 574)
  AUTHORS   Friedrich,T. and Scheide,D.
  TITLE     The respiratory complex I of bacteria, archaea and eukarya and its
            module common with membrane-bound multisubunit hydrogenases
  JOURNAL   FEBS Lett 479 (1-2), 1-5 (2000)
   PUBMED   10940377
REFERENCE   4  (residues 1 to 574)
  AUTHORS   Walker,J.E.
  TITLE     The NADH:ubiquinone oxidoreductase (complex I) of respiratory
            chains
  JOURNAL   Q Rev Biophys 25 (3), 253-324 (1992)
   PUBMED   1470679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..574
                     /product="complex I subunit 4 family protein"
                     /GO_component="GO:0045271 - respiratory chain complex I
                     [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048039 - ubiquinone binding [Evidence
                     IEA]"
                     /GO_process="GO:0015990 - electron transport coupled
                     proton transport [Evidence IEA]"
                     /GO_process="GO:0042773 - ATP synthesis coupled electron
                     transport [Evidence IEA]"
                     /calculated_mol_wt=59257
     Region          14..571
                     /region_name="NuoM"
                     /note="NADH:ubiquinone oxidoreductase subunit 4 (chain M)
                     [Energy production and conversion]; COG1008"
                     /db_xref="CDD:440632"
     Region          <482..>551
                     /region_name="rad23"
                     /note="UV excision repair protein Rad23; TIGR00601"
                     /db_xref="CDD:273167"
ORIGIN      
        1 mtvidispsv mqfllafivv apllgavaal lpappglkgr npdqavlrhg vtvtgavlia
       61 aivlatgfdh dhpatmqatt diswipaldv rihlgidgis lplllltall tflcalysyf
      121 kppagpspka ftalvlvles gtlatfavld lllfflafem vlipmyflia rwggdqrraa
      181 awkfilytll gsvvmllgll liglrsgtfd mvalatdngr glttsvqvia vlaigvglav
      241 ktpmwplhsw lpdahtaapt vgsvllagvl lkmgtygfvr illpvapdgm htfapylaaf
      301 avvgivygsl aclalarkga kgdlkrliay ssvghmgfvl lgiatmtptg vngalfania
      361 hglitgllff lvgavkdryg tadldtlaga tgaalygrap rlgallafaa vaslglpgla
      421 gfwgemltlf gayspaegls rpafrtfmai gafgtlltaa ymlivvrrvc mgehtphsel
      481 spaatpadap esadapepad apgpsgtgps attpprpaap qpgattpqla diqtyeavtw
      541 tplaaltvla glwpavllgl tdpavqklla ggks
//
LOCUS       WP_392012129             251 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces sp.
            NPDC015140].
ACCESSION   WP_392012129
VERSION     WP_392012129.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015140
  ORGANISM  Streptomyces sp. NPDC015140
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616714
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Streptomyces sp. NPDC015140"
                     /db_xref="taxon:3364943"
     Protein         1..251
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25264
     Region          4..230
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 mtgfaalhrp geplllpcaw dhasahalaa rgfgavgtts lgvaaanglp dgaaatrdet
       61 lrlaltlgsg pflltvdaes gfaddpddvg efarqlaavg avginledal gpadrhaaki
      121 aavrsaapgl fvnartdtyw sgdgdpgetv rrleayreag adgvfvpglt dpariaslaa
      181 hfdvplnilh spagptlphl adlgvarvsl gsllyrralg aaletvadia agrppegtap
      241 ayeevtalsg g
//
LOCUS       WP_392012264             335 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            bacillaris].
ACCESSION   WP_392012264
VERSION     WP_392012264.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (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
REFERENCE   4  (residues 1 to 335)
  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 11448557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..335
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=36063
     Region          38..99
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
ORIGIN      
        1 madhhpirpa rpgpsvpssp sspdalspqg rgrppsafgq alrearerkg ltlarlrdhl
       61 arrgvrvstv tlshwqrgrs qperpeslra vsaiesilgc paggllallg prrprgrplp
      121 tpperlenar pvygpeplla ralgeeefsr lnegtvpvsv qetvhldrtg rtarhtvtqv
      181 vrathdgadh vtahlnvdep pgppmtasaq cgvlldqrcv palglttlri gfgrplarge
      241 stvvaytvdl gphghrtthh eralplhvrh yflhvvfhpe alpasvygyy rahdgaprad
      301 irtlplsgsg tahilpadaa agvhgifwkw pgttt
//
LOCUS       WP_392012371             398 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            bacillaris].
ACCESSION   WP_392012371
VERSION     WP_392012371.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 398)
  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 398)
  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 398)
  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 10611723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..398
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=40204
     Region          17..79
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(23,27,52)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(26,51)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(33..34,45,48,52..53)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          <107..>224
                     /region_name="PTZ00395"
                     /note="Sec24-related protein; Provisional"
                     /db_xref="CDD:185594"
     Region          298..377
                     /region_name="DUF2690"
                     /note="Protein of unknown function (DUF2690); pfam10901"
                     /db_xref="CDD:402475"
ORIGIN      
        1 mprwkalpde ldpqirefas rlrrivehsg ldvnavadrt gfsatawery lsgqllpprr
       61 avvaladvtg tpqhhltalw etaerawsra gtrqdvatet lrirqvggap gsaeaagaap
      121 rgatatgtsd hggpgghdsg ayaddpyang pyangpfang pygngpfang pyandpygsd
      181 pygndphhpd gdgraphipa qrgsgapdpq qqprqgvrrn gppgggsnav mlgvgavgal
      241 ivitgavmla pgdepakatp ttaattpaat ptdggpagga seepaalpdg vecrgdecag
      301 qnpdamgcgg ehartvttta igtarvevry sevcsaawar lteagpgdtv titgsaaaaa
      361 qngrvsvrea ytpmvaveka adakacatlt sgtkgctt
//
LOCUS       WP_392012715             298 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            bacillaris].
ACCESSION   WP_392012715
VERSION     WP_392012715.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..298
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=32787
     Region          28..276
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 msgvllrgrd epgegraedv tgdggssrlt irlfgplhvs rgattlelgp pkqrallavl
       61 llrpgmetgv dqltealwge eypayaknli qksvsglral lqpggegerg avihwsgggy
      121 rldagdadvd fytyerlavt glaaahdgrl qeasellera rtmstgplve gldgpmmere
      181 rlfrqerflt dmevlaevel qlgrhrhavp llhyavhkyp lrerfawllm lalhrsdrgs
      241 ealvvyaqhr arlvaelgse pgpalralha rllaqdpelm elptlredsp gdryrvps
//
LOCUS       WP_392013899             398 aa            linear   BCT 20-JAN-2025
DEFINITION  threonine synthase [Streptomyces omiyaensis].
ACCESSION   WP_392013899
VERSION     WP_392013899.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces omiyaensis
  ORGANISM  Streptomyces omiyaensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 398)
  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 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
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Parsot,C.
  TITLE     Evolution of biosynthetic pathways: a common ancestor for threonine
            synthase, threonine dehydratase and D-serine dehydratase
  JOURNAL   EMBO J 5 (11), 3013-3019 (1986)
   PUBMED   3098560
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423064
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Streptomyces omiyaensis"
                     /db_xref="taxon:68247"
     Protein         1..398
                     /product="threonine synthase"
                     /EC_number="4.2.3.1"
                     /GO_function="GO:0004795 - threonine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009088 - threonine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40786
     Region          79..398
                     /region_name="ThrC"
                     /note="Threonine synthase [Amino acid transport and
                     metabolism]; COG0498"
                     /db_xref="CDD:440264"
ORIGIN      
        1 mtslaraqrs ladpsvrhpl wppltagcpv tsteevaypl eveydydavp adlfdapaah
       61 glerwapllp plaapglgeg ntplvrladg vwvkdesrnp twshkdrlnr vavsaaaasg
      121 argvvvsssg nhgaaaaaya araglpcavf tppdappava shlraygatv ltvphaavrp
      181 lmrrivdelg fqsvssvtds ahtghpfgpe gyktiayeia lalgrapaav hvptgygell
      241 fgvakgfqel arlgatgsvp rmygvepaaa galtealrsg rpvarvpvgp taayaidcev
      301 nsyqgvlavr rtgggartvt edrlaaarse laaqgvwcev saaaglaglr ahgpdpaged
      361 gpvvcvvtss gykdvatgse avapmdadwd avrallar
//
LOCUS       WP_392014109             223 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces chartreusis].
ACCESSION   WP_392014109
VERSION     WP_392014109.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces chartreusis
  ORGANISM  Streptomyces chartreusis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Streptomyces chartreusis"
                     /db_xref="taxon:1969"
     Protein         1..223
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23876
     Region          2..213
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 mssrerilgr vrraladvpr eeapyeeavp rdylrehgdr svaqtvdlla enladyraiv
       61 hrctpadlap tiagmlaarg aksvlvppgl dtgwlaaada eriadrpest pheldevdsv
      121 vtacavavae tgtivldgsp dqgrrritlv pdhhicvvrv peqvvssvpq alerldpvrp
      181 ltwisgpsat sdieldrveg vhgprtlevv lvgedqssad vta
//
LOCUS       WP_392014324             988 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            omiyaensis].
ACCESSION   WP_392014324
VERSION     WP_392014324.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces omiyaensis
  ORGANISM  Streptomyces omiyaensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 988)
  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 988)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 988)
  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 988)
  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 18640657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..988
                     /organism="Streptomyces omiyaensis"
                     /db_xref="taxon:68247"
     Protein         1..988
                     /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=102971
     Region          <647..848
                     /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          805..987
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          929..983
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mttvphgplp arapgaagpp apvgreellt rlesvlharg ralltgpagv gktevalaaa
       61 araeargetv lwlaalpadr aipgaaaaal vasvaatvar pgprtepgpp gedgpahpdg
      121 spvpgasgal psgvfasgvf ddlpgpqrta vamlcreapi qqggwdpial rlgiarilrv
      181 ltsrgpvllv vdgaefldpd stdllrfalh lappslrvva vetpepygdt hradgpgpga
      241 ghtahlwvps eadlllvppl hadeiaelli hhrlpsrmag rihrasggnp rlalavgrsl
      301 adartpvhha ealtlsgrar dlarqllgaa pppvratlll aalalrpsat lvrragrpea
      361 eaelaaaera glvslaedgs lvftagllps tlvhdacwae rsaghaalae vvddpveavr
      421 hralasdrpd eelaaevaaa aeaarrrgnn tlaaelalla aestpgrdgv rriarlvdaa
      481 eeaaraarad lamrattdll ardasptdrv rarlavldta gqgltdlddm yvhamedseg
      541 etalraavql rlavkyvlad gdpersrtaa mesaalaasv gdprtaaqal tvqarmeral
      601 gspdaepvla rarelelaer plgirnaaqi ltirhalfdd rltdardeln allplvqrrg
      661 svedaielyr tlaeiesrig tcpaalahag qslaltleag lspgpawyal alaetaggsl
      721 graasyarrs vqaseeegdr vflsrsryal grvqlingdv aaaletlrrv qaderaqstv
      781 dpsmlrwhee laeallghda vegalallae vrpvaerlgr stvllgcdrv ralclaaegr
      841 tdeaaelltg tagrfaeagl pleqgralma larverkrrr rsaaqaalhg aatvferaga
      901 apwlalatea pagelpgaap ggdeaptala slteaelrla rlvgqgasnq eaaaklflsv
      961 ktvearltri yqkldvrsra qlatalrp
//
LOCUS       WP_392014360             214 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nicotinamide mononucleotide transporter family
            protein [unclassified Streptomyces].
ACCESSION   WP_392014360
VERSION     WP_392014360.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Hemberger,S., Pedrolli,D.B., Stolz,J., Vogl,C., Lehmann,M. and
            Mack,M.
  TITLE     RibM from Streptomyces davawensis is a riboflavin/roseoflavin
            transporter and may be useful for the optimization of riboflavin
            production strains
  JOURNAL   BMC Biotechnol 11, 119 (2011)
   PUBMED   22136195
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Zhu,N., Olivera,B.M. and Roth,J.R.
  TITLE     Genetic characterization of the pnuC gene, which encodes a
            component of the nicotinamide mononucleotide transport system in
            Salmonella typhimurium
  JOURNAL   J Bacteriol 171 (8), 4402-4409 (1989)
   PUBMED   2546921
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..214
                     /product="nicotinamide mononucleotide transporter family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0034257 - nicotinamide riboside
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_process="GO:0034258 - nicotinamide riboside transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23617
     Region          1..205
                     /region_name="PnuC"
                     /note="Nicotinamide riboside transporter PnuC [Coenzyme
                     transport and metabolism]; COG3201"
                     /db_xref="CDD:442434"
ORIGIN      
        1 mnwlnseaft lfdqhikwsd mignvigllg lalgwrrsiw twpvqfvsgl vlftafatah
       61 lsgsagkqiv vmavaawgfw qwnrgrrqnq dgsiavrfat wrergvlaaa aaagtlavgg
      121 lftvfptlsw dpwpdayifv gtvvamyaqa rgmvefwfaw llvdlvgvpl nfangfafsg
      181 fvyvlygalv lwglrdwwlr srtaarpvpe gapa
//
LOCUS       WP_392014543             321 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces chartreusis].
ACCESSION   WP_392014543
VERSION     WP_392014543.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces chartreusis
  ORGANISM  Streptomyces chartreusis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces chartreusis"
                     /db_xref="taxon:1969"
     Protein         1..321
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=32915
     Region          47..315
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mtavrlhagr llrrvpirqi lvllplalvv lvavqhrtvl aegighlata kwqwllaaag
       61 atcltwvaaa vtrqgavvdr lpklrllvtq faagsanhll ptglgasavn lrfmtvcglp
      121 larssaalal yllaesvarv gllaalliaf phalqlgpll pdgawgplll vigavvvviv
      181 alfalvrrlr tavlsflrta lgearsvhtr psralalwgg siafpalqaa glvlvgmalg
      241 ldvppahmal aylaatvava lvptpgglgs veaalivalv aaggpvavat avvlayriit
      301 vwlpllpgal tlgalvrfkv i
//
LOCUS       WP_392015042             128 aa            linear   BCT 20-JAN-2025
DEFINITION  TOBE domain-containing protein [Streptomyces chartreusis].
ACCESSION   WP_392015042
VERSION     WP_392015042.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces chartreusis
  ORGANISM  Streptomyces chartreusis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 128)
  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 10007583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Streptomyces chartreusis"
                     /db_xref="taxon:1969"
     Protein         1..128
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13336
     Region          1..128
                     /region_name="MopI"
                     /note="Molybdopterin-binding protein MopI [Coenzyme
                     transport and metabolism]; COG3585"
                     /db_xref="CDD:442804"
ORIGIN      
        1 mhtyrigdaa allgvsadtv rrlvdggklt avrdgqghri ipgpalaaya rqlhraares
       61 tgssarnrfs givtdvalgd vsaqveiqag pfrvvamvsr esaedlrlep gvpavaviks
      121 tnvvverp
//
LOCUS       WP_392014434             818 aa            linear   BCT 20-JAN-2025
DEFINITION  GcvT family protein [Streptomyces sp. NPDC015140].
ACCESSION   WP_392014434
VERSION     WP_392014434.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015140
  ORGANISM  Streptomyces sp. NPDC015140
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 818)
  AUTHORS   Stauffer,L.T., Ghrist,A. and Stauffer,G.V.
  TITLE     The Escherichia coli gcvT gene encoding the T-protein of the
            glycine cleavage enzyme system
  JOURNAL   DNA Seq 3 (6), 339-346 (1993)
   PUBMED   8219277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..818
                     /organism="Streptomyces sp. NPDC015140"
                     /db_xref="taxon:3364943"
     Protein         1..818
                     /product="GcvT family protein"
                     /calculated_mol_wt=89269
     Region          22..394
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
     Region          380..435
                     /region_name="FAO_M"
                     /note="FAD dependent oxidoreductase central domain;
                     pfam16350"
                     /db_xref="CDD:465100"
     Region          430..817
                     /region_name="GcvT"
                     /note="Glycine cleavage system protein T
                     (aminomethyltransferase) [Amino acid transport and
                     metabolism]; COG0404"
                     /db_xref="CDD:440173"
ORIGIN      
        1 msghglrpsp rvvvigagvv gcsladelta rgwtdvtvle qgplpapggs tshapglvfr
       61 tspsrtltaf arytvekfts ltwdgapcfq rvgglelatt perladlhrr agyaaswgvt
      121 geivdaarck elwplldesv vlggfhtpgd glaravpacr aqldratarg arflerhtvt
      181 gierqdgrvt gvvtdrgafp adhvvsaagf wgpvvgrmag vdvplqplah qyartgplpe
      241 lsgatqeask pilrfqdrdl yfrehgdrlg vgsyahrplp vdpfavpgyd esrarhmdmp
      301 ssypftpqdw apswedcrrl mpalrhsdve sgfngvfsft pdgmpvlges rdlrgfwlae
      361 avwvthsagv akavaewmvn grpsldvhec dltrfeeaqr spayvrerga rqftevydvi
      421 hplqpmerpr plrvspfhar qrelgayfle gggwerphwy eanaglapda rlpgrdawsa
      481 rhwspiaaae arvtrerval ydmtplrrle vtgpgalafl drmtsnnlrk kpgavtytll
      541 ldesggirsd ltvarlapdr fqvganspad ldhllrhapg gevhirdits gtccvgvwgp
      601 lardlvqplt pddftheafg yfraretyvg hvpvtamrls yvgelgwely ttadlglrlw
      661 dtlweagrdl gviaagrsaf nslrlekgyr awgtdmtaed npyeagvgfa vrmdkadfvg
      721 raalaragep grrltpllld dpaavvlgke pvhvdgaaag yvtsasygyt lgrcvayawl
      781 paglaagtgv hveyfgekvp amvaeeplfd prmtrirr
//
LOCUS       WP_392015124             441 aa            linear   BCT 20-JAN-2025
DEFINITION  DUF1800 domain-containing protein [Streptomyces sp. NPDC015140].
ACCESSION   WP_392015124
VERSION     WP_392015124.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015140
  ORGANISM  Streptomyces sp. NPDC015140
            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 10009155
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Streptomyces sp. NPDC015140"
                     /db_xref="taxon:3364943"
     Protein         1..441
                     /product="DUF1800 domain-containing protein"
                     /calculated_mol_wt=47867
     Region          7..439
                     /region_name="COG5267"
                     /note="Uncharacterized conserved protein, DUF1800 family
                     [Function unknown]"
                     /db_xref="CDD:444080"
ORIGIN      
        1 makldeqarv lrllqrtgfg gagedalgqg gagegwdqal ervldtaddp dapsppdlgp
       61 lpdrgkaddd tadgtrqayr ravreqreal tiwwldrmta terpwiekrt llwhdhwats
      121 iqkvksgram laqnqtlrrl gagefrtmar amvqdpalml wldasgntae apnenlarel
      181 melfvlgvgh yeeedvrqaa aaltgwsvdr rgdgdwsarf rpqrhadgaq tvlgrrtdft
      241 atalvdhlva qpecprhvas rlwarlvsad sgpsdgsldr iadagdltam vraicedpaf
      301 adsanvvvrq pveyvvgtlr algvrparle rkargqllrt lsglgqvpfa ppsvggwphg
      361 tawlttaaar vrigfaqqtv rqgdlsavet apakerpevl arllgvrrws ertaavlaga
      421 agepdraaai altapeyllh p
//
LOCUS       WP_392015236             285 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Streptomyces sp.
            NPDC015140].
ACCESSION   WP_392015236
VERSION     WP_392015236.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015140
  ORGANISM  Streptomyces sp. NPDC015140
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 285)
  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 285)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptomyces sp. NPDC015140"
                     /db_xref="taxon:3364943"
     Protein         1..285
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=28705
     Region          23..283
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mplastgdlv graaaarsav aafnvitleh ieavvagaes vrmpvvlqvs enavkyrygr
       61 llplaaaava vaegaavpva lhldhvqsdg llrqardagf ssvmydasrl tyaenlaatr
      121 aavgwahaqg iwieaelgev ggkngaapld ahapgartnp aearafvaes gvdalavavg
      181 sshamtsrta aldhdllkal ssaldvplvl hgssgvpdae laaavtggia kvnvgtalni
      241 amtgairehl aahpdavdsr gyltagream vrtvatiiqv vgats
//
LOCUS       WP_392015647             270 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015140].
ACCESSION   WP_392015647
VERSION     WP_392015647.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015140
  ORGANISM  Streptomyces sp. NPDC015140
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (residues 1 to 270)
  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 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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Streptomyces sp. NPDC015140"
                     /db_xref="taxon:3364943"
     Protein         1..270
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30152
     Region          1..65
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          86..264
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 medeeseavl rtvgrqvkmw reaagmtqpe lgaaigyged lvssvergrr ipkpdfldna
       61 devlgaggkl asmkvdveka rypkkvrdla rledeavelg ayaghhihgl lqtpeyaral
      121 yamrrpafte eevdryvsar marktvfdrv praqltfvqe evtlrrplgg rmvlrqqleh
      181 llevgglrhv eiqvmptare dhagmagslq llklrggkaf ghaegqlhnr visephdiqt
      241 ldlrygiira qaltpresla fiekvmgeet
//
LOCUS       WP_392015098             403 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces omiyaensis].
ACCESSION   WP_392015098
VERSION     WP_392015098.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces omiyaensis
  ORGANISM  Streptomyces omiyaensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  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 403)
  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
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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   5  (residues 1 to 403)
  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   6  (residues 1 to 403)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 403)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces omiyaensis"
                     /db_xref="taxon:68247"
     Protein         1..403
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41018
     Region          14..77
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          77..379
                     /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 metpgsqtsl hranlervvr avrmagsltq aeiarstgls aatvsnivre lkdggtvevt
       61 ptsaggrrar svslsgdagi vigvdfghth lrvavgnlah qvlaeeaepl dvdasaaegf
      121 draerlvnrl ieatgigrdk vigvglgvpg pidvssgtlg stsilpgwsg inpaeelsar
      181 lgvpvhvdnd anlgalgelv wgsgrgvrdl ayikvasgvg aglvidgrvy rgpggtagei
      241 ghitldesgp vcrcgnrgcl etftaaryvl pllqpshgpd ltmervvqla regdpgcrrv
      301 iadvgrhigs gianlcnlln psrvvlggdi aeagelvlap vrdsvgryai psaarqlslv
      361 qgalggraev lgalalvlse mgdstllgss lpavvpasap aft
//
LOCUS       WP_392015867             462 aa            linear   BCT 20-JAN-2025
DEFINITION  alpha,alpha-trehalose-phosphate synthase (UDP-forming)
            [Streptomyces sp. NPDC015140].
ACCESSION   WP_392015867
VERSION     WP_392015867.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015140
  ORGANISM  Streptomyces sp. NPDC015140
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 462)
  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 462)
  AUTHORS   Eastmond,P.J. and Graham,I.A.
  TITLE     Trehalose metabolism: a regulatory role for trehalose-6-phosphate?
  JOURNAL   Curr Opin Plant Biol 6 (3), 231-235 (2003)
   PUBMED   12753972
REFERENCE   3  (residues 1 to 462)
  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   4  (residues 1 to 462)
  AUTHORS   Elbein,A.D., Pan,Y.T., Pastuszak,I. and Carroll,D.
  TITLE     New insights on trehalose: a multifunctional molecule
  JOURNAL   Glycobiology 13 (4), 17R-27R (2003)
   PUBMED   12626396
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 929-939 (1997)
   PUBMED   9334165
  REMARK    Erratum:[Biochem J 1998 Feb 1;329(Pt 3):719]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Streptomyces sp. NPDC015140"
                     /db_xref="taxon:3364943"
     Protein         1..462
                     /product="alpha,alpha-trehalose-phosphate synthase
                     (UDP-forming)"
                     /EC_number="2.4.1.15"
                     /GO_function="GO:0003825 - alpha,alpha-trehalose-phosphate
                     synthase (UDP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0005992 - trehalose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50197
     Region          8..462
                     /region_name="OtsA"
                     /note="Trehalose-6-phosphate synthase, GT20 family
                     [Carbohydrate transport and metabolism]; COG0380"
                     /db_xref="CDD:440149"
ORIGIN      
        1 massfgaaqv lvasnrgpvs yevredgslh akrgggglvs glssigpdag alwvcsalgd
       61 gdreavrrgv gedgvrmldv padvhadayn giansvlwfv hhmlyqtpve pvfdaefrrq
      121 wasyeaynra faealaeeaa egavaivqdy hltlvpgmlr elrpdlrigh fshtpwapvd
      181 yfrllpddia eqvlrgmlga drlgfltrrw adaftaccda lvgglgstet gvhglgadad
      241 flrkrshead vdermaalre eigegrrtiv rvdrtelskn ivrgllayre llatrpewre
      301 rvvhvafayp srqdlavyrd ytaevqrvad avnaefgtag wtpvvlhvkd dfarslaayr
      361 ladvalvnpv rdgmnlvake vpvvsdegcv lvlsreagay eelgedavvv npydvsgtae
      421 alhtalsvpa aeraerskrl aaagtalppa rwfleqlral rg
//
LOCUS       WP_392016289             424 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces omiyaensis].
ACCESSION   WP_392016289
VERSION     WP_392016289.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces omiyaensis
  ORGANISM  Streptomyces omiyaensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 424)
  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 424)
  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
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 424)
  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   5  (residues 1 to 424)
  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   6  (residues 1 to 424)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 424)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 424)
  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 20650276
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Streptomyces omiyaensis"
                     /db_xref="taxon:68247"
     Protein         1..424
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41742
     Region          17..59
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          85..397
                     /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 mrpapespad vrrhnlarvl rhladhgpss rgeaaaatgl ahgsltalta dlvgrglvre
       61 agtasgggrg rprqrletvp grvvsvavrv trerlhlava dlagtlghra elahatpggh
      121 pgalagtlad avretvaaar aahpgahlag tfvavpgpvt aggrvfstdf gwpgpvdlgs
      181 llrerlgesa gpvvlandan laalaeyral tvrrgaaprs laylkadvgv ggglvldgri
      241 eagrhgvage pghmpvafdg ppcacggrgc lalylgpeal tdaaglgalr aergteaava
      301 algralaage pdavaaldaa gevlgaavla vtslldaddv vlggyladwh pwlarglear
      361 lagrrtltag aapvphplpg vlgadaplag avalardtvl adpasvplge gtgpsgcggg
      421 gaca
//
LOCUS       WP_392016277             347 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AfsR/SARP family transcriptional regulator
            [unclassified Streptomyces].
ACCESSION   WP_392016277
VERSION     WP_392016277.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..347
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=36907
     Region          31..280
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mehptdgaph gatggpgtag plspeafget efrllgpvgl hdgatgadvv psgpkqrall
       61 salvlhagrl lsadrlteel wgdrpptnas nalqahvarl rrllpvpggg srghewistl
      121 ptgyllslgs attdverfqr lsalgraavs adpayavrll rhalslwrgp alqdsrlgpl
      181 caseadrlee hrltalesly easlgcaqhg qitgeleklt vdhplherfy dllmvalyrg
      241 grqaealgvy erarrrlvea lgiepgpalr arleavlnha pdlsapphph pgggpatlse
      301 alelggevar lqrrideltr sqealvrryd tmvarlaggp svqrvap
//
LOCUS       WP_392015942             289 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptomyces sp.
            NPDC015140].
ACCESSION   WP_392015942
VERSION     WP_392015942.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015140
  ORGANISM  Streptomyces sp. NPDC015140
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 289)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 289)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces sp. NPDC015140"
                     /db_xref="taxon:3364943"
     Protein         1..289
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31436
     Region          19..102
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          126..287
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 misalnrlid lveehlteel dvpalagtlg tteyhlrrmf sslagmplse yvrrrrmtva
       61 aadvvrgedd llgiavrhgy gsteafgraf rsvhgaapre vrraggplqs qpqlrfrltv
      121 egstpmdtrf adrpafrlig hatrvplihe gvnphiqehi aalppqehar lkslgdtdpa
      181 gllqvcddla pdsaegtdlt ylhgvavtrd tpapddldai evpagmwavf rtsgphpeal
      241 qtawaatate wfpsnpwrlr pgpslvavls rtddfttatc elwlpvepa
//
LOCUS       WP_392016589             333 aa            linear   BCT 20-JAN-2025
DEFINITION  heme/hemin ABC transporter substrate-binding protein [Streptomyces
            omiyaensis].
ACCESSION   WP_392016589
VERSION     WP_392016589.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces omiyaensis
  ORGANISM  Streptomyces omiyaensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Naoe,Y., Nakamura,N., Rahman,M.M., Tosha,T., Nagatoishi,S.,
            Tsumoto,K., Shiro,Y. and Sugimoto,H.
  TITLE     Structural basis for binding and transfer of heme in bacterial
            heme-acquisition systems
  JOURNAL   Proteins 85 (12), 2217-2230 (2017)
   PUBMED   28913898
REFERENCE   2  (residues 1 to 333)
  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   3  (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   4  (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   5  (residues 1 to 333)
  AUTHORS   Ho,W.W., Li,H., Eakanunkul,S., Tong,Y., Wilks,A., Guo,M. and
            Poulos,T.L.
  TITLE     Holo- and apo-bound structures of bacterial periplasmic
            heme-binding proteins
  JOURNAL   J Biol Chem 282 (49), 35796-35802 (2007)
   PUBMED   17925389
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Streptomyces omiyaensis"
                     /db_xref="taxon:68247"
     Protein         1..333
                     /product="heme/hemin 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=33571
     Region          64..333
                     /region_name="ChuT"
                     /note="ABC-type hemin transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG4558"
                     /db_xref="CDD:443619"
ORIGIN      
        1 mrrtrlagal tavialalta tgcgggdgpe pargataaaa pdrveplasp hsprlpvtva
       61 sadgrrvtvg saerivplsg slseivftlg lgdrvvakdv tatfeqaagl pvvtrahdvs
      121 aesvlslkpt lvlaesttgp aeaiaqirda gvplvvvpaa knlddvgsri dgvaaalgvp
      181 aageelrert aerldavrek ipahadrprv aflyvrgsaa vyllggaesg asslleaaga
      241 vdagkesglk kdftpittea laqaapdail vmtkglrsvg gvdglvkipg vaetpagadr
      301 rvvsvddgvl lnygprtdqv laslvdqlyg egk
//
LOCUS       WP_392016948             305 aa            linear   BCT 20-JAN-2025
DEFINITION  quinone oxidoreductase family protein [Streptomyces omiyaensis].
ACCESSION   WP_392016948
VERSION     WP_392016948.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces omiyaensis
  ORGANISM  Streptomyces omiyaensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 305)
  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 305)
  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 305)
  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   4  (residues 1 to 305)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Streptomyces omiyaensis"
                     /db_xref="taxon:68247"
     Protein         1..305
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=31696
     Region          1..303
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 mlairfdrfg gpevltpvdv papvpgpgev lvaveaagvn fadtfqvdgs yldpallphv
       61 pggevvgrte dgrrvlakva hgyaelavar eaalvevpee ldaaralall tqgltawhll
      121 rsaarlrpge svvvhsaagg vgslavqlar efgagrvlaq astpdkerla ldlgadepar
      181 yplarradvi ldaaggelfa halgsladfg rlvtygnasr aafaaldpgr lgrlnasvvg
      241 fwlrptlalp galdgplkel faltlqgrlr pvagpeypla qartaheell arrttgkvvl
      301 rpgav
//
LOCUS       WP_392017104             292 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces chartreusis].
ACCESSION   WP_392017104
VERSION     WP_392017104.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces chartreusis
  ORGANISM  Streptomyces chartreusis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415139
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptomyces chartreusis"
                     /db_xref="taxon:1969"
     Protein         1..292
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=31693
     Region          1..260
                     /region_name="LysX"
                     /note="Glutathione synthase, LysX or RimK-type ligase,
                     ATP-grasp superfamily [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism,
                     Translation, ribosomal structure and biogenesis, Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0189"
                     /db_xref="CDD:439959"
ORIGIN      
        1 mprialvtcr pgaqisvdrd lpvlaralte agaeadivhw ddetadwgry dlavirstwd
       61 yswraaefla waercgkatr lanpagvvrw nadkrylgdl aaagvpvvpt rylapgdtad
      121 lptgheyvvk ptsgagarfa arytpdehet avrqlarmha egftamvqpy vesidvsger
      181 alqffggrfl haarkgavlt pgtpyderki ahpglepwtp tpaelavaer alaavpeaae
      241 llyarvdlvd gedgqprvme lelvepnlfl wlhpgsvprv veailaeaaa sr
//
LOCUS       WP_392017181             278 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Streptomyces omiyaensis].
ACCESSION   WP_392017181
VERSION     WP_392017181.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces omiyaensis
  ORGANISM  Streptomyces omiyaensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 278)
  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 278)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Streptomyces omiyaensis"
                     /db_xref="taxon:68247"
     Protein         1..278
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=28123
     Region          2..275
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mplsvtheiv aaayagttgv gafnvvqieh aeaivagaer aglpvilqis entvryhgsl
       61 apialaslal adgaavpvsv hldhaesadl vheavdlgit svmfdasklp yaenvaathe
      121 itarchragv wveaelgevg gkdgahapgv rtdpdeaaaf vaatgvdala vavgsshaml
      181 tldavldfal iarlraavat plvlhgssgv gdaglaeava sgmtkvnvst hlnkaftrvv
      241 rahlgahpdv vdprkylgpa ratvadevar llgvlagr
//
LOCUS       WP_392017462             335 aa            linear   BCT 20-JAN-2025
DEFINITION  heme/hemin ABC transporter substrate-binding protein [Streptomyces
            chartreusis].
ACCESSION   WP_392017462
VERSION     WP_392017462.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces chartreusis
  ORGANISM  Streptomyces chartreusis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Naoe,Y., Nakamura,N., Rahman,M.M., Tosha,T., Nagatoishi,S.,
            Tsumoto,K., Shiro,Y. and Sugimoto,H.
  TITLE     Structural basis for binding and transfer of heme in bacterial
            heme-acquisition systems
  JOURNAL   Proteins 85 (12), 2217-2230 (2017)
   PUBMED   28913898
REFERENCE   2  (residues 1 to 335)
  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   3  (residues 1 to 335)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 335)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Ho,W.W., Li,H., Eakanunkul,S., Tong,Y., Wilks,A., Guo,M. and
            Poulos,T.L.
  TITLE     Holo- and apo-bound structures of bacterial periplasmic
            heme-binding proteins
  JOURNAL   J Biol Chem 282 (49), 35796-35802 (2007)
   PUBMED   17925389
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Streptomyces chartreusis"
                     /db_xref="taxon:1969"
     Protein         1..335
                     /product="heme/hemin 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=33862
     Region          65..334
                     /region_name="ChuT"
                     /note="ABC-type hemin transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG4558"
                     /db_xref="CDD:443619"
ORIGIN      
        1 mrrlrtrltg allavlaltt agcggagnag tgaqstgaka danrveplag kpdpdlpvtv
       61 rsvdggkvtv gkadrvvpls gslgelvftl glgdrvvard itatfeqaak lpvvtrghdv
      121 saesvlslrp dlvlaetttg paeamdqira agipvlvvap arglddvdpr ieavaaalgv
      181 paagkeltdr terriaavrk gvprekekpr vaflylrgsa svyliggkgs gatslieaag
      241 gvdagaesgl akdfttitse alvkaapdai lvmskglesv ggvdglvkip giaqtpagad
      301 rrivsiedga llsygprtdq vlksvvaqly egdaa
//
LOCUS       WP_392018158             594 aa            linear   BCT 20-JAN-2025
DEFINITION  caspase family protein [Streptomyces sp. NPDC015140].
ACCESSION   WP_392018158
VERSION     WP_392018158.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015140
  ORGANISM  Streptomyces sp. NPDC015140
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Van Opdenbosch,N. and Lamkanfi,M.
  TITLE     Caspases in Cell Death, Inflammation, and Disease
  JOURNAL   Immunity 50 (6), 1352-1364 (2019)
   PUBMED   31216460
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Tsiatsiani,L., Van Breusegem,F., Gallois,P., Zavialov,A., Lam,E.
            and Bozhkov,P.V.
  TITLE     Metacaspases
  JOURNAL   Cell Death Differ 18 (8), 1279-1288 (2011)
   PUBMED   21597462
REFERENCE   3  (residues 1 to 594)
  AUTHORS   Zhang,J.H., Zhang,Y. and Herman,B.
  TITLE     Caspases, apoptosis and aging
  JOURNAL   Ageing Res Rev 2 (4), 357-366 (2003)
   PUBMED   14522240
REFERENCE   4  (residues 1 to 594)
  AUTHORS   Salvesen,G.S.
  TITLE     Caspases and apoptosis
  JOURNAL   Essays Biochem 38, 9-19 (2002)
   PUBMED   12463158
REFERENCE   5  (residues 1 to 594)
  AUTHORS   Villa,P., Kaufmann,S.H. and Earnshaw,W.C.
  TITLE     Caspases and caspase inhibitors
  JOURNAL   Trends Biochem Sci 22 (10), 388-393 (1997)
   PUBMED   9357314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Streptomyces sp. NPDC015140"
                     /db_xref="taxon:3364943"
     Protein         1..594
                     /product="caspase family protein"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=64087
     Region          5..235
                     /region_name="COG4249"
                     /note="Uncharacterized conserved protein, contains caspase
                     domain [General function prediction only]"
                     /db_xref="CDD:443391"
ORIGIN      
        1 mtslpdpaas ravligveqy teplqplptv annlaglkdv ltgpdswrlp pehctvlsnp
       61 esatqvldav haaateatda lfvyfaghgl lspvgdlyla lsdsppgrlf havaydqlry
      121 qvaeecaals rvvvldccys gralhgymga pleladcgdi dgtyvltasa etkramapkg
      181 ehytafsgal lravtegvph gpdmldmetv yrhvrrelqa rkrpvpqqra rneghritla
      241 rnrwspaagp eaqeyaaalr kavrdggnaa dpdtapylrg ervaprafvd aladrlpetg
      301 ltrlhdlrrt aqraapdaat qlqywqeeve llthrltrag dysrdiegel traqervrql
      361 dvevrvlnrq vrllldekgr dtttaealvg aaatqseaag savrggvppk tpaergapgt
      421 apaprppapv artswtlavl avlyvviawa ftldtvalty dsgrkpasmp stsdlpsgeg
      481 phyvwdvetd vtstfrpden daadkltgdl vvsvprpced rtieweitid gregdrgslv
      541 gdtehqvpld iplngspdrv tisaswaggt escpsfglvw tdprlavdld lvpw
//
LOCUS       WP_392018488             362 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces chartreusis].
ACCESSION   WP_392018488
VERSION     WP_392018488.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces chartreusis
  ORGANISM  Streptomyces chartreusis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Streptomyces chartreusis"
                     /db_xref="taxon:1969"
     Protein         1..362
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=36991
     Region          87..360
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mssslplsdl pgplptcpvp avaalttvpa psaapaeagt hspltpadsp faparlarha
       61 ltllplvlvg awaaadwhtv rdgaarlasa dpwwllaglf ftcmgwvcaa vvrqgaipdr
      121 lppglllasq faagaanqvl pasigahavt lrflqsqgip largtaslal yslakpvakt
      181 vvllgflvaf pellhlgelv pdrrtwvlva agvvtalvta allmttvral rrpllgfvrt
      241 altdarilha rpsrvlalwg gaaatpllqa sviasvgfal glplswtqvt lalllastav
      301 gavpapggig pvdaalvftm vtfgapmgla aatvigyrvl tvwvpllpga lvlsimvqrk
      361 il
//
LOCUS       WP_392018552             387 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces chartreusis].
ACCESSION   WP_392018552
VERSION     WP_392018552.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces chartreusis
  ORGANISM  Streptomyces chartreusis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 387)
  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   5  (residues 1 to 387)
  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   6  (residues 1 to 387)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 387)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 387)
  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 11973053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Streptomyces chartreusis"
                     /db_xref="taxon:1969"
     Protein         1..387
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39787
     Region          <9..54
                     /region_name="COG3398"
                     /note="Predicted transcriptional regulator, contains two
                     HTH domains [Transcription]"
                     /db_xref="CDD:442625"
     Region          75..372
                     /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 mieksgsltr rilellasgq astrtelsel lgaapstvsf avgklldygl vteegtlssn
       61 ggrprkvlrl gggdgyavaa elggkhahvg ivhsggglad vstvpfatad gpeaslpglv
      121 etlqgladrh grellrgvgl clpgpvdvea glvtlparmp gwnrfpvrdw lqerfgvpva
      181 iendancmav gehsvrpaaq rqaimvkagt gigagviadg rlyrggsgaa geithvrvea
      241 ahdipcscgn tgcletvasg aalvrilrer glevtstedv vrlagdadpe atravrqagr
      301 ylgtvlapnv nffnpdavyl ggilstlepf vaavrsqlye gchplvtehl vieraglgad
      361 aglvgagqfa lqralahalh tatgahp
//
LOCUS       WP_392018686             497 aa            linear   BCT 20-JAN-2025
DEFINITION  alpha,alpha-trehalose-phosphate synthase (UDP-forming)
            [Streptomyces chartreusis].
ACCESSION   WP_392018686
VERSION     WP_392018686.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces chartreusis
  ORGANISM  Streptomyces chartreusis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 497)
  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 497)
  AUTHORS   Eastmond,P.J. and Graham,I.A.
  TITLE     Trehalose metabolism: a regulatory role for trehalose-6-phosphate?
  JOURNAL   Curr Opin Plant Biol 6 (3), 231-235 (2003)
   PUBMED   12753972
REFERENCE   3  (residues 1 to 497)
  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   4  (residues 1 to 497)
  AUTHORS   Elbein,A.D., Pan,Y.T., Pastuszak,I. and Carroll,D.
  TITLE     New insights on trehalose: a multifunctional molecule
  JOURNAL   Glycobiology 13 (4), 17R-27R (2003)
   PUBMED   12626396
REFERENCE   5  (residues 1 to 497)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 929-939 (1997)
   PUBMED   9334165
  REMARK    Erratum:[Biochem J 1998 Feb 1;329(Pt 3):719]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Streptomyces chartreusis"
                     /db_xref="taxon:1969"
     Protein         1..497
                     /product="alpha,alpha-trehalose-phosphate synthase
                     (UDP-forming)"
                     /EC_number="2.4.1.15"
                     /GO_function="GO:0003825 - alpha,alpha-trehalose-phosphate
                     synthase (UDP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0005992 - trehalose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=53698
     Region          14..497
                     /region_name="OtsA"
                     /note="Trehalose-6-phosphate synthase, GT20 family
                     [Carbohydrate transport and metabolism]; COG0380"
                     /db_xref="CDD:440149"
ORIGIN      
        1 mastqdapga hgaakvlvas nrgpvsyqvg ddgsltskrg gggvvsglsa igpdagalwv
       61 csalsdgdre avrrgivgag peappqrggg grragedgvl mldvpadvha dayngiansv
      121 lwfvhhmlyq tplepvfdae frrqwtsyea ynrafaeala graapgaavl vqdyhltlvp
      181 gmlrelrpdl righfshtpw appeyfrmlp ddiaeqvlrg mlgadrlgfl trrwadafea
      241 ccarfadglg gtrigvhglg adadflrers hradvtermt alrdeigsap dgtarrtivr
      301 vdrtelskni vrgllsyrql lddhpewrer vvhvafayps rqdlavyrdy taevqrlade
      361 lnsqygtpgw tpvvlhvkdd farslaayrl advalvnpir dgmnlvakem plvsdegcal
      421 vlsreagahe elgedaitvn pydvvgtara lhealsvgpe eraerskrla aaatalppaq
      481 wfldqlhale eqpgpsa
//
LOCUS       WP_392019149             232 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Streptomyces chartreusis].
ACCESSION   WP_392019149
VERSION     WP_392019149.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces chartreusis
  ORGANISM  Streptomyces chartreusis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 232)
  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 10007985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Streptomyces chartreusis"
                     /db_xref="taxon:1969"
     Protein         1..232
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24613
     Region          32..222
                     /region_name="COG3786"
                     /note="L,D-peptidoglycan transpeptidase YkuD,
                     ErfK/YbiS/YcfS/YnhG family [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443000"
ORIGIN      
        1 mrpgvvalas asllvlgaap gegprplpar madtgggsql itavaprags tsgtvtwwnr
       61 aggrwvkags asarfgakgl vrgakrrqgt nttptglygl pyafgiekap rgttyryrrv
      121 hqgswwcqdn gsraynrwse prardcraae sehlisygap yahalvigfn ydrpvkgrga
      181 giflhvkgrg atagcvsvsr gamrrilkwa epkrrphiai gtaggttait ry
//
LOCUS       WP_392019269             415 aa            linear   BCT 20-JAN-2025
DEFINITION  caspase family protein [Streptomyces pactum].
ACCESSION   WP_392019269
VERSION     WP_392019269.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pactum
  ORGANISM  Streptomyces pactum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Van Opdenbosch,N. and Lamkanfi,M.
  TITLE     Caspases in Cell Death, Inflammation, and Disease
  JOURNAL   Immunity 50 (6), 1352-1364 (2019)
   PUBMED   31216460
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Tsiatsiani,L., Van Breusegem,F., Gallois,P., Zavialov,A., Lam,E.
            and Bozhkov,P.V.
  TITLE     Metacaspases
  JOURNAL   Cell Death Differ 18 (8), 1279-1288 (2011)
   PUBMED   21597462
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Zhang,J.H., Zhang,Y. and Herman,B.
  TITLE     Caspases, apoptosis and aging
  JOURNAL   Ageing Res Rev 2 (4), 357-366 (2003)
   PUBMED   14522240
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Salvesen,G.S.
  TITLE     Caspases and apoptosis
  JOURNAL   Essays Biochem 38, 9-19 (2002)
   PUBMED   12463158
REFERENCE   5  (residues 1 to 415)
  AUTHORS   Villa,P., Kaufmann,S.H. and Earnshaw,W.C.
  TITLE     Caspases and caspase inhibitors
  JOURNAL   Trends Biochem Sci 22 (10), 388-393 (1997)
   PUBMED   9357314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces pactum"
                     /db_xref="taxon:68249"
     Protein         1..415
                     /product="caspase family protein"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43852
     Region          11..228
                     /region_name="COG4249"
                     /note="Uncharacterized conserved protein, contains caspase
                     domain [General function prediction only]"
                     /db_xref="CDD:443391"
     Region          268..>378
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Site            order(268..269,272..273,275,304,307..308,311..312,
                     314..315,343,346..347,350..351,354)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          268..293
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          298..332
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          342..370
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mtrlpdpdas ravligtaay qhldqlpava anlrdladtl gdallwglpr ehcaqvmdpa
       61 daaamldpvh qageaasdtl lvyfaghglr dpdsadlylg lngsrehagy tavayehlra
      121 avrasrarrr ivvldccfsg raaralsgsg dalaaqlava gayvltaspr drvalapdge
      181 phtaftgell gvlrqglpdg pelidldtly rvlgerlrsk nrplpqrsqe ndigrlplvr
      241 nraraddrgp agpvlesevr aamvstglgl artlraagrn rdalpvlrla lterapgsmg
      301 stfavqlels elladtgrsr eaievleqaf hhtrttqgpe avlvcrrlaa llqesgnhiq
      361 acevlkhald laenagaapa rdtppvravp rplpygppag hggpdavsrr tpagp
//
LOCUS       WP_392019591             322 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces pactum].
ACCESSION   WP_392019591
VERSION     WP_392019591.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pactum
  ORGANISM  Streptomyces pactum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 322)
  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 322)
  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 322)
  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 18542080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces pactum"
                     /db_xref="taxon:68249"
     Protein         1..322
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=36227
     Region          25..>67
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
     Region          114..316
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mfsdsnavvr parpsgpdwt ptaanimlgr avkdlrerag ltqkdlagri hvsaatinrl
       61 enadttpmrr tvesvigllg pdsatrdgll mmlarteepe wfqhrfedct pdhlrrllgl
      121 esmaihitsy dvrlvsgllq tpeyaahiir tglhltewrg peagrrlaqr lerqervlgq
      181 adpprcvflm desvlirrvg pdevmrgqlv rlreltdlph ivirfvlfdr fiagnagsma
      241 gsmaqlqfgr gglpdlvyve gyekadyftp pprrarsper pptprenhfe rhlqlllriq
      301 geacaspaes rrmldeaisr ys
//
LOCUS       WP_392019795             292 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC014894].
ACCESSION   WP_392019795
VERSION     WP_392019795.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014894
  ORGANISM  Streptomyces sp. NPDC014894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 292)
  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 292)
  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 292)
  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 18542080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptomyces sp. NPDC014894"
                     /db_xref="taxon:3364931"
     Protein         1..292
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32915
     Region          32..87
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
     Region          109..287
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mtdgtsgtdd eaeavacgst svggepessd smrtfgavvs alrehhgysr eefaplvrys
       61 rhtvvsielg rrmpdkpfie raeellgntg alrksvehls rqpglaawfr qwarlegkai
      121 slntyecrli pgllqteaya rtlfvnqlpp lgarqietql karlerqrll rerentaynf
      181 ileeqlfhrc mggaevtrdl idhvldlaql wnievqlmpl vreshagldg pmqlletpen
      241 rwyaycegqe sgllisepkv vsmlqmryar mrsqalsfed svsllqrirg al
//
LOCUS       WP_392020069             404 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC014894].
ACCESSION   WP_392020069
VERSION     WP_392020069.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014894
  ORGANISM  Streptomyces sp. NPDC014894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 404)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Streptomyces sp. NPDC014894"
                     /db_xref="taxon:3364931"
     Protein         1..404
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43453
     Region          55..241
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          248..373
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mrhvlrragr ggafalasaa liaaglsgcs ggaldlggka gspeetiriv pgdgakdvdp
       61 ggrlevrlps grlervavtr ienekparvp ggisedglrw rpkdgvrldl aakysvdvva
      121 ldghgrrsar httfttevpd hrfigyfkpe nratvgtgmi vsfdfnqkia draavqravk
      181 vtadppvpva ghwfgdtrld frpekywepg tevtvdvrlr dveaapgayg iqqrkisfti
      241 grsqhslvda eektmrvrre gaapvtvpvt vgavkmptyn gkmvvsemhd mtrmdgrtvg
      301 fggeydikdv phamrltksg tflhgnywaa petfgqanvs hgcvglrdvk ggsgdtpagw
      361 ffdrtlvgdv vevinstdke vapdnglsgw nmdwgrwrag salg
//
LOCUS       WP_392020071             419 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC014894].
ACCESSION   WP_392020071
VERSION     WP_392020071.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014894
  ORGANISM  Streptomyces sp. NPDC014894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 419)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Streptomyces sp. NPDC014894"
                     /db_xref="taxon:3364931"
     Protein         1..419
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=44178
     Region          79..260
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          266..393
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mlkerpkaga taaavrgrgg salraaaaaa llvlvtacgg gdgdaesgsa dgkggardsg
       61 rvadeasrav vtvaprdgak avatsgalkv tadrgrlttv tvrdskgvei egelaadgds
      121 wqplhhlaga trykvhavar dedgresakd tsfttlvpkn tfighytped rttvgvgmpv
      181 sinftrgitd paaveravtv taepsvpieg hwfgndrldf rpekywapgt kvtvklnldg
      241 vqgrpgvygk qaktvsftig rsqistvdak tqrmrvvrdg rlvkdlpita gapatttyng
      301 qmvisekyev trmngatvgf ggeydikdvp hamrlstsgt fihgnywaap stfgsanvsh
      361 gcvglrdvrg grdakspaaw fydrsllgdv vvvknskdel iapdnglngw nmpwsewkk
//
LOCUS       WP_392020261             380 aa            linear   BCT 20-JAN-2025
DEFINITION  threonine synthase [Streptomyces sp. NPDC014894].
ACCESSION   WP_392020261
VERSION     WP_392020261.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014894
  ORGANISM  Streptomyces sp. NPDC014894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 380)
  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 380)
  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   3  (residues 1 to 380)
  AUTHORS   Parsot,C.
  TITLE     Evolution of biosynthetic pathways: a common ancestor for threonine
            synthase, threonine dehydratase and D-serine dehydratase
  JOURNAL   EMBO J 5 (11), 3013-3019 (1986)
   PUBMED   3098560
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423064
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Streptomyces sp. NPDC014894"
                     /db_xref="taxon:3364931"
     Protein         1..380
                     /product="threonine synthase"
                     /EC_number="4.2.3.1"
                     /GO_function="GO:0004795 - threonine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009088 - threonine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40060
     Region          4..372
                     /region_name="ThrC"
                     /note="Threonine synthase [Amino acid transport and
                     metabolism]; COG0498"
                     /db_xref="CDD:440264"
ORIGIN      
        1 mtahylders gtrypltdpl rwrsdsgapl svsplpgitr advdtarrsi wryraalpve
       61 irepvslgeg ctplvdgewd gvpvsyklew faptgsfkdr gtsvmisfla qhgvrevved
      121 ssgnggssvs aycaaagira rilapestsp akvlqsrayg advrlvpgdr eataaealrq
      181 sadtyyashn whpfflqgtk tlayeiwedl gfrapdqivt vagagstvlg cflgfsella
      241 agqierlprl lvaqpancap lhasfragae tavptdfapt vaegtaiqrp vrlpevlrav
      301 rrsggdmaai geaaiedavr rlaarglyae ptsataaaav gefaargavr pgtrtvvvlt
      361 gsglkaagam ervtargsar
//
LOCUS       WP_392020274             281 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            chartreusis].
ACCESSION   WP_392020274
VERSION     WP_392020274.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces chartreusis
  ORGANISM  Streptomyces chartreusis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 281)
  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 281)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces chartreusis"
                     /db_xref="taxon:1969"
     Protein         1..281
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30797
     Region          9..72
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          94..275
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mtamaraenk teaggtahlv aalakalreq hgltqpqlgd klgytaaavs ametcaqpas
       61 dqmlvkleae iggglgvfek arkwilleky parfrgfsel eagaitlcsy qtlivdglfq
      121 tedyaralig gsyppvseqr reelvdarla rraifdrdpa phielilees vlrrpfgswd
      181 vmggqlrsla adarrdnvfv qvlplnrglh gtyagdrgam qvvetkdheh vvymeiedqg
      241 ilvndpaevs hlarryanir aqalspdesl sfieqlagee r
//
LOCUS       WP_392020451             403 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces chartreusis].
ACCESSION   WP_392020451
VERSION     WP_392020451.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces chartreusis
  ORGANISM  Streptomyces chartreusis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces chartreusis"
                     /db_xref="taxon:1969"
     Protein         1..403
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=42967
     Region          63..246
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          251..371
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 msrsraviha rvraavvaga aaalltplaa cssgsqgssd dgrnpgaddr pvrvtvtprg
       61 ekvpagepvk vtasggrlts vtvtdgeghr lagkvaadgr swvsdrksvp gaaysvtaat
      121 rseggtakst raafttaeag kvnkvdwrpg tgttvgvaqp islvfdnpvk nraevekqlr
      181 ittsndtegs wgwmrdwsgr drvdwrpkey wkpgtevtln arlngtdsgt aggwfvrdyt
      241 ttftigarqi vkvdlddhrl tlvrdgetvr ripvsggtpg gdkrswrgta vlmakegtin
      301 mnsetvglad aydkmvdysm rltwsgmyah aapwnaryfg nsnhssgcig msdanaswfy
      361 sqvhpgdpfe ikgkdtkgvv apgngfgawn vswtewqgms alr
//
LOCUS       WP_392020607             282 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            chartreusis].
ACCESSION   WP_392020607
VERSION     WP_392020607.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces chartreusis
  ORGANISM  Streptomyces chartreusis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 282)
  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 282)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces chartreusis"
                     /db_xref="taxon:1969"
     Protein         1..282
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31426
     Region          17..68
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          90..263
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mvhvrqldpt aspldyfgye lrrkreeagl tlkqlgsvlf csgsligqie ttlkvptref
       61 aervdaalvt dgmfsrlvgl vlrsqlptwf qpfadmeaka tyvstyqcql vygllqtkey
      121 aravlatgqp ekldellaar merqrilkrt rppltlvvld eavlhrpvgg vevmrdqllh
      181 llslkderwi rlqvlpfrvg ehvslagsft llrfdddpdv vytedlisgh mtassetire
      241 aalryaglqg aalsvedsae likgvleery gqqagtgqrp la
//
LOCUS       WP_392020755             230 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease H family protein [Streptomyces chartreusis].
ACCESSION   WP_392020755
VERSION     WP_392020755.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces chartreusis
  ORGANISM  Streptomyces chartreusis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 230)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Streptomyces chartreusis"
                     /db_xref="taxon:1969"
     Protein         1..230
                     /product="ribonuclease H family protein"
                     /EC_number="3.1.26.4"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=24363
     Region          8..149
                     /region_name="RNase_HI_prokaryote_like"
                     /note="RNase HI family found mainly in prokaryotes;
                     cd09278"
                     /db_xref="CDD:260010"
     Site            order(14..17,49..51,54,76,126,146)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260010"
ORIGIN      
        1 migrmlervv aacdgaskgn pgpagwawvv adesetparw eagplgkatn nvaeltaler
       61 llaaidpgvp leirmdsqya mkavttwlpg wkrngwktsa gkpvanqdlv vridelldgr
      121 kvefryvpah qvdgdplndf adraasqaat vqesagselg spqpppspdt pqtkaprrka
      181 aaarkngsss rtikakfpgr clcgrgyaag eqiaknaqgw ghpecrtada
//
LOCUS       WP_392020760             279 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces pactum].
ACCESSION   WP_392020760
VERSION     WP_392020760.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pactum
  ORGANISM  Streptomyces pactum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415139
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces pactum"
                     /db_xref="taxon:68249"
     Protein         1..279
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=29161
     Region          1..264
                     /region_name="LysX"
                     /note="Glutathione synthase, LysX or RimK-type ligase,
                     ATP-grasp superfamily [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism,
                     Translation, ribosomal structure and biogenesis, Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0189"
                     /db_xref="CDD:439959"
ORIGIN      
        1 mrvglitaep ghpllaaats llraaghrve avdpsaarda taepadvyll ksrtpdalal
       61 aralerlgap vvnsaaatar cqdrtamaer aaaaglpfaa trtfatlsgl ardsrtagpv
      121 vvksrhsrrh dlvaraddga rlrelaaawp eepvvvqdfa pndgwdhklw aigdrvfaal
      181 rrselspggr gptrpldpes lppgrtalvr rvgevftldv ygvdivettg gtplivdina
      241 fpgvrgqrda paalvdltlr aaarrlcrpg rsgaggtap
//
LOCUS       WP_392021409             214 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nicotinamide mononucleotide transporter family
            protein [unclassified Streptomyces].
ACCESSION   WP_392021409
VERSION     WP_392021409.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Hemberger,S., Pedrolli,D.B., Stolz,J., Vogl,C., Lehmann,M. and
            Mack,M.
  TITLE     RibM from Streptomyces davawensis is a riboflavin/roseoflavin
            transporter and may be useful for the optimization of riboflavin
            production strains
  JOURNAL   BMC Biotechnol 11, 119 (2011)
   PUBMED   22136195
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Zhu,N., Olivera,B.M. and Roth,J.R.
  TITLE     Genetic characterization of the pnuC gene, which encodes a
            component of the nicotinamide mononucleotide transport system in
            Salmonella typhimurium
  JOURNAL   J Bacteriol 171 (8), 4402-4409 (1989)
   PUBMED   2546921
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..214
                     /product="nicotinamide mononucleotide transporter family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0034257 - nicotinamide riboside
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_process="GO:0034258 - nicotinamide riboside transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23120
     Region          10..205
                     /region_name="PnuC"
                     /note="Nicotinamide riboside transporter PnuC [Coenzyme
                     transport and metabolism]; COG3201"
                     /db_xref="CDD:442434"
ORIGIN      
        1 msalstlnsv aftafgqdik wsdmigntig lialalgwrr svwtwpaqll sgvvligaya
       61 saqlsggvgk qllvilvalw gwrlwtrgsr qaqdgsvavr fatwkergll aagavagtla
      121 vgwlftlyps lswspwaday ifvgtivamv aqarglvefw fawllvdivg vplafssgla
      181 fsglvyviyf alvlwglrdw wlrsrtpvlk gapa
//
LOCUS       WP_392021702             178 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC014894].
ACCESSION   WP_392021702
VERSION     WP_392021702.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014894
  ORGANISM  Streptomyces sp. NPDC014894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 178)
  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 178)
  AUTHORS   Tyrrell,R., Verschueren,K.H., Dodson,E.J., Murshudov,G.N., Addy,C.
            and Wilkinson,A.J.
  TITLE     The structure of the cofactor-binding fragment of the LysR family
            member, CysB: a familiar fold with a surprising subunit arrangement
  JOURNAL   Structure 5 (8), 1017-1032 (1997)
   PUBMED   9309218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444001
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Streptomyces sp. NPDC014894"
                     /db_xref="taxon:3364931"
     Protein         1..178
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19613
     Region          6..61
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
ORIGIN      
        1 mkvhgrdlrc fasvaeeldv traagrsfvs rpsvsghvcr wsgarrfhrd rgtvrptatg
       61 eappqcvgcr rrgppgetas rshrmtrtgq rchgyrvars lrqseldapa rareggqper
      121 arpvrrvtvs pahagqegrt rpcprrfplr prprrcprfs tppvisphrt vsatgasc
//
LOCUS       WP_392022300             281 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            chartreusis].
ACCESSION   WP_392022300
VERSION     WP_392022300.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces chartreusis
  ORGANISM  Streptomyces chartreusis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 281)
  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 281)
  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 10611723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces chartreusis"
                     /db_xref="taxon:1969"
     Protein         1..281
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29245
     Region          10..66
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(16,20,45)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(19,44)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(26..27,38,41,45..46)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          164..252
                     /region_name="DUF2690"
                     /note="Protein of unknown function (DUF2690); pfam10901"
                     /db_xref="CDD:402475"
ORIGIN      
        1 mtapsperar laaalrelkc rtglslagla aktafskssw drylngrtlp prdavqelcr
       61 lagepegrcl alweiaeseg sgraaaqppe eaapveddrr rgsadqssvh rratlvavla
      121 svsavvvggv aaaalllpdr ggepgaalsp ppsvagprcr gevcegkspm rmkcagaplt
      181 lasyrtatga slelrysqec gtswarmwgt rigdrlemsa tggagdgtrs grvrsveirn
      241 gvdadsyvyt pmtaadpgsv vracfdpvag geecfdsrva r
//
LOCUS       WP_392022333             281 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AfsR/SARP family transcriptional regulator
            [unclassified Streptomyces].
ACCESSION   WP_392022333
VERSION     WP_392022333.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..281
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=31153
     Region          21..270
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mtalmetrip drgardtgph tvalrllgpl eiavdavevp lpqrklrqll atllirpnat
       61 asnetlirel wgdrppatal aalrvyvsql rkflirhdld grwctlqtra pgyrlrvddg
      121 ildtvcfdrl calaagsaea grhelaarqy qealalrrgp tledlrerta lsgaalqyde
      181 awttalkrrv dldlrlgrhl eivgelrrlv aedplnegfc arlmmalhrs grsadalasy
      241 rrtrgqlvee lgiepslelr tahrtvladd aeiplgarvs t
//
LOCUS       WP_392022346             412 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces chartreusis].
ACCESSION   WP_392022346
VERSION     WP_392022346.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces chartreusis
  ORGANISM  Streptomyces chartreusis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Streptomyces chartreusis"
                     /db_xref="taxon:1969"
     Protein         1..412
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=45636
     Region          66..323
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mhivlvnrwp rfsdgirwdn eltryeefid hdkhrvsyvv dalgaegvlv dpariahfvq
       61 vedvndydal rsavqevtek agpvdqlial seftleiaar vrvalgipgp speqvavyrd
      121 kvrmkevlae agvrvprfap cadlescvaf agstgypvil kpvdgaasig vhrvddeatl
      181 relvptldlt ryeieefvtg vihhvdgfad arcqvpfqva svyvndclaf gsgsplgsvv
      241 lheselrtri edftreciav lgmydtpfhl elfvtesgel vflevggrvg gsevphlvnk
      301 lfgvnlyeaw lralsgesvd lppksgdpsg gwlvlpkpdg lplrvrrasp mkerfetiwr
      361 elvprpgqvl epggsydalh sgrfillhed qqrvtddihr iiatfefeve qp
//
LOCUS       WP_392022438             302 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Streptomyces pactum].
ACCESSION   WP_392022438
VERSION     WP_392022438.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pactum
  ORGANISM  Streptomyces pactum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces pactum"
                     /db_xref="taxon:68249"
     Protein         1..302
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32014
     Region          1..296
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mlldtaslyf rayfgvpdtv rapdgtpvna vrglldfiar lvqdhrpddl vacmdfdwrp
       61 gwrvelipty kahrvaeatp agvpdeeevp dtlspqvpvi davldavgia rvgaagyead
      121 dvigtltara tgpvdivtgd rdlyqlvdda ravrvlypvk gvgtlqvvde svlrekygvd
      181 grgyadlatl rgdpsdglpg vpgigektaa kllaahgdla giiaaaehpt sritpaqrrr
      241 llearpylav aprvvavapd valppvdpal psaprdpeal aalaerwglg gslqrllttl
      301 rr
//
LOCUS       WP_392022945             397 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC014894].
ACCESSION   WP_392022945
VERSION     WP_392022945.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014894
  ORGANISM  Streptomyces sp. NPDC014894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Streptomyces sp. NPDC014894"
                     /db_xref="taxon:3364931"
     Protein         1..397
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=43525
     Region          56..307
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mqmyvlalnp tdsvtegflp aarrlglsvt lltdqpdahr dryrevhpda eilacdvrdf
       61 havisavsgh rrpdavfsns dhlqtqtala agyfglpakd wratlrtkdk aqmrrcpsae
      121 pvravelaph qdpaellgpd lpfpcvvkpr egvasedvvh agdpaellrh caairarrpg
      181 aalvveeylp gelhtletlg dgrrlhvlgg frtelsplpy fieermtfvp ahpepivaqv
      241 laqldalgvg fgvchtefvv hrgrarliev nyraigdqcd lllaellgvp lfehilrthl
      301 geplpadlna rtdgaarlvy pladragtls aapgpadlti ddvrityrpt rrtgerhdly
      361 htnrdflgii ratgtdqtsv dravddflag lsweitp
//
LOCUS       WP_392022979             521 aa            linear   BCT 20-JAN-2025
DEFINITION  sodium:solute symporter family protein [Streptomyces sp.
            NPDC014894].
ACCESSION   WP_392022979
VERSION     WP_392022979.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014894
  ORGANISM  Streptomyces sp. NPDC014894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Henriquez,T., Wirtz,L., Su,D. and Jung,H.
  TITLE     Prokaryotic Solute/Sodium Symporters: Versatile Functions and
            Mechanisms of a Transporter Family
  JOURNAL   Int J Mol Sci 22 (4), 1880 (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Wright,E.M. and Turk,E.
  TITLE     The sodium/glucose cotransport family SLC5
  JOURNAL   Pflugers Arch 447 (5), 510-518 (2004)
   PUBMED   12748858
  REMARK    Erratum:[Pflugers Arch. 2004 Feb;447(5):813-5]
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Jung,H.
  TITLE     The sodium/substrate symporter family: structural and functional
            features
  JOURNAL   FEBS Lett 529 (1), 73-77 (2002)
   PUBMED   12354616
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001756
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Streptomyces sp. NPDC014894"
                     /db_xref="taxon:3364931"
     Protein         1..521
                     /product="sodium:solute symporter family protein"
                     /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=53020
     Region          36..492
                     /region_name="PutP"
                     /note="Na+/proline symporter [Amino acid transport and
                     metabolism]; COG0591"
                     /db_xref="CDD:440356"
ORIGIN      
        1 mteaaaaaaf lavvgaasll aararrlhar dtlpalegwa ladrglgagw swlllggtmf
       61 taytftavpa laygngapaf favpytvivc plafvllprl wsvardggyv tvadfvrary
      121 gspplalava ltgilatmpy lalqllgira vlaaggvgds svltgdlata vvfaglavat
      181 yrhglrapal isglkavavf gsaaaagwlv ldrfggpgal faaasarlgd rggpqaslll
      241 addqrlafas lalgsalall myphvltaaf aasgpsalrr vcvalpawta vlalfgllgi
      301 aavaagvrvp gpgaesavpm lvdrlmpapl tglvlgaitv galvpaavms vaaatsfvrn
      361 vyveyvhpta tpkrqvriar avslaakaga vafvlglrdq aainlqllgg vwilqifpav
      421 aiglytrrlh hralllgwaa gmvfgtvmvv rqgfspvvpl gpgghtveiy aglaalvlna
      481 gvavigtall rrwgvparpd ttplavrthq rprpqtgtss p
//
LOCUS       WP_392023107             326 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Streptomyces pactum].
ACCESSION   WP_392023107
VERSION     WP_392023107.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pactum
  ORGANISM  Streptomyces pactum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 326)
  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 326)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces pactum"
                     /db_xref="taxon:68249"
     Protein         1..326
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=32551
     Region          23..281
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mplvataelv aaaraagrgv aafnvitleh aeaiaagaea agrpavlqvs qnavrfhggr
       61 lgplaaamae varaadvpla lhldhvtsve llrsapahgf gsvmfdasal pyarnvaata
      121 davrwghehg vwveaelgrv ggkdgeppld ahapgvrtdp eeaagyaaat gvdalavavg
      181 sshamterta aldhglirrl rravpvplvl hgssgvpdae lrravtagmv kinigtalnt
      241 aftgavrahl aghpgvvdpr rylapardam artvahfigl ldgeaaaadg tapepsanta
      301 gtgnaagtrt gngnaagdpv tadggs
//
LOCUS       WP_392023235             407 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC014894].
ACCESSION   WP_392023235
VERSION     WP_392023235.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014894
  ORGANISM  Streptomyces sp. NPDC014894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Streptomyces sp. NPDC014894"
                     /db_xref="taxon:3364931"
     Protein         1..407
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=43458
     Region          53..305
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mallllnrrp ildrvptwlp gaslivvter saarsaptgd fvrteivddy tsprvdrlid
       61 avcatgrier vlttaesdvv raararerhg lpgqrtasal afrdklrmrr laarhgiavp
      121 aaavardagd vadfvrahgl pvvvkpadga gsvgvrvlrd rravracvlp agrthlverf
      181 vpgtvchvdg lmsegavlha vpsrylhpnl atatdgvpsv sgmlaprdpl arrleeaasa
      241 vvaalppvag ttafhaeffh tpedalvlce iacrpggcgi veahelatgv nlyaaqlrgq
      301 aglpvpgrep glprhgwawf pplpatlerl pescslpyah rfaahgetgv rhdgprsstd
      361 siaelvfrld dggadgnrdg vgdgsedvte rlrevedwws revrwaa
//
LOCUS       WP_392023242             391 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces chartreusis].
ACCESSION   WP_392023242
VERSION     WP_392023242.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces chartreusis
  ORGANISM  Streptomyces chartreusis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Streptomyces chartreusis"
                     /db_xref="taxon:1969"
     Protein         1..391
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=42786
     Region          52..301
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mrlyllalnp tdavsegflp aaarlgldvt vltdqpaahr rahpdievlg cdvrdfravi
       61 srvsthhrpd avftnsdhlq tqaalaadyf glpgkdwraa lrckdkaemr rrlaaagvdt
      121 vwsteltepv apgdapypcv lkpregvase dvvlvdgpee lvahakeile rrpgaallve
      181 eylpgdlftl etlgdgrvrh vlggfrtdls pppyfieerl tyvpahpgpv vaqvleqlda
      241 lgvgfgacht efvvragrar iievnyraig dqcdlllarl leiplfehil rthlgeplpa
      301 dlgarrdgaa rldypcadra gtlvdappat eldvegahlt yrplravger helyrtnrdy
      361 lgvlratgid qtavdravae flagrrweiq s
//
LOCUS       WP_392024348             326 aa            linear   BCT 20-JAN-2025
DEFINITION  quinone oxidoreductase family protein [Streptomyces chartreusis].
ACCESSION   WP_392024348
VERSION     WP_392024348.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces chartreusis
  ORGANISM  Streptomyces chartreusis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 326)
  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 326)
  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 326)
  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   4  (residues 1 to 326)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces chartreusis"
                     /db_xref="taxon:1969"
     Protein         1..326
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=33257
     Region          1..326
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 mkavqasqfg apsvltvtdl pdptpgpgqi aidvthaavg lidvylrqgl fkdapglpqp
       61 pyvpglevag tvralgegvt gftvgekvvs lsthgtggya svyvsdqtrv vstqdydidp
      121 alavaavpna lmahialtra ismsagesil ihgalgglaa afpgiarqlg asrvvgtlrs
      181 ermgtaaask lpydtivdsa qlpdvlgdek fdvivdpvgg lvrthsldll apsgrlllvg
      241 nasgdwdhgi dgnriwqgni tvagfnagsy vpahpeavqp aaeaalkavt ggladteiei
      301 lpladaatah erlenhatdg rivltp
//
LOCUS       WP_392024425             130 aa            linear   BCT 20-JAN-2025
DEFINITION  TOBE domain-containing protein [Streptomyces sp. NPDC014894].
ACCESSION   WP_392024425
VERSION     WP_392024425.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014894
  ORGANISM  Streptomyces sp. NPDC014894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 130)
  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 10007583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Streptomyces sp. NPDC014894"
                     /db_xref="taxon:3364931"
     Protein         1..130
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13737
     Region          1..127
                     /region_name="MopI"
                     /note="Molybdopterin-binding protein MopI [Coenzyme
                     transport and metabolism]; COG3585"
                     /db_xref="CDD:442804"
ORIGIN      
        1 mqsytigqaa rllgvspdta rrwadagrva thrdesgrrl iegrdlaafs ievgqsggde
       61 easytsarna fpgivtavkl gdvaaqveiq agphrlvsll treaveelgl evgmratarv
      121 kstnvhidlv
//
LOCUS       WP_392024544             308 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptomyces chartreusis].
ACCESSION   WP_392024544
VERSION     WP_392024544.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces chartreusis
  ORGANISM  Streptomyces chartreusis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 308)
  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 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   3  (residues 1 to 308)
  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   4  (residues 1 to 308)
  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 308)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Streptomyces chartreusis"
                     /db_xref="taxon:1969"
     Protein         1..308
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33373
     Region          70..296
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <181..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 msssttslik prlvhlsgsg pdldhavver greladgkrp saqppigpss hvlvvhtgts
       61 tnlrwsadgh arrerfhrgq slinpagwas rprweddvel mlvafdpawl ekladeggfr
      121 gtleiapdyh rndpflammv erlvleyeqk gpadtlyaqs lvqavaahvi katasrgagl
      181 apapsglppr llaqvtdyih thlaervald dlarvagvsp shftrvfras tgqsphqyvl
      241 gqrleqarra llttdtaiad iagtcgfadq shltrtmrrh lgltpsalrt drtqaattgn
      301 dddgrfea
//
LOCUS       WP_392024558             274 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces pactum].
ACCESSION   WP_392024558
VERSION     WP_392024558.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pactum
  ORGANISM  Streptomyces pactum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 274)
  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 274)
  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 274)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Streptomyces pactum"
                     /db_xref="taxon:68249"
     Protein         1..274
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30535
     Region          12..68
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          86..263
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 meierrprtp rekygeelrl rrmaagltqe tlservvcsp tlishfeagr rlpkpddaar
       61 idqalgtdgf farwredles kynhyfaava eleqqatliq qfaltlvpgv lqtedyagal
      121 frayrpnyta eeldefvvir tkrrrildgp srpvvwtlld eavlrrcvgg phvmaeqlrr
      181 itdlaeagrl rlhvlpfavg ahalqqsllt lmsfedsapv ayvegfltgn lvddpalvsa
      241 sqtayalals dalsqqesla lvraaaeeha hgrq
//
LOCUS       WP_392025003             413 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces chartreusis].
ACCESSION   WP_392025003
VERSION     WP_392025003.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces chartreusis
  ORGANISM  Streptomyces chartreusis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 413)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Streptomyces chartreusis"
                     /db_xref="taxon:1969"
     Protein         1..413
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43357
     Region          74..255
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          261..387
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mnvrpisgas vdgrggrgrt glaalagvll iavtacgggg gtdtgagdgk ggdsstaeak
       61 ksqavvtiap gdgaksvdts galkvtaakg kltdvevkdv kgnaidgkis gdggtwtpst
      121 hlaaatkytv havakdadgl eaakeadftt ltpkntfigr ftpedgskvg vgmpfslrfd
      181 rgitnpedve kaitvktepa vevaghwfgn drldfrpeky wksgtkvtve lnldgvegrd
      241 gvygeqdkkv tftigrnqvs vvdvktkkmk vtqdgkvvkt ipvttgkpgy dtwngqmvmt
      301 ekfvqtrmng dtvgydgeyd iddvphatrl tdsgtfihgn ywgggafgny nashgciglr
      361 dvkgawdkst paawffnhsm igdvvvvkns adatvapeng lngwnmswek wka
//
LOCUS       WP_392025106             345 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces pactum].
ACCESSION   WP_392025106
VERSION     WP_392025106.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pactum
  ORGANISM  Streptomyces pactum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Streptomyces pactum"
                     /db_xref="taxon:68249"
     Protein         1..345
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=34405
     Region          105..339
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mtesavtesp aagvptvata paaagvpavi rpararsarr lpvrtllcll pvvavavwav
       61 rhravvadgm drllaadpal llvavavtal swvaaactrq galvrrlpag rllatqfaag
      121 aanhllpsgl gagavnlrfm tvcgvplaqa ssalalylva gavgrlaltl vllaavpgal
      181 pldrllpdgv gvataglvav gvvvtlvlvv galrrvvrrf lvtvaheara vhrrparvla
      241 lwggavlfpa lqaaglvava lslgvrvpva hlalaylaat aaaalvptpg gigsveaalt
      301 ialvgtgvta asatavvlgy rlitiwlpll pgaltlavlv rckvl
//
LOCUS       WP_392025118             243 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces sp.
            NPDC014894].
ACCESSION   WP_392025118
VERSION     WP_392025118.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014894
  ORGANISM  Streptomyces sp. NPDC014894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616714
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Streptomyces sp. NPDC014894"
                     /db_xref="taxon:3364931"
     Protein         1..243
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25025
     Region          6..237
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 msveifrslh hdrapgdplv lpgpwdaaaa rafadagfea latpsagvaa slgyedgdtp
       61 agemfaavar ivrsvdvpvs adveagygls akelvarlle tgavgcnled sragalqdpg
      121 rhadwlaevr aeaggslfvn aridsflrgv adpaegaara rlyaaagadc vypimmppeh
      181 lpllseaari pvnaaprpgd grspaelgrl gaaritfgpy lqrraagavr eiaerlragd
      241 lvg
//
LOCUS       WP_392025257             424 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [unclassified Streptomyces].
ACCESSION   WP_392025257
VERSION     WP_392025257.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 424)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..424
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=44378
     Region          77..257
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          263..394
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mekrvmtdsk rrralmaasa alsgvlvlsa cgggdgggdk nggdsqsgkk tqaqvdeaaa
       61 kkvsdariai tpkngvtnas innaakvtvs egtltevklt taagaavkgt laadrkswqp
      121 dtalerstay klsvtakdsg gltahenssf ttvspdnsfi gnftpedgst vgvgmpvsin
      181 fnkpitnrkd vqkgitvstt ggqevvghwf nsqrldfrpd qywkegstvs lklaldgvea
      241 spgvvgvqqk tvkfkigrnq vstvdaatkt mtvtqdgktv rsipisagap stptyngemv
      301 isekfketrm ngatvgftds dgkgeydikd vphamrlsts gtfihgnywg kgifgkants
      361 hgcvgledvq gagdankaga wffnnsllgd vvivknskdk tiapdnglng wnmdwdkwka
      421 gsav
//
LOCUS       WP_392025269             211 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Streptomyces
            pactum].
ACCESSION   WP_392025269
VERSION     WP_392025269.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pactum
  ORGANISM  Streptomyces pactum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 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 10007860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Streptomyces pactum"
                     /db_xref="taxon:68249"
     Protein         1..211
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21869
     Region          122..210
                     /region_name="CadC1"
                     /note="DNA-binding winged helix-turn-helix (wHTH) domain
                     [Transcription]; COG3710"
                     /db_xref="CDD:442924"
ORIGIN      
        1 myvlaqsltp edlavladac aevgltlhhs epgsappdps dallvsfhrv gadpaggpta
       61 qelkeiggya vavldgiaag avlaavtngy sftlasplrr prlvetltyl khitppentq
      121 vltldgagsl hspskstpvt daeagllrml aarpgqivsr edlteatgge dvsrvtsvlk
      181 qklldidsga kllkiphlgf rlvgtvrqda r
//
LOCUS       WP_392025513             541 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: peptide ABC transporter substrate-binding protein
            [unclassified Streptomyces].
ACCESSION   WP_392025513
VERSION     WP_392025513.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11467924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..541
                     /product="peptide 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=58442
     Region          33..536
                     /region_name="OppA"
                     /note="ABC-type oligopeptide transport system, periplasmic
                     component [Amino acid transport and metabolism]; COG4166"
                     /db_xref="CDD:443327"
ORIGIN      
        1 mrgamrarwa acavavalta tacggggasg sgpdgivsas wgdpqnplep antnevqggk
       61 vldmvfrglk rydpktgeaq dmlaesiets dsvnftitvk dgwtfsngek vtaasfvdaw
      121 nygadlrnnq rnayffgyid gypalhpdsg eptatalsgl kvtgertftv rlsqkfstwp
      181 dtlgyaafap lpraffddha gwlakpvgng pytvdayarg sqmslrrwdg ypgadkalng
      241 gidlvvytdn ntaytnllag nldlvddvpa sqlknvrsdl gdryintpag iiqtlafpyy
      301 dkawnapdga klrtglsrai nrrqitdtif qktrtpakdw tspvlgvdgg fqdtlcgdsc
      361 eydaaaakkl vdeaggipgg qmkitynadt gshkdwvdav cnsinnalge dracvgnpig
      421 tfadfrgqit eskmpgpfra gwqmdypliq nflqplyytn assndgkwsn qdfddlvdra
      481 naesdtarav rtfqqaeevv rdemaaiplw yqngsagysh risnvalnpf svpvyneikv
      541 a
//
LOCUS       WP_392025839             358 aa            linear   BCT 20-JAN-2025
DEFINITION  heme/hemin ABC transporter substrate-binding protein [Streptomyces
            sp. NPDC014894].
ACCESSION   WP_392025839
VERSION     WP_392025839.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014894
  ORGANISM  Streptomyces sp. NPDC014894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Naoe,Y., Nakamura,N., Rahman,M.M., Tosha,T., Nagatoishi,S.,
            Tsumoto,K., Shiro,Y. and Sugimoto,H.
  TITLE     Structural basis for binding and transfer of heme in bacterial
            heme-acquisition systems
  JOURNAL   Proteins 85 (12), 2217-2230 (2017)
   PUBMED   28913898
REFERENCE   2  (residues 1 to 358)
  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   3  (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   4  (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   5  (residues 1 to 358)
  AUTHORS   Ho,W.W., Li,H., Eakanunkul,S., Tong,Y., Wilks,A., Guo,M. and
            Poulos,T.L.
  TITLE     Holo- and apo-bound structures of bacterial periplasmic
            heme-binding proteins
  JOURNAL   J Biol Chem 282 (49), 35796-35802 (2007)
   PUBMED   17925389
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Streptomyces sp. NPDC014894"
                     /db_xref="taxon:3364931"
     Protein         1..358
                     /product="heme/hemin 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=36561
     Region          87..358
                     /region_name="ChuT"
                     /note="ABC-type hemin transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG4558"
                     /db_xref="CDD:443619"
ORIGIN      
        1 mrwndrtvps vlsqpsarsv rrfrlvgaal taftvalvat gcggdsgsps gkdapakaet
       61 aaaadrvepl astprpelpv tvpsadgrkv tvdsadrivp ltgslseivy tlglggevva
      121 rdvtatfeqa eklpvvtrgh dvsaesvlsl kptvvlaetv sgpaesiqqi rdagiplvvv
      181 ktakglddvg aridavaeal gvpasgselk krtqdriaav qkdvprpadg ekprvaflyl
      241 rgtasvyllg gadsgassll eaagavdagk esglkkdfta itsealakaa pdailvmskg
      301 ldsvggvdgl vkipgvaqtp agmdrrvvsv pdgvllnygp rtdevltslv dqlyangk
//
LOCUS       WP_392026059             258 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: metallophosphoesterase family protein [unclassified
            Streptomyces].
ACCESSION   WP_392026059
VERSION     WP_392026059.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 258)
  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 258)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..258
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28213
     Region          5..248
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 mrgtrvnvvs dvhgnardla iagegadali clgdlvlfld yadhsrgifp dlfgvanadl
       61 ivslrtarrf dearelarrl wtelgvdrdt aiesavrkqy aelfaafptp tyatygnvdi
      121 pglwpeyarp gttvldgera eigglvfgfv ggglrtpmrt pyeisdeeya akvealgevd
      181 vlcshippdv peltydtvar rfergsaall dairrtrpry alfghvhqpl aarkrvgate
      241 cvnvghfast grpwtlaw
//
LOCUS       WP_392026113            1160 aa            linear   BCT 20-JAN-2025
DEFINITION  Rne/Rng family ribonuclease, partial [Streptomyces pactum].
ACCESSION   WP_392026113
VERSION     WP_392026113.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pactum
  ORGANISM  Streptomyces pactum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1160)
  AUTHORS   Kime,L., Jourdan,S.S. and McDowall,K.J.
  TITLE     Identifying and characterizing substrates of the RNase E/G family
            of enzymes
  JOURNAL   Methods Enzymol 447, 215-241 (2008)
   PUBMED   19161846
REFERENCE   2  (residues 1 to 1160)
  AUTHORS   Callaghan,A.J., Marcaida,M.J., Stead,J.A., McDowall,K.J.,
            Scott,W.G. and Luisi,B.F.
  TITLE     Structure of Escherichia coli RNase E catalytic domain and
            implications for RNA turnover
  JOURNAL   Nature 437 (7062), 1187-1191 (2005)
   PUBMED   16237448
REFERENCE   3  (residues 1 to 1160)
  AUTHORS   Li,Z., Pandit,S. and Deutscher,M.P.
  TITLE     RNase G (CafA protein) and RNase E are both required for the 5'
            maturation of 16S ribosomal RNA
  JOURNAL   EMBO J 18 (10), 2878-2885 (1999)
   PUBMED   10329633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..1160
                     /organism="Streptomyces pactum"
                     /db_xref="taxon:68249"
     Protein         <1..1160
                     /product="Rne/Rng family ribonuclease"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
     Region          430..828
                     /region_name="CafA"
                     /note="Ribonuclease G or E [Translation, ribosomal
                     structure and biogenesis]; COG1530"
                     /db_xref="CDD:441139"
ORIGIN      
        1 paaqtvaepa aeqsveeakp artrrrasrr atapagapaa deapaaeaap eavpaaeepa
       61 apavaesage eeqpetprrt rrratrkata epaaqqpaea aapaeepaaa epapraarrs
      121 raaapaaaeq apaagarete pepparlrrr avrpptavfq apvftepmfq tpetaaaaaa
      181 aeaqagrave eeadeeslrp arrrrrrrae lieerlraee apeateepgt deddeaeaea
      241 gaehehedes gdrpsrrrrr ggrrrrrgea adageesaeq apsgraaeet gaeavdaeda
      301 hdgeetedtg aggeepegep slgggstssr rrrrrrrrsg dggdtevaad dpertvvkvr
      361 eprkreeatd fqdavqsikg strleakkqr rregreqgrr rvpiiteaef larreaverv
      421 mvvrqsgert qigvleddvl vehfvnkeqa tsyvgnvylg kvqnvlpsme aafvdigkgr
      481 navlyagevn fealglangp rrietalksg qsvlvqvtkd pighkgarlt sqvslpgryl
      541 vyvpegsmtg isrklpdter arlkqilkki vpedagvivr taaegaseee lardvsrlqa
      601 qweeirkkak tgnapallyg epdmtvrvvr difnedfskv ivsgdeawet ihgyvshvap
      661 dladrlqrwt sdvdvfatyr ideqlmkald rkvwlpsggs lvidrteamv vvdvntgkft
      721 gqggnleetv trnnleaaee ivrqlrlrdl ggiividfid mvlesnrdlv lrrlleclgr
      781 drtkhqvaev tslglvqmtr krvgqglles fseqcvhcng rgvivhmdqp savggggkrk
      841 kkkaaaqqae vaeqaveave aatevaaeta aevaaetaae vaaevveerp apepafapde
      901 elyssaaeae aaalrsrprr ratrkatapa gsprsaeprp vvvpaeetrp epepeaapva
      961 pepaepvavt aepapapepe aapaprprrr atrkvsapag ppagaeeaav vvvsapaaps
     1021 rpaeeapvaa eapeapaaea qveaaaqvea gaeeapaeea agaepdaeda apakktarkt
     1081 aakkapakka takktaakkt takkaaaktt taktttakat akkttakktt akkttakkta
     1141 akktaaaaep sagsatadeg
//
LOCUS       WP_392026297             398 aa            linear   BCT 20-JAN-2025
DEFINITION  M20 metallopeptidase family protein [Streptomyces pactum].
ACCESSION   WP_392026297
VERSION     WP_392026297.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pactum
  ORGANISM  Streptomyces pactum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Lindner,H.A., Lunin,V.V., Alary,A., Hecker,R., Cygler,M. and
            Menard,R.
  TITLE     Essential roles of zinc ligation and enzyme dimerization for
            catalysis in the aminoacylase-1/M20 family
  JOURNAL   J Biol Chem 278 (45), 44496-44504 (2003)
   PUBMED   12933810
REFERENCE   2  (residues 1 to 398)
  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 11444961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Streptomyces pactum"
                     /db_xref="taxon:68249"
     Protein         1..398
                     /product="M20 metallopeptidase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42154
     Region          5..375
                     /region_name="AbgB"
                     /note="Metal-dependent
                     amidase/aminoacylase/carboxypeptidase [General function
                     prediction only]; COG1473"
                     /db_xref="CDD:441082"
ORIGIN      
        1 maqsavdaev tglergliel rrdihrhpem pgqewrtagv varelraagl avttgvgghg
       61 vvgilrgarp grtvayradm davppkdivg ggpapahacg hdihttvalg aaqvlarlrr
      121 rlsgtvvflf qpaeetlsga ravidagvlg rtgveeihal hcgpfpvgef avtpgygmpg
      181 qdkaevtlsg pdahdaarrl aaeigalatv slpqtpadie rivadaqmpn gplarfvavr
      241 agaqearvnv syrcwpqery tevredirrl atsyagaevh fptgpfpamv cpehdarmla
      301 rhlrrtlgrd avtvlhaafp pfsgedfaly ldrvpgtytf lgvrapgapi ttayphypdf
      361 apderaigig vramtgwiaq rthraqelpg ghglsggs
//
LOCUS       WP_392026300             570 aa            linear   BCT 20-JAN-2025
DEFINITION  peptide ABC transporter substrate-binding protein [Streptomyces
            pactum].
ACCESSION   WP_392026300
VERSION     WP_392026300.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pactum
  ORGANISM  Streptomyces pactum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 570)
  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 570)
  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 570)
  AUTHORS   ter Beek,J., 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 570)
  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 570)
  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 11467924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Streptomyces pactum"
                     /db_xref="taxon:68249"
     Protein         1..570
                     /product="peptide 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=61822
     Region          75..562
                     /region_name="OppA"
                     /note="ABC-type oligopeptide transport system, periplasmic
                     component [Amino acid transport and metabolism]; COG4166"
                     /db_xref="CDD:443327"
ORIGIN      
        1 mrgatptgag tsppapvrtt agtgtggaga rrsvclrwaa clvavaaaat acgggdgggg
       61 gggsvvrasw gdpqnplepa ntnevqggkv ldmvfrglkr ydpvtgeakd mvaerietsd
      121 qqnytvtikp gwtfsngekv taksfvdawn ygalldnqqr nayffeyieg ydkvhptegr
      181 ptaktlsglt vkddrtftvk ltqkfstwpe tlgynafapl praffddhda wvkkpigngp
      241 ylvdaytrgs vmklrrwdgy qgpdkarndg vdlrvytdnn taytdlqagn ldlvddipas
      301 qltnvksdlg dryinqpagi iqtlafpfyd krwggpdtdk lrrglsmain reqitdrifq
      361 ktrtpatdwt spvlgkdggy qsgvcgdace ydpeqakkli ddagglpggr vtitynadtg
      421 shkdwvdavc nsinnaldks kacvgnpvgt fadfrnqitd rqmkgpfrag wqmdypliqn
      481 flqplyytna ssndggwsnq rfddlvdran aeadtakais tfqdaegvla qempaiplwy
      541 qngsagysdr lsgvklnpfs vpvydqikvs
//
LOCUS       WP_392026358             343 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: gluconeogenesis factor YvcK family protein
            [unclassified Streptomyces].
ACCESSION   WP_392026358
VERSION     WP_392026358.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            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 10785358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..343
                     /product="gluconeogenesis factor YvcK family protein"
                     /GO_function="GO:0043743 - LPPG:FO 2-phospho-L-lactate
                     transferase activity [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=36505
     Region          20..331
                     /region_name="CofD"
                     /note="Archaeal 2-phospho-L-lactate transferase/Bacterial
                     gluconeogenesis factor, CofD/UPF0052 family [Carbohydrate
                     transport and metabolism, Coenzyme transport and
                     metabolism]; COG0391"
                     /db_xref="CDD:440160"
ORIGIN      
        1 mtarslrlrr lrksvtptgr rrgaqpkvva lgggrglsas laslrritgd ltavvtvadd
       61 ggssgrlree lgvlppgdlr kalaalcgdd dwgqtwsrvi qhrfqsqgdl hehavgnlli
      121 valweqlgdh vqaldlvgrl lgahgrvlpm savplelqal vrghdpdrpg evttvrgqat
      181 valtpgdvqs vhlvpndppa vpeavaavld adwvvlgpgs wfssviphll vpelldalve
      241 trarrvlsln lapqpgeteg fspqrhlevl grhapkltld vvladeaavp drdsladaak
      301 rlgaavelap vaspdsvskh dpellaaayd rifrmhgrig pwr
//
LOCUS       WP_392026480             635 aa            linear   BCT 20-JAN-2025
DEFINITION  caspase family protein [Streptomyces pactum].
ACCESSION   WP_392026480
VERSION     WP_392026480.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pactum
  ORGANISM  Streptomyces pactum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 635)
  AUTHORS   Van Opdenbosch,N. and Lamkanfi,M.
  TITLE     Caspases in Cell Death, Inflammation, and Disease
  JOURNAL   Immunity 50 (6), 1352-1364 (2019)
   PUBMED   31216460
REFERENCE   2  (residues 1 to 635)
  AUTHORS   Tsiatsiani,L., Van Breusegem,F., Gallois,P., Zavialov,A., Lam,E.
            and Bozhkov,P.V.
  TITLE     Metacaspases
  JOURNAL   Cell Death Differ 18 (8), 1279-1288 (2011)
   PUBMED   21597462
REFERENCE   3  (residues 1 to 635)
  AUTHORS   Zhang,J.H., Zhang,Y. and Herman,B.
  TITLE     Caspases, apoptosis and aging
  JOURNAL   Ageing Res Rev 2 (4), 357-366 (2003)
   PUBMED   14522240
REFERENCE   4  (residues 1 to 635)
  AUTHORS   Salvesen,G.S.
  TITLE     Caspases and apoptosis
  JOURNAL   Essays Biochem 38, 9-19 (2002)
   PUBMED   12463158
REFERENCE   5  (residues 1 to 635)
  AUTHORS   Villa,P., Kaufmann,S.H. and Earnshaw,W.C.
  TITLE     Caspases and caspase inhibitors
  JOURNAL   Trends Biochem Sci 22 (10), 388-393 (1997)
   PUBMED   9357314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..635
                     /organism="Streptomyces pactum"
                     /db_xref="taxon:68249"
     Protein         1..635
                     /product="caspase family protein"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=67421
     Region          1..251
                     /region_name="COG4249"
                     /note="Uncharacterized conserved protein, contains caspase
                     domain [General function prediction only]"
                     /db_xref="CDD:443391"
ORIGIN      
        1 mrtvyallvg iddypeddlr lrgcvadvra aerwltgrpd ltvrarplyd sdasraavld
       61 girghlgrgg pgdtallwfs ghgsreetad preatgmaqa lvchdssapg grplfdselg
      121 alldgiagrg ahvlavldcc ysggatrdet agrarsaawr pwwraprgrd aqggdpgrgr
      181 hvllaasrld epayedlldg ehrglfshtv ldtlgrhgta vtyrklhsrv harvqerrpl
      241 qhpdlvgrad gyvlsgdpap aapfllrhta sgwqvdcgsa hglrapggef tvlpedaapg
      301 eagrpghaap pgspghraga rvvvrevhpe tadveplgwl pgrderdrvy pvapsalafp
      361 ptpvavaggg pwhravtaal dtapglspae atagrraplc celddervrv vhpgvdmvrt
      421 lplrssgdvg rlvdclahma rwrrlrdlts pdpslsalvr vtleplrgtm tvspsgehvf
      481 tcgpagtlpr arvrihndsp hrlwcvlldl tdsyaaspel yegdfvgprr qavalagapv
      541 dlwlppdrpf rpgasvqdwl kllvteneln tapfvlpaws pdaptarggg gdggllrlsa
      601 pgtrsgsrdm gagsrpaadp grwgtalvpv rtvvp
//
LOCUS       WP_392026523             274 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces pactum].
ACCESSION   WP_392026523
VERSION     WP_392026523.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pactum
  ORGANISM  Streptomyces pactum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Streptomyces pactum"
                     /db_xref="taxon:68249"
     Protein         1..274
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=29968
     Region          1..253
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mdikllgpls veafgqsivp tagkprqila llsvyanqml pvptlmeeiw gsdmprsalt
       61 tlqtyilqlr rriaaaygpq apqaskdvla tryggyllea epgsvdvqey drlvsagnda
      121 ldagddvqas llfrqalsvw rgpalvdvrv gpileievar leesrlgvle rrieadlrlg
      181 rhaalltelt eltarhplhe glhaqcmaal yragrpwqal evyqglrarl vedlglepsp
      241 rlqklqqavl asdpaldfdl gagwrrpvld lfaa
//
LOCUS       WP_392026582             705 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: DNA gyrase/topoisomerase IV subunit B [unclassified
            Streptomyces].
ACCESSION   WP_392026582
VERSION     WP_392026582.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 705)
  AUTHORS   Tari,L.W., Trzoss,M., Bensen,D.C., Li,X., Chen,Z., Lam,T.,
            Zhang,J., Creighton,C.J., Cunningham,M.L., Kwan,B., Stidham,M.,
            Shaw,K.J., Lightstone,F.C., Wong,S.E., Nguyen,T.B., Nix,J. and
            Finn,J.
  TITLE     Pyrrolopyrimidine inhibitors of DNA gyrase B (GyrB) and
            topoisomerase IV (ParE). Part I: Structure guided discovery and
            optimization of dual targeting agents with potent, broad-spectrum
            enzymatic activity
  JOURNAL   Bioorg Med Chem Lett 23 (5), 1529-1536 (2013)
   PUBMED   23352267
REFERENCE   2  (residues 1 to 705)
  AUTHORS   Gadelle,D., Filee,J., Buhler,C. and Forterre,P.
  TITLE     Phylogenomics of type II DNA topoisomerases
  JOURNAL   Bioessays 25 (3), 232-242 (2003)
   PUBMED   12596227
REFERENCE   3  (residues 1 to 705)
  AUTHORS   Wang,J.C.
  TITLE     Cellular roles of DNA topoisomerases: a molecular perspective
  JOURNAL   Nat Rev Mol Cell Biol 3 (6), 430-440 (2002)
   PUBMED   12042765
REFERENCE   4  (residues 1 to 705)
  AUTHORS   Champoux,J.J.
  TITLE     DNA topoisomerases: structure, function, and mechanism
  JOURNAL   Annu Rev Biochem 70, 369-413 (2001)
   PUBMED   11395412
REFERENCE   5  (residues 1 to 705)
  AUTHORS   Roca,J.
  TITLE     The mechanisms of DNA topoisomerases
  JOURNAL   Trends Biochem Sci 20 (4), 156-160 (1995)
   PUBMED   7770916
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..705
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..705
                     /product="DNA gyrase/topoisomerase IV subunit B"
                     /EC_number="5.6.2.2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003918 - DNA topoisomerase type II
                     (double strand cut, ATP-hydrolyzing) activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006265 - DNA topological change [Evidence
                     IEA]"
                     /calculated_mol_wt=77214
     Region          20..699
                     /region_name="GyrB"
                     /note="DNA gyrase/topoisomerase IV, subunit B
                     [Replication, recombination and repair]; COG0187"
                     /db_xref="CDD:439957"
ORIGIN      
        1 mtaetsvpst alltaerdgs nytarhllvl egleavrkrp gmyigstdsr glmhclweii
       61 dnsvdealgg ycdhievilh edgsvevrdn grgipvdvep ktglsgvevv ltklhaggkf
      121 gggsyaasgg lhgvgasvvn alsarldvev drnsathsis frrgvpgift eqgpdspfdp
      181 angllkgkrv prtrtgtrvr ywadrqiflk eaklsletly qrarqtaflv pgltivvnde
      241 rdlegegksq eifrfdggis efceylaqdr avcdvlrltg qgtfketvpv lddrghmtpt
      301 evtrelgvdi alrwgtgyds riksfvniia tpkggthvtg fersitktvn evlrsakllr
      361 vaeddivkdd alegltavvt vrlaepqfeg qtkevlgtsa anrivanvva kelkafltst
      421 krdakaqara vlekavaaar triaarqhke aqrrktales sslpakladc rsddversel
      481 fivegdsalg taklarnsef qallpirgki lnvqkssvsd mlknaecgai iqvigagsgr
      541 tfdldaaryg kivllvdadv dgahirclll tlfqrymrpm veagrvfaav pplhrielvq
      601 pkkgqdkyvy tysdnelrqt lleyqrknir ykdsiqrykg lgemdadqla ettmdprfrt
      661 lrrinigdle saegvfdllm gnevaprkef itssaatldr srida
//
LOCUS       WP_392027692             215 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces coeruleorubidus].
ACCESSION   WP_392027692
VERSION     WP_392027692.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coeruleorubidus
  ORGANISM  Streptomyces coeruleorubidus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Streptomyces coeruleorubidus"
                     /db_xref="taxon:116188"
     Protein         1..215
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23075
     Region          2..213
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 mnsrervlgr vrraladvpr ddvpyeqavs rdyarehgdr saeqtvella enladyravv
       61 hrtdadglag liagllekrg sasvlvpsgl dggwlsrtgv trvtdraest preldrvdsv
      121 vtacavaiae tgtivldgsp dqgrrritlv pdhhicvvrv pgqvvssvpq glerldparp
      181 ltwisgpsat sdieldrveg vhgprtlevi lvdda
//
LOCUS       WP_392027694             291 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces pactum].
ACCESSION   WP_392027694
VERSION     WP_392027694.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pactum
  ORGANISM  Streptomyces pactum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Streptomyces pactum"
                     /db_xref="taxon:68249"
     Protein         1..291
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=32161
     Region          1..252
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mefavlgplk vseqgrlytp tapkqrqlla llllnanqvv strscieelw edtppnsals
       61 tiqsyilqlr ralgkipqig slqaarrvle trdggyllvv rsdeldvnaf tslvrqgrar
      121 lhrddaaasd llgralrvwq gsalsdvqvg pvlrahlvgl eeerisvqeq ridadlrlgr
      181 hhevigelsa lttkyptqey lhaqlmvalh rsgrrtqale vvqrlrrvmh delglepspr
      241 irslhqavla cdpvidnpmg tdsildlagr tepadarcrg gpgtvaderl r
//
LOCUS       WP_392027791             390 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces coeruleorubidus].
ACCESSION   WP_392027791
VERSION     WP_392027791.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coeruleorubidus
  ORGANISM  Streptomyces coeruleorubidus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Streptomyces coeruleorubidus"
                     /db_xref="taxon:116188"
     Protein         1..390
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=42298
     Region          52..296
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mrlyllalnp tdsvtegflp aaarlgldvt vltdqpgahr rtcpdievle cdvrdfravv
       61 arvsgrhrpd avftnsdhlq tqaalaaayf glpgkdwraa lrckdkaemr rrlaaagvdt
      121 vwsaeltepa pldapypcvv kpregvased vvlvdgpedl vtraeealer rpgttlvvee
      181 ylpgelhtle tlgdgrvrhv lggfrtelsp pphfvekrlt fvpahpepvv aqvlaqldal
      241 gvgfgachte fvvhdgrari ievnyrnigd qcdlllarll giplfelvlg thlgeplpag
      301 lgarrdgaal veypcadrag tladapaatd ltvdgvrlty rplravgerh elyrtnrdyl
      361 gvlratgtgq etvdrvaagf latcrweiqa
//
LOCUS       WP_392027850             384 aa            linear   BCT 20-JAN-2025
DEFINITION  M20 metallopeptidase family protein [Streptomyces coeruleorubidus].
ACCESSION   WP_392027850
VERSION     WP_392027850.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coeruleorubidus
  ORGANISM  Streptomyces coeruleorubidus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Lindner,H.A., Lunin,V.V., Alary,A., Hecker,R., Cygler,M. and
            Menard,R.
  TITLE     Essential roles of zinc ligation and enzyme dimerization for
            catalysis in the aminoacylase-1/M20 family
  JOURNAL   J Biol Chem 278 (45), 44496-44504 (2003)
   PUBMED   12933810
REFERENCE   2  (residues 1 to 384)
  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 11444961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Streptomyces coeruleorubidus"
                     /db_xref="taxon:116188"
     Protein         1..384
                     /product="M20 metallopeptidase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41149
     Region          5..375
                     /region_name="AbgB"
                     /note="Metal-dependent
                     amidase/aminoacylase/carboxypeptidase [General function
                     prediction only]; COG1473"
                     /db_xref="CDD:441082"
ORIGIN      
        1 mgkgavdaea arleggliel rrdihrhpel pgeerrtagv varelraagl tvttgvgghg
       61 vvgvlhgarp grtvayradm davppkdivg gghaaahlcg hdihttvalg vakvlarlrr
      121 hlsgtvvflf qpaeeslsga ralieagvle rtrveeihal hcgpfpvgrf avtggygmpg
      181 qdkaevtlrg pdapdaarrl aarigalatv tppqtpadie rmvtdaqtpd gpftrfvalr
      241 asaqetkvsv syrcwpqery tevreeirrl aepyvgaavs fpaepfpalv cpepdaralt
      301 rhlrrrlgrd svatlhsafp pfsgedyaly lervpgtytf lgvrapgapi ttsyphfpdf
      361 apdersigig vramagwiae rthr
//
LOCUS       WP_392027909             303 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces pactum].
ACCESSION   WP_392027909
VERSION     WP_392027909.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pactum
  ORGANISM  Streptomyces pactum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 303)
  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 303)
  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 303)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces pactum"
                     /db_xref="taxon:68249"
     Protein         1..303
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33491
     Region          41..85
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          120..298
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 maethadada sadadagrgp gqrrpepied gdetvdlfra vgkqvkllre ragltqrelg
       61 drlgygeeli ssvergrrtp qpefldaadd cleaggllki akedvvraka karvkhpawf
      121 rdyarlerea velsfystlt vpgllqtegy aravfasrqp lldeetieqr vaarlsrqei
      181 ttrwpppmvs aviqevvllq pfggravrkg qleqllrlgr mrnvqiqvmp tdreehagmg
      241 gpftlltpkg rpqlaylevq nlsrlitdpe evrvlatkyg sirgqaltpq dsliliekll
      301 gaa
//
LOCUS       WP_392028240             263 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nicotinamide mononucleotide transporter family
            protein [unclassified Streptomyces].
ACCESSION   WP_392028240
VERSION     WP_392028240.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Hemberger,S., Pedrolli,D.B., Stolz,J., Vogl,C., Lehmann,M. and
            Mack,M.
  TITLE     RibM from Streptomyces davawensis is a riboflavin/roseoflavin
            transporter and may be useful for the optimization of riboflavin
            production strains
  JOURNAL   BMC Biotechnol 11, 119 (2011)
   PUBMED   22136195
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Zhu,N., Olivera,B.M. and Roth,J.R.
  TITLE     Genetic characterization of the pnuC gene, which encodes a
            component of the nicotinamide mononucleotide transport system in
            Salmonella typhimurium
  JOURNAL   J Bacteriol 171 (8), 4402-4409 (1989)
   PUBMED   2546921
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..263
                     /product="nicotinamide mononucleotide transporter family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0034257 - nicotinamide riboside
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_process="GO:0034258 - nicotinamide riboside transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28838
     Region          4..210
                     /region_name="PnuC"
                     /note="Nicotinamide riboside transporter PnuC [Coenzyme
                     transport and metabolism]; COG3201"
                     /db_xref="CDD:442434"
ORIGIN      
        1 msafawlneq fsffgfpvyw sdflgnilal atvwlalrrs lvawpvqilg svllliasln
       61 vdlggnaarq iviiasaswg watwrrsrer egtinvrwas wrertvllva mvagtfafga
      121 llktteasfy pgapwwmvla dawifvgsil amytqarryv efwfawlavd lvgvplaihs
      181 elyfsgivya iffvmvligi rdwasrskeq giasplepai vlesrddtav avdspaapsv
      241 aeppaarpat etlsgpgapp aer
//
LOCUS       WP_392028450             225 aa            linear   BCT 20-JAN-2025
DEFINITION  4'-phosphopantetheinyl transferase family protein [Streptomyces
            coeruleorubidus].
ACCESSION   WP_392028450
VERSION     WP_392028450.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coeruleorubidus
  ORGANISM  Streptomyces coeruleorubidus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459479
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Streptomyces coeruleorubidus"
                     /db_xref="taxon:116188"
     Protein         1..225
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=24185
     Region          18..222
                     /region_name="EntD"
                     /note="4'-phosphopantetheinyl transferase EntD
                     (siderophore biosynthesis) [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2977"
                     /db_xref="CDD:442216"
ORIGIN      
        1 migellpqtv vtveayghes adaplypeea alvaravakr rrefavvrsc arrameklgv
       61 ppqpilpger gaprwpaglv gsmthcdgyc aaalvratdl aslgidaeah gplpegvlpa
      121 valpaeaerl rrlaaqrpev hwdrllfsak esvykawfpl tgkwldftea dieisadpge
      181 qprgtfratl lvpgpqvgdr rlghfdghwt adrglvatav avphd
//
LOCUS       WP_392028467             413 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [unclassified Streptomyces].
ACCESSION   WP_392028467
VERSION     WP_392028467.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 413)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..413
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43231
     Region          77..256
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          261..381
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 msstplrpap hrstpatapv rprdrrgrrs tvvaatglal llsacstggg sqddakggek
       61 kpaakpeisv nltgraaapg kpvtvklaeg elkdvkvaga kgaplggtvs kdggtwtsqr
      121 aaapgtsytv eattkdggsa raafataaag kvnklemtps kgstvgiaqp vsivfdhpvk
      181 nkaaverslk ittsndttgs wgwidhydgr sridwrpkey wrtgtevrlq aelngvdsgt
      241 aggwfvrdyd lsftigapqv vkvdlgtkrl klvrggetlr sipmsagtpg gvkrswggts
      301 vlmakegtin mnsetvglgd aydkmvdhsm rltwsgmyah aapwntahfg nanrssgcig
      361 msdgdaswly sqvrpgdpfe isgpghkgnp apgngygewn lswddwraks ala
//
LOCUS       WP_392028738             547 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HAL/PAL/TAL family ammonia-lyase [unclassified
            Streptomyces].
ACCESSION   WP_392028738
VERSION     WP_392028738.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Turner,N.J.
  TITLE     Ammonia lyases and aminomutases as biocatalysts for the synthesis
            of alpha-amino and beta-amino acids
  JOURNAL   Curr Opin Chem Biol 15 (2), 234-240 (2011)
   PUBMED   21131229
REFERENCE   2  (residues 1 to 547)
  AUTHORS   Louie,G.V., Bowman,M.E., Moffitt,M.C., Baiga,T.J., Moore,B.S. and
            Noel,J.P.
  TITLE     Structural determinants and modulation of substrate specificity in
            phenylalanine-tyrosine ammonia-lyases
  JOURNAL   Chem Biol 13 (12), 1327-1338 (2006)
   PUBMED   17185228
REFERENCE   3  (residues 1 to 547)
  AUTHORS   Baedeker,M. and Schulz,G.E.
  TITLE     Autocatalytic peptide cyclization during chain folding of histidine
            ammonia-lyase
  JOURNAL   Structure 10 (1), 61-67 (2002)
   PUBMED   11796111
REFERENCE   4  (residues 1 to 547)
  AUTHORS   Schwede,T.F., Retey,J. and Schulz,G.E.
  TITLE     Crystal structure of histidine ammonia-lyase revealing a novel
            polypeptide modification as the catalytic electrophile
  JOURNAL   Biochemistry 38 (17), 5355-5361 (1999)
   PUBMED   10220322
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..547
                     /product="HAL/PAL/TAL family ammonia-lyase"
                     /EC_number="4.3.1.-"
                     /GO_function="GO:0016841 - ammonia-lyase activity
                     [Evidence IEA]"
                     /GO_process="GO:0170035 - L-amino acid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57656
     Region          10..534
                     /region_name="HutH"
                     /note="Histidine ammonia-lyase [Amino acid transport and
                     metabolism]; COG2986"
                     /db_xref="CDD:442225"
ORIGIN      
        1 mnawtdparv eldgasltlr dvvrlsrptp hgrparavlh paaaaeaeks vrlrdrlmaa
       61 rkpiygvttg fgdsvtqqis peraaqlqhn liryhlngvg pdapadvvra tllirancla
      121 rgnsgirpqi ierlldhlda dilplvperg slgasgdlvp lcyiaaallg egeaqvgkrv
      181 ravadaqrea giapvalqak eglalingta fttafavlaa hdaariataa eiatafvsea
      241 llgnashfda flhrakphpg qitsaarlrd lldgsrlstt yeeildatga ldggdhreld
      301 rriqdhysvr capqvvgvlr dtlswvepwl ttevnastdn plfaadegrp hhggnfyagh
      361 vgqamdslkt atanvadlld rqlalivdpk fsgglpanlv ppaprseagl hhgfkgmqia
      421 asavtaealk talpatlfsr steahnqdkv smattaarda rtvneltgqv aaiallagaq
      481 aldlrgadaa aprtrsvhal irsrapfadr drrmdrdiaa varlisdgsl araagspder
      541 dtdaaas
//
LOCUS       WP_392028771             310 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Streptomyces coeruleorubidus].
ACCESSION   WP_392028771
VERSION     WP_392028771.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coeruleorubidus
  ORGANISM  Streptomyces coeruleorubidus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces coeruleorubidus"
                     /db_xref="taxon:116188"
     Protein         1..310
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32337
     Region          4..308
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mrpllrpprl vpgarvavva psgpvpeerl qagldvlrgw dldpvvaphv lgrhrefgyl
       61 agtdaqraad lqnawcdpav aavlcarggy gaqrmvdlld weamrsagpk vfagfsditv
      121 lhqafatrlg latlygpaaa gvdflkhara qehlratlfd pesvrtvtav spggttlvpg
      181 rargvtlggc lsllasdlgt phalagargg llliedvges pyrvdryltq llrtgwldgv
      241 agivlgswaa cgpyeelrav ladrlgglgv pvveefgfgh cegaltmplg lsveldastg
      301 tltfdapals
//
LOCUS       WP_392029284             261 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            coeruleorubidus].
ACCESSION   WP_392029284
VERSION     WP_392029284.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coeruleorubidus
  ORGANISM  Streptomyces coeruleorubidus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   4  (residues 1 to 261)
  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 18542080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Streptomyces coeruleorubidus"
                     /db_xref="taxon:116188"
     Protein         1..261
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29150
     Region          1..57
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
     Region          79..256
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mrmvgallal freaagytqk slgeifvvge qqiasieqgr rplkmdlaeq ldqlldtkga
       61 lvaalsempe vdlvplwaee fldrereaia issyenqvlp gllqteayaw avfrsrvpfy
      121 dedtiaqlva arierqgilh sknppitcfv vwepvlrapi ggrevwveql rhlracsdlp
      181 glmfqvlpln rtshaglngp fvlletpehq rlvytenqrg sqliadpnev ailtqkcaml
      241 rsqaltpedt rdlldrllge a
//
LOCUS       WP_392029470             333 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces coeruleorubidus].
ACCESSION   WP_392029470
VERSION     WP_392029470.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coeruleorubidus
  ORGANISM  Streptomyces coeruleorubidus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Streptomyces coeruleorubidus"
                     /db_xref="taxon:116188"
     Protein         1..333
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=34340
     Region          58..331
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 msrlrletlp aplpaaprrr fpaaarlvrp vlallplllv ggwalvdrra vyegaarlas
       61 adpgwllvaf vctcltwvaa acvrqgalpe rlppgllvas qfaagaanqv lpagigahav
      121 tlrflqrrgi plpratasla lyslvkpvar tvvllaflva fpdvlrfgal vpddrtllla
      181 aggallalaa tavtlvtvra lrrpvlgflr taltdarelh trpcrvlalw ggaaatpllq
      241 gsviatvgfs lglplswaqv ilallvagta vgavpapggi gpvdaalvft maafgapvat
      301 atatvigyrv ltvwlpllpg alvlsallhr kvl
//
LOCUS       WP_392029534             161 aa            linear   BCT 20-JAN-2025
DEFINITION  SRPBCC family protein [Streptomyces coeruleorubidus].
ACCESSION   WP_392029534
VERSION     WP_392029534.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coeruleorubidus
  ORGANISM  Streptomyces coeruleorubidus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 161)
  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 10008053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Streptomyces coeruleorubidus"
                     /db_xref="taxon:116188"
     Protein         1..161
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=17956
     Region          8..156
                     /region_name="YndB"
                     /note="Chalcone/flavanone-binding protein YndB,
                     AHSA1/START/SRPBCC domain [Lipid transport and
                     metabolism]; COG3832"
                     /db_xref="CDD:443044"
ORIGIN      
        1 msvttvdkdl dnltltliad faapvervwr lwadprqler wwgpptypat veehdltpgg
       61 evtyfmtgpe gdrhrgwwri tsvaeptsle ftdgfadddg kpkddmptms vavrlsehgg
      121 gtrmemrslf dsreqmeqli tmgmeeglke avgqidalla a
//
LOCUS       WP_392030032             286 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Streptomyces].
ACCESSION   WP_392030032
VERSION     WP_392030032.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 286)
  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 286)
  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 16111081
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..286
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32392
     Region          25..68
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(29..30,41,44,48..49)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          97..277
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 masnvnptvr rrrlglelrr lrelkgmtae evaerllvsq skisrlengr rsisqrdvrd
       61 lcgvyevddh rivdslmqma kdsrqqgwwh afgdipysvy igletdaasl rvyepqvvpg
      121 llqtrpyaea liagalpesg gadvekrvsv rmrrqerika delplrlwav ideaalhrvv
      181 ggeqlmreql eylielsllp hvtvqvlpfe mgahpgingq yailefpdat dssvvyiegv
      241 tsdlylekan dvhkysvmye hlraqalnve qtrafienia eryakp
//
LOCUS       WP_392031316             418 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces coeruleorubidus].
ACCESSION   WP_392031316
VERSION     WP_392031316.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coeruleorubidus
  ORGANISM  Streptomyces coeruleorubidus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 418)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Streptomyces coeruleorubidus"
                     /db_xref="taxon:116188"
     Protein         1..418
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=44958
     Region          57..228
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          251..366
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mshtaisrpr tvvsctllvi alcvgltacg sdgnplshrp ydaadqisfn apsegrkkad
       61 pdkplevvae dsdgritdvt aydaagryva gelaadggrw hstsplaana sytvrvsted
      121 edgapgrkvl tfdtgkttsk krlnvtfgpk agtygvgqpi taelsrpvkd rsqravvera
      181 lkvssmpatd gawhwvddkk lhyrpkdywp rqatiqvrsn legikigdrm rggkakplti
      241 ntadkviavt daaahqmtvy kndkivrrip vttgrpgydt rngvkvvlak egtvrmtsas
      301 igasdfydlm vhhsvrvtns geyvhaapws vgsqgsanvs hgctgmsten aawfyenire
      361 gdivkvmnsg gdtmtpfgng fgdwnlewkq wrtgsaltag tpegptpadr arlrpqsv
//
LOCUS       WP_392031606             469 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: alpha,alpha-trehalose-phosphate synthase
            (UDP-forming) [unclassified Streptomyces].
ACCESSION   WP_392031606
VERSION     WP_392031606.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 469)
  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 469)
  AUTHORS   Eastmond,P.J. and Graham,I.A.
  TITLE     Trehalose metabolism: a regulatory role for trehalose-6-phosphate?
  JOURNAL   Curr Opin Plant Biol 6 (3), 231-235 (2003)
   PUBMED   12753972
REFERENCE   3  (residues 1 to 469)
  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   4  (residues 1 to 469)
  AUTHORS   Elbein,A.D., Pan,Y.T., Pastuszak,I. and Carroll,D.
  TITLE     New insights on trehalose: a multifunctional molecule
  JOURNAL   Glycobiology 13 (4), 17R-27R (2003)
   PUBMED   12626396
REFERENCE   5  (residues 1 to 469)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 929-939 (1997)
   PUBMED   9334165
  REMARK    Erratum:[Biochem J 1998 Feb 1;329(Pt 3):719]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..469
                     /product="alpha,alpha-trehalose-phosphate synthase
                     (UDP-forming)"
                     /EC_number="2.4.1.15"
                     /GO_function="GO:0003825 - alpha,alpha-trehalose-phosphate
                     synthase (UDP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0005992 - trehalose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51364
     Region          11..469
                     /region_name="OtsA"
                     /note="Trehalose-6-phosphate synthase, GT20 family
                     [Carbohydrate transport and metabolism]; COG0380"
                     /db_xref="CDD:440149"
ORIGIN      
        1 mvseppaapv raqilvasnr gpisytlgdd galdarrggg glvsglsaig sdedalwvcs
       61 algdgdreav rrgigepgvl mldidaetha aayngvansv lwfvhhllyq tplepvfdad
      121 frrqwsayes ynrdfarala dhaadgaavl vqdyhlalvp gllrelrpdl righfshtpw
      181 apadyfrllp ddiaeqllrg llgadrtcfl trrwadlftd catrvlgeka vagarigvhg
      241 lgadagflte rahrpdvder maalreqigp drktivrvdr telsknivrg llayrelldt
      301 rpewrgrvvh vafaypsrqd lavyrdytae vrrvadsine eygdegwtpv vlhvkddfar
      361 slaayrladv alvnpirdgm nlvakeipvv sdagcalvls reagayeelg edaitvnpyd
      421 vtgtaealhr altmpaders rrtarlaaaa talpphrwfl dqlealral
//
LOCUS       WP_392032151             289 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces coeruleorubidus].
ACCESSION   WP_392032151
VERSION     WP_392032151.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coeruleorubidus
  ORGANISM  Streptomyces coeruleorubidus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415139
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces coeruleorubidus"
                     /db_xref="taxon:116188"
     Protein         1..289
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=31242
     Region          1..260
                     /region_name="LysX"
                     /note="Glutathione synthase, LysX or RimK-type ligase,
                     ATP-grasp superfamily [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism,
                     Translation, ribosomal structure and biogenesis, Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0189"
                     /db_xref="CDD:439959"
ORIGIN      
        1 mprialvtyd sgpepgkdqd lpllvralrd agaeavavpw dapgadwggf dlavirstwd
       61 yswrteefaa wvercgtltr lanppavvrw ntdkrylgdl aaagvpvvpt ryiapgepag
      121 lpdhqeyvvk ptsgagarfa arythdehet avrqlkrmha egftamvqpy mrsidsager
      181 alqffggrll hasrkgavla pgtpydadki ahpdlepwep taaeldvaar alaavpgqpe
      241 llyarvdlvt gpdgepcvme lelvepnlfl wlhpesvprv veavlaaag
//
LOCUS       WP_392032329             270 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces pilosus].
ACCESSION   WP_392032329
VERSION     WP_392032329.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pilosus
  ORGANISM  Streptomyces pilosus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Streptomyces pilosus"
                     /db_xref="taxon:28893"
     Protein         1..270
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=29819
     Region          5..245
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mtsdvrfeil gpprlvfdgr pqairsrnls vilttllvrs grvvsveeli gevwhqpprr
       61 ardaiyvyis klrerignga vdsqfpgytm lvrgqqldvq vfgryradgh lsmadgdheg
      121 aartwrkala lhrgslaggv ysgpilssfd swlqqsrtec veltawaqls aglyheaigf
      181 ltqqvprnpl neilhqqlml afllsrhraq alrvfgsacr tfserlgvep ggdlmkvhdi
      241 vrsddigrak ravssavaar vsshrspvst
//
LOCUS       WP_392032769             403 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces
            coeruleorubidus].
ACCESSION   WP_392032769
VERSION     WP_392032769.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coeruleorubidus
  ORGANISM  Streptomyces coeruleorubidus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  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 403)
  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
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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   5  (residues 1 to 403)
  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   6  (residues 1 to 403)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 403)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces coeruleorubidus"
                     /db_xref="taxon:116188"
     Protein         1..403
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42124
     Region          1..>61
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          81..391
                     /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 magtagtpgt prvlramndr aaldlllehg qlsrtrigkl tglskptasq llarleaagl
       61 vlatgttegr pgpnaqlyev npaagyaagl dvtpqrilaa vaditgrtvg rhelptpgrr
      121 tdtpvvqqvt daldgavkaa glarddihrl vigtpgafdp ttgrlryash lpgwhsptll
      181 delaaalpmp feyendvnlv alaeqrlgaa rdhtdfvllw nqeglgaalv lggrlhrgwt
      241 ggagevgflp vpgtplvrqv tkansggyqe lagsqavpgl arelgiedip agpyteaaah
      301 lvaraaetdd ephrrllqty atrlatglas lvsvldpelv vlsgasltsg getlralvqa
      361 eleelaasrp rlvvgdvreh pvlrgalesa lattrdevfd tsr
//
LOCUS       WP_392032903              96 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces pilosus].
ACCESSION   WP_392032903
VERSION     WP_392032903.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pilosus
  ORGANISM  Streptomyces pilosus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 96)
  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 96)
  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 96)
  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 11448557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Streptomyces pilosus"
                     /db_xref="taxon:28893"
     Protein         1..96
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10082
     Region          9..69
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
ORIGIN      
        1 mlmlkagams eeserlakal iafrkaegis vrelarrtql sqatirrhes drgglpvpfa
       61 arrfeevlgr vpgsipaaag gptdvglrpd sdgvtg
//
LOCUS       WP_392033270             358 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein
            [unclassified Streptomyces].
ACCESSION   WP_392033270
VERSION     WP_392033270.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 358)
  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 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   3  (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   4  (residues 1 to 358)
  AUTHORS   Igarashi,K., Ito,K. and Kashiwagi,K.
  TITLE     Polyamine uptake systems in Escherichia coli
  JOURNAL   Res Microbiol 152 (3-4), 271-278 (2001)
   PUBMED   11421274
REFERENCE   5  (residues 1 to 358)
  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   6  (residues 1 to 358)
  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 11430824
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..358
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0019808 - polyamine binding [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:0015846 - polyamine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=38159
     Region          39..356
                     /region_name="PotD"
                     /note="Spermidine/putrescine-binding periplasmic protein
                     [Amino acid transport and metabolism]; COG0687"
                     /db_xref="CDD:440451"
ORIGIN      
        1 mrtrrvprtv lavsaataca lvaagcsgsg adsgggggkk lniyawagei pesvvkkfea
       61 etgievtldt fdsnetmtak lssgsagydl vepsqytvqq ligqqliqpl dhsrikgldn
      121 laekfrdpsy dpgnkysvpw iwgttgfayn etcvpsatsw ktlfdkkhrg kvymldnmla
      181 ayiaglqitg sratstdege ieaatkaled qkkilagyns tnypqllstg qacaaqawsg
      241 tamakvvaan ekvhyvvpee ggsiwtdgls vpkgakntda ayqfinftlr peiaamatdd
      301 ggsastnaka refvkdkkal enpaiyasde aienadflld pgpamkhfqq gwtkvkas
//
LOCUS       WP_392033582             429 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces pilosus].
ACCESSION   WP_392033582
VERSION     WP_392033582.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pilosus
  ORGANISM  Streptomyces pilosus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 429)
  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 429)
  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
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 429)
  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   5  (residues 1 to 429)
  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   6  (residues 1 to 429)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 429)
  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 20170230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Streptomyces pilosus"
                     /db_xref="taxon:28893"
     Protein         1..429
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45109
     Region          <20..>60
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          80..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 magrngrtvr dlrranrtav lqrlyfdgpl srfelgpatg lssgsvsnvv adlvadglve
       61 eagsvdsdgg rprtllrvap asghmigvdv getrvrvelf dltltelara erpltqqrye
      121 vevivdhirs gidevlaaag laperllgvg igvpgiveht peggavvhgq tigwdaiple
      181 sllrtgsplp gsvpyfidng artlgqaemw fgagrgarna lvvlfgsgvg aclatpeveh
      241 gravewghlt vrvrgrrcrc galgcleaya gaesllarwr eeggavpggt deetaltaml
      301 aaaypagdta pdpvalavle etaeylgagl sdlinlfqpe rilmggwagl qlgsrflpav
      361 rrhalsyalr hpaekvtiel grlgpdavtv gaailpladf fgrggrrpap dpespppawr
      421 taledrapr
//
LOCUS       WP_392033638             213 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces pilosus].
ACCESSION   WP_392033638
VERSION     WP_392033638.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pilosus
  ORGANISM  Streptomyces pilosus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Streptomyces pilosus"
                     /db_xref="taxon:28893"
     Protein         1..213
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23213
     Region          2..213
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 mssrerilgr vrraladgpv ddtpyeravp rgylrehger tveetvdlla enladyravv
       61 hrtdseelpy limrllaerg sqsvlvppgl ppewmpaagp trvhdravst pheldrvdsv
      121 vtacavaiae tgtivldgsp dqgrrritlv pdhhicvvrv pdqvvssvpq alerldaarp
      181 ltwisgpsat sdieldrveg vhgprtlevv lvg
//
LOCUS       WP_392033699             293 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptomyces
            coeruleorubidus].
ACCESSION   WP_392033699
VERSION     WP_392033699.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coeruleorubidus
  ORGANISM  Streptomyces coeruleorubidus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 293)
  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 293)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 293)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 293)
  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   5  (residues 1 to 293)
  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   6  (residues 1 to 293)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Streptomyces coeruleorubidus"
                     /db_xref="taxon:116188"
     Protein         1..293
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32018
     Region          20..102
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          126..288
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mldrlnqamd qiernlgdsv dvtdlartac tseyhlrrlf salagmplse yirrrrltva
       61 gaevlsgdat lleiairygy gsgeafaraf rtmhgvgpgk arrtgaalvs qprlafrltv
      121 egnssmhyrv vdrpafsvmg fkarvplihs gpnqaiidfv rgldksavdq leklsdqepr
      181 gpvavcddld psraegteld yyhgvitsap assaapegtt alpvapgtwa vfttsgpapq
      241 aiqelwrdvf tewfpsnpyr trpgpeilrt hlspdgread aelwlpvere ttr
//
LOCUS       WP_392033857             266 aa            linear   BCT 20-JAN-2025
DEFINITION  caspase family protein [Streptomyces sp. NPDC014894].
ACCESSION   WP_392033857
VERSION     WP_392033857.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014894
  ORGANISM  Streptomyces sp. NPDC014894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Van Opdenbosch,N. and Lamkanfi,M.
  TITLE     Caspases in Cell Death, Inflammation, and Disease
  JOURNAL   Immunity 50 (6), 1352-1364 (2019)
   PUBMED   31216460
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Tsiatsiani,L., Van Breusegem,F., Gallois,P., Zavialov,A., Lam,E.
            and Bozhkov,P.V.
  TITLE     Metacaspases
  JOURNAL   Cell Death Differ 18 (8), 1279-1288 (2011)
   PUBMED   21597462
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Zhang,J.H., Zhang,Y. and Herman,B.
  TITLE     Caspases, apoptosis and aging
  JOURNAL   Ageing Res Rev 2 (4), 357-366 (2003)
   PUBMED   14522240
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Salvesen,G.S.
  TITLE     Caspases and apoptosis
  JOURNAL   Essays Biochem 38, 9-19 (2002)
   PUBMED   12463158
REFERENCE   5  (residues 1 to 266)
  AUTHORS   Villa,P., Kaufmann,S.H. and Earnshaw,W.C.
  TITLE     Caspases and caspase inhibitors
  JOURNAL   Trends Biochem Sci 22 (10), 388-393 (1997)
   PUBMED   9357314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Streptomyces sp. NPDC014894"
                     /db_xref="taxon:3364931"
     Protein         1..266
                     /product="caspase family protein"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=29472
     Region          17..258
                     /region_name="COG4249"
                     /note="Uncharacterized conserved protein, contains caspase
                     domain [General function prediction only]"
                     /db_xref="CDD:443391"
ORIGIN      
        1 matglslhig lntvdpakyg gwdgrlvace ndahdlaria gdagfetsvv ltadgtvkni
       61 tselrkaaer lvrddillft ysghggqvpd ttgpddepdr rdetlvlydr eflddelrre
      121 farfadgvri lvfldschsg savelapgag aavrampddk qreiyerdrd ffqglqrrlr
      181 edrgreepas allisacqdd qtasdgpvng lftetllkvw nhgaftedyr tfhedivnrm
      241 prnqtpnlyl lgspgedfla qrpftv
//
LOCUS       WP_392034801             405 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces pilosus].
ACCESSION   WP_392034801
VERSION     WP_392034801.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pilosus
  ORGANISM  Streptomyces pilosus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 405)
  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 405)
  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
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 405)
  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   5  (residues 1 to 405)
  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   6  (residues 1 to 405)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 405)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 405)
  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 18565976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Streptomyces pilosus"
                     /db_xref="taxon:28893"
     Protein         1..405
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42007
     Region          12..107
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
     Region          81..393
                     /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 magtagppgt prvlramndr taldlllehg plsrsrigrl tglskptasq llarleaagl
       61 vlatgttegr pgpgaqlyev npaaahaagl dvsprriraa vadltgrtvg rfelptpgrr
      121 spapavqqvt daldgavkaa glcrsdihhl vigtpgafdp ntgrlryash lpgwhspall
      181 delaaalpmp fayendvnlv alaeqrrgaa rdhtdfvllw neeglgaalv lggrlhrgwt
      241 ggagevgflp vpgtplvrqv gransggfqe lagaqavpvl arelgvrdip pgpyteqaaa
      301 llaraaaspp gdgperrllr ayatrlatgl aslvsvldpe lvvlsgtglt sggevlralv
      361 qaeleelaap rprlvlgdvr ehpvlrgale salaatrdev fdtsr
//
LOCUS       WP_392034938            1400 aa            linear   BCT 20-JAN-2025
DEFINITION  Rne/Rng family ribonuclease [Streptomyces pilosus].
ACCESSION   WP_392034938
VERSION     WP_392034938.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pilosus
  ORGANISM  Streptomyces pilosus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1400)
  AUTHORS   Kime,L., Jourdan,S.S. and McDowall,K.J.
  TITLE     Identifying and characterizing substrates of the RNase E/G family
            of enzymes
  JOURNAL   Methods Enzymol 447, 215-241 (2008)
   PUBMED   19161846
REFERENCE   2  (residues 1 to 1400)
  AUTHORS   Callaghan,A.J., Marcaida,M.J., Stead,J.A., McDowall,K.J.,
            Scott,W.G. and Luisi,B.F.
  TITLE     Structure of Escherichia coli RNase E catalytic domain and
            implications for RNA turnover
  JOURNAL   Nature 437 (7062), 1187-1191 (2005)
   PUBMED   16237448
REFERENCE   3  (residues 1 to 1400)
  AUTHORS   Li,Z., Pandit,S. and Deutscher,M.P.
  TITLE     RNase G (CafA protein) and RNase E are both required for the 5'
            maturation of 16S ribosomal RNA
  JOURNAL   EMBO J 18 (10), 2878-2885 (1999)
   PUBMED   10329633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1400
                     /organism="Streptomyces pilosus"
                     /db_xref="taxon:28893"
     Protein         1..1400
                     /product="Rne/Rng family ribonuclease"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=147517
     Region          633..1032
                     /region_name="CafA"
                     /note="Ribonuclease G or E [Translation, ribosomal
                     structure and biogenesis]; COG1530"
                     /db_xref="CDD:441139"
ORIGIN      
        1 mlepnepteg sepntpsdtl pprrrraasr pagppaatag ttaaetvtta aptaesadtp
       61 gpagladtpg saateekpev aaprrrravr raaapagapa aaeaaetvvp atpaaerata
      121 apepvaaaes pedaaprrtr rratrtvttp pagpeatgtp dapgtpeate atasagaaea
      181 papaeaaeda aprrtrrrat rtaaapapta eadvtadgae qaqtpaeqaq pagtdgtded
      241 aaprrtrrra arrasapaga pvtagtaegd adepaqatpt aeeapvtede kpeqapapte
      301 rtpqadeapa ddaaprrrrr avrkaaagfa epartargad sadsdeaegs prrparpava
      361 vfqppvftep rfqtperaaa eaaaevvapd gpeeeteefa eeqpaasrrr rrrrgagdea
      421 eaaapaaeta pathaedead eadepaddha dtddqddses sgarrrrrrg grrrrrgesa
      481 dsdveggepg dedtdteria seqaaqdaed taeqteedae dredrddsgg ssssrrrrrr
      541 rrragdsgge gdattddper tvvkvreprk asepsdevqs ikgstrleak kqrrregreq
      601 grrrvpiite aeflarreav ervmvvrqyg drtqigvled gvlvehyvnk eqatsyvgnv
      661 ylgkvqnvlp smeaafidig kgrnavlyag evnfealgmg hgprriesal ksgqsvlvqv
      721 tkdpighkga rltsqvslpg rylvyvpegs mtgisrklpd tersrlktil kkivpedagv
      781 ivrtaaegas edelrrdver lqaqweeikk ksknggnapt llygepdmtv rvvrdifned
      841 fskvvvsgdd awetihgyvs hvapdlagrl srwtsevdvf atyrideqla kaldrkvwlp
      901 sggslvidrt eamvvvdvnt gkftgqggnl eetvtrnnle aaeeivrqlr lrdlggiivi
      961 dfidmvlesn rdlvlrrlle clgrdrtkhq vaevtslglv qmtrkrvgqg llesfsetcv
     1021 hcngrgvlvh ldqpaaaggg skrrkrarag gaeapheheh eiagtaeqea eaeaesvaev
     1081 aagtaepaal papeftpdee lyssaaeaea aatrgrtrrr asrrasapag apkretdraa
     1141 rtaevpqapk aadertgepv aaeepvptaq dvtaaeeaar pvqpesaada laepaaveda
     1201 vvpeeaapka rtrrratrkv sapagspaga eaavvtvaep arteeapaae eapaeapapa
     1261 qpeaparprr ravrkpstst asedtavvvv psapaeeqap aeepaaaste tadgeaeaap
     1321 akktarkaak katakkaatk ktttakktaa kkttakkata tktaaktaaa kkttakkaas
     1381 kktaaaeqqp sssvtatted
//
LOCUS       WP_392034940             527 aa            linear   BCT 20-JAN-2025
DEFINITION  complex I subunit 4 family protein [Streptomyces sp. NPDC014894].
ACCESSION   WP_392034940
VERSION     WP_392034940.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014894
  ORGANISM  Streptomyces sp. NPDC014894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 527)
  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 527)
  AUTHORS   Galemou Yoga,E., Angerer,H., Parey,K. and Zickermann,V.
  TITLE     Respiratory complex I - Mechanistic insights and advances in
            structure determination
  JOURNAL   Biochim Biophys Acta Bioenerg 1861 (3), 148153 (2020)
   PUBMED   31935361
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Friedrich,T. and Scheide,D.
  TITLE     The respiratory complex I of bacteria, archaea and eukarya and its
            module common with membrane-bound multisubunit hydrogenases
  JOURNAL   FEBS Lett 479 (1-2), 1-5 (2000)
   PUBMED   10940377
REFERENCE   4  (residues 1 to 527)
  AUTHORS   Walker,J.E.
  TITLE     The NADH:ubiquinone oxidoreductase (complex I) of respiratory
            chains
  JOURNAL   Q Rev Biophys 25 (3), 253-324 (1992)
   PUBMED   1470679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Streptomyces sp. NPDC014894"
                     /db_xref="taxon:3364931"
     Protein         1..527
                     /product="complex I subunit 4 family protein"
                     /GO_component="GO:0045271 - respiratory chain complex I
                     [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048039 - ubiquinone binding [Evidence
                     IEA]"
                     /GO_process="GO:0015990 - electron transport coupled
                     proton transport [Evidence IEA]"
                     /GO_process="GO:0042773 - ATP synthesis coupled electron
                     transport [Evidence IEA]"
                     /calculated_mol_wt=54737
     Region          12..524
                     /region_name="NuoM"
                     /note="NADH:ubiquinone oxidoreductase subunit 4 (chain M)
                     [Energy production and conversion]; COG1008"
                     /db_xref="CDD:440632"
ORIGIN      
        1 midisesvmq fllafivvgp llgavaallp appglrgknp gqavlrhgvt vtgailaaai
       61 alvigfdhdr psrmqaqtdi swipaldvrv hlgvdgislp llvltalltf lcalysyykm
      121 pegpspkgfv alllvlesgt lltfavldlv lfflafemvl ipmyfliarw ggrarraaaw
      181 kfilytllgs vimllgllli glqagtfdmv alatdngrgl tlstqviavl aigiglavkt
      241 pmwplhswlp dahtaaptvg svllagvllk mgtygfvril lpaapdgmrv fapylaafav
      301 vgiiygslac lalakkgagg dlkrliayss vghmgfvllg iatmtptgvn galfaniahg
      361 litgllfflv galkdrygta dldtlagaag aalygsaprl gallafaava slglpglagf
      421 wgemlalfga fdpaaglsrp afltfmaigg fgtlltaayl livvrrvcmg vprpggretr
      481 aiadvqtyel vtwsplvalt vlaglwpavl lgltdpavqk llaggks
//
LOCUS       WP_392035453             528 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Streptomyces
            coeruleorubidus].
ACCESSION   WP_392035453
VERSION     WP_392035453.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coeruleorubidus
  ORGANISM  Streptomyces coeruleorubidus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 528)
  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 528)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Streptomyces coeruleorubidus"
                     /db_xref="taxon:116188"
     Protein         1..528
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=56419
     Region          264..441
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 marvpaavls vlnpirkaph altrryrsrq apatvelvpq phpwsravgl vavvllgawl
       61 gllvvgnvrv pvgpmnttmt lrpsftggtk inisplgalq ldshiapvrl dvnvdqldpe
      121 rsqalvdhpe rlsglqdevt qdvgrgtldl avrssvavvg gatalglavy rrprralaag
      181 glaltllaas ggtafatwrp dsvlepkfsg lltsapslvg narsivtefd vyqkelarlv
      241 tnvtklydat stlpayapdp stirvlhvsd ihlnpaswki iaslveqykv dvivdsgdtm
      301 dhgtaaengf ldpiedlgap yvwvrgnhds mitqrylegl knvhvlddgr aktikglrfa
      361 gigdpqftpd rskqpgneqs qelagarlat alrdqrtvgt pvdiaiahep saarevdgev
      421 plvlaghvhh demevlkygt rlriegstgg sglraiegkh pdpieasily fdrdnrrlqa
      481 wdeielgglg lttaevsrhi peenqpgatq sptapatesp sqsptpsp
//
LOCUS       WP_392035587             544 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Streptomyces pilosus].
ACCESSION   WP_392035587
VERSION     WP_392035587.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pilosus
  ORGANISM  Streptomyces pilosus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 544)
  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 544)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Streptomyces pilosus"
                     /db_xref="taxon:28893"
     Protein         1..544
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=57642
     Region          265..458
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 marvpsavtn avhrirripr altrrhrsrr papvtaglap aarpwtraag lvavvvlgaw
       61 lgllvvgnvr vpvgpmnttm tlrpsftggt kinvsplgal qldshtapvr ldvnvdqldp
      121 ersqalvdhp erlsglqdev trdiahgtad lavrscvavv tgatalgllv yrrprralaa
      181 gglaltllaa sggtayatwn pdsvleprfs gllssapslv gdarsivtef dvyqkelarl
      241 vtnvtklyda tstlpayqpd pttlrvlhvs dihlnpaswk iiaslveqyr vdvivdtgdt
      301 mdhgtaaeng fldpiedlga pyvwvrgnhd srvtqryleg lenvhvlddg raktvaglrf
      361 agigdpqftp drsartgaeq sqelagarla salrdqraag tpvdvalahe psaarevdgt
      421 vplvlaghih reetevmryg trlrvegstg gsglraiegk ypdpietsil yfdrdsrrlq
      481 awdsielggl glttaevsrh lpeenqpgan tspapsgsps sspsgppaas ppspspgsrs
      541 tpap
//
LOCUS       WP_392035964             310 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: S66 peptidase family protein [unclassified
            Streptomyces].
ACCESSION   WP_392035964
VERSION     WP_392035964.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..310
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32864
     Region          6..308
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mtlapltrpr rlrhgdrvav vapsgpvpdd rldegleilr swgldpvvmp hvrgrhrqfg
       61 ylsaydgdra rdlteawcdp svaavlcarg gygvqrmtdr ldwtairaag pkpfvgysdv
      121 talheafalr aglatlhgpm vgtltflkde ttreslratl fepgtarvig rptaralvpg
      181 rargvtfggc asllaadagt pharasaegg lliledvges dyrldrvltq llrggllagv
      241 tgvalgswae cgpyervrev lrdrlgglgv pvveelgfgh gdvnltvplg vtavldadag
      301 tltleepalr
//
LOCUS       WP_392036068             357 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            coeruleorubidus].
ACCESSION   WP_392036068
VERSION     WP_392036068.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coeruleorubidus
  ORGANISM  Streptomyces coeruleorubidus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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   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   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Streptomyces coeruleorubidus"
                     /db_xref="taxon:116188"
     Protein         1..357
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38796
     Region          5..340
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 mdtttpvfsv eglwkvfgpk adrvpadpel taldpaelra rtgctaavrd vsfdvrkgev
       61 fvvmglsgsg kstlvrcltr lieptagtia idgedvramd rsrlrelrrh raamvfqhfg
      121 llphrtvldn vaygleiqgm gkaerreraa evvakvgleg mehrrpgqls ggqrqrvgla
      181 ralavdpevl lfdepfsald pmirrdmqee vvrlhqeegr tmvfithdlq ealklgdria
      241 lmrdgrvvql gtpeeivgsp addyvrefvr dvpreqvmtv rtamrspsad qdgsgpavrp
      301 eatvseaiea varagaparv mdegrcvgvi dsdtllgvva gteqpappgt eqpkeav
//
LOCUS       WP_392036076             239 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces
            coeruleorubidus].
ACCESSION   WP_392036076
VERSION     WP_392036076.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coeruleorubidus
  ORGANISM  Streptomyces coeruleorubidus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616714
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Streptomyces coeruleorubidus"
                     /db_xref="taxon:116188"
     Protein         1..239
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24689
     Region          7..238
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 msktdvfrdl hqnrvpgdpl vlpgpwdaas arvfaeagfp alatpsagva aslgyedgqv
       61 pademfaava rivravdvpv sadveggygl apkelverll eagvvgcnle dseggvlkdp
      121 rahadwlaev rsaaadrlfv narvdtftcg vadperaier aalyvaagad cvypigappe
      181 vlpllragir gpinvgapte ggptpaelga rgatritfgp glqrraaral reiaeglrp
//
LOCUS       WP_392036236             347 aa            linear   BCT 20-JAN-2025
DEFINITION  BMP family lipoprotein [Streptomyces coeruleorubidus].
ACCESSION   WP_392036236
VERSION     WP_392036236.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coeruleorubidus
  ORGANISM  Streptomyces coeruleorubidus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Yousief,S.W., Bahey-El-Din,M. and Zaghloul,T.I.
  TITLE     Immunization with the basic membrane protein (BMP) family ABC
            transporter elicits protection against Enterococcus faecium in a
            murine infection model
  JOURNAL   Microbes Infect 22 (3), 127-136 (2020)
   PUBMED   31585177
REFERENCE   2  (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   3  (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   4  (residues 1 to 347)
  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   5  (residues 1 to 347)
  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 11448319
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Streptomyces coeruleorubidus"
                     /db_xref="taxon:116188"
     Protein         1..347
                     /product="BMP family lipoprotein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /calculated_mol_wt=35750
     Region          34..345
                     /region_name="Med"
                     /note="Lipoprotein Med, regulator of KinD/Spo0A, PBP1-ABC
                     superfamily, includes NupN [Signal transduction
                     mechanisms]; COG1744"
                     /db_xref="CDD:441350"
ORIGIN      
        1 mrriskltrv avgvaslglv atacggtssd ngdsdskdrg vaiaydvggr gdqsfndaay
       61 agltkakdef gyqtadiept egetsadkeq rlvslarqgy npvigvgfvy gpameaaaak
      121 ypdttfgivd svvegknvas lvfaeeqasy lagvaaakat ksdvvgfvgg vdtplihkfe
      181 agykqgvedt kpgvqvlsqy ltqtaeeggf sspdkgkaaa egqiekkadv lyaaaglsgq
      241 gvieaaakak vwaigvdsdq ykhpalapyk nyiltsalkd vggavyalsk svqdgkpltg
      301 tqtfdlkvng vglsesnpef akvaglkdav ekakqgiddg sikvkte
//
LOCUS       WP_392036358             416 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces coeruleorubidus].
ACCESSION   WP_392036358
VERSION     WP_392036358.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coeruleorubidus
  ORGANISM  Streptomyces coeruleorubidus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 416)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Streptomyces coeruleorubidus"
                     /db_xref="taxon:116188"
     Protein         1..416
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43733
     Region          67..248
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          255..386
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mtvskrrkgl tvasallggv lmlsacsggd dsasggdggd ssqskvdeaa akkaseaqik
       61 itpedgsdna sinnsaavtv akgtltsvkm ttsdgtevsg qisadkkswk pstqlerstt
      121 yklaaeakds egrvahenas fttvspansf ignftpddgt tvgvgmpvsi nfdkaitnka
      181 dvqkgvkvst tsgqevachw fnanrmdcrp edywkegstv tlklaldgvq gaegvygvqq
      241 ktvtfkvgrn qvsyvdaktk qmkitqdgkv vrtipisags penktyqgim vmsekfketr
      301 mngatvgftd ddgkgeydik dvphairlss sgtfihgnyw gaksifgnvn tshgcvglqd
      361 akgaddpntp gawfynnsmi gdvvvventg dktiapdngl ngwnmswadw kagsav
//
LOCUS       WP_392036938             918 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces pilosus].
ACCESSION   WP_392036938
VERSION     WP_392036938.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pilosus
  ORGANISM  Streptomyces pilosus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 918)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 918)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..918
                     /organism="Streptomyces pilosus"
                     /db_xref="taxon:28893"
     Protein         1..918
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=97733
     Region          642..917
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mkqqgahpgd aegspdassr pdtadpgrpd pdtahidele gdepllparv hrpsdlmrll
       61 ggvlavvvll aiaafahgtt sgleqditkg tgqapdllik iaglassiai llvpvafaie
      121 rlikrdglri adgvlaavla hgvtlatdlw varaapdsiq daltqpspgd ihaltdpvhg
      181 ylapviaymt avgmsrrprw ravlwvvlll dafsmlvtgy ttpfsiiltv ligwtvaygt
      241 lyavgspnvr ptgrtlmagl rtvgfrpvta sreeapdase tgdrgrryfv tledgppldv
      301 tvvdreqqaq gffyrawrnl alrgfatrss lqslrqaleq eallayaaia aganapklia
      361 tselgpdavm lvyehsggrt ldslpdeeit dellrdtwhq vralqsrria hrrlvgdail
      421 vdpsgtvilt dlrggeiaag elllrmdvsq llvtlglrvg aeravasals vlgpdavadc
      481 lpmlqpials rstratlrrl areraerere avleasrqsr pvraelsgsh daaaertsfd
      541 gtadrsdrsd rsdrsdrsdk kvvraeqrae kraidealee areedlltqi rhevlrirpq
      601 apveparler vrprtlisli agaigayfll tqlthiefgp lianaewgwv aaavlfsaas
      661 yvaaamallg fvpervpfvr tvaaqvagsf vkivapaavg gvalntrflq ragvrpglav
      721 asvgasqlfg lgchilmlla fgyltgtekt pslspsrtvi gglltvavlv lvvtsvpflr
      781 kfvvtrvrsl fagvvprmld vlqrpqklvt giggmlllta cfvmcldasi rafgdettsv
      841 siasvavvfl agnalgsaap tpggvgavea tltvgliavg lpkevaapav llfrlltlwl
      901 pvlpgwiafn hltrkaal
//
LOCUS       WP_392037248             349 aa            linear   BCT 20-JAN-2025
DEFINITION  BMP family lipoprotein [Streptomyces pilosus].
ACCESSION   WP_392037248
VERSION     WP_392037248.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pilosus
  ORGANISM  Streptomyces pilosus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Yousief,S.W., Bahey-El-Din,M. and Zaghloul,T.I.
  TITLE     Immunization with the basic membrane protein (BMP) family ABC
            transporter elicits protection against Enterococcus faecium in a
            murine infection model
  JOURNAL   Microbes Infect 22 (3), 127-136 (2020)
   PUBMED   31585177
REFERENCE   2  (residues 1 to 349)
  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   3  (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   4  (residues 1 to 349)
  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   5  (residues 1 to 349)
  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 11448319
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Streptomyces pilosus"
                     /db_xref="taxon:28893"
     Protein         1..349
                     /product="BMP family lipoprotein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /calculated_mol_wt=35749
     Region          38..347
                     /region_name="Med"
                     /note="Lipoprotein Med, regulator of KinD/Spo0A, PBP1-ABC
                     superfamily, includes NupN [Signal transduction
                     mechanisms]; COG1744"
                     /db_xref="CDD:441350"
ORIGIN      
        1 mrristltra avgvaslala atacggtssd sndsggsked lgvaiaydig gkgdqsfnda
       61 ayagltkakd efgyktadve ptegetdadk eqrlsslakq gydpvigvgf aygpameava
      121 akypdttfgi vdsvvegdnv aslvfaeeqa sylagvaaak atktktvgfv ggvdiplihk
      181 fqagyeqgvk dtdpavkvip qyltqtaeeg gfsspdkgka aaegqiekka dviyqaagls
      241 gqgvieaaak akvwaigvds dqykqealap yrdyiltsal kdvggavyal sksvqddkpl
      301 tgtqvfdlkv dgvglsdsnp kmaevagltd avakaeegit sgsikvate
//
LOCUS       WP_392037319             373 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            pilosus].
ACCESSION   WP_392037319
VERSION     WP_392037319.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pilosus
  ORGANISM  Streptomyces pilosus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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   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   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Streptomyces pilosus"
                     /db_xref="taxon:28893"
     Protein         1..373
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39751
     Region          16..347
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 mtttatpatg tpvfavdglw kvfgpkadrv pgdpalaald paelrsrtgc taavrdvgfd
       61 vrkgevfvvm glsgsgkstl vrcltrliep tagtiaidge dvramdgarl ralrrhraam
      121 vfqhfgllph rtvldnvayg leiqgmgrae rrekaaevva kvglegmeqr rpaqlsggqr
      181 qrvglarala vdpevllfde pfsaldplir rdmqeevvrl hreegrtmvf ithdlqealk
      241 lgdrialmrd grvvqlgtpe eivgspaddy vrafvrdvpr eqvltvrtam rpaatseeaa
      301 tgpgvrpdat vseaieavsr agtsvrvldd gkcvgvvdar alldvvagdv aaarpaqrre
      361 paapgaaatg epv
//
LOCUS       WP_392037494             171 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SRPBCC family protein [unclassified Streptomyces].
ACCESSION   WP_392037494
VERSION     WP_392037494.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 171)
  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 10008053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..171
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=18294
     Region          5..143
                     /region_name="YndB"
                     /note="Chalcone/flavanone-binding protein YndB,
                     AHSA1/START/SRPBCC domain [Lipid transport and
                     metabolism]; COG3832"
                     /db_xref="CDD:443044"
ORIGIN      
        1 mtipatpmdt vtlerriaag petvfglfvd rakwlswmgv dgtfdfepgg syrtrvtgqd
       61 vaagrfitvd pprrivfswg wetgavpapp ssepvppgts tveitlepap egtllhlihs
      121 glpsseacea haegwqhyvd rlairaeggd pgpdawtrge pgngpraprd r
//
LOCUS       WP_392037410             283 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces pilosus].
ACCESSION   WP_392037410
VERSION     WP_392037410.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pilosus
  ORGANISM  Streptomyces pilosus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 283)
  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 283)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Streptomyces pilosus"
                     /db_xref="taxon:28893"
     Protein         1..283
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31024
     Region          27..79
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          114..278
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mesggdsgag veggagadsn geflrcfgrq mkllreaagl tqaqlgervg ygealiaave
       61 qgrriprpel vdavdrevgg rgllvamkge vakarypsff refaaleada aelhaydahv
      121 vngllqceey aravfsmwrp lldaetieqr vsarldrhkl lvrrpkplls fvieetvlrr
      181 plggeeamra qlehlllvgh ernvelqvmp tgrdehagva gpftliltrq qrrmaytevq
      241 snsalhtapa kvqgfestyg vlraqamtpr eslawiekll gel
//
LOCUS       WP_392038377             414 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces coeruleorubidus].
ACCESSION   WP_392038377
VERSION     WP_392038377.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coeruleorubidus
  ORGANISM  Streptomyces coeruleorubidus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Streptomyces coeruleorubidus"
                     /db_xref="taxon:116188"
     Protein         1..414
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=43919
     Region          56..316
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mparpvvlvv apgdenyrgy cleqvadayd vvlltgteps wekphitdya vvdlsdpaal
       61 lsggralagr hnlagvmtwd ewsvvptarl arqlglstta pevmqgcrnk atarslfarh
      121 gvpsaasvsv rtrkeaeaaa erigypvvlk pashagaigv lrvddrdqlt aayqaaerta
      181 gqgtestsvl veeyldgsei svecvtyrga ttvvavnrkt isppphfeql ahsvaaddpl
      241 letvaptara ainalgitdg vshiemrlvd grprlievna rlagdmighl vrlatgidlp
      301 raaadiacdr apdltptrss aaairllypd tsgtlthlty dgprphwldr lhfqcrpgdq
      361 lllpadggnl ytgrigylit taatgqqara radrtaravt avldrtpgtr ssaa
//
LOCUS       WP_392038728             131 aa            linear   BCT 20-JAN-2025
DEFINITION  TOBE domain-containing protein [Streptomyces pilosus].
ACCESSION   WP_392038728
VERSION     WP_392038728.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pilosus
  ORGANISM  Streptomyces pilosus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 131)
  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 10007583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Streptomyces pilosus"
                     /db_xref="taxon:28893"
     Protein         1..131
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13909
     Region          1..128
                     /region_name="MopI"
                     /note="Molybdopterin-binding protein MopI [Coenzyme
                     transport and metabolism]; COG3585"
                     /db_xref="CDD:442804"
ORIGIN      
        1 mqsytigqaa kllgvspdtt rrwadagrlt thrddagrrl vdgrdlaafs velaragaae
       61 edtpytsarn afpgivtaik lgdvaaqvei qagphrlvsl ltreaveelg levgmeatar
      121 vkstnvhidr t
//
LOCUS       WP_392038980             356 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            sp. NPDC015492].
ACCESSION   WP_392038980
VERSION     WP_392038980.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015492
  ORGANISM  Streptomyces sp. NPDC015492
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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   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   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Streptomyces sp. NPDC015492"
                     /db_xref="taxon:3364958"
     Protein         1..356
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38465
     Region          11..345
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 mthppqdtta pvfsvrelwk vfgpkaervp adpelatlda aelrertgct aavrdvsfdv
       61 rkgevfvvmg lsgsgkstlv rcltrliept agtvaldged vlsmdggrlr elrrhraamv
      121 fqhfgllphr tvldnvaygl eiqgvgrger rsraaefvtk vglegmehrr pgqlsggqqq
      181 rvglaralav dpevllfdep fsaldplirr dmqeevvrlh reegrtmvfi thdlsealkl
      241 gdrialmrdg rivqlgtpee ivgapaddyv rdfvrdvpre qvltvrsamr pavadeseag
      301 palapsatvh eaieavartg gnarvvengr clgvvdhvgl lgvvagvpaa prkava
//
LOCUS       WP_392040036             243 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Streptomyces pilosus].
ACCESSION   WP_392040036
VERSION     WP_392040036.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pilosus
  ORGANISM  Streptomyces pilosus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 243)
  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 11440233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Streptomyces pilosus"
                     /db_xref="taxon:28893"
     Protein         1..243
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=26528
     Region          12..240
                     /region_name="GCD1"
                     /note="NDP-sugar pyrophosphorylase, includes eIF-2Bgamma,
                     eIF-2Bepsilon, and LPS biosynthesis protein s
                     [Translation, ribosomal structure and biogenesis, Cell
                     wall/membrane/envelope biogenesis]; COG1208"
                     /db_xref="CDD:440821"
ORIGIN      
        1 mtdpravsrp vqavilaggq gsrlrpytdd rpkpmveipg tgtpiighql twlaeegvtd
       61 vvvscghlae vlqkwldste lpvsvttvve teplgrgggl kyaaahlphp drpwyatngd
      121 iwtrfslrdm adfhterdav atlalarpri pwgavrtdgf ghitdfieap pstfeinagv
      181 yvfsaefagl lpergdhert tfprlarerr lagfpipqgs ywraidtakd lteaakelaa
      241 qgr
//
LOCUS       WP_392040200             223 aa            linear   BCT 20-JAN-2025
DEFINITION  4'-phosphopantetheinyl transferase family protein [Streptomyces sp.
            NPDC015492].
ACCESSION   WP_392040200
VERSION     WP_392040200.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015492
  ORGANISM  Streptomyces sp. NPDC015492
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459479
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Streptomyces sp. NPDC015492"
                     /db_xref="taxon:3364958"
     Protein         1..223
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=23569
     Region          26..221
                     /region_name="EntD"
                     /note="4'-phosphopantetheinyl transferase EntD
                     (siderophore biosynthesis) [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2977"
                     /db_xref="CDD:442216"
ORIGIN      
        1 migallppaa vsvdvfgdvl dadrypearl fadeekaiar avdkrrreft svrfcarral
       61 aglgwgpval vpgergapgw ppgvvgsmth cagyraatva seadvaslgi daepalplph
      121 gvfeavttad ergplaalal arpgipwdrl lfcakeavyk awfpltrsrl dfgeaavdfq
      181 pggrfrarll vpgptvdgrq lggftgrwlv rdgiaaaavt ver
//
LOCUS       WP_392040109             462 aa            linear   BCT 20-JAN-2025
DEFINITION  alpha,alpha-trehalose-phosphate synthase (UDP-forming)
            [Streptomyces coeruleorubidus].
ACCESSION   WP_392040109
VERSION     WP_392040109.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coeruleorubidus
  ORGANISM  Streptomyces coeruleorubidus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 462)
  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 462)
  AUTHORS   Eastmond,P.J. and Graham,I.A.
  TITLE     Trehalose metabolism: a regulatory role for trehalose-6-phosphate?
  JOURNAL   Curr Opin Plant Biol 6 (3), 231-235 (2003)
   PUBMED   12753972
REFERENCE   3  (residues 1 to 462)
  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   4  (residues 1 to 462)
  AUTHORS   Elbein,A.D., Pan,Y.T., Pastuszak,I. and Carroll,D.
  TITLE     New insights on trehalose: a multifunctional molecule
  JOURNAL   Glycobiology 13 (4), 17R-27R (2003)
   PUBMED   12626396
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 929-939 (1997)
   PUBMED   9334165
  REMARK    Erratum:[Biochem J 1998 Feb 1;329(Pt 3):719]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Streptomyces coeruleorubidus"
                     /db_xref="taxon:116188"
     Protein         1..462
                     /product="alpha,alpha-trehalose-phosphate synthase
                     (UDP-forming)"
                     /EC_number="2.4.1.15"
                     /GO_function="GO:0003825 - alpha,alpha-trehalose-phosphate
                     synthase (UDP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0005992 - trehalose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50359
     Region          8..462
                     /region_name="OtsA"
                     /note="Trehalose-6-phosphate synthase, GT20 family
                     [Carbohydrate transport and metabolism]; COG0380"
                     /db_xref="CDD:440149"
ORIGIN      
        1 mastygaaqv lvasnrgpvs ytvgeggsld akrgggglvs glsaigsdad alwvcsalsd
       61 gdreavrrgv gedgvrmldi padvhadayn giansvlwfv hhmlyqtple pvfdaefrrr
      121 wtsyetynra faealaeeaa rgaavvvqdy hltlvpgmlr elrpdlrigh fshtpwappe
      181 yfrmlpddva gqvlrgmlga drlgfltqrw adaftacaeq fagglggtri gvhglgadad
      241 flrkrshead veermaalre eigegrrtiv rvdrtelskn ivrgllayrr llethaewre
      301 rvvhvafayp srqdlavyrd ytaevrrlse einaeygtpg wtpvvlnlkd dfarslaayr
      361 ladvalvnpi rdgmnlvake vpvisdagca lvlsreagaf eelgedaivv npydvtgtaa
      421 alhealsmgp eeraerskrl saaatalppa qwfldqldal rg
//
LOCUS       WP_392040247             135 aa            linear   BCT 20-JAN-2025
DEFINITION  TOBE domain-containing protein [Streptomyces sp. NPDC015492].
ACCESSION   WP_392040247
VERSION     WP_392040247.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015492
  ORGANISM  Streptomyces sp. NPDC015492
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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 10007583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Streptomyces sp. NPDC015492"
                     /db_xref="taxon:3364958"
     Protein         1..135
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13184
     Region          <44..132
                     /region_name="MopI"
                     /note="Molybdopterin-binding protein MopI [Coenzyme
                     transport and metabolism]; COG3585"
                     /db_xref="CDD:442804"
ORIGIN      
        1 mdsrvivges gtraesttyp qvsepsraav tafadlpnqq aesglaagta vkalvkstev
       61 alatgpvegl sirnqlagsv tevatgaamg svkvsvegge ltaaitkdav edlglaagts
      121 vvalikstei alsaa
//
LOCUS       WP_392040603             524 aa            linear   BCT 20-JAN-2025
DEFINITION  complex I subunit 4 family protein [Streptomyces pilosus].
ACCESSION   WP_392040603
VERSION     WP_392040603.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pilosus
  ORGANISM  Streptomyces pilosus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 524)
  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 524)
  AUTHORS   Galemou Yoga,E., Angerer,H., Parey,K. and Zickermann,V.
  TITLE     Respiratory complex I - Mechanistic insights and advances in
            structure determination
  JOURNAL   Biochim Biophys Acta Bioenerg 1861 (3), 148153 (2020)
   PUBMED   31935361
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Friedrich,T. and Scheide,D.
  TITLE     The respiratory complex I of bacteria, archaea and eukarya and its
            module common with membrane-bound multisubunit hydrogenases
  JOURNAL   FEBS Lett 479 (1-2), 1-5 (2000)
   PUBMED   10940377
REFERENCE   4  (residues 1 to 524)
  AUTHORS   Walker,J.E.
  TITLE     The NADH:ubiquinone oxidoreductase (complex I) of respiratory
            chains
  JOURNAL   Q Rev Biophys 25 (3), 253-324 (1992)
   PUBMED   1470679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Streptomyces pilosus"
                     /db_xref="taxon:28893"
     Protein         1..524
                     /product="complex I subunit 4 family protein"
                     /GO_component="GO:0045271 - respiratory chain complex I
                     [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048039 - ubiquinone binding [Evidence
                     IEA]"
                     /GO_process="GO:0015990 - electron transport coupled
                     proton transport [Evidence IEA]"
                     /GO_process="GO:0042773 - ATP synthesis coupled electron
                     transport [Evidence IEA]"
                     /calculated_mol_wt=54213
     Region          65..521
                     /region_name="NuoM"
                     /note="NADH:ubiquinone oxidoreductase subunit 4 (chain M)
                     [Energy production and conversion]; COG1008"
                     /db_xref="CDD:440632"
ORIGIN      
        1 midisesvmq fllaflvvgp llgaaaallp appglkgksp eqavlrhgvt vtgavlaaai
       61 vlalgfdhsr patmqattdi swipaldvri hlgtdgislp llvltalltf lsalysyfkp
      121 pagpspkafv alllvlesgt latfavldlv lfflafetvl ipmyfliarw ggegraeaal
      181 kfilytllgs vvmllgllli gikagtfdmv alatdngrsl tasvqviavl aigiglavkt
      241 pmwplhswlp dahtaaptvg svllagvllk mgtygfvril lpaapdgfrt fapylaafav
      301 vgivygslac lalagrgang dlkrliayss vghmgfvllg iatmtptgvn galfaniahg
      361 litgllfflv galkdrtgst dldtlaketg aalygraprl ggllafaava slglpglagf
      421 wgemlalfga fdpaaglsrp afltfmaiga fgtlltaayl livvrrvcmg aapqdaprlt
      481 dvrayefaaw tplvvltvva glwpkallgl tdpavqqllt ggtr
//
LOCUS       WP_392041049             541 aa            linear   BCT 20-JAN-2025
DEFINITION  peptide ABC transporter substrate-binding protein [Streptomyces sp.
            NPDC015492].
ACCESSION   WP_392041049
VERSION     WP_392041049.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015492
  ORGANISM  Streptomyces sp. NPDC015492
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11467924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Streptomyces sp. NPDC015492"
                     /db_xref="taxon:3364958"
     Protein         1..541
                     /product="peptide 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=58445
     Region          37..533
                     /region_name="OppA"
                     /note="ABC-type oligopeptide transport system, periplasmic
                     component [Amino acid transport and metabolism]; COG4166"
                     /db_xref="CDD:443327"
ORIGIN      
        1 mrgathakwa alatavalaa tacgggdsgg gggadgivss swgdpqnple pantnevqgg
       61 kvlsmifrgl kqydpktgea kdmlaekiet tdstnftitv kdgwtfsnge kvtaksfvda
      121 wnyganlknn qknayffgqi egydqvhpek geptaetmsg lkvtgpqtft vkltqkfstw
      181 pitlgyaafs plpqtfytdh aawlskpvgn gpytvdsysk gsqmalkrwd aypgtdkaqn
      241 ggitlkvytd nntaytdlta gnldlvddvp asqlknvead lgdryinvpa giiqtlsfpf
      301 ydpawnkpgq eklrqglsma idrnqitdti fqktrtpavd wtspvlgedg gfkdvcgdfc
      361 kydaaeakkl vaegggipgg tmkisynadt gshkewvdav cnsinralgn nkacvgnpvg
      421 tfadfrnqvt qskmdgpfra gwqmdypliq nflqplyytn assndgkytd pqfdklvnea
      481 naeadtakai glfqqaeevl rddmgaiplw yqngsagyse rvsnvtlnpf svpvydqikv
      541 n
//
LOCUS       WP_392041562             139 aa            linear   BCT 20-JAN-2025
DEFINITION  TOBE domain-containing protein [Streptomyces coeruleorubidus].
ACCESSION   WP_392041562
VERSION     WP_392041562.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coeruleorubidus
  ORGANISM  Streptomyces coeruleorubidus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 139)
  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 10007583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Streptomyces coeruleorubidus"
                     /db_xref="taxon:116188"
     Protein         1..139
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13777
     Region          1..139
                     /region_name="MopI"
                     /note="Molybdopterin-binding protein MopI [Coenzyme
                     transport and metabolism]; COG3585"
                     /db_xref="CDD:442804"
ORIGIN      
        1 mslsirnqlp gtvtavtpge amatvrvrlt ggqaltaait reaaddlgla pgtavralvk
       61 stevslatap veglsirnrl pgtvtdiatg damasvrvtv eggeltaait rdaaddlals
      121 agtpvvalik stevslaae
//
LOCUS       WP_392041792             254 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Streptomyces
            coeruleorubidus].
ACCESSION   WP_392041792
VERSION     WP_392041792.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coeruleorubidus
  ORGANISM  Streptomyces coeruleorubidus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  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 254)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces coeruleorubidus"
                     /db_xref="taxon:116188"
     Protein         1..254
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26562
     Region          3..231
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 miriaavgdi hmgpdsqgll rpafetlper adllllagdl trhgtpeear vvagevrdlg
       61 vpvvavlgnh dhhddrpdev mailrdagah vlegqgtvvt sggarigvag tkgfgggfvg
      121 rcagefgepv mkefvrysrr cadslrtsle qlgeegcdar ialthfspvp dtlageplei
      181 ypflgsylla eaidtagadl avhghahagt ehgmtsggvr vrnvaqpvig rafhvyhlpv
      241 rehattgaaa qaar
//
LOCUS       WP_392041581             309 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Streptomyces pilosus].
ACCESSION   WP_392041581
VERSION     WP_392041581.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pilosus
  ORGANISM  Streptomyces pilosus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Streptomyces pilosus"
                     /db_xref="taxon:28893"
     Protein         1..309
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32998
     Region          7..303
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mrdvtgrlml ldtaslyfra yfgvpdsvra pdgspvnavr glldfidrlv kdhrpdhlva
       61 cmdadwrpqw rvdlipsyka hrvaeeraqg pdeeevpdtl spqvpvieav ldavgiarvg
      121 vagyeaddvi gtftaravgp vdivtgdrdl yqlvddargv rvlyplkgvg tlqitdeatl
      181 rekygvdgkg yadlallrgd psdglpgvpg vgektaakll drfgdlagil aavddrqagl
      241 tptqrgrlda arpylavapk vvrvaddvpl pdvdtalpra prdpaglesl aarwglggsl
      301 qrllttlsa
//
LOCUS       WP_392042548             415 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces pilosus].
ACCESSION   WP_392042548
VERSION     WP_392042548.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pilosus
  ORGANISM  Streptomyces pilosus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces pilosus"
                     /db_xref="taxon:28893"
     Protein         1..415
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43594
     Region          76..257
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          263..389
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mnvgpisgas vgarrrggrk laalalglal avtacgggga dagagqddgk gkgkdsaaaq
       61 skqseavvgi apedgaesvk tsgalkvtas kgkltevvvk npdgdpvega isgdgatwtp
      121 sthlaastky tvhavakdse grtaaedstf ttltpkntfv ghftpedgse vgvgmpfslr
      181 ftrgitnpdd vekavritte ppveveghwf gndrldfrpe aywkagtkvt vdlnldgveg
      241 regvygkqsk kvsftigrsq vsvvdakklt mkvqrdgkvi ktipvttgka gmetwngqmv
      301 iserlkvtrm ngetvgygge ydikdvpham rlttsgtflh gnywggdafg nynashgcig
      361 lrdvrggwdk kapgawffen smigdvvvvk nsddavvapd nglngwnmsw ekwka
//
LOCUS       WP_392042999            1275 aa            linear   BCT 20-JAN-2025
DEFINITION  Rne/Rng family ribonuclease [Streptomyces sp. NPDC015492].
ACCESSION   WP_392042999
VERSION     WP_392042999.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015492
  ORGANISM  Streptomyces sp. NPDC015492
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1275)
  AUTHORS   Kime,L., Jourdan,S.S. and McDowall,K.J.
  TITLE     Identifying and characterizing substrates of the RNase E/G family
            of enzymes
  JOURNAL   Methods Enzymol 447, 215-241 (2008)
   PUBMED   19161846
REFERENCE   2  (residues 1 to 1275)
  AUTHORS   Callaghan,A.J., Marcaida,M.J., Stead,J.A., McDowall,K.J.,
            Scott,W.G. and Luisi,B.F.
  TITLE     Structure of Escherichia coli RNase E catalytic domain and
            implications for RNA turnover
  JOURNAL   Nature 437 (7062), 1187-1191 (2005)
   PUBMED   16237448
REFERENCE   3  (residues 1 to 1275)
  AUTHORS   Li,Z., Pandit,S. and Deutscher,M.P.
  TITLE     RNase G (CafA protein) and RNase E are both required for the 5'
            maturation of 16S ribosomal RNA
  JOURNAL   EMBO J 18 (10), 2878-2885 (1999)
   PUBMED   10329633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1275
                     /organism="Streptomyces sp. NPDC015492"
                     /db_xref="taxon:3364958"
     Protein         1..1275
                     /product="Rne/Rng family ribonuclease"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=135527
     Region          569..967
                     /region_name="CafA"
                     /note="Ribonuclease G or E [Translation, ribosomal
                     structure and biogenesis]; COG1530"
                     /db_xref="CDD:441139"
     Region          <1040..1184
                     /region_name="rne"
                     /note="ribonuclease E; Reviewed; PRK10811"
                     /db_xref="CDD:236766"
ORIGIN      
        1 mlesnedtna pgdklpprrr rraasrpagp pvtgtaaeaa esapaaetta paavesapae
       61 aapaeaapap rtrrratrka tapaaeaaap aaetsepvae tpaaepaaae eaaeeaapar
      121 prrratrkat spvtapaaae apeetapvaq pepaaaeeaa eaaparprrr atrkatspvt
      181 spaaaeepta aaaeapavea apaaepapaa eetaapaprt rrratrqtas petapeaatg
      241 etlptaavaq itadeaevaa aetaatrgrg rrratspqft seaaparesr raarpsvavf
      301 qapvftepmf qtpetaaaaa aaapvepede etveetetve avteveetpe paerpegsrr
      361 rrrrrgepva vepvpatvad epeveaaade aeeadeaeen deyedrpsrr rrrggrrrrr
      421 geladsedge ephaedeten aedaedgeee heeseafagg ssssrrrrrr rrrsgdasad
      481 aegtdeegvr tvvkvreprp areksepgtg adevqsikgs trleakkqrr regreqgrrr
      541 vpiiteaefl arreavervm vvrqsgertq igvlednvlv ehyvnkeqat syvgnvylgk
      601 vqnvlpsmea afvdigkgrn avlyagevnf ealgmgngpr riesalksgq svlvqvtkdp
      661 ighkgarlts qvslpgrylv yvpegsmtgi srklpdtera rlktilkkiv pedagvivrt
      721 aaegasedel rrdverlqaq wediqkkaks gnaptllyge pdmtvrvvrd ifnedfskvi
      781 vsgddaweti hgyvhhvapd ltdrlskwts evdvfatyri deqlmkaldr kvwlpsggsl
      841 vidkteamiv vdvntgkftg qggnleetvt rnnleaaeei vrqlrlrdlg givvidfidm
      901 vlesnrdlvl rrlleclgrd rtkhqvaevt slglvqmtrk rvgqgllesf setcvhcngr
      961 gvivhmeqpt taggggggkr skkrgrggae hvhehehaev aetgaetaet eteaevaael
     1021 aapvalpepi aadeelygsv aeaeaaatrg rgrrratrrv sapatarpvv etesvefeak
     1081 pkaeptpepv aepvteaaep vveetaapap rarrratrrv tspvvsttep aaeptvvepv
     1141 veaapepepv vapvaevaep vaeeapvaap prarrrvvrk atapagspsg aedaavvvvt
     1201 aapaeapaes aeaaeaepap akktaarkta akkttakkaa tkktaatkkt aakktttkka
     1261 takkaaekta apaqd
//
LOCUS       WP_392043202             232 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Streptomyces coeruleorubidus].
ACCESSION   WP_392043202
VERSION     WP_392043202.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coeruleorubidus
  ORGANISM  Streptomyces coeruleorubidus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 232)
  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 10007985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Streptomyces coeruleorubidus"
                     /db_xref="taxon:116188"
     Protein         1..232
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24641
     Region          36..222
                     /region_name="COG3786"
                     /note="L,D-peptidoglycan transpeptidase YkuD,
                     ErfK/YbiS/YcfS/YnhG family [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443000"
ORIGIN      
        1 mrpgavalav sclvvlgagp papsaalpar mtdtgggtql itavapgtas ttgtvtwwdl
       61 tdgrwvkags aparfgangl vegasrkqgt nttptglygl pyafgikaap rgtayeyrrv
      121 hrdswwcqdn dsrsynrwte praadcraae sehlitygeq yahalvigfn yerpvrrrga
      181 giflhvdgrg atagcvsvpk ramrtilrwa dparrphiav gtasgttavt ry
//
LOCUS       WP_392043308             363 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            coeruleorubidus].
ACCESSION   WP_392043308
VERSION     WP_392043308.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coeruleorubidus
  ORGANISM  Streptomyces coeruleorubidus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   3  (residues 1 to 363)
  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   4  (residues 1 to 363)
  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 363)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Streptomyces coeruleorubidus"
                     /db_xref="taxon:116188"
     Protein         1..363
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39684
     Region          2..338
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 msarlqaesl ykvfgrrpdq avqrlrdgad rdelraegvt aavidasftv epgeifvvmg
       61 lsgsgkstll rmlngllept aghvrfdgqd lttlgdrelr evrskkismv fqhfalfphr
      121 svrenaaygl evqgvpraer vrradealal cglagweksw pdelsggmqq rvglaralat
      181 dadlllmdes fsaldplirr dmqdqllelq qklkktivfi thdlneamrl gdriavmrdg
      241 rivqngtaqd illrpaddyv asftqdvdrs rvltagelmd tsvtgddpgc hcetattgta
      301 ftelcaisar lshpvsvvde dnkligvvpr qrlvgflgde rdatpepcds prgkggekvt
      361 ara
//
LOCUS       WP_392044797             256 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces sp.
            NPDC015492].
ACCESSION   WP_392044797
VERSION     WP_392044797.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015492
  ORGANISM  Streptomyces sp. NPDC015492
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616714
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces sp. NPDC015492"
                     /db_xref="taxon:3364958"
     Protein         1..256
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27007
     Region          13..248
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 mdhnttvera rrlaklhaey eplvlptvwd vwsartavda gfpaltvgsh pladsrgaad
       61 hegqtfeevl aavrpiiaav dvpvsvdlea gygqepadli agltgvggvg lnledtvhsq
      121 ggrvrgtqeh aayvaglraa addagipvwv ngrtdlflha edpsgalpev ierlralqqa
      181 gadsvypvgi qdddgllaav vdavtvpvna tahpvkheve rfrrlgvrri tygpllqfam
      241 adamremlgp wgtdga
//
LOCUS       WP_392046316             361 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            coeruleorubidus].
ACCESSION   WP_392046316
VERSION     WP_392046316.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coeruleorubidus
  ORGANISM  Streptomyces coeruleorubidus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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   4  (residues 1 to 361)
  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 361)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Streptomyces coeruleorubidus"
                     /db_xref="taxon:116188"
     Protein         1..361
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39812
     Region          20..355
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 mttqtevsqr rgtpqdsgst pvisvrrlwk vfgpkadqvp dseelrglar relmdrtgct
       61 aavrdvhfdv spgevfvvmg lsgsgkstlv rcltrliept ageivfegen irdaddkrlr
      121 elrrskfsmv fqhfgllphr rvvdnvsfgl eirgmsraer tkralevvel vglegyensf
      181 pdqlsggmqq rvglaralag npdvlffdep fsaldplirr dmqnevirlh hevgktmvfi
      241 thdlsealkl gdrilimrdg kmvqcgtgde lvgapaddyv refvkdvprg dvltlrwimr
      301 plkdgdaldg pemgpdvvvr eatravlaad kpvkvvengk llgivgddei lavvagqegd
      361 m
//
LOCUS       WP_392048264             270 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces
            olivaceoviridis].
ACCESSION   WP_392048264
VERSION     WP_392048264.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces olivaceoviridis
  ORGANISM  Streptomyces olivaceoviridis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616714
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Streptomyces olivaceoviridis"
                     /db_xref="taxon:1921"
     Protein         1..270
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27330
     Region          16..238
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 mtaepapaps faglhhrpge plllpnawdh asaavlaarg fpaigttsla vaaavglpdg
       61 egatrehtvg lalilgsgpy llsvdaedgf sddpaevael arelwavgav gvnledglgp
      121 vrrhaakiaa vkaavpglfv nartdtywsg dgdeketlrr ldayqeagad gvfvpgvtdp
      181 griaalvrht avplnvlhsp tgptlghlag lgvrrvslgs llyrralgaa ldavtdiaag
      241 rapagttpsy advralersv sasesanstg
//
LOCUS       WP_392048716             307 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Streptomyces olivaceoviridis].
ACCESSION   WP_392048716
VERSION     WP_392048716.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces olivaceoviridis
  ORGANISM  Streptomyces olivaceoviridis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces olivaceoviridis"
                     /db_xref="taxon:1921"
     Protein         1..307
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32215
     Region          4..305
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mkellrprrl apgarvavva tsgpvpeerl qagldvlrgw dldpvvgphv ldrhpefgyl
       61 agadadraad lqnawcdptv davlcarggy gaqrmvdlld wdalraagpk vfvgfsdltv
      121 lheafatrlg latlhgpmaa gvdfiknara qehlratlfa petvrtiasd gtalvpgrar
      181 gvtlggclsl laaelgtpha rpsarggllc ledvgeetyr ldryltqllr sgwlegvrgv
      241 llgswegcsd yaglrpllad rlgglgvpva envgfghgeg altmplgvaa tldaeagtlt
      301 ldepalr
//
LOCUS       WP_392049703             941 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces erythrochromogenes].
ACCESSION   WP_392049703
VERSION     WP_392049703.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces erythrochromogenes
  ORGANISM  Streptomyces erythrochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 941)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 941)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..941
                     /organism="Streptomyces erythrochromogenes"
                     /db_xref="taxon:285574"
     Protein         1..941
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=99198
     Region          666..940
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mirdqeetdv ttkeqgvspp egaagddgar pddgpasrpq nrpedlapgl pagrtpgadd
       61 nggagdsavg ghedaeaphg hapteadrve vdepllaarv hrpsdlvrll vgilgiavll
      121 giaafahgtt vgleediskg tgqapdllik vaalvssiav lllpvafaie rlikrdglri
      181 adgvlaavla hgvtlatdlw vsqaapgtiq daltrpaggg altdpvhgyl apviaymtav
      241 gmtrrphwrv alwvvlllna ltmlvngytt pfsiiltvli gwsvaygtly avgspnvrpt
      301 gqnllaglrr vgfqpvsamr aegpegpeas etgdrgrryh vtledgppld vtvvdreqqa
      361 qgffyrvwrr ltlrgittrr slqslrqale qeallayaai aaganaqkli atselgpdav
      421 mlvyehlggr tldslpdeei tdeltrnawe qvralqsrri ahrrltgdal vvdrsgnvil
      481 tdlrggeiaa gdlvlrmdva qllatlglrv gaersvasav svlgpdivad clpllqpial
      541 srstratlrk lareraerer eavlessraa kaareagsaa apaptsaaae rkaekraldd
      601 aldeareedl lsqirrqvll irpqapvepa rlerirprtl vsfiagafga yflltqlahv
      661 plaetvadae wgwvgaalaf salsylaaam sllgfvperv sfartvvaqv agsfvklvap
      721 aavggvalnt rflqragirp glavasvgas qlfglashil lllsfgyltg tektpemtps
      781 raviaglltv avlvlvvtav pfmrkfvvtr vralfagvvp rmldvlqrpk klvtgiggml
      841 lltgcfvmcl dasirafggg eaisyasiav vflagnalgs aaptpggmga veatltlglv
      901 aaglekevai savllfrlmt fwlpvlpgwi sfnfltrkea i
//
LOCUS       WP_392049782             542 aa            linear   BCT 20-JAN-2025
DEFINITION  peptide ABC transporter substrate-binding protein [Streptomyces
            erythrochromogenes].
ACCESSION   WP_392049782
VERSION     WP_392049782.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces erythrochromogenes
  ORGANISM  Streptomyces erythrochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 542)
  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 542)
  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 542)
  AUTHORS   ter Beek,J., 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 542)
  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 542)
  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 11467924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Streptomyces erythrochromogenes"
                     /db_xref="taxon:285574"
     Protein         1..542
                     /product="peptide 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=58780
     Region          34..534
                     /region_name="OppA"
                     /note="ABC-type oligopeptide transport system, periplasmic
                     component [Amino acid transport and metabolism]; COG4166"
                     /db_xref="CDD:443327"
ORIGIN      
        1 mrgathakwa acavavalaa tacgggsdsg gggeagiiss swgdpqnple pantnevqgg
       61 kvldmlfrgl krydpktgea nnmlaesiqt tdsqnftvtl kdgwkfsnde pvtaqsfvda
      121 wnygadvrnk qnnspffsdi vgyddvhpas gepksktmsg lvvkdpktft valknkfstw
      181 petlgyqafs plpkafftdh aawldkpign gpytvdsytk gtgmklrtwd aypgtdkaqn
      241 ggvdlkvytd nntaytdlis gnldlvddvp aqqlknvknd lgdryinqpa liiqtltfpl
      301 ydpqwskpgt ekvrqgisra inrdeitkqi fretrtpakd wtspalgekg gfsatacgda
      361 cvydpaeakk liqeggglpg gkvtltsnvd tgshrdwmda vcnsvnnalg egpvctvnpv
      421 gtfadfrnqq ssykltgpfr sgwqadypli qnflqplyyt gassnygkfs nkefdalvdq
      481 anqesdpaka iasfqeseki laeqmpsipl wyqngsagys erledvtlnq fsvpvydqik
      541 vi
//
LOCUS       WP_392050740             453 aa            linear   BCT 20-JAN-2025
DEFINITION  alpha,alpha-trehalose-phosphate synthase (UDP-forming)
            [Streptomyces erythrochromogenes].
ACCESSION   WP_392050740
VERSION     WP_392050740.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces erythrochromogenes
  ORGANISM  Streptomyces erythrochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 453)
  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 453)
  AUTHORS   Eastmond,P.J. and Graham,I.A.
  TITLE     Trehalose metabolism: a regulatory role for trehalose-6-phosphate?
  JOURNAL   Curr Opin Plant Biol 6 (3), 231-235 (2003)
   PUBMED   12753972
REFERENCE   3  (residues 1 to 453)
  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   4  (residues 1 to 453)
  AUTHORS   Elbein,A.D., Pan,Y.T., Pastuszak,I. and Carroll,D.
  TITLE     New insights on trehalose: a multifunctional molecule
  JOURNAL   Glycobiology 13 (4), 17R-27R (2003)
   PUBMED   12626396
REFERENCE   5  (residues 1 to 453)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 929-939 (1997)
   PUBMED   9334165
  REMARK    Erratum:[Biochem J 1998 Feb 1;329(Pt 3):719]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Streptomyces erythrochromogenes"
                     /db_xref="taxon:285574"
     Protein         1..453
                     /product="alpha,alpha-trehalose-phosphate synthase
                     (UDP-forming)"
                     /EC_number="2.4.1.15"
                     /GO_function="GO:0003825 - alpha,alpha-trehalose-phosphate
                     synthase (UDP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0005992 - trehalose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49326
     Region          3..453
                     /region_name="OtsA"
                     /note="Trehalose-6-phosphate synthase, GT20 family
                     [Carbohydrate transport and metabolism]; COG0380"
                     /db_xref="CDD:440149"
ORIGIN      
        1 masqvlvaan rgplsyalsd drtlsarrgg gglvsglsaa laeqpgalwi caalsdadre
       61 avrrdvsepg vrmldidptm yddayngian svlwfthhhl ydvprepvfd aafrrrwasy
      121 vayneaftra laeeaaqgar vlvqdyhlal vpgqlrelrp dlriahftht pwasrefldm
      181 lpedvrsqlv wgmlgadvvg fhtrawadaf agaaqpddsr rvavfplgvd adelralahr
      241 pevdaklael raevagrrti arvdrtelsk nilrgllayr ellavhpewr gevvhlasay
      301 psrqdlkvyr dytaavsela aeinaefgtk dwqpvlvsvk ddfarslavy rmadvalvnp
      361 vrdgmnlvak eipvvseagc avvlstgaga yeelredalt vnpydvsata ealhaalsmp
      421 aaeraertkr laaaatalpp aawftaqlaa lea
//
LOCUS       WP_392051010             406 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces erythrochromogenes].
ACCESSION   WP_392051010
VERSION     WP_392051010.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces erythrochromogenes
  ORGANISM  Streptomyces erythrochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 406)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Streptomyces erythrochromogenes"
                     /db_xref="taxon:285574"
     Protein         1..406
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43530
     Region          56..243
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          249..375
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mtrragagla avvvwagllg glagctqdgk spveiqlpgr vrspaeairi tpddnakdvp
       61 adgrltvtvp egrlervkvt kvedaqqeev pgaiaadgls wsptpqagrl alaakytvda
      121 valdghnrrq arrttfttyv peerfigyfk penrstvgtg mivsfkfsra verradvera
      181 ikvtsdpave vvghwfgker ldfrpkqywk pgtkvtvqma lrdvegapgs ygiqsktitf
      241 tvgrsqistv daaahtmevr rdgellstvp isagapkttt yngkmvvmel fdvtrmngqt
      301 vgfggeydip dvphamrltn sgtflhgnyw sspdtfgstn vshgcvglrd dkgggsdtpa
      361 gwffdrtlig dvvevvnsqd ktvaadnglg gwnmswadwv agsava
//
LOCUS       WP_392051876             322 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC016562].
ACCESSION   WP_392051876
VERSION     WP_392051876.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016562
  ORGANISM  Streptomyces sp. NPDC016562
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415139
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces sp. NPDC016562"
                     /db_xref="taxon:3364966"
     Protein         1..322
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=32847
     Region          1..254
                     /region_name="LysX"
                     /note="Glutathione synthase, LysX or RimK-type ligase,
                     ATP-grasp superfamily [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism,
                     Translation, ribosomal structure and biogenesis, Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0189"
                     /db_xref="CDD:439959"
ORIGIN      
        1 mrlcflveeh yrhdgmpnev igqltawghr vdvvhpggsl lrmteavdtg ahdawvlktv
       61 sggpgltlle aaasagmttv ndarsirgvr dkalaaaigr grglplppty avarpellre
      121 ipaaryplvv kpadgssgra vhlvpaperl eallpvlage gmliaqpyvp nsgtdikvya
      181 vggelfater csplhpdpsv rerrvplsae vaaiatqvga vygldlygvd vllgpdgpvv
      241 vdvndfpsfr qvpdaaarva ravlglakag agagpaappv gaarplalpv sipaqasapv
      301 hasapaqasa paqvsagtge ca
//
LOCUS       WP_392051879             269 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC016562].
ACCESSION   WP_392051879
VERSION     WP_392051879.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016562
  ORGANISM  Streptomyces sp. NPDC016562
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415139
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces sp. NPDC016562"
                     /db_xref="taxon:3364966"
     Protein         1..269
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=28023
     Region          41..261
                     /region_name="LysX"
                     /note="Glutathione synthase, LysX or RimK-type ligase,
                     ATP-grasp superfamily [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism,
                     Translation, ribosomal structure and biogenesis, Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0189"
                     /db_xref="CDD:439959"
ORIGIN      
        1 mriglitpep ghpvlaatta llatehvvea vdpaapgdac lrpadvyllk artpqaldla
       61 relerrdvpv vnsaaatalc qdrtemaala lraglpfaat rtyaslavya sgasvpspvv
      121 vksrrshrgd lvaraddapa vrelalawpq epvvvqeyap nsgwdhklwa igdrvfsalr
      181 rselapegdg ptpppalgel psgwtalvre vgvvfaldvy gvdvidtggg tplivdvnaf
      241 pgirgqsgap ealaelalrr atggtrtgf
//
LOCUS       WP_392051909             353 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            erythrochromogenes].
ACCESSION   WP_392051909
VERSION     WP_392051909.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces erythrochromogenes
  ORGANISM  Streptomyces erythrochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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   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   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Streptomyces erythrochromogenes"
                     /db_xref="taxon:285574"
     Protein         1..353
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37832
     Region          1..339
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 mstlqaehvy kvfgdrpdda vraleggsdr aelradgata avidvsfdve pgqifvvmgl
       61 sgsgkstllr mlngllepta grilfggqdl talsarelrr vrstkismvf qhfalfphrn
      121 vlenagygle vqgvsraerd rratealalc glegwemawp delsggmqqr vglaralatd
      181 adlllmdesf saldplirrd mqdqllelqr slrktivfit hdlneamrlg daiavmrdgr
      241 vvqqgtaedi ltrpaddyva sfvqdvdrsr vltadavmtt tgparphagi cgcptvsadt
      301 pladlcavsa rvphpvavtg tdgavvgsvp qdrlvafigd eqrapvrcae vaa
//
LOCUS       WP_392053355             351 aa            linear   BCT 20-JAN-2025
DEFINITION  BMP family lipoprotein [Streptomyces olivaceoviridis].
ACCESSION   WP_392053355
VERSION     WP_392053355.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces olivaceoviridis
  ORGANISM  Streptomyces olivaceoviridis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Yousief,S.W., Bahey-El-Din,M. and Zaghloul,T.I.
  TITLE     Immunization with the basic membrane protein (BMP) family ABC
            transporter elicits protection against Enterococcus faecium in a
            murine infection model
  JOURNAL   Microbes Infect 22 (3), 127-136 (2020)
   PUBMED   31585177
REFERENCE   2  (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   3  (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   4  (residues 1 to 351)
  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   5  (residues 1 to 351)
  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 11448319
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Streptomyces olivaceoviridis"
                     /db_xref="taxon:1921"
     Protein         1..351
                     /product="BMP family lipoprotein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /calculated_mol_wt=35842
     Region          39..348
                     /region_name="Med"
                     /note="Lipoprotein Med, regulator of KinD/Spo0A, PBP1-ABC
                     superfamily, includes NupN [Signal transduction
                     mechanisms]; COG1744"
                     /db_xref="CDD:441350"
ORIGIN      
        1 mrrvaklsaa ciasaalalt atacgstssd ndsgspasgd gkgvkvgiaf dvggrgdrsf
       61 ndsaargadk akkefggdik eltaktsdte adreqrlsdl adagynpivg vgyayaasmt
      121 kvaakypktt fgivdsvvng knvdsitfte eqgsylagva aalktktkhv gfiggvdvpl
      181 ikkfeagyvq gvkdtdpkik idtqylshgs dtsgfaspdk gkeaaqgmld ngadviysaa
      241 gssgngaiea vagkkgawai gvdsdqysip glakyknsil tsvvknvdvg vydlvksvhd
      301 gkpltgtnty slakngvsls tsggfiddik akldaaqkki vdgsikvktt p
//
LOCUS       WP_392053624             319 aa            linear   BCT 20-JAN-2025
DEFINITION  aldo/keto reductase [Streptomyces erythrochromogenes].
ACCESSION   WP_392053624
VERSION     WP_392053624.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces erythrochromogenes
  ORGANISM  Streptomyces erythrochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 319)
  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 319)
  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   3  (residues 1 to 319)
  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   4  (residues 1 to 319)
  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 10790928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Streptomyces erythrochromogenes"
                     /db_xref="taxon:285574"
     Protein         1..319
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /calculated_mol_wt=35030
     Region          1..319
                     /region_name="YdhF"
                     /note="Predicted oxidoreductase YdhF [General function
                     prediction only]; COG4989"
                     /db_xref="CDD:444013"
ORIGIN      
        1 mtnegvgmsd drvlygcmgl ggswdpqpyg pgdidvaeaa veaaldsgit vfdhadiyrh
       61 gkseavfgev lartpglrgr itlqtkcgir lgdedrpgmy dlrgetitrr veesltrlrt
      121 dvidvlllhr pdpladvdsi aealtslhrq glvrhfgvsn mgaaqiahlq arldqplvan
      181 qlemslhtrd wveagvllnt paatangfpf gtlehcrdhg irlqawgala qgrftgrqqt
      241 paerataell aelarrkgtt petvllwwli rhpsriapvi gtarpdrira crdaalrepd
      301 ltheewyelw vtargvplp
//
LOCUS       WP_392053764             301 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptomyces
            erythrochromogenes].
ACCESSION   WP_392053764
VERSION     WP_392053764.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces erythrochromogenes
  ORGANISM  Streptomyces erythrochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 301)
  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 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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Streptomyces erythrochromogenes"
                     /db_xref="taxon:285574"
     Protein         1..301
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32315
     Region          21..176
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          205..285
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mdleelrtll arharpdatt avdgvlvskv drsdapepat tgtvlaviaq gakrlalgdr
       61 vleygagqyl vasvdlpvtg qflrvgpdrp algfglvlep sdiaelllla gpgdvpragp
      121 ggtavpalav cdapdellda vvrllrlldr prdravlapl ikreilwrvm tgeqggtvrq
      181 lgladsglsh varavawirs hyaqpfrved larlsgmsqs afyrnfqavt amsplrfqkq
      241 irlqearlll aarpgdvtgv ahrvgydsps qfsreyrrqf gtppsrdaar llldtpgarq
      301 g
//
LOCUS       WP_392054267             221 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces erythrochromogenes].
ACCESSION   WP_392054267
VERSION     WP_392054267.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces erythrochromogenes
  ORGANISM  Streptomyces erythrochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Streptomyces erythrochromogenes"
                     /db_xref="taxon:285574"
     Protein         1..221
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23711
     Region          2..210
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 mtskdrilar irraaaqqgp epgadadipr dylhvhgtrt pqervdllaa hlaeyrarvh
       61 rtgedglrel lgrllagaat vqlppnlgfg lprdpsltfv pdraeqtpre ldrvdavvtg
      121 calaiaetgt ivldggpdqg rrritlvpdh hiclvrvpeq vvdsvpqalp lldpsrpltw
      181 isgpsatsdi eldrvegvhg prrldvvlvg argavrgpgt q
//
LOCUS       WP_392054389             234 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Streptomyces olivaceoviridis].
ACCESSION   WP_392054389
VERSION     WP_392054389.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces olivaceoviridis
  ORGANISM  Streptomyces olivaceoviridis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 234)
  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 10007985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Streptomyces olivaceoviridis"
                     /db_xref="taxon:1921"
     Protein         1..234
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24391
     Region          41..224
                     /region_name="COG3786"
                     /note="L,D-peptidoglycan transpeptidase YkuD,
                     ErfK/YbiS/YcfS/YnhG family [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443000"
ORIGIN      
        1 mrpgvvlalv sasalallga apgrgpvplp agmadtgggh qlivaqapdt gattgtvsww
       61 dlrdgrwvra gsaparfgag glvdgatrrq gtnttptgly glpfgfgtka apagthvayr
      121 pvresswwcq dndsrsynrw vdplpadcra aqsehlidyg tqyayglvia fnydrpvrgr
      181 gagiflhvng hgatagcvsv pedamrrilt wtdpaakphi aigtekgata vgry
//
LOCUS       WP_392054513             392 aa            linear   BCT 20-JAN-2025
DEFINITION  caspase family protein [Streptomyces sp. NPDC016562].
ACCESSION   WP_392054513
VERSION     WP_392054513.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016562
  ORGANISM  Streptomyces sp. NPDC016562
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Van Opdenbosch,N. and Lamkanfi,M.
  TITLE     Caspases in Cell Death, Inflammation, and Disease
  JOURNAL   Immunity 50 (6), 1352-1364 (2019)
   PUBMED   31216460
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Tsiatsiani,L., Van Breusegem,F., Gallois,P., Zavialov,A., Lam,E.
            and Bozhkov,P.V.
  TITLE     Metacaspases
  JOURNAL   Cell Death Differ 18 (8), 1279-1288 (2011)
   PUBMED   21597462
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Zhang,J.H., Zhang,Y. and Herman,B.
  TITLE     Caspases, apoptosis and aging
  JOURNAL   Ageing Res Rev 2 (4), 357-366 (2003)
   PUBMED   14522240
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Salvesen,G.S.
  TITLE     Caspases and apoptosis
  JOURNAL   Essays Biochem 38, 9-19 (2002)
   PUBMED   12463158
REFERENCE   5  (residues 1 to 392)
  AUTHORS   Villa,P., Kaufmann,S.H. and Earnshaw,W.C.
  TITLE     Caspases and caspase inhibitors
  JOURNAL   Trends Biochem Sci 22 (10), 388-393 (1997)
   PUBMED   9357314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Streptomyces sp. NPDC016562"
                     /db_xref="taxon:3364966"
     Protein         1..392
                     /product="caspase family protein"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42504
     Region          12..255
                     /region_name="COG4249"
                     /note="Uncharacterized conserved protein, contains caspase
                     domain [General function prediction only]"
                     /db_xref="CDD:443391"
ORIGIN      
        1 maaftvhlde ntgpaathal vigvgryahl aggtaptthp gatglrqlss pprsarafat
       61 wlidqyhdpa rplgslalll seespasfvh phthaeqlaq patidnivaa vkewkdrgdh
      121 dearlvfyfc ghgvslgldt sllaadvfad edsplngaln fealrrglnr cragqqvffv
      181 dscrsgsdtl vsqvgtdtvg rvpvsgnirp egfvprehav lyatldgees faragrlslf
      241 tdallrsfdg sasentegqv wrvttgtlih avfrfmaerp fagslakaqv pvssesvdfg
      301 fhelrgdpvv pvyigckdpe dnaraefvcr hpqqeerrrp pppageepdl gewalflpfg
      361 ryeveavlgp edvrrqelda rppmfrvgla rl
//
LOCUS       WP_392054963             407 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces olivaceoviridis].
ACCESSION   WP_392054963
VERSION     WP_392054963.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces olivaceoviridis
  ORGANISM  Streptomyces olivaceoviridis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Streptomyces olivaceoviridis"
                     /db_xref="taxon:1921"
     Protein         1..407
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43752
     Region          60..245
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          252..376
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mrhvtgrarr vgaalaavlt wagllagcsm dgpgplgmgg tlgkppaped virvtpddgs
       61 kavrpgdrlq vrvpggrlek vtvvksqdaq etpvpgrigg dgltwrpded rlalaarytv
      121 davaldshgr rsarhttftt yvpdqrfiay vspenratvg tgmivslsfs qeitdraavq
      181 ravrvsarpp veirphwfgk grldfrpery wkpgtevtvd ldlrdvqgar giyglqdktf
      241 sftvgrsqts lvdvaqhtmd vrrdghllat vpitagapkh ptyngkmvvm dmlevtrmns
      301 qtvglgaeyd ipdvphamkl tdsgtflhgn ywapdapgqv nvshgcvglm dvkggssdtp
      361 agwffdrslv gdvievvnsk dktvapdngl ggwnmgwkaw kagsavk
//
LOCUS       WP_392055798             314 aa            linear   BCT 20-JAN-2025
DEFINITION  aldo/keto reductase [Streptomyces olivaceoviridis].
ACCESSION   WP_392055798
VERSION     WP_392055798.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces olivaceoviridis
  ORGANISM  Streptomyces olivaceoviridis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  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 314)
  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   3  (residues 1 to 314)
  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   4  (residues 1 to 314)
  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 10790928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces olivaceoviridis"
                     /db_xref="taxon:1921"
     Protein         1..314
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /calculated_mol_wt=34324
     Region          5..314
                     /region_name="YdhF"
                     /note="Predicted oxidoreductase YdhF [General function
                     prediction only]; COG4989"
                     /db_xref="CDD:444013"
ORIGIN      
        1 maaetdirah klvygcmglg ggwdtspctp edihraeaav eaalaagita fdhadiyryg
       61 kseavfgevl arspglrqri vvqtkcgirl pdgdrpghyd lrgasivrrv eeslvrlrtd
      121 fldvlllhrp dpladprevg avlnslhaqg lvrqfgvsnm ngpqiaslra hsdvplvvnq
      181 lemsldrrdw vesgvlfnta daardgfapg tlewcaangv rlqawsplag grlmsdkdtr
      241 vyrlvaelar rkgttpesil lwwlqrhpag iapvvgttrp erisacadav rrqpdlthee
      301 wyalwiaarg vplp
//
LOCUS       WP_392056032             264 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Streptomyces sp.
            NPDC016562].
ACCESSION   WP_392056032
VERSION     WP_392056032.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016562
  ORGANISM  Streptomyces sp. NPDC016562
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Streptomyces sp. NPDC016562"
                     /db_xref="taxon:3364966"
     Protein         1..264
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27343
     Region          3..239
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 mirvaavgdi hlgpgqsgll rpafdtlgec adllllagdl trhgtreear vvagevagla
       61 vpvvavlgnh dyqsdqapav teeltaagvh vlegegvllg ingtrvgiag tkgfcggfag
      121 rcgsefgepe mkafirytrs cadglgraln rlredgsdlr ialthfapvp dtlageplei
      181 ypflgsylla eamdeagadl avhghahsgt ehgmtaggir vrnvampvid rafavyhlsa
      241 sgtgvhaapp emswtvpppa awkr
//
LOCUS       WP_392057003             282 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC016562].
ACCESSION   WP_392057003
VERSION     WP_392057003.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016562
  ORGANISM  Streptomyces sp. NPDC016562
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 282)
  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 282)
  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 16111081
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces sp. NPDC016562"
                     /db_xref="taxon:3364966"
     Protein         1..282
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31454
     Region          20..71
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(22,26,51)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(25,50)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(32..33,44,47,51..52)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          90..264
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mvqvrdldps aspldyyaye lrrlreaagl klgqlgdiiy ctgsligmie htkrvptrdf
       61 servdaalgt dghfsrlvgl vlrsvlpswf qayaemeara nflstfqcql vhgllqtedy
      121 araliavdrp dqvdelvaar melqrllere hppalwvvls eavlhqevgg revmsgqlah
      181 llgfldqpwv qiqvlpfaag qhtgmlgsft llrftdepdl iyeegyargh mtanppvike
      241 rsvgyarlqa aalspehsat liarvmeery gerpeadera ma
//
LOCUS       WP_392057373            1337 aa            linear   BCT 20-JAN-2025
DEFINITION  Rne/Rng family ribonuclease [Streptomyces sp. NPDC016562].
ACCESSION   WP_392057373
VERSION     WP_392057373.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016562
  ORGANISM  Streptomyces sp. NPDC016562
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1337)
  AUTHORS   Kime,L., Jourdan,S.S. and McDowall,K.J.
  TITLE     Identifying and characterizing substrates of the RNase E/G family
            of enzymes
  JOURNAL   Methods Enzymol 447, 215-241 (2008)
   PUBMED   19161846
REFERENCE   2  (residues 1 to 1337)
  AUTHORS   Callaghan,A.J., Marcaida,M.J., Stead,J.A., McDowall,K.J.,
            Scott,W.G. and Luisi,B.F.
  TITLE     Structure of Escherichia coli RNase E catalytic domain and
            implications for RNA turnover
  JOURNAL   Nature 437 (7062), 1187-1191 (2005)
   PUBMED   16237448
REFERENCE   3  (residues 1 to 1337)
  AUTHORS   Li,Z., Pandit,S. and Deutscher,M.P.
  TITLE     RNase G (CafA protein) and RNase E are both required for the 5'
            maturation of 16S ribosomal RNA
  JOURNAL   EMBO J 18 (10), 2878-2885 (1999)
   PUBMED   10329633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1337
                     /organism="Streptomyces sp. NPDC016562"
                     /db_xref="taxon:3364966"
     Protein         1..1337
                     /product="Rne/Rng family ribonuclease"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=140982
     Region          588..988
                     /region_name="CafA"
                     /note="Ribonuclease G or E [Translation, ribosomal
                     structure and biogenesis]; COG1530"
                     /db_xref="CDD:441139"
ORIGIN      
        1 mpnnendtte ntspsdnlpp rrrrraasrp agppgataae ttpvteaapa aapaaeepaa
       61 paprarrrat ravtapeapa aevvveapaa apvaeepaap aprarrratr avtapeapaa
      121 vaepapvvee eapaapapra rrratravta peapaavaep tpvaeaapvv eeeapaapap
      181 rarrratrav tapeapaaev vveapataap vaeepaapap rarrratrav aapaapaaea
      241 paaavedeaa eaeavveeap kaaarsftva daldspkrgg rrratrsaap aapsqpaaqp
      301 aesaepaapa garraarpav avfqapvfae pmfqtpetaa maaaaaaaaa paeaeeeeel
      361 tevtaeteaa aapqpagrrr rrgrgapesa pvslpevlae eepeaeaael deesaefdeg
      421 desgerpsrr rrrggrrrrr geaadldesa eeeteaeqes aeheageeed eeaeealgss
      481 ssrrrrrrrr rtgdtaadsa eagdedgvrt vvkvreprpa rekaepgtga devqsikgst
      541 rleakkqrrr egreqgrrrv piiteaefla rreavervmv vrqsgertqi gvlednvlve
      601 hyvnkeeats yvgnvylgkv qnvlpsmeaa fidigkgrna vlyagevnfe algmangprr
      661 iesalksgqs vlvqvtkdpi ghkgarltsq vslpgrylvy vpegsmtgis rklpdterar
      721 lktilkkivp edagvivrta aegasedelr rdverlqaqw ediqkkakqi stsspsllyg
      781 epdmtvrvvr difnedfskv ivsgdsawet ihgyvnhvap dladrlsrwt sevdvfatyr
      841 ideqlakald rkvwlpsggs lvidkteami vidvntgkft gqggnleetv trnnleaaee
      901 ivrqlrlrdl ggivvidfid mvlesnrdlv lrrmleclgr drtkhqvaev tslglvqmtr
      961 krvgqglles fsetcvhcng rgvivhmeqp ttiggggngk rakrrggrge fdqhdhevet
     1021 ietvetaeve gfeteteaev aaeaaapral pepefvadee lysspaeaea aagvsgrrnr
     1081 rratrkatap agaprgahtp aqapapvaev iaepvtepad tvlepvaevv aeaveaaeti
     1141 eaapveeaap kgrtrrratr katapagapa paaeaapepv vvaepepvve aepvvepepv
     1201 vepepvveaa papvaeeapv aeaaparprr ratrkatapa gspagaaeaa vvvvetpvte
     1261 tatpveeaap akkaakkapa kkattakkap akkaaaakkt vakkaattkk tvakratkkt
     1321 saaeqqtpps vsaptea
//
LOCUS       WP_392058301             282 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            erythrochromogenes].
ACCESSION   WP_392058301
VERSION     WP_392058301.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces erythrochromogenes
  ORGANISM  Streptomyces erythrochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 282)
  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 282)
  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 16111081
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces erythrochromogenes"
                     /db_xref="taxon:285574"
     Protein         1..282
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31346
     Region          20..70
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(22,26,51)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(25,50)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(32..33,44,47,51..52)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          90..264
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mvlardidps aspldyysye lrrlreeagl kqsqlgaiif ctgsligmve ngrrvptrdf
       61 servdaaldt gghfsrlvgl vlrsvlptwf qayaemeara ayisayqpql vhgllqteay
      121 aravlasglp eqleelvaar merhrilrre kppvvwvvld egvlyrsigg rrvmreqlah
      181 llsfhenrwv qiqvlpndag ehagligafn gmrfasgpdv vytedlisgh ttanpdtvre
      241 aalryarlqa aalsvedsaa litrvmeery aeqpephgrl va
//
LOCUS       WP_392058868             286 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Streptomyces
            olivaceoviridis].
ACCESSION   WP_392058868
VERSION     WP_392058868.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces olivaceoviridis
  ORGANISM  Streptomyces olivaceoviridis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 286)
  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 286)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces olivaceoviridis"
                     /db_xref="taxon:1921"
     Protein         1..286
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=28856
     Region          23..285
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mplastgeli traaaarsav aafnvitleh ieaviagaes vgapvvlqvs enavkfrsgr
       61 llplaraava aaeraavpva lhldhvqsdd llrqapgagf ssvmydaarl pytgnlaatr
      121 aavdwahgqn lwieaelgqi ggkdgrppld ahapgartdp grardfvagt gvdalavaig
      181 sthamttrta vldlgllgrl saaltvplvl hgssgvpddg lvaavgrgia kvnvgtalna
      241 amtgairefl aarpeavdsr tylgagream asevrriigv lsgagg
//
LOCUS       WP_392058802             297 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptomyces
            erythrochromogenes].
ACCESSION   WP_392058802
VERSION     WP_392058802.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces erythrochromogenes
  ORGANISM  Streptomyces erythrochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 297)
  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 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   3  (residues 1 to 297)
  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   4  (residues 1 to 297)
  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 297)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Streptomyces erythrochromogenes"
                     /db_xref="taxon:285574"
     Protein         1..297
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32329
     Region          21..171
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          201..280
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msldelrdll grharpdlst aidgvricra epgaepeyam sgvmlaviaq gakrlalgdr
       61 vyeygvgqyl vasadlpvvg ritqgpelgf gmtlepavia elmlqagpgd lppstrsvrp
      121 gitvsdapge lidaivrllr lldrprdrrv lvplvkreil wllmtgeqge avrqlglads
      181 glthitravg wirdnyaeaf rvedlarsfg msvsafhrnf qavtamspiq fqkqirlqaa
      241 rlllarrpnd vtavassvgy dspsqfsrey krqfgappra daarmrtrph qaavatv
//
LOCUS       WP_392059958             218 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Streptomyces
            erythrochromogenes].
ACCESSION   WP_392059958
VERSION     WP_392059958.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces erythrochromogenes
  ORGANISM  Streptomyces erythrochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 218)
  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 10007985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Streptomyces erythrochromogenes"
                     /db_xref="taxon:285574"
     Protein         1..218
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=23382
     Region          18..208
                     /region_name="COG3786"
                     /note="L,D-peptidoglycan transpeptidase YkuD,
                     ErfK/YbiS/YcfS/YnhG family [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443000"
ORIGIN      
        1 mlpqgagssa gplparladt gggsqlitav apapgsttgr ltwwdrragr wyeagsapar
       61 fgangltega trtqgtnttp tglyelpyaf girrapagte yryrrvtads wwcqdnasaa
      121 ynrwveplpa dcapgeaehl vtydkqyaha lliafnydrp vrgrgagifl hvngkgatag
      181 cvsvperdmr allrwadpdr rphiaigtqe gplaitry
//
LOCUS       WP_392060322             420 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces olivaceoviridis].
ACCESSION   WP_392060322
VERSION     WP_392060322.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces olivaceoviridis
  ORGANISM  Streptomyces olivaceoviridis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Streptomyces olivaceoviridis"
                     /db_xref="taxon:1921"
     Protein         1..420
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=45482
     Region          66..311
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mkililhrvp yfkieyhrgi shdrhdvtyf gtdqalatlp shlrcervsr pglgsafeea
       61 rdwlarrprd fdrvisvsey elldaallre ylgvpgapad qvalardkvl mkqaveeagl
      121 rvprflalpr fldldgrvlw dgrtvlkphr gassedvlvf dtprqaaaav tggrtgipgi
      181 dagsgladfe veefvagpir hfdglvqggd vlvlsgseyv gtclqyaqgg plgsfqlals
      241 eeerawvsra laavriqdgs fhleaiahrg elvflevgnr vggadvvatv elatgvhlps
      301 yelrallger vtgtipeppa drrlygwfvc pghhlagref qgldgtaafr ddpavvawne
      361 lppgsplpdh ityqsgetvl agivagdtpe ggrrwiadlf aslsvrtrpa arttseqvpa
//
LOCUS       WP_392060921             353 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces olivaceoviridis].
ACCESSION   WP_392060921
VERSION     WP_392060921.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces olivaceoviridis
  ORGANISM  Streptomyces olivaceoviridis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Streptomyces olivaceoviridis"
                     /db_xref="taxon:1921"
     Protein         1..353
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=35290
     Region          79..347
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mpslspsgsl ppgaaarpec aapapsvtga cpgttatarp asrvstrpvr lalclaplll
       61 aagwavanrp vvyegvrrla aadpgwllag agftcltwva ascarqgalp drlppgllla
      121 sqfaagaanh alpaglgaha vtlrflrgqg vpleratasi glyslarsta ktlvllvfla
      181 vspawrrlgd lvpdgrllvp laavaggava vagvlltvvr plrrpatgll rsaladvrav
      241 hsrprrvlal wggavamplv qagtlacvga slglglpweq vvlaylaagt avgavpapgg
      301 lavdaalvwt lvtfgagpav atatvigyrv lsdwvpllpg alvlsalira kal
//
LOCUS       WP_392061036             427 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            erythrochromogenes].
ACCESSION   WP_392061036
VERSION     WP_392061036.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces erythrochromogenes
  ORGANISM  Streptomyces erythrochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Streptomyces erythrochromogenes"
                     /db_xref="taxon:285574"
     Protein         1..427
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=45268
     Region          20..270
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mranppagga arptapadpg vsfrllgtle iateagplpl rgmnqravla flllhanqvv
       61 atgdlmqvlw pngdapatar kvlqntvsal rgvlaggavp thvaslvsqa pgymlrmapg
      121 aldlerfrvl adqgrealaa gqpesaarll raalglwrgr aaqelaesgv ewpqlavvds
      181 artaafedyc daelrngrhh eviggleaga aaepsrersc hllmlalyra ghqaealray
      241 erlhqqlskd fgvqpgrevr dlhqaiinqd pallpsdgpd idfsspsdpe ldllfallal
      301 vqrqrrphvv tlaggpgggq gwllselast lrqdgqvtvw hvrtgpdgaa lgddlraalr
      361 ratpyrplvv vaenlhdvgg gvpecvgevi rtagrtpllv vltaraepes lwpgwnaavp
      421 wsttimv
//
LOCUS       WP_392062190             407 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces
            erythrochromogenes].
ACCESSION   WP_392062190
VERSION     WP_392062190.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces erythrochromogenes
  ORGANISM  Streptomyces erythrochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Streptomyces erythrochromogenes"
                     /db_xref="taxon:285574"
     Protein         1..407
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=42708
     Region          52..316
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mgirradpyi qqavrglaaq gieaglfhts gspgdddfpg hrhrldrevt prqladtvaa
       61 wgadaavsis lpcenalrda taaslldaag iptvmtplaa tmllvdkwet kqlcrraglh
      121 vpdgiradsg llagrglpvp ayrealraqa arlgyplmak pvwdstsagi rtlrtpaeld
      181 awlagppeas avleevvegd lctvdivgrp gsyqvlplcw tgragadpvf tfadvrwcgp
      241 rpeadaafah varalvrlcg elgvygsvnv dmvhtagrfv vlevnprigg attlscaasg
      301 tntfttlarm arglppgggp arrtgwavef ltddavppaa laelrdhvtv vtahelvidg
      361 asrgdivvlt lpegqeaptl raltdlhtrt gfpsagvlck ltsllvr
//
LOCUS       WP_392063220             291 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptomyces
            erythrochromogenes].
ACCESSION   WP_392063220
VERSION     WP_392063220.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces erythrochromogenes
  ORGANISM  Streptomyces erythrochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 291)
  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 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   3  (residues 1 to 291)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 291)
  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   5  (residues 1 to 291)
  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   6  (residues 1 to 291)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Streptomyces erythrochromogenes"
                     /db_xref="taxon:285574"
     Protein         1..291
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31354
     Region          19..102
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          126..287
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 misalnqlvd lveehlaeep dvqglagalg tteyhlrrmf sslagmplse yvrrrrmtva
       61 aadvvrgead llsiavrhgy gsneafgraf ravhgagpge vrrtggplrt qprlrfrltv
      121 egsipmdtrl vsrpafrlvg haarvplihq gvnphiqqhi aalppeehlr lkalgdtepg
      181 gllqvsdgvd pdgtegselt ylhgvaldrd tpapdgldai evpggmwavf rtsgphpqal
      241 qttwaatatd wfpsnpwrlr pgpsivatle haadfstatc elwlpvepep a
//
LOCUS       WP_392064511             417 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces olivaceoviridis].
ACCESSION   WP_392064511
VERSION     WP_392064511.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces olivaceoviridis
  ORGANISM  Streptomyces olivaceoviridis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 417)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Streptomyces olivaceoviridis"
                     /db_xref="taxon:1921"
     Protein         1..417
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43772
     Region          75..247
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          253..385
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mekrlitlft rrtglvattg vlggvlaita lggtsnaatg gndagnpptp qarasqpatq
       61 easdarieis pgqgaynvgi ndpvgvtvsk gkltkvtmta vatgaetpgt lsadgtswkp
      121 ngrleratky qitaeaedak grsvtgnati ttvspandfi ghvspedgst vgvgmpvtvt
      181 fdkaigdkat veseiqvsss sgqqvvghwl ndhrldfrpe kywtsgstvt vtlsrdgiqk
      241 tvtfkigrsq istvdaktkq mtvvrdgkti ktipissgsa ehptyngqmv isekfghvhm
      301 ngasvgltek dgkpsydika vphamrltds gtfihgnywa adsifgkvnt shgcvglkdv
      361 rggddgrqpa awffdqsmig divvvknsed ktnlapdngl sdwnmpwqqw vaggptt
//
LOCUS       WP_392064919             422 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces
            olivaceoviridis].
ACCESSION   WP_392064919
VERSION     WP_392064919.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces olivaceoviridis
  ORGANISM  Streptomyces olivaceoviridis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  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 422)
  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
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 422)
  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   5  (residues 1 to 422)
  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   6  (residues 1 to 422)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 422)
  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 20324439
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces olivaceoviridis"
                     /db_xref="taxon:1921"
     Protein         1..422
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43617
     Region          <27..>78
                     /region_name="COG3355"
                     /note="Predicted transcriptional regulator
                     [Transcription]"
                     /db_xref="CDD:442583"
     Region          90..386
                     /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 mteisardrk stkgvnpkga alatrvlelv asgqassrae laqllgtaps tisltvaelv
       61 ergliaeegt qsstggrprr vlragstdey avaadvggrh arigvvlpgs gvrdvanvpf
      121 eiadgpeaal srlaehvesl aeqrgrdrlr gvglslpgpv dvaagavvlp srmpgwnrfp
      181 vaawleerfg vpavvdndan cmavgeqsvr paehrrtitv kigsaigagv iidghlyrga
      241 tgaagdithi rieggadipc scgntgclet vasgaalvri lrergvevas tedvvqlatd
      301 adpeatgavr ragdhlgrvl aanvnffnpd avylggilst lepfvaavrs qlyeschpla
      361 tehltierai lgadaglvgv glfalqrala ralgdaggvg tdrfhavvpp qkwltprtpr
      421 sg
//
LOCUS       WP_392066228             399 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            sp. NPDC015171].
ACCESSION   WP_392066228
VERSION     WP_392066228.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015171
  ORGANISM  Streptomyces sp. NPDC015171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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   4  (residues 1 to 399)
  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 399)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Streptomyces sp. NPDC015171"
                     /db_xref="taxon:3364945"
     Protein         1..399
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=42855
     Region          14..349
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 mtltvptrkp ptdspvfsvd glwkvfgpkp eripgdpels tldpaglrar tgctaavrdv
       61 sfdvrkgevf vvmglsgsgk stlvrcltrl ieptagtisi dgedvramdk arlrelrrhr
      121 aamvfqhfgl lphrtvldnv aygleiqgvg kaerreraae fvtkvglegm ekrrpgqlsg
      181 gqrqrvglar alavdpevll fdepfsaldp lirrdmqdev trlheeegrt mvfithdlse
      241 alklgdrial mrdgrvvqlg tpeeivgspa ddyvrefvrd vpreqvmtvr tamrpasaee
      301 taagpavrpq atvaeaieav aragaparvm degrclgvvg heqlldvvag vngaaapnad
      361 avpaqaarta kdapapkpaa lrkrgqavpp aprtspeav
//
LOCUS       WP_392065812             540 aa            linear   BCT 20-JAN-2025
DEFINITION  peptide ABC transporter substrate-binding protein [Streptomyces sp.
            NPDC015171].
ACCESSION   WP_392065812
VERSION     WP_392065812.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015171
  ORGANISM  Streptomyces sp. NPDC015171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 540)
  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 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   3  (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
REFERENCE   4  (residues 1 to 540)
  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 540)
  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 11467924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Streptomyces sp. NPDC015171"
                     /db_xref="taxon:3364945"
     Protein         1..540
                     /product="peptide 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=58690
     Region          10..535
                     /region_name="OppA"
                     /note="ABC-type oligopeptide transport system, periplasmic
                     component [Amino acid transport and metabolism]; COG4166"
                     /db_xref="CDD:443327"
ORIGIN      
        1 mrgiahtrwa acvvatalaa vgcggpgsgg nggavlsasw sdpqnplepa ntnevqggkv
       61 ldmifrglkk ydprtgkaqd wlarsietkd sqhftvrlrg gwtfsdgekv tarsfvdawn
      121 ygaslrnnqk nayffgyidg ydkvhpaggr qsadrlsglk vvddrtftvt lnqkfsgfpd
      181 tlgyaafvpl prvfftdhaa wldkpvgngp ytiesytkga qmylrkrddy pgpdkarndg
      241 vtllvytdtn taytdllagn ldltddipaa qlknvkgdlg gryinspagi iqtlafpyyd
      301 kawnrpgsvk vrtglsmavn relitgtlfr ktrtpatdwt spvlgaaggf kaglcgpach
      361 ydpararrli eegggipggq vkitynadag shrewvdavc nsinnalgdd kacvgnpvgt
      421 fadfrnrlgq hrmtgpfrag wqmdypliqn flqplyytga ssndgrwsnk efdrlvdran
      481 aetdtakava gfqqaekvvr dnmaaiplwy qngnagyser lsdvalnpfs vpvyneikvg
//
LOCUS       WP_392066241             422 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015171].
ACCESSION   WP_392066241
VERSION     WP_392066241.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015171
  ORGANISM  Streptomyces sp. NPDC015171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 422)
  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 422)
  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 422)
  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 10611723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces sp. NPDC015171"
                     /db_xref="taxon:3364945"
     Protein         1..422
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=41896
     Region          17..73
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Region          <114..264
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          321..404
                     /region_name="DUF2690"
                     /note="Protein of unknown function (DUF2690); pfam10901"
                     /db_xref="CDD:402475"
ORIGIN      
        1 mprwkalped lepqiteftg rlrglvdssg lsiavladrt gysklswery ldgrllapkg
       61 avialaeatg thpghlttlw elaerawsra emrhdttmda lrvsearaal gegraggpda
      121 rkgaggtavp giagpagvsp tipaqpsdpe sgardgaapg padggdasag rnswglagyr
      181 gpsqasarpg gtrrpdgppa pagppgtpsa psgtpsgtps vpsgtapsgp agpaapagap
      241 gtpgpqpevp apgarwsarr qqvtmflagl igvlvliggv lffthrggvg hqgegaaksp
      301 spsasartsp ppgvkcagsa cvgkdaetmg csgdlvttak tatvgtttle vrysracgta
      361 wgritngapg dtvevsagke rqtgditaag dtigytpmvv vrkpaearac atlasgltgc
      421 tk
//
LOCUS       WP_392066697             131 aa            linear   BCT 20-JAN-2025
DEFINITION  TOBE domain-containing protein [Streptomyces erythrochromogenes].
ACCESSION   WP_392066697
VERSION     WP_392066697.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces erythrochromogenes
  ORGANISM  Streptomyces erythrochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 131)
  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 10007583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Streptomyces erythrochromogenes"
                     /db_xref="taxon:285574"
     Protein         1..131
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13976
     Region          1..128
                     /region_name="MopI"
                     /note="Molybdopterin-binding protein MopI [Coenzyme
                     transport and metabolism]; COG3585"
                     /db_xref="CDD:442804"
ORIGIN      
        1 mqsytigqaa rllgvspdta rrwadagrvv thrdefgrrl ingrdlaafs vevgqgahte
       61 dgepytsarn afpgivtavr lgdvsaqvdi qagphrlvsl ltreaveelg levgmratar
      121 vkstsvhidr a
//
LOCUS       WP_392067556             307 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Streptomyces sp. NPDC015171].
ACCESSION   WP_392067556
VERSION     WP_392067556.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015171
  ORGANISM  Streptomyces sp. NPDC015171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces sp. NPDC015171"
                     /db_xref="taxon:3364945"
     Protein         1..307
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32227
     Region          4..305
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mkelvrphrl apgarvavva tsgpvpeerl qagldvlrgw dldpvagdhv ldrhaefgyl
       61 agsdadraad fqrawcdpgv davlcarggy gvqrmidlld wdalraagpk lfvgfsdltv
      121 lheaiaarlg latlygpmaa gidfiknara qehlratlfa petvrtiass gtplvpgrar
      181 gvtlggclcl laaergtphs rasarggllc ledvgeeayr ldryltqllr sgwlegvrgv
      241 llgswegcgd paglrtmlad rlgglgvpva advgfghceg altipfgvpa eldadagtlt
      301 lekpalr
//
LOCUS       WP_392067609             267 aa            linear   BCT 20-JAN-2025
DEFINITION  S1 family peptidase [Streptomyces sp. NPDC015171].
ACCESSION   WP_392067609
VERSION     WP_392067609.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015171
  ORGANISM  Streptomyces sp. NPDC015171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Querino Lima Afonso,M., da Fonseca,N.J. Jr., de Oliveira,L.C.,
            Lobo,F.P. and Bleicher,L.
  TITLE     Coevolved Positions Represent Key Functional Properties in the
            Trypsin-Like Serine Proteases Protein Family
  JOURNAL   J Chem Inf Model 60 (2), 1060-1068 (2020)
   PUBMED   31895561
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Waldner,B.J., Kraml,J., Kahler,U., Spinn,A., Schauperl,M.,
            Podewitz,M., Fuchs,J.E., Cruciani,G. and Liedl,K.R.
  TITLE     Electrostatic recognition in substrate binding to serine proteases
  JOURNAL   J Mol Recognit 31 (10), e2727 (2018)
   PUBMED   29785722
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Pelc,L.A., Chen,Z., Gohara,D.W., Vogt,A.D., Pozzi,N. and Di Cera,E.
  TITLE     Why Ser and not Thr brokers catalysis in the trypsin fold
  JOURNAL   Biochemistry 54 (7), 1457-1464 (2015)
   PUBMED   25664608
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Perona,J.J. and Craik,C.S.
  TITLE     Evolutionary divergence of substrate specificity within the
            chymotrypsin-like serine protease fold
  JOURNAL   J Biol Chem 272 (48), 29987-29990 (1997)
   PUBMED   9374470
REFERENCE   5  (residues 1 to 267)
  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 10595581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Streptomyces sp. NPDC015171"
                     /db_xref="taxon:3364945"
     Protein         1..267
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=28664
     Region          18..147
                     /region_name="Trypsin_2"
                     /note="Trypsin-like peptidase domain; pfam13365"
                     /db_xref="CDD:433149"
ORIGIN      
        1 mtgpgywvdl yqarqrlggg flltrrfvlt alhclrgvap eecvdirlad grsvggricr
       61 qdqeadlalv eiaadhhvdl pipaadvard gdrwqgpyrp aadevhlsgr idrtaphlca
      121 ggatiealql tadqqlgdys gysggpvegv ppgderqpav vgilieqtpd rsdgsraanv
      181 liaatlgeam rrfdhldvah lvdvlrprgs raaaarpqpp rfsgteallr qlddwaerri
      241 ldpaqladlk fltvqklidk elgggga
//
LOCUS       WP_392067663             456 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces sp. NPDC015171].
ACCESSION   WP_392067663
VERSION     WP_392067663.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015171
  ORGANISM  Streptomyces sp. NPDC015171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Streptomyces sp. NPDC015171"
                     /db_xref="taxon:3364945"
     Protein         1..456
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=45755
     Region          93..358
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 msaraaagtr padpvrarvt pgagpartcv asahparprt apappapapa aqtparrrlg
       61 sralrthagt aagvvilaal lwrlgtgall dglrridtvs vlaalgiglv ttvfsawrwq
      121 lvarglrlrl plvpavadyy ralflnaalp ggilgdvhra vrhgqsagdl rrgvkavvle
      181 rvagqlaltv agaallltlp spvraevrgf aplaalaavg alavvlavrm nraparrgga
      241 lrqtlgearg glasrqsgpg vwlssaivla ghlamfvvaa riagsaapva vllpiavlal
      301 vamglplnig gfgpregvta wafgaaglga dtgiavavvy gvlsfaaslp gavvlvrrwy
      361 aglrggatap tasapaapvp acapapaagr rpsgdrlpag aapmgpgrrt apgyarpaae
      421 vtsakydskd sarlsssafp fsaepregrp mtpdsv
//
LOCUS       WP_392068391             245 aa            linear   BCT 20-JAN-2025
DEFINITION  4'-phosphopantetheinyl transferase family protein [Streptomyces
            bacillaris].
ACCESSION   WP_392068391
VERSION     WP_392068391.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459479
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..245
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=26322
     Region          25..232
                     /region_name="EntD"
                     /note="4'-phosphopantetheinyl transferase EntD
                     (siderophore biosynthesis) [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2977"
                     /db_xref="CDD:442216"
ORIGIN      
        1 mierllpayv scaatrevsv adgnlfpeee eliaravpkr rndfatarac arramgrlgl
       61 epvavlhgkr gmplwpegiv gslthcegyr aaalaragdv lslgidaeph aplpdgvael
      121 vvlpsererf aaaggeagdi hwdrllfsak esvfktwypl tlteldfeea dltfhreape
      181 gregkqagvg ssgravegtf sarllrtdpa vppvlegrwr iedgivatal llradqreag
      241 apqsp
//
LOCUS       WP_392068446             247 aa            linear   BCT 20-JAN-2025
DEFINITION  SRPBCC family protein [Streptomyces sp. NPDC015171].
ACCESSION   WP_392068446
VERSION     WP_392068446.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015171
  ORGANISM  Streptomyces sp. NPDC015171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 247)
  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 10008053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Streptomyces sp. NPDC015171"
                     /db_xref="taxon:3364945"
     Protein         1..247
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=27017
     Region          1..113
                     /region_name="YndB"
                     /note="Chalcone/flavanone-binding protein YndB,
                     AHSA1/START/SRPBCC domain [Lipid transport and
                     metabolism]; COG3832"
                     /db_xref="CDD:443044"
ORIGIN      
        1 mprefkvnrt qvlprpperv whavatgegn lgwlypmeie prvggtvsrg sstvltwqpp
       61 hrfacrtpdl dgfsntlsyt vqaledgtsr lsmsihwvht gtpddswdvr aaaaekhvdf
      121 yqhslaqyle hfdgrpaayi kaarpapars pdafaavrer lgvpasaaag dpvevtlpda
      181 pggpveavvd htdgdflglr tahalyrfyn gsawnwpiwa ghhlfspgph tdeaeqawta
      241 wlaltap
//
LOCUS       WP_392068789             132 aa            linear   BCT 20-JAN-2025
DEFINITION  TOBE domain-containing protein [Streptomyces sp. NPDC015171].
ACCESSION   WP_392068789
VERSION     WP_392068789.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015171
  ORGANISM  Streptomyces sp. NPDC015171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 132)
  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 10007583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Streptomyces sp. NPDC015171"
                     /db_xref="taxon:3364945"
     Protein         1..132
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13908
     Region          1..132
                     /region_name="MopI"
                     /note="Molybdopterin-binding protein MopI [Coenzyme
                     transport and metabolism]; COG3585"
                     /db_xref="CDD:442804"
ORIGIN      
        1 mptysigqaa rllrvspetv rrwsdagrlp mgrdgtgnrv idgvglarfa rekaaeders
       61 gapgpptsvr naltgivtam tmddvvarve iqagphrvvs lvtreavdel glavgvtvva
      121 rvkstslhve rp
//
LOCUS       WP_392068705             668 aa            linear   BCT 20-JAN-2025
DEFINITION  caspase family protein [Streptomyces sp. NPDC015171].
ACCESSION   WP_392068705
VERSION     WP_392068705.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015171
  ORGANISM  Streptomyces sp. NPDC015171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Van Opdenbosch,N. and Lamkanfi,M.
  TITLE     Caspases in Cell Death, Inflammation, and Disease
  JOURNAL   Immunity 50 (6), 1352-1364 (2019)
   PUBMED   31216460
REFERENCE   2  (residues 1 to 668)
  AUTHORS   Tsiatsiani,L., Van Breusegem,F., Gallois,P., Zavialov,A., Lam,E.
            and Bozhkov,P.V.
  TITLE     Metacaspases
  JOURNAL   Cell Death Differ 18 (8), 1279-1288 (2011)
   PUBMED   21597462
REFERENCE   3  (residues 1 to 668)
  AUTHORS   Zhang,J.H., Zhang,Y. and Herman,B.
  TITLE     Caspases, apoptosis and aging
  JOURNAL   Ageing Res Rev 2 (4), 357-366 (2003)
   PUBMED   14522240
REFERENCE   4  (residues 1 to 668)
  AUTHORS   Salvesen,G.S.
  TITLE     Caspases and apoptosis
  JOURNAL   Essays Biochem 38, 9-19 (2002)
   PUBMED   12463158
REFERENCE   5  (residues 1 to 668)
  AUTHORS   Villa,P., Kaufmann,S.H. and Earnshaw,W.C.
  TITLE     Caspases and caspase inhibitors
  JOURNAL   Trends Biochem Sci 22 (10), 388-393 (1997)
   PUBMED   9357314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Streptomyces sp. NPDC015171"
                     /db_xref="taxon:3364945"
     Protein         1..668
                     /product="caspase family protein"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=70876
     Region          1..259
                     /region_name="COG4249"
                     /note="Uncharacterized conserved protein, contains caspase
                     domain [General function prediction only]"
                     /db_xref="CDD:443391"
ORIGIN      
        1 mgtvyalfag iddypielrr lrgavndvea aarlladlgd gafeplllrn deatteavvt
       61 avrdhlgaag pgdtalfwfs ghgtdyeavl plhrrteatg ryqalvcads treggrplvd
      121 kelgalldsv aargahvaav ldccfsggat rrpappdhta ryappaawwg eprgeqraag
      181 atgapagrhv llaagrlnql syerdfdgvp ygvfthalle alraagpgat yrdllaaahc
      241 rvqteradqh pvlfppepgg iadqpflgga vtrtrgphll rngpygwevd cgrvhglrdd
      301 gpgaaeftvt apgaaprvvr aravhadrte vapagwepdr rqvypvalsa lalpptrvrv
      361 etpdassaar raaglvreal gsagpdgapt pllrlvddpg papghllrvv vsptpgtglg
      421 aavlrrdgsa avpplrlggp edarqvadcl hhlarwhqll tldnpasplt dlvrveilpw
      481 tydgpwssdg pspilpdgsg eivcrygasp sgrprepwls irlhnrsptr tlwcvllnlt
      541 dsyaahtgly pghfigpgrt gfalddrpva ltvparrarp gaevrdwlkl ivaegevntv
      601 pfhlppwdph gsddrgtrra apdgllrlap pghgdrdmge traqgpgqwt trtiplrtvi
      661 paqdpahg
//
LOCUS       WP_392068875             415 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            bacillaris].
ACCESSION   WP_392068875
VERSION     WP_392068875.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  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 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   3  (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   4  (residues 1 to 415)
  AUTHORS   Igarashi,K., Ito,K. and Kashiwagi,K.
  TITLE     Polyamine uptake systems in Escherichia coli
  JOURNAL   Res Microbiol 152 (3-4), 271-278 (2001)
   PUBMED   11421274
REFERENCE   5  (residues 1 to 415)
  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   6  (residues 1 to 415)
  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 11430824
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..415
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0019808 - polyamine binding [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:0015846 - polyamine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45175
     Region          28..413
                     /region_name="PotD"
                     /note="Spermidine/putrescine-binding periplasmic protein
                     [Amino acid transport and metabolism]; COG0687"
                     /db_xref="CDD:440451"
ORIGIN      
        1 mesyepeclt pvqlaamrrs ltngrgaltr rsllrasgmg alalggiatl gacgippagr
       61 aegaaaaddh serekvvnfs nwteymdvsd deksrptlaa ftertgikvk ytedindnve
      121 ffgkikpqla agqdtgrdli cvtdwlaari irlgwaqkld asnlphafan vsaqfrspdw
      181 dpgraysypw tgiptviayn akatggrkvd svtqllddpk lkgrvsflse mrdtvgmtll
      241 dqgkdpgkft dadfdgaigr lqkavdkkqi rrftgndyta dlskgdiaac vawagdiiql
      301 qadnpdikft ipaagyiiss dsllvpaqar hktnaeklid yyyeppvaaq laayinyvcp
      361 vdgvreelar idesmasntl ilpdremask srafrslste eetayeekfa kliga
//
LOCUS       WP_392069303             404 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces bacillaris].
ACCESSION   WP_392069303
VERSION     WP_392069303.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 404)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..404
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=42423
     Region          64..247
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          252..372
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mshprlaaal laaallapla acspgttgst dtagttgata aaqatpgted rpvtvavtpt
       61 gkqvpagepv rvtatggtlt svtvtdadgr tlsgkitadg rtwtsdrkav pgaaytvkta
      121 trsaggtags staafttapa gkvnkvdwrp ggattvgiaq pislvfdhpv knraevekql
      181 kvttsndteg swgwlrdwsg rdrvdwrprt ywkpgtqvtl daelngtdsg adggwfvrdy
      241 rtaftvgagq ivkvdldrhr lslvrdgktl rhipvsggtp ggdkrswrgt avlmakegti
      301 nmnsetvglg naydkmvdhs mrltwsgmya haapwnarff grsnqssgci gmsdadaawf
      361 yaqvrpgdpf eitgkdtkgv vapgngfgaw nlswtewqek salr
//
LOCUS       WP_392069342             456 aa            linear   BCT 20-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Streptomyces bacillaris].
ACCESSION   WP_392069342
VERSION     WP_392069342.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            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 10481000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..456
                     /product="FAD-binding oxidoreductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47979
     Region          19..153
                     /region_name="FAD_binding_4"
                     /note="FAD binding domain; pfam01565"
                     /db_xref="CDD:426326"
     Region          <404..454
                     /region_name="ALO"
                     /note="D-arabinono-1,4-lactone oxidase; cl21623"
                     /db_xref="CDD:451334"
ORIGIN      
        1 msvdtvsltg wgrtapttav rfrprtyeea aavvrgrgpr galarglgra pgdaaqnagg
       61 svldmtgldr iraldevagt vrcdagvsle rllrvlpprg wfppvvpgtg rmtvggaigs
      121 dvhgldhlaa gslarhvval elltadgevr tvtpgtalfd attgglgltg vilsatlrlr
      181 rvatgliavs terardlddl larftaggdr lpyasawvdl sargrsagrg vltrgehapl
      241 svlpaharrt aarrqrepwa aalsalpggl lgpaaaalvd evryrsapra rsgelrtpaa
      301 ffhpldatpv tdrlhrlsal stgrsglvry rftvgygqee algrvvrria arrctalrae
      361 lqrfgaaspg wlsfpapgwa ltvelpaalp glgrfldgld aevaaaggrv claqdsrmrp
      421 etaaamyprl pefrelrael dptgafrsdl arrlgl
//
LOCUS       WP_392069409             336 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            bacillaris].
ACCESSION   WP_392069409
VERSION     WP_392069409.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 336)
  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 336)
  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 336)
  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 11448557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..336
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=36136
     Region          38..99
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
ORIGIN      
        1 madhhpirpa rpgpsapssp sspdalspqg rgrppsafgq alrearerkg ltlarlrdhl
       61 arrgvrvstv tlshwqrgrs qperpeslra vsaiesilgc paggllallg prrprgrplp
      121 tpperlenar pvygpeplla ralgeeefsr lnegtvpvsv qetvhldrtg rtarhtvtqv
      181 vrathdgadh vtahlnvdep pgppmtasaq cgvlldqrcv palglttlri gfgrplarge
      241 stvvaytvdl gphghrtthh eralplhvrh yflhvvfhpe alpasvygyy rahdgaprad
      301 irtlplsgsg tahilpadaa agvhgifwkw pgtttt
//
LOCUS       WP_392070227             355 aa            linear   BCT 20-JAN-2025
DEFINITION  heme/hemin ABC transporter substrate-binding protein [Streptomyces
            bacillaris].
ACCESSION   WP_392070227
VERSION     WP_392070227.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Naoe,Y., Nakamura,N., Rahman,M.M., Tosha,T., Nagatoishi,S.,
            Tsumoto,K., Shiro,Y. and Sugimoto,H.
  TITLE     Structural basis for binding and transfer of heme in bacterial
            heme-acquisition systems
  JOURNAL   Proteins 85 (12), 2217-2230 (2017)
   PUBMED   28913898
REFERENCE   2  (residues 1 to 355)
  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   3  (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   4  (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   5  (residues 1 to 355)
  AUTHORS   Ho,W.W., Li,H., Eakanunkul,S., Tong,Y., Wilks,A., Guo,M. and
            Poulos,T.L.
  TITLE     Holo- and apo-bound structures of bacterial periplasmic
            heme-binding proteins
  JOURNAL   J Biol Chem 282 (49), 35796-35802 (2007)
   PUBMED   17925389
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..355
                     /product="heme/hemin 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=36115
     Region          84..352
                     /region_name="ChuT"
                     /note="ABC-type hemin transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG4558"
                     /db_xref="CDD:443619"
ORIGIN      
        1 mrisqdhgph qgqdagrpvr gragaaltvl valallltgc ggggndsask pakgagdadr
       61 veplaaapap klpvtvdsad gkkvtidstd rivpltgsls eivftlgfgk qvvarditat
      121 feqaeklpvv trahdvsaes vlslkptvvl adtttgpaea idqirsagip llvvepakgl
      181 ddvgrridtv aealgvpaag telkertear iaavqktipd hadgekprva flylrgsasv
      241 yllggaesga sslleaagav dagktsglkk dftaitseal akaapdaill mtkgfdsvgg
      301 mgglvkipgi aetpagmdrr vvtiddgvll nygprtdrvl adiveqlyak ggkgq
//
LOCUS       WP_392070249             479 aa            linear   BCT 20-JAN-2025
DEFINITION  alpha,alpha-trehalose-phosphate synthase (UDP-forming)
            [Streptomyces sp. NPDC015171].
ACCESSION   WP_392070249
VERSION     WP_392070249.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015171
  ORGANISM  Streptomyces sp. NPDC015171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 479)
  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 479)
  AUTHORS   Eastmond,P.J. and Graham,I.A.
  TITLE     Trehalose metabolism: a regulatory role for trehalose-6-phosphate?
  JOURNAL   Curr Opin Plant Biol 6 (3), 231-235 (2003)
   PUBMED   12753972
REFERENCE   3  (residues 1 to 479)
  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   4  (residues 1 to 479)
  AUTHORS   Elbein,A.D., Pan,Y.T., Pastuszak,I. and Carroll,D.
  TITLE     New insights on trehalose: a multifunctional molecule
  JOURNAL   Glycobiology 13 (4), 17R-27R (2003)
   PUBMED   12626396
REFERENCE   5  (residues 1 to 479)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 929-939 (1997)
   PUBMED   9334165
  REMARK    Erratum:[Biochem J 1998 Feb 1;329(Pt 3):719]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Streptomyces sp. NPDC015171"
                     /db_xref="taxon:3364945"
     Protein         1..479
                     /product="alpha,alpha-trehalose-phosphate synthase
                     (UDP-forming)"
                     /EC_number="2.4.1.15"
                     /GO_function="GO:0003825 - alpha,alpha-trehalose-phosphate
                     synthase (UDP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0005992 - trehalose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51797
     Region          10..478
                     /region_name="OtsA"
                     /note="Trehalose-6-phosphate synthase, GT20 family
                     [Carbohydrate transport and metabolism]; COG0380"
                     /db_xref="CDD:440149"
ORIGIN      
        1 mastrgaadk aqvlvasnrg pvayqvgedg slharrgggg lvsglsaiga dadsvwvcaa
       61 lgdgdraavr raaggllpae etggqrvrml didatvhaea yngiansvlw fvhhmlyqtp
      121 lepvfgtefr rqwasyeayn rafaealaee aaegaavliq dyhlalaprm lrqlrpdlri
      181 ghfshtpwap pdyfrllpdd iaaellggil gadraafltr rwadaftdcc htvlgpgips
      241 gtrigvhglg adaeflrkra qepdvaerma alraeigpgr rtivrvdrte lsknivrgll
      301 ayeqllagrp ewrervvhva faypsrqdla vyrdytaevq rvadginery gtadwtpvvl
      361 hvkddfarsl aayrladval vnpirdgmnl vakevpvvsd egcalvlsre agayeelged
      421 afvvnpydit gtaealheal slpadvraer skrlaaaata lpparwfldq lnaltgqps
//
LOCUS       WP_392071763             404 aa            linear   BCT 20-JAN-2025
DEFINITION  threonine synthase [Streptomyces bacillaris].
ACCESSION   WP_392071763
VERSION     WP_392071763.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 404)
  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 404)
  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   3  (residues 1 to 404)
  AUTHORS   Parsot,C.
  TITLE     Evolution of biosynthetic pathways: a common ancestor for threonine
            synthase, threonine dehydratase and D-serine dehydratase
  JOURNAL   EMBO J 5 (11), 3013-3019 (1986)
   PUBMED   3098560
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423064
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..404
                     /product="threonine synthase"
                     /EC_number="4.2.3.1"
                     /GO_function="GO:0004795 - threonine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009088 - threonine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42476
     Region          83..399
                     /region_name="ThrC"
                     /note="Threonine synthase [Amino acid transport and
                     metabolism]; COG0498"
                     /db_xref="CDD:440264"
ORIGIN      
        1 mttislatgq rslgdpdisy plwpplthgc prtssdamsy pleidydytr vtsdfitgqg
       61 rprsgldrwa pllpplaapg lgeggtplia igdgvyvkde srnptwshkd rlnritvsaa
      121 vavgapgvvv assgnhgasa aayaaraglr cvvlgsselp pavasflsay gavvlpveta
      181 rrwplteriv eefgfhpvsn ltpfhtghaf gaegyktvay eiaadivdpg avfvptgyge
      241 llfgiwkgft elhrlgllsr vprlfscepa aggplaaalr qglpatrvev adteaygiac
      301 pvnsyrgvra itgsggralt vddeamhraq aelagqglwv elssaaglag lrtlpddeti
      361 egpmvcvtts sgfkdtrvgd hhltpvdpsw esvrarlrae girs
//
LOCUS       WP_392072397             282 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015171].
ACCESSION   WP_392072397
VERSION     WP_392072397.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015171
  ORGANISM  Streptomyces sp. NPDC015171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 282)
  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 282)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces sp. NPDC015171"
                     /db_xref="taxon:3364945"
     Protein         1..282
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31319
     Region          17..68
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          90..263
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mvnireldps aspldyfgse lrrkreaagl tqkelgavif ctgsligqie ttlkvptref
       61 aeradaallt dgffsrlvgl vlrsqlptwf qpfaeleaka tyistyqaqm iygllqteay
      121 asavletgmp dkldelvaar merqrilare qppltwvvld eaalhrpigg advmrdqlah
      181 llsfrddkwv riqvlpfrvg ehasligsft glrfndhpdl iytedlisgh ttanpetvre
      241 aafryahlqa salsvedsaa litcvmeery ahtpgpdera ma
//
LOCUS       WP_392072531             404 aa            linear   BCT 20-JAN-2025
DEFINITION  M20 metallopeptidase family protein [Streptomyces sp. NPDC015171].
ACCESSION   WP_392072531
VERSION     WP_392072531.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015171
  ORGANISM  Streptomyces sp. NPDC015171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Lindner,H.A., Lunin,V.V., Alary,A., Hecker,R., Cygler,M. and
            Menard,R.
  TITLE     Essential roles of zinc ligation and enzyme dimerization for
            catalysis in the aminoacylase-1/M20 family
  JOURNAL   J Biol Chem 278 (45), 44496-44504 (2003)
   PUBMED   12933810
REFERENCE   2  (residues 1 to 404)
  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 11444961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Streptomyces sp. NPDC015171"
                     /db_xref="taxon:3364945"
     Protein         1..404
                     /product="M20 metallopeptidase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42020
     Region          9..401
                     /region_name="AbgB"
                     /note="Metal-dependent
                     amidase/aminoacylase/carboxypeptidase [General function
                     prediction only]; COG1473"
                     /db_xref="CDD:441082"
ORIGIN      
        1 mtgrqldpal vedlvrlred lhrepelgld lprtqakvla aldglpleit tgrglssvta
       61 vlrggagddr dgdrpavllr admdalplte ssgvpytski egrmhacghd lhtamlvgaa
      121 rllaegrggl rgdvvfmfqp geeghhgarl mieegvldaa grrpvaayav hvassmlpag
      181 wvltrkgpll aggdvlrvtv rgrgghdsqp qllrdpvpaa cemtlalqty asrgfdpfdp
      241 vllsvgsiha gtsaniipde aelkigvrtf gpgakaevie gvtrvlegia aahgvsvtvd
      301 hsmdypvtvv dpaeadfaag tvervlgpgr flwapntlsp sedfsfvlge vpgamlflga
      361 cppdrdpgta sfnhsadaaf gsevlgdgal llaclaedrl asag
//
LOCUS       WP_392073240             409 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC015171].
ACCESSION   WP_392073240
VERSION     WP_392073240.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015171
  ORGANISM  Streptomyces sp. NPDC015171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 409)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Streptomyces sp. NPDC015171"
                     /db_xref="taxon:3364945"
     Protein         1..409
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43192
     Region          70..251
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          258..383
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mnirpfsgas aqgrrgrrel aliagalvls ltacgggges gskaggdkga gsrqgtqsaa
       61 avsiapksga tgvdtsgalk vgvakgklte vtvkdekgak vdgaitggga swtpsthlag
      121 gtkytvhava kdsegreaae dssfttltpk ntfignftpe dgstvgvgmp fsvrftrgit
      181 hpqdvekair irtepavdve ghwfgndrld frpekywkeg tkvtveldld gvegrdgvyg
      241 kqrktvtfti grnqvsyvda kkhtmkvtqd gkvvktipvt tgkpgydtwn gqmvmreklv
      301 vtrmngetvg yggeydikdv phairltdsg tfvhgnywgg gafgnynash gciglrdvrg
      361 gydssvpaaw ffnhsmsgdv vvvknshdat vapdnglngw nmswadwkk
//
LOCUS       WP_392074530             355 aa            linear   BCT 20-JAN-2025
DEFINITION  gluconeogenesis factor YvcK family protein [Streptomyces sp.
            NPDC015171].
ACCESSION   WP_392074530
VERSION     WP_392074530.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015171
  ORGANISM  Streptomyces sp. NPDC015171
            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 10785358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Streptomyces sp. NPDC015171"
                     /db_xref="taxon:3364945"
     Protein         1..355
                     /product="gluconeogenesis factor YvcK family protein"
                     /GO_function="GO:0043743 - LPPG:FO 2-phospho-L-lactate
                     transferase activity [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=37925
     Region          38..343
                     /region_name="CofD"
                     /note="Archaeal 2-phospho-L-lactate transferase/Bacterial
                     gluconeogenesis factor, CofD/UPF0052 family [Carbohydrate
                     transport and metabolism, Coenzyme transport and
                     metabolism]; COG0391"
                     /db_xref="CDD:440160"
ORIGIN      
        1 mtertprlsr lrrmvpdara grpaevrggr prrrgaqpkv valgggmgls aslaalrrit
       61 gdltavvtva ddggssgrlr delgvlppgd lrkalaalcg ddewgqtwar viqhrfqskg
      121 dlhehavgnv livalweqlg dhvqaldlvg kllgahgrvl pmsavplelq alvkghdper
      181 pdevdtvrgq atvaltpgev qsvhlvpndp pavpeavaav ldadwvvlgp gswfssviph
      241 llvpelldal tqtkarrvls lnlepqpget egfspqrhle vlgrhapkla ldvvladdaa
      301 vpdrdsltea akrlgaavel apvartdgsp rhdpellaaa ydrifrmhgr igpwr
//
LOCUS       WP_392075282             356 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces sp. NPDC015171].
ACCESSION   WP_392075282
VERSION     WP_392075282.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015171
  ORGANISM  Streptomyces sp. NPDC015171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Streptomyces sp. NPDC015171"
                     /db_xref="taxon:3364945"
     Protein         1..356
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=35600
     Region          82..350
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 msslspsrsl tpaprpcpkt papapapgpv pvacpgsaap aspvswmsgr pvrlalclap
       61 lllaagwaaa nrpvvyegvr rlvaadpwwl lagagltcls wvaascvrqg alsdrlppgl
      121 llasqfaaga anhalpgglg ahavtlrflr aqgvpldrat asiglyslar saaktvvllv
      181 flaaspawrr lgdlipdgrl lvplaavagg alavagvllt vvrplrrpvt gllraavada
      241 rlvhtrparv lalwggavam plvqagtlac vgaslglglp weqvvlacla agtavgavpa
      301 pgglavdaal vwtlvtfgaa paaatatvig yrvltdwvpl vpgalvlsal irgkal
//
LOCUS       WP_392075722             237 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Streptomyces sp.
            NPDC015171].
ACCESSION   WP_392075722
VERSION     WP_392075722.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015171
  ORGANISM  Streptomyces sp. NPDC015171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 237)
  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 11440233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Streptomyces sp. NPDC015171"
                     /db_xref="taxon:3364945"
     Protein         1..237
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=26033
     Region          3..230
                     /region_name="GCD1"
                     /note="NDP-sugar pyrophosphorylase, includes eIF-2Bgamma,
                     eIF-2Bepsilon, and LPS biosynthesis protein s
                     [Translation, ribosomal structure and biogenesis, Cell
                     wall/membrane/envelope biogenesis]; COG1208"
                     /db_xref="CDD:440821"
ORIGIN      
        1 mhavilaggk gvrlrpytta lpkplvpigd qhaileivlr qlsaagftrc tiaighlgei
       61 irayvgdgtq wgmnvdyate esplgtmgpl lnlrdrlper flvmngdilt dldyadvlrr
      121 hetsgaplti atyarkvhid fgvlttdasr vvaftekpsm dyrvsmgvyg lsretldgyt
      181 aglplgfdel vldllriqnp phayefdgyw ldigrpddyd ranaeftsrk slllkga
//
LOCUS       WP_392076030             416 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC015171].
ACCESSION   WP_392076030
VERSION     WP_392076030.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015171
  ORGANISM  Streptomyces sp. NPDC015171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Streptomyces sp. NPDC015171"
                     /db_xref="taxon:3364945"
     Protein         1..416
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=45530
     Region          66..311
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mkilvlhrvp yfkieyhrgi shdrhdvtyf gtdqalatlp phlrcervsr pglrtafeea
       61 rdwlahrprh fdrvisvsey elldaallre hlgvpgapad qvalardkvl mkqavegagl
      121 rvprflslps fldlagrvpw egrtvlkphr gassedvlvf dtprqavaav tarrtgvprl
      181 dagedladfe aeefvsgpir hfdglvqdge llvltaseyv gtclryaqgs plgsfqlals
      241 qeerawvara laavriedgs fhleaiahrg etvflevgnr vggadvvatv elatgvhlps
      301 yelrallger vtgtlpeppa dqrlygwfvc pghhlagref qgldgtaafr dhpsviawne
      361 lppgsplphh ityqsgetvl agiiasdtpe ggrrwiadlf tslavrtrpa seqvpa
//
LOCUS       WP_392076319             139 aa            linear   BCT 20-JAN-2025
DEFINITION  TOBE domain-containing protein [Streptomyces sp. NPDC015171].
ACCESSION   WP_392076319
VERSION     WP_392076319.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015171
  ORGANISM  Streptomyces sp. NPDC015171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 139)
  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 10007583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Streptomyces sp. NPDC015171"
                     /db_xref="taxon:3364945"
     Protein         1..139
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=14236
     Region          1..138
                     /region_name="MopI"
                     /note="Molybdopterin-binding protein MopI [Coenzyme
                     transport and metabolism]; COG3585"
                     /db_xref="CDD:442804"
ORIGIN      
        1 mtlsirnqfp gtvtevhpge vmatvkvrld sgpeltaait leaveqlals pgmpvralvk
       61 stevslatqr veglsirnql pgtiarlttg eamasvkvsl agdeltavit kdavgdlglf
      121 vgsdvialik atevslata
//
LOCUS       WP_392077197             280 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015350].
ACCESSION   WP_392077197
VERSION     WP_392077197.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015350
  ORGANISM  Streptomyces sp. NPDC015350
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 280)
  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 280)
  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 10611723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Streptomyces sp. NPDC015350"
                     /db_xref="taxon:3364955"
     Protein         1..280
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28681
     Region          9..71
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(15,19,44)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(18,43)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(25..26,37,40,44..45)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          173..255
                     /region_name="DUF2690"
                     /note="Protein of unknown function (DUF2690); pfam10901"
                     /db_xref="CDD:402475"
ORIGIN      
        1 mtastvggql aeelrgvker sglslaalat rtpysksswe rylngkkpap rqavealcal
       61 tgtppgrlla lweladaews grarpvsapk apdepaeaep erlaaapsap aaragvrrwa
      121 vaaavagvva aglagttflg agtarpgaep ddgrphavte ppvrnpgcra dgcegknpva
      181 mgcggagmit tlathtasgg rrlelrhaal chtlwvrttg lrpgdrvels lptgrtqqvt
      241 atggrdtrqy latpmaagds gagtriclek pgsrpecftg
//
LOCUS       WP_392077662             242 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces sp.
            NPDC015350].
ACCESSION   WP_392077662
VERSION     WP_392077662.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015350
  ORGANISM  Streptomyces sp. NPDC015350
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptomyces sp. NPDC015350"
                     /db_xref="taxon:3364955"
     Protein         1..242
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=26545
     Region          1..235
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 msisllggfd ivvgdepvtv pggskrllaf ivlqyraavp ralvagslwp easdqgantn
       61 lrsalsrlqg lgkqalnicp aelrlarevt vdlfrarsla qqildpnvpa edldldvaai
      121 dqlsadllpg wydewvlpea eqwrqlrlha lealtgtfig lkefawavta ahaavqadpl
      181 ressqaslir ahlaednrse alcdferyeq hlrdelglrp tprlcrlvse lqrsrpgkcr
      241 gk
//
LOCUS       WP_392078748             502 aa            linear   BCT 20-JAN-2025
DEFINITION  SWIM zinc finger family protein [Streptomyces sp. NPDC015350].
ACCESSION   WP_392078748
VERSION     WP_392078748.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015350
  ORGANISM  Streptomyces sp. NPDC015350
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Hassan,I.U., Rehman,H.M., Liu,Z., Zhou,L., Samma,M.K., Wang,C.,
            Rong,Z., Qi,X., Cai,D. and Zhao,H.
  TITLE     Genome-wide identification and spatiotemporal expression profiling
            of zinc finger SWIM domain-containing protein family genes
  JOURNAL   Zool Res 44 (3), 663-674 (2023)
   PUBMED   37161653
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     SWIM, a novel Zn-chelating domain present in bacteria, archaea and
            eukaryotes
  JOURNAL   Trends Biochem Sci 27 (8), 384-386 (2002)
   PUBMED   12151216
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10516955
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Streptomyces sp. NPDC015350"
                     /db_xref="taxon:3364955"
     Protein         1..502
                     /product="SWIM zinc finger family protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51014
     Region          69..99
                     /region_name="SWIM"
                     /note="SWIM zinc finger; pfam04434"
                     /db_xref="CDD:309540"
     Region          <165..280
                     /region_name="Gdh2"
                     /note="NAD-specific glutamate dehydrogenase [Amino acid
                     transport and metabolism]; COG2902"
                     /db_xref="CDD:442147"
ORIGIN      
        1 mllshggeps rtatavarwt veqvlalapd easrkagskl gsagpwsggg cdgsgavwgl
       61 ckgsgskpyr tvvdvtgpay kcscpsrkfp ckhalglllv wasdgaalpg geapdwagew
      121 ltgrraraae rtgkdapggg aasgpadpea arrraerrae ritggaqele erladllrgg
      181 laaagqsgyg lweetaarmv daqapglaar vrelgsvpgs gqgwpvrlle ecallhllds
      241 awlgidrlpe plaatvrtrv gltthaegpp vrdhwlvlar ydtpdgriva rriwlhgrrt
      301 grtalllsfa apgrspapal pvgvtidaei tpypgagqlr aelgeqfgtp spvgtpppgg
      361 taadaigayg ralrddpwld swpvtlgevi pvpsgdgwql vdaaggaalp vapaalsrpg
      421 lwklvalsgg apvtvfgecg hrgfdplaaw steaeagaea eadtgngaga dtgtgtgadg
      481 adgteglgag ptdaafgtvp li
//
LOCUS       WP_392079054             276 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Streptomyces].
ACCESSION   WP_392079054
VERSION     WP_392079054.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 276)
  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 276)
  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 276)
  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 16111081
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..276
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30374
     Region          23..75
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(23,27,52)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(26,51)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(33..34,45,48,52..53)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          94..269
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 miegadqaqe pangavyfge etkalrealr lsqeqfadkl hyrqaqvskv engtvlasea
       61 fadamdrvag tpgvyarlra klskqghpew fvpyitlees asgitdysct flmgllqtpe
      121 yaraviraaf pretadqier rvelrirrqv vierdappll wvviheavlr acvggrdvmi
      181 gqlehliaqm asphvtvqvl pyragaapsh lpftllslnd tphavytetp thggqvddsp
      241 svvttavgmf drlrmaalse edsltlirki medhat
//
LOCUS       WP_392080204             432 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces omiyaensis].
ACCESSION   WP_392080204
VERSION     WP_392080204.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces omiyaensis
  ORGANISM  Streptomyces omiyaensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Streptomyces omiyaensis"
                     /db_xref="taxon:68247"
     Protein         1..432
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=46456
     Region          75..322
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mnrqserqpa vivmsdlaal arqhrlitdi aarglaplvv vgpttdltkl tghvadpahp
       61 lsrieavrqf pdaaiagvla svqdwiadyd irgvicsgev fvdpcgvlse alglpgpgaw
      121 aarvcrdkvm qrvilrdhgp vwrafaphqr esaaadsypa vvkpagrmfs sgvvrvende
      181 elraaltaye pdetilveel vtgpefsvea lvhhgeliws gvtakltned ssrffteigh
      241 tspadlplah tdalvaanaa ilkalrfdsg ithaefrlrd gqpvlmeiaa rlpgdaitmm
      301 whlatglpie paivdlalgv rpdyptptrr avqrfvehtp grltdvryeg epvswivdda
      361 fwpsveattp daparcasvm valargarlg tlndssgrsa yvvadlpwda dpvaevlayt
      421 drveltvead pa
//
LOCUS       WP_392080371             275 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015350].
ACCESSION   WP_392080371
VERSION     WP_392080371.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015350
  ORGANISM  Streptomyces sp. NPDC015350
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (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
REFERENCE   4  (residues 1 to 275)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Streptomyces sp. NPDC015350"
                     /db_xref="taxon:3364955"
     Protein         1..275
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31121
     Region          1..65
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          87..264
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mageeipear vlygkelrsr reaagltqeq lsqraflsrt hiahmeagrr lpspedaerl
       61 dqvletggff arflptlddd hkvaeyfeav aeferqatvi rhygpklipg llqteayare
      121 vlssgfppks eeerdrllvt rlkrarvldn fespvvwvll deavlhrpig gpalmaeqlr
      181 hvvklgerrr vrvhvlpfsv gyhallegmv slmwfedlpp iayteglksg rvwenpsavr
      241 ecqvaydhal gdalshresl alirsvaeey eheaq
//
LOCUS       WP_392080473             288 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptomyces sp.
            NPDC015350].
ACCESSION   WP_392080473
VERSION     WP_392080473.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015350
  ORGANISM  Streptomyces sp. NPDC015350
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 288)
  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 288)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 288)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 288)
  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   5  (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   6  (residues 1 to 288)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces sp. NPDC015350"
                     /db_xref="taxon:3364955"
     Protein         1..288
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31976
     Region          19..102
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          126..284
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mleklnqame hiedrldrri evtelariam tseyhfrrmf salagmplse yvrrrrltla
       61 gaevltgert lleiavrygy ssgeafaraf ramhgvgpge arragaalrs qprmsfrlvv
      121 egsssmqyri vekgefrvvg krarvplvhe gmnpaiaefi rgigkettgr iaalsdqqpe
      181 givgvsdkld esraegteld yyhgvvtgad vpddldalvv pagswavfen sgpfpqalqy
      241 lwrdvftqwf psnpyrsrpg peilrtrlsp dgaraeaelw ipveptas
//
LOCUS       WP_392082088             287 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces sp.
            NPDC015350].
ACCESSION   WP_392082088
VERSION     WP_392082088.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015350
  ORGANISM  Streptomyces sp. NPDC015350
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789410
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Streptomyces sp. NPDC015350"
                     /db_xref="taxon:3364955"
     Protein         1..287
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31616
     Region          4..259
                     /region_name="PrpB"
                     /note="2-Methylisocitrate lyase and related enzymes, PEP
                     mutase family [Carbohydrate transport and metabolism];
                     COG2513"
                     /db_xref="CDD:442003"
ORIGIN      
        1 mrygsalree vrspgttpli giydmysasv varhyegffv sgfgfaashy glpdigfiaw
       61 pdmvafverl rlafpshhll vdiddgyvdp evachvvqrl erigasgvil edqkrprrcg
      121 hadgkqvlpl eeyleklnlv lesrrdlvvv artdateedd ilrraealag tdadvvlvdg
      181 vrsvewikri rkvvgdkpll fnqiaggksp rlslseltdl ecqvaiystp clfaahaaid
      241 saltdlkead grlpefvpae gigvqrstel leknisrhhs vresvsv
//
LOCUS       WP_392080646             761 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Streptomyces sp. NPDC015350].
ACCESSION   WP_392080646
VERSION     WP_392080646.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015350
  ORGANISM  Streptomyces sp. NPDC015350
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 761)
  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 761)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
REFERENCE   3  (residues 1 to 761)
  AUTHORS   Linder,P., Lasko,P.F., Ashburner,M., Leroy,P., Nielsen,P.J.,
            Nishi,K., Schnier,J. and Slonimski,P.P.
  TITLE     Birth of the D-E-A-D box
  JOURNAL   Nature 337 (6203), 121-122 (1989)
   PUBMED   2563148
  REMARK    Erratum:[Nature 1989 Jul 20;340(6230):246]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423480
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Streptomyces sp. NPDC015350"
                     /db_xref="taxon:3364955"
     Protein         1..761
                     /product="ATP-dependent DNA helicase"
                     /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_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0032508 - DNA duplex unwinding [Evidence
                     IEA]"
                     /calculated_mol_wt=76181
     Region          238..757
                     /region_name="RecD"
                     /note="ATPase/5#-3# helicase helicase subunit RecD of the
                     DNA repair enzyme RecBCD (exonuclease V) [Replication,
                     recombination and repair]; COG0507"
                     /db_xref="CDD:440273"
ORIGIN      
        1 mtalprgetp gspaaaddgv vdpspavsar sagdeehapa gdaveadgpe egggseated
       61 gdgaatgttg eedegetaad aaggdaapal seaeaelaaq refreriekr ksekkgpvsa
      121 gtklsgtaad llaavraves gekpaapfld rpapaaapgr papapspapa rprapeptpa
      181 prsaspetla ataavlaegg apaalagpva evlgaqaaea lredpwrlla vpgvrpeqad
      241 gfarallgag cgpdderrta aliglllera alrghtaqda atvraalagh avtdpgaave
      301 havaegvvla frdgpenpep eaaeepgard ecgddgdgpe pvrvllgldr yalaeeslad
      361 glarlvnace kdadwteaas aagsssasel iravaahglv ahtggeaara epaalltaar
      421 glglralgta hsadgrhrla datgdpatav tlagllsgae gpgrdeegal avdllvvlda
      481 pqldvetaam lvesladgtr lvlsgdpgvl gsagagrvfa dvlaaracpq iasrtpdpgp
      541 igelvsgigi gelnqveapg revvivpvrd ageavhrtvq lvadsvprai gvpssdtqvi
      601 tvghggsagt ralnaalkqr lnpgpgrfgg fdpgdrvvhv pvpgrtvpav vvsadaeglr
      661 ldcggtevvv prervesavr hgwalsahqa agtrwpavvv vlpgdaaqgl srawvytafg
      721 rgerhlsvvh gvdqalprav aqspaqdrtt rlrdlleaas r
//
LOCUS       WP_392082868            1216 aa            linear   BCT 20-JAN-2025
DEFINITION  Rne/Rng family ribonuclease, partial [Streptomyces sp. NPDC015350].
ACCESSION   WP_392082868
VERSION     WP_392082868.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015350
  ORGANISM  Streptomyces sp. NPDC015350
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1216)
  AUTHORS   Kime,L., Jourdan,S.S. and McDowall,K.J.
  TITLE     Identifying and characterizing substrates of the RNase E/G family
            of enzymes
  JOURNAL   Methods Enzymol 447, 215-241 (2008)
   PUBMED   19161846
REFERENCE   2  (residues 1 to 1216)
  AUTHORS   Callaghan,A.J., Marcaida,M.J., Stead,J.A., McDowall,K.J.,
            Scott,W.G. and Luisi,B.F.
  TITLE     Structure of Escherichia coli RNase E catalytic domain and
            implications for RNA turnover
  JOURNAL   Nature 437 (7062), 1187-1191 (2005)
   PUBMED   16237448
REFERENCE   3  (residues 1 to 1216)
  AUTHORS   Li,Z., Pandit,S. and Deutscher,M.P.
  TITLE     RNase G (CafA protein) and RNase E are both required for the 5'
            maturation of 16S ribosomal RNA
  JOURNAL   EMBO J 18 (10), 2878-2885 (1999)
   PUBMED   10329633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..1216
                     /organism="Streptomyces sp. NPDC015350"
                     /db_xref="taxon:3364955"
     Protein         <1..1216
                     /product="Rne/Rng family ribonuclease"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
     Region          484..885
                     /region_name="CafA"
                     /note="Ribonuclease G or E [Translation, ribosomal
                     structure and biogenesis]; COG1530"
                     /db_xref="CDD:441139"
     Region          <941..1120
                     /region_name="rne"
                     /note="ribonuclease E; Reviewed; PRK10811"
                     /db_xref="CDD:236766"
ORIGIN      
        1 evveaveetp apeaevetve eaaparprrr avrkatapag apkaaevvev veetpaaepv
       61 vepepaaprg rtrrrasapa gapqqteape vveaveetpa peaevetvee aaparprrra
      121 vrkatapaga pkaaevvevv eetpaaepvv eeapaaeaee aaprgrqrrr ataaagrpef
      181 tgkpeftgkd eepvrrsrra srpavavfqa pvfaepmfqt petaaaaaaa srhdeveeea
      241 etveeptavt eapaaeaapq ggsrrrrrrr geaveaaepe qaavpeeepa eeepeaeada
      301 ehegegegde tdeygerpsr rrrrggrrrr rgeasendea leqhgeeaad hsedepeqaq
      361 eseeeeedhe avaagssssr rrrrrrrrsg daaadtdsga ddpertvvkv reprrkdsdr
      421 eagtgfdevq sikgstrmea kkqrrregre qgrrrvpiit eaeflarrea vervmvvrqn
      481 gertqigvle dnvlvehyvn keqatsyvgn vylgkvqnvl psmeaafvdi gkgrnavlya
      541 gevnfealgm ahgprrieta lksgqsvlvq vtkdpighkg arltsqvslp grylvyvpeg
      601 smtgisrklp dterarlkti lkkivpedag vivrtaaega sedelrrdve rlqqqwediq
      661 kkakstgssn aptllygepd mtvrvvrdif nedfskvivs gdeawetihg yvsqvapdlt
      721 drlsrwtsev difatyride qlmkaldrkv ylpsggslvi dkteamvvvd vntgkftgqg
      781 gnleetvtkn nleaaeeivr qlrlrdlggi vvvdfidmvl esnrdlvlrr lleclgrdrt
      841 khqvaevtsl glvqmtrkrv gqgllesfse tcvhcngrgv ivhmeqpssv ggggkrskkr
      901 grggaghdhe htveqghept agteveteae vaaevaapva lpepefvpde elysspaeae
      961 aavrgrgrrr atrkvsapag apkaaaepvv apepvakpep aavepepvva aepvdttpva
     1021 vepqpaeetp vaeapqgrtr rratrkatap agapkaaaep vvveeaaera vpeqaaepap
     1081 qaeeapvaea pkaeatpeev apeaapprar rrvtrkvtap agspagadga evvvvtapkt
     1141 eskpdaepka dtepaetaee aapakktark takkatakka atkktaakkt atkktaakkt
     1201 takkaakaav padaes
//
LOCUS       WP_392083052             363 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            sp. NPDC015350].
ACCESSION   WP_392083052
VERSION     WP_392083052.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015350
  ORGANISM  Streptomyces sp. NPDC015350
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   3  (residues 1 to 363)
  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   4  (residues 1 to 363)
  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 363)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Streptomyces sp. NPDC015350"
                     /db_xref="taxon:3364955"
     Protein         1..363
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38904
     Region          2..341
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 mfgrrpdqav rrledgadrd elrsdgttaa vidasftvep gqifvvmgls gsgkstllrm
       61 lnglleptag rvlfdgqdlt altpaelrhv rsskismvfq hfalfphrsv lenaayglev
      121 qgvpraerek raaealeltg lagwekswpd elsggmqqrv glaralatda dlllmdesfs
      181 aldplirrdm qdqllelqkr lkktivfith dlneamrlgd riavmrdgri vqlgtaedil
      241 vtpandyvas ftqdvdrtrv ltagaimaep htvmgtstdd gkelrtaadv iaaapatvte
      301 stpiaelftp csqsgvavav tdaggklvgv vprarllavl gepmtpaeap kdvpadlkkv
      361 asv
//
LOCUS       WP_392083639             263 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015350].
ACCESSION   WP_392083639
VERSION     WP_392083639.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015350
  ORGANISM  Streptomyces sp. NPDC015350
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 263)
  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 263)
  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 11448557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Streptomyces sp. NPDC015350"
                     /db_xref="taxon:3364955"
     Protein         1..263
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29469
     Region          11..71
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
ORIGIN      
        1 mapiddpnng vgrlarelre arsrrgltrr elasrinrsl ttiqraeage vrptllvare
       61 iaeacgigad dieilwkkas rlgrghrmtd aprlnlvrts adlaaalrrv weengeptsr
      121 qmeeraears kefaplsrms awrirerkqp vtsvrqmhay liacevpees fpgwvkawqr
      181 akrderrtpr papapapghp rrkvtpseaf sfmlqaglkp ldpfpgqmap wtavcttcss
      241 isrvryskvk mgigcriclr daa
//
LOCUS       WP_392084256             402 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC015350].
ACCESSION   WP_392084256
VERSION     WP_392084256.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015350
  ORGANISM  Streptomyces sp. NPDC015350
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 402)
  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 402)
  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
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 402)
  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   5  (residues 1 to 402)
  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   6  (residues 1 to 402)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 402)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 402)
  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 18565976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Streptomyces sp. NPDC015350"
                     /db_xref="taxon:3364955"
     Protein         1..402
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40873
     Region          15..>89
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
     Region          82..391
                     /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 mwkdpgmpas pstaralndr lalrllqqeg pltaaqlkkl tglsrptvad lverlreagl
       61 vevvgesgae rrgpnarlyg ivadrahlaa ldvrtrgvam avadllgntl aeatlpvdgd
      121 tdadtaaeqa aalleriare agpaplhsvg igapglidpv tgelrdttgl pawhrrlvrv
      181 lqerlpatvl venetnlaav aehrsgaard rdtfvlfwlg hgigaavmld galrrgasgg
      241 ageigflpvp gavgvpsaln cdggfhslvg stpvcelaaa hgivvppgta ggekepgaas
      301 avraalageg rheafldvla erlalgaaai asvldpgcvv lagevghagg dalaarveer
      361 lvtmsplrte vragrlggga vlrgallaar eaaqdelftp tg
//
LOCUS       WP_392084716             279 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            eurythermus].
ACCESSION   WP_392084716
VERSION     WP_392084716.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces eurythermus
  ORGANISM  Streptomyces eurythermus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 279)
  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 279)
  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 10611723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces eurythermus"
                     /db_xref="taxon:42237"
     Protein         1..279
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28808
     Region          10..72
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(16,20,45)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(19,44)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(26..27,38,41,45..46)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          168..>229
                     /region_name="DUF2690"
                     /note="Protein of unknown function (DUF2690); pfam10901"
                     /db_xref="CDD:402475"
ORIGIN      
        1 mtalapecaa laeglravka rtglsltgla ertpysrssw erylngkkpv prqavealca
       61 magepsarll alweladaew sgrarstgpt appvptappa sagagtgalg rarreyrlvv
      121 gaglavvaaa mtgvlivvls vlnpgtghpa raalpaldpv pgcqgrtceg kdpdrmfcgl
      181 pgradslgpe hrtatgahve irystvcaaa wgriwharvg dtielsapga rsrrtviena
      241 sdtgvyrfta migaparstl rlcflpvsga grkecvspg
//
LOCUS       WP_392086583             290 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Streptomyces omiyaensis].
ACCESSION   WP_392086583
VERSION     WP_392086583.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces omiyaensis
  ORGANISM  Streptomyces omiyaensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces omiyaensis"
                     /db_xref="taxon:68247"
     Protein         1..290
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=30393
     Region          2..282
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 malvapagpv ndhetalava lleswglrpr ttsrlsathr gylagsdgtr ladfteawld
       61 pavravlcvr ggygtqrvad rldhrrlaaa gpkflvgssd itclhqalge glrlvtlhap
      121 mpacrpvhdd dhtaealraa lfgpsprsfs ldgpvlvagr aegtltggnl tvlasslgta
      181 tapltddril lledvgeepy rldrsltqlr ragvlqraag vvlgdftdcg ppdqvdallr
      241 aclsdlgvpv aaglpaghgp rqltvplgar avldtarrrl tlppherntp
//
LOCUS       WP_392086980             307 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Streptomyces eurythermus].
ACCESSION   WP_392086980
VERSION     WP_392086980.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces eurythermus
  ORGANISM  Streptomyces eurythermus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces eurythermus"
                     /db_xref="taxon:42237"
     Protein         1..307
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32084
     Region          4..305
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mkelvrphrl apgarvavva tsgpvpeerl qagldvlrgw dldpvpgpha ldrhpgfgyl
       61 agtdadraad frnawcdpav davlcarggy gaqrmvdlld wdalraagpk lfigfsdvta
      121 lheaiatrlg lvtlhgpvaa gadfiknqra qehlratlfa petvrtlafg gtalvpgrar
      181 gvtlggclsl laaelgtpha rpsarggllc ledvgepayr ldrcltqllr agrldgvrgv
      241 llgswedcag qeelralfad rlgglgipva envgfghceg altvplgvaa tldteagtlt
      301 ldepalr
//
LOCUS       WP_392088189             424 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces eurythermus].
ACCESSION   WP_392088189
VERSION     WP_392088189.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces eurythermus
  ORGANISM  Streptomyces eurythermus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Streptomyces eurythermus"
                     /db_xref="taxon:42237"
     Protein         1..424
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=46727
     Region          72..314
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mkaeqgpfll lntkkivsrl hewfpdaare lvvvttkadi psadisayar rflhlevvpn
       61 lwelsddell glarrfgvrr ilslgerevl raariraelg lpgqslasat ayrdkhvmks
      121 tlaaagidva pmrkfrtndd laefawkvgf pvvvkeldsg asngtvvlmd eedlralper
      181 ataaprlaea wvegdfyhvn glmkdgevvl avpsrnlysd wfsvaydapt mtgmmpddhp
      241 lserlrsiar qvvaalpavp dlcafhlelf htaddrvvvc eiacragaal vsdvheavlg
      301 vnfhgasllg qagrgdqvei rptgerlgfv wfppakgvlr alpdtcplpg tvsyrpcgdi
      361 grrygsssgl grpvaemvfr ltepdtgael rrieewwddn vvwehrtnav pdrwktprrk
      421 pada
//
LOCUS       WP_392089134             506 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Streptomyces eurythermus].
ACCESSION   WP_392089134
VERSION     WP_392089134.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces eurythermus
  ORGANISM  Streptomyces eurythermus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 506)
  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 506)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Streptomyces eurythermus"
                     /db_xref="taxon:42237"
     Protein         1..506
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53683
     Region          246..423
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 mpnrtpprvr prplprlela arprpwaral glaavvlaga wlgllvvgav rvpvgpvdtt
       61 malrpsltgg tridvsplga lsldshaapl rldvnvdrld pprsqalvdh perisglqde
      121 ivrdvehgtr dlavrscvav vlgagvlgla vyrrprrala agglalvlla asgasayatw
      181 npksvleprf sgllasapsv vgnarsivte fdvyqqelar lvtnvtklyd atstlpayrp
      241 dpttirvlhv sdihlnpasw kiigslvkqy qvnvivdsgd tmdhgtaaen gfldpigdlg
      301 vpyvwvrgnh dsrttqrhle rmrnvrvldd gravtvgglr fagigdpqft pdrsaapgge
      361 aaerlagarl asalrdqqaa gtpvdvavah eptaaeetdg qvplvlcghl hhegtqmlpy
      421 gtrlrregst ggsglraver ehpapiqasi lyfdrdsrrl qawdaielgg lglttaevsr
      481 hlvdenqpga tapsgspspa sprtsp
//
LOCUS       WP_392089438             326 aa            linear   BCT 20-JAN-2025
DEFINITION  quinone oxidoreductase family protein [Streptomyces sp.
            NPDC014870].
ACCESSION   WP_392089438
VERSION     WP_392089438.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014870
  ORGANISM  Streptomyces sp. NPDC014870
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 326)
  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 326)
  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 326)
  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   4  (residues 1 to 326)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces sp. NPDC014870"
                     /db_xref="taxon:3364925"
     Protein         1..326
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=32751
     Region          1..323
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 mraiefeqtg gpevlrtvea alpepgpgqv sidvahagvn fadlkaraeg yrvpalpyrp
       61 gleasgrira lgagvtglsv geqvtalteg gayaevvlad attvfplpag idlrtaatlp
      121 tvlptayalv htvgrirpge silvqgaagg igtvvgqlak aagagavygv vsseakadha
      181 lahgydevfv gafekavrda tggrgvdlal dpvggdtfra alaslavfgr lvsfgnagsa
      241 epwrvgqpel yptgltvggf silslaqtap aelralaera fatvadgtvt lpvtaefpla
      301 eaaeahrlmg arastgklll tvaggn
//
LOCUS       WP_392091085             278 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC014870].
ACCESSION   WP_392091085
VERSION     WP_392091085.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014870
  ORGANISM  Streptomyces sp. NPDC014870
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 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   4  (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 16111081
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Streptomyces sp. NPDC014870"
                     /db_xref="taxon:3364925"
     Protein         1..278
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31103
     Region          22..69
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(22,26,51)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(25,50)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(32..33,44,47,51..52)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          91..272
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mtrsenrepv gtaarmvavm akklrvrkgl tqeqlgsrmg ysgaaisame rmlhpisdem
       61 lenveealgd gsgffegmre lvrmeklpeq frdyapieqt avslwlyanh vvhglfqtea
      121 ymraligggy pepsaeriee lvagrmarka lfdrkptcei elvldesvll rpfgsqevmr
      181 aqllylaeca rrknvnlqvl pldaglrgey aadrgnltvv etpqhdrvtf leiqgeslli
      241 tdrtkvsthm qryakiraqa ldpreslgli erlagatr
//
LOCUS       WP_392092711             425 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC014870].
ACCESSION   WP_392092711
VERSION     WP_392092711.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014870
  ORGANISM  Streptomyces sp. NPDC014870
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Streptomyces sp. NPDC014870"
                     /db_xref="taxon:3364925"
     Protein         1..425
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=46019
     Region          69..311
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mkililhrvp yfkieyhrgi shgrhdvtyf gteaalatlp pelrcervgr pgarpafeea
       61 rdwlagsprt fdriismsey elldaarlre hlgvpgapve qvalardkvl mkraveeagl
      121 rvprflplpr llqldgrapw dgrtvlkphr gassedvlvh dspreavaav tagrtgvarl
      181 dagrefadfq veefvtgpir hfdglvqdge vlaltaseyl gtcleyargr pmgsfqigcs
      241 eetrawvsra laavriedgt fhleaivhgg elvflevgnr vggadvvatf elatgvhlps
      301 yelrvllgep vrgtlpepdp dglryawfvh pghhlagray gglagvgafr sgprvvawhe
      361 lppgaplpdh ityqagetvl agivagdtpe etrewmaalf gslsvdtrpa taapltpgtp
      421 eqvpa
//
LOCUS       WP_392092712             441 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC014870].
ACCESSION   WP_392092712
VERSION     WP_392092712.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014870
  ORGANISM  Streptomyces sp. NPDC014870
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Streptomyces sp. NPDC014870"
                     /db_xref="taxon:3364925"
     Protein         1..441
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=48010
     Region          72..315
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mtrpillivd ynlsridevr hlrdhartrh gasvvlirae pteadhtiad evidldplgd
       61 rfpelaekll gdrrerigag ivfsdnavhs gaellhrlgv pvdsprqaag afskyryrld
      121 earvadllta qrimvpafae iasldqlref giahpegfvv kpsaegnnrg vvvvrpgddl
      181 taafaevlpy leggviceel ipyarefsyd glgplsflte kvsargrypv eiaqvlparl
      241 deheratler agrqanwlvg qcdgpfhnei klsddglraa ivepnrrpag mkiwalarwv
      301 ygidlhhrwv dtafgtaada gplvpgcaaa tvmlgvgsdr sfspddvpag adpfadavra
      361 taeqfglaeg eltvtefawm sadrrdlhav ardnadfaaq gcvvlrgdra dirtvvhalr
      421 eawsqaldqa vavptparka r
//
LOCUS       WP_392092999             451 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC014870].
ACCESSION   WP_392092999
VERSION     WP_392092999.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014870
  ORGANISM  Streptomyces sp. NPDC014870
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Streptomyces sp. NPDC014870"
                     /db_xref="taxon:3364925"
     Protein         1..451
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=48291
     Region          71..323
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 menargvlll shvgfsfled lartvrargl kvhvlsslpe pqhqgsrpga ladladdvri
       61 tgehvltphd veehldrlra agvsvacclt vwegyrhlma lanarlgvpd ldekqvpelr
      121 dkltlrnrla daglsrgras altpetlaar qrdggrhfvk pvsglasfgt fpltpattwt
      181 dleriaaear adtvyasafg tepggrgmef lvedyvpgre fsfevivvdg ashvvavhek
      241 cevtetpgtv lenacvsppt slsreetaag lrwlarvldt lgldqgcfhv earydppagw
      301 dlievnprvg gslispsvaa ltggpglldl wldallaggg drttatylkt leslsygsdg
      361 ttpspyatff rvffadpgtl ravgpgdglp lrpvlsqill kagdvvessa revflgqvlw
      421 smdradrdai lpgllpaser aieivyeteh a
//
LOCUS       WP_392093096             305 aa            linear   BCT 20-JAN-2025
DEFINITION  quinone oxidoreductase family protein [Streptomyces caelestis].
ACCESSION   WP_392093096
VERSION     WP_392093096.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces caelestis
  ORGANISM  Streptomyces caelestis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 305)
  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 305)
  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 305)
  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   4  (residues 1 to 305)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Streptomyces caelestis"
                     /db_xref="taxon:36816"
     Protein         1..305
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=31206
     Region          1..305
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 mrrvryksrg galfleeapv pgpgpgellv raeaigvtlp vvrkvtegae pvplggeiag
       61 evtavgegvt rfgtgdrvtg lcsghgyadf allhetmasp vpadadavta valvrgglva
      121 lgaleaarpe pgeaalvtaa asgvghlavq larrrgagrv vgavsdsvka dfvrglgadh
      181 vvtygddswg apvdyaldgv ggellpqalt alapegrlva yssgggtvqa ydllvgaksv
      241 tgfqmariar gkpelyeqwr eelwrlfaag elqpvvhgef aledaakahg eiearanlgk
      301 vvlip
//
LOCUS       WP_392093158             310 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Streptomyces caelestis].
ACCESSION   WP_392093158
VERSION     WP_392093158.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces caelestis
  ORGANISM  Streptomyces caelestis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces caelestis"
                     /db_xref="taxon:36816"
     Protein         1..310
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32266
     Region          6..308
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mrqlprpprl apgarvavva psgpvpeerl qagldvlrgw dldpvvaphv ldrhreldyl
       61 agtdaqraad lqnawcdpav aavlcarggy gaqrmadlld weamraagpk vfagfsditv
      121 lhqafatrlg latlygpaaa gvdfvknara qehlratlfd pesvrtvtav ppggtalvpg
      181 rargvtlggc lsllasdlgt phalagargg llliedvges pyridryltq llrtgwldgv
      241 agivlgswag cgpyqelrav fadrlgglgv pvveefgfgh cegaltmplg ataeldaatg
      301 tltfdapals
//
LOCUS       WP_392095755             286 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            caelestis].
ACCESSION   WP_392095755
VERSION     WP_392095755.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces caelestis
  ORGANISM  Streptomyces caelestis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 286)
  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 286)
  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 16111081
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces caelestis"
                     /db_xref="taxon:36816"
     Protein         1..286
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32116
     Region          18..72
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(20,24,49)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(23,48)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(30..31,42,45,49..50)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          100..281
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mseprsaptv gqvvlgrrll dlreragmkr eeaarilhva patvrrmema evalkipylq
       61 lllkaygisg eeadafvqla eeankpgwwq rfhdilpgwf smyvslegaa gvirsyephf
      121 vpgllqtedy argvlrsgai gqtrpddier hvalrmqrqe lltrkdaprl wvvmdetvlr
      181 rpvggpevmr aqidrlleat klpnvtlqva pfavgphpgt ygpfvlfrfa mpelpdmvys
      241 eyltgavyld araevathle vmdrmaaqaa tahrtkeilr dlrkel
//
LOCUS       WP_392096020             319 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            caelestis].
ACCESSION   WP_392096020
VERSION     WP_392096020.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces caelestis
  ORGANISM  Streptomyces caelestis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 319)
  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 319)
  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 319)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Streptomyces caelestis"
                     /db_xref="taxon:36816"
     Protein         1..319
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=36497
     Region          15..70
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          94..269
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 msrrnggaes gastaavfge vlrhfreaal ltqeglarqm pcdrshvarv eagtrvpqeg
       61 fakkcdellg tggvllrlwg ridwypqveh pdwfrrraem devavtlrey qervipgllq
      121 tpeyaralss ryvsgvelee rvrarmsrqq rflaeggply ivvldesclr nvvggpavmr
      181 dqcahllsva qrpniriqva pagpleivrp sgsmslitlp egrqwlyses lnrghftndp
      241 alyerynqfy dvlradalsa pqsaalihea meryehygpe rarrsdldqe qlqrwqrrql
      301 hrnspryprr rphprqqnp
//
LOCUS       WP_392096352             399 aa            linear   BCT 20-JAN-2025
DEFINITION  threonine synthase [Streptomyces sp. NPDC014870].
ACCESSION   WP_392096352
VERSION     WP_392096352.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014870
  ORGANISM  Streptomyces sp. NPDC014870
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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   3  (residues 1 to 399)
  AUTHORS   Parsot,C.
  TITLE     Evolution of biosynthetic pathways: a common ancestor for threonine
            synthase, threonine dehydratase and D-serine dehydratase
  JOURNAL   EMBO J 5 (11), 3013-3019 (1986)
   PUBMED   3098560
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423064
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Streptomyces sp. NPDC014870"
                     /db_xref="taxon:3364925"
     Protein         1..399
                     /product="threonine synthase"
                     /EC_number="4.2.3.1"
                     /GO_function="GO:0004795 - threonine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009088 - threonine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=41725
     Region          79..380
                     /region_name="ThrC"
                     /note="Threonine synthase [Amino acid transport and
                     metabolism]; COG0498"
                     /db_xref="CDD:440264"
ORIGIN      
        1 mnslasgqrs lrdpavrhpl wppltagdpa tstdsvaypl didydydrvp ddlftrpaah
       61 glerwapllp plaapglgeg ntplvrladg vwikdesrnp twshkdrlnr lavsaaaasg
      121 argivvsssg nhgasaaaya araglpctvf tspyappava shlraygatv ltvpydsvrp
      181 lmrrivdelg yqpvssvtdt ahtghpfgpe gyktiayeia velgrapaav hlptgygell
      241 ygvakgflel arlgvtdsvp rmyatepaaa galtqamrtg adtarvpvgp taayaidcei
      301 sgyrgvvalr etggeartvt ddqmaqaqae laaqglwcev saaaglaglr thgpadedgp
      361 vvcvatssgy kdtatardth apvnltweel ktrlaqart
//
LOCUS       WP_392096972             517 aa            linear   BCT 20-JAN-2025
DEFINITION  complex I subunit 4 family protein [Streptomyces sp. NPDC014870].
ACCESSION   WP_392096972
VERSION     WP_392096972.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014870
  ORGANISM  Streptomyces sp. NPDC014870
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 517)
  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 517)
  AUTHORS   Galemou Yoga,E., Angerer,H., Parey,K. and Zickermann,V.
  TITLE     Respiratory complex I - Mechanistic insights and advances in
            structure determination
  JOURNAL   Biochim Biophys Acta Bioenerg 1861 (3), 148153 (2020)
   PUBMED   31935361
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Friedrich,T. and Scheide,D.
  TITLE     The respiratory complex I of bacteria, archaea and eukarya and its
            module common with membrane-bound multisubunit hydrogenases
  JOURNAL   FEBS Lett 479 (1-2), 1-5 (2000)
   PUBMED   10940377
REFERENCE   4  (residues 1 to 517)
  AUTHORS   Walker,J.E.
  TITLE     The NADH:ubiquinone oxidoreductase (complex I) of respiratory
            chains
  JOURNAL   Q Rev Biophys 25 (3), 253-324 (1992)
   PUBMED   1470679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Streptomyces sp. NPDC014870"
                     /db_xref="taxon:3364925"
     Protein         1..517
                     /product="complex I subunit 4 family protein"
                     /GO_component="GO:0045271 - respiratory chain complex I
                     [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048039 - ubiquinone binding [Evidence
                     IEA]"
                     /GO_process="GO:0015990 - electron transport coupled
                     proton transport [Evidence IEA]"
                     /GO_process="GO:0042773 - ATP synthesis coupled electron
                     transport [Evidence IEA]"
                     /calculated_mol_wt=53392
     Region          4..514
                     /region_name="NuoM"
                     /note="NADH:ubiquinone oxidoreductase subunit 4 (chain M)
                     [Energy production and conversion]; COG1008"
                     /db_xref="CDD:440632"
ORIGIN      
        1 mqfllaliva gpllgavaal lpappglkgk spdqavlrhg vtvtgvilla aivlalgfdh
       61 dqpskiqast dikwipaldv rlhlgvdgis lpllvmtall tflcalysyf kmpsgpspkg
      121 fvalllvles gtlatfavld lilfflafem vlipmyflia rwggagrqaa awkfilftll
      181 gsvvmllgll ligvkagtfd mvalaadngr glstavqvia vlsigiglav ktpmwplhsw
      241 lpdahtaapt vgsvllagvl lkmgtygfvr illpitpdgm rtfapylaaf aavgiiygsl
      301 aclaltrpgv ngdlkrliay ssvghmgfvl lgiatmtptg vngalfania hglitgllff
      361 lvgavkdryg tadldtlaga tgaalygrap rlggllafaa vaslglpgla gfwgemlalf
      421 gafepaegls rpafltfmvm ggigtlltaa ylllvvrrvc mggprpsgeg aladvqgyef
      481 aawtplvalt vlaglwpavl lgltdpavqq llaggns
//
LOCUS       WP_392097175             250 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            caelestis].
ACCESSION   WP_392097175
VERSION     WP_392097175.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces caelestis
  ORGANISM  Streptomyces caelestis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 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
REFERENCE   4  (residues 1 to 250)
  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 16111081
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Streptomyces caelestis"
                     /db_xref="taxon:36816"
     Protein         1..250
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28331
     Region          1..49
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(2,6,31)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(5,30)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(12..13,24,27,31..32)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          71..245
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mkrwrtkani sreelaaaan ysldtiksme qgvrmptpra ldtadelcga egflsaakey
       61 lqrekfpara qdfmererea isiwwyevsl ipgllqtkey aralienrip pldeetveer
      121 iaarmerqai lterkppvgl sfvlyeavlr splvdahqlr hllevsrlrn vvlqvlpfer
      181 aissallgpm vlletrdher faftegplas elsadpgavn rvterlsmir tqaldpdgsa
      241 rfiermvdqs
//
LOCUS       WP_392097425             363 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            caelestis].
ACCESSION   WP_392097425
VERSION     WP_392097425.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces caelestis
  ORGANISM  Streptomyces caelestis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   3  (residues 1 to 363)
  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   4  (residues 1 to 363)
  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 363)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Streptomyces caelestis"
                     /db_xref="taxon:36816"
     Protein         1..363
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39572
     Region          5..338
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 msaglqaesl ykvfgrrpdq averlrdgad reelraegvt aavidasftv epgqifvvmg
       61 lsgsgkstll rmlngllept agkvridgqd lttlgdrelr evrskkismv fqhfalfphr
      121 svrenaaygl evqgvpraer vrradealal cglagweksw pdelsggmqq rvglaralat
      181 daelllmdes fsaldplirr dmqdqllelq qklkktivfi thdlneamrl gdriavmrdg
      241 rivqngtaqd illrpandyv asftqdvdrs rvltagelmd tsvtaddpgc hcrtattgts
      301 ftelcaisar lshpvsvvde dnkligvvpr qrlvgflgda pdstpqscds prdkggekvt
      361 ara
//
LOCUS       WP_392098652             405 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces caelestis].
ACCESSION   WP_392098652
VERSION     WP_392098652.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces caelestis
  ORGANISM  Streptomyces caelestis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Streptomyces caelestis"
                     /db_xref="taxon:36816"
     Protein         1..405
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=43151
     Region          57..309
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 matvvmleal afglerlsaa agrlgvdlvl ltfdrayysr qlqrageirv vdvdtfdada
       61 vrhaldglgr vdgmvsntdt waplaeqlas ergfpnvisq aarlrdkvwv rnrlvdaglt
      121 rlravrgsdw aalpaasrpa mavvkdaagt ssknvllaer qeevearite lvergvpaer
      181 vtvepylcgp lysaetytte sgtvlfgins rtiselpdfr emdltfpvdr ggawekeiad
      241 wacevlgaig rgvgpshief iqtasgpevv evnprlgggh igeavlrvtg vdpyelllvq
      301 aleprleerh vaaatcrpta ggfaqvlkya srtgplgpve gadvlslfpg ditwtplkgp
      361 dtvidsvadq gacygfltat gpnpdtalsr alaaarhlrt sasap
//
LOCUS       WP_392099432             280 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            olivaceus].
ACCESSION   WP_392099432
VERSION     WP_392099432.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces olivaceus
  ORGANISM  Streptomyces olivaceus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 280)
  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 280)
  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 16111081
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Streptomyces olivaceus"
                     /db_xref="taxon:47716"
     Protein         1..280
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31320
     Region          20..71
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(22,26,51)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(25,50)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(32..33,44,47,51..52)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          90..261
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 maniqsldpt aspldyygwe lrrqreahgl kqgqlgdiif ctgsligqie ttkkvptrdf
       61 servdaalgt dglfsrligl vlrsqlptwf qpyaemeana ayistyqaql vygllqteey
      121 aravlatgrp gqldsllaar lerqrildwe kppvalvild eavlhrpvgg ddvmrrqlgh
      181 llkcirhrwm riqvlplssg ehpglegaft ifrfddhpdv fytedmmsgh mtadpdtike
      241 anlnyahlqa aalsvkdsaa ltarvmeery adrterspva
//
LOCUS       WP_392100743             292 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015237].
ACCESSION   WP_392100743
VERSION     WP_392100743.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015237
  ORGANISM  Streptomyces sp. NPDC015237
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 292)
  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 292)
  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 292)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptomyces sp. NPDC015237"
                     /db_xref="taxon:3364949"
     Protein         1..292
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32456
     Region          30..>72
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          109..287
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mtsgprqnna egrpeppeda dglldlnrav grqvkllrer agltqkdlgd rlgygedlvs
       61 slergrrtpq pefldaaddl ldaggllkat kedvaraktr arvrhpawfr dyarlegeav
      121 evndysshdi pglfqterra ralygmrtpl ldvetieqrv vsrlarqdil akwpppmvta
      181 vieesvlrrp iggaevhkeq mshllalgrl rsvelqvmpl erdehagmgg pfilltpkgk
      241 pqvgyvevqd iarlatdaee vrilaarygs iraqaltpre slaliermqt el
//
LOCUS       WP_392100098             411 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces olivaceus].
ACCESSION   WP_392100098
VERSION     WP_392100098.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces olivaceus
  ORGANISM  Streptomyces olivaceus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 411)
  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 411)
  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
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 411)
  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   5  (residues 1 to 411)
  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   6  (residues 1 to 411)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 411)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 411)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Streptomyces olivaceus"
                     /db_xref="taxon:47716"
     Protein         1..411
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42905
     Region          13..>58
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          77..391
                     /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 mrrgsnqlrl adynqavvle lvrrsrgvsr adlqresgls sqtisnitrr lideqlires
       61 tpggsargrp siplvtdpdg aysvgvhidp arltvvlldl agevrlgrqe htpqvtdpse
      121 vtafiadtvh gliteagvdr arvlglgiaa pgpldadagv lldppqlpnw rdvrlgadlr
      181 eatglpvllg kdvtaaatae lrasqetsnt fvflylgsgv gasvvldnqv vrgttnnige
      241 vgdllvdsda eqlewsgrrg glaaacvpea lvlqaarvgl mplpdlndyv avddacsalc
      301 araaegdava arllrraahr vavglgvlvn lldvprvvig gplwdrlspa flpvigdlva
      361 relvaargve vqgsavgdrv aaqgaaelvl dqflaprasa lmvgrpargd g
//
LOCUS       WP_392101148             289 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015237].
ACCESSION   WP_392101148
VERSION     WP_392101148.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015237
  ORGANISM  Streptomyces sp. NPDC015237
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 289)
  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 289)
  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 289)
  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 10611723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces sp. NPDC015237"
                     /db_xref="taxon:3364949"
     Protein         1..289
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31000
     Region          7..63
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(13,17,42)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(16,41)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(23..24,35,38,42..43)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          168..250
                     /region_name="DUF2690"
                     /note="Protein of unknown function (DUF2690); pfam10901"
                     /db_xref="CDD:402475"
ORIGIN      
        1 mstehtrlva alrelrsrag lslaalaert pysksswery lngkslpprh avrelcrlad
       61 epdgrllvlr eiaeshwsgr avatapaasp destrphpqe lpppdgtrrl rlrrsrllvv
      121 laaaytvvvg gvaallflll pdseareaes lpasvpfsfa plcegaaceg qdpmrlicgv
      181 gpdtlasyrt atgarvelrh sekcgaswar iwatevgdrv dvsaggpths vrirdkddaa
      241 tfvytemtev hpgstvracf rpastggere cfearvgaat ttpapsspe
//
LOCUS       WP_392101295             707 aa            linear   BCT 20-JAN-2025
DEFINITION  DNA gyrase/topoisomerase IV subunit B [Streptomyces sp.
            NPDC015237].
ACCESSION   WP_392101295
VERSION     WP_392101295.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015237
  ORGANISM  Streptomyces sp. NPDC015237
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Tari,L.W., Trzoss,M., Bensen,D.C., Li,X., Chen,Z., Lam,T.,
            Zhang,J., Creighton,C.J., Cunningham,M.L., Kwan,B., Stidham,M.,
            Shaw,K.J., Lightstone,F.C., Wong,S.E., Nguyen,T.B., Nix,J. and
            Finn,J.
  TITLE     Pyrrolopyrimidine inhibitors of DNA gyrase B (GyrB) and
            topoisomerase IV (ParE). Part I: Structure guided discovery and
            optimization of dual targeting agents with potent, broad-spectrum
            enzymatic activity
  JOURNAL   Bioorg Med Chem Lett 23 (5), 1529-1536 (2013)
   PUBMED   23352267
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Gadelle,D., Filee,J., Buhler,C. and Forterre,P.
  TITLE     Phylogenomics of type II DNA topoisomerases
  JOURNAL   Bioessays 25 (3), 232-242 (2003)
   PUBMED   12596227
REFERENCE   3  (residues 1 to 707)
  AUTHORS   Wang,J.C.
  TITLE     Cellular roles of DNA topoisomerases: a molecular perspective
  JOURNAL   Nat Rev Mol Cell Biol 3 (6), 430-440 (2002)
   PUBMED   12042765
REFERENCE   4  (residues 1 to 707)
  AUTHORS   Champoux,J.J.
  TITLE     DNA topoisomerases: structure, function, and mechanism
  JOURNAL   Annu Rev Biochem 70, 369-413 (2001)
   PUBMED   11395412
REFERENCE   5  (residues 1 to 707)
  AUTHORS   Roca,J.
  TITLE     The mechanisms of DNA topoisomerases
  JOURNAL   Trends Biochem Sci 20 (4), 156-160 (1995)
   PUBMED   7770916
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Streptomyces sp. NPDC015237"
                     /db_xref="taxon:3364949"
     Protein         1..707
                     /product="DNA gyrase/topoisomerase IV subunit B"
                     /EC_number="5.6.2.2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003918 - DNA topoisomerase type II
                     (double strand cut, ATP-hydrolyzing) activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006265 - DNA topological change [Evidence
                     IEA]"
                     /calculated_mol_wt=77310
     Region          21..701
                     /region_name="GyrB"
                     /note="DNA gyrase/topoisomerase IV, subunit B
                     [Replication, recombination and repair]; COG0187"
                     /db_xref="CDD:439957"
ORIGIN      
        1 mtaetsvpst allagadrdg snytarhllv legleavrkr pgmyigstds rglmhclwei
       61 idnsvdealg dhcdhievil hddgsvevrd ngrgipvdve pktglsgvev vmtklhaggk
      121 fgggsyaasg glhgvgasvv nalsarldie vdrdghthai sfrrgvpgaf agagadarfe
      181 aknglrkakk ipksrsgtrv rywadrqifl kdaklsldtl hqrarqtafl vpgltivvrd
      241 elglgdggsk geesfrfdgg isefceflas drpvcdvlrf sgqgsfketv pvldehgqmt
      301 ptevtrdlgv dvamrwgtgy dttlrsfvni iatpkggthv agfeqavtrt mnevlrtkkm
      361 lrvaeddvvk ddalegltav vtvrlaepqf egqtkevlgt saarrivnnv itkelkaflt
      421 stkrdaaqqa rvvmekavaa artriaarqh kdaqrrktal essslpakla dcrsddvdrs
      481 elfivegdsa lgtaklarns efqallpirg kilnvqkssv tdmlknaecg aiiqvigags
      541 grtfdidaar ygkiimmtda dvdgshirtl lltlfhrymr pmveagrvfa avpplhriel
      601 vqpkkgqdky vytysdrelr drlmefqgkn irykdsiqry kglgemdadq laettmdprr
      661 rtlrrinltd lesaeqvfdl lmgndvaprk efisnsaatl drsrida
//
LOCUS       WP_392102147             311 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Streptomyces sp. NPDC015237].
ACCESSION   WP_392102147
VERSION     WP_392102147.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015237
  ORGANISM  Streptomyces sp. NPDC015237
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Streptomyces sp. NPDC015237"
                     /db_xref="taxon:3364949"
     Protein         1..311
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32750
     Region          9..309
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 msgaaveptr pdrlapgarv avvapsgpvp eerlqagldv lrgwdldpvv aphvldrhst
       61 fdylagtdtd raadlqaawc dpsvdavlca rggygvqrma dlldweamra agpkvfvgfs
      121 ditalheafa trlglvtlhg pmaagvdfik naraqehlra slfapdtvrv iasggspmvp
      181 grargvtlgg clallaaelg spharpsarg gllcledvge etyridrylt qllragwldg
      241 vagvllgswq ecepyerlrp lladrlgglg vpvvehfgfg hcegaltvpf gvtaeldada
      301 gtltlerpal r
//
LOCUS       WP_392103998             236 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator, partial [Streptomyces
            olivaceus].
ACCESSION   WP_392103998
VERSION     WP_392103998.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces olivaceus
  ORGANISM  Streptomyces olivaceus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Streptomyces olivaceus"
                     /db_xref="taxon:47716"
     Protein         1..>236
                     /product="AfsR/SARP family transcriptional regulator"
                     /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]"
     Region          1..236
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mkiqvlgpls aevnggsivp tagkprqils llalypgrvm pvpmlmeeiw gteppqsalt
       61 tlqtyilqlr rrlgtamgpd apgaakevla trhggylmqi passvdvhey ermvtegraa
      121 feagdddasa ghfraaldlw rgpalvdvrl gpileievmr leesrlgtve rridadlrlg
      181 rhseliaelt eltarypqhe glhsqamval yrsgrqasal diyrklrvrl ieelgv
//
LOCUS       WP_392104309             594 aa            linear   BCT 20-JAN-2025
DEFINITION  caspase family protein [Streptomyces sp. NPDC015237].
ACCESSION   WP_392104309
VERSION     WP_392104309.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015237
  ORGANISM  Streptomyces sp. NPDC015237
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Van Opdenbosch,N. and Lamkanfi,M.
  TITLE     Caspases in Cell Death, Inflammation, and Disease
  JOURNAL   Immunity 50 (6), 1352-1364 (2019)
   PUBMED   31216460
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Tsiatsiani,L., Van Breusegem,F., Gallois,P., Zavialov,A., Lam,E.
            and Bozhkov,P.V.
  TITLE     Metacaspases
  JOURNAL   Cell Death Differ 18 (8), 1279-1288 (2011)
   PUBMED   21597462
REFERENCE   3  (residues 1 to 594)
  AUTHORS   Zhang,J.H., Zhang,Y. and Herman,B.
  TITLE     Caspases, apoptosis and aging
  JOURNAL   Ageing Res Rev 2 (4), 357-366 (2003)
   PUBMED   14522240
REFERENCE   4  (residues 1 to 594)
  AUTHORS   Salvesen,G.S.
  TITLE     Caspases and apoptosis
  JOURNAL   Essays Biochem 38, 9-19 (2002)
   PUBMED   12463158
REFERENCE   5  (residues 1 to 594)
  AUTHORS   Villa,P., Kaufmann,S.H. and Earnshaw,W.C.
  TITLE     Caspases and caspase inhibitors
  JOURNAL   Trends Biochem Sci 22 (10), 388-393 (1997)
   PUBMED   9357314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Streptomyces sp. NPDC015237"
                     /db_xref="taxon:3364949"
     Protein         1..594
                     /product="caspase family protein"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=64095
     Region          5..235
                     /region_name="COG4249"
                     /note="Uncharacterized conserved protein, contains caspase
                     domain [General function prediction only]"
                     /db_xref="CDD:443391"
ORIGIN      
        1 mtslpdpaas ravligveqy teplqplptv annlaglkdv ltgpdswrlp pehctvlsnp
       61 esatqvldav haaateatda lfvyfaghgl lspvgdlyla lsdsppgrlf havaydqlry
      121 qvaeecaals rvvvldccys gralhgymga pleladcgdi dgtyvltasa etkramapkg
      181 ehytafsgal lravtegvph gpdmldmetv yrhvrrelqa rkrpvpqqra rneghritla
      241 rnrwspaagp eaqeyaaalr kavrdgdnaa dpdtapylrg ervaprafvd aladrlpetg
      301 ltrlhdlrrt aqraapdaat qlqywqeeve lltdrltrag dysrdiegel traqervrql
      361 dvevrvlnrq vrllldekgr dtttaealvg aaatqseaag saerggvppr tpaergapgt
      421 apaprppapv artswtlavl avlyvviawa ftldtvalty dsgrkpasmp stsdlpsgeg
      481 phyvwdvetd vtstfrpden daadkltgdl vvsvprpced rtieweitid gregdrgsla
      541 gdtehqvplg iplngspdrv tisaswaggt escpsfglvw tdprlavdld lvpw
//
LOCUS       WP_392104406             241 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: metallophosphoesterase family protein [unclassified
            Streptomyces].
ACCESSION   WP_392104406
VERSION     WP_392104406.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 241)
  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 241)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..241
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25218
     Region          3..231
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 mirvaavgdi hmgpdsqgll rpafetlpdc adllllagdl trhgtpeear vvaeevrglp
       61 vpvvavlgnh dhhderpdkv aallrdagvt vlegegvvve cagtrvgiag akgfcggfvg
      121 rsagefgepl mkefvrttrr sadslrsale elagrdcavr ialthfspva dtlageppei
      181 ypflgsylla eaidtagadl avhghahlgt ehgmtaggvr vrnvaqpvir rafnvyqlna
      241 a
//
LOCUS       WP_392104767             307 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Streptomyces eurythermus].
ACCESSION   WP_392104767
VERSION     WP_392104767.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces eurythermus
  ORGANISM  Streptomyces eurythermus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces eurythermus"
                     /db_xref="taxon:42237"
     Protein         1..307
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32062
     Region          4..305
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mkelvrphrl apgariavva tsgpvpeerl qagldvlrgw dldpvagpht ldrhpgfgyl
       61 agtdadraad fqnawcdpav davlcarggy gaqrmidlld wdalraagpk lfigfsdvta
      121 lheaiaarlg lvtlhgpvaa gadfiknqra qehlratlfa petvrtlafg gtalvpgrar
      181 gvtlggclsl laaelgtpha rpsargglvc ledvgepayr ldrcltqllr agwldgargv
      241 llgswedcag qeelralfad rlgglgtpva envgfghceg altvplgvaa tldtevgtlt
      301 ldepalr
//
LOCUS       WP_392105731             429 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces eurythermus].
ACCESSION   WP_392105731
VERSION     WP_392105731.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces eurythermus
  ORGANISM  Streptomyces eurythermus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 429)
  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 429)
  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
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 429)
  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   5  (residues 1 to 429)
  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   6  (residues 1 to 429)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 429)
  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 20170230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Streptomyces eurythermus"
                     /db_xref="taxon:42237"
     Protein         1..429
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45185
     Region          <20..>60
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          86..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 magrngrtvr dlrrgnrtav lqrlyfdgpl srfelgpatg lssgsvsnvv adliadglve
       61 eagsvdsdgg rprtllrvap hsgqmigvdv getrvrvelf dlaltelarv erpltpqgyd
      121 vdviaghird gvaevltaeq aapdrllgvg vgvpgiveht pdqgavvhgq tigwdavple
      181 rllrsasplp dgvpylidng aktlgqaemw fgagrgarna vvvlfgsgvg aclvtpeveh
      241 gravewghlt vrvrgrrcrc gapgcleaya gaesllarwr eeggrppedt deetaltaml
      301 aaayppegta pdpvalavle etaeylgagl sdlinlfqpe riliggwagl qlgtrflpav
      361 rrhaatyalr hpgdqvtidl grlgpdavtv gaailpladf fagggrrpep agrtplptwh
      421 talqeraph
//
LOCUS       WP_392105749             213 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces eurythermus].
ACCESSION   WP_392105749
VERSION     WP_392105749.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces eurythermus
  ORGANISM  Streptomyces eurythermus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Streptomyces eurythermus"
                     /db_xref="taxon:42237"
     Protein         1..213
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23174
     Region          2..213
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 mnsrerilgr vrraladvtp derpyeqtvs rdylrahger taeetvella enladyraiv
       61 hrtdaeelpt lvmrllaehg srevlvppgl peewlaatda vrvadgpadt agrldrvdsv
      121 vtgcavaiae tgtlvldgsp dqgrrrisli pdhhicvvrv peqvvssvpq alerldparp
      181 ltwisgpsat sdieldrveg vhgprtlevv llg
//
LOCUS       WP_392106534             327 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces paradoxus].
ACCESSION   WP_392106534
VERSION     WP_392106534.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces paradoxus
  ORGANISM  Streptomyces paradoxus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces paradoxus"
                     /db_xref="taxon:66375"
     Protein         1..327
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33724
     Region          53..321
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mtavqlpelr qgrlprrvpv rrlrqifcll plllvtvvav qhrsvlaagf ahlrtaewpw
       61 llaaagatcl twvaasctrq gavverlprr rllatqfaag aanhllptgl gasavnlrfm
      121 tvcglplars saalglylla esigrvallg alliafpdal rlgtlvpeta fgpllagvav
      181 vlviaaavlv lvrrlrsalv sflrtalgea rsvhtrpara lalwggsfaf palqasvlvl
      241 tgralgldip pahmavayla atvavalvpt pggigsveaa lvvalvaagg paavatavvl
      301 afrvitvwlp lvpgaltlaa lvrlkvi
//
LOCUS       WP_392107610             239 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease H family protein [Streptomyces eurythermus].
ACCESSION   WP_392107610
VERSION     WP_392107610.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces eurythermus
  ORGANISM  Streptomyces eurythermus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 239)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Streptomyces eurythermus"
                     /db_xref="taxon:42237"
     Protein         1..239
                     /product="ribonuclease H family protein"
                     /EC_number="3.1.26.4"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=25069
     Region          8..150
                     /region_name="RNase_HI_prokaryote_like"
                     /note="RNase HI family found mainly in prokaryotes;
                     cd09278"
                     /db_xref="CDD:260010"
     Site            order(14..17,50..52,55,77,127,147)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260010"
ORIGIN      
        1 miermrervv aacdgaskgn pgpagwawvv sdgdertpar waagplgrat nnvaeltale
       61 rllaavdpdv pleirmdsqy amkavttwlp gwkrngwkta agkpvanqdl vvridellgg
      121 rsvefryvpa hqvdgdplnd fadraasqaa svqesagsel gspepppspd tpasagaprr
      181 kaprragaga sssstssssr tikakfpgrc lcgrsyaage kiaknaqgwg hpecrtaea
//
LOCUS       WP_392107985             273 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            paradoxus].
ACCESSION   WP_392107985
VERSION     WP_392107985.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces paradoxus
  ORGANISM  Streptomyces paradoxus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 273)
  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 273)
  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 273)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Streptomyces paradoxus"
                     /db_xref="taxon:66375"
     Protein         1..273
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30499
     Region          14..68
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          86..263
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mderrmlrtp rqkygeemrl rrtaarltqe elgdqvvcsp tlishfeagr rlpkpddaqr
       61 idralgtdgf farwledles rytdhfaava eleqlatqvq qfalslvpgv lqtdgyaral
      121 fgayrpnhtp eeldelvvir tqrrrildgp eqpvvwtlld eavlrrrvgg prvmaeqlhk
      181 vanmaesgrl rlhvlpygvg ahalmqsllt lmtfedsapv ayvegfqtgn lmdepalvsa
      241 cqtayalals dalsqqesla lvraaaeeha hde
//
LOCUS       WP_392108548             263 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces sp.
            NPDC015242].
ACCESSION   WP_392108548
VERSION     WP_392108548.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015242
  ORGANISM  Streptomyces sp. NPDC015242
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Streptomyces sp. NPDC015242"
                     /db_xref="taxon:3364951"
     Protein         1..263
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=28546
     Region          1..252
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mltwrtlgpl rathdgrdvt ptapkvrqvl alllarrntv vplaaiaeel wsgqaprsav
       61 ttvqtyayql rkalhegqep dspdggpltt hahgyllrvg pgecdaeeft sltgeartal
      121 acgdpataet ltgraldlcd gppfadvahg pllrgyalrm gelhlqaqel rvtaglqlgr
      181 hrelvgdlke lacayplhew fqgsliialq rcgrrseale vyqrlrvvlr delgldpspg
      241 lqqlrqhvlt drvstadldl lpg
//
LOCUS       WP_392108637             315 aa            linear   BCT 20-JAN-2025
DEFINITION  quinone oxidoreductase family protein [Streptomyces sp.
            NPDC015242].
ACCESSION   WP_392108637
VERSION     WP_392108637.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015242
  ORGANISM  Streptomyces sp. NPDC015242
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 315)
  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 315)
  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 315)
  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   4  (residues 1 to 315)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Streptomyces sp. NPDC015242"
                     /db_xref="taxon:3364951"
     Protein         1..315
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=32455
     Region          1..315
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 mravrfhawg dapvldevpe pvrapgevlv qvtaggvshl datvatggfe fkpvlpyvgg
       61 vegagtvlea daesgltpgt qvvlrggglg llrdgtwaer vsvkrksvtp laapldpsva
      121 asffvpatta yvalhdiarl gpdedvvvvg aagavgamva qqalaagarv tgvvgrqdql
      181 advpkraqav tlddahglar drsasllvdt lggaglpgrs rwvrpggrav vigyvagprv
      241 eldlpswlld evallpvnmi rqerrarevs ddlvrqlsag eltlaverfg ladaaaaldv
      301 lrtgrvrgra vllpg
//
LOCUS       WP_392108700             452 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces paradoxus].
ACCESSION   WP_392108700
VERSION     WP_392108700.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces paradoxus
  ORGANISM  Streptomyces paradoxus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 452)
  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 452)
  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
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 452)
  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   5  (residues 1 to 452)
  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   6  (residues 1 to 452)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 452)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 452)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Streptomyces paradoxus"
                     /db_xref="taxon:66375"
     Protein         1..452
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44070
     Region          27..>101
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          94..425
                     /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 mhgaggagtt gpvgpggvgv nllalrshna alvldllrta gdegisrlel aertgltpqa
       61 vskitarlre dglaaeagrr astggkprtv lrlvpeagha vgvhldrdev ravlvdlrgt
      121 vvgerraaln lgagaeavlg avretvtgvt aaagggrlsr lgevrlggag glgvaepgga
      181 arlggagsgg aartgaagvd eaarqgtaeg dgssrqgaar lvgtsrqrsa plgpallgvg
      241 valpgpldha rgvlhrvtgf pewdgfplre alaerlgvpv vvdkdtnaaa vglaaggesg
      301 sfaylhlgtg lgaglviggs phrgartgag efghqviqld gppctcgnrg cvealclgav
      361 argdlreaar vlgagaanlv glldidvvll ggrtvaaape aftdgvgavl eawarrtgqd
      421 avpvrvatgg ggavavgaae lvlgpvfgrg gv
//
LOCUS       WP_392108816             304 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            eurythermus].
ACCESSION   WP_392108816
VERSION     WP_392108816.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces eurythermus
  ORGANISM  Streptomyces eurythermus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptomyces eurythermus"
                     /db_xref="taxon:42237"
     Protein         1..304
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34614
     Region          17..71
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          93..271
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mvrrkdidgs vsvlnlygke lrwkreaagl sleklvegsf fgksllsdie rgqrrmpldl
       61 arhvdrvlgt dgfferhced vrkarkdgha eyfsdvlele eqaleieewn prlipgplql
      121 epyiraiila ayptepeesl aakiagrrsr awlfedkdsp enwvilhesv lwepilppge
      181 maeqlahlve vlrkrrtftq lvlrnagahp fltsparfmt fadappvmyt enmysgqlid
      241 dpllvkqysk aygrlratal dtetslrlie rtaecyrdgk qpleaaghfp atawtpfita
      301 lksr
//
LOCUS       WP_392109192             237 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Streptomyces paradoxus].
ACCESSION   WP_392109192
VERSION     WP_392109192.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces paradoxus
  ORGANISM  Streptomyces paradoxus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 237)
  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 11440233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Streptomyces paradoxus"
                     /db_xref="taxon:66375"
     Protein         1..237
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25832
     Region          3..230
                     /region_name="GCD1"
                     /note="NDP-sugar pyrophosphorylase, includes eIF-2Bgamma,
                     eIF-2Bepsilon, and LPS biosynthesis protein s
                     [Translation, ribosomal structure and biogenesis, Cell
                     wall/membrane/envelope biogenesis]; COG1208"
                     /db_xref="CDD:440821"
ORIGIN      
        1 mhavilaggk gvrlrpytta lpkplvpigd qhaileivlr qlstagfttc tiaighlgei
       61 irayvgdgsr wglavdyate dsplgtmgpl lnlrhrlpet flvmngdvlt dldyadvlrr
      121 hrasgaplti atyarkvhid fgvlttdssk vvaftekpsm dyrvsmgvyg lsratldgyt
      181 aglplgfdel vldllktqnq phayefdgyw ldigrpddyd ranaefttrk slllkga
//
LOCUS       WP_392109550             314 aa            linear   BCT 20-JAN-2025
DEFINITION  aldo/keto reductase [Streptomyces eurythermus].
ACCESSION   WP_392109550
VERSION     WP_392109550.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces eurythermus
  ORGANISM  Streptomyces eurythermus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  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 314)
  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   3  (residues 1 to 314)
  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   4  (residues 1 to 314)
  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 10790928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces eurythermus"
                     /db_xref="taxon:42237"
     Protein         1..314
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /calculated_mol_wt=34329
     Region          3..314
                     /region_name="YdhF"
                     /note="Predicted oxidoreductase YdhF [General function
                     prediction only]; COG4989"
                     /db_xref="CDD:444013"
ORIGIN      
        1 maartdirah kllygcmglg ggwdtepyta ddirhaerai eaalsagita fdhadiykyg
       61 kseavfgevl arspglrqri vvqtkcgirl pegdrpglyd lrgagivrrv eeslarlrtd
      121 vldvlllhrp dpltepgeia aaltslhaqg lvrqfgvsnm sgpqiaalqa rtdlplvvnq
      181 lemslarrdw veagvlfntp dathngfapg tlewcaangv rlqawgplar grftsgtdtr
      241 asrlvaelar rkdttpetil lwwlrrhpag iapvigttrp erigacadaa rrepdlthee
      301 wyelwttard aplp
//
LOCUS       WP_392110105             284 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015242].
ACCESSION   WP_392110105
VERSION     WP_392110105.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015242
  ORGANISM  Streptomyces sp. NPDC015242
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 284)
  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 284)
  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 16111081
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces sp. NPDC015242"
                     /db_xref="taxon:3364951"
     Protein         1..284
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32162
     Region          20..71
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(22,26,51)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(25,50)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(32..33,44,47,51..52)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          93..272
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mgqrkdidgs tgvptfygse lrwkreeagl tlqqlvegsf ygpshlseie rgtrrmpael
       61 aehvdrvlgt dgffrrrced vrrakrrgha syfervleae qhaksieewc ptlipgllqt
      121 dayaralvqa amplaqeeev eekvsarlar arlfednhkt pmywailsev mlrqpvlppq
      181 qtaeqlehia alarrrrivp qvlpwncgph plmmgmakvm tfvdapplvy lesqhsgdti
      241 ddpalveeyr rsydllraaa lppeaslali qqtaedvrng kqrd
//
LOCUS       WP_392110905             316 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015242].
ACCESSION   WP_392110905
VERSION     WP_392110905.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015242
  ORGANISM  Streptomyces sp. NPDC015242
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 316)
  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 316)
  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 316)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Streptomyces sp. NPDC015242"
                     /db_xref="taxon:3364951"
     Protein         1..316
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35669
     Region          15..69
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          94..269
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 msrrnggaes gastaavfge vlrhfreaal ltqeglarqi pcdrshvarv eagtrvpqds
       61 faktcdella tggvlarlwa ridwyprveh pdwfrrraem deeavalrey qervmpgllq
      121 tadyaralfs llvsgeevee rvrarlsrqq rfladggply ivvldesclr nmigsaavmr
      181 dqcahlldvg krpnirvqva pagclglfrp sgsmslirlp dghewvyses ldqghfndnp
      241 aliarhshty dvlradalsa sqsaaliret meryeqhgpe pahlgqeqlq rrqrrqlhrn
      301 sprfprnrpr arqqep
//
LOCUS       WP_392110988             329 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015242].
ACCESSION   WP_392110988
VERSION     WP_392110988.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015242
  ORGANISM  Streptomyces sp. NPDC015242
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 329)
  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 329)
  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 329)
  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 10611723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Streptomyces sp. NPDC015242"
                     /db_xref="taxon:3364951"
     Protein         1..329
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34134
     Region          15..71
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(21,25,50)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(24,49)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(31..32,43,46,50..51)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          220..301
                     /region_name="DUF2690"
                     /note="Protein of unknown function (DUF2690); pfam10901"
                     /db_xref="CDD:402475"
ORIGIN      
        1 mtptppaglp perarlvcrm relrdgtgls laalaaktaf skssweryln gktlppgqav
       61 relcrlagep egrclalwel aesewsgraa arppgteapr aarppespsp prarsprsps
      121 ppapsprsps pqppppspps plpstpppst repgvrpafl vrgrraggrg rfmavlaalc
      181 alaagglsva lvllagqste prpvpaspsv paprcrgaac egsspmlmkc gtaprtlash
      241 rtstgahlel rysaacgagw armwstrigd rleldgpggg rphsaeirdg laaqsyvytp
      301 mtaarpgtkl racfrpvtga ggecfeagv
//
LOCUS       WP_392111097             347 aa            linear   BCT 20-JAN-2025
DEFINITION  BMP family lipoprotein [Streptomyces paradoxus].
ACCESSION   WP_392111097
VERSION     WP_392111097.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces paradoxus
  ORGANISM  Streptomyces paradoxus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Yousief,S.W., Bahey-El-Din,M. and Zaghloul,T.I.
  TITLE     Immunization with the basic membrane protein (BMP) family ABC
            transporter elicits protection against Enterococcus faecium in a
            murine infection model
  JOURNAL   Microbes Infect 22 (3), 127-136 (2020)
   PUBMED   31585177
REFERENCE   2  (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   3  (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   4  (residues 1 to 347)
  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   5  (residues 1 to 347)
  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 11448319
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Streptomyces paradoxus"
                     /db_xref="taxon:66375"
     Protein         1..347
                     /product="BMP family lipoprotein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /calculated_mol_wt=35763
     Region          41..345
                     /region_name="Med"
                     /note="Lipoprotein Med, regulator of KinD/Spo0A, PBP1-ABC
                     superfamily, includes NupN [Signal transduction
                     mechanisms]; COG1744"
                     /db_xref="CDD:441350"
ORIGIN      
        1 mrriskltrv avgvaslglv atacggtssd sgdsdsserg vaiaydvggq gdqsfndaay
       61 agltkakdef gyktadiept egetdadkeq rlaslakqgy npvigvgfay apameamask
      121 ypdttfgivd avvegknvas lvfaeeqasy lagvaaakat ksdvvgfvgg vdnplihkfe
      181 agyrqgvedt kpgvevlsqy ltqtaeeggf sspdkgkaaa egqiekkadv lyaaaglsgq
      241 gvieaaakak vwaigvdsdq ykqaalapyk nyiltsalkd vggavyalsk svqddkpltg
      301 vktfdlkvng vglsesnpef akvaglkeav ekakqgiddg sikvkte
//
LOCUS       WP_392112084             404 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces eurythermus].
ACCESSION   WP_392112084
VERSION     WP_392112084.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces eurythermus
  ORGANISM  Streptomyces eurythermus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 404)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Streptomyces eurythermus"
                     /db_xref="taxon:42237"
     Protein         1..404
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=42179
     Region          59..240
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          246..374
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mttpdiaarr alvacaalmv galtltacgg dasakndgkg gdspktsaak iaisakdgst
       61 gasinatgvk vsdgkltevk mtvagsgqav pgaisadght wkperrlerg tkyeinatak
      121 dsegrtaaan sifttvspan sfigtytpdd gatvgvgmpv sftfdksitd kkavqshitv
      181 ntssgqqvvg hwfgdrrldf rpqeywkags kvtmnidldg vqgaqgvygv qkktvsftvg
      241 rsqvstvdvn tqtmtvvrdg qtiksvpisa gspehttyng qmvvsekftq trmngstvgf
      301 ggeydipdvp hamrlttsgt fihgnywynk gnppfgrtgt shgcvgladv qgaqgdtsak
      361 wfydntligd vvivknspdt tvapdnglng wnmqwsawta gsav
//
LOCUS       WP_392113518             417 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces paradoxus].
ACCESSION   WP_392113518
VERSION     WP_392113518.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces paradoxus
  ORGANISM  Streptomyces paradoxus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 417)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Streptomyces paradoxus"
                     /db_xref="taxon:66375"
     Protein         1..417
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=44442
     Region          57..242
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          250..365
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mshtaifrpr tvvgctllvi alcagvtacg sdgnplaarp ydaadqvsfn apsegrkkad
       61 pdkpleived sdgritdvta hdasgryvag elaadgsrwh stsplaanas ytvrvstede
      121 dgapgrkvvt fdtgkpttkk slnvtfgpka gtygvgqpvt aelsqpvkdk aqravveral
      181 kvsstpstdg awhwvddkkl hyrpkdywpa qatvqvrsnl qgikigdrmw ggkakpltft
      241 tgdklvavtd aaahqmtvyk ndevvrqipv ttgmpgydtr ngvkvvlake gtvrmtsasi
      301 gasdfydlmv hhsvrvtnsg eyvhaapwsv gsqgfanvsh gctgmstena awfydtvreg
      361 divkvvnsgg dmmapfgngf gdwnldwakw rtgsallggt pdgpteadra rlrpqsv
//
LOCUS       WP_392113569             265 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Streptomyces paradoxus].
ACCESSION   WP_392113569
VERSION     WP_392113569.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces paradoxus
  ORGANISM  Streptomyces paradoxus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 265)
  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 265)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptomyces paradoxus"
                     /db_xref="taxon:66375"
     Protein         1..265
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29187
     Region          12..255
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 maptpagnhr trvhvisdvh gnardlarag egadalvclg dlvlfldyad hsrgifpdlf
       61 gvenadrlva lrtarrfeea rvlgaelwag lqedratvie eavrkqyaem faafpsptya
      121 tygnvdmppl wreyagpgtt vldgeraeig grvfgfvggg lrtpmrtpye isdeeyaaki
      181 eavgevdvlc thippevpel vydtvarrfe rgsralldai rrtrpryslf ghvhqplvkr
      241 mrigatecvn vghfaatgtp walew
//
LOCUS       WP_392114053             263 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces sp.
            NPDC015242].
ACCESSION   WP_392114053
VERSION     WP_392114053.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015242
  ORGANISM  Streptomyces sp. NPDC015242
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616714
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Streptomyces sp. NPDC015242"
                     /db_xref="taxon:3364951"
     Protein         1..263
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26813
     Region          14..240
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 mtesprrptp vtafaalhhg deplllpnaw dfasarafag qgfravatts lgvaavaglp
       61 dgaaatreet lrlalalgsq plllsvdaeg gfsddpdeva rfaaelyavg vvginledgl
      121 gpperlaaki tavkravpal fvnartdthw lgdgdtadtl arldayqaag adgvfvpglt
      181 dlrritvlar cldvplnvly aptgppvrql adagarrisl gsllyrtalg aaleavadvr
      241 agrapggaap sygdvagllp ppg
//
LOCUS       WP_392114122             306 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Streptomyces eurythermus].
ACCESSION   WP_392114122
VERSION     WP_392114122.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces eurythermus
  ORGANISM  Streptomyces eurythermus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Streptomyces eurythermus"
                     /db_xref="taxon:42237"
     Protein         1..306
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32768
     Region          1..300
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mtgrlmlldt aslyfrayfg vpdsvrapdg tpvnavrgll dfidrlvkdh rpdhlvacmd
       61 adwrprwrvd liptykahrv aeehtgapda eevpdtlapq vpvieevlda igiarvgvae
      121 yeaddvigtf tarargpvdi vtgdrdlyql vddergvrvl yplkgvgtlq vtdeavlrek
      181 ygvdgrgyad lallrgdpsd glpgvagige ktaakllaef gdlagimaav ddpgakltps
      241 qrkrltearp ylavapkvvr vaddvplpev gtalpdaprd paalaglarr wglggslerl
      301 lttlts
//
LOCUS       WP_392114623             541 aa            linear   BCT 20-JAN-2025
DEFINITION  peptide ABC transporter substrate-binding protein [Streptomyces
            eurythermus].
ACCESSION   WP_392114623
VERSION     WP_392114623.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces eurythermus
  ORGANISM  Streptomyces eurythermus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11467924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Streptomyces eurythermus"
                     /db_xref="taxon:42237"
     Protein         1..541
                     /product="peptide 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=59491
     Region          36..536
                     /region_name="OppA"
                     /note="ABC-type oligopeptide transport system, periplasmic
                     component [Amino acid transport and metabolism]; COG4166"
                     /db_xref="CDD:443327"
ORIGIN      
        1 mrrstharra acaaaalala atgcagvgag gnggavlsss wadpqnplep antnevqggk
       61 vldmifrglk rydprtgkar dwlarsietr dsrtftvrlk dgwifsngek vtarsfvdaw
      121 nyganlrnnq knayffgyid gydevhpeng rqradtlrgl kvlddhtftv rlnqkfsgfp
      181 dtlgyaafap lprafftdha awvrkpvgng pytiesytkg aqmylkrwdr ypgpdkarnd
      241 gvtllvytds ntaytdllag nldladdipa aqlknvesdl gerylntpag ilqtlafpyy
      301 dkdwsrpgae kvrtglsmai nrrqitdtif rgtrtpatdw tspvlgaagg ykkglcgrac
      361 dydpgrarel ieegggipgg rltvtynads gshrqwvdav cnsinnalgd dracvgnpvg
      421 tfadfrdqlg ghrmtgpfra gwqmdypliq nflqplyytg assndgawsd eefdrlvdra
      481 naetdparsv slfqraeevv rdhmaaiplw yqngnagyse rlshvalnpf svpvyneirv
      541 g
//
LOCUS       WP_392115253             228 aa            linear   BCT 20-JAN-2025
DEFINITION  4'-phosphopantetheinyl transferase family protein [Streptomyces sp.
            NPDC015242].
ACCESSION   WP_392115253
VERSION     WP_392115253.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015242
  ORGANISM  Streptomyces sp. NPDC015242
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459479
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Streptomyces sp. NPDC015242"
                     /db_xref="taxon:3364951"
     Protein         1..228
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=24307
     Region          18..216
                     /region_name="EntD"
                     /note="4'-phosphopantetheinyl transferase EntD
                     (siderophore biosynthesis) [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2977"
                     /db_xref="CDD:442216"
ORIGIN      
        1 mieellpetv vtveaygyde pdtplypeea alvaravpkr qrefavvrsc arrameklgv
       61 pprpilpger gapgwpagla gsmthcdgfc aaalvragdl aslgidaevh aplpdgvlas
      121 valpgeverl rrlvaehpgv cwdrllfsak eavykawfpl tgkwldfmea dieigphggf
      181 qarllvpgpl vgghrldrfe grwttarglv atavvvphse paagvtps
//
LOCUS       WP_392114896             292 aa            linear   BCT 20-JAN-2025
DEFINITION  S1 family peptidase [Streptomyces eurythermus].
ACCESSION   WP_392114896
VERSION     WP_392114896.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces eurythermus
  ORGANISM  Streptomyces eurythermus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Querino Lima Afonso,M., da Fonseca,N.J. Jr., de Oliveira,L.C.,
            Lobo,F.P. and Bleicher,L.
  TITLE     Coevolved Positions Represent Key Functional Properties in the
            Trypsin-Like Serine Proteases Protein Family
  JOURNAL   J Chem Inf Model 60 (2), 1060-1068 (2020)
   PUBMED   31895561
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Waldner,B.J., Kraml,J., Kahler,U., Spinn,A., Schauperl,M.,
            Podewitz,M., Fuchs,J.E., Cruciani,G. and Liedl,K.R.
  TITLE     Electrostatic recognition in substrate binding to serine proteases
  JOURNAL   J Mol Recognit 31 (10), e2727 (2018)
   PUBMED   29785722
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Pelc,L.A., Chen,Z., Gohara,D.W., Vogt,A.D., Pozzi,N. and Di Cera,E.
  TITLE     Why Ser and not Thr brokers catalysis in the trypsin fold
  JOURNAL   Biochemistry 54 (7), 1457-1464 (2015)
   PUBMED   25664608
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Perona,J.J. and Craik,C.S.
  TITLE     Evolutionary divergence of substrate specificity within the
            chymotrypsin-like serine protease fold
  JOURNAL   J Biol Chem 272 (48), 29987-29990 (1997)
   PUBMED   9374470
REFERENCE   5  (residues 1 to 292)
  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 10595581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptomyces eurythermus"
                     /db_xref="taxon:42237"
     Protein         1..292
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=30020
     Region          79..230
                     /region_name="Trypsin_2"
                     /note="Trypsin-like peptidase domain; pfam13365"
                     /db_xref="CDD:433149"
ORIGIN      
        1 mnkpllaals avatiglgat palaaphspa pqttaphsak aakaakaalt vdfagtvsls
       61 ncsgsvirfp gsadtdpalv ltnghcletg mpsagqvitg qsssrtfgll nsagtkiatl
      121 ranqvvystm tdtdvtiyrt tttyaaikss ygispltvqd thpvagtaik vvsgywkriy
      181 scnidgfvyr lkegdwtfkd svrytsacnt iggtsgspvi dattgkvvav nntgnedgqr
      241 ctvnnpcevd asgnvtvrqg inyaqetyni pacfttgnkl nlsaagctlp kp
//
LOCUS       WP_392115732             290 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Streptomyces eurythermus].
ACCESSION   WP_392115732
VERSION     WP_392115732.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces eurythermus
  ORGANISM  Streptomyces eurythermus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 290)
  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 12830887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces eurythermus"
                     /db_xref="taxon:42237"
     Protein         1..290
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=30943
     Region          88..148
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          178..288
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mritgrpaal lasaaavtaf aalagctvqp qdtdakrglp vhiqlpsspa paptgmagtt
       61 pttpppratt ptpaappapp prvlwahgss gpavrelqar lrqvgwlsat ptgtygprtv
      121 ravlgfqakr glpatgrldt vtwqrllamt hrptrwelyp mggqpaaapd arcmtgrvlc
      181 idktsrtlrw midgrtvdtl svrfgtqytp tregvfkvyw ksrhhvstly hspmpyamff
      241 sggqavhysa dfaargyagg shgcvnvrde aaiarlfaqv kvgdkvvvsr
//
LOCUS       WP_392116282             211 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces sp. NPDC015242].
ACCESSION   WP_392116282
VERSION     WP_392116282.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015242
  ORGANISM  Streptomyces sp. NPDC015242
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Streptomyces sp. NPDC015242"
                     /db_xref="taxon:3364951"
     Protein         1..211
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22389
     Region          2..209
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 mnsrerilgr vrraladapa detpiardyl rehgtrtvae tvellaenla dyraivhrtd
       61 edglagliag llnrrgsasv lvppglderw laatgvtrva draestpgel drvdsvvtac
      121 avaiaetgti vldgspdqgr rritlvpdhh vcvvrvpdqv vssvpqglgr ldparpltwi
      181 sgpsatsdie ldrvegvhgp rtlevvlvgg a
//
LOCUS       WP_392117020             245 aa            linear   BCT 20-JAN-2025
DEFINITION  TerD family protein [Streptomyces paradoxus].
ACCESSION   WP_392117020
VERSION     WP_392117020.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces paradoxus
  ORGANISM  Streptomyces paradoxus
            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 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Streptomyces paradoxus"
                     /db_xref="taxon:66375"
     Protein         1..245
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=27433
     Region          <13..240
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mglfdglrrg reaqfdsgda stnaieltkr raqisltkqg aatghlrvnl swrmrtsdig
       61 gsqresllrh pfralkppev vghsqsmvnv dldlgclyel qdgskgvvqp lggyfgdtna
      121 apyvklsgdd rfgsasgetm yinldhrdsi krllvfvyiy dqtpafdrah aivtlypsng
      181 prieihlder qpqarscavv miekvkneii vrreakfvyg fqaeldrlyg wglqwgrgyk
      241 tkvdr
//
LOCUS       WP_392117632             339 aa            linear   BCT 20-JAN-2025
DEFINITION  quinone oxidoreductase family protein [Streptomyces eurythermus].
ACCESSION   WP_392117632
VERSION     WP_392117632.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces eurythermus
  ORGANISM  Streptomyces eurythermus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 339)
  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   4  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Streptomyces eurythermus"
                     /db_xref="taxon:42237"
     Protein         1..339
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=34739
     Region          1..326
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 mravriheyg gpevlrieev rmpepgpgqv liaaeaisvg faqvqmrrni fpapmwrpef
       61 pvtlggdvig dvvavgpgvt giaigdrvga ftlhgayaey vaveadtvlp vpaaldaaqa
      121 talpapgpia mgtmgtaala pgesvlvhaa sggighlavq larlagagtv iatagtpekc
      181 ayarslgadv avdysraqwp davreatggr gvdvildsvg gevlrqgvgl lapfgrlvfy
      241 gsaggglgip avspmeligm rfltgfalsa wrnarperyl adhdtltarl ltgtvrqtvy
      301 atlpledvak aheivegrah lgrivlltgr gnrtaggaa
//
LOCUS       WP_392117636             258 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            eurythermus].
ACCESSION   WP_392117636
VERSION     WP_392117636.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces eurythermus
  ORGANISM  Streptomyces eurythermus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Streptomyces eurythermus"
                     /db_xref="taxon:42237"
     Protein         1..258
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=28911
     Region          1..249
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mkfhllgpfe ittkdgrsci pptpkasqvl alllsrpkei vpvdafiqel waenpprsal
       61 ttlqtyiyhl rkilvgegla garertlvtr spgylidptg hgldtlefee lvksgrraad
      121 rgfleeaart lgdaldlwtg pvlaniaigr vltgytmyle elrvraverr vealkqlgne
      181 rdlipelral iqqyplnewf haqlidslsn cgrraealkv yrdlwrsldd elgiepspdv
      241 qrlhyevlnp varsgraa
//
LOCUS       WP_392117944             524 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Streptomyces paradoxus].
ACCESSION   WP_392117944
VERSION     WP_392117944.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces paradoxus
  ORGANISM  Streptomyces paradoxus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 524)
  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 524)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Streptomyces paradoxus"
                     /db_xref="taxon:66375"
     Protein         1..524
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55853
     Region          264..430
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 marvpaavls vlkpirnapr alarhyrsrq apatielvaq phpwtravgl lavvllgawl
       61 gllvvgnvrv pvgpmnttmt lrpsftggtk inisplgale lnshiapvrl dvnvdqldpd
      121 rsqalvdhpe rlsglqdevt edvgrgtldl avrsgvavvv gatalglavy rrprramaag
      181 glaltllaas ggtayatwrp dsvlepkfsg lltsapslvg narsivtefd vyqkelarlv
      241 tnvtklydat stlpayapdp stirvlhvsd ihlnpaswki iaslveqykv dvivdsgdtm
      301 dhgtaaengf ldpiedlgap yvwvrgnhds mitqrymqgl rnvhvldegk aktikglrfa
      361 gigdpqftpd rsrqigarqs qelagarlat alrdqsaagt pvdiaiahep aaargvdgev
      421 plvlaghlhh demeilkygt rlriegstgg sglraiegkh pdpieasily fdrdtrhlqa
      481 wdeielgglg lttaevsrhl pkenqpgatp spstpteatp spss
//
LOCUS       WP_392118291             416 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces eurythermus].
ACCESSION   WP_392118291
VERSION     WP_392118291.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces eurythermus
  ORGANISM  Streptomyces eurythermus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Streptomyces eurythermus"
                     /db_xref="taxon:42237"
     Protein         1..416
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=45610
     Region          61..317
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 madrlgpsyl vlnryddefg eyhrfvdpdr crlfyltvpd glgvldtesa wetvvvddle
       61 yetvlpvaqr lvrqygefdg ivglseydlv taarlrdalg vpgwsedfvl gfrdkvrmkh
      121 lvesaglpvp rytdlagpav tadhvvsevg lpvilkprag aasngvlrid dkeslehalq
      181 svergayece eyvageiyhv dgvrrgggfh fvsasvyvnt clefaqglpl gsvlldpgpr
      241 rdetvafaaa cldalalddg pfhlelmrrp sgelvflevg lrpggaevaf ihrdlygidl
      301 mgeafratlg lppltaaeef prhraggwal mpeprplpsr vvgcrpvree ipevyeeivp
      361 avgevfdgtg gyghvggrfr lrgaderavr aavlrimdry hldaepvaar teritt
//
LOCUS       WP_392118562             707 aa            linear   BCT 20-JAN-2025
DEFINITION  DNA gyrase/topoisomerase IV subunit B [Streptomyces eurythermus].
ACCESSION   WP_392118562
VERSION     WP_392118562.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces eurythermus
  ORGANISM  Streptomyces eurythermus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Tari,L.W., Trzoss,M., Bensen,D.C., Li,X., Chen,Z., Lam,T.,
            Zhang,J., Creighton,C.J., Cunningham,M.L., Kwan,B., Stidham,M.,
            Shaw,K.J., Lightstone,F.C., Wong,S.E., Nguyen,T.B., Nix,J. and
            Finn,J.
  TITLE     Pyrrolopyrimidine inhibitors of DNA gyrase B (GyrB) and
            topoisomerase IV (ParE). Part I: Structure guided discovery and
            optimization of dual targeting agents with potent, broad-spectrum
            enzymatic activity
  JOURNAL   Bioorg Med Chem Lett 23 (5), 1529-1536 (2013)
   PUBMED   23352267
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Gadelle,D., Filee,J., Buhler,C. and Forterre,P.
  TITLE     Phylogenomics of type II DNA topoisomerases
  JOURNAL   Bioessays 25 (3), 232-242 (2003)
   PUBMED   12596227
REFERENCE   3  (residues 1 to 707)
  AUTHORS   Wang,J.C.
  TITLE     Cellular roles of DNA topoisomerases: a molecular perspective
  JOURNAL   Nat Rev Mol Cell Biol 3 (6), 430-440 (2002)
   PUBMED   12042765
REFERENCE   4  (residues 1 to 707)
  AUTHORS   Champoux,J.J.
  TITLE     DNA topoisomerases: structure, function, and mechanism
  JOURNAL   Annu Rev Biochem 70, 369-413 (2001)
   PUBMED   11395412
REFERENCE   5  (residues 1 to 707)
  AUTHORS   Roca,J.
  TITLE     The mechanisms of DNA topoisomerases
  JOURNAL   Trends Biochem Sci 20 (4), 156-160 (1995)
   PUBMED   7770916
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Streptomyces eurythermus"
                     /db_xref="taxon:42237"
     Protein         1..707
                     /product="DNA gyrase/topoisomerase IV subunit B"
                     /EC_number="5.6.2.2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003918 - DNA topoisomerase type II
                     (double strand cut, ATP-hydrolyzing) activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006265 - DNA topological change [Evidence
                     IEA]"
                     /calculated_mol_wt=77163
     Region          21..701
                     /region_name="GyrB"
                     /note="DNA gyrase/topoisomerase IV, subunit B
                     [Replication, recombination and repair]; COG0187"
                     /db_xref="CDD:439957"
ORIGIN      
        1 mtaetsvpst allagadrdg snytarhllv legleavrkr pgmyigstds rglmhclwei
       61 idnsvdeala gvcdrievil hddgsvevrd ngrgipvdve prtglsgvev vmtklhaggk
      121 fgggsyaasg glhgvgasvv nalsarldve vdrgghthai sfrrgvpgaf aadgaeakfe
      181 aksglrktkk ipktrtgtrv rywadrqifl kdaklsletl hqrarqtafl vpgltivvrd
      241 efglgeggsk geesfrfdgg isefceylan dkaicdvlrf sgkgtfketv pvldehgqmt
      301 ptevtrelgv dialrwgtgy dttvrsfvni iatpkggthv tgfeqaltqt lndvlrakkl
      361 lrvaednivk ddalegltav vtvrlaepqf egqtkevlgt saarrivnnv vsselkaflt
      421 atkrdaaaqa rvvmekvvaa artrvaarqh kdaqrrktal essslpakla dcrsddvdrs
      481 elfivegdsa lgtaklarns efqallpirg kilnvqrssv tdmlknaecg aiiqvigags
      541 grtfdidqar ygkiimmtda dvdgshircl lltlfqrymr pmveagrvfa avpplhriel
      601 iqpkkgqeky vytysdrelr dklmefqskg irykdtiqry kglgemdadq laettmdprh
      661 rtlrrinlsd leaaeqvfdl lmgndvaprk efisssaatl drsrida
//
LOCUS       WP_392119839             261 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptomyces paradoxus].
ACCESSION   WP_392119839
VERSION     WP_392119839.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces paradoxus
  ORGANISM  Streptomyces paradoxus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 261)
  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 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   3  (residues 1 to 261)
  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   4  (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   5  (residues 1 to 261)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Streptomyces paradoxus"
                     /db_xref="taxon:66375"
     Protein         1..261
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28073
     Region          23..261
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <151..261
                     /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 mpnfvelple lppdlvhagv gvhgsagphe vfrlphlwql hlygysgtle fggarhpirp
       61 ghlslvppgt evhfhydaar cehlyahfrl pgegerrrlp amqdagaeaa vlsallrqti
      121 aacaqspara saelwaalwr ttglaeatet psgsrhpalr aamahieehl adplsvpgia
      181 raagvshthl trlfredtgr tvvgyvrrrr merarhllia stlaipavaa tvgipdlqaf
      241 nktcrkelga spravrqaag a
//
LOCUS       WP_392120016             269 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            eurythermus].
ACCESSION   WP_392120016
VERSION     WP_392120016.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces eurythermus
  ORGANISM  Streptomyces eurythermus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces eurythermus"
                     /db_xref="taxon:42237"
     Protein         1..269
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=29614
     Region          1..254
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 meidvlgplg arvnglsivp tagkprqila llairagrvv svetlieevw gdavprsaap
       61 tlqtyilqlr kkitdalpad seltakdila tsyggyqlap vepircdlve fqrltahgtr
      121 amaehaphva seklreglal wrgnalvdvp lgevlrmevi gmqeartral elrieadlql
      181 grhaeligel rmlvaqqplh enlcaqlmta lyraghpwra levfqslrqs lvdelgveps
      241 prlqrlhrai landdrldrf tpaqrllsa
//
LOCUS       WP_392120753             816 aa            linear   BCT 20-JAN-2025
DEFINITION  GcvT family protein [Streptomyces sp. NPDC015242].
ACCESSION   WP_392120753
VERSION     WP_392120753.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015242
  ORGANISM  Streptomyces sp. NPDC015242
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 816)
  AUTHORS   Stauffer,L.T., Ghrist,A. and Stauffer,G.V.
  TITLE     The Escherichia coli gcvT gene encoding the T-protein of the
            glycine cleavage enzyme system
  JOURNAL   DNA Seq 3 (6), 339-346 (1993)
   PUBMED   8219277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..816
                     /organism="Streptomyces sp. NPDC015242"
                     /db_xref="taxon:3364951"
     Protein         1..816
                     /product="GcvT family protein"
                     /calculated_mol_wt=88894
     Region          20..392
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
     Region          378..433
                     /region_name="FAO_M"
                     /note="FAD dependent oxidoreductase central domain;
                     pfam16350"
                     /db_xref="CDD:465100"
     Region          428..815
                     /region_name="GcvT"
                     /note="Glycine cleavage system protein T
                     (aminomethyltransferase) [Amino acid transport and
                     metabolism]; COG0404"
                     /db_xref="CDD:440173"
ORIGIN      
        1 msstpvnprv vvvgagivgc sladeltarg wtdvtvleqg plpapggsts hapglvfqts
       61 psrtltafar ytvekfgsld vdgvpcfqqv gglelattpe rlaelhrrag yaaswgvrge
      121 vvtaarckel wplidesvvl ggfhtpddgl arallaaraq mmratargar flerhtvtgi
      181 errgglvtav atdrgtfpad hvvsaagfwg pvigrmagvd vplqplahqy artgplpels
      241 gataeaskpi lrfqdrdlyf rehtdrlgig syahrplpvd pfavppydea rardmdmpss
      301 ypftardwap swedcrrlmp alrhagveag fngvfsftpd gmpvlgesrh lrgfwlaeav
      361 wvthsagvar avaewmvdgr psldlhecdl trfeeaqrsp syvlergarq fvevydvihp
      421 lqpmeqprpl rvspfyarqq qlgayflegg gwerphwyea naplvdalgp lperdawsar
      481 hwspvaaaea ratregvaly dmtplrrlev sgpgalafld rmssnnlrkk pgavtytlll
      541 deaggirsdl tvarlapdrf qvganspadh drllrhapgd vvvrditsgt ccvgvwgpla
      601 rdlvqpltpd dfsheafgyf raretyvghv pvtalrlsyv gelgwelytt adlglrlwdt
      661 lweagrelgv vaagrsafns lrlekgyraw gidmtgeddp feagvgfavr mdkegfvgqd
      721 alrgrqepsr rltplllddp aavvlgkepv yaggapsgyv tsasygytlg rcvayawlpa
      781 gltagtgvhi eyfgekvpat vadeplfdpk msrirr
//
LOCUS       WP_392120807             213 aa            linear   BCT 20-JAN-2025
DEFINITION  nicotinamide mononucleotide transporter family protein
            [Streptomyces sp. NPDC015242].
ACCESSION   WP_392120807
VERSION     WP_392120807.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015242
  ORGANISM  Streptomyces sp. NPDC015242
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Hemberger,S., Pedrolli,D.B., Stolz,J., Vogl,C., Lehmann,M. and
            Mack,M.
  TITLE     RibM from Streptomyces davawensis is a riboflavin/roseoflavin
            transporter and may be useful for the optimization of riboflavin
            production strains
  JOURNAL   BMC Biotechnol 11, 119 (2011)
   PUBMED   22136195
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Zhu,N., Olivera,B.M. and Roth,J.R.
  TITLE     Genetic characterization of the pnuC gene, which encodes a
            component of the nicotinamide mononucleotide transport system in
            Salmonella typhimurium
  JOURNAL   J Bacteriol 171 (8), 4402-4409 (1989)
   PUBMED   2546921
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Streptomyces sp. NPDC015242"
                     /db_xref="taxon:3364951"
     Protein         1..213
                     /product="nicotinamide mononucleotide transporter family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0034257 - nicotinamide riboside
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_process="GO:0034258 - nicotinamide riboside transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23465
     Region          8..204
                     /region_name="PnuC"
                     /note="Nicotinamide riboside transporter PnuC [Coenzyme
                     transport and metabolism]; COG3201"
                     /db_xref="CDD:442434"
ORIGIN      
        1 mntlnseaft lfgqhikwad mignlfglaa lalgwrrsiw twpvqflagl ilfgaffghl
       61 tgsagkqavv vivalygwwq wrrgtgqged ghiavrfatw reraamaaaa aagtvavall
      121 ftaypklswd pwpdayifvg tvvamyaqar gmvefwfawl lvdlvgvpln fangyafsgf
      181 vyviygalvl wglrdwwlrs rqaarptleg apa
//
LOCUS       WP_392121320             232 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease H family protein [Streptomyces paradoxus].
ACCESSION   WP_392121320
VERSION     WP_392121320.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces paradoxus
  ORGANISM  Streptomyces paradoxus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 232)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 232)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Streptomyces paradoxus"
                     /db_xref="taxon:66375"
     Protein         1..232
                     /product="ribonuclease H family protein"
                     /EC_number="3.1.26.4"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=24390
     Region          8..149
                     /region_name="RNase_HI_prokaryote_like"
                     /note="RNase HI family found mainly in prokaryotes;
                     cd09278"
                     /db_xref="CDD:260010"
     Site            order(14..17,49..51,54,76,126,146)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260010"
ORIGIN      
        1 miermrervv aacdgaskgn pgpagwawvv adasgtperw eagplgkatn nvaeltaler
       61 llaatdpdvp leirmdsqya mkavttwlpg wkrngwktsa gkpvanrdlv vridellggr
      121 svefryvpah qvdgdrlndf adraasqaat vqepagsglg spepppapdt pakaprsrpr
      181 ttkaagskgs artikakfpg rcqcgrsyaa gepiakndsg wghpecraga gv
//
LOCUS       WP_392121690             213 aa            linear   BCT 20-JAN-2025
DEFINITION  nicotinamide mononucleotide transporter family protein
            [Streptomyces paradoxus].
ACCESSION   WP_392121690
VERSION     WP_392121690.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces paradoxus
  ORGANISM  Streptomyces paradoxus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Hemberger,S., Pedrolli,D.B., Stolz,J., Vogl,C., Lehmann,M. and
            Mack,M.
  TITLE     RibM from Streptomyces davawensis is a riboflavin/roseoflavin
            transporter and may be useful for the optimization of riboflavin
            production strains
  JOURNAL   BMC Biotechnol 11, 119 (2011)
   PUBMED   22136195
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Zhu,N., Olivera,B.M. and Roth,J.R.
  TITLE     Genetic characterization of the pnuC gene, which encodes a
            component of the nicotinamide mononucleotide transport system in
            Salmonella typhimurium
  JOURNAL   J Bacteriol 171 (8), 4402-4409 (1989)
   PUBMED   2546921
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Streptomyces paradoxus"
                     /db_xref="taxon:66375"
     Protein         1..213
                     /product="nicotinamide mononucleotide transporter family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0034257 - nicotinamide riboside
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_process="GO:0034258 - nicotinamide riboside transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23423
     Region          8..204
                     /region_name="PnuC"
                     /note="Nicotinamide riboside transporter PnuC [Coenzyme
                     transport and metabolism]; COG3201"
                     /db_xref="CDD:442434"
ORIGIN      
        1 mnslnseaft lfgqhilwsd mvgnlfglaa lalgwrrsiw twpvqflagl ilfgaffghl
       61 tgsagkqavv vlvavygwwq wqrgkgqgdd ghiavrfatw reraamaaaa aagtvavall
      121 ftaypklswd pwpdayifvg tivamyaqar gmvefwfawl lvdlvgvpln fangyafsgf
      181 vyviygalvl wglrdwwlrs rqaarptleg apa
//
LOCUS       WP_392123255             281 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Streptomyces sp.
            NPDC014940].
ACCESSION   WP_392123255
VERSION     WP_392123255.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014940
  ORGANISM  Streptomyces sp. NPDC014940
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 281)
  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 281)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces sp. NPDC014940"
                     /db_xref="taxon:3364932"
     Protein         1..281
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29120
     Region          1..275
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mlcrsadlma eahasgsgia afnvitlehv qavadaaert grpaivqisq navrhyggdv
       61 mplaaataaa atrgrarlal hldhvedtgl lhrtaecgas svmfdasrlg deeniaatra
      121 aarwahdhgl fveaelgeig gkgsahdpgv rtdpkeaarf vaetgvdala vavgsshamv
      181 srtaqldlel isrirtevav plvlhgssgv phptlraave hgmtkinigt llnvaftrav
      241 revlaegpdl vdprrylapa raamtdtiad cltalappgs p
//
LOCUS       WP_392123637             289 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC014940].
ACCESSION   WP_392123637
VERSION     WP_392123637.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014940
  ORGANISM  Streptomyces sp. NPDC014940
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415139
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces sp. NPDC014940"
                     /db_xref="taxon:3364932"
     Protein         1..289
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=31309
     Region          1..260
                     /region_name="LysX"
                     /note="Glutathione synthase, LysX or RimK-type ligase,
                     ATP-grasp superfamily [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism,
                     Translation, ribosomal structure and biogenesis, Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0189"
                     /db_xref="CDD:439959"
ORIGIN      
        1 mprialatyd pgdrpsrdrd lpvlvdvlre agadaearyw ddpaadwagy dlvlirstwd
       61 yswraaefga wvdrvgaltr lanpaavvrw nsdkrylgel aaagvptvet ryvapgepae
      121 lpgdheyvik ptsgagarfa arytpdrhet avrqlarmha egftamvqpy lrnidvsger
      181 alqffggrll hasrkgavla pgtpydaekv ahpglepwqp tdaelavaek alasvpgapg
      241 llyarvdlvd gedglprvme lelvepnlfl flhpaslprv veailaaag
//
LOCUS       WP_392123960             277 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            flaveolus].
ACCESSION   WP_392123960
VERSION     WP_392123960.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 277)
  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 277)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         1..277
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30698
     Region          1..64
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          87..264
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mangsrqaaw effgtelkrr redagitqae lgarvfvsgg yigqfeqair kpqldvaqri
       61 davlqtdgif erlcrklidd pryadyfaha velerlatri cefaptvvpg llqtkeyaya
      121 vtisanpfks dsyveeivta rlerslildd aarpeywvtl henalrvpvg gphamaaqle
      181 hiarlmrert awvtvlpyma gahaamngsl klmefedapq vaytetsfsg tlvddpavvk
      241 raqraydllr vatlspeasl aliesaaedf rrcastt
//
LOCUS       WP_392124021            1188 aa            linear   BCT 20-JAN-2025
DEFINITION  Rne/Rng family ribonuclease, partial [Streptomyces flaveolus].
ACCESSION   WP_392124021
VERSION     WP_392124021.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1188)
  AUTHORS   Kime,L., Jourdan,S.S. and McDowall,K.J.
  TITLE     Identifying and characterizing substrates of the RNase E/G family
            of enzymes
  JOURNAL   Methods Enzymol 447, 215-241 (2008)
   PUBMED   19161846
REFERENCE   2  (residues 1 to 1188)
  AUTHORS   Callaghan,A.J., Marcaida,M.J., Stead,J.A., McDowall,K.J.,
            Scott,W.G. and Luisi,B.F.
  TITLE     Structure of Escherichia coli RNase E catalytic domain and
            implications for RNA turnover
  JOURNAL   Nature 437 (7062), 1187-1191 (2005)
   PUBMED   16237448
REFERENCE   3  (residues 1 to 1188)
  AUTHORS   Li,Z., Pandit,S. and Deutscher,M.P.
  TITLE     RNase G (CafA protein) and RNase E are both required for the 5'
            maturation of 16S ribosomal RNA
  JOURNAL   EMBO J 18 (10), 2878-2885 (1999)
   PUBMED   10329633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..1188
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         <1..1188
                     /product="Rne/Rng family ribonuclease"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
     Region          417..827
                     /region_name="CafA"
                     /note="Ribonuclease G or E [Translation, ribosomal
                     structure and biogenesis]; COG1530"
                     /db_xref="CDD:441139"
ORIGIN      
        1 rratrrvsap agepaaaepa etttetgaae aaaapetapa tapveeaaed aaprrtrrra
       61 trrvsapage paaaepaett tetgaaeaap aaeatpapea arsaepaapv eeeaaprrar
      121 rrsarkaagg faeparsaaa sdeadapkrp arpavavfqa pvfaepkfqt peraaaeaaa
      181 eaaapepeqa vreteapeef peetagsrrr rrrraagpee ttedrtptra aaeepeadae
      241 aeadepgddh gddaegseey gsrrrrrrgg rrrrrgdlae gsedsadddd aehtaaeqaa
      301 qdaedtaeqa eedaeegeda tgenggssss rrrrrrrrra gdssgdaets addpertvvk
      361 vreprpkaep sdevqsikgs trleakkqrr regreqgrrr vpiiteaefl arreavervm
      421 ivrqhgertq igvledgvlv ehyvnkeqat syvgnvylgk vqnvlpsmea afidigkgrn
      481 avlyagevnf eslgmghgpr riesalksgq svlvqvtkdp ighkgarlts qvslpgrylv
      541 yvpegsmtgi srklpdters rlktilkriv pedagvivrt aaegasedel rrdverlqaq
      601 weeiqkkakn gnaptllyge pdmtvrvvrd ifnedfskvv vsgddawqti hgyvshvapd
      661 ladrlskwts evdvfatyri deqlakaldr kvwlpsggsl vidrteamvv vdvntgkftg
      721 qggnleetvt rnnleaaeei vrqlrlrdlg giividfidm vlesnrdlvl rrlleclgrd
      781 rtkhqvaevt slglvqmtrk rvgqgllesf setcvhcngr gvivhldqps sagggggkrr
      841 kraragageh dheavagvet vptaeqeadt esesevaaev aepvalpaef tpdeelyssa
      901 aeaeaaatrg rgrrrasrra sapagapkaa kgeaarseaq vptaqdvtva eeierpvvqe
      961 taaevlaepa avedalsgap apaadeaapk grtrrratrk vsapagspag aeaavltvpe
     1021 taqaepapqa pavaeapaae eaapaaesaa parprrravr kpttstasee aavvvvpsap
     1081 aeaeapaeae apaepevaea pavdasgdea apakkaaark takkatakka atkktaakkt
     1141 ttakkatakk aaktttakka takktaskkt aaaeqaapss vtaatdeg
//
LOCUS       WP_392124236             245 aa            linear   BCT 20-JAN-2025
DEFINITION  SRPBCC family protein [Streptomyces sp. NPDC014940].
ACCESSION   WP_392124236
VERSION     WP_392124236.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014940
  ORGANISM  Streptomyces sp. NPDC014940
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 245)
  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 10008053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Streptomyces sp. NPDC014940"
                     /db_xref="taxon:3364932"
     Protein         1..245
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=26399
     Region          1..107
                     /region_name="YndB"
                     /note="Chalcone/flavanone-binding protein YndB,
                     AHSA1/START/SRPBCC domain [Lipid transport and
                     metabolism]; COG3832"
                     /db_xref="CDD:443044"
ORIGIN      
        1 mpeefeivre fevgvpperv wgaltigtag ylwpmdppep reggrgpfgs tvtawdpprr
       61 ytirsedvgr pgqsldrldh tvepldegrr arvrhvhsgv ftddwnkryd aaskhtnfyl
      121 htlceylthf aprpaafara egpaasatag alaavghalh laddaaagtg vgargpgght
      181 lhgvldyrsp yfiglrtdsa lvrffgrghw gaplgvsvhd fapgadgraq gaawqdwlng
      241 vfgqs
//
LOCUS       WP_392124340             150 aa            linear   BCT 20-JAN-2025
DEFINITION  SRPBCC family protein [Streptomyces flaveolus].
ACCESSION   WP_392124340
VERSION     WP_392124340.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 150)
  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 10008053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         1..150
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=15792
     Region          7..141
                     /region_name="YndB"
                     /note="Chalcone/flavanone-binding protein YndB,
                     AHSA1/START/SRPBCC domain [Lipid transport and
                     metabolism]; COG3832"
                     /db_xref="CDD:443044"
ORIGIN      
        1 msteqtstad gfsyaltrtl dapvarvwea wttpeayarw ahaapgsvem dvrpggawka
       61 tmltpdggaf pltgsyveva epsrlvlgmd vpgrpdqvtm tlelteqgpa rteivlsqac
      121 dtaeerdmae qgsgmlldgl agylaegarg
//
LOCUS       WP_392124655             261 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC014940].
ACCESSION   WP_392124655
VERSION     WP_392124655.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014940
  ORGANISM  Streptomyces sp. NPDC014940
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   4  (residues 1 to 261)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Streptomyces sp. NPDC014940"
                     /db_xref="taxon:3364932"
     Protein         1..261
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29151
     Region          4..58
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          79..256
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mrmlgrqlat arraaglsqs glsaalnine etiasieqgr rtlkpdiaei lddylgtkgt
       61 laagvanlpe vdqfplwaee ymdqervaia lswydalvvp gllqtksyar allsgrvpay
      121 dadeletkae arvqrrnilh rkepptlsfv iwepalrwpt ggrqvhqeql qfmreyselp
      181 clslqvlpld rahhagdagp ftlletpdhq hlaytesqrg sqwvsdpdev silarkyaml
      241 rtqaltveds rslldrllge q
//
LOCUS       WP_392125518             452 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces flaveolus].
ACCESSION   WP_392125518
VERSION     WP_392125518.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 452)
  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 452)
  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
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 452)
  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   5  (residues 1 to 452)
  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   6  (residues 1 to 452)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 452)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 452)
  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 20170230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         1..452
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=46738
     Region          1..112
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          82..402
                     /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 marasgrtvr dlrrenraav lqrlyfdgpm srvalgsaag lssgsvsnvv aellaeglve
       61 eagslgadgg rprtlvrias ghgrligvdv getrvrvelf dlsmaelart erplpghgtr
      121 sydvgvvagh ildgvaevld aagdgrgsgd llgvgvgvpg ivehtaggal vhgqtigwda
      181 vplerllrgs grlpahvplf idngaktlgq aemwfgggrg ahnavvvlfg sgvgacvvth
      241 dveqgravew ghltvrvrgr rcrcgargcl eayagaeall arwreaggrp psgtddeeta
      301 ltdllraahp pdgrepdpva arvlaetaey lgaglsdlin lfqperilvg gwaglrlgsg
      361 fvdsvrthay ahalrhpagr vgitlgqlgp davtvgaavl plaaffargg hrapvdspaq
      421 ppawrtalgg rlagtgrrag qderpegrah vp
//
LOCUS       WP_392125644             403 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces parvulus].
ACCESSION   WP_392125644
VERSION     WP_392125644.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces parvulus
  ORGANISM  Streptomyces parvulus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  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 403)
  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
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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   5  (residues 1 to 403)
  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   6  (residues 1 to 403)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 403)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces parvulus"
                     /db_xref="taxon:146923"
     Protein         1..403
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41482
     Region          1..>61
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          81..391
                     /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 magtagtpgt prvlramndr aaldlllehg plsrtrigkl tglskptasq llarleaagl
       61 vlaggttegs pgpgaqlyev npaaayaagl dvtpdrvlaa vadvtgrtvg ryelptpgrr
      121 paapvvqqvt daldgavkaa glaradvhrl vigtpgafdp gtgrlryash lpgwhsptll
      181 delaaalpmp veyendvnla avaeqrlgaa rghedfvllw nqeglgaalv lggrlhrgwt
      241 ggagevgflp vpgaplvrkv sragsggfqe lagsqalpal arelgltdlp pgpyheaaaa
      301 lvaraartdd aphrrllqty atrlatglas lvsvldpelv vlsgtalaag getlrdlvrd
      361 eleelaasrp rlvvgdvtdh pvlrgalesa laatrdevfd tsr
//
LOCUS       WP_392125958             336 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces flaveolus].
ACCESSION   WP_392125958
VERSION     WP_392125958.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         1..336
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33654
     Region          62..330
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mtavrlpetp lsgrvptvgh gragldgrar pvrrlvcvlp lllvtvvavr hrsvlaegfg
       61 rlsdaegswl laaagvtclt wvaaactrqg avverlpsgr llatqfaaga anhllptglg
      121 asavnlrfmt vcglplarss aalalyllae sagrlallgg lllafpgalr lgtllpegav
      181 gplllaagtv pvvaagalvl vrrlrtalvs flrtalgear svharparal alwggalafp
      241 alqatalvlv gralglgvpp ghmavaylaa tvavalvptp ggigsveaal vvalvaaggp
      301 aavatavvla frvitvwlpl lpgaltlavl vrtkvl
//
LOCUS       WP_392127135             301 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Streptomyces flaveolus].
ACCESSION   WP_392127135
VERSION     WP_392127135.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         1..301
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32216
     Region          1..295
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mlldtaslyf rayfgvpdsv kapdgtpvna vrglldfidr lvkdhrpdhl vacmdadwrp
       61 hwrvelipsy kahrvaeerp agpdaeevpd tlspqvpvie avldalgiar vgvpeyeadd
      121 vigtytarak gpvdivtgdr dlyqlvddar gvrvlypikg vgtlqltdea alrekygvdg
      181 rgyadlallr gdpsdglpgv agigektaak llaefgdlag ilaavddpaa kltpsqrkrl
      241 tearpylava pkvvrvaddv plpdvttalp htprdkaale elaarwglgg slerllttlt
      301 a
//
LOCUS       WP_392127499             233 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Streptomyces sp. NPDC014940].
ACCESSION   WP_392127499
VERSION     WP_392127499.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014940
  ORGANISM  Streptomyces sp. NPDC014940
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 233)
  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 10007985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Streptomyces sp. NPDC014940"
                     /db_xref="taxon:3364932"
     Protein         1..233
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24071
     Region          33..223
                     /region_name="COG3786"
                     /note="L,D-peptidoglycan transpeptidase YkuD,
                     ErfK/YbiS/YcfS/YnhG family [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443000"
ORIGIN      
        1 mrpgvvlalv saslcvlglt pargtdplpa rmadtgggtq litaqapaag stsgtvtwwd
       61 lrdgtwtetg saparfgang lveggarvqg tdttptglyg lpfgfglraa pagtrvgyrp
      121 vtaaswwcqd ndsasynrwt eplpadclas rsekldsyap qygyalvigf nydrpvrgrg
      181 agiflhvngk gatagcvsvp edamrailgw adparephia igtadgatav try
//
LOCUS       WP_392127754             412 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces flaveolus].
ACCESSION   WP_392127754
VERSION     WP_392127754.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 412)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         1..412
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=44204
     Region          64..249
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          256..381
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mrhvhgrarr agaapaavmt wavllagaaa ctsggsgigp gngevfgkpp apedvirvtp
       61 ddaskgvrpe relsvrvpeg rlesvkvvks qdaqetpvpg risadglswk pagdrlalaa
      121 kytvdavald ghgrrsarht tfttyvpeer figyvapedr svvgtgmivs lefnreitdr
      181 aaveravsvt akpatdvrph wfgkdrldfr pkkywkpgtk vtvalklrdv egapgvyglq
      241 hrtfsftvgr sqlslvdave rtmevrrdgt llatvpitag apstptyngk mvvtemldvt
      301 rmnsrtvgfg geydipdvph airltssgtf lhgnywasad tfgranvshg cvglrdvkgg
      361 gsdtpagwff drsligdvve vvrskdkevd pdnglggwnm swtawkagse vr
//
LOCUS       WP_392127756             419 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces flaveolus].
ACCESSION   WP_392127756
VERSION     WP_392127756.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 419)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         1..419
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=44184
     Region          80..261
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          267..393
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mnvrpisgts sagirgqsgr rtgrrlpalm lgvllavsac ggggadsgsg dgkggnakda
       61 taaqskqsea vvtiapadga kavdtsgalk vgaakgklte vvvkdaegdp vegrisgdga
      121 twtpsthlaa staytvhava edsegrtaae dsrfttltpk ntftgtftpe dgskvgvgmp
      181 fsirfsrgit hpedvekair iktepaveve ghwfgndrld frpeqywqag tkvtvdlald
      241 gvegregvyg kqtktvsftv grkqvsvvda kkltmqvvrd dkvlrtvkvt tgapgyetwn
      301 gkmvitekld vtrmngetvg yggeydikdv phamrlstsg tfihgnywgg dafgnrnash
      361 gcvglrdvqg gwdgktpaaw ffdnsligdv vvvknsndet iapdnglngw nmsweqwka
//
LOCUS       WP_392128369             215 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces sp. NPDC014940].
ACCESSION   WP_392128369
VERSION     WP_392128369.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014940
  ORGANISM  Streptomyces sp. NPDC014940
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Streptomyces sp. NPDC014940"
                     /db_xref="taxon:3364932"
     Protein         1..215
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22746
     Region          2..213
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 mssrerilgr vrraladlpa detpyeeava rdylrehggl tagqtvella enladyravv
       61 hrtdaaglpd liarllaerg servlvppgl pagwlaatgp arvadstgst areldrvdsv
      121 vtgcavaiae tgtivldgsp dqgrrritli pdhhvcvvrv pdqvvasvpq algrldparp
      181 ltwisgpsat sdieldrveg vhgprtlevv lvdge
//
LOCUS       WP_392128424             299 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces parvulus].
ACCESSION   WP_392128424
VERSION     WP_392128424.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces parvulus
  ORGANISM  Streptomyces parvulus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Streptomyces parvulus"
                     /db_xref="taxon:146923"
     Protein         1..299
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=30097
     Region          25..293
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mlplllvtvv avrhrsvlae gfghlatarw pwllaaagat cltwvaaact rqgavverlp
       61 rrrlvatqfa agaanhllpt glgasavnlr fmavcglpla rssaalalyl laesvgrlal
      121 laalfvafld alrlgtllpe gavgpllvaa aavpvvaaav lvlaprlrga lvsflrtalg
      181 earsvhrlpa ralalwggal afpalqasal vlvglslglp vpvahmavay laatvavalv
      241 ptpggigsve aalvvalvaa ggpaavatav vlafrlltvw lpllpgaltl aalvrmrvi
//
LOCUS       WP_392128520             244 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Streptomyces flaveolus].
ACCESSION   WP_392128520
VERSION     WP_392128520.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 244)
  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 11440233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         1..244
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=26665
     Region          13..241
                     /region_name="GCD1"
                     /note="NDP-sugar pyrophosphorylase, includes eIF-2Bgamma,
                     eIF-2Bepsilon, and LPS biosynthesis protein s
                     [Translation, ribosomal structure and biogenesis, Cell
                     wall/membrane/envelope biogenesis]; COG1208"
                     /db_xref="CDD:440821"
ORIGIN      
        1 mtdpnaasrr pvqavvlagg qgsrlrpytd drpkpmveip gtgtpiighq lawlaeegvt
       61 dvvvscghla evlqrwleta dlplsvttvv epeplgrggg lkyaaarlph pdrpwyatng
      121 diwtrfslrd madfhterda vatlalarpr lpwgavqtdg fghitdfiea ppstfeinag
      181 vyvfspafae mlpergdher ttfprlareh rlagfpipqg sywraidtak dlteaarela
      241 alsr
//
LOCUS       WP_392128869             310 aa            linear   BCT 20-JAN-2025
DEFINITION  quinone oxidoreductase family protein [Streptomyces parvulus].
ACCESSION   WP_392128869
VERSION     WP_392128869.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces parvulus
  ORGANISM  Streptomyces parvulus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 310)
  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 310)
  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 310)
  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   4  (residues 1 to 310)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces parvulus"
                     /db_xref="taxon:146923"
     Protein         1..310
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=31092
     Region          4..310
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 magayggpev lsvidvavpe prpnevritv raagvnpfdy ksysgafgvd perlpvrlgv
       61 eaagvvtavg adaigpagpi avgdevityt apgayaaeiv vpassvvpkp valsweqagg
      121 llaagvtavh tleavglgkg etvlihgaag gvglvavqla vargatvvat asrakhdllr
      181 elgaipvvyg pgladrvrav apegvhaaad lvgteeavdv svelvpdrlr iatiagherg
      241 aragikllgg vpgadpgtei rraarlqlte aatggrlriv iadsyplrea atahreimag
      301 httgkivlvp
//
LOCUS       WP_392129169             410 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces parvulus].
ACCESSION   WP_392129169
VERSION     WP_392129169.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces parvulus
  ORGANISM  Streptomyces parvulus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Streptomyces parvulus"
                     /db_xref="taxon:146923"
     Protein         1..410
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=43633
     Region          99..316
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mgirradpfv qravrelaad gieaglfhts gtaadedfpg yrerldravt preladavaa
       61 wgadaavsis lpcenalrda aakafldsvg iptvmtplpa tmllvdkwet krlcaqagla
      121 vpegfrvdsd llagrglpvp gyrdalrvra erlgyplmak pvwdstsmgi rtlrssadle
      181 tllaggpetv stvvervveg dlcsvdvvgr pgayrvlppc wtgragpepv ftfadlrwcg
      241 prpeadavfr dvartltalc gelgvhgsvn vdmvytggrf vvleinprig gattlscaas
      301 gtntftslar larglpftgg taprtrwave flaagrvppe vlaelrrrvq vvtahelvid
      361 gtshgdivvf tlaegeeert vktlthlhet ygfpsagvma kigrllgpar
//
LOCUS       WP_392129258             707 aa            linear   BCT 20-JAN-2025
DEFINITION  DNA gyrase/topoisomerase IV subunit B [Streptomyces sp.
            NPDC014940].
ACCESSION   WP_392129258
VERSION     WP_392129258.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014940
  ORGANISM  Streptomyces sp. NPDC014940
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Tari,L.W., Trzoss,M., Bensen,D.C., Li,X., Chen,Z., Lam,T.,
            Zhang,J., Creighton,C.J., Cunningham,M.L., Kwan,B., Stidham,M.,
            Shaw,K.J., Lightstone,F.C., Wong,S.E., Nguyen,T.B., Nix,J. and
            Finn,J.
  TITLE     Pyrrolopyrimidine inhibitors of DNA gyrase B (GyrB) and
            topoisomerase IV (ParE). Part I: Structure guided discovery and
            optimization of dual targeting agents with potent, broad-spectrum
            enzymatic activity
  JOURNAL   Bioorg Med Chem Lett 23 (5), 1529-1536 (2013)
   PUBMED   23352267
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Gadelle,D., Filee,J., Buhler,C. and Forterre,P.
  TITLE     Phylogenomics of type II DNA topoisomerases
  JOURNAL   Bioessays 25 (3), 232-242 (2003)
   PUBMED   12596227
REFERENCE   3  (residues 1 to 707)
  AUTHORS   Wang,J.C.
  TITLE     Cellular roles of DNA topoisomerases: a molecular perspective
  JOURNAL   Nat Rev Mol Cell Biol 3 (6), 430-440 (2002)
   PUBMED   12042765
REFERENCE   4  (residues 1 to 707)
  AUTHORS   Champoux,J.J.
  TITLE     DNA topoisomerases: structure, function, and mechanism
  JOURNAL   Annu Rev Biochem 70, 369-413 (2001)
   PUBMED   11395412
REFERENCE   5  (residues 1 to 707)
  AUTHORS   Roca,J.
  TITLE     The mechanisms of DNA topoisomerases
  JOURNAL   Trends Biochem Sci 20 (4), 156-160 (1995)
   PUBMED   7770916
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Streptomyces sp. NPDC014940"
                     /db_xref="taxon:3364932"
     Protein         1..707
                     /product="DNA gyrase/topoisomerase IV subunit B"
                     /EC_number="5.6.2.2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003918 - DNA topoisomerase type II
                     (double strand cut, ATP-hydrolyzing) activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006265 - DNA topological change [Evidence
                     IEA]"
                     /calculated_mol_wt=76943
     Region          21..693
                     /region_name="GyrB"
                     /note="DNA gyrase/topoisomerase IV, subunit B
                     [Replication, recombination and repair]; COG0187"
                     /db_xref="CDD:439957"
ORIGIN      
        1 mtadtsvpst allagadrdg snytarhllv legleavrkr pgmyigstds rglmhclwei
       61 idnavdealg gycdhievil hddasvevrd ngrgipvdve pktglsgvev vmtklhaggk
      121 fgggsyaasg glhgvgasvv nalsarldve vdrggnthai sfrrgvpgaf rgngteakfe
      181 pgsglakgkk ipksrtgtrv rywadrqifl kdaklsletl hqrarqtafl vpgltivvrd
      241 efglgeggsk geesfrfdgg isefceylas dkavcdvlrf sgqgtfketv pvldehgqmt
      301 ptevarelgv dvalrwgtgy daklrsfvni iatpkggthv agfeqaitqt mnevlrakkm
      361 lrvaednivk ddalegltav vtvrlaepqf egqtkevlgt saarrivnnv vtkelkaflt
      421 stkrdaaaqa rvvmekvvaa artrvaarqh kdaqrrktal essslpakla dcrsddvdrs
      481 elfivegdsa lgtaklarns efqallpirg kilnvqrssv tdmlknaecg aiiqvigags
      541 grtfdidaar ygkiimmtda dvdgshircl lltlfqrymr pmvesgrvfa avpplhriel
      601 iqpkkgqdky vytysdrelr dklmefqskg vrykdsiqry kglgemdadq laettmdprh
      661 rtlrrinlsd leaaeqvfdl lmgndvaprk efisgsaatl drsrida
//
LOCUS       WP_392129310             259 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces parvulus].
ACCESSION   WP_392129310
VERSION     WP_392129310.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces parvulus
  ORGANISM  Streptomyces parvulus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616714
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Streptomyces parvulus"
                     /db_xref="taxon:146923"
     Protein         1..259
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26072
     Region          4..230
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 mtafaalhrp gsplllpcaw dhasafalag qgfpavgtts lgvaaanglp dgasatrdet
       61 lrlaltlgsg pflltvdaes gfaddpdevg efarqlaavg aaginledal gppgrhaaki
      121 aavksaapgl fvnartdtyw sgdgdpgeta rrldayreag adgvfvpglt dpariaelaa
      181 rldvplnvlh spngptlphl adlgvarvsl gsllyrralg aaletatdia agrptvgtsp
      241 syeevaalsg grqgpvcrp
//
LOCUS       WP_392129875             414 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces parvulus].
ACCESSION   WP_392129875
VERSION     WP_392129875.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces parvulus
  ORGANISM  Streptomyces parvulus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Streptomyces parvulus"
                     /db_xref="taxon:146923"
     Protein         1..414
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=43826
     Region          56..316
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 msarpvvlvv apgdenyrgy cleqvadays vvlltgteps wekphitdha vvdfsdpaal
       61 laggralaar hdlagvmtwd ewsvvptarl arqlglstta pevmqgcrnk atarslfarh
      121 gvpsaasvsv rtrkeaeaaa drigypvvlk pashagaigv lrvddrdqlt aayraaerta
      181 gqgtestsvl veefldgpei svecvtyrga ttvvavnrkt istpphfeql ahsvdatdpl
      241 letvapaara ainalgitdg vshiemrlvd grphlievng rlagdmighl vrlatgidlv
      301 raaadiacdr apdltptrss aaairllypd tsgtlthlty dgprptwldr lhyqcrpgdq
      361 lllpadggnl ytgrigylit tattgqqara radeaaravt avldrtsgtr staa
//
LOCUS       WP_392130165             310 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Streptomyces parvulus].
ACCESSION   WP_392130165
VERSION     WP_392130165.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces parvulus
  ORGANISM  Streptomyces parvulus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces parvulus"
                     /db_xref="taxon:146923"
     Protein         1..310
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32425
     Region          8..308
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 msappepvrp prlapgarva vvapsgpvpe erlqagldvl rgwdldpvva phvldrhgtf
       61 dylagtdadr aadlqsawcd pavdavlcar ggygaqrmad lldwdamraa gpkvfvgfsd
      121 italheafat rlglvtlhgp maagidfvkn araqdhlrat lfapetvrvi asggtpmvpg
      181 rargvtlggc lallaaelga pharpsargg llcleevgee tyrvdryltq llragwldgv
      241 agvllgswqd cepyerlrpl ladrlgglgv pvvedfgfgh cegaltvpfg vaaeldadag
      301 tlalerpala
//
LOCUS       WP_392131805             303 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces parvulus].
ACCESSION   WP_392131805
VERSION     WP_392131805.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces parvulus
  ORGANISM  Streptomyces parvulus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 303)
  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 303)
  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 303)
  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 10611723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces parvulus"
                     /db_xref="taxon:146923"
     Protein         1..303
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31789
     Region          7..69
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(13,17,42)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(16,41)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(23..24,35,38,42..43)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          171..253
                     /region_name="DUF2690"
                     /note="Protein of unknown function (DUF2690); pfam10901"
                     /db_xref="CDD:402475"
ORIGIN      
        1 mtpehtrlvt alrelrvgag lslaalaert aysksswery lngkslppre avrelcrlad
       61 apqgrvlalw eiaeshwsgr aaaspapvta rpapedgspl prtrepaatg agrrpgrsrl
      121 lvllaaaytv ivggvaavlf lllpdsaeqe edplpasvpf slaplchgaa cegrdpmrli
      181 cgigpdtlaa yrtatgahve lrhsekcgas wartwgteig drldvtaegp thtvlianad
      241 daaafmytem tevtrgstvr acfrpaaadg erecfearvg drvgeagpat rgpsrpapsg
      301 sgg
//
LOCUS       WP_392130644             305 aa            linear   BCT 20-JAN-2025
DEFINITION  quinone oxidoreductase family protein [Streptomyces sp.
            NPDC014940].
ACCESSION   WP_392130644
VERSION     WP_392130644.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014940
  ORGANISM  Streptomyces sp. NPDC014940
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 305)
  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 305)
  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 305)
  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   4  (residues 1 to 305)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Streptomyces sp. NPDC014940"
                     /db_xref="taxon:3364932"
     Protein         1..305
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=31424
     Region          1..305
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 mrrvryesag gplfveeaav pvagpgellv rcaavgvtlp vvrkvaeaae pvplggeiag
       61 tvvavgegvs rfragdrvtg lcfghgyadh allheamasp vpagasfvda valvrsglva
      121 lgalhaagpv rgeavlvtaa asgvgqlavr lartrgarrv vgavsdpaka dfvrslgadd
      181 cvrygderwg epydcvldav ggdllapala alashgrlva yssgggtiqa ydllvgaksv
      241 igfqmaliar grpalyerwr relwrlfsdg tlrpavhgef aledaakahe aittrsnlgk
      301 vvlrp
//
LOCUS       WP_392132119             288 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptomyces flaveolus].
ACCESSION   WP_392132119
VERSION     WP_392132119.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 288)
  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 288)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 288)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 288)
  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   5  (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   6  (residues 1 to 288)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         1..288
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31896
     Region          19..102
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          126..284
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mlerlnqame hieshldqqi dvaelarvaw tseyhfrrmf salsgmplse yvrrrrltva
       61 gaevlagert lldvavrygy gsgeafaraf ralhgvgpge arrtgaalhs qprmsfrivv
      121 egssgmryri ldkkqfrvvg rkarvplvhe gvnpsiaafv rgigpeplrr laalsdqepe
      181 gvvgvsdqld psraegteld yyhavvtgae apedmdvlev pagtwavfes sgpfpqalqy
      241 lwrdvytqwf psnpyrsrpg peilrvrvse dgaqadaevw ipveravg
//
LOCUS       WP_392132771             393 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces flaveolus].
ACCESSION   WP_392132771
VERSION     WP_392132771.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 393)
  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 393)
  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
REFERENCE   3  (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   4  (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   5  (residues 1 to 393)
  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   6  (residues 1 to 393)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (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 20021635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         1..393
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40497
     Region          16..>74
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          83..385
                     /region_name="ASKHA_ATPase_ROK_CYANR"
                     /note="ATPase-like domain of
                     cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and
                     similar proteins; cd24073"
                     /db_xref="CDD:466923"
ORIGIN      
        1 mspskirfse lvgeqtraei fatvltagpi srtqlaqrlg lvpssvtrml ppllehdylr
       61 etdtapqgrg rpqkmlqvnp dkhivvgmki gpaqvsavvt dmaanvlara eepiadctpe
      121 talsaaaalt srllseapeg adrvlglgvg vsghvdsasg icrysalldw nkvdvagplh
      181 eatglpvvvn ndvntlvvae rwfgqgrdvd sfavvtlgpg igcgllldga lfsgatglag
      241 elghlpldpt gpmcscgrrg clealagdra vlrhlrdagv pcttiseaid larssggsar
      301 tvarsafaea gdalgrglag mcnllnlqki iiagegavay dllgpaasha leahafstaa
      361 rdcdihvdpv rhdlwargaa clvirdavga ais
//
LOCUS       WP_392132899             462 aa            linear   BCT 20-JAN-2025
DEFINITION  alpha,alpha-trehalose-phosphate synthase (UDP-forming)
            [Streptomyces parvulus].
ACCESSION   WP_392132899
VERSION     WP_392132899.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces parvulus
  ORGANISM  Streptomyces parvulus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 462)
  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 462)
  AUTHORS   Eastmond,P.J. and Graham,I.A.
  TITLE     Trehalose metabolism: a regulatory role for trehalose-6-phosphate?
  JOURNAL   Curr Opin Plant Biol 6 (3), 231-235 (2003)
   PUBMED   12753972
REFERENCE   3  (residues 1 to 462)
  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   4  (residues 1 to 462)
  AUTHORS   Elbein,A.D., Pan,Y.T., Pastuszak,I. and Carroll,D.
  TITLE     New insights on trehalose: a multifunctional molecule
  JOURNAL   Glycobiology 13 (4), 17R-27R (2003)
   PUBMED   12626396
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 929-939 (1997)
   PUBMED   9334165
  REMARK    Erratum:[Biochem J 1998 Feb 1;329(Pt 3):719]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Streptomyces parvulus"
                     /db_xref="taxon:146923"
     Protein         1..462
                     /product="alpha,alpha-trehalose-phosphate synthase
                     (UDP-forming)"
                     /EC_number="2.4.1.15"
                     /GO_function="GO:0003825 - alpha,alpha-trehalose-phosphate
                     synthase (UDP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0005992 - trehalose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50238
     Region          8..462
                     /region_name="OtsA"
                     /note="Trehalose-6-phosphate synthase, GT20 family
                     [Carbohydrate transport and metabolism]; COG0380"
                     /db_xref="CDD:440149"
ORIGIN      
        1 massfgaaqv lvasnrgpvs yevredgslh akrgggglvs glssigpdag alwvcsalgd
       61 gdreavrrgv gedgvrmldv padvhadayn giansvlwfv hhmlyqtpve pvfdaefrrq
      121 wasyeaynra faealaeeaa egavaivqdy hltlvpgmlr elrpdlrigh fshtpwapvd
      181 yfrllpddia dqvlrgmlga drlgfltrrw adaftaccda lvgglggtet gvhglgadad
      241 flrkrshead vdermaalre eigegrrtiv rvdrtelskn ivrgllayre llatrpewre
      301 rvvhvafayp srqdlavyrd ytaevqrvad avneefgtpg wtpvvlhvkd dfarslaayr
      361 ladvalvnpv rdgmnlvake vpvvseegca lvlsreagay eelgedavvv npydvsgtae
      421 alhtalsvpp aeraerskrl aaagtalppa rwfleqldal rs
//
LOCUS       WP_392133009             308 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Streptomyces flaveolus].
ACCESSION   WP_392133009
VERSION     WP_392133009.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         1..308
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32441
     Region          4..306
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mkpllrpsrl gpgarvavva psgpvpeerl qagldvlrgw dldpvvaphv ldrhatfdyl
       61 agtdadraad lqsawcdpav davlcarggy gvqrmidlld weamraagpk vfvgfsdits
      121 lheafarrlg lvtlhgpmaa gidflknara qdhlkatlfa petvrviasd gstpmvpgra
      181 rgvtlggcla llaaelgtph arpsarggll cledvgeepy rldrcltqll ragwldgvag
      241 vllgsweqce paerlrpmla drlaglgvpv vedfgfghca galtvpfgvt aeldadagtl
      301 tldepalr
//
LOCUS       WP_392133555             466 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces parvulus].
ACCESSION   WP_392133555
VERSION     WP_392133555.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces parvulus
  ORGANISM  Streptomyces parvulus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 466)
  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 466)
  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 466)
  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 10611723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Streptomyces parvulus"
                     /db_xref="taxon:146923"
     Protein         1..466
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46172
     Region          17..73
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(23,27,52)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(26,51)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(33..34,45,48,52..53)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          364..448
                     /region_name="DUF2690"
                     /note="Protein of unknown function (DUF2690); pfam10901"
                     /db_xref="CDD:402475"
ORIGIN      
        1 mprwkalpee ldpqikeftg qlrrlvdrse lsvasvadat gysktswery lngrllapkg
       61 aivalaevtg tnplhlttmw elaerawsrs emrhdmtmea irisqaraal gdlgassgna
      121 akeakaakda ksgngagggr gsrssgrhag gapvaglagp agvaptlgpt vpvqptaads
      181 pdsaagpvrg ggptggpstp fpgapsagga tegnswglag yrgpaptgdr tarpahrags
      241 gtaatamgpa aapgpgahsg pggysgpsgg ygspsggydd psaghgepph rgpdrrgrts
      301 gggsrrmttf vagvvgvlvv iagaffllnd gggeenqdak pspsptvsre qqlppgvkcg
      361 gddctgkdpe vmgcggdlvt taatatvgtt avevrysktc gtawarvtqa aqgdevkisa
      421 agrnqqtgtv sgvgdtvayt pmvavksaad aeacvttasg vegcte
//
LOCUS       WP_392133562             240 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces parvulus].
ACCESSION   WP_392133562
VERSION     WP_392133562.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces parvulus
  ORGANISM  Streptomyces parvulus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616714
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Streptomyces parvulus"
                     /db_xref="taxon:146923"
     Protein         1..240
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23957
     Region          8..239
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 mtaaaerfra lhrgrapedp lvlpgpwdaa sarafaeagf palatpsagi aaslgyadgr
       61 tpagemfaav ariaravdvp vsadveggyg lapeelverl leagavgcnl edsadgalkd
      121 paehaewlag vraaaggdlf vnarvdtfvr gvddpgaaig raaayvaaga dcvypigapa
      181 avlpllragi qgplnvlarp gedpspaalg glgatrvtfg pglqryadga vrefaarlag
//
LOCUS       WP_392133876             256 aa            linear   BCT 20-JAN-2025
DEFINITION  SRPBCC family protein [Streptomyces sp. NPDC015345].
ACCESSION   WP_392133876
VERSION     WP_392133876.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015345
  ORGANISM  Streptomyces sp. NPDC015345
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  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 10008053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces sp. NPDC015345"
                     /db_xref="taxon:3364953"
     Protein         1..256
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=28535
     Region          10..121
                     /region_name="YndB"
                     /note="Chalcone/flavanone-binding protein YndB,
                     AHSA1/START/SRPBCC domain [Lipid transport and
                     metabolism]; COG3832"
                     /db_xref="CDD:443044"
ORIGIN      
        1 mldvpakgpa dggkrfeiar efevegspae vwaalttgtg gwlwpmkyep reggaapfgg
       61 tvtrwepphr ltarvqgadh gpgrppdrld qldhtieprd ggrrswlryv qrgsfaddwd
      121 rryddairht dfhlhtlcqy mayfagrpav fsalngppts vapdaftrla ralglpddaa
      181 egarvrveap geeldavidf rsryfiglrt ddalhrffgr nhsgapvrvs vhdfgpqadt
      241 krtelawqdw lhhlyg
//
LOCUS       WP_392133631             346 aa            linear   BCT 20-JAN-2025
DEFINITION  BMP family lipoprotein [Streptomyces parvulus].
ACCESSION   WP_392133631
VERSION     WP_392133631.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces parvulus
  ORGANISM  Streptomyces parvulus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Yousief,S.W., Bahey-El-Din,M. and Zaghloul,T.I.
  TITLE     Immunization with the basic membrane protein (BMP) family ABC
            transporter elicits protection against Enterococcus faecium in a
            murine infection model
  JOURNAL   Microbes Infect 22 (3), 127-136 (2020)
   PUBMED   31585177
REFERENCE   2  (residues 1 to 346)
  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   3  (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   4  (residues 1 to 346)
  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   5  (residues 1 to 346)
  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 11448319
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Streptomyces parvulus"
                     /db_xref="taxon:146923"
     Protein         1..346
                     /product="BMP family lipoprotein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /calculated_mol_wt=35652
     Region          34..344
                     /region_name="Med"
                     /note="Lipoprotein Med, regulator of KinD/Spo0A, PBP1-ABC
                     superfamily, includes NupN [Signal transduction
                     mechanisms]; COG1744"
                     /db_xref="CDD:441350"
ORIGIN      
        1 mrrtsrlirv avgaaslala atacggtssd sgdgkddkgl aiaydiggkg dqsfndaaya
       61 glerakkefg yetadieptd getdadkeqr ltslakqgyn pvigvgfayg pamkavaaky
      121 pdttfgivds vvegknvasl vfaeneasyl agvaaakatk tktvgfvggv dvplihkfea
      181 gyeqgvkdtd pkvqvisqyl tqtaeeggfs spdkgraaae gqiekkadvv yqaaglsgqg
      241 vieaaakakv waigvdsdqy gqealaahkd yiltsalkdi ngavyalaks veddkpltgt
      301 qtfdlksdgv glsdsnpkfa eipgaqdava kakegitsgs ikvkte
//
LOCUS       WP_392133933             213 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces flaveolus].
ACCESSION   WP_392133933
VERSION     WP_392133933.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         1..213
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22276
     Region          6..211
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 mtppsssrdr vlgrvrrala dapeapevsr dylvghtpdd patvldllhe nladyragvh
       61 rstrqglaal igellaghga rsvvvppglp gdwlagsdar qrcddvpltp eeldsvdavv
      121 tgcalavaet gtvvldagpg qgrraltlvp dvhicvvdar tqvvaslpqa lprldptrps
      181 twisgpsats dieldrvegv hgprtlevvl vvd
//
LOCUS       WP_392134413             256 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: metallophosphoesterase family protein [unclassified
            Streptomyces].
ACCESSION   WP_392134413
VERSION     WP_392134413.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  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 256)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..256
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28287
     Region          5..246
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 mpafrvnvvs dvhgnaadla ragdgadalv clgdlvlfld yadhsrgifp dlfgarnasr
       61 lvelrtarrf eearefgrrl wagvdrgpai eravrkqyae lfaafptpty atygnvdmpi
      121 lwreyagpgt tvldgervei ggrvfgfvgg glrtpmrtpy eisdeeyaak ieavgevdvl
      181 cthippdvpe llydtvarrf ergsrallda irrtrpkyal fghvhqplvq rmrvgatecv
      241 nvghfagsgr pwalew
//
LOCUS       WP_392134683             295 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            flaveolus].
ACCESSION   WP_392134683
VERSION     WP_392134683.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 295)
  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 295)
  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 295)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         1..295
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32695
     Region          36..89
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          112..290
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mdvvgvegea agsagaravp agewerephp sdslrtfgav vqalrehagl srvdlgalvq
       61 yskhtvesve lgrrmpdeaf veraeealgn tgalrkaarh ltrgeaglav wfrrwarler
      121 eavslctyec rlvpgllqse ayaravfdns iplltdeqte aqvtarmerq ammrerptvp
      181 fgfiveesvf rrelggaqvq anmldyvlel taprnvtlqv vplklefhgc ldgpvqlvet
      241 segrrlgyse gqqngrlisd akevsllcrr ydtlrsqaln pkesrdller lrgel
//
LOCUS       WP_392138255             342 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            bacillaris].
ACCESSION   WP_392138255
VERSION     WP_392138255.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 342)
  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 342)
  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 342)
  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 11448557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..342
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=36679
     Region          44..105
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
ORIGIN      
        1 madhhplrpa rpgpsapssp sspsspsspd alspqgrgrp psafgqalre arerkgltla
       61 rlrdhlarrg vrvstvtlsh wqrgrsqper peslravsai esilgcpagg llallgprrp
      121 rgrplptppe rlenarpvyg pepllaralg eeefsrlneg tvpvsvqetv hldrtgrtar
      181 htvtqvvrat hdgadhvtah lnvdeppgpp mtasaqcgvl ldqrcvpalg lttlrigfgr
      241 plargestvv aytvdlgphg hrtthheral plhvrhyflh vvfhpealpa svygyyrahd
      301 gapradirtl plsgsgtahi lpadaaagvh gifwkwpgtt tt
//
LOCUS       WP_392134742             337 aa            linear   BCT 20-JAN-2025
DEFINITION  heme/hemin ABC transporter substrate-binding protein [Streptomyces
            sp. NPDC015345].
ACCESSION   WP_392134742
VERSION     WP_392134742.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015345
  ORGANISM  Streptomyces sp. NPDC015345
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Naoe,Y., Nakamura,N., Rahman,M.M., Tosha,T., Nagatoishi,S.,
            Tsumoto,K., Shiro,Y. and Sugimoto,H.
  TITLE     Structural basis for binding and transfer of heme in bacterial
            heme-acquisition systems
  JOURNAL   Proteins 85 (12), 2217-2230 (2017)
   PUBMED   28913898
REFERENCE   2  (residues 1 to 337)
  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   3  (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   4  (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   5  (residues 1 to 337)
  AUTHORS   Ho,W.W., Li,H., Eakanunkul,S., Tong,Y., Wilks,A., Guo,M. and
            Poulos,T.L.
  TITLE     Holo- and apo-bound structures of bacterial periplasmic
            heme-binding proteins
  JOURNAL   J Biol Chem 282 (49), 35796-35802 (2007)
   PUBMED   17925389
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Streptomyces sp. NPDC015345"
                     /db_xref="taxon:3364953"
     Protein         1..337
                     /product="heme/hemin 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=34727
     Region          66..337
                     /region_name="ChuT"
                     /note="ABC-type hemin transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG4558"
                     /db_xref="CDD:443619"
ORIGIN      
        1 mprslriaga waaalalglt acaapdgdas aqprkaasra aapdrvepvk sgakpelpvt
       61 vtsadgrrvt vrdadrivpl tgslneivft lglgenvvar ditatfeqae klpvvtrahd
      121 vsaesvlslk ptvvladttt gpaeaidqir dagvplvvfd pakslddvsp rieavaktlg
      181 veksgaeltr rterridaar kgipaggrak kprvaflylr gsasvyllgg rdsgasslle
      241 aagavdagke sglkkdftai tsealaeaap dailvmtkgl asvngvdgll kvpgvaetpa
      301 gldrrvvsid dgvllnygpr tdqvlkslve qlhgdtk
//
LOCUS       WP_392138295             470 aa            linear   BCT 20-JAN-2025
DEFINITION  SWIM zinc finger family protein [Streptomyces bacillaris].
ACCESSION   WP_392138295
VERSION     WP_392138295.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Hassan,I.U., Rehman,H.M., Liu,Z., Zhou,L., Samma,M.K., Wang,C.,
            Rong,Z., Qi,X., Cai,D. and Zhao,H.
  TITLE     Genome-wide identification and spatiotemporal expression profiling
            of zinc finger SWIM domain-containing protein family genes
  JOURNAL   Zool Res 44 (3), 663-674 (2023)
   PUBMED   37161653
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     SWIM, a novel Zn-chelating domain present in bacteria, archaea and
            eukaryotes
  JOURNAL   Trends Biochem Sci 27 (8), 384-386 (2002)
   PUBMED   12151216
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10516955
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..470
                     /product="SWIM zinc finger family protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48801
     Region          69..99
                     /region_name="SWIM"
                     /note="SWIM zinc finger; pfam04434"
                     /db_xref="CDD:309540"
ORIGIN      
        1 mllshggeps patepvarwt veqvlslapd dasrkagnkl asaghwsgtg hdasgavwgl
       61 ckgsgskpyq tvvdttgpay kcscpsrkfp ckhalgllll rasgdgqvqq gepadwasqw
      121 legrrgraea kqaaaasges apgpadtaaa rkraerraer aasgaleleq rltdllrggl
      181 atadragytl weetaarmvd aqapglagrv relgaipgsg pgwpvrllee csllhlldta
      241 wlgrerlpep laatvrtrvg lpvsaegppv rdhwlvlaqy dtadgrlttr riwlygresa
      301 rtalllsfga agrapelalp vgvtidaelt pypggglrad lgrrfatplp vpgtpppggp
      361 aeaalaayge alrgdpwldg wpvtlrdvip vpsgggwqla daegtdalpl apaalsrqgl
      421 wklvalsgga pvtvfgelgh rgfdpftawd tgagreggpg esgggtvrli
//
LOCUS       WP_392137482             393 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC015345].
ACCESSION   WP_392137482
VERSION     WP_392137482.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015345
  ORGANISM  Streptomyces sp. NPDC015345
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 393)
  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 393)
  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
REFERENCE   3  (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   4  (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   5  (residues 1 to 393)
  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   6  (residues 1 to 393)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (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 20170230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Streptomyces sp. NPDC015345"
                     /db_xref="taxon:3364953"
     Protein         1..393
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39866
     Region          <10..>74
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          77..384
                     /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 mtarpanahq arllrllrdg gpnsraqlgd qvdlsrskla vevdrlletg lvvadglaas
       61 rggrrshnir lapalrflgv digatsvdva vtnaelevlg hinqpmdvre gpvavfeqvl
      121 amaaklqasg laegfdgagi gvpgpvrfpe gvpvappimp gwdgfpvrea lsqdlgcpvm
      181 vdndvnlmam geqhagvars vgdflcvkig tgigcgivvg gevhrgttgs agdighiqae
      241 pdgrpcacgn rgcleayfsg aalardaeea atqgrsaela arldeagrls avdvaaaaaa
      301 gdaaaldlir eggnrtgqvl aalvsffnpg lvvigggvtg lghtllaair tqvyrqslpl
      361 atgnlpivlg elgptagvig garlisdhlf spa
//
LOCUS       WP_392138306             388 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            bacillaris].
ACCESSION   WP_392138306
VERSION     WP_392138306.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 388)
  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 388)
  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 388)
  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 10611723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..388
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=39333
     Region          17..79
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(23,27,52)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(26,51)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(33..34,45,48,52..53)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          <136..>214
                     /region_name="PTZ00395"
                     /note="Sec24-related protein; Provisional"
                     /db_xref="CDD:185594"
     Region          288..367
                     /region_name="DUF2690"
                     /note="Protein of unknown function (DUF2690); pfam10901"
                     /db_xref="CDD:402475"
ORIGIN      
        1 mprwkalpde ldpqirefas qlrrivehsg ldvnavadrt gfsatawery lsgqllpprr
       61 avvaladvtg tpqhhltalw epaerawsra gtrqdmttet lrirqvggap gsaeaagaag
      121 rtatatgtsd hggpgghdsg pyangpyand pyakapygnd pyandpygsd pygndphhpd
      181 gdgraphipa qrgsgapdpq qqprqgarrn gppgggsnav mlgvgavgal ivitgavmla
      241 pgdepakatp ttaattpaat psdgdpagga seepaalpdg vecrgdecag qnpdamgcgg
      301 eyartvatta igtarvevry sevcsaawar lteagpgdtv titgsaaaaa qngrvsvtea
      361 ytpmvaveka adakacatlt sgtkgctt
//
LOCUS       WP_392138630             298 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            bacillaris].
ACCESSION   WP_392138630
VERSION     WP_392138630.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..298
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=32986
     Region          28..276
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 msgvllrgrd epgegraedv tedggpsrlt irlfgplhvs rgatvlelgp pkqrallavl
       61 llrpgmetgv dqltealwge eypayaknli qksvsglral lhpggegerg tvihwsgggy
      121 rldagdadvd fytyerlavd glaaardgrl qeasellera rtmstgplve gldgpmmere
      181 rlfrqerflt dmevlaevel qlgrhrhavp llhyavhkyp lrerfawllm lalhrsdrgs
      241 ealvvyaqhr arlvaelgse pgpalralha rllaqdpelm elptvredsp gdryrvpf
//
LOCUS       WP_392138686             401 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces bacillaris].
ACCESSION   WP_392138686
VERSION     WP_392138686.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   3  (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   4  (residues 1 to 401)
  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   5  (residues 1 to 401)
  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   6  (residues 1 to 401)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 401)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 401)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..401
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41728
     Region          16..>59
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          79..389
                     /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 mtgttpgtpr vlramndraa ldlllehgpl srtrigkltg lskptasqll arleaaglvv
       61 atgtsegrpg psaqlytvna raahvagldv nsrrimaava dvtgsvvgef elatpgrrad
      121 svvrqvsdal dgaveeaglv radihrivig tpgafdpgtg rlryashlpg whsptlldel
      181 aaalpmpvey endvnlvava eqrlgaargh edfvllwnee glgaalving rlhrgftgga
      241 gevgflpvpg tplvrqvvka nsggfqelgg aqavprlara lgidtpqqph araaaellsr
      301 aaeaydrdea ltellgqyah rlatglasvt avldpglivl sggavaagge ilrsliqsel
      361 aelaasrprl vlgeidrtpv lrgalerala dtrdevfdts r
//
LOCUS       WP_392138727            1384 aa            linear   BCT 20-JAN-2025
DEFINITION  Rne/Rng family ribonuclease [Streptomyces bacillaris].
ACCESSION   WP_392138727
VERSION     WP_392138727.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1384)
  AUTHORS   Kime,L., Jourdan,S.S. and McDowall,K.J.
  TITLE     Identifying and characterizing substrates of the RNase E/G family
            of enzymes
  JOURNAL   Methods Enzymol 447, 215-241 (2008)
   PUBMED   19161846
REFERENCE   2  (residues 1 to 1384)
  AUTHORS   Callaghan,A.J., Marcaida,M.J., Stead,J.A., McDowall,K.J.,
            Scott,W.G. and Luisi,B.F.
  TITLE     Structure of Escherichia coli RNase E catalytic domain and
            implications for RNA turnover
  JOURNAL   Nature 437 (7062), 1187-1191 (2005)
   PUBMED   16237448
REFERENCE   3  (residues 1 to 1384)
  AUTHORS   Li,Z., Pandit,S. and Deutscher,M.P.
  TITLE     RNase G (CafA protein) and RNase E are both required for the 5'
            maturation of 16S ribosomal RNA
  JOURNAL   EMBO J 18 (10), 2878-2885 (1999)
   PUBMED   10329633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1384
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..1384
                     /product="Rne/Rng family ribonuclease"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=146202
     Region          639..1040
                     /region_name="CafA"
                     /note="Ribonuclease G or E [Translation, ribosomal
                     structure and biogenesis]; COG1530"
                     /db_xref="CDD:441139"
     Region          <1104..1267
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          <1207..>1318
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
ORIGIN      
        1 mpqsnepaan gnneentpgd klpprrrrra asrpagppgg avtpaaeeta apaaeaaave
       61 tpaaapeeta ppartrrrav rkatapagap etaevvepaa pepvaaetpa apaaeepaae
      121 eapaprtrrr avrkatapag apqaaeavea vavvetpaep laedeedeep vavepeaape
      181 paaprrrras rkatapagap qaaeaavive ptapaepvae aaavasepaa eaprgrtrrr
      241 asapagapqa ataepaeepa aepaaeeapa prsrrrasrk atapagapaa eepveagesl
      301 paavaeelaa evdeveeaap rgrqrrrata aagspeftak aeepsrkgrr aarpavavfq
      361 apvfaepmfq tpetaaaaaa aagssspydd idetedeqta qtaqvsapae aapqggsrrr
      421 rrrrgeaaea eqtavpaapv eepadeapea eadehegden deygdrpsrr rrrggrrrrr
      481 geahdtdeae qhadeapapa radetrtede qpqaqeadde eesdsdstas gssssrrrrr
      541 rrrrsgdaap esdngtddpe rtvvkvrepr kkeerepgtg fdevqsikgs trmeakkqrr
      601 regreqgrrr vpiiteaefl arreavervm vvrqsgertq igvlednvlv ehyvnkeqat
      661 syvgnvylgk vqnvlpsmea afvdigkgrn avlyagevnf ealgmahgpr rietalksgq
      721 svlvqvtkdp ighkgarlts qvslpgrylv yvpegsmtgi srklpdters rlktilkkiv
      781 pedagvivrt aaegasedel rrdverlqqq wediqkkakg tsgsnaptll ygepdmtvrv
      841 vrdifnedfs kvivsgddaw etihgyvshv apdltdrlsr wtsevdvfat yrideqlmka
      901 ldrkvylpsg gslvidktea mvvvdvntgk ftgqggnlee tvtrnnleaa eeivrqlrlr
      961 dlggivvidf idmvlesnrd lvlrrllecl grdrtkhqva evtslglvqm trkrvgqgll
     1021 esfsetcvhc ngrgvivhme qptsvggggg kksrkrgrgg aghdhehedh tavepaetea
     1081 elaaevaapv avepevtade efysspaeae aaasrrgrrr asrkasapag aprteapapv
     1141 aetveeqapa aepvtepavs epeaatepaa epaaaaepav vvpepeaaep eaapqgrtrr
     1201 ratrkasapa gspkqaepae pvrpaeptad pvaaedpvve aaaepapvte apeaeapkea
     1261 apprarrrvt rkvtapagsp tgaeeaavvv vesapeakap etapetapea dgsdepapak
     1321 ktarkaaakk apakktaakk taakktaakk ttaktaakkt tkktvaaeqs ssavtasaps
     1381 tdge
//
LOCUS       WP_392138815             324 aa            linear   BCT 20-JAN-2025
DEFINITION  quinone oxidoreductase family protein [Streptomyces sp.
            NPDC015345].
ACCESSION   WP_392138815
VERSION     WP_392138815.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015345
  ORGANISM  Streptomyces sp. NPDC015345
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 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   4  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Streptomyces sp. NPDC015345"
                     /db_xref="taxon:3364953"
     Protein         1..324
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=32771
     Region          1..322
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 mravqfkeyg gpevlevvaa avpepgpgqv tvdvaytgvn fadikarsdg yrvpalphvp
       61 gievsgrvra vgadvtglrp gqevaaltag gayaevalad aatvfalpdg mdlrtaatlp
      121 tvlptahalv hevgrltage svlvqgaagg vgtvvgqvak aagatvygvv sgpakaeyal
      181 khgydevfvg dtfaadarra tggrgvdlal dpvggdtfrq smaalaafgr lvsfgnasga
      241 epwrvgqpel fpgahtvsaf siltlaqsap ealrtlagra frlvadgtvt lpvtaefpls
      301 eaaeahrlmg grtttgklll rvsp
//
LOCUS       WP_392139411             235 aa            linear   BCT 20-JAN-2025
DEFINITION  4'-phosphopantetheinyl transferase family protein [Streptomyces sp.
            NPDC015345].
ACCESSION   WP_392139411
VERSION     WP_392139411.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015345
  ORGANISM  Streptomyces sp. NPDC015345
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459479
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Streptomyces sp. NPDC015345"
                     /db_xref="taxon:3364953"
     Protein         1..235
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=24761
     Region          23..226
                     /region_name="EntD"
                     /note="4'-phosphopantetheinyl transferase EntD
                     (siderophore biosynthesis) [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2977"
                     /db_xref="CDD:442216"
ORIGIN      
        1 mrqvpgssgp lasllsavpv tvvethddpa davlfpeeea vvanavakrr nefttvrhca
       61 raalksigvp papilpgqrg aprwpagvvg smthcagyra avvaradevt slgidaepge
      121 plrdpdvlgl iadeaeraal adlgarhpgt pwdrllfsak esvyktwfpl tgrwlgfeea
      181 rveldpdgtf tarllvegpv vegvelkvfs gqwivrdgia ataivlplgt pavrs
//
LOCUS       WP_392140073             518 aa            linear   BCT 20-JAN-2025
DEFINITION  sodium:solute symporter family protein [Streptomyces sp.
            NPDC015345].
ACCESSION   WP_392140073
VERSION     WP_392140073.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015345
  ORGANISM  Streptomyces sp. NPDC015345
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Henriquez,T., Wirtz,L., Su,D. and Jung,H.
  TITLE     Prokaryotic Solute/Sodium Symporters: Versatile Functions and
            Mechanisms of a Transporter Family
  JOURNAL   Int J Mol Sci 22 (4), 1880 (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Wright,E.M. and Turk,E.
  TITLE     The sodium/glucose cotransport family SLC5
  JOURNAL   Pflugers Arch 447 (5), 510-518 (2004)
   PUBMED   12748858
  REMARK    Erratum:[Pflugers Arch. 2004 Feb;447(5):813-5]
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Jung,H.
  TITLE     The sodium/substrate symporter family: structural and functional
            features
  JOURNAL   FEBS Lett 529 (1), 73-77 (2002)
   PUBMED   12354616
REFERENCE   4  (residues 1 to 518)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001756
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Streptomyces sp. NPDC015345"
                     /db_xref="taxon:3364953"
     Protein         1..518
                     /product="sodium:solute symporter family protein"
                     /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=53992
     Region          40..486
                     /region_name="PutP"
                     /note="Na+/proline symporter [Amino acid transport and
                     metabolism]; COG0591"
                     /db_xref="CDD:440356"
ORIGIN      
        1 mlspsggsfp ffclvvtgva vaawalsrlr dpgelphpag wtlarrdvgl ggtavllggt
       61 vytaytviav pgltyatggf glyaltytll ltpaalivlp rlhkaarrhg lvtaadlala
      121 rhgshalsla vvisgllatm pylalqvigl gaalrgmgid ptsprvipgl llvftlltag
      181 flprglrvcv rvaafkavlm atlltvalil llrhgtgggw vfdeagqrla argmslappa
      241 gtgtayitla lgsvlaqlmy pqvltvalaa rctdtlrrat lalplwtial gvfaylgfaa
      301 laygietpag haelaapall rrlaapwlag lllgglavaa llpaavmaig matlvarnly
      361 teyfnptatp khevriarfa apviisgalv fsfllqpqda vnlhllggvw iiqtvpavgc
      421 alytrwfhhr allvgwaigm ttgtaltvah gfdsvvtlef ghthlsfyva faalvlnlia
      481 aalltplldr agvmrgpdtf aargglprrg srfafrvd
//
LOCUS       WP_392140288             416 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces bacillaris].
ACCESSION   WP_392140288
VERSION     WP_392140288.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 416)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..416
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=44863
     Region          61..248
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          255..385
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mnhvaksart gsatvltwag lltalavlvl ltgctdtrea llngkegspa dvisifpedg
       61 akevgaetki rvkipdgrle svkvmrieda qqqtvagria ddglswepep gaarlalaak
      121 ysvdavavda sgqrsarhat fttlvpehrf igyfkpenrs tvgtgmivsf sfnravtdra
      181 avqrairvta kpevevvghw fgkdrldfrp eeywkpgtev tvdiglrdve gapkvygsqd
      241 kkvtftvgrs qvslvdaeak tmevrrdgkl vstvpitaga pktttyngkm vvtemhevtr
      301 mngatvgftd eegkgeydik dvphairltt sgtflhgnyw adesvfgken vshgciglrd
      361 akggsattpg gwffdrtlig dvvevvnskd kkvapdngls gwnldwkqwk agsavr
//
LOCUS       WP_392141691             438 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces bacillaris].
ACCESSION   WP_392141691
VERSION     WP_392141691.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..438
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=48645
     Region          49..332
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mpddsrknif vigmdeanrr tleavpdadr hrlhplltie elqegqvtvd ellararavl
       61 daheggidai vgywdfpvst lvpllseeyg tvstslesvv kcehkywsrl eqrkvtdayp
      121 rfgmvdlesd dprppeglrf pmwvkpalay sselafgvad laefrsavae iregiarvgk
      181 pfeaildlle lppemagvgg evclaeeamt giqvavegyv hrgevtvygv ldsinypgss
      241 sflrhqypst lpapvirrlh evsertmrqi gmdratfsie yfydpktadi rlleinprhs
      301 qshaemfqfv dgvpnhhrmf rlalggdpav ppgggryrva akwyyrwfge grvhgvptae
      361 dlaaiqreip gvhidmvpae gqrlstvhgq dsysyevahi ftggddeddl rrkfdacvaa
      421 lgltfdetep ggrgrngs
//
LOCUS       WP_392141746             230 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease H family protein [Streptomyces sp. NPDC015345].
ACCESSION   WP_392141746
VERSION     WP_392141746.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015345
  ORGANISM  Streptomyces sp. NPDC015345
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 230)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Streptomyces sp. NPDC015345"
                     /db_xref="taxon:3364953"
     Protein         1..230
                     /product="ribonuclease H family protein"
                     /EC_number="3.1.26.4"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=24146
     Region          5..145
                     /region_name="RNase_HI_prokaryote_like"
                     /note="RNase HI family found mainly in prokaryotes;
                     cd09278"
                     /db_xref="CDD:260010"
     Site            order(10..13,45..47,50,72,122,142)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260010"
ORIGIN      
        1 msdliiaacd gaakknpgpa awawvvadae grpqrweagp lghstnnvae ltalaelles
       61 tdpavplevr mdsqyamnav tkwiaswkrn gwltaakkpv ankdivvrid allqgravtf
      121 rhvaahqvdg dhlnaiadva asdaattqqp agtahgapei pepraermta sptsrvpkka
      181 aarakktgpg pvikakfpgr chcgqpyaag ekiaknahgw ghvecrdggd
//
LOCUS       WP_392142528             428 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Streptomyces bacillaris].
ACCESSION   WP_392142528
VERSION     WP_392142528.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces bacillaris
  ORGANISM  Streptomyces bacillaris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 428)
  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 428)
  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 11417965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Streptomyces bacillaris"
                     /db_xref="taxon:68179"
     Protein         1..428
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46258
     Region          1..287
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
ORIGIN      
        1 mkalhtsdwh lgrtlqrrsr ddefdavpae itaiaesvqp dlivhsgdlf dsyrpahkdv
       61 lralrclnaf ariaptvvlg gnhdspelfd llnyvaalrp dadqhrlrfi hsrgdtdpga
      121 vldfdsrdgh qrirlaalpy vhpnrylhlf pgfgttegay aaglrelqeg llarlrdgyd
      181 perdvllfta hqyvasavpa qsermwevre pyatdadalp qvaycalghi hkpqpvgagr
      241 lparyagspl qmdfgeseet ksvtvveagp grrtlitpht lhsgrrlarf hgtleelgvd
      301 aaqytgvylk avirsdepvp rlgdrvaelv pqaivvdvee dcaatrasvl tgadaaddsk
      361 lditavfsay laeagtpgqs adevvaafad llntpdatsa pspaeqllae alatswtgaa
      421 rgrtetas
//
LOCUS       WP_392142659             821 aa            linear   BCT 20-JAN-2025
DEFINITION  GcvT family protein [Streptomyces sp. NPDC015345].
ACCESSION   WP_392142659
VERSION     WP_392142659.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015345
  ORGANISM  Streptomyces sp. NPDC015345
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 821)
  AUTHORS   Stauffer,L.T., Ghrist,A. and Stauffer,G.V.
  TITLE     The Escherichia coli gcvT gene encoding the T-protein of the
            glycine cleavage enzyme system
  JOURNAL   DNA Seq 3 (6), 339-346 (1993)
   PUBMED   8219277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Streptomyces sp. NPDC015345"
                     /db_xref="taxon:3364953"
     Protein         1..821
                     /product="GcvT family protein"
                     /calculated_mol_wt=89272
     Region          14..399
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
     Region          385..440
                     /region_name="FAO_M"
                     /note="FAD dependent oxidoreductase central domain;
                     pfam16350"
                     /db_xref="CDD:465100"
     Region          435..820
                     /region_name="GcvT"
                     /note="Glycine cleavage system protein T
                     (aminomethyltransferase) [Amino acid transport and
                     metabolism]; COG0404"
                     /db_xref="CDD:440173"
ORIGIN      
        1 mrrsaahatv gptarprvvv igagivgcsl adeltargwt dvtvldqgpl papggstsha
       61 pglvfrtgps ktltafaayt vekftslevd glscflpvgg lelattperw adlhrkagla
      121 aswgvraelv gperckelwp lvdatrlhgg lytpddglar avpacraqme rarargarfl
      181 drhtvtgier dgdrvaavvt drgtfpadhv vsaagfwgpv vgrmagvdvp llplahqyak
      241 tgplpgtagv tgpdaeasrp ilrfqdrdly frehadrigi gsyahrplpv dpftvpaydd
      301 aedmpssypf teedfapswe ecrwlmpslk eteieegfng vfsftpdgmp llgpsralrg
      361 fwlaeavwvt hsagvakava ewmvegrpsl dlheceltrf edaqrspayv aergarqfie
      421 vydvihplqp paeprplrvs pfharqqdlg avflegggwe rphwyeanap lakgievppr
      481 dawaachwsp iaaaearatr egvalydmtp lrrlevtgpg slaflqrmts nnlakkpgsv
      541 tytlllneag girsdltvar lapdrfqvga nspadldwll rhapddvqlr ditsgtccvg
      601 vwgplaralv qpltrddfsh eafgyfkake tyighvpvta mrlsyvgelg welyttadlg
      661 lrlwdtlwea grahgviaag rsafnslrle kgyrawghdm tsehnpyeag vgfavrmnkg
      721 efvgrsalee lgaptrrlta lllddpaavv lgkepvyvdg apvgyvtsas ygytlgrcva
      781 yawlppletg tgvhveyfge kvpatvavep lfdpemtrir r
//
LOCUS       WP_392142829             289 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: class II fructose-bisphosphate aldolase
            [Streptomyces].
ACCESSION   WP_392142829
VERSION     WP_392142829.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 289)
  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 289)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            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="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29604
     Region          2..282
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mplvstgelv eqaraaghgv aafnvitleh aeaialgaer agtpailqis enavrfhggr
       61 lsaiaaataa vahasparla lhldhvtdve llraahpegf gsvmfdaskl aygenvkata
      121 davrwgherg mwieaelgev ggkegeapld ahapgvrtdp aeaaayvadt gvdalavavg
      181 sthamterta sldheliasl aaavpvplvl hgssgvpdae irraiasgmv kinvgtalnt
      241 aftgevrayl kgdpkgvdpr kylvpaream agtvagflgl lkppredgr
//
LOCUS       WP_392143420             405 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC015345].
ACCESSION   WP_392143420
VERSION     WP_392143420.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015345
  ORGANISM  Streptomyces sp. NPDC015345
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 405)
  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 405)
  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
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 405)
  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   5  (residues 1 to 405)
  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   6  (residues 1 to 405)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 405)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 405)
  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 11973053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Streptomyces sp. NPDC015345"
                     /db_xref="taxon:3364953"
     Protein         1..405
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41126
     Region          <15..60
                     /region_name="COG3398"
                     /note="Predicted transcriptional regulator, contains two
                     HTH domains [Transcription]"
                     /db_xref="CDD:442625"
     Region          75..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 magtplgepg saqhivhlvs tgtassradl vrelglaast vslrvqelvd aglltesgeg
       61 asrggrrprl lrvaphggva vaadlgshha rlgvvdlggt vsdavdlphd itagpesavd
      121 wlcgqvdglv arqreegrtv ralgvafpgp vqpgtgrvls psrmpgwhry alrdvlaerl
      181 gfpvtvdnda tmmavgehrv arpgldhlvv vkagrgigsg visagrphdg angsagdish
      241 vrvdaagdrp cscgnigcle tvasgaalir elalhgvevs dtsdllrlva dgdprattlv
      301 rtagrhigtv lsvvvnffnp qavalggvla taeplvaavr gvlyerclpl atadleittt
      361 vtgvdagllg agltalrrhl pttpaalpgp gpdparapqe esapa
//
LOCUS       WP_392144022            1201 aa            linear   BCT 20-JAN-2025
DEFINITION  Rne/Rng family ribonuclease, partial [Streptomyces flaveolus].
ACCESSION   WP_392144022
VERSION     WP_392144022.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1201)
  AUTHORS   Kime,L., Jourdan,S.S. and McDowall,K.J.
  TITLE     Identifying and characterizing substrates of the RNase E/G family
            of enzymes
  JOURNAL   Methods Enzymol 447, 215-241 (2008)
   PUBMED   19161846
REFERENCE   2  (residues 1 to 1201)
  AUTHORS   Callaghan,A.J., Marcaida,M.J., Stead,J.A., McDowall,K.J.,
            Scott,W.G. and Luisi,B.F.
  TITLE     Structure of Escherichia coli RNase E catalytic domain and
            implications for RNA turnover
  JOURNAL   Nature 437 (7062), 1187-1191 (2005)
   PUBMED   16237448
REFERENCE   3  (residues 1 to 1201)
  AUTHORS   Li,Z., Pandit,S. and Deutscher,M.P.
  TITLE     RNase G (CafA protein) and RNase E are both required for the 5'
            maturation of 16S ribosomal RNA
  JOURNAL   EMBO J 18 (10), 2878-2885 (1999)
   PUBMED   10329633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..1201
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         <1..1201
                     /product="Rne/Rng family ribonuclease"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
     Region          418..828
                     /region_name="CafA"
                     /note="Ribonuclease G or E [Translation, ribosomal
                     structure and biogenesis]; COG1530"
                     /db_xref="CDD:441139"
ORIGIN      
        1 rrratrrvsa pagepaaaep aetttetgaa eaaaapetap aaapveeaae daaprrtrrr
       61 atrrvsapag epaaaepaet ttetgaaeaa paaeatpape aarsaepaap veeeaaprra
      121 rrrsarkaag gfaeparsaa asdeadapkr parpavavfq apvfaepkfq tperaaaeaa
      181 aeaaapepeq avreteapee fpeetagsrr rrrrraagpe ettedrtptr aaaeepeada
      241 eaeadepgdd hgddaegsee ygsrrrrrrg grrrrrgdla egsedsaddd daehtaaeqa
      301 aqdaedtaeq aeedaeeged atgenggsss srrrrrrrrr agdssgdaet saddpertvv
      361 kvreprpkae psdevqsikg strleakkqr rregreqgrr rvpiiteaef larreaverv
      421 mivrqhgert qigvledgvl vehyvnkeqa tsyvgnvylg kvqnvlpsme aafidigkgr
      481 navlyagevn feslgmghgp rriesalksg qsvlvqvtkd pighkgarlt sqvslpgryl
      541 vyvpegsmtg isrklpdter srlktilkri vpedagvivr taaegasede lrrdverlqa
      601 qweeiqkkak ngnaptllyg epdmtvrvvr difnedfskv vvsgddawqt ihgyvshvap
      661 dladrlskwt sevdvfatyr ideqlakald rkvwlpsggs lvidrteamv vvdvntgkft
      721 gqggnleetv trnnleaaee ivrqlrlrdl ggiividfid mvlesnrdlv lrrlleclgr
      781 drtkhqvaev tslglvqmtr krvgqglles fsetcvhcng rgvivhldqp ssagggggkr
      841 rkraragage hdheavagve tvptaeqead tesesevaae vaepvalpae ftpdeelyss
      901 aaeaeaaatr grgrrrasrr asapagapka akgeaarsea qvptaqdvtv aeeierpvvq
      961 etaaevlaep aavedalsga papaadeaap kgrtrrratr kvsapagspa gaeaavltvp
     1021 etaqaepapq apavaeapaa eeaapaaesa aparprrrav rkpttstase eaavvvvpsa
     1081 paeaeapaep eapaepeapa epeapaepev aeapavdasg deaapakkaa arktakkata
     1141 kkaatkktaa kktttakkat akkaakttta kkatakktas kktaaaeqaa pssvtaatde
     1201 g
//
LOCUS       WP_392144679             261 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015345].
ACCESSION   WP_392144679
VERSION     WP_392144679.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015345
  ORGANISM  Streptomyces sp. NPDC015345
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   4  (residues 1 to 261)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Streptomyces sp. NPDC015345"
                     /db_xref="taxon:3364953"
     Protein         1..261
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28908
     Region          4..56
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          79..256
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mkmlgaqvga lrraagltqr qlagrlvvde etvasieqgr rplkedlaaa leeivnargv
       61 ltaglenmpe vdlfprwaee ymdlereaia lswydnqvlp gvlqtdpyar avfsnevptl
      121 heddialrva armerqeilh rkapptasfv isevtvrdrl ggdevyfgql rhlreaadlp
      181 gvtlqimpig rdvhaglsgp ftlletpdhq riayveaqrg sqlvadpdev sllerkyaml
      241 rtqalnaqes kglldrllge q
//
LOCUS       WP_392144883             233 aa            linear   BCT 20-JAN-2025
DEFINITION  JAB domain-containing protein [Streptomyces flaveolus].
ACCESSION   WP_392144883
VERSION     WP_392144883.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Attaiech,L., Granadel,C., Claverys,J.P. and Martin,B.
  TITLE     RadC, a misleading name?
  JOURNAL   J Bacteriol 190 (16), 5729-5732 (2008)
   PUBMED   18556794
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Ambroggio,X.I., Rees,D.C. and Deshaies,R.J.
  TITLE     JAMM: a metalloprotease-like zinc site in the proteasome and
            signalosome
  JOURNAL   PLoS Biol 2 (1), E2 (2004)
   PUBMED   14737182
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449512
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         1..233
                     /product="JAB domain-containing protein"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=24278
     Region          12..227
                     /region_name="RadC"
                     /note="DNA repair protein RadC, contains a
                     helix-hairpin-helix DNA-binding motif [Replication,
                     recombination and repair]; COG2003"
                     /db_xref="CDD:441606"
ORIGIN      
        1 mtrsiepgli gmrmrevpaq drprerlldr gaealsdrel lalllgagla gqdavelagr
       61 liarhgglha lsrvpahela tglpgvgpak aarvaaafql grrvavqqap gmrrisgsad
      121 laavaspllr glrheravlv tcdgagavlr tsvltdgasd rtlvpvrdtl arvlalggaa
      181 fgvahnhptg rltpseadrl ttsrlmtgaq avglrfldhv vvtdsgwrrv ppd
//
LOCUS       WP_392146063             462 aa            linear   BCT 20-JAN-2025
DEFINITION  alpha,alpha-trehalose-phosphate synthase (UDP-forming)
            [Streptomyces flaveolus].
ACCESSION   WP_392146063
VERSION     WP_392146063.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 462)
  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 462)
  AUTHORS   Eastmond,P.J. and Graham,I.A.
  TITLE     Trehalose metabolism: a regulatory role for trehalose-6-phosphate?
  JOURNAL   Curr Opin Plant Biol 6 (3), 231-235 (2003)
   PUBMED   12753972
REFERENCE   3  (residues 1 to 462)
  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   4  (residues 1 to 462)
  AUTHORS   Elbein,A.D., Pan,Y.T., Pastuszak,I. and Carroll,D.
  TITLE     New insights on trehalose: a multifunctional molecule
  JOURNAL   Glycobiology 13 (4), 17R-27R (2003)
   PUBMED   12626396
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 929-939 (1997)
   PUBMED   9334165
  REMARK    Erratum:[Biochem J 1998 Feb 1;329(Pt 3):719]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         1..462
                     /product="alpha,alpha-trehalose-phosphate synthase
                     (UDP-forming)"
                     /EC_number="2.4.1.15"
                     /GO_function="GO:0003825 - alpha,alpha-trehalose-phosphate
                     synthase (UDP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0005992 - trehalose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50372
     Region          8..462
                     /region_name="OtsA"
                     /note="Trehalose-6-phosphate synthase, GT20 family
                     [Carbohydrate transport and metabolism]; COG0380"
                     /db_xref="CDD:440149"
ORIGIN      
        1 massfgaaqv lvasnrgpvs yevredgslh akrgggglvs glsaigpdad alwvcsalsd
       61 gdreavrrgv gedgvrmldv padvhadayn giansvlwfv hhmlyqtple pvfdaefrrq
      121 wasyeafnra faealaeeaa egavaivqdy hltlvpgmlr elrpdlrigh fshtpwapvd
      181 yfrmlpddia eqvlrgmlga drlgfltrrw adaftaccda lvgglggtei gvhglgadad
      241 flrkrshead vdermaalrd eigegrrtiv rvdrtelskn ivrgmlayrr lladrpewre
      301 rvvhvafayp srqdlavyrd ytaevqrvaq einaefgtag wtpvvlhvkd dfarslaayr
      361 ladvalvnpi rdgmnlvake vpvvsdegcv lvlsreagay eelgddalvv npydicgtad
      421 alhealsvpa geraerskrl saaatalppa rwfldqlaal rg
//
LOCUS       WP_392146177             817 aa            linear   BCT 20-JAN-2025
DEFINITION  GcvT family protein [Streptomyces flaveolus].
ACCESSION   WP_392146177
VERSION     WP_392146177.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 817)
  AUTHORS   Stauffer,L.T., Ghrist,A. and Stauffer,G.V.
  TITLE     The Escherichia coli gcvT gene encoding the T-protein of the
            glycine cleavage enzyme system
  JOURNAL   DNA Seq 3 (6), 339-346 (1993)
   PUBMED   8219277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         1..817
                     /product="GcvT family protein"
                     /calculated_mol_wt=88811
     Region          11..394
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
     Region          380..435
                     /region_name="FAO_M"
                     /note="FAD dependent oxidoreductase central domain;
                     pfam16350"
                     /db_xref="CDD:465100"
     Region          430..816
                     /region_name="GcvT"
                     /note="Glycine cleavage system protein T
                     (aminomethyltransferase) [Amino acid transport and
                     metabolism]; COG0404"
                     /db_xref="CDD:440173"
ORIGIN      
        1 msstpahgsp rvvvigagiv gcsladelta rgwtdvtvle qgplpapggs tshapglvfr
       61 tspsktltaf aqytvekfgt leadgvpcfl pvgglelatt perladlhrr aglaaswgvr
      121 gevvsaarck elwplidesv vlgglhtpdd glarallasr aqmdratarg arfldrhtvt
      181 gverrnghvt gvvtdrgtfp adhvvsaagf wgpvigrmag vdvplqplah qyaktgplpp
      241 lsgataeasr pilrfqdrdl yfrehtdrvg igsyahrplp vdpfavppyd earardldmp
      301 ssfpftpedw apswedcrrl lpalrdceid qgfngvfsft pdgmpllges rdlkgfwlae
      361 avwvthsagv akavaewmvd grpsldvhec eltrfeeaqr spayirergs qqfvevydvv
      421 hplqpmerpr plrvspfhar qqqlgacfle gggwerphwy eanaglvtgl dlperdawsa
      481 rhwspiaaae aratrdkval ydmtplrrle vtgpgaldfl drmttnnlrk kpgavtytll
      541 ldeaggirsd ltvarlgpdr fqvgantpad ldrllrhapd gvhvrditsg tccvgvwgpl
      601 ardlvqpltp ddfshgafgy fraketyvgh vpvtamrlsy vgelgwelyt tadlglrlwd
      661 tlweagrelg vvaagrsafn slrlekgyra wgvdmtgehn pfeaglgfav rmdkedftgk
      721 aalenagapa rrltpllldd paavvlgkep vyvdgspagy vtsasygytl grcvayawlp
      781 sglpsgtgvh veyfgekvla tvadeplfdp emtrirr
//
LOCUS       WP_392146921             192 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces sp.
            NPDC014872].
ACCESSION   WP_392146921
VERSION     WP_392146921.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014872
  ORGANISM  Streptomyces sp. NPDC014872
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Streptomyces sp. NPDC014872"
                     /db_xref="taxon:3364926"
     Protein         1..192
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=20396
     Region          44..>165
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mvrgrpsvnl rkslnpswpg rpaaprvavg vvgrlkgvsv atlfgilgti evrrdgvpvd
       61 aghavqrrvl aallvdaerv vsadalvdrv wgdagttsgr tklygyvsrp rqvlageaaa
      121 ltrergggyr lavepasvdv hrfrelsgla rkagtderae gapargprpv agqrvrrrgh
      181 slvqraarsp rr
//
LOCUS       WP_392146927             131 aa            linear   BCT 20-JAN-2025
DEFINITION  SRPBCC family protein [Streptomyces flaveolus].
ACCESSION   WP_392146927
VERSION     WP_392146927.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 131)
  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 10008053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         1..131
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=14200
     Region          15..123
                     /region_name="YndB"
                     /note="Chalcone/flavanone-binding protein YndB,
                     AHSA1/START/SRPBCC domain [Lipid transport and
                     metabolism]; COG3832"
                     /db_xref="CDD:443044"
ORIGIN      
        1 mptgltqdag wqigvsrtlp hppsvvwdfi sdaeglalwl gldtvlsper gtpyrtaegv
       61 tgevrgyhag kkirvthgtt tvqvalapaa egartmlrfh qehlagpeer errrthwqrv
      121 msrvaaaldg a
//
LOCUS       WP_392147903             317 aa            linear   BCT 20-JAN-2025
DEFINITION  quinone oxidoreductase family protein [Streptomyces flaveolus].
ACCESSION   WP_392147903
VERSION     WP_392147903.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 317)
  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 317)
  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 317)
  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   4  (residues 1 to 317)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         1..317
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=32399
     Region          1..297
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 mlaarlhtwn avpdlaetap vgppgdgevt veveaaavth ldltvmtgtf ahrpalpftp
       61 gtagagtvve ggaallgrrv lvrgggvgle rdgtwaerva vpagavreip rdadaalaat
      121 cyspmttawa aveavgriae gervlvtgaa gavgslcvql aaragahvva vvrnedaaga
      181 vpdaahevlv rpvaeevagk ggadvlldtv ggdtvpafle amrpggravl igyvagttlr
      241 velpalmard vtllpmnmvr rhvpaevfdr llrdltegrl tlrttalpfa riaeavetrr
      301 ggggrgtlav lmgdprr
//
LOCUS       WP_392147458             452 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces flaveolus].
ACCESSION   WP_392147458
VERSION     WP_392147458.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 452)
  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 452)
  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
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 452)
  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   5  (residues 1 to 452)
  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   6  (residues 1 to 452)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 452)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 452)
  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 20170230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         1..452
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=46854
     Region          1..112
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          82..402
                     /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 marasgrtvr dlrrenraav lqrlyfdgpm srvalgsaag lssgsvsnvv aellaeglve
       61 eagslgadgg rprtlvrias ghgrligvdv getrvrvelf dlsmaelart erplpghgtr
      121 sydvgvvagh ildgvaevld aagdgrgsgd llgvgvgvpg ivehtaggal vhgqtigwda
      181 vplerllrgs grlpthvplf idngaktlgq aemwfgggrg ahnavvvlfg sgvgacvvth
      241 dveqgravew ghltvrvrgr rcrcgargcl eayagaeall arwreaggrp psgtddeeta
      301 ltdllraahp pddrepdpva arvlaetaey lgaglsdlin lfqperilvg gwaglrlgsg
      361 fvdsvrthay ahalrhpagr vgitlgqlgp davtvgaavl plaaffargg hrapvdspaq
      421 ppawrtalgg rlagtgrrag rderpegrah vp
//
LOCUS       WP_392148380             257 aa            linear   BCT 20-JAN-2025
DEFINITION  quinone oxidoreductase family protein [Streptomyces sp.
            NPDC014872].
ACCESSION   WP_392148380
VERSION     WP_392148380.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014872
  ORGANISM  Streptomyces sp. NPDC014872
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 257)
  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 257)
  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 257)
  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   4  (residues 1 to 257)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Streptomyces sp. NPDC014872"
                     /db_xref="taxon:3364926"
     Protein         1..257
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=27072
     Region          <5..255
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 mtedgrriag lvqgggyaqk aavrnnqcwe ipdsvdddqa iavalqgnta yhllfsqlqi
       61 ranetvlipa aaggvgslav qlaaangtkv vamasteekr qlaldlgaka vvdssteedl
      121 aqritaaaqe angnrrdgin aalemtggsm fattldviqr ngrvatfgya sgiwpslkse
      181 dllqtllkks vtlsgfwlpn vdathqafst kslftmitrg qlqiinggty alsdaaqahr
      241 dlarrtvtgk lsldpsq
//
LOCUS       WP_392148353             449 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC014872].
ACCESSION   WP_392148353
VERSION     WP_392148353.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014872
  ORGANISM  Streptomyces sp. NPDC014872
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Streptomyces sp. NPDC014872"
                     /db_xref="taxon:3364926"
     Protein         1..449
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=46926
     Region          99..354
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mnpsgsnpls eaatgtrrrh vpnpqdqqan ansphtpllv vlgagsrtwr gyglqhiaar
       61 hpvalldhqp pawadahvav svavdltdae avadavatla adrgvagvlt ymenhvvlaa
      121 rltdrfalpg ntpaaveacr dkyltrslla aagvpsarsy lvadaetave yavllggpvv
      181 ikprslggsa gvhradtpdq vrdafhaakg aslfgiertg aagvlieeyl dgpevsvecv
      241 vlghgtvhia avtrkylgde pafqevghlv dptdplladl rirdvalgal tavgissgvm
      301 hvemrltrqg priveinarl ggdliphlvh latglnlpqi tadlavgvdp elvpsqsqsa
      361 avrflypavt ghvtavntgv faawldrfew taapgshvta ppratlldrt alavvtgpdp
      421 dtchrrlqlv eersgihiqa dtattacvv
//
LOCUS       WP_392148603             288 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptomyces flaveolus].
ACCESSION   WP_392148603
VERSION     WP_392148603.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 288)
  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 288)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 288)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 288)
  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   5  (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   6  (residues 1 to 288)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         1..288
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31897
     Region          19..102
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          126..284
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mlerlnqame hieshldqqi dvaelarvaw tseyhfrrmf salsgmplse yvrrrrltva
       61 gaevlagert lldvavrygy gsgeafaraf ralhgvgpge arrtgaalhs qprmsfrivv
      121 egssgmryri ldkkefrvvg rkarvplvhe gvnpsiaafv rgigpeplrr laalsdqepe
      181 gvvgvsdqld psraegteld yyhavvtgae apedmdvlev pagtwavfes sgpfpqalqy
      241 lwrdvytqwf psnpyrsrpg peilrvrvse dgaqadaevw ipveravg
//
LOCUS       WP_392148783             618 aa            linear   BCT 20-JAN-2025
DEFINITION  SWIM zinc finger family protein [Streptomyces sp. NPDC014872].
ACCESSION   WP_392148783
VERSION     WP_392148783.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014872
  ORGANISM  Streptomyces sp. NPDC014872
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 618)
  AUTHORS   Hassan,I.U., Rehman,H.M., Liu,Z., Zhou,L., Samma,M.K., Wang,C.,
            Rong,Z., Qi,X., Cai,D. and Zhao,H.
  TITLE     Genome-wide identification and spatiotemporal expression profiling
            of zinc finger SWIM domain-containing protein family genes
  JOURNAL   Zool Res 44 (3), 663-674 (2023)
   PUBMED   37161653
REFERENCE   2  (residues 1 to 618)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     SWIM, a novel Zn-chelating domain present in bacteria, archaea and
            eukaryotes
  JOURNAL   Trends Biochem Sci 27 (8), 384-386 (2002)
   PUBMED   12151216
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..618
                     /organism="Streptomyces sp. NPDC014872"
                     /db_xref="taxon:3364926"
     Protein         1..618
                     /product="SWIM zinc finger family protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=67000
     Region          71..577
                     /region_name="SWIM"
                     /note="Uncharacterized protein, contains SWIM-type Zn
                     finger domain [Function unknown]; COG4715"
                     /db_xref="CDD:443750"
ORIGIN      
        1 mvcpsasrng wlthvrgtgg pgravdtgcp aatdgplfrr iagpvrppvv gcvsitstrt
       61 gagvgrvakg lteanlrala gtrsfergtg yldavtgiev ggsgatatvh gteryevelt
      121 ldgprglsge cdcpyglegn fckhlvalgl sllarsaslp kqrkaarsra qtldawlsdl
      181 sreellelvr driaedrqfr rrlelrvass rgdlawarsr irelldigpf aqygyveyaa
      241 arayadqagq aasaigeltg sgraadaipl areairllag aaenvddsdg wlgqvgaala
      301 dahhdacraa dpdpeelahw lvehalhddg dftdidpldy edvlgeqgmt alrrhaveaw
      361 rsnrtgwaek ylmerlakag gdadmviavh aadlapdgst hltiareldt agrpaealew
      421 aergirdiee aadldaalvd yladrytqad rladavalrr dhfdahrtlp ayqhlraaaq
      481 aadgwppere ralallrada errpgshsvs vlvdallddk didaawqaat etgahdrqwl
      541 aladrpsdal dvylrlaepl trqtgnalye rlvglllsmr dchrrldtpd eftayvtalr
      601 ttqrrkrnlm rlmdehgl
//
LOCUS       WP_392149809             225 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces flaveolus].
ACCESSION   WP_392149809
VERSION     WP_392149809.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces flaveolus
  ORGANISM  Streptomyces flaveolus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Streptomyces flaveolus"
                     /db_xref="taxon:67297"
     Protein         1..225
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24106
     Region          2..223
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 mssrerilgr vrraladvph ddtppvperp grdpqygdav ardylrehgd rtvartvell
       61 aenladyrai vhrcaagdva atvtgllaar gartvlvppg ldpdwlagsg peripdrpes
      121 tpheldrvds vvtgcaiaia etgtivldgs pdqgrrritl vpdhhicvvr vpgqvvasvp
      181 qalerldpar pltwisgpsa tsdieldrve gvhgprtlev vlvte
//
LOCUS       WP_392150724             542 aa            linear   BCT 20-JAN-2025
DEFINITION  peptide ABC transporter substrate-binding protein [Streptomyces sp.
            NPDC015661].
ACCESSION   WP_392150724
VERSION     WP_392150724.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015661
  ORGANISM  Streptomyces sp. NPDC015661
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 542)
  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 542)
  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 542)
  AUTHORS   ter Beek,J., 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 542)
  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 542)
  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 11467924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Streptomyces sp. NPDC015661"
                     /db_xref="taxon:3364961"
     Protein         1..542
                     /product="peptide 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=58340
     Region          38..542
                     /region_name="OppA"
                     /note="ABC-type oligopeptide transport system, periplasmic
                     component [Amino acid transport and metabolism]; COG4166"
                     /db_xref="CDD:443327"
ORIGIN      
        1 mrgathakwa alatavalaa tacgggdsgg ggggaegivs sswgdpqnpl epantnevqg
       61 gkvlsmifrg lkqydpktge aknmlaekid ttdsqnftit vksgwtfsng ekvtaksfvd
      121 awnyaaqlkn nqknasffgq iegydqvhpe kgeataetms glkvtgdqtf tvkltqkfst
      181 wpdtlgyaaf splpqaffdd haawlskpvg ngpytidsys kgsqmalkkw daypgpdkaq
      241 nggitlkvyt dnntaytdlt agnldlvddv pasqlknvqa dlggryinvp agiiqtlsfp
      301 fydpawnkpg qeklrqglsm ainrqqitet ifqktrtpav dwtspvlgee ggykdicgdf
      361 ckydaeqakk lvaegggipg gtmtisynad tgshkewvda vcnsinnalg nnkacvgnpi
      421 gtfadfrsqv stqkmkgpfr agwqmdypli qnflqplyyt nassndgkys dpefdklvnq
      481 anaesdtaka vglfqqaegv lrddmgaipl wyqngsagys dkienvtlnp fsvpvydqik
      541 vk
//
LOCUS       WP_392150880             422 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC015661].
ACCESSION   WP_392150880
VERSION     WP_392150880.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015661
  ORGANISM  Streptomyces sp. NPDC015661
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces sp. NPDC015661"
                     /db_xref="taxon:3364961"
     Protein         1..422
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=44121
     Region          73..254
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          260..392
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mekrvmtvgk rrrslaaaaa vlggvlvlsa cndgdkggsa sgsatpqsqa qvdeaaaqkt
       61 skaqitispk ngaqnasinn dakvtvaegk ltevtmtsae gasvkgdiaa dglswkpseq
      121 lkratvykia atatdaegle ahenssfttv sqansfignf tpedgstvgv gmpvsinfnk
      181 aitdkkavqs gitvssssgq evvghwfnst rldfrpdayw tegstvtlkl dldgvegadg
      241 vfgvqqktvt ftigrnqvst vdvatktmtv kqdgktikti pisagspent tyngqmvise
      301 kfketrmnga tvgftdddgk geydikdvph amrlstsgtf ihgnywgars ifgsvntshg
      361 cvgladvkga gdpnqtaawl fdnsivgdvv ivknsndkti kpdnglngwn mswsewkags
      421 av
//
LOCUS       WP_392151492             277 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Streptomyces sp.
            NPDC015661].
ACCESSION   WP_392151492
VERSION     WP_392151492.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015661
  ORGANISM  Streptomyces sp. NPDC015661
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 277)
  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 277)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Streptomyces sp. NPDC015661"
                     /db_xref="taxon:3364961"
     Protein         1..277
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=28793
     Region          2..275
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mpltptdeiv rraraagtgv gafnvlqleh aqaivagaen adrpvvlqis entvryhgal
       61 epvalaslav araaktpvav hldhaenpdl vreavalglg svmfdasklp yaenvaatre
      121 vvehchshgv wveaelgevg gkggahtpgv rtdpeearaf vaatgvdala vavgsshqmv
      181 trdavldldl iarlraavdv plvlhgssgv sdphlaeait agmtkvnvst hlnkaftgav
      241 rthltehpdt vdprhyltpa raavarevth llavlap
//
LOCUS       WP_392151677             260 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Streptomyces sp.
            NPDC015661].
ACCESSION   WP_392151677
VERSION     WP_392151677.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015661
  ORGANISM  Streptomyces sp. NPDC015661
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 260)
  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 260)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Streptomyces sp. NPDC015661"
                     /db_xref="taxon:3364961"
     Protein         1..260
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26911
     Region          17..253
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 mtpesprtdg rgdhvvrvaa vgdihlgpdc agrlrpaflt lpacadllll agdltrhgtv
       61 dearvvadev rdvgvpvvav lgnhdyhsdq evevtrtlaa agvsvlegrs avfrvaghrv
      121 gvagakgfcg gfagrsagaf gepemrawvr vahvgaerls salqelaadg cavrvalthf
      181 apvpdtlage pveiypflgs yllaeaidsv gadlavhgha hlgtehgmta ggvrvrnvaq
      241 pvidrafaly elpvpghepd
//
LOCUS       WP_392151796             370 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            erythrochromogenes].
ACCESSION   WP_392151796
VERSION     WP_392151796.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces erythrochromogenes
  ORGANISM  Streptomyces erythrochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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   4  (residues 1 to 370)
  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 370)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Streptomyces erythrochromogenes"
                     /db_xref="taxon:285574"
     Protein         1..370
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38753
     Region          22..358
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 mnttpaapat pdtapasgpa gssvfsvngl wkvfgpdraa akvpgsadag lpaaelrert
       61 gctaavrdvs fdvrkgevfv vmglsgsgks tlvrcltrli eptagslsid gedvlamdat
      121 rlralrrhra amvfqhfgll phrtvldnva ygleiqgvgr gdrrtkaael iakvgldgle
      181 drrpgqlsgg qqqrvglara laadpevllf depfsaldpl irremqeeva rlhheegrtm
      241 vfithdlaea lrlgdrialm rdgrivqlgt peeivgspad dyvrdfvrdv preqvltvrt
      301 amrpaaagea eqgpalgpat tvveaiqava rsggparvvd ggrclgvvdd agllavvagl
      361 paptgrgvaa
//
LOCUS       WP_392152486             390 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Streptomyces sp. NPDC015661].
ACCESSION   WP_392152486
VERSION     WP_392152486.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015661
  ORGANISM  Streptomyces sp. NPDC015661
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 390)
  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 15739078
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Streptomyces sp. NPDC015661"
                     /db_xref="taxon:3364961"
     Protein         1..390
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=40974
     Region          55..233
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          237..342
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(313..314,317,332..335,337)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mlpirtsrpa lavvaltvsl tactaqaadg gpsgarvgas eappakvtvv kktagspvtv
       61 tatggtlrav rvvdadggvl kgrtdaggts wvsdrkavpg tsytievtsr tadgkestsr
      121 ssfatpepgk vnkltlapgk nttvgiahpl sivfdlpvtr kadvekqlkv ttsngtegsw
      181 gwvkdysgrd rvdwrpreyw kpgtkvtlea dldgtdsggg wfvrdyrtgf tvgaaqvvkv
      241 dldahrltlv rdgravrtip vsggtpggdk rswrgtavlm akegtinmns etvglgdayn
      301 kdvdysmrlt wsgmyahaap wnaayfgran hssgcigmsd enaaavyaav kvgdpfeitg
      361 retkgtvaeg ngygawnlnw pawksrsalh
//
LOCUS       WP_392153604             165 aa            linear   BCT 20-JAN-2025
DEFINITION  response regulator [Streptomyces erythrochromogenes].
ACCESSION   WP_392153604
VERSION     WP_392153604.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces erythrochromogenes
  ORGANISM  Streptomyces erythrochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 165)
  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 165)
  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 11467115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Streptomyces erythrochromogenes"
                     /db_xref="taxon:285574"
     Protein         1..165
                     /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=17627
     Region          31..>136
                     /region_name="PleD"
                     /note="Two-component response regulator, PleD family,
                     consists of two REC domains and a diguanylate cyclase
                     (GGDEF) domain [Signal transduction mechanisms,
                     Transcription]; COG3706"
                     /db_xref="CDD:442920"
ORIGIN      
        1 mgrphgveva ktrtrgpast ysrvvpgvsg rvlvvddnkv irqlikvnle legfevvtan
       61 dgaecldvvh rvcpdvitld vvmprldgfg aaaqlradpr trdvpvaivs acsqqeveag
      121 iaagvdafla kpfeptelvr vvrrlverkd rrdgrkgapa grgrg
//
LOCUS       WP_392154918             301 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Streptomyces sp. NPDC015661].
ACCESSION   WP_392154918
VERSION     WP_392154918.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015661
  ORGANISM  Streptomyces sp. NPDC015661
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Streptomyces sp. NPDC015661"
                     /db_xref="taxon:3364961"
     Protein         1..301
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32146
     Region          1..295
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mlldtaslyf rayfgvpdsv rapdgtpvna vrglldfitr lvqdhhpddl vacwdedwrp
       61 qwrvdlipsy kahrvavete tgpdveeipd tlspqvpvie evlaalgiar vgsagyeadd
      121 vigtlagrag gpvdivtgdr dlfqlvddar gvrvlyprkg vgdcdlvdae lirtkygvrp
      181 dqyadfaalr gdasdglpgv kgigektaaq liteygdlag vraaaedrts kltpakrrgi
      241 veaaayldva ptvvrvaada plpefdpalp aaprdpaale alvkrwnlgg avgrllpvle
      301 r
//
LOCUS       WP_392155301             403 aa            linear   BCT 20-JAN-2025
DEFINITION  threonine synthase [Streptomyces sp. NPDC015661].
ACCESSION   WP_392155301
VERSION     WP_392155301.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015661
  ORGANISM  Streptomyces sp. NPDC015661
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  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 403)
  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   3  (residues 1 to 403)
  AUTHORS   Parsot,C.
  TITLE     Evolution of biosynthetic pathways: a common ancestor for threonine
            synthase, threonine dehydratase and D-serine dehydratase
  JOURNAL   EMBO J 5 (11), 3013-3019 (1986)
   PUBMED   3098560
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423064
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces sp. NPDC015661"
                     /db_xref="taxon:3364961"
     Protein         1..403
                     /product="threonine synthase"
                     /EC_number="4.2.3.1"
                     /GO_function="GO:0004795 - threonine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009088 - threonine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=41971
     Region          80..397
                     /region_name="ThrC"
                     /note="Threonine synthase [Amino acid transport and
                     metabolism]; COG0498"
                     /db_xref="CDD:440264"
ORIGIN      
        1 mtaslavaqr sladpsvrhp lwppltrgcp vtstedvayp ldidyaydrv padlfkrpaa
       61 hglerwapll pplaapglge gntplvelad gvwikdesrn ptwshkdrln rvavsaavas
      121 gargivvsss gnhgaaaaay aaraglpcav ftspyappav ashlraygat vltvpyesvr
      181 plmrrivdel gfqsvssvtd tahtghpfgp egyktlayel aldlgrapae vhlptgygel
      241 lfgvakgfqe larlgvtdsv prvyaaepaa agaltealrt grpvarvpvg ptaayaidce
      301 vnsyrgvlav retggaaatv tddqmaaara elaaqgiwce tssaaglagl rargprqndg
      361 pvvcvvtssg ykdiataket feptapdwep ikaaltarea gpr
//
LOCUS       WP_392155632             307 aa            linear   BCT 20-JAN-2025
DEFINITION  quinone oxidoreductase family protein [Streptomyces sp.
            NPDC015661].
ACCESSION   WP_392155632
VERSION     WP_392155632.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015661
  ORGANISM  Streptomyces sp. NPDC015661
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 307)
  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 307)
  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 307)
  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   4  (residues 1 to 307)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces sp. NPDC015661"
                     /db_xref="taxon:3364961"
     Protein         1..307
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=31626
     Region          1..307
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 mrrvrhevtg gpevlfveev pvpepgpgel lvrseavgvt lpavrkvreg pepgplggev
       61 agtvaavgeg vtgfavgdrv tglcfshaya elavvheama sripdratav davalvrsgl
      121 vargayeagh prpgdavmvt aaasavgtla lqyaraggas rvvaavgsad kaefvralga
      181 devvlygdes wgdpvdlvid gvggellgpa vrvlapggrl vafssgggti dayellvrga
      241 svigfqmaai argkpevyar wrdelwelhr dkvlrprvaa eiplaeaara helvasrrnl
      301 gkvvlip
//
LOCUS       WP_392156956             415 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Streptomyces sp.
            NPDC015661].
ACCESSION   WP_392156956
VERSION     WP_392156956.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015661
  ORGANISM  Streptomyces sp. NPDC015661
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  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 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   3  (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   4  (residues 1 to 415)
  AUTHORS   Igarashi,K., Ito,K. and Kashiwagi,K.
  TITLE     Polyamine uptake systems in Escherichia coli
  JOURNAL   Res Microbiol 152 (3-4), 271-278 (2001)
   PUBMED   11421274
REFERENCE   5  (residues 1 to 415)
  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   6  (residues 1 to 415)
  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 11430824
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces sp. NPDC015661"
                     /db_xref="taxon:3364961"
     Protein         1..415
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0019808 - polyamine binding [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:0015846 - polyamine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44973
     Region          28..413
                     /region_name="PotD"
                     /note="Spermidine/putrescine-binding periplasmic protein
                     [Amino acid transport and metabolism]; COG0687"
                     /db_xref="CDD:440451"
ORIGIN      
        1 meqyepdsls aaqlaairrs mtsgrgalsr rsmlraggvg altvgglagl sacgippakr
       61 egngpasida sakeksvafs nwteymdvse deksrptlea fakrtgikvk ytedindnve
      121 ffgkikpqla agqdtgrdli cvtdwlaari irlgwaqkld panlpnayan lssqfrrpdw
      181 dpgrsysypw tgistviayn skatggkkvd svtqllddps lkgrvgflte mrdsvgmtll
      241 dmgkdpgnft dadydaaigr lqkgvdkkqi rrftgndyts dldkgdiaac lawagdiiql
      301 qadnpdikya ipsagyitss dnllvpaqar hktnaeklid yyyelpvaaq laayinyvcp
      361 vdgvkdeltk idpelanntl ilpdkamakk shafrslssa eetayeekfa kliga
//
LOCUS       WP_392156279             311 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Streptomyces sp. NPDC015661].
ACCESSION   WP_392156279
VERSION     WP_392156279.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015661
  ORGANISM  Streptomyces sp. NPDC015661
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Streptomyces sp. NPDC015661"
                     /db_xref="taxon:3364961"
     Protein         1..311
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32373
     Region          12..309
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mtplealara erlapgarva vvapsgpvpe erltagldil rgwglepvva phvlethpal
       61 gylagadrar ardlteawcd ptvsavlcar ggfgaqrmvd lvdwtairaa gpkvfvgysd
      121 vtalheafav ragfatlhgp mvaaatflsd prtreslrtt lfepedaltl gletaralvp
      181 grargvtlgg cvsllaadlg tphgrpsarg glllledvge epyrldrilt qllrsgwldg
      241 vagiglgswe ecgpyeavra vladrlgglg vpvleemgfg hsptaltlpl glpavldaet
      301 gtltleapal r
//
LOCUS       WP_392158544             131 aa            linear   BCT 20-JAN-2025
DEFINITION  TOBE domain-containing protein [Streptomyces sp. NPDC015661].
ACCESSION   WP_392158544
VERSION     WP_392158544.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015661
  ORGANISM  Streptomyces sp. NPDC015661
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 131)
  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 10007583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Streptomyces sp. NPDC015661"
                     /db_xref="taxon:3364961"
     Protein         1..131
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13909
     Region          1..128
                     /region_name="MopI"
                     /note="Molybdopterin-binding protein MopI [Coenzyme
                     transport and metabolism]; COG3585"
                     /db_xref="CDD:442804"
ORIGIN      
        1 mqsytigqaa rllgvspdta rrwadagrva thrdengrrl idgrdlaafs ievgqgsqgd
       61 ddepytsarn afpgivtavk lgdvaaqvei qagphrlvsl ltreaveelg levgmqatar
      121 vkstsvhidr t
//
LOCUS       WP_392158697             287 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces sp.
            NPDC015661].
ACCESSION   WP_392158697
VERSION     WP_392158697.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015661
  ORGANISM  Streptomyces sp. NPDC015661
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789410
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Streptomyces sp. NPDC015661"
                     /db_xref="taxon:3364961"
     Protein         1..287
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30929
     Region          4..248
                     /region_name="PrpB"
                     /note="2-Methylisocitrate lyase and related enzymes, PEP
                     mutase family [Carbohydrate transport and metabolism];
                     COG2513"
                     /db_xref="CDD:442003"
ORIGIN      
        1 msygsslrea vaapgttpli gvydmysasv aadhydgmfv sgfgfaasyy glpdigfiaw
       61 pdmvafvqrl rgafprhhll vdiddgyvdp evachvvegl erigasgvil edqkrprrcg
      121 hadgkqvlpl deylaklkmv latrrdmvvv artdatdead ilrraeclaa tdadvvlvdg
      181 vrsvewihri revvggkpll fnqiaggksp rlsldelsdl gvdvaiystp clfaaheamd
      241 salvelkran grlpsfdpet gvgvaastrl lerniarhqa apervga
//
LOCUS       WP_392159249             451 aa            linear   BCT 20-JAN-2025
DEFINITION  alpha,alpha-trehalose-phosphate synthase (UDP-forming)
            [Streptomyces sp. NPDC015661].
ACCESSION   WP_392159249
VERSION     WP_392159249.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015661
  ORGANISM  Streptomyces sp. NPDC015661
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 451)
  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 451)
  AUTHORS   Eastmond,P.J. and Graham,I.A.
  TITLE     Trehalose metabolism: a regulatory role for trehalose-6-phosphate?
  JOURNAL   Curr Opin Plant Biol 6 (3), 231-235 (2003)
   PUBMED   12753972
REFERENCE   3  (residues 1 to 451)
  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   4  (residues 1 to 451)
  AUTHORS   Elbein,A.D., Pan,Y.T., Pastuszak,I. and Carroll,D.
  TITLE     New insights on trehalose: a multifunctional molecule
  JOURNAL   Glycobiology 13 (4), 17R-27R (2003)
   PUBMED   12626396
REFERENCE   5  (residues 1 to 451)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 929-939 (1997)
   PUBMED   9334165
  REMARK    Erratum:[Biochem J 1998 Feb 1;329(Pt 3):719]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Streptomyces sp. NPDC015661"
                     /db_xref="taxon:3364961"
     Protein         1..451
                     /product="alpha,alpha-trehalose-phosphate synthase
                     (UDP-forming)"
                     /EC_number="2.4.1.15"
                     /GO_function="GO:0003825 - alpha,alpha-trehalose-phosphate
                     synthase (UDP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0005992 - trehalose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49855
     Region          1..450
                     /region_name="OtsA"
                     /note="Trehalose-6-phosphate synthase, GT20 family
                     [Carbohydrate transport and metabolism]; COG0380"
                     /db_xref="CDD:440149"
ORIGIN      
        1 matvlvasnr gpvsyvlged gsldarkggg glasalstid sreslwvcaa lgegdreavr
       61 rgtgepgvrm ldidpgvyad ayngiansvl wflhhhlydi prepvfdaef rrrwesyrsy
      121 nrafaealaa eaaeggavlv qdyhlalvpg qlrdlrpdlr iahfthtpwa spaylrmlpt
      181 direellrgm lgadrlgfht rawaeafeng agdpgrtrva ayplgvdadd lralayrpev
      241 ddrlarlree igdrktivrv drtelsknil rglqayrell tthpewrnrv vhlasaypsr
      301 qdlesyrayt aavkelaeei ntefgtadwq pvlvsvkddf trslaayrla dvalvnpvrd
      361 gmnlvakeip vvsesgcalv lstgagayee lkedaltvnp fdvtetaqal htaltmppte
      421 radrtkrlaa aatalppqrw fldqlealre r
//
LOCUS       WP_392160804             398 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces anulatus].
ACCESSION   WP_392160804
VERSION     WP_392160804.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 398)
  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 398)
  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 398)
  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 10611723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..398
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=40955
     Region          17..74
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(23,27,52)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(26,51)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(33..34,45,48,52..53)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          296..377
                     /region_name="DUF2690"
                     /note="Protein of unknown function (DUF2690); pfam10901"
                     /db_xref="CDD:402475"
ORIGIN      
        1 mprwkalpee ldpqirefas qlrrlvdrsg lninavadrt gysktswery lngrllaprg
       61 avvalaevtg tpqhhlttmw elaerawsra emrhdmtmea iritqaraal gelgttapda
      121 sagsrsgrss aggrhsasga rvpaaaspag tdapprdvhg kdpygggaye pgdddtrqll
      181 vptqrgtapn parhqdrayd ggsnrggqrp erntaestgp gsgrnvhgar pgrtpagrrk
      241 gpmlavgavg alivvvgall lapgddaaka tptpsvapte aapelpvgve csgadcagqd
      301 peamgcggef artvagavvg gskievryse vcaaswarlt eaaigdtvri tagegvqnge
      361 vmgdtdaytp mvavkkasda kacatltsgt kgctepge
//
LOCUS       WP_392161056             470 aa            linear   BCT 20-JAN-2025
DEFINITION  alpha,alpha-trehalose-phosphate synthase (UDP-forming)
            [Streptomyces anulatus].
ACCESSION   WP_392161056
VERSION     WP_392161056.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 470)
  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 470)
  AUTHORS   Eastmond,P.J. and Graham,I.A.
  TITLE     Trehalose metabolism: a regulatory role for trehalose-6-phosphate?
  JOURNAL   Curr Opin Plant Biol 6 (3), 231-235 (2003)
   PUBMED   12753972
REFERENCE   3  (residues 1 to 470)
  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   4  (residues 1 to 470)
  AUTHORS   Elbein,A.D., Pan,Y.T., Pastuszak,I. and Carroll,D.
  TITLE     New insights on trehalose: a multifunctional molecule
  JOURNAL   Glycobiology 13 (4), 17R-27R (2003)
   PUBMED   12626396
REFERENCE   5  (residues 1 to 470)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 929-939 (1997)
   PUBMED   9334165
  REMARK    Erratum:[Biochem J 1998 Feb 1;329(Pt 3):719]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..470
                     /product="alpha,alpha-trehalose-phosphate synthase
                     (UDP-forming)"
                     /EC_number="2.4.1.15"
                     /GO_function="GO:0003825 - alpha,alpha-trehalose-phosphate
                     synthase (UDP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0005992 - trehalose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51267
     Region          17..469
                     /region_name="OtsA"
                     /note="Trehalose-6-phosphate synthase, GT20 family
                     [Carbohydrate transport and metabolism]; COG0380"
                     /db_xref="CDD:440149"
ORIGIN      
        1 mvsehaepes gpaadstaqv lvasnrgpvs ytldeegtld akrgggglvs glsavddklw
       61 vcaalgdgdr eavrrgvgea gvrmldidag vhadayngia nsvlwfvhhl lyqtpvepvf
      121 daefrrqwas yetynrafae alaeeagpga svlvqdyhla lvpgmlrelr pdlrighfsh
      181 tpwapvdyfr llpddiaeql lrgilgadra afltrrwada figccteilg gtgrtrigvh
      241 glgadadflr rrsheadvde rmaalreqvg egrktivrvd rtelsknivr glhayralld
      301 arpewrervv hiafaypsrq dlavyrdyta avqalatein gaygteswtp vvlhvkddfa
      361 rslaayrlad valvnpirdg mnlvakevpv vsdhgcalvl sreagayeel gedaivvnpy
      421 dvvgtaealh ealtmsgder sgrtkrlaea atalppqrwf ldqlealrqg
//
LOCUS       WP_392162913             290 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ATP-grasp domain-containing protein [unclassified
            Streptomyces].
ACCESSION   WP_392162913
VERSION     WP_392162913.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415139
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..290
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=31231
     Region          1..289
                     /region_name="LysX"
                     /note="Glutathione synthase, LysX or RimK-type ligase,
                     ATP-grasp superfamily [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism,
                     Translation, ribosomal structure and biogenesis, Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0189"
                     /db_xref="CDD:439959"
ORIGIN      
        1 mprialatyd pgaepvrdtd lavlvralrd agaeaearfw ddpeadwggy dlvvirstwd
       61 yswraaefaa wvervgaltr lanpapvvrw ntdkrylgel aaagvptvpt ryiapgepag
      121 lpdghefvvk ptsgagarfa arytpgehdt avrqlarmha egftamvqpy vrgidvsger
      181 alqffggrll hasrkgavlt pgtpydadkv phpdlvpwqp tdaelavaeq alavvpggsg
      241 llyarvdlvd gedgeprlme lelvepnlfl wlhpaslprv teailaaaeg
//
LOCUS       WP_392161760             420 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [unclassified Streptomyces].
ACCESSION   WP_392161760
VERSION     WP_392161760.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 420)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..420
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=44927
     Region          55..241
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          246..368
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mnrlprtrtv vsctllvaal gagvtacgpd gnplsakpyd aadqisfngp teagkradpd
       61 kpleitaesg dgritdvtaq dstgrfvage laadgsrwhs tsplaanahy tvsvsteddd
      121 gapgrkvlef dtskptskkt lavtfgpdag eygvgqpita mlgqeikdka qravveralr
      181 vdsvpavqgs wywvsdkelh yrpkeywpeh atvqvhsnld gvrigdrlwg gkskalkitt
      241 gdkvevvtda aahqltyykn gkqveqipvt tgkpgfetrn gvkvvlekqy fvrmrgttvg
      301 iaegssdsyd lpvyyatrvt wsgeyvhaap wsvgsqgyan vshgctgmst snaewffdnv
      361 regdivkvvn sgghemepfg ngfgdwnvdw tkwrtgsalt agtsggptpg davrlrptav
//
LOCUS       WP_392163302             288 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptomyces sp.
            NPDC015684].
ACCESSION   WP_392163302
VERSION     WP_392163302.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015684
  ORGANISM  Streptomyces sp. NPDC015684
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 288)
  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 288)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 288)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 288)
  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   5  (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   6  (residues 1 to 288)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces sp. NPDC015684"
                     /db_xref="taxon:3364963"
     Protein         1..288
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31891
     Region          23..102
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          126..284
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mlerlnramd hiecrldgri egadlarial tseyhlrrlf salagmplse yvrrrrltva
       61 gaevlagdrt lleiavrygy tsgeafaraf ravhgvgpge arrsgarles qprlsfrltv
      121 egsssmryri vqkdefrvvg rkarvplvhl gvntaiaafv rglgpetler iqslsdqepq
      181 givavtdgld pgraegteld yyhgvvtraa aprdmdaltv pagswavfen sgpfpealqy
      241 lwrevfthwf psnpyqsrpg peilrtvlsp datradaelw ipvertpl
//
LOCUS       WP_392164557             320 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Streptomyces anulatus].
ACCESSION   WP_392164557
VERSION     WP_392164557.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..320
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=33126
     Region          14..318
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 miredrgpaa alarpprlrp gsrvavvaps gpvpadrlee glaflrdwgl epvvgahvst
       61 ehpeldylag adagraedle rawcdpsvea vlcarggyga hrmvdmvdwa avraagpkvf
      121 vgysditvlh ealalragfa tlhgpmvate aflkdaatre hlratlfape tvttlglesa
      181 galvpgrarg vlyggcvsll aadtgtpggr aharggllvi edtgeepyrl dgiltrllrs
      241 galdgvagva cgswqecgpy ekiravladr lgplgipvve elgfghgpta ltiplgvpai
      301 ldapadggrc tltveapalr
//
LOCUS       WP_392163414             457 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC015684].
ACCESSION   WP_392163414
VERSION     WP_392163414.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015684
  ORGANISM  Streptomyces sp. NPDC015684
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Streptomyces sp. NPDC015684"
                     /db_xref="taxon:3364963"
     Protein         1..457
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=47302
     Region          58..336
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mskvlyvhak ggppvghals rvaarsavhl lalselpatv aaeaarlcat avttpdadgv
       61 dlvdlitara revgaeavit fseyavvava eaarrlglkg pgpaatlard krlmraawer
      121 hgipqprfrg vrtvaeldaa greltyplll kaawsagsta hqiidspadl hgawarsgav
      181 mtesarlgfa elhvtgaged fiveeivsgc aeewfdgpgw gdyvsvegvv vdgvfqpvcl
      241 sgrmptiapf teragitpaa lggeaqdriv elarravaal glencgthte iklgaegrmw
      301 vietaarfgg amtvpqieev fgldlvgmft dqllgrspdw parvltpdda dgaagslvvl
      361 avngdgkawp qrhvwdasav vrsaplgpgs tlsvvaessl pdgtpvpvyd paagantmag
      421 lcllsadrpq svvrdfaalv dalphllaaa vggeara
//
LOCUS       WP_392164590             407 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [unclassified Streptomyces].
ACCESSION   WP_392164590
VERSION     WP_392164590.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..407
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43814
     Region          60..245
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          252..376
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mrhvqgrarr alaalaaavm wtgltagcsa dgsgplgigg slgkppaped virvtpddgs
       61 kavrpdgrlr vrvpggrlek vtvvrsqdaq dtpvpgrisg dgltwqpeea klalaakytv
      121 dvvaldsrgr rsarhttftt yvpdqrfigy vtpenrsvvg tgmivslafs reitdraave
      181 ravhvsarpp veirphwfgk drldfrpehy wkpgtevtvd ldlrdvegar gayglqdktf
      241 sftvgrsqvs lvdaakhtmd vrrdgqllat vpitagapkh ptyngkmvvm dmlevtrmns
      301 rtvgfggeyd ipdvphamkl tdsgtflhgn ywapdapgqv nvshgcvglm dvkggssdtp
      361 agwffdrslv gdvvevvhsk dktvspdngl ggwnmtwnvw kagsavk
//
LOCUS       WP_392165000             210 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces anulatus].
ACCESSION   WP_392165000
VERSION     WP_392165000.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..210
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22259
     Region          4..206
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 mniaretvlg rirdalalap apavvvprdy ctgralpdde rlalftdrll dykarvhpct
       61 adrtaevvgd vlrkhgvrri gvpagldarw larydgevrq ddadvphtql daldavvtas
      121 avgcaetgti fldgspgqgr ralslvpdlh lcvvdlsave vgvpeavarl aperpttlis
      181 gpsatsdiel ervegvhgpr tlavvirtda
//
LOCUS       WP_392165498             234 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Streptomyces anulatus].
ACCESSION   WP_392165498
VERSION     WP_392165498.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 234)
  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 10007985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..234
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24664
     Region          34..224
                     /region_name="COG3786"
                     /note="L,D-peptidoglycan transpeptidase YkuD,
                     ErfK/YbiS/YcfS/YnhG family [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443000"
ORIGIN      
        1 mrrslvtaav llalagslga gpasdvpplp drladtgggt qlitaeapdt gsttgtvtww
       61 errggrwtaa gsaparfgsn gltegttreq gtsttptgly dlpyafgiee apagttypyr
      121 kvnedswwcq dndsdaynrw veprpahcra aeaehlvsyg tqyaralvig fnyerpvrnr
      181 gagiflhvng rgatagcvsv padamaeila wadparephi avgtssgpta itry
//
LOCUS       WP_392166094             156 aa            linear   BCT 20-JAN-2025
DEFINITION  SRPBCC family protein [Streptomyces anulatus].
ACCESSION   WP_392166094
VERSION     WP_392166094.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 156)
  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 10008053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..156
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=16623
     Region          17..141
                     /region_name="YndB"
                     /note="Chalcone/flavanone-binding protein YndB,
                     AHSA1/START/SRPBCC domain [Lipid transport and
                     metabolism]; COG3832"
                     /db_xref="CDD:443044"
ORIGIN      
        1 msttdengtp qdavqvpdil hstlvraapd vvfdllssgt gwdkwftngs tfgpsegspv
       61 hlvwrgwtdd gsdvtddgvv mecvpnerfa ftwgtppslv tfttaehpdg twltvvetgl
      121 pqtaaglarf gecapgwgea ltlvrcyaeh girlst
//
LOCUS       WP_392165627             396 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces anulatus].
ACCESSION   WP_392165627
VERSION     WP_392165627.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 396)
  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   5  (residues 1 to 396)
  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   6  (residues 1 to 396)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 396)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 396)
  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 19786117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..396
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39717
     Region          13..>59
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
     Region          76..385
                     /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 mpaspstara indrlalrll qqdgpltatq lktltglsrp tvadlverlq gagliqvvge
       61 sgavrrgpna klygivadra hlaaldvrlg svsvvvtdll gatlaegslp igsdtgtepa
      121 vegaaaller taraagtvpl hsvgvgapgl idpvtgelrd stglpawhrg lvrelqrrlp
      181 atvlvenetn laavaehrag aardqetfvl lwlgqgigaa vmldgklrqg asggageigf
      241 lpvpgvsglp savncdggfh slagsaalce laaahglldp gavadgreea aavdavrtal
      301 etgeagepfl keladrlalg aaavvsvldp gcvllagavg haggaelaar veerlvtmsp
      361 lrtevragsl gdgavlrgal itardaaqda lfapeg
//
LOCUS       WP_392166737             515 aa            linear   BCT 20-JAN-2025
DEFINITION  sodium:solute symporter family protein [Streptomyces anulatus].
ACCESSION   WP_392166737
VERSION     WP_392166737.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Henriquez,T., Wirtz,L., Su,D. and Jung,H.
  TITLE     Prokaryotic Solute/Sodium Symporters: Versatile Functions and
            Mechanisms of a Transporter Family
  JOURNAL   Int J Mol Sci 22 (4), 1880 (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Wright,E.M. and Turk,E.
  TITLE     The sodium/glucose cotransport family SLC5
  JOURNAL   Pflugers Arch 447 (5), 510-518 (2004)
   PUBMED   12748858
  REMARK    Erratum:[Pflugers Arch. 2004 Feb;447(5):813-5]
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Jung,H.
  TITLE     The sodium/substrate symporter family: structural and functional
            features
  JOURNAL   FEBS Lett 529 (1), 73-77 (2002)
   PUBMED   12354616
REFERENCE   4  (residues 1 to 515)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001756
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..515
                     /product="sodium:solute symporter family protein"
                     /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=53792
     Region          36..435
                     /region_name="PutP"
                     /note="Na+/proline symporter [Amino acid transport and
                     metabolism]; COG0591"
                     /db_xref="CDD:440356"
ORIGIN      
        1 mnavvatsvf avfmvaaval gllalrgrgk gggltewsvg grslgpvfiw vlmagegyts
       61 fsylgaagwg ynygapvlyv vaymscgyai gyvvgpmlwg yarrhglvgi tdmvahrfgr
      121 pwlgavvavl atvfllpyiq lqitgmgvvl svisygavsl nwayfvafav ttgfvvvsgl
      181 rgsawvsvlk dvlviatlgf lafyvplhyf dgygpfldrl vteksdwltl pghggggsgg
      241 sglgelwfis ttflnsltvv ifpttvagyl garnadalrr namylpaynv llfvpmllgl
      301 aalfvvpgla gaesnlalfk lvvdslpawv vgvigvaagl ssivpmavfm lvigtmwgrs
      361 vlslvprlae rqksaaqvvv vvagglalll tytapntlvr lslisyegma qllpmvllal
      421 vwrrltfrga fsglivgvav vcvlvfsgnd plggvnaglv alaanlaval avtfagprda
      481 dprpdaevla hdpvgeegdp pavtraarsa sdhrv
//
LOCUS       WP_392167438             278 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces anulatus].
ACCESSION   WP_392167438
VERSION     WP_392167438.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 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   4  (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 18542080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..278
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31350
     Region          17..70
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
     Region          93..263
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mqpgthsirr vtswqligaq lrhfrklagl tqasladqlg vgedtiasie qgrralqldl
       61 avqldelldt kgalkvaver vpkkeryqal vkdfvqyeqg avslfsyesq lipgllqtet
      121 yarlvfsshy ppleeeviee rvatrlnrqk ilerkprpil hfileesily aelgdpevmr
      181 eqllhlrrcm dlpfvsiqim prktprhagl agplvlletp dhdqlayvem hlraelyddp
      241 advsalmqky gmlrtqalta eesarlldal laallget
//
LOCUS       WP_392167740             314 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces anulatus].
ACCESSION   WP_392167740
VERSION     WP_392167740.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 314)
  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 314)
  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 314)
  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 18542080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..314
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34699
     Region          11..>59
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
     Region          90..266
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 makaidpqss maalfgsrlr klrvaagltq aevgvlahvv ssriaqlera tgakptlelt
       61 rvldkelvad ellidlwpyv yreafpdwsr afiaysaraa vireyashav pgllqtpqya
      121 rallsvghtl rddehleerl aarldrqvrl tgpdrpelwi ildeavlrrp vggaavmrgq
      181 lekllrmaee pnvtiqvlpf dqgahgslgg sltvlvmpdg sevaytegah ygqlteepde
      241 verfvltydq lramalpplm slalirsvle adyraasvps rsdrrrlaqq qlqqpggrql
      301 rtgggriprr rprp
//
LOCUS       WP_392168406             253 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Streptomyces].
ACCESSION   WP_392168406
VERSION     WP_392168406.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   2  (residues 1 to 253)
  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 253)
  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 253)
  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 10611723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..253
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26234
     Region          18..75
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(19,23,48)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(22,47)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(29..30,41,44,48..49)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          144..227
                     /region_name="DUF2690"
                     /note="Protein of unknown function (DUF2690); pfam10901"
                     /db_xref="CDD:402475"
ORIGIN      
        1 mghpqrsttp dehltaglre lrdrtglsla alaartpysk sawhrylsga qrpprpavea
       61 lcrlaggdpe avlplwdaad arpsaspppp pgpnrrrtwl pvsavvlcga aaalgatlgl
      121 sggpgtapaa qtlpavsrcq gracqgelpd asvcardaqt rssvdargyt vrlrwspacg
      181 tawsevrvrs prarevsvra gqdvfsasys ardtgghssp mlsvrsprgv eacaeadgkv
      241 actgldadle eqg
//
LOCUS       WP_392168992             306 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 5'-3' exonuclease [unclassified Streptomyces].
ACCESSION   WP_392168992
VERSION     WP_392168992.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..306
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32752
     Region          1..300
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mtgrlmlldt aslyfrayfg vpdsvkapdg tpvnavrgll dfidrlvkdh rpdrlvacmd
       61 adwrpqwrvd liptykahrv aeeheggpde eevpdtlspq vpviedvlda igiarvgvag
      121 yeaddvigtf tahadgpvdi vtgdrdlyql vddgrgirvl ypvkgvgtlq ltdeavlrek
      181 ygvdgrgyad lallrgdpsd glpgvagige ktaakllaef gdlagimaav ddprakltps
      241 qrkrlteagp yvavapkvvr vagdvplpdv dtalphtprd paaledlakr wglggslqrl
      301 ldtlae
//
LOCUS       WP_392169080             234 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase family protein [unclassified
            Streptomyces].
ACCESSION   WP_392169080
VERSION     WP_392169080.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 234)
  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 10007985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..234
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24550
     Region          34..224
                     /region_name="COG3786"
                     /note="L,D-peptidoglycan transpeptidase YkuD,
                     ErfK/YbiS/YcfS/YnhG family [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443000"
ORIGIN      
        1 mrpgvvlalv svsslgllgl raapepaalp arladtgggt qlitaqaadt gatsgtvaww
       61 dlrdgqwaqa gsaparfgan glveggarkq gtnttptgly dlpfafgtka apegthvtyr
      121 pvldsswwcq dndsdaynrw vdplpadcra aesehlvsyp tqyayglvig fnydrpvrgr
      181 gagiflhvng raatagcvsv pedamrrilq waepgrkphv aigtdggdta itry
//
LOCUS       WP_392169104             273 aa            linear   BCT 20-JAN-2025
DEFINITION  S1 family peptidase [Streptomyces anulatus].
ACCESSION   WP_392169104
VERSION     WP_392169104.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces anulatus
  ORGANISM  Streptomyces anulatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Querino Lima Afonso,M., da Fonseca,N.J. Jr., de Oliveira,L.C.,
            Lobo,F.P. and Bleicher,L.
  TITLE     Coevolved Positions Represent Key Functional Properties in the
            Trypsin-Like Serine Proteases Protein Family
  JOURNAL   J Chem Inf Model 60 (2), 1060-1068 (2020)
   PUBMED   31895561
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Waldner,B.J., Kraml,J., Kahler,U., Spinn,A., Schauperl,M.,
            Podewitz,M., Fuchs,J.E., Cruciani,G. and Liedl,K.R.
  TITLE     Electrostatic recognition in substrate binding to serine proteases
  JOURNAL   J Mol Recognit 31 (10), e2727 (2018)
   PUBMED   29785722
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Pelc,L.A., Chen,Z., Gohara,D.W., Vogt,A.D., Pozzi,N. and Di Cera,E.
  TITLE     Why Ser and not Thr brokers catalysis in the trypsin fold
  JOURNAL   Biochemistry 54 (7), 1457-1464 (2015)
   PUBMED   25664608
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Perona,J.J. and Craik,C.S.
  TITLE     Evolutionary divergence of substrate specificity within the
            chymotrypsin-like serine protease fold
  JOURNAL   J Biol Chem 272 (48), 29987-29990 (1997)
   PUBMED   9374470
REFERENCE   5  (residues 1 to 273)
  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 10595581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Streptomyces anulatus"
                     /db_xref="taxon:1892"
     Protein         1..273
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=29919
     Region          37..199
                     /region_name="Trypsin_2"
                     /note="Trypsin-like peptidase domain; pfam13365"
                     /db_xref="CDD:433149"
ORIGIN      
        1 msntnegktp hlgfyqlysp cllcvetcdk ngepgvgtaf higdgylvta rhvvegrrlt
       61 slipardgsv sidsveviyp sdptvdlall ktdfsldhym knvhfwgrdd vrkvdhleig
      121 ghlndwiddg lvlmrvvafg yppiptsprs elvavrgevn aiidpyvgsk hplfvispma
      181 rggfsggpvl tedgwllgvv tsslltdhat pelgygaalt veplwdllve nrifpasnad
      241 vlfelrhgws lnegdfpfda nklqrlkene kra
//
LOCUS       WP_392169395             139 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TOBE domain-containing protein [unclassified
            Streptomyces].
ACCESSION   WP_392169395
VERSION     WP_392169395.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 139)
  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 10007583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..139
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=14066
     Region          1..138
                     /region_name="MopI"
                     /note="Molybdopterin-binding protein MopI [Coenzyme
                     transport and metabolism]; COG3585"
                     /db_xref="CDD:442804"
ORIGIN      
        1 mtlsirnqlp gtvtevrpge vmatvkvrlt ggqnltaait leaveelgla pgsevralvk
       61 stevalatsr teglsirnqv pgtvtqlllg evmatvkvsm pggeltaait kdaagdlglf
      121 vgsdvialik stevalata
//
LOCUS       WP_392169499             353 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces sp. NPDC015684].
ACCESSION   WP_392169499
VERSION     WP_392169499.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015684
  ORGANISM  Streptomyces sp. NPDC015684
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Streptomyces sp. NPDC015684"
                     /db_xref="taxon:3364963"
     Protein         1..353
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=35274
     Region          79..352
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mssvsplppl gpaaappcpg pgtaagplvp gsgacaparp ssplygrpar lalclapvll
       61 aggwavtnrp vlyegvrrll aadpwwllag agltclnwva aacvrqgalp dplppgrlla
      121 sqfaagaanh vlpgalgaha vtlrflrarg vpldratasi glyslakssa ktlvllvfla
      181 vspasrrlgd lvpdgrllvp aaavtggvla iagvlltvvr plrrpvtgll rsaladarav
      241 harpcrvaal wggavamplv qastlacvgt slglglpweq valahlaagt aggavpapgg
      301 lavdaalvwt livfgaappm atatvigfrv ltdwlpllpg altlsamfrg ral
//
LOCUS       WP_392170413             403 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC015684].
ACCESSION   WP_392170413
VERSION     WP_392170413.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015684
  ORGANISM  Streptomyces sp. NPDC015684
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces sp. NPDC015684"
                     /db_xref="taxon:3364963"
     Protein         1..403
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=42844
     Region          53..307
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mtllligags qayrayllrs vaeeydihll adreptwetp ylsghtvldt tdvaamreaa
       61 ralpcegvlt wddtrvvqta rlaadlglpg tppeaalrcr dkratreald ragvpqarsi
      121 lvttlpqara aaarvgyplv lkpralnast gvvkvgsadv lprsfrlara atapgaqeva
      181 pgdvlveeyl dgpevsvdaa whegrmtpaf varkecgfap yfeetghlvd ggdpllsdpr
      241 llevvqaaht avgfttgwth telrltargp kiveinartg gdripdigrl algvdaarta
      301 aqvacgrlpq ltarhhrvaa vrflypetdc iardvriepg alpgsvdsae aialpgqelr
      361 lppnghvsgr yalitvages aeqcradldk aseavalevl ral
//
LOCUS       WP_392170984             248 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: metallophosphoesterase family protein [unclassified
            Streptomyces].
ACCESSION   WP_392170984
VERSION     WP_392170984.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 248)
  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 248)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..248
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25653
     Region          3..230
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 mirvaavgdi hmapesqgtl rpsfdtlpec advlllagdl trhgtpeeaa vvareiegla
       61 vpvvavlgnh dhhderpeev tailrdagah vlegeavvvt aggarigvag tkgfgggfvg
      121 rcagefgepl mkefvrytrr sadalhgalk dlggrdcdvr ialthfapvp dtlageplei
      181 ypflgsylla eaidtggadl avhghahagt ehgmtsggvr vrnvaqpvig qafhvyhlpg
      241 gpdpqqga
//
LOCUS       WP_392174504             132 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TOBE domain-containing protein [unclassified
            Streptomyces].
ACCESSION   WP_392174504
VERSION     WP_392174504.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 132)
  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 10007583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..132
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13893
     Region          1..129
                     /region_name="MopI"
                     /note="Molybdopterin-binding protein MopI [Coenzyme
                     transport and metabolism]; COG3585"
                     /db_xref="CDD:442804"
ORIGIN      
        1 mqsytigqaa rllgvspdta rrwadagrva thrdeggrrl idgrdlaafs veiaqgggtg
       61 deeqpytsar nafpgivtav klgdvaaqve iqagphrlvs lltreaveel glevgmqata
      121 rvkstsvhid rt
//
LOCUS       WP_392173867             217 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LutC/YkgG family protein [unclassified Streptomyces].
ACCESSION   WP_392173867
VERSION     WP_392173867.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..217
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22945
     Region          7..215
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 msrphpssrd lvlgriraav agapeapepe rtylrqhapd dpaalvdllh enladyravv
       61 hrtdpaglpg lvarllaghr aasvvvppgl pqewlsevpr dvqlhpdrge ltarqldatd
      121 aavtgcavav aetgtlvlda gpaqgrralt lvpdvhlcvv rvpdqvvasv plalprldpr
      181 rpltwisgps atsdieldrv egvhgprrld vlllgdg
//
LOCUS       WP_392172413             312 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: quinone oxidoreductase family protein [unclassified
            Streptomyces].
ACCESSION   WP_392172413
VERSION     WP_392172413.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 312)
  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 312)
  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 312)
  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   4  (residues 1 to 312)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..312
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=31334
     Region          1..312
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 mrrvrhtvng gpevlfvedv pvpepgtgel lvrveavgvs lagvrrvrgg epgplggeva
       61 gtvealgpdt agsgfavger vtgicfghgy aelalvhtam asrvpdgasa vdavslvrsg
      121 lvargaldaa rlrpgesvlv tgaasgvgql avplarllga grvvaaagsp gkaaflrglg
      181 adevvgygpe dagrswgepv dvvldavggd llpralaala pggrlvafss gggtvpahdl
      241 lagatsvigf qmahlartrp rdhaawrdel wslhaagrla pavharvpla raaeahaiie
      301 rrenlgkvvl vp
//
LOCUS       WP_392174817             239 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ribonuclease H family protein [unclassified
            Streptomyces].
ACCESSION   WP_392174817
VERSION     WP_392174817.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 239)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..239
                     /product="ribonuclease H family protein"
                     /EC_number="3.1.26.4"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=24837
     Region          4..141
                     /region_name="RNase_HI_prokaryote_like"
                     /note="RNase HI family found mainly in prokaryotes;
                     cd09278"
                     /db_xref="CDD:260010"
     Site            order(10..13,45..47,50,72,122)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260010"
ORIGIN      
        1 mtdkiiaacd gaskgnpgpa awawvigted geiahweagp lgtatnnvae ltallrller
       61 idpavpaevr mdsqyamkav ttwlpgwrrk gwktsagtpv ankdlvvrid elltdrrvef
      121 vytpahqvdg dplndaadra ashtarsqlp agsaagselp ppepasarpa aakrprkatg
      181 asgparagtr sgtrsgssap slkarfpgrc rcgqayakgd titknadgwg hpacaeavs
//
LOCUS       WP_392175483             260 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: metallophosphoesterase family protein [unclassified
            Streptomyces].
ACCESSION   WP_392175483
VERSION     WP_392175483.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 260)
  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 260)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..260
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26894
     Region          17..253
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 mtpasartdg hadhavrvaa vgdihlgpdc agrlrpaflt lperadvlll agdltrhgtv
       61 dearvvaeev rdvgvpvvav lgnhdyhsdr aeevtrtlad agvtvlegds avfpagghri
      121 gvagakgfcg gfagrsagaf gepemrawvk vahvaaerls salrelaedg cevrvalthf
      181 apvpdtlage pveiypflgs yllaeaidsv gadlavhgha hlgtehgmta ggvrvrnvaq
      241 pvidrafaly elpvpgheaa
//
LOCUS       WP_392176547             418 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [unclassified Streptomyces].
ACCESSION   WP_392176547
VERSION     WP_392176547.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 418)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..418
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=44596
     Region          55..239
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          244..366
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mndtprirtv lsctllaltv tagatacagg eahplsarpy daadqvafna pgdgkkadpe
       61 kpleitatde dgritdvrat deagrhlage ltadgrkwrs tvalaagary tvqvsteded
      121 gapgartfsf etapakralt vafgpeagty gvgqpvtael slpvkdraar avveralkvr
      181 svpavegswy wvddkklhfr pkeywptgat vtvtgnldgi kvgdklyggp skplkitigd
      241 rieavadads hhmtvrrnge vintipvttg kpgfstrngi kvvlgkeyyv rmrgtsigia
      301 egssesydlp vyyatrvtws geyvhaapws vgsqgvanvs hgcvgmstdn aawfyenvrp
      361 gdivrvvnse gemmdpfgng fgdwnldwak wrqgsalvae kgdptateda karlrpsi
//
LOCUS       WP_392176813             245 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TerD family protein [unclassified Streptomyces].
ACCESSION   WP_392176813
VERSION     WP_392176813.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            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 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..245
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=27209
     Region          <14..242
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mgffdnlfpg rgdpfdaggs aagsidltrr rpsvsltqqg aatgnlrvnl swrmrssdie
       61 arprgsssll rhplrlfkpe evqahtqgmv nvdldlgcly eladgskgvv qplggffgel
      121 neppyvklsg ddrfgapsge tifvnldhrd eikrllffvy iydqtpafdr thakatlyps
      181 ngprieield ehapqarsca ifslentkge lvvrrevrfv ygfqaeldrl ygwglqwgrg
      241 dkskt
//
LOCUS       WP_392177175             423 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [unclassified Streptomyces].
ACCESSION   WP_392177175
VERSION     WP_392177175.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 423)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..423
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=44372
     Region          74..255
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          261..393
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mekrvmtdgk rrkglaaaaa vlggvlvlsa cndgdkggsa adasqsgqsq aqvdeaaaqk
       61 tskaqititp kngaqnasin ddakvtvtdg kltevtmtsa egktvageia adglswkpsg
      121 qlergtvyki satakdaegl eahentsftt vskansfign ftpedgstvg vgmpvsinfn
      181 kgitdkkavq sgisvtsssg qevvghwfns trldfrpqsy wtegstvtlk ldldgvegad
      241 gvygvqkktv tfkigrnqvs tvdvktktmt vtrdgrtvkt ipisagspdn ttyngqmvis
      301 ekfketrmng atvgftdddg kgeydikdvp hamrlstsgt fihgnywgar sifgsvntsh
      361 gcvgladvkg agdpnqqaaw fydnsiigdv vivknsadkv iapdnglngw nmsweqwkag
      421 sav
//
LOCUS       WP_392178124             392 aa            linear   BCT 20-JAN-2025
DEFINITION  M20 metallopeptidase family protein [Streptomyces sp. NPDC015532].
ACCESSION   WP_392178124
VERSION     WP_392178124.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015532
  ORGANISM  Streptomyces sp. NPDC015532
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Lindner,H.A., Lunin,V.V., Alary,A., Hecker,R., Cygler,M. and
            Menard,R.
  TITLE     Essential roles of zinc ligation and enzyme dimerization for
            catalysis in the aminoacylase-1/M20 family
  JOURNAL   J Biol Chem 278 (45), 44496-44504 (2003)
   PUBMED   12933810
REFERENCE   2  (residues 1 to 392)
  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 11444961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Streptomyces sp. NPDC015532"
                     /db_xref="taxon:3364960"
     Protein         1..392
                     /product="M20 metallopeptidase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41687
     Region          17..375
                     /region_name="AbgB"
                     /note="Metal-dependent
                     amidase/aminoacylase/carboxypeptidase [General function
                     prediction only]; COG1473"
                     /db_xref="CDD:441082"
ORIGIN      
        1 mkqaavaaea arvdrvliql rrdfhqhpea pgqeqrtaav varelraagl dvttgvgghg
       61 vvgvlrgsrp grtvayradm davppqdivg ggpapahlcg hdihttvgig aarvlarlrr
      121 qlsgaavflf qpaeetlsga ralidsgvle rehveeihal hcgpfpvgrf avtpgygmpg
      181 qdkaeialsg pdaldaarrl avdigalatv alprtpadle riiaaaqvpd gplarfvalr
      241 asaqeakvsv syrcwpqery aevresirra atpyagagvr fpaepfpavv cperdarlla
      301 rhlrrtvgqd rvielraafp pfsgedfalf ldripgtytf lgvhapgtpi tagyphypdf
      361 spderaigvg vramagwiae rthraqglpg ra
//
LOCUS       WP_392179022             431 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC015532].
ACCESSION   WP_392179022
VERSION     WP_392179022.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015532
  ORGANISM  Streptomyces sp. NPDC015532
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 431)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Streptomyces sp. NPDC015532"
                     /db_xref="taxon:3364960"
     Protein         1..431
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=44678
     Region          91..268
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          274..401
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mgvpeianrp esaprdpgrv rrspgrpaws rrgilaalga avpalalsgc ggpagategk
       61 datptgaaga gatakaqvkt ptvtvspadg tkradftapv vvsvadgtls svevsgndgs
      121 tlagsfddgr trwtsagnpy sgtkytvtak aegaaehtat fvtrspgetf agyftpeans
      181 tsgvgmpvsi nftqavkdra avekaitvta epavevvghw fgntrldfrp arywaagtki
      241 tlslrlrdve gtdgvygvqs kdvtfhigrr qvstvdlakk tmtverdgva lagypvsgga
      301 adhttwsgim viserfketr messtvglgd eydiadvpha qrlttsgtfi hgnywaaasv
      361 fggsntshgc vglhdtkgan dssvpgyrfy essmlgdvvv vensgertve psnglngwnl
      421 swadwkagsa l
//
LOCUS       WP_392178730             287 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces sp.
            NPDC015532].
ACCESSION   WP_392178730
VERSION     WP_392178730.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015532
  ORGANISM  Streptomyces sp. NPDC015532
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Streptomyces sp. NPDC015532"
                     /db_xref="taxon:3364960"
     Protein         1..287
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=30719
     Region          1..259
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mdidvlgald vrengvsiap tapkprqvla llavhadrvv pvaslieelw sgrpprsart
       61 tlqtyvlqlr eligaalerg ggqrsaagpe rrtakdvlvt lpggyllaaa ggtsdvrefd
      121 rlaglgyram dagdfagasr slaaalglws gsaladvqtg aqlamearrl degrlcaldq
      181 rieadlrlgr hrevlaeltv ltsryrshen lhaqfmialh rsgrrgealn aythlrttlg
      241 rdlglepspr lrrlqhsill dapettpapt aravhrpdaa aravagr
//
LOCUS       WP_392179129             278 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces sp.
            NPDC015532].
ACCESSION   WP_392179129
VERSION     WP_392179129.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015532
  ORGANISM  Streptomyces sp. NPDC015532
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616714
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Streptomyces sp. NPDC015532"
                     /db_xref="taxon:3364960"
     Protein         1..278
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27641
     Region          14..237
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 mtpterlrds alafralhvp grplvlanaw davsarivee egaaavatts aglawalgav
       61 dgdrldrdda laavariaav vrvpvsadie sgyasdargv adtvravlaa gavgvnieda
      121 lygqgagplr praeqaeria avraaadaag vplfvnarvd tflrgaggve etleraaafl
      181 gagadgvfvp gtvdpatvka lvegiegpvn ilvgpgapsv gelaalgvar istgsslaaa
      241 ahalvrraar ellgtgtcet liggfdyagl nalmgrag
//
LOCUS       WP_392179192             308 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces sp. NPDC015532].
ACCESSION   WP_392179192
VERSION     WP_392179192.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015532
  ORGANISM  Streptomyces sp. NPDC015532
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Streptomyces sp. NPDC015532"
                     /db_xref="taxon:3364960"
     Protein         1..308
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=30715
     Region          40..306
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 msvrdgrvgr haglsllvlv aagflahrhw pvieagagml ahadrgwllv aavatlatwv
       61 csalaqqgav aeplpagrlv avqfaaasan hvlpsglgag avnlrfltrc glplarsata
      121 lavkacagtv vrgcliggla lacpgalrlp rlaasawtva awtagvvvaa vaaalfagpl
      181 rralrrvlld vravhelpar aaalwggslv faalhatvvi avaqaiglpl sparvalvyl
      241 aassaavllp tpgglgslda alalaltlag apggaaastv lgyrlltvwl pllpglvtlg
      301 vlirrrvl
//
LOCUS       WP_392179197             308 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Streptomyces sp. NPDC015532].
ACCESSION   WP_392179197
VERSION     WP_392179197.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015532
  ORGANISM  Streptomyces sp. NPDC015532
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Streptomyces sp. NPDC015532"
                     /db_xref="taxon:3364960"
     Protein         1..308
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32159
     Region          4..306
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mtaltrparl aagariavva psgpvpeerl eagldilrgw gldpvvaphv ldrhaefayl
       61 agtdadraad fqaawcdpdv aavlcarggy gaqrmiglld wdairaagpk vfvgfsdita
      121 lheafarrvg latlhgpmvs algflkspga qehlratlfe pesvrtiasg eavplvpgra
      181 rgvtlggcas llaaelgtph aragarggll liedvgeeay rldriltqll rsgwldgvag
      241 valgswvdcg pyerlravfa drlgtlgvpv vehfgfghae gtltmpfgvr aeldadagtl
      301 tleepalr
//
LOCUS       WP_392179997             293 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptomyces sp.
            NPDC015532].
ACCESSION   WP_392179997
VERSION     WP_392179997.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015532
  ORGANISM  Streptomyces sp. NPDC015532
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 293)
  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 293)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 293)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 293)
  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   5  (residues 1 to 293)
  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   6  (residues 1 to 293)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Streptomyces sp. NPDC015532"
                     /db_xref="taxon:3364960"
     Protein         1..293
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32150
     Region          19..102
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          126..285
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mlerlnqald hleacldqev dmaevariaa vseyhfrrmf salagmpltv yvrrrrmtla
       61 gaevlagept lldvavrygy gsgeafaraf rsvhgigpge arrtgavlsa qprmsfrvvv
      121 egsttmryri vekesfqvvg rkarvplvhe glnaaaaahv qslderaivr mkelgdrepe
      181 gvlsavvylt dsreegaead ywvgvvtgpe vvaeeldald vpagtwavfd nhgpypsalq
      241 elwrdvftqw fpsnryttrp gpellrtrpv eigaetnsql wipvergngs aga
//
LOCUS       WP_392180215             409 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC015532].
ACCESSION   WP_392180215
VERSION     WP_392180215.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015532
  ORGANISM  Streptomyces sp. NPDC015532
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 409)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Streptomyces sp. NPDC015532"
                     /db_xref="taxon:3364960"
     Protein         1..409
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43976
     Region          62..247
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          254..378
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mkhvhtrarr agaalaavlt wagllagasg ctsggisdgi geafgkprsp kdvihispdd
       61 nskgvrprep llvrvpggrl esvkvvksqd arespvpghi sddglswrpd dgrlalaaky
      121 tvdavaldgg ghrsarhttf ttavpderfi gyvtpedrsv vgtgmivsle fnreienraa
      181 verairvear paveirahwf gggrvdfrpe rywkpgtkvt vtlrlrdveg asgvyglqsr
      241 tfsftvgrdq tslvdaraht mevrrdgdll atvpitagap ktttyngkmv vtemlevtrm
      301 nsrtvgfgge ydipdvpham rltdsgtflh gnywapdafg ntnvshgcvg lrdvkgggsd
      361 tpagwffdrs ligdvvevvh skdkkvapdn glggwnmgwk ewktggavk
//
LOCUS       WP_392182741             227 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces sp. NPDC015532].
ACCESSION   WP_392182741
VERSION     WP_392182741.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015532
  ORGANISM  Streptomyces sp. NPDC015532
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Streptomyces sp. NPDC015532"
                     /db_xref="taxon:3364960"
     Protein         1..227
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24650
     Region          2..225
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 msgrdlilgr vrraladvpr dddtppvpge pwrdpryeea vgrsylrehg trsvaetvdl
       61 laenladyra ivhrtteegl pdlierllae rgpryvlvpp glppewmgaa dptrvddrav
      121 stpgeldkvg svvtgcalav aetgtivldg gpdqgrrrit lipdhhicvv rvpdqvvasv
      181 pqalerldpt rpltwisgps atsdieldrv egvhgprtle vvlvger
//
LOCUS       WP_392183113             407 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC015032].
ACCESSION   WP_392183113
VERSION     WP_392183113.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015032
  ORGANISM  Streptomyces sp. NPDC015032
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  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 407)
  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
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 407)
  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   5  (residues 1 to 407)
  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   6  (residues 1 to 407)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 407)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Streptomyces sp. NPDC015032"
                     /db_xref="taxon:3364937"
     Protein         1..407
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41997
     Region          16..>59
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          79..395
                     /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 magttpgtpr vlramndraa ldlllehgpl srtrigkltg lskptasqll srleaaglvv
       61 atgtvagrpg pnaqlyavna raahvagldv narrivaava dvtgetvgef elrtpgrrad
      121 svvrqvadal dgavkdaglt rsdvhrvvig tpgafdpgtg rlryashlpg whspalldel
      181 aaflpmpvey endvnlvava eqrlgaargh ddfvllwnee glgaalving rlhrgftgga
      241 gevgflpvpg vplvrqvtkv naggfqelag aqvlsrlark lgiddatvsa pgthhevaag
      301 liaraaeaae ageggpyprl ldlfatglat glasmvavld pevvvlsgel iaaggeplrg
      361 rveselvela asrprliaga vthrpvlrga lesalattrd evfdtsh
//
LOCUS       WP_392183898             325 aa            linear   BCT 20-JAN-2025
DEFINITION  quinone oxidoreductase family protein [Streptomyces sp.
            NPDC015032].
ACCESSION   WP_392183898
VERSION     WP_392183898.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015032
  ORGANISM  Streptomyces sp. NPDC015032
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 325)
  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   4  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Streptomyces sp. NPDC015032"
                     /db_xref="taxon:3364937"
     Protein         1..325
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=33244
     Region          1..325
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 mrivrhhefg apsvlrleea dtpvpgpgqv lirteavgvn faecqrrqgi pvggpatlpg
       61 spggdvagvv eqvgdgvdqv gvgdrvvtgv ahdgyaeyvv tqagwlfavp egidagqats
      121 lpipgqtayh vivtaaklqp gesvlitaaa ggighllvqm aktlgagqii aaargaekla
      181 faaslgadvt vdygedgwde kvraatggrg vdvaletvgg dvltksvnlt aqfgrtvvyg
      241 aaggelpaie vgdifdnriv mgfsmwgvmg ekpdvmakga relldmvasg kvrpvvhael
      301 plkdaaaahe lmesrsqlgr vvlvp
//
LOCUS       WP_392184510             473 aa            linear   BCT 20-JAN-2025
DEFINITION  SWIM zinc finger family protein [Streptomyces sp. NPDC015032].
ACCESSION   WP_392184510
VERSION     WP_392184510.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015032
  ORGANISM  Streptomyces sp. NPDC015032
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Hassan,I.U., Rehman,H.M., Liu,Z., Zhou,L., Samma,M.K., Wang,C.,
            Rong,Z., Qi,X., Cai,D. and Zhao,H.
  TITLE     Genome-wide identification and spatiotemporal expression profiling
            of zinc finger SWIM domain-containing protein family genes
  JOURNAL   Zool Res 44 (3), 663-674 (2023)
   PUBMED   37161653
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     SWIM, a novel Zn-chelating domain present in bacteria, archaea and
            eukaryotes
  JOURNAL   Trends Biochem Sci 27 (8), 384-386 (2002)
   PUBMED   12151216
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10516955
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Streptomyces sp. NPDC015032"
                     /db_xref="taxon:3364937"
     Protein         1..473
                     /product="SWIM zinc finger family protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48963
     Region          69..99
                     /region_name="SWIM"
                     /note="SWIM zinc finger; pfam04434"
                     /db_xref="CDD:309540"
ORIGIN      
        1 mllshggepl rtaepaarwt veqvlalapd dasrkagskl gsagpwsgsg cdgsgavwgl
       61 ckgsgskpyq tvvdttgpay kcscpsrkfp ckhalglllv wasgasalpt gevpdwagew
      121 ltgrrgraae kgetggpttd gapatgpadp vaarrraerr aaritggaqe lqqrladllr
      181 gglaaadqpe yglweetaar mvdaqapgla srvrelgavp asgagwpvrl leecallhll
      241 drawlgisrl peplaatvrt rvglpapaeg ppirdhwlvl aqydtpdgri varriwlhgr
      301 esgrtvllls fgaagrspgp alptgvtida eitlhpgtnr lraelgrqfg apspvgtppp
      361 ggtaataiga ygdalrddpw ldawpvtlre vipvpsghgw qlvdaageta lplapsalsr
      421 pglwklvals ggspvtvfge cghrgfdpfa awtsdagdta ggadmtfetv plv
//
LOCUS       WP_392184807             516 aa            linear   BCT 20-JAN-2025
DEFINITION  complex I subunit 4 family protein [Streptomyces sp. NPDC015032].
ACCESSION   WP_392184807
VERSION     WP_392184807.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015032
  ORGANISM  Streptomyces sp. NPDC015032
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 516)
  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 516)
  AUTHORS   Galemou Yoga,E., Angerer,H., Parey,K. and Zickermann,V.
  TITLE     Respiratory complex I - Mechanistic insights and advances in
            structure determination
  JOURNAL   Biochim Biophys Acta Bioenerg 1861 (3), 148153 (2020)
   PUBMED   31935361
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Friedrich,T. and Scheide,D.
  TITLE     The respiratory complex I of bacteria, archaea and eukarya and its
            module common with membrane-bound multisubunit hydrogenases
  JOURNAL   FEBS Lett 479 (1-2), 1-5 (2000)
   PUBMED   10940377
REFERENCE   4  (residues 1 to 516)
  AUTHORS   Walker,J.E.
  TITLE     The NADH:ubiquinone oxidoreductase (complex I) of respiratory
            chains
  JOURNAL   Q Rev Biophys 25 (3), 253-324 (1992)
   PUBMED   1470679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Streptomyces sp. NPDC015032"
                     /db_xref="taxon:3364937"
     Protein         1..516
                     /product="complex I subunit 4 family protein"
                     /GO_component="GO:0045271 - respiratory chain complex I
                     [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048039 - ubiquinone binding [Evidence
                     IEA]"
                     /GO_process="GO:0015990 - electron transport coupled
                     proton transport [Evidence IEA]"
                     /GO_process="GO:0042773 - ATP synthesis coupled electron
                     transport [Evidence IEA]"
                     /calculated_mol_wt=53570
     Region          4..513
                     /region_name="NuoM"
                     /note="NADH:ubiquinone oxidoreductase subunit 4 (chain M)
                     [Energy production and conversion]; COG1008"
                     /db_xref="CDD:440632"
ORIGIN      
        1 mqfllafivv vpligavaal lpappglkgs spdqavlrhg vtvtgavlla aivlaagfdh
       61 dhpakmqatt diswipalgv rihlgidgis lpllvltall tflcalhsyf kppagpspka
      121 fvalvlvles gtlatfavld lllfflafem vlipmyflia rwggaqkqaa awkfilytll
      181 gsvimllgll liglksgtfd mvalatdngr gltssvqvia vlaiglglav ktpmwplhsw
      241 lpdahtaapt vgsvllagvl lkmgtygfvr illpiapdgm htfapylaaf avvgivygsl
      301 aclalarpgs kgdlkrliay ssvghmgfvl lgiasmtptg vngalfania hglitgllff
      361 lvgavkdryg tadldtlsga tgaalygrap rlggllafaa vaslglpgla gfwgemlalf
      421 gsfdpadgls rpafltfmsi aafgtlltaa ymlivvrrvc mgekpeepqr ladvqtyefa
      481 awtplvaltv laglwpavll gltdpavqkl laggks
//
LOCUS       WP_392186400             412 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC015032].
ACCESSION   WP_392186400
VERSION     WP_392186400.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015032
  ORGANISM  Streptomyces sp. NPDC015032
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 412)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Streptomyces sp. NPDC015032"
                     /db_xref="taxon:3364937"
     Protein         1..412
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=42898
     Region          68..249
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          255..382
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mekrvmtgsk rrrglvaasa llggvlvlta csdgssadgs knsqaaadka aaedaseaqi
       61 aiapkngatn asinkdakvt vtkgtlsevt mttsagaavk gtlaadgksw kpdgqlerst
      121 tykisatakd skgreahent sfttvspans fignftpedg stvgvgmpvs infnkaitdk
      181 kavqdaitvt sssgqevvgh wfnsqrldlr penywqggst vtlklaldgv egakgvfgvq
      241 qktvtfkvgr nqvstvdant ktmtvtrdgk tvktipisag ssanptyngq mvisekfqet
      301 rmngdtvgfg geydikdvph amrlstsgtf ihgnywsgsg vfgsantshg cvglqdakga
      361 gdanqpgawf ynnsmvgdvv ivknspdrti tpdnglngwn mswadwkads aa
//
LOCUS       WP_392186575             706 aa            linear   BCT 20-JAN-2025
DEFINITION  DNA gyrase/topoisomerase IV subunit B [Streptomyces sp.
            NPDC015032].
ACCESSION   WP_392186575
VERSION     WP_392186575.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015032
  ORGANISM  Streptomyces sp. NPDC015032
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Tari,L.W., Trzoss,M., Bensen,D.C., Li,X., Chen,Z., Lam,T.,
            Zhang,J., Creighton,C.J., Cunningham,M.L., Kwan,B., Stidham,M.,
            Shaw,K.J., Lightstone,F.C., Wong,S.E., Nguyen,T.B., Nix,J. and
            Finn,J.
  TITLE     Pyrrolopyrimidine inhibitors of DNA gyrase B (GyrB) and
            topoisomerase IV (ParE). Part I: Structure guided discovery and
            optimization of dual targeting agents with potent, broad-spectrum
            enzymatic activity
  JOURNAL   Bioorg Med Chem Lett 23 (5), 1529-1536 (2013)
   PUBMED   23352267
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Gadelle,D., Filee,J., Buhler,C. and Forterre,P.
  TITLE     Phylogenomics of type II DNA topoisomerases
  JOURNAL   Bioessays 25 (3), 232-242 (2003)
   PUBMED   12596227
REFERENCE   3  (residues 1 to 706)
  AUTHORS   Wang,J.C.
  TITLE     Cellular roles of DNA topoisomerases: a molecular perspective
  JOURNAL   Nat Rev Mol Cell Biol 3 (6), 430-440 (2002)
   PUBMED   12042765
REFERENCE   4  (residues 1 to 706)
  AUTHORS   Champoux,J.J.
  TITLE     DNA topoisomerases: structure, function, and mechanism
  JOURNAL   Annu Rev Biochem 70, 369-413 (2001)
   PUBMED   11395412
REFERENCE   5  (residues 1 to 706)
  AUTHORS   Roca,J.
  TITLE     The mechanisms of DNA topoisomerases
  JOURNAL   Trends Biochem Sci 20 (4), 156-160 (1995)
   PUBMED   7770916
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Streptomyces sp. NPDC015032"
                     /db_xref="taxon:3364937"
     Protein         1..706
                     /product="DNA gyrase/topoisomerase IV subunit B"
                     /EC_number="5.6.2.2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003918 - DNA topoisomerase type II
                     (double strand cut, ATP-hydrolyzing) activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006265 - DNA topological change [Evidence
                     IEA]"
                     /calculated_mol_wt=77007
     Region          21..700
                     /region_name="GyrB"
                     /note="DNA gyrase/topoisomerase IV, subunit B
                     [Replication, recombination and repair]; COG0187"
                     /db_xref="CDD:439957"
ORIGIN      
        1 mtadtsvpst alltgadrdg snytarhllv legleavrkr pgmyigstds rglmhclwei
       61 idnsvdealg gycdhievvl hddnsvevrd ngrgipvdve pktglsgvev vmtklhaggk
      121 fgggsyaasg glhgvgasvv nalsarldve vdrssathsi sfrrgvpgif teqgpdspfd
      181 pangllkgkr vpkartgtrv rywadrqifl kdaklnletl hqrarqtafl vpgltivvrd
      241 ergldgggkv eetfcfdggi sefceylaqd kavcdvlrlt gqgtfketvp vlderghmta
      301 tevtrelgvd ialrwgtgyd tnlksfvnii atpkggthvt gfersvtktv nevlrsakll
      361 rvaeddivkd dalegltavv tvrlaepqfe gqtkevlgts aanrivanvv skelkaflts
      421 tkrdqkaqar avldkavaaa rtriaarqhk daqrrktale tsslpaklad crsddverse
      481 lfivegdsal gtaklarnse fqallpirgk ilnvqkssvs dmlknaecga iiqvigagsg
      541 rtfdidaary gkivllvdad vdgahircll ltlfqrymrp mveagrvfaa vpplhrielv
      601 qpkkgqdkyv ytysdnelrq rllalqrknv rykdsiqryk glgemdadql aettmdprhr
      661 tlrrinigdl esservfdll mgnevaprke fiasaaatld rsrida
//
LOCUS       WP_392186847             288 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015032].
ACCESSION   WP_392186847
VERSION     WP_392186847.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015032
  ORGANISM  Streptomyces sp. NPDC015032
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   3  (residues 1 to 288)
  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 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 16111081
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces sp. NPDC015032"
                     /db_xref="taxon:3364937"
     Protein         1..288
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31814
     Region          22..77
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(24,28,53)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(27,52)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(34..35,46,49,53..54)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          108..283
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mevgsggard astlrqrrla aelrklrera gltsmmaaac vgvqqarmsm ieagryavsa
       61 drvramansy scddaalvda maemtggrer gwwdeyrell paglievaec enwatsmrvg
      121 vvvsmpglaq tleyaravfr qsvpqlrphe iehrasfrvk rqavlfrevt lpytaivhea
      181 alrmrfggpe vtraqlrhma ammeqgnvti rvipferqdf paagrpityv agqvpqldtv
      241 vldsdhgcdf ldaeaqlary rsvldrmesc alspaqsrdf vhkiagsl
//
LOCUS       WP_392188369             263 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015032].
ACCESSION   WP_392188369
VERSION     WP_392188369.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015032
  ORGANISM  Streptomyces sp. NPDC015032
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 263)
  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 263)
  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 18568518
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Streptomyces sp. NPDC015032"
                     /db_xref="taxon:3364937"
     Protein         1..263
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=27583
     Region          1..63
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          95..250
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mtrqqtcpta lvggatlrda rerhmmlpee padllgigpd tvlamesgsr avsasaital
       61 srlyrcgadt ralqrlmaga aepetlrdge pghaprlrac arqaasvrwl stvrlppplq
      121 trayalaaee hstalrgapl apggdtvyvl dsrvitcgsg tpslmaeqla hlmqlagsgt
      181 virvvaeahp ipqppghlve ltfpagrvva qpsedgvtyh rsdgwsrtid dafkvtdpas
      241 srealaqaav lhragarttt gpl
//
LOCUS       WP_392188528             547 aa            linear   BCT 20-JAN-2025
DEFINITION  peptide ABC transporter substrate-binding protein [Streptomyces sp.
            NPDC015032].
ACCESSION   WP_392188528
VERSION     WP_392188528.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015032
  ORGANISM  Streptomyces sp. NPDC015032
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 547)
  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 547)
  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 547)
  AUTHORS   ter Beek,J., 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 547)
  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 547)
  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 11467924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Streptomyces sp. NPDC015032"
                     /db_xref="taxon:3364937"
     Protein         1..547
                     /product="peptide 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=58472
     Region          39..547
                     /region_name="OppA"
                     /note="ABC-type oligopeptide transport system, periplasmic
                     component [Amino acid transport and metabolism]; COG4166"
                     /db_xref="CDD:443327"
ORIGIN      
        1 mrgatqakwa acavavalaa tacggggsgg ggggggsgan givssswgdp qnplepantn
       61 evqggkvldm ifrglkrydp ktgaamnmla ekidtkdnqn ftitvkdgwt fsngekvtak
      121 sfvdawnyga llknnqknay ffgyidgyak vhpesgsasa ntlsglklvn dktftvkltq
      181 kfslwpdtlg ypafaplpra fftdhaawvs kpigngpyti dkytkgssmn lrkwdgypga
      241 dkaqnggidl kvytdnntay tdltagnldl vddvpaaqlk nvkadlgdry intpagiiqt
      301 lafpfydkkw dtpggikvrq glsmainreq itsqifqktr tpasdwtspv lgasggfkkg
      361 lcgapcefna anakkliqeg ggipggqlki synadtgshk ewvdavcnsi nkvmgnnkac
      421 vggpvgtfad frsqvsqqkl agawragwqm dypliqnflq pvyytdassn dgkwsskkfd
      481 glvdkanaes dkatavstfq daekvlveqm pviplwyqng sagysdriss valnqfsvpv
      541 yeqikvk
//
LOCUS       WP_392189506             314 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Streptomyces sp. NPDC015032].
ACCESSION   WP_392189506
VERSION     WP_392189506.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015032
  ORGANISM  Streptomyces sp. NPDC015032
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces sp. NPDC015032"
                     /db_xref="taxon:3364937"
     Protein         1..314
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32713
     Region          6..312
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mtlapltrpa rlrpgariav vspsgpvpad rldagldvlr swglepveap hvrdvhpeld
       61 ylagtdeara rdlqeawcdp svdavicarg gygahrmvdl vdwaamraag pkvfvgysdi
      121 tvlheafalr mglatlhgpm vgtetflkdp dtqeslratl fepetvrslg lpsarvlvpg
      181 sargityggc vsllaadlgt pharrpargg llviedtted pysidriltq llragaldgt
      241 agvacgswad cgpyekvrav ladrlgplgv pvveelgfgh gptaltiplg vpavldapad
      301 ggpatltieg palv
//
LOCUS       WP_392189561             282 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015032].
ACCESSION   WP_392189561
VERSION     WP_392189561.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015032
  ORGANISM  Streptomyces sp. NPDC015032
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 282)
  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 282)
  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 16111081
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces sp. NPDC015032"
                     /db_xref="taxon:3364937"
     Protein         1..282
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31592
     Region          20..71
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(22,26,51)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(25,50)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(32..33,44,47,51..52)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          90..264
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mpniqtldps aspldyygwe lrrqreavnl kqgqlgdiif ctgsligqie ttkkvptrdf
       61 servdaalgt dgvfsrligl vlrsqlptwf qpyaemesca ayistyqaql vygllqteey
      121 aravlatgmp ddlenlvaar merqrilere rpplawavld eavlhrpigg hevmrkqlqr
      181 lldvadhrwm qiqvlpfaag ehaslagsfn tlrfdddpdl vytedvisgh mtanpdtvre
      241 aslryarlqa aalsvedsaa litrvmeery gdrsraeera va
//
LOCUS       WP_392190814             456 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC014864].
ACCESSION   WP_392190814
VERSION     WP_392190814.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014864
  ORGANISM  Streptomyces sp. NPDC014864
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 456)
  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 456)
  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 456)
  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 10611723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Streptomyces sp. NPDC014864"
                     /db_xref="taxon:3364924"
     Protein         1..456
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45102
     Region          17..74
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(23,27,52)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(26,51)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(33..34,45,48,52..53)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          <105..>262
                     /region_name="PRK07003"
                     /note="DNA polymerase III subunit gamma/tau"
                     /db_xref="CDD:235906"
     Region          355..438
                     /region_name="DUF2690"
                     /note="Protein of unknown function (DUF2690); pfam10901"
                     /db_xref="CDD:402475"
ORIGIN      
        1 mprwkalpde ldpqvrefas qlrrlvdrsg lsvaaladrt gysktswery lggrllapkg
       61 aivalaevtg tnpvhlttmw elaerawsra emrhdrtmea irisqaraal gesgamsaad
      121 gkgvgtvrrs gsatvapeaa gpagtsptvp sqptaadadv rdavprttpp gpasspgtgp
      181 gagtgsdvvs asasapvsep aadagadpgt gsataepvns wglagyrgps paggrasgsa
      241 sspsggptrt atspsgaaar ppagpgaytg agagagtvpa agtpqtprpg angarrqqal
      301 mflaglvgvl vligavfylt gggaekpega kkspaaspsv dpnlppgvkc sgasctgkda
      361 egmgcsgefv ttaqsatvgt tvvevryskt cgaawgritq aaqgdevrvt vgsrqetgti
      421 ttagdtiayt pmvavkdaar mkacatlasg qqgctr
//
LOCUS       WP_392191717             428 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC014864].
ACCESSION   WP_392191717
VERSION     WP_392191717.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014864
  ORGANISM  Streptomyces sp. NPDC014864
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 428)
  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 428)
  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
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 428)
  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   5  (residues 1 to 428)
  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   6  (residues 1 to 428)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 428)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 428)
  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 20170230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Streptomyces sp. NPDC014864"
                     /db_xref="taxon:3364924"
     Protein         1..428
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45062
     Region          <20..>60
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          80..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 magrngrtvr dlrrgnrtav lqrlyfdgpl srfelgpatg lssgsvsnvv adliadglve
       61 eagsvdsdgg rprtllrvap asghmigvdv getrvrvelf dltltelart qrplepqryd
      121 vevitghird gvaevlgaag lapeqllgvg igvpgivert pergavvhgq tigwdavple
      181 ellragsrlp gsvpyfidng aktlgqaemw fgagrgagna vvvlfgsgvg aclvtpeveh
      241 gravewghlt vrvrgrrcrc galgcleaya gaesllarwr eeggrpprda deesaltaml
      301 aaacppegte adpvalavle etaeylgagl sdlinlfqpe riliggwagl qlgarflsav
      361 rrhavayalr hpaervtvdl grlgpdavtv gaailpladf farggrraep apraqlpawq
      421 aalegrrp
//
LOCUS       WP_392192107             403 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC014864].
ACCESSION   WP_392192107
VERSION     WP_392192107.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014864
  ORGANISM  Streptomyces sp. NPDC014864
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces sp. NPDC014864"
                     /db_xref="taxon:3364924"
     Protein         1..403
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=42365
     Region          61..233
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          239..371
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mvatagalgg alaltalagt gnaatsdnna dthlksqara draaapdasd arlritpghg
       61 aynvgvnapv kvtvsngklt kvtmtavatg aevpgtlsah gtswkshgkl hratkyqvaa
      121 eaedakgrsv tqnatittvs panefighls pqsgstvgvg mpvtvtfdka ignksamesk
      181 iqvssssgqr vvghwfnndr ldfrpknywk pgstvtvkln lhgthktvtf kigrsqistv
      241 daktklmtvv rngktiktip issgsrehpt yngrmvisek frqihmsgas vgltkkdgkp
      301 eydikavpha mrlsdsgtfi hgnywspasv fgkvnashgc vglkdvkggg ngrlpaawff
      361 dhsmigdvvi vknsddktkl aadnglsdwn mpwnewvags ais
//
LOCUS       WP_392192696              57 aa            linear   BCT 20-JAN-2025
DEFINITION  MFS transporter small subunit [Streptomyces sp. NPDC014864].
ACCESSION   WP_392192696
VERSION     WP_392192696.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014864
  ORGANISM  Streptomyces sp. NPDC014864
            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  :: HMM
            Evidence Accession :: NF047966.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..57
                     /organism="Streptomyces sp. NPDC014864"
                     /db_xref="taxon:3364924"
     Protein         1..57
                     /product="MFS transporter small subunit"
                     /calculated_mol_wt=5579
ORIGIN      
        1 mshdsspspp dpaapgsags gagtptalia vawlwvgapl ayglyelvrk atqlftg
//
LOCUS       WP_392193085             245 aa            linear   BCT 20-JAN-2025
DEFINITION  TerD family protein [Streptomyces sp. NPDC014864].
ACCESSION   WP_392193085
VERSION     WP_392193085.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014864
  ORGANISM  Streptomyces sp. NPDC014864
            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 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Streptomyces sp. NPDC014864"
                     /db_xref="taxon:3364924"
     Protein         1..245
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=26960
     Region          <13..240
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mgffdgllgg rvadfdsgsa atnaieltkr hhqvsltkqg aatghlrvnl twrmrtsdig
       61 gsaresllrh pfkalkppev mghsqsmvnv dldlgclyel adgtkgvvqp lggflgdvns
      121 ppyvklsgdd rfgsasgeti yvnldhrdai krllvfvyiy dqtpafdrth aivtlypsng
      181 prieiglder hpqarscavv lienvkgell vrrevkfvyg fqaeldrlyg wglqwgrgyk
      241 stadr
//
LOCUS       WP_392193624             325 aa            linear   BCT 20-JAN-2025
DEFINITION  quinone oxidoreductase family protein [Streptomyces sp.
            NPDC014864].
ACCESSION   WP_392193624
VERSION     WP_392193624.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014864
  ORGANISM  Streptomyces sp. NPDC014864
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 325)
  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   4  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Streptomyces sp. NPDC014864"
                     /db_xref="taxon:3364924"
     Protein         1..325
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=33867
     Region          1..325
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 mrivrhyehg apsvlrveea ekpqpgpgev lirseavgvt faevqrrqgi pigghaelpg
       61 apggdvagtv ealgegvanl rvgdrvvvdv drgayadhvv adaawaisip atmdaaeatl
      121 lpspaqtayh alkeagqlkp getvlidaas ggvghlavqi akamgagkvi atastrakld
      181 fvrelgadvt vnytdedwde qvkaatdgrg advvletvgg diltksialt aqfgrlvfyg
      241 sasgdiqpvn plmlsrmktv agfalyamly nkpeaiaagq rdlldmigsg kvrpvvherl
      301 pltdavkahe lmearaqlgk vvlvp
//
LOCUS       WP_392194174             479 aa            linear   BCT 20-JAN-2025
DEFINITION  alpha,alpha-trehalose-phosphate synthase (UDP-forming)
            [Streptomyces sp. NPDC014864].
ACCESSION   WP_392194174
VERSION     WP_392194174.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014864
  ORGANISM  Streptomyces sp. NPDC014864
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 479)
  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 479)
  AUTHORS   Eastmond,P.J. and Graham,I.A.
  TITLE     Trehalose metabolism: a regulatory role for trehalose-6-phosphate?
  JOURNAL   Curr Opin Plant Biol 6 (3), 231-235 (2003)
   PUBMED   12753972
REFERENCE   3  (residues 1 to 479)
  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   4  (residues 1 to 479)
  AUTHORS   Elbein,A.D., Pan,Y.T., Pastuszak,I. and Carroll,D.
  TITLE     New insights on trehalose: a multifunctional molecule
  JOURNAL   Glycobiology 13 (4), 17R-27R (2003)
   PUBMED   12626396
REFERENCE   5  (residues 1 to 479)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 929-939 (1997)
   PUBMED   9334165
  REMARK    Erratum:[Biochem J 1998 Feb 1;329(Pt 3):719]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Streptomyces sp. NPDC014864"
                     /db_xref="taxon:3364924"
     Protein         1..479
                     /product="alpha,alpha-trehalose-phosphate synthase
                     (UDP-forming)"
                     /EC_number="2.4.1.15"
                     /GO_function="GO:0003825 - alpha,alpha-trehalose-phosphate
                     synthase (UDP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0005992 - trehalose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=52309
     Region          6..478
                     /region_name="OtsA"
                     /note="Trehalose-6-phosphate synthase, GT20 family
                     [Carbohydrate transport and metabolism]; COG0380"
                     /db_xref="CDD:440149"
ORIGIN      
        1 masthgaevl vasnrgpvsy elredgslqa rrgggglvsg lsaigpeaga vwvcaalgda
       61 dreaarrfeg grrlpsdatg gqqvrmldid aavfadayng iansvlwfvh hmlyqtplep
      121 vfdaefrrqw asyeaynlaf aealaeeaae gaavvvqdyh ltlvpgmlrd frpdvrighf
      181 shtpwapvdy frmlpddvae qvlrgmlgad rlgfltrrwa daftgcceal vdglggtrvg
      241 vhglgadaef lrerahradv dermaalree igtapdgapr rtvvrvdrte lsknivrgll
      301 ayeqlledrp ewqervthla faypsrqdla vyrdytaevq rvaqeindrf gtpgwtpvvl
      361 hvrddfarsl aayrladval vnpirdgmnl vakevpvvsd agcalvlsre agayaelged
      421 avvvnpydvt gtaralheal tmpaheraer skrlaaaata lppaqwfldq ltelngrpd
//
LOCUS       WP_392194220             243 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Streptomyces sp.
            NPDC014864].
ACCESSION   WP_392194220
VERSION     WP_392194220.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014864
  ORGANISM  Streptomyces sp. NPDC014864
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 243)
  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 11440233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Streptomyces sp. NPDC014864"
                     /db_xref="taxon:3364924"
     Protein         1..243
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=26363
     Region          12..240
                     /region_name="GCD1"
                     /note="NDP-sugar pyrophosphorylase, includes eIF-2Bgamma,
                     eIF-2Bepsilon, and LPS biosynthesis protein s
                     [Translation, ribosomal structure and biogenesis, Cell
                     wall/membrane/envelope biogenesis]; COG1208"
                     /db_xref="CDD:440821"
ORIGIN      
        1 mthpnaasrp aqavilaggq gsrlrpytdd rpkpmveipg tgtpiighqi awlaeegvtd
       61 vvvscghlae vlqtwlksta lpvkvttvve teplgrgggl rfaaahlphp drpwyatngd
      121 iwtrfslrdm adfhterdav atlalarprl pwgavktdgf ghitdfieap pstveinagv
      181 yvfapefagl lpergdhert tfprlarerr lagfplpqga ywraidtakd lteaakelaa
      241 lnr
//
LOCUS       WP_392194482             408 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC014864].
ACCESSION   WP_392194482
VERSION     WP_392194482.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014864
  ORGANISM  Streptomyces sp. NPDC014864
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces sp. NPDC014864"
                     /db_xref="taxon:3364924"
     Protein         1..408
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43537
     Region          62..246
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          253..377
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mrhvqgragr agaalaavlt wagllagaag ctsggtdgfg gllggppaae dvirvspddg
       61 dkgvradgkl rvragdgrle svrvvraqda qdtpvpgrlt sggrewrpdd drlalaakyt
      121 vdavavdsrg rrsarhtsft tyvpeerfig yvtpenrstv gtgmivsltf nrkiadraav
      181 eravhvtadp pveirahwfg gerldlrprt ywspgtqvtv dlrlrdvega pgvyglqdks
      241 fsftigrsqv slvdaaahtm evrregtlla tvpvtagapk sttyngkmvv memqevtrmn
      301 srtvgfggey dipdvphamr ltdsgtflhg nywsqdvfgr vnvshgcvgl qdvkgggaet
      361 pagwffdrsl vgdvvevvhs ddgyvapdng lggwnmdwtq wtagsaln
//
LOCUS       WP_392194521             451 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC014864].
ACCESSION   WP_392194521
VERSION     WP_392194521.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014864
  ORGANISM  Streptomyces sp. NPDC014864
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 451)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Streptomyces sp. NPDC014864"
                     /db_xref="taxon:3364924"
     Protein         1..451
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=47810
     Region          86..261
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          280..399
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mstngfirga gagaeeatvl gpsgpgasas spsarlrtrg vvgsallvaa lgagatacga
       61 dgnplaadpy daadqitfng ptetgkkadp dkplevtvdg sdgritdvta vdtagrhvsg
      121 elsadgtrwh stsplaagah ytlrvstedd dgspgrkvls vdtskprtqk rvnvkfgpqa
      181 gtygvgqpit aeldqpirdr aqravvesal rvdsmpsaqg awywvddthl hyrpkeywpa
      241 haqirvhsnl enikisdrlw ggtakplrit tgdrivavtd aaahtmsvyq ndqmikqlpv
      301 ttgkpgfdtr ngvkvilakq ylvrmksstv giaanssday dldvyyatrv twsgeyvhaa
      361 pwsvdaqgla nvshgctgms drnaawffdt vhegdvvqvv nskghmmepf gngfgdwnvs
      421 wtkwlqgsal ttggkadrpr teqarlspqg l
//
LOCUS       WP_392195221             203 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces sp. NPDC014864].
ACCESSION   WP_392195221
VERSION     WP_392195221.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014864
  ORGANISM  Streptomyces sp. NPDC014864
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Streptomyces sp. NPDC014864"
                     /db_xref="taxon:3364924"
     Protein         1..203
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=21109
     Region          1..199
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 mlgrvrdala lapqppvtve rayrtgralp aaerldlfvd rlvdyragvh tcvtadtaat
       61 varvlrerga rtvgvpagld pawlagfdgt vhidspdvpa prldaldgvv tasavscaet
      121 gtifldgsaa qgrralslvp dlhvcvvdls tveagvpeal arlvptrptt lisgpsatsd
      181 ielervegvh gprtldviir tda
//
LOCUS       WP_392195438             287 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC014864].
ACCESSION   WP_392195438
VERSION     WP_392195438.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014864
  ORGANISM  Streptomyces sp. NPDC014864
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 287)
  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 287)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Streptomyces sp. NPDC014864"
                     /db_xref="taxon:3364924"
     Protein         1..287
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32161
     Region          17..68
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          93..271
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 marrkdidgs vsvptfygke lrwkreaagl sleallqgsf ygktylsdie rgerrmpldl
       61 arhvdqvlat dgfferhced vrkarrgpha ayfekaleae kqaesielwa piifpgllqt
      121 apyartlvrs ahpaasdewv eekvmarlar arlfeedlst peywavlhes lvtdsilppl
      181 emaeqlgrvv elaerrritp qiiprscgay plmaasimvm tfpdappliy teasysgdti
      241 ddpalvkqyr kaydrlrava lspeasltii kaaagdyrng kqpgrle
//
LOCUS       WP_392195624             813 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces sp. NPDC014864].
ACCESSION   WP_392195624
VERSION     WP_392195624.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014864
  ORGANISM  Streptomyces sp. NPDC014864
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 813)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 813)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..813
                     /organism="Streptomyces sp. NPDC014864"
                     /db_xref="taxon:3364924"
     Protein         1..813
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=84095
     Region          <347..>390
                     /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"
     Region          537..810
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mdappprqvr raadlsrllv sgavlvvavl pavaalaptr rmqqalldaa talptglrdg
       61 vvgavqvvav vaplvavgvl varrrgdail rivpaaalga llswlvthla mtrsrpgvwp
      121 qvlagrgalv dadwppaayl aacaaavvaa gpwldtrlrr twwtltvgca glsitaaalm
      181 pleavaalav ggmagsavll lagapadrpa pqavadalva cgiplaalre tpppdqrsge
      241 gvgygaettt garltvqvlg pedrtrdlfh rlarlallrh ptdtdahtpl aavehellml
      301 vfagrtgara aepviaypva kggallvtie haarplsafp geeitdqilt gvwtsvarlq
      361 khrlahralr pehilvepdg asrliafara rlgatpdalg sdiaellatt atrigvprat
      421 qcalaglgpp llatvlpylq plallgparr evarhdqara raagagtkrr avrpggrpsl
      481 lrdlsaavve atgaepasla plarftwkti fglvgaflvl hlvlpqfasa pavvaalrka
      541 dwwwvlaalp vtfisqvfst clqmgtipar lpfgptyevq fassflnrit pnnvggmaln
      601 lrylqktgie tgaatasvgl qslvsavsna vlaawffawv grhhtevrlh vpagryvlpa
      661 falalaaggl lgvtpagrrf lrekvwpflr aavstvtgva sdpaklallv tgalglpliq
      721 vvglalsvra fggdlpfvqa gavymaarlv anaapvpggl galeagliag ltalgvtaga
      781 atsavlvyrl ltfwlnvplg alalravqrk gya
//
LOCUS       WP_392196419             324 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces sp. NPDC014864].
ACCESSION   WP_392196419
VERSION     WP_392196419.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014864
  ORGANISM  Streptomyces sp. NPDC014864
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Streptomyces sp. NPDC014864"
                     /db_xref="taxon:3364924"
     Protein         1..324
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33051
     Region          50..318
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mtalqlpelp pgraprrlpv rqvlclvpll lvllvavrhr svlaegfvhl rsaewpwlla
       61 aagatcltwv aaaftrqgav verlprrrll atqfaagaan hllptglgas avnlrflavc
      121 gvplarssaa lalyllaeti grltllavlf avfpdalrlg sllptgargp llltagavlp
      181 avsgalvcvr rlrgavsgfl rtalgearsv harparalal wggsfafpal qaaglalvgr
      241 alglpvppah malaylaatv avalvptpgg lgsvdaalvv alvaaggpaa latavvlafr
      301 litvwlpllp galtlgalvr lkvi
//
LOCUS       WP_392196854             420 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC014991].
ACCESSION   WP_392196854
VERSION     WP_392196854.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014991
  ORGANISM  Streptomyces sp. NPDC014991
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 420)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Streptomyces sp. NPDC014991"
                     /db_xref="taxon:3364935"
     Protein         1..420
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=45141
     Region          54..241
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          249..368
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mnhiprtrtv vsctllvtal gagvtacgsd gnplsakpyd aaglisfngp tgaekradpd
       61 kplevtangd egritdvtaq dstgryvage laadgsrwhs tsplaanahy tvrvsteded
      121 gapgrrvltf dtskptskkr lnvtfgpqag tygvgqpita qldheikdka qravveralr
      181 vestpavqga wywvdakelh yrpkeywpth atvrvhsnld gvrindrlwg gaakplkitt
      241 gdrveavtda sshqmtvykn gaeinqipvt tgkpgyetrn gvkvvlgkqy fvrmrsttvg
      301 iaegssdsyd lpvyyatrvt wsgeyvhaap wsvgsqgyan vshgctgmnt snaewffdtv
      361 regdivrvvn sdgdamepfg ngfgdwnvdw akwrqgsalf ngtpdgpapg dalrlqptav
//
LOCUS       WP_392196948             287 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC014991].
ACCESSION   WP_392196948
VERSION     WP_392196948.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014991
  ORGANISM  Streptomyces sp. NPDC014991
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 287)
  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 287)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Streptomyces sp. NPDC014991"
                     /db_xref="taxon:3364935"
     Protein         1..287
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32480
     Region          17..71
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          93..271
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 margkdidgs vsvptfygke lrwkreaagm sletflegsf ygktylsdie hgerrmpldl
       61 arhadrvlgt dgfferhced vrkarrgpha ayfekvleae nyaetieewc pitlpgllqt
      121 apyartlvrs ahpaasdewv eekvtarlar arlfeedhst peywavlres litdpllppl
      181 emaeqldriv elaerrritp qivprtcgay plmaasimvm tfpdappliy teasysgdti
      241 ddpalvkqyr kaydrlrava lspdtslami kaaaedyrng eqrdrle
//
LOCUS       WP_392197043             244 aa            linear   BCT 20-JAN-2025
DEFINITION  TerD family protein [Streptomyces sp. NPDC014991].
ACCESSION   WP_392197043
VERSION     WP_392197043.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014991
  ORGANISM  Streptomyces sp. NPDC014991
            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 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Streptomyces sp. NPDC014991"
                     /db_xref="taxon:3364935"
     Protein         1..244
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=27154
     Region          <24..239
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mgffdgllgg raadfdsgna tntieltrrh qavsltkqda atghlrvnlt wrmrtsdfdg
       61 grrpsllrhp fralkppeil ghgesmvdvd ldlgclyela dgtkgvvqpl ggylgdvnap
      121 pyiklsgddr fgsgsgetmy vnldhrdalk rllvfvyiyd rtpafdrtha ivtlypsngp
      181 rieiglderh pqarscavvm ienvkgelvv rrevkfvygf qgeldrlygw glqwgrgykt
      241 kvdr
//
LOCUS       WP_392197434             518 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Streptomyces sp.
            NPDC014991].
ACCESSION   WP_392197434
VERSION     WP_392197434.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014991
  ORGANISM  Streptomyces sp. NPDC014991
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 518)
  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 518)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Streptomyces sp. NPDC014991"
                     /db_xref="taxon:3364935"
     Protein         1..518
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=54997
     Region          258..435
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 marvplaalr tmpnrtsnrt rparplpsle paarprpwlr vlgltgvvli gawlgllvvg
       61 dvrapvgpmd ttmalrpsla ggtkinvspl galtldshva pvrldvnvdq ldplrsqalv
      121 dhperlsglq devardvehg tldlavrscv avvsgatalg lavyrrprpa laagglalvl
      181 laasgasaya twnpksvlep rfsgllssap svvgnarsiv tefdvyqkel arlvtnvtql
      241 ydvtstlpay rpdpstirvl hvsdihlnpa swkiiaslvn qykvdvivds gdtmdhgtaa
      301 engfldpvrd lgvpyvwvrg nhdsratqqy lermrnvhvl ddgraetvag lrfagvgdpq
      361 ftpdrsalpg rdaseelagd rlasalrdqr tagtpadvav ahepsaaret dgevplvlcg
      421 hlhhegtqml pygtrlrmeg stggsglrav ehgdpapiea silyfdrdsr rlqawdairl
      481 gglglttaev srhladenrp dagdashaps pagsatsp
//
LOCUS       WP_392198586             350 aa            linear   BCT 20-JAN-2025
DEFINITION  BMP family lipoprotein [Streptomyces sp. NPDC014991].
ACCESSION   WP_392198586
VERSION     WP_392198586.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014991
  ORGANISM  Streptomyces sp. NPDC014991
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Yousief,S.W., Bahey-El-Din,M. and Zaghloul,T.I.
  TITLE     Immunization with the basic membrane protein (BMP) family ABC
            transporter elicits protection against Enterococcus faecium in a
            murine infection model
  JOURNAL   Microbes Infect 22 (3), 127-136 (2020)
   PUBMED   31585177
REFERENCE   2  (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   3  (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   4  (residues 1 to 350)
  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   5  (residues 1 to 350)
  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 11448319
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Streptomyces sp. NPDC014991"
                     /db_xref="taxon:3364935"
     Protein         1..350
                     /product="BMP family lipoprotein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /calculated_mol_wt=35824
     Region          40..347
                     /region_name="Med"
                     /note="Lipoprotein Med, regulator of KinD/Spo0A, PBP1-ABC
                     superfamily, includes NupN [Signal transduction
                     mechanisms]; COG1744"
                     /db_xref="CDD:441350"
ORIGIN      
        1 mrrvaklsaa ciasaalamt atacgstssd ndspsssgdg kgvkiglafd vggrgdrsfn
       61 dsaargadqa kkefggdike ltaktsdtea dreqrlsdla eagynpvvgv gyayaasmtk
      121 vaakypktsf givdsvvdak nvdsinftee qgsylagvaa alktkskhvg fvggvdvpli
      181 kkfeagyvqg vkdtnpkikv dtqylshgsd tsgfaspdkg keaaqgmldn gadviytaag
      241 ssgngaieav sgkkgawaig vdsdqynipg lakyksailt smvknvdvgv ydfiksvhgg
      301 kpltgtnsys lakdgvklat sggfisdiqa kldaakkkiv dgsikvkttp
//
LOCUS       WP_392199541             314 aa            linear   BCT 20-JAN-2025
DEFINITION  aldo/keto reductase [Streptomyces sp. NPDC014991].
ACCESSION   WP_392199541
VERSION     WP_392199541.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014991
  ORGANISM  Streptomyces sp. NPDC014991
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  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 314)
  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   3  (residues 1 to 314)
  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   4  (residues 1 to 314)
  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 10790928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces sp. NPDC014991"
                     /db_xref="taxon:3364935"
     Protein         1..314
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /calculated_mol_wt=34460
     Region          5..314
                     /region_name="YdhF"
                     /note="Predicted oxidoreductase YdhF [General function
                     prediction only]; COG4989"
                     /db_xref="CDD:444013"
ORIGIN      
        1 maaetdirah klihgcmglg ggwdtkpytp edvqhaetai etalaagita fdhadiyryg
       61 kseavfgevl arssglreri vlqskcgirl pdgdrpgyyd lrgagilrrv eeslvrlrtd
      121 vldvlllhrp dpladpveia ealaalhaqg lvrrfgvsnm sgpqiaslqa hvdvplvvnq
      181 lemslaqrdw leagvlfntp datrngfatg tlewcaangi rlqawsplar grfttrtdtr
      241 vnrlvaglar rkgttpetiv lwwlqrhpag itpvvgttrp erisacedav frepdlthee
      301 wydlwitarg aplp
//
LOCUS       WP_392200481             236 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Streptomyces sp. NPDC014991].
ACCESSION   WP_392200481
VERSION     WP_392200481.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014991
  ORGANISM  Streptomyces sp. NPDC014991
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 236)
  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 10007985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Streptomyces sp. NPDC014991"
                     /db_xref="taxon:3364935"
     Protein         1..236
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24847
     Region          36..226
                     /region_name="COG3786"
                     /note="L,D-peptidoglycan transpeptidase YkuD,
                     ErfK/YbiS/YcfS/YnhG family [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443000"
ORIGIN      
        1 mrpgvvlalv pasclallgv apvpgpvplp lparmadtgg ggqlitaeap dtaatagtvs
       61 wwdlregqwv ragsaparfg snglveggtr sqgtnttptg lydlpfgfgi rpapagttvt
      121 yrpvretsww cqddestayn rwtdplpadc radrsehlis ygtqyayglv vgfnydrpvr
      181 grgagiflhv ngqgatagcv svpedamrqm lrwarpdqrp hiaigtvgga talary
//
LOCUS       WP_392200750             307 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Streptomyces sp. NPDC014991].
ACCESSION   WP_392200750
VERSION     WP_392200750.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014991
  ORGANISM  Streptomyces sp. NPDC014991
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces sp. NPDC014991"
                     /db_xref="taxon:3364935"
     Protein         1..307
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32228
     Region          4..305
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mnelvrprrl apgarvavva tsgpvpeerl qagldvlrgw dldpvtgphv ldrhpelgyl
       61 agtdadraad lqnawcdpav davlcarggy gaqrvidlld weamraagpk ilvgfsdvta
      121 lheafatrlg latlygpmaa gvdfvkntra qehlratlfa petvrviasg gtalvpgrar
      181 gvtlggclcl laaelgtlha rpsarggllc ledvgeetyr ldryltqllr agwleglrgv
      241 llgswegcad earlrhllad rlgglgvpva envgfghcag altipfgvsa eldadggtlt
      301 ldepalr
//
LOCUS       WP_392201437             139 aa            linear   BCT 20-JAN-2025
DEFINITION  TOBE domain-containing protein [Streptomyces sp. NPDC014991].
ACCESSION   WP_392201437
VERSION     WP_392201437.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014991
  ORGANISM  Streptomyces sp. NPDC014991
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 139)
  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 10007583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Streptomyces sp. NPDC014991"
                     /db_xref="taxon:3364935"
     Protein         1..139
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13983
     Region          1..138
                     /region_name="MopI"
                     /note="Molybdopterin-binding protein MopI [Coenzyme
                     transport and metabolism]; COG3585"
                     /db_xref="CDD:442804"
ORIGIN      
        1 mtlsirnqlp gtvtevhpge vmatvgvrlt ggqnltaait leaveqlgla pgssvhalvk
       61 stevslatnr vtglsirnql pgavtqlvvg dvmasvkvtv dggeltavit rdaaedlglf
      121 vgsdvialik atevslata
//
LOCUS       WP_392201622             279 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC014991].
ACCESSION   WP_392201622
VERSION     WP_392201622.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014991
  ORGANISM  Streptomyces sp. NPDC014991
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 279)
  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 279)
  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 16111081
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces sp. NPDC014991"
                     /db_xref="taxon:3364935"
     Protein         1..279
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31369
     Region          21..72
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(23,27,52)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(26,51)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(33..34,45,48,52..53)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          93..269
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mpqrlvitgr sqeprarfte elrhlrserg lslrdlakev gwdssqfskl esgqtlggpe
       61 vvqaldqfyg tpgllvtlwe lavadptqfr eqyrrymvle seaislwhya vsappgllqt
      121 agyarealaa gglkgseldq qvearvgrrm llegddappf rvilseavlr tplrdtkawr
      181 eqmeylaeas qrpnitlhvl pfsagphglm ntavkflrll dgrtvayten dvrgelieen
      241 nevehlqrty davrdlslyp aesqtfilrm leepcesst
//
LOCUS       WP_392199739             387 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC014991].
ACCESSION   WP_392199739
VERSION     WP_392199739.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014991
  ORGANISM  Streptomyces sp. NPDC014991
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 387)
  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   5  (residues 1 to 387)
  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   6  (residues 1 to 387)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 387)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 387)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Streptomyces sp. NPDC014991"
                     /db_xref="taxon:3364935"
     Protein         1..387
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38847
     Region          40..>68
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          89..378
                     /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 mgrvnrtrsg gpaganlgav rshngalvlg llrdagaegi srlelaertg ltpqavskit
       61 arlreeglaa eagrrastgg kprtvlrlvp eaghavgvhl drdelrvvla dldgavvrer
      121 raaldlgaga ravldavcgt veglvaerlg aaaageggla gvgsllgvgv alpgpldhvr
      181 gilhrvtgfp ewdgfplrda lagrlkvpvv vdkdtnaaal glavgneega agdsfaylhl
      241 gtglgaglvi ggsvhrgart gagefghqvi qldgplcecg nrgcvevlcl gaaargevae
      301 aarvlgvaag nlvglldidv vllggrtvag apevyvrgvg evlrararre gtraggvpvr
      361 vaprgerava egaaqlllap lfgrget
//
LOCUS       WP_392202691             224 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces sp. NPDC014991].
ACCESSION   WP_392202691
VERSION     WP_392202691.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014991
  ORGANISM  Streptomyces sp. NPDC014991
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Streptomyces sp. NPDC014991"
                     /db_xref="taxon:3364935"
     Protein         1..224
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24281
     Region          2..213
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 mssrervlgr vrraladaer ddrtyeqavp reylrehgag dvgrtvella enladyralv
       61 hrttpeelpy limrllaerg srsvvvppgl ppewlsaada trvhdraast pheldrvdsv
      121 vtgcavaiae tgtivldgsp dqgrrritlv pdhhicvvrv peqvvssvpq glerldptrp
      181 ltwisgpsat sdielnrveg vhgprtlevv lvggqpsges pvav
//
LOCUS       WP_392203294             242 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease H family protein [Streptomyces sp. NPDC014891].
ACCESSION   WP_392203294
VERSION     WP_392203294.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014891
  ORGANISM  Streptomyces sp. NPDC014891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptomyces sp. NPDC014891"
                     /db_xref="taxon:3364929"
     Protein         1..242
                     /product="ribonuclease H family protein"
                     /EC_number="3.1.26.4"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=24791
     Region          4..141
                     /region_name="RNase_HI_prokaryote_like"
                     /note="RNase HI family found mainly in prokaryotes;
                     cd09278"
                     /db_xref="CDD:260010"
     Site            order(10..13,45..47,50,72,122)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260010"
ORIGIN      
        1 mgekiiaacd gaskgnpgpa awawvigrad gaidrweagp lgratnnvae ltalerllet
       61 ldpatpvevr mdsqyamkav ttwlpgwrrk gwktssgspv ankdlvvrid alltgrsvdf
      121 vyvpahqvdg dplndaadra ashtartqep assaagaplp ppesptrasa prtrssapsg
      181 sagasaagsa vgsggasgar rtrssgatlk arfpgrcrcg kaydkgetia knpdgwghpa
      241 cv
//
LOCUS       WP_392203408             253 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Streptomyces sp.
            NPDC014891].
ACCESSION   WP_392203408
VERSION     WP_392203408.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014891
  ORGANISM  Streptomyces sp. NPDC014891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 253)
  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 253)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptomyces sp. NPDC014891"
                     /db_xref="taxon:3364929"
     Protein         1..253
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25757
     Region          3..239
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 mvrvaavgdi hlgeesggll rpsfatlplc advlllagdl trhgtvaeae vvaeevrnlg
       61 vpvvavlgnh dyhadqeeev arvltgagvs vlegasvtlp vgggtvgiag akgfcggfag
      121 rsagefgepv mkefvrtarr aadglhrala elasdgcrar ialthyapvp dtlageptei
      181 hpflgsylla eaidasgadl avhghahlgt ehgltaggvr vrnvaqpvig rafalyhlpl
      241 trtggaidpe arg
//
LOCUS       WP_392204575             435 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC014891].
ACCESSION   WP_392204575
VERSION     WP_392204575.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014891
  ORGANISM  Streptomyces sp. NPDC014891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 435)
  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 435)
  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
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 435)
  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   5  (residues 1 to 435)
  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   6  (residues 1 to 435)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 435)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 435)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Streptomyces sp. NPDC014891"
                     /db_xref="taxon:3364929"
     Protein         1..435
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45525
     Region          10..>60
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          80..403
                     /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 mhartgrtvr dlrrenrtav lrrlyfegpm srltlgpatg lssgsvsnvv aelvadglve
       61 eagsvdsagg rprtlvriap ssgfmigvdi getrvrielf dltltelart erplacsgpr
      121 tarydvdlvv ghlrdgiaev lrlaevpadr ligvgvgvpg ivardagdga vvhgqtvgwd
      181 avpferllra avdlpesvpy widngaktlg qaemwfgagr garsavvvlf gsgvgacvvt
      241 dpmgpgraie wghltvgvrg rrcrcgaqgc leayagaeal lerwreaggv ppagadeeta
      301 ltamlaaayp aepgtepdat alavlaetae ylgagfadli nlfqperilv ggwaglqlgt
      361 rfletvtgya rdyaltypas rtgiglgtlg peavtvgaal lplvdffaqg grrperepav
      421 papawqsalq drvst
//
LOCUS       WP_392204647             217 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces sp. NPDC014891].
ACCESSION   WP_392204647
VERSION     WP_392204647.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014891
  ORGANISM  Streptomyces sp. NPDC014891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Streptomyces sp. NPDC014891"
                     /db_xref="taxon:3364929"
     Protein         1..217
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22813
     Region          9..214
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 mtggspvpda rarvlarira avadapeppe vtrdylgrhg tedpdalldl lhenltdyra
       61 hvhrtppsgl pglvarilae rgarsvvvpp glpeewlaat raerrtdtpr ltpraldgtd
      121 avvtgcalav aetgtivldg gpgqgrralt lvpdlhvcvv rapgqvaasv pqalprldpt
      181 rpltwisgps atsdieldrv egvhgprtle vvlltes
//
LOCUS       WP_392204978             171 aa            linear   BCT 20-JAN-2025
DEFINITION  SRPBCC family protein [Streptomyces sp. NPDC014891].
ACCESSION   WP_392204978
VERSION     WP_392204978.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014891
  ORGANISM  Streptomyces sp. NPDC014891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 171)
  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 10008053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Streptomyces sp. NPDC014891"
                     /db_xref="taxon:3364929"
     Protein         1..171
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=18125
     Region          5..143
                     /region_name="YndB"
                     /note="Chalcone/flavanone-binding protein YndB,
                     AHSA1/START/SRPBCC domain [Lipid transport and
                     metabolism]; COG3832"
                     /db_xref="CDD:443044"
ORIGIN      
        1 mtipatpmdt vtlerhiaag petvfglfvd rakwlswmgv dgtfdfgpgg syrtrvtged
       61 vaagrfitvd pprrivfswg wetgampapp ssepvppgts tveitlepap egtllhlihs
      121 glpsseacea haegwqhyvd rlairaeggd pgpdawarge pgngprapqd c
//
LOCUS       WP_392205825             420 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC014891].
ACCESSION   WP_392205825
VERSION     WP_392205825.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014891
  ORGANISM  Streptomyces sp. NPDC014891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 420)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Streptomyces sp. NPDC014891"
                     /db_xref="taxon:3364929"
     Protein         1..420
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43477
     Region          80..261
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          267..394
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mngqpisgas vgatgrrgrr ggvrlqalaa galllvltac gggetangga ggqgpaaqgg
       61 gkqdnaasqa vvtilpkdga davatsgvlk vtaaqgkltt vtvadskgta vegriaadga
      121 swtptahlaa atqykvhaia kdaegresak dttfttlvpk ntfigqytpe dgstvgvgmp
      181 vsinftrgit dpeavekaik vtavpsvpie ghwfgndrld frpenywaag tkvtvhlnld
      241 gvegrpgvyg kqkktisfti grrqvstvda saktmkverd gkiiktipit agapstttyn
      301 gqmvisekyk vtrmngatvg fggeydikdv phamrlstsg tfvhgnywag agtfgsanvs
      361 hgcvglqdar gagdgsmpaa wfydrsiigd vvvvknskdk qiqpenglng wnmdwsewik
//
LOCUS       WP_392206064             541 aa            linear   BCT 20-JAN-2025
DEFINITION  peptide ABC transporter substrate-binding protein [Streptomyces sp.
            NPDC014891].
ACCESSION   WP_392206064
VERSION     WP_392206064.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014891
  ORGANISM  Streptomyces sp. NPDC014891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11467924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Streptomyces sp. NPDC014891"
                     /db_xref="taxon:3364929"
     Protein         1..541
                     /product="peptide 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=58425
     Region          37..533
                     /region_name="OppA"
                     /note="ABC-type oligopeptide transport system, periplasmic
                     component [Amino acid transport and metabolism]; COG4166"
                     /db_xref="CDD:443327"
ORIGIN      
        1 mrgathakwa alatavalaa tacgggdsgg gggadgivss swgdpqnple pantnevqgg
       61 kvlsmifrgl kqydpktgea kdmlaekiet tdstnftitv kdgwtfsnge kvtaksfvda
      121 wnyganlknn qknayffgqi egydqvhpek geptaetmsg lkvtgpqtft vkltqkfstw
      181 pitlgyaafs plpqtfytdh aawlskpvgn gpytvdsysk gsqmalkrwd aypgpdkaqn
      241 ggitlkvytd nntaytdlta gnldlvddvp asqlknvead lgdryinvpa giiqtlsfpf
      301 ydpawnkpgq eklrqglsma idrdqitqti fqktrtpavd wtspvlgedg gfkdvcgdfc
      361 kydaaeakkl vaegggipgg tmkisynadt gshkewvdav cnsinralgn nkacvgnpvg
      421 tfadfrnqvt qskmdgpfra gwqmdypliq nflqplyytn assndgkytd pqfdklvnea
      481 naeadtakai glfqqaeevl rddmgaiplw yqngsagyse rvgnvtlnpf svpvydqikv
      541 n
//
LOCUS       WP_392206412             301 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Streptomyces sp. NPDC014891].
ACCESSION   WP_392206412
VERSION     WP_392206412.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014891
  ORGANISM  Streptomyces sp. NPDC014891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Streptomyces sp. NPDC014891"
                     /db_xref="taxon:3364929"
     Protein         1..301
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31966
     Region          1..295
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mlldtaslyf rayfgvpdsv rapdgspvna vrglldfitr lvqdhrpdel vacwdddwrp
       61 qwrvdlipsy kahrvaeete tgpdeeeipd tlspqvpvie dvlaalgiar igaagyeadd
      121 vigtlagrap gpvdivtgdr dlfqlvddar gvrvlyprkg vgdcdlvdae fiaakygvrp
      181 dqyadfaalr gdasdglpgv kgigektaaq lvteygdlag vraaagdrts kltpakrrgi
      241 veaaayldva ptvvrvagdv plpefdatlp kaprdpaald alakrwglgg avgrllpvla
      301 h
//
LOCUS       WP_392206616             276 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC014891].
ACCESSION   WP_392206616
VERSION     WP_392206616.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014891
  ORGANISM  Streptomyces sp. NPDC014891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 276)
  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 276)
  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 276)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptomyces sp. NPDC014891"
                     /db_xref="taxon:3364929"
     Protein         1..276
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30638
     Region          17..68
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          90..264
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mvnirsldps aspldyygse lrrlreaagl gqsqlggvvf ctgsligqie takkvptrdf
       61 seridaalmt ggfftrlvgl vlrsqlptwf qpyaemeaka ayistyqcql vygllqtpay
      121 aravlgvehs drldemvaar verqrilerd rppvvwvvld eaaltreigg rhvmraqley
      181 lltfasepwv qiqvlpfkag ehaavmgsft llrfdgdpdl fyaesydmgh mtanpevmre
      241 rsvgyarlqa talsvedsae liarvmeery ghggla
//
LOCUS       WP_392208496             279 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            griseoluteus].
ACCESSION   WP_392208496
VERSION     WP_392208496.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseoluteus
  ORGANISM  Streptomyces griseoluteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 279)
  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 279)
  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 10611723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces griseoluteus"
                     /db_xref="taxon:29306"
     Protein         1..279
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29153
     Region          15..77
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(21,25,50)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(24,49)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(31..32,43,46,50..51)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          169..253
                     /region_name="DUF2690"
                     /note="Protein of unknown function (DUF2690); pfam10901"
                     /db_xref="CDD:402475"
ORIGIN      
        1 mtgtappaat pactrlakal qdlksrtgls ltalagrtay sksswaryln gsqlaprevv
       61 ealcalagqp perllalwel aevewsgrhr tsaapsplpa rpagdaatgd rpahrwntrr
      121 rralaaaaca vtlaaatwlt asrgthtega agrtapsaap apgcraekct dedpemmgca
      181 vpgqtrrvdp pyrtrtgarl vvvlstrcha awalgwntrp gdafelsvpg gavervevad
      241 aldaedplft pmidagdlsg lrtcfipavg rqecvtaqg
//
LOCUS       WP_392208558             284 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces sp.
            NPDC014891].
ACCESSION   WP_392208558
VERSION     WP_392208558.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014891
  ORGANISM  Streptomyces sp. NPDC014891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces sp. NPDC014891"
                     /db_xref="taxon:3364929"
     Protein         1..284
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=30357
     Region          1..263
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mririlgplh aetagapvvp saaktrqima llalhpghpv pvavlkeelw galppssahs
       61 tlqtyvlrlr rslaaalggp ygtegtgags gaararalla tghdgyllrv aesdvdafaf
      121 qraaqaghsa fadgdsaraa rllrealalw kgpalvdvra gaalrihaar leearllate
      181 rrldaelrlg lhgellaelv eltrlhpane rlhaqamvaf yragrqseal qlyrglrrrl
      241 veelglepap rlqrlhqaml svdprldapa hggrptptfd lyaa
//
LOCUS       WP_392209167             380 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            griseoluteus].
ACCESSION   WP_392209167
VERSION     WP_392209167.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseoluteus
  ORGANISM  Streptomyces griseoluteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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   4  (residues 1 to 380)
  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 380)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Streptomyces griseoluteus"
                     /db_xref="taxon:29306"
     Protein         1..380
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40750
     Region          20..354
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 mtltvptrkp ptsaegsdap vfavdglwkv fgpkpervpa dpalaalspa elraetgcta
       61 avrdvsfevr kgevfvvmgl sgsgkstlvr cltrliepta gtiaidgedv ramdrgrlre
      121 lrrhraamvf qhfgllphrt vldnvaygle iqgmgraerr ekaaevvakv glagmekrrp
      181 gqlsggqrqr vglaralavd pevllfdepf saldplirrd mqdevarlhs eegrtmvfit
      241 hdltealklg drialmrdgr vvqlgtpeei vnspaddyvr efvrdvpreq vvtcrtamrp
      301 asleeagrgp avrpeapvae aieavarage parvmdhgtc mgvvdsdall nvvagtgtaa
      361 paereaeptl vsaapeskav
//
LOCUS       WP_392209260             351 aa            linear   BCT 20-JAN-2025
DEFINITION  BMP family lipoprotein [Streptomyces griseoluteus].
ACCESSION   WP_392209260
VERSION     WP_392209260.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseoluteus
  ORGANISM  Streptomyces griseoluteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Yousief,S.W., Bahey-El-Din,M. and Zaghloul,T.I.
  TITLE     Immunization with the basic membrane protein (BMP) family ABC
            transporter elicits protection against Enterococcus faecium in a
            murine infection model
  JOURNAL   Microbes Infect 22 (3), 127-136 (2020)
   PUBMED   31585177
REFERENCE   2  (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   3  (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   4  (residues 1 to 351)
  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   5  (residues 1 to 351)
  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 11448319
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Streptomyces griseoluteus"
                     /db_xref="taxon:29306"
     Protein         1..351
                     /product="BMP family lipoprotein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /calculated_mol_wt=35869
     Region          39..348
                     /region_name="Med"
                     /note="Lipoprotein Med, regulator of KinD/Spo0A, PBP1-ABC
                     superfamily, includes NupN [Signal transduction
                     mechanisms]; COG1744"
                     /db_xref="CDD:441350"
ORIGIN      
        1 mrrvaklsaa ciataalals atacgstsse ndkssassgd gkgvkiglaf dvggrgdhsf
       61 ndsaargtdk askefggsvk eltakssdte adreqrlsdl adagynpiva vgyayatsvd
      121 kvaakypkts fgivdsvvka knadsitfte eqgsylagva aalktktkhv gfiggvdvpl
      181 ikkfqagyaq gvkdtdpkik vdvqylshgs dtsgfaspdk gkeaaqgmld ngadivysaa
      241 gssgngaiea vngkkgawai gvdsdqynip glakykssil tsvvknvdvg vydfiksvhd
      301 gkpltgnnvy slakngvsla tsggfiddvq pkldaaktki vdgsvkvktt p
//
LOCUS       WP_392209328             415 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces griseoluteus].
ACCESSION   WP_392209328
VERSION     WP_392209328.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseoluteus
  ORGANISM  Streptomyces griseoluteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces griseoluteus"
                     /db_xref="taxon:29306"
     Protein         1..415
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43354
     Region          68..247
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          254..385
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mtdskrrkgl tvasallggv lvltgcsggg nasasdgges sqakadeaaa qksseaqiai
       61 tpkdgsnnas innsatvkva kgtltgvsmt tadgkpvegt lsadklswkp ttqlerstty
      121 klaaeakdsd grvahenasf ttvspsnsfi gnftpdngst vgvgmpvsin fdkaitnkaa
      181 vqkgitvsss sgqevvghwf nanridfrpe sywkenstvt lklsldgveg angvygvqqk
      241 tvtfhvgrnq vsyvdaktkq mkvtqdgkvv kqipisagsp enktyagvmv msekfeqtrm
      301 ngatvgftdd dgkgeydikd vphairltgs gtflhgnywg aksifgsent shgcvglsdt
      361 kgakdpntpa awvfnhslvg dvvvikntgd ktvapdngln gwnmdwaqwk agsav
//
LOCUS       WP_392209486             540 aa            linear   BCT 20-JAN-2025
DEFINITION  peptide ABC transporter substrate-binding protein [Streptomyces
            griseoluteus].
ACCESSION   WP_392209486
VERSION     WP_392209486.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseoluteus
  ORGANISM  Streptomyces griseoluteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 540)
  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 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   3  (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
REFERENCE   4  (residues 1 to 540)
  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 540)
  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 11467924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Streptomyces griseoluteus"
                     /db_xref="taxon:29306"
     Protein         1..540
                     /product="peptide 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=59045
     Region          8..535
                     /region_name="OppA"
                     /note="ABC-type oligopeptide transport system, periplasmic
                     component [Amino acid transport and metabolism]; COG4166"
                     /db_xref="CDD:443327"
ORIGIN      
        1 mrgftharwl tgaaavmlva tgcgggasgt adggmltssw gdpqnplepa ntnevqggkv
       61 ldmvfrglkr ydpktgearn mlaqsiettd srhytvklke gwtfsngekv tarsftdawn
      121 ygaslknkqk nayfygyieg ydqvhpemgs qhadtlsglk vvddrtftvt lnqkfsgfpd
      181 tlgyaafapl prafftdhaa wlktpvgngp ytiesytkgs qmtlrkwngy pggdkalndg
      241 vilkvytdsn taytdlmagn ldladdipap qlknvrtdlg eryintpagi iqtlafpyyd
      301 erwnrpgmek vrtglsmain rdqitrtifq rtrtpatdwt spvlgtdggf kaglcgract
      361 ydpaaakrlv rqgggipggs lkltynadtg shrewvdavc nsinhalgdd nacvgnpvgt
      421 fadfrnqmgq hkmsgpfrag wqmdypliqn flqplyftga ssndgqwsns efdelvdran
      481 aetdpaksva tfqqaeevvr dnmaaiplwy qngnagysqr ltgvqlnpfs vpvynqikvs
//
LOCUS       WP_392210242             408 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC014891].
ACCESSION   WP_392210242
VERSION     WP_392210242.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014891
  ORGANISM  Streptomyces sp. NPDC014891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 408)
  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 408)
  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 408)
  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 11448557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces sp. NPDC014891"
                     /db_xref="taxon:3364929"
     Protein         1..408
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43988
     Region          1..64
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
ORIGIN      
        1 mpddnvqmtv dnellkarre hrglsrsalg glvgrsedwv kkvergdrtv rslamivqla
       61 rvlgcqdvne ltradvsvpv ydggkvthpg vtalrsaiha plfaaagtpe dvghlagrvr
      121 qawdvwhrar dqrtavasvl pslieaghat vraaegaekr rasvvlsety alaqqyvahi
      181 vepelywviv drarmaaeqa ddpialasaa wiignglrvs gyteealrmv adaadilrpq
      241 leggsdrlrg mfgslclhaa vtaaqdgrdg dawrwhsead rtatnlgaqy ahpwtmfgtg
      301 nvvvhavtig adlrtpgial qqltetdpss ipsverrsrl fldaakaehv rkekasalqy
      361 lrlayetspe avryvpsgra laadlertst galaftahql aedigvaa
//
LOCUS       WP_392210366             420 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces griseoluteus].
ACCESSION   WP_392210366
VERSION     WP_392210366.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseoluteus
  ORGANISM  Streptomyces griseoluteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 420)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Streptomyces griseoluteus"
                     /db_xref="taxon:29306"
     Protein         1..420
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=44697
     Region          54..241
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          249..368
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mnhtartrtv vssamlvaal gagvtgcgsd gnalssepyd aadqivfnap tdkakqvdpd
       61 kplevtlkss egritdvtam datgryvage laadggrwhs tsplaanahy tvrvsteddd
      121 gapgrkvlnf dttktagkks lgvtfgpeag eygvgqpita nldqpvkdka qravvesglr
      181 vdsvpavqgs wywvsdkelh yrpkeywpah atvqvhsnld gikitdrlrg gkskdlkiti
      241 gdkveaitda athkltfykn gevintipvt tgkpgfdtrn gvkvilekqy mvrmrgttvg
      301 iaegssdsyd lsvyyaarvt wsgeyvhaap wsvgsqgyan vshgctgmst gnaewffdhv
      361 ragdivkvvn snghamedfg ngfgdwnvdw kkwgtgsalt gaaqngsapr dsvrlrpaaa
//
LOCUS       WP_392210766             383 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces griseoluteus].
ACCESSION   WP_392210766
VERSION     WP_392210766.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseoluteus
  ORGANISM  Streptomyces griseoluteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 383)
  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 383)
  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
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 383)
  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   5  (residues 1 to 383)
  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   6  (residues 1 to 383)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 383)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 383)
  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 11973053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Streptomyces griseoluteus"
                     /db_xref="taxon:29306"
     Protein         1..383
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40066
     Region          <10..62
                     /region_name="COG3398"
                     /note="Predicted transcriptional regulator, contains two
                     HTH domains [Transcription]"
                     /db_xref="CDD:442625"
     Region          84..368
                     /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 mgqltggdps llrrinsavv lralrdtdca tlteitratg lsrptvegvv eglteaglvv
       61 eraaeegtar rqgrparrfr fraeaghllg leigahrvva avsdldgrvl gtqtrdvdek
      121 apaderlerl rgtvaellrr tgvprgslra vgvgtpgive adgtvrlgta lpqwtglhlg
      181 erlsrsfrcp vlvendanva avaehwqgaa kdtddvvfvl aglspgagsl iggrlhrgyg
      241 gaageigalh llgreatpea llsttdeplp pldeqavtev falaregdgs alaaverfiq
      301 rlvhdvaalv laldpelvvv ggwaagldgv ldplrrelar yclrppaval sllgeavvat
      361 galrlaldhv erqlfavega vga
//
LOCUS       WP_392211150             420 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC014983].
ACCESSION   WP_392211150
VERSION     WP_392211150.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014983
  ORGANISM  Streptomyces sp. NPDC014983
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 420)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Streptomyces sp. NPDC014983"
                     /db_xref="taxon:3364933"
     Protein         1..420
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=44600
     Region          55..240
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          248..367
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mnhiprtrtv vscvllvtal gagttacgsd gdplsaapyd aaglisfngp tgagkradpd
       61 kplevtvkde gritdvtaqd stgryvagel aadgsrwhst splaasahyt vtvstedddg
      121 apgrkvlsfd ttkpatkkql gitfgpdtgq ygvgqiitaq lgqeikdkaq ravverglrv
      181 dsvpavpgsw ywvsgkelhy rpkdywpvha tiqvhsnldg vkiggglwgg rtkpvklttg
      241 drvealtdaa ahemtvfrng aviktmpvtt gkpgyetrng vkvvlekqyf vrmrgvtvgi
      301 aegsrdsydl pvyyatrvtw sgeyvhaapw svgsqgyanv shgctgmsts naqwffntvq
      361 egdivrvvns ggepmepfgn gfgdwnvtwk kwrtgsaltg lpgngqspss davrlqptav
//
LOCUS       WP_392211504             707 aa            linear   BCT 20-JAN-2025
DEFINITION  DNA gyrase/topoisomerase IV subunit B [Streptomyces sp.
            NPDC014983].
ACCESSION   WP_392211504
VERSION     WP_392211504.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014983
  ORGANISM  Streptomyces sp. NPDC014983
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Tari,L.W., Trzoss,M., Bensen,D.C., Li,X., Chen,Z., Lam,T.,
            Zhang,J., Creighton,C.J., Cunningham,M.L., Kwan,B., Stidham,M.,
            Shaw,K.J., Lightstone,F.C., Wong,S.E., Nguyen,T.B., Nix,J. and
            Finn,J.
  TITLE     Pyrrolopyrimidine inhibitors of DNA gyrase B (GyrB) and
            topoisomerase IV (ParE). Part I: Structure guided discovery and
            optimization of dual targeting agents with potent, broad-spectrum
            enzymatic activity
  JOURNAL   Bioorg Med Chem Lett 23 (5), 1529-1536 (2013)
   PUBMED   23352267
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Gadelle,D., Filee,J., Buhler,C. and Forterre,P.
  TITLE     Phylogenomics of type II DNA topoisomerases
  JOURNAL   Bioessays 25 (3), 232-242 (2003)
   PUBMED   12596227
REFERENCE   3  (residues 1 to 707)
  AUTHORS   Wang,J.C.
  TITLE     Cellular roles of DNA topoisomerases: a molecular perspective
  JOURNAL   Nat Rev Mol Cell Biol 3 (6), 430-440 (2002)
   PUBMED   12042765
REFERENCE   4  (residues 1 to 707)
  AUTHORS   Champoux,J.J.
  TITLE     DNA topoisomerases: structure, function, and mechanism
  JOURNAL   Annu Rev Biochem 70, 369-413 (2001)
   PUBMED   11395412
REFERENCE   5  (residues 1 to 707)
  AUTHORS   Roca,J.
  TITLE     The mechanisms of DNA topoisomerases
  JOURNAL   Trends Biochem Sci 20 (4), 156-160 (1995)
   PUBMED   7770916
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Streptomyces sp. NPDC014983"
                     /db_xref="taxon:3364933"
     Protein         1..707
                     /product="DNA gyrase/topoisomerase IV subunit B"
                     /EC_number="5.6.2.2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003918 - DNA topoisomerase type II
                     (double strand cut, ATP-hydrolyzing) activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006265 - DNA topological change [Evidence
                     IEA]"
                     /calculated_mol_wt=77075
     Region          21..701
                     /region_name="GyrB"
                     /note="DNA gyrase/topoisomerase IV, subunit B
                     [Replication, recombination and repair]; COG0187"
                     /db_xref="CDD:439957"
ORIGIN      
        1 mtadtsvpst allagadrdg snytarhllv legleavrkr pgmyigstds rglmhclwei
       61 idnsvdealg gycdhievil hddasvevrd ngrgipvdve pktglsgvev vmtklhaggk
      121 fgggsyaasg glhgvgasvv nalsarldve vdrsgsthai sfrrgvpgaf agagadakfe
      181 aksglrkskk ipktrtgtrv rywadrqifl kdaklsldtl hqrarqtafl vpgltivvrd
      241 eyglgeggsk geesfrfdgg isefceylan dkpvcdvlrf sgkgtfketv pvldehgqmt
      301 ptevarelgv dvalrwgtgy dttlrsfvni iatpkggthv sgfeqaltqt mndvlrakkl
      361 lrvaednivk ddalegltav vtvrlaepqf egqtkevlgt saarrivnqv vtkelkaflt
      421 atkrdaaaqa rvvmekvvaa artrvaarqh kdaqrrktal essslpakla dcrsddvdrs
      481 elfivegdsa lgtaklarns efqallpirg kilnvqrssv tdmlknaecg aiiqvigags
      541 grtfdidqar ygkiimmtda dvdgshircl lltlfqrymr pmveagrvfa avpplhriev
      601 vqpkkgqdky vytysdrelr dklmefqtkg irykdsiqry kglgemdadq laettmdprh
      661 rtlrrinlsd leaaeqvfdl lmgndvaprk efisssaatl drsrida
//
LOCUS       WP_392211702             388 aa            linear   BCT 20-JAN-2025
DEFINITION  M20 metallopeptidase family protein [Streptomyces sp. NPDC014983].
ACCESSION   WP_392211702
VERSION     WP_392211702.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014983
  ORGANISM  Streptomyces sp. NPDC014983
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Lindner,H.A., Lunin,V.V., Alary,A., Hecker,R., Cygler,M. and
            Menard,R.
  TITLE     Essential roles of zinc ligation and enzyme dimerization for
            catalysis in the aminoacylase-1/M20 family
  JOURNAL   J Biol Chem 278 (45), 44496-44504 (2003)
   PUBMED   12933810
REFERENCE   2  (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 11444961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Streptomyces sp. NPDC014983"
                     /db_xref="taxon:3364933"
     Protein         1..388
                     /product="M20 metallopeptidase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40232
     Region          11..368
                     /region_name="AbgB"
                     /note="Metal-dependent
                     amidase/aminoacylase/carboxypeptidase [General function
                     prediction only]; COG1473"
                     /db_xref="CDD:441082"
ORIGIN      
        1 mssptdsaal lraelerqip aavelrhrlh ahpcpsgdea etrdavlaal ptphgvtkta
       61 dtgavvrigg pgpavavrge mdalavpeet gvswrsrrpg lmhacghdvh laavvalara
      121 vdrvggprpl lvvlqpreet ypsgareiie egvlereqcr avvgahvqpl lpagevsctp
      181 gvvnassdef tvtvrgsggh aayphltsdp vlalahvvva lqslvsraid pmtsvvlsvt
      241 vlsagdaanv vpgtatargi vramrtadre tiharmaeva slvarsqgce aeveivhgep
      301 aldndvalaa aatpllrqag levshslrsa gsddfsyfse rfpslmlfvg thggaarlhs
      361 ssflpsddrv rdvaeallag ylaaalpv
//
LOCUS       WP_392211886             307 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Streptomyces sp. NPDC014983].
ACCESSION   WP_392211886
VERSION     WP_392211886.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014983
  ORGANISM  Streptomyces sp. NPDC014983
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptomyces sp. NPDC014983"
                     /db_xref="taxon:3364933"
     Protein         1..307
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32225
     Region          4..305
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mkpltrpprl apgarvavva psgpvpeerv qagldvlrgw dldpvvmphv ldrhaelgyl
       61 agrdadraad lqrawcdpsv aavlcarggy gaqrmadlvd weamraagpk vfvgfsdvth
      121 lhqafatrld lvtlygpvaa gidfiksara qehlkatlfa petvrtltta gtalvpgraq
      181 gvtlggylgg laadlgtpla rtgarggllm iedvtelpyr idrlitqllr sgwldgvagi
      241 glgswercgp yeevravlad rlgglgvpvl eemgfghced altvpfgvaa eldadagtlt
      301 ltepals
//
LOCUS       WP_392212454             403 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC014983].
ACCESSION   WP_392212454
VERSION     WP_392212454.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014983
  ORGANISM  Streptomyces sp. NPDC014983
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  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 403)
  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
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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   5  (residues 1 to 403)
  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   6  (residues 1 to 403)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 403)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces sp. NPDC014983"
                     /db_xref="taxon:3364933"
     Protein         1..403
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41705
     Region          1..>63
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          81..392
                     /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 magtagtpgt prvlramndr aaldlllehg plsrtrigdl tglskptasq llarleaagl
       61 vrvtgtsegr pgpsaqlyav dpgaayaagl dvapgriraa vaditgrtvg eyelptpgrr
      121 paqsvvrqvt daldgavkaa glargevhrl vigtpgafdp ntgrlryash lpgwhspall
      181 ddlaaalpmp veyendvnlv alaeqrlgaa rghgdfvllw neeglgaalv lggrlhrgwt
      241 ggagevgflp vpgtplvrqv tkansggyqe lagaqelpkl arelgvpdvp sgpyteaagh
      301 llaraadhat gphrellrty atrlatglaa lvsvldpelv vlsgsaltag gevlraliqa
      361 eleelaaarp rlvlgdlreh pvlrgaleaa lattrdevfd tsr
//
LOCUS       WP_392212526            1490 aa            linear   BCT 20-JAN-2025
DEFINITION  Rne/Rng family ribonuclease [Streptomyces sp. NPDC014983].
ACCESSION   WP_392212526
VERSION     WP_392212526.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014983
  ORGANISM  Streptomyces sp. NPDC014983
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1490)
  AUTHORS   Kime,L., Jourdan,S.S. and McDowall,K.J.
  TITLE     Identifying and characterizing substrates of the RNase E/G family
            of enzymes
  JOURNAL   Methods Enzymol 447, 215-241 (2008)
   PUBMED   19161846
REFERENCE   2  (residues 1 to 1490)
  AUTHORS   Callaghan,A.J., Marcaida,M.J., Stead,J.A., McDowall,K.J.,
            Scott,W.G. and Luisi,B.F.
  TITLE     Structure of Escherichia coli RNase E catalytic domain and
            implications for RNA turnover
  JOURNAL   Nature 437 (7062), 1187-1191 (2005)
   PUBMED   16237448
REFERENCE   3  (residues 1 to 1490)
  AUTHORS   Li,Z., Pandit,S. and Deutscher,M.P.
  TITLE     RNase G (CafA protein) and RNase E are both required for the 5'
            maturation of 16S ribosomal RNA
  JOURNAL   EMBO J 18 (10), 2878-2885 (1999)
   PUBMED   10329633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1490
                     /organism="Streptomyces sp. NPDC014983"
                     /db_xref="taxon:3364933"
     Protein         1..1490
                     /product="Rne/Rng family ribonuclease"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=156741
     Region          <281..429
                     /region_name="rne"
                     /note="ribonuclease E; Reviewed; PRK10811"
                     /db_xref="CDD:236766"
     Region          735..1138
                     /region_name="CafA"
                     /note="Ribonuclease G or E [Translation, ribosomal
                     structure and biogenesis]; COG1530"
                     /db_xref="CDD:441139"
ORIGIN      
        1 mleptepneg selntpsdtl pprrrrraas rpagppvaae apaevtvpai paaeteetde
       61 aveaeeaaaa ataveteeaa aaqaaeeaap aarprrratr rasapvgapa ateaaetvap
      121 apaaevaegg evvvgedaap rrvrrratrs vatpsaveae avaaeapaee eapaarprrr
      181 ttrraaapaa evaeavasve tvvpaaetaa agaetveevp aarprrratr raaapaaeva
      241 eavasaeava saeavvpaaa eaapgteeaa paarprrrat rrvsapvgsp esaeatetvv
      301 ratvedaaea vtadeepaae aaparprrra trrasapaga pkaaeetpva aevlvaeapl
      361 aevpvaeapv aepvvevtde daaprrtrrr atrrvtapes tpaaeaahtp evpvtthtte
      421 papaaesvpa aaeasgaaes aaprrarrra vrpasgfsep araaeaeegs rrparpavav
      481 fqapvfaepr fqtperaaae aaaeavevae paepeesaey aeeraetgsr rrrrrraerv
      541 eeapaaeava edeeeepesa egegegedae gyeesssrrr rrrggrrrrr gdaaegegae
      601 dgteelaaeq aeqdaedtae qeeeddeear geesggssag srrrrrrrrr agdtsmdtep
      661 ssddpertvv kvreprkqse psdevqsikg strleakkqr rregreqgrr rvpiiteaef
      721 larreaverv mvvrqhgert qigvlednvl vehyvnkeqs tsyvgnvylg kvqnvlpsme
      781 aafidigkgr navlyagevn fealgmgngp rrietalksg qsvlvqvtkd pighkgarlt
      841 sqvslpgryl vyvpegsmtg isrklpdter arlktilkki vpedagvivr taaegasede
      901 lrrdverlqa qwediqkkak sgnaptllyg epdmtvrvvr difnedfskv ivsgddawqt
      961 ihgyvahvap dlagrlskwt sevdafatyr ideqlakald rkvwlpsggs lvidrteamv
     1021 vidvntgkft gqggnleetv trnnleaaee ivrqlrlrdl ggiividfid mvlesnrdlv
     1081 lrrlleclgr drtkhqvaev tslglvqmtr krvgqglles fsetcvhcng rgvivhleqp
     1141 gsggggggkr kkrgrggegq eqphehvhet aavavetgea vepeietaae vaaeiaapva
     1201 laapefapde elyssvaeae aaagrgrvrr rasrrvsapa gapkaerpar kaaarakdse
     1261 eaveptaqdv taeeaaarpv rpepaaeala gpvaaedqvv papeaaevae eaapkgrtrr
     1321 ratrkvsapa gspagaeatv vtvaetapaa pvaepaveea papaesaapa rprrravrqa
     1381 aaptapeeta vvvvpaaase aaaeasveap agevpaeeas veeaaapakk tarkaakkat
     1441 akkaatkkta akktaakkta akkttakkaa atktaaakka aatkqptsvd
//
LOCUS       WP_392212593             277 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC014983].
ACCESSION   WP_392212593
VERSION     WP_392212593.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014983
  ORGANISM  Streptomyces sp. NPDC014983
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 277)
  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 277)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Streptomyces sp. NPDC014983"
                     /db_xref="taxon:3364933"
     Protein         1..277
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31020
     Region          1..64
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          87..264
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mangsrqaaw effgaelkrr renaaltqse lgtlvfvsgg yigqfeqair kpqldvaqrl
       61 dtvlqtdgff erlwkklikd qryteyfaha aelerlatei ceyapavvpg llqtreyaqa
      121 vfwasnpfan eehieelvkg rtdrarllkd atrpvywavl hetvlripvg gpavmahqld
      181 hiaaltqehk allqvlpfaa gahpemgkmm wlmefedapp tvyteavrsg nlvdeplvvk
      241 rvrasydhir aaalspeasl aliesvaedy rrcastt
//
LOCUS       WP_392213519             213 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces sp. NPDC014983].
ACCESSION   WP_392213519
VERSION     WP_392213519.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014983
  ORGANISM  Streptomyces sp. NPDC014983
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Streptomyces sp. NPDC014983"
                     /db_xref="taxon:3364933"
     Protein         1..213
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23291
     Region          2..213
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 mnsrerilgr vrraladvpa nerpyeeavp rdylrehger tteetvdlla rnladyraiv
       61 hradaeelpl limrllaerg sqevmvppgl ppswmaaadp vrihdraglt pdridrvgsv
      121 vtgcavaiae tgtivldgsp dqgrrritlv pdhhicvvev pgrvvasvpq alerldptrp
      181 ltwisgpsat sdieldrveg vhgprtlevi llg
//
LOCUS       WP_392213617             280 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            griseoluteus].
ACCESSION   WP_392213617
VERSION     WP_392213617.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseoluteus
  ORGANISM  Streptomyces griseoluteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 280)
  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 280)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Streptomyces griseoluteus"
                     /db_xref="taxon:29306"
     Protein         1..280
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30794
     Region          <22..69
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          91..273
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 maraanklaa sgtarmvaaf akarreqmdl tqeelgalig ytasaisame tcaqpasdkm
       61 ltelervlgd gmgifemark fvlldkyppq fqdfalmeae avtlssyety vvaglfqtad
      121 yaraliggsf prlpdeqveq lvdarlarra lfdraeptam ielildesal rrpfgnwkil
      181 sgqlrslaed aerdnvciqi mpmergargt hagergnmvl vetaehhhvv ylevhdesvl
      241 vsdpakvarl ahryakirtq alspddsasl irklageqrt
//
LOCUS       WP_392213843             409 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC014983].
ACCESSION   WP_392213843
VERSION     WP_392213843.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014983
  ORGANISM  Streptomyces sp. NPDC014983
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Streptomyces sp. NPDC014983"
                     /db_xref="taxon:3364933"
     Protein         1..409
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=43961
     Region          62..328
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mtsspthrpt eavtprplav llharqpltt dpaatfdpar wetvvltdae adavlredap
       61 gdtpavhrap rdrwateirr lagdrpvqiv tndeyclisc aelragfglp arhpdhpahy
      121 idkvlmkerl aaagvrvprf laltdgvpdp gtgvplvtgt iglpavakpr reansrgvav
      181 lctepelrdw laghqgeegw qieefldgtf hhvnslvrdg vatpvqtgty lgplldlpdg
      241 rrlggwtvpf gselarrahe lndavvaalg aegsfvvhte favnredelv vvevagrapg
      301 alvselarlh aglnleeanl alqadlpvpq phptgtqaaw vwipvmpger hrytpettsk
      361 rlvhvrraaq hthtgtsgal gvsvllwhtd pdvlaadvrt aateawcga
//
LOCUS       WP_392214773             237 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Streptomyces sp. NPDC014983].
ACCESSION   WP_392214773
VERSION     WP_392214773.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014983
  ORGANISM  Streptomyces sp. NPDC014983
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 237)
  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 10007985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Streptomyces sp. NPDC014983"
                     /db_xref="taxon:3364933"
     Protein         1..237
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24833
     Region          37..227
                     /region_name="COG3786"
                     /note="L,D-peptidoglycan transpeptidase YkuD,
                     ErfK/YbiS/YcfS/YnhG family [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443000"
ORIGIN      
        1 mrhgvvasll plcalgllga apaprgpapv plparmadtg ggtqliiaqa pdtrsttgtv
       61 twwdlrngaw tqagsaparf ganglvegds rkqgtrttpt glydlpfgfg traapagtgi
      121 syravkessw wcqdnasssy nrwtdplped crateaehls ayggqyaygl vvgfnyhrpv
      181 rnrgagiflh vngkgatagc vsvpedsmrr ilrwvvpgkg phialgtssg vtgisry
//
LOCUS       WP_392215576             415 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC014983].
ACCESSION   WP_392215576
VERSION     WP_392215576.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014983
  ORGANISM  Streptomyces sp. NPDC014983
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces sp. NPDC014983"
                     /db_xref="taxon:3364933"
     Protein         1..415
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43290
     Region          66..247
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          254..385
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mtdgkrrngl vaasallggv lllsacsggd kasahgsges sqaqadaaaa qksseaqiav
       61 tpkdgsdnas innsgtvtvs kgtltgvtmt tedgkavagq laadklswkp tvqlerstty
      121 riaatakdsq griahenasf ttvspgnsfi gtftpdngst vgvgmpvsin fdkaitdkaa
      181 vqkgitvtss sgqevachwf nanrmdcrpe dywkegatvt lklaldgvqg angvygvqqk
      241 tvtfhigrnq vsyvdakthq mkitqdgkvv ktipisagap dhttyegrmv isekfkqtrm
      301 ngatvgftdd dgkgeydikd vphamrltts gtfihgnywg assvfgsvnt shgcvglqdv
      361 kgagdantpa awfydhslig dvvvvqntgd ktvspdngln gwnmdwaqwk agsav
//
LOCUS       WP_392215813             274 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC014983].
ACCESSION   WP_392215813
VERSION     WP_392215813.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014983
  ORGANISM  Streptomyces sp. NPDC014983
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 274)
  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 274)
  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 274)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Streptomyces sp. NPDC014983"
                     /db_xref="taxon:3364933"
     Protein         1..274
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30497
     Region          12..68
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          86..263
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 msvdrrprtp rekygeelrl rrlaagltqe elseqivcsp tlishyesgr rlpkpddarr
       61 vdralgtdgf fqrwledles kyidyfapva eleeqaaliq qfalslvpgv lqtddyaral
      121 frayspnhta ekldeavvtr tkrrrildgs trpvvwtlld eavvrrcvgg phvmaeqlhk
      181 vadmaeagrl rlhvlpygsg ahalmesylt lmsfedsapv ayvegfltgh lmddptlvaa
      241 sqtayalals dalsqqesla lvraaaeehv hgqq
//
LOCUS       WP_392216217             328 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC014983].
ACCESSION   WP_392216217
VERSION     WP_392216217.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014983
  ORGANISM  Streptomyces sp. NPDC014983
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 328)
  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 11599008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces sp. NPDC014983"
                     /db_xref="taxon:3364933"
     Protein         1..328
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=33999
     Region          63..160
                     /region_name="LDT_IgD_like_2"
                     /note="IgD-like repeat domain of mycobacterial
                     L,D-transpeptidases; cd13432"
                     /db_xref="CDD:240447"
     Region          165..290
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mgrrkggiai alvtgamlmg asacggggga kaggddakap grstasasas ptkpagppml
       61 ldtitpqtga tvgvampisv vftdpvaaka ratvekhmkv sasqpvagaw hwfgdrradw
      121 rpktywpsgt kvridadmkg vgngagrygv hdythtftvg ddvradvsvt ghtmrvtrng
      181 klvrtlsina gsaqyptwng tmavidkqek vhmtscsvgi scdkgspnyy dltlpwdvhl
      241 tqsgtyvhys tgdpnpgsgs argshgcvhl slsdakwfyg qveqgdpvti tgsprakaap
      301 dngyaafnls wdqwlagsss geattgtl
//
LOCUS       WP_392217408             218 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces sp. NPDC014983].
ACCESSION   WP_392217408
VERSION     WP_392217408.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014983
  ORGANISM  Streptomyces sp. NPDC014983
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Streptomyces sp. NPDC014983"
                     /db_xref="taxon:3364933"
     Protein         1..218
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22953
     Region          3..214
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 mttaretvlg rvrdalalsg rvpdleedaa apavprayrt grtlpdperl ellvdrlvdy
       61 raavrtcvaa rtseaiaeal rehgarrvgv pagldetwla gydgevlrds sdlpaprlav
      121 ldgvvtasav tcaetgtifl dgspdqgrra lslvpdlhvc vvdlssvvvg vpeavarlvp
      181 erpttlisgp satsdieler vegvhgprtl vvvirtda
//
LOCUS       WP_392217895             306 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Streptomyces griseoluteus].
ACCESSION   WP_392217895
VERSION     WP_392217895.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseoluteus
  ORGANISM  Streptomyces griseoluteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Streptomyces griseoluteus"
                     /db_xref="taxon:29306"
     Protein         1..306
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32893
     Region          1..300
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mtgrlmlldt aslyfrayfg vpdsvrapdg tpvnavrgll dfidrlvkdh rpdklvacmd
       61 adwrpqwrvd lipsykahrv aeehegapda eevpdtlspq vpvieevlda lgiarvgvag
      121 yeaddvigtf taradgpvdi vtgdrdlyql vddardirvl yplkgvgtlq ltdepwlrdk
      181 ygvdgrgyad lallrgdpsd glpgvpgvge ktaakllaef gdlagivaav edpkakltpt
      241 qrkrlteaap ylavapkvvr vaddaplpev dtalphtprd paaldalavr wglgsslqrl
      301 lttlea
//
LOCUS       WP_392218186             314 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Streptomyces sp. NPDC014983].
ACCESSION   WP_392218186
VERSION     WP_392218186.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014983
  ORGANISM  Streptomyces sp. NPDC014983
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces sp. NPDC014983"
                     /db_xref="taxon:3364933"
     Protein         1..314
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33421
     Region          7..303
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mrdvtgrlml ldtaslyfra yfgvpdsvka pdgtpvnavr glldfidrlv rdhrpthlva
       61 cmdadwrpkw rveliptyka hrvaeehtga pdaeevpdtl apqvpviesv ldaigiarvg
      121 vaayeaddvi gtftaraagp vdivtgdrdl yqlvddgrgi rvlyplkgvg tlqvtdeavl
      181 rekygvdgrg yadlallrgd psdglpgvag igektaarll aefgdlagim aavddpkarl
      241 tpsqrrrlte arpyvavapk vvrvaadvpl pdvdtalpga prdpaaleel sarwglggsl
      301 qrllttlgar dgaa
//
LOCUS       WP_392218554             386 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC014983].
ACCESSION   WP_392218554
VERSION     WP_392218554.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014983
  ORGANISM  Streptomyces sp. NPDC014983
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces sp. NPDC014983"
                     /db_xref="taxon:3364933"
     Protein         1..386
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=42077
     Region          47..299
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mtvvclgyra gfveaarrrn ldlhfvvdkl kpglsglsyt rvadladaee vlravteypg
       61 ggisavvtgh ehpmfaatvv rsvfglpgdt dparclrfrd kriqkravsp avptadcvyv
      121 kpsdpdyaal aerlgatfvv kpadgfgsqa teavhdqael ddylrrhpfv sdvrtvaesf
      181 vegreihvdg vwwdgrplwa avssyldplm gwtrgkavad aplgpaesel adhatrfaad
      241 vlrelaapdt vfhleafirp dgelvlgevg arpagaltpe vlrmthgvdl ygatidvalr
      301 rvpevpaqes epadlfgwiy lvrspdpdlt edsfrdrfel veldypapen grqgiygrcg
      361 haivkaathk elvrelraia dfnrsa
//
LOCUS       WP_392218853             374 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces griseoluteus].
ACCESSION   WP_392218853
VERSION     WP_392218853.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseoluteus
  ORGANISM  Streptomyces griseoluteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 374)
  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 374)
  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
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 374)
  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   5  (residues 1 to 374)
  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   6  (residues 1 to 374)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 374)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 374)
  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 20283677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Streptomyces griseoluteus"
                     /db_xref="taxon:29306"
     Protein         1..374
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37162
     Region          17..71
                     /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            17..18
                     /site_type="active"
                     /note="putative switch regulator [active]"
                     /db_xref="CDD:238044"
     Site            order(37..39,48)
                     /site_type="other"
                     /note="non-specific DNA interactions [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            48..54
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            order(49..50,54)
                     /site_type="other"
                     /note="sequence specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238044"
     Site            49..50
                     /site_type="other"
                     /note="putative cAMP binding site [chemical binding]"
                     /db_xref="CDD:238044"
     Region          85..365
                     /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 mnrtrsnpag anllavrshn talvldllrg agaegisrle laertgltpq avskitarlr
       61 edgfaaeagr rastggkprt vlrlvpeagh avgvhldrde lrvvlldlng tvvgerrgdt
      121 glgggaeavl alvadevtal vaevlggegp adagtllgvg valpgpldhv ggvlhrvtgf
      181 pewegfalrd alagrlgvpv vvdkdtnaaa lglaaggegg sfaylhlgtg lgaglviggs
      241 lhrgartgag efghqviqld gppcecgdrg clealclaav grgetgeaar vlgvgagnla
      301 glldidrvll ggrtvaaapg eyvegvagil aararregml gdavpvllap ggervvavga
      361 gqlllapvfg ragg
//
LOCUS       WP_392219009             747 aa            linear   BCT 20-JAN-2025
DEFINITION  caspase family protein [Streptomyces sp. NPDC014983].
ACCESSION   WP_392219009
VERSION     WP_392219009.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014983
  ORGANISM  Streptomyces sp. NPDC014983
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 747)
  AUTHORS   Van Opdenbosch,N. and Lamkanfi,M.
  TITLE     Caspases in Cell Death, Inflammation, and Disease
  JOURNAL   Immunity 50 (6), 1352-1364 (2019)
   PUBMED   31216460
REFERENCE   2  (residues 1 to 747)
  AUTHORS   Tsiatsiani,L., Van Breusegem,F., Gallois,P., Zavialov,A., Lam,E.
            and Bozhkov,P.V.
  TITLE     Metacaspases
  JOURNAL   Cell Death Differ 18 (8), 1279-1288 (2011)
   PUBMED   21597462
REFERENCE   3  (residues 1 to 747)
  AUTHORS   Zhang,J.H., Zhang,Y. and Herman,B.
  TITLE     Caspases, apoptosis and aging
  JOURNAL   Ageing Res Rev 2 (4), 357-366 (2003)
   PUBMED   14522240
REFERENCE   4  (residues 1 to 747)
  AUTHORS   Salvesen,G.S.
  TITLE     Caspases and apoptosis
  JOURNAL   Essays Biochem 38, 9-19 (2002)
   PUBMED   12463158
REFERENCE   5  (residues 1 to 747)
  AUTHORS   Villa,P., Kaufmann,S.H. and Earnshaw,W.C.
  TITLE     Caspases and caspase inhibitors
  JOURNAL   Trends Biochem Sci 22 (10), 388-393 (1997)
   PUBMED   9357314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Streptomyces sp. NPDC014983"
                     /db_xref="taxon:3364933"
     Protein         1..747
                     /product="caspase family protein"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=80212
     Region          4..240
                     /region_name="COG4249"
                     /note="Uncharacterized conserved protein, contains caspase
                     domain [General function prediction only]"
                     /db_xref="CDD:443391"
ORIGIN      
        1 mslpdparsr aviigfpsye tlddlpavan nvrglqkilt sphswnlpak hcvvlpslse
       61 peapvsrddv ldvlhtaaaa aedallvyfa ghgllsesge lhlavprsdh rrlyravaye
      121 dvrhelvtnc rarsrlvild ccysgsaltg ymgdevvanr aqlegayima saaktapala
      181 ppgetytaft gellaaledg vpyasallrt devfqhvrrq lqnarprrpv pqqrarndgh
      241 aivlarnrwt ppppesrvpp avrqqrrrpa htrvparvig aaaaavllta glgsdrpavg
      301 cdvrltqvgd ecigisdgsm vftselddvf rhiaaenraa aekphatial ltpmtalddq
      361 grrrileqvy gayiaqrean msiggsppir lalaqpgttg ggwrqlagql tkmvddprnn
      421 lravvgfnag dtnidnavrl lasrgvltvg gnftperssg psglpmvwta ptaadqlkal
      481 apfsspqekq lliddrrpgd lyvrglrqaf laknplprel sytsssagap vpssvfremv
      541 apicdspahv eeiffagrpt hlwqfltafk drtcrdrnvt vvsgsdtael shdeellrdl
      601 rgrgitvryt svadpdawak aepqdregaq egdlirrqaq qlgphgladg eaisvhdsvi
      661 taitairaav stsqpvpgsr dvrneldtlr gartvhgasg wicldnqgya ydkavavltl
      721 dgsgtgphan giawpegkps rgcyppa
//
LOCUS       WP_392219271            1422 aa            linear   BCT 20-JAN-2025
DEFINITION  Rne/Rng family ribonuclease [Streptomyces griseoluteus].
ACCESSION   WP_392219271
VERSION     WP_392219271.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseoluteus
  ORGANISM  Streptomyces griseoluteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1422)
  AUTHORS   Kime,L., Jourdan,S.S. and McDowall,K.J.
  TITLE     Identifying and characterizing substrates of the RNase E/G family
            of enzymes
  JOURNAL   Methods Enzymol 447, 215-241 (2008)
   PUBMED   19161846
REFERENCE   2  (residues 1 to 1422)
  AUTHORS   Callaghan,A.J., Marcaida,M.J., Stead,J.A., McDowall,K.J.,
            Scott,W.G. and Luisi,B.F.
  TITLE     Structure of Escherichia coli RNase E catalytic domain and
            implications for RNA turnover
  JOURNAL   Nature 437 (7062), 1187-1191 (2005)
   PUBMED   16237448
REFERENCE   3  (residues 1 to 1422)
  AUTHORS   Li,Z., Pandit,S. and Deutscher,M.P.
  TITLE     RNase G (CafA protein) and RNase E are both required for the 5'
            maturation of 16S ribosomal RNA
  JOURNAL   EMBO J 18 (10), 2878-2885 (1999)
   PUBMED   10329633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1422
                     /organism="Streptomyces griseoluteus"
                     /db_xref="taxon:29306"
     Protein         1..1422
                     /product="Rne/Rng family ribonuclease"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=150315
     Region          676..1079
                     /region_name="CafA"
                     /note="Ribonuclease G or E [Translation, ribosomal
                     structure and biogenesis]; COG1530"
                     /db_xref="CDD:441139"
     Region          <1163..>1276
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
ORIGIN      
        1 mleptepneg selntpsdtl pprrrrraas rpagspaaaa gtetgaqpea aetapraeap
       61 eapaetaprp rrrttrrasa pvgtptaaea atvtepavpa asageqadaa daaaetaapa
      121 prrtrrrasa pagsptqvta ednkaeeadv aqdtednkaa epeaaaetpa arprrratrr
      181 asapagapka aeapeagqpa aeqpaepvpa aeteteteap aarprrratr rasapaaeaa
      241 vtetpaaeae papaaeaeaa pagrarrrat rrvsapvetp avetpavqap aaeaepvaea
      301 epvaeaapea eaapgrarrr atrrasapag apaaaeekpe eekpraaepe peprparkat
      361 qsepaepegg rrrrravrqa aggfsapapa egdaprraar pavatfqapv fteprfqtpq
      421 raaaeaaaqa agvrepekae eaekpeepta apeaaastde rdngrrrrrr rgapaeetra
      481 veekpepvee paedeaddsd daegsddsgs rrrrrrggrr rrrgdaydgd dngegtedge
      541 sgelaaeqae qdaedtaeqe eedaedaeea rgeesggsss srrrrrrrrr agdsggesep
      601 astddpertv vkvreprkaa epsdevqsik gstrleakkq rrregreqgr rrvpiiteae
      661 flarreaver vmvvrqhger tqigvledgv lvehyvnkeq atsyvgnvyl gkvqnvlpsm
      721 eaafidigkg rnavlyagev nfealgmang prriesalks gqpvlvqvtk dpighkgarl
      781 tsqvslpgry lvyvpegsmt gisrklpdte rarlktilkk ivpedagviv rtaaegased
      841 elrrdverlq gqweeikkka ktgnapally gepdmtvrvv rdifnedfsk vivsgdeaws
      901 tihgyvshva pdltdrlqkw tgevdvfaty rideqlakal drkvwlpsgg slvidrteam
      961 vvvdvntgkf tgqggnleet vtrnnleaae eivrqlrlrd lggiividfi dmvlesnrdl
     1021 vlrrlleclg rdrtkhqvae vtslglvqmt rkrvgqglle sfsetcvhcn grgvivhmeq
     1081 ptsvgggggg krkkrgrgdg qaheheheta apvetetvae vaaeaaepla lpapdftpde
     1141 elyssvaeae aaagrgrsrr kagrrasapa gapkegsrrs aeraerfera aeeaptaasv
     1201 tageaaatsv lpepaaeaha epmaaedpvv apepaaeeaa pkgrarrrvt rkvsapagsp
     1261 agaeaavvtv aepapvaepe pqpeaapaae esaaparprr ravrkatapt aseetavvvv
     1321 psaapepaae epaseepaae aepeeaapak ktarkaakka pakktaakkt taakkttaak
     1381 ktaaktttak kttakkaakt aktaakstak ktatvpapdg en
//
LOCUS       WP_392220319             409 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces griseoluteus].
ACCESSION   WP_392220319
VERSION     WP_392220319.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseoluteus
  ORGANISM  Streptomyces griseoluteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 409)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Streptomyces griseoluteus"
                     /db_xref="taxon:29306"
     Protein         1..409
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43258
     Region          70..251
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          258..383
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mnvrpisgas agtrhrgrkg lalvagalvl slaacggget tgsgsdnakn kdgrdeqssa
       61 avtiapksga tavdtsgaln vkvaggrlts vvvkdsrgte vdgtlakgga awtparhlaa
      121 atkytvhava edsrgrkaae dssfttltpk ntfmgtftpe dgstvgvgmp fslrftrgit
      181 dpaavekair iktepavdva ghwfgndrld frpenywkpg tkvtvdldld gvegrdgvyg
      241 kqrktvkfti grsqisyvda kkhtmkvvrd gktlktlpvt tgkpgyetwn gkmvmtekla
      301 vtrmngetvg yggeydikdv phairltdsg tfihgnywgg gafgnynash gcvglrdvrg
      361 gydggvpaaw ffnrsmvgdv vvvknshdrt vapdnglngw nmswadwkk
//
LOCUS       WP_392220800             221 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces sp. NPDC015131].
ACCESSION   WP_392220800
VERSION     WP_392220800.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015131
  ORGANISM  Streptomyces sp. NPDC015131
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Streptomyces sp. NPDC015131"
                     /db_xref="taxon:3364941"
     Protein         1..221
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22652
     Region          11..217
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 msgespageg ardrilgrvr aavsgapdap epvrdyrvsh spgdpgalld lldrnlteyr
       61 arvhraaege lpsliarlla ergaasvvvp pglpgawlad taaelrhdap grplspyald
      121 gtdavvtgca laiaetgtiv ldgsagqgrr altlvpdlhv cvvrapgqvv asvplalprl
      181 dpgrpltwis gpsatsdiel drvegvhgpr tldvvlvaap s
//
LOCUS       WP_392222188             355 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC015131].
ACCESSION   WP_392222188
VERSION     WP_392222188.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015131
  ORGANISM  Streptomyces sp. NPDC015131
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 355)
  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 355)
  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
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 355)
  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   5  (residues 1 to 355)
  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   6  (residues 1 to 355)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 355)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 355)
  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 20283677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Streptomyces sp. NPDC015131"
                     /db_xref="taxon:3364941"
     Protein         1..355
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35669
     Region          17..67
                     /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(31,33..35,44)
                     /site_type="other"
                     /note="non-specific DNA interactions [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            44..50
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            order(45..46,50)
                     /site_type="other"
                     /note="sequence specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238044"
     Site            45..46
                     /site_type="other"
                     /note="putative cAMP binding site [chemical binding]"
                     /db_xref="CDD:238044"
     Region          81..349
                     /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 mnsdtgvnlp alrshnaalv ldllrtagee gasrlelaer tgltpqavsk itarlrdegl
       61 aadagrrast ggkprtvlrl vpgaahavgl hldrdeltav lvdlagavva sgvvpldlgs
      121 gaevvmevva gevaalttrp llgvgvampg pldhaagvph rvtgfpewdg fplrdalarr
      181 lglpvvldkd tnaaalnlal sgagadsfay lhlgtglgag lvlgggvyrg artgagefgh
      241 qtvqldgppc gcggrgclea lclaavargd ldgaarvlgt gaanlvtlld idrvllggrv
      301 vtgaaerfvr gvravleera rrggdapvpv alaegsehpv aegaaqlvla pvfgr
//
LOCUS       WP_392222429             416 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC015131].
ACCESSION   WP_392222429
VERSION     WP_392222429.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015131
  ORGANISM  Streptomyces sp. NPDC015131
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 416)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Streptomyces sp. NPDC015131"
                     /db_xref="taxon:3364941"
     Protein         1..416
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43442
     Region          76..257
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          263..390
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mdvqpisgas agagrrgtga grgplalvlg vllllvtacg gsesaggkgg ekdgggaavk
       61 naasqalvti apkdgatsva tsgalkitae kgrlttvtva dskgnkvegr ttadgtawep
      121 vrhlaaatqy kvhavakdae gresakdttf ttlvpkntfi ghytpedgst vgvgmpvsln
      181 fsrgitnpea veravrvtae psvpieghwf gndrldfrpe kywapgtkvt vrldldgveg
      241 rpgvygkqqk tvrftigrsq vstvdasakt mkvvrdgkli ktipitagap stttyngqmv
      301 isekykvtrm ngatvgfgge ydikdvpham rlstsgtfvh gnywasgstf gsanvshgcv
      361 glrdvrgayd gstpaawfyn qsiigdvvvv knskdkqiqp englngwnmp wsewta
//
LOCUS       WP_392222430             411 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC015131].
ACCESSION   WP_392222430
VERSION     WP_392222430.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015131
  ORGANISM  Streptomyces sp. NPDC015131
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 411)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Streptomyces sp. NPDC015131"
                     /db_xref="taxon:3364941"
     Protein         1..411
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=44128
     Region          57..243
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          249..380
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mrhvlkragl rvaaavacag lmagltgctg gggldlgigg kgrspgdtir vtpddgakgv
       61 apdgrvevrv psgrlervrv tqvedaqpvr vpgeisedgl rwrpapgtrl alaakysvda
      121 valdahgrrs arhttfttav pehrfigyfk penrstvgtg mivsfgfsrp ienraavera
      181 irvtsrpave vvghwfgker ldfrprtywk pgtevtvdlr lrdvegapgv ygiqrktvgf
      241 tvgrsqesvv daeahtmevr rdgrlvttlp itagapkttt yngkmvvtel fdvtrmngat
      301 vgfkkkdgkg eydikdvpha mrltdsgtfl hgnywapast fgsanvshgc vglrdvkggg
      361 tdtpagwffe rtligdvvev vnstdrkvsp dnglggwnld warwkagsal r
//
LOCUS       WP_392222537             406 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC015131].
ACCESSION   WP_392222537
VERSION     WP_392222537.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015131
  ORGANISM  Streptomyces sp. NPDC015131
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Streptomyces sp. NPDC015131"
                     /db_xref="taxon:3364941"
     Protein         1..406
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=44399
     Region          60..308
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mrhvlifakt pytktpydrw lagsgiepvv ltttefapgy ahlppgrvha fddydtnqlv
       61 ektalrlare yaveavfara eadvvraaql rellglpgqh tasalafrdk vvmkdhlagg
      121 pvdtpvyrra dsayalveft aehgypvvvk pvsesgslga rvirdeadld aylarpwrgt
      181 sqvetfvegq myhvdglvag gevvfvhpfr yvndclsfrd ddwvgclpls pgdpaydrlv
      241 kaagavlael ptppqtafha elwitpddrv vfceiasrtg ggmisamvrh afgvdldkew
      301 lyaecglpst lgdpvyrpag clnippgkgv lehlptggep dgvremsftg avgreyqggv
      361 ksglylvgyv idgdtedeve rrmrtvadwy sahvrwrpta peenar
//
LOCUS       WP_392222830             422 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC015131].
ACCESSION   WP_392222830
VERSION     WP_392222830.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015131
  ORGANISM  Streptomyces sp. NPDC015131
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces sp. NPDC015131"
                     /db_xref="taxon:3364941"
     Protein         1..422
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=44502
     Region          73..254
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          260..392
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mekrvmtdsk rrkglaaasa llggvlvlsa csggedkgda sgdgsktsqs qvdaaaakda
       61 sqarititpk ngtqnagind dakvtvsegt ltevtltdpe gkavkgemsa dktswtpaeq
      121 leratvykia vsakdsegre ahenssfttv skensfignf tpedgstvgv gmpvsltfnk
      181 aitdkkavqs gitvstssgq evvghwfnnq rldfrpenyw aegskvtlkl dldgvqgadg
      241 vygvqqktvt ftigrnqvst vdaatktmtv tqdgktvkti pisagapenp tyngqmvise
      301 kfketrmdgs tvgftkkdgk geydikdvph amrlstsgtf ihgnywgsds ifgkvntshg
      361 cvglndakga ndpsqpgawf fdnsivgdvv ivknskdkti apdnglngwn mswaewkags
      421 av
//
LOCUS       WP_392224643             524 aa            linear   BCT 20-JAN-2025
DEFINITION  complex I subunit 4 family protein [Streptomyces griseoluteus].
ACCESSION   WP_392224643
VERSION     WP_392224643.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseoluteus
  ORGANISM  Streptomyces griseoluteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 524)
  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 524)
  AUTHORS   Galemou Yoga,E., Angerer,H., Parey,K. and Zickermann,V.
  TITLE     Respiratory complex I - Mechanistic insights and advances in
            structure determination
  JOURNAL   Biochim Biophys Acta Bioenerg 1861 (3), 148153 (2020)
   PUBMED   31935361
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Friedrich,T. and Scheide,D.
  TITLE     The respiratory complex I of bacteria, archaea and eukarya and its
            module common with membrane-bound multisubunit hydrogenases
  JOURNAL   FEBS Lett 479 (1-2), 1-5 (2000)
   PUBMED   10940377
REFERENCE   4  (residues 1 to 524)
  AUTHORS   Walker,J.E.
  TITLE     The NADH:ubiquinone oxidoreductase (complex I) of respiratory
            chains
  JOURNAL   Q Rev Biophys 25 (3), 253-324 (1992)
   PUBMED   1470679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Streptomyces griseoluteus"
                     /db_xref="taxon:29306"
     Protein         1..524
                     /product="complex I subunit 4 family protein"
                     /GO_component="GO:0045271 - respiratory chain complex I
                     [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048039 - ubiquinone binding [Evidence
                     IEA]"
                     /GO_process="GO:0015990 - electron transport coupled
                     proton transport [Evidence IEA]"
                     /GO_process="GO:0042773 - ATP synthesis coupled electron
                     transport [Evidence IEA]"
                     /calculated_mol_wt=54454
     Region          37..521
                     /region_name="NuoM"
                     /note="NADH:ubiquinone oxidoreductase subunit 4 (chain M)
                     [Energy production and conversion]; COG1008"
                     /db_xref="CDD:440632"
ORIGIN      
        1 migisesvmq fllafvvavp llgaaaallp appglkgksp dqavlrhgvt vtgvvliaai
       61 vlalgldhdh pskmqattdi swipalhvri hlgidgislp lllltalltf lcalyscfkp
      121 pagpspkaft alvllleggt lasfavldlv lfflafetvl ipmyfliarw ggegrtraaw
      181 kfilytllgs vimllgllli gikagtfdmv alatdngrsl ttsvqviavl aigiglavka
      241 pmwplhswlp dahtaaptvg svllagvllk mgtygfvril lpvapdgfrv fapylaafav
      301 vgiiygslac lslarrgakg dlkrliayss vghmgfvllg istmtptgvn galfaniahg
      361 litgllfflv galkdrtgst dldtlaahsg galygraprl ggllafgava slglpglagf
      421 wgemlalfga fqpaaglsra aylvflaiga fgtlltaayl lvvvrrvcmg dpnqdlpela
      481 dvrgyefaaw tplvvltvla glwprallgl sdpavqqlla ggtr
//
LOCUS       WP_392225950             427 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            sp. NPDC015131].
ACCESSION   WP_392225950
VERSION     WP_392225950.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015131
  ORGANISM  Streptomyces sp. NPDC015131
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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   4  (residues 1 to 427)
  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 427)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Streptomyces sp. NPDC015131"
                     /db_xref="taxon:3364941"
     Protein         1..427
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=44668
     Region          1..383
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 msrlhaehly kvfgrrpdea vrrleagadr delradgtta avidasfsve pgqifvvmgl
       61 sgsgkstllr mlngllepts grvlfdgqdl talgdrdlrr vrshrismvf qhfalfphrs
      121 vlenaaygle vqgvpraere rragealelc glggwakswp delsggmqqr vglaralatd
      181 adlllmdesf saldplirrd mqdqllelqk rlkktivfit hdlneamrlg driavmrdgr
      241 ivqlgsaedi lvrpandyva sfiqdvdrsr vltagavmep vetvlgtpae pgapaesgap
      301 aepgtpaesg gparsgrqar taadqprtaa dvlaaapaav paatplaelf gpcagsaapv
      361 avtdeaggla gvvtrarlfa aladgaapgt gpgtgattap eaeaeadaqa daqtgaepag
      421 rkevara
//
LOCUS       WP_392225645             286 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Streptomyces
            griseoluteus].
ACCESSION   WP_392225645
VERSION     WP_392225645.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseoluteus
  ORGANISM  Streptomyces griseoluteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 286)
  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 286)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces griseoluteus"
                     /db_xref="taxon:29306"
     Protein         1..286
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29660
     Region          2..285
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mpltttgeli traarfrtav aafnivtleh veavvagaet agapvvlqvs qnavkfrngh
       61 lrplaraava aaeqaavpva lhldhvqsda llrrapdagf ssvmydaarl pyaenlaath
      121 aaadwaharg lwieaelgqi ggkdgrppld ahapgartdp aeardfvart gvdalavavg
      181 sthamttrta aldhvllkrl aaelavplvl hgssgvpdde lvraveggig kvnvgtalnt
      241 altravrehl grhpqavdpr tylaagrtam adevarivrv lgrvga
//
LOCUS       WP_392226431             292 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces griseoluteus].
ACCESSION   WP_392226431
VERSION     WP_392226431.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseoluteus
  ORGANISM  Streptomyces griseoluteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415139
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptomyces griseoluteus"
                     /db_xref="taxon:29306"
     Protein         1..292
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=31696
     Region          1..291
                     /region_name="LysX"
                     /note="Glutathione synthase, LysX or RimK-type ligase,
                     ATP-grasp superfamily [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism,
                     Translation, ribosomal structure and biogenesis, Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0189"
                     /db_xref="CDD:439959"
ORIGIN      
        1 mprialatyd pgtapskdpd laglvaelra agadaearfw ddpaadwagy dlvlvrstwd
       61 yawrpaefla wvdrvdaltr llnpadvvhw nadkrylgel asagvptvpt rylppgaepd
      121 lptgheyvik pasgagarya arytpeerer avgqlahlha egltamvqpy mrgvdrhger
      181 alhffggrll hasrkgavlv sgtpfdadkt ahpklekwqp tgaeldvaer alaavpggae
      241 rllygrvdli dgedgqpcvl eleliephlf ldlhpesmpr vaqlviraak ss
//
LOCUS       WP_392226935             410 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces griseoluteus].
ACCESSION   WP_392226935
VERSION     WP_392226935.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseoluteus
  ORGANISM  Streptomyces griseoluteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Streptomyces griseoluteus"
                     /db_xref="taxon:29306"
     Protein         1..410
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=43551
     Region          51..310
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mtlvlisprh tslpfahwlp eragrmvava aagtpigdgf revrtvadyr ddaavlaaar
       61 dlanrhrptt llalaesdle rasllrgefg lpglgsaaaa ayrdkvlmke yarkagirvp
      121 dfapvrrpsd vtdflaarpg pvvvkprsas gatgvyvvds vseaaalpag llestpyeve
      181 efvegqlyhv dafrvdgcrv aavasryttp gclshwsdsp hgsrtltagd plrpllvqea
      241 wrlvealpsp ptvcvhaeff vtpegsvvlc evaarvaggt ipvmlrhvlg tdprelwarv
      301 ecglpndlda vrehvaaapl aaccglpprr grirrtphap agaldftlhn gagddwgger
      361 yaqrksgdfv aswvvtaddd erltaaldat vaqvsagfdw eleavsgavi
//
LOCUS       WP_392227535             131 aa            linear   BCT 20-JAN-2025
DEFINITION  TOBE domain-containing protein [Streptomyces sp. NPDC015131].
ACCESSION   WP_392227535
VERSION     WP_392227535.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015131
  ORGANISM  Streptomyces sp. NPDC015131
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 131)
  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 10007583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Streptomyces sp. NPDC015131"
                     /db_xref="taxon:3364941"
     Protein         1..131
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13869
     Region          1..128
                     /region_name="MopI"
                     /note="Molybdopterin-binding protein MopI [Coenzyme
                     transport and metabolism]; COG3585"
                     /db_xref="CDD:442804"
ORIGIN      
        1 mqsytigqaa rllgvspdta rrwadagrva thrdesgrrl idgkslaafs teiaqhgtge
       61 ddssytsarn afpgivtair lgdiaaqvti qagphrlvsl ltreaveelg ldvgmratar
      121 vkstsvhidr t
//
LOCUS       WP_392228600             394 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Streptomyces sp.
            NPDC014806].
ACCESSION   WP_392228600
VERSION     WP_392228600.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014806
  ORGANISM  Streptomyces sp. NPDC014806
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 394)
  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 394)
  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 394)
  AUTHORS   ter Beek,J., 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 394)
  AUTHORS   Igarashi,K., Ito,K. and Kashiwagi,K.
  TITLE     Polyamine uptake systems in Escherichia coli
  JOURNAL   Res Microbiol 152 (3-4), 271-278 (2001)
   PUBMED   11421274
REFERENCE   5  (residues 1 to 394)
  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   6  (residues 1 to 394)
  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 11430824
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Streptomyces sp. NPDC014806"
                     /db_xref="taxon:3364920"
     Protein         1..394
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0019808 - polyamine binding [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:0015846 - polyamine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=43830
     Region          8..391
                     /region_name="PotD"
                     /note="Spermidine/putrescine-binding periplasmic protein
                     [Amino acid transport and metabolism]; COG0687"
                     /db_xref="CDD:440451"
ORIGIN      
        1 mplprrplsr rsllralggt avlgalagcg vpaayvppgd raaadtsard krltwsnwpl
       61 yidtdddhps rrptleafek rsgiavdyve eindndeffg kispalmnhq ptgrdlvvis
      121 dwmcarfvrl gwvqeldaar mphvarhldp llrspafdpg rrftvpwqsg itgiaynrrk
      181 lgreirhvsd lwaddlrgrv tllsgldeaf allmlgngvd itrwtaddfh rvcdqveaqv
      241 rrgqirrftg ndytkdlvgg dvlacqaysg dvvqlradnp diefvvpeeg aelwaeslmv
      301 pdlarhkana erlidhyyrp evaaelaawv tyvcpvpaar evlasssdad taaladepli
      361 fpdaamrrrl atardvtaqe rvefakrwnk iagl
//
LOCUS       WP_392229939             322 aa            linear   BCT 20-JAN-2025
DEFINITION  quinone oxidoreductase family protein [Streptomyces sp.
            NPDC014806].
ACCESSION   WP_392229939
VERSION     WP_392229939.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014806
  ORGANISM  Streptomyces sp. NPDC014806
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 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   4  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces sp. NPDC014806"
                     /db_xref="taxon:3364920"
     Protein         1..322
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=33607
     Region          1..320
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 mraiqfkrfg gpevlteaqv pepvarpget vveveaagvn fgdikqiage qpdgpyapkg
       61 plpripgmev vgrtadgrrv lghvlqggya ertvvadrdl vtvpegvsag ealavhvqgl
      121 tawhllrsva rirpgesvvv haaaggtgsl avqlarefga grviatasse gkrafaldlg
      181 advaidgeaq gyrervlaan dgrqvdivld aiggpvldaa ldtlgylgrl vtygasarqp
      241 asaispsrla vesltvagfw ltpllvrega agaplqelld ltarrrlrpl vggqyplgqa
      301 rqahedllar rtkgkllllp ht
//
LOCUS       WP_392230832             321 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC014806].
ACCESSION   WP_392230832
VERSION     WP_392230832.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014806
  ORGANISM  Streptomyces sp. NPDC014806
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415139
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces sp. NPDC014806"
                     /db_xref="taxon:3364920"
     Protein         1..321
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=33010
     Region          1..254
                     /region_name="LysX"
                     /note="Glutathione synthase, LysX or RimK-type ligase,
                     ATP-grasp superfamily [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism,
                     Translation, ribosomal structure and biogenesis, Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0189"
                     /db_xref="CDD:439959"
ORIGIN      
        1 mklcflveeq yrhdgmpvev irqltswghq vdvvrpggsl lhmtealhga ghdawilktv
       61 sggpgltlle aaaaagttti ndarsirgvr dkalaasigr gsglplppty aaarpemlaq
      121 ipeseypivv kpadgssgra vhlvtspghl tamagelaaq gmliaqpyip nsgvdikvyc
      181 vggelyater rsplhpehav perrvpltae vaaiaaraga vygldlygvd vvlgpdgpvv
      241 vdvndfpsfr qvpdaaarva ravlalaaag sradapegtv prmpeqraqg avppagppvf
      301 paapgprsgp aqvplavgkt g
//
LOCUS       WP_392230834             264 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC014806].
ACCESSION   WP_392230834
VERSION     WP_392230834.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014806
  ORGANISM  Streptomyces sp. NPDC014806
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415139
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Streptomyces sp. NPDC014806"
                     /db_xref="taxon:3364920"
     Protein         1..264
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=27284
     Region          1..247
                     /region_name="LysX"
                     /note="Glutathione synthase, LysX or RimK-type ligase,
                     ATP-grasp superfamily [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism,
                     Translation, ribosomal structure and biogenesis, Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0189"
                     /db_xref="CDD:439959"
ORIGIN      
        1 mriglitsap ghpllaaata lladghtvrv ldpetaaapg psepladvyl lkartprais
       61 laralegrga rvlnsaaata lcqdrvamae harraglpfa ptrfhatlar ladgtglrgp
      121 lvvksrhsrk hdlvarvdse grlaelaaah preavvvqdf vpnsgwdhkl waigdrvfaa
      181 lrrselspeg rgptvplglg slppgwaalv hrvgevfgld vygvdvldtg ggvplivdin
      241 afpgvrdqpg apqalaalal aaga
//
LOCUS       WP_392230919             812 aa            linear   BCT 20-JAN-2025
DEFINITION  GcvT family protein [Streptomyces sp. NPDC014806].
ACCESSION   WP_392230919
VERSION     WP_392230919.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014806
  ORGANISM  Streptomyces sp. NPDC014806
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 812)
  AUTHORS   Stauffer,L.T., Ghrist,A. and Stauffer,G.V.
  TITLE     The Escherichia coli gcvT gene encoding the T-protein of the
            glycine cleavage enzyme system
  JOURNAL   DNA Seq 3 (6), 339-346 (1993)
   PUBMED   8219277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..812
                     /organism="Streptomyces sp. NPDC014806"
                     /db_xref="taxon:3364920"
     Protein         1..812
                     /product="GcvT family protein"
                     /calculated_mol_wt=88907
     Region          5..385
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
     Region          370..426
                     /region_name="FAO_M"
                     /note="FAD dependent oxidoreductase central domain;
                     pfam16350"
                     /db_xref="CDD:465100"
     Region          421..812
                     /region_name="GcvT"
                     /note="Glycine cleavage system protein T
                     (aminomethyltransferase) [Amino acid transport and
                     metabolism]; COG0404"
                     /db_xref="CDD:440173"
ORIGIN      
        1 magprvviig agvvgaalad eisargwtev tvvdqgplpa tggssshapg lvfqtnaskt
       61 mtelarytve kfsslevdgk pcflqvggle vatsperlae iqrrhgwlas wgidsrllna
      121 decverhplv drdkilgglf vptdglakav laveaqirra tergvrflar hevldvrqse
      181 grvtgvvtdh geidadivvc cagiwgpkia rmvgmnlplt plahqlawtg pvpalagqte
      241 eavrpilrhq dadlyyrdry dgigigyygh rpmpvsaddi lsvdeaeemp svlkfteedf
      301 epawtetrsl lpatqeakve eginglfsft tdgypllges pqvkgfwvae avwvthsagv
      361 gravaewlvd gycssfdlhe cdvnrfephq lspeyvlard cqnfvevydi lhplqpsgdp
      421 rpirtspfya rqqahgaffl eangwerpqw yeanaplveg rniptpndwa arywspivga
      481 eaqatretva lydmtalkrl evtgpgaaaf lerlctgkid ksvgsvtytl lldhdggirs
      541 dvtvarlard rfqvgangnl dldwfsrhlp adgtvqvrdi tagtcciglw gplarevlqp
      601 lteedfsneg lkyfrakhay igavpvtamr lsyvgelgwe lyttadqglk lwdtlwaaaq
      661 plggviagrg afnslrlekg yrsfgtdmty ehdpyeagvg favkldkddf igkaalqrrk
      721 advrrrltcl tiddpravvl gkepvydgeh avgyvtsaay gytvgkgiay awlpaglaep
      781 gtrlhigyfd qrieavvaee plfdptmsrl rg
//
LOCUS       WP_392231662             139 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TOBE domain-containing protein [unclassified
            Streptomyces].
ACCESSION   WP_392231662
VERSION     WP_392231662.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 139)
  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 10007583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..139
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13894
     Region          1..138
                     /region_name="MopI"
                     /note="Molybdopterin-binding protein MopI [Coenzyme
                     transport and metabolism]; COG3585"
                     /db_xref="CDD:442804"
ORIGIN      
        1 mtlsirnqlp gtvtavhpge amamvklrld ggqeltaait teaaedlgla pgsavralvk
       61 stevsvathr veglsirnql pgaviglttg aamasvrisv pggeltaait rdaardlglf
      121 vgsdvialik atevalata
//
LOCUS       WP_392231687             291 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptomyces globisporus].
ACCESSION   WP_392231687
VERSION     WP_392231687.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 291)
  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 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   3  (residues 1 to 291)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 291)
  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   5  (residues 1 to 291)
  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   6  (residues 1 to 291)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..291
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32215
     Region          19..103
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          127..286
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mlerlndamg hieahlgeri eaadlariam tseyhfrrmf salaglplse yirrrrmtva
       61 gaevlgdrdr slldvamryg ydtgegfara fravhgigpg earrtgaalr sqqrltfrlv
      121 vegssamryg lvekdafrvv gkkarvplih egpnpaiaef irgigreeld riaalsdqkp
      181 agivgvsdql dpsraegtel dywhgvvtga aeppedldal evpagtwavf esegefpqal
      241 qylwrdvftq wfpsnpyasr pgpeilrvrl tedgkraeae lwipversae s
//
LOCUS       WP_392231810             415 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            globisporus].
ACCESSION   WP_392231810
VERSION     WP_392231810.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  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 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   3  (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   4  (residues 1 to 415)
  AUTHORS   Igarashi,K., Ito,K. and Kashiwagi,K.
  TITLE     Polyamine uptake systems in Escherichia coli
  JOURNAL   Res Microbiol 152 (3-4), 271-278 (2001)
   PUBMED   11421274
REFERENCE   5  (residues 1 to 415)
  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   6  (residues 1 to 415)
  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 11430824
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..415
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0019808 - polyamine binding [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:0015846 - polyamine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45363
     Region          28..413
                     /region_name="PotD"
                     /note="Spermidine/putrescine-binding periplasmic protein
                     [Amino acid transport and metabolism]; COG0687"
                     /db_xref="CDD:440451"
ORIGIN      
        1 mesyeperlt pvqlaamrrs ltsgrgaltr rsllrasgmg alavggiatl gacgippakr
       61 adaglasddh sekekvlnfs nwteymdvse deksrptlea ftqrtgirvk ytedindnve
      121 ffgkikpqla agqdtgrdli cvtdwlaari irlgwaqkld asnlphafan vsaqfrspdw
      181 dpgraysypw tgiptviayn kkatggrkvd svtqllddpk lkgrvsflse mrdtvgmtll
      241 dqgkdpgkfs dadfdgaigr lqkavdkkqi rrftgndyta dlskgdiaac vawagdviql
      301 qadnpdieya ipaagyitss dsllvpaqar hktnaeklid yyyeppvaaq laayinyvcp
      361 vdgvreelar idesmasntl ilpdkemaak srsfrslste eetayeekfa kliga
//
LOCUS       WP_392231864             449 aa            linear   BCT 20-JAN-2025
DEFINITION  SWIM zinc finger family protein [Streptomyces sp. NPDC014806].
ACCESSION   WP_392231864
VERSION     WP_392231864.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014806
  ORGANISM  Streptomyces sp. NPDC014806
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Hassan,I.U., Rehman,H.M., Liu,Z., Zhou,L., Samma,M.K., Wang,C.,
            Rong,Z., Qi,X., Cai,D. and Zhao,H.
  TITLE     Genome-wide identification and spatiotemporal expression profiling
            of zinc finger SWIM domain-containing protein family genes
  JOURNAL   Zool Res 44 (3), 663-674 (2023)
   PUBMED   37161653
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     SWIM, a novel Zn-chelating domain present in bacteria, archaea and
            eukaryotes
  JOURNAL   Trends Biochem Sci 27 (8), 384-386 (2002)
   PUBMED   12151216
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Streptomyces sp. NPDC014806"
                     /db_xref="taxon:3364920"
     Protein         1..449
                     /product="SWIM zinc finger family protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46993
     Region          43..415
                     /region_name="SWIM"
                     /note="Uncharacterized protein, contains SWIM-type Zn
                     finger domain [Function unknown]; COG4715"
                     /db_xref="CDD:443750"
ORIGIN      
        1 mtqqgvrwsa dqvlalapda asrtagsrlg aagpwsgags sgegavwglc egsgstpyrt
       61 vvdlvdasgp astcscpsrk fpckhalgll llwsagegav praeppewar rwlegrrnra
      121 aqqrtaetag sapadpeaar rraerraeri tagateleqr ladllrsgla taeqagyglw
      181 eetaarmvda qapglaarvr elgaipgsgp gwpvrlleec allhlldqgw lgrerlpegl
      241 vatvrsrvgl psapdgppvr dewlvlaqyd tsdgklttrr twlhgaatdr valllsygaa
      301 grapelalpv glaldaevsa ypgdgrhrva lgerfappap tavrpkgvtt aqatarygea
      361 lrddpwlesv pvtlesvipt pagkswqlad adgegalplt paaagrpglw rlvalsggap
      421 vtvfgecghr gftpltawpr sdgevvslh
//
LOCUS       WP_392232010             284 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces globisporus].
ACCESSION   WP_392232010
VERSION     WP_392232010.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415139
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..284
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=29957
     Region          7..284
                     /region_name="LysX"
                     /note="Glutathione synthase, LysX or RimK-type ligase,
                     ATP-grasp superfamily [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism,
                     Translation, ribosomal structure and biogenesis, Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0189"
                     /db_xref="CDD:439959"
ORIGIN      
        1 mgavhpialv adriaweerl likaapafgl ridwvndeal slghpdapai kgydtllirs
       61 rsytrgglia slaeaagvpt lntaraihac enkaalravl qtagvpapdh rlvlsrkdfd
      121 kaladlplpl vlkpvfggmg krvtlirhad tahsvydyie dlahafeqas vvepylggss
      181 vrclvvgrel igaaefesgg sdwrnnaalg nknraiahdp dvvkivdgvv dvlgpgiygv
      241 dlfatpdgyv vnevnhapgf ravasatgad ipsaigryvq ella
//
LOCUS       WP_392232520             302 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Streptomyces globisporus].
ACCESSION   WP_392232520
VERSION     WP_392232520.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..302
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32689
     Region          1..296
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mlldtaslyf rayfgvpdsv rapdgtpvna vrglldfigr lvhdhrpdel vacwdndwrp
       61 qwrvdlipty kahrvaeetp agqtdeeeip dtlspqvpii edvlaalgia rvgvtpyead
      121 dvigtltara qgpvdivtgd rdlyqlvdda rqvrvlyplk gvgtlqltde awlrekygvd
      181 gagyvdlall rgdpsdglpg vpgigektaa klldaygdld gimaavddpk akltpsqrkr
      241 ldesrayvav apkvvrvagd vplpdfdpal preprdpaal ealaeqwgls gaiqrllavl
      301 qh
//
LOCUS       WP_392232922             467 aa            linear   BCT 20-JAN-2025
DEFINITION  alpha,alpha-trehalose-phosphate synthase (UDP-forming)
            [Streptomyces sp. NPDC014806].
ACCESSION   WP_392232922
VERSION     WP_392232922.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014806
  ORGANISM  Streptomyces sp. NPDC014806
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 467)
  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 467)
  AUTHORS   Eastmond,P.J. and Graham,I.A.
  TITLE     Trehalose metabolism: a regulatory role for trehalose-6-phosphate?
  JOURNAL   Curr Opin Plant Biol 6 (3), 231-235 (2003)
   PUBMED   12753972
REFERENCE   3  (residues 1 to 467)
  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   4  (residues 1 to 467)
  AUTHORS   Elbein,A.D., Pan,Y.T., Pastuszak,I. and Carroll,D.
  TITLE     New insights on trehalose: a multifunctional molecule
  JOURNAL   Glycobiology 13 (4), 17R-27R (2003)
   PUBMED   12626396
REFERENCE   5  (residues 1 to 467)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 929-939 (1997)
   PUBMED   9334165
  REMARK    Erratum:[Biochem J 1998 Feb 1;329(Pt 3):719]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Streptomyces sp. NPDC014806"
                     /db_xref="taxon:3364920"
     Protein         1..467
                     /product="alpha,alpha-trehalose-phosphate synthase
                     (UDP-forming)"
                     /EC_number="2.4.1.15"
                     /GO_function="GO:0003825 - alpha,alpha-trehalose-phosphate
                     synthase (UDP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0005992 - trehalose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50997
     Region          10..466
                     /region_name="OtsA"
                     /note="Trehalose-6-phosphate synthase, GT20 family
                     [Carbohydrate transport and metabolism]; COG0380"
                     /db_xref="CDD:440149"
ORIGIN      
        1 masshaadqk arvlvasnrg pvsytvgddg slhakrgggg lvsglsaigp dagalwvcsa
       61 lsdgdreavr rgageqgvrm ldipadvhad ayngiansvl wfvhhmlyqt plepvfdaef
      121 rrqwasyety nrafaealae eaaegavviv qdyhltlvpg mlrelrpdlr ighfshtpwa
      181 ppeyfrmlpd diarqvlrgm lgadrlgflt rrwadaftac ceqfagglgd trigvhglga
      241 dadflrerah qadvgermta lreqigagrr tivrvdrtel sknivrglla frqllddhpe
      301 wrervvhvaf aypsrqdlav yrdytaevqr vaeeinaayg tegwtpvvlh veddfarsla
      361 ayrladvalv npirdgmnlv akevpvvsde gcvlvlsrea gayeelgeda iavnpydvig
      421 taaalheals mapgertdrv krlaaaatal ppakwfleql ealrdlg
//
LOCUS       WP_392233368             129 aa            linear   BCT 20-JAN-2025
DEFINITION  SRPBCC family protein [Streptomyces globisporus].
ACCESSION   WP_392233368
VERSION     WP_392233368.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 129)
  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 10008053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..129
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=14186
     Region          6..125
                     /region_name="YndB"
                     /note="Chalcone/flavanone-binding protein YndB,
                     AHSA1/START/SRPBCC domain [Lipid transport and
                     metabolism]; COG3832"
                     /db_xref="CDD:443044"
ORIGIN      
        1 mptgltqdag weigvsrtih rpltavwdfv tgpegvalwl gldgplptgk gapyrtadgi
       61 egeirsfrpg drvrlthgts tvqvavtpgs sedrtvlrfh qerlasaeer eerrthwknv
      121 mdrieaelt
//
LOCUS       WP_392234495             357 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            globisporus].
ACCESSION   WP_392234495
VERSION     WP_392234495.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 357)
  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 357)
  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 357)
  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 11448557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..357
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=38448
     Region          58..124
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
ORIGIN      
        1 mssdtdtdea hatgahatnp rateaqaaps rateahataa rtgeaittsa lhaaatgadt
       61 fpgvlrealn rrglslervs erlrvrgiti sqatlsswqr grsqperars lqavdvleei
      121 lelpagalrs llgprrprgr ttppdaegaa lqilgedsvv ekalgarfrh fnqetsslmv
      181 hdivrvgetg tlsgisttnv lrakragadr aifvlsfdde aaepvdikvt cgrlaeatyl
      241 kglkslvlei hfgrelakld ttvvsyavev spsetpathy erwsrtnlhe ylqqvffhpg
      301 alpadchryv rdkvgdpprg rrriplseah dvhvltsrck pgvhgvawey gtgtgga
//
LOCUS       WP_392235082             265 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            globisporus].
ACCESSION   WP_392235082
VERSION     WP_392235082.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 265)
  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 265)
  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 18542080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..265
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29337
     Region          1..58
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
     Region          83..251
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 msntygewlk aqreaagltq qqladlalmt rshishieag rrmpseedar rldralgtgn
       61 vlatfrpqed drsvaehfeg arkleeqatf icefavayfp gilqtrryan avlgaafppy
      121 sdeerdeavv srlerakile rptspvvwal ldeavfrrva gnadimaeqi mhvvglaerg
      181 rirvhvlplg gpictlhqsm vtlmhfadqp pvaysegtkv aklhdaphlv eriqgaysla
      241 msdalslses lntlraaake ygyre
//
LOCUS       WP_392235174            1315 aa            linear   BCT 20-JAN-2025
DEFINITION  Rne/Rng family ribonuclease [Streptomyces sp. NPDC015408].
ACCESSION   WP_392235174
VERSION     WP_392235174.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015408
  ORGANISM  Streptomyces sp. NPDC015408
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1315)
  AUTHORS   Kime,L., Jourdan,S.S. and McDowall,K.J.
  TITLE     Identifying and characterizing substrates of the RNase E/G family
            of enzymes
  JOURNAL   Methods Enzymol 447, 215-241 (2008)
   PUBMED   19161846
REFERENCE   2  (residues 1 to 1315)
  AUTHORS   Callaghan,A.J., Marcaida,M.J., Stead,J.A., McDowall,K.J.,
            Scott,W.G. and Luisi,B.F.
  TITLE     Structure of Escherichia coli RNase E catalytic domain and
            implications for RNA turnover
  JOURNAL   Nature 437 (7062), 1187-1191 (2005)
   PUBMED   16237448
REFERENCE   3  (residues 1 to 1315)
  AUTHORS   Li,Z., Pandit,S. and Deutscher,M.P.
  TITLE     RNase G (CafA protein) and RNase E are both required for the 5'
            maturation of 16S ribosomal RNA
  JOURNAL   EMBO J 18 (10), 2878-2885 (1999)
   PUBMED   10329633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1315
                     /organism="Streptomyces sp. NPDC015408"
                     /db_xref="taxon:3364956"
     Protein         1..1315
                     /product="Rne/Rng family ribonuclease"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=138742
     Region          <323..434
                     /region_name="MSCRAMM_ClfA"
                     /note="MSCRAMM family adhesin clumping factor ClfA;
                     NF033609"
                     /db_xref="CDD:468110"
     Region          555..958
                     /region_name="CafA"
                     /note="Ribonuclease G or E [Translation, ribosomal
                     structure and biogenesis]; COG1530"
                     /db_xref="CDD:441139"
ORIGIN      
        1 mlepteptes sttstdsesn tpsdtlpprr rrraasrpag ppsggsdapa etvapaevta
       61 vtdeaeetee teaaqaaapa peaaparprr ravrrasapa gtptsteaae tvvaapsgae
      121 apvaepvaea gevtedpapr rsrrratrsv ttpaepaaae taeatpaepa aadaepaaap
      181 aagteaedaa pkgrtrrrat rrvtapaeap aeaaaevrep tpepvreaap eaakdaepae
      241 daaprrarrr strkaaggfa apaqtaasdd adapkrpsrp avavfqapvf aepqfqtper
      301 aaaeaaaeaa gaapakpaev aeeqseeqsa gsrrrrrrrg aaeegtedrt paaarderet
      361 dtradsdadt eadadsdesg edhddadgse dsgsrrrrrr ggrrrrrgds adgdlndges
      421 eqtadqaeqd gadtaeqaee daeesaesag dgggssssrr rrrrrrragd gsgdgdastd
      481 dpertvvkvr eprpprekse psdevqsikg strleakkqr rregreqgrr rvpiiteaef
      541 larreaverv mvvrqhgert qigvledgvl vehyvnkeqa tsyvgnvylg kvqnvlpsme
      601 aafidigkgr navlyagevn fealgmangp rriesalksg qsvlvqvtkd pighkgarlt
      661 sqvslpgryl vyvpegsmtg isrklpdter srlktilkki vpedagvivr taaegasede
      721 lrrdverlqa qwediqkkak sgnaptllyg epdmtvrvvr difnedfsqv vvsgddawqt
      781 ihgyvshvap dladrlskwt sevdvfatyr ideqlakald rkvwlpsggs lvidrteami
      841 vvdvntgkft gqggnleetv trnnleaaee ivrqlrlrdl ggiividfid mvlesnrdlv
      901 lrrlleclgr drtkhqvaev tslglvqmtr krvgqglles fsetcvhcng rgvivhldqp
      961 taaggggggs krrkraraga dqpheheava gvetgptaeq eadtesesev aaevaepval
     1021 papdftadee lyssaaeaea aatrgrgrrr asrrasapag apkagkgeae raegptaqdv
     1081 tvqeeverpv rresatevla epaavedava gghvtapaea papaaeeaap kgrtrrratr
     1141 kvsapagspa gaeaavvtvp etapapqaeq apqapaeapa epaaeeaapa rprrravrks
     1201 taptaseeaa vmvvpsagpe eeraeqaasd tetaeeaapa kkaaarktak katakkaatk
     1261 ktaakkttta kkatakkaak tttakkttak ktaskktaaa aqqapssvta atdeg
//
LOCUS       WP_392235514             388 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces sp. NPDC015408].
ACCESSION   WP_392235514
VERSION     WP_392235514.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015408
  ORGANISM  Streptomyces sp. NPDC015408
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Streptomyces sp. NPDC015408"
                     /db_xref="taxon:3364956"
     Protein         1..388
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=39293
     Region          62..331
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 msapavpadl rrtappadav gdtpppapas rslrahlgtl agtailgvll wrmgtgvfld
       61 glrridaptv laalgiglvt tvfsawrwal varglrirlp lgpavadyyr alflnaalpg
      121 gvlgdvhrav hhgrsagdlg rgvravvler vagqlaligv gvvvlltlps pvlgearraa
      181 plvtlavlga lavivalrmn raparggrvl ratlgearqg llsrrnlpgv avssavvlag
      241 hlvmfglaar vagsgatvae ltplavlall amglplnvgg wgpregvtaw afgaaglgag
      301 tglgvavvyg vlsfvaslpg vvvlvvrrfa rpdgsygrpg lfpaagsavg savrkekyvp
      361 kesarlasss fpfsaepseg rpmtpesv
//
LOCUS       WP_392235728             414 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC015408].
ACCESSION   WP_392235728
VERSION     WP_392235728.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015408
  ORGANISM  Streptomyces sp. NPDC015408
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Streptomyces sp. NPDC015408"
                     /db_xref="taxon:3364956"
     Protein         1..414
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=43817
     Region          56..316
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 msarpvvlvv apgdknyrgy cleqvaaayd vvlltgtels wekphitdha vvdlsdpaal
       61 laggralagr hdlagvmtwd ewnvvptarl arqlglptsa pevmqgcrnk atarslfarh
      121 gvpsaasvsv rtrqeaeaaa erigypvvlk pashagaigv rrvddrdqlt aayqaaerta
      181 gqgtestsvl veefldgpei svecvtyrga ttvvavnrkt lsppphfeql ahsvdaadpl
      241 retvapaara ainalgitdg vshiemrlvd grprlievna rlagdmighl vrlatgidlv
      301 raaadiacgr apdltptrss aaairllypd tsgtlthlty dgprptwldr lqfqcrpgdq
      361 lllptdggnl ytgrigylit tattgqqara radqaaravt avldrtsgtr staa
//
LOCUS       WP_392235909             399 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces globisporus].
ACCESSION   WP_392235909
VERSION     WP_392235909.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 399)
  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   5  (residues 1 to 399)
  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   6  (residues 1 to 399)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 399)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..399
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40493
     Region          14..77
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          77..379
                     /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 metpgsqtsl hranlervvr avrmagsltq aeiarstgls aatvsnivre lkeggtvevt
       61 ptsaggrrar svslsgdagi vigvdfghth lrvavgnlah qvlaeesepl dvdassaegf
      121 graevlvnrl iaatgigpdk vigvglgvpg pidvesgtlg stsilpgwtg inpseelsgr
      181 lgvpvyvdnd anlgalgelv wgsgrgvkdl ayikvasgvg aglvidgtiy rgpggtagei
      241 ghitldesgp vcrcgnrgcl etftaaryvl pllqpshgpg ltmervvqla regdpgcrrv
      301 igdvgrhigs gvanlcnlln psrvvlggsl aeagelvlgp irdsvsryai psaarqlsvl
      361 pgalggraev lgalalvlse mgdstllest lpvatpaft
//
LOCUS       WP_392235982             295 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            globisporus].
ACCESSION   WP_392235982
VERSION     WP_392235982.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 295)
  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 295)
  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 295)
  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 18542080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..295
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33229
     Region          36..94
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
     Region          112..290
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mthgsdsmds mdspvygtfg ngsgrspepe pqyslkmfge vvktfrkrar ltqeqfaplv
       61 gyspetvasv eqgrrlpppd faeradsild afgvilaaak hltrrkglas wfrqwaelel
      121 salslytyec rlipgllqta ayartlfadq lppladeqie aqlaarldrq rllherpnta
      181 fsfileehlf lrdlggkevt relldhildl selrnvdiqi mpllrhhhag lhgpmrllet
      241 pdhqwfgyle gqehgqlvsd pkvisalqmr casmrsqals lddskslmrq mrgar
//
LOCUS       WP_392236068             410 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC015408].
ACCESSION   WP_392236068
VERSION     WP_392236068.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015408
  ORGANISM  Streptomyces sp. NPDC015408
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Streptomyces sp. NPDC015408"
                     /db_xref="taxon:3364956"
     Protein         1..410
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=43547
     Region          73..316
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mgirradpyi qravrelaad gieaglfhts gtagdddfpg hrerldravt preiadavaa
       61 wgadaavsis lpcenalrda aakafldavg iptvmtplaa tmllvdkwet kqlcrragld
      121 vpdgfrvdsd llagrgltvp gyrdalrvqa ervgyplmsk pvwdstsmgi rtlrspadld
      181 ahlkpgpqtv stvveqvveg dlcsvdivgr pgsyrilplc wtgragaepv ftfaglrwcg
      241 preevdtafa evartlaglc edlgvhgsvn vdmiytggrf tvleinprig gattlscaas
      301 gtntftslar marglpltgg marrtcwave flaadgippa alaelarhvr vvtahelvid
      361 gvchgdivvf tlargeedrt vkaltelhet sgfpsaevma klgalldpnr
//
LOCUS       WP_392236589             360 aa            linear   BCT 20-JAN-2025
DEFINITION  heme/hemin ABC transporter substrate-binding protein [Streptomyces
            globisporus].
ACCESSION   WP_392236589
VERSION     WP_392236589.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Naoe,Y., Nakamura,N., Rahman,M.M., Tosha,T., Nagatoishi,S.,
            Tsumoto,K., Shiro,Y. and Sugimoto,H.
  TITLE     Structural basis for binding and transfer of heme in bacterial
            heme-acquisition systems
  JOURNAL   Proteins 85 (12), 2217-2230 (2017)
   PUBMED   28913898
REFERENCE   2  (residues 1 to 360)
  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   3  (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   4  (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   5  (residues 1 to 360)
  AUTHORS   Ho,W.W., Li,H., Eakanunkul,S., Tong,Y., Wilks,A., Guo,M. and
            Poulos,T.L.
  TITLE     Holo- and apo-bound structures of bacterial periplasmic
            heme-binding proteins
  JOURNAL   J Biol Chem 282 (49), 35796-35802 (2007)
   PUBMED   17925389
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..360
                     /product="heme/hemin 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=36777
     Region          89..357
                     /region_name="ChuT"
                     /note="ABC-type hemin transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG4558"
                     /db_xref="CDD:443619"
ORIGIN      
        1 mrisqdfapt gpdaattarr rpargraaaa ltaavafalv ltgcggggda apksasaqss
       61 adadrveplt gapapklpvt vdsadgdkvt idstdrivpl tgslseivft lgfgkqvvar
      121 ditatfeqae klpvvtrahd vsaesvlslk ptivladttt gpaeaieqir dagipllvve
      181 pakglsdvgr ridavaealg vpsagtelre rtekriadvq ksipvrtdgk kprvaflylr
      241 gsasvyllgg agsgasslle aagavdagke sgldkdftai tsealakaap daillmtkgf
      301 esvggmdglv kipgiaetpa gmdrrvvtvd dgvllnygpr tdrvlteive qlyakggkgq
//
LOCUS       WP_392236898             289 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Streptomyces globisporus].
ACCESSION   WP_392236898
VERSION     WP_392236898.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 289)
  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 289)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..289
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29871
     Region          42..281
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mplaatgdli aeaaaqhrav aafnvitleh aeaiaegaea agspvilqis enavayhrgr
       61 prpiaraaae vadqaavpvs lhldhvqste llhraadcgf ssamfdaarl pytenlaatr
      121 aavvwaherg lwleaelgqv ggkngeppln ahapgartdp eearsfvaat gvdalavavg
      181 tshamtsrda vidhellggl rvavpvplvl hgssgasdee laravaggir kvnigtalni
      241 amtgairerl aqdergvdpr ryladgrdam artvtrlmav laqgpvhaa
//
LOCUS       WP_392237821             285 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Streptomyces sp.
            NPDC015408].
ACCESSION   WP_392237821
VERSION     WP_392237821.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015408
  ORGANISM  Streptomyces sp. NPDC015408
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 285)
  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 285)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptomyces sp. NPDC015408"
                     /db_xref="taxon:3364956"
     Protein         1..285
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=28725
     Region          23..283
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mplastgdlv graaaarsav aafnvitleh ieavvagaes vrmpvvlqvs enavkyrygr
       61 llplaaaava aaegaavpva lhldhvqsdg llrqardagf ssvmydasrl tyaenlaatr
      121 aavgwahaqg iwieaelgev ggkngaapld ahapgartnp aearafvaes gvdalavavg
      181 sshamtsrta aldhdllkal ssaldvplvl hgssgvpdae laaavtggia kvnvgtalni
      241 amtgairehl aahpdavdsr gyltagream vrtvatiiqv fgats
//
LOCUS       WP_392237695             708 aa            linear   BCT 20-JAN-2025
DEFINITION  DNA gyrase/topoisomerase IV subunit B [Streptomyces globisporus].
ACCESSION   WP_392237695
VERSION     WP_392237695.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Tari,L.W., Trzoss,M., Bensen,D.C., Li,X., Chen,Z., Lam,T.,
            Zhang,J., Creighton,C.J., Cunningham,M.L., Kwan,B., Stidham,M.,
            Shaw,K.J., Lightstone,F.C., Wong,S.E., Nguyen,T.B., Nix,J. and
            Finn,J.
  TITLE     Pyrrolopyrimidine inhibitors of DNA gyrase B (GyrB) and
            topoisomerase IV (ParE). Part I: Structure guided discovery and
            optimization of dual targeting agents with potent, broad-spectrum
            enzymatic activity
  JOURNAL   Bioorg Med Chem Lett 23 (5), 1529-1536 (2013)
   PUBMED   23352267
REFERENCE   2  (residues 1 to 708)
  AUTHORS   Gadelle,D., Filee,J., Buhler,C. and Forterre,P.
  TITLE     Phylogenomics of type II DNA topoisomerases
  JOURNAL   Bioessays 25 (3), 232-242 (2003)
   PUBMED   12596227
REFERENCE   3  (residues 1 to 708)
  AUTHORS   Wang,J.C.
  TITLE     Cellular roles of DNA topoisomerases: a molecular perspective
  JOURNAL   Nat Rev Mol Cell Biol 3 (6), 430-440 (2002)
   PUBMED   12042765
REFERENCE   4  (residues 1 to 708)
  AUTHORS   Champoux,J.J.
  TITLE     DNA topoisomerases: structure, function, and mechanism
  JOURNAL   Annu Rev Biochem 70, 369-413 (2001)
   PUBMED   11395412
REFERENCE   5  (residues 1 to 708)
  AUTHORS   Roca,J.
  TITLE     The mechanisms of DNA topoisomerases
  JOURNAL   Trends Biochem Sci 20 (4), 156-160 (1995)
   PUBMED   7770916
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..708
                     /product="DNA gyrase/topoisomerase IV subunit B"
                     /EC_number="5.6.2.2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003918 - DNA topoisomerase type II
                     (double strand cut, ATP-hydrolyzing) activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006265 - DNA topological change [Evidence
                     IEA]"
                     /calculated_mol_wt=77209
     Region          21..702
                     /region_name="GyrB"
                     /note="DNA gyrase/topoisomerase IV, subunit B
                     [Replication, recombination and repair]; COG0187"
                     /db_xref="CDD:439957"
ORIGIN      
        1 mtaetsvpst amlaaaggdr dssnytarhl lvlegleavr krpgmyigst dsrglmhclw
       61 eiidnsvdea lgghcdqiev ilhddasvev rdngrgipvd vepktglsgv evvmtklhag
      121 gkfgggsyaa sgglhgvgas vvnalssrld vevdrssath sisfrrgvpg mfteqgpdsp
      181 fdpanglrkg krvpktrtgt rvrywadrqi flkdaklnle tlhqrarqta flvpgltiiv
      241 rdergidgeg kteetfrfdg gisefceyla qdkavcdvqr lsgtgtfket vpvlddrghm
      301 tatevtrela vdialrwgtg ydttvrsfvn iiatpkggth vsgfersltk tvnealrsak
      361 mlrvaeddiv kddaleglta vvtvrlaepq fegqtkevlg tsaanrivag vvakelkafl
      421 tstkrdakaq aravlekava aartriaarq hkdaqrrkta lessslpakl adcrsddvdr
      481 selfivegds algtaklarn sefqallpir gkilnvqkss vsdmlknaec gaiiqvigag
      541 sgrtfdidaa rygkvimmtd advdgshirt llltlfqrym rpmveagrvf aavpplhrie
      601 lvqpkkgqdk yvytysdnel rqtllelqrk nvrikesiqr ykglgemdad qlaettmdpr
      661 hrtlrrinig dlesseqvfd llmgnevapr kefitssaat ldrsrida
//
LOCUS       WP_392238755             466 aa            linear   BCT 20-JAN-2025
DEFINITION  alpha,alpha-trehalose-phosphate synthase (UDP-forming)
            [Streptomyces globisporus].
ACCESSION   WP_392238755
VERSION     WP_392238755.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 466)
  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 466)
  AUTHORS   Eastmond,P.J. and Graham,I.A.
  TITLE     Trehalose metabolism: a regulatory role for trehalose-6-phosphate?
  JOURNAL   Curr Opin Plant Biol 6 (3), 231-235 (2003)
   PUBMED   12753972
REFERENCE   3  (residues 1 to 466)
  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   4  (residues 1 to 466)
  AUTHORS   Elbein,A.D., Pan,Y.T., Pastuszak,I. and Carroll,D.
  TITLE     New insights on trehalose: a multifunctional molecule
  JOURNAL   Glycobiology 13 (4), 17R-27R (2003)
   PUBMED   12626396
REFERENCE   5  (residues 1 to 466)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 929-939 (1997)
   PUBMED   9334165
  REMARK    Erratum:[Biochem J 1998 Feb 1;329(Pt 3):719]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..466
                     /product="alpha,alpha-trehalose-phosphate synthase
                     (UDP-forming)"
                     /EC_number="2.4.1.15"
                     /GO_function="GO:0003825 - alpha,alpha-trehalose-phosphate
                     synthase (UDP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0005992 - trehalose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51077
     Region          13..465
                     /region_name="OtsA"
                     /note="Trehalose-6-phosphate synthase, GT20 family
                     [Carbohydrate transport and metabolism]; COG0380"
                     /db_xref="CDD:440149"
ORIGIN      
        1 mvtehaeatg pstaqvlvas nrgpvtytlg edgtldakrg ggglvsglsa vddklwvcaa
       61 lgdgdreavr rgvgepgvrm ldidaevhad ayngiansvl wfvhhllyqt pvepvfdtef
      121 rrqwaayety nrafaealaq eagpgaavlv qdyhlalvpg mlrelrpdlr ighfshtpwa
      181 pvdyfrllpd diaeqllrgi lgadraaflt rrwadafigc cteilggtgr trigvhglga
      241 dadflrrrsh eadvdermaa lreqvgegrk tivrvdrtel sknivrglha yrtlletrpe
      301 wrervvhiaf aypsrqdlsv yrdytaavqs lateingeyg teswtpvvlh vkddfarsla
      361 ayrladvalv npirdgmnlv akevpvvsdq gcalvlsrea gayeelgeda ivvnpydvtg
      421 taealhealt msgdersgrt krlaeaatal ppqrwfldql ealrqg
//
LOCUS       WP_392239786             218 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces sp. NPDC015408].
ACCESSION   WP_392239786
VERSION     WP_392239786.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015408
  ORGANISM  Streptomyces sp. NPDC015408
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Streptomyces sp. NPDC015408"
                     /db_xref="taxon:3364956"
     Protein         1..218
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23348
     Region          2..209
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 mssrerilgr vrraladapa devpvardyl rehgrrttgq tvdllaenla dyraivhrca
       61 dgelsellmr llaahgsrsv vvppglppdw lkavdatrvh draastpqel drvdsvvtgc
      121 avavaetgti vldgspdqgr rritlvpdhh icvvrvpdqv vssvpqaler ldparpltwi
      181 sgpsatsdie ldrvegvhgp rtlevvlvgg qpsgnvts
//
LOCUS       WP_392240422             413 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC014882].
ACCESSION   WP_392240422
VERSION     WP_392240422.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014882
  ORGANISM  Streptomyces sp. NPDC014882
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 413)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Streptomyces sp. NPDC014882"
                     /db_xref="taxon:3364927"
     Protein         1..413
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43342
     Region          74..255
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          261..387
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mnvrpisgas vggrprvrdr rlalvvggll ltvtacggga sgaeetkdgk gagaataasg
       61 qseavvsiap kdgaksvdts galkvtaakg kltevvvkda egakvegtis adgagwtpst
      121 hlaaatkyqv havakdaegr taaedasftt ltpentfvgt ftpedgstvg vgmpfslrft
      181 rgitapddve kavrittvpa vdvqghwfgn drldfrpeky wkagtkvtve lnldgvegrk
      241 gvygkqskki sftigrdqvs vvdakkqtmk vmregkvvkt ipvttgkagy atwngqmvis
      301 ekftvtrmng dtvgydgeyd ikdvphamrl tdsgtfvhgn ywggdafgny nashgciglr
      361 dvrggydsgv paawffnqsm tgdvvvvkns tdpvvspsng lngwnipwae wtk
//
LOCUS       WP_392240746             540 aa            linear   BCT 20-JAN-2025
DEFINITION  peptide ABC transporter substrate-binding protein [Streptomyces sp.
            NPDC014882].
ACCESSION   WP_392240746
VERSION     WP_392240746.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014882
  ORGANISM  Streptomyces sp. NPDC014882
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 540)
  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 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   3  (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
REFERENCE   4  (residues 1 to 540)
  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 540)
  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 11467924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Streptomyces sp. NPDC014882"
                     /db_xref="taxon:3364927"
     Protein         1..540
                     /product="peptide 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=58476
     Region          34..532
                     /region_name="OppA"
                     /note="ABC-type oligopeptide transport system, periplasmic
                     component [Amino acid transport and metabolism]; COG4166"
                     /db_xref="CDD:443327"
ORIGIN      
        1 mrgatharwa acaaavalta tacgggsggd sgavlssswg dpqnplepan tnevqggkvl
       61 dmifrglkky dpetgkaedm laekietsds qnftvtikdg wtfsngekvt aksfvdawny
      121 gaglknnqkn ayffgyiegy dkthpedgsk qtadtlsglk vvddktftvk lnqkfstfpd
      181 tlgypayapl pqafftdhag wlakpvgngp yavdsytkgs qmslrkwady pgddaaqngg
      241 vdlkvytdnn taytdllagn ldlvddvpaa qlknvkndlg drylntpagi lqtlafpfyd
      301 pqwnrsgsdk vrtglsraid reqitetifq ktrtpatdwt spvlgedggf keglcgdacd
      361 ydpaeakkli qeggglpggq vkitynadtg shkqwvdavc nsinnalgnd kacvgnpvgt
      421 fadfrsqigd rkmagpfrag wqmdypliqn flqplyytna ssndgkwsnk efddlvdkan
      481 aetdtgkave tfqqaeevvr dnmaaiplwy qngsagyaer lsnvklnpfs vpvydeikvs
//
LOCUS       WP_392241142             281 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC014882].
ACCESSION   WP_392241142
VERSION     WP_392241142.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014882
  ORGANISM  Streptomyces sp. NPDC014882
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 281)
  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 281)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces sp. NPDC014882"
                     /db_xref="taxon:3364927"
     Protein         1..281
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31251
     Region          23..76
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          98..276
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mvvdgqtaga gsgepessds lrtfgavvqa lrefnglsre efgglvgfsk htvasvelgr
       61 rmpdvdfvea aeralgntga lrraaehlvr qpglaawfrr wasmeklait lytyecrmip
      121 gllqtdsyar qlfvdelppl ddeqieaswa araerqkllr drpntafgfi ieehvllrqt
      181 ggkqvsfgai ehllnlsdlr nieiqvmplv rkahaglhgs mqlletpkhk wfaymeapet
      241 gqlvsdpkai svlqqryarm rsqalsieds vsllhrmrgd l
//
LOCUS       WP_392241495             468 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC014882].
ACCESSION   WP_392241495
VERSION     WP_392241495.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014882
  ORGANISM  Streptomyces sp. NPDC014882
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 468)
  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 468)
  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
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 468)
  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   5  (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   6  (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
REFERENCE   7  (residues 1 to 468)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 468)
  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 20283677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Streptomyces sp. NPDC014882"
                     /db_xref="taxon:3364927"
     Protein         1..468
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45489
     Region          74..130
                     /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            77..78
                     /site_type="active"
                     /note="putative switch regulator [active]"
                     /db_xref="CDD:238044"
     Site            order(96..98,107)
                     /site_type="other"
                     /note="non-specific DNA interactions [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            107..113
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            order(108..109,113)
                     /site_type="other"
                     /note="sequence specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238044"
     Site            108..109
                     /site_type="other"
                     /note="putative cAMP binding site [chemical binding]"
                     /db_xref="CDD:238044"
     Region          144..426
                     /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 mdrtnggttg gwggaigasr psgvggvggl sgvgglsgvg gvggpprpgg tsgtggadga
       61 ggtaggavga nllavrshna alvldllrta gpdgisrlel aertgltpqa vskitarlre
      121 eglaaeagrr astggkprtv lrlvpeaaha vgvhldrdel rivltdldgs vvrehrgpld
      181 lgagaeavlg avergvgrtv geaegpvqgp gtgagpgpap gpgseperep vrgrvsrllg
      241 vgvalpgpld htrgvlhrvt gfpewdgfpl rdalarrlgv pvvvdkdtna aalglavage
      301 rgsfaylhlg tglgaglvia grvhrgtrtg agefghqvvq ldgppcscgd rgcvealcla
      361 aigrgdvaea arvlgvaaan laglldidqi llggrtiaaa pdpfvagvag vlaaraareg
      421 spdlavpvrl apggsggsge fggsggpagv aegaahlllg pvfgrtdv
//
LOCUS       WP_392241800             429 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC014882].
ACCESSION   WP_392241800
VERSION     WP_392241800.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014882
  ORGANISM  Streptomyces sp. NPDC014882
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 429)
  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 429)
  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 429)
  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 11448557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Streptomyces sp. NPDC014882"
                     /db_xref="taxon:3364927"
     Protein         1..429
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45688
     Region          22..75
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
ORIGIN      
        1 mpgdplwnsa kvrelvarrq pgglvrlgre hrewtlaelg ehlgcsaatv srmerrtrvt
       61 dltlihraas tvgvprhvlv sslappapsg lpstrvsasp haeedpmrrr sllaatatvp
      121 aamllgmdra ladtppptgr galdarvasa rdlydkgaht qllgllpgll adghaaassr
      181 reldqarlss vyslsaallt klgsyeqarl tadrartwae vsgsplaaaa afrelaivlr
      241 hqdrgeeaqa lmesaaarve vtglrtdaas sayaqmlctl aytaarggrr aealamaeea
      301 rraaqrlplq appgrlfpis paavdlyavg vhwalgdaga aleagrnlrp eyfptaerka
      361 rlgtdmaraw wawgrpeqta ralldahras pgevrdrpai rsivtelaqr hpravgvrel
      421 haavsapas
//
LOCUS       WP_392241821             300 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Streptomyces goshikiensis].
ACCESSION   WP_392241821
VERSION     WP_392241821.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces goshikiensis
  ORGANISM  Streptomyces goshikiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 300)
  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 12830887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Streptomyces goshikiensis"
                     /db_xref="taxon:1942"
     Protein         1..300
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=31331
     Region          94..157
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          190..280
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mhrqrvmart lglatavala atacgsqktg ntgsastaps asaavttpes spssddkpag
       61 dpsaspsasa ssaspsasas assspsasps vkavmangdd seqvrelqar lkqlklmsva
      121 ptgfygsktt tavksfqsrn gltasgsvda etwkkiqglt kkptadelrp ptvnevdapd
      181 prcmtgrvmc iskesrtlaw midgkvistm dvrfgsentp tregvfdvgw kakewtstiy
      241 htpmpyamff sggqavhysa dfaargysga shgcvnvrdk aklsklfddv kvgdkvvvyw
//
LOCUS       WP_392241833             440 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces goshikiensis].
ACCESSION   WP_392241833
VERSION     WP_392241833.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces goshikiensis
  ORGANISM  Streptomyces goshikiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Streptomyces goshikiensis"
                     /db_xref="taxon:1942"
     Protein         1..440
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=44699
     Region          79..300
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mgqrtviegr gpvavllspr pavvaaarra gartvvvapd psvpsdrega errvrtdwrd
       61 hhrlvgavgr ledvrrgraa vfgfdaagal aaaraneelg lpgtpaaavt almdkaalra
      121 rsntlhaarp vsfarcgras llpfittlig ypcvikprag adgegvrlvr gaaegeaaar
      181 dypavtdllv eeylegpela veslsragch rvlgwsrrlp gpgpglaaag hdlpaaldpa
      241 taaavralvr gvldlaghrd gpshteivlt ahgprlveah arpgaeeltq llrlahgtdv
      301 lglalaaglg lpgplrrpha ahaalryvdf rpglrvdglg palaaarslp gvmrvglrip
      361 agatvrrapt galhhahila aaptaaalar tldlsaalla ppgppgspgp pgspgppgsp
      421 gppgrlipgp rpgqsdagra
//
LOCUS       WP_392242541             433 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces goshikiensis].
ACCESSION   WP_392242541
VERSION     WP_392242541.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces goshikiensis
  ORGANISM  Streptomyces goshikiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 433)
  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 433)
  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
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 433)
  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   5  (residues 1 to 433)
  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   6  (residues 1 to 433)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 433)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 433)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Streptomyces goshikiensis"
                     /db_xref="taxon:1942"
     Protein         1..433
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44514
     Region          21..>87
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          80..404
                     /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 mttgrsgrtv rdlrrgnrga vlqklyfggp msrqelgpat glssgsvsnv vgeliadgll
       61 eeagvvdsdg grprtllrvs pgsahligvd vgetrvrvel fdltltelar aetpllprgc
      121 ydvgpivdhi rsgigavlaq agvgtdrllg vgvgvpgivd reapggavvh gqtigwdavp
      181 leallratga lpqevpylid ngartlgqae mwfgagrgar davvvlfgsg vgaslitdgs
      241 peggstegtp lewghltvsv rgrrcrcgar gcleaytgae sllarwaerg gggppdaagp
      301 adeeealaal lasalagdpv ardvldetae ylgaglsdli nlfrperili ggwaglllgp
      361 yvlpavreha rrhalrhpaa rvsidlgslg pdavtvgaat lplsaffttg grrtappaap
      421 eqpgwrtalt rrg
//
LOCUS       WP_392243157             501 aa            linear   BCT 20-JAN-2025
DEFINITION  complex I subunit 4 family protein [Streptomyces sp. NPDC014882].
ACCESSION   WP_392243157
VERSION     WP_392243157.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014882
  ORGANISM  Streptomyces sp. NPDC014882
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 501)
  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 501)
  AUTHORS   Galemou Yoga,E., Angerer,H., Parey,K. and Zickermann,V.
  TITLE     Respiratory complex I - Mechanistic insights and advances in
            structure determination
  JOURNAL   Biochim Biophys Acta Bioenerg 1861 (3), 148153 (2020)
   PUBMED   31935361
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Friedrich,T. and Scheide,D.
  TITLE     The respiratory complex I of bacteria, archaea and eukarya and its
            module common with membrane-bound multisubunit hydrogenases
  JOURNAL   FEBS Lett 479 (1-2), 1-5 (2000)
   PUBMED   10940377
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Walker,J.E.
  TITLE     The NADH:ubiquinone oxidoreductase (complex I) of respiratory
            chains
  JOURNAL   Q Rev Biophys 25 (3), 253-324 (1992)
   PUBMED   1470679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Streptomyces sp. NPDC014882"
                     /db_xref="taxon:3364927"
     Protein         1..501
                     /product="complex I subunit 4 family protein"
                     /GO_component="GO:0045271 - respiratory chain complex I
                     [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048039 - ubiquinone binding [Evidence
                     IEA]"
                     /GO_process="GO:0015990 - electron transport coupled
                     proton transport [Evidence IEA]"
                     /GO_process="GO:0042773 - ATP synthesis coupled electron
                     transport [Evidence IEA]"
                     /calculated_mol_wt=52730
     Region          1..501
                     /region_name="NuoM"
                     /note="NADH:ubiquinone oxidoreductase subunit 4 (chain M)
                     [Energy production and conversion]; COG1008"
                     /db_xref="CDD:440632"
ORIGIN      
        1 mlsvvtflpl lvcaalmllp rvlpdrvyvw twiataaadl alvvalwagf dtgggmqyeq
       61 rarwipsagv gyhvgvdgls lplvaltgll flavavyslr esrrvrsyvc lflflqtvct
      121 glfvaldlil ffvffdlsiv gmffviagwg hgeraraaal kfflytfvgs lalllgfigl
      181 ylaadphtfd itdltrtnpl agnglyaglv llaigvglav ktpavpfhtw lppahteapa
      241 vgsailagvl lkmgtygfvr iampllpgsw rhyalvvvvv gvvsvvygal valaqtdfkr
      301 miaytsvnhm gyivlavgaa gtlagtddra rslavtgavt qmvshglitg alflltgvly
      361 drggtnamda ysglaahtpr faavtavaaf aslgipgfsg fiaefqiftg slasrttata
      421 vavtgilita alfltalrrm flgvprlpps vptggvadlr rhealptvtl lalalvigvv
      481 prwlldviep agrtltglva r
//
LOCUS       WP_392243221             340 aa            linear   BCT 20-JAN-2025
DEFINITION  heme/hemin ABC transporter substrate-binding protein [Streptomyces
            goshikiensis].
ACCESSION   WP_392243221
VERSION     WP_392243221.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces goshikiensis
  ORGANISM  Streptomyces goshikiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Naoe,Y., Nakamura,N., Rahman,M.M., Tosha,T., Nagatoishi,S.,
            Tsumoto,K., Shiro,Y. and Sugimoto,H.
  TITLE     Structural basis for binding and transfer of heme in bacterial
            heme-acquisition systems
  JOURNAL   Proteins 85 (12), 2217-2230 (2017)
   PUBMED   28913898
REFERENCE   2  (residues 1 to 340)
  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   3  (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   4  (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   5  (residues 1 to 340)
  AUTHORS   Ho,W.W., Li,H., Eakanunkul,S., Tong,Y., Wilks,A., Guo,M. and
            Poulos,T.L.
  TITLE     Holo- and apo-bound structures of bacterial periplasmic
            heme-binding proteins
  JOURNAL   J Biol Chem 282 (49), 35796-35802 (2007)
   PUBMED   17925389
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Streptomyces goshikiensis"
                     /db_xref="taxon:1942"
     Protein         1..340
                     /product="heme/hemin 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=34377
     Region          70..340
                     /region_name="ChuT"
                     /note="ABC-type hemin transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG4558"
                     /db_xref="CDD:443619"
ORIGIN      
        1 mptpaapprf prlvtalaal altlavtgcg gaatranspa ptvssapdrv epltpapapa
       61 lpvtvtsadg tevtvtsaer vipltgslne ivqtlglsgr vvarditatf eqaaklpvvt
      121 rghdvsaesv lslrptlvla ettsgpaeai rqirdagipl lviapaksld dvpkrietva
      181 galgvrdaga rlkqrtaeri aaarkdipgd asgkkprvaf lylrgsasvy llggsdsgaa
      241 slleaagavd tgkesglgkd ftpitseala aaapdailvm skglesvggl dglvkipgva
      301 qtpagmdrrv vsvddgvlln ygprtdqvlt slidqlygka
//
LOCUS       WP_392243579             283 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC014882].
ACCESSION   WP_392243579
VERSION     WP_392243579.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014882
  ORGANISM  Streptomyces sp. NPDC014882
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 283)
  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 283)
  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 16111081
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Streptomyces sp. NPDC014882"
                     /db_xref="taxon:3364927"
     Protein         1..283
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31354
     Region          17..68
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(19,23,48)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(22,47)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(29..30,41,44,48..49)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          99..277
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mparppltar rlrlavelrk mreragmtat daartlgtsq gqlsnvesgr fgvsperirs
       61 lariyscpdq pfvealvgma sektpgwwes yrevlpsgll dlaelehhai airtaytshm
      121 pgllqtadha reifrrvipt ptppevehrv thrvkrqgvl yradptsyst vvheaalrmg
      181 vggrdvaraq llhlldmser ehirirvlpf gigafpgsgq sinylygavp qldtaqldqf
      241 hgpllldaea hlqkyrslld vvetialsae ksrdlihtia qsl
//
LOCUS       WP_392243624             456 aa            linear   BCT 20-JAN-2025
DEFINITION  alpha,alpha-trehalose-phosphate synthase (UDP-forming)
            [Streptomyces goshikiensis].
ACCESSION   WP_392243624
VERSION     WP_392243624.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces goshikiensis
  ORGANISM  Streptomyces goshikiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 456)
  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 456)
  AUTHORS   Eastmond,P.J. and Graham,I.A.
  TITLE     Trehalose metabolism: a regulatory role for trehalose-6-phosphate?
  JOURNAL   Curr Opin Plant Biol 6 (3), 231-235 (2003)
   PUBMED   12753972
REFERENCE   3  (residues 1 to 456)
  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   4  (residues 1 to 456)
  AUTHORS   Elbein,A.D., Pan,Y.T., Pastuszak,I. and Carroll,D.
  TITLE     New insights on trehalose: a multifunctional molecule
  JOURNAL   Glycobiology 13 (4), 17R-27R (2003)
   PUBMED   12626396
REFERENCE   5  (residues 1 to 456)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 929-939 (1997)
   PUBMED   9334165
  REMARK    Erratum:[Biochem J 1998 Feb 1;329(Pt 3):719]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Streptomyces goshikiensis"
                     /db_xref="taxon:1942"
     Protein         1..456
                     /product="alpha,alpha-trehalose-phosphate synthase
                     (UDP-forming)"
                     /EC_number="2.4.1.15"
                     /GO_function="GO:0003825 - alpha,alpha-trehalose-phosphate
                     synthase (UDP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0005992 - trehalose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49309
     Region          3..455
                     /region_name="OtsA"
                     /note="Trehalose-6-phosphate synthase, GT20 family
                     [Carbohydrate transport and metabolism]; COG0380"
                     /db_xref="CDD:440149"
ORIGIN      
        1 massvlvaan rgplsyalaa dgaltarrgg gglvsglsaa lakqpdavwi caalseadre
       61 avrrgvsepg vrmldidetv yddayngian svlwfthhhl ydiptapvfd aefrrrwdsy
      121 vaynhafara laeeaaegaa vlvqdyhlal vpgalrelrp dlrishftht pwaspdfldm
      181 lpgdvrrqlm rgmlgadvag fhtrawadgf lacaqpqcpg stevavfplg vdgddlrela
      241 hrpevedrla elraevgdrk aivrvdrtel sknivrglla yrelltvhpe wrgrvvhlas
      301 aypsrqdlav yrayteavae laerinaefg tqdwqpvlvs vkddfarsla ayrmadvalv
      361 npvrdgmnlv akeipvvsdg gcalvlstga gaygelreda ltvnpfdvte taralhtals
      421 mpvaeraert grlaaaatal ppsawfeaql talrgg
//
LOCUS       WP_392244500             338 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC014882].
ACCESSION   WP_392244500
VERSION     WP_392244500.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014882
  ORGANISM  Streptomyces sp. NPDC014882
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415139
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Streptomyces sp. NPDC014882"
                     /db_xref="taxon:3364927"
     Protein         1..338
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=36134
     Region          1..288
                     /region_name="LysX"
                     /note="Glutathione synthase, LysX or RimK-type ligase,
                     ATP-grasp superfamily [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism,
                     Translation, ribosomal structure and biogenesis, Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0189"
                     /db_xref="CDD:439959"
ORIGIN      
        1 msrpcialia dptssegcre yladavellt gtppvrvdar hfatgasgrg vrdggrlrlr
       61 vaeegldfvp divllyeipp hrrralagfq qllerhdvvt lgtgpeawrt ateknltver
      121 frrdgiaqme tvvlsrptvr eageaferlg gdtwarpvvg tggddtfhvt trarleeatg
      181 yyaghgtdwm lsrdagnfta dglrhqfrvf vlggrvvhar ehlqpaadtp cntcrgatpv
      241 piappdlppr ltelavaata svglpfagvd lavenggvvf evnvqpafvd geletvalpy
      301 vkahldahar aaggprtarr phptqaigtg grdfsapa
//
LOCUS       WP_392245098             219 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LutC/YkgG family protein [unclassified Streptomyces].
ACCESSION   WP_392245098
VERSION     WP_392245098.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..219
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23776
     Region          2..216
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 msgrerilgr vrraladvpr gdsphkgyed avardylreh gersvaetve llaenladyr
       61 avvhrtdeeg lpllvmrlla ergpryvlvp pglppewmsa adptrvhdra vstpreldgv
      121 esvvtgcala vaetgtivld gspdqgrrri tlvpdhhicv vrvpdqvvas vpqalerldp
      181 arpltwisgp satsdieldr vegvhgprtl evilvgqgl
//
LOCUS       WP_392245109             448 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces goshikiensis].
ACCESSION   WP_392245109
VERSION     WP_392245109.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces goshikiensis
  ORGANISM  Streptomyces goshikiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 448)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Streptomyces goshikiensis"
                     /db_xref="taxon:1942"
     Protein         1..448
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=47491
     Region          91..273
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          281..400
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mrmpdpdaar gaagsaeasv tllvsrvlee gsggaggrcg reafhaglcd dgrqqrvlat
       61 argagavlrd pvsrkaaara artialptda dgpleislve pgqltdvtvh dahgrylgga
      121 lgaknrhwtn teplragevy tvrvgaqdaa gtpvgvtmaf rtappteder ltvefgprag
      181 tygagqivta slshpvpasd ptsrarlera lqvtsepave gawhwvddst lhyrprtywp
      241 ahavvrvrgg ldgvafgdhl yggpseslql aigdrieavt dsaahemtvr rngrvlrtip
      301 vttgkagfrt rtgvkvvlgk eyqvrmrgdt vgirpgtsef ydlpvfyatr vtwsgeyvha
      361 apwsveaqge envshgctgm stqdaawffe tvrvgdivev vnsggeemap fangfgdwnl
      421 dwrawlagsa ladgvrapaa lprlsplt
//
LOCUS       WP_392245962             307 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: S66 peptidase family protein [unclassified
            Streptomyces].
ACCESSION   WP_392245962
VERSION     WP_392245962.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..307
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=31981
     Region          4..305
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mkelvrpprl apgarvavva psgpvaeerl qagldllrgw dldpfaaphv ldvhgalphl
       61 agtdadraad lqrawcdpsv davicarggy gaqrmvdlld wdalraagpk vflgfsdstt
      121 lheafavrlg lvtlygpvaa gvdfvknara qehlratlfa petvrtltst gtalapgrar
      181 gvtlggcltl latgygtpht rsgargglll ledvgerpyr vdrtlthllr tgwldgvagi
      241 algswaqcgp yeelrpvlad rlgglgvpvv eelgfghcdg altvpfgiaa eldadtgtlt
      301 latpals
//
LOCUS       WP_392246036             355 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: gluconeogenesis factor YvcK family protein
            [unclassified Streptomyces].
ACCESSION   WP_392246036
VERSION     WP_392246036.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            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 10785358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..355
                     /product="gluconeogenesis factor YvcK family protein"
                     /GO_function="GO:0043743 - LPPG:FO 2-phospho-L-lactate
                     transferase activity [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=37598
     Region          38..343
                     /region_name="CofD"
                     /note="Archaeal 2-phospho-L-lactate transferase/Bacterial
                     gluconeogenesis factor, CofD/UPF0052 family [Carbohydrate
                     transport and metabolism, Coenzyme transport and
                     metabolism]; COG0391"
                     /db_xref="CDD:440160"
ORIGIN      
        1 mtgrtprlgr lrrtapegrt grpvearggr prrrgtqpkv valgggmgls asltalrrit
       61 gdltgvvtva ddggssgrlr delgvlppgd lrkalaalcg dddwgqtwar viqhrfqsqg
      121 einghavgnl livalweqlg dhvqaldlvg kllgaqgrvl pmsavplelq alvkghdpar
      181 pedvdtvrgq atvalttgev qsvhlvpsdp pavpeavaav ldadwvvlgp gswfssviph
      241 llvpelldal tetkarrvls lnlapqpget egfspqrhle vlgrhapkla ldvvladaaa
      301 vpdrdsltda akrfgaavel apvarpdgtp rhdpellaaa ydrifrmhgr igpwr
//
LOCUS       WP_392246313             265 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: metallophosphoesterase family protein [unclassified
            Streptomyces].
ACCESSION   WP_392246313
VERSION     WP_392246313.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 265)
  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 265)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..265
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29064
     Region          12..255
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 mastpsgtpg trihvvsdvh gnardlslag egadaliclg dlvlfldyad rsrgifpdlf
       61 gvenahrive lrtarrfaea relgarlwag igedraavie ravrgqyaem faafptptya
      121 tygnvdmpal wpeyagpgtt vldgerveig grvfgfvggg lrtpmrtpye iddeeyaaki
      181 eavgevdvlc thippevpel vydtvarrfe rgsralldai rrtrpryslf ghvhqplvrr
      241 mrigatecvn vghfastgkp wvlqw
//
LOCUS       WP_392247205             360 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            sp. NPDC014882].
ACCESSION   WP_392247205
VERSION     WP_392247205.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014882
  ORGANISM  Streptomyces sp. NPDC014882
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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   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   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Streptomyces sp. NPDC014882"
                     /db_xref="taxon:3364927"
     Protein         1..360
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39209
     Region          2..338
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 mssrleadhl ykvfgrrqde averlrrgad rdelrgdgtt aavidasftv dpgqifvvmg
       61 lsgsgkstll rmlngllept agrvlfdged ltalgdrelr evrarkismv fqhfalfphr
      121 svldnagygl avqgvpraer eeragealrl cglagweksw pdelsggmqq rvglaralat
      181 dadlllmdes fsaldplirr dmqdqlltlq ktlkktivfi thdlneamrl gdriavmrdg
      241 rivqngtaed ilvrpaddyv asfiqdvdrs rvltasavmd tavrgdeadc gcatadpdtp
      301 ftelcalsar tthpvavvna rrelvgvvpr rrlvgflgde hgeptacadp rdggkvtara
//
LOCUS       WP_392247511             326 aa            linear   BCT 20-JAN-2025
DEFINITION  aldo/keto reductase [Streptomyces goshikiensis].
ACCESSION   WP_392247511
VERSION     WP_392247511.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces goshikiensis
  ORGANISM  Streptomyces goshikiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 326)
  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 326)
  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   3  (residues 1 to 326)
  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   4  (residues 1 to 326)
  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 10790928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces goshikiensis"
                     /db_xref="taxon:1942"
     Protein         1..326
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /calculated_mol_wt=35326
     Region          19..326
                     /region_name="YdhF"
                     /note="Predicted oxidoreductase YdhF [General function
                     prediction only]; COG4989"
                     /db_xref="CDD:444013"
ORIGIN      
        1 madnlntdds argdaagdrv lygcmglggs wepdpygpdd idvaeaavea aldsgittfd
       61 hadiyrhgka eavfgevlar tpglreritl qtkcgirlgg eggpgrydlr gpsivrrvee
      121 sltrlrtdvi dvlllhrpdp ladpdetaga lmslhrqglv rsfgvsnmga pqitalqarl
      181 dvplvanqle mslhsrdwve agvllntpay asngfpfgtl ehcrdhgirl qawgalaqgr
      241 ftgrqstsae hataelladl arkkdttpet illwwlarhp agiapvigsa rpdriracrd
      301 aavrepdlth eewyelwita ravplp
//
LOCUS       WP_392247467             213 aa            linear   BCT 20-JAN-2025
DEFINITION  nicotinamide mononucleotide transporter family protein
            [Streptomyces sp. NPDC014882].
ACCESSION   WP_392247467
VERSION     WP_392247467.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014882
  ORGANISM  Streptomyces sp. NPDC014882
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Hemberger,S., Pedrolli,D.B., Stolz,J., Vogl,C., Lehmann,M. and
            Mack,M.
  TITLE     RibM from Streptomyces davawensis is a riboflavin/roseoflavin
            transporter and may be useful for the optimization of riboflavin
            production strains
  JOURNAL   BMC Biotechnol 11, 119 (2011)
   PUBMED   22136195
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Zhu,N., Olivera,B.M. and Roth,J.R.
  TITLE     Genetic characterization of the pnuC gene, which encodes a
            component of the nicotinamide mononucleotide transport system in
            Salmonella typhimurium
  JOURNAL   J Bacteriol 171 (8), 4402-4409 (1989)
   PUBMED   2546921
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Streptomyces sp. NPDC014882"
                     /db_xref="taxon:3364927"
     Protein         1..213
                     /product="nicotinamide mononucleotide transporter family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0034257 - nicotinamide riboside
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_process="GO:0034258 - nicotinamide riboside transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23501
     Region          8..202
                     /region_name="PnuC"
                     /note="Nicotinamide riboside transporter PnuC [Coenzyme
                     transport and metabolism]; COG3201"
                     /db_xref="CDD:442434"
ORIGIN      
        1 mntlnseafv lldqhilwsd mignifglaa lalgwrrslw swpvqflsgl ilfgaffghl
       61 tgsagkqavv mavalygwwr wnrdrsgsad ghiaprfatw reraamtgaa aagtvavall
      121 ftayptlswd pwpdayifvg tvvamyaqak gmvefwfawl lvdivgvpln fangyafsgf
      181 vyviygalvl wgmrdwwlrs rrgtrpaleg apa
//
LOCUS       WP_392247549             309 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 5'-3' exonuclease [unclassified Streptomyces].
ACCESSION   WP_392247549
VERSION     WP_392247549.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..309
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33039
     Region          7..303
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mrgvtgrlml ldtaslyfra yfgvpdsvra pdgtpvnavr glldfidrlv rdhrpdelva
       61 cmdadwrprw rvdlipsyka hrvaeeheag pdeeevpdtl spqvpvieav ldalgiarvg
      121 vagyeaddvi gtftarakgp vdivtgdrdl yqlvddargv rvlyplkgvg tlqttdeawl
      181 rekygvdgrg yadlallrgd psdglpgvpg igektaakll aefgdlagil aavddpgarl
      241 tptqrkrlge agpylavapk vvrvaddvpl pavttrlpra arepaelagl aerwglggsl
      301 qrllttlga
//
LOCUS       WP_392247772             258 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces sp.
            NPDC014882].
ACCESSION   WP_392247772
VERSION     WP_392247772.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014882
  ORGANISM  Streptomyces sp. NPDC014882
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Streptomyces sp. NPDC014882"
                     /db_xref="taxon:3364927"
     Protein         1..258
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=28351
     Region          4..245
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mnsgilgpll lsdagvnlvp sapkprqlla flmlhtpqmv rasdcitelw gstppksams
       61 tlqtyvlhir qalrgprrdr shllltrnqg yqlaletadf drfrfteltr lghlaaatgd
      121 hrtaskmftl alaqwrgpal sdvstgplss phlaelaetr qgvleqriea dlalgkhrel
      181 vdelsdlaar hpthenvhaq lmvalyrsge reragdvfhh lrralgdslg iepvprmqrl
      241 yqavlvgssa ldapavhr
//
LOCUS       WP_392248803             393 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC014882].
ACCESSION   WP_392248803
VERSION     WP_392248803.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014882
  ORGANISM  Streptomyces sp. NPDC014882
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 393)
  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 393)
  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
REFERENCE   3  (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   4  (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   5  (residues 1 to 393)
  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   6  (residues 1 to 393)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (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 20170230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Streptomyces sp. NPDC014882"
                     /db_xref="taxon:3364927"
     Protein         1..393
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39941
     Region          <10..>74
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          77..384
                     /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 mtarpanahq arllrllrdg gpnsraqlgd qvdlsrskla vevdrlletg lvvadglaas
       61 rggrrshnvr lnpqlrflgv digatsvdva vtnaeletlg hlnqpldvre gpvavfeqvl
      121 amaaklkatg laegfdgagi gvpgpvrfpe gvpvappimp gwdgfpvrea lsqelgcpvm
      181 vdndvnlmam geqhagvart vadflcvkig tgigcgivvg gqvyrgttgs agdighiqav
      241 pdgrpcacgn rgcleayfsg aalardarea aqqglsaela arleangglt avdvaaaaaa
      301 gdataldlir eggdrvgqvi aglvsffnpg lvvigggvtg lghtllaair tqvyrqslpl
      361 atgnlpivlg elgptagvig aarlisdhlf spa
//
LOCUS       WP_392248859             283 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC014882].
ACCESSION   WP_392248859
VERSION     WP_392248859.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014882
  ORGANISM  Streptomyces sp. NPDC014882
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 283)
  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 283)
  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 10611723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Streptomyces sp. NPDC014882"
                     /db_xref="taxon:3364927"
     Protein         1..283
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29712
     Region          10..>59
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(16,20,45)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(19,44)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(26..27,38,41,45..46)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          174..258
                     /region_name="DUF2690"
                     /note="Protein of unknown function (DUF2690); pfam10901"
                     /db_xref="CDD:402475"
ORIGIN      
        1 mttpapecaa laeglravra rtglslaala ertpyskssw erylngklpv prqavealca
       61 magehpgrll alweladaew sgrarspapa paapgsaipg satprpgtpd agrtapharq
      121 arwwrlpvlg agaavaaaam taalwwlphq tsgrpttpds stldpapgcr geacdgkdpa
      181 rmscglpgra dalgpphrtr tganveirys tvcaaawgrv whtrvgdave vsapgapprr
      241 vvvrttadts vyrftpmlgg dhrtdlrlcf lpadgtarec yrp
//
LOCUS       WP_392249000             458 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC014882].
ACCESSION   WP_392249000
VERSION     WP_392249000.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014882
  ORGANISM  Streptomyces sp. NPDC014882
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Streptomyces sp. NPDC014882"
                     /db_xref="taxon:3364927"
     Protein         1..458
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=49010
     Region          89..324
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mttfrdsgar saadaaaphr pavivitdlv viakhlrlld tagrrgvtpl fvfgpetpgd
       61 elarhrrdpr hplsrladed lrhvadtsld tllravapwl rdrpvravln vgevfveaag
      121 alaqslglpg pgahaarvcr nkllqrlaap alaprwmlld parppaadgw dtypavlkpa
      181 srmsssgvra vagpdavppl lpdygpdell lleeritgre fsvetlvrdg avlwtgitak
      241 dtnesatsff tetghtspap hltpaqekll fdanaeflra vrfgtgmsha efrltaedrv
      301 vlmeaaarpp gdaitrlwrl atgmdldaal ldlalgteps tapprrrarq vyldhprgll
      361 advtaedvpv hwvgergrwp dlpplagdap arahavlvsr srgdllgdls dsrgrsvsvv
      421 ldaplgsdlg pttqdatarv tihavqpspa etseealr
//
LOCUS       WP_392249187             407 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC014882].
ACCESSION   WP_392249187
VERSION     WP_392249187.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014882
  ORGANISM  Streptomyces sp. NPDC014882
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Streptomyces sp. NPDC014882"
                     /db_xref="taxon:3364927"
     Protein         1..407
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=43012
     Region          56..316
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 msdrpvvlvv apgdanyrgy cleqvadtyd vvlltaaqps weeahiidhv vadlddpaal
       61 qaggralaar hdlagvmtwd ewclvptarl aralglpans vevtracrnk atarslfarh
      121 gvpsavslsv rslpeaqaaa aqigypvvlk paahagamgv qrvdtpdqla aahhvaqlta
      181 gpaaennqvl veefldgpei svecvtyrgt ttvvavnrkt isppphfeql ahrvdaadpl
      241 lgivtpaara airalritng vshiemrlvd grprlievng rlagdmighl vrlttgidlp
      301 raaadlacgq apdltasrvg aaaigmiyph tsgtlthlgy tgtrppwldr lcfqhrpgdr
      361 lllpqdggtl ftaragfyiv tgstpaqvne rlsvvadeit vavkadr
//
LOCUS       WP_392249273             445 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces gardneri].
ACCESSION   WP_392249273
VERSION     WP_392249273.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces gardneri
  ORGANISM  Streptomyces gardneri
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 445)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Streptomyces gardneri"
                     /db_xref="taxon:66892"
     Protein         1..445
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=46882
     Region          87..266
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          274..393
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mplavgavlv gtaaqppagp atlaagapds tavvsvdacg sglcsaprht valsaggtsa
       61 artltgrsvm lgdqatgpvt lllrtpgrla dvtvtdrrgr rvagvpsadg trwtsdtalp
      121 aggrytarlv verpdheagp eaphrhlarl efrtavatid erltvtfgpe ggrtygvgrp
      181 itaelsrpvp adspgarrlv eralqvrtep rvegswhwvd sttlhyrprd ywparavirv
      241 hsgldgqrvg gglyggpsrp ltfttgdrve avtdvaalkm tvfhdgravr tfpvttgkag
      301 yrtrggikvv lgkeplvrmr gdsigivrgs rdfydlkvrw atrvtwsgey lhaapwslda
      361 qgsenvshgc tgmstedaaw lfrtvregdl vrvvngygep mtpfgngfgd wnlgwaewrr
      421 gsaladpaaa agpaaaaags lrpal
//
LOCUS       WP_392249731             418 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC015680].
ACCESSION   WP_392249731
VERSION     WP_392249731.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015680
  ORGANISM  Streptomyces sp. NPDC015680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 418)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Streptomyces sp. NPDC015680"
                     /db_xref="taxon:3364962"
     Protein         1..418
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=44431
     Region          57..239
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          247..366
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mnhtprirpv vsctllvvsl vagvaacggs gghplaekpy daaddvsana sdgdekvdpg
       61 kplevtvngd dgritdvsav dttgrhlage ldadgkrwhs tlplaagtry tvrvgveddd
      121 gapgsrtlsf gttsakkflk vafgpqagty gvgqpitael sapvkdkasr anveralrvr
      181 stpavtgswy wvddktlhyr pkdywparat idvtsglagv kvtdalygap tkplrlttgd
      241 rieavtnaaa hsmtvkrdgk vintipvttg kpgfstrngv kvvlgkeyrv rmrgetigia
      301 egssdsydlq vyyatrvtws geyvhaapws tgsqgyanvs hgctgmstsq aewfyntvrp
      361 gdivtvvgse getmtpfdng fgdwnlswak wlkgsalqkn tapdrtetiq aarlrpev
//
LOCUS       WP_392253797             131 aa            linear   BCT 20-JAN-2025
DEFINITION  TOBE domain-containing protein [Streptomyces globisporus].
ACCESSION   WP_392253797
VERSION     WP_392253797.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 131)
  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 10007583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..131
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13768
     Region          1..128
                     /region_name="MopI"
                     /note="Molybdopterin-binding protein MopI [Coenzyme
                     transport and metabolism]; COG3585"
                     /db_xref="CDD:442804"
ORIGIN      
        1 mqsytigqaa rllgvspdta rrwadagrva thrdeagrrl vdgralaafs ievgqsagae
       61 dedsytsarn afpgivtavk lgdvaaqvei qagphrlvsl ltreaveelg levgmqatar
      121 vkstsvhidr t
//
LOCUS       WP_392252383             183 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            globisporus].
ACCESSION   WP_392252383
VERSION     WP_392252383.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..183
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=19483
     Region          39..>133
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mdsscvlpvp gtasvparrs ctvlrtsrsr askslsgiva vpltktrert alallalnrg
       61 qriskehllq avwgerlpst vnsqvsiimy nlraclaagk sdvivsaggs ytlldeacdt
      121 dlafaesqir qargaapvpa avtawrqvws ttsrsrkqnp sqvahhetlr sassssfgrp
      181 slr
//
LOCUS       WP_392255258             289 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Streptomyces globisporus].
ACCESSION   WP_392255258
VERSION     WP_392255258.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 289)
  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 289)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..289
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29909
     Region          42..281
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mplaatgdli aeaaaqhrav aafnvitleh aeaiaegaea agspvilqis enavayhrgr
       61 prpiaraaae vadqaavpvs lhldhvqste llhraadcgf ssamfdaarl pytenlaatr
      121 aavvwaherg lwleaelgqv ggkngeppln ahapgartdp eearsfvtat gvdalavavg
      181 tshamtsrda vidhellggl raavpvplvl hgssgasdee laravaggir kvnigtalni
      241 amtgairerl aqddrgvdpr ryladgrdam artvtrlmav laqgrvqaa
//
LOCUS       WP_392256106             417 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces globisporus].
ACCESSION   WP_392256106
VERSION     WP_392256106.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 417)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..417
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=44348
     Region          57..239
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          247..366
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mnhtprirtv vsctllvvtl aagatacgsp dghplstkpy dagdqvsfng psdkekadpd
       61 kplevtvkgd dgritdvsav dtggrhlage lsadgkrwrs taplaagtgy tvrvstengd
      121 gapgvrtlsf dtsspkkllk vafgpeggty gvgqpitael sapitdkasr atveralkvr
      181 stpattgswy wvddkklhyr pkeywpanat vevrsnlagi kvtnalygae akplklttgd
      241 rieavtdaan hsltvyrnge vintipvttg kpgfstrngv kvvlakeqfv rmrgesigia
      301 agssesydlp vywatrvtws geyvhaapws tgsqgnanvs hgctgmstsn aewffdtvrm
      361 gdivkvvgse geemdpfgng fgdwnlswek wqqgsalheg apdspqtlqt arlrphv
//
LOCUS       WP_392256561            1385 aa            linear   BCT 20-JAN-2025
DEFINITION  Rne/Rng family ribonuclease [Streptomyces globisporus].
ACCESSION   WP_392256561
VERSION     WP_392256561.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1385)
  AUTHORS   Kime,L., Jourdan,S.S. and McDowall,K.J.
  TITLE     Identifying and characterizing substrates of the RNase E/G family
            of enzymes
  JOURNAL   Methods Enzymol 447, 215-241 (2008)
   PUBMED   19161846
REFERENCE   2  (residues 1 to 1385)
  AUTHORS   Callaghan,A.J., Marcaida,M.J., Stead,J.A., McDowall,K.J.,
            Scott,W.G. and Luisi,B.F.
  TITLE     Structure of Escherichia coli RNase E catalytic domain and
            implications for RNA turnover
  JOURNAL   Nature 437 (7062), 1187-1191 (2005)
   PUBMED   16237448
REFERENCE   3  (residues 1 to 1385)
  AUTHORS   Li,Z., Pandit,S. and Deutscher,M.P.
  TITLE     RNase G (CafA protein) and RNase E are both required for the 5'
            maturation of 16S ribosomal RNA
  JOURNAL   EMBO J 18 (10), 2878-2885 (1999)
   PUBMED   10329633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1385
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..1385
                     /product="Rne/Rng family ribonuclease"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=145913
     Region          <15..429
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <37..>151
                     /region_name="PRK07003"
                     /note="DNA polymerase III subunit gamma/tau"
                     /db_xref="CDD:235906"
     Region          643..1044
                     /region_name="CafA"
                     /note="Ribonuclease G or E [Translation, ribosomal
                     structure and biogenesis]; COG1530"
                     /db_xref="CDD:441139"
ORIGIN      
        1 mpqpnepgtt gnneentpgd klpprrrrra asrpagppgg pvsaaedvtp aipaetsaap
       61 atddtpgdpv aetappartr rravrkaaap agapveteta epapvaetpa qpavdeepaa
      121 paprsrrrav rkatspagap qsaeapapvv espaepalep aaeeetevav etpdeapapr
      181 rrrasrkats pagtpqsaea avvvepvaaa aepapaaepa vtepaaprgr arrrasapag
      241 apqsaepvaq pepavaapaa papaaeaeat eeapaprtrr rasrkasapa gapqateaae
      301 sveepvetge slpaavaeel aadadeveea aprgrqrrra taaagrpeft akteestrkg
      361 rratrpavav fqapvfaepm fqtpetaaaa aaaagsstad devdeteeqq taeaeqstap
      421 aeaapqggsr rrrrrrgeae ateqaadeap eaeadehege dtdeygdrps rrrrrggrrr
      481 rrgeandtdd eqttedapar aeeprsedeq dagrgqsqea aeesdeddds sasgsssssr
      541 rrrrrrrrsg dtatdtdngs ddpertvvkv reprkkeere pgtgfdevqs ikgstrmeak
      601 kqrrregreq grrrvpiite aeflarreav ervmvvrqng ertqigvled nvlvehyvnk
      661 eqatsyvgnv ylgkvqnvlp smeaafvdig kgrnavlyag evnfealgma hgprrietal
      721 ksgqsvlvqv tkdpighkga rltsqvslpg rylvyvpegs mtgisrklpd tersrlktil
      781 kkivpedagv ivrtaaegas edelrrdver lqqqwediqk kakgtsgsna ptllygepdm
      841 tvrvvrdifn edfskvivsg ddawetihgy vshvapdlte rlsrwtsevd vfatyrideq
      901 lmkaldrkvy lpsggslvid kteamvvvdv ntgkftgqgg nleetvtrnn leaaeeivrq
      961 lrlrdlggiv vvdfidmvle snrdlvlrrl leclgrdrtk hqvaevtslg lvqmtrkrvg
     1021 qgllesfset cvhcngrgvi vhmeqptsgg gggggkkskk rgrggagqdh ehdhahgsdd
     1081 hgsaepvete teaelaaeva apvavepavr eddefygspa eaeaaasrrg rrrasrkasa
     1141 pagapkaeap apvveapvae apvaevaevt aaaetpeaaq apeapaeaap qgrtrrratr
     1201 katapagspk qaeaaepvqp aepsadpvav edpvveapaa eapapeaeap vaapprarrr
     1261 atrkatapag sptgsddgei vvvasapepk apeeiaesga adagtadsep teaapakkta
     1321 rkaaakkapa kkaaakktaa kktaakktta ktaakkatkk tvaaeqssps vtvnapsaeg
     1381 essas
//
LOCUS       WP_392256727             274 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            globisporus].
ACCESSION   WP_392256727
VERSION     WP_392256727.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 274)
  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 274)
  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 274)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..274
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30569
     Region          14..68
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          86..263
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mgtkqgprtp rqkygeelrl rriaagltqe alsemvvcsp tlishyeagr rlpspedarr
       61 idqalgtdgf ferwlqdlet kyndhfaava eleqqavliq qfaltlvpgl lqtddyaral
      121 feayrpnhrk edidkevvir terarvldgp lnpvlwtlld eavlrrrvgg pqvmasqlrk
      181 iadlaeagrl rlhvlpfeag ahslqqsllt lmsfsdsapv ayveafqtgn lmddprlvts
      241 srtaydlalg dalshqesva rvraaaeehe hghq
//
LOCUS       WP_392257353             349 aa            linear   BCT 20-JAN-2025
DEFINITION  BMP family lipoprotein [Streptomyces sp. NPDC015184].
ACCESSION   WP_392257353
VERSION     WP_392257353.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015184
  ORGANISM  Streptomyces sp. NPDC015184
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Yousief,S.W., Bahey-El-Din,M. and Zaghloul,T.I.
  TITLE     Immunization with the basic membrane protein (BMP) family ABC
            transporter elicits protection against Enterococcus faecium in a
            murine infection model
  JOURNAL   Microbes Infect 22 (3), 127-136 (2020)
   PUBMED   31585177
REFERENCE   2  (residues 1 to 349)
  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   3  (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   4  (residues 1 to 349)
  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   5  (residues 1 to 349)
  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 11448319
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Streptomyces sp. NPDC015184"
                     /db_xref="taxon:3364946"
     Protein         1..349
                     /product="BMP family lipoprotein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /calculated_mol_wt=36010
     Region          34..346
                     /region_name="Med"
                     /note="Lipoprotein Med, regulator of KinD/Spo0A, PBP1-ABC
                     superfamily, includes NupN [Signal transduction
                     mechanisms]; COG1744"
                     /db_xref="CDD:441350"
ORIGIN      
        1 mrritriatv glasaalals atacgsktss dagsdskeak taiaydvggr gdqsfndaay
       61 aglakaekel gfkgteaeps dgeadadkvq rlttlaragn npvigvgfay apaikkvaak
      121 fpkttfgiid dasvtdknia nmvfneeqgs ylagvaaakv tksktvgfig gvetplikkf
      181 qagfeqgvkd tdssvkvlsq yltqppnfdg fskpdlgkaa aqgqldkkad viyaaaglag
      241 sgsieataka gkwaigvdsd qynqkglaay kdqiltsvtk dvadsvynli ksvkdgkpqs
      301 gevrygldkd gvgladsnpa ftkmtdviaa vdkakkdiid gkvtvkttp
//
LOCUS       WP_392257423             420 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC015184].
ACCESSION   WP_392257423
VERSION     WP_392257423.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015184
  ORGANISM  Streptomyces sp. NPDC015184
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 420)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Streptomyces sp. NPDC015184"
                     /db_xref="taxon:3364946"
     Protein         1..420
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=44082
     Region          71..252
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          258..390
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mekrvmtdsk rrrglmaasa llggvlvlta cndgtdksad gskksqaaev dkaaaqdase
       61 aqitispkng atnasinnda kvtvtkgkls evvmttsaga avkgtlsadg kswkpdvqle
      121 rsttykitat akdskgreah enssfttvsp ansfignftp edgstvgvgm pvsinfnkpi
      181 tdrkavqsgi tvtsssgqqv vghwfnsqrl dlrpedywqg gstvtlklal dgvegadgvf
      241 gvqqktvtfk vgrnqvstvd akaktmtvtq dgktiktipi sagssdnpty ngqmvisekf
      301 ketrmngatv gftdddgkge ydikdvpham rlstsgtfih gnywgarsif gsantshgcv
      361 gladvkgagd sgqpaawfyn nsligdvviv knspdktitp dnglngwnms wsqwtagsav
//
LOCUS       WP_392257676             291 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptomyces globisporus].
ACCESSION   WP_392257676
VERSION     WP_392257676.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 291)
  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 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   3  (residues 1 to 291)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 291)
  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   5  (residues 1 to 291)
  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   6  (residues 1 to 291)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..291
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32277
     Region          19..103
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          127..286
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mlerlndame hieahlgeri eaadlariat tseyhfrrmf salaglplse yirrrrmtva
       61 gaevlgdrdr slldvamryg ydtgegfara fravhgigpg earrtgavlr sqqrltfrlv
      121 vegssamrys lveknafrvv gkkarvplih egpnpaiaef irgigreeld riaalsdqkp
      181 agivgvsdql dpsraegtel dyyhgvvtge aeppedldal dvpagtwavf esegafpqal
      241 qylwrdvftq wfpsnpyasr pgpeilrvrl tedgkraeae lwipversae s
//
LOCUS       WP_392257802             415 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            globisporus].
ACCESSION   WP_392257802
VERSION     WP_392257802.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  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 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   3  (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   4  (residues 1 to 415)
  AUTHORS   Igarashi,K., Ito,K. and Kashiwagi,K.
  TITLE     Polyamine uptake systems in Escherichia coli
  JOURNAL   Res Microbiol 152 (3-4), 271-278 (2001)
   PUBMED   11421274
REFERENCE   5  (residues 1 to 415)
  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   6  (residues 1 to 415)
  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 11430824
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..415
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0019808 - polyamine binding [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:0015846 - polyamine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45332
     Region          28..413
                     /region_name="PotD"
                     /note="Spermidine/putrescine-binding periplasmic protein
                     [Amino acid transport and metabolism]; COG0687"
                     /db_xref="CDD:440451"
ORIGIN      
        1 mesyeperlt pvqlaamrrs ltsgrgaltr rsllrasgmg alavggiatl gacgippakr
       61 adaglasddh sekekvlnfs nwteymdvse deksrptlea ftertgirvk ytedindnve
      121 ffgkikpqla agqdtgrdli cvtdwlaari irlgwaqkld psnlphafan vsaqfrspdw
      181 dpgraysypw tgiptviayn kkatggrkvd svtqllddpk lkgrvsflse mrdtvgmtll
      241 dqgkdpgkfs dadfdgaigr lqkavdkkqi rrftgndyta dlskgdiaac vawagdviql
      301 qadnpdieya ipaagyitss dsllvpaqar hktnaeklid yyyeppvaaq laayinyvcp
      361 vdgvreelar idasmasntl ilpdkemaak srsfrslste eetayeekfa kliga
//
LOCUS       WP_392257898             415 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces globisporus].
ACCESSION   WP_392257898
VERSION     WP_392257898.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..415
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43504
     Region          75..256
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          262..389
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mngqpisgas agasgkrrgg pgllalvlga llvlvtacgg ggadagdkkg paggtkkedt
       61 tasqavvtia pkdgadsvat sgalkigaeq gklttvkvad pkgnevegei sadgaswtpe
      121 rhlaastkyt vhavakdseg resakdttft tlvpantfig hytpedgstv gvgmpvsinf
      181 trgitdpdav ekgvkvtaep aveieghwfg ndrldfrpet ywkpgtkvtv elnldgvegr
      241 pgvygkqvkk vsftigrsqv stvdasskrm kvvrdgkqik dipisagapa tttyngemvi
      301 seklkvtrmn gdtvgfggey dikdvphamr lstsgtflhg nywgassifg ntntshgcvg
      361 lrdvrggydn qtpaawfynk smigdvvivk nskdkqiapd nglngwnmdw eewkk
//
LOCUS       WP_392258971             510 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Streptomyces sp. NPDC015184].
ACCESSION   WP_392258971
VERSION     WP_392258971.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015184
  ORGANISM  Streptomyces sp. NPDC015184
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 510)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Streptomyces sp. NPDC015184"
                     /db_xref="taxon:3364946"
     Protein         1..510
                     /product="amidohydrolase family protein"
                     /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=54904
     Region          44..479
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mptrrealaa saaltggall saapsaaaap rvtprhatsv sdrssgttia lahatvlgag
       61 adhtvlvrdg ritrtgrsae vpippgatvy dltgkyivpg glveshvhnd gpenvlpplf
      121 plngvtavre mwgrpvhhew rdkvragell gprwviagsi idgspslwag dldervvevt
      181 dapsarravr etkasgadfv kvysrltpga yeaiadesrr qglryaghcp dtlpiarasd
      241 agqqsiehlh alllatsare peirramakv ridpaigtsf eryaswfrqv havewqavqt
      301 ydvgrtralf drlaangtrv vptltvhhsl ertdqlpens pefaylpgwm tgywptvwsa
      361 ltagrtardt arihriyehr lhlvaelhra gvqllagtdt gtgyavpgfs lhhelellae
      421 aglptrdvlh aataaparml glpadradll vldadprtdv rhtrridsvl vagryldrae
      481 rlrllsdvar aaaasepptt gvaaphvcvh
//
LOCUS       WP_392258055             344 aa            linear   BCT 20-JAN-2025
DEFINITION  gluconeogenesis factor YvcK family protein [Streptomyces sp.
            NPDC015184].
ACCESSION   WP_392258055
VERSION     WP_392258055.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015184
  ORGANISM  Streptomyces sp. NPDC015184
            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 10785358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Streptomyces sp. NPDC015184"
                     /db_xref="taxon:3364946"
     Protein         1..344
                     /product="gluconeogenesis factor YvcK family protein"
                     /GO_function="GO:0043743 - LPPG:FO 2-phospho-L-lactate
                     transferase activity [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=36500
     Region          21..332
                     /region_name="CofD"
                     /note="Archaeal 2-phospho-L-lactate transferase/Bacterial
                     gluconeogenesis factor, CofD/UPF0052 family [Carbohydrate
                     transport and metabolism, Coenzyme transport and
                     metabolism]; COG0391"
                     /db_xref="CDD:440160"
ORIGIN      
        1 mtsrnlrlrr lrratpalsg rkrgaqpkvv algggmglsa slaslrritg dltavvtvad
       61 dggssgrlre elgvlppgdl rkalaalcgd ddwgqtwsrv iqhrfqskgd lhehavgnll
      121 ivalweqlgd hvqaldlvgk llgahgrvlp msavplelqa lvrghdpdrp gdvdtvrgqa
      181 tvaltpgevq svhlvphdpp avpeavaavl dadwvvlgpg swfssviphl lvpelldalv
      241 etkarkvlsl nlapqpgetd gfspqrhlev lgrhapklal dvvladeaav pdresladaa
      301 krfgaavela pvaspdgvpi hdpellaaay drifrmhgri gpwr
//
LOCUS       WP_392259795             581 aa            linear   BCT 20-JAN-2025
DEFINITION  type I restriction-modification system subunit M [Streptomyces
            globisporus].
ACCESSION   WP_392259795
VERSION     WP_392259795.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 581)
  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   2  (residues 1 to 581)
  AUTHORS   Youell,J. and Firman,K.
  TITLE     Mechanistic insight into Type I restriction endonucleases
  JOURNAL   Front Biosci (Landmark Ed) 17 (6), 2122-2139 (2012)
   PUBMED   22652768
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Sistla,S. and Rao,D.N.
  TITLE     S-Adenosyl-L-methionine-dependent restriction enzymes
  JOURNAL   Crit Rev Biochem Mol Biol 39 (1), 1-19 (2004)
   PUBMED   15121719
REFERENCE   4  (residues 1 to 581)
  AUTHORS   Murray,N.E.
  TITLE     Type I restriction systems: sophisticated molecular machines (a
            legacy of Bertani and Weigle)
  JOURNAL   Microbiol Mol Biol Rev 64 (2), 412-434 (2000)
   PUBMED   10839821
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114514
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..581
                     /product="type I restriction-modification system subunit
                     M"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=64797
     Region          4..134
                     /region_name="HsdM_N"
                     /note="HsdM N-terminal domain; pfam12161"
                     /db_xref="CDD:463478"
     Region          149..409
                     /region_name="HsdM"
                     /note="Type I restriction-modification system, DNA
                     methylase subunit [Defense mechanisms]; COG0286"
                     /db_xref="CDD:440055"
ORIGIN      
        1 mstlgsfiws iadqlrgpyr pnqygtvvlp ftilrrldci lepdqatare laakfdnpnr
       61 lkvevkkatg rtfyntsnys fanlladadg ladnladyid rfsadvdvfe yfdfkkeila
      121 lekagllrei vksfgkvdlh pdvvsnsdmg dafeyiirkf neaanetsgd hytprdairl
      181 lvdllfaekd vdlteggiir slydptagtg gmlslaeehl laenpgaklg lygqeynpqs
      241 yaicksdlla kghdatniaf gntltddafk grqfdycmsn ppygvdwkqy akavkeerds
      301 agpygrfapg lpatsdgqml fllhlahkmr apedgggrvg ivmngsplfn gaaesgpsni
      361 rrwllendlv eaivalptnm ffntgiatyi wildntkhpd rqgkvqlidg tsfwtkmrkn
      421 lgakgreisd adraevlrly ddfedadpef skvlpndqfg ywtitverpl ldeggnpvan
      481 rkgdpkpdsk krdtenvpft yggstagava erefiqayfd aevkphvpda widwaktkag
      541 yeipftrhfy kyvpprplae idadlekqvs kildllreve q
//
LOCUS       WP_392260615             247 aa            linear   BCT 20-JAN-2025
DEFINITION  S1 family peptidase, partial [Streptomyces sp. NPDC015184].
ACCESSION   WP_392260615
VERSION     WP_392260615.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015184
  ORGANISM  Streptomyces sp. NPDC015184
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Querino Lima Afonso,M., da Fonseca,N.J. Jr., de Oliveira,L.C.,
            Lobo,F.P. and Bleicher,L.
  TITLE     Coevolved Positions Represent Key Functional Properties in the
            Trypsin-Like Serine Proteases Protein Family
  JOURNAL   J Chem Inf Model 60 (2), 1060-1068 (2020)
   PUBMED   31895561
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Waldner,B.J., Kraml,J., Kahler,U., Spinn,A., Schauperl,M.,
            Podewitz,M., Fuchs,J.E., Cruciani,G. and Liedl,K.R.
  TITLE     Electrostatic recognition in substrate binding to serine proteases
  JOURNAL   J Mol Recognit 31 (10), e2727 (2018)
   PUBMED   29785722
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Pelc,L.A., Chen,Z., Gohara,D.W., Vogt,A.D., Pozzi,N. and Di Cera,E.
  TITLE     Why Ser and not Thr brokers catalysis in the trypsin fold
  JOURNAL   Biochemistry 54 (7), 1457-1464 (2015)
   PUBMED   25664608
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Perona,J.J. and Craik,C.S.
  TITLE     Evolutionary divergence of substrate specificity within the
            chymotrypsin-like serine protease fold
  JOURNAL   J Biol Chem 272 (48), 29987-29990 (1997)
   PUBMED   9374470
REFERENCE   5  (residues 1 to 247)
  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 10595581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Streptomyces sp. NPDC015184"
                     /db_xref="taxon:3364946"
     Protein         1..>247
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
     Region          29..183
                     /region_name="Trypsin_2"
                     /note="Trypsin-like peptidase domain; pfam13365"
                     /db_xref="CDD:433149"
ORIGIN      
        1 mslvkdatvr ihrpepgyap gesggdflgs gffiapswvl tcahvasegr grqvdvvykt
       61 arggeavtvg gtvvaalpee rpatggwpap dlaliqllrp vdhpcvylse rstglgrgay
      121 yfagwadgga gklkrlgrec rvvgtiddws dgdeqmliea sqlypgmsgg plvdlargev
      181 vgilksrsdd atggtaigie rlrtlpvpga aaappspapd pagvhapdrd paappdhpra
      241 gaaawga
//
LOCUS       WP_392260819             413 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC015184].
ACCESSION   WP_392260819
VERSION     WP_392260819.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015184
  ORGANISM  Streptomyces sp. NPDC015184
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 413)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Streptomyces sp. NPDC015184"
                     /db_xref="taxon:3364946"
     Protein         1..413
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=44228
     Region          63..250
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          256..382
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mkhvakrakr tvagsatvpv ragllavlav lavltgcsgv gsifsgkarp pqeailitpk
       61 drakdvgpdd rvevrvpdgr lqsvrvtrie daqrrelpgr isddglswep gkgaarlgla
      121 akysvdavav ddsgnrtarh ttfttavpah rfigyfkpen ratvgtgmiv sfdfnrpitd
      181 raavqrairv tsdppvevvg hwfgadrldf rpekywepgt evtvvvglrd vegaphvygs
      241 qdktiafevg rsqtsvvdaa ahtmevrrdg rtvatfpita gspgtatyng kmvvsemnev
      301 trmdgrtvgf ggeydiadvp halrltdsgt flhgnywsde gvfgsdnvsh gcvglldvkg
      361 ggddtpagrf fdrtligdvv evvnsadkrv apdnglsgwn ldwahwrags alr
//
LOCUS       WP_392261017             363 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            sp. NPDC015184].
ACCESSION   WP_392261017
VERSION     WP_392261017.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015184
  ORGANISM  Streptomyces sp. NPDC015184
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   3  (residues 1 to 363)
  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   4  (residues 1 to 363)
  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 363)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Streptomyces sp. NPDC015184"
                     /db_xref="taxon:3364946"
     Protein         1..363
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38845
     Region          2..341
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 mfgrrpdqav rrledgadrd elradgttaa vidasfavep gqifvvmgls gsgkstllrm
       61 lnglleptag rvlfdgqdlt alspaelrhv rsskismvfq hfalfphrsv lenaayglev
      121 qgvpraerek raaealeltg lagwekswpd elsggmqqrv glaralatda dlllmdesfs
      181 aldplirrdm qdqllelqkr lkktivfith dlneamrlgd riavmrdgri vqlgtaedil
      241 vtpandyvas ftqdvdrtrv ltagaimaep htvmgtstdd geelrtaadv iaaapatvte
      301 stpiaelftp csqsgvavav tdaggklvgv vprarllavl gepmtpaeap kdvpadlkkv
      361 asv
//
LOCUS       WP_392261460             287 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces sp.
            NPDC015184].
ACCESSION   WP_392261460
VERSION     WP_392261460.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015184
  ORGANISM  Streptomyces sp. NPDC015184
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789410
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Streptomyces sp. NPDC015184"
                     /db_xref="taxon:3364946"
     Protein         1..287
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31626
     Region          4..259
                     /region_name="PrpB"
                     /note="2-Methylisocitrate lyase and related enzymes, PEP
                     mutase family [Carbohydrate transport and metabolism];
                     COG2513"
                     /db_xref="CDD:442003"
ORIGIN      
        1 mrygsalree vrspgttpli giydmysasv varhyegffv sgfgfaashy glpdigfiaw
       61 pdmvafverl rlafpshhll vdiddgyvdp evachvvqrl erigasgvil edqkrprrcg
      121 hadgkqvlpl eeyleklnlv lesrrdlvvv artdateedd ilrraealag tdadvvlvdg
      181 vrsvewikri rkvvgdkpll fnqiaggksp rlslseltdl ecqvaiystp clfaahaaid
      241 saltdlkead grlpefvpae gigvqrstel leknisrhhp vresvsv
//
LOCUS       WP_392261593             690 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces sp.
            NPDC015184].
ACCESSION   WP_392261593
VERSION     WP_392261593.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015184
  ORGANISM  Streptomyces sp. NPDC015184
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 690)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 690)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 690)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Streptomyces sp. NPDC015184"
                     /db_xref="taxon:3364946"
     Protein         1..690
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=73585
     Region          2..248
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mrvefgvlga viarngagdp lplkgprhra vlarlvvahr rvvpvarlve dlwgeppada
       61 vgavrtfvgd lrravepdrp prtpprllvt egpgyalrvp kddvdawrfe avldglgdag
      121 pdrvadrlae algwwrgpaf adfgderwlr tersrltelr lhaverraea rirlgdaaga
      181 vpdldahvae hpwreegwrl lalalyrsar qadalsvlrr argmlrehlg vdpgprlrrl
      241 eedvlrhagh ldpdapsavd lvwsrataay esslaarart rlestaglmr dlavtggggl
      301 esarrhrvaa vaaaeqlgdp eltarvigly dvpavwtrsd dpeqarwlvg aaertlrllp
      361 sgghdatrcr llatvavesr gvlptdgpvs epvngsvsep gegtvdgsvs gaaarpllaa
      421 rraeeiarrl ddasllafal ngtfmqtfrr tglaarrdav gaelvalsar hqlvryevlg
      481 hlvriqarsa vadlagadrh aaaadalaar hdlplvsvft twyralrtam teppatalaa
      541 yeeaarclpg sgmpglhsgl lplallsvrl rhgepvvadh dadwgpyepw vrpvllvgeg
      601 rveeagealr aapapprdlm seamwclvar aavavgdrdv mararaelap aaseqggags
      661 glitlgpvad hlgmlasasa sapvsdsdsd
//
LOCUS       WP_392261614             313 aa            linear   BCT 20-JAN-2025
DEFINITION  quinone oxidoreductase family protein [Streptomyces sp.
            NPDC015184].
ACCESSION   WP_392261614
VERSION     WP_392261614.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015184
  ORGANISM  Streptomyces sp. NPDC015184
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 313)
  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 313)
  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 313)
  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   4  (residues 1 to 313)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Streptomyces sp. NPDC015184"
                     /db_xref="taxon:3364946"
     Protein         1..313
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=32060
     Region          1..313
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 mrrvrhevng gpevlfveea pvpepgpgel lvraeaigvt lpavrkvrgg dgpgplggev
       61 agtvaavgeg vtdfsvgdrv tglcfshaya elalihrtma srvpdrasav eavalvrsgl
      121 valgahaagr prpgesvlvt aaagavgtla lqyarasgas rvvaavgsad kgefvrslga
      181 devviygnge eerggawgdp vdvvldgvgg kllgpavral tpggrlvafs sgggtidaye
      241 llvrgasaig fqmaalarne pgvyahrige lwelhrdral rprvfaeipl veaarahevi
      301 esrrnlgkvv lip
//
LOCUS       WP_392262228             531 aa            linear   BCT 20-JAN-2025
DEFINITION  sodium:solute symporter family protein [Streptomyces sp.
            NPDC015184].
ACCESSION   WP_392262228
VERSION     WP_392262228.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015184
  ORGANISM  Streptomyces sp. NPDC015184
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Henriquez,T., Wirtz,L., Su,D. and Jung,H.
  TITLE     Prokaryotic Solute/Sodium Symporters: Versatile Functions and
            Mechanisms of a Transporter Family
  JOURNAL   Int J Mol Sci 22 (4), 1880 (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Wright,E.M. and Turk,E.
  TITLE     The sodium/glucose cotransport family SLC5
  JOURNAL   Pflugers Arch 447 (5), 510-518 (2004)
   PUBMED   12748858
  REMARK    Erratum:[Pflugers Arch. 2004 Feb;447(5):813-5]
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Jung,H.
  TITLE     The sodium/substrate symporter family: structural and functional
            features
  JOURNAL   FEBS Lett 529 (1), 73-77 (2002)
   PUBMED   12354616
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001756
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Streptomyces sp. NPDC015184"
                     /db_xref="taxon:3364946"
     Protein         1..531
                     /product="sodium:solute symporter family protein"
                     /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=55237
     Region          4..484
                     /region_name="PutP"
                     /note="Na+/proline symporter [Amino acid transport and
                     metabolism]; COG0591"
                     /db_xref="CDD:440356"
ORIGIN      
        1 mnatvatsvf gvfmvvtval gllatrgrrk gkgdgglaew svggrslgtv fiwvlmageg
       61 ytsfsylgaa gwgynygapv lyvvaymscg yavgyvvgpm lwayarrhgl vgitdmvahr
      121 fgrpwlgalv avlatvfllp yiqlqitgmg vvvstisyga iglnqayfia favttgfvvv
      181 sglrgsawvs vlkdvlviat lgflavyvpm hyfdgygpfl drlvaeksew lafpghgdsg
      241 lgqawfitts flnsltvvif pttvagylga knadvlrrna mllpaynvll fvpmllgmaa
      301 lfvvpglvga esnlalfklv vdslpawtvg lvgvaaalss ivpmavfmlv igtmwgrsvl
      361 slvprwerrq kgaaqvvvvv agslalllty tapntlvrls lisyegmaql lpmvllglvw
      421 rrltllgams glvvgvgvvc gfvftendpv wgvnagival ganlavalav tyagprerdd
      481 rpddevlard eigpvvrdae sgdggggggg ggggvrtstg agagmeagag g
//
LOCUS       WP_392262428             402 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC015184].
ACCESSION   WP_392262428
VERSION     WP_392262428.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015184
  ORGANISM  Streptomyces sp. NPDC015184
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 402)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Streptomyces sp. NPDC015184"
                     /db_xref="taxon:3364946"
     Protein         1..402
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=41609
     Region          65..246
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          251..371
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mfaarrpvrr taapgrpvrf altagtavlg ltltacsgaa asdsaasgsa gaargaeisv
       61 nlrgdaaapg kpvkvtlgsg klksvavsad ggdaltgris adgrtwtsdr vaapgtayrv
      121 earnteggsg taafttsaad kvnkltlapg knttvgiaqp lsivfdnpvk draaveralk
      181 vstsngtegs wgwlqdysgk drvdwrpeey wksgtkvtld adlngvdsgp sggwfvrdyr
      241 ttftigdeqv vkvdldrhrl alqrsgktvl dvpmsagtpg gekaswrgta vlmakegtin
      301 mrsetvglgn aydkmvdssm rltwsgmyah aapwnaahfg sanrssgcig msdadagaly
      361 gqvrpgdpfe itgadakgtv aegngygawn vswadwraks al
//
LOCUS       WP_392262569             364 aa            linear   BCT 20-JAN-2025
DEFINITION  heme/hemin ABC transporter substrate-binding protein [Streptomyces
            sp. NPDC015184].
ACCESSION   WP_392262569
VERSION     WP_392262569.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015184
  ORGANISM  Streptomyces sp. NPDC015184
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Naoe,Y., Nakamura,N., Rahman,M.M., Tosha,T., Nagatoishi,S.,
            Tsumoto,K., Shiro,Y. and Sugimoto,H.
  TITLE     Structural basis for binding and transfer of heme in bacterial
            heme-acquisition systems
  JOURNAL   Proteins 85 (12), 2217-2230 (2017)
   PUBMED   28913898
REFERENCE   2  (residues 1 to 364)
  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   3  (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   4  (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   5  (residues 1 to 364)
  AUTHORS   Ho,W.W., Li,H., Eakanunkul,S., Tong,Y., Wilks,A., Guo,M. and
            Poulos,T.L.
  TITLE     Holo- and apo-bound structures of bacterial periplasmic
            heme-binding proteins
  JOURNAL   J Biol Chem 282 (49), 35796-35802 (2007)
   PUBMED   17925389
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Streptomyces sp. NPDC015184"
                     /db_xref="taxon:3364946"
     Protein         1..364
                     /product="heme/hemin 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=37218
     Region          89..361
                     /region_name="ChuT"
                     /note="ABC-type hemin transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG4558"
                     /db_xref="CDD:443619"
ORIGIN      
        1 mrfsqdfapp gqggdrrpgh rpgrargplg alaaalaltl altgcgngsg tdprtgtgaa
       61 rpeqavdrve plattpeprl patvksadgt rvtigsadri vpltgglsei vftlglgdrv
      121 varditatfe qaaelpvvtr ahdvsaesvl slrptvvlae tttgpaeave qirdagiplv
      181 vvapakelsd vdrridavaa algapdagte lknrtrsrie avrksvpapa kgrgkprvaf
      241 lylrgsasvy llggrdsgas slieaagavd agkasglrkd ftaitseala kaapdailvm
      301 rkglesvggv dglvkipgia etpagmdrrl vsiddgvlln ygprtdrvls dliaqlhped
      361 gadg
//
LOCUS       WP_392263241             214 aa            linear   BCT 20-JAN-2025
DEFINITION  nicotinamide mononucleotide transporter family protein
            [Streptomyces sp. NPDC015184].
ACCESSION   WP_392263241
VERSION     WP_392263241.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015184
  ORGANISM  Streptomyces sp. NPDC015184
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Hemberger,S., Pedrolli,D.B., Stolz,J., Vogl,C., Lehmann,M. and
            Mack,M.
  TITLE     RibM from Streptomyces davawensis is a riboflavin/roseoflavin
            transporter and may be useful for the optimization of riboflavin
            production strains
  JOURNAL   BMC Biotechnol 11, 119 (2011)
   PUBMED   22136195
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Zhu,N., Olivera,B.M. and Roth,J.R.
  TITLE     Genetic characterization of the pnuC gene, which encodes a
            component of the nicotinamide mononucleotide transport system in
            Salmonella typhimurium
  JOURNAL   J Bacteriol 171 (8), 4402-4409 (1989)
   PUBMED   2546921
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Streptomyces sp. NPDC015184"
                     /db_xref="taxon:3364946"
     Protein         1..214
                     /product="nicotinamide mononucleotide transporter family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0034257 - nicotinamide riboside
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_process="GO:0034258 - nicotinamide riboside transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23179
     Region          4..205
                     /region_name="PnuC"
                     /note="Nicotinamide riboside transporter PnuC [Coenzyme
                     transport and metabolism]; COG3201"
                     /db_xref="CDD:442434"
ORIGIN      
        1 mtalnwlnse aftvlgqhii wsdmigntvg lialtlgwlr svwtwpaqll sgvvlvaana
       61 svqqagsvgk qvvviavavw gwqqwtrgrq qaqdgsiavr fatwrergyl lggavlgtla
      121 vgglftafps lswspwaday ifagtlvaml aqargmvefw fawllvdlvg vplnfhsgla
      181 fsgliyvvyg alvlwgmrdw wlrsrtpale gata
//
LOCUS       WP_392263617             387 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC015184].
ACCESSION   WP_392263617
VERSION     WP_392263617.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015184
  ORGANISM  Streptomyces sp. NPDC015184
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 387)
  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   5  (residues 1 to 387)
  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   6  (residues 1 to 387)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 387)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 387)
  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 20283677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Streptomyces sp. NPDC015184"
                     /db_xref="taxon:3364946"
     Protein         1..387
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40228
     Region          18..66
                     /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"
     Region          82..369
                     /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 mnasrpvggd laqlrrlnaf galralrsag apvtltelat ltglsrasae dlateltdqg
       61 waaevppapg tvgrparryr fraesghvfg ldigahsvla vladlcgtvv ttarrtvppd
      121 irradrlavi gevmtecldd agidahqiwt isagttgvvg pegevvlaga aadwtgvrla
      181 ehldercagt vlvdndtrla alaeqrlgaa rdiedavyih aglglsaali iggrvhrgyg
      241 gaageigsfp vtpwataatr laccpavpsd vpprnaaahv laaarrgdtv avravdryas
      301 dvalglaamv ltvdpqrvvl ggglaqsadv llprlrnrle plcirvpdlq psslgddrva
      361 lgaiwraveh iettylahnr rptaahp
//
LOCUS       WP_392264206             289 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptomyces sp.
            NPDC015184].
ACCESSION   WP_392264206
VERSION     WP_392264206.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015184
  ORGANISM  Streptomyces sp. NPDC015184
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 289)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 289)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces sp. NPDC015184"
                     /db_xref="taxon:3364946"
     Protein         1..289
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31548
     Region          19..102
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          126..287
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 misalnqlvd mveeqlteel dvralaallg tteyhlrrmf sslagmplse yvrrrrmtva
       61 aadivrgded llsiavrhgy gsseafgraf ravhgagpgd vrrdggplrs qpqlrfrltv
      121 egsnpmdtri vgrpafrlvg haarvplihv gvnphmqehi aslpqeehar lkglsatepa
      181 gllqvcddtd pdsregtelt ylhgvaqgrd tpapddldvi evpggmwavf rtsgphpdal
      241 qttwaatate wfpsnpwrlr pgpsivavle raedfstatc elwlpveae
//
LOCUS       WP_392264798             422 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC015220].
ACCESSION   WP_392264798
VERSION     WP_392264798.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015220
  ORGANISM  Streptomyces sp. NPDC015220
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces sp. NPDC015220"
                     /db_xref="taxon:3364947"
     Protein         1..422
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=44814
     Region          57..243
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          251..370
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 msttprtrtr tvvscallvs algagatacg pggnplaatp ydaadeisfs gptdagkkad
       61 pdkplvvtae ssdgritdvt atdstgrhvs gelaadgsrw hstsalaagt hytvtvsted
      121 ddgapgrkvl tfdtskptaq khlnvkfgpd agtygvgqpi taeldqpvkd kaqrtvverg
      181 lrvestpavq gswywvddkh lhyrpkgywp ahatvavrsd lenirigdrl wggaakpltl
      241 ttgdrvvavt daaahrltvy rndekvkeip ittgkpgfet rngvkvilak qylvrmksst
      301 igiaagssds ydlsvyyaar vtwsgefvha apwsvgsqgm anvshgctgm stpnakwffd
      361 fvhegdivqv vnsngrpmet fdngfgdwnl awqkwqqgsa lhggaqgagt rtdtavlrpm
      421 sl
//
LOCUS       WP_392265761             290 aa            linear   BCT 20-JAN-2025
DEFINITION  S1 family peptidase [Streptomyces sp. NPDC015220].
ACCESSION   WP_392265761
VERSION     WP_392265761.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015220
  ORGANISM  Streptomyces sp. NPDC015220
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Querino Lima Afonso,M., da Fonseca,N.J. Jr., de Oliveira,L.C.,
            Lobo,F.P. and Bleicher,L.
  TITLE     Coevolved Positions Represent Key Functional Properties in the
            Trypsin-Like Serine Proteases Protein Family
  JOURNAL   J Chem Inf Model 60 (2), 1060-1068 (2020)
   PUBMED   31895561
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Waldner,B.J., Kraml,J., Kahler,U., Spinn,A., Schauperl,M.,
            Podewitz,M., Fuchs,J.E., Cruciani,G. and Liedl,K.R.
  TITLE     Electrostatic recognition in substrate binding to serine proteases
  JOURNAL   J Mol Recognit 31 (10), e2727 (2018)
   PUBMED   29785722
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Pelc,L.A., Chen,Z., Gohara,D.W., Vogt,A.D., Pozzi,N. and Di Cera,E.
  TITLE     Why Ser and not Thr brokers catalysis in the trypsin fold
  JOURNAL   Biochemistry 54 (7), 1457-1464 (2015)
   PUBMED   25664608
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Perona,J.J. and Craik,C.S.
  TITLE     Evolutionary divergence of substrate specificity within the
            chymotrypsin-like serine protease fold
  JOURNAL   J Biol Chem 272 (48), 29987-29990 (1997)
   PUBMED   9374470
REFERENCE   5  (residues 1 to 290)
  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 10595581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces sp. NPDC015220"
                     /db_xref="taxon:3364947"
     Protein         1..290
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=29823
     Region          77..228
                     /region_name="Trypsin_2"
                     /note="Trypsin-like peptidase domain; pfam13365"
                     /db_xref="CDD:433149"
ORIGIN      
        1 mnkpllaala tlvitgagma paaaatqtgg aapapatktt gaapalqavd fagtvalsnc
       61 sgsvvrlpas adsdpalvls nghcletgfp spgqvivnqa ssrtfgllns agtrvatlra
      121 skvvystmtd tdvtlyqlts tyaqikssyg igaltlsdth pvagtaikvv sgywkriysc
      181 nidgfvyrlk egdwtwkdsv rytsacntig gtsgspvvdn atgkvvavnn tgnedgqrct
      241 ennpcevdan gnvtvrqgin yaeetyqipa cfttgnrldl srsgcvlpkp
//
LOCUS       WP_392265838             294 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Streptomyces sp. NPDC015220].
ACCESSION   WP_392265838
VERSION     WP_392265838.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015220
  ORGANISM  Streptomyces sp. NPDC015220
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 294)
  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 12830887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Streptomyces sp. NPDC015220"
                     /db_xref="taxon:3364947"
     Protein         1..294
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=31226
     Region          83..151
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          182..293
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mrtrgtrgvg aavaallllt amcgcrvqea gagaggapga gtdgrhrspa gtqvpssrsp
       61 ggrspadgrp gtapgpargr taaparvlws rgdtgrdvre lqarlrqiaw lsgaptgtyg
      121 elteravrgf qarrglpatg rtdtvtwqrl lgmthepgtw elypmggqpa gapdarcltg
      181 rvlcidkttr tlrwmiggrt istmavrfgt qytptregvf hiywksrhhv stlyhspmpy
      241 amffsggqav hyssdfaarg yaggshgcvn vrdesaiaqv faqvrtgdkv vvhw
//
LOCUS       WP_392266174             343 aa            linear   BCT 20-JAN-2025
DEFINITION  BMP family lipoprotein [Streptomyces sp. NPDC015220].
ACCESSION   WP_392266174
VERSION     WP_392266174.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015220
  ORGANISM  Streptomyces sp. NPDC015220
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Yousief,S.W., Bahey-El-Din,M. and Zaghloul,T.I.
  TITLE     Immunization with the basic membrane protein (BMP) family ABC
            transporter elicits protection against Enterococcus faecium in a
            murine infection model
  JOURNAL   Microbes Infect 22 (3), 127-136 (2020)
   PUBMED   31585177
REFERENCE   2  (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   3  (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   4  (residues 1 to 343)
  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   5  (residues 1 to 343)
  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 11448319
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Streptomyces sp. NPDC015220"
                     /db_xref="taxon:3364947"
     Protein         1..343
                     /product="BMP family lipoprotein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /calculated_mol_wt=35197
     Region          36..341
                     /region_name="Med"
                     /note="Lipoprotein Med, regulator of KinD/Spo0A, PBP1-ABC
                     superfamily, includes NupN [Signal transduction
                     mechanisms]; COG1744"
                     /db_xref="CDD:441350"
ORIGIN      
        1 mavavvalaa agcgksstds gggsssesgk ysgkgiglay dvggkgdqsf ndaafsglek
       61 aqkdfslggr diepqdgesn adkvqrleql akagynpvig vgfvyapavk evaakypktt
      121 fgiidddtvk agnvvdlvfh eeqasylagv aaakatkknh igfvggvdip lihkfeagfd
      181 qgarsvnpki kiesqyltqt aqeggfsspd kgkdaangqi ekgadviyha aglsgqgviq
      241 saaahkvwai gvdsdqyqqs alagykdwil gsalknvgga vydltksvvd gkpltgevrg
      301 dlksggvgfa dsnpkyqamk dvvaavdkak qditdgkvtv atk
//
LOCUS       WP_392267863             419 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC015220].
ACCESSION   WP_392267863
VERSION     WP_392267863.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015220
  ORGANISM  Streptomyces sp. NPDC015220
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 419)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Streptomyces sp. NPDC015220"
                     /db_xref="taxon:3364947"
     Protein         1..419
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43716
     Region          80..261
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          267..393
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mnvrpisgas vdarvrggra gtrgrrglla lvsgalvlav tacggggsds gsgqskgkda
       61 gtteskqsqa vvsiapkdga tsvdtsgalk vaasggtltq vvvkdakgte isgkisggga
      121 swtpsthlaa stkytvhava kdsagrqaae dssfttltpr ntfvgsftpe dgstvgvgmp
      181 fsvnftrgit rpgavekair iktepaveve ghwfgndrld frpehywkag tkvtvkldld
      241 gvegrpgvyg kqsktvsfti grnqvsvvda skhtmkvtqd gkvvrtipvt tgkpgydtwn
      301 grmviseklt vtrmngetvg yggeydikdv phamrlttsg tfihgnywgg gafgnfnash
      361 gcvglrdvrg gydsgvpaaw ffnhsligdv vevqnsqdkt vapdnglngw nmswsewka
//
LOCUS       WP_392268070             286 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015220].
ACCESSION   WP_392268070
VERSION     WP_392268070.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015220
  ORGANISM  Streptomyces sp. NPDC015220
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 286)
  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 286)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces sp. NPDC015220"
                     /db_xref="taxon:3364947"
     Protein         1..286
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31823
     Region          25..78
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          100..281
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mayestdggt gsgraepgts dslrtfgavv qalrehagls reefaalvry skhtvasveq
       61 grrmpdrdfv ergeaalgnt galrraaptl trqaglaswf rqwarleata islytyecrv
      121 vpgllqteay aravsldvpp lpdpeeleqr iaarlarqel lavtrkppta fsfiveqavl
      181 erwtggeevt relfdhllel iernwnvefq vmplrrpsha gldgpvrlae apdnqwfays
      241 egqqngrlia drkeisllqq ryaklrsqam tpedslgllk rlrgal
//
LOCUS       WP_392268057             399 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC015220].
ACCESSION   WP_392268057
VERSION     WP_392268057.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015220
  ORGANISM  Streptomyces sp. NPDC015220
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 399)
  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   5  (residues 1 to 399)
  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   6  (residues 1 to 399)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 399)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Streptomyces sp. NPDC015220"
                     /db_xref="taxon:3364947"
     Protein         1..399
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40541
     Region          14..77
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          77..379
                     /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 metpgsqssl hranlervvr avrlagsltq aeiarttgls aatvsnivre lkdggtvqvt
       61 ptsaggrrar svslsgdagi vigvdfghah lrvaignlah qvlaeesepl dvdaswvqgf
      121 draeelvnrl iaatgvdrak vagvglgvpg pidvesgtlg stailpgwgg ikpaeelrgr
      181 lgvpvhvdnd anlgalgelv wgsgrgvrdl ayikiasgvg aglvingkiy rgpggtagei
      241 ghitldeagp vcrcgnrgcl etftaaryvl pllqpshgtd ltmegvvrla rdgdpgcrrv
      301 iadvgrhvgs gvanlcnlln psrvvlggdl aeagelvlgp iresvgryai psaarqlsil
      361 pgalggraev lgalalalse mgdstlldga lsaaapaft
//
LOCUS       WP_392268428             314 aa            linear   BCT 20-JAN-2025
DEFINITION  aldo/keto reductase [Streptomyces sp. NPDC015220].
ACCESSION   WP_392268428
VERSION     WP_392268428.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015220
  ORGANISM  Streptomyces sp. NPDC015220
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  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 314)
  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   3  (residues 1 to 314)
  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   4  (residues 1 to 314)
  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 10790928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces sp. NPDC015220"
                     /db_xref="taxon:3364947"
     Protein         1..314
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /calculated_mol_wt=33701
     Region          3..314
                     /region_name="YdhF"
                     /note="Predicted oxidoreductase YdhF [General function
                     prediction only]; COG4989"
                     /db_xref="CDD:444013"
ORIGIN      
        1 mtahtdirth pllygcmglg ggwdtapwta edvrhaeaai eaalaagisa fdhadiyrhg
       61 kseavfgevl arapglrqri vlqskcgirl pdgdrpghyd lraasivrrv eesltrlrtd
      121 vldvlllhrp dpltgpeeia gavaslhsqg lvrqfgvsnm sgaqlsalqa hldvplvvdq
      181 lemslarrdw veagvlfntp aaagvgcppg tvehchangv rlqawgalar grfadgadtp
      241 vnrlvadlar rhgttpetvl lwwlrkhpag iapvvgttrp eriracadav arepglshee
      301 wyelwvaarg aplp
//
LOCUS       WP_392268785             290 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Streptomyces sp.
            NPDC015220].
ACCESSION   WP_392268785
VERSION     WP_392268785.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015220
  ORGANISM  Streptomyces sp. NPDC015220
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 290)
  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 290)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces sp. NPDC015220"
                     /db_xref="taxon:3364947"
     Protein         1..290
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29378
     Region          23..283
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mplaatselv ggaaaarsav vafniitleh ieavvagaee agasvvlqis enavrfrygr
       61 llplaraava aaeraavpva lhldhvqsdd llrqapeagf ssvmydasrl pyaenlaatr
      121 aaaewahaqg lwleaelgev ggkdgrppld ahapgartdp geahafvsgs gvdalavavg
      181 nahamterta aldhdllkgl agavdvplvl hgssglpege laaavtggia kvnvgtalni
      241 amtravrgyl aghpeavdsr kylgvgream aaevtrligv vgtprttpts
//
LOCUS       WP_392269003             424 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC015220].
ACCESSION   WP_392269003
VERSION     WP_392269003.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015220
  ORGANISM  Streptomyces sp. NPDC015220
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 424)
  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 424)
  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
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 424)
  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   5  (residues 1 to 424)
  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   6  (residues 1 to 424)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 424)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 424)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Streptomyces sp. NPDC015220"
                     /db_xref="taxon:3364947"
     Protein         1..424
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44114
     Site            order(15..17,31..33,42..45,47..48,51..52,60..61,67..69,
                     74..76)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Region          20..>86
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          80..400
                     /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 mvdrsgrtvr dlrrksragv lqqlyfdgpm srhslipatg lssgavsnvv aeliadglve
       61 eagsvdsrrg rprvlvriap gsghligvdv getgvrvelf dlsleqlars eipltrrsgr
      121 sydvdavvra iadgvaevlr tsavdagsll gvgigvpgiv dsgveggavv hgqtigweav
      181 plerllrrtg rlpahvpyvi angamtlgqa emwfgagrga rsavvvlfgs gvgacvvtdg
      241 vergravewg hltvevrgrr crcgasgcle ayagaealld rwreaggrss agadqekaft
      301 elltaaypqh ggradpvaaa vlaetaeylg aglsdlinlf qperilvggw aglllgprfl
      361 rsvrthalah alrhpaarvd iglgrlgada vtlgaaalpl tdffahggrl prpaperahs
      421 gepg
//
LOCUS       WP_392269195             254 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Streptomyces sp.
            NPDC015220].
ACCESSION   WP_392269195
VERSION     WP_392269195.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015220
  ORGANISM  Streptomyces sp. NPDC015220
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  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 254)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces sp. NPDC015220"
                     /db_xref="taxon:3364947"
     Protein         1..254
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26516
     Region          3..231
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 miriaavgdi hmapetrgtl rpafetlpdc advlllagdl trhgtpeear vvaeeirdlg
       61 vpvvavlgnh dhhadrpeev tavledagaq vlegsgvvvp cdgarvgvag tkgfgggfvg
      121 rcagefgepl mkefvrytrr cadnlrtsle qlgeqgcdvr ialthyspvp etlageplei
      181 ypflgsylla eavdtagadl avhghahagt engmtsggvr vrnvaqpvig rafhvyhvha
      241 rrpvpagapg ghpg
//
LOCUS       WP_392269298             428 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC015220].
ACCESSION   WP_392269298
VERSION     WP_392269298.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015220
  ORGANISM  Streptomyces sp. NPDC015220
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 428)
  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 428)
  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
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 428)
  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   5  (residues 1 to 428)
  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   6  (residues 1 to 428)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 428)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 428)
  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 20170230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Streptomyces sp. NPDC015220"
                     /db_xref="taxon:3364947"
     Protein         1..428
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45408
     Region          <20..>60
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          80..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 magrngrtvr dlrranrtav lqrlyfdgpl srfelgpatg lssgsisnvv adlvadglve
       61 eagsvdsdgg rprtllrvap gsghmigvdv getrvrvelf dlaltelara erpltpqryd
      121 vdvitghird giaevlaaag paperllgvg igvpgiieht pdrgavvhgq tigwdavple
      181 allrtgsqlp dsvpyfieng aktlgqaemw fgagrgagna vvvlfgsgvg aclvtpever
      241 gravewghlt vrvrgrrcrc galgcleaya gaesllarwr eeggrpprdt deetaltaml
      301 aaayppegtd adpvalavle etaeylgagl sdlinlfqpe riliggwagl qlgsrflpsv
      361 rrhatayalr hpaqrvtidl grlgpdavtv gaailpladf ftrggrraes drqdrlpawq
      421 taleerra
//
LOCUS       WP_392269309             215 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces sp. NPDC015220].
ACCESSION   WP_392269309
VERSION     WP_392269309.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015220
  ORGANISM  Streptomyces sp. NPDC015220
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Streptomyces sp. NPDC015220"
                     /db_xref="taxon:3364947"
     Protein         1..215
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22992
     Region          2..212
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 mssrdrilgr vrraladvpa ddppyeravp rdylrqhggr saeetvella enlvdyravv
       61 hrgdlralpa liahllgerg stsvlvppgl dagwlaatsv eriedrprst pleldrvdsv
      121 vtgcavaiae tgtivldgsp dqgsrritli pdhhicvvrv pgqvvssvpq alarltpqrp
      181 ltwisgpsat sdieldrveg vhgprtlevv lvsgg
//
LOCUS       WP_392269448             707 aa            linear   BCT 20-JAN-2025
DEFINITION  DNA gyrase/topoisomerase IV subunit B [Streptomyces sp.
            NPDC015220].
ACCESSION   WP_392269448
VERSION     WP_392269448.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015220
  ORGANISM  Streptomyces sp. NPDC015220
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Tari,L.W., Trzoss,M., Bensen,D.C., Li,X., Chen,Z., Lam,T.,
            Zhang,J., Creighton,C.J., Cunningham,M.L., Kwan,B., Stidham,M.,
            Shaw,K.J., Lightstone,F.C., Wong,S.E., Nguyen,T.B., Nix,J. and
            Finn,J.
  TITLE     Pyrrolopyrimidine inhibitors of DNA gyrase B (GyrB) and
            topoisomerase IV (ParE). Part I: Structure guided discovery and
            optimization of dual targeting agents with potent, broad-spectrum
            enzymatic activity
  JOURNAL   Bioorg Med Chem Lett 23 (5), 1529-1536 (2013)
   PUBMED   23352267
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Gadelle,D., Filee,J., Buhler,C. and Forterre,P.
  TITLE     Phylogenomics of type II DNA topoisomerases
  JOURNAL   Bioessays 25 (3), 232-242 (2003)
   PUBMED   12596227
REFERENCE   3  (residues 1 to 707)
  AUTHORS   Wang,J.C.
  TITLE     Cellular roles of DNA topoisomerases: a molecular perspective
  JOURNAL   Nat Rev Mol Cell Biol 3 (6), 430-440 (2002)
   PUBMED   12042765
REFERENCE   4  (residues 1 to 707)
  AUTHORS   Champoux,J.J.
  TITLE     DNA topoisomerases: structure, function, and mechanism
  JOURNAL   Annu Rev Biochem 70, 369-413 (2001)
   PUBMED   11395412
REFERENCE   5  (residues 1 to 707)
  AUTHORS   Roca,J.
  TITLE     The mechanisms of DNA topoisomerases
  JOURNAL   Trends Biochem Sci 20 (4), 156-160 (1995)
   PUBMED   7770916
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Streptomyces sp. NPDC015220"
                     /db_xref="taxon:3364947"
     Protein         1..707
                     /product="DNA gyrase/topoisomerase IV subunit B"
                     /EC_number="5.6.2.2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003918 - DNA topoisomerase type II
                     (double strand cut, ATP-hydrolyzing) activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006265 - DNA topological change [Evidence
                     IEA]"
                     /calculated_mol_wt=77220
     Region          21..701
                     /region_name="GyrB"
                     /note="DNA gyrase/topoisomerase IV, subunit B
                     [Replication, recombination and repair]; COG0187"
                     /db_xref="CDD:439957"
ORIGIN      
        1 mtadtsvpst allagadrdg snytarhllv legleavrkr pgmyigstds rglmhclwei
       61 idnsvdealg gycdhievil hddgsvevqd ngrgipvdve pktglsgvev vmtklhaggk
      121 fgggsyaasg glhgvgasvv nalsarldve vdrvghthav sfrrgvpgaf tgdgpeakfe
      181 aksglrkark ipktrsgtrv rywadrqifl kdaklsletl hqrarqtafl vpgltilvrd
      241 eyglgeggsk geesfrfdgg isefceylat drpvcdvlrf ngqgsfketv pvldehgqmt
      301 ptevtrelgv dvalrwgtgy dttlrsfvni iatpkggthv agfeqavtqt lnevlrakkl
      361 lrvaednivk ddalegltav vtvrlaepqf egqtkevlgt saarrivnnv vtkelkaflt
      421 stkrdaaqqa rvimekavaa artriaarqh kdaqrrktal essslpakla dcrsddvdrs
      481 elfivegdsa lgtaklarns efqallpirg kilnvqkssv tdmlknaecg aiiqvigags
      541 grtfdldaar ygkiimmtda dvdgshirtl lltlfhrymr pmveagrvfa avpplhrvel
      601 iqpkkgqdky vytysdrelr drllefqtkn irykdsiqry kglgemdadq laettmdprh
      661 rtlrrinlsd leaaegvfdl lmgndvaprk efiassaatl drsrida
//
LOCUS       WP_392269547             237 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Streptomyces sp.
            NPDC015220].
ACCESSION   WP_392269547
VERSION     WP_392269547.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015220
  ORGANISM  Streptomyces sp. NPDC015220
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 237)
  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 11440233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Streptomyces sp. NPDC015220"
                     /db_xref="taxon:3364947"
     Protein         1..237
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25713
     Region          3..230
                     /region_name="GCD1"
                     /note="NDP-sugar pyrophosphorylase, includes eIF-2Bgamma,
                     eIF-2Bepsilon, and LPS biosynthesis protein s
                     [Translation, ribosomal structure and biogenesis, Cell
                     wall/membrane/envelope biogenesis]; COG1208"
                     /db_xref="CDD:440821"
ORIGIN      
        1 mhavilaggk gvrlrpytta lpkplvpigd qhaileivlr qlsaagftsc tiaighlgqi
       61 irayvgngsq wgmsvdyste esplgtmgpl ltmrdrlpet flvmngdvlt dldyadvlrr
      121 hrssgaplti atyarqvhid fgvlttdask vvaftekpsm dyrvsmgvyg lsratldgyt
      181 pglplgfdel vldllgdgrp phayefdgyw ldigrpddyd ranaefttrk slllkga
//
LOCUS       WP_392270514             130 aa            linear   BCT 20-JAN-2025
DEFINITION  TOBE domain-containing protein [Streptomyces sp. NPDC015220].
ACCESSION   WP_392270514
VERSION     WP_392270514.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015220
  ORGANISM  Streptomyces sp. NPDC015220
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 130)
  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 10007583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Streptomyces sp. NPDC015220"
                     /db_xref="taxon:3364947"
     Protein         1..130
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13714
     Region          1..127
                     /region_name="MopI"
                     /note="Molybdopterin-binding protein MopI [Coenzyme
                     transport and metabolism]; COG3585"
                     /db_xref="CDD:442804"
ORIGIN      
        1 mqsytigqaa rllgvspdta rrwadagrvs thrdesgrrl idgrdlaafs velagsggee
       61 dpsytsvrna fsgivtavkl gdvaaqveiq agphrlvsll treaveelgl evgmeatarv
      121 kstnvhidra
//
LOCUS       WP_392270888             214 aa            linear   BCT 20-JAN-2025
DEFINITION  nicotinamide mononucleotide transporter family protein
            [Streptomyces sp. NPDC015220].
ACCESSION   WP_392270888
VERSION     WP_392270888.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015220
  ORGANISM  Streptomyces sp. NPDC015220
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Hemberger,S., Pedrolli,D.B., Stolz,J., Vogl,C., Lehmann,M. and
            Mack,M.
  TITLE     RibM from Streptomyces davawensis is a riboflavin/roseoflavin
            transporter and may be useful for the optimization of riboflavin
            production strains
  JOURNAL   BMC Biotechnol 11, 119 (2011)
   PUBMED   22136195
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Zhu,N., Olivera,B.M. and Roth,J.R.
  TITLE     Genetic characterization of the pnuC gene, which encodes a
            component of the nicotinamide mononucleotide transport system in
            Salmonella typhimurium
  JOURNAL   J Bacteriol 171 (8), 4402-4409 (1989)
   PUBMED   2546921
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Streptomyces sp. NPDC015220"
                     /db_xref="taxon:3364947"
     Protein         1..214
                     /product="nicotinamide mononucleotide transporter family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0034257 - nicotinamide riboside
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_process="GO:0034258 - nicotinamide riboside transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23706
     Region          1..203
                     /region_name="PnuC"
                     /note="Nicotinamide riboside transporter PnuC [Coenzyme
                     transport and metabolism]; COG3201"
                     /db_xref="CDD:442434"
ORIGIN      
        1 mnwlnseaft lfgqhikwsd mignviglig lafgwrrsiw swptqfvsgl ilfaafatah
       61 lsgsagkqiv vmvvavygww qwnrgrgrda dghiavrfat wreravllgg aavgtvavaa
      121 lfkaypslsw dpwpdayifv gtvvamyaqa rgmvefwfaw llvdavgvpl nfangfafsg
      181 fvyvvygalv lwgmrdwwqr srrsprpvpe gapa
//
LOCUS       WP_392271618             371 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            sp. NPDC015220].
ACCESSION   WP_392271618
VERSION     WP_392271618.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015220
  ORGANISM  Streptomyces sp. NPDC015220
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (residues 1 to 371)
  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   4  (residues 1 to 371)
  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 371)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Streptomyces sp. NPDC015220"
                     /db_xref="taxon:3364947"
     Protein         1..371
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40540
     Region          3..338
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 masrleaehl ykvfgrrpdd gverlrrgad reelradgtt aavidasftv dpgqifvvmg
       61 lsgsgkstll rmlngllept agqvrfdgqd ltalsdrelr evrsrkismv fqhfalfphr
      121 svrenaaygl evqgvpraer ghradealal cglagwedsw pdelsggmqq rvglaralat
      181 dadlllmdes fsaldplirr dmqdqllqlq rtlkktivfi thdlneamrl gdriavmrdg
      241 rivqtgtaed illrpaddyv asftrdvdrs rvltaeavmd rdvrgdeadc gcetatpdtp
      301 ftelcaisar lshpvavlda hralvgvvpr qrlvsflgde taeesgpaep aapvtcdgpr
      361 rkdggkvvar a
//
LOCUS       WP_392271734             290 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptomyces sp.
            NPDC015220].
ACCESSION   WP_392271734
VERSION     WP_392271734.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015220
  ORGANISM  Streptomyces sp. NPDC015220
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 290)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 290)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces sp. NPDC015220"
                     /db_xref="taxon:3364947"
     Protein         1..290
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32233
     Region          20..102
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          126..285
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mldrlnqame hieghldqhi evaelaritv tseyhfrrlf sslagmplse yirrrrltva
       61 gaevlagkpa lleiairygy tsreafaraf ravhgvgpge arrtgaalns qprlsfrltv
      121 egnstmryri vekeafrvvg kkarvplihq gvnphiaehv rsippetmlr iaglsdqepd
      181 gvvsatvrls dgfeegseld yyhavvttaa espedldvld cpagtwavfe ntgpfpqalq
      241 rmwgdvaaqw ipsnpyeyrp gpeilrarps qddptrseaq lwipvtrttv
//
LOCUS       WP_392272424             241 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces sp.
            NPDC016309].
ACCESSION   WP_392272424
VERSION     WP_392272424.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016309
  ORGANISM  Streptomyces sp. NPDC016309
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616714
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Streptomyces sp. NPDC016309"
                     /db_xref="taxon:3364965"
     Protein         1..241
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24663
     Region          8..238
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 mtdaaaafra lhhdrapgdp lvlpgpwdaa sarafeeagf palatpsagv aaslgyadga
       61 tpagemfaav ariarsvsvp vsadveagyg lapgelvarv ldagavgvnl edsragvlvd
      121 preqaellae vraeaggrlf vnarvdtfvr glddpedaia rarlytaaga dcvypigvpp
      181 ahlpllrari egplnvapfp ggpavaelgr lgvtritfgp wllhramaav rdiagqlrrs
      241 s
//
LOCUS       WP_392272434             366 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            sp. NPDC016309].
ACCESSION   WP_392272434
VERSION     WP_392272434.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016309
  ORGANISM  Streptomyces sp. NPDC016309
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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   4  (residues 1 to 366)
  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 366)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Streptomyces sp. NPDC016309"
                     /db_xref="taxon:3364965"
     Protein         1..366
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38818
     Region          23..357
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 msapvstpap tpadtspgts aptpvfsvdg lwkvfgpkag rvpgsdlael paaelrertg
       61 ctaavrdvsf hvrkgevfvv mglsgsgkst lvrcltrlie ptsgtvaidg edilamdtsr
      121 lrelrrhraa mvfqhfgllp hrsvldnvay gleiqgmgra erraraaevv tkvglagmee
      181 rrpgqlsggq qqrvglaral avdpevllfd epfsaldpli rrdmqeevir lhreegrtmi
      241 fithdlneal rlgdrialmr dgrivqlgtp eeivgspadd yvrdfvrdvp reqvltvrta
      301 mrppcagead sgpavapgat vseaieavar sggpvrvvds grcvgvvdha gllsvvagvp
      361 agkaaa
//
LOCUS       WP_392273287             413 aa            linear   BCT 20-JAN-2025
DEFINITION  M20 metallopeptidase family protein [Streptomyces sp. NPDC016309].
ACCESSION   WP_392273287
VERSION     WP_392273287.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016309
  ORGANISM  Streptomyces sp. NPDC016309
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Lindner,H.A., Lunin,V.V., Alary,A., Hecker,R., Cygler,M. and
            Menard,R.
  TITLE     Essential roles of zinc ligation and enzyme dimerization for
            catalysis in the aminoacylase-1/M20 family
  JOURNAL   J Biol Chem 278 (45), 44496-44504 (2003)
   PUBMED   12933810
REFERENCE   2  (residues 1 to 413)
  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 11444961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Streptomyces sp. NPDC016309"
                     /db_xref="taxon:3364965"
     Protein         1..413
                     /product="M20 metallopeptidase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44010
     Region          34..392
                     /region_name="AbgB"
                     /note="Metal-dependent
                     amidase/aminoacylase/carboxypeptidase [General function
                     prediction only]; COG1473"
                     /db_xref="CDD:441082"
ORIGIN      
        1 mvwggmgkav aggwrgpvkq aavaaeaarl drvliqlrrd ihrhpetpgq eqrtaavvar
       61 elraaglavt tgvgghgvvg vlqgsrpgrt vayradmdav ppkdivgggp apahlcghdi
      121 httvsigvar vlarlrqqlr gtvvflfqpa eetlsgaral idsgvlerey veevhalhcg
      181 pfpvgqfavt pgygmpgqdk aevtlsgpda ldaarrlavd igalatvdlp etpadleriv
      241 aeaqtpngpl arfvavraaa qeakvsvsyr cwpqeryvev resirrvamp yagagvsfpa
      301 epfpamvcse rdarllahhl rrtvgqdmvt qlcaafppfs gedfalflnr ipgtytflgv
      361 rapgtsitts yphypdfspd eraigvgvra magwiaerty raqnlsveva emg
//
LOCUS       WP_392274960             241 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Streptomyces sp.
            NPDC016309].
ACCESSION   WP_392274960
VERSION     WP_392274960.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016309
  ORGANISM  Streptomyces sp. NPDC016309
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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 11440233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Streptomyces sp. NPDC016309"
                     /db_xref="taxon:3364965"
     Protein         1..241
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=26074
     Region          7..239
                     /region_name="GCD1"
                     /note="NDP-sugar pyrophosphorylase, includes eIF-2Bgamma,
                     eIF-2Bepsilon, and LPS biosynthesis protein s
                     [Translation, ribosomal structure and biogenesis, Cell
                     wall/membrane/envelope biogenesis]; COG1208"
                     /db_xref="CDD:440821"
ORIGIN      
        1 mhtsptqavv laggqgsrlr pytddrpkpm veipgtgtpi ighqlswlaa egvtdavisc
       61 ghlaevleqw lattelplrv ttvveseplg rggglkyaaa hlphpdepwy atngdiwtrf
      121 slremaafha erdatatlal arpripwgav etdtfghitd fiesppspyl inagvyvfsp
      181 dftgalpdrg dherttfprl arerrlagfp lphgaywrai dtakdlreaa kelaaatgpt
      241 p
//
LOCUS       WP_392276746             312 aa            linear   BCT 20-JAN-2025
DEFINITION  quinone oxidoreductase family protein [Streptomyces sp.
            NPDC016309].
ACCESSION   WP_392276746
VERSION     WP_392276746.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016309
  ORGANISM  Streptomyces sp. NPDC016309
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 312)
  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 312)
  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 312)
  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   4  (residues 1 to 312)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Streptomyces sp. NPDC016309"
                     /db_xref="taxon:3364965"
     Protein         1..312
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=32309
     Region          1..312
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 mrrvrfyeyg gpevlrveda eapkpgpgel lvrteaigvt lpsvrkvrgd ggrtplpgvl
       61 ggeiagtvia lgpevtdfqv gdritsltfs ggsyselava pgfmasripd gasavqaval
      121 vrsghvafaa latarplvse svlitgaasg vghlavqlak lqgiervvaa vsshtkaefl
      181 rglgadeivt ydsehwgepv dvvldgvggd llpravsala pggrlvffns gggtvpafdl
      241 lagsktitgl smarfagthr elydqhgeel wkltlsgqlq pvvharipla dvaraheiie
      301 aranlgkvvl lp
//
LOCUS       WP_392277875             319 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Streptomyces sp. NPDC015144].
ACCESSION   WP_392277875
VERSION     WP_392277875.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015144
  ORGANISM  Streptomyces sp. NPDC015144
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Streptomyces sp. NPDC015144"
                     /db_xref="taxon:3364944"
     Protein         1..319
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=33056
     Region          11..317
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mtlepptlep ltrparlrpg arvavvspsg pvpadrmeag ldilrgwgle vveapharav
       61 hprldylagt dearaadlqa awcdpsvdav icarggygah rmadlvdwaa mraagpkvfv
      121 gysdvtvlhe afarhlgivt lhgpmagtet flkdpdtqes lrttlfvpes vrtlglpaar
      181 alvpgrargi vyggcvslla adlgtpsart sarggllaie dtgedpysld riltqllrag
      241 alngiagvvc gswsgcgpye rvravladrl gplgvpvvee lgfghgptsl tvplgvsavl
      301 dapadggpat ltveepalr
//
LOCUS       WP_392278437             283 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Streptomyces sp.
            NPDC015144].
ACCESSION   WP_392278437
VERSION     WP_392278437.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015144
  ORGANISM  Streptomyces sp. NPDC015144
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 283)
  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 283)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Streptomyces sp. NPDC015144"
                     /db_xref="taxon:3364944"
     Protein         1..283
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=28918
     Region          2..283
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mplvstgelv saaqargrgi aafnvitleh aeaiaagaer agapailqis enavkfhggr
       61 lsgiaaaaaa vartssapla lhldhvesve llhqahtegf gsvmfdasrl pyeenvrata
      121 eavawgherg iwieaelgkv ggkegeapld ahapgvrtdp deaaayvrat gvdalavavg
      181 sshamterta aldheligrl raavpvplvl hgssgvpdae irravtssgm vkinvgtaln
      241 taftgavray laehtsgvdp rkylapgrea mtgtvagfla lmg
//
LOCUS       WP_392278704             359 aa            linear   BCT 20-JAN-2025
DEFINITION  heme/hemin ABC transporter substrate-binding protein [Streptomyces
            sp. NPDC015144].
ACCESSION   WP_392278704
VERSION     WP_392278704.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015144
  ORGANISM  Streptomyces sp. NPDC015144
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Naoe,Y., Nakamura,N., Rahman,M.M., Tosha,T., Nagatoishi,S.,
            Tsumoto,K., Shiro,Y. and Sugimoto,H.
  TITLE     Structural basis for binding and transfer of heme in bacterial
            heme-acquisition systems
  JOURNAL   Proteins 85 (12), 2217-2230 (2017)
   PUBMED   28913898
REFERENCE   2  (residues 1 to 359)
  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   3  (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   4  (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   5  (residues 1 to 359)
  AUTHORS   Ho,W.W., Li,H., Eakanunkul,S., Tong,Y., Wilks,A., Guo,M. and
            Poulos,T.L.
  TITLE     Holo- and apo-bound structures of bacterial periplasmic
            heme-binding proteins
  JOURNAL   J Biol Chem 282 (49), 35796-35802 (2007)
   PUBMED   17925389
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Streptomyces sp. NPDC015144"
                     /db_xref="taxon:3364944"
     Protein         1..359
                     /product="heme/hemin 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=36126
     Region          84..356
                     /region_name="ChuT"
                     /note="ABC-type hemin transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG4558"
                     /db_xref="CDD:443619"
ORIGIN      
        1 mrfspdfapp grrtprtpar grlgapaagl alalaltgca gattggtdga apaatgaaat
       61 adrveplaat prpklpatvr sadgarttvt sadrivplsg glseivftlg lgpkvvardi
      121 tatfeqaakl pvvtrahdvs aesvlslrpt vvlaetttgp aeaveqirea giplvvvkpa
      181 eqlsdvgrri eavaaalgvp dagaeldart asridavrts vpapadgrkk prvaflylrg
      241 sasvhllggr esgassliea aggidagkas gltkdftait sealakaapd vflvmrkgle
      301 svggvdgllk lpgiaetpag ldrrivavdd gvllnygprt drvlaelvak lhpesgaeg
//
LOCUS       WP_392279438             499 aa            linear   BCT 20-JAN-2025
DEFINITION  sodium:solute symporter family protein [Streptomyces sp.
            NPDC015144].
ACCESSION   WP_392279438
VERSION     WP_392279438.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015144
  ORGANISM  Streptomyces sp. NPDC015144
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Henriquez,T., Wirtz,L., Su,D. and Jung,H.
  TITLE     Prokaryotic Solute/Sodium Symporters: Versatile Functions and
            Mechanisms of a Transporter Family
  JOURNAL   Int J Mol Sci 22 (4), 1880 (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Wright,E.M. and Turk,E.
  TITLE     The sodium/glucose cotransport family SLC5
  JOURNAL   Pflugers Arch 447 (5), 510-518 (2004)
   PUBMED   12748858
  REMARK    Erratum:[Pflugers Arch. 2004 Feb;447(5):813-5]
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Jung,H.
  TITLE     The sodium/substrate symporter family: structural and functional
            features
  JOURNAL   FEBS Lett 529 (1), 73-77 (2002)
   PUBMED   12354616
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001756
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Streptomyces sp. NPDC015144"
                     /db_xref="taxon:3364944"
     Protein         1..499
                     /product="sodium:solute symporter family protein"
                     /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=52893
     Region          4..447
                     /region_name="PutP"
                     /note="Na+/proline symporter [Amino acid transport and
                     metabolism]; COG0591"
                     /db_xref="CDD:440356"
ORIGIN      
        1 mnatvatsvf gafmvvtval gllaargrrk ggeggglaew svggrslgtv fiwvlmageg
       61 ytsfsylgaa gwgynygtpv lyvvaymscg yavgyvvgpm lwayarehgl vgitdmvahr
      121 fgrpwlgafl avlvtvfllp yiqlqitgmg vvvstisygs islnwayfia favttgfvvv
      181 sglrgsawvs vlkdvlviat lgflafyvpa hyfggygpfl drlvteksew ltfpghgdsg
      241 lgqawfitts flnsltvvif pttvagylga knadvlrrna mllpaynvll fvpmllgmaa
      301 lfvvpglvga esnlalfklv vdslpawavg vigvaaalss ivpmavfmlv igtmwgrsvv
      361 sllprlerrq kgaaqsvvvv agslalllty tapntlvrls lisyeamaql lpmvllglvw
      421 rrltlwgals glavgvalvc gfvftehdpv wgvnagival aanlavalav tyagprerdd
      481 rpdeevlard evrppvave
//
LOCUS       WP_392280271             275 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015144].
ACCESSION   WP_392280271
VERSION     WP_392280271.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015144
  ORGANISM  Streptomyces sp. NPDC015144
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (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
REFERENCE   4  (residues 1 to 275)
  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 18542080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Streptomyces sp. NPDC015144"
                     /db_xref="taxon:3364944"
     Protein         1..275
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31393
     Region          17..71
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
     Region          94..270
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mhtpkprksk qlttwtmign lvadhrndln ltqvtlagmc gvsvdtlssv eqgrrplqmd
       61 lavvldkflg tkrtfqtlaq smpsrdrlpv fihdfldyeq daltltsyqt qvvpgllqte
      121 eyarfvfecq yppldedere swvaarmdrq rllerkprpi lhfileesil rsrlgdpamm
      181 rnqirhlrrl melpflglqi mpielpkhas ldgpmvllet pehdhlayve gqltsylhed
      241 pdqvsvllqk cgmlrsqals vdasaclmde mlget
//
LOCUS       WP_392280332             416 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Streptomyces sp.
            NPDC015144].
ACCESSION   WP_392280332
VERSION     WP_392280332.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015144
  ORGANISM  Streptomyces sp. NPDC015144
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 416)
  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 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   3  (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   4  (residues 1 to 416)
  AUTHORS   Igarashi,K., Ito,K. and Kashiwagi,K.
  TITLE     Polyamine uptake systems in Escherichia coli
  JOURNAL   Res Microbiol 152 (3-4), 271-278 (2001)
   PUBMED   11421274
REFERENCE   5  (residues 1 to 416)
  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   6  (residues 1 to 416)
  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 11430824
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Streptomyces sp. NPDC015144"
                     /db_xref="taxon:3364944"
     Protein         1..416
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0019808 - polyamine binding [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:0015846 - polyamine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45503
     Region          28..414
                     /region_name="PotD"
                     /note="Spermidine/putrescine-binding periplasmic protein
                     [Amino acid transport and metabolism]; COG0687"
                     /db_xref="CDD:440451"
ORIGIN      
        1 meqyeperls aaqiaamrrs ltsgrgaltr rsllrasgmg alaigglgtl sacgippaqr
       61 egdaaaasdd hsaeekqvnf snwteymdig edkksrptle aftkrtgisv kytedindnv
      121 effgkikpqm aagqdtgrdl iivtdwlaar iirlgwaqrl dasnlphafa nlsaqfrtpd
      181 wdpgraysyp wtgiptviay nsratggrkv dsvtqllddp alkgrvsfls emrdtigmtl
      241 ldqgkdpasf tdadydaain rlqkgvdkkq irrftgndyt adldkgdiaa cvawagdiiq
      301 lqagnpdiky aipaagyits sdnmlvpaka rhktnaeklm dyyyeppvaa rlaafinfvc
      361 pvdgvrdela ridekmaant lilpdremaa rshsfrslst keetayeekf akliga
//
LOCUS       WP_392280896             261 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015144].
ACCESSION   WP_392280896
VERSION     WP_392280896.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015144
  ORGANISM  Streptomyces sp. NPDC015144
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   4  (residues 1 to 261)
  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 18542080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Streptomyces sp. NPDC015144"
                     /db_xref="taxon:3364944"
     Protein         1..261
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29486
     Region          1..68
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
     Region          80..256
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mkmvgrlmaf yrdridvtqv qlaemtghhp etissieqgr rvllrslavk vdevlgtgga
       61 lavaieelpe idlipqwade yleleldalt lswydnqvmp gllqtpryae tlfrnriptf
      121 seaevafqte trlkrqeilh rpspptlsfv vwepvlslql tddeahaeql rhllecadlp
      181 gvclqvlpls hrthaglagp filletpdfq rlaysetqrg sllvsdpdei silsqkyaml
      241 rtqaltpedt rrllkrllge q
//
LOCUS       WP_392282001             226 aa            linear   BCT 20-JAN-2025
DEFINITION  4'-phosphopantetheinyl transferase family protein [Streptomyces sp.
            NPDC016566].
ACCESSION   WP_392282001
VERSION     WP_392282001.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016566
  ORGANISM  Streptomyces sp. NPDC016566
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459479
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Streptomyces sp. NPDC016566"
                     /db_xref="taxon:3364967"
     Protein         1..226
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=24794
     Region          19..223
                     /region_name="EntD"
                     /note="4'-phosphopantetheinyl transferase EntD
                     (siderophore biosynthesis) [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2977"
                     /db_xref="CDD:442216"
ORIGIN      
        1 mieellpesv vaveafgdhe dqesslypee rrlveravtk rrrefaavrv carrameklg
       61 vppqpvlpge rgaprwpagl lgsmthcdgy raaalvraad laslgidaev hgplpegvfe
      121 sialpaeqdr hrqlctgrpg vhwgrvlfsa kesvykawfp larawldfse adielvtepg
      181 pgtrgrfhar llvpgpevdg vrltgfdgrw lvseglvltt vtvphr
//
LOCUS       WP_392282023             429 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC016566].
ACCESSION   WP_392282023
VERSION     WP_392282023.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016566
  ORGANISM  Streptomyces sp. NPDC016566
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 429)
  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 429)
  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
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 429)
  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   5  (residues 1 to 429)
  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   6  (residues 1 to 429)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 429)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Streptomyces sp. NPDC016566"
                     /db_xref="taxon:3364967"
     Protein         1..429
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44447
     Region          20..>60
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          81..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 maglggrtvr dlrresrsav lqrlyfdgpm srqalgpatg lssgsvsnva aelltdglve
       61 eagvigsdag rprrllrirp dsgrligvdv getrvrvelf dlglrelara evplgprgyd
      121 vdavvghvqe gmaevlrtsa lapddllgvg igvpgiieda gdegavvhgq tigwdavple
      181 rrlrlsgqlp shipyfidng aktlgqaemw fgagrgarna vvvlfgsgvg acvvteeaaq
      241 gravewghlt vrvggrrcrc gargcleaya gaealvarwr eaggqpspga geeraltell
      301 aaarpsngst pdpvaaavla etaeylgagl sdlinlfqpe rvliggwagl qlggafldev
      361 rthalaqalr fpagrvgigl grlgpdavtv gaavlplaaf farggqrprp aarpvkapaw
      421 raavdgrlv
//
LOCUS       WP_392282143             546 aa            linear   BCT 20-JAN-2025
DEFINITION  S1 family peptidase [Streptomyces sp. NPDC016566].
ACCESSION   WP_392282143
VERSION     WP_392282143.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016566
  ORGANISM  Streptomyces sp. NPDC016566
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Querino Lima Afonso,M., da Fonseca,N.J. Jr., de Oliveira,L.C.,
            Lobo,F.P. and Bleicher,L.
  TITLE     Coevolved Positions Represent Key Functional Properties in the
            Trypsin-Like Serine Proteases Protein Family
  JOURNAL   J Chem Inf Model 60 (2), 1060-1068 (2020)
   PUBMED   31895561
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Waldner,B.J., Kraml,J., Kahler,U., Spinn,A., Schauperl,M.,
            Podewitz,M., Fuchs,J.E., Cruciani,G. and Liedl,K.R.
  TITLE     Electrostatic recognition in substrate binding to serine proteases
  JOURNAL   J Mol Recognit 31 (10), e2727 (2018)
   PUBMED   29785722
REFERENCE   3  (residues 1 to 546)
  AUTHORS   Pelc,L.A., Chen,Z., Gohara,D.W., Vogt,A.D., Pozzi,N. and Di Cera,E.
  TITLE     Why Ser and not Thr brokers catalysis in the trypsin fold
  JOURNAL   Biochemistry 54 (7), 1457-1464 (2015)
   PUBMED   25664608
REFERENCE   4  (residues 1 to 546)
  AUTHORS   Perona,J.J. and Craik,C.S.
  TITLE     Evolutionary divergence of substrate specificity within the
            chymotrypsin-like serine protease fold
  JOURNAL   J Biol Chem 272 (48), 29987-29990 (1997)
   PUBMED   9374470
REFERENCE   5  (residues 1 to 546)
  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 10595581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Streptomyces sp. NPDC016566"
                     /db_xref="taxon:3364967"
     Protein         1..546
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=59470
     Region          13..160
                     /region_name="Trypsin_2"
                     /note="Trypsin-like peptidase domain; pfam13365"
                     /db_xref="CDD:433149"
ORIGIN      
        1 marieeqdgq vlgagvllap drvltaahvv rpglpyvvhf vgvpgvpgva atvradehvp
       61 qredafgdri gdlallrlaq pqpaehttrl yrlasphgpv smygfpagdd ggrwhgatlv
      121 aargrdhqvq lrpqtqgela apgfsgggvv dhetdevigi vlsvddgpns vfsymsptet
      181 ilshlpqaaa wsegaeavdp tlrpgatgta grldlpfate laswfrgegw pvlvtvvpar
      241 sgrawtltra vtladrelrt qqntsafshd ppetvppagg hdlaldvrgm tegqvmdria
      301 erlgirgdpr perlgalrvp laavlvgvdq aaepdallgl lerlaqqgar lllvfrrrgg
      361 raaqaaesfv rlplharwtr lhreldhivd elgpalderr grvaadpgtr qlldraeagv
      421 rrtrmllawv ahspererep rradvlftfe daaerrrrrl eeaisllder lrrreellgr
      481 vtaewplcre raaarggdrv meayrlyela lsllrqspcd vdeaetavrh fvgfcsgtap
      541 gregtp
//
LOCUS       WP_392282432            1365 aa            linear   BCT 20-JAN-2025
DEFINITION  Rne/Rng family ribonuclease [Streptomyces sp. NPDC016566].
ACCESSION   WP_392282432
VERSION     WP_392282432.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016566
  ORGANISM  Streptomyces sp. NPDC016566
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1365)
  AUTHORS   Kime,L., Jourdan,S.S. and McDowall,K.J.
  TITLE     Identifying and characterizing substrates of the RNase E/G family
            of enzymes
  JOURNAL   Methods Enzymol 447, 215-241 (2008)
   PUBMED   19161846
REFERENCE   2  (residues 1 to 1365)
  AUTHORS   Callaghan,A.J., Marcaida,M.J., Stead,J.A., McDowall,K.J.,
            Scott,W.G. and Luisi,B.F.
  TITLE     Structure of Escherichia coli RNase E catalytic domain and
            implications for RNA turnover
  JOURNAL   Nature 437 (7062), 1187-1191 (2005)
   PUBMED   16237448
REFERENCE   3  (residues 1 to 1365)
  AUTHORS   Li,Z., Pandit,S. and Deutscher,M.P.
  TITLE     RNase G (CafA protein) and RNase E are both required for the 5'
            maturation of 16S ribosomal RNA
  JOURNAL   EMBO J 18 (10), 2878-2885 (1999)
   PUBMED   10329633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1365
                     /organism="Streptomyces sp. NPDC016566"
                     /db_xref="taxon:3364967"
     Protein         1..1365
                     /product="Rne/Rng family ribonuclease"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=143851
     Region          623..1026
                     /region_name="CafA"
                     /note="Ribonuclease G or E [Translation, ribosomal
                     structure and biogenesis]; COG1530"
                     /db_xref="CDD:441139"
ORIGIN      
        1 mleptepreg selntpsdtl pprrrrrass rpagppvaae aptevtvpai paaeaeeite
       61 eqaatveapp aveepapaar ttrrratrra sapagapaaa etvetvvtad tavatvaaea
      121 vepaeaveav eevapaprtr rratrrasap agapaaaeae ektevkaeek aaaetapaae
      181 vetapaveae aapaartrrr atrrasapag aaaeavetvv paaaaapgae aveepaaaet
      241 veaaeapaaa dvaeeaaprr trrratrqvs apvgapatae apvvaeqaaa eeaetpepva
      301 vqataegapr rrrrvvrqaa sgfsapahsa aaeaeaeaea eadaprrpar pavavfqapv
      361 faepkfqtpe raaaeaaaea agteetekta epaetagtgt yaeeraeags rrrrrrrgaa
      421 faeepqavea atedeepeea eeaaaedlae gdeteeaega eeagsrrrrr rggrrrrrgd
      481 avegeagegg daeadelaae qaaqdaedtv eqeeedaeda rdesgssssr rrrrrrrrag
      541 dtsvdtepde tdpertvvkv reprkpaeps devqsikgst rleakkqrrr egreqgrrrv
      601 piiteaefla rreavervmv vrqhgertqi gvledgvlve hyvnkeqats yvgnvylgkv
      661 qnvlpsmeaa fidigkgrna vlyagevnfe algmangprr iesalksgqs vlvqvtkdpi
      721 ghkgarltsq vslpgrylvy vpegsmtgis rklpdterar lktilkkivp edagvivrta
      781 aegaseeelr rdverlqaqw ediqkkaksg naptllygep dmtvrvvrdi fnedfskvvv
      841 sgdeawqtih gyvshvapdl aerlskwtse vdafatyrid eqlakaldrk vwlpsggslv
      901 idrteamvvv dvntgkftgq ggnleetvtr nnleaaeeiv rqlrlrdlgg iividfidmv
      961 lesnrdlvlr rlleclgrdr tkhqvaevts lglvqmtrkr vgqgllesfs etcvhcngrg
     1021 vivhmeqpta vggggggkrk krgrggdgql pehevaavav etgeavepaa etvvevaael
     1081 aepvalpapd fapdeelyss vaeaeaaagr grsrrrvsrr asapagapka errragkate
     1141 ateateaaet aevvvpaeea vlpaqpepvv eaqaepvaaa apepaaeeaa pkgrtrrrat
     1201 rkvsapagsp agaeaavvtv aetapeapve qpeaeapapv eeapaesaap arprrravrk
     1261 atapttseet avvvvpatap eaaaaeapav eaaeeaveea apakktarka akkatakkaa
     1321 tkktvakkta akkttakkaa ktaktaaaks takktttvsa aades
//
LOCUS       WP_392282952             185 aa            linear   BCT 20-JAN-2025
DEFINITION  4'-phosphopantetheinyl transferase family protein [Streptomyces sp.
            NPDC016566].
ACCESSION   WP_392282952
VERSION     WP_392282952.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016566
  ORGANISM  Streptomyces sp. NPDC016566
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459479
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Streptomyces sp. NPDC016566"
                     /db_xref="taxon:3364967"
     Protein         1..185
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=20112
     Region          3..175
                     /region_name="EntD"
                     /note="4'-phosphopantetheinyl transferase EntD
                     (siderophore biosynthesis) [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2977"
                     /db_xref="CDD:442216"
ORIGIN      
        1 msrrrefata rwcarhalse lgvppgpvlr gphgapqwpd gvvgsithca gyraavvaha
       61 trfrllgvda epraalppgi letivlpger swvrdlrags pgvhwdrllf cvketvhrsw
      121 ypatarwlgf edarifvdpv agtfsarilv ptplrrqgrp isrlsgrwlv geglvpaala
      181 tpcdp
//
LOCUS       WP_392283411             420 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC016566].
ACCESSION   WP_392283411
VERSION     WP_392283411.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016566
  ORGANISM  Streptomyces sp. NPDC016566
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 420)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Streptomyces sp. NPDC016566"
                     /db_xref="taxon:3364967"
     Protein         1..420
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=45001
     Region          57..241
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          249..368
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mnhtprtrtv vsctllvaal gagvtgcgsd gnplsakpyd aadqisfngp mgtgkqadpd
       61 kpleittstd dgritdvtay datgrfvage laadgsrwhs tsplaanahy tvvvsteded
      121 gapgrktlsf dttkpsttkr lnvtfgpdsg qygvgqpita qldhevkdka qravverglr
      181 vdatpavqga wywvsdkelh yrpkeywpah atiqvhsnld gvkigdrlwg gkskalkiti
      241 gdrieavtda aahqltfykn gqavqsipvt tgkpgfetrn gvkvvlakqy fvrmrgttvg
      301 iaegssdsyd lpvyyatrvt wsgeyvhaap wsvgsqgyen vshgctgmst snaewffnni
      361 hegdivkvvn sngnpmepfg ngfgdwnvdw kkwrtgsalv ngtpdgpapq dalrlqptav
//
LOCUS       WP_392283456             364 aa            linear   BCT 20-JAN-2025
DEFINITION  gluconeogenesis factor YvcK family protein [Streptomyces sp.
            NPDC016566].
ACCESSION   WP_392283456
VERSION     WP_392283456.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016566
  ORGANISM  Streptomyces sp. NPDC016566
            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 10785358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Streptomyces sp. NPDC016566"
                     /db_xref="taxon:3364967"
     Protein         1..364
                     /product="gluconeogenesis factor YvcK family protein"
                     /GO_function="GO:0043743 - LPPG:FO 2-phospho-L-lactate
                     transferase activity [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=38737
     Region          47..352
                     /region_name="CofD"
                     /note="Archaeal 2-phospho-L-lactate transferase/Bacterial
                     gluconeogenesis factor, CofD/UPF0052 family [Carbohydrate
                     transport and metabolism, Coenzyme transport and
                     metabolism]; COG0391"
                     /db_xref="CDD:440160"
ORIGIN      
        1 mtertsrlsr lrrvvpegra sraandaraa rpvevrggrv rrrgaqpkvv algggmglsa
       61 slaalrritg dltavvtvad dggssgrlrd elgvlppgdl rkalaalcgd ddwgqtwarv
      121 iqhrfqsqge mhghavgnll ivalweqlgd hvqaldlvgk llgahgrvlp msavplelqa
      181 lvkghdperp devdtvrgqa tvaltpgevq svhlvphdpp avpeavaavl dadwvvlgpg
      241 swfssviphl lvpdlldalt etkarkvlsl nlapqpgete gfspqrhlev lgrhapklal
      301 dvvladeaav pdrdslteaa krlgaavela pvartdgspr hdpellaaay drifrmhgri
      361 gpwr
//
LOCUS       WP_392283883             330 aa            linear   BCT 20-JAN-2025
DEFINITION  quinone oxidoreductase family protein [Streptomyces sp.
            NPDC016566].
ACCESSION   WP_392283883
VERSION     WP_392283883.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016566
  ORGANISM  Streptomyces sp. NPDC016566
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 330)
  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 330)
  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 330)
  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   4  (residues 1 to 330)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Streptomyces sp. NPDC016566"
                     /db_xref="taxon:3364967"
     Protein         1..330
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=35285
     Region          1..327
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 mhairhhrfg dpdvlrweqm ptpepgpgev llrveaaavn rydllsragi nprlplprtv
       61 gidctgtveh ydgprtdlap gtsvvvlgdr lgnggpgaya thvcitadev fplpldtcdi
      121 taaclgipyv tayyalfqrh hirpgetllv pgaggsvata aiqlahhagi rvlatshgpa
      181 rcsrarrlga decfdyradd ipaqvrkatd grgvdvvina vggdtiaqgl qclrdrgrll
      241 aigsaqgrqf afdgfrfllr eqqvigvnvt pltptrrfai fqkllaliqa ghitvpidhf
      301 qpmaqaaeah rriesgaafg ktvlipppap
//
LOCUS       WP_392285180             408 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC015346].
ACCESSION   WP_392285180
VERSION     WP_392285180.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015346
  ORGANISM  Streptomyces sp. NPDC015346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  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 408)
  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
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 408)
  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   5  (residues 1 to 408)
  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   6  (residues 1 to 408)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 408)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 408)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces sp. NPDC015346"
                     /db_xref="taxon:3364954"
     Protein         1..408
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42321
     Region          23..>66
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          94..396
                     /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 magttpgttp gtpgtprvlr amndraaldl llehgplsrt rigkltglsk ptasqllarl
       61 eaaglvvatg ttagrpgpsa qlyavnaraa faagldvtph riraavadit gqvvgafelp
      121 tpgraaegvv rqvttaldga akdagitpad vhrlvigtpg afdpatgrlr yashlpgwhs
      181 ptllaelaav lpmpfeyend vnlvavaeqr rgaarghqdf vllwneeglg aalvlggrlh
      241 rgftggagev gflpvpgtpl vrqvtkansg gfqelagvqa vpriaralri etaeqpyvpt
      301 asrllahaaa hhgddpryaa lldryaerla tglaslvavl dpellvlsge vivaggeplr
      361 ervqselael aasrprlvlg dvsehpvlrg alesalaatr devfdtsr
//
LOCUS       WP_392285376             390 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC015346].
ACCESSION   WP_392285376
VERSION     WP_392285376.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015346
  ORGANISM  Streptomyces sp. NPDC015346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 390)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Streptomyces sp. NPDC015346"
                     /db_xref="taxon:3364954"
     Protein         1..390
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=41227
     Region          53..230
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          237..357
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mlrtriplfl ltavsalalt acsagtvtea pprsaapaed rpakvtvapp aagrpvtvta
       61 tdgtlavvkv adadggvlag rtavggaswv sdrkaapgts ytveitarsa ggrettsrss
      121 fsipeadrvn kltlapgknt tvgiaqplsi vfdrpvthka dverqlkvtt sngtegswgw
      181 lkdwsgrdrv dwrpraywkp gtkvtldatl dgtdsgggwf trdyrsgftv datarvvkvd
      241 ldrkrltver dgravrtilv sggtpggdkr swrgtavlma kegtinmnse tvglgdaydk
      301 mvdhsmrltw sgmyahaapw naryfgranm ssgcigmsaa daasfyasvr pgdpfeitga
      361 dtkgtvapgn gygawnvswe qwraksalar
//
LOCUS       WP_392285852             390 aa            linear   BCT 20-JAN-2025
DEFINITION  bifunctional cobalt-precorrin-7
            (C(5))-methyltransferase/cobalt-precorrin-6B
            (C(15))-methyltransferase [Streptomyces sp. NPDC015346].
ACCESSION   WP_392285852
VERSION     WP_392285852.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015346
  ORGANISM  Streptomyces sp. NPDC015346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Moore,S.J., Lawrence,A.D., Biedendieck,R., Deery,E., Frank,S.,
            Howard,M.J., Rigby,S.E. and Warren,M.J.
  TITLE     Elucidation of the anaerobic pathway for the corrin component of
            cobalamin (vitamin B12)
  JOURNAL   Proc Natl Acad Sci U S A 110 (37), 14906-14911 (2013)
   PUBMED   23922391
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Padmanabhan,B., Yokoyama,S. and Bessho,Y.
  TITLE     Crystal structure of putative CbiT from Methanocaldococcus
            jannaschii: an intermediate enzyme activity in cobalamin (vitamin
            B12) biosynthesis
  JOURNAL   BMC Struct Biol 13, 10 (2013)
   PUBMED   23688113
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Heldt,D., Lawrence,A.D., Lindenmeyer,M., Deery,E., Heathcote,P.,
            Rigby,S.E. and Warren,M.J.
  TITLE     Aerobic synthesis of vitamin B12: ring contraction and cobalt
            chelation
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 815-819 (2005)
   PUBMED   16042605
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Rodionov,D.A., Vitreschak,A.G., Mironov,A.A. and Gelfand,M.S.
  TITLE     Comparative genomics of the vitamin B12 metabolism and regulation
            in prokaryotes
  JOURNAL   J Biol Chem 278 (42), 41148-41159 (2003)
   PUBMED   12869542
REFERENCE   5  (residues 1 to 390)
  AUTHORS   Keller,J.P., Smith,P.M., Benach,J., Christendat,D., deTitta,G.T.
            and Hunt,J.F.
  TITLE     The crystal structure of MT0146/CbiT suggests that the putative
            precorrin-8w decarboxylase is a methyltransferase
  JOURNAL   Structure 10 (11), 1475-1487 (2002)
   PUBMED   12429089
REFERENCE   6  (residues 1 to 390)
  AUTHORS   Roessner,C.A., Santander,P.J. and Scott,A.I.
  TITLE     Multiple biosynthetic pathways for vitamin B12: variations on a
            central theme
  JOURNAL   Vitam Horm 61, 267-297 (2001)
   PUBMED   11153269
REFERENCE   7  (residues 1 to 390)
  AUTHORS   Raux,E., Schubert,H.L. and Warren,M.J.
  TITLE     Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum
  JOURNAL   Cell Mol Life Sci 57 (13-14), 1880-1893 (2000)
   PUBMED   11215515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454932
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Streptomyces sp. NPDC015346"
                     /db_xref="taxon:3364954"
     Protein         1..390
                     /product="bifunctional cobalt-precorrin-7
                     (C(5))-methyltransferase/cobalt-precorrin-6B
                     (C(15))-methyltransferase"
                     /EC_number="2.1.1.132"
                     /EC_number="2.1.1.196"
                     /EC_number="2.1.1.289"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008276 - protein methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009236 - cobalamin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40068
     Region          20..390
                     /region_name="CobL"
                     /note="Precorrin-6B methylase 2 [Coenzyme transport and
                     metabolism]; COG2242"
                     /db_xref="CDD:441843"
ORIGIN      
        1 mitvigsgag adagswagep alvvdvrgde lttgeldlid khaaeggtra vvralgdpgf
       61 fgvvrtlerr fgaraldvrp gpaavgvafa rlglawddav vadgselhen aldravnvcr
      121 ahpkvavlpg pgvgpaelga ellhrvtsrt lvvfsalgdp frerfervep aeamcrtwdg
      181 vslvvcldes raegpapavt gplrgpgrwa lpdrefgptd gsvlpyeara lalarlgpra
      241 gdlvweigtg cgavavecar lgaaavavek taagverira ntaahgvevr avhgaaptvl
      301 shladpdgvf vggggrelka ivlaaarrar ravvvavtal eqvtpvrsal escgfaaegv
      361 llhsqrlltl pdgsssmapa apvflvwgtr
//
LOCUS       WP_392285959             329 aa            linear   BCT 20-JAN-2025
DEFINITION  heme/hemin ABC transporter substrate-binding protein [Streptomyces
            sp. NPDC015346].
ACCESSION   WP_392285959
VERSION     WP_392285959.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015346
  ORGANISM  Streptomyces sp. NPDC015346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Naoe,Y., Nakamura,N., Rahman,M.M., Tosha,T., Nagatoishi,S.,
            Tsumoto,K., Shiro,Y. and Sugimoto,H.
  TITLE     Structural basis for binding and transfer of heme in bacterial
            heme-acquisition systems
  JOURNAL   Proteins 85 (12), 2217-2230 (2017)
   PUBMED   28913898
REFERENCE   2  (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   3  (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   4  (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   5  (residues 1 to 329)
  AUTHORS   Ho,W.W., Li,H., Eakanunkul,S., Tong,Y., Wilks,A., Guo,M. and
            Poulos,T.L.
  TITLE     Holo- and apo-bound structures of bacterial periplasmic
            heme-binding proteins
  JOURNAL   J Biol Chem 282 (49), 35796-35802 (2007)
   PUBMED   17925389
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Streptomyces sp. NPDC015346"
                     /db_xref="taxon:3364954"
     Protein         1..329
                     /product="heme/hemin 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=32787
     Region          58..329
                     /region_name="ChuT"
                     /note="ABC-type hemin transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG4558"
                     /db_xref="CDD:443619"
ORIGIN      
        1 msalalalva tgcgdgggag ggagdggtsr taaapdrvep lagvpesrlp vtvesadgre
       61 vtvtstkriv pltgslseiv ftlglgervv arditatfeq aadlpavtra hdvsaesvls
      121 lrptlvladt stgpaeavaq irdagiplvv vepakeladv striaavaaa lgvpdsgaal
      181 qkrtrdriaa aregvpahgg egkprvafly vrgsaavyll ggaesgatsl leaagavdag
      241 kesgltkdft pltsealaaa apdallvmsk glesvggvdg lvklpgvaqt pagmarrvvs
      301 iddgvllnyg prtdevlrsl vsqlygesk
//
LOCUS       WP_392286280             971 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces sp.
            NPDC015346].
ACCESSION   WP_392286280
VERSION     WP_392286280.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015346
  ORGANISM  Streptomyces sp. NPDC015346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 971)
  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 971)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 971)
  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 971)
  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 18640657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..971
                     /organism="Streptomyces sp. NPDC015346"
                     /db_xref="taxon:3364954"
     Protein         1..971
                     /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=101158
     Region          <628..846
                     /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          791..970
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          912..966
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mttaphlpvr pagvggppap vgreellsrl ervlhargra lltgpagvgk tevalaeaar
       61 aeargetvlw laalpadrdi pgaaaaalva svaatvtwpg vagtgaatdv pgpagsgpda
      121 paaaraaipr qvpgpgasgv fdglpgpqrt avamlcreap lhdggwdpia lrlgiaqilr
      181 gltargpall vvdgvqhida dsadllrfal hlappalrvv avetpeayga qeahdihlwv
      241 pseadillvp plqadeiael lihhrlpsrm agrihkasgg nprlalavgr sladartpvh
      301 haealtlsgr arelarqllg tappavretl llaalalrps aalirragrp daeadlaaae
      361 radlvslaed gtvtftagll pstlvhdacw aersaghaal akvvddsvea vrhralatdi
      421 pdealaaeva aaadlarrrg nsalaaelal laaestpmeh atqriarlvd aaeeaaraar
      481 adlamraatd llardaspsd rvrarlavld tagqgltgld emyvhameds eghtalraav
      541 qlrlavkyvl adgdplrsra aavesaalaa smgdprtaaq altvqarmdr algaseaeav
      601 laqarglema erplgirnaa qiltirhalf ddrladardq lnallplvrr rgsvedtiel
      661 fstlaaiesr lgacpaalah agqslaltle aglspgpawy tlalaetagg sfgraasyar
      721 rsvqaseeeg drvflsrsly algrvqling dvasaletlr rvqaneraqs tvdpsmlrwh
      781 eelaeallan daaqeaagll aevrpvaerl grttvllgcd rayalylaag gktdeaaell
      841 trtaerfaea glplehgral ialarverrr rrrsaaqsal qaaaavfera gaapwlalts
      901 etpagedtlp alssltdael rlarlvgqga snqeaaakly lsvktvearl triyqkldvr
      961 sraqlasalr g
//
LOCUS       WP_392287320             284 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Streptomyces sp.
            NPDC015346].
ACCESSION   WP_392287320
VERSION     WP_392287320.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015346
  ORGANISM  Streptomyces sp. NPDC015346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 284)
  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 284)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces sp. NPDC015346"
                     /db_xref="taxon:3364954"
     Protein         1..284
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29969
     Region          2..277
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mpltttdeiv lgarernaga gafnvvqieh aqaivagaea aglpvilqis entaryhgsl
       61 epiglatlai arraavpvsv hldhaestel vreavalgfr svmfdasklp yeenlaatre
      121 ttdychrhdv wveaelgevg gkdgahapga rtdpdearaf vkatavdsla vavgsshamv
      181 trdavldfel iarlreavgv plvlhgssgv gdvdlawavs agmtkvnvat hlnkaftrav
      241 rshleeqpat vdprrylgpa rdavahevth llqvlaadve lsrt
//
LOCUS       WP_392288327             238 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Streptomyces sp.
            NPDC015346].
ACCESSION   WP_392288327
VERSION     WP_392288327.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015346
  ORGANISM  Streptomyces sp. NPDC015346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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 11440233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Streptomyces sp. NPDC015346"
                     /db_xref="taxon:3364954"
     Protein         1..238
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25591
     Region          7..228
                     /region_name="GCD1"
                     /note="NDP-sugar pyrophosphorylase, includes eIF-2Bgamma,
                     eIF-2Bepsilon, and LPS biosynthesis protein s
                     [Translation, ribosomal structure and biogenesis, Cell
                     wall/membrane/envelope biogenesis]; COG1208"
                     /db_xref="CDD:440821"
ORIGIN      
        1 mhtfptqavv laggqgsrlr pytddrpkpm veipgtgtpi ighqlswlaa egvtdavvsc
       61 ghlaevlqdw lagadlplrv ttvveseplg rggglkyaaa hlpepaqpwy atngdiwtrf
      121 slremaafha eraatatlal arpripwgav etdtfghitd fiesppspyl inagvyvfsa
      181 efttllpdlg dherttfpql ardrrlagfp lpqgaywrai dtakdlteaa kelaaqaa
//
LOCUS       WP_392288617             275 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015346].
ACCESSION   WP_392288617
VERSION     WP_392288617.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015346
  ORGANISM  Streptomyces sp. NPDC015346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (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
REFERENCE   4  (residues 1 to 275)
  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 18542080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Streptomyces sp. NPDC015346"
                     /db_xref="taxon:3364954"
     Protein         1..275
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30706
     Region          24..70
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
     Region          91..270
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mqpgkkprkk vpswevvgal vglyrknagm tqphlaslvc igletlgsie qgrrplrikl
       61 aaeldeildt kgaltaavak vpqrerypef vqdfveeeak alslcsyqnq vvpgllqtpe
      121 yaravfdcly ppiteqeaee rllaridrqq vfeqkpwppm msfllnesvl eqpiggsevl
      181 lgqirhlrqv aelpflalqi lpkdltrhag lngpmvlvet pehthlayie gqrvsflied
      241 pdevgilqrk ygmlrsqalt peetkglldr maget
//
LOCUS       WP_392288970             541 aa            linear   BCT 20-JAN-2025
DEFINITION  peptide ABC transporter substrate-binding protein [Streptomyces sp.
            NPDC015346].
ACCESSION   WP_392288970
VERSION     WP_392288970.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015346
  ORGANISM  Streptomyces sp. NPDC015346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11467924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Streptomyces sp. NPDC015346"
                     /db_xref="taxon:3364954"
     Protein         1..541
                     /product="peptide 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=58764
     Region          37..536
                     /region_name="OppA"
                     /note="ABC-type oligopeptide transport system, periplasmic
                     component [Amino acid transport and metabolism]; COG4166"
                     /db_xref="CDD:443327"
ORIGIN      
        1 mrgathakwa atalavalaa tacggggdgg gsgadgivss swgdpqnple pantnevqgg
       61 kvlamifrgl kqydpktgea enmlaesiet tdstnfritl kngwtfsnge kvtaksfvda
      121 wnygahlknn qknafffgqi egydqvhpee gqakaetmsg lkvvddrtft vklsqkfslw
      181 petlgyaafa plpraffvdh dawlskpvgn gpytvdsysk gsqmalkrwd gypgedkaqn
      241 ggvtlkvytd nntaytdlta gnldlvddvp asqlknvqad lgdryinlpa giiqtlsipf
      301 ydkawntpng dklrkgisra inreqiteti fqktrtpavd wtspvlgeeg gyknicgdfc
      361 tydaaeakkl vaegggipgg tmkisynadt gshkewvdav cnsinnalgn nracvgnpvg
      421 tfadyrnqvt tqkmtgpfra gwqmdypliq nflqplyytn assndgkwsn pefdklvdqa
      481 naepdtkkav eifqraeevl rddmgaiplw yqngsagyse rvsnvalnpf svpvyneikv
      541 d
//
LOCUS       WP_392290152             456 aa            linear   BCT 20-JAN-2025
DEFINITION  M20 metallopeptidase family protein [Streptomyces sp. NPDC015346].
ACCESSION   WP_392290152
VERSION     WP_392290152.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015346
  ORGANISM  Streptomyces sp. NPDC015346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Lindner,H.A., Lunin,V.V., Alary,A., Hecker,R., Cygler,M. and
            Menard,R.
  TITLE     Essential roles of zinc ligation and enzyme dimerization for
            catalysis in the aminoacylase-1/M20 family
  JOURNAL   J Biol Chem 278 (45), 44496-44504 (2003)
   PUBMED   12933810
REFERENCE   2  (residues 1 to 456)
  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 11444961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Streptomyces sp. NPDC015346"
                     /db_xref="taxon:3364954"
     Protein         1..456
                     /product="M20 metallopeptidase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47735
     Region          37..449
                     /region_name="AbgB"
                     /note="Metal-dependent
                     amidase/aminoacylase/carboxypeptidase [General function
                     prediction only]; COG1473"
                     /db_xref="CDD:441082"
ORIGIN      
        1 mssaethdgr aaasqdgaaa ggggtvnpdg gaavheeldr raeevaarvv awrrhlhrnp
       61 elpnreagta rfvadhlrsl gldevrtgia ghgvvgvlrg gapggrvaal radmdalpvp
      121 dlcgeefasd vvdaaypggp fpvshacghd chtamlmgaa tvlaearerl pgtvlfvfqp
      181 aeegppvtee ggaramveag aftdpvptma fgmhvtpypk gyvgfrvgnq ygastllkiv
      241 itgeqthgst pwqgidpmpa agavltgigq lyrqvsafda itvsighved vgrfniiget
      301 vtlwgtvrca vesdmaevrr rlttlaehta aaygatasvt ylqpvppvhn saewveaglp
      361 tirrvvgeer tvetgatlgy ddvsefvnrf gglyvmlgvq dasldadgrp lplpdgrglv
      421 tnhnprfyad ddtlvtgvrl hahmaydhlt gaaapv
//
LOCUS       WP_392291312             279 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015501].
ACCESSION   WP_392291312
VERSION     WP_392291312.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015501
  ORGANISM  Streptomyces sp. NPDC015501
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 279)
  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 279)
  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 18542080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces sp. NPDC015501"
                     /db_xref="taxon:3364959"
     Protein         1..279
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30983
     Region          17..70
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
     Region          93..273
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 manikqlnpe aspqaafgar lrrmreergw iqdqladmlg csgrhisaie tgrkpatlpf
       61 arkadrlfdl igsdqsferq wqemkhgnll egfpeyvgye graveirlfq vglipvllqt
      121 peyaravafg dvergsitve qanervafla erqaalvrpr ppmvfavmde sclhqvvggl
      181 dvmdaqlqrl iemstrpnwi iqvapfslga rrafnlpvnl ltmadrsiva yaesqtqgsv
      241 eretsfvvpm ltayhqfqse alskaasvak iselrkgap
//
LOCUS       WP_392291609            1390 aa            linear   BCT 20-JAN-2025
DEFINITION  Rne/Rng family ribonuclease [Streptomyces sp. NPDC015414].
ACCESSION   WP_392291609
VERSION     WP_392291609.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015414
  ORGANISM  Streptomyces sp. NPDC015414
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1390)
  AUTHORS   Kime,L., Jourdan,S.S. and McDowall,K.J.
  TITLE     Identifying and characterizing substrates of the RNase E/G family
            of enzymes
  JOURNAL   Methods Enzymol 447, 215-241 (2008)
   PUBMED   19161846
REFERENCE   2  (residues 1 to 1390)
  AUTHORS   Callaghan,A.J., Marcaida,M.J., Stead,J.A., McDowall,K.J.,
            Scott,W.G. and Luisi,B.F.
  TITLE     Structure of Escherichia coli RNase E catalytic domain and
            implications for RNA turnover
  JOURNAL   Nature 437 (7062), 1187-1191 (2005)
   PUBMED   16237448
REFERENCE   3  (residues 1 to 1390)
  AUTHORS   Li,Z., Pandit,S. and Deutscher,M.P.
  TITLE     RNase G (CafA protein) and RNase E are both required for the 5'
            maturation of 16S ribosomal RNA
  JOURNAL   EMBO J 18 (10), 2878-2885 (1999)
   PUBMED   10329633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1390
                     /organism="Streptomyces sp. NPDC015414"
                     /db_xref="taxon:3364957"
     Protein         1..1390
                     /product="Rne/Rng family ribonuclease"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=145987
     Region          630..1033
                     /region_name="CafA"
                     /note="Ribonuclease G or E [Translation, ribosomal
                     structure and biogenesis]; COG1530"
                     /db_xref="CDD:441139"
ORIGIN      
        1 mleptepneg selntpsdtl pprrrrraas rpagppgaae apaevtvpai paaevdeiae
       61 aedvaapaaa eepappartr rratrraaap agapaaaeaa etvvpateaa gsaepaeave
      121 dagtteepap prtrrratrr asapagapae teaavpaaet qparteante eaaeseaaap
      181 arprrratrr avapagepka tetpevseaa pvaeapaaae tpaateeaap agrtrrratr
      241 rasapagapa aaetaeavvp aaaapapeae aaaeeptaap aaeeaaprrt rrratrgaaa
      301 paaeeatata eppaeetrap eapkapaaet paeeggprrr rrvvrqaatg faapartead
      361 eagsprrpar pavavfqapv faepqfqtpq raaaqaaaea agaeepeeet eaypeeraea
      421 garrrrrrrg aaeetrpaea eepeeaeaaa edlaegdegd eaegseesgs rrrrrrggrr
      481 rrrgdaadge agegadaesd elaaeqaaqd aedtaeqede daeeardees ggssssrrrr
      541 rrrrragesg geaesgtddp ertvvkvrep rkpaepsdev qsikgstrle akkqrrregr
      601 eqgrrrvpii teaeflarre avervmvvrq hgertqigvl eddvlvehyv nkeqstsyvg
      661 nvylgkvqnv lpsmeaafid igkgrnavly agevnfgalg mgngprriea alksgqsvlv
      721 qvtkdpighk garltsqvsl pgrylvyvpe gsmtgisrkl pdterarlkt ilkkivpeda
      781 gvivrtaaeg asedelrrdv erlqaqweei qkkaksgnap tllygepdmt vrvvrdifne
      841 dfskvvvsgd eawqtihgyv shvapdlaer lskwtsevdv fatyrideql akaldrkvwl
      901 psggslvidr teamvvvdvn tgkftgqggn leetvtrnnl eaaeeivrql rlrdlggiiv
      961 idfidmvles nrdlvlrrll eclgrdrtkh qvaevtslgl vqmtrkrvgq gllesfsetc
     1021 vhcngrgviv hmeqpvaagg ggggkrkkrg rggdaqehvh etaavavetg eavepeveta
     1081 vevaaelaep valpgpdfap deelyssvae aeaaagrgrs rrrasrrasa pagapkaert
     1141 pkaeraaqap epekapstea avaaaaptaq dvtaeeaaar pvrpepaaea laepvaaedq
     1201 tvpepkaepa aeeaapkgrt rrratrkvsa pagspagaea avltvsetap aapveqpaae
     1261 apapaaeaes aaparprrra vrkataptas eetavtvvps aapeetpaaa gtvteapaae
     1321 etveeavpak kaarktakka takkaatkkt aakktaakkt takkaaktvk taaakttakk
     1381 tttvpagdeg
//
LOCUS       WP_392291919             324 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: quinone oxidoreductase family protein [unclassified
            Streptomyces].
ACCESSION   WP_392291919
VERSION     WP_392291919.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 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   4  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..324
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=32872
     Region          1..323
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 mraiefqryg gpevltavta eapepgpgqv svdvawtgvn fadlkarseg yrvprlpfvp
       61 glevsgrira lgagvtglav gqevaaltgs gayaevavae aatvfplpag vdlrtaatlp
      121 tvlptayalv hsvgrlqpge tvlvqgaagg vgtavgrlar aagagavygv vssaakaaha
      181 rkygydevft gdfrqrvrea tggrgadlvl dpvggdtlre glaslapfgr lvsfgnassa
      241 epwsvgqpel yplgvsvagf siltlagtap aelrrltera fakvadgtvs lpvtaefale
      301 eaadahrlmg trtstgklll rvga
//
LOCUS       WP_392292024             393 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015414].
ACCESSION   WP_392292024
VERSION     WP_392292024.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015414
  ORGANISM  Streptomyces sp. NPDC015414
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 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 10611723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Streptomyces sp. NPDC015414"
                     /db_xref="taxon:3364957"
     Protein         1..393
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=39798
     Region          17..74
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(23,27,52)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(26,51)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(33..34,45,48,52..53)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          292..375
                     /region_name="DUF2690"
                     /note="Protein of unknown function (DUF2690); pfam10901"
                     /db_xref="CDD:402475"
ORIGIN      
        1 mprwkalpde ldpqikefts qlralvdrsg lsiaaladrt gysktswery lggrllapkg
       61 aivalaevtg thpvhlttmw elaerawsra emrhdrtmeq irisqaraal gefgaaeaea
      121 qgaggtrtah rgtgtaavpg aagpagappr vpaqptasda ddreragrap apevnswgla
      181 gyegpsragg rpgtrpptlp dgagtppvpp apygaqqqpa paanrsaqgs ggrrwltlfl
      241 asagavlvvv aavflfthrg ggkgegaaka pspaastrps lpagvkcaga actgkdaeam
      301 gcsgtlvsta ktatvgattl evrysrtcgt awgritggvp gdqvevsagk arqkgditaa
      361 gdtiaytpmv avkdpadaea catlasgqtg ctk
//
LOCUS       WP_392292501             414 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC015414].
ACCESSION   WP_392292501
VERSION     WP_392292501.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015414
  ORGANISM  Streptomyces sp. NPDC015414
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 414)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Streptomyces sp. NPDC015414"
                     /db_xref="taxon:3364957"
     Protein         1..414
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=42913
     Region          72..244
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          250..382
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mlavtalggt shaatggnga gdqqqtqtpv asstpaapdt satpgasaps aaptatqdvs
       61 darikitpgq gahdvgtddp vrvtvsdgkl tkvtmtavat gaevrgtlsa dgtswkpdgp
      121 lkratryqva aeakddkgrs aaenatiatv spandfvghv splngqtvgv gmpvsvtfnk
      181 avtdkaavqs eiqvssssgq qvvghwlndg rldfrpetyw kpgstvtvdm nvggvhkavt
      241 fkigrsqvst vdaktkqmtv vrngkkikti pissgspehp tyngqmvise kfrhirmnaa
      301 svnltekdgk psydiaavph amrlsdsgtf ihgnywgads vfgkvntshg cvglkdvrgg
      361 gdstkpaawf fdhsligdvv ivknsddktk lapdnglsdw nvpwsewvag gatn
//
LOCUS       WP_392292796             304 aa            linear   BCT 20-JAN-2025
DEFINITION  quinone oxidoreductase family protein [Streptomyces sp.
            NPDC015414].
ACCESSION   WP_392292796
VERSION     WP_392292796.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015414
  ORGANISM  Streptomyces sp. NPDC015414
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 304)
  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 304)
  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 304)
  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   4  (residues 1 to 304)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptomyces sp. NPDC015414"
                     /db_xref="taxon:3364957"
     Protein         1..304
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=31491
     Region          1..304
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 mrrvryesag gplfveeaav pepgagellv rceavgvtlp vvrkvaeaae pvplggevag
       61 tvvaagegvs rfrtgdrvtg lcfghgyadf allreamasp vpdhatcvda vallrsglva
      121 lgvldaagpv rgqavlvtaa asgvgqlavr larvrgarrv vgavsdpaka gfvrslgadd
      181 cvrygderwg epydcvldav ggdllapala alaphgrlay ssgggtvray dllvgaksvi
      241 gfqmaliarg rpelyerwrr elwrlfsdgt lkpavhgefa ledaakahea iaartnlgkv
      301 vlrp
//
LOCUS       WP_392293860             340 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces sp. NPDC015414].
ACCESSION   WP_392293860
VERSION     WP_392293860.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015414
  ORGANISM  Streptomyces sp. NPDC015414
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Streptomyces sp. NPDC015414"
                     /db_xref="taxon:3364957"
     Protein         1..340
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33881
     Region          70..334
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mrkdvvpvss psplpplspp agpppcppar rvslpaarpv rlvlclspvl lagcwaladr
       61 pvasegasrl aaadpgwlla gaaltcltwv aaacvrqgsl pdklppglll asqfaagaan
      121 hvlpgglgah avtlrflrar gvpldratas iglyslarsv trtlvllafl aacparrrlg
      181 elvpdgpvpv paaavaggal avagvlltvv ppvrrpvtgl vraaladara vhgrpcrvla
      241 lwggsaampl vqagtlvcvg tslglglpwe qvvlahlaag tavgavpapg glavdaalvs
      301 fgavpavaaa tvighrvlnd wlpllpgalt lsaliraral
//
LOCUS       WP_392294111             253 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces sp.
            NPDC015414].
ACCESSION   WP_392294111
VERSION     WP_392294111.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015414
  ORGANISM  Streptomyces sp. NPDC015414
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616714
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptomyces sp. NPDC015414"
                     /db_xref="taxon:3364957"
     Protein         1..253
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26713
     Region          13..248
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 mdvrttvera qrlgrlhaey kplvlptvwd vwsaraaaaa gfpaltigsh pladsrgaad
       61 qegqtfeevl aavrpiieav dipvsvdles gygrtpaeli tglteaggag lniedtvhse
      121 ggrvrstqeh adyvaglraa addkgipvwv ngrtdlfkha adasavldea ierlraleea
      181 gadsvypvgi qdndellaav tgavavpvns tahpgkhdld rfrrlgvgri tngpllqval
      241 advmkdmlgp wrp
//
LOCUS       WP_392294385             359 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: quaternary amine ABC transporter ATP-binding protein
            [unclassified Streptomyces].
ACCESSION   WP_392294385
VERSION     WP_392294385.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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   4  (residues 1 to 359)
  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 359)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..359
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39149
     Region          3..338
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 mqprleaehl fkvfgrrpdq aveklregtd reelradgtt aavidasfqv eageifvvmg
       61 lsgsgkstll rmlngllept agrvrfdgrd ltglgdrelr elrsrkismv fqhfalfphr
      121 svrdnaaygl svqgvpraer erradealal cglagwedsw pdelsggmqq rvglaralat
      181 dadlllmdes fsaldplirr dmqdqllelq ktlkktivfi thdlneamrl gdrvavmrdg
      241 rivqtgtaed illrpaddyv asfikdvdrs rvltaaavmd tdvrgdeadc gcetaapgtp
      301 ftelcaisar lshpvavlda grelvgvvpr qrllgllgde qgdptacdnd nggkviara
//
LOCUS       WP_392294425             233 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase family protein [unclassified
            Streptomyces].
ACCESSION   WP_392294425
VERSION     WP_392294425.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 233)
  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 10007985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..233
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24367
     Region          33..223
                     /region_name="COG3786"
                     /note="L,D-peptidoglycan transpeptidase YkuD,
                     ErfK/YbiS/YcfS/YnhG family [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443000"
ORIGIN      
        1 mrqgvvlalv sasvcvlgvs prhgpeplpa rmadtgggtq litasapgtg stsgtvtwwd
       61 lrdgqwveag saparfgang lveggarrqg tdttptglyg ipfgfgikaa pagtrveyrp
      121 vtaaswwcqd ndsasynrwt eplpadcraa qseklssydp qygyalvigf nydrpvrgrg
      181 agiflhvngk aatagcvsvp edamrkilsw adparephva igtedgatav try
//
LOCUS       WP_392295074             414 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [unclassified Streptomyces].
ACCESSION   WP_392295074
VERSION     WP_392295074.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 414)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..414
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43689
     Region          75..256
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          262..388
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mnvrpisgas vggrrfgrkg lvlisgallv avtacggggd resgtgagdg kgqdagtrqs
       61 eqstaavsis pksgatgvdt sgalkvsvak gkltevtvkd tkgakvdgav tgdgaawkps
      121 thlaagtkys vhavakdsag reaaedssft tltprntfvg yftpedgstv gvgmpfsvrf
      181 trgitspadv ekaisvrtep pvdveghwfg ndrldfrpek ywkegtkvtv dlnldgvegr
      241 dgvygkqrkt vkftigrnqv svvdakkhtm kvtqdgkvvk tipvttgkpg yetwngqmvm
      301 seklavtrmn getvgyggey dikdvphair ltnsgtfvhg nywgggafgn ynashgcvgl
      361 rdvrggydkg vpaawffnhs mlgdvvvvkh shdrtvapdn glngwnmswe dwkk
//
LOCUS       WP_392295179             415 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Streptomyces sp.
            NPDC015414].
ACCESSION   WP_392295179
VERSION     WP_392295179.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015414
  ORGANISM  Streptomyces sp. NPDC015414
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  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 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   3  (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   4  (residues 1 to 415)
  AUTHORS   Igarashi,K., Ito,K. and Kashiwagi,K.
  TITLE     Polyamine uptake systems in Escherichia coli
  JOURNAL   Res Microbiol 152 (3-4), 271-278 (2001)
   PUBMED   11421274
REFERENCE   5  (residues 1 to 415)
  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   6  (residues 1 to 415)
  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 11430824
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces sp. NPDC015414"
                     /db_xref="taxon:3364957"
     Protein         1..415
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0019808 - polyamine binding [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:0015846 - polyamine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45584
     Region          28..413
                     /region_name="PotD"
                     /note="Spermidine/putrescine-binding periplasmic protein
                     [Amino acid transport and metabolism]; COG0687"
                     /db_xref="CDD:440451"
ORIGIN      
        1 meqyepdrlt ppqaaamrrs lrngraamtr rsllrasagg altvgglgal sgcgipaagk
       61 tqggtsaqdh saqekvvnfs nwteyidvdd sgkrhptlet frrrtgitvk ytedindnne
      121 ffgkikpqla agqatgrdli vltdwlaarl irlgwvqkld psnlphaytn lspqfrdpdw
      181 dpgraysypw qgiptviayn kkaldgievk svsdlldnpk lkgrvsflse mrdsigmtll
      241 dmgkdpakft dddfdavtar lqkavdkgqi rrftgndyts dltkgdivac vawagdvvql
      301 kadspdvdfv ipdsgymtst dnllvpnkar hktnaerlid fyyepqqaae laayinyatp
      361 vdgvkpylak idndaannpl ivpdkamqak shsfrslsqk eetayeekfa kltga
//
LOCUS       WP_392295571             215 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LutC/YkgG family protein [unclassified Streptomyces].
ACCESSION   WP_392295571
VERSION     WP_392295571.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..215
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22999
     Region          2..212
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 msgrerilgr vrraladlpa derpyeeava raylrehgdr tagqtvella enladyravv
       61 hrteaghlpe llarllaarg servlvppgl ppgwlaaagp trvhdraast areldrvdsv
      121 vtgcavaiae tgtlvldgsp dqgrrritli pdhhicvvrv pdqvvasvpq algrldparp
      181 ltwisgpsat sdieldrveg vhgprtlevv lmsgt
//
LOCUS       WP_392297140             341 aa            linear   BCT 20-JAN-2025
DEFINITION  heme/hemin ABC transporter substrate-binding protein [Streptomyces
            sp. NPDC015130].
ACCESSION   WP_392297140
VERSION     WP_392297140.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015130
  ORGANISM  Streptomyces sp. NPDC015130
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Naoe,Y., Nakamura,N., Rahman,M.M., Tosha,T., Nagatoishi,S.,
            Tsumoto,K., Shiro,Y. and Sugimoto,H.
  TITLE     Structural basis for binding and transfer of heme in bacterial
            heme-acquisition systems
  JOURNAL   Proteins 85 (12), 2217-2230 (2017)
   PUBMED   28913898
REFERENCE   2  (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   3  (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   4  (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   5  (residues 1 to 341)
  AUTHORS   Ho,W.W., Li,H., Eakanunkul,S., Tong,Y., Wilks,A., Guo,M. and
            Poulos,T.L.
  TITLE     Holo- and apo-bound structures of bacterial periplasmic
            heme-binding proteins
  JOURNAL   J Biol Chem 282 (49), 35796-35802 (2007)
   PUBMED   17925389
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Streptomyces sp. NPDC015130"
                     /db_xref="taxon:3364940"
     Protein         1..341
                     /product="heme/hemin 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=33848
     Region          72..339
                     /region_name="ChuT"
                     /note="ABC-type hemin transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG4558"
                     /db_xref="CDD:443619"
ORIGIN      
        1 mrrtrlagal tavlalalaa tgcgdgggsg tggttpggap aaqaasaapd rveplaapaa
       61 prlpvtvpsa dgravtvast drivplsgsl neivftlglg gkvvardita tfeqaaglpv
      121 vtrahdvsae svlslrptvv laesttgpae avaqirdagi plvvvkpake ladvgtrida
      181 vaaalgvrds gtalkdrteq ridaarngvp alpekprvaf lyvrgsaavy llggagsgas
      241 slleaagavd agkesgltkd ftpltseala qaapdailvm rkglesvggv dglvklpgva
      301 qtpagagrrv vsvddgvlln ygprtdqvlk slvgqlyger k
//
LOCUS       WP_392297180             258 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces sp.
            NPDC015130].
ACCESSION   WP_392297180
VERSION     WP_392297180.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015130
  ORGANISM  Streptomyces sp. NPDC015130
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Streptomyces sp. NPDC015130"
                     /db_xref="taxon:3364940"
     Protein         1..258
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=27359
     Region          1..243
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mkidmlgpfs aaiagvpiap sarkprrila llalhagqav pvsavvdevw gaaaapkahm
       61 tvqtyvlqlr nsigqalkdp raardvlvtr pgsyallage davdvhtydr lcargqsafe
      121 tgddaaaaal frealalwkg raldgvqdgp algleamrle qsrtdvlerc ltaelrlgag
      181 erllpelsal veehphheal hgllmtalar sgrvsgalsv yesvtarlde rfgllpspdl
      241 mrlgeelrql agqashha
//
LOCUS       WP_392297281             393 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC015130].
ACCESSION   WP_392297281
VERSION     WP_392297281.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015130
  ORGANISM  Streptomyces sp. NPDC015130
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 393)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Streptomyces sp. NPDC015130"
                     /db_xref="taxon:3364940"
     Protein         1..393
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=40796
     Region          53..236
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          241..361
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mlpirtprsv lvavalgvsl tacsaqaasg pgagpakage pgaaaapakv tvvdpaagrp
       61 vsvtasggtl avvkvadaeg gvlsgrtgag gtswtsdrka vpgtsytvev tsrtadgkes
      121 ttrssfetpe pkavnkltla pgknttvgig hplsivfdlp vtkkadverq lkvttsnate
      181 gswgwvkdws grdradwrpk eywkpgtkvt lqadldgtds gggwfvrdyr tgftvgaaqv
      241 vkvdldrqkl tlerdgravr tipvsggtpg gdkrswrgta vlmakegtin mnsetvglgd
      301 aydkmvdhsm rltwsgmyah aapwnaayfg kanrssgcig msdanaasfy asvnvgdpfe
      361 itgrdtkgtv aegngygawn lswaqwkaks alg
//
LOCUS       WP_392297921              88 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015130].
ACCESSION   WP_392297921
VERSION     WP_392297921.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015130
  ORGANISM  Streptomyces sp. NPDC015130
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 88)
  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 88)
  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 88)
  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 11448557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Streptomyces sp. NPDC015130"
                     /db_xref="taxon:3364940"
     Protein         1..88
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9458
     Region          1..61
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
ORIGIN      
        1 mieeserlak alielreaeg ltvrelahlt glsqatimah erdggcpplp faarrfeevl
       61 gwapgsiptp areitdlelp pfpgtlae
//
LOCUS       WP_392298249             275 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces sp.
            NPDC015130].
ACCESSION   WP_392298249
VERSION     WP_392298249.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015130
  ORGANISM  Streptomyces sp. NPDC015130
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616714
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Streptomyces sp. NPDC015130"
                     /db_xref="taxon:3364940"
     Protein         1..275
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27715
     Region          11..246
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 mtnlvdkarl frslhvpgkp lvlpnawdaa sarvvaeaga savattsagv awslghgdgd
       61 hlnrdealga iariaaavdv pvtadiergy atdpagvaet vrgvlaagav gvnledslrp
      121 vaeqaeriaa arraadeagv plfvnaridt hrlpsedrsa wlaetlvrar ayaaagadgv
      181 fvlggldaat igllvdgspl pvnvaagpga lpvpalaqag aarvsagssi aeaayglvrr
      241 aarellaqgt tdaledgfdy atlnallltd rtaes
//
LOCUS       WP_392298379             288 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015130].
ACCESSION   WP_392298379
VERSION     WP_392298379.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015130
  ORGANISM  Streptomyces sp. NPDC015130
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   3  (residues 1 to 288)
  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 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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces sp. NPDC015130"
                     /db_xref="taxon:3364940"
     Protein         1..288
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32036
     Region          22..84
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          105..283
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 msvdeangaa vedtgwevdp gdepgaavva tvgrqirlwr etkglrpaef geligysedl
       61 irkvergdri prpefldkad galgagglia gmrndlmevr ypkkvrdlak legravefcm
      121 ysnfdvhgll qteefsrail rtwrpaygpe elerflsarv arrsvlektp apefsfvqee
      181 vslrrpiggr mvlrrqlehl levgelpnve iqvmpterad hpatggrial lkfgdgtavg
      241 rmdgdfggrp vsdlkrlril elrygiirsk altpaesrdf ieqllget
//
LOCUS       WP_392298608             487 aa            linear   BCT 20-JAN-2025
DEFINITION  alpha,alpha-trehalose-phosphate synthase (UDP-forming)
            [Streptomyces sp. NPDC015130].
ACCESSION   WP_392298608
VERSION     WP_392298608.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015130
  ORGANISM  Streptomyces sp. NPDC015130
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 487)
  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 487)
  AUTHORS   Eastmond,P.J. and Graham,I.A.
  TITLE     Trehalose metabolism: a regulatory role for trehalose-6-phosphate?
  JOURNAL   Curr Opin Plant Biol 6 (3), 231-235 (2003)
   PUBMED   12753972
REFERENCE   3  (residues 1 to 487)
  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   4  (residues 1 to 487)
  AUTHORS   Elbein,A.D., Pan,Y.T., Pastuszak,I. and Carroll,D.
  TITLE     New insights on trehalose: a multifunctional molecule
  JOURNAL   Glycobiology 13 (4), 17R-27R (2003)
   PUBMED   12626396
REFERENCE   5  (residues 1 to 487)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 929-939 (1997)
   PUBMED   9334165
  REMARK    Erratum:[Biochem J 1998 Feb 1;329(Pt 3):719]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Streptomyces sp. NPDC015130"
                     /db_xref="taxon:3364940"
     Protein         1..487
                     /product="alpha,alpha-trehalose-phosphate synthase
                     (UDP-forming)"
                     /EC_number="2.4.1.15"
                     /GO_function="GO:0003825 - alpha,alpha-trehalose-phosphate
                     synthase (UDP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0005992 - trehalose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=53497
     Region          1..487
                     /region_name="OtsA"
                     /note="Trehalose-6-phosphate synthase, GT20 family
                     [Carbohydrate transport and metabolism]; COG0380"
                     /db_xref="CDD:440149"
ORIGIN      
        1 matvlvasnr gpvsyklged gtltprrggg glvsglsavs addsqeslwv caalgegdre
       61 avrrgvgepg vrmldippdv yadayngian svlwflhhhl ydisrepvfd aefrrrwesy
      121 raynrafaea laaeasegae vlvqdyhlal vpgmlrdlrp dlriahftht pwgspaylgm
      181 lpddireelv wgmlgadelg fhtwqwaaaf vsgasmdter gvaqglsptg tpwrgvehlr
      241 ygvgkgrttv rayplgvdae elralahrpe vdeklaalra evgdrrtivr vdrtelskni
      301 lrgllayrel ltthpewrdr vvhlasayps rqdlesyrsy taavrtlaee intefgtagw
      361 qpvlvsvqdd fprslaayrl advalvnpvr dgmnlvakei pvvseagcal vlsreagayt
      421 elrddaltvn pfdvsetaea lhtalsmpps ersdrtkrla aaatalppqr wflaqlealr
      481 epmqppa
//
LOCUS       WP_392299108             386 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC015130].
ACCESSION   WP_392299108
VERSION     WP_392299108.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015130
  ORGANISM  Streptomyces sp. NPDC015130
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 386)
  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 386)
  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
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 386)
  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   5  (residues 1 to 386)
  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   6  (residues 1 to 386)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 386)
  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 20283677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces sp. NPDC015130"
                     /db_xref="taxon:3364940"
     Protein         1..386
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38715
     Region          19..64
                     /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(33,35..37,46)
                     /site_type="other"
                     /note="non-specific DNA interactions [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            46..52
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            order(47..48,52)
                     /site_type="other"
                     /note="sequence specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238044"
     Site            47..48
                     /site_type="other"
                     /note="putative cAMP binding site [chemical binding]"
                     /db_xref="CDD:238044"
     Region          84..380
                     /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 myakglggvn vpalrshnaa lvldllrtag esgisrlela ertgltpqav skitarlrte
       61 glaaeaghra stggkprtvl rlepsaghav gvhldrdelt tlltdlagtv vtlrrrpvnl
      121 gagagpvlda vteevrallg eggrepageg greplgeggr esageggrep agpgprpvlg
      181 vgvampgpld hragmpgrvt gfpswdgypv rdelarrlgl pvvldkdtna aalglalrpg
      241 apgsfayvhl gtglgaglvl ggaplrgart gagelghqav qldgppcdcg grgclevlcl
      301 aavargelpg aarilgagaa nlvrlldidq vllggrvvlg apevfadgvr evlarlglpt
      361 pvavasapqa vavgaawlvl apifgq
//
LOCUS       WP_392300123             301 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Streptomyces sp. NPDC015130].
ACCESSION   WP_392300123
VERSION     WP_392300123.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015130
  ORGANISM  Streptomyces sp. NPDC015130
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Streptomyces sp. NPDC015130"
                     /db_xref="taxon:3364940"
     Protein         1..301
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32166
     Region          1..295
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mlldtaslyf rayfgvpdsv rapdgtpvna vrglldfitr lvqdhrpdel vacwdedwrp
       61 qwrvdlipsy kahrvvvete tgpdveeipd tlspqvpvie dvlaalgiar vgsagyeadd
      121 vigtlagraa gpvdivtgdr dlfqlvddar gvrvlyprkg vgdcdlvdde lirtkygvrp
      181 dqyadfaalr gdasdglpgv kgigektaaq liteygdlag vraaaedrts kltpakrrgi
      241 veaaayldva ptvvrvagdv plpefdpalp taprdpaald alvkrwglgg avgrllpvla
      301 r
//
LOCUS       WP_392300695             388 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015130].
ACCESSION   WP_392300695
VERSION     WP_392300695.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015130
  ORGANISM  Streptomyces sp. NPDC015130
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 388)
  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 388)
  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 388)
  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 10611723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Streptomyces sp. NPDC015130"
                     /db_xref="taxon:3364940"
     Protein         1..388
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=37886
     Region          17..78
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Region          286..364
                     /region_name="DUF2690"
                     /note="Protein of unknown function (DUF2690); pfam10901"
                     /db_xref="CDD:402475"
ORIGIN      
        1 mpgwkalsde ldpdvrafae rlrrlidrsg lgvtavaert ghdrslwdac ldgrrpvprt
       61 alaglaevtg tdagdlaadw eraerawarn rhpdeardsg raggaggsgg asaaggsdgs
      121 dgsdgssasg gsggasaasa aggsdesdes desggsdgas aaggaagveg gdaadgprdd
      181 rtmqirrlep aptpspspsp spspspsptp tsdsappsrp rrtlllyvta glgallvvta
      241 avllvdlggt gdgtddrata ppsptaptaa pstdlpagvk csgagctgrd peamgcggpl
      301 attvararsg tvlvevrhse tcaaawaris gaapgetvtv kvagatrras vpapadtday
      361 tpmlavtaaa datacatlad gtetctan
//
LOCUS       WP_392300745             346 aa            linear   BCT 20-JAN-2025
DEFINITION  BMP family lipoprotein [Streptomyces sp. NPDC015130].
ACCESSION   WP_392300745
VERSION     WP_392300745.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015130
  ORGANISM  Streptomyces sp. NPDC015130
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Yousief,S.W., Bahey-El-Din,M. and Zaghloul,T.I.
  TITLE     Immunization with the basic membrane protein (BMP) family ABC
            transporter elicits protection against Enterococcus faecium in a
            murine infection model
  JOURNAL   Microbes Infect 22 (3), 127-136 (2020)
   PUBMED   31585177
REFERENCE   2  (residues 1 to 346)
  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   3  (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   4  (residues 1 to 346)
  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   5  (residues 1 to 346)
  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 11448319
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Streptomyces sp. NPDC015130"
                     /db_xref="taxon:3364940"
     Protein         1..346
                     /product="BMP family lipoprotein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /calculated_mol_wt=35222
     Region          34..343
                     /region_name="Med"
                     /note="Lipoprotein Med, regulator of KinD/Spo0A, PBP1-ABC
                     superfamily, includes NupN [Signal transduction
                     mechanisms]; COG1744"
                     /db_xref="CDD:441350"
ORIGIN      
        1 mrrvskitaa cavtaalalt atacgesste dtgsdsgsik vgmaydvggr gdnsfndsaa
       61 rgldkakadl gvetkeltak tgetpadreq rltslaeggf npvigvgfay kdaidkvaak
      121 fpkttfglvd svseaknvds ivfteeqgsy lagvaaalks kdgkigfigg vdtplikkfa
      181 agfqqgvkdt kpnasvtiqy lstgtdfsgf gapdkgkaaa kgmldkgidv iyaaaggsga
      241 gsieavaakp gawaigvdsd qakdpalsky agsimtsmvk nvdtgvfeli ksvdegkpat
      301 gvhtyslaed gvsltttgdh lkdiqaqide akkkivdgqi kvattl
//
LOCUS       WP_392301048             415 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Streptomyces sp.
            NPDC015130].
ACCESSION   WP_392301048
VERSION     WP_392301048.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015130
  ORGANISM  Streptomyces sp. NPDC015130
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  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 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   3  (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   4  (residues 1 to 415)
  AUTHORS   Igarashi,K., Ito,K. and Kashiwagi,K.
  TITLE     Polyamine uptake systems in Escherichia coli
  JOURNAL   Res Microbiol 152 (3-4), 271-278 (2001)
   PUBMED   11421274
REFERENCE   5  (residues 1 to 415)
  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   6  (residues 1 to 415)
  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 11430824
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces sp. NPDC015130"
                     /db_xref="taxon:3364940"
     Protein         1..415
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0019808 - polyamine binding [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:0015846 - polyamine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45135
     Region          28..413
                     /region_name="PotD"
                     /note="Spermidine/putrescine-binding periplasmic protein
                     [Amino acid transport and metabolism]; COG0687"
                     /db_xref="CDD:440451"
ORIGIN      
        1 meqyepesls aaqlaamrrs mtngrgalsr rsmlraggvg altvgglagl sacgippakr
       61 egqgpastdl sakeksiafs nwteymdise deksrptlea ftkrtgikvk ytedindnve
      121 ffgkikpqla agqdtgrdli cvtdwlaarm irlgwaqrld panlpnafan lsaqfrrpdw
      181 dpgraysypw tgistviayn skatggkkvd svtqllddps lkgrvgflte mrdtvgmtll
      241 dmgkdpgkft daeydeaigr lqkavdkkqi rrftgndyts dldkgdlaac lawagdviql
      301 qadnpdikfa ipsagyitss dnllvpaqak hkanaeklid hyyelpvaaq laayinyvcp
      361 vdgvkdelak idpelanntl ilpdkamakk srafrsltsa eetayeekfa kliga
//
LOCUS       WP_392303096             289 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC014889].
ACCESSION   WP_392303096
VERSION     WP_392303096.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014889
  ORGANISM  Streptomyces sp. NPDC014889
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415139
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces sp. NPDC014889"
                     /db_xref="taxon:3364928"
     Protein         1..289
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=30919
     Region          1..260
                     /region_name="LysX"
                     /note="Glutathione synthase, LysX or RimK-type ligase,
                     ATP-grasp superfamily [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism,
                     Translation, ribosomal structure and biogenesis, Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0189"
                     /db_xref="CDD:439959"
ORIGIN      
        1 mprialvtcr papgisddrd lpvlvealae agaearavaw ddpgtdwggf dlavirstwd
       61 yswrvaefte waercakatr lanpvdvvrw nvdkrylgql gaagvpvvpt rylapgdpad
      121 lpdgheyvik pasgagarfa aryapgerdt avrqlarmha egltamvqpy mrridagger
      181 alqffggrll hagrkgavla pgvayderka ahpgiapwtp tpaelavaer alaavpgape
      241 llfarvdlvd gedgeprlme lelvepnlfl wlhpesvaav trailaaag
//
LOCUS       WP_392304585            1458 aa            linear   BCT 20-JAN-2025
DEFINITION  Rne/Rng family ribonuclease [Streptomyces sp. NPDC014889].
ACCESSION   WP_392304585
VERSION     WP_392304585.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014889
  ORGANISM  Streptomyces sp. NPDC014889
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1458)
  AUTHORS   Kime,L., Jourdan,S.S. and McDowall,K.J.
  TITLE     Identifying and characterizing substrates of the RNase E/G family
            of enzymes
  JOURNAL   Methods Enzymol 447, 215-241 (2008)
   PUBMED   19161846
REFERENCE   2  (residues 1 to 1458)
  AUTHORS   Callaghan,A.J., Marcaida,M.J., Stead,J.A., McDowall,K.J.,
            Scott,W.G. and Luisi,B.F.
  TITLE     Structure of Escherichia coli RNase E catalytic domain and
            implications for RNA turnover
  JOURNAL   Nature 437 (7062), 1187-1191 (2005)
   PUBMED   16237448
REFERENCE   3  (residues 1 to 1458)
  AUTHORS   Li,Z., Pandit,S. and Deutscher,M.P.
  TITLE     RNase G (CafA protein) and RNase E are both required for the 5'
            maturation of 16S ribosomal RNA
  JOURNAL   EMBO J 18 (10), 2878-2885 (1999)
   PUBMED   10329633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1458
                     /organism="Streptomyces sp. NPDC014889"
                     /db_xref="taxon:3364928"
     Protein         1..1458
                     /product="Rne/Rng family ribonuclease"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=153047
     Region          697..1097
                     /region_name="CafA"
                     /note="Ribonuclease G or E [Translation, ribosomal
                     structure and biogenesis]; COG1530"
                     /db_xref="CDD:441139"
     Region          <1203..1367
                     /region_name="rne"
                     /note="ribonuclease E; Reviewed; PRK10811"
                     /db_xref="CDD:236766"
ORIGIN      
        1 mleptepivg seelntpsdt lpprrrrraa srpagppaaa sseaaaeita pavpaaaaae
       61 laeqveetpg taeaaeaepa vvagedteet egaeeaaeaa aeeaaparrt rrrasapagt
      121 pkategeaaa etvvqaaava etpatgsgav etpagsvevg eaaaprrtrr ratrsvttpa
      181 asteaveaav paaptesaep rtsvetvaep aaeapepaar trrratrrvs apatsaapae
      241 etvpqaaatg epaaeaeget vgedaaprrt rrratrrvse paaapvsvaa esasaapaae
      301 aqagaaaeta atetgtaere sdaevvedaa prrtrrratr rvsepaaqta avseapears
      361 devpgegeap aevtpaaees gtrrsrrrvv rraatgfsep aaestagdge strrparpav
      421 avfqapvfte pmfqtperaa aaaaaeaaes eelpeeqpeq veqtehsdqg gsrrrrrrrg
      481 sggeesetrt aatadesaed eseeesaesa ddavegedge esgsrrrrrr ggrrrrrges
      541 aeagedaees delaaeqaaq daedtaeqld edeedasgae dsadedegrq ggggssssrr
      601 rrrrrrragd gagegepsad dpertvvkvr eprkaaepsd evqsikgstr leakkqrrre
      661 greqgrrrvp iiteaeflar reavervmav rqhgdrtqig vledgvlveh yvnkeqstsy
      721 vgnvylgkvq nvlpsmeaaf idigkgrnav lyagevnfea lgmangprri esalksgqsv
      781 lvqvtkdpig hkgarltsqv slpgrylvyv pegsmtgisr klpdterarl ktilkkivpe
      841 dagvivrtaa egasedelrr dverlqsqwe dikkkakggs ssapsllyge pdmtvrvvrd
      901 ifnedfskvi vsgdeaweti hgyvshvapd laprlqrwts evdvfatyri deqlakaldr
      961 kvwlpsggsl vidrteamvv idvntgkftg qggnleetvt rnnleaaeei vrqlrlrdlg
     1021 giividfidm vlesnrdlvl rrlleclgrd rtkhqvaevt slglvqmtrk rvgqgllesf
     1081 setcvhcngr gvivhleqps agggggskrr kraragaeqp heheavaaev vaptaeeeae
     1141 teseaagpit lpalemapde elyssvaeae aaasrgrtrr rasrrasapa gapkahadgg
     1201 apaptaqdvt aaeeaarpvl pepaeqaqae pvavedptvp avaeeaapkg rarrratrkv
     1261 sapagspega easvvtvpea apaapaeard tvgeaaevpa aqpeapaesa aparprrrav
     1321 rkataptape dtavvvvpsg taeeavaqdt rnavtesaep aaeqaavdpe saetaaeeav
     1381 pakktarkva kkatakkaat kkavakkttt akktaakkat akkaaktakt ataakksask
     1441 ktaaaeqssp svsasted
//
LOCUS       WP_392304747             349 aa            linear   BCT 20-JAN-2025
DEFINITION  BMP family lipoprotein [Streptomyces sp. NPDC014889].
ACCESSION   WP_392304747
VERSION     WP_392304747.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014889
  ORGANISM  Streptomyces sp. NPDC014889
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Yousief,S.W., Bahey-El-Din,M. and Zaghloul,T.I.
  TITLE     Immunization with the basic membrane protein (BMP) family ABC
            transporter elicits protection against Enterococcus faecium in a
            murine infection model
  JOURNAL   Microbes Infect 22 (3), 127-136 (2020)
   PUBMED   31585177
REFERENCE   2  (residues 1 to 349)
  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   3  (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   4  (residues 1 to 349)
  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   5  (residues 1 to 349)
  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 11448319
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Streptomyces sp. NPDC014889"
                     /db_xref="taxon:3364928"
     Protein         1..349
                     /product="BMP family lipoprotein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /calculated_mol_wt=35451
     Region          37..347
                     /region_name="Med"
                     /note="Lipoprotein Med, regulator of KinD/Spo0A, PBP1-ABC
                     superfamily, includes NupN [Signal transduction
                     mechanisms]; COG1744"
                     /db_xref="CDD:441350"
ORIGIN      
        1 mrrvsriava svataalavt vsacgsssss sssgggdknl glalaydvgg kgdqsfndaa
       61 tagmekadqe fgykstakep qdgesdadkv qrletlakqg ynpvvgvgfa yapavkaaaa
      121 kfpkttfgiv ddstitasnv adlvfheeqa sylagvaaak ttksntvgfi ggvdvplihk
      181 feagfkqgva dtkkgvtvks qyltqtaeeg gfaspdkgen aangqidaga dvvyaaagls
      241 gqgvikaase hkvwaigvds dqyqqgalak ykdsiltsam kdvsgavynl aksvkdgkpq
      301 tgevraslat ggvslsdsnp vfknnaglqk aikkaeeaik sgsitvkds
//
LOCUS       WP_392304971             933 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces sp. NPDC014889].
ACCESSION   WP_392304971
VERSION     WP_392304971.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014889
  ORGANISM  Streptomyces sp. NPDC014889
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 933)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 933)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..933
                     /organism="Streptomyces sp. NPDC014889"
                     /db_xref="taxon:3364928"
     Protein         1..933
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=99660
     Region          657..930
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mkqqgvhpdd aegtsgassr pgtggtqapk aqdtdapkad rkpaeedavt hadeiegdep
       61 llparvhrps dlmrllvgvl aivvllaiag fahgttsgle qdinkgtgqa pdllikiagl
      121 assiaillvp vafaierlik rdglriadgv laavlahgvt latdlwvakg aphsiqdalt
      181 qpspsnvhal tdpvhgylap viaymtavgm srrprwrsvl wivllldafs mlvtgyttpf
      241 siiltvligw tiaygtlyav gspnvrptgr tlvarlrtvg fhpvsaaree vtetadngdr
      301 grryfvtled gppldvtvvd reqqaqgffy rvwrnltlrg fatrrslqsl rqaleqeall
      361 ayaaiaagan apkliatsel gpdavmlvye htggrtldsl adeeitdell hrtweqvral
      421 qsrriahrrl agdailvdrs rrviltdlrg geiaagdlll rmdiaqlltt lglrvgaers
      481 vasavgvlgp davadclpml qpialtrstr atlrrlarer aqrereavle tsqqakqarl
      541 eqaaqdtgga gpvslekpee pekaektgkp dkkdkkaera earaekraig ealeeareed
      601 lltqirhqvl rirpqapvep arlerirprt lisfiagaig ayylltqlth iefgtlvaha
      661 qwgwviaavl fsalsyvaaa mallgfvper vpfvrtvaaq vagsfvkiva paavggvaln
      721 trflqragvr pglavasvga sqlfglgchi lmllsfgylt gtektpslsp srtviagllt
      781 vavlvlvvts vpflrkfvvt rvrslfagvv prmldvlqrp qklvtgiggm llltfcfvmc
      841 ldasirafgd qstsisiasv avvflagnal gsaaptpggv gaveatltvg liavglpkev
      901 aapavlmfrl ltlwlpvlpg wlafnhlsrk gal
//
LOCUS       WP_392305163             393 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC014889].
ACCESSION   WP_392305163
VERSION     WP_392305163.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014889
  ORGANISM  Streptomyces sp. NPDC014889
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 393)
  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 393)
  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
REFERENCE   3  (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   4  (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   5  (residues 1 to 393)
  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   6  (residues 1 to 393)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (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 20170230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Streptomyces sp. NPDC014889"
                     /db_xref="taxon:3364928"
     Protein         1..393
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39812
     Region          <10..>74
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          77..384
                     /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 mtarpanthq arllkllrdg gpssraqlgd rvelsrskla vevdrlletg lvvadglaas
       61 rggrrshnvr lapelrflgv digatsvdva vtnaelevlg hlnqpldvre gpvavfeqvl
      121 amaaklrasg laegydgagi gvpgpvrfpq gvpvappimp gwdgfpvrea lsqelgcpvm
      181 vdndvnlmam geqhagvars vgdflcvkig tgigcgivvg gevhrgttgs agdighiqav
      241 pdgrpcvcgn qgcleahfsg aalardalea aqqgrsaela trleangalt gvdvaaaaaa
      301 gdatclglir dggtrtgqvi aglvsffnpg lvvigggvtg lghtllaair tqvyrqslpl
      361 atgnlpivlg elgpaagvig aarlisdhlf spa
//
LOCUS       WP_392305798             476 aa            linear   BCT 20-JAN-2025
DEFINITION  alpha,alpha-trehalose-phosphate synthase (UDP-forming)
            [Streptomyces sp. NPDC014889].
ACCESSION   WP_392305798
VERSION     WP_392305798.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014889
  ORGANISM  Streptomyces sp. NPDC014889
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 476)
  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 476)
  AUTHORS   Eastmond,P.J. and Graham,I.A.
  TITLE     Trehalose metabolism: a regulatory role for trehalose-6-phosphate?
  JOURNAL   Curr Opin Plant Biol 6 (3), 231-235 (2003)
   PUBMED   12753972
REFERENCE   3  (residues 1 to 476)
  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   4  (residues 1 to 476)
  AUTHORS   Elbein,A.D., Pan,Y.T., Pastuszak,I. and Carroll,D.
  TITLE     New insights on trehalose: a multifunctional molecule
  JOURNAL   Glycobiology 13 (4), 17R-27R (2003)
   PUBMED   12626396
REFERENCE   5  (residues 1 to 476)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 929-939 (1997)
   PUBMED   9334165
  REMARK    Erratum:[Biochem J 1998 Feb 1;329(Pt 3):719]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Streptomyces sp. NPDC014889"
                     /db_xref="taxon:3364928"
     Protein         1..476
                     /product="alpha,alpha-trehalose-phosphate synthase
                     (UDP-forming)"
                     /EC_number="2.4.1.15"
                     /GO_function="GO:0003825 - alpha,alpha-trehalose-phosphate
                     synthase (UDP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0005992 - trehalose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51897
     Region          6..476
                     /region_name="OtsA"
                     /note="Trehalose-6-phosphate synthase, GT20 family
                     [Carbohydrate transport and metabolism]; COG0380"
                     /db_xref="CDD:440149"
ORIGIN      
        1 masthgaevl vasnrgpvsy qvredgslhs rrgggglvsg lsaigpeaga vwvcaalsda
       61 drqaagrfeg grrlpseaag gqqvrmldid arvfsdayng iansvlwfvh hmlyqtplep
      121 vfdaefrrrw ksyeaynlaf aealaeeaae gaavvvqdyh ltlvpgmlrd frpdvrighf
      181 shtpwapady frilpddiae qvlrgmlgad rlgfltrrwa dafagccdal vgglggtrig
      241 vhglgadaef lrershradv kermaalree igagpdggpr rtivrvdrte lsknivrglh
      301 ayrelleerp ewrervvhva faypsrqdla vyreytqevr rvaeeinary gtpgwtpvll
      361 hveddfarsl aayriadval vnpirdgmnl vakevpvvsd sgcalvlsre agayaelgdd
      421 avvvnpydvv gtagalhral smpgperaer tkrlaaaata lppaqwfldq lqelgg
//
LOCUS       WP_392306439             237 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Streptomyces sp.
            NPDC014889].
ACCESSION   WP_392306439
VERSION     WP_392306439.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014889
  ORGANISM  Streptomyces sp. NPDC014889
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 237)
  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 11440233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Streptomyces sp. NPDC014889"
                     /db_xref="taxon:3364928"
     Protein         1..237
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25720
     Region          3..230
                     /region_name="GCD1"
                     /note="NDP-sugar pyrophosphorylase, includes eIF-2Bgamma,
                     eIF-2Bepsilon, and LPS biosynthesis protein s
                     [Translation, ribosomal structure and biogenesis, Cell
                     wall/membrane/envelope biogenesis]; COG1208"
                     /db_xref="CDD:440821"
ORIGIN      
        1 mhavilaggk gvrlrpytta lpkplvpigd qhaileivlr qlstagfttc tiaighlgei
       61 irayvgdgsq wgmkvdyste dsplgtmgpl ltmldrlpet flvmngdvlt dldyadvlhr
      121 hrasgaplti atyarkvhid fgvlttdasr vvaftekpsl dyrvsmgvyg lsrstldgyt
      181 aglplgfdel vldlladgrp pyayefdgyw ldigrpddyd qanaefttrk slllkga
//
LOCUS       WP_392306470             399 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC014889].
ACCESSION   WP_392306470
VERSION     WP_392306470.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014889
  ORGANISM  Streptomyces sp. NPDC014889
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 399)
  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   5  (residues 1 to 399)
  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   6  (residues 1 to 399)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 399)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Streptomyces sp. NPDC014889"
                     /db_xref="taxon:3364928"
     Protein         1..399
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40582
     Region          14..77
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          77..379
                     /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 metpgsqssl hranlervvr avrlagsltq aeiarttgls aatvsnivre lkdggtvqvt
       61 ptsaggrrar svslsgdagi vigvdfghth lrvaignlah qvlaeesepl dvdassaqgf
      121 draeelvnrl vaatgvdhsk iagvgvgvpg pidvesgtlg stailpgwtg vrpaeelrgr
      181 lgvpvhvdnd anlgalgelv wgsgrgvrdl ayikiasgvg aglvingriy rgpggtagei
      241 ghitldesgp vcrcgnrgcl etftaagyvl pllrpshgtd ltmegvvrla rdgdpgcrrv
      301 iadvgrhigs gvanlcnlln psrvllggdl aeagelvlgp iresvgryai psaarqlsvl
      361 pgalggraev lgalalalse mgdstlldgt lhaatpaft
//
LOCUS       WP_392306613             234 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease H family protein [Streptomyces sp. NPDC014889].
ACCESSION   WP_392306613
VERSION     WP_392306613.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014889
  ORGANISM  Streptomyces sp. NPDC014889
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 234)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Streptomyces sp. NPDC014889"
                     /db_xref="taxon:3364928"
     Protein         1..234
                     /product="ribonuclease H family protein"
                     /EC_number="3.1.26.4"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=24466
     Region          8..143
                     /region_name="RNase_HI_prokaryote_like"
                     /note="RNase HI family found mainly in prokaryotes;
                     cd09278"
                     /db_xref="CDD:260010"
     Site            order(14..17,49..51,54,76,126)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260010"
ORIGIN      
        1 miepmrervv aacdgaskgn pgpagwawvv sddagspvrw eagalgtatn nvaeltaler
       61 lltatepdvp levrmdsqya mkavttwlpg wkrngwktaa gkpvanrelv vridellqgr
      121 svdfryvpah qvdgdplndf adraasqaas aqlsagsalg spepppsapv saaprrrang
      181 tstarprtgg sstrtikakf pgrcvcgrpy aagesiarnd qgwghpecra aaag
//
LOCUS       WP_392307483             270 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces sp.
            NPDC014889].
ACCESSION   WP_392307483
VERSION     WP_392307483.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014889
  ORGANISM  Streptomyces sp. NPDC014889
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616714
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Streptomyces sp. NPDC014889"
                     /db_xref="taxon:3364928"
     Protein         1..270
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26830
     Region          12..230
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 mtssqsakar lfrslhtsta plalanawdv asarvvesag asaiattsag vawslgspdg
       61 dalgcdqalg lisrvaaava vpvtadiegg ygqdaaevae tvtevlaaga vgvniedgtr
      121 apaelatrla aarraaerag gelflnarvd tyllglgdpd trleetlara rryvdagadg
      181 vfvpgvtdta tiaalaegvs vplnvmagpg algvaelgal gvarvslgpg vaqaayaaar
      241 raarelfdtg gydslsgglt fpelntllsk
//
LOCUS       WP_392308370             305 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces sp. NPDC014889].
ACCESSION   WP_392308370
VERSION     WP_392308370.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014889
  ORGANISM  Streptomyces sp. NPDC014889
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Streptomyces sp. NPDC014889"
                     /db_xref="taxon:3364928"
     Protein         1..305
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=31000
     Region          31..299
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mrqvlcllpv llvavaavrh rsvlaegfah lrtaewpwll aavgttcltw vaaavtrqga
       61 vvqrlprrrl latqfaagaa nhllptglga savnlrfltv cgvslarssa alalymlaes
      121 varlallaal llafpdalrl ggllpsgvag pllytvggvl vaaagaawcv rrlrtavaaf
      181 vrtalsears vhsrparala lwggslafpa lqavslvavg ralslpvpsv ymalaylaat
      241 tavalvptpg gigsveaalv valvaaggpa avvtavvvay riitvwlpll pgaltlgalv
      301 rlkvi
//
LOCUS       WP_392308563             478 aa            linear   BCT 20-JAN-2025
DEFINITION  SWIM zinc finger family protein [Streptomyces sp. NPDC014889].
ACCESSION   WP_392308563
VERSION     WP_392308563.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014889
  ORGANISM  Streptomyces sp. NPDC014889
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Hassan,I.U., Rehman,H.M., Liu,Z., Zhou,L., Samma,M.K., Wang,C.,
            Rong,Z., Qi,X., Cai,D. and Zhao,H.
  TITLE     Genome-wide identification and spatiotemporal expression profiling
            of zinc finger SWIM domain-containing protein family genes
  JOURNAL   Zool Res 44 (3), 663-674 (2023)
   PUBMED   37161653
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     SWIM, a novel Zn-chelating domain present in bacteria, archaea and
            eukaryotes
  JOURNAL   Trends Biochem Sci 27 (8), 384-386 (2002)
   PUBMED   12151216
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10516955
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Streptomyces sp. NPDC014889"
                     /db_xref="taxon:3364928"
     Protein         1..478
                     /product="SWIM zinc finger family protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50314
     Region          <424..446
                     /region_name="SWIM"
                     /note="SWIM zinc finger; pfam04434"
                     /db_xref="CDD:309540"
ORIGIN      
        1 mtrslqavay rrpsvlessg ggqllglets rgatpsgvqd hprffsgflt spqvasagll
       61 avadvaaary yqpqlrasld pvvtgngdrl rfesfsgccg vyarldvlrs gldggevghg
      121 ttnvdvnnpl realsrigsd dplhmrvgpq elavttldgp vvekkvplpd rwlrgfaeaq
      181 vmaagfdlra elpaaeavrf lrslprsgpr gagggprwvv pagralrptt rpvpgsvclp
      241 gperlaalqr vlrhatalrv ygpavagaaa tasaweavlp gmrltltlsp dasrgfsgeg
      301 gvldalatde aaedaeliav llaweprvdv adlaassglt pervraalvr lgtsgrvgyd
      361 taeaayfhre lpydadraer hnprlraara lvaagavald gtlatvtaed ghahrvreer
      421 gvlscscqww akdrggrgpc khalavrmar rgsaeverda leqdaveqgv arvdggvr
//
LOCUS       WP_392309058             358 aa            linear   BCT 20-JAN-2025
DEFINITION  response regulator [Streptomyces sp. NPDC014889].
ACCESSION   WP_392309058
VERSION     WP_392309058.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014889
  ORGANISM  Streptomyces sp. NPDC014889
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 358)
  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 358)
  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 11467115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Streptomyces sp. NPDC014889"
                     /db_xref="taxon:3364928"
     Protein         1..358
                     /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=39361
     Region          <62..>268
                     /region_name="COG4913"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal ATPase domain [Function unknown]"
                     /db_xref="CDD:443941"
     Region          229..>345
                     /region_name="PleD"
                     /note="Two-component response regulator, PleD family,
                     consists of two REC domains and a diguanylate cyclase
                     (GGDEF) domain [Signal transduction mechanisms,
                     Transcription]; COG3706"
                     /db_xref="CDD:442920"
ORIGIN      
        1 mgelrplgdd lndasralae alrelfeslh lsvrryaarr rldpgtvsry lngtrlppwq
       61 visdlftdva ehrgtavtte aielvrglyg savdaasspk haveileqql adadhvsrrs
      121 svrgdvlgda lldrtqriad letllnqlea driaeqkrad elaqahpdvs gliqernvlq
      181 leverlgaal reaqaqrasa edrcdllerq leaveqataa vlpagpqdmp kilivddqpd
      241 nllamtavla tleqelvtvs sgrealkall dhddfaviim dvqmpdmdgy etcahikrrp
      301 rtrdvpiifl tamgigsehs argyaagavd yiskpfdpwa lrakvavfts iylerhsq
//
LOCUS       WP_392309213             178 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein, partial [Streptomyces sp.
            NPDC014889].
ACCESSION   WP_392309213
VERSION     WP_392309213.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014889
  ORGANISM  Streptomyces sp. NPDC014889
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 178)
  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 11440233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Streptomyces sp. NPDC014889"
                     /db_xref="taxon:3364928"
     Protein         <1..178
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
     Region          <1..175
                     /region_name="GCD1"
                     /note="NDP-sugar pyrophosphorylase, includes eIF-2Bgamma,
                     eIF-2Bepsilon, and LPS biosynthesis protein s
                     [Translation, ribosomal structure and biogenesis, Cell
                     wall/membrane/envelope biogenesis]; COG1208"
                     /db_xref="CDD:440821"
ORIGIN      
        1 ghlaevlekw lnsadlpvrv ctvvepeplg rggglkfaaa qlphpdqpwy atngdiwtrf
       61 slrdmadfht erdaiatlal arpripwgav rtdgfghitd fieappstfe inagvyvfss
      121 efaallperg dherttfphl arqrrlagft ipqgaywrai dtakdlteaa kelaalgr
//
LOCUS       WP_392309310             707 aa            linear   BCT 20-JAN-2025
DEFINITION  DNA gyrase/topoisomerase IV subunit B [Streptomyces sp.
            NPDC014889].
ACCESSION   WP_392309310
VERSION     WP_392309310.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014889
  ORGANISM  Streptomyces sp. NPDC014889
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Tari,L.W., Trzoss,M., Bensen,D.C., Li,X., Chen,Z., Lam,T.,
            Zhang,J., Creighton,C.J., Cunningham,M.L., Kwan,B., Stidham,M.,
            Shaw,K.J., Lightstone,F.C., Wong,S.E., Nguyen,T.B., Nix,J. and
            Finn,J.
  TITLE     Pyrrolopyrimidine inhibitors of DNA gyrase B (GyrB) and
            topoisomerase IV (ParE). Part I: Structure guided discovery and
            optimization of dual targeting agents with potent, broad-spectrum
            enzymatic activity
  JOURNAL   Bioorg Med Chem Lett 23 (5), 1529-1536 (2013)
   PUBMED   23352267
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Gadelle,D., Filee,J., Buhler,C. and Forterre,P.
  TITLE     Phylogenomics of type II DNA topoisomerases
  JOURNAL   Bioessays 25 (3), 232-242 (2003)
   PUBMED   12596227
REFERENCE   3  (residues 1 to 707)
  AUTHORS   Wang,J.C.
  TITLE     Cellular roles of DNA topoisomerases: a molecular perspective
  JOURNAL   Nat Rev Mol Cell Biol 3 (6), 430-440 (2002)
   PUBMED   12042765
REFERENCE   4  (residues 1 to 707)
  AUTHORS   Champoux,J.J.
  TITLE     DNA topoisomerases: structure, function, and mechanism
  JOURNAL   Annu Rev Biochem 70, 369-413 (2001)
   PUBMED   11395412
REFERENCE   5  (residues 1 to 707)
  AUTHORS   Roca,J.
  TITLE     The mechanisms of DNA topoisomerases
  JOURNAL   Trends Biochem Sci 20 (4), 156-160 (1995)
   PUBMED   7770916
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Streptomyces sp. NPDC014889"
                     /db_xref="taxon:3364928"
     Protein         1..707
                     /product="DNA gyrase/topoisomerase IV subunit B"
                     /EC_number="5.6.2.2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003918 - DNA topoisomerase type II
                     (double strand cut, ATP-hydrolyzing) activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006265 - DNA topological change [Evidence
                     IEA]"
                     /calculated_mol_wt=77124
     Region          21..701
                     /region_name="GyrB"
                     /note="DNA gyrase/topoisomerase IV, subunit B
                     [Replication, recombination and repair]; COG0187"
                     /db_xref="CDD:439957"
ORIGIN      
        1 mtaetsvpst allagadrdg snytarhllv legleavrkr pgmyigstds rglmhclwei
       61 idnsvdealg gycdhidvvl hddgsvevrd ngrgipvdve pktglsgvev vmtklhaggk
      121 fgggsyaasg glhgvgasvv nalsarldve vdrgghthai sfrrgvpgaf taggpeakfe
      181 pgsglrkark ipksrsgtrv rywadrqifl kdaklaletl hqrarqtafl vpgltivvrd
      241 eyglgeggsk geesfrydgg isefceylas dravcdvlrf tghgtfketv pvlddhgqmt
      301 ptevtrelgv dvalrwgtgy dttlrsfvni iatpkggthm agfeqavart mnevlrakkm
      361 lrvaeddivk ddalegltav vtvrlaepqf egqtkevlgt saarrivnnv vtkelkdflt
      421 stkrdaaqqa rvvlekavaa artriaarqh kdaqrrktal essslpakla dcrsddvdrs
      481 elfivegdsa lgtaklarns efqallpirg kilnvqkssv tdmlknaecg aiiqvigags
      541 grtfdidaar ygkiimmtda dvdgshirtl lltlfhrymr pmveagrvfa avpplhriel
      601 iqpkrgqdky vytysdrelr dkllefqskg vrykdsiqry kglgemdadq laettmdprh
      661 rtlrrinlsd leaaeqvfdl lmgndvaprk efiassaatl drsrida
//
LOCUS       WP_392309368             216 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces sp. NPDC014889].
ACCESSION   WP_392309368
VERSION     WP_392309368.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014889
  ORGANISM  Streptomyces sp. NPDC014889
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Streptomyces sp. NPDC014889"
                     /db_xref="taxon:3364928"
     Protein         1..216
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22873
     Region          2..209
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 mssrdailgr ieaaladvpa detpvdvpip rnyrrshiqp gddivalfae rvadyratvt
       61 rtdpaglpaa iaaaltarra rrlalpegfp aellppgdwq whsepldvpa ldaldgaltl
      121 aavgiavtgt lvldtgpgqg rraltlvpdy hlcviraeqi aadvpdalrr ldparpltfv
      181 sgpsatsdie ldrvegvhgp rtldvvivdp thpeqp
//
LOCUS       WP_392310218             305 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC014892].
ACCESSION   WP_392310218
VERSION     WP_392310218.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014892
  ORGANISM  Streptomyces sp. NPDC014892
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 305)
  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 305)
  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 18542080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Streptomyces sp. NPDC014892"
                     /db_xref="taxon:3364930"
     Protein         1..305
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33960
     Region          1..63
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
     Region          80..256
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 maalfgarvr rlrtaagltq aelgdrthvv stritqiera sgakptlela raldaalgad
       61 dllvdlwpyv yreafpdwsr kfmefaqrav vireyaahvv pgllqtedya ravlrtgrtl
      121 gseeqleerv alrmgrqerl gtpdrpelwv vldeavlrrp vggqavmrgq larlvrtste
      181 hhitvqvlpf dqgehevmgg sltvltmpds seiaytegah ygqliedpde vrsftltydr
      241 lraaalpplm sldmirsvme dnhrgakvps rserrrlaqe qlqqsggrql rgsgrgiprg
      301 rrpgp
//
LOCUS       WP_392310279             385 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Streptomyces sp.
            NPDC014892].
ACCESSION   WP_392310279
VERSION     WP_392310279.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014892
  ORGANISM  Streptomyces sp. NPDC014892
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Igarashi,K., Ito,K. and Kashiwagi,K.
  TITLE     Polyamine uptake systems in Escherichia coli
  JOURNAL   Res Microbiol 152 (3-4), 271-278 (2001)
   PUBMED   11421274
REFERENCE   5  (residues 1 to 385)
  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   6  (residues 1 to 385)
  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 11430824
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Streptomyces sp. NPDC014892"
                     /db_xref="taxon:3364930"
     Protein         1..385
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0019808 - polyamine binding [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:0015846 - polyamine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42900
     Region          2..382
                     /region_name="PotD"
                     /note="Spermidine/putrescine-binding periplasmic protein
                     [Amino acid transport and metabolism]; COG0687"
                     /db_xref="CDD:440451"
ORIGIN      
        1 mltrrsllga aaslgvltgc gvpaayvapg dragvdlsar dkrlswsnwp lyidtddedd
       61 trrptleafe ertgiavdyv eeindndeff gkispalmnh qqtgrdlvvv sdwmcarfvr
      121 lgwvqemdra rqpnvsrhld pqlrspafdp graftvpwqs gitgiaynrr rvgreirrva
      181 dlwaddlkgr vtllsgldea fallmqgngv dvtrwtaddf htvcdqvasr vrrghirrft
      241 gndyikdlss gdvlacqays gdiiqlqadd pdirfvvpee gaelwseslm ipnlarhkts
      301 aerlvdhyyd pevaaelaaw vnyvcpvpaa rdvlasakde etaalaedpl ifpddamrar
      361 lavarditsg errefarrwn givgl
//
LOCUS       WP_392312385             219 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces sp. NPDC014892].
ACCESSION   WP_392312385
VERSION     WP_392312385.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014892
  ORGANISM  Streptomyces sp. NPDC014892
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Streptomyces sp. NPDC014892"
                     /db_xref="taxon:3364930"
     Protein         1..219
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23361
     Region          2..212
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 mssrdlimgr vrraladvrr ddtpyeqavp rgylrehggl gpaetvella enladyralv
       61 hradadglad viagllrahg sktvlvppgl reewlsatdl arvadrgest aheldqvdsv
      121 vtacalaiae tgtivldgsp dqgrrritlv pdhhicvvrv pdqvvssvpq alelldptrp
      181 ltwisgpsat sdieldrveg vhgprtlevv lvtggdsqg
//
LOCUS       WP_392311269             263 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC014892].
ACCESSION   WP_392311269
VERSION     WP_392311269.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014892
  ORGANISM  Streptomyces sp. NPDC014892
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415139
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Streptomyces sp. NPDC014892"
                     /db_xref="taxon:3364930"
     Protein         1..263
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=27751
     Region          56..254
                     /region_name="LysX"
                     /note="Glutathione synthase, LysX or RimK-type ligase,
                     ATP-grasp superfamily [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism,
                     Translation, ribosomal structure and biogenesis, Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0189"
                     /db_xref="CDD:439959"
ORIGIN      
        1 mtatlagrrv vlvhgkkptp hsivwtvlag lraegarigt wqdapdlprs vftgadlvvl
       61 rsvhpvtadl aragappeas wcnppeatav vadrvetwrr llaadlpvpa srvvrdprav
      121 tamaaegpvv aktplgsrge gvtvlergdg rpvvgrgpwl vqdripgdgw drklfvigsh
      181 vhgtlrrwpa rslsdkwgrp lrldsrltal alaagdvfgl caygvdvidg pdgpvivdvn
      241 afpgfkgvpg apgllfdhll ghl
//
LOCUS       WP_392312821             265 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptomyces sp.
            NPDC014892].
ACCESSION   WP_392312821
VERSION     WP_392312821.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014892
  ORGANISM  Streptomyces sp. NPDC014892
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 265)
  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 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   3  (residues 1 to 265)
  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   4  (residues 1 to 265)
  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 265)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptomyces sp. NPDC014892"
                     /db_xref="taxon:3364930"
     Protein         1..265
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28268
     Region          22..253
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <144..253
                     /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 mreteihlge ppdvaligvg vhgvasrtdv frlpelwqlh lyqyeaeltv dgtshalrpg
       61 rvslvppgtt vryryrgrse hlfahlritp sgaprtvpvv qdtgpelptl tglllqavaa
      121 apsepdrtra elwtalwrva rltppvaaap gphpavttai ahieahlaap ltipavarva
      181 gvshnhltrl fhaetggtvv ayirrrrler ahhllrattl sipavaasvg ipdlqafnka
      241 crrelgaspr alrgagfpag vansa
//
LOCUS       WP_392313847             251 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Streptomyces sp.
            NPDC014892].
ACCESSION   WP_392313847
VERSION     WP_392313847.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014892
  ORGANISM  Streptomyces sp. NPDC014892
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 251)
  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 251)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Streptomyces sp. NPDC014892"
                     /db_xref="taxon:3364930"
     Protein         1..251
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26006
     Region          3..239
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 mirvaavgdi hlgpdsrgll rpafdtlpdh adllllagdl trhgtpeear vvadevaglp
       61 vpvvavlgnh dhhaerpedv tavlrdagvt vlegegtvvr vdgvrvgvag tkgfgggfag
      121 rsgsefgepe mkafvrhtrg langlrrald elaedgcavr ialthfspvp dtlvgeplei
      181 ypflgsylla eamdesgadl avhghahlgt ehgitsggvr vrnvaqpvir rafavyrlpv
      241 ggdrgaggdg s
//
LOCUS       WP_392314258             543 aa            linear   BCT 20-JAN-2025
DEFINITION  complex I subunit 4 family protein [Streptomyces sp. NPDC014892].
ACCESSION   WP_392314258
VERSION     WP_392314258.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014892
  ORGANISM  Streptomyces sp. NPDC014892
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 543)
  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 543)
  AUTHORS   Galemou Yoga,E., Angerer,H., Parey,K. and Zickermann,V.
  TITLE     Respiratory complex I - Mechanistic insights and advances in
            structure determination
  JOURNAL   Biochim Biophys Acta Bioenerg 1861 (3), 148153 (2020)
   PUBMED   31935361
REFERENCE   3  (residues 1 to 543)
  AUTHORS   Friedrich,T. and Scheide,D.
  TITLE     The respiratory complex I of bacteria, archaea and eukarya and its
            module common with membrane-bound multisubunit hydrogenases
  JOURNAL   FEBS Lett 479 (1-2), 1-5 (2000)
   PUBMED   10940377
REFERENCE   4  (residues 1 to 543)
  AUTHORS   Walker,J.E.
  TITLE     The NADH:ubiquinone oxidoreductase (complex I) of respiratory
            chains
  JOURNAL   Q Rev Biophys 25 (3), 253-324 (1992)
   PUBMED   1470679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Streptomyces sp. NPDC014892"
                     /db_xref="taxon:3364930"
     Protein         1..543
                     /product="complex I subunit 4 family protein"
                     /GO_component="GO:0045271 - respiratory chain complex I
                     [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048039 - ubiquinone binding [Evidence
                     IEA]"
                     /GO_process="GO:0015990 - electron transport coupled
                     proton transport [Evidence IEA]"
                     /GO_process="GO:0042773 - ATP synthesis coupled electron
                     transport [Evidence IEA]"
                     /calculated_mol_wt=57056
     Region          9..540
                     /region_name="NuoM"
                     /note="NADH:ubiquinone oxidoreductase subunit 4 (chain M)
                     [Energy production and conversion]; COG1008"
                     /db_xref="CDD:440632"
ORIGIN      
        1 midinesvmq vllalivvgp llgavaallp appglkgksp eqavlrhgit vtgavliaai
       61 vlalgfdhdq pskmqastdi swipaldvri hlgidgislp llvltalltf lcalysyfkq
      121 qhqrltpraa gpspkafval llvlesgtla tfavldlllf flafemvlip myfliarwgg
      181 eertraawkf ilytllgsvv mllgllligi kagtfdmval atdshpsltt svqviavlsi
      241 giglavktpm wplhswlpda htaaptvgsv llagillkmg tygfvrillp itpdgfrtfa
      301 pylaafavvg iiygslacla larqgakgdl krliayssvg hmgfvllgia tmtptgvnga
      361 lfaniahgli tgllfflvga lkdrtgttdl dtlaqetgaa lygraprlgg llafaavasl
      421 glpglagfwg emlalfgafd paeglsrpaf ltfmtiaafg tlltaaylli vvrrvcmgav
      481 pkepqegpgr tdertyalad vqtyefaawt plvaltvlag lwpaallglt dpavqqllag
      541 gtr
//
LOCUS       WP_392314468             343 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Streptomyces sp. NPDC014892].
ACCESSION   WP_392314468
VERSION     WP_392314468.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014892
  ORGANISM  Streptomyces sp. NPDC014892
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Streptomyces sp. NPDC014892"
                     /db_xref="taxon:3364930"
     Protein         1..343
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36035
     Region          9..332
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mtgsalpqll rpralkpgdl vvvaalsgpl davhepdlqq avavleqmgf rvrrapllea
       61 grhrwwsaaa pteiagefna llrdpevrai iahdggqtal gyldlidfea iaadpkpilg
      121 ysdisllhlv lyartglvgf hadvatrglg gywqsapaar ratleklyst lltgdeaiga
      181 lpatpswecw ragraeggli ggvinrialv qatsfalpld cfdgavlfwe eaggqashvw
      241 sylqvlrhsg ildrisgmvv gvpdgidglg tadapdaspt laeivldvlg drdipvlgnv
      301 efghagpnlp mpvgirvgld ahqrtlslle pavrplattg pvg
//
LOCUS       WP_392314934             295 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC014892].
ACCESSION   WP_392314934
VERSION     WP_392314934.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014892
  ORGANISM  Streptomyces sp. NPDC014892
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415139
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Streptomyces sp. NPDC014892"
                     /db_xref="taxon:3364930"
     Protein         1..295
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=31983
     Region          7..265
                     /region_name="LysX"
                     /note="Glutathione synthase, LysX or RimK-type ligase,
                     ATP-grasp superfamily [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism,
                     Translation, ribosomal structure and biogenesis, Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0189"
                     /db_xref="CDD:439959"
ORIGIN      
        1 martaapria latydpgprv nhdrdlpvlv ealreagada aavrwddpaa dwaaydlvvi
       61 rstwdyswra aefvawaekt geatrlanpa evvrwntdkr yigdlaragv pvvptdylap
      121 gdplrlpeah eyvvkptsga garfaarytp dqretvaahv ermraeglta mvqpfvtsid
      181 tegeralqff ggrllhasrk gavlapgtay daektahpdl vpwtpteael avaeralaav
      241 pdrpellyar vdlvtgadgq pwvmelelve pnlflwlhpd slprvvgail aaatg
//
LOCUS       WP_392315357             429 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC015139].
ACCESSION   WP_392315357
VERSION     WP_392315357.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015139
  ORGANISM  Streptomyces sp. NPDC015139
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 429)
  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 429)
  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
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 429)
  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   5  (residues 1 to 429)
  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   6  (residues 1 to 429)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 429)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Streptomyces sp. NPDC015139"
                     /db_xref="taxon:3364942"
     Protein         1..429
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44300
     Region          20..>60
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          81..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 maglsgrtvr dlrresrstv lqrlyvdgpm srhalgpatg lssgsvsnvv aelladglve
       61 eagligadvg rprrllrvrr dsgrligvdv getrvrvelf dlgmrelawa erplgprgye
      121 vdavvghvad gigevlrvsg laagellgvg igvpgiiedg gadgavvhgq tigwdavple
      181 lllrrtgrlp vqvpyfvdng akalgqaemw fgagrgarna vvvlfgsgvg acvvaeeaeq
      241 gravewghlt vrvggrrcrc gargcleaya gaealvarwr eaggrpsags geeraltell
      301 aaarpadgre adpvaaavla etaaylgagl sdlinlfqpe rvliggwagl qlgggfldev
      361 rghalahalr fpasrvgidl grlgpdavtv gaavlplaaf farggrrprp sggtvpspaw
      421 qaaldgrla
//
LOCUS       WP_392315560             327 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces sp. NPDC015139].
ACCESSION   WP_392315560
VERSION     WP_392315560.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015139
  ORGANISM  Streptomyces sp. NPDC015139
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Streptomyces sp. NPDC015139"
                     /db_xref="taxon:3364942"
     Protein         1..327
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33120
     Region          53..321
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mtavplpplp plsggrlprr vpvrqvlclv plvlvavaav rhrsvlaegf gqlraaswpw
       61 llaaagttcl twvaaaftrq gavvqplpkg rllatqfaag aanhllptgl gagavnlrfm
      121 tvcgvplars saalalylma ecvgrlglla alliafpgal rlgtllpdgs llplllgvag
      181 llvvaaavvl svrrlrtrlv afarealgea rsvhtrpara lalwggslaf palqaaglaa
      241 vgqalrlpvp pvhmalayla atvavalvpt pgglgsveaa livalvavgg paaiatavvl
      301 ayriitvwmp lvpgaltlga lvrlkvi
//
LOCUS       WP_392315856             380 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC015139].
ACCESSION   WP_392315856
VERSION     WP_392315856.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015139
  ORGANISM  Streptomyces sp. NPDC015139
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 380)
  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 380)
  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
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 380)
  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   5  (residues 1 to 380)
  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   6  (residues 1 to 380)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 380)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 380)
  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 20650276
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Streptomyces sp. NPDC015139"
                     /db_xref="taxon:3364942"
     Protein         1..380
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39577
     Region          5..60
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          81..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 mtswlplspa ersvaievlv hgplsrtela rrlhlsqgsl trltkpltes gllveapaag
       61 gaarqgrpsq pldvraeass flgfkitadt vygvvttlrs evtdrldrpl athdpgavad
      121 lvaetaaela arhpgvagig vgvggrvrer avvaesaflg wrdvpfaall qertglpvvv
      181 endvaalvea etwfgagrgl drfavltiga gigyglvlgg trvpfdeedr gfgrywildp
      241 sgpltpdgar gsavslltvp gieyqiraat gadaryedil agagagepma srvigeaara
      301 lgtlvaqian fampqkilla gegvglmdva gntvretvra hrhplaapvd letrvsdfhd
      361 wargaavlai qvlvlgragk
//
LOCUS       WP_392317003             540 aa            linear   BCT 20-JAN-2025
DEFINITION  peptide ABC transporter substrate-binding protein [Streptomyces sp.
            NPDC015139].
ACCESSION   WP_392317003
VERSION     WP_392317003.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015139
  ORGANISM  Streptomyces sp. NPDC015139
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 540)
  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 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   3  (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
REFERENCE   4  (residues 1 to 540)
  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 540)
  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 11467924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Streptomyces sp. NPDC015139"
                     /db_xref="taxon:3364942"
     Protein         1..540
                     /product="peptide 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=58293
     Region          10..535
                     /region_name="OppA"
                     /note="ABC-type oligopeptide transport system, periplasmic
                     component [Amino acid transport and metabolism]; COG4166"
                     /db_xref="CDD:443327"
ORIGIN      
        1 mrgtgpvgrt agalalvfla vacgsgasgv ggpgtltssw gdpqnplepa ntnevqggkv
       61 ldmifrglkr ydprtgkatd mlaeridttd srnfsvtvkd gwrfsngepv tassfvdawn
      121 ygaslrnnqk nayffgyieg ydkvhpdsga qtadtlsglk vtgprtftvr lnqkfssfpd
      181 tlgyvafapl prtfftdhaa wvsrpvgngp yqvqsytkgs amalrkwsay pgpdrarndg
      241 vsllvytdts taytdvlagn ldlvddvpaa qlknvetdld gryintpagi lqtlafpfyd
      301 pkwntagark vrtglsmain rkqitetifr gtrtpatdwt spvlgvdggf kaglcgpace
      361 ydpvrakqli eegggipggr lkitynadsg shkqwvdavc nsinnalgnd tacvgnpigt
      421 fadfrnqitq hrmsgpfrag wqmdypliqn flqplyytga ssndgkwsdk rfdrlvdean
      481 aesdtpkaia lfqqaegvvr dnmaavplwy qngsagysar lshvalnpfs vpvyneikvg
//
LOCUS       WP_392318036             245 aa            linear   BCT 20-JAN-2025
DEFINITION  SRPBCC family protein [Streptomyces sp. NPDC015139].
ACCESSION   WP_392318036
VERSION     WP_392318036.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015139
  ORGANISM  Streptomyces sp. NPDC015139
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 245)
  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 10008053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Streptomyces sp. NPDC015139"
                     /db_xref="taxon:3364942"
     Protein         1..245
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=26727
     Region          1..105
                     /region_name="YndB"
                     /note="Chalcone/flavanone-binding protein YndB,
                     AHSA1/START/SRPBCC domain [Lipid transport and
                     metabolism]; COG3832"
                     /db_xref="CDD:443044"
ORIGIN      
        1 mskefeivre fevdvpserv weavttgtgg ylwpmdppep rvggkgpsgs tvtawdpphr
       61 yahrsgdagp gvqslglldh tieprdegrr srvryvhsgv ftddwnnqyd gaskhtnfhl
      121 htlceylthf aprpvafarl dgprtsatpr alaavgralg laddaaagtr tavrgpggrt
      181 ldvvidyrsp yfvglrtdda lirffgrgsw gaplgisihd fapdadaead rtawqdwlng
      241 vfsrs
//
LOCUS       WP_392318228             394 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC015139].
ACCESSION   WP_392318228
VERSION     WP_392318228.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015139
  ORGANISM  Streptomyces sp. NPDC015139
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 394)
  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   5  (residues 1 to 394)
  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   6  (residues 1 to 394)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 394)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 394)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Streptomyces sp. NPDC015139"
                     /db_xref="taxon:3364942"
     Protein         1..394
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41334
     Region          21..>68
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          86..380
                     /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 mpvsdaveqq eqpwsrrrlr stnerllldr lrgagaasra qlaretglsk ptvssalasl
       61 eaaglvreag thapgrgrta vlyapdpaag yalgvdigrg wlrvavvdld gtvaaradvr
      121 nrtrasaala dlvvgtarqv vensgvdpae vvhgvigtpg vydegqrrvr yamhlpgwgr
      181 tgivdrmree lgvplevhnd anlaalgeyt ygvgegsrlf ayiligtglg mgvvsegrlf
      241 tgahglagei gflpwpgrqk perledavsg vavvesarrf gmsgqltaka vfdaarrgdp
      301 aaaraveleg eriahtvaaa aavldpdlvv lggglghsvd lllrpvrehv raltplrpri
      361 vpsrlgedav llgavatald tardvvferr tags
//
LOCUS       WP_392319106             393 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC015139].
ACCESSION   WP_392319106
VERSION     WP_392319106.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015139
  ORGANISM  Streptomyces sp. NPDC015139
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 393)
  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 393)
  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
REFERENCE   3  (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   4  (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   5  (residues 1 to 393)
  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   6  (residues 1 to 393)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (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 11973053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Streptomyces sp. NPDC015139"
                     /db_xref="taxon:3364942"
     Protein         1..393
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39852
     Region          <12..76
                     /region_name="COG3398"
                     /note="Predicted transcriptional regulator, contains two
                     HTH domains [Transcription]"
                     /db_xref="CDD:442625"
     Region          77..384
                     /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 mtarpanthq arllkllrdg gpnsraqlgd ridlsrskla vevdrlletg lvvadglaas
       61 rggrrshnvr lnpelrflgv digatsvdva vtnaeleilg hlnqpmdvre gpvavfeqvl
      121 dmagklkatg laegfdgagi gvpgpvrfpe gvpvappimp gwdgfpvrea lsqelgcpvm
      181 vdndvnlmam geqhagvart tadflcvkig tgigcgivvg grvhrgttgs agdighiqav
      241 pdgrpcacgn rgcleahfsg aalardavqa agqglsaela arleangtls avdvaaaaaa
      301 gdataldlir eggthvgqvi aglvsffnpg lvvigggvtg lghtllaair sqvyrqslpl
      361 atgnlpivlg elgpsagvtg aarlisdhlf spa
//
LOCUS       WP_392319209             253 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015139].
ACCESSION   WP_392319209
VERSION     WP_392319209.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015139
  ORGANISM  Streptomyces sp. NPDC015139
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   2  (residues 1 to 253)
  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 253)
  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 253)
  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 10611723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptomyces sp. NPDC015139"
                     /db_xref="taxon:3364942"
     Protein         1..253
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26231
     Region          18..75
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(19,23,48)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(22,47)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(29..30,41,44,48..49)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          144..227
                     /region_name="DUF2690"
                     /note="Protein of unknown function (DUF2690); pfam10901"
                     /db_xref="CDD:402475"
ORIGIN      
        1 mghpqrsttp derltaglre lrdrtglsla alaartpysk sawhrylsga qrppraavea
       61 lcrlaggape avlplwdaad arpsaspqpp prpnrrrawl plsavvlcga aaalgatlgl
      121 sggpgtapaa qtlpavprch gpacqgelpd asactrdaqt rssvdargyt vrlrwspacg
      181 tawsevrmrs prarevsvra gqdvlsasys ahdtagdssp mlfvpsprgv eacaeadgkv
      241 actgldadle eqg
//
LOCUS       WP_392320783             430 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC015139].
ACCESSION   WP_392320783
VERSION     WP_392320783.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015139
  ORGANISM  Streptomyces sp. NPDC015139
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Streptomyces sp. NPDC015139"
                     /db_xref="taxon:3364942"
     Protein         1..430
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=45934
     Region          67..314
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mserrrtlav lyddgaasag eigvgladlg divfllpptg haerlrpvle nfgtvvpltg
       61 ttkgdialar dlapdavvty sermvrrtae iaealglpsh tpevastvtd kirqrqvmrd
      121 agvdkvrshp lsspdewprv ydavglpaiv kpvrgggsrd tyavttaaem eellprlfpe
      181 gteaaytvee llqgvpsapy gdyvsvesvc tpqgvrhlav tgkfpllkpf relgsywpsh
      241 lpadvlaevt dlttraldal gvrygithte lkltadgprv ievngrlsgh lnlmsrrvcg
      301 vdmvrlggll algdtsqipe fdyggrvhfl fntmapvepc rleaihgatd vrkvggidgi
      361 rpyvrpgtdl aggvmttpld viwgscadht amldaleeal pkltyvftrp dgtvreataa
      421 altdvseaga
//
LOCUS       WP_392320917             850 aa            linear   BCT 20-JAN-2025
DEFINITION  GcvT family protein [Streptomyces sp. NPDC015139].
ACCESSION   WP_392320917
VERSION     WP_392320917.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015139
  ORGANISM  Streptomyces sp. NPDC015139
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 850)
  AUTHORS   Stauffer,L.T., Ghrist,A. and Stauffer,G.V.
  TITLE     The Escherichia coli gcvT gene encoding the T-protein of the
            glycine cleavage enzyme system
  JOURNAL   DNA Seq 3 (6), 339-346 (1993)
   PUBMED   8219277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..850
                     /organism="Streptomyces sp. NPDC015139"
                     /db_xref="taxon:3364942"
     Protein         1..850
                     /product="GcvT family protein"
                     /calculated_mol_wt=92922
     Region          28..411
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
     Region          397..452
                     /region_name="FAO_M"
                     /note="FAD dependent oxidoreductase central domain;
                     pfam16350"
                     /db_xref="CDD:465100"
     Region          447..849
                     /region_name="GcvT"
                     /note="Glycine cleavage system protein T
                     (aminomethyltransferase) [Amino acid transport and
                     metabolism]; COG0404"
                     /db_xref="CDD:440173"
ORIGIN      
        1 msstaedfrh pahqaartpd hqpapsprvv vigagivgcs ladeltgrgw tdvtvleqgp
       61 lpapggstsh apglvfrtsp sktlaefaky tvekfrslev dgvacfdqvg glelattper
      121 laelhrragy aaswgiraev vstarckelw plldesmvlg glhtpddgla rallaaraqm
      181 dratargarf lerhtvtgie rehgrvtavv tdrgtfpadh vvsaagfwgp vvgamagvdv
      241 plqplahqya ktaplpelsg aaaeatrpil rfqdrdlyfr ehgdrigigs yahrpmpvdp
      301 favpaydear ardmpmpssy pftaedwaps wedcrrllpa lresrieagf ngvfsftpdg
      361 mpvlgetrql rgfwlaeavw vthsagvara vaewmvdgrp sldvhecdht rfeevqrsps
      421 yvrergsqqf vevydvlhpl qpmerprplr vspfharqqq lgafflegag werphwyean
      481 aalldgpggl dgpgdhgdhg dhgglperda wsarywspia aaeamatrek valydmtplr
      541 rlevtgpgal afldrmtsnn lrrkpgavty tllldetggi rsdltvarla pdrfqigans
      601 padldrllry apddvrirdi tsgtccvgvw gplaralvqp ltaddfsheg fgyfrvrrtw
      661 vghvpvtamr lsyvgelgwe lyttadlglr lwdtlweagq elgviaagrs afdslrlekg
      721 yrawgtdmtd ehtpfeaglg favrmdkeef vgqealsglp eptrrltpll lddpaavvlg
      781 kepvhvdgvp agyvtsasyg ytlgrcvaya wlpaglptgt gvqvvyfgek vaatvadepl
      841 fdpkmtrirr
//
LOCUS       WP_392320957             213 aa            linear   BCT 20-JAN-2025
DEFINITION  nicotinamide mononucleotide transporter family protein
            [Streptomyces sp. NPDC015139].
ACCESSION   WP_392320957
VERSION     WP_392320957.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015139
  ORGANISM  Streptomyces sp. NPDC015139
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Hemberger,S., Pedrolli,D.B., Stolz,J., Vogl,C., Lehmann,M. and
            Mack,M.
  TITLE     RibM from Streptomyces davawensis is a riboflavin/roseoflavin
            transporter and may be useful for the optimization of riboflavin
            production strains
  JOURNAL   BMC Biotechnol 11, 119 (2011)
   PUBMED   22136195
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Zhu,N., Olivera,B.M. and Roth,J.R.
  TITLE     Genetic characterization of the pnuC gene, which encodes a
            component of the nicotinamide mononucleotide transport system in
            Salmonella typhimurium
  JOURNAL   J Bacteriol 171 (8), 4402-4409 (1989)
   PUBMED   2546921
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Streptomyces sp. NPDC015139"
                     /db_xref="taxon:3364942"
     Protein         1..213
                     /product="nicotinamide mononucleotide transporter family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0034257 - nicotinamide riboside
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_process="GO:0034258 - nicotinamide riboside transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23823
     Region          1..205
                     /region_name="PnuC"
                     /note="Nicotinamide riboside transporter PnuC [Coenzyme
                     transport and metabolism]; COG3201"
                     /db_xref="CDD:442434"
ORIGIN      
        1 mnwlnseaft lfgqhiiwsd mvgnilglit lalgwrrslw twpvqflsgl vlfaafyghl
       61 tgsagkqvvv mavalygwwq wqrnkdravd ghivprfatw reraamlgaa avgtvavall
      121 ftaypslswd pwpdayifvg tvvamyaqak gmvefwfawl lvdlvgvpln fangyafsgf
      181 vyviygalvl wgmrdwwlrs rrspqpvleg apa
//
LOCUS       WP_392321113             160 aa            linear   BCT 20-JAN-2025
DEFINITION  SRPBCC family protein [Streptomyces sp. NPDC015139].
ACCESSION   WP_392321113
VERSION     WP_392321113.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015139
  ORGANISM  Streptomyces sp. NPDC015139
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 10008053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Streptomyces sp. NPDC015139"
                     /db_xref="taxon:3364942"
     Protein         1..160
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=17180
     Region          10..153
                     /region_name="YndB"
                     /note="Chalcone/flavanone-binding protein YndB,
                     AHSA1/START/SRPBCC domain [Lipid transport and
                     metabolism]; COG3832"
                     /db_xref="CDD:443044"
ORIGIN      
        1 mtvadpatln eitvtrvfda praavyrawt epelfarwwg prgfttdpgt valdvrvggt
       61 wkatmaaegv gefpftgvyr evvenerlvf tlvdpndenv aaraargeae elttvgfadt
      121 eggtrlsfqq vgqvdaekta eveagwnsfl dslgdhlaga
//
LOCUS       WP_392321242             139 aa            linear   BCT 20-JAN-2025
DEFINITION  TOBE domain-containing protein [Streptomyces sp. NPDC015139].
ACCESSION   WP_392321242
VERSION     WP_392321242.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015139
  ORGANISM  Streptomyces sp. NPDC015139
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 139)
  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 10007583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Streptomyces sp. NPDC015139"
                     /db_xref="taxon:3364942"
     Protein         1..139
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=14026
     Region          1..138
                     /region_name="MopI"
                     /note="Molybdopterin-binding protein MopI [Coenzyme
                     transport and metabolism]; COG3585"
                     /db_xref="CDD:442804"
ORIGIN      
        1 mtlsirnqlp gtvtevrpge vmatvkvrla ggqnltaait leaveelgla pgsevralvk
       61 stevalstsr teglsirnqv pgtvtqlllg evmatvkvsm aggeltaait kdaagdlglf
      121 vgsdvialik stevalata
//
LOCUS       WP_392321688             324 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015139].
ACCESSION   WP_392321688
VERSION     WP_392321688.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015139
  ORGANISM  Streptomyces sp. NPDC015139
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 324)
  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 324)
  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 324)
  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 11448557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Streptomyces sp. NPDC015139"
                     /db_xref="taxon:3364942"
     Protein         1..324
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=37659
     Region          14..69
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
ORIGIN      
        1 mdahseeitv eqaaedfaae vahwrevrgm skralaqamg fdpsyvshve sgrhkpteef
       61 arladehlna gkaiwrrwcd yeqartrsrr gptappaqrr heqpyatgsa lvvehdaarl
      121 qydghsyrlt mrrllrntgd epvtryliri svdrypgype rsnahyrahp ltwdeldlta
      181 tcrgetmrwq akhdrdafke vwllfdnehg rfplypgesv wieyaytvgd dkwgnwfqra
      241 vrlpteqlev qlafptaldp vvwgtetsmt aeasplrtpp vrsddgelrq ftwitttpal
      301 haryrlewrf rarpehnaeq gdfr
//
LOCUS       WP_392322225             601 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces sp.
            NPDC015139].
ACCESSION   WP_392322225
VERSION     WP_392322225.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015139
  ORGANISM  Streptomyces sp. NPDC015139
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 601)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 601)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Streptomyces sp. NPDC015139"
                     /db_xref="taxon:3364942"
     Protein         1..601
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=63787
     Region          355..592
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 maphradrqs aplpallaar itphaiqllp rqtgrplppp atagtggwwe lphdadlpaa
       61 rsapfpcptl iplgtsptgd lllldltepg allltgrpdd varvctalll eyalapwagd
      121 lhliatgfad dllhapladn ivyaptpaaa vhalaerlle ahqqphtrpr acilltatal
      181 daattrdlar laahpaplpv iavapapgvq dhfpdavild asatrpqplh ttgqdltarl
      241 tdsvdagppa parahadtdk ppvqahteep ahsptapaap aqaraegdhl fpalttaaah
      301 ttepdrtdst rsregqagsd rahgaahpar ptapaapfgp lpaaqptaas stplapqirv
      361 lgpievdgvp htghgprtaq laallyfrpg rtadtlcanm dpttpwttat lsarlhqlrr
      421 algntpdgdp yvprrqhadd pyrlhpgirc dwtefrtltd haldqgtegl naleaaltlv
      481 rgrpfgsral pwtephsqel ttrivhtadv iarlrtppgp hhdltkarha ittaldiddt
      541 aeslyqawfl ieaqadnrpg lhtaitrlqy inaaldrpls heterlidel lhpqsppaar
      601 p
//
LOCUS       WP_392323798             437 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC015127].
ACCESSION   WP_392323798
VERSION     WP_392323798.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015127
  ORGANISM  Streptomyces sp. NPDC015127
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Streptomyces sp. NPDC015127"
                     /db_xref="taxon:3364939"
     Protein         1..437
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=46024
     Region          70..317
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mksrvgvlls prgaatvrdi lvaagddiev vpllrtgvre qwpglaalts rlfgepvevn
       61 erqldvpgap lagvvtfads elelaaavgd hlgvrhrrae sadkyvqrtt lggaglsama
      121 artladaddl daartalglp fvvkprrgag gtdvtvvdta drcealkrsw regsslyaeq
      181 fiptaapsde twqadyvsve vqsiagrhdv itvfgkfpvy trgrkggghg qvattgdilp
      241 crlpadlrqq veqlvigahh algmddgvth tevklgsdgp eiieincrvg ghlsrllkrh
      301 sgfdlvrqal litaglpaqp lpsraegrsv agmfvpfasa egdvlsrvsp ahlkaagaat
      361 vdeiaregap rtdtdaiacn vvldcadade lrrttveflg hvremfakdg vgdqdwtadm
      421 itllggepar tpaaage
//
LOCUS       WP_392323995            1405 aa            linear   BCT 20-JAN-2025
DEFINITION  Rne/Rng family ribonuclease [Streptomyces sp. NPDC015127].
ACCESSION   WP_392323995
VERSION     WP_392323995.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015127
  ORGANISM  Streptomyces sp. NPDC015127
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1405)
  AUTHORS   Kime,L., Jourdan,S.S. and McDowall,K.J.
  TITLE     Identifying and characterizing substrates of the RNase E/G family
            of enzymes
  JOURNAL   Methods Enzymol 447, 215-241 (2008)
   PUBMED   19161846
REFERENCE   2  (residues 1 to 1405)
  AUTHORS   Callaghan,A.J., Marcaida,M.J., Stead,J.A., McDowall,K.J.,
            Scott,W.G. and Luisi,B.F.
  TITLE     Structure of Escherichia coli RNase E catalytic domain and
            implications for RNA turnover
  JOURNAL   Nature 437 (7062), 1187-1191 (2005)
   PUBMED   16237448
REFERENCE   3  (residues 1 to 1405)
  AUTHORS   Li,Z., Pandit,S. and Deutscher,M.P.
  TITLE     RNase G (CafA protein) and RNase E are both required for the 5'
            maturation of 16S ribosomal RNA
  JOURNAL   EMBO J 18 (10), 2878-2885 (1999)
   PUBMED   10329633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1405
                     /organism="Streptomyces sp. NPDC015127"
                     /db_xref="taxon:3364939"
     Protein         1..1405
                     /product="Rne/Rng family ribonuclease"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=147563
     Region          706..1104
                     /region_name="CafA"
                     /note="Ribonuclease G or E [Translation, ribosomal
                     structure and biogenesis]; COG1530"
                     /db_xref="CDD:441139"
ORIGIN      
        1 mlepigsgta gdnnqehatp sdtlpprrrr raasrpagpp savaagdnav lsesvpaeat
       61 sgpgaeavea aapaaggtep aeaaaptada eaaaprtrrr atrkatapag spepaepaap
      121 rtrrraarkt tapaaapvqa eavpaetgae veteeiaepv vadetaasrr trrrasapag
      181 apkaveateg aeaaeaaeaa ptqaeaaqav vpavagvsav vgesaeaeaa aprtrrratr
      241 katapagapq vveteeaqaa vpaadteaea paprtrrrat rkatapeave aveaadtaaa
      301 vpsaeaaepe tvepeaveaa aprrrrrasa pagapkataa eepqaeteap aprarraark
      361 atapagapaa veadeqages lpesaveqia ageaevvaae kaatrgrtrr raaapeftaq
      421 praaapaeea pargrrarpa vptfqapvft epmfqtpeta aaaaaaaasv pepeedeevt
      481 eavaeavvea papeqpagrr rrrrrgepae pvepveapaa eavpaeeeae peqaeaeqge
      541 esdeyedrps rrrrrggrrr rrgeaadaee saeeaaeeae aaaeeadeed edeseagtps
      601 aagtsssrrr rrrrrrsgda aaepeaaeee gvrtvvkvre prkkeepsde vqsikgstrl
      661 eakkqrrreg reqgrrrvpi iteaeflarr eavervmvvr qsgertqigv lednvlvehy
      721 vnkeqatsyv gnvylgkvqn vlpsmeaafv digkgrnavl yagevnfeal gmangprrie
      781 aalksgqsvl vqvtkdpigh kgarltsqvs lpgrylvyvp egsmtgisrk lpdterarlk
      841 tilkkivped agvivrtaae gasedelrrd verlqaqwee iqkkaksgna ptllygepdm
      901 tvrvvrdifn edftkvvvsg deawetihgy vshvapdlsd rlqrwtsevd vfaanrideq
      961 lmkaldrkvw lpsggslvid kteamvvidv ntgkftgqgg nleetvtrnn leaaeeivrq
     1021 lrlrdlggiv vvdfidmvle snrdlvmrrl leclgrdrtk hqvaevtslg lvqmtrkrvg
     1081 qgllesfset cvhcngrgvi vhmeqpsaag ggggkrakkr grggavvehe hvepqavpae
     1141 pepeteaeva aeaaapvale epafapdeel yssiaeaeaa vsrgrgrrra trkvsapaga
     1201 pkaaepavva vpepepavvp epepefapea paepapagrg rrratrkvsa pagspaqaev
     1261 tvapvakpep apepapvaep epevaavvae eapvaappra rrrvtrkvta pagspsgaee
     1321 aavvvvpaep kaaepeaeqa epeaapvakk aarktakkat akkaaakkta akkttakkta
     1381 akkvskktva aeqssssvsa ttsed
//
LOCUS       WP_392324481              98 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015127].
ACCESSION   WP_392324481
VERSION     WP_392324481.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015127
  ORGANISM  Streptomyces sp. NPDC015127
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 98)
  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 98)
  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 98)
  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 11448557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Streptomyces sp. NPDC015127"
                     /db_xref="taxon:3364939"
     Protein         1..98
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10456
     Region          25..93
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
ORIGIN      
        1 mpqgdarrlp praycadgvw peavmaehhg arvaqamaar lkaavddkgw siahlarisg
       61 vgrytiakal ageawpdllt ianlekalec dlwpgrdv
//
LOCUS       WP_392325051             255 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Streptomyces sp.
            NPDC015127].
ACCESSION   WP_392325051
VERSION     WP_392325051.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015127
  ORGANISM  Streptomyces sp. NPDC015127
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 255)
  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 255)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Streptomyces sp. NPDC015127"
                     /db_xref="taxon:3364939"
     Protein         1..255
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28165
     Region          2..245
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 mrvnvvsdvh gnaqdlatag dgadalvclg dlvlfldyad hsrgifpdlf gvenahlive
       61 lrtarrfdea rdlgrrlwae lgidresaie tavrrqyael faafptptya tygnvdipgl
      121 wpefarpgtt vldgerveig grvfgfvggg lrtpmrtpye isdeeyaakv ealgdvdvlc
      181 shippdvpel tydtvarrfe rgsrallaai rrtrpryalf ghvhqplarr mrlgatecvn
      241 vghfastgrp wtltw
//
LOCUS       WP_392325458             408 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC015127].
ACCESSION   WP_392325458
VERSION     WP_392325458.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015127
  ORGANISM  Streptomyces sp. NPDC015127
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces sp. NPDC015127"
                     /db_xref="taxon:3364939"
     Protein         1..408
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43575
     Region          54..240
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          246..377
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mrhvlkwagr caalavagag lvaglagctg gtldigskpr apedtirvtp gdgaqgvspd
       61 tpllvklpsg rlervkvtrv eaagrtevpg svsddglrwa piegtrlqla akysvdvval
      121 dahgrrtarh ttfttavper hfigyfkpen rstvgtgmiv sftfnrpien raaverairv
      181 tsspavevvg hwfgkerldf rprsywqpgt evtvdmrlrd vaaapgiygi qqktitftvg
      241 rsqvstvdaa ahtmrvvrdg allatvpvta gapktttyng kmvvtemfdv trmngatvgf
      301 tkkdgkgeyd ikdvphairl ttsgtflhgn ywaapetfgs anvshgcvgl rddkggsses
      361 pagwffdrtl igdvvevvns kdktvapdng lggwnmdwqs wkagsalq
//
LOCUS       WP_392325796             302 aa            linear   BCT 20-JAN-2025
DEFINITION  quinone oxidoreductase family protein [Streptomyces sp.
            NPDC015127].
ACCESSION   WP_392325796
VERSION     WP_392325796.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015127
  ORGANISM  Streptomyces sp. NPDC015127
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 302)
  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 302)
  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 302)
  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   4  (residues 1 to 302)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces sp. NPDC015127"
                     /db_xref="taxon:3364939"
     Protein         1..302
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=31122
     Region          1..302
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 mraiqfsrfg gpevleavet pdpvpgpgev litveaagvn yadtlvvdgs yavaeslpli
       61 pgsevvgrta dgrrvlarva sgyaelavak esavvaipde ldagqalall vqgltawhll
      121 esaarlrpge tvvvhaaggg vgslavqlat ifgagrvlaq astpekrela lklgadavae
      181 yplaeradvv ldatggelfd qalasladyg rlvtygdatg kglppvdpar lsrlnaavvg
      241 fwlrpalarp gavsgpltsm lrlvsegrlt pvvsppyalg earrafedlr arrttgktvl
      301 rp
//
LOCUS       WP_392325913             278 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015127].
ACCESSION   WP_392325913
VERSION     WP_392325913.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015127
  ORGANISM  Streptomyces sp. NPDC015127
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 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   4  (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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Streptomyces sp. NPDC015127"
                     /db_xref="taxon:3364939"
     Protein         1..278
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30948
     Region          6..69
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          91..272
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 maraenkesa gpttrlvadm arrmrarkgw tqeqlgdrig ftasavsame tcaqpasdem
       61 lvqleaalgd glglfeqare yvrldkypaq fknyalleqk alglhlyatl vvhglfqtee
      121 yaraligggy pplpehrvee lvearmarra lferepvali evvleesvlr rtiggeevmr
      181 gqmrylaecg rrrnvtlqvl pldvglsgey agghggmtlv etpehdhlvy leiqeeslli
      241 kdptkvstya qryakiraqa lgpresldli erlagdrq
//
LOCUS       WP_392326195             399 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC015127].
ACCESSION   WP_392326195
VERSION     WP_392326195.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015127
  ORGANISM  Streptomyces sp. NPDC015127
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 399)
  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   5  (residues 1 to 399)
  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   6  (residues 1 to 399)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 399)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Streptomyces sp. NPDC015127"
                     /db_xref="taxon:3364939"
     Protein         1..399
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40489
     Region          14..77
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          77..379
                     /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 metpgsqtsl hranlervvr avrmagsltq aeiarstgls aatvsnivre lkdggtvevt
       61 ptsaggrrar svslsgdagi vigvdfghth lrvavgnlah qvlaeeaepl dvdassaegf
      121 draealvnrl veatgigpgk iigvglgvpg pidvesgtlg stailpgwtg inpsdelsgr
      181 lgvpvyvdnd anlgalgelv wgggrgvkdl ayikvasgvg aglvidgqiy rgpggtagei
      241 ghitldesgp vcrcgnrgcl etfaaaryvl pllrpshgdg ltmekvvrla rdgdpgcrrv
      301 vadvgrhigs gvanlcnlln psrvvlggdl aeagelvlgp iresvsryai psaarqlsva
      361 pgalggraev lgalalvlse mgdstllesa lptrapaft
//
LOCUS       WP_392326333             465 aa            linear   BCT 20-JAN-2025
DEFINITION  SWIM zinc finger family protein [Streptomyces sp. NPDC015127].
ACCESSION   WP_392326333
VERSION     WP_392326333.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015127
  ORGANISM  Streptomyces sp. NPDC015127
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Hassan,I.U., Rehman,H.M., Liu,Z., Zhou,L., Samma,M.K., Wang,C.,
            Rong,Z., Qi,X., Cai,D. and Zhao,H.
  TITLE     Genome-wide identification and spatiotemporal expression profiling
            of zinc finger SWIM domain-containing protein family genes
  JOURNAL   Zool Res 44 (3), 663-674 (2023)
   PUBMED   37161653
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     SWIM, a novel Zn-chelating domain present in bacteria, archaea and
            eukaryotes
  JOURNAL   Trends Biochem Sci 27 (8), 384-386 (2002)
   PUBMED   12151216
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10516955
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Streptomyces sp. NPDC015127"
                     /db_xref="taxon:3364939"
     Protein         1..465
                     /product="SWIM zinc finger family protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=49083
     Region          <421..443
                     /region_name="SWIM"
                     /note="SWIM zinc finger; pfam04434"
                     /db_xref="CDD:309540"
ORIGIN      
        1 mtrslqafay srasalvsaq dsrllglets sgltprgaea hphffsgfla spqaaargll
       61 avadvaaary hdptvrpild pvvtgngdrl rfesfsgcng vyarldvlpe gldgadtghg
      121 ttnvdvnnpl realsrltgd dplhlrvgpd qlavttlega vvekkvplpd rwlrgfaeaq
      181 vatvgfdlra elpaaeavrf lrslprgsgg strglqwvvp agqtlrpttr pgpgavclpa
      241 perlaalqrv lrqarslrvy gpvcdglpta sawevvlpgm rltltlspda srgfsgeggv
      301 lealateeaa qdaelvsvll awepridpad laaqsgltpe rvraaltrlg tagrvgydla
      361 daayfhrelp ydadraerhn prltaarglv cagavdlsge patvrsderr yqvrdtggal
      421 sctcqwwtgh qgrrgpckha lavrmarrga tvpagaasst tggnr
//
LOCUS       WP_392326589             812 aa            linear   BCT 20-JAN-2025
DEFINITION  GcvT family protein [Streptomyces sp. NPDC015127].
ACCESSION   WP_392326589
VERSION     WP_392326589.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015127
  ORGANISM  Streptomyces sp. NPDC015127
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 812)
  AUTHORS   Stauffer,L.T., Ghrist,A. and Stauffer,G.V.
  TITLE     The Escherichia coli gcvT gene encoding the T-protein of the
            glycine cleavage enzyme system
  JOURNAL   DNA Seq 3 (6), 339-346 (1993)
   PUBMED   8219277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..812
                     /organism="Streptomyces sp. NPDC015127"
                     /db_xref="taxon:3364939"
     Protein         1..812
                     /product="GcvT family protein"
                     /calculated_mol_wt=88799
     Region          5..385
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
     Region          370..426
                     /region_name="FAO_M"
                     /note="FAD dependent oxidoreductase central domain;
                     pfam16350"
                     /db_xref="CDD:465100"
     Region          421..812
                     /region_name="GcvT"
                     /note="Glycine cleavage system protein T
                     (aminomethyltransferase) [Amino acid transport and
                     metabolism]; COG0404"
                     /db_xref="CDD:440173"
ORIGIN      
        1 magprvviig agvvgaalad eisergwtdv tvvdqgplpa tggstshapg lvfqtnsskt
       61 mtemarytve kfcsldvegk pcflqvggle vattperlae lhrrhgwita wgiesrilta
      121 aecvekhplv drdkvlggll vptdglakav laveaqirra tergvrflar hevldvlkad
      181 gevtgvltdq geipadivvc cagiwgpkia rmvgmnlplt plahqlawtg pipalasqte
      241 eavrpilrhq dadlyyrdrf dglgigyygh rpmpisaddi lsvdeademp svlkfteedf
      301 eqawsetqal lpstreakve eginglfsft tdnfpllges pdvkgfwvae avwvthsagv
      361 gramaewlvd ghcssfdlhe cdvnrfephq lspeyvlard cqnfvevydi lhplqpsgdp
      421 rpirtspfha rqqehgaffl easgwerpqw yeanaqlveg rsiptpndwa aqfwspivga
      481 eaqatretva mydmtalkrl evsgpgsaef lerlctskva ksvgsvtytl lldhdggirs
      541 ditvarlard vfqvgangnl dldwfsrhlp adgtvqvrdi tqgtcciglw gplarkvlqp
      601 ltdedfsndg lkyfrakray igsvpvtamr lsyvgelgwe lyttadqglk lwdtlwqaag
      661 plggviagrg afnslrlekg yrsfgtdmty ehdpyeagvg favkldkgdf igkaalerrk
      721 advrrkltcl tiddphsvvl gkepvydgdr avgyvtsaay gytigkgiay awlpaelatp
      781 gtpvqigyfd qrveavvaee plfdptmsrl rg
//
LOCUS       WP_392328183             217 aa            linear   BCT 20-JAN-2025
DEFINITION  nicotinamide mononucleotide transporter family protein
            [Streptomyces sp. NPDC015127].
ACCESSION   WP_392328183
VERSION     WP_392328183.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015127
  ORGANISM  Streptomyces sp. NPDC015127
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Hemberger,S., Pedrolli,D.B., Stolz,J., Vogl,C., Lehmann,M. and
            Mack,M.
  TITLE     RibM from Streptomyces davawensis is a riboflavin/roseoflavin
            transporter and may be useful for the optimization of riboflavin
            production strains
  JOURNAL   BMC Biotechnol 11, 119 (2011)
   PUBMED   22136195
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Zhu,N., Olivera,B.M. and Roth,J.R.
  TITLE     Genetic characterization of the pnuC gene, which encodes a
            component of the nicotinamide mononucleotide transport system in
            Salmonella typhimurium
  JOURNAL   J Bacteriol 171 (8), 4402-4409 (1989)
   PUBMED   2546921
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Streptomyces sp. NPDC015127"
                     /db_xref="taxon:3364939"
     Protein         1..217
                     /product="nicotinamide mononucleotide transporter family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0034257 - nicotinamide riboside
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_process="GO:0034258 - nicotinamide riboside transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23287
     Region          11..209
                     /region_name="PnuC"
                     /note="Nicotinamide riboside transporter PnuC [Coenzyme
                     transport and metabolism]; COG3201"
                     /db_xref="CDD:442434"
ORIGIN      
        1 msalswlnte aftlfgqhim wsdmigntig lvalalgwrr svltwpaqll sgvvlvgaya
       61 sahlsggvgk qllvigvaaw gwhqwtrgrr qaqdgsiavr fatwkergll aagavlgtla
      121 vgalftayps lswspwaday ifvgtlvamv aqarglvefw fawllvdlvg vplafssgla
      181 fsglvyviyf alvvwgaydw wqrsrqsaap alegvaa
//
LOCUS       WP_392329441             991 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces sp.
            NPDC014861].
ACCESSION   WP_392329441
VERSION     WP_392329441.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014861
  ORGANISM  Streptomyces sp. NPDC014861
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 991)
  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 991)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 991)
  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 991)
  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 18640657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..991
                     /organism="Streptomyces sp. NPDC014861"
                     /db_xref="taxon:3364923"
     Protein         1..991
                     /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=103359
     Region          <647..853
                     /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          810..990
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          932..986
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mttvphgtlp arapggagpa apvgreella rletvlharg ralltgpagv gktevalaaa
       61 araetrgetv lwlaalpadr aipgaaaaal vasvaatvtw pgpraeagpl gddtpagpag
      121 lsgpgslptg vfasgvfddl pgpqrtavam lcreapiqqg gwdpialrlg iarilralts
      181 rgpvllvvdg aefldpdstd llrfalhlap pslrviavet pepygdthra dgsapgtpgr
      241 phtggsahlw vpseadlllv pplhadeiae llihhrlpsr magrihrasg gnprlalavg
      301 rsladartpv hhaealtlsg rardlarqll gaapppvrat lllaalalrp satlvrragr
      361 peaeaelaaa eraglislae dgslaftagl lpstlvhdac waersaghaa laevvddpve
      421 avrhralatd rpdeelaaev aaaaeaarrr gnnalaaela llaaestpgr dgaqriarlv
      481 daaeeaaraa radlamratt dllardaspt drvrarlavl dtagqgltdl ddmyvhamed
      541 segetalraa vqlrlavkyv ladgdpersr taamesaala asvgdprtaa qaltvqarme
      601 ralgspdsep vlararelel terplgirna aqiltirhal fddrltdard elnallplvq
      661 rrgsvedaie lfrtlaeies rigacaaala hagqslaltl eaglspgpaw yalalaetag
      721 gslgraasya rrsvqaseee gdrvflsrsr yalgrvqlin gdvaaaletl rrvqtderaq
      781 stvdpsmlrw heelaealla hdavedaltl laevrpvaer lgrttvllgc draqalclaa
      841 egrtdeaael ltrtagrfae aglpleqgra lmalarverk rrrrsaaqsa lhgaatvfer
      901 agaapwlala teapagelpg aapggeeapt alaslteael rlarlvgqga snqeaaaklf
      961 lsvktvearl triyqkldvr srsqlatalr p
//
LOCUS       WP_392329737             434 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC014861].
ACCESSION   WP_392329737
VERSION     WP_392329737.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014861
  ORGANISM  Streptomyces sp. NPDC014861
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 434)
  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 434)
  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
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 434)
  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   5  (residues 1 to 434)
  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   6  (residues 1 to 434)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 434)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 434)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Streptomyces sp. NPDC014861"
                     /db_xref="taxon:3364923"
     Protein         1..434
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45170
     Region          10..>60
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          80..402
                     /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 mtrpngrtvr dlrrenrtav lrrlyfdgpm srfslgpatg lssgsisnvv aelvaeglve
       61 eagsvdsagg rprillrvap asgrmigvdv getririelf dltltelart erplapaaeg
      121 aeryevgivv dhiregiaev lrtadvpaea llgvgvgvpg ivehpaggga lvhgqtvgwd
      181 avplerllre avelpaevpy ridngaktlg qaemwfgagr gassavvvlf gsgvgacvtt
      241 dppapgrale wghlkvqvrg rrcrcgalgc leayagaeal lerwreagge ppagageeaa
      301 laamtaaahp sdggepdaaa vavlaetaey lgagfadlin lfqperilvg gwaglllgtr
      361 flaeverhar ayalaypaar vtlglgtlgp davtvgaail pladffargg rredpapaee
      421 ppawtetvrd rtah
//
LOCUS       WP_392330576             233 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease H family protein [Streptomyces sp. NPDC014861].
ACCESSION   WP_392330576
VERSION     WP_392330576.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014861
  ORGANISM  Streptomyces sp. NPDC014861
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 233)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Streptomyces sp. NPDC014861"
                     /db_xref="taxon:3364923"
     Protein         1..233
                     /product="ribonuclease H family protein"
                     /EC_number="3.1.26.4"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=24270
     Region          4..141
                     /region_name="RNase_HI_prokaryote_like"
                     /note="RNase HI family found mainly in prokaryotes;
                     cd09278"
                     /db_xref="CDD:260010"
     Site            order(10..13,45..47,50,72,122)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260010"
ORIGIN      
        1 mlekiiaacd gaskgnpgpa awawvigrad gtvdrweagp lgratnnvae ltalerllet
       61 ldpaapaeir mdsqyamkav ttwlpgwrrk gwktaagtpv ankdlvvrid alltgrdvdf
      121 vytpahqadg dplndaadra ashsartqep lgsdagsalp dpepasarss apraprnras
      181 apggsgasga rrsrpsggtl kakfpgrcrc graydkgeni aknaegwghp tcv
//
LOCUS       WP_392330911             278 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Streptomyces sp.
            NPDC014861].
ACCESSION   WP_392330911
VERSION     WP_392330911.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014861
  ORGANISM  Streptomyces sp. NPDC014861
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 278)
  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 278)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Streptomyces sp. NPDC014861"
                     /db_xref="taxon:3364923"
     Protein         1..278
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=28324
     Region          2..259
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mplaptgdii gpasagdrgv gafnvvqieh aeaivagaer aglpvilqis entvryhgal
       61 apiaaaslsl adaasvpvav hldhaettal vheavalgfs svmfdasrlp yganvaatra
      121 itdhchragv wveaelgevg gkdgahapgv rtdpgearaf aaatavdala vavgsshaml
      181 trdavldldl itrlreslgi plvlhgssgv gdedlvkava agmtkvnist hlnqlftrti
      241 rerlaeapgv adprrylgpa reavaaevar llgllagr
//
LOCUS       WP_392331298             255 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Streptomyces sp.
            NPDC014861].
ACCESSION   WP_392331298
VERSION     WP_392331298.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014861
  ORGANISM  Streptomyces sp. NPDC014861
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 255)
  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 255)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Streptomyces sp. NPDC014861"
                     /db_xref="taxon:3364923"
     Protein         1..255
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28011
     Region          2..254
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 mrvhvvsdvh gnsgalarag dgadaliclg dlvlfldyad hsrgifpdlf gvanadrive
       61 lrtarrfdea rdlgrslwag lavdretaie aavrrqyael faafptptya tygnvdiptl
      121 wpeyarpgtt vldgqrielg gltfgfvggg lrtpmrtpye ipdeeyaakv ealgevdvlc
      181 shippevpdl tydtvarrfe rgsralldai hrtrprwslf ghvhqplarr mrigatecvn
      241 vghfaaggrp fvlew
//
LOCUS       WP_392332670             267 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC014861].
ACCESSION   WP_392332670
VERSION     WP_392332670.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014861
  ORGANISM  Streptomyces sp. NPDC014861
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Streptomyces sp. NPDC014861"
                     /db_xref="taxon:3364923"
     Protein         1..267
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30042
     Region          5..56
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          84..262
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mfkalgkilk vlrqnaglsq aqlaadthcs edlvsamerg vrtpqpefll raedvlragg
       61 vlaaavedte raiararvrh pdwfrsfaaa esvavalhyy apqvvpgilq thayaeavfr
      121 hhrplyeede iekrlndrla rqvllerrpa ptisfviees vlhrpmggre afreqirhia
      181 evsglrnvhl qimpnertdh palegqftll tlkgkrevay aesygtarlf tdpeeartya
      241 erygimraqa ltpleslehl kqllgev
//
LOCUS       WP_392332710             288 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC014861].
ACCESSION   WP_392332710
VERSION     WP_392332710.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014861
  ORGANISM  Streptomyces sp. NPDC014861
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   3  (residues 1 to 288)
  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 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 16111081
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces sp. NPDC014861"
                     /db_xref="taxon:3364923"
     Protein         1..288
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32192
     Region          36..84
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(37,41,66)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(40,65)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(47..48,59,62,66..67)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          106..283
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 msvdevdgvv vedagwevdp gdepgkaila tvgrqlktwr eargmsaaef ggltgygedm
       61 irklergdri prpefldrad tvldanglva emrqdiaevr ypkpirdlak legravefcm
      121 ysnfnvhgll qteefsraim qtwrpafgpe qlerylaarv arrevlektp apefsfiqee
      181 vslrrpiggk mvlrrqlehl levselshve iqvmptahad hpgnggrial lkfvdgtavg
      241 rmdgdfggrp vsdlkrlril dlrygiirtq altpaesrdf ieqllget
//
LOCUS       WP_392332917             517 aa            linear   BCT 20-JAN-2025
DEFINITION  complex I subunit 4 family protein [Streptomyces sp. NPDC014861].
ACCESSION   WP_392332917
VERSION     WP_392332917.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014861
  ORGANISM  Streptomyces sp. NPDC014861
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 517)
  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 517)
  AUTHORS   Galemou Yoga,E., Angerer,H., Parey,K. and Zickermann,V.
  TITLE     Respiratory complex I - Mechanistic insights and advances in
            structure determination
  JOURNAL   Biochim Biophys Acta Bioenerg 1861 (3), 148153 (2020)
   PUBMED   31935361
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Friedrich,T. and Scheide,D.
  TITLE     The respiratory complex I of bacteria, archaea and eukarya and its
            module common with membrane-bound multisubunit hydrogenases
  JOURNAL   FEBS Lett 479 (1-2), 1-5 (2000)
   PUBMED   10940377
REFERENCE   4  (residues 1 to 517)
  AUTHORS   Walker,J.E.
  TITLE     The NADH:ubiquinone oxidoreductase (complex I) of respiratory
            chains
  JOURNAL   Q Rev Biophys 25 (3), 253-324 (1992)
   PUBMED   1470679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Streptomyces sp. NPDC014861"
                     /db_xref="taxon:3364923"
     Protein         1..517
                     /product="complex I subunit 4 family protein"
                     /GO_component="GO:0045271 - respiratory chain complex I
                     [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048039 - ubiquinone binding [Evidence
                     IEA]"
                     /GO_process="GO:0015990 - electron transport coupled
                     proton transport [Evidence IEA]"
                     /GO_process="GO:0042773 - ATP synthesis coupled electron
                     transport [Evidence IEA]"
                     /calculated_mol_wt=53321
     Region          4..514
                     /region_name="NuoM"
                     /note="NADH:ubiquinone oxidoreductase subunit 4 (chain M)
                     [Energy production and conversion]; COG1008"
                     /db_xref="CDD:440632"
ORIGIN      
        1 mqfllvliva apllgavaal lpappglkgk speqavlrhg vtvtgvilla alaltlgfdh
       61 ddpsrmqatt diswiraldv rihlgvdgis lpllvltall tflcalysff kppagpspka
      121 fvalllvlea gtlatfavld lvlfflafem vlvpmyflia rwggegrraa agkfilytll
      181 gsvimllgll ligveagtfd mvalatdngr glttsvqvta vlaigvglav ktpmwplhsw
      241 lpdahtaapt vgsvllagvl lkmgtygfvr ialpiapdgm htlapylaaf aaagivygsl
      301 aclalarpga kgdlkrliay ssvghmgfvl lgiatltptg vngalfania hglitgllff
      361 lvgalkdryg tadldtlaga tgaalygrap rlgallafaa vaslglpgla gfwgemlalf
      421 aafdpaegln rtaylvfmal gglgtlltaa yllivvrrvc mggprpagep eladvqpyel
      481 aawtplvalt vlaglwpavl lgltdpavqq llaggtq
//
LOCUS       WP_392333238             383 aa            linear   BCT 20-JAN-2025
DEFINITION  threonine synthase [Streptomyces sp. NPDC014861].
ACCESSION   WP_392333238
VERSION     WP_392333238.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014861
  ORGANISM  Streptomyces sp. NPDC014861
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 383)
  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 383)
  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   3  (residues 1 to 383)
  AUTHORS   Parsot,C.
  TITLE     Evolution of biosynthetic pathways: a common ancestor for threonine
            synthase, threonine dehydratase and D-serine dehydratase
  JOURNAL   EMBO J 5 (11), 3013-3019 (1986)
   PUBMED   3098560
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423064
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Streptomyces sp. NPDC014861"
                     /db_xref="taxon:3364923"
     Protein         1..383
                     /product="threonine synthase"
                     /EC_number="4.2.3.1"
                     /GO_function="GO:0004795 - threonine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009088 - threonine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40708
     Region          15..381
                     /region_name="ThrC"
                     /note="Threonine synthase [Amino acid transport and
                     metabolism]; COG0498"
                     /db_xref="CDD:440264"
ORIGIN      
        1 mnaeqhstvy dlfdrsgrry pldelrwrge dgsplavaal pglrpeqidt aerslwryra
       61 alpvdaarrv slgegctpmi pvhwagrrvh fklewfnpts sfkdrgvsvm mshlvalgad
      121 rvledssgng gcavaayaaa agvrakiiap aatseakilq araygaeiei vsgtrdevad
      181 eairqaekvp yashnwhpmf iqgtktiaye iweslgftap dnvvlvagag stilgcdlaf
      241 gellgagqid rrprlfvgqp ehwatiadtf ngvdpahrga rmptiaegas iarpvrlpea
      301 veairrshga ayavpeaeih aavralssrg lfaeptssva aatldhflat gdiapdettv
      361 vvltgtglks aekmasvfag paa
//
LOCUS       WP_392333966             289 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptomyces sp.
            NPDC014861].
ACCESSION   WP_392333966
VERSION     WP_392333966.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014861
  ORGANISM  Streptomyces sp. NPDC014861
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 289)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 289)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces sp. NPDC014861"
                     /db_xref="taxon:3364923"
     Protein         1..289
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31643
     Region          19..102
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          126..287
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 misalnrlvd lveehlseel dvdalarslg tteyhlrrmf sslagmplse yvrrrrmtva
       61 aadvvrgedd lltvavrhgy gsgeafgraf ravhgagpgd vrrdggplrt qpqlrfrltv
      121 egstpmdtrl vdrpafrlvg hsarvplihe gvnphivrhi salpqeehlr lkalgdtqpe
      181 gllqvsddld ldaaegselt ylhgvaldgd tpvpegldai evqagrwavf rtsgphpqal
      241 qkawaatate wfpsnpwrlr rgpsivavle raddfttatc elwlpvepa
//
LOCUS       WP_392334518             350 aa            linear   BCT 20-JAN-2025
DEFINITION  BMP family lipoprotein [Streptomyces sp. NPDC014861].
ACCESSION   WP_392334518
VERSION     WP_392334518.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014861
  ORGANISM  Streptomyces sp. NPDC014861
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Yousief,S.W., Bahey-El-Din,M. and Zaghloul,T.I.
  TITLE     Immunization with the basic membrane protein (BMP) family ABC
            transporter elicits protection against Enterococcus faecium in a
            murine infection model
  JOURNAL   Microbes Infect 22 (3), 127-136 (2020)
   PUBMED   31585177
REFERENCE   2  (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   3  (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   4  (residues 1 to 350)
  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   5  (residues 1 to 350)
  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 11448319
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Streptomyces sp. NPDC014861"
                     /db_xref="taxon:3364923"
     Protein         1..350
                     /product="BMP family lipoprotein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /calculated_mol_wt=35716
     Region          41..347
                     /region_name="Med"
                     /note="Lipoprotein Med, regulator of KinD/Spo0A, PBP1-ABC
                     superfamily, includes NupN [Signal transduction
                     mechanisms]; COG1744"
                     /db_xref="CDD:441350"
ORIGIN      
        1 mrritrittv giasaalals atacgkssse ggsgsdtkas kaaiaydigg rgdqsfndaa
       61 yaglkkaede ldvdgseaep ssgegdadkv qrltslarag nnpvigvgfa yapaikkvaa
      121 qfpdttfgii ddtsvtgkni anmvfneeqg sylagvaaak asksgtvgfi ggvevplikk
      181 feagyvqgvk dtnpkakvlt qyltqppnfd gfakpdlgka aaegqldkga dviyaaagla
      241 gsgaieaask agkwaigvds dqynqaglae ykdailtsvt kdvsdsvfnl iksvkdgkpq
      301 vgevryglat dgvaladsnp kyksmtdlia avdkakkdii dgkitvktap
//
LOCUS       WP_392334709             132 aa            linear   BCT 20-JAN-2025
DEFINITION  TOBE domain-containing protein [Streptomyces sp. NPDC014861].
ACCESSION   WP_392334709
VERSION     WP_392334709.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014861
  ORGANISM  Streptomyces sp. NPDC014861
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 132)
  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 10007583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Streptomyces sp. NPDC014861"
                     /db_xref="taxon:3364923"
     Protein         1..132
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13757
     Region          9..129
                     /region_name="MopI"
                     /note="Molybdopterin-binding protein MopI [Coenzyme
                     transport and metabolism]; COG3585"
                     /db_xref="CDD:442804"
ORIGIN      
        1 mpsysmgqaa qllgvssetv rrwadggkla mvrdgagrrv iegvdlaafa qergaglhav
       61 peddvptsvr nsfvgivtgv rvddvaaqve vqsgphrlvs lvtreaveel aldvgvtvta
      121 rvkstsvhid lp
//
LOCUS       WP_392335387             538 aa            linear   BCT 20-JAN-2025
DEFINITION  peptide ABC transporter substrate-binding protein [Streptomyces sp.
            NPDC014861].
ACCESSION   WP_392335387
VERSION     WP_392335387.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014861
  ORGANISM  Streptomyces sp. NPDC014861
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 538)
  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 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   3  (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   4  (residues 1 to 538)
  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 538)
  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 11467924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Streptomyces sp. NPDC014861"
                     /db_xref="taxon:3364923"
     Protein         1..538
                     /product="peptide 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=59041
     Region          1..525
                     /region_name="OppA"
                     /note="ABC-type oligopeptide transport system, periplasmic
                     component [Amino acid transport and metabolism]; COG4166"
                     /db_xref="CDD:443327"
ORIGIN      
        1 mrgaksakwv tgaiivalaa tacggsdggt kkdskaagkp egyvsidvge pqnplipadt
       61 nesnggyair alftqllsfd dkgeivltna esvetkdskl wtvklkdgwk fhngeavtak
      121 syvdawnwya naknkqknay wfsdikgydd lnpekgdpka eamsglkvld dstftielkt
      181 kvpyfnyklg yttfaplpkv fyddpkafgl kpvgngpyqf ekwdrkkliq mkafddykgp
      241 nralnkglqf ksyttveaay kdllsgnldi vktvgptdlp kykqdlgega levsfagvqs
      301 lvpawysktf kdidpkvvqg lsmaidrdti tktvlnntrt pakgftppqv kgfqelgeit
      361 efnpakakql itegggvpgn kftiqynsdg ghkewvtavc esirnatgvd cvgdpkpdfp
      421 tdleardanq vkgmyrggwi adypvnvnfl kelyhskaes nsgrfsdkei delmakgdna
      481 nsiedsvkay qevekklaqk mpaiplwyyr tnaghgkavt nvtvdfhgei vlnavtpk
//
LOCUS       WP_392335574             211 aa            linear   BCT 20-JAN-2025
DEFINITION  nicotinamide mononucleotide transporter family protein
            [Streptomyces sp. NPDC014861].
ACCESSION   WP_392335574
VERSION     WP_392335574.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014861
  ORGANISM  Streptomyces sp. NPDC014861
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Hemberger,S., Pedrolli,D.B., Stolz,J., Vogl,C., Lehmann,M. and
            Mack,M.
  TITLE     RibM from Streptomyces davawensis is a riboflavin/roseoflavin
            transporter and may be useful for the optimization of riboflavin
            production strains
  JOURNAL   BMC Biotechnol 11, 119 (2011)
   PUBMED   22136195
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Zhu,N., Olivera,B.M. and Roth,J.R.
  TITLE     Genetic characterization of the pnuC gene, which encodes a
            component of the nicotinamide mononucleotide transport system in
            Salmonella typhimurium
  JOURNAL   J Bacteriol 171 (8), 4402-4409 (1989)
   PUBMED   2546921
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Streptomyces sp. NPDC014861"
                     /db_xref="taxon:3364923"
     Protein         1..211
                     /product="nicotinamide mononucleotide transporter family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0034257 - nicotinamide riboside
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_process="GO:0034258 - nicotinamide riboside transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22888
     Region          8..198
                     /region_name="PnuC"
                     /note="Nicotinamide riboside transporter PnuC [Coenzyme
                     transport and metabolism]; COG3201"
                     /db_xref="CDD:442434"
ORIGIN      
        1 mnwlnseaft ifgqhimwsd migntiglia lalgwrrsil twpaqllsgl ilvgayasan
       61 laggvgkqll vigvaawgww qwnrgrqqaq dgsiavrfat wkergllagg avlgtlavgg
      121 lftlypslsw spwadayifv gtlvamvaqa rglvefwfaw llvdlvgvpl afssglafsg
      181 lvyvvyfalv lwgmrdwwlr trtpalegap a
//
LOCUS       WP_392336234              84 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Pantoea stewartii].
ACCESSION   WP_392336234
VERSION     WP_392336234.1
KEYWORDS    RefSeq.
SOURCE      Pantoea stewartii
  ORGANISM  Pantoea stewartii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 84)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   3  (residues 1 to 84)
  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 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 10007349
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Pantoea stewartii"
                     /db_xref="taxon:66269"
     Protein         1..84
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9496
     Region          9..76
                     /region_name="SfsB"
                     /note="Predicted transcriptional regulator, lambda
                     repressor-like DNA-binding domain [Transcription];
                     COG3423"
                     /db_xref="CDD:442649"
ORIGIN      
        1 mkaqkksqtq sdwhradiva alhkqgwslh rlsihhgyks agslknaldr pwpkgqkiia
       61 eaiglppeai wptrydkrfs gewn
//
LOCUS       WP_392336449             439 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter large permease [Loktanella salsilacus].
ACCESSION   WP_392336449
VERSION     WP_392336449.1
KEYWORDS    RefSeq.
SOURCE      Loktanella salsilacus
  ORGANISM  Loktanella salsilacus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Loktanella.
REFERENCE   1  (residues 1 to 439)
  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 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   3  (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
REFERENCE   4  (residues 1 to 439)
  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 10008688
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Loktanella salsilacus"
                     /db_xref="taxon:195913"
     Protein         1..439
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma 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=48028
     Region          3..438
                     /region_name="FcbT3"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, large permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4664"
                     /db_xref="CDD:443701"
ORIGIN      
        1 msyemiaalm fstmllmmlt gqrvfgaigf vavvaaillw gpggsdmgfs simklmkwna
       61 lltlpmfifm gyvmsesrla edlykmfyvw fgplpgglai gtimlmvmis amnglsvagm
      121 aigatialpe llkrnydklm isgviqggss lgilippsvv lvlfaqiarq pvsqlwlagl
      181 mpgllmatlf viyivvrcrl npslapamsa eeraditwae rirllraall piiifaammi
      241 pfikgwtslt easvigalts vavavikgrf trdvfetatr ntlaitvmfm liimaalsfg
      301 avfdglgagr aienlfvqdl gltpwqilil mqlsflimgm flddtamlvi vapiyvglak
      361 algfdliwyg vlytitcqia yltppfgynl flmralappe ftltliyrsv fpfvlvmllt
      421 lilvmifpqi alwlpekll
//
LOCUS       WP_392336459             401 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator, partial [Loktanella
            salsilacus].
ACCESSION   WP_392336459
VERSION     WP_392336459.1
KEYWORDS    RefSeq.
SOURCE      Loktanella salsilacus
  ORGANISM  Loktanella salsilacus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Loktanella.
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
REFERENCE   3  (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   4  (residues 1 to 401)
  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   5  (residues 1 to 401)
  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   6  (residues 1 to 401)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 401)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 401)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Loktanella salsilacus"
                     /db_xref="taxon:195913"
     Protein         <1..401
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          26..>66
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          86..384
                     /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 skppprpsrt akgknpgrsr ehnrrvvlel lrrggalgrk eladlahist qavtniidel
       61 maenllidmg rkrterglpp iqyainpega itigleiavg altavvldlg gnlrakqqlp
      121 lpdmksdivl dvicetvtrl ratyqaqlmg igvvmpgpfe ieglsgvgpt tlpdwsgvdv
      181 arllnqrcgv pvtvdndana aavgemlfgl gqnvshfcll yfgagvgmgg ivadqplrga
      241 fgnageighi vvapgglpcq cgqagclery vslhaltewm trdgvapdtd alhdlqaagd
      301 pallawldra aphlslmigl lenifdpqtv ilggkmprai lddligrlai ptsvanrrnr
      361 alprvqrgqt gqesaaigaa alpffnaitp qlhqtedqst r
//
LOCUS       WP_392336500             164 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Loktanella salsilacus].
ACCESSION   WP_392336500
VERSION     WP_392336500.1
KEYWORDS    RefSeq.
SOURCE      Loktanella salsilacus
  ORGANISM  Loktanella salsilacus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Loktanella.
REFERENCE   1  (residues 1 to 164)
  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 10007985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Loktanella salsilacus"
                     /db_xref="taxon:195913"
     Protein         1..164
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=18568
     Region          3..164
                     /region_name="COG3786"
                     /note="L,D-peptidoglycan transpeptidase YkuD,
                     ErfK/YbiS/YcfS/YnhG family [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443000"
ORIGIN      
        1 mkaadlvvtp tnlrflgrqf prtigrggfm nrkvegdgat prgvhrivgm lyrpdriaqp
       61 adwavpirpg dlwsddvrdv dynmmvrvph afshedlrra dpmydlviit dwnwpyavkg
      121 rgsaifihqw rgkgrptagc valsrahlhw iaprikhntr lvia
//
LOCUS       WP_392336696             372 aa            linear   BCT 20-JAN-2025
DEFINITION  response regulator [Loktanella salsilacus].
ACCESSION   WP_392336696
VERSION     WP_392336696.1
KEYWORDS    RefSeq.
SOURCE      Loktanella salsilacus
  ORGANISM  Loktanella salsilacus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Loktanella.
REFERENCE   1  (residues 1 to 372)
  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 372)
  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 11467115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Loktanella salsilacus"
                     /db_xref="taxon:195913"
     Protein         1..372
                     /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=40593
     Region          50..>170
                     /region_name="PleD"
                     /note="Two-component response regulator, PleD family,
                     consists of two REC domains and a diguanylate cyclase
                     (GGDEF) domain [Signal transduction mechanisms,
                     Transcription]; COG3706"
                     /db_xref="CDD:442920"
ORIGIN      
        1 mallagiril misivqarlt qrsdegaddv eqlemselgr isrnkgdeaa lrilavdddp
       61 fileliavia ghagltnvvs vgssehalrv lanpgltfdy flfdirmpgl dgielcrrvr
      121 qmpryrdtlv tmltgmrdva ymneafraga sdyvmkpfev adlelrlrla qdaymsgyda
      181 qaapsrrseg tslqlitdgf erlgglwhnr rhhlvdrval snyltqvpqk elgnvsvfav
      241 iiggseashm avseeartvl hndiaaaaae slgpdlaima ytrdadlliv thcthrlhai
      301 slelditrrl snsagtkgat nyenlvisvg vavrlqgake gratfatdra lmlaedriad
      361 kqgrsltalh ks
//
LOCUS       WP_392336855             294 aa            linear   BCT 20-JAN-2025
DEFINITION  transglutaminase family protein [Loktanella salsilacus].
ACCESSION   WP_392336855
VERSION     WP_392336855.1
KEYWORDS    RefSeq.
SOURCE      Loktanella salsilacus
  ORGANISM  Loktanella salsilacus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Loktanella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12090973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Loktanella salsilacus"
                     /db_xref="taxon:195913"
     Protein         1..294
                     /product="transglutaminase family protein"
                     /calculated_mol_wt=31197
     Region          3..83
                     /region_name="Bact_transglu_N"
                     /note="Bacterial transglutaminase-like N-terminal region;
                     pfam08379"
                     /db_xref="CDD:462455"
     Region          69..246
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 miydirltia tdyagfasag rhlvcvmprd lggeqrliag llnlhpapah rhdrvdffgn
       61 avvefainap hqgvevsvqa riektapsaa papslplsal anavarcrdm gpdspvhfta
      121 asprvpldas mtrfaaaqit sdmttaqaii avgralhetm rfdaaattvd tpaseafakr
      181 hgvcqdfshi miaclrgigi pagyvsgylr tqppqgmprl egadamhawv rawcgpnagw
      241 lafdptndrv adqshiivah grdyadvspi rgilrgsggq ksrqsvdvip lget
//
LOCUS       WP_392337666             523 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Loktanella salsilacus].
ACCESSION   WP_392337666
VERSION     WP_392337666.1
KEYWORDS    RefSeq.
SOURCE      Loktanella salsilacus
  ORGANISM  Loktanella salsilacus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Loktanella.
REFERENCE   1  (residues 1 to 523)
  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 11459492
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Loktanella salsilacus"
                     /db_xref="taxon:195913"
     Protein         1..523
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=57577
     Region          1..514
                     /region_name="YcbB"
                     /note="Murein L,D-transpeptidase YcbB/YkuD [Cell
                     wall/membrane/envelope biogenesis]; COG2989"
                     /db_xref="CDD:442228"
ORIGIN      
        1 mfaavmtlwv lgtapaqaqv tafrqavaes aardedlatf yrardfqgiw agddraattr
       61 rnalltalsn agahglpear ynaeeliaql qaattpaqqg amevalstvf ltyardvqtg
      121 iltpskvvpl ivrevplrsr latlqgflqs npdaflralp psspeyarlm reklrlenll
      181 aqggygpavq asslapgasg qavvdlrnrl ilmghldrta tqtydatiqa avqrfqqsmg
      241 lsadgtagsd tmkeinvpld krmqsvivam ererwinrpr glrhiwvnlt dftativdnd
      301 rvtfstrsvi gandtdrqsp efsdvmeymv inpswyvprs ivvneylpql qsnsnavshl
      361 dvtdrsgnvv prgsvkagny tartfpysmr qgpsernalg lvkfmfpnky niylhdtpsk
      421 slfsresraf shgcirlndp fdfayallak qesnpealfq srlktgaesr vtleepvpvh
      481 ivyrtaftnv tgalqfrrdv ygrdaaiwna lsqtgvavra vqg
//
LOCUS       WP_392338107             816 aa            linear   BCT 20-JAN-2025
DEFINITION  GcvT family protein [Loktanella salsilacus].
ACCESSION   WP_392338107
VERSION     WP_392338107.1
KEYWORDS    RefSeq.
SOURCE      Loktanella salsilacus
  ORGANISM  Loktanella salsilacus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Loktanella.
REFERENCE   1  (residues 1 to 816)
  AUTHORS   Stauffer,L.T., Ghrist,A. and Stauffer,G.V.
  TITLE     The Escherichia coli gcvT gene encoding the T-protein of the
            glycine cleavage enzyme system
  JOURNAL   DNA Seq 3 (6), 339-346 (1993)
   PUBMED   8219277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..816
                     /organism="Loktanella salsilacus"
                     /db_xref="taxon:195913"
     Protein         1..816
                     /product="GcvT family protein"
                     /calculated_mol_wt=89254
     Region          7..385
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
     Region          371..426
                     /region_name="FAO_M"
                     /note="FAD dependent oxidoreductase central domain;
                     pfam16350"
                     /db_xref="CDD:465100"
     Region          420..816
                     /region_name="GcvT"
                     /note="Glycine cleavage system protein T
                     (aminomethyltransferase) [Amino acid transport and
                     metabolism]; COG0404"
                     /db_xref="CDD:440173"
ORIGIN      
        1 mavlpssarv viigggisgc svayhlaklg wtdivllerk kltsgttwha aglvgqlras
       61 qnmtrlakys adlystleae tglatglrqc gsitvaltae rqeelrrqaa marvfgvevn
      121 elspsdilsl yphlnmkdvv sgvhlpgdgq adpgnialal akgarmlgaq ivegvivnev
      181 tqadgrvtgv twqqgeetgt iatghvvncc gmwgrdlaar ngvtlplhac ehfyivtesi
      241 pglaqlpvlr vpdecayyke dagkillgaf epkakpwgmd gipadfcfdq lpedfdhfep
      301 ileaavnrmp ilaeagihtf fngpesftpd dryylgeape ltgywvaagy nsigivssgg
      361 agmalaqwmn dgeppfdlwe vdirraqpfq knrrylrerv tetlgllyad hfpyrqmats
      421 rgirrsplhe hlkargavfg evagweranw fadegqtaqy eytwgrpnwf qnsraehmal
      481 retvglldmt sfgkirvegr daltflqric anqmdvaigr ivytqmlner ggiecdltvt
      541 rlseaafflv vpgatlqrdl awlrrhlgde fvvitdvtaa eavlplmgpn arnllsaisp
      601 adlsndehpf gtareievgm tlarahrvty vgelgwelyv psdqaahvfe alveagadhg
      661 lklcglhamd scriekgyrh fghditdedh vleaglgfav ktdkgafigr eavlrkrdag
      721 larrmlqfrl tdpepllfhn epvlrdgviv gyltsgnygh alggavglgy vpcrhagetv
      781 eetltstyqi dvagrmvgae aslsplydpk sqrirv
//
LOCUS       WP_392338595             310 aa            linear   BCT 20-JAN-2025
DEFINITION  response regulator [Loktanella salsilacus].
ACCESSION   WP_392338595
VERSION     WP_392338595.1
KEYWORDS    RefSeq.
SOURCE      Loktanella salsilacus
  ORGANISM  Loktanella salsilacus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Loktanella.
REFERENCE   1  (residues 1 to 310)
  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 310)
  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 11467115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Loktanella salsilacus"
                     /db_xref="taxon:195913"
     Protein         1..310
                     /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=34941
     Region          1..>124
                     /region_name="PleD"
                     /note="Two-component response regulator, PleD family,
                     consists of two REC domains and a diguanylate cyclase
                     (GGDEF) domain [Signal transduction mechanisms,
                     Transcription]; COG3706"
                     /db_xref="CDD:442920"
ORIGIN      
        1 mkilivdddv fiiellgmal eamgfanfea annahealam vkrandpyec flidiqmpgm
       61 dgmelcrelr qdqaykrtpi imltamsdre yiqksfsaga ndyivkpfqf ndlmarieta
      121 arlsrqitst drlvrqiasa cqgqgilsgl kfedavsfeg ttgyleqpaf rnyidrmers
      181 qfrlggvasv kfqnplqlfe nstpqeflgl lsdisealsv alrqeqchft yggygcflvm
      241 kvateksnfq teleflvrke lsridlrhpa sdlnpiemsv grvflktsgd fdsidetllr
      301 arqrtqikca
//
LOCUS       WP_392338928             130 aa            linear   BCT 20-JAN-2025
DEFINITION  bactofilin family protein [Loktanella salsilacus].
ACCESSION   WP_392338928
VERSION     WP_392338928.1
KEYWORDS    RefSeq.
SOURCE      Loktanella salsilacus
  ORGANISM  Loktanella salsilacus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Loktanella.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Deng,X., Gonzalez Llamazares,A., Wagstaff,J.M., Hale,V.L.,
            Cannone,G., McLaughlin,S.H., Kureisaite-Ciziene,D. and Lowe,J.
  TITLE     The structure of bactofilin filaments reveals their mode of
            membrane binding and lack of polarity
  JOURNAL   Nat Microbiol 4 (12), 2357-2368 (2019)
   PUBMED   31501539
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Ingerson-Mahar,M. and Gitai,Z.
  TITLE     A growing family: the expanding universe of the bacterial
            cytoskeleton
  JOURNAL   FEMS Microbiol Rev 36 (1), 256-266 (2012)
   PUBMED   22092065
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Kuhn,J., Briegel,A., Morschel,E., Kahnt,J., Leser,K., Wick,S.,
            Jensen,G.J. and Thanbichler,M.
  TITLE     Bactofilins, a ubiquitous class of cytoskeletal proteins mediating
            polar localization of a cell wall synthase in Caulobacter
            crescentus
  JOURNAL   EMBO J 29 (2), 327-339 (2010)
   PUBMED   19959992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Loktanella salsilacus"
                     /db_xref="taxon:195913"
     Protein         1..130
                     /product="bactofilin family protein"
                     /calculated_mol_wt=12941
     Region          16..130
                     /region_name="CcmA"
                     /note="Cytoskeletal protein CcmA, bactofilin family
                     [Cytoskeleton]; COG1664"
                     /db_xref="CDD:441270"
ORIGIN      
        1 malvsdtsps sagagsnggr shfaagakls gdltvpglme lsghidgkit adsivieang
       61 saigellads vaikgrfdgs ilgqdvilhs sakvsgeify qtltiengae vnsscfrqns
      121 setekagsas
//
LOCUS       WP_392339998             619 aa            linear   BCT 20-JAN-2025
DEFINITION  sensor histidine kinase [Moritella marina].
ACCESSION   WP_392339998
VERSION     WP_392339998.1
KEYWORDS    RefSeq.
SOURCE      Moritella marina
  ORGANISM  Moritella marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Moritellaceae; Moritella.
REFERENCE   1  (residues 1 to 619)
  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 619)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20493667
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Moritella marina"
                     /db_xref="taxon:90736"
     Protein         1..619
                     /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=69490
     Region          34..275
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          <332..587
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mlttrkflig fylisliivs swvwrsgyak lvsqsnqqld ifathlqsql qrfdaipkll
       61 fdqkqvvasl qdpdnsqlqq ktnrylkhvn ntigasdtyl idingttiaa nnwrdkqtfi
      121 gknfafrpyf qqavsgqqgr yfalgttsgq rgyyfsspvi nagniigvvv vkmdlskiek
      181 ewtgkqahfm vtdddnvifi sntqswllhs ltplsaeklq ridrsrrygn ktiaalnftg
      241 qlednpallq lttskpfatn ylsmskhmpt agwtvrvftp lttifidiai glvllslvfw
      301 llnlrlklsm hkhqrakdke qlriktkykl kqevkrrtad lnneiierqk meqtlrdtqk
      361 eliqtaklav lgqlsasish elnnplaair syadnalvfl qreqyqstdd nlqriihlte
      421 rmakissqlk ffarkssgel hpvpllnvin maielvkpql ksnqvaitld danievlvnv
      481 dqvqleqvlv nllsnamqav eessnkhihv slcrvqqqvi vqvddsgpgi skdnlsqlfd
      541 pffttketgl glglsishki mrnmqgniia enrpnagarf slslpltmvp tattsattip
      601 ataipvtttq atiypqapv
//
LOCUS       WP_392341140             122 aa            linear   ENV 20-JAN-2025
DEFINITION  YaaA family protein, partial [uncultured Shewanella sp.].
ACCESSION   WP_392341140
VERSION     WP_392341140.1
KEYWORDS    ENV; RefSeq.
SOURCE      uncultured Shewanella sp.
  ORGANISM  uncultured Shewanella sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella; environmental samples.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Liu,Y., Bauer,S.C. and Imlay,J.A.
  TITLE     The YaaA protein of the Escherichia coli OxyR regulon lessens
            hydrogen peroxide toxicity by diminishing the amount of
            intracellular unincorporated iron
  JOURNAL   J Bacteriol 193 (9), 2186-2196 (2011)
   PUBMED   21378183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10011746
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="uncultured Shewanella sp."
                     /db_xref="taxon:173975"
                     /environmental_sample
     Protein         1..>122
                     /product="YaaA family protein"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
     Region          1..>122
                     /region_name="PRK02101"
                     /note="peroxide stress protein YaaA"
                     /db_xref="CDD:234999"
ORIGIN      
        1 mlvlvspakt ldfenppitn thsqpcllkq sqalidicre ltpmdiaslm kvsdkiagln
       61 aarfadwqpp fsldnakqai fafrgdvytg fdadhlsepq iassqkhlri lsglygllkp
      121 ld
//
LOCUS       WP_392342254             806 aa            linear   BCT 20-JAN-2025
DEFINITION  GcvT family protein [Phaeobacter sp. BS52].
ACCESSION   WP_392342254
VERSION     WP_392342254.1
KEYWORDS    RefSeq.
SOURCE      Phaeobacter sp. BS52
  ORGANISM  Phaeobacter sp. BS52
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Phaeobacter.
REFERENCE   1  (residues 1 to 806)
  AUTHORS   Stauffer,L.T., Ghrist,A. and Stauffer,G.V.
  TITLE     The Escherichia coli gcvT gene encoding the T-protein of the
            glycine cleavage enzyme system
  JOURNAL   DNA Seq 3 (6), 339-346 (1993)
   PUBMED   8219277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..806
                     /organism="Phaeobacter sp. BS52"
                     /db_xref="taxon:2907241"
     Protein         1..806
                     /product="GcvT family protein"
                     /calculated_mol_wt=88863
     Region          4..381
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
     Region          367..420
                     /region_name="FAO_M"
                     /note="FAD dependent oxidoreductase central domain;
                     pfam16350"
                     /db_xref="CDD:465100"
     Region          415..806
                     /region_name="GcvT"
                     /note="Glycine cleavage system protein T
                     (aminomethyltransferase) [Amino acid transport and
                     metabolism]; COG0404"
                     /db_xref="CDD:440173"
ORIGIN      
        1 mrseaqavvi gggvigcsil yhltklgwsd vvllerdelt sgstwhaaan ihglhdstni
       61 sriqhytmtl ykeleaetgq scgvfqpgsl ylaqteereh qlklqaakak lygmnfyeis
      121 leeakrlnpl vnydgircvm yepdggnvdp sgvtnayavg arqrgaeihr ftpvtateqq
      181 adgswlvktp kgdihtpwvv naaglwgrev aalagielpl qptehqyfvt etmadvenhg
      241 trlpsvsdrd geyylrqegq gllvgayekd mkfwaedgtp ldfahdlfpd dleriednmm
      301 naierlpavg eagikrving pmiwspdanv lmgpvpeldg yfccngiipg fsqsggmglm
      361 aaqwiieget qydmfawdma rfdgwatkef tkarvqdqya hrfaihfpne ersagrpart
      421 rpiyalqaem gavfglnagw ehplwfadtp gakdtngftr qnwwgpvgee crmlrnragi
      481 idisnfakyr cagpdaeawl navfantmpk avgrscltpl iskrggiagd ftvtrvaede
      541 fwiigsgmae ryhkrffkev plpagtvfes ktddtcgfnv agpksremlq rltntslate
      601 dfpfmrsati dlagievlal rvsftgdlgw elhcksedqq rlyaillaag eeysagpvgs
      661 ralmslrvek gygswsreys peywphevgl drlcklqkdf lnkgsvqgvl enpareqlvl
      721 lhldemetea snadatggep ifkdgkgigr vtsgaygysv gmslalgfvr dagpgdevqv
      781 mvlgrphrav ileqppfdpa gtilrg
//
LOCUS       WP_392343362             344 aa            linear   BCT 20-JAN-2025
DEFINITION  PDDEXK nuclease domain-containing protein [Pseudoalteromonas
            prydzensis].
ACCESSION   WP_392343362
VERSION     WP_392343362.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas prydzensis
  ORGANISM  Pseudoalteromonas prydzensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 344)
  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 10008845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Pseudoalteromonas prydzensis"
                     /db_xref="taxon:182141"
     Protein         1..344
                     /product="PDDEXK nuclease domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39793
     Region          1..338
                     /region_name="YhcG"
                     /note="Predicted nuclease of restriction endonuclease-like
                     (RecB) superfamily, DUF1016 family [General function
                     prediction only]; COG4804"
                     /db_xref="CDD:443832"
ORIGIN      
        1 msnltslapl sqelsalihs akqraavavn seitllywqv gnrinqavlg geradygkrv
       61 iatlsneltg qfgkgwskrn laqmvkfaev fwdieivhal rtqlswthir qliaidepik
      121 rdfyttmaiq erwstrtlde rigallfert aiskkpddti vaelselrnt gqynqelllk
      181 dpyildflel ndrylekdle dailrdieqf llelgagfsf varqkriqid nddfyidllf
      241 ynrklkrlva idlklekfkh shksqmelyl nwlkkyetee genpplgiil csskkqeqie
      301 llemegsdih vaeylthlmd velleqklqh siakakqrln kkdg
//
LOCUS       WP_392344445              33 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Pseudoalteromonas
            prydzensis].
ACCESSION   WP_392344445
VERSION     WP_392344445.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas prydzensis
  ORGANISM  Pseudoalteromonas prydzensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 33)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 33)
  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 33)
  AUTHORS   Tyrrell,R., Verschueren,K.H., Dodson,E.J., Murshudov,G.N., Addy,C.
            and Wilkinson,A.J.
  TITLE     The structure of the cofactor-binding fragment of the LysR family
            member, CysB: a familiar fold with a surprising subunit arrangement
  JOURNAL   Structure 5 (8), 1017-1032 (1997)
   PUBMED   9309218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444001
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..33
                     /organism="Pseudoalteromonas prydzensis"
                     /db_xref="taxon:182141"
     Protein         1..33
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=3608
     Region          8..>33
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
ORIGIN      
        1 mwhgldeflh vvehgsftqa akamevstsh isr
//
LOCUS       WP_392344723             583 aa            linear   BCT 20-JAN-2025
DEFINITION  SWIM zinc finger family protein [Pseudoalteromonas prydzensis].
ACCESSION   WP_392344723
VERSION     WP_392344723.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas prydzensis
  ORGANISM  Pseudoalteromonas prydzensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 583)
  AUTHORS   Hassan,I.U., Rehman,H.M., Liu,Z., Zhou,L., Samma,M.K., Wang,C.,
            Rong,Z., Qi,X., Cai,D. and Zhao,H.
  TITLE     Genome-wide identification and spatiotemporal expression profiling
            of zinc finger SWIM domain-containing protein family genes
  JOURNAL   Zool Res 44 (3), 663-674 (2023)
   PUBMED   37161653
REFERENCE   2  (residues 1 to 583)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     SWIM, a novel Zn-chelating domain present in bacteria, archaea and
            eukaryotes
  JOURNAL   Trends Biochem Sci 27 (8), 384-386 (2002)
   PUBMED   12151216
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Pseudoalteromonas prydzensis"
                     /db_xref="taxon:182141"
     Protein         1..583
                     /product="SWIM zinc finger family protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=66595
     Region          1..>275
                     /region_name="SWIM"
                     /note="Uncharacterized protein, contains SWIM-type Zn
                     finger domain [Function unknown]; COG4715"
                     /db_xref="CDD:443750"
ORIGIN      
        1 mfdlndiqqr tasktfdlgc elyasnsvsk lliidnqama svmgqykykv sleksasgqc
       61 lasctcpaad yqeickhava valkvnslsa aeleevnang ttqdnersel iawfldkpsd
      121 eltniimgfl deseheydkw almmsndkqa ldaselskli tkalpktpvw gwnevssyfa
      181 gadslfelil paiaklpveq qwkltlkalv rlndvleeid dsggfrfeie gqlnqnlsel
      241 fnqlpwsdeq kaqwifehfa dykydvfprv pedfeitpsv nalflsqcta aiekrlqagv
      301 dfddwrqksa ltrltsvlik haqaqddwqq qlrlikitah dsadylkita lckarndlld
      361 aeyylkqayq rahkphella ckrdeidirl elsefkaawa iawqifadnp sfngfkdlqa
      421 lqqktgiida eftqtveqll lslsnqgtql nkgvhrftny prelldfyid qhniekarsw
      481 aakhkvkssq likladlima qhpqesidly hkslsdiiek tnndayreat nllikieksl
      541 kdksadctpl ynmiaalikd fkqkrnmmkl lreyfprlfl skk
//
LOCUS       WP_392345214             116 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein, partial [Parasynechococcus
            sp.].
ACCESSION   WP_392345214
VERSION     WP_392345214.1
KEYWORDS    RefSeq.
SOURCE      Parasynechococcus sp.
  ORGANISM  Parasynechococcus sp.
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Prochlorococcaceae; Parasynechococcus.
REFERENCE   1  (residues 1 to 116)
  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 11440233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Parasynechococcus sp."
                     /db_xref="taxon:3101203"
     Protein         1..>116
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
     Region          2..>115
                     /region_name="GCD1"
                     /note="NDP-sugar pyrophosphorylase, includes eIF-2Bgamma,
                     eIF-2Bepsilon, and LPS biosynthesis protein s
                     [Translation, ribosomal structure and biogenesis, Cell
                     wall/membrane/envelope biogenesis]; COG1208"
                     /db_xref="CDD:440821"
ORIGIN      
        1 mkamilaagk gtrvqpithv ipkpmipilq kpvmefllel lkehgftevm vnvshlaeei
       61 enyfrdgqrf gveiaysfeg riedgelign algsagglkk iqdfqnffdd tfvvlc
//
LOCUS       WP_392346462              31 aa            linear   ENV 20-JAN-2025
DEFINITION  pilin, partial [uncultured Polaribacter sp.].
ACCESSION   WP_392346462
VERSION     WP_392346462.1
KEYWORDS    ENV; RefSeq.
SOURCE      uncultured Polaribacter sp.
  ORGANISM  uncultured Polaribacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; environmental samples.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..31
                     /organism="uncultured Polaribacter sp."
                     /db_xref="taxon:174711"
                     /environmental_sample
     Protein         1..>31
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
     Region          1..>31
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkqtqkgftl ielmiviaii gilaavalpa y
//
LOCUS       WP_392346724             529 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Parasynechococcus sp.].
ACCESSION   WP_392346724
VERSION     WP_392346724.1
KEYWORDS    RefSeq.
SOURCE      Parasynechococcus sp.
  ORGANISM  Parasynechococcus sp.
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Prochlorococcaceae; Parasynechococcus.
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
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Linder,P., Lasko,P.F., Ashburner,M., Leroy,P., Nielsen,P.J.,
            Nishi,K., Schnier,J. and Slonimski,P.P.
  TITLE     Birth of the D-E-A-D box
  JOURNAL   Nature 337 (6203), 121-122 (1989)
   PUBMED   2563148
  REMARK    Erratum:[Nature 1989 Jul 20;340(6230):246]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423480
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Parasynechococcus sp."
                     /db_xref="taxon:3101203"
     Protein         1..529
                     /product="ATP-dependent DNA helicase"
                     /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_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0032508 - DNA duplex unwinding [Evidence
                     IEA]"
                     /calculated_mol_wt=57662
     Region          77..527
                     /region_name="RecD"
                     /note="ATPase/5#-3# helicase helicase subunit RecD of the
                     DNA repair enzyme RecBCD (exonuclease V) [Replication,
                     recombination and repair]; COG0507"
                     /db_xref="CDD:440273"
ORIGIN      
        1 mtellpqgts twpssftagl haalqrripp ladgpalkel srdlvlaleq geltvaltpe
       61 rlavaqasgw legdvspllv qgdrlgwrrw lqameqvvae lverahapvp npvkavdpel
      121 sdrlnaeqca avraldqasv vllsggpgtg ktstvveila raearhpdlr iglaaptgka
      181 arrlgeavla qrpplpcstl hrwleagsrg crgfgrhrqr pleldllvid emsmldlalt
      241 qallealpsa crllfvgdpa qlppvgsgav whrlqqpavr grfgagavhl ertyrnrgal
      301 aqvahqlrkg dlqafaadla alpeqanlqv hpsplrrfpd lvrqrwiqrl qqlqeltidl
      361 drctgqelma esrplfalle qdlllcprrr gpwslddvhr tllganaagk verwpiglpv
      421 icgsnqpelg langdlgvvi gvgserrllf qvvdpdgqlk vrrlhparlr rlepavalti
      481 hraqgseadr vivlwpdple agpaaehqrr llytaitrar asldlvtll
//
LOCUS       WP_392347119             401 aa            linear   ENV 20-JAN-2025
DEFINITION  THUMP domain-containing class I SAM-dependent RNA methyltransferase
            [uncultured Polaribacter sp.].
ACCESSION   WP_392347119
VERSION     WP_392347119.1
KEYWORDS    ENV; RefSeq.
SOURCE      uncultured Polaribacter sp.
  ORGANISM  uncultured Polaribacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; environmental samples.
REFERENCE   1  (residues 1 to 401)
  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 401)
  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 401)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     THUMP--a predicted RNA-binding domain shared by 4-thiouridine,
            pseudouridine synthases and RNA methylases
  JOURNAL   Trends Biochem Sci 26 (4), 215-217 (2001)
   PUBMED   11295541
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="uncultured Polaribacter sp."
                     /db_xref="taxon:174711"
                     /environmental_sample
     Protein         1..401
                     /product="THUMP domain-containing 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:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=45317
     Region          5..373
                     /region_name="RlmL"
                     /note="23S rRNA G2445 N2-methylase RlmL [Translation,
                     ribosomal structure and biogenesis]; COG0116"
                     /db_xref="CDD:439886"
ORIGIN      
        1 mekdfkmtat tlfglegvla eelknlgaqd vkeavrsvsf rgdkgfmyka nialrtavri
       61 lkpikickiy deedlydsiq kikwenyldv egtfaigavv nsknfttnsh yislkskdav
      121 adyfrhkysk rpnvdlkypd vkihihiqke wltvsidssg dslhkrgyrt atniapinev
      181 laagmvllsg ytgeenfidp mcgsgtilie aamiannipa ninrklfafe qwkdydedly
      241 ftiqesllkk irsshfkimg fdkapsavek aianvananl defigvhhvn ffnskkevfg
      301 nttilfnppy gerlnidtee fykkigdtlk nnypgstawl itsdtdalka vglrtsrria
      361 lknadldckf vkyelyegtr kfkepkldsd seiddegdiq e
//
LOCUS       WP_392349172             333 aa            linear   ENV 20-JAN-2025
DEFINITION  S66 peptidase family protein [uncultured Polaribacter sp.].
ACCESSION   WP_392349172
VERSION     WP_392349172.1
KEYWORDS    ENV; RefSeq.
SOURCE      uncultured Polaribacter sp.
  ORGANISM  uncultured Polaribacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; environmental samples.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="uncultured Polaribacter sp."
                     /db_xref="taxon:174711"
                     /environmental_sample
     Protein         1..333
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36664
     Region          27..328
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mkrlivftaf lltisasina qekihtlitp sylkkgdtia ivapagilkk rittvleakr
       61 laekwglhvv lgknifnqkn hfagtdaera adfqsaldnk nikaiwvarg gygsvrildl
      121 ldfstfiqfp kwiigysdvt afhghvhnfg vetihgmlat sleenpeeii qtiasfkkal
      181 fgaplyytip saidnripls eiitgqlvgg nlaivasmlg sesqlntdgk ilfieeigey
      241 kysidrmlqs lkragyftkv kavivgdiss ikqnstnwgs sveqlilevv pqdipvlfnf
      301 pagheadnra lifgrniklv adkenysvif snn
//
LOCUS       WP_392349859             452 aa            linear   BCT 20-JAN-2025
DEFINITION  gluconeogenesis factor YvcK family protein [Parasynechococcus sp.].
ACCESSION   WP_392349859
VERSION     WP_392349859.1
KEYWORDS    RefSeq.
SOURCE      Parasynechococcus sp.
  ORGANISM  Parasynechococcus sp.
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Prochlorococcaceae; Parasynechococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Parasynechococcus sp."
                     /db_xref="taxon:3101203"
     Protein         1..452
                     /product="gluconeogenesis factor YvcK family protein"
                     /GO_function="GO:0043743 - LPPG:FO 2-phospho-L-lactate
                     transferase activity [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=48686
     Region          119..439
                     /region_name="CofD"
                     /note="Archaeal 2-phospho-L-lactate transferase/Bacterial
                     gluconeogenesis factor, CofD/UPF0052 family [Carbohydrate
                     transport and metabolism, Coenzyme transport and
                     metabolism]; COG0391"
                     /db_xref="CDD:440160"
ORIGIN      
        1 mraqrrrdlm trstravrwl qpglvvkrwl ltsglglmma llggavwadl kpiywileal
       61 sgllgilttv mprevtgplv liigiglvlw gqsrsfgaiq qalvpdkdtv lidalqaksr
      121 lnrgpnivai gggtglstll sglkrysshi taivtvaddg gssgvlrrel gvlppgdirn
      181 claalsteep lltrlfqyrf sagngleghs fgnlflsalt aitgnletai tassrvlavq
      241 gqvvpatsad vrlwaeleng eriegesnig harspivrlg clperppalp raleaianad
      301 livlgpgsly tsllpnllvp elvaaiqrsr aprlyicnlm tqpgetdgld vrghiraiea
      361 qlaslgiqqr lfnavlaqnd ltpsplvehy rsrgaepvic daeglrrdgy disqaplqga
      421 rptatlrhds rslalavmrf yrshrrdqsh rs
//
LOCUS       WP_392350727             328 aa            linear   BCT 20-JAN-2025
DEFINITION  KpsF/GutQ family sugar-phosphate isomerase [Parasynechococcus sp.].
ACCESSION   WP_392350727
VERSION     WP_392350727.1
KEYWORDS    RefSeq.
SOURCE      Parasynechococcus sp.
  ORGANISM  Parasynechococcus sp.
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Prochlorococcaceae; Parasynechococcus.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Meredith,T.C. and Woodard,R.W.
  TITLE     Characterization of Escherichia coli D-arabinose 5-phosphate
            isomerase encoded by kpsF: implications for group 2 capsule
            biosynthesis
  JOURNAL   Biochem J 395 (2), 427-432 (2006)
   PUBMED   16390329
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Meredith,T.C. and Woodard,R.W.
  TITLE     Identification of GutQ from Escherichia coli as a D-arabinose
            5-phosphate isomerase
  JOURNAL   J Bacteriol 187 (20), 6936-6942 (2005)
   PUBMED   16199563
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002722
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Parasynechococcus sp."
                     /db_xref="taxon:3101203"
     Protein         1..328
                     /product="KpsF/GutQ family sugar-phosphate isomerase"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34233
     Region          6..310
                     /region_name="GutQ"
                     /note="D-arabinose 5-phosphate isomerase GutQ
                     [Carbohydrate transport and metabolism, Cell
                     wall/membrane/envelope biogenesis]; COG0794"
                     /db_xref="CDD:440557"
ORIGIN      
        1 msaltrclqe eanaiasaad rlssaqveaa lqllercadr kaklvitgvg ksgivarkia
       61 atfssiglma lflnptdalh gdlgvvaped vclllsnsge ttellevlph ltrrgtgria
      121 ivgrsdssla rgsdvvleag vdrevcplnl aptastavam aigdalaavw merrgispad
      181 falnhpagsl gkqltltaad lmipagklhp ldtttplpev iggltrdgig sgwvqqpdqp
      241 galaglitdg dlrralqlnr adhwisltaa dlmtadpitv qgdvlvvkal eqmehnrrkp
      301 isvlpvvdan kqllgllrlh dliqagla
//
LOCUS       WP_392352193              57 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Mesorhizobium
            atlanticum].
ACCESSION   WP_392352193
VERSION     WP_392352193.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium atlanticum
  ORGANISM  Mesorhizobium atlanticum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 57)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 57)
  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 57)
  AUTHORS   Tyrrell,R., Verschueren,K.H., Dodson,E.J., Murshudov,G.N., Addy,C.
            and Wilkinson,A.J.
  TITLE     The structure of the cofactor-binding fragment of the LysR family
            member, CysB: a familiar fold with a surprising subunit arrangement
  JOURNAL   Structure 5 (8), 1017-1032 (1997)
   PUBMED   9309218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444001
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..57
                     /organism="Mesorhizobium atlanticum"
                     /db_xref="taxon:2233532"
     Protein         1..57
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=5966
     Region          2..>28
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
ORIGIN      
        1 maehggsrra anvlnlsrst vsrriqllgf esrmsltaap avilsvlvmv afspgnr
//
LOCUS       WP_392354060              94 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Brevundimonas sp. LF-1].
ACCESSION   WP_392354060
VERSION     WP_392354060.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. LF-1
  ORGANISM  Brevundimonas sp. LF-1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 94)
  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 94)
  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   3  (residues 1 to 94)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11150091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Brevundimonas sp. LF-1"
                     /db_xref="taxon:3126100"
     Protein         1..94
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=10352
     Region          2..94
                     /region_name="DUF559"
                     /note="Protein of unknown function (DUF559); pfam04480"
                     /db_xref="CDD:398268"
     Site            order(3,32,49,56)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:411708"
ORIGIN      
        1 maeaalwkll rdrrlagvkf rrqapigryi adfccpalrr iieldggvhv lraesdaerd
       61 awltaqgftv lrfgneavls npsvvfdavr qava
//
LOCUS       WP_392354633             296 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Brevundimonas sp. LF-1].
ACCESSION   WP_392354633
VERSION     WP_392354633.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. LF-1
  ORGANISM  Brevundimonas sp. LF-1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415139
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Brevundimonas sp. LF-1"
                     /db_xref="taxon:3126100"
     Protein         1..296
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=31601
     Region          1..296
                     /region_name="LysX"
                     /note="Glutathione synthase, LysX or RimK-type ligase,
                     ATP-grasp superfamily [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism,
                     Translation, ribosomal structure and biogenesis, Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0189"
                     /db_xref="CDD:439959"
ORIGIN      
        1 mtdvavltpd padptystlw pgvldrlgea latagitarp tpwtdhvena ralmdfplvl
       61 pllvwgyhqg hdrwvqactt waeagaplan paatlrwnad krylallaek gvavpetifa
      121 dhvdaavlea afaatgaetl ivkptvsgga wrtlrvaagd lldaaladap vggtmiqpyl
      181 kaietegets llyfggelsh vvnkrpgaag efriqtqygg qyqalkaapq galdlaertl
      241 avidedllya ridmtkgddg dwvlmeaeli epdfylaaap eagarfgqav rarler
//
LOCUS       WP_392355574             341 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease, partial [Corynebacterium bovis].
ACCESSION   WP_392355574
VERSION     WP_392355574.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium bovis
  ORGANISM  Corynebacterium bovis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Corynebacterium bovis"
                     /db_xref="taxon:36808"
     Protein         1..>341
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
     Region          23..307
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 maqsgetete rtspaddrdg tapdrgtlll ldghslafra fyalpaanfs ttggqhtnav
       61 ygflgmflgl veqehpthva aafdmsgptf reerfpqyka qrpaappefa gqveliqqal
      121 ralgvtvlek esyeaddiia tlatrgaeag mrtlvctgdr dslqlvsddv tvlytlkgvs
      181 elhrftpeav eekygvtpaq ypdlaalrgd tsdnmpgvpg vgpktaqkwi ttygslagvi
      241 dhmddiggkv gqnlrdavgd valarditam vrdldlgcgl ddlrpgdvdp realevfeel
      301 qfganlrnrt frvlgvefdd aapvpvtvdd vddgrlgawl a
//
LOCUS       WP_392356519             302 aa            linear   BCT 20-JAN-2025
DEFINITION  aldo/keto reductase [Staphylococcus aureus].
ACCESSION   WP_392356519
VERSION     WP_392356519.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus aureus
  ORGANISM  Staphylococcus aureus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 302)
  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 302)
  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   3  (residues 1 to 302)
  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   4  (residues 1 to 302)
  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 10790928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     Protein         1..302
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /calculated_mol_wt=34607
     Region          1..302
                     /region_name="YdhF"
                     /note="Predicted oxidoreductase YdhF [General function
                     prediction only]; COG4989"
                     /db_xref="CDD:444013"
ORIGIN      
        1 meqiminhyv hfsrlvqgfw ranewkmtak elnyfinelv ergittmdht diygdyqces
       61 lfgnaldlsp elrnkiqivt kcgiilpskq fdftnghryd lsskhivksv eqslinlnvd
      121 yldsllihrp splmdpeqva daltklvkqg klksfgvsnf nhsqyqllnq yimkerlhis
      181 inqlelspyh vdslqdgtmd smyqnhvqim awspfaggki fdkedikaqr imkvvqsiad
      241 kygvsdtavm iawlvkiphs impilgtsql kridqaiegl qlnlddqswf diytaiigqd
      301 ip
//
LOCUS       WP_392357070             302 aa            linear   BCT 20-JAN-2025
DEFINITION  aldo/keto reductase [Staphylococcus aureus].
ACCESSION   WP_392357070
VERSION     WP_392357070.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus aureus
  ORGANISM  Staphylococcus aureus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 302)
  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 302)
  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   3  (residues 1 to 302)
  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   4  (residues 1 to 302)
  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 10790928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     Protein         1..302
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /calculated_mol_wt=34646
     Region          1..302
                     /region_name="YdhF"
                     /note="Predicted oxidoreductase YdhF [General function
                     prediction only]; COG4989"
                     /db_xref="CDD:444013"
ORIGIN      
        1 meqiminhyv hfsrlvqgfw ranewkmtak elnyfinelv ergittmdha diygdyqces
       61 lfgnaldlsp elrnkiqivt kcgiilpskq fdftnghryd lsskhivksv eqslinlnvd
      121 yldsllihrs splmdpeqva daltklvkqg klksfgvpnf nhsqyqllnq yimkerlhis
      181 inqlelspyh vdslqdgtmd smyqnhvqim awspfaggki fdkedikaqr imkvvqsiad
      241 kygvsdtavm iawlvkiphr impilgtsql kridqaiegl qlnlddqswf diytaiigqd
      301 ip
//
LOCUS       WP_392357319             367 aa            linear   BCT 20-JAN-2025
DEFINITION  PDDEXK nuclease domain-containing protein [Salmonella enterica].
ACCESSION   WP_392357319
VERSION     WP_392357319.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 367)
  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 10008845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..367
                     /product="PDDEXK nuclease domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42097
     Region          1..345
                     /region_name="YhcG"
                     /note="Predicted nuclease of restriction endonuclease-like
                     (RecB) superfamily, DUF1016 family [General function
                     prediction only]; COG4804"
                     /db_xref="CDD:443832"
ORIGIN      
        1 mtnptlvpqs deyqqihdgi irlvdtarte tvrsinaimt atyweigrri vefeqggear
       61 aaygtqlier lsvdlsqryk rgfstrnlwq irtfylcfqq ieipqtlsae ssnliplakt
      121 fplpwsayvr llsvknpdar tfyeketlrn gwsvrqldrq iatqfyertl lshdksamlq
      181 qpapaepnvl peqalrdpfi leflnlkdey sesdledall shlmdfmlel gddfafvgrq
      241 rrlriddswf rvdllffhrr lrclllvdlk vgkfgyadag qmnmylnyak ehwtmpgenp
      301 pvglvlcagk gageahyalt glpntimase ykvqlpdekl ltdelirsqt mletqltrgg
      361 slttekn
//
LOCUS       WP_392357549             226 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces sp. NPDC016172].
ACCESSION   WP_392357549
VERSION     WP_392357549.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016172
  ORGANISM  Streptomyces sp. NPDC016172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Streptomyces sp. NPDC016172"
                     /db_xref="taxon:3364964"
     Protein         1..226
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24217
     Region          2..224
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 mnsrerilgr vrraladvpr ddappvperp grdpqyerav srdyvrehge rrvpetvdll
       61 aenladyrai vhrtdtggla gliagllekr gaasvlvppg ldegwlaatg vprvadraes
      121 tpgeldlvds vvtacavaia etgtivldgs pdqgrrritl vpdhhicvvr vpdqvvssvp
      181 qglerldpar pltwisgpsa tsdieldrve gvhgprtlev ilvdgt
//
LOCUS       WP_392357846             812 aa            linear   BCT 20-JAN-2025
DEFINITION  GcvT family protein [Streptomyces sp. NPDC016172].
ACCESSION   WP_392357846
VERSION     WP_392357846.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016172
  ORGANISM  Streptomyces sp. NPDC016172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 812)
  AUTHORS   Stauffer,L.T., Ghrist,A. and Stauffer,G.V.
  TITLE     The Escherichia coli gcvT gene encoding the T-protein of the
            glycine cleavage enzyme system
  JOURNAL   DNA Seq 3 (6), 339-346 (1993)
   PUBMED   8219277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..812
                     /organism="Streptomyces sp. NPDC016172"
                     /db_xref="taxon:3364964"
     Protein         1..812
                     /product="GcvT family protein"
                     /calculated_mol_wt=88313
     Region          5..385
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
     Region          370..426
                     /region_name="FAO_M"
                     /note="FAD dependent oxidoreductase central domain;
                     pfam16350"
                     /db_xref="CDD:465100"
     Region          421..812
                     /region_name="GcvT"
                     /note="Glycine cleavage system protein T
                     (aminomethyltransferase) [Amino acid transport and
                     metabolism]; COG0404"
                     /db_xref="CDD:440173"
ORIGIN      
        1 magprvviig agvvgaalad eisargwtev tvvdqgplpa tggssshapg lvfqtnpskt
       61 mtemarytve kfcsldvdgq pcflqvggle vatspervte lqrrhgwlas wgiasrllst
      121 eecveqhplv npdkvlagll vptdglakav laveaqirra tergvrflar hevldvqrad
      181 gqvtgvltdq geipadivvc cagiwgpkia rmagmnlplt plahqlawtg pvpalagqtq
      241 eavrpilrhq dadlyyrdrf dglgigyygh rpmpisaddi lsvdeademp svlkfteedf
      301 eeawsetqsl lpatkdakve eginglfsft tdglpllges pdvkgfwvae avwvthsagv
      361 gramaewlvd gycssfdlhe cdvnrfephq lspeyvlard cqnfvevydi lhplqpsgdp
      421 rpirtspfht rqqelgaffl eangwerpqw yeanaglveg rsivtpndwa arywspivaa
      481 eaqttretva mydmtalkrl evsgrgagef lerlctgkva ksvgsvtytl lldhdggirs
      541 dvtvarlasd lfqvgangnl dldwftrhlp adgtvqvrdi tpgtcciglw gprardvlqp
      601 ltdadfsatg lkyfrakrah igsvpvtamr lsyvgelgwe lyttadlggk lwdtlwqaae
      661 plggiaagrg afnslrlekg yrsfgtdmty ehdpyeagvg favkldkddf igkaalerrk
      721 advrrkltcl tiddpkavvm gkepvydgdc avgyvtsaay gytigkgiay awlpvelaap
      781 gtvvhigyfd qsveavvaee plfdptmsrl rg
//
LOCUS       WP_392357999             462 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC016172].
ACCESSION   WP_392357999
VERSION     WP_392357999.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016172
  ORGANISM  Streptomyces sp. NPDC016172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Streptomyces sp. NPDC016172"
                     /db_xref="taxon:3364964"
     Protein         1..462
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=50199
     Region          89..350
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 menargvlll shvgfsfmed lasavttrgl kiyvlsslpe pqhqgsrpra ladladdvrv
       61 taehvltqrd vedyldqlea agmsalcclt vwegyrhlma lanarlgvpd ldekqilelr
      121 dklalrnrla daglsrgras altpetlaer qreggryfvk pvsgiasfgt fpltpdttwa
      181 dleriaaeah sntvyasaft tdptptdpad tdvsmahdlg lpveflvedy vpgrefsfev
      241 ivvddephvv avhekcevte aagtvlenac vspptslsqe eladgihwva svldilglgw
      301 gcfhvearya psgwdlievn prvggslisp svaaltggpg lvdlwmdsll tarqpaeflk
      361 alkdlsfatd gttqngnatf frvffadpgt irevgpnddl plqpvvshvl lkpgdvvess
      421 shevflgqvl wrmdraerde ilpellpase haieiqyete rg
//
LOCUS       WP_392359000             293 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC016172].
ACCESSION   WP_392359000
VERSION     WP_392359000.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016172
  ORGANISM  Streptomyces sp. NPDC016172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 293)
  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 293)
  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 293)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Streptomyces sp. NPDC016172"
                     /db_xref="taxon:3364964"
     Protein         1..293
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32687
     Region          34..87
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          110..288
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mgivegdvae gvearavpag ewerephpsd slrtfgavvq alrehaglsr aelatrvrys
       61 khtvesvelg rrmpdtpfvd raeealgntg alrkaarylt rgeaglaawf rrwarlerea
      121 vslctyecrl vpgllqseay aravfegtip lrtdgeleaq laarmerqam mrerptvpfs
      181 fiveehvfrr rfgdaeamre lfdhvlersa prnvtlqvvp legglhacld gpvriletpa
      241 gqrlgysegq engrlisdpk evsllcqryd tlrsqalspt esrallerlr gel
//
LOCUS       WP_392359393             267 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces sp.
            NPDC016172].
ACCESSION   WP_392359393
VERSION     WP_392359393.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016172
  ORGANISM  Streptomyces sp. NPDC016172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616714
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Streptomyces sp. NPDC016172"
                     /db_xref="taxon:3364964"
     Protein         1..267
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27360
     Region          17..241
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 mtadqqqtps gravtafagl hrageplllp nawdhasara lagqgfravg ttslgvaaaa
       61 glpdgaaatr eetlrlavtl gsgpflltvd aeggfsddpd evaefarely avgavginle
      121 dglgpaarha akiaavkraa pglfvnartd thwlgdgdgt larldayrqa gadgvfvpgl
      181 tdlrgietlv rhldvplnil yspggppvrh ladvgvrrvs lgsllyrral gaaleavadi
      241 ragrtpagat psydevagpa rridatr
//
LOCUS       WP_392361181             440 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC016172].
ACCESSION   WP_392361181
VERSION     WP_392361181.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016172
  ORGANISM  Streptomyces sp. NPDC016172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Streptomyces sp. NPDC016172"
                     /db_xref="taxon:3364964"
     Protein         1..440
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=49385
     Region          67..331
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 msdetvknvf vigldeanlp tlqqvpgadr lrfhqlltve elqhgevhlp tlfdkaqgvl
       61 dafdgsidai vgywdfpvst lvpmlseryg trstslesvv kcehkywsrl eqqkatdrhp
      121 rfdqvdlsad pprppekvtf pmwlkpalsy sselafgvgd eeefhkavae irdgisrigr
      181 pfehilerid lppemngvgg rvclaeeams gvqvavegyv hqgevtvygv ldsiqypdsp
      241 cflrhqypsm lpppviaqlh evservmrqi gmdsatfsie yfydprtqei nlleinprhs
      301 qshaelfqyv dgvpnhhcmv slalgedphm phregsyama akwyhrwftd gvvrrapspe
      361 eiarieretp gvrievipeq gdrlselpgq dsysyelahi ytggadeael rekfdhcvaa
      421 lglafedapa aeaeaeaare
//
LOCUS       WP_392362426             403 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC016172].
ACCESSION   WP_392362426
VERSION     WP_392362426.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016172
  ORGANISM  Streptomyces sp. NPDC016172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  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 403)
  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
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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   5  (residues 1 to 403)
  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   6  (residues 1 to 403)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 403)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces sp. NPDC016172"
                     /db_xref="taxon:3364964"
     Protein         1..403
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41849
     Region          1..>61
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          81..391
                     /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 magtagtpgt prvlramndr aaldlllehg qlsrtrigkl tglskptasq llarleaagl
       61 vlatgttegr pgpsaqlyev npaagyaagl dvtpqrilaa vaditgrtvg rhelptpgrr
      121 tgtpvvqqvt daldgavkaa glarddihrl vigtpgafdp ttgrlryash lpgwhsptll
      181 delaaalpmp feyendvnlv alaeqrlgaa rghadfvllw nqeglgaalv lggrlhrgwt
      241 ggagevgflp vpgtplvrqv tkansggyqe lagsqavprl ardlgiedvp pgpyaeaaae
      301 lvaraaqagd dahrqllqty atrlatglas lvsvldpelv vlsgasltsg geplralvqa
      361 eleelaasrp rlvvgdvreh pvlrgalesa lattrdevfd tsr
//
LOCUS       WP_392362990             232 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Streptomyces sp. NPDC016172].
ACCESSION   WP_392362990
VERSION     WP_392362990.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016172
  ORGANISM  Streptomyces sp. NPDC016172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 232)
  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 10007985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Streptomyces sp. NPDC016172"
                     /db_xref="taxon:3364964"
     Protein         1..232
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24672
     Region          32..222
                     /region_name="COG3786"
                     /note="L,D-peptidoglycan transpeptidase YkuD,
                     ErfK/YbiS/YcfS/YnhG family [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443000"
ORIGIN      
        1 mrpgavalav sslivlgagp papspplpar madtgggtql itavapkras ttgtvtwwdr
       61 adgrwvkrgs aparfgangl vegarrtqgt nttptglygl pyafgikaap rgtaytyrrv
      121 hqdswwcqds gsrsynrwse praadcraae sehlityraq yahalvigfn yerpvrgrga
      181 giflhvngrg atagcvsvse eamrrilvwa dtarrphiav gtqsgstavt rl
//
LOCUS       WP_392363033             363 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            sp. NPDC016172].
ACCESSION   WP_392363033
VERSION     WP_392363033.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016172
  ORGANISM  Streptomyces sp. NPDC016172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   3  (residues 1 to 363)
  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   4  (residues 1 to 363)
  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 363)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Streptomyces sp. NPDC016172"
                     /db_xref="taxon:3364964"
     Protein         1..363
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39771
     Region          5..338
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 msatleaesl ykvfgrrpdr averlrdgad reelraegtt aavidasftv epgqifvvmg
       61 lsgsgkstll rmlngllept aghvrfdgqd lttlggrelr evrskkismv fqhfalfphr
      121 svrenaaygl evqgvpraer arradealal cglagweksw pdelsggmqq rvglaralat
      181 dadlllmdes fsaldplirr dmqdqllelq qklkktivfi thdlneamrl gdriavmrdg
      241 rivqigtaqd illrpendyv asftqdvdrs rvltageimd dsvtgddpgc hcetattdtp
      301 ftelcaisar lshpvsvvdk dnkqvgvvpr qrlvgflgde qdatpqpcds prdkggekvt
      361 ara
//
LOCUS       WP_392363317             308 aa            linear   BCT 20-JAN-2025
DEFINITION  S1 family peptidase [Streptomyces sp. NPDC016172].
ACCESSION   WP_392363317
VERSION     WP_392363317.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016172
  ORGANISM  Streptomyces sp. NPDC016172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Querino Lima Afonso,M., da Fonseca,N.J. Jr., de Oliveira,L.C.,
            Lobo,F.P. and Bleicher,L.
  TITLE     Coevolved Positions Represent Key Functional Properties in the
            Trypsin-Like Serine Proteases Protein Family
  JOURNAL   J Chem Inf Model 60 (2), 1060-1068 (2020)
   PUBMED   31895561
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Waldner,B.J., Kraml,J., Kahler,U., Spinn,A., Schauperl,M.,
            Podewitz,M., Fuchs,J.E., Cruciani,G. and Liedl,K.R.
  TITLE     Electrostatic recognition in substrate binding to serine proteases
  JOURNAL   J Mol Recognit 31 (10), e2727 (2018)
   PUBMED   29785722
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Pelc,L.A., Chen,Z., Gohara,D.W., Vogt,A.D., Pozzi,N. and Di Cera,E.
  TITLE     Why Ser and not Thr brokers catalysis in the trypsin fold
  JOURNAL   Biochemistry 54 (7), 1457-1464 (2015)
   PUBMED   25664608
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Perona,J.J. and Craik,C.S.
  TITLE     Evolutionary divergence of substrate specificity within the
            chymotrypsin-like serine protease fold
  JOURNAL   J Biol Chem 272 (48), 29987-29990 (1997)
   PUBMED   9374470
REFERENCE   5  (residues 1 to 308)
  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 10595581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Streptomyces sp. NPDC016172"
                     /db_xref="taxon:3364964"
     Protein         1..308
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=31585
     Region          95..246
                     /region_name="Trypsin_2"
                     /note="Trypsin-like peptidase domain; pfam13365"
                     /db_xref="CDD:433149"
ORIGIN      
        1 mrkplaaafc alaiagagaa pataadaapt gvgkaadtge vtsavsgvat sveqtlsglr
       61 grqaksvnfa gtvalsncsg svvrmpdsea ddpalvmtng hclesgfpgp gevlvdkass
      121 rtftllnasg srvatlraak laygtmtdtd valyqlttty aqikssynin pltlndshpv
      181 agtaisipsg ywkriyscti dgfvptlkeg dwtwkdsvry tsacntiggt sgspvvdqat
      241 nkvvainntg nedgerctvn npcevdangn vtvrkginya qetygipacf gidnkldlsa
      301 sgctlpkp
//
LOCUS       WP_392364316             320 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC016172].
ACCESSION   WP_392364316
VERSION     WP_392364316.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC016172
  ORGANISM  Streptomyces sp. NPDC016172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 320)
  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 320)
  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 320)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces sp. NPDC016172"
                     /db_xref="taxon:3364964"
     Protein         1..320
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=36018
     Region          15..70
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          94..270
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 msrrnggaes gastaavfge vlrhfreaal ltqealarri pcdrshvarv eagtrvpqdt
       61 faktcdellg tggvllrlwg ridwypqveh pdwfgrrarm daeavavray qtqvipgllq
      121 tpgyatalfg rrltdsqdva ervrarlsrq qrflveggpf ylvvldescl rhmvggpevm
      181 rdqcehlldv grlpnirvqi apssrpeidr pdtslsliel pggerwvyse sldrghfsdd
      241 pavftqhmrs ydvlradals apqsaalisd vregyeahdq ppaargdldq eqpqrrqrrg
      301 lhrnsprfpr rrphprqqep
//
LOCUS       WP_392365680             269 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces sp.
            NPDC014846].
ACCESSION   WP_392365680
VERSION     WP_392365680.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014846
  ORGANISM  Streptomyces sp. NPDC014846
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616714
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Streptomyces sp. NPDC014846"
                     /db_xref="taxon:3364922"
     Protein         1..269
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27706
     Region          10..223
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 msaettmmsf aalhhrpgvp lllpnawdha saaalaargf paigttslav aaavglpdge
       61 aatrehtlrl amtlgsepyp isvdaengfs ddpdevaela relwaagvag inledglgps
      121 grhaakiaav kaavpelfvn artdthwsgd gdardtlrrl dayqeagadg vfvpgltdpr
      181 riasltrhle aplnvlyspt gptvpelarl gvrrvslgsl lyrralgaal daaadiaagr
      241 apagptpsya dvralernvs asrsanssg
//
LOCUS       WP_392366502             328 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC014846].
ACCESSION   WP_392366502
VERSION     WP_392366502.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014846
  ORGANISM  Streptomyces sp. NPDC014846
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 328)
  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 11599008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces sp. NPDC014846"
                     /db_xref="taxon:3364922"
     Protein         1..328
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=34183
     Region          63..160
                     /region_name="LDT_IgD_like_2"
                     /note="IgD-like repeat domain of mycobacterial
                     L,D-transpeptidases; cd13432"
                     /db_xref="CDD:240447"
     Region          165..290
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mgrrkggigi alvtaamlvg asacggggsd kaggddakap gkpgasasps pkkpkgppml
       61 letitpqsgt tvgvampisv vftnpvaaka ranvekhmkv stsqpvtgaw hwfgdkradw
      121 rpqtywpsgt rvkidadmtg vgngngrygv hgythtfkig ddvradvsvt ghtmkvtrnd
      181 ktvrtlsina gspqyptwng tmavidkqek vhmtscsvgi scdkgspnyy dltlpwdvhl
      241 tqsgtyvhys tgdpnpgsgs argshgcvhl smsdakwfyg qvkqgdpvti tgssrakapa
      301 dngyaafnls wdqwlagsas gkgttsal
//
LOCUS       WP_392366570             291 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC014846].
ACCESSION   WP_392366570
VERSION     WP_392366570.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014846
  ORGANISM  Streptomyces sp. NPDC014846
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 291)
  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 291)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Streptomyces sp. NPDC014846"
                     /db_xref="taxon:3364922"
     Protein         1..291
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32588
     Region          16..68
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          89..263
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mrsreldpsa spldyygyel rraresaglt laqlgavvfc tgsligqiet aarvpqrdfs
       61 erldaalgtg glfsrlvgmv lrsqlpswfq qyadmeakat yistyqcqlv ygllqtesya
      121 ravlgvdqsd rldamvaarl drqrllsqeq ppvlwvvlde avlyrevggr evmreqlahl
      181 aglygrpwme lqvlpfsvgq ntglmgsfnl lrfeghpdly ysenydsghm tanpqvirer
      241 slgyarlqae alspresaal igrvleeryg hepgldghdm akvvlqrqqr r
//
LOCUS       WP_392367245             537 aa            linear   BCT 20-JAN-2025
DEFINITION  caspase family protein [Streptomyces sp. NPDC014846].
ACCESSION   WP_392367245
VERSION     WP_392367245.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014846
  ORGANISM  Streptomyces sp. NPDC014846
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Van Opdenbosch,N. and Lamkanfi,M.
  TITLE     Caspases in Cell Death, Inflammation, and Disease
  JOURNAL   Immunity 50 (6), 1352-1364 (2019)
   PUBMED   31216460
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Tsiatsiani,L., Van Breusegem,F., Gallois,P., Zavialov,A., Lam,E.
            and Bozhkov,P.V.
  TITLE     Metacaspases
  JOURNAL   Cell Death Differ 18 (8), 1279-1288 (2011)
   PUBMED   21597462
REFERENCE   3  (residues 1 to 537)
  AUTHORS   Zhang,J.H., Zhang,Y. and Herman,B.
  TITLE     Caspases, apoptosis and aging
  JOURNAL   Ageing Res Rev 2 (4), 357-366 (2003)
   PUBMED   14522240
REFERENCE   4  (residues 1 to 537)
  AUTHORS   Salvesen,G.S.
  TITLE     Caspases and apoptosis
  JOURNAL   Essays Biochem 38, 9-19 (2002)
   PUBMED   12463158
REFERENCE   5  (residues 1 to 537)
  AUTHORS   Villa,P., Kaufmann,S.H. and Earnshaw,W.C.
  TITLE     Caspases and caspase inhibitors
  JOURNAL   Trends Biochem Sci 22 (10), 388-393 (1997)
   PUBMED   9357314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Streptomyces sp. NPDC014846"
                     /db_xref="taxon:3364922"
     Protein         1..537
                     /product="caspase family protein"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=56994
     Region          14..>190
                     /region_name="COG4249"
                     /note="Uncharacterized conserved protein, contains caspase
                     domain [General function prediction only]"
                     /db_xref="CDD:443391"
ORIGIN      
        1 masrwssssd rcvmarhral ligasdyemp gvarlpfvpg dlarlgsvle drgfdvlvva
       61 gredgkqvsr nfvdgqvigf lrragrddtl lillsghgvh argrdflvpe diqedthpfe
      121 sgcvaidwra hldetpagrv vflidacreg ieqesmgvat vrqwgrqkvs aalrrkvayv
      181 yacspgqfal fvrsrdktvd pvagvrpgds fsifsrsvsd vitahpgtva lglqefqrsv
      241 qdritelhrt yrkagqpqtl rivtdiptdd fsflppprtp ntrsgrspgp svvrpdadtt
      301 tykstamaal agtprsarra rsfgpaaral salvligslg vtvwvmvtkn gntddrgtas
      361 gkagsatsaa pgssspetsr tnskghdgvs gspkavasga astlpncsps avqlalrsvh
      421 nsysldqtpt feltaknssn vdckidlgpk navltvtpad tdstfwssad cprgagnlvf
      481 rasagesity tvkwdrrpsa phcatprags akagtyllea rapgfakpqa sfvlstd
//
LOCUS       WP_392368655             326 aa            linear   BCT 20-JAN-2025
DEFINITION  quinone oxidoreductase family protein [Streptomyces sp.
            NPDC014846].
ACCESSION   WP_392368655
VERSION     WP_392368655.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014846
  ORGANISM  Streptomyces sp. NPDC014846
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 326)
  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 326)
  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 326)
  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   4  (residues 1 to 326)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces sp. NPDC014846"
                     /db_xref="taxon:3364922"
     Protein         1..326
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=33303
     Region          1..326
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 mkavraskfg aprvltitdl pdptpgpgqi aidvthaavg lidvyirqgl fkdvpglpqp
       61 pyipglevag tvralgegvt gftvgekvva lssygtggya svyvsdqerv vstqdydidp
      121 alavavvpna imahialtra ismsagesvl vhgalgglaa afpgiarqlg asrvvgtvrs
      181 ertgaaaasr lpydsivdsa rlpdvlggek fdvivdpvgg lvrtqsldll apsgrlllvg
      241 nasgdwdhsi dgnrvwqgni tvagfnaggy lpahpeavqp aaeaalkava ggladieiev
      301 lpladaatah erlenhatdg rivltp
//
LOCUS       WP_392368908             416 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC014986].
ACCESSION   WP_392368908
VERSION     WP_392368908.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014986
  ORGANISM  Streptomyces sp. NPDC014986
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 416)
  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 416)
  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
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 416)
  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   5  (residues 1 to 416)
  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   6  (residues 1 to 416)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 416)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 416)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Streptomyces sp. NPDC014986"
                     /db_xref="taxon:3364934"
     Protein         1..416
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43273
     Region          1..>61
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          81..393
                     /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 mggtagapgt prvlramndr aaldlllehg plsrtrvgrl tglskptasq llarleaagl
       61 vlatgttegr pgpnaqlyev npgaahaagi dvtprriraa vaditgrtvg hhelpaparr
      121 sgtpvvqqvt daldgavkaa glsradvhrl vigtpgafdp ntgrlryash lpgwhsptll
      181 delaaalpmp feyendvnlv avaeqrlgaa rdhtdfvllw nqeglgaalv lggrlhrgwt
      241 ggagevgflp vpgtplvrqv tkansggyqe lagsqavprl arelgvedip qgpyaevaat
      301 lveraaaapd ddgphrrllg ayatrlatgl aslvsvldpe lvvlsgtglt sggevlralv
      361 qaeleelaaa rprlvvgdvr ehpvlrgale salattrdev fdtsrrpplp hrptap
//
LOCUS       WP_392369085             310 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Streptomyces sp. NPDC014986].
ACCESSION   WP_392369085
VERSION     WP_392369085.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014986
  ORGANISM  Streptomyces sp. NPDC014986
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Streptomyces sp. NPDC014986"
                     /db_xref="taxon:3364934"
     Protein         1..310
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32509
     Region          7..308
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 msgteplrrp arlapgarva vvapsgpvpe erlragldvl rgwdldpvva phvldrhdef
       61 gylagsdadr aadlqsawcd pdvdavlcar ggygaqrmvd lldwpamraa gpkvfvgfsd
      121 italheafav rlglvtlhgp maagvdfvks araqdhlrst lfapetvrtl hsdgtalvpg
      181 rargvtlggc lsllsaglgt sharpsargg llcledvgee tyrldrcltq llrtgwldgv
      241 rglllgswar cepyhgvram ladrlgglgv pvaeqfgfgh cgdaltvpfg vaaeldadag
      301 tltldepals
//
LOCUS       WP_392369448             540 aa            linear   BCT 20-JAN-2025
DEFINITION  peptide ABC transporter substrate-binding protein [Streptomyces sp.
            NPDC014986].
ACCESSION   WP_392369448
VERSION     WP_392369448.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014986
  ORGANISM  Streptomyces sp. NPDC014986
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 540)
  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 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   3  (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
REFERENCE   4  (residues 1 to 540)
  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 540)
  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 11467924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Streptomyces sp. NPDC014986"
                     /db_xref="taxon:3364934"
     Protein         1..540
                     /product="peptide 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=59353
     Region          35..532
                     /region_name="OppA"
                     /note="ABC-type oligopeptide transport system, periplasmic
                     component [Amino acid transport and metabolism]; COG4166"
                     /db_xref="CDD:443327"
ORIGIN      
        1 mrgvmharwa acavavalaa tacggggsgg dagavlsasw gdpqnplepa ntnevqggkv
       61 ldmifrglkr yhpetgeaed mlaerietpd srnftvtvkd gwtfsngekv tarsfvdawn
      121 ygaslrnnqr nsyffgyieg ydkahpeqge qsadtlsglk vvdertftvr ltqkfstfpd
      181 tlgynafapl praffddhda wvakpvgngp yrvdsytrgs qmslrtweey pgedkarngg
      241 vdlkvytdnn taytdlmagn ldladdvpaa qlrnvendlg drylntpagi iqtlafphyd
      301 rnwgragmek vrkglsmaid reqitdtifq gtrtpatdwt spvlgeaggf redlcgeaca
      361 yrpdearkli eeggglpggr vtitfnadtg shrewvnavc nsindaldde ractanpvgt
      421 fadfrnritd rkmggpfrag wqmdypliqn flqplyytna ssndgkwsne efdglvdran
      481 qetdtaaavd lfqqaeevvr ddmaaiplwy qsgsagwser lsdvklnpfs vpvyeqikvg
//
LOCUS       WP_392369812             288 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptomyces sp.
            NPDC014986].
ACCESSION   WP_392369812
VERSION     WP_392369812.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014986
  ORGANISM  Streptomyces sp. NPDC014986
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 288)
  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 288)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 288)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 288)
  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   5  (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   6  (residues 1 to 288)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces sp. NPDC014986"
                     /db_xref="taxon:3364934"
     Protein         1..288
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31681
     Region          22..102
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          126..284
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mlerlnqale yiecrldqdv eveelarvaa tseyhlrrmf salagmplse yvrrrrltla
       61 gaevlagrgt lleiavrygy ssgeafaraf ramhgvgpge arrtgaalss qsrmafrlti
      121 egsssmryrv vdkagftvvg lrarvplvha gpnraimdfv rgidlrtler leelsdqeph
      181 givavcddld psraegteld yhhgvitsaa apegmtalav pagtwavftt sgpapraiqe
      241 lwrdvftewf psnpyrtrtg peilrtrlsp dgteadaelw lpveperg
//
LOCUS       WP_392369854             274 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces sp.
            NPDC014986].
ACCESSION   WP_392369854
VERSION     WP_392369854.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014986
  ORGANISM  Streptomyces sp. NPDC014986
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Streptomyces sp. NPDC014986"
                     /db_xref="taxon:3364934"
     Protein         1..274
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=29620
     Region          1..>200
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mqfrvlgvpe vhddvadrwv pltspkqrql lgallarpgv pvstarliee lwsgrapgka
       61 vnalqahvsr lrqllieaep srantprlma rdtgyvlqar peeldsarfr lataravsll
      121 gsdpraarvl lkealelwrg pamagstggp lcagaaaele eerlsaleal ydvqlrlgph
      181 reavgelrrl taahpgrerf gggrpweaav areadlppvt aaaapgpgdg gellrlrarv
      241 delvdeqrll rsqverlsll ltrrgrapga lthr
//
LOCUS       WP_392370060             403 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            sp. NPDC014986].
ACCESSION   WP_392370060
VERSION     WP_392370060.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014986
  ORGANISM  Streptomyces sp. NPDC014986
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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   4  (residues 1 to 403)
  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 403)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces sp. NPDC014986"
                     /db_xref="taxon:3364934"
     Protein         1..403
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=42516
     Region          18..353
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 mttatpstgv adrapaapvf svrglwkvfg pkagripgdp elaaldpagl rsrtgctaav
       61 rdvsfdvrkg evfvvmglsg sgkstlvrcl trlveptagt iaidgedvra mdrarlralr
      121 rhraamvfqh fgllphrtvl dnvaygleiq gmgraerrer aaevvakvgl egmeqrrpaq
      181 lsggqrqrvg laralavdpe vllfdepfsa ldplirrdmq eevvrlhree grtmvfithd
      241 lqealklgdr ialmrdgrvv qlgtpedivg spaddyvraf vrdvpreqvl tvrtvmrpaa
      301 sadeagtgpa irpdatvsea ieavaragts arvldrgrcv gvvdsdvlld vvaggvaavp
      361 rlaaparaae ggvpagaepg agrapagrrg ptaptattge egv
//
LOCUS       WP_392370106             349 aa            linear   BCT 20-JAN-2025
DEFINITION  BMP family lipoprotein [Streptomyces sp. NPDC014986].
ACCESSION   WP_392370106
VERSION     WP_392370106.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014986
  ORGANISM  Streptomyces sp. NPDC014986
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Yousief,S.W., Bahey-El-Din,M. and Zaghloul,T.I.
  TITLE     Immunization with the basic membrane protein (BMP) family ABC
            transporter elicits protection against Enterococcus faecium in a
            murine infection model
  JOURNAL   Microbes Infect 22 (3), 127-136 (2020)
   PUBMED   31585177
REFERENCE   2  (residues 1 to 349)
  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   3  (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   4  (residues 1 to 349)
  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   5  (residues 1 to 349)
  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 11448319
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Streptomyces sp. NPDC014986"
                     /db_xref="taxon:3364934"
     Protein         1..349
                     /product="BMP family lipoprotein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /calculated_mol_wt=36178
     Region          43..347
                     /region_name="Med"
                     /note="Lipoprotein Med, regulator of KinD/Spo0A, PBP1-ABC
                     superfamily, includes NupN [Signal transduction
                     mechanisms]; COG1744"
                     /db_xref="CDD:441350"
ORIGIN      
        1 mrrisritva gaataslala ltacggtsts sssseskgdk glaiaydvgg kgdqsfndaa
       61 yaglerakke fgyetadvep tegetdadke qrlaslakqg ynpvigvgya yaaavkgaae
      121 kfpdttfgiv ddatieaenv adlvfseeqa sylagvaaak atrtgtvgfv ggvdiplihk
      181 fqagfeqgvk dtdpevrvip qyltqtaeeg gfsspdkgkt aaegqiekka dvvyaaagls
      241 gqgvieaaaa nevwaigvds dqyrqealar ykdsiltsam kdvakavhnl aksvedgkpe
      301 tgivrgdlkt gevslsnsnp kfaddaelqe aietakekii sgeikvkss
//
LOCUS       WP_392373458             288 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces sp.
            NPDC015125].
ACCESSION   WP_392373458
VERSION     WP_392373458.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015125
  ORGANISM  Streptomyces sp. NPDC015125
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789410
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces sp. NPDC015125"
                     /db_xref="taxon:3364938"
     Protein         1..288
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31030
     Region          4..247
                     /region_name="PrpB"
                     /note="2-Methylisocitrate lyase and related enzymes, PEP
                     mutase family [Carbohydrate transport and metabolism];
                     COG2513"
                     /db_xref="CDD:442003"
ORIGIN      
        1 mrygqalrde iaaegttpli gvhdmhsasi aaahyngffv sgfgfaasyy glpdigfiaw
       61 pdmvafverl rgafprhhll vdiddgyvdp evachvvqrl erigatgvil edqkrprrcg
      121 hadgklllpl eeyleklnlv lasrtdllvv artdatqede mlrraaalag tdadvvlvdg
      181 vrsvegirri ravlgtkpll fnqiaggksp rlslteltgl gvdvaiystp clfaahrame
      241 tamaelkyad grlpatggsg geigvkeate llarnisrhh pvretvpa
//
LOCUS       WP_392373851             250 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Streptomyces sp.
            NPDC015125].
ACCESSION   WP_392373851
VERSION     WP_392373851.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015125
  ORGANISM  Streptomyces sp. NPDC015125
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616714
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Streptomyces sp. NPDC015125"
                     /db_xref="taxon:3364938"
     Protein         1..250
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25740
     Region          13..243
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 mtttdrplaa talralhhgp elplvlpgpw daasarvfad agfpalatps agiaaslgye
       61 dgrtpademf aavarivrsv dipvsadvea gyglsaeelv grlmdagvvg cnledtdpat
      121 galrdpqeqa dwlarvraea gealvlnari dtylhgvqdt eeavrrgrly aaagadcvyp
      181 flapppelaa laagiglpvn avvtpdgptp relgalgaar itfgpglqcr tmaavagmae
      241 rlreelvaed
//
LOCUS       WP_392374125             256 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces sp.
            NPDC015125].
ACCESSION   WP_392374125
VERSION     WP_392374125.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015125
  ORGANISM  Streptomyces sp. NPDC015125
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces sp. NPDC015125"
                     /db_xref="taxon:3364938"
     Protein         1..256
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=27730
     Region          18..251
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mssddlifsw ppassrptvh iallggfdlv vndvpvtvpv gskrllafva lngraaaprs
       61 lvagslwpea ceqsayanlr salsrlrgig rkaldvcpte vrlarkvtvd lhharslaqr
      121 ildpgvpaed lninaatvdq ltddllpgwy dewalreaeq wqqlrlhale alagafidtk
      181 qfagavaaah aavqanplre ssqaslirah laegnpseal deferythrl rdelglrptp
      241 rlchlvdglq rpgsgw
//
LOCUS       WP_392375521            1296 aa            linear   BCT 20-JAN-2025
DEFINITION  Rne/Rng family ribonuclease [Streptomyces sp. NPDC015125].
ACCESSION   WP_392375521
VERSION     WP_392375521.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015125
  ORGANISM  Streptomyces sp. NPDC015125
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1296)
  AUTHORS   Kime,L., Jourdan,S.S. and McDowall,K.J.
  TITLE     Identifying and characterizing substrates of the RNase E/G family
            of enzymes
  JOURNAL   Methods Enzymol 447, 215-241 (2008)
   PUBMED   19161846
REFERENCE   2  (residues 1 to 1296)
  AUTHORS   Callaghan,A.J., Marcaida,M.J., Stead,J.A., McDowall,K.J.,
            Scott,W.G. and Luisi,B.F.
  TITLE     Structure of Escherichia coli RNase E catalytic domain and
            implications for RNA turnover
  JOURNAL   Nature 437 (7062), 1187-1191 (2005)
   PUBMED   16237448
REFERENCE   3  (residues 1 to 1296)
  AUTHORS   Li,Z., Pandit,S. and Deutscher,M.P.
  TITLE     RNase G (CafA protein) and RNase E are both required for the 5'
            maturation of 16S ribosomal RNA
  JOURNAL   EMBO J 18 (10), 2878-2885 (1999)
   PUBMED   10329633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1296
                     /organism="Streptomyces sp. NPDC015125"
                     /db_xref="taxon:3364938"
     Protein         1..1296
                     /product="Rne/Rng family ribonuclease"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=137056
     Region          627..1027
                     /region_name="CafA"
                     /note="Ribonuclease G or E [Translation, ribosomal
                     structure and biogenesis]; COG1530"
                     /db_xref="CDD:441139"
ORIGIN      
        1 mlepieptrs tqsqdrgadd nhspsdtlpp rrrrraasrp agppvadgaa eaevvsteat
       61 aapavdpald devaasavtt gdeakparsr rratrkatap agapqpagge paeapaepaa
      121 etpaaaagtp aeepaetpqp edaaprrgrr ratrkvtapa gspqheagqe pvaaeepapv
      181 apaaaeepap aaqpapaaae epedaaprrt rrratrkvta pagtpqasda deavaetaap
      241 aaraetaapa araesteeea paaaedakpa rsrrratrka tapagapqaa grtaeaeaeq
      301 apaaeaeaap aeaaqgetae aprrrarrrg eraaeqpaae apraeeepaq eapqrgrrra
      361 qrpptavfqa pvftepmfqt petaaaaaaa arqeeteaep vveeqpaaga rrrrrrgapa
      421 epepvsaapv eepaaeeaea aaepeteeae sghgedesdg rpsrrrrrgg rrrrrgesae
      481 ggeeqpaegr gaeeresdra epeeadeqpe aedeaeeqpg ggssssrrrr rrrrrtgdtg
      541 edgttgtddp ertvvkvrep rkkdestsad evqsikgstr leakkqrrre greqgrrrvp
      601 iiteaeflar reavervmvv rqsgertqig vlednvlveh fvnkeqatsy vgnvylgkvq
      661 nvlpsmeaaf vdigkgrnav lyagevnfea lgmsngprri etalksgqsv lvqvtkdpig
      721 hkgarltsqv slpgrylvyv pegsmtgisr klpdterarl kqilkkivpe dagvivrtaa
      781 egasedelar dvqrlqaqwe eiqkkakaas tsspsllyge pdmtvrvvrd ifnedfskvi
      841 vsgdeaweti hgyvahvapd ltdrlqkwts dvdvfatyri deqlmkaldr kvwlpsggsl
      901 vidkteamiv idvntgkftg qggnleetvt rnnleaaeei vrqlrlrdlg givvidfidm
      961 vlesnrdlvl rrmleclgrd rtkhqvaevt slglvqmtrk rvgqgllesf sescvhcngr
     1021 gvivhmdqpa vaggggkrkk kgkgaqpeph vheaeaaepa peggapelep aavteaelqp
     1081 avegadewfg spaeaeaaag rsrgrrrasr kasapagapk aaesaaaivv paeqapaaep
     1141 ekapepvaea paaepaparp rrratrkvta pagapkaaee aaaivvpaes apsaepvtep
     1201 epaeatepae gagveaepaa kktakktaak katakktaak kttakktaak ktttttttkk
     1261 atakktttkk attkkaaakk taaaeqpsea qaegva
//
LOCUS       WP_392375671             264 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces sp.
            NPDC015125].
ACCESSION   WP_392375671
VERSION     WP_392375671.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015125
  ORGANISM  Streptomyces sp. NPDC015125
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Streptomyces sp. NPDC015125"
                     /db_xref="taxon:3364938"
     Protein         1..264
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=29227
     Region          1..248
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mrfrilgple vatdhgegat pqalklrsll atlcvhadrv vptqrlinal wagapprtas
       61 talqvyiskl rrhfgnlgvg ssiittqspg yalrlkhhsl dlrqfdstvl qareavhagl
      121 preaaqllse avqlwngpal advratpaln gyarqleerr natyeqrlel elglgrhsel
      181 mgelyglvhd hpmwenlhay lmialyrsgr ireclkvysn irqalveeig vepcallrnl
      241 hhavlsresr lddpgrglli ssps
//
LOCUS       WP_392375718             293 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Streptomyces sp.
            NPDC015125].
ACCESSION   WP_392375718
VERSION     WP_392375718.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015125
  ORGANISM  Streptomyces sp. NPDC015125
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 293)
  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 293)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Streptomyces sp. NPDC015125"
                     /db_xref="taxon:3364938"
     Protein         1..293
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=30389
     Region          2..277
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mplvptssiv daarearvga aafnvihlet aealvtaaer teiplilqis enciryhgsl
       61 lpltratlal aegstapiav hldhitdael vhqgiaagvg svmvdasalp yeenvattae
      121 lttwchdrga yveaelgevg gkdgvhapgv rtdpgealsf vratgvdala vavgsshamh
      181 ertavldkal iealhttlpv plvlhgssgv pddelrraia agmtkinist hlvsvfthsi
      241 rhtlgadpsl vdsrkylkpa reavaeeaar llevlgtpaa vpdqcaaqap arg
//
LOCUS       WP_392376015             255 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Streptomyces sp. NPDC015125].
ACCESSION   WP_392376015
VERSION     WP_392376015.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015125
  ORGANISM  Streptomyces sp. NPDC015125
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 255)
  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 10007985
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Streptomyces sp. NPDC015125"
                     /db_xref="taxon:3364938"
     Protein         1..255
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=26265
     Region          51..245
                     /region_name="COG3786"
                     /note="L,D-peptidoglycan transpeptidase YkuD,
                     ErfK/YbiS/YcfS/YnhG family [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443000"
ORIGIN      
        1 mratvrsraa gplsavtlal lalaaptpaa sapapaasas gaapvqhipl pvlmadtggg
       61 dqlitarapt trattgtvrw wqrhngrwrq agwaparfga gglaegstrv qgtsttptgl
      121 ydlpfafgta ppppgtalpy rragadawwc edsasasynr wvaplppdca ageserlady
      181 ptqyaralvi gfnyhrpvhg rgagiflhvn gkgatagcvs vpagamaril swvrpsarph
      241 iavgtaygpt avtry
//
LOCUS       WP_392376407             347 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC015125].
ACCESSION   WP_392376407
VERSION     WP_392376407.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015125
  ORGANISM  Streptomyces sp. NPDC015125
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415139
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Streptomyces sp. NPDC015125"
                     /db_xref="taxon:3364938"
     Protein         1..347
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=35551
     Region          1..272
                     /region_name="LysX"
                     /note="Glutathione synthase, LysX or RimK-type ligase,
                     ATP-grasp superfamily [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism,
                     Translation, ribosomal structure and biogenesis, Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0189"
                     /db_xref="CDD:439959"
ORIGIN      
        1 mrlcflveeq yrhdgmpldv irqlgawghq vdvlwpgrsl ipiseaiqag shdawvlktv
       61 sggpgltlle aaasvglttv ndvrairgvr dkalaaviar rsglpvpvty aaarpeefae
      121 iaeaefplvv kpadgssgra vrlvatpdrl ldpvepagag dlgapgggll iaqpyvpnsg
      181 tdlkvysvag elyatercsp lhpahavrer qvpltpdiar laaevgtvfg ldlygvdill
      241 gpdgpvvvdi ndfpsfrqvp davarvsaai ldlarhgtag qgagpaaqrt seqpttgqpt
      301 tgqptaapat tgpaaaasat tppftaapva ppvprpsrpa asigggr
//
LOCUS       WP_392378853             345 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Streptomyces sp. NPDC015125].
ACCESSION   WP_392378853
VERSION     WP_392378853.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015125
  ORGANISM  Streptomyces sp. NPDC015125
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Streptomyces sp. NPDC015125"
                     /db_xref="taxon:3364938"
     Protein         1..345
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=34502
     Region          55..336
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mtpltarlpk salrllglls saaglvllal avpkaagtdw aavrthlghi sgpqvallca
       61 lagatlwsyt yvlgaalpgl tlrqallvhc tssavsnllp lgggagvavt yamtrrwghp
      121 pgavavcval tgvcnvaarl vlsavgalll agtpvpgigw aaaaggvala lpvalaagwp
      181 vlrrcrrapg ahrraaapdg alrhlarrar qlavrlrdds rdvvrrswar lvcgmtatla
      241 aqgalflacl qaagsrtgag ealavfaasr lltqiavtpg gigvtecaaa valvalggap
      301 aavasamllf atfthlleip lgaltgalwl lrggrrhpap apaap
//
LOCUS       WP_392379290             545 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces sp.
            NPDC015125].
ACCESSION   WP_392379290
VERSION     WP_392379290.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015125
  ORGANISM  Streptomyces sp. NPDC015125
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 545)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Streptomyces sp. NPDC015125"
                     /db_xref="taxon:3364938"
     Protein         1..545
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=57816
     Region          3..230
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          255..>423
                     /region_name="FxSxx_TPR"
                     /note="FxSxx-COOH system tetratricopeptide repeat protein;
                     NF040586"
                     /db_xref="CDD:468560"
ORIGIN      
        1 mvipsskptv llgalllhan etvsqeylrn alwgderpta agaaihttml rlrklldkya
       61 lggasagnie tvpggyrisa dagtldllaf rkavqragea asekdelgll rsalsnwqga
      121 pvanlvspal hdgvaaalae erinslarch eielalgnca aiiphlralt aeyrgneqlt
      181 aqlmealyra grqsealgay gsisrflret fgvdpgpalr qlhlailrge mlgaavppar
      241 qgtvvavarp padlkdfsgr hseladiqel lvhqstpaiv vvsglpgvgk talavrlarh
      301 lceglpdssg fpggwhflda rhkalpdrpa pqehalivld gvrssdealp aldwaeahtv
      361 vitsrhslad lvisrgatvf rlrswrraes lafltsvlgp rsteaepeaa delaalcgdh
      421 plalrilttr lllrpghdla savgtvrats pasltvggrq gasvgqrfdd ylgtlpppca
      481 ellrelaaap enrfklsega allgrsedel qsrldellea gaveyrpggl ygihtlmrsy
      541 lafgs
//
LOCUS       WP_392379558             424 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces sp. NPDC015125].
ACCESSION   WP_392379558
VERSION     WP_392379558.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015125
  ORGANISM  Streptomyces sp. NPDC015125
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 424)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Streptomyces sp. NPDC015125"
                     /db_xref="taxon:3364938"
     Protein         1..424
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=45088
     Region          54..239
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          247..366
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mshrprtrtv lscglllvpl avsatacggs dsetlsgtpy daagqitant pdgtkkadpd
       61 kplevsvkgd daritdvtat dttgrfvrge lsadgrhwrt taplaagsry tvrvsteeed
      121 gspgrktlvv ntrdadgqlt atfgpkegey gvgqpvtael sqpvkdqkar aivesalkvd
      181 smprvqgawh wvddkklhfr pkeywpahat isvhsnlagl kvakglyggp skpvklttgd
      241 rveaitdaat hqmtvlrnge sintipvttg kpgfstrngv kvvlgkesfv rmrsstvgia
      301 agsgdsydlp vhwatrvtws geyvhaapws vgsqgaanvs hgctgmstsn aqwffntvrv
      361 gdivkvvnsg gdtmtpfdng fgdwnmpwqe wregsalksk adtttgaagr vqnpaddarl
      421 rpkf
//
LOCUS       WP_392379597             845 aa            linear   BCT 20-JAN-2025
DEFINITION  GcvT family protein [Streptomyces sp. NPDC015125].
ACCESSION   WP_392379597
VERSION     WP_392379597.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015125
  ORGANISM  Streptomyces sp. NPDC015125
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 845)
  AUTHORS   Stauffer,L.T., Ghrist,A. and Stauffer,G.V.
  TITLE     The Escherichia coli gcvT gene encoding the T-protein of the
            glycine cleavage enzyme system
  JOURNAL   DNA Seq 3 (6), 339-346 (1993)
   PUBMED   8219277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..845
                     /organism="Streptomyces sp. NPDC015125"
                     /db_xref="taxon:3364938"
     Protein         1..845
                     /product="GcvT family protein"
                     /calculated_mol_wt=91673
     Region          8..418
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
     Region          404..459
                     /region_name="FAO_M"
                     /note="FAD dependent oxidoreductase central domain;
                     pfam16350"
                     /db_xref="CDD:465100"
     Region          454..844
                     /region_name="GcvT"
                     /note="Glycine cleavage system protein T
                     (aminomethyltransferase) [Amino acid transport and
                     metabolism]; COG0404"
                     /db_xref="CDD:440173"
ORIGIN      
        1 msrtpanrsr vvvigagivg csladeltar gwtevtvleq gplpapggst shapglvfrt
       61 gpsktmtefa aytvekfgal evdglpcfhp vggleiatte arwadlhrka glaaswgvrg
      121 allspqqckq lwplldetkl yggfhtpddg laravlacra qtaraesrga rflerhtvtg
      181 ieredgrvtg vvtdrgtfpa dhvvsaagfw gpvigamagv dvpllplahq yatteplpel
      241 dgvndphggt pcsseaeslg eeaskpilrf qdrdlyfreh hdrlgigsya hrpmpvdpft
      301 vpafddaaps pqlgssrghp pvmpsslpft eddfapswqd svgllpalga srvaegfngv
      361 fsftpdgmpv lgesrelrgf wlaeavwvth sagvakavae wmtdgrpgid ihecdlyrfe
      421 daqrspayva drgaqsfiev ydvihplqpm eqprplrtsp fyprqqelga yfleaggwer
      481 phwyeanapl teglalperd awsarywspi aaaearatre kvalydmtpl rrlevtgpga
      541 laflqhmttn nlakkpgavt ytllldetgg irsdltvarl apdrfqvgan sasdldwllr
      601 hapeegvqvr ditsgtccig vwgplardlv qpltrddfsh qafgyfkakq thlghvpvta
      661 mrlsyvgelg welyttadlg lrlwdtlwea grehgviaag rsafnslrle kgyrswghdm
      721 ttehdpyeag vgfavrpakg dflgrdaleg rseetaarkl scltlddpga vvlgkepvhv
      781 dgvpvgyvts aaygytlgrg iayawlpaaa tapgtavhie yfgekipatv aqeplfdpqm
      841 erirr
//
LOCUS       WP_392379606             212 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces sp. NPDC015125].
ACCESSION   WP_392379606
VERSION     WP_392379606.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015125
  ORGANISM  Streptomyces sp. NPDC015125
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Streptomyces sp. NPDC015125"
                     /db_xref="taxon:3364938"
     Protein         1..212
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22409
     Region          4..208
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 msataretvl rrvqdalars drpevtvpra yrtgrvlpdg erlalftdrl vdykaqvrtc
       61 tagttatvia ealrahgarr igvppgldpa wlagwdgeir tdspdvpapr ldaldgvvta
      121 savscaetgt ifldgaaadq grraltlvpd lhvcvvdlss vrtgvpeava rllpehpttl
      181 isgpsatsdi elervegvhg prtlevvirt dv
//
LOCUS       WP_392379775             547 aa            linear   BCT 20-JAN-2025
DEFINITION  complex I subunit 4 family protein [Streptomyces sp. NPDC015125].
ACCESSION   WP_392379775
VERSION     WP_392379775.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015125
  ORGANISM  Streptomyces sp. NPDC015125
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 547)
  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 547)
  AUTHORS   Galemou Yoga,E., Angerer,H., Parey,K. and Zickermann,V.
  TITLE     Respiratory complex I - Mechanistic insights and advances in
            structure determination
  JOURNAL   Biochim Biophys Acta Bioenerg 1861 (3), 148153 (2020)
   PUBMED   31935361
REFERENCE   3  (residues 1 to 547)
  AUTHORS   Friedrich,T. and Scheide,D.
  TITLE     The respiratory complex I of bacteria, archaea and eukarya and its
            module common with membrane-bound multisubunit hydrogenases
  JOURNAL   FEBS Lett 479 (1-2), 1-5 (2000)
   PUBMED   10940377
REFERENCE   4  (residues 1 to 547)
  AUTHORS   Walker,J.E.
  TITLE     The NADH:ubiquinone oxidoreductase (complex I) of respiratory
            chains
  JOURNAL   Q Rev Biophys 25 (3), 253-324 (1992)
   PUBMED   1470679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Streptomyces sp. NPDC015125"
                     /db_xref="taxon:3364938"
     Protein         1..547
                     /product="complex I subunit 4 family protein"
                     /GO_component="GO:0045271 - respiratory chain complex I
                     [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048039 - ubiquinone binding [Evidence
                     IEA]"
                     /GO_process="GO:0015990 - electron transport coupled
                     proton transport [Evidence IEA]"
                     /GO_process="GO:0042773 - ATP synthesis coupled electron
                     transport [Evidence IEA]"
                     /calculated_mol_wt=56128
     Region          9..545
                     /region_name="NuoM"
                     /note="NADH:ubiquinone oxidoreductase subunit 4 (chain M)
                     [Energy production and conversion]; COG1008"
                     /db_xref="CDD:440632"
ORIGIN      
        1 mnptalqyll aavvvlpllg avgallpapp glkgrnpdqa vlrhgvtatg vvlaaalala
       61 agfdhdhpar mqattdiswi paldirihlg idgislplvv ltalltflca lysyfhmptg
      121 pspkafvall ltleagtlas favldlmlff lafemvlipm yfliarwgga ekqaaawkfi
      181 lytllgsvvm llgllligvk sgtfdmvala tdngpkaqls htvqllavla igiglavksp
      241 lwplhswlpd ahtaaptvgs vllagvllkm gtygfvrial pitpegmhtv apylgalaai
      301 giiygslacl alvrkgaggd lkrliayssv ghmgfvllgi asmtptgvng alfaniahgl
      361 itgllfflvg alkdrygstd ldtlsgstga alygkaprfg gllafgavas lgipglagfw
      421 gemlamfgaf rpaaglsrpa fltfmalagl gtlltaayll lvvrrvcmgg tpaaveavpa
      481 veegtataae aatvapaapa pvipdlarye yaawtplavl tvlaglwpaa llgltdpavq
      541 qllgggk
//
LOCUS       WP_392379844             285 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015125].
ACCESSION   WP_392379844
VERSION     WP_392379844.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015125
  ORGANISM  Streptomyces sp. NPDC015125
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 285)
  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 285)
  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 16111081
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptomyces sp. NPDC015125"
                     /db_xref="taxon:3364938"
     Protein         1..285
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32261
     Region          20..71
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(22,26,51)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(25,50)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(32..33,44,47,51..52)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          93..273
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mparkdvdgs asvpafygae lrwkreaagr tlqetahgsf fgpsylseie ratrrmplel
       61 arhvdrvlgt dgfferrced vrkarrgaha eyfapiaeae trarvierws nalipgllqt
      121 gayaravihs thpldlpeev evkvrarlqr aklfdapkkl eywvilhesl vrgadpllap
      181 semaeqldqi aglvrrrrvf pqilpcnapt rpfmelslmf mefddepplm ytegpyhgqt
      241 fddpalvhqy rkaydrlraa alppeaslai ieeaaedyrn gqqnp
//
LOCUS       WP_392379961             882 aa            linear   BCT 20-JAN-2025
DEFINITION  S1 family peptidase [Streptomyces sp. NPDC015125].
ACCESSION   WP_392379961
VERSION     WP_392379961.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015125
  ORGANISM  Streptomyces sp. NPDC015125
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 882)
  AUTHORS   Querino Lima Afonso,M., da Fonseca,N.J. Jr., de Oliveira,L.C.,
            Lobo,F.P. and Bleicher,L.
  TITLE     Coevolved Positions Represent Key Functional Properties in the
            Trypsin-Like Serine Proteases Protein Family
  JOURNAL   J Chem Inf Model 60 (2), 1060-1068 (2020)
   PUBMED   31895561
REFERENCE   2  (residues 1 to 882)
  AUTHORS   Waldner,B.J., Kraml,J., Kahler,U., Spinn,A., Schauperl,M.,
            Podewitz,M., Fuchs,J.E., Cruciani,G. and Liedl,K.R.
  TITLE     Electrostatic recognition in substrate binding to serine proteases
  JOURNAL   J Mol Recognit 31 (10), e2727 (2018)
   PUBMED   29785722
REFERENCE   3  (residues 1 to 882)
  AUTHORS   Pelc,L.A., Chen,Z., Gohara,D.W., Vogt,A.D., Pozzi,N. and Di Cera,E.
  TITLE     Why Ser and not Thr brokers catalysis in the trypsin fold
  JOURNAL   Biochemistry 54 (7), 1457-1464 (2015)
   PUBMED   25664608
REFERENCE   4  (residues 1 to 882)
  AUTHORS   Perona,J.J. and Craik,C.S.
  TITLE     Evolutionary divergence of substrate specificity within the
            chymotrypsin-like serine protease fold
  JOURNAL   J Biol Chem 272 (48), 29987-29990 (1997)
   PUBMED   9374470
REFERENCE   5  (residues 1 to 882)
  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 10595581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..882
                     /organism="Streptomyces sp. NPDC015125"
                     /db_xref="taxon:3364938"
     Protein         1..882
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=94017
     Region          21..180
                     /region_name="Trypsin_2"
                     /note="Trypsin-like peptidase domain; pfam13365"
                     /db_xref="CDD:433149"
ORIGIN      
        1 msahlrqrav evsnprdetf gsgtiiapgl vltaahvacr qgpdgqpvlv raldggpavn
       61 aqvtwhdqgl dsailqtdrq qlgvdvpivr wgeltcehpa erpvctaigf pramrrrflr
      121 rsrevmvsdp kvvhgyiypt taarsqryal evsdarpser tlwqgmsgag ifcegllvgl
      181 atqapenwda slllatpisw llaaegfaks vsaatglpaq lqpadlqall ddapnprlsa
      241 syllsaqaqi vpmsgleeqs erlaqwchsg rridvaavtg tggvgktrla sellrqlgep
      301 qtgidsprpw aggflsetpl rtaqyealtt anrplllivd yaetrldqvd ellnivsgsg
      361 gtaqpirlll lardqgswwq pfrrsrqgsa amgaglgvev ndcidstapq safeaakhaf
      421 aerirtlkaa gveddwgsaa itpatptrig pierhstvlt lhmaalaevl teinpafaey
      481 ghpvdvllah eerywkriar argldgvfdr qpgllqtmva tqslagaddr anaraaivag
      541 lgahhhglpa gagpdahlvd aveemltvly psgsgarwgs igpdllagev ireaeeasdh
      601 qfiacllqhp slaqeqrqqg ltvisraada qpelavsaak avaeapdvll slathevadq
      661 lgkssalqwi tevktavedr aqqaatdpdl skwaismtqh alnrlrtrsa aaaepvppag
      721 ppdwadvhae aqqvlsllqd arsraiqhgl asrddssgss eyiadmiaql swingarvda
      781 tvvedtfggk vecladkpvv igianachsi agvpfddght ralseavdrv vtltrrvqas
      841 qsrpspsppa grvgnggsym slddflrlqg dryrsgpenp de
//
LOCUS       WP_392380595             275 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC015125].
ACCESSION   WP_392380595
VERSION     WP_392380595.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015125
  ORGANISM  Streptomyces sp. NPDC015125
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (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
REFERENCE   4  (residues 1 to 275)
  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 10611723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Streptomyces sp. NPDC015125"
                     /db_xref="taxon:3364938"
     Protein         1..275
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29295
     Region          1..59
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(6,10,35)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(9,34)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(16..17,28,31,35..36)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          148..231
                     /region_name="DUF2690"
                     /note="Protein of unknown function (DUF2690); pfam10901"
                     /db_xref="CDD:402475"
ORIGIN      
        1 makelralke rtglsldgla rktpysksaw hrylngeklp prsavealgq vagadqerll
       61 avhdaayrar tapvatppva ptaplppert gwarkilrsa gvlrttgalv altalvatmg
      121 aaasiveipa raartdggas hachghrcqg rypwrpgcnr darvestivd ttytvrlrfs
      181 pscgtvwsev qprsggaqkv siwvgrdarl tshthgregl avspmlatsd lrqavacakv
      241 tdrvactgai eltspalrhd gddfpgptfl drvmr
//
LOCUS       WP_392380321             320 aa            linear   BCT 20-JAN-2025
DEFINITION  quinone oxidoreductase family protein [Streptomyces sp.
            NPDC015125].
ACCESSION   WP_392380321
VERSION     WP_392380321.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC015125
  ORGANISM  Streptomyces sp. NPDC015125
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 320)
  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   4  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces sp. NPDC015125"
                     /db_xref="taxon:3364938"
     Protein         1..320
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=33115
     Region          1..320
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 mramqferfg gpevlteaev pdpvagpggt lveveasgvn fgdikhiage htdgpnapkg
       61 plpripgmev vgrtadgrrv lgyvpqggya aktvvpdrdl valpegvsag ealalllqgl
      121 tawhvlrsva rvrpgesvvv haaaggtgsl avqlarefga grviatasse ekrafalelg
      181 adaaidgdae gykervldan qgrpvdiild aiggpvldsa ldalgylgrl vtygassrqa
      241 aaalapsrla venigvagfw lipllarngp ggpaleelld ltargrlrpl vgaeydlara
      301 rdahrdllgr rtrgklvlrp
//
LOCUS       WP_392381777             213 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces sp. NPDC014805].
ACCESSION   WP_392381777
VERSION     WP_392381777.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014805
  ORGANISM  Streptomyces sp. NPDC014805
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Streptomyces sp. NPDC014805"
                     /db_xref="taxon:3364919"
     Protein         1..213
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22888
     Region          2..213
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 mssrerilgr vrraladvtp derpyeeala rdylrehger tveqtvella enladyravv
       61 hrtsaadlas tvagilaahg srtvlvpqgl ppewlsaaea tpvgdraest pheldqvdsv
      121 vtgcavaiae tgtlvldgsp dqgrrritli pdhhicvvrv peqvvssvpq alerldpsrp
      181 ltwisgpsat sdieldrveg vhgprtlevv lvg
//
LOCUS       WP_392382800             373 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Streptomyces
            sp. NPDC014805].
ACCESSION   WP_392382800
VERSION     WP_392382800.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014805
  ORGANISM  Streptomyces sp. NPDC014805
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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   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   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Streptomyces sp. NPDC014805"
                     /db_xref="taxon:3364919"
     Protein         1..373
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40108
     Region          18..352
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 mtmtvptrkp pttasdapvf svdglwkvfg pkadripgdp eltaldaael rrrtgctaav
       61 rdvsfdvrkg evfvvmglsg sgkstlvrcl trlieptagt iaidgedvra mdrsrlralr
      121 rhraamvfqh fgllphrtvl dnvaygleiq glgrserrer aaevvakvgl egmehrrpgq
      181 lsggqrqrvg laralavdpe vllfdepfsa ldplirrdmq eevvrlhree grtmvfithd
      241 lsealklgdr ialmrdgrvv qlgtpeeiva spaddyvref vrdvpreqvv tvrkamrpas
      301 adeagsgpav rpdatvseai eavaragepa rvvdqgrclg vvdadtllgv vagtaetppd
      361 aaagpavtea ega
//
LOCUS       WP_392383116             812 aa            linear   BCT 20-JAN-2025
DEFINITION  GcvT family protein [Streptomyces sp. NPDC014805].
ACCESSION   WP_392383116
VERSION     WP_392383116.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014805
  ORGANISM  Streptomyces sp. NPDC014805
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 812)
  AUTHORS   Stauffer,L.T., Ghrist,A. and Stauffer,G.V.
  TITLE     The Escherichia coli gcvT gene encoding the T-protein of the
            glycine cleavage enzyme system
  JOURNAL   DNA Seq 3 (6), 339-346 (1993)
   PUBMED   8219277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..812
                     /organism="Streptomyces sp. NPDC014805"
                     /db_xref="taxon:3364919"
     Protein         1..812
                     /product="GcvT family protein"
                     /calculated_mol_wt=88923
     Region          5..385
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
     Region          370..426
                     /region_name="FAO_M"
                     /note="FAD dependent oxidoreductase central domain;
                     pfam16350"
                     /db_xref="CDD:465100"
     Region          421..812
                     /region_name="GcvT"
                     /note="Glycine cleavage system protein T
                     (aminomethyltransferase) [Amino acid transport and
                     metabolism]; COG0404"
                     /db_xref="CDD:440173"
ORIGIN      
        1 magprvviig agvvgaalad eisargwtev tvvdqgplpa tggssshapg lvfqtnaskt
       61 mtelarytve kfsslevdgk pcflqvggle vatsperlae iqrrhgwlas wgidsrllna
      121 decverhplv drdkilgglf vptdglakav laveaqirra tergvrflar hevldvrqse
      181 grvtgvvtdh geidadivvc cagiwgpkia rmvgmnlplt plahqlawtg pvpalagqte
      241 eavrpilrhq dadlyyrdry dgigigyygh rpmpvsaddi lsvdeaeemp svlkfteedf
      301 epawtetrsl lpatqeakve eginglfsft tdgypllges pqvkgfwvae avwvthsagv
      361 gravaewlvd gycssfdlhe cdvnrfephq lspeyvlard cqnfvevydi lhplqpsgdp
      421 rpirtspfya rqqahgaffl eangwerpqw yeanaplveg rniptpndwa arywspivga
      481 eaqatretva lydmtalkrl evtgpgaaaf lerlctgkid ksvgsvtytl lldhdggirs
      541 dvtvarlard rfqvgangnl dldwfsrhlp adgtvqvrdi tagtcciglw gplarevlqp
      601 lteedfsneg lkyfrakhay igsvpvtamr lsyvgelgwe lyttadqglk lwdtlwaaaq
      661 plggviagrg afnslrlekg yrsfgtdmty ehdpyeagvg favkldkddf igkaalqrrk
      721 advrrrltcl tiddpravvl gkepvydgeh avgyvtsaay gytvgkgiay awlpaglaep
      781 gtrlhigyfd qrieavvaee plfdptmsrl rg
//
LOCUS       WP_392383312             282 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC014805].
ACCESSION   WP_392383312
VERSION     WP_392383312.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014805
  ORGANISM  Streptomyces sp. NPDC014805
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 282)
  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 282)
  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 18098837
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces sp. NPDC014805"
                     /db_xref="taxon:3364919"
     Protein         1..282
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31470
     Region          16..70
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          95..268
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mttgardlep arsarelygt elrrqrqlag lsldrlsdiv nyskthlhgv etaerlplpp
       61 lsekldvafg tgelfqglwg vikrehtprr fdhcleleak aariqafgas iipgllqtea
      121 ymralftege pglcpkeidr lvaarlgrqe ilrrdcppdl wwilgeatlr qivggpavmr
      181 eqlaallplv htrhttiqva pfesdvcalm ngtlilltlp dnsttvyheg sgygeifddq
      241 qtvmrrvrey drkkacalsp qesagliksm mekyepcepp qt
//
LOCUS       WP_392383619             264 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptomyces sp. NPDC014805].
ACCESSION   WP_392383619
VERSION     WP_392383619.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014805
  ORGANISM  Streptomyces sp. NPDC014805
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415139
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Streptomyces sp. NPDC014805"
                     /db_xref="taxon:3364919"
     Protein         1..264
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=27514
     Region          1..247
                     /region_name="LysX"
                     /note="Glutathione synthase, LysX or RimK-type ligase,
                     ATP-grasp superfamily [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism,
                     Translation, ribosomal structure and biogenesis, Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0189"
                     /db_xref="CDD:439959"
ORIGIN      
        1 mriglitsdp ghpllaaata lladghtvrv ldpetagmpg rsgpladvyl lkartprais
       61 laralerrga rvlnsaaata lcqdrvamae harraglpfa ptrfhatlar ladgpglrgp
      121 lvvksrhsrk hdlvarvdse grlaelaaah preavvvqdf vpnngwdhkl waigdrvfaa
      181 lrrselspeg rgptvplglg slppgwaalv hrvgevfgld vygvdvldtg ggvplivdin
      241 afpgvrdqpg apqalaalal taga
//
LOCUS       WP_392383802             556 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Marinomonas primoryensis].
ACCESSION   WP_392383802
VERSION     WP_392383802.1
KEYWORDS    RefSeq.
SOURCE      Marinomonas primoryensis
  ORGANISM  Marinomonas primoryensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinomonas.
REFERENCE   1  (residues 1 to 556)
  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 11459492
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Marinomonas primoryensis"
                     /db_xref="taxon:178399"
     Protein         1..556
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=63621
     Region          29..549
                     /region_name="YcbB"
                     /note="Murein L,D-transpeptidase YcbB/YkuD [Cell
                     wall/membrane/envelope biogenesis]; COG2989"
                     /db_xref="CDD:442228"
ORIGIN      
        1 mtpakkllpl lcvslllsac stsnsnkqfi vippsesqie ssvkdqvslt lnaftpvagq
       61 alpnhsvlev ykargydpiw iqdkkinmsi yklvdileqs ythglnpihy htaiikeyle
      121 lkqptpqqla emdvittial asyahdlsng ryepqlidpn wqldapnnnw kdllyfdsat
      181 dmvnslplla prspqyqvlq kwlvyyqdla akekdifvna gvplspgdeg prvaqlrarl
      241 vqlgdirfst rkvneeqfdl rlkealirfq rrhhimadga agsktiemln tplkvrakqi
      301 aynlerwrwl pseleanriw vdltnytvdm hlngeltsmk avigkpdrkt pvfkglmtym
      361 vtnptwrvph riarenllpk lqadpnylvk hgykvyssws igakeldstk inwqdiseek
      421 lafrfeqepd egnalgqykf mfpnkneiyl hdtpskhlfr eedrafssgc vrlenpaefa
      481 reitkgskqf nemtkalkne sntvislpty ipvylvyftv vpnangmlef rndiyerdal
      541 meeamgyaaf rardsi
//
LOCUS       WP_392384108             141 aa            linear   BCT 20-JAN-2025
DEFINITION  bactofilin family protein [Marinomonas primoryensis].
ACCESSION   WP_392384108
VERSION     WP_392384108.1
KEYWORDS    RefSeq.
SOURCE      Marinomonas primoryensis
  ORGANISM  Marinomonas primoryensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinomonas.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Deng,X., Gonzalez Llamazares,A., Wagstaff,J.M., Hale,V.L.,
            Cannone,G., McLaughlin,S.H., Kureisaite-Ciziene,D. and Lowe,J.
  TITLE     The structure of bactofilin filaments reveals their mode of
            membrane binding and lack of polarity
  JOURNAL   Nat Microbiol 4 (12), 2357-2368 (2019)
   PUBMED   31501539
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Ingerson-Mahar,M. and Gitai,Z.
  TITLE     A growing family: the expanding universe of the bacterial
            cytoskeleton
  JOURNAL   FEMS Microbiol Rev 36 (1), 256-266 (2012)
   PUBMED   22092065
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Kuhn,J., Briegel,A., Morschel,E., Kahnt,J., Leser,K., Wick,S.,
            Jensen,G.J. and Thanbichler,M.
  TITLE     Bactofilins, a ubiquitous class of cytoskeletal proteins mediating
            polar localization of a cell wall synthase in Caulobacter
            crescentus
  JOURNAL   EMBO J 29 (2), 327-339 (2010)
   PUBMED   19959992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Marinomonas primoryensis"
                     /db_xref="taxon:178399"
     Protein         1..141
                     /product="bactofilin family protein"
                     /calculated_mol_wt=14830
     Region          7..124
                     /region_name="CcmA"
                     /note="Cytoskeletal protein CcmA, bactofilin family
                     [Cytoskeleton]; COG1664"
                     /db_xref="CDD:441270"
ORIGIN      
        1 mgifggqnrv ksqsstttli aegctvnghl kvadqlqidg hvegqieaan qlkisqsgnv
       61 lgeittehli inghfegich atrieilscg rvsgtvysdn lsiepggkfm gvtnpsekta
      121 stqeipdltd nltlisndpd l
//
LOCUS       WP_392385157             293 aa            linear   BCT 20-JAN-2025
DEFINITION  transglutaminase family protein [Marinomonas primoryensis].
ACCESSION   WP_392385157
VERSION     WP_392385157.1
KEYWORDS    RefSeq.
SOURCE      Marinomonas primoryensis
  ORGANISM  Marinomonas primoryensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12090973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Marinomonas primoryensis"
                     /db_xref="taxon:178399"
     Protein         1..293
                     /product="transglutaminase family protein"
                     /calculated_mol_wt=32822
     Region          3..78
                     /region_name="Bact_transglu_N"
                     /note="Bacterial transglutaminase-like N-terminal region;
                     pfam08379"
                     /db_xref="CDD:462455"
     Region          101..247
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mryrvrhite ytygapvslc ynmahllprd trnqlcihqk iqinpppvyq negedyfgnq
       61 tfyfsiqeah kklvidvstd feispinvle wqaqntitcg elrsllsapn tpelrmakey
      121 lldspqirrs adlgayaqst faddkpilqa tlafthkift efkfdpsttt vatpleqvlk
      181 qrsgvcqdfa hlaigclrsv giparyisgy letlpppgqe klvgadasha wfaifiptlg
      241 wvefdptndl mpneqhlvta wgrdysdvtp lqgvifeggg sqqlavsvdv rrv
//
LOCUS       WP_392385251             160 aa            linear   BCT 20-JAN-2025
DEFINITION  FKBP-type peptidyl-prolyl cis-trans isomerase [Marinomonas
            primoryensis].
ACCESSION   WP_392385251
VERSION     WP_392385251.1
KEYWORDS    RefSeq.
SOURCE      Marinomonas primoryensis
  ORGANISM  Marinomonas primoryensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinomonas.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Quistgaard,E.M., Weininger,U., Ural-Blimke,Y., Modig,K.,
            Nordlund,P., Akke,M. and Low,C.
  TITLE     Molecular insights into substrate recognition and catalytic
            mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD
  JOURNAL   BMC Biol 14 (1), 82 (2016)
   PUBMED   27664121
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Gothel,S.F. and Marahiel,M.A.
  TITLE     Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous
            folding catalysts
  JOURNAL   Cell Mol Life Sci 55 (3), 423-436 (1999)
   PUBMED   10228556
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Trandinh,C.C., Pao,G.M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships among the immunophilins:
            two ubiquitous families of peptidyl-prolyl cis-trans isomerases
  JOURNAL   FASEB J 6 (15), 3410-3420 (1992)
   PUBMED   1464374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Marinomonas primoryensis"
                     /db_xref="taxon:178399"
     Protein         1..160
                     /product="FKBP-type peptidyl-prolyl cis-trans isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=17435
     Region          3..137
                     /region_name="SlpA"
                     /note="Peptidyl-prolyl cis-trans isomerase, FKBP type
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1047"
                     /db_xref="CDD:440668"
ORIGIN      
        1 msiadnqvvq fhytlrhgee lietsagkdp atylhghgnv ipglekameg kavgdefevt
       61 vacadayger hedrtqqmpi khlqgakrwk tgmvamvktd qgmrqvtiik aglkhatvdl
      121 nhplsgkdlt fniqivdare gtndeiahgh shgvgghhhh
//
LOCUS       WP_392385670             276 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Marinomonas primoryensis].
ACCESSION   WP_392385670
VERSION     WP_392385670.1
KEYWORDS    RefSeq.
SOURCE      Marinomonas primoryensis
  ORGANISM  Marinomonas primoryensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinomonas.
REFERENCE   1  (residues 1 to 276)
  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 276)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 276)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 276)
  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   5  (residues 1 to 276)
  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   6  (residues 1 to 276)
  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 10007405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Marinomonas primoryensis"
                     /db_xref="taxon:178399"
     Protein         1..276
                     /product="AraC 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:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32191
     Region          1..276
                     /region_name="SbmC"
                     /note="DNA gyrase inhibitor GyrI/SbmC [Replication,
                     recombination and repair]; COG3449"
                     /db_xref="CDD:442672"
ORIGIN      
        1 mhivcdyiyk hlneeltvda lcnvagfsky hfhrqfsnym gmgvfkfvqq lrlkrasyel
       61 vfytdkriid iamdaqfdhp esfsrafkkv flqspmafrr qpdwlqwhre yrvvenrmal
      121 dldvklvnfv gtqvaafehr gpvermless atfrgwrqrt gissirtsrt fgiiydnpec
      181 vpaedfrfdi agevhqaigd nqegivnkfl aggrcavvrh ygthenmgdv vcalydvwlp
      241 naneelrdap cffhwhnffp hvaehelitd iylplk
//
LOCUS       WP_392385688             536 aa            linear   BCT 20-JAN-2025
DEFINITION  peptide ABC transporter substrate-binding protein [Marinomonas
            primoryensis].
ACCESSION   WP_392385688
VERSION     WP_392385688.1
KEYWORDS    RefSeq.
SOURCE      Marinomonas primoryensis
  ORGANISM  Marinomonas primoryensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinomonas.
REFERENCE   1  (residues 1 to 536)
  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 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   3  (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   4  (residues 1 to 536)
  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 536)
  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 11467924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Marinomonas primoryensis"
                     /db_xref="taxon:178399"
     Protein         1..536
                     /product="peptide 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=60500
     Region          1..535
                     /region_name="OppA"
                     /note="ABC-type oligopeptide transport system, periplasmic
                     component [Amino acid transport and metabolism]; COG4166"
                     /db_xref="CDD:443327"
ORIGIN      
        1 mkktllasai iatsfitlqa qaadvpasve laekqelvrg ggaepatldp qkmegtpgsi
       61 rskdlfegly nqdgngnqvp gvatsydvna dntqytfhlr kdakwsngdp vtaedfvyaf
      121 travdpalas pyawfmeips ivnatkiiag eakpstlgvk aldaytfqvt lerpvpyfvk
      181 mtshqtmfpv pkkvvekwgn dwtkpehmvs ngaykmdewi vnekmvftrn anywndakti
      241 inkvtylpie spnaelkrfq agqmdlsyei pndhfkqlmr dipdevvvtp klgtyyyqyn
      301 itkapyndvr vrkalsyaid rdvitkfvtg tgelpaysft pevvndfspa tpeyatwtqk
      361 ernekakell keagftssnp lsfsllyntn enhkkiaiai asmwkktlgv svtlenqewk
      421 tyletkkhqq fdiaragwig dyneastmld llttthgnnd gkysntkydk llhdartmqh
      481 paanynkaee iaieqdmava piyqytekrl vksylggymp npednvyvrd myiikh
//
LOCUS       WP_392385902             453 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter large permease [Marinomonas primoryensis].
ACCESSION   WP_392385902
VERSION     WP_392385902.1
KEYWORDS    RefSeq.
SOURCE      Marinomonas primoryensis
  ORGANISM  Marinomonas primoryensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinomonas.
REFERENCE   1  (residues 1 to 453)
  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 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   3  (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
REFERENCE   4  (residues 1 to 453)
  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 10008688
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Marinomonas primoryensis"
                     /db_xref="taxon:178399"
     Protein         1..453
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma 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=48685
     Region          5..453
                     /region_name="FcbT3"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, large permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4664"
                     /db_xref="CDD:443701"
ORIGIN      
        1 mfeayellvi amlgcfilli fsgfpvawil aglaivfsvv gvltsqyldw dtyymndwri
       61 ygtivqriya qmsnwvlval pmfifmglml ersgvaerlm vnfvnlfgrf rgglgvavil
      121 igilfaastg ivgasvvlla mlsmpvmleq kyspsfasgi vassgtlgil ippsimliim
      181 adqlslsvgn lfmgalipgl llgvlyiayv iisaifnptv cqppqnlppv tmgliwsalk
      241 avfpplalil svlgsifmgi vspteaagvg algatllail nkrfnmkmla evcrkttitt
      301 sfvfgiflga tafavvlrtl ggdefisdll qgiplspagi ivvilliafv agffldwlei
      361 slillplvgp vvvaldfnlv wfvvlfalal qtsfltppvg fslfylkgva ppgvttlhiy
      421 kgvipfvllq llavllvflf pdlvlwlpev iyg
//
LOCUS       WP_392386062             304 aa            linear   BCT 20-JAN-2025
DEFINITION  heme/hemin ABC transporter substrate-binding protein [Marinomonas
            primoryensis].
ACCESSION   WP_392386062
VERSION     WP_392386062.1
KEYWORDS    RefSeq.
SOURCE      Marinomonas primoryensis
  ORGANISM  Marinomonas primoryensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinomonas.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Naoe,Y., Nakamura,N., Rahman,M.M., Tosha,T., Nagatoishi,S.,
            Tsumoto,K., Shiro,Y. and Sugimoto,H.
  TITLE     Structural basis for binding and transfer of heme in bacterial
            heme-acquisition systems
  JOURNAL   Proteins 85 (12), 2217-2230 (2017)
   PUBMED   28913898
REFERENCE   2  (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   3  (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   4  (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   5  (residues 1 to 304)
  AUTHORS   Ho,W.W., Li,H., Eakanunkul,S., Tong,Y., Wilks,A., Guo,M. and
            Poulos,T.L.
  TITLE     Holo- and apo-bound structures of bacterial periplasmic
            heme-binding proteins
  JOURNAL   J Biol Chem 282 (49), 35796-35802 (2007)
   PUBMED   17925389
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Marinomonas primoryensis"
                     /db_xref="taxon:178399"
     Protein         1..304
                     /product="heme/hemin 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=32922
     Region          5..283
                     /region_name="ChuT"
                     /note="ABC-type hemin transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG4558"
                     /db_xref="CDD:443619"
ORIGIN      
        1 mimyrlfflt civflansvt yaapseriav aggsiteiiy rlgeqhrivg vdstsqfped
       61 akkfpllgyv rnvsvegvls lnpdlllged dtgptkalkq iaavgvktvi ikkdnsipal
      121 qekiaqiagl lgvedkgksl ldemqidida lsyakqhlsa sakktppkvl flltlkngap
      181 iaagnttsah tvieeagain vlaqykgwek lspesalkld pdviivmnrg qdifeqvgal
      241 phfkyttavk nkavytidgs yllgfgprtp qaivelgtmi hkdfplpagy kfryqhdvts
      301 maeh
//
LOCUS       WP_392390060             179 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Acinetobacter courvalinii].
ACCESSION   WP_392390060
VERSION     WP_392390060.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter courvalinii
  ORGANISM  Acinetobacter courvalinii
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Acinetobacter courvalinii"
                     /db_xref="taxon:280147"
     Protein         1..179
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=18060
     Region          1..122
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mqkgftliel mivvaiigil aaiaipayqd ynirarvteg lgiansakla istdgaaaqa
       61 dlnrvvttwn aqangtgans kyvdsvlmta ntglitvtyn pttvglasse nlitltpwvr
      121 dgdagegqsl qaaqtagstg tvdwgcaset aataaargit aaalgatgvr akyapaecr
//
LOCUS       WP_392390306             516 aa            linear   BCT 20-JAN-2025
DEFINITION  HAL/PAL/TAL family ammonia-lyase [Aeromonas sobria].
ACCESSION   WP_392390306
VERSION     WP_392390306.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas sobria
  ORGANISM  Aeromonas sobria
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Turner,N.J.
  TITLE     Ammonia lyases and aminomutases as biocatalysts for the synthesis
            of alpha-amino and beta-amino acids
  JOURNAL   Curr Opin Chem Biol 15 (2), 234-240 (2011)
   PUBMED   21131229
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Louie,G.V., Bowman,M.E., Moffitt,M.C., Baiga,T.J., Moore,B.S. and
            Noel,J.P.
  TITLE     Structural determinants and modulation of substrate specificity in
            phenylalanine-tyrosine ammonia-lyases
  JOURNAL   Chem Biol 13 (12), 1327-1338 (2006)
   PUBMED   17185228
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Baedeker,M. and Schulz,G.E.
  TITLE     Autocatalytic peptide cyclization during chain folding of histidine
            ammonia-lyase
  JOURNAL   Structure 10 (1), 61-67 (2002)
   PUBMED   11796111
REFERENCE   4  (residues 1 to 516)
  AUTHORS   Schwede,T.F., Retey,J. and Schulz,G.E.
  TITLE     Crystal structure of histidine ammonia-lyase revealing a novel
            polypeptide modification as the catalytic electrophile
  JOURNAL   Biochemistry 38 (17), 5355-5361 (1999)
   PUBMED   10220322
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Aeromonas sobria"
                     /db_xref="taxon:646"
     Protein         1..516
                     /product="HAL/PAL/TAL family ammonia-lyase"
                     /EC_number="4.3.1.-"
                     /GO_function="GO:0016841 - ammonia-lyase activity
                     [Evidence IEA]"
                     /GO_process="GO:0170035 - L-amino acid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56331
     Region          1..506
                     /region_name="HutH"
                     /note="Histidine ammonia-lyase [Amino acid transport and
                     metabolism]; COG2986"
                     /db_xref="CDD:442225"
ORIGIN      
        1 mheihfgarp ltieevvala erratprlnp apefrariqr gadyldrlla eegviygvtt
       61 gygdsvtrav pldlvdtlpl hltrfhgcgm genlslaatr avlatrlnsl aqgvsgvslp
      121 llerltwlle qdllpripee gsvgasgdlt plsyvaaali gereiyrnge lasaaelyre
      181 lgitplklrp keglalmngt svmtalacla yarcdylmrl ctritalvsv amegnafhfd
      241 erlfaakphp gqqqiaawlr adlqsgelph hsnrlqdrys lrcaphvigv vadslpwwrt
      301 lienelnsan dnplidgdge hvmhgghfyg ghiamamdsm kvavanladl ldrqlaqlvd
      361 skfnqrlpsn lsgasaerrf inhgfkavqi gasawtaeal khtmpasvfs rstechnqdk
      421 vsmgtiaard alrvltlteq vasasllaav qgvelrlalq ghdlttlspa laatveavrr
      481 dhpflcedrp leaelramma rlqarhypiy devshv
//
LOCUS       WP_392390804             414 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Micromonospora aurantiaca (nom. illeg.)].
ACCESSION   WP_392390804
VERSION     WP_392390804.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora aurantiaca (nom. illeg.)
  ORGANISM  Micromonospora aurantiaca (nom. illeg.)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 414)
  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 15739075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Micromonospora aurantiaca (nom. illeg.)"
                     /db_xref="taxon:47850"
     Protein         1..414
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43252
     Region          64..250
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          256..374
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mgalvltasl altgcgggde gkkpefvpgq qqvggvsssa pdpsvapsds aaappltvsp
       61 adgasgrpvs teisaripgg gtvskvalat adgasvagrm rrdgsswvps aalkygtkyt
      121 atvtgagkdg qtyqgtstft tmakpksmig sglymfsgkt ygvampvvae fspgipkkdr
      181 aavqkrmfvq tdppqpgawh wvdngtqayy rapeywktgt titvrlalag iplsngrygn
      241 idrsataeig rafemtvdna tkqmtvseng tvirtlpvsl gkkstpsssg tmvvmekkes
      301 tvfdtrsepd panryvteid faqritwgge yihaapwseg vqgrrnvshg cvnvsmangr
      361 wlfgktmvgd pitvkgterr lapgngwtaw smswsqfvag salpvpqggq papf
//
LOCUS       WP_392391520             241 aa            linear   BCT 20-JAN-2025
DEFINITION  IspD/TarI family cytidylyltransferase [Murimonas intestini].
ACCESSION   WP_392391520
VERSION     WP_392391520.1
KEYWORDS    RefSeq.
SOURCE      Murimonas intestini
  ORGANISM  Murimonas intestini
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Murimonas.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Bjorkelid,C., Bergfors,T., Henriksson,L.M., Stern,A.L., Unge,T.,
            Mowbray,S.L. and Jones,T.A.
  TITLE     Structural and functional studies of mycobacterial IspD enzymes
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 5), 403-414 (2011)
   PUBMED   21543842
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Illarionova,V., Kaiser,J., Ostrozhenkova,E., Bacher,A., Fischer,M.,
            Eisenreich,W. and Rohdich,F.
  TITLE     Nonmevalonate terpene biosynthesis enzymes as antiinfective drug
            targets: substrate synthesis and high-throughput screening methods
  JOURNAL   J Org Chem 71 (23), 8824-8834 (2006)
   PUBMED   17081012
REFERENCE   3  (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   4  (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   5  (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 10003116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Murimonas intestini"
                     /db_xref="taxon:1337051"
     Protein         1..241
                     /product="IspD/TarI family cytidylyltransferase"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0070567 - cytidylyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26630
     Region          10..237
                     /region_name="IspD"
                     /note="2-C-methyl-D-erythritol 4-phosphate
                     cytidylyltransferase [Lipid transport and metabolism];
                     COG1211"
                     /db_xref="CDD:440824"
ORIGIN      
        1 medtdmntal iiaggsgarm hqdipkqflt vnekpvivyt leafqkapei dviavvcisg
       61 weqvlwayan qfnitklkhv vpggengqas irngvfelek nyskddvvli hdairpmvse
      121 eiisdcivkt kqfgcaiasv pcaeamlete dgiladksyp renlkrtqtp qgfhigdice
      181 lhrnalekgi tnsvasctlm iemgqrvyfs agsekniklt tvedidifka lllakrsewl
      241 k
//
LOCUS       WP_392391981             399 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase family protein [Parabacteroides
            goldsteinii].
ACCESSION   WP_392391981
VERSION     WP_392391981.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides goldsteinii
  ORGANISM  Parabacteroides goldsteinii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Vollmer,W., Joris,B., Charlier,P. and Foster,S.
  TITLE     Bacterial peptidoglycan (murein) hydrolases
  JOURNAL   FEMS Microbiol Rev 32 (2), 259-286 (2008)
   PUBMED   18266855
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436722
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Parabacteroides goldsteinii"
                     /db_xref="taxon:328812"
     Protein         1..399
                     /product="N-acetylmuramoyl-L-alanine amidase family
                     protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44560
     Region          7..254
                     /region_name="AmiC"
                     /note="N-acetylmuramoyl-L-alanine amidase [Cell
                     wall/membrane/envelope biogenesis]; COG0860"
                     /db_xref="CDD:440621"
ORIGIN      
        1 marisflyin llmalfltlp vlqarektft vvidaghggk dpgargtvin ekainlsval
       61 klgdkiaagh ddvkviytrk tdrfielder anianrnkad lfisihtnsv kkgstargte
      121 tytlglartd enlavamren sailleddyq qkyegfdpns sesyiifefm qnkhmeqsvs
      181 faseiqkcfv sakradrgvr qagflvlrkt smpsvlvelg yisnrdeerf mkssdgqnrl
      241 asalydafsr ykkeydrkqg glsgsvqgit ssevsyveye ateeavpags eedilnkkkn
      301 asvssqkkqt taatrtksna tgkfvykvqi ltsdkklspg akvfkgyknv dffvekgiyk
      361 ytygettdfd sirklrrqaa kdfkdafiva fkdgkkvky
//
LOCUS       WP_392391635              75 aa            linear   BCT 20-JAN-2025
DEFINITION  FeoA family protein [Zongyangia hominis].
ACCESSION   WP_392391635
VERSION     WP_392391635.1
KEYWORDS    RefSeq.
SOURCE      Zongyangia hominis
  ORGANISM  Zongyangia hominis
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Zongyangia.
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   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 10004922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Zongyangia hominis"
                     /db_xref="taxon:2763677"
     Protein         1..75
                     /product="FeoA family protein"
                     /GO_function="GO:0046914 - transition metal ion binding
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=8258
     Region          3..74
                     /region_name="FeoA"
                     /note="Fe2+ transport protein FeoA [Inorganic ion
                     transport and metabolism]; COG1918"
                     /db_xref="CDD:441522"
ORIGIN      
        1 mktlnqmrig kkarivavgg egalrdrlld mgltphtqvm irkvapmgdp ielmlrgyel
       61 tlrvddakni vveed
//
LOCUS       WP_392391598             222 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Paenibacillus ihumii].
ACCESSION   WP_392391598
VERSION     WP_392391598.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus ihumii
  ORGANISM  Paenibacillus ihumii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Paenibacillus ihumii"
                     /db_xref="taxon:687436"
     Protein         1..222
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24518
     Region          15..222
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 mdkhekperl ewsgkavkpe qplrgapefw rtfhwdkqer ierftqnfrs vgghverlas
       61 peeasefiad karelrakyi vrqqepdleq lhleaklpea evavwnsdgs gtdywkaraa
      121 eadigvvmad havaytgsva vmsspekgrs vsllptvlmi lipadciktr lgevlkefde
      181 lgpgrlpagi hfisgpsrss diendltigv hgpgivyali vg
//
LOCUS       WP_392393752             344 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Paraburkholderia caledonica].
ACCESSION   WP_392393752
VERSION     WP_392393752.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caledonica
  ORGANISM  Paraburkholderia caledonica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415139
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Paraburkholderia caledonica"
                     /db_xref="taxon:134536"
     Protein         1..344
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=36461
     Region          25..322
                     /region_name="LysX"
                     /note="Glutathione synthase, LysX or RimK-type ligase,
                     ATP-grasp superfamily [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism,
                     Translation, ribosomal structure and biogenesis, Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0189"
                     /db_xref="CDD:439959"
ORIGIN      
        1 mslplpsdst amdagtdtpg aqaplriaim tdetgwhtgr lkkafrarga earcidladc
       61 ridttwephg lvlpgfghgl pdavfvrgia ggtfeqvtlr lgilhalres gvpvyndara
      121 iersvdksmt sfllhrhgvp tpatwagesa afaqrvlmre aaagrqvvlk plfgsqghgl
      181 krlglrstpp ralaplpslk pysqvaylqr fidggrpgfd wrvlviggra vaamrriggk
      241 gwihnfaqga tceaaeldaa laqtavrate algldyagvd lildphdaar plvlevngva
      301 awrglqsvts idiaaaladd llfrklpaqr geaaavvalh grhg
//
LOCUS       WP_392393195             429 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein
            [Paraburkholderia caledonica].
ACCESSION   WP_392393195
VERSION     WP_392393195.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caledonica
  ORGANISM  Paraburkholderia caledonica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
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   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   4  (residues 1 to 429)
  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 429)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Paraburkholderia caledonica"
                     /db_xref="taxon:134536"
     Protein         1..429
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=46487
     Region          35..421
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 mtpnltfapd sivhpgtfga ddvsaaakpv aisgtdiltv knlskifgpk peraaelirq
       61 glsrneifeq tgnmvavndv slsvkageif vvmglsgsgk stlvrllnrl ieptsgqvil
      121 esrdiapmst pelrdvrrkk mamvfqsfal lpnrtvldni ayglevaglk kaerydiara
      181 altrvglgsy ekllpgelsg gmqqrvglar alavnpsvll mdeafsaldp lirfemqsel
      241 lrlqkeeqrt ivfishdiee aikiggrigi mkdgcliqvg tpaeliqspa dnyvrdffrn
      301 vdvsrflkas slmtrverel iscdvaapse rylnqlidsg adcgyvcdea gryqgcvtpa
      361 slrktgahsi reafvndvna vpldadlhql atialnqqhd vpvtdtagrl agivscrail
      421 kqvmerraa
//
LOCUS       WP_392394610             538 aa            linear   BCT 20-JAN-2025
DEFINITION  peptide ABC transporter substrate-binding protein [Paraburkholderia
            caledonica].
ACCESSION   WP_392394610
VERSION     WP_392394610.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caledonica
  ORGANISM  Paraburkholderia caledonica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 538)
  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 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   3  (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   4  (residues 1 to 538)
  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 538)
  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 11467924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Paraburkholderia caledonica"
                     /db_xref="taxon:134536"
     Protein         1..538
                     /product="peptide 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=59954
     Region          1..537
                     /region_name="OppA"
                     /note="ABC-type oligopeptide transport system, periplasmic
                     component [Amino acid transport and metabolism]; COG4166"
                     /db_xref="CDD:443327"
ORIGIN      
        1 mktpfayata lsalvltfts safavtvppg vtlaasqeit rqvpaetesl dpahieswtg
       61 ntialdmfeg ltridaagav vpgvaqswtr tgpdtwvfkl rhdarwsngq pvtaadfiya
      121 wqrvldpktg skytvlvefv knakailagk aplaslgara vdpytievtt evpaaffpql
      181 aamptmapvn rdvvarfgne wtrpgnfvgn gpymladwqp nnrlvgaksk tywnaskvvi
      241 tkvtylpien detamrmyqa gqfdytysip sgiyaqvskq fgpelktglq iatyyyslnn
      301 edpifkdkrv rqalsmvldr dlltqrltad gelpmyglis kgtqgaavfk pdwagwpmak
      361 rvdyarnllk sagysdakpl tftltyntnd lhkkvalfat sewrtklgvn tklenveykv
      421 llgqrhdgkv qasrdgwfvd yndamsyfdl ircnsvqndq rycnpqvdki vdeanqqldd
      481 akrtelltka hdtamndypm vplfqysavr lvkpyvggyt stnyvdqrat qdmylikh
//
LOCUS       WP_392395002             511 aa            linear   BCT 20-JAN-2025
DEFINITION  DUF1800 domain-containing protein [Paraburkholderia caledonica].
ACCESSION   WP_392395002
VERSION     WP_392395002.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caledonica
  ORGANISM  Paraburkholderia caledonica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009155
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Paraburkholderia caledonica"
                     /db_xref="taxon:134536"
     Protein         1..511
                     /product="DUF1800 domain-containing protein"
                     /calculated_mol_wt=54865
     Region          2..511
                     /region_name="COG5267"
                     /note="Uncharacterized conserved protein, DUF1800 family
                     [Function unknown]"
                     /db_xref="CDD:444080"
ORIGIN      
        1 maaqpnltaa aialnrfglg araddtppad pkawllaqfd qyqpkpvawa sqpdslaisg
       61 eleqqrmqlr mqtqrnpgga smpaqtnaqt geqaasqsda rkdkeaerka iraeirdnyr
      121 ssvnarvvsa lttqtpfver lvhfwsnhfa vstekpavaa lagsfeaeai rphvlgrfed
      181 mlvaverhpa mqlfldqtrs vgpdsvaamr aaqrnpqskr glnenlarei melhtlgvrs
      241 gynqedvtef araltgwsla tgprnpgnia nagssasagm qasrpmqeas apgsfvfrda
      301 lhepgsrtim grrydepgeq qalailhdla sapataqhig sklarhfiad nppagvserl
      361 agvfersggd lpsvyralld mpqawspvav kfktpwewai ssmrglgwqd lgnqqaapil
      421 aqlgqpvwrp gspagyddia aswaapdalv rrvevaqrla arvgdrldar slgqvllpgs
      481 lsapsavava raesastaia lllvspdfqr r
//
LOCUS       WP_392395120             290 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Paraburkholderia
            caledonica].
ACCESSION   WP_392395120
VERSION     WP_392395120.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caledonica
  ORGANISM  Paraburkholderia caledonica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789410
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Paraburkholderia caledonica"
                     /db_xref="taxon:134536"
     Protein         1..290
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30432
     Region          6..271
                     /region_name="PrpB"
                     /note="2-Methylisocitrate lyase and related enzymes, PEP
                     mutase family [Carbohydrate transport and metabolism];
                     COG2513"
                     /db_xref="CDD:442003"
ORIGIN      
        1 mealnklrkq leskelivap gawdgisarl ieqagfpvay mtgagvaaan gypdfglvtl
       61 temtaaartl trsvsipvia dadtgfgnal nvrrtvqeye ksgvaaiqie dqlfpkrcgh
      121 legkelvqtt efvekiaaaa aargeggmli vartdaravt glddaiervn raldagadia
      181 fveapqsvee aaaiarrvng pcllnlvpgg ktpniplkdv aelgfciail pgllltsmmg
      241 aadlalstvr ntgrvevrpd alpirdlfnr lgalewqypa asatgrdgar
//
LOCUS       WP_392395518             130 aa            linear   BCT 20-JAN-2025
DEFINITION  bactofilin family protein [Paraburkholderia caledonica].
ACCESSION   WP_392395518
VERSION     WP_392395518.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caledonica
  ORGANISM  Paraburkholderia caledonica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Deng,X., Gonzalez Llamazares,A., Wagstaff,J.M., Hale,V.L.,
            Cannone,G., McLaughlin,S.H., Kureisaite-Ciziene,D. and Lowe,J.
  TITLE     The structure of bactofilin filaments reveals their mode of
            membrane binding and lack of polarity
  JOURNAL   Nat Microbiol 4 (12), 2357-2368 (2019)
   PUBMED   31501539
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Ingerson-Mahar,M. and Gitai,Z.
  TITLE     A growing family: the expanding universe of the bacterial
            cytoskeleton
  JOURNAL   FEMS Microbiol Rev 36 (1), 256-266 (2012)
   PUBMED   22092065
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Kuhn,J., Briegel,A., Morschel,E., Kahnt,J., Leser,K., Wick,S.,
            Jensen,G.J. and Thanbichler,M.
  TITLE     Bactofilins, a ubiquitous class of cytoskeletal proteins mediating
            polar localization of a cell wall synthase in Caulobacter
            crescentus
  JOURNAL   EMBO J 29 (2), 327-339 (2010)
   PUBMED   19959992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Paraburkholderia caledonica"
                     /db_xref="taxon:134536"
     Protein         1..130
                     /product="bactofilin family protein"
                     /calculated_mol_wt=13581
     Region          7..117
                     /region_name="CcmA"
                     /note="Cytoskeletal protein CcmA, bactofilin family
                     [Cytoskeleton]; COG1664"
                     /db_xref="CDD:441270"
ORIGIN      
        1 mkshplnvtl lstglsihgn vildhglssf givdgsvvsn sgllhigqgg mvkgqvegeh
       61 vridgtvegd vhargvlein grvkgnvyyy gtirlgprat legqikrkse ltienssnvq
      121 qlsraaagnt
//
LOCUS       WP_392395421             399 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein
            [Paraburkholderia].
ACCESSION   WP_392395421
VERSION     WP_392395421.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 399)
  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 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   3  (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   4  (residues 1 to 399)
  AUTHORS   Igarashi,K., Ito,K. and Kashiwagi,K.
  TITLE     Polyamine uptake systems in Escherichia coli
  JOURNAL   Res Microbiol 152 (3-4), 271-278 (2001)
   PUBMED   11421274
REFERENCE   5  (residues 1 to 399)
  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   6  (residues 1 to 399)
  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 11430824
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..399
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0019808 - polyamine binding [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:0015846 - polyamine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44600
     Region          7..397
                     /region_name="PotD"
                     /note="Spermidine/putrescine-binding periplasmic protein
                     [Amino acid transport and metabolism]; COG0687"
                     /db_xref="CDD:440451"
ORIGIN      
        1 mhpsrvelrv lgttvtlqeh irkraeqdlg irlrfivqdg gavqrdgamh pdryelydqw
       61 fhsldclwpt halqpielar irrwdevnvl prtgrigrap arhaagklsg agctpadrly
      121 vqpdgslark pservsmlpl thnadsfvyl edampaslte geeswawlla pelagrvalq
      181 adaaigaida alaveasglm rfddignlsi eeidgliail idfkrrghfa gfwssfaeaa
      241 qlmiankvai qsiwspatve leraglkfrl arpregyraw fggigisrla hgrvldaaye
      301 ylnwwlegwa gatvarqgfy isnpersrah meanewaywy dgarasadlp gpiskhlvpa
      361 gqmrdggsyv armsrvavwd svmdehnylv rrwtefmrs
//
LOCUS       WP_392395952             350 aa            linear   BCT 20-JAN-2025
DEFINITION  PDDEXK nuclease domain-containing protein [Paraburkholderia
            caledonica].
ACCESSION   WP_392395952
VERSION     WP_392395952.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caledonica
  ORGANISM  Paraburkholderia caledonica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 350)
  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 10008845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Paraburkholderia caledonica"
                     /db_xref="taxon:134536"
     Protein         1..350
                     /product="PDDEXK nuclease domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39967
     Region          12..340
                     /region_name="YhcG"
                     /note="Predicted nuclease of restriction endonuclease-like
                     (RecB) superfamily, DUF1016 family [General function
                     prediction only]; COG4804"
                     /db_xref="CDD:443832"
ORIGIN      
        1 mtndltnlgr sedyrlwlsd lkqrverarq raaasvnrel iklywqignd ilhrqqqrgw
       61 gtavvdqlar dlksafpdmr gfsprnlkym ralaqawpep efvqqpaaql pwfhlctlld
      121 kvkdvahrdw yaakalehgw srsvlvmqie taahartsna vtnfaerlpp pqsdlardal
      181 kdpyifdflg ltenaqerdi ehaltqhitr fllelgagfa fvgrqyrlev ggdeffvdll
      241 fyhlklrcyv vvelkttpfk peyagqlnfy lsaidaqvka redqptigll lckeknrlva
      301 eyalrgvanp mgvaeyqllr hvpeslengl psidqieael rpdlpdaqgq
//
LOCUS       WP_392396148             388 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Paraburkholderia caledonica].
ACCESSION   WP_392396148
VERSION     WP_392396148.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caledonica
  ORGANISM  Paraburkholderia caledonica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 388)
  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 388)
  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
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 388)
  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   5  (residues 1 to 388)
  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   6  (residues 1 to 388)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 388)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 388)
  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 20170230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Paraburkholderia caledonica"
                     /db_xref="taxon:134536"
     Protein         1..388
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42026
     Region          <26..>72
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          93..383
                     /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 madfpavarq phsaywrslg dkavaspner lvldliwrrr aasradlvra tgltaqsimr
       61 lvdelierql lrmgdplprg grgkpspaie iapdfaytvg vsigtdsvst alidmggkvl
      121 qqtyvavrdf danglvtllr kqindyvrky klreerlfgv gvgitgffvg dgarvnpplp
      181 lerlalidle tlltrelalp vwldndgtva avgesllgag rwaanfvyly fshglgggvv
      241 vdgrvvrgsh gnagevaaml pmqklerptl eqlrsmledd giafpdigem lasfdpnwla
      301 cdrwtrqarr alsliasaaa alidpdaivf ggripyplaq rlideitidn larrgrgrpe
      361 prlvpaeaps dtaaigaall pfkeclfg
//
LOCUS       WP_392397319             368 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Rhizobium
            ruizarguesonis].
ACCESSION   WP_392397319
VERSION     WP_392397319.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium ruizarguesonis
  ORGANISM  Rhizobium ruizarguesonis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
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   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   4  (residues 1 to 368)
  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 368)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Rhizobium ruizarguesonis"
                     /db_xref="taxon:2081791"
     Protein         1..368
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39816
     Region          10..352
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 mktvnadind vlidcqslwk vfgdksaaam ksikerglgk kevlkefncv vgvsdasiev
       61 rrgeifcimg lsgsgkstli rllnklitps sgkvlvkgrd laalspvdlr qmrarnigmv
      121 fqsvallphr tvlenaafgl evqgiakper nktaaaalek vgladwvsry pnelsggmqq
      181 rvglaralas dpeiilmdep fsaldplirr qlqdefrqlt kalgksavfi thdldeairi
      241 gdriaimkdg viiqtgtaee iilnpadayv aefvagisrl hlikahsvmr svaefqrsqp
      301 nsdiaslart tpdadideli tltmqserda iavvdndqvv gvvtprsllm gvkgtsthdl
      361 taashnws
//
LOCUS       WP_392397387              82 aa            linear   BCT 20-JAN-2025
DEFINITION  Ig-like domain-containing protein [Citrobacter sedlakii].
ACCESSION   WP_392397387
VERSION     WP_392397387.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sedlakii
  ORGANISM  Citrobacter sedlakii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 82)
  AUTHORS   Fraser,J.S., Yu,Z., Maxwell,K.L. and Davidson,A.R.
  TITLE     Ig-like domains on bacteriophages: a tale of promiscuity and deceit
  JOURNAL   J Mol Biol 359 (2), 496-507 (2006)
   PUBMED   16631788
REFERENCE   2  (residues 1 to 82)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   3  (residues 1 to 82)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
REFERENCE   4  (residues 1 to 82)
  AUTHORS   Bork,P., Holm,L. and Sander,C.
  TITLE     The immunoglobulin fold. Structural classification, sequence
            patterns and common core
  JOURNAL   J Mol Biol 242 (4), 309-320 (1994)
   PUBMED   7932691
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475235
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Citrobacter sedlakii"
                     /db_xref="taxon:67826"
     Protein         1..82
                     /product="Ig-like domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=7836
     Region          <2..>82
                     /region_name="YjdB"
                     /note="Uncharacterized conserved protein YjdB, contains
                     Ig-like domain [General function prediction only];
                     COG5492"
                     /db_xref="CDD:444243"
ORIGIN      
        1 mpatgitvtp etasvdvgdt tsltaalapa gatdtvswes sdpvvatvna sgvvtgvaag
       61 tatitakart ftdtvtitvt ep
//
LOCUS       WP_392400821             252 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Aeromonas salmonicida].
ACCESSION   WP_392400821
VERSION     WP_392400821.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas salmonicida
  ORGANISM  Aeromonas salmonicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 252)
  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 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
REFERENCE   3  (residues 1 to 252)
  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   4  (residues 1 to 252)
  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 252)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Aeromonas salmonicida"
                     /db_xref="taxon:645"
     Protein         1..252
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27709
     Region          1..248
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <140..247
                     /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 mtrpraasll statpfslrh yqsdisshsh dfaqlviplg gpleievqgq grrlapgfvc
       61 viapgerhdy aadpalsflv qesdwlpgnl aarpfivlde pqrhylaflh rmvaagrqvv
      121 gmeqvwlgll aqgqgmhssa pphlaarilk vqrhieahla eplgnerlaa iaclgqsqfk
      181 htfrqqlgms vshyirarrm tlartllsht qlpigeiasr cgyqnqgafa erflaesglt
      241 pslwrqqngl lp
//
LOCUS       WP_392401806             688 aa            linear   BCT 20-JAN-2025
DEFINITION  type I restriction-modification system subunit M [Streptomyces sp.
            NPDC014793].
ACCESSION   WP_392401806
VERSION     WP_392401806.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014793
  ORGANISM  Streptomyces sp. NPDC014793
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 688)
  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   2  (residues 1 to 688)
  AUTHORS   Youell,J. and Firman,K.
  TITLE     Mechanistic insight into Type I restriction endonucleases
  JOURNAL   Front Biosci (Landmark Ed) 17 (6), 2122-2139 (2012)
   PUBMED   22652768
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 688)
  AUTHORS   Sistla,S. and Rao,D.N.
  TITLE     S-Adenosyl-L-methionine-dependent restriction enzymes
  JOURNAL   Crit Rev Biochem Mol Biol 39 (1), 1-19 (2004)
   PUBMED   15121719
REFERENCE   4  (residues 1 to 688)
  AUTHORS   Murray,N.E.
  TITLE     Type I restriction systems: sophisticated molecular machines (a
            legacy of Bertani and Weigle)
  JOURNAL   Microbiol Mol Biol Rev 64 (2), 412-434 (2000)
   PUBMED   10839821
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114514
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Streptomyces sp. NPDC014793"
                     /db_xref="taxon:3364914"
     Protein         1..688
                     /product="type I restriction-modification system subunit
                     M"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=78024
     Region          8..140
                     /region_name="HsdM_N"
                     /note="HsdM N-terminal domain; pfam12161"
                     /db_xref="CDD:463478"
     Region          153..425
                     /region_name="HsdM"
                     /note="Type I restriction-modification system, DNA
                     methylase subunit [Defense mechanisms]; COG0286"
                     /db_xref="CDD:440055"
ORIGIN      
        1 msdtnqqlad fiwsvadllr gdykrseyak vilpltvlrr ldcvleekgt rqavrdraes
       61 ytgerphall ravaelpfyn vskqdfktig sddknvytnl kdfirgfspe ateiidrydf
      121 hiqierlnda gllyqvvkkf sdidlsprwv snhdmgyvfe elirkfadas netagehftp
      181 reivklmvel llgpddkafl rpgqvvdild pacgtggmla aaeehikqin pdtrvnlygq
      241 einaesyaic rsdmllkgha adnirfgnsf trdwhegstf tymlanppfg vewkksekav
      301 keeyeekgfa grfgaglpri ndgsflflqh mlhkmkqpkk neqgeltggs riaivfngsp
      361 lftggagsge seirrwilec dyleaivglp dqlfyntgis tyfwilsnrk pkqrkgkvil
      421 ldarsecvkr rkslgekrke iseeqirhic amyrdaeqia adenhpdhak ikilpnkeyg
      481 ykritvdrpl klrfevtedt laqlaesaal gkvlgdkttd pqelakrqre fadalkplig
      541 gvwrtkaeaw dalhnaitaa gllwpssatf qkalrdavgv rdpegevqyl kgkqpehdpe
      601 lrdaenvpmg qdideyleae vkphvndawi aeiknpktkt terykegyei pftrhfyvye
      661 ppkplakida elksleakiq rllgevta
//
LOCUS       WP_392402520             287 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            NPDC014793].
ACCESSION   WP_392402520
VERSION     WP_392402520.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014793
  ORGANISM  Streptomyces sp. NPDC014793
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 287)
  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 287)
  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 16111081
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Streptomyces sp. NPDC014793"
                     /db_xref="taxon:3364914"
     Protein         1..287
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32473
     Region          20..71
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(22,26,51)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(25,50)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(32..33,44,47,51..52)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          93..271
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mvrrkdidgs vsvpdfygke lrwqreaagl slerlvegsf ygkshlsdie hgkrrmpmdl
       61 arhvdrvlgt dgyferhced vrrarrgpha ayferaleae khaesielws pstlpgllqt
      121 apyaralvhs ahpsvsddwv eekvrarldr arlfeddhav peywailhes lltdaivsse
      181 dmaeqldrma elaerrrivp qvvsrrsgay plmassimim tfpdappliy teasysgdti
      241 ddpalvkqyr kaydrlrava lspgaslami kaaaedyrng krpdrle
//
LOCUS       WP_392402766             395 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Streptomyces sp.
            NPDC014793].
ACCESSION   WP_392402766
VERSION     WP_392402766.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014793
  ORGANISM  Streptomyces sp. NPDC014793
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 395)
  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 395)
  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 395)
  AUTHORS   ter Beek,J., 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 395)
  AUTHORS   Igarashi,K., Ito,K. and Kashiwagi,K.
  TITLE     Polyamine uptake systems in Escherichia coli
  JOURNAL   Res Microbiol 152 (3-4), 271-278 (2001)
   PUBMED   11421274
REFERENCE   5  (residues 1 to 395)
  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   6  (residues 1 to 395)
  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 11430824
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Streptomyces sp. NPDC014793"
                     /db_xref="taxon:3364914"
     Protein         1..395
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0019808 - polyamine binding [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:0015846 - polyamine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=43863
     Region          10..392
                     /region_name="PotD"
                     /note="Spermidine/putrescine-binding periplasmic protein
                     [Amino acid transport and metabolism]; COG0687"
                     /db_xref="CDD:440451"
ORIGIN      
        1 mtrtpppaps rrsllraltg aaalgtlagc gvpaayvepg drsvtdesaa drrltwanwp
       61 lyidtddddt srrptldafe khtgisvgyt eeindndeff gkispalmnh qrtgrdlivv
      121 sdwmcarfvr lgwvqrmdrs rqpnvaehld pllrspafdp grgstvpwqs gitgiaydrr
      181 rlgreirgva dlwasdlkgr vtllsgldea fallmqgdgv ditrwttddf hrvcdrvere
      241 vhrgqirrft gndytkdlvs gdvlacqays gdviqlqadn pdirfvvpes gaelwsdslm
      301 ipdrarhksn aerlidyyyq pevaarlaaw vnyvcpvpaa revlaasrdk dtaalagnpl
      361 ifpdsamrgr lavarditst erpelakrwn tivgl
//
LOCUS       WP_392402844             454 aa            linear   BCT 20-JAN-2025
DEFINITION  SWIM zinc finger family protein [Streptomyces sp. NPDC014793].
ACCESSION   WP_392402844
VERSION     WP_392402844.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014793
  ORGANISM  Streptomyces sp. NPDC014793
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Hassan,I.U., Rehman,H.M., Liu,Z., Zhou,L., Samma,M.K., Wang,C.,
            Rong,Z., Qi,X., Cai,D. and Zhao,H.
  TITLE     Genome-wide identification and spatiotemporal expression profiling
            of zinc finger SWIM domain-containing protein family genes
  JOURNAL   Zool Res 44 (3), 663-674 (2023)
   PUBMED   37161653
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     SWIM, a novel Zn-chelating domain present in bacteria, archaea and
            eukaryotes
  JOURNAL   Trends Biochem Sci 27 (8), 384-386 (2002)
   PUBMED   12151216
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Streptomyces sp. NPDC014793"
                     /db_xref="taxon:3364914"
     Protein         1..454
                     /product="SWIM zinc finger family protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47258
     Region          4..420
                     /region_name="SWIM"
                     /note="Uncharacterized protein, contains SWIM-type Zn
                     finger domain [Function unknown]; COG4715"
                     /db_xref="CDD:443750"
ORIGIN      
        1 mteqgvrwta dqvlalapda asrkagsrlg tagpwsgags gegtvwglck gsgsrpyqtv
       61 vdladatgpg ckcscpsrkf pckhalglll lwaegdgsvp vaaeppdwag qwlagrrera
      121 egrragadgg aasgspdpea arrraerrae rvtagatele qrladllrgg laaaeqagyg
      181 lweetaarmv daqapglaar vrelgavpas gpgwparlle esallhllvr gwlrrdrlpd
      241 alaatvrsrl glpatpdgpp lrdrwlvlaq ydtsdakltt rriwlhgads gltrlllsyg
      301 aagrapelsl pvglaldadl svfpgagqvr aalgeqyalp apaalrppgg ttaeaaaryg
      361 ealrgdpwle svpvtldrvv paqdaeagga wqladaeads alpltesfrs rpglwrlval
      421 sggapvrvfg ecghrgftpl tawpegpgdp vtlc
//
LOCUS       WP_392402947             290 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptomyces sp.
            NPDC014793].
ACCESSION   WP_392402947
VERSION     WP_392402947.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014793
  ORGANISM  Streptomyces sp. NPDC014793
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 290)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 290)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces sp. NPDC014793"
                     /db_xref="taxon:3364914"
     Protein         1..290
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32121
     Region          19..102
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          126..285
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mldrlnqame hieghldqri evsalaritl tseyhfrrlf sslagmplse yvrrrrltva
       61 gaevlagrpt lleigvrygy tsgeafaraf ramhgvgpge arhtgaalns qprlsfrltv
      121 egnstmryri vekdafrvvg rkarvplihq gvnphiaehv rsispetmlr iaglsdqdpe
      181 gvvsatvrls egfeegseld yyhavvtsaa efpegldvld cpagtwavfd ntgpfpealq
      241 rmwgavaaqw ipsnpyeyrp gpeilrtrps eddptwsdaq lwipvtrtta
//
LOCUS       WP_392403001             393 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. NPDC014793].
ACCESSION   WP_392403001
VERSION     WP_392403001.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014793
  ORGANISM  Streptomyces sp. NPDC014793
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 393)
  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 393)
  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
REFERENCE   3  (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   4  (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   5  (residues 1 to 393)
  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   6  (residues 1 to 393)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (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 20170230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Streptomyces sp. NPDC014793"
                     /db_xref="taxon:3364914"
     Protein         1..393
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39703
     Region          <10..>71
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          77..384
                     /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 mtarpanahq arllkllrdg gpnsraqlgd qvdlsrskla vevdrlletg lvvadglaas
       61 rggrrshnvr ldpglrflgv digatsvdva vtnaeleilg hlnqpmdvre gpvavfeqvl
      121 dmagklkatg laegfdgagi gvpgpvrfpe gvpvappimp gwdgfpvrea lsqelgcpvm
      181 vdndvnlmam geqhagvart vadflcvkig tgigcgivvg ghvhrgttgs agdighiqav
      241 pdgrpcacgn rgcleahfsg aalardavqa agqglsaela arlaangtls avdvaaaaaa
      301 gdptaldlir eggtrvgqvi aglvsffnpg lvvigggvtg lghtllaair tqvyrqslpl
      361 atgnlpivlg elgptagvtg aarlisdhlf spa
//
LOCUS       WP_392403553             707 aa            linear   BCT 20-JAN-2025
DEFINITION  DNA gyrase/topoisomerase IV subunit B [Streptomyces sp.
            NPDC014793].
ACCESSION   WP_392403553
VERSION     WP_392403553.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NPDC014793
  ORGANISM  Streptomyces sp. NPDC014793
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Tari,L.W., Trzoss,M., Bensen,D.C., Li,X., Chen,Z., Lam,T.,
            Zhang,J., Creighton,C.J., Cunningham,M.L., Kwan,B., Stidham,M.,
            Shaw,K.J., Lightstone,F.C., Wong,S.E., Nguyen,T.B., Nix,J. and
            Finn,J.
  TITLE     Pyrrolopyrimidine inhibitors of DNA gyrase B (GyrB) and
            topoisomerase IV (ParE). Part I: Structure guided discovery and
            optimization of dual targeting agents with potent, broad-spectrum
            enzymatic activity
  JOURNAL   Bioorg Med Chem Lett 23 (5), 1529-1536 (2013)
   PUBMED   23352267
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Gadelle,D., Filee,J., Buhler,C. and Forterre,P.
  TITLE     Phylogenomics of type II DNA topoisomerases
  JOURNAL   Bioessays 25 (3), 232-242 (2003)
   PUBMED   12596227
REFERENCE   3  (residues 1 to 707)
  AUTHORS   Wang,J.C.
  TITLE     Cellular roles of DNA topoisomerases: a molecular perspective
  JOURNAL   Nat Rev Mol Cell Biol 3 (6), 430-440 (2002)
   PUBMED   12042765
REFERENCE   4  (residues 1 to 707)
  AUTHORS   Champoux,J.J.
  TITLE     DNA topoisomerases: structure, function, and mechanism
  JOURNAL   Annu Rev Biochem 70, 369-413 (2001)
   PUBMED   11395412
REFERENCE   5  (residues 1 to 707)
  AUTHORS   Roca,J.
  TITLE     The mechanisms of DNA topoisomerases
  JOURNAL   Trends Biochem Sci 20 (4), 156-160 (1995)
   PUBMED   7770916
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Streptomyces sp. NPDC014793"
                     /db_xref="taxon:3364914"
     Protein         1..707
                     /product="DNA gyrase/topoisomerase IV subunit B"
                     /EC_number="5.6.2.2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003918 - DNA topoisomerase type II
                     (double strand cut, ATP-hydrolyzing) activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006265 - DNA topological change [Evidence
                     IEA]"
                     /calculated_mol_wt=76973
     Region          21..693
                     /region_name="GyrB"
                     /note="DNA gyrase/topoisomerase IV, subunit B
                     [Replication, recombination and repair]; COG0187"
                     /db_xref="CDD:439957"
ORIGIN      
        1 mtadtsvpst allagadrdg snytarhllv legleavrkr pgmyigstds rglmhclwei
       61 idnavdealg gygdhievil hddasvevrd ngrgipvdve pktglsgvev vmtklhaggk
      121 fgggsyaasg glhgvgasvv nalsarldve vdrsgnthai sfrrgvpgaf rgngadakfe
      181 agsglaktkk ipksrtgtrv rywadrqifl kdaklsletl hqrarqtafl vpgltivvrd
      241 efglgeggsk geesfrfdgg isefceylas dkavcdvlrf sgqgtfketv pvldehgqmt
      301 ptevarelgv dialrwgtgy daklrsfvni iatpkggthv agfeqaitqt mnevlrtkkm
      361 lrvaednivk ddalegltav vtvrlaepqf egqtkevlgt saarrivnnv vtrelkaflt
      421 stkrdaaaqa rvvmekvvaa artrvaarqh kdaqrrktal essslpakla dcrsddvdrs
      481 elfivegdsa lgtaklarns efqallpirg kilnvqrssv tdmlknaecg aiiqvigags
      541 grtfdidaar ygkiimmtda dvdgshircl lltlfqrymr pmvesgrvfa avpplhriel
      601 iqpkkgqdky vytysdrelr dklmefqskg vrykdsiqry kglgemdadq laettmdprh
      661 rtlrrinlsd leaaeqvfdl lmgndvaprk efisgsaatl drsrida
//
LOCUS       WP_392404730             250 aa            linear   BCT 20-JAN-2025
DEFINITION  4'-phosphopantetheinyl transferase family protein [Edwardsiella
            piscicida].
ACCESSION   WP_392404730
VERSION     WP_392404730.1
KEYWORDS    RefSeq.
SOURCE      Edwardsiella piscicida
  ORGANISM  Edwardsiella piscicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Hafniaceae; Edwardsiella.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459479
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Edwardsiella piscicida"
                     /db_xref="taxon:1263550"
     Protein         1..250
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=27084
     Region          59..250
                     /region_name="EntD"
                     /note="4'-phosphopantetheinyl transferase EntD
                     (siderophore biosynthesis) [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2977"
                     /db_xref="CDD:442216"
ORIGIN      
        1 mrsssgsivp rvsrdgaeqg ddadfiqgvt wlsfpgypgr igacrfslsr yraegayqgi
       61 alplslqqaa pkrqaefiag rwvarqvmta lgicdgviar gadhapqwpp giagsishaa
      121 gmalcaahpt srrggvgidv etwlapsrar tlqsaiahph elaallgtap asrrlitllf
      181 sakeslfkal ypevkrwfdf hdaqmtaidw rrrtfrltll tslasdypag rcfhgqflsd
      241 deavmtliyc
//
LOCUS       WP_392405416             142 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Edwardsiella
            piscicida].
ACCESSION   WP_392405416
VERSION     WP_392405416.1
KEYWORDS    RefSeq.
SOURCE      Edwardsiella piscicida
  ORGANISM  Edwardsiella piscicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Hafniaceae; Edwardsiella.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 142)
  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 142)
  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 142)
  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 10009358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Edwardsiella piscicida"
                     /db_xref="taxon:1263550"
     Protein         1..142
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15548
     Region          16..139
                     /region_name="HigA"
                     /note="Antitoxin component HigA of the HigAB
                     toxin-antitoxin module, contains an N-terminal HTH domain
                     [Defense mechanisms]; COG5499"
                     /db_xref="CDD:444250"
ORIGIN      
        1 mmyddavkaa kvlasivpll ggsqdrtdye salsliehll etdpdsplvd mlsakidaye
       61 nsapefaefn yrlagentgi avlqmlmknh gmaqsdlqde igskalvsri lsgqrnltle
      121 hmrklahrfn vpvtafidtq vq
//
LOCUS       WP_392405711             280 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Cardiobacterium hominis].
ACCESSION   WP_392405711
VERSION     WP_392405711.1
KEYWORDS    RefSeq.
SOURCE      Cardiobacterium hominis
  ORGANISM  Cardiobacterium hominis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cardiobacteriales; Cardiobacteriaceae; Cardiobacterium.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 280)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 280)
  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   6  (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 10007405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Cardiobacterium hominis"
                     /db_xref="taxon:2718"
     Protein         1..280
                     /product="AraC 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:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31228
     Region          1..279
                     /region_name="SbmC"
                     /note="DNA gyrase inhibitor GyrI/SbmC [Replication,
                     recombination and repair]; COG3449"
                     /db_xref="CDD:442672"
ORIGIN      
        1 mrhpeynear fakvlqhlhq hyphdidlar ladiaclspc hwhrlyravm getiyetlkr
       61 irlhhaahll ldgnkplpdi aracgyggna qsfarifrda ygmspqdyra rggvpypapl
      121 penasaaysv eirdiaalpv vslphhgdym gigasfsqle tlltlrghlp apqaryfgiy
      181 yddpagcpsa qlraaaaval ggadatpplq tltlaagrya vlehrgayae lhraydwlyr
      241 dwllnspyql adapcleeyl ndwqqvppqe lrtniylpli
//
LOCUS       WP_392406074             326 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Delftia].
ACCESSION   WP_392406074
VERSION     WP_392406074.1
KEYWORDS    RefSeq.
SOURCE      unclassified Delftia
  ORGANISM  unclassified Delftia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Delftia.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 326)
  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   6  (residues 1 to 326)
  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 10007405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="unclassified Delftia"
                     /db_xref="taxon:2613839"
     Protein         1..326
                     /product="AraC 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:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36123
     Region          10..325
                     /region_name="SbmC"
                     /note="DNA gyrase inhibitor GyrI/SbmC [Replication,
                     recombination and repair]; COG3449"
                     /db_xref="CDD:442672"
ORIGIN      
        1 mtnkpseqas raeyarrinr vlnyidahld qpldgahlad ianfsrfhfh rifaawmget
       61 lgsyaqrrrl ekaafrlscg sketvletal atgfqsgeaf arafklkfgc tpsawrsttl
      121 erlktqaaai gqqpgsqqsn pdqvfgnlhq edlrafgepq gschlkeeia mdvriidlpk
      181 ahvayqrlig pygpaigqfw rgtiapwmhs nglsdqtcyg igyddpsltp tnkcrydacv
      241 evpahfvasg qvdtqtlpgg ryavarfkgk peglanawmw ltrewmpssg mqcddrpcfe
      301 mfsavnamda etgefccdic ipvral
//
LOCUS       WP_392406417             119 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Cardiobacterium
            hominis].
ACCESSION   WP_392406417
VERSION     WP_392406417.1
KEYWORDS    RefSeq.
SOURCE      Cardiobacterium hominis
  ORGANISM  Cardiobacterium hominis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cardiobacteriales; Cardiobacteriaceae; Cardiobacterium.
REFERENCE   1  (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   2  (residues 1 to 119)
  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 119)
  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 119)
  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 10582316
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Cardiobacterium hominis"
                     /db_xref="taxon:2718"
     Protein         1..119
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13537
     Region          7..60
                     /region_name="HTH_19"
                     /note="Helix-turn-helix domain; pfam12844"
                     /db_xref="CDD:463728"
ORIGIN      
        1 mklsdlgkft rkyridknil lkdmaeelgi staflsavet gkkavpanfy drltknysfn
       61 neemkelkaa idmtikqati pvpdndldrr lvgafcrsfq dldeqkkrdf lrileggne
//
LOCUS       WP_392409335             285 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Achromobacter sp.
            413638].
ACCESSION   WP_392409335
VERSION     WP_392409335.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter sp. 413638
  ORGANISM  Achromobacter sp. 413638
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789410
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Achromobacter sp. 413638"
                     /db_xref="taxon:3342385"
     Protein         1..285
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30081
     Region          6..285
                     /region_name="PrpB"
                     /note="2-Methylisocitrate lyase and related enzymes, PEP
                     mutase family [Carbohydrate transport and metabolism];
                     COG2513"
                     /db_xref="CDD:442003"
ORIGIN      
        1 mntlskqlvq gpvlapgvyd alsalaaeqa gfqalylsga siaytrlgrs dvglttysev
       61 edtlariaer vrariivdad tgfgnalnvq rtvrglerag aamiqledqt fpkrcghldg
      121 ksvvpaaemc gklraavdar qsretlilar tdalasegld aaleraeryl eagadalfie
      181 alrsgeqmra acgrfagrap llanmveggk tpvqgaqela algfgivifp ggtaravaht
      241 lagyygslrq hgsttpwrdr mldfdglnam igtpellaag kryea
//
LOCUS       WP_392409698             389 aa            linear   BCT 20-JAN-2025
DEFINITION  PDDEXK nuclease domain-containing protein [Achromobacter sp.
            413638].
ACCESSION   WP_392409698
VERSION     WP_392409698.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter sp. 413638
  ORGANISM  Achromobacter sp. 413638
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Achromobacter sp. 413638"
                     /db_xref="taxon:3342385"
     Protein         1..389
                     /product="PDDEXK nuclease domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43814
     Region          19..377
                     /region_name="YhcG"
                     /note="Predicted nuclease of restriction endonuclease-like
                     (RecB) superfamily, DUF1016 family [General function
                     prediction only]; COG4804"
                     /db_xref="CDD:443832"
ORIGIN      
        1 mtirktpaaa gkrsalpvgy agihggivel ldaarqaaar svnalmtasy weigrrivea
       61 eqkgkrragy geqlmerlsa dlttrfgrgf spdnlenmrr ffvayplsai setlsrksgd
      121 glpiensetv srkfdlskla qvftlpwsay vrllsvkddh arqfyeaeal rggwsvrqld
      181 rqigsqfyer talskdkaam lvkgavakpe davkpndaik dpyvlefldl kdeysesdle
      241 aaliqrleyf llelgegftf vgrqrrlrid qtwyrvdllf fhrklhclvi vdlklgslth
      301 advgqmhmyc nyakehwayp denppvglil cadkghalar yaldglpnkv maanyrtvlp
      361 daellqkele ntrrllesrg tlslkddkp
//
LOCUS       WP_392409890             311 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Achromobacter sp. 413638].
ACCESSION   WP_392409890
VERSION     WP_392409890.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter sp. 413638
  ORGANISM  Achromobacter sp. 413638
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Achromobacter sp. 413638"
                     /db_xref="taxon:3342385"
     Protein         1..311
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=33302
     Region          2..309
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mpplrpggrv aivapasaap naaddaadwl lsrgyqprim paarsrldtp fdylagtdae
       61 raadlhaaft sadidavwcl qggfgswrll dlldyellrr hakpfigysd italhlaiqr
      121 hagfvtfhgp mlaqdllngr eeptesalya mvggrmgqga wigapdyalp ttlmpgtatg
      181 rlaggnlali camqgsrhei dtrdailfie dvneavprvd rmlsqlaaag kfesikgvla
      241 gsftrsgard daqfqyafhp llrerfgplg ipvlagwpsg hgdpnltlpl garvtldatr
      301 qglrleqavt r
//
LOCUS       WP_392411218             329 aa            linear   BCT 20-JAN-2025
DEFINITION  KpsF/GutQ family sugar-phosphate isomerase [Achromobacter sp.
            413638].
ACCESSION   WP_392411218
VERSION     WP_392411218.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter sp. 413638
  ORGANISM  Achromobacter sp. 413638
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Meredith,T.C. and Woodard,R.W.
  TITLE     Characterization of Escherichia coli D-arabinose 5-phosphate
            isomerase encoded by kpsF: implications for group 2 capsule
            biosynthesis
  JOURNAL   Biochem J 395 (2), 427-432 (2006)
   PUBMED   16390329
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Meredith,T.C. and Woodard,R.W.
  TITLE     Identification of GutQ from Escherichia coli as a D-arabinose
            5-phosphate isomerase
  JOURNAL   J Bacteriol 187 (20), 6936-6942 (2005)
   PUBMED   16199563
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002722
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Achromobacter sp. 413638"
                     /db_xref="taxon:3342385"
     Protein         1..329
                     /product="KpsF/GutQ family sugar-phosphate isomerase"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33974
     Region          8..322
                     /region_name="GutQ"
                     /note="D-arabinose 5-phosphate isomerase GutQ
                     [Carbohydrate transport and metabolism, Cell
                     wall/membrane/envelope biogenesis]; COG0794"
                     /db_xref="CDD:440557"
ORIGIN      
        1 mtehpslssd talssarrtl qiesqalqdl sarlddsfaq vvalllacrg rvvvsgigkt
       61 ghvarkiaat lastgtpaff vhaaeavhgd lgmitrddvl iaisysgsgq elltilpvar
      121 rmgaklvait gnpqselall advhldasva qeacplnlap tasttaalal gdalavacle
      181 argfgpqdfa rshpggalgr rllthvrdvm rqgdalpiva tgtpvpqalk tmsakgmgmt
      241 vvadaagrpq giftdgdlrr liasqgdirg lavddgmtrs prsigpdala veaaqqmdel
      301 rlnhmlvlds dgallgalhm hdlmaakvv
//
LOCUS       WP_392411253             303 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Achromobacter sp. 413638].
ACCESSION   WP_392411253
VERSION     WP_392411253.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter sp. 413638
  ORGANISM  Achromobacter sp. 413638
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Achromobacter sp. 413638"
                     /db_xref="taxon:3342385"
     Protein         1..303
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=31930
     Region          26..286
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 maivvavvmy vgmatlanwt afgaavsalp gllwvqvval silsyllrfa rwhhfivalg
       61 hkvpilrnle iylaafaltl tpgkagetir svylhpygvs yphsigafvs erlldlvave
      121 alallavsmf peyrlwmfaa iacivivill lrsrllslig rraagssvvg daanlvatvr
      181 fllsgrrvam aaplslmawm aqgvslyliv halgyeltas tavtiyclsi lagaasfipg
      241 glgateaaiv lllsatgvgq tdaitaslis rsltlwlavg igvvamtkta vviqqtrsvq
      301 rge
//
LOCUS       WP_392412160             267 aa            linear   BCT 20-JAN-2025
DEFINITION  transglutaminase family protein [Achromobacter sp. 413638].
ACCESSION   WP_392412160
VERSION     WP_392412160.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter sp. 413638
  ORGANISM  Achromobacter sp. 413638
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12090973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Achromobacter sp. 413638"
                     /db_xref="taxon:3342385"
     Protein         1..267
                     /product="transglutaminase family protein"
                     /calculated_mol_wt=28883
     Region          5..78
                     /region_name="Bact_transglu_N"
                     /note="Bacterial transglutaminase-like N-terminal region;
                     pfam08379"
                     /db_xref="CDD:462455"
     Region          <110..219
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mkqiithvth yrytapvtys iqtlrltprd dehqrvlrwh ieapgalerq vdaygnitht
       61 ltlngphtdi elrvvgqvvv galargalgg edsrlpvhay cvqtaltqad etilaftrha
      121 lpdglntpdd alalaraicd rvayepgmtd vttaanqvla mghgvcqdha hlflacargl
      181 gvparyvsgy lyttaehaas hawadiwlpg agwtsvditn rqfasechcr lavardydsa
      241 spvrgvrngg geesmevtvq vqtaaqq
//
LOCUS       WP_392413275             576 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SWIM zinc finger family protein [unclassified
            Delftia].
ACCESSION   WP_392413275
VERSION     WP_392413275.1
KEYWORDS    RefSeq.
SOURCE      unclassified Delftia
  ORGANISM  unclassified Delftia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Delftia.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Hassan,I.U., Rehman,H.M., Liu,Z., Zhou,L., Samma,M.K., Wang,C.,
            Rong,Z., Qi,X., Cai,D. and Zhao,H.
  TITLE     Genome-wide identification and spatiotemporal expression profiling
            of zinc finger SWIM domain-containing protein family genes
  JOURNAL   Zool Res 44 (3), 663-674 (2023)
   PUBMED   37161653
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     SWIM, a novel Zn-chelating domain present in bacteria, archaea and
            eukaryotes
  JOURNAL   Trends Biochem Sci 27 (8), 384-386 (2002)
   PUBMED   12151216
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10516955
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="unclassified Delftia"
                     /db_xref="taxon:2613839"
     Protein         1..576
                     /product="SWIM zinc finger family protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=64515
     Region          509..547
                     /region_name="SWIM"
                     /note="SWIM zinc finger; pfam04434"
                     /db_xref="CDD:309540"
ORIGIN      
        1 mefryqyygs tqvsdtatqq afsfapdllr pptrfdgllr rdgpaflqvr eglsalhsvv
       61 vsdmrtrgrd ktayrewlqe hesqllagfm adtggaqara keisvelkdl retrnqvlap
      121 fykaqrkyfd wlyqanrdaw yvldpvitvh pdrllfeafs qdessycavs irheafehag
      181 ericgttnid ysaslyeefq kirsyrdtrl tldpagfavq vgadpalree kidlpdswlr
      241 gfvqvssama lpatvvelhp mdlfnicarl rarrerhgpr alrfeltpgq ppavvfepwe
      301 erlatrrshv vsdalgaggg tirlwgrrrl ltlerlipqa trvrvhllgs gmpsfwvvel
      361 gqvtvtlgls gwsandwaas arfhlmapqa evtpaqveav grqlqscwqa gaqelaqatg
      421 lapaqvhtam trwmqagrav ydldagryaw rellreplta qqlqpanpee dkalalvrgk
      481 aiappridrk dgfsritgqi pradgkrlfd tqlelnader ltdarcscnh yqqhrlrqgp
      541 cehmialrlv aqaqldaarq pagpqqaaaa gqgeia
//
LOCUS       WP_392415939             576 aa            linear   BCT 20-JAN-2025
DEFINITION  SWIM zinc finger family protein [Delftia sp. WSY_7].
ACCESSION   WP_392415939
VERSION     WP_392415939.1
KEYWORDS    RefSeq.
SOURCE      Delftia sp. WSY_7
  ORGANISM  Delftia sp. WSY_7
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Delftia.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Hassan,I.U., Rehman,H.M., Liu,Z., Zhou,L., Samma,M.K., Wang,C.,
            Rong,Z., Qi,X., Cai,D. and Zhao,H.
  TITLE     Genome-wide identification and spatiotemporal expression profiling
            of zinc finger SWIM domain-containing protein family genes
  JOURNAL   Zool Res 44 (3), 663-674 (2023)
   PUBMED   37161653
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     SWIM, a novel Zn-chelating domain present in bacteria, archaea and
            eukaryotes
  JOURNAL   Trends Biochem Sci 27 (8), 384-386 (2002)
   PUBMED   12151216
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10516955
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Delftia sp. WSY_7"
                     /db_xref="taxon:3367202"
     Protein         1..576
                     /product="SWIM zinc finger family protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=64573
     Region          509..547
                     /region_name="SWIM"
                     /note="SWIM zinc finger; pfam04434"
                     /db_xref="CDD:309540"
ORIGIN      
        1 mefryqyygs tqvsdtatqq afsfapdllr pptrfdgllr rdgpaflqvr eglsalhsvv
       61 vsdmrtrgrd ktayrewlqe hesqllagfm adtggaqara reisaelkdl retrnqvlap
      121 fykaqrkyfd wlyqanrdaw yvldpvitvh pdrllfeafs qdessycavs irheafehag
      181 ericgttnid ysaslyeefq kirsyrdtrl tldpagfavq vgadpalree kidlpdswlr
      241 gfvqvssama lpatvvelhp mdlfnicarl rarrerhgpr alrfeltpgq ppavvfepwe
      301 erlatrrshv vsdalgtggg tirlwgrrrl ltlerlipqa trvrvhllgs gmpsfwvvel
      361 gqvtvtlgls gwsandwaas arfhlmapqa evtpaqveav grqlqscwqa gaqelaqatg
      421 lvpaqvhtam trwmqagrav ydldagryaw rellreplta qqlqpanpee dkalalvrgk
      481 aiappridrk dgfsritgqi pradgkrlfd tqlelnader ltdarcscnh yqqhrlrqgp
      541 cehmialrlv aqaqldaarq pagpqqaaaa gqgeia
//
LOCUS       WP_392416604             534 aa            linear   BCT 20-JAN-2025
DEFINITION  peptide ABC transporter substrate-binding protein [Aeromonas
            media].
ACCESSION   WP_392416604
VERSION     WP_392416604.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas media
  ORGANISM  Aeromonas media
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 534)
  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 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   3  (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
REFERENCE   4  (residues 1 to 534)
  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 534)
  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 11467924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Aeromonas media"
                     /db_xref="taxon:651"
     Protein         1..534
                     /product="peptide 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=59596
     Region          1..533
                     /region_name="OppA"
                     /note="ABC-type oligopeptide transport system, periplasmic
                     component [Amino acid transport and metabolism]; COG4166"
                     /db_xref="CDD:443327"
ORIGIN      
        1 mkgwspllal lgcvcvqaad vpagtqlaae qavvrhlkde paslsplklv glpelqvlrd
       61 lyeglltqga dgkvlpgvaa swenegnqkf tfhlrpdarw sngdpvrasd fvygwrklvd
      121 peeaatfawf aqlahfdkvd eivegklppe algvqalddh tlqvtlsqpv pyflsllthp
      181 slsplhrasm eqygnqwtqp gklvgngafv lnhrvvnekl eltpnpyywd rahtvltrvt
      241 fvpinqesaa tnrylagdlh itesfpkeqy hklmkqipee vytpeqlgty yyafntqrap
      301 lndvrvrqal sytidralia dkvlgtgekp ayhftpdvta gfvpkpnlls tssqqaldek
      361 arallteagy gpgnplkltl lyntaeihkk malaianlwk qklgarvelt nqewktylds
      421 rqsgqfevir sswvadyndp saflglwgsh hsgnmarfan pgydalltra assqdpaera
      481 rlfdeaetil qeeapiapiy qytnarlikp wlkgypinnp edvaysrqly lvkh
//
LOCUS       WP_392416867             279 aa            linear   BCT 20-JAN-2025
DEFINITION  heme/hemin ABC transporter substrate-binding protein [Aeromonas
            media].
ACCESSION   WP_392416867
VERSION     WP_392416867.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas media
  ORGANISM  Aeromonas media
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Naoe,Y., Nakamura,N., Rahman,M.M., Tosha,T., Nagatoishi,S.,
            Tsumoto,K., Shiro,Y. and Sugimoto,H.
  TITLE     Structural basis for binding and transfer of heme in bacterial
            heme-acquisition systems
  JOURNAL   Proteins 85 (12), 2217-2230 (2017)
   PUBMED   28913898
REFERENCE   2  (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   3  (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   4  (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   5  (residues 1 to 279)
  AUTHORS   Ho,W.W., Li,H., Eakanunkul,S., Tong,Y., Wilks,A., Guo,M. and
            Poulos,T.L.
  TITLE     Holo- and apo-bound structures of bacterial periplasmic
            heme-binding proteins
  JOURNAL   J Biol Chem 282 (49), 35796-35802 (2007)
   PUBMED   17925389
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Aeromonas media"
                     /db_xref="taxon:651"
     Protein         1..279
                     /product="heme/hemin 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=28838
     Region          3..279
                     /region_name="ChuT"
                     /note="ABC-type hemin transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG4558"
                     /db_xref="CDD:443619"
ORIGIN      
        1 mgrrfalals llgcsalslp avaqerivsi gpattelima lggeqsliat dvsspepkgl
       61 prvgyhrala aegilslapt rlvgsdemgp ppaleqlrra gvevtvlpta ptlanlneri
      121 dalagllgdl aagtrlkadi avqsdklaaq akqnkplkva flllhkgqpt siaggnttas
      181 alvtlaggvn pvarlhdykp vsteslielq pdlvlvsgrd wqqyqsvdsv laqvpalaat
      241 pagknraiha idghalqggl slrslqqanq iaqwikqgs
//
LOCUS       WP_392416845             212 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: FKBP-type peptidyl-prolyl cis-trans isomerase
            [Aeromonas].
ACCESSION   WP_392416845
VERSION     WP_392416845.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Quistgaard,E.M., Weininger,U., Ural-Blimke,Y., Modig,K.,
            Nordlund,P., Akke,M. and Low,C.
  TITLE     Molecular insights into substrate recognition and catalytic
            mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD
  JOURNAL   BMC Biol 14 (1), 82 (2016)
   PUBMED   27664121
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Gothel,S.F. and Marahiel,M.A.
  TITLE     Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous
            folding catalysts
  JOURNAL   Cell Mol Life Sci 55 (3), 423-436 (1999)
   PUBMED   10228556
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Trandinh,C.C., Pao,G.M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships among the immunophilins:
            two ubiquitous families of peptidyl-prolyl cis-trans isomerases
  JOURNAL   FASEB J 6 (15), 3410-3420 (1992)
   PUBMED   1464374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437275
            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="FKBP-type peptidyl-prolyl cis-trans isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=22274
     Region          3..138
                     /region_name="SlpA"
                     /note="Peptidyl-prolyl cis-trans isomerase, FKBP type
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1047"
                     /db_xref="CDD:440668"
ORIGIN      
        1 mkvaplsvvt leytvtdehg evidttvgke plvylhgtry lvsgleaele grsvgeafdv
       61 tltpnqayge ydenlvqevp gelfdgmevs egdtfvaetd dghrpvtvie vseefikvdg
      121 nhplagvtlg fkveikdvra ataeelahgh vhgaggcghd hghdhghdhd hdhdhggccg
      181 ghghdhghdh gdeqghggcc ggggcggkgh qh
//
LOCUS       WP_392419074             610 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter large permease [Delftia sp. WSY_7].
ACCESSION   WP_392419074
VERSION     WP_392419074.1
KEYWORDS    RefSeq.
SOURCE      Delftia sp. WSY_7
  ORGANISM  Delftia sp. WSY_7
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Delftia.
REFERENCE   1  (residues 1 to 610)
  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 610)
  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 610)
  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 610)
  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 10008688
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Delftia sp. WSY_7"
                     /db_xref="taxon:3367202"
     Protein         1..610
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma 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=65060
     Region          5..525
                     /region_name="FcbT3"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, large permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4664"
                     /db_xref="CDD:443701"
ORIGIN      
        1 mefvihnlap imfaglilfl lvgfpvafsl gacglffafv gielgvlpea llqalplrif
       61 gimqnetmla ipfftlmgli lersgmaedl letvgqlfgp vrggvafavi fvgallaatt
      121 gvvaasvism glislpimmr ygydrrvasg viaasgtlaq iippslvliv ladqlgrsvg
      181 dmykgaflpg lmlmgfyalf ivvlaifkpa mvpalppear tlrepngnsg lpstlvltvl
      241 cvaasmvvaq ympqlhtwws gdvvekvald etivvsmcfg valafiaamf nkltglhlls
      301 rmaervtfvl ippllliflv lgtiflgvat pteggamgal gaavmafvrg rlsmdllkqa
      361 lmsttklscf vmfiligatm fgltfqgvdg pkwveellvs lpggeigfli vvnimifvla
      421 ffldffelsf ivvpllapva dklgidlvwf gvllavnmqt sfmhppfgfa lfflrsvapa
      481 kayvdkvtkk mtepvttmqi yagaipflli qlvmvaliii fpgivssgld kkveydldkv
      541 rqemeasmpe aidfndpmfn gdganqppap egtpgepsap aggeddalka lqdqlqreqp
      601 atpgesksgs
//
LOCUS       WP_392419361             472 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Capnocytophaga canis].
ACCESSION   WP_392419361
VERSION     WP_392419361.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga canis
  ORGANISM  Capnocytophaga canis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
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
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Linder,P., Lasko,P.F., Ashburner,M., Leroy,P., Nielsen,P.J.,
            Nishi,K., Schnier,J. and Slonimski,P.P.
  TITLE     Birth of the D-E-A-D box
  JOURNAL   Nature 337 (6203), 121-122 (1989)
   PUBMED   2563148
  REMARK    Erratum:[Nature 1989 Jul 20;340(6230):246]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423480
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Capnocytophaga canis"
                     /db_xref="taxon:1848903"
     Protein         1..472
                     /product="ATP-dependent DNA helicase"
                     /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_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0032508 - DNA duplex unwinding [Evidence
                     IEA]"
                     /calculated_mol_wt=54583
     Region          <8..467
                     /region_name="RecD"
                     /note="ATPase/5#-3# helicase helicase subunit RecD of the
                     DNA repair enzyme RecBCD (exonuclease V) [Replication,
                     recombination and repair]; COG0507"
                     /db_xref="CDD:440273"
ORIGIN      
        1 mdkttfynal leafnhsptp lqnialqqls iflldtktnn klfllkgfag tgktsitnsl
       61 iqnlpkikhr avllaptgra akvmshfakq qaytihkhiy ypknqngsfs ynlkpnkfkn
      121 tlfivdeasm iadndgqffe rnsllddlml yvysgegcrl llmgdtaqlp pvnslyspal
      181 dirnlesryq kdvshielte vvrqekksgi lynatklres lnqtfysnfe fqtkgfkdii
      241 rlresseiqe aiedayndyg tehtsiivrs nkravlynkq irkvildned eltagdllmv
      301 vknnyfwlkd ssevsfiang dtleilriya freyygfrfa evsvqlidyp nqppfdtvll
      361 lntleseqas lshqdsqrly eevlldyeee tssykkyqkv kenpyfnalq vkfsyaitch
      421 ksqggqwdvi fiekpylpng adedyyrwly taltrstkkv yllnfkdedf ks
//
LOCUS       WP_392417512             499 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type I restriction-modification system subunit M
            [unclassified Vibrio].
ACCESSION   WP_392417512
VERSION     WP_392417512.1
KEYWORDS    RefSeq.
SOURCE      unclassified Vibrio
  ORGANISM  unclassified Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 499)
  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   2  (residues 1 to 499)
  AUTHORS   Youell,J. and Firman,K.
  TITLE     Mechanistic insight into Type I restriction endonucleases
  JOURNAL   Front Biosci (Landmark Ed) 17 (6), 2122-2139 (2012)
   PUBMED   22652768
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Sistla,S. and Rao,D.N.
  TITLE     S-Adenosyl-L-methionine-dependent restriction enzymes
  JOURNAL   Crit Rev Biochem Mol Biol 39 (1), 1-19 (2004)
   PUBMED   15121719
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Murray,N.E.
  TITLE     Type I restriction systems: sophisticated molecular machines (a
            legacy of Bertani and Weigle)
  JOURNAL   Microbiol Mol Biol Rev 64 (2), 412-434 (2000)
   PUBMED   10839821
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114514
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="unclassified Vibrio"
                     /db_xref="taxon:2614977"
     Protein         1..499
                     /product="type I restriction-modification system subunit
                     M"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=56893
     Region          9..135
                     /region_name="HsdM_N"
                     /note="HsdM N-terminal domain; pfam12161"
                     /db_xref="CDD:463478"
     Region          148..393
                     /region_name="HsdM"
                     /note="Type I restriction-modification system, DNA
                     methylase subunit [Defense mechanisms]; COG0286"
                     /db_xref="CDD:440055"
ORIGIN      
        1 msalnkkkle dllwgaaefl rgqidasdyk qyifpllfyk rlsdvyleey tealeihegd
       61 aeyaampmfh rfdipkearw ekvrhtskni geaiqnalrl ieannprlhg vfgdaqwtnk
      121 erlpdhllsd liehfskipl giksvaqddl geayeylikk faddsghtaa efytnrtvvh
      181 lmtrimglkp getaydptcg tggmllnavm dlrsqgkewr svhlhgqevn lltsaiarmn
      241 mflhdieefd vlrgdtlaep kfiendqlkq fdvifanppy sikkwnrdkf aadpygrnly
      301 gvppqgcady afythiiksl kpdtgraaml wphgvlfrds eqsirkqvie sdiieavigl
      361 gpnlfynspm escvvvlnfn kpaerknkvl fingvehvtr erahsrlsne dlsvlceayf
      421 tpekqsdita lvdiatiken lynlsiplyv qaqnngevhd iehaieawkv srvqlkkqtn
      481 klfkslkelg fevngeevq
//
LOCUS       WP_392419875             338 aa            linear   BCT 20-JAN-2025
DEFINITION  PDDEXK nuclease domain-containing protein [Capnocytophaga canis].
ACCESSION   WP_392419875
VERSION     WP_392419875.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga canis
  ORGANISM  Capnocytophaga canis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 338)
  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 10008845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Capnocytophaga canis"
                     /db_xref="taxon:1848903"
     Protein         1..338
                     /product="PDDEXK nuclease domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39725
     Region          1..329
                     /region_name="YhcG"
                     /note="Predicted nuclease of restriction endonuclease-like
                     (RecB) superfamily, DUF1016 family [General function
                     prediction only]; COG4804"
                     /db_xref="CDD:443832"
ORIGIN      
        1 mkkdtkplnk nllselsvli engqqqivyy anstltlvfw qvgkrinedv lnneratygk
       61 rivpmianel eskygrnfte knirrmmqfa evfpdfqivv tlsrqlswsq flvliplknh
      121 earmfyaelt aneslsvrdl rkqittkafe rmqianlqvq qseiipintf kdpylldflg
      181 lrsdylekdi etailhkles filelgrgfa fverqkrmii dgedfyldll ffhrklkrli
      241 aielkigkfq akhkgqmely lkwlnkyerq egeeapigli lcaenskeqv elleihkdgi
      301 mvaeywtelp skkqlekklh eafieareqf enkgllnk
//
LOCUS       WP_392420668             305 aa            linear   BCT 20-JAN-2025
DEFINITION  aldo/keto reductase [Edwardsiella piscicida].
ACCESSION   WP_392420668
VERSION     WP_392420668.1
KEYWORDS    RefSeq.
SOURCE      Edwardsiella piscicida
  ORGANISM  Edwardsiella piscicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Hafniaceae; Edwardsiella.
REFERENCE   1  (residues 1 to 305)
  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 305)
  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   3  (residues 1 to 305)
  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   4  (residues 1 to 305)
  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 10790928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Edwardsiella piscicida"
                     /db_xref="taxon:1263550"
     Protein         1..305
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /calculated_mol_wt=33689
     Region          1..305
                     /region_name="YdhF"
                     /note="Predicted oxidoreductase YdhF [General function
                     prediction only]; COG4989"
                     /db_xref="CDD:444013"
ORIGIN      
        1 mkqmtlgadg pqvsaialgc mrltelddrq aaslidhala lgisafdhad iygggecerr
       61 faraarlnsa rregvfiqsk cgirrgyydf sfrhimasvd dilqrlqcdy ldmlllhrpd
      121 alvepqevae afdrlqvsgk vrafgvsnha plqmallqkf ltqplrvnqm qfgiahcgmv
      181 rsginvnvqs daavdrdgdt lnycrlhdit lqawspfqfg mfsgvfldhp dfaplnqale
      241 tiaarhgvsk ttlatawilr hpaqmqvvag smnaerlaqi aqacevslsr eewyqiylaa
      301 gnplp
//
LOCUS       WP_392423423             117 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Eikenella halliae].
ACCESSION   WP_392423423
VERSION     WP_392423423.1
KEYWORDS    RefSeq.
SOURCE      Eikenella halliae
  ORGANISM  Eikenella halliae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Eikenella.
REFERENCE   1  (residues 1 to 117)
  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 117)
  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   3  (residues 1 to 117)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11150091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Eikenella halliae"
                     /db_xref="taxon:1795832"
     Protein         1..117
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=13455
     Region          15..109
                     /region_name="DUF559"
                     /note="Protein of unknown function (DUF559); pfam04480"
                     /db_xref="CDD:398268"
     Site            order(18,47,64,71)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:411708"
ORIGIN      
        1 mtqptlakam rqemseaeak lwqhlragrl ngykfrrqqp mgnyivdfmc itpklivead
       61 ggqhteqaay dhartaylns lgftvlrfwn heilqqtndv laeilrvlqe lekqpar
//
LOCUS       WP_392424549             307 aa            linear   BCT 20-JAN-2025
DEFINITION  transglutaminase family protein [Barrientosiimonas humi].
ACCESSION   WP_392424549
VERSION     WP_392424549.1
KEYWORDS    RefSeq.
SOURCE      Barrientosiimonas humi
  ORGANISM  Barrientosiimonas humi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermacoccaceae; Barrientosiimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12090973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Barrientosiimonas humi"
                     /db_xref="taxon:999931"
     Protein         1..307
                     /product="transglutaminase family protein"
                     /calculated_mol_wt=33961
     Region          16..95
                     /region_name="Bact_transglu_N"
                     /note="Bacterial transglutaminase-like N-terminal region;
                     pfam08379"
                     /db_xref="CDD:462455"
     Region          76..257
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 maeqpakedv ysprsylvrh qttytysddv tscyergclq pretvsqtvr ssdievspep
       61 dlvtehrdff gnyshyvevr tphrelivtk tsrvdvawpr pdldrlnett vaqardlvaa
      121 qadpvertty llpsplvdvv pqvrdyaqty lpddaplgda lvaltrgifa dfryakgats
      181 vkttlpelle qregvcqdfa hlaagclrsv glpgryvsgy letfpppgkk klqgsdatha
      241 wtaamvpggg widldptndh lvdsryvvta wgrdfrdvsp lkgviyteae sselkvavdv
      301 lrqdgsg
//
LOCUS       WP_392425100             405 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Dolosigranulum pigrum].
ACCESSION   WP_392425100
VERSION     WP_392425100.1
KEYWORDS    RefSeq.
SOURCE      Dolosigranulum pigrum
  ORGANISM  Dolosigranulum pigrum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Carnobacteriaceae; Dolosigranulum.
REFERENCE   1  (residues 1 to 405)
  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 405)
  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 11417965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Dolosigranulum pigrum"
                     /db_xref="taxon:29394"
     Protein         1..405
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46743
     Region          4..245
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
ORIGIN      
        1 mvsfihvadl hldspfkgli hlsdewfeav qnstfqafeq ivsqaiknav dfvviagdly
       61 dasersiraq tflreqfkrl ntaqinvyii ygnhdfidrq ylyidmpenv hifdetpeti
      121 yyqsaqgetv aisgfsydqq hikdnrlqky pprdmaadyh igllhgncqg ietpssvyap
      181 fsvadvrrln ydylalghih krgsihsslp ayysgniqgr hrkelgdkgc ylvkceqgqc
      241 hpefisaapi iweaitvnms eatslqqtln kitqilheql erqankryli dltchfeeld
      301 aalvamlttd qinqlidssd ywithitcek qtdqhlidsf ierypsawqk aihsvtdddh
      361 ftllqqelqt qvplkywqqd wdhdfkerik qqaiqaieqa lvdne
//
LOCUS       WP_392425471             547 aa            linear   BCT 20-JAN-2025
DEFINITION  complex I subunit 4 family protein [Barrientosiimonas humi].
ACCESSION   WP_392425471
VERSION     WP_392425471.1
KEYWORDS    RefSeq.
SOURCE      Barrientosiimonas humi
  ORGANISM  Barrientosiimonas humi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermacoccaceae; Barrientosiimonas.
REFERENCE   1  (residues 1 to 547)
  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 547)
  AUTHORS   Galemou Yoga,E., Angerer,H., Parey,K. and Zickermann,V.
  TITLE     Respiratory complex I - Mechanistic insights and advances in
            structure determination
  JOURNAL   Biochim Biophys Acta Bioenerg 1861 (3), 148153 (2020)
   PUBMED   31935361
REFERENCE   3  (residues 1 to 547)
  AUTHORS   Friedrich,T. and Scheide,D.
  TITLE     The respiratory complex I of bacteria, archaea and eukarya and its
            module common with membrane-bound multisubunit hydrogenases
  JOURNAL   FEBS Lett 479 (1-2), 1-5 (2000)
   PUBMED   10940377
REFERENCE   4  (residues 1 to 547)
  AUTHORS   Walker,J.E.
  TITLE     The NADH:ubiquinone oxidoreductase (complex I) of respiratory
            chains
  JOURNAL   Q Rev Biophys 25 (3), 253-324 (1992)
   PUBMED   1470679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Barrientosiimonas humi"
                     /db_xref="taxon:999931"
     Protein         1..547
                     /product="complex I subunit 4 family protein"
                     /GO_component="GO:0045271 - respiratory chain complex I
                     [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048039 - ubiquinone binding [Evidence
                     IEA]"
                     /GO_process="GO:0015990 - electron transport coupled
                     proton transport [Evidence IEA]"
                     /GO_process="GO:0042773 - ATP synthesis coupled electron
                     transport [Evidence IEA]"
                     /calculated_mol_wt=55970
     Region          58..406
                     /region_name="NuoM"
                     /note="NADH:ubiquinone oxidoreductase subunit 4 (chain M)
                     [Energy production and conversion]; COG1008"
                     /db_xref="CDD:440632"
ORIGIN      
        1 mviamvaavl vplvvggalv csdrmprpvg qrtasavala aavasaacvg vtlvdrpvld
       61 rpwvtavgmr lslavdgisa pllaltaaig vlvvlygiar pprarygtyl gclllvvgaa
      121 lltflardav lfflafeivl vpmwllikgf gdpatrdaaa arfvlytvlg stlmlvgila
      181 ltfaagtadl telartrgsa lgttqqtiva alllvglgik vplfpfhswl paahtaaptt
      241 gsvllaavll kmgtygvvrl avgavpegfa rlapvvgvla vvgilwgglv clverslkrl
      301 iawssvahmg fvmlalaagg tlgvqaallg niahgvvsal lffvvgglkd rwhgddldta
      361 reglrdarpr lglalvvgma gslalpglat fwgevltila awdpapgrpe tlfawlavla
      421 alggvlaaay alrvlrivwa gggapgraad erlrtdetrv dvarvdvara gatradetrd
      481 esladgetpa gdpptgavav aspdavgaew vvitvlvvav lavgvlptal laisepdvlr
      541 mlgevar
//
LOCUS       WP_392425932             321 aa            linear   BCT 20-JAN-2025
DEFINITION  quinone oxidoreductase family protein [Barrientosiimonas humi].
ACCESSION   WP_392425932
VERSION     WP_392425932.1
KEYWORDS    RefSeq.
SOURCE      Barrientosiimonas humi
  ORGANISM  Barrientosiimonas humi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermacoccaceae; Barrientosiimonas.
REFERENCE   1  (residues 1 to 321)
  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 321)
  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 321)
  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   4  (residues 1 to 321)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Barrientosiimonas humi"
                     /db_xref="taxon:999931"
     Protein         1..321
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=33864
     Region          1..320
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 mravyadrps pdapldalvv gerpdpepgp gqvavdvraa slnmhdvwtl rgvgikaeqf
       61 pmilgmdaag tledgsevvv ypvvndpdwg gdrtldprrs mltedlqgsf aervivpkan
      121 vlpkptslsf aeaaclgtaw ltayrmlttr sglhagqtml vqgasggvst alitlgvaag
      181 lrvwvtgstq ekrdlasklg ahatfepgar lpervdgvfd svgkatwshs ikslkpggvl
      241 vtcgattgep dsaeltriff lqlrvigstm gtrqeladll tlcetadlhp qvglelpmeq
      301 apeafaamie grtagkivlt r
//
LOCUS       WP_392425978             314 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Barrientosiimonas humi].
ACCESSION   WP_392425978
VERSION     WP_392425978.1
KEYWORDS    RefSeq.
SOURCE      Barrientosiimonas humi
  ORGANISM  Barrientosiimonas humi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermacoccaceae; Barrientosiimonas.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Barrientosiimonas humi"
                     /db_xref="taxon:999931"
     Protein         1..314
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33605
     Region          1..302
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mtarrlmlld saslyfrafy gvpdrraspd qppnnavrgf tdmiatlvta yaptdlvacw
       61 dndwrpafrv eaipsykthr lvdgsdvqee speeltpqvp vivdllaavg itrlgvdgye
      121 addvigtlah rahgvstvdv vtgdrdlfql addeqsvrvl ytarggvrep dlvdesflqa
      181 kygitggray aemavlrgdt sdglpgvagi gektaatlin rygdlagirr aladgdpqlk
      241 gaqrtrleaa sdyldvapkv vdvaldvpvp dgldtalptr vadpdrlael aqtydartpv
      301 grllaaldlp plpa
//
LOCUS       WP_392426633             252 aa            linear   BCT 20-JAN-2025
DEFINITION  response regulator transcription factor [Brevibacillus porteri].
ACCESSION   WP_392426633
VERSION     WP_392426633.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus porteri
  ORGANISM  Brevibacillus porteri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 252)
  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 252)
  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   3  (residues 1 to 252)
  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   4  (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
REFERENCE   5  (residues 1 to 252)
  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   6  (residues 1 to 252)
  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   7  (residues 1 to 252)
  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 14435958
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Brevibacillus porteri"
                     /db_xref="taxon:2126350"
     Protein         1..252
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=28973
     Region          4..124
                     /region_name="REC_YesN-like"
                     /note="phosphoacceptor receiver (REC) domain of YesN and
                     related helix-turn-helix containing response regulators;
                     cd17536"
                     /db_xref="CDD:381091"
     Site            order(9..12,15..17,20,106..107)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381091"
     Region          161..244
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mykvllvede rmireglkml ietgtsgfav maeaengkda lhylrtempd livtdirmre
       61 vdgltligki remyeelpiv iisgygdfhy aqkalkykvs dyllkpidrl elvstltkir
      121 qvldrkkkvr eeensvdgsh reerqiirkv kacihdhldg dlrlqtlaes vhlnpiylsq
      181 lfktetgenv sdyitqvrmn rakqllhets lkvydiarlv gyqsakhfml vfkkevgmtp
      241 gsyrdlvgsk dl
//
LOCUS       WP_392426706             244 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Salmonella
            enterica].
ACCESSION   WP_392426706
VERSION     WP_392426706.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 244)
  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 244)
  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 10007860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..244
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28114
     Region          11..107
                     /region_name="CadC1"
                     /note="DNA-binding winged helix-turn-helix (wHTH) domain
                     [Transcription]; COG3710"
                     /db_xref="CDD:442924"
ORIGIN      
        1 mnesiflldk rvvfdstkmt lshgneiiri seaethllla fwhglykked iihfvwenrg
       61 gcvsessyyk linqmrndfs siglqpsdiv trprvgvsls vaiepikkit slkvsdenvk
      121 gtptrenify kikrhsvfvv ltgaiilalf ygvftiykap vrnspdsfft ylgeyndyai
      181 yktkedkvtl sevvfafnsl kikvyrqngr hlyyirepnm niflqclnpv emavpkcitv
      241 kery
//
LOCUS       WP_392427563             496 aa            linear   BCT 20-JAN-2025
DEFINITION  sodium:solute symporter family protein [Brevibacillus porteri].
ACCESSION   WP_392427563
VERSION     WP_392427563.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus porteri
  ORGANISM  Brevibacillus porteri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Henriquez,T., Wirtz,L., Su,D. and Jung,H.
  TITLE     Prokaryotic Solute/Sodium Symporters: Versatile Functions and
            Mechanisms of a Transporter Family
  JOURNAL   Int J Mol Sci 22 (4), 1880 (2021)
   PUBMED   33668649
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Wright,E.M. and Turk,E.
  TITLE     The sodium/glucose cotransport family SLC5
  JOURNAL   Pflugers Arch 447 (5), 510-518 (2004)
   PUBMED   12748858
  REMARK    Erratum:[Pflugers Arch. 2004 Feb;447(5):813-5]
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Jung,H.
  TITLE     The sodium/substrate symporter family: structural and functional
            features
  JOURNAL   FEBS Lett 529 (1), 73-77 (2002)
   PUBMED   12354616
REFERENCE   4  (residues 1 to 496)
  AUTHORS   Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     A functional superfamily of sodium/solute symporters
  JOURNAL   Biochim Biophys Acta 1197 (2), 133-166 (1994)
   PUBMED   8031825
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001756
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Brevibacillus porteri"
                     /db_xref="taxon:2126350"
     Protein         1..496
                     /product="sodium:solute symporter family protein"
                     /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=54131
     Region          1..453
                     /region_name="PutP"
                     /note="Na+/proline symporter [Amino acid transport and
                     metabolism]; COG0591"
                     /db_xref="CDD:440356"
ORIGIN      
        1 mnialiiifa flllsfysgi raqrgkdmnm eqwavggrgf gsififllva geiyttftfl
       61 ggsgwayskg apsyyvlsyi slayvisywl lppiwryake hklvsqsdff vskykspilg
      121 ilvaavgvia iipylvlqfk glgiivseas ygsispvaai wigviavtiy vmisgihgsa
      181 wtaaikdimi ffvvvflgiy lpfhyygdiq pmfeavqasn pdfltfpeeg lsiswyistv
      241 lvtvfgfymw phtfgsvfsa knanvfrknt imlplytlml lfvffvgfta ilqvpglkga
      301 dgdlsllrls lqtfdpwvvg iigaagllta lvpgsmllmt gatllaknvy kvmaphtsda
      361 qiariakwlv pvislislyf amsggdtlvt lllmgyslvt qlfpallfsl pakpwvnkfg
      421 afagilcgvs tvayvtifqv tiatmfpnwp avvkdlnigv vallvnlvvm ftvtfltknl
      481 falnrhaant egtptl
//
LOCUS       WP_392427799             375 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Brevibacillus porteri].
ACCESSION   WP_392427799
VERSION     WP_392427799.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus porteri
  ORGANISM  Brevibacillus porteri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 375)
  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 375)
  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 11417965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Brevibacillus porteri"
                     /db_xref="taxon:2126350"
     Protein         1..375
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42849
     Region          4..250
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
ORIGIN      
        1 mlsfihtadv hldaplqmlg eryelrqddf rqtmkricdl vrekeadfwl iagdlleyhg
       61 grrstamflr dlfasiapip vviapgnhdp wradsfyqtl ewsgnvywft pewgvyefpe
      121 kscviygwgf gqphvyespl etfpgklegy ahhlmvlhas vlsnsgdeeh hpyapvtlqq
      181 lvqtgmdyia mghihkpeqf mhpvkkqpfa aypgspeglt skeagernvl ygeldhdgrl
      241 qltaipvqsr kirkleikgn gvettdqlid rmeeqlaeek dsdimyitlt geraahfqpp
      301 msvlqqrfsr ffvlqltdrt wpdvdedkli aeggvwgrwl sklaeaesra qnedereivr
      361 lakqealari ggtir
//
LOCUS       WP_392428190             408 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Brevibacillus
            porteri].
ACCESSION   WP_392428190
VERSION     WP_392428190.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus porteri
  ORGANISM  Brevibacillus porteri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
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   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   4  (residues 1 to 408)
  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 408)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Brevibacillus porteri"
                     /db_xref="taxon:2126350"
     Protein         1..408
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=45129
     Region          1..388
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 mpkmkvhqlt kvfgkqpela lkllaegrtk eqiykqtgqs igvnqvsfev eegeifvimg
       61 lsgsgkstli rlcnrlidpt sgsieidgee ivnmkasalr evrrkklgmv fqnfalfpqr
      121 tvrenvefgl eiqqvppglr qekarealal vgliewenay pdqlsggmrq rvglaralan
      181 npdillmdea fsaldplirk dmqeellelq mtmkktilfi thdlhealrl gdriafmkdg
      241 qiiqigrpee imadpadefv rkfvedadls rvlvaenvmk raeaitpdkg arvalqlmmd
      301 ngvsslyvvd kkrtllglit aydvslaigt gdsletimkt dlptvspdar lhslfpmmad
      361 lhvpiavvge qqrllgvivk gavlgglvgk vnvqehqrae vmsdgrra
//
LOCUS       WP_392428359             368 aa            linear   BCT 20-JAN-2025
DEFINITION  GerAB/ArcD/ProY family transporter [Brevibacillus porteri].
ACCESSION   WP_392428359
VERSION     WP_392428359.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus porteri
  ORGANISM  Brevibacillus porteri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Brevibacillus porteri"
                     /db_xref="taxon:2126350"
     Protein         1..368
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=41167
     Region          8..368
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 msaqtlaekm isknhmgini asvtigvgil tfprslakat gafdgwisvv isglcaclig
       61 wllaklaarf prktffeyss iiaskpiayi ltflvciytm lfvsfeirai gniakqylfy
      121 ntpvemitls fllivqysvv gsriamlrln llflpvvlvv mfivllfttq lfevenirpy
      181 fssdwrslla gskdvglsys gfeiilfytm lmknpqegar avtlglsipi llymtiymfv
      241 igvfsadvat nltyptiela keveipggff ervesiffti wimtifntca mwlditvlnl
      301 ssmffnvhkt vwvlilspvi yfvamlpqnl vdfftfadsv tyfgiavvyl cpilllviav
      361 lrgvksne
//
LOCUS       WP_392428645             289 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Brevibacillus porteri].
ACCESSION   WP_392428645
VERSION     WP_392428645.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus porteri
  ORGANISM  Brevibacillus porteri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 289)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 289)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Brevibacillus porteri"
                     /db_xref="taxon:2126350"
     Protein         1..289
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33119
     Region          23..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          133..288
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mdtykriqda idyveehlqe emniteiasq ahfsafhfqr lfqaisgfsv qeyirkrrls
       61 eaalalkqts dnvleiavay qyqsqealtr afekqfgitp gryrkdnhsl pylakmdfla
      121 frqtikgeit mnkptiatld eiciigrrfq tslqdeqhfk dipgfyyefg rnqdylripn
      181 kaaedmsygi acefeddgsf sfvigeavhr apdelpegfi slvlpggkya efkvtgdadl
      241 vqntrryiyg twlpqsnyer gegpdfevtd vrgssfpeam kisiyipll
//
LOCUS       WP_392431431             326 aa            linear   BCT 20-JAN-2025
DEFINITION  quinone oxidoreductase family protein [Brevibacillus porteri].
ACCESSION   WP_392431431
VERSION     WP_392431431.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus porteri
  ORGANISM  Brevibacillus porteri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 326)
  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 326)
  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 326)
  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   4  (residues 1 to 326)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Brevibacillus porteri"
                     /db_xref="taxon:2126350"
     Protein         1..326
                     /product="quinone oxidoreductase family protein"
                     /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]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=34470
     Region          1..325
                     /region_name="Qor"
                     /note="NADPH:quinone reductase or related Zn-dependent
                     oxidoreductase [Energy production and conversion, General
                     function prediction only]; COG0604"
                     /db_xref="CDD:440369"
ORIGIN      
        1 mkailvtelg gpemmkytev emptmsptqv lirvemtsvn fadiksrygk kgaaklpfip
       61 gldatgvieq vgaevqslkv gqrviafpan gsyaeyivag esltfalpdq istetaaacp
      121 vvsftsyqll akvariakge tvlihaaagg igttaiqlak llgagrvigt vgneakaela
      181 lsagadhvic ndredfvekv reltdgagad vildsisgtv sersleclaw ygrlvhfgna
      241 sgeigqikti dlhascrsvl gfsfgttrkl rphllqdtak qvleylangq ldikigkhfa
      301 leeaasahaw iesrastgkv lldvrs
//
LOCUS       WP_392431796             305 aa            linear   BCT 20-JAN-2025
DEFINITION  aldo/keto reductase [Brevibacillus porteri].
ACCESSION   WP_392431796
VERSION     WP_392431796.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus porteri
  ORGANISM  Brevibacillus porteri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 305)
  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 305)
  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   3  (residues 1 to 305)
  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   4  (residues 1 to 305)
  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 10790928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Brevibacillus porteri"
                     /db_xref="taxon:2126350"
     Protein         1..305
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /calculated_mol_wt=34498
     Region          1..305
                     /region_name="YdhF"
                     /note="Predicted oxidoreductase YdhF [General function
                     prediction only]; COG4989"
                     /db_xref="CDD:444013"
ORIGIN      
        1 mrtiplgtsk levpviaigc mrigsldklq aerfvqtale eganffdhad iygkgrceev
       61 faeaiqmsps vrerillqsk cgirpgmfdf skeyilnavd gilkrlktey ldvlllhrpd
      121 tlvepeevae afdllestgk vrhfgvsnqn pmqiqllnky vkqpivanql qlsimnatmi
      181 sqgfnvnmen nsavnrdgsv ldfcrlhdit iqpwspfqyg ffegsflgne kfpelnkkid
      241 eiaaryevsn ttiaiawllr hpanmqpvig ttnidrmkec vkathirltr eewydiyrsa
      301 gnvlp
//
LOCUS       WP_392432481             173 aa            linear   BCT 20-JAN-2025
DEFINITION  ubiquinone anaerobic biosynthesis accessory factor UbiT [Yersinia
            fenwicki].
ACCESSION   WP_392432481
VERSION     WP_392432481.1
KEYWORDS    RefSeq.
SOURCE      Yersinia fenwicki
  ORGANISM  Yersinia fenwicki
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Arias-Cartin,R., Kazemzadeh Ferizhendi,K., Sechet,E., Pelosi,L.,
            Loeuillet,C., Pierrel,F., Barras,F. and Bouveret,E.
  TITLE     Role of the Escherichia coli ubiquinone-synthesizing UbiUVT pathway
            in adaptation to changing respiratory conditions
  JOURNAL   mBio 14 (4), e0329822 (2023)
   PUBMED   37283518
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Vo,C.D., Michaud,J., Elsen,S., Faivre,B., Bouveret,E., Barras,F.,
            Fontecave,M., Pierrel,F., Lombard,M. and Pelosi,L.
  TITLE     The O2-independent pathway of ubiquinone biosynthesis is essential
            for denitrification in Pseudomonas aeruginosa
  JOURNAL   J Biol Chem 295 (27), 9021-9032 (2020)
   PUBMED   32409583
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Pelosi,L., Vo,C.D., Abby,S.S., Loiseau,L., Rascalou,B., Hajj
            Chehade,M., Faivre,B., Gousse,M., Chenal,C., Touati,N., Binet,L.,
            Cornu,D., Fyfe,C.D., Fontecave,M., Barras,F., Lombard,M. and
            Pierrel,F.
  TITLE     Ubiquinone Biosynthesis over the Entire O2 Range: Characterization
            of a Conserved O2-Independent Pathway
  JOURNAL   mBio 10 (4), e01319-19 (2019)
   PUBMED   31289180
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF047962.3
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Yersinia fenwicki"
                     /db_xref="taxon:3344550"
     gene            1..173
                     /gene="ubiT"
     Protein         1..173
                     /product="ubiquinone anaerobic biosynthesis accessory
                     factor UbiT"
                     /GO_component="GO:0110142 - ubiquinone biosynthesis
                     complex [Evidence IEA]"
                     /GO_process="GO:0006744 - ubiquinone biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=19517
     Region          7..166
                     /region_name="UbiT"
                     /note="Ubiquinone biosynthesis accessory factor UbiT,
                     lipid carrier SCP2 domain [Coenzyme transport and
                     metabolism]; COG3154"
                     /db_xref="CDD:442388"
ORIGIN      
        1 mlgelrarlv rqgpallrrp lkftpfalqr qvleqvlgwq frqalldgdl eflesrwlki
       61 evrdlalqwf mtvengrlvv sqqaeadvsf sgdandlili aarkedpdtl ffqrrlrieg
      121 dtelglyvkn lmdaielesm ptllrvglqq laefieagqq egaastsrtl asc
//
LOCUS       WP_392433220             273 aa            linear   BCT 20-JAN-2025
DEFINITION  transglutaminase family protein [Yersinia fenwicki].
ACCESSION   WP_392433220
VERSION     WP_392433220.1
KEYWORDS    RefSeq.
SOURCE      Yersinia fenwicki
  ORGANISM  Yersinia fenwicki
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12090973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Yersinia fenwicki"
                     /db_xref="taxon:3344550"
     Protein         1..273
                     /product="transglutaminase family protein"
                     /calculated_mol_wt=30077
     Region          3..79
                     /region_name="Bact_transglu_N"
                     /note="Bacterial transglutaminase-like N-terminal region;
                     pfam08379"
                     /db_xref="CDD:462455"
     Region          <106..219
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mrlnvdhsth ytyvqqvqhs tqylrltpqd sahqrilswq ltlpeeaict tdafgnvlhv
       61 ltldkphqai tiqaqgvvei ednveddsgd hlsplvflrh spltqpdaai rqfaagyceg
      121 vssaagqldc lthlmgella kmpyspgttt vqdsaaqafa aeqgvcqdht hvflaccrsl
      181 niparyvsgy lytessshva thawaevwln gywqsfdvtn ntckpnqhlk lavgidylda
      241 cpvrgirrgg gyedmqtiaa vhmlsnprld msq
//
LOCUS       WP_392434909              81 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Yersinia fenwicki].
ACCESSION   WP_392434909
VERSION     WP_392434909.1
KEYWORDS    RefSeq.
SOURCE      Yersinia fenwicki
  ORGANISM  Yersinia fenwicki
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 81)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 81)
  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 81)
  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 81)
  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 10007349
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Yersinia fenwicki"
                     /db_xref="taxon:3344550"
     Protein         1..81
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9045
     Region          3..69
                     /region_name="SfsB"
                     /note="Predicted transcriptional regulator, lambda
                     repressor-like DNA-binding domain [Transcription];
                     COG3423"
                     /db_xref="CDD:442649"
ORIGIN      
        1 mqtnrqdwhr adiraaleks gtnlrtlsva aglskdtlrn alvrpwpkge rliahaigvn
       61 petiwpsrym klkevadiqt i
//
LOCUS       WP_392435286             538 aa            linear   BCT 20-JAN-2025
DEFINITION  peptide ABC transporter substrate-binding protein [Yersinia
            fenwicki].
ACCESSION   WP_392435286
VERSION     WP_392435286.1
KEYWORDS    RefSeq.
SOURCE      Yersinia fenwicki
  ORGANISM  Yersinia fenwicki
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 538)
  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 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   3  (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   4  (residues 1 to 538)
  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 538)
  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 11467924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Yersinia fenwicki"
                     /db_xref="taxon:3344550"
     Protein         1..538
                     /product="peptide 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=59953
     Region          1..537
                     /region_name="OppA"
                     /note="ABC-type oligopeptide transport system, periplasmic
                     component [Amino acid transport and metabolism]; COG4166"
                     /db_xref="CDD:443327"
ORIGIN      
        1 mryfryalca alvgaalgta naavipagtv laekqelvrh ikdepasldp mkavglieaq
       61 vardlfeglv nqdshgqiip gvatnwntsd nqtyiftlrk dakwsngdpv taqdfvyswr
      121 rlvdpkslsp fawfaelagm enaqqiiagk mppetlgvsa vndytlkvkl skpvpyfpsl
      181 tanfslfpvp stivkkygsd wtkvgnlvgn gafklqdrvv neklvlvpnd yywdhahtvl
      241 tkvtfipinq eanatkryqa gdiditesfp knlyqkllkd ipdqvytpdq lgtyyyafnt
      301 qraptndvrv rkalsyaidr kiiaekvlgt gekpayhftp dvtagyhpvt nllqqqdqde
      361 lnaqakallh aagygpdkpl klsllyntsd nnqklaiaia smwkktlgvd vkminqewkt
      421 yidsrntgnf dvvraswvgd ynepstflsl ltsthsgnia kftsvdydrl lneagkqtnp
      481 kalsddynka eqiiaeqvpi apiyqftngr likpwvkgyp itnpedvays qmiyiikh
//
LOCUS       WP_392436076             341 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Finegoldia magna].
ACCESSION   WP_392436076
VERSION     WP_392436076.1
KEYWORDS    RefSeq.
SOURCE      Finegoldia magna
  ORGANISM  Finegoldia magna
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Finegoldia.
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
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Igarashi,K., Ito,K. and Kashiwagi,K.
  TITLE     Polyamine uptake systems in Escherichia coli
  JOURNAL   Res Microbiol 152 (3-4), 271-278 (2001)
   PUBMED   11421274
REFERENCE   5  (residues 1 to 341)
  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   6  (residues 1 to 341)
  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 11430824
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Finegoldia magna"
                     /db_xref="taxon:1260"
     Protein         1..341
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0019808 - polyamine binding [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:0015846 - polyamine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=39568
     Region          18..339
                     /region_name="PotD"
                     /note="Spermidine/putrescine-binding periplasmic protein
                     [Amino acid transport and metabolism]; COG0687"
                     /db_xref="CDD:440451"
ORIGIN      
        1 mkkillfllt illltscskd dsnvlyvynw geyiepalie kfeketgikv iydtfeqned
       61 mymkvkeggn nydvvvpsdy maekmikqgm lekidyskip nfkyidekfr nldydpkney
      121 tvpymwgtvg ilynknkvke kvdswnilwd ekykdniimm nstrdtlgva lkrlgysmns
      181 rneaelekak kslikqkdiv laylvdetkn qmvneeadia vmysgdaiva ksenenleyv
      241 ipkegsnlwf dtlailknak hkenaekfin fltdpenaki naeyigyslp steakklldk
      301 evqedatayp dlskhknmei fkdpsdfvek yddiwadika n
//
LOCUS       WP_392436724             387 aa            linear   BCT 20-JAN-2025
DEFINITION  THUMP domain-containing class I SAM-dependent RNA methyltransferase
            [Cruoricaptor ignavus].
ACCESSION   WP_392436724
VERSION     WP_392436724.1
KEYWORDS    RefSeq.
SOURCE      Cruoricaptor ignavus
  ORGANISM  Cruoricaptor ignavus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Cruoricaptor.
REFERENCE   1  (residues 1 to 387)
  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 387)
  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 387)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     THUMP--a predicted RNA-binding domain shared by 4-thiouridine,
            pseudouridine synthases and RNA methylases
  JOURNAL   Trends Biochem Sci 26 (4), 215-217 (2001)
   PUBMED   11295541
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Cruoricaptor ignavus"
                     /db_xref="taxon:1118202"
     Protein         1..387
                     /product="THUMP domain-containing 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:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=44857
     Region          6..372
                     /region_name="RlmL"
                     /note="23S rRNA G2445 N2-methylase RlmL [Translation,
                     ribosomal structure and biogenesis]; COG0116"
                     /db_xref="CDD:439886"
ORIGIN      
        1 mdtenleiqi ktffgmeevl aaeiqklggr nvaaknravs ctgdlgflyk inysartavk
       61 ilvpifsfka fneqkfydkl srfdwsefmd vsqtfaidat vnsdrfthsr fmtlkmkdav
      121 vdffqekfhr rpdidtrnpd ikfhlhidrd wvtisldssg eplykrgyrk aqgkaplnev
      181 laagmlqiag wdgkgnfldp mcgsgtlpie aammamelpa qifresfgfq nwknyddelf
      241 tkiknfrlnr iqefsgkiia ydadneaien arkniaaael edvieieqrn ffdtkkkhfp
      301 llmvfnppyd ermkiqdydf ykkigdtfkn qypntlawii tsdleaakki glrpsrkikl
      361 fngkletrfl qyemyegskk qkftdnq
//
LOCUS       WP_392437831             335 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Cruoricaptor ignavus].
ACCESSION   WP_392437831
VERSION     WP_392437831.1
KEYWORDS    RefSeq.
SOURCE      Cruoricaptor ignavus
  ORGANISM  Cruoricaptor ignavus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Cruoricaptor.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415139
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Cruoricaptor ignavus"
                     /db_xref="taxon:1118202"
     Protein         1..335
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=38811
     Region          1..268
                     /region_name="LysX"
                     /note="Glutathione synthase, LysX or RimK-type ligase,
                     ATP-grasp superfamily [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism,
                     Translation, ribosomal structure and biogenesis, Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0189"
                     /db_xref="CDD:439959"
ORIGIN      
        1 mkkigilfgm edtfpwafid kvnelgngef vaepvmihrv eqgaatdyav iidrisqdvp
       61 fyraylknaa mngtyiinnp fwwsadekff nnalmtkigi plpktvilpt yerpantket
      121 sfrnmyfphd wdyifdyvgf pafmkphdgg gwrdvykvhn aeelfdahsk shtlvmmlqe
      181 nidfedyyrv yclgrkyvhi mpyeprnphh lryatthkte gearekllkt iedytlkink
      241 algydfntve favrdgipya idfcnpapda drnsvgeenf qwivehaakl aiekarefep
      301 gkikidwgef vrnsmkttet tdetkakpkp gtqkk
//
LOCUS       WP_392437833             403 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Cruoricaptor ignavus].
ACCESSION   WP_392437833
VERSION     WP_392437833.1
KEYWORDS    RefSeq.
SOURCE      Cruoricaptor ignavus
  ORGANISM  Cruoricaptor ignavus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Cruoricaptor.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Cruoricaptor ignavus"
                     /db_xref="taxon:1118202"
     Protein         1..403
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=45750
     Region          62..312
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 metktivcla csfkgsdfit efakngdril litsahlrek pwpwhaiadv fymeetepwk
       61 wnlqhlvegf ahllrrekvd aiialddydv ekaaklrevf risgmgqsth rnfrdklamr
      121 mkaldegipv peftavfndd avndfaekip apwvlkprse asamgirkih sreelwqein
      181 elgnqrhlfl leafkpgdvf htdslvyknr vaflcasqyg qppmqvshng gifqtrtldk
      241 ktdeykalek lnakvlkafg lkhgaahtef irnnengewy fletssrvgg ahiadmveaa
      301 tevniwaewa riehavlhge ryklkkpkpk pagltvalss qqkqdysrfs qdnilktiel
      361 dyhfvivhqa endedlaksm ddaaakisqs tlsvmpaktg grt
//
LOCUS       WP_392437990             319 aa            linear   BCT 20-JAN-2025
DEFINITION  KpsF/GutQ family sugar-phosphate isomerase [Cruoricaptor ignavus].
ACCESSION   WP_392437990
VERSION     WP_392437990.1
KEYWORDS    RefSeq.
SOURCE      Cruoricaptor ignavus
  ORGANISM  Cruoricaptor ignavus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Cruoricaptor.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Meredith,T.C. and Woodard,R.W.
  TITLE     Characterization of Escherichia coli D-arabinose 5-phosphate
            isomerase encoded by kpsF: implications for group 2 capsule
            biosynthesis
  JOURNAL   Biochem J 395 (2), 427-432 (2006)
   PUBMED   16390329
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Meredith,T.C. and Woodard,R.W.
  TITLE     Identification of GutQ from Escherichia coli as a D-arabinose
            5-phosphate isomerase
  JOURNAL   J Bacteriol 187 (20), 6936-6942 (2005)
   PUBMED   16199563
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002722
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Cruoricaptor ignavus"
                     /db_xref="taxon:1118202"
     Protein         1..319
                     /product="KpsF/GutQ family sugar-phosphate isomerase"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33964
     Region          5..313
                     /region_name="GutQ"
                     /note="D-arabinose 5-phosphate isomerase GutQ
                     [Carbohydrate transport and metabolism, Cell
                     wall/membrane/envelope biogenesis]; COG0794"
                     /db_xref="CDD:440557"
ORIGIN      
        1 mkeyeildea kkaiqteise leklvkrldg sfaraallia gnagklvvvg igksahvaak
       61 ivatlnstgt psqflhaaea ihgdlgiiqp qdvvlcisns gnspeivnil pylkayssal
      121 igmtgnlqsk laeasdiild tfvekeacpn slaptssttv qmalgdalaa vlmkmknfgn
      181 edfakfhpgg slgknltakv sqflsgnkpq veesapvrdv iiaisssrhg itavtyegki
      241 tgvitdgdlr rmllnnreit nitasdimsr kpktiesgel aktalrilke ynigqllvte
      301 ngeykgiidl hrlldegin
//
LOCUS       WP_392438089             277 aa            linear   BCT 20-JAN-2025
DEFINITION  THUMP domain-containing class I SAM-dependent RNA
            methyltransferase, partial [Staphylococcus sp.
            231237_7MaSpsaltlick].
ACCESSION   WP_392438089
VERSION     WP_392438089.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus sp. 231237_7MaSpsaltlick
  ORGANISM  Staphylococcus sp. 231237_7MaSpsaltlick
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
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]
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     THUMP--a predicted RNA-binding domain shared by 4-thiouridine,
            pseudouridine synthases and RNA methylases
  JOURNAL   Trends Biochem Sci 26 (4), 215-217 (2001)
   PUBMED   11295541
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Staphylococcus sp. 231237_7MaSpsaltlick"
                     /db_xref="taxon:3367518"
     Protein         <1..277
                     /product="THUMP domain-containing 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:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
     Region          <1..273
                     /region_name="RlmL"
                     /note="23S rRNA G2445 N2-methylase RlmL [Translation,
                     ribosomal structure and biogenesis]; COG0116"
                     /db_xref="CDD:439886"
ORIGIN      
        1 vkstlysvpd cqaivkkaiv erlkrayeer gwlnetgaky pvevailkde alltidtsgs
       61 glnkrgyrla qgeapiketl aaslirlanw tgdtplidpf cgsgtiaiea sliaqniapg
      121 fnrdfvsetw dimpdnlyne mrdeadqqan ydreieiyas didpemieia krnaeevgla
      181 diinfsvkdv ntltidtnep valignppyg erigdrdeve kmyryigkll hqharlsayv
      241 ltsnsefehl tnrkatkrrk lfngyiecty yqywgqr
//
LOCUS       WP_392440289             514 aa            linear   BCT 20-JAN-2025
DEFINITION  HAL/PAL/TAL family ammonia-lyase [Vibrio sp. CJQ_6].
ACCESSION   WP_392440289
VERSION     WP_392440289.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. CJQ_6
  ORGANISM  Vibrio sp. CJQ_6
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Turner,N.J.
  TITLE     Ammonia lyases and aminomutases as biocatalysts for the synthesis
            of alpha-amino and beta-amino acids
  JOURNAL   Curr Opin Chem Biol 15 (2), 234-240 (2011)
   PUBMED   21131229
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Louie,G.V., Bowman,M.E., Moffitt,M.C., Baiga,T.J., Moore,B.S. and
            Noel,J.P.
  TITLE     Structural determinants and modulation of substrate specificity in
            phenylalanine-tyrosine ammonia-lyases
  JOURNAL   Chem Biol 13 (12), 1327-1338 (2006)
   PUBMED   17185228
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Baedeker,M. and Schulz,G.E.
  TITLE     Autocatalytic peptide cyclization during chain folding of histidine
            ammonia-lyase
  JOURNAL   Structure 10 (1), 61-67 (2002)
   PUBMED   11796111
REFERENCE   4  (residues 1 to 514)
  AUTHORS   Schwede,T.F., Retey,J. and Schulz,G.E.
  TITLE     Crystal structure of histidine ammonia-lyase revealing a novel
            polypeptide modification as the catalytic electrophile
  JOURNAL   Biochemistry 38 (17), 5355-5361 (1999)
   PUBMED   10220322
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Vibrio sp. CJQ_6"
                     /db_xref="taxon:3367165"
     Protein         1..514
                     /product="HAL/PAL/TAL family ammonia-lyase"
                     /EC_number="4.3.1.-"
                     /GO_function="GO:0016841 - ammonia-lyase activity
                     [Evidence IEA]"
                     /GO_process="GO:0170035 - L-amino acid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56397
     Region          7..514
                     /region_name="HutH"
                     /note="Histidine ammonia-lyase [Amino acid transport and
                     metabolism]; COG2986"
                     /db_xref="CDD:442225"
ORIGIN      
        1 mtmnnnnkir fgaerltied vvaiangaqa amndseayka ridrgvafle rllkeegviy
       61 gvttgygdsc tvaippslvd dlplnltrfh gcglgdilth eqsravlatr lcslaqgvsg
      121 vshdvldqli nlinfdiapr ipqegsvgas gdltplsyva atligerevl ykgqlrdtrd
      181 vfaelgitpi qlkpkeglal mngtsvmtal aclaykraey laqlstkita lvsvgmhgnd
      241 fhfdealfav kphpgqqqia awlrddlqad cpprnsdrlq dryslrcaph vigtvqdalp
      301 wlrqlienel nsandnpiid gdnervlhgg hfygghiama mdtlktgvan ladlldrqma
      361 qlmdykfnng lpfnltgaeg arkpinhgfk avqigisawt aealkhtmpa svfsrstech
      421 nqdkvsmgti aardclrvlq lteqvaaasl laatqaielr krhneldeqh mshslkqmvd
      481 avqsefdfvv edrpleadlr lfieriqaqh wtly
//
LOCUS       WP_392441840             417 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Aeromonas bivalvium].
ACCESSION   WP_392441840
VERSION     WP_392441840.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas bivalvium
  ORGANISM  Aeromonas bivalvium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Aeromonas bivalvium"
                     /db_xref="taxon:440079"
     Protein         1..417
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=45922
     Region          60..308
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mtpcfvivgy nnvriydvak lrqlahgrfd cqlvlvvera slqdwqaadl viqaelgqsp
       61 alarvceala daamtpvgil pfsdrgvplg amlaqhyrlp garpeaalag ldkgrframe
      121 aevpapdhyl pltaraidsl aslvatreaf ggtgfikpva egnsrgcmav hedtdcaavw
      181 eelapyhasg immepliega refswdyvag crwltekhtt qgeyraeyqq ivparltpeq
      241 trwlnqaggf mrrllaeewg ayhnelflre qgasavesnm rpagmhiwdl aalsfeafdp
      301 wqrwlhwart gqthtalprq lgysgirmlr prqsgtlsrq adiprlarsl gitlhqggys
      361 kavgervsar vtdnggfmgq ivlhhadypt llawldalad aieadteiac dqpvvhc
//
LOCUS       WP_392442231             383 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Vibrio sp.
            CJQ_6].
ACCESSION   WP_392442231
VERSION     WP_392442231.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. CJQ_6
  ORGANISM  Vibrio sp. CJQ_6
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 383)
  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 383)
  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 10007860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Vibrio sp. CJQ_6"
                     /db_xref="taxon:3367165"
     Protein         1..383
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44182
     Region          3..100
                     /region_name="CadC1"
                     /note="DNA-binding winged helix-turn-helix (wHTH) domain
                     [Transcription]; COG3710"
                     /db_xref="CDD:442924"
ORIGIN      
        1 mkvkfdttkn iiinnktkik erlsnkekhl lvelfdkskl ghissrsdlk savwphsina
       61 dsslnkyils lrrkfsnlgf ddviytvptv gyyikdvsvl ifienkinhi drinhlsvrn
      121 iiyygisasi tmfllcdyyn nqdsyshkvs ndvvslysin nndvdygkil ylfnnipavk
      181 erklsttilv tdkmlsihvf nisdivinii hndnfelidq wvkkvsdive sdygnlvhtk
      241 nafsdtmsiy gqssvychsk fkslddciyk ynkallykin kdvyhqenhv kiqlsdgqei
      301 asyhsngnvk gneikgnyqs nrynlsynle lpdgfelfkn yshilnmpvs dndlfykkvn
      361 gdiyfstnyn geiiylhgvs nii
//
LOCUS       WP_392442424             299 aa            linear   BCT 20-JAN-2025
DEFINITION  aldo/keto reductase [Aeromonas bivalvium].
ACCESSION   WP_392442424
VERSION     WP_392442424.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas bivalvium
  ORGANISM  Aeromonas bivalvium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 299)
  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 299)
  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   3  (residues 1 to 299)
  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   4  (residues 1 to 299)
  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 10790928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Aeromonas bivalvium"
                     /db_xref="taxon:440079"
     Protein         1..299
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /calculated_mol_wt=33460
     Region          4..299
                     /region_name="YdhF"
                     /note="Predicted oxidoreductase YdhF [General function
                     prediction only]; COG4989"
                     /db_xref="CDD:444013"
ORIGIN      
        1 mtvsrlplhp qgpefsrlim gywrlmewql sptalldlik yhldlgitti dhadiyggyq
       61 ceeafgralr lepalrsrme lvskcgialt akpehalnhy ntgkghiias aeaslqklgt
      121 dhldlllihr pdplmdadev aeafialrqa gkirhagvsn ftarqfellq srlpfplvtn
      181 qleisplnqd ltldgtldqc qqlrikpmaw sclgggslfh darheglrhe larireevga
      241 qtleqvvyaw vmmlpsqplp iigsgkreri asavaseqvq lnrqqwfrir kaalgydvp
//
LOCUS       WP_392443857             508 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: alpha,alpha-trehalose-phosphate synthase
            (UDP-forming) [unclassified Delftia].
ACCESSION   WP_392443857
VERSION     WP_392443857.1
KEYWORDS    RefSeq.
SOURCE      unclassified Delftia
  ORGANISM  unclassified Delftia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Delftia.
REFERENCE   1  (residues 1 to 508)
  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 508)
  AUTHORS   Eastmond,P.J. and Graham,I.A.
  TITLE     Trehalose metabolism: a regulatory role for trehalose-6-phosphate?
  JOURNAL   Curr Opin Plant Biol 6 (3), 231-235 (2003)
   PUBMED   12753972
REFERENCE   3  (residues 1 to 508)
  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   4  (residues 1 to 508)
  AUTHORS   Elbein,A.D., Pan,Y.T., Pastuszak,I. and Carroll,D.
  TITLE     New insights on trehalose: a multifunctional molecule
  JOURNAL   Glycobiology 13 (4), 17R-27R (2003)
   PUBMED   12626396
REFERENCE   5  (residues 1 to 508)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 929-939 (1997)
   PUBMED   9334165
  REMARK    Erratum:[Biochem J 1998 Feb 1;329(Pt 3):719]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="unclassified Delftia"
                     /db_xref="taxon:2613839"
     Protein         1..508
                     /product="alpha,alpha-trehalose-phosphate synthase
                     (UDP-forming)"
                     /EC_number="2.4.1.15"
                     /GO_function="GO:0003825 - alpha,alpha-trehalose-phosphate
                     synthase (UDP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0005992 - trehalose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56394
     Region          1..467
                     /region_name="OtsA"
                     /note="Trehalose-6-phosphate synthase, GT20 family
                     [Carbohydrate transport and metabolism]; COG0380"
                     /db_xref="CDD:440149"
ORIGIN      
        1 msrlvvisnr vadprraaag glavamgdal rqtgglwfgw sgtvtddgaq aapaghvhrt
       61 qagnvtlatv dldradhdsy yagysngvlw pvfhgrldla sfdtghaagy rrvnqllarr
      121 llpllaqddi lwvhdyhlip laaelralgc rqrigfflhi plppptllaa ipehawlmrc
      181 lfaydlvglq trqdvhhfer yvcdeaggqs lgdgalrahg qrlvcrafpi gidvdgfmal
      241 aqggasrdmy ermkheyaqr rlllgidrld yskglpqrlr afrellarhp eqrrratliq
      301 igsptregld ayadirrele slcgavngdy geldwmpvry ihqtlprdgi pglcraaavg
      361 lvtplrdgmn lvakeyvaaq dpadpgvlvl srfagaaeql qeamlvnpyd vhgtaavvqq
      421 alqmplqerr qrhqrllqri aeqdvhwwrk aflsalkear plehrereaf gipvpsirqe
      481 qaplrlelaa cpadgverda crsvvsdr
//
LOCUS       WP_392444994             343 aa            linear   BCT 20-JAN-2025
DEFINITION  PDDEXK nuclease domain-containing protein [Sneathia vaginalis].
ACCESSION   WP_392444994
VERSION     WP_392444994.1
KEYWORDS    RefSeq.
SOURCE      Sneathia vaginalis
  ORGANISM  Sneathia vaginalis
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Leptotrichiaceae; Sneathia.
REFERENCE   1  (residues 1 to 343)
  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 10008845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Sneathia vaginalis"
                     /db_xref="taxon:187101"
     Protein         1..343
                     /product="PDDEXK nuclease domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40165
     Region          1..343
                     /region_name="YhcG"
                     /note="Predicted nuclease of restriction endonuclease-like
                     (RecB) superfamily, DUF1016 family [General function
                     prediction only]; COG4804"
                     /db_xref="CDD:443832"
ORIGIN      
        1 mnnknnidrv hddvfnsikt lmnkarneva revnnilvqt ywevgriive deqghserad
       61 ygrellkdls krltkefgrg fsvsnlqfmr rffqeyeiqq tvsvkltwsh ycellsisde
      121 kkrsfyekes inanwsvrel krqiktslfe rlllsagekn kekvldlalk gneikkasdl
      181 vkdpyvfefl glpeekpmme sdlekalidh iekfllelgk gfmyvgsqqr vtlgnthyyv
      241 dmvfynkilr syvlielkts klmpeavgqi nmylnyykae vndemdnepi giilctdkyg
      301 vqaeyalgnl snkifaskyt lyipnreele eqvekvieky kek
//
LOCUS       WP_392445056             238 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Aeromonas
            bivalvium].
ACCESSION   WP_392445056
VERSION     WP_392445056.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas bivalvium
  ORGANISM  Aeromonas bivalvium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
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   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 238)
  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 10007860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Aeromonas bivalvium"
                     /db_xref="taxon:440079"
     Protein         1..238
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26241
     Region          4..112
                     /region_name="CadC1"
                     /note="DNA-binding winged helix-turn-helix (wHTH) domain
                     [Transcription]; COG3710"
                     /db_xref="CDD:442924"
ORIGIN      
        1 mpntrlqfgs filhgahrrl lkhtpegeit vrlagaevai lqhllshpdt lcaketltel
       61 gwqgrpvsan alpvaianlr kqltteppqi eirniprqgy llalsvplme meepaavpls
      121 pvtqeeppve egplsevsta ldpsqaqtsk qskrlwpslm iglkainlll lgflillgpl
      181 iykewidvrc akdeqgetcv vdnselrqae wparhqgqll lvsgrhwliv drvevasp
//
LOCUS       WP_392445219             279 aa            linear   BCT 20-JAN-2025
DEFINITION  heme/hemin ABC transporter substrate-binding protein [Aeromonas
            bivalvium].
ACCESSION   WP_392445219
VERSION     WP_392445219.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas bivalvium
  ORGANISM  Aeromonas bivalvium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Naoe,Y., Nakamura,N., Rahman,M.M., Tosha,T., Nagatoishi,S.,
            Tsumoto,K., Shiro,Y. and Sugimoto,H.
  TITLE     Structural basis for binding and transfer of heme in bacterial
            heme-acquisition systems
  JOURNAL   Proteins 85 (12), 2217-2230 (2017)
   PUBMED   28913898
REFERENCE   2  (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   3  (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   4  (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   5  (residues 1 to 279)
  AUTHORS   Ho,W.W., Li,H., Eakanunkul,S., Tong,Y., Wilks,A., Guo,M. and
            Poulos,T.L.
  TITLE     Holo- and apo-bound structures of bacterial periplasmic
            heme-binding proteins
  JOURNAL   J Biol Chem 282 (49), 35796-35802 (2007)
   PUBMED   17925389
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Aeromonas bivalvium"
                     /db_xref="taxon:440079"
     Protein         1..279
                     /product="heme/hemin 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=28552
     Region          4..279
                     /region_name="ChuT"
                     /note="ABC-type hemin transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG4558"
                     /db_xref="CDD:443619"
ORIGIN      
        1 mgprlalalt llgcsvmalp agaqerivsi gpattelila lggqssliat dvsspepkgl
       61 prvgyhrala aegilslapt rligsdemgp apvldqlrra gvevkvleta ptlanlnari
      121 etlarllgdp aagtrlqaei qaqsdalaaq asgnqplkva flllhkgqpt siaggnttas
      181 alltlaggvn pvaqlrdykp vsaeslielq pdlvlvsgrd wqlyqdpasv laqvpalaat
      241 pagrrgaiha idgqalqggl slrslqqaaq iaqwikqgs
//
LOCUS       WP_392445518             307 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Aeromonas bivalvium].
ACCESSION   WP_392445518
VERSION     WP_392445518.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas bivalvium
  ORGANISM  Aeromonas bivalvium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 307)
  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 307)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Aeromonas bivalvium"
                     /db_xref="taxon:440079"
     Protein         1..307
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33657
     Region          32..176
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          211..292
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mstnqpvvat hqsalasrla alaphpgita apvpgvhliy ttehhdripv lyrprmiiil
       61 qghkvgylsd ftfrydpehy lmmtlplpce cecfaspesp lvglsveidv aalqalllem
      121 gdaapapaep grgvvsvpls etmlcaverl idvmdkplha rvlgpqivre ilfhalhegg
      181 aaallamasr hsqvsqiarv lrimeqrfte nltveelare anmsvsafhh hfkaatatsp
      241 lqyiktlrlh rarlmmlhdg lkagvaadkv gyesgsqfsr eykrffgntp sehaarfrsg
      301 qlriveg
//
LOCUS       WP_392446600             374 aa            linear   BCT 20-JAN-2025
DEFINITION  protein-glutamate methylesterase/protein-glutamine glutaminase
            [Shewanella mangrovisoli].
ACCESSION   WP_392446600
VERSION     WP_392446600.1
KEYWORDS    RefSeq.
SOURCE      Shewanella mangrovisoli
  ORGANISM  Shewanella mangrovisoli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 374)
  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   2  (residues 1 to 374)
  AUTHORS   Skerker,J.M., Prasol,M.S., Perchuk,B.S., Biondi,E.G. and Laub,M.T.
  TITLE     Two-component signal transduction pathways regulating growth and
            cell cycle progression in a bacterium: a system-level analysis
  JOURNAL   PLoS Biol 3 (10), e334 (2005)
   PUBMED   16176121
REFERENCE   3  (residues 1 to 374)
  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   4  (residues 1 to 374)
  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
REFERENCE   5  (residues 1 to 374)
  AUTHORS   Anand,G.S., Goudreau,P.N. and Stock,A.M.
  TITLE     Activation of methylesterase CheB: evidence of a dual role for the
            regulatory domain
  JOURNAL   Biochemistry 37 (40), 14038-14047 (1998)
   PUBMED   9760239
REFERENCE   6  (residues 1 to 374)
  AUTHORS   Volz,K.
  TITLE     Structural conservation in the CheY superfamily
  JOURNAL   Biochemistry 32 (44), 11741-11753 (1993)
   PUBMED   8218244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Shewanella mangrovisoli"
                     /db_xref="taxon:2864211"
     Protein         1..374
                     /product="protein-glutamate
                     methylesterase/protein-glutamine glutaminase"
                     /EC_number="3.1.1.61"
                     /EC_number="3.5.1.44"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0008984 - protein-glutamate
                     methylesterase activity [Evidence IEA]"
                     /GO_function="GO:0050568 - protein-glutamine glutaminase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006482 - protein demethylation [Evidence
                     IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0018277 - protein deamination [Evidence
                     IEA]"
                     /calculated_mol_wt=39424
     Region          1..374
                     /region_name="PRK00742"
                     /note="chemotaxis-specific protein-glutamate
                     methyltransferase CheB"
                     /db_xref="CDD:234828"
ORIGIN      
        1 maikvlvvdd ssffrrrvse ivnqdpelev iatasngaea vkmaaelnpq vitmdiempv
       61 mdgitavrei makcptpilm fsslthdgak atldaldaga ldflpkrfed iatnkddail
      121 llqqrvkalg rrrifrpvvr pttptppprq sassvlgsts thaqpapapv rsspatsirp
      181 sgkqykllli gtstggpval qkiltqfpan yphpilliqh mpaaftpafa nrlnglckie
      241 vkeaangdvl rpgcaylapg gmqmmverag vtgrvkvlag saemnykpcv ditfasaska
      301 yggdvlavvl tgmgadgreg armlksagat iwaqdeascv vygmpqavas agiatqsisl
      361 dnmaesilke sarg
//
LOCUS       WP_392448914             550 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Shewanella mangrovisoli].
ACCESSION   WP_392448914
VERSION     WP_392448914.1
KEYWORDS    RefSeq.
SOURCE      Shewanella mangrovisoli
  ORGANISM  Shewanella mangrovisoli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 550)
  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 11459492
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Shewanella mangrovisoli"
                     /db_xref="taxon:2864211"
     Protein         1..550
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=62073
     Region          <145..536
                     /region_name="YcbB"
                     /note="Murein L,D-transpeptidase YcbB/YkuD [Cell
                     wall/membrane/envelope biogenesis]; COG2989"
                     /db_xref="CDD:442228"
ORIGIN      
        1 mmpvsrltpn pnkrkrswss vkrwplstll mglslvlies yaakppvtap lsvephtvel
       61 ladatsieva epdtaveqil gqtlllslad vspvfsanyq qliqwrqral dneeqvklqq
      121 mqlqlnnywr yldaqaecmt pcssatllpk dvyfravvik lkqlmalaes stwdtliled
      181 klspgqespl itpiaqrlfl lgflenmlst aseplselgs epviksdtis pdattpagtv
      241 aqskqvatvn nplryddelv saikafqtqh glqadgvigk qtlywlnqsp yarvqllakn
      301 tlrqliftrt lpasylmini pafelqfvea gkvilnskvi vgkasrptpl lsshissvvl
      361 npqwrvprti vrrdilphir qdghylqdrg fdvydydgar vehspqewqe lasshfpyrl
      421 vqrpgaknal grykfhfdns fsvylhgtse pslfkktdra lssgcirvek veelarwfqt
      481 hlvkdtrlwd klapnttqsq wfalsdtmpv ytvywtawld dagqiqyrnd iyqleaeftl
      541 avpaaifyil
//
LOCUS       WP_392449128             249 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Shewanella
            mangrovisoli].
ACCESSION   WP_392449128
VERSION     WP_392449128.1
KEYWORDS    RefSeq.
SOURCE      Shewanella mangrovisoli
  ORGANISM  Shewanella mangrovisoli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
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   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 249)
  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 10007860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Shewanella mangrovisoli"
                     /db_xref="taxon:2864211"
     Protein         1..249
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=27786
     Region          2..97
                     /region_name="CadC1"
                     /note="DNA-binding winged helix-turn-helix (wHTH) domain
                     [Transcription]; COG3710"
                     /db_xref="CDD:442924"
ORIGIN      
        1 mqigacwfna qeqvlvdsas grswllsade fqilsllsaq rgkvvsrmel qqairpqlkl
       61 smraddllns tirrlrlflg ddaahllvnv anqgfilyat prkqsrteln splfklgmpq
      121 fmllmlltla tlfwvgsris hptniapnya tqlpmhnggl seiqfytgqp tnhsmkplve
      181 hflaqvsaca vfpwqsiaat istdqkfvsl vlknedadgl rfetikmmse dfnadvidel
      241 wlkmvgica
//
LOCUS       WP_392449445             296 aa            linear   BCT 20-JAN-2025
DEFINITION  aldo/keto reductase [Shewanella mangrovisoli].
ACCESSION   WP_392449445
VERSION     WP_392449445.1
KEYWORDS    RefSeq.
SOURCE      Shewanella mangrovisoli
  ORGANISM  Shewanella mangrovisoli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 296)
  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 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   3  (residues 1 to 296)
  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   4  (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 10790928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Shewanella mangrovisoli"
                     /db_xref="taxon:2864211"
     Protein         1..296
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /calculated_mol_wt=33001
     Region          1..296
                     /region_name="YdhF"
                     /note="Predicted oxidoreductase YdhF [General function
                     prediction only]; COG4989"
                     /db_xref="CDD:444013"
ORIGIN      
        1 msgspfsfse fvagfwrmhs wqmspaerln lieqylnlgv ttmdhadiyg qyqcetlfge
       61 alalkpglrq qmqlvskcgi kpafdcrper yvnhydtska hiiasveqsl kqlktdyldl
      121 lllhrpdplm dadqvadafa dlkqagkvqh fgvsnftnaq fsllqsrltd plvtnqieis
      181 pltmaslhdg tldlcqerri rpmawsclgg gkifdnshpq airlqqtlav iadeigaqdi
      241 sqviyawvrm lpsrpvpiig sgniarikta vasqsltldr qqwfsiwqas tghsvp
//
LOCUS       WP_392450236             262 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Delftia sp. WSY_22].
ACCESSION   WP_392450236
VERSION     WP_392450236.1
KEYWORDS    RefSeq.
SOURCE      Delftia sp. WSY_22
  ORGANISM  Delftia sp. WSY_22
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Delftia.
REFERENCE   1  (residues 1 to 262)
  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 11440233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Delftia sp. WSY_22"
                     /db_xref="taxon:3367213"
     Protein         1..262
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28263
     Region          22..258
                     /region_name="GCD1"
                     /note="NDP-sugar pyrophosphorylase, includes eIF-2Bgamma,
                     eIF-2Bepsilon, and LPS biosynthesis protein s
                     [Translation, ribosomal structure and biogenesis, Cell
                     wall/membrane/envelope biogenesis]; COG1208"
                     /db_xref="CDD:440821"
ORIGIN      
        1 mtaspippfp aakalflteq ppamllaagr germrpltdt cpkpllqvqg rpllqhhlqa
       61 laqagvrrav vntgwlgeqi parfgarfap dtggeplhla yspepeqale taggiaralp
      121 lldtvfwlaa gdvyapdfdf pfeaarefaa sgrlahlwlv pnpehhrrgd fgvdelglac
      181 dwpegdarpr qtygtiallr aelfaapwcd ippgnpdgwr vplvallrra maagqvsasl
      241 yagrwtdvgt perlqrlntp aa
//
LOCUS       WP_392452784             551 aa            linear   BCT 20-JAN-2025
DEFINITION  SWIM zinc finger family protein [Streptococcus parasuis].
ACCESSION   WP_392452784
VERSION     WP_392452784.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus parasuis
  ORGANISM  Streptococcus parasuis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Hassan,I.U., Rehman,H.M., Liu,Z., Zhou,L., Samma,M.K., Wang,C.,
            Rong,Z., Qi,X., Cai,D. and Zhao,H.
  TITLE     Genome-wide identification and spatiotemporal expression profiling
            of zinc finger SWIM domain-containing protein family genes
  JOURNAL   Zool Res 44 (3), 663-674 (2023)
   PUBMED   37161653
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Makarova,K.S., Aravind,L. and Koonin,E.V.
  TITLE     SWIM, a novel Zn-chelating domain present in bacteria, archaea and
            eukaryotes
  JOURNAL   Trends Biochem Sci 27 (8), 384-386 (2002)
   PUBMED   12151216
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Streptococcus parasuis"
                     /db_xref="taxon:1501662"
     Protein         1..551
                     /product="SWIM zinc finger family protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=64379
     Region          2..489
                     /region_name="SWIM"
                     /note="Uncharacterized protein, contains SWIM-type Zn
                     finger domain [Function unknown]; COG4715"
                     /db_xref="CDD:443750"
ORIGIN      
        1 mknwmdyfkp hivdrgcslf lddavqglee vgegyyalvs gsqvyqveid lehgqlvsmw
       61 cecphaqemn hckhmaavlf aiselesqpv vegkdvslaq lldkltveql rafvlelaqe
      121 drelanriql rftaqlttqq venvkkaiid lglpfedryk gyieykrtgd yeqavtkamh
      181 qylqplldrc eyanflaisd afyhqicrqe lddsdgttgs llyrlagywk klltvapysi
      241 aqvlldwcle klngyevaed llmefvemef qeeqflqqkl tyfqadlqai iekgdmssws
      301 rkfrrdrial lcyrlqvqlg sseadllnfq anhwevaglr klaiaqaven qqleravhll
      361 qeskrldaqy rglvsdysrq lreiyrsqgq ddkvreelle mifsagdtdl klieelqdfv
      421 sieewqsyld dllkdrrfqs qqlkllqlad rpqelldrit tsywflenld rfedylsekl
      481 peqlrdaytq avcqqmevan srnryrqlar ylakiaslpd getvseslra lwkvqyprrk
      541 amieeldavr w
//
LOCUS       WP_392453914             333 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase LdtE [Salmonella enterica].
ACCESSION   WP_392453914
VERSION     WP_392453914.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Monton Silva,A., Otten,C., Biboy,J., Breukink,E., VanNieuwenhze,M.,
            Vollmer,W. and den Blaauwen,T.
  TITLE     The Fluorescent D-Amino Acid NADA as a Tool to Study the
            Conditional Activity of Transpeptidases in Escherichia coli
  JOURNAL   Front Microbiol 9, 2101 (2018)
   PUBMED   30233559
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Cava,F., de Pedro,M.A., Lam,H., Davis,B.M. and Waldor,M.K.
  TITLE     Distinct pathways for modification of the bacterial cell wall by
            non-canonical D-amino acids
  JOURNAL   EMBO J 30 (16), 3442-3453 (2011)
   PUBMED   21792174
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Magnet,S., Dubost,L., Marie,A., Arthur,M. and Gutmann,L.
  TITLE     Identification of the L,D-transpeptidases for peptidoglycan
            cross-linking in Escherichia coli
  JOURNAL   J Bacteriol 190 (13), 4782-4785 (2008)
   PUBMED   18456808
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF047955.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..333
                     /gene="ldtE"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
     Protein         1..333
                     /product="L,D-transpeptidase LdtE"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=35996
     Region          19..303
                     /region_name="PRK10260"
                     /note="L,D-transpeptidase; Provisional"
                     /db_xref="CDD:182341"
ORIGIN      
        1 mkrasfitlt iigaysalqa awavdyplpp egsrligqnq tytvqegdkn lqaiarrfdt
       61 aamlileann tiapvpkpgt litipsqmll pdapregviv nlaelrlyyy ppgenrvqvy
      121 pigiglqgle tpvmdtrigq kipnptwtpt agirqrsler gitlppvipa gpnnplgrya
      181 lrlahgngey lihgtsapds vglrvssgci rmnapdikal faqvrtgtpv kvinqpvkfs
      241 vepngiryve vhrplspeee qnvqtmpyvl paeftafrna qgvdsrlvdk alyrragypv
      301 svsagqapav nttavesaqn gfvgeegqtr vtq
//
LOCUS       WP_392454314             178 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase family protein [Chryseomicrobium
            aureum].
ACCESSION   WP_392454314
VERSION     WP_392454314.1
KEYWORDS    RefSeq.
SOURCE      Chryseomicrobium aureum
  ORGANISM  Chryseomicrobium aureum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Chryseomicrobium.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Vollmer,W., Joris,B., Charlier,P. and Foster,S.
  TITLE     Bacterial peptidoglycan (murein) hydrolases
  JOURNAL   FEMS Microbiol Rev 32 (2), 259-286 (2008)
   PUBMED   18266855
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436722
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Chryseomicrobium aureum"
                     /db_xref="taxon:1441723"
     Protein         1..178
                     /product="N-acetylmuramoyl-L-alanine amidase family
                     protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19489
     Region          3..176
                     /region_name="AmiC"
                     /note="N-acetylmuramoyl-L-alanine amidase [Cell
                     wall/membrane/envelope biogenesis]; COG0860"
                     /db_xref="CDD:440621"
ORIGIN      
        1 mcivldpghg pftagkrspd grlreyhvna aiakfvqqel egivtchftt ngdrdvplwe
       61 rsqfanqlka slfvsihana ygsiwnavsg ieiyiapras kkshlvakav qaqlvkktgr
      121 ldrgvktgnf hvltrttmpa ilvevgfmtn rvecelllse eyqrkcakgi aagirsvl
//
LOCUS       WP_392455510             316 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Chryseomicrobium aureum].
ACCESSION   WP_392455510
VERSION     WP_392455510.1
KEYWORDS    RefSeq.
SOURCE      Chryseomicrobium aureum
  ORGANISM  Chryseomicrobium aureum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Chryseomicrobium.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415139
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Chryseomicrobium aureum"
                     /db_xref="taxon:1441723"
     Protein         1..316
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=35532
     Region          1..293
                     /region_name="LysX"
                     /note="Glutathione synthase, LysX or RimK-type ligase,
                     ATP-grasp superfamily [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism,
                     Translation, ribosomal structure and biogenesis, Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0189"
                     /db_xref="CDD:439959"
ORIGIN      
        1 mskvyiihen sewtthltnr leelqvpyee whldqglvdl teappegify nrmsasshtr
       61 ghryapelts svlawlehhg rtifngsnal rlelskvlqy talnaagiqt pdtiaavgke
      121 qiikaaeklg vssfitkhnr agkglgvqlf ysidglrnyv ygptfdepvd gvtliqkyik
      181 apepfitrce fingnfqyav kvdtsegfel cpadacqidd lfcpvgeqpt sspkfqiiqg
      241 fkepiiekye aflkqnqikv agiefiysed geiytydvnt ntnynadaek aagqynmltl
      301 akvlkeelnk qyveir
//
LOCUS       WP_392455980             382 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Chryseomicrobium aureum].
ACCESSION   WP_392455980
VERSION     WP_392455980.1
KEYWORDS    RefSeq.
SOURCE      Chryseomicrobium aureum
  ORGANISM  Chryseomicrobium aureum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Chryseomicrobium.
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 11417965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Chryseomicrobium aureum"
                     /db_xref="taxon:1441723"
     Protein         1..382
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43979
     Region          3..240
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
ORIGIN      
        1 mvirffhaad lhlespfaki qsmpehwqqr irnasfgafd sfvqdaitnk pdfillagdi
       61 ydgetrslra qayfkkamet laqydipvyi ihgnhdhlag nwtrfklppn vtifgetpes
      121 yeleidgqvv qisgfsyprr hlpesyieky pprksyadya igllhgseqt qqehdvyapf
      181 tleqlrqtsy dywalghihk rqqlstkpai ayagtlqgrn rkeqgvqgyy hvelsnsept
      241 ltfqkasqvv fdeievvfes tasidhfqeq likalepktd hiytlvqvti ktpkedwmlt
      301 tnenelrefi leqvnqtiqt vyithlnlhw tteldpafqq lmnqfalpti ptamqqvlds
      361 stledqvker mhailtdrsg gq
//
LOCUS       WP_392456089             359 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Chryseomicrobium
            aureum].
ACCESSION   WP_392456089
VERSION     WP_392456089.1
KEYWORDS    RefSeq.
SOURCE      Chryseomicrobium aureum
  ORGANISM  Chryseomicrobium aureum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Chryseomicrobium.
REFERENCE   1  (residues 1 to 359)
  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 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   3  (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   4  (residues 1 to 359)
  AUTHORS   Igarashi,K., Ito,K. and Kashiwagi,K.
  TITLE     Polyamine uptake systems in Escherichia coli
  JOURNAL   Res Microbiol 152 (3-4), 271-278 (2001)
   PUBMED   11421274
REFERENCE   5  (residues 1 to 359)
  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   6  (residues 1 to 359)
  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 11430824
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Chryseomicrobium aureum"
                     /db_xref="taxon:1441723"
     Protein         1..359
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0019808 - polyamine binding [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:0015846 - polyamine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=40344
     Region          2..353
                     /region_name="PotD"
                     /note="Spermidine/putrescine-binding periplasmic protein
                     [Amino acid transport and metabolism]; COG0687"
                     /db_xref="CDD:440451"
ORIGIN      
        1 mksllqitgv llvavavliy insqltdtss rassgtitvf nwgeyidpel vtqfeeetgi
       61 rviyetfdsn eamltkiqqg gtrydiavps eymiekmkee dlllpidqsk ipnlenidpy
      121 fldlpfdpgn qysipyfwgt vgiafnptll dgqtfeswsd lwspeleqqv ilvdgarevm
      181 gmglntlgys lnstdeqelr qatdrlkelg pnvkaiigde ivetmrrgea aialvwsgqa
      241 adimyvnedi dysvpqegsn lwfdnmiipk tagnvegaha finfmldaei aaqnadyvgy
      301 stpnlpaldl mdpevtgdtr fyptedmree levyrnlgpv mlgkyneyfl efkmsmnrn
//
LOCUS       WP_392456660             288 aa            linear   BCT 20-JAN-2025
DEFINITION  aldo/keto reductase [Chryseomicrobium aureum].
ACCESSION   WP_392456660
VERSION     WP_392456660.1
KEYWORDS    RefSeq.
SOURCE      Chryseomicrobium aureum
  ORGANISM  Chryseomicrobium aureum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Chryseomicrobium.
REFERENCE   1  (residues 1 to 288)
  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 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   3  (residues 1 to 288)
  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   4  (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 10790928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Chryseomicrobium aureum"
                     /db_xref="taxon:1441723"
     Protein         1..288
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /calculated_mol_wt=32401
     Region          1..288
                     /region_name="YdhF"
                     /note="Predicted oxidoreductase YdhF [General function
                     prediction only]; COG4989"
                     /db_xref="CDD:444013"
ORIGIN      
        1 mgcmrinelt dqeltewvqh alelgihtfd hadiyargec etrfgnvikn epslrdkmvl
       61 qtkasiragy ydsskehlls svdaslsrlq tdyidvfmlh rpdalmelde iadvfdtlag
      121 sgkvrsfgvs nfnryqlewl qaathqpiei nqlqfspvhs sllttgiqan tefsgaidrd
      181 ggvltycqqq siriqawspf qfgffegvyl dhprfpelnk vleelathyg vtksaiiaaw
      241 ilrhsanmqv vagstkvnri keivagaeit lsrkdwytiy qaagnrlp
//
LOCUS       WP_392457338              98 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Aeromonas
            media].
ACCESSION   WP_392457338
VERSION     WP_392457338.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas media
  ORGANISM  Aeromonas media
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 98)
  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 98)
  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 10008602
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Aeromonas media"
                     /db_xref="taxon:651"
     Protein         1..98
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10756
     Region          2..98
                     /region_name="COG4519"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443593"
ORIGIN      
        1 msepsktrss fyrrlyvahl isqgtdtvpa imaatgmprr taqdtlsala eldiscafeq
       61 tegarhlqgh yrisdwgpin pawikaqlpv ikqtlgyp
//
LOCUS       WP_392459163             241 aa            linear   BCT 20-JAN-2025
DEFINITION  4'-phosphopantetheinyl transferase family protein [Aeromonas
            media].
ACCESSION   WP_392459163
VERSION     WP_392459163.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas media
  ORGANISM  Aeromonas media
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459479
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Aeromonas media"
                     /db_xref="taxon:651"
     Protein         1..241
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=25728
     Region          34..241
                     /region_name="EntD"
                     /note="4'-phosphopantetheinyl transferase EntD
                     (siderophore biosynthesis) [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2977"
                     /db_xref="CDD:442216"
ORIGIN      
        1 mphlspltaf llqrdhlllp gappltlhri cfdaaaftpa cfaahdmalp aslqraapkr
       61 lgeflagrla arealrpfgl agkgvaigsa replwplgme gsishsqlag lgvalcgvrr
      121 aqggmgldle awlgteqgsq lwpgivdede wgrleggara lgldrarglt lvfsakeslf
      181 kalhprvgry fdfldarwlg mtaqsltlel kvpltptlpa gwrctlhwqp lpggvltall
      241 l
//
LOCUS       WP_392459532             299 aa            linear   BCT 20-JAN-2025
DEFINITION  aldo/keto reductase [Aeromonas media].
ACCESSION   WP_392459532
VERSION     WP_392459532.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas media
  ORGANISM  Aeromonas media
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 299)
  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 299)
  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   3  (residues 1 to 299)
  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   4  (residues 1 to 299)
  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 10790928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Aeromonas media"
                     /db_xref="taxon:651"
     Protein         1..299
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /calculated_mol_wt=33088
     Region          4..299
                     /region_name="YdhF"
                     /note="Predicted oxidoreductase YdhF [General function
                     prediction only]; COG4989"
                     /db_xref="CDD:444013"
ORIGIN      
        1 msvsrlalhh qgptfsrlim gywrlmewql spaalldlmk yhldlgitti dhadiyggyq
       61 ceeafgqalr lepslrsrme ivskcgialt akpehalnhy ntskghivas aeaslqklgt
      121 dhldlllihr pdplmnadev aeafislkqa gkikhagvsn ftphqfallq srlpfplvtn
      181 qleisplhqe gtldgaldqc qqlgikpmaw sclgggrlfn dpayaplrae lelirqelga
      241 qtmeqvvyaw vmmlpsqplp ligsgkreri saavaaesiq lsrqqwfrir kaalgydvp
//
LOCUS       WP_392459560             171 aa            linear   BCT 20-JAN-2025
DEFINITION  ubiquinone anaerobic biosynthesis accessory factor UbiT [Aeromonas
            media].
ACCESSION   WP_392459560
VERSION     WP_392459560.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas media
  ORGANISM  Aeromonas media
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Arias-Cartin,R., Kazemzadeh Ferizhendi,K., Sechet,E., Pelosi,L.,
            Loeuillet,C., Pierrel,F., Barras,F. and Bouveret,E.
  TITLE     Role of the Escherichia coli ubiquinone-synthesizing UbiUVT pathway
            in adaptation to changing respiratory conditions
  JOURNAL   mBio 14 (4), e0329822 (2023)
   PUBMED   37283518
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Vo,C.D., Michaud,J., Elsen,S., Faivre,B., Bouveret,E., Barras,F.,
            Fontecave,M., Pierrel,F., Lombard,M. and Pelosi,L.
  TITLE     The O2-independent pathway of ubiquinone biosynthesis is essential
            for denitrification in Pseudomonas aeruginosa
  JOURNAL   J Biol Chem 295 (27), 9021-9032 (2020)
   PUBMED   32409583
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Pelosi,L., Vo,C.D., Abby,S.S., Loiseau,L., Rascalou,B., Hajj
            Chehade,M., Faivre,B., Gousse,M., Chenal,C., Touati,N., Binet,L.,
            Cornu,D., Fyfe,C.D., Fontecave,M., Barras,F., Lombard,M. and
            Pierrel,F.
  TITLE     Ubiquinone Biosynthesis over the Entire O2 Range: Characterization
            of a Conserved O2-Independent Pathway
  JOURNAL   mBio 10 (4), e01319-19 (2019)
   PUBMED   31289180
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF047962.3
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Aeromonas media"
                     /db_xref="taxon:651"
     gene            1..171
                     /gene="ubiT"
     Protein         1..171
                     /product="ubiquinone anaerobic biosynthesis accessory
                     factor UbiT"
                     /GO_component="GO:0110142 - ubiquinone biosynthesis
                     complex [Evidence IEA]"
                     /GO_process="GO:0006744 - ubiquinone biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=19260
     Region          7..165
                     /region_name="UbiT"
                     /note="Ubiquinone biosynthesis accessory factor UbiT,
                     lipid carrier SCP2 domain [Coenzyme transport and
                     metabolism]; COG3154"
                     /db_xref="CDD:442388"
ORIGIN      
        1 mfqqlqrrlv eqaphllrrp lklvpftlqq nlmeallaqa fkeaiqdgdf aflagkwlkv
       61 evsdlelcwf vseregklvv ardceradvc fsgssqdlil iagrkedpds lffqrrlkie
      121 gdtelglevk nlmdsldldg lpglmkyplm dlatliervr saqdplpasm a
//
LOCUS       WP_392459917             332 aa            linear   BCT 20-JAN-2025
DEFINITION  BMP family lipoprotein [Aeromonas media].
ACCESSION   WP_392459917
VERSION     WP_392459917.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas media
  ORGANISM  Aeromonas media
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Yousief,S.W., Bahey-El-Din,M. and Zaghloul,T.I.
  TITLE     Immunization with the basic membrane protein (BMP) family ABC
            transporter elicits protection against Enterococcus faecium in a
            murine infection model
  JOURNAL   Microbes Infect 22 (3), 127-136 (2020)
   PUBMED   31585177
REFERENCE   2  (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   3  (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   4  (residues 1 to 332)
  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   5  (residues 1 to 332)
  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 11448319
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Aeromonas media"
                     /db_xref="taxon:651"
     Protein         1..332
                     /product="BMP family lipoprotein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /calculated_mol_wt=35163
     Region          26..322
                     /region_name="Med"
                     /note="Lipoprotein Med, regulator of KinD/Spo0A, PBP1-ABC
                     superfamily, includes NupN [Signal transduction
                     mechanisms]; COG1744"
                     /db_xref="CDD:441350"
ORIGIN      
        1 mtkvlklatv aaltlaalsa qaasepaviy dtagkfdksf neavfrngve vynkdkgvkv
       61 kefepqneaq reqglrrlas rgngpivavg fnmgsavekv atefpntqft iidmvvdkpn
      121 vqslifkehe gsflvgalaa iasksgkvgf vggmdiplir kfqcgyeqga kyinpkidvy
      181 qnmtgstpaa fadpakgael aksqfakgad vvyaaaggtg igvyqaakde gklaigvdsn
      241 qnhlqpgtml tsmvkdvgla aykswdeaak gswkpgiqtl glaeggvdwa ldennaklit
      301 pemkakvesi kadiiagkik vhdymsdnsc ky
//
LOCUS       WP_392460310              95 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Aeromonas
            media].
ACCESSION   WP_392460310
VERSION     WP_392460310.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas media
  ORGANISM  Aeromonas media
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 95)
  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 95)
  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 10007860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Aeromonas media"
                     /db_xref="taxon:651"
     Protein         1..95
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10801
     Region          <1..71
                     /region_name="CadC1"
                     /note="DNA-binding winged helix-turn-helix (wHTH) domain
                     [Transcription]; COG3710"
                     /db_xref="CDD:442924"
ORIGIN      
        1 mgskevsllk ylaknsgyvi sktellhhvw reqnvhentv lvtlsgirki frkagldcrc
       61 ivtiakfgyi fyprraglem egfndsgkhs ilwfn
//
LOCUS       WP_392461542             402 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptococcus parasuis].
ACCESSION   WP_392461542
VERSION     WP_392461542.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus parasuis
  ORGANISM  Streptococcus parasuis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Streptococcus parasuis"
                     /db_xref="taxon:1501662"
     Protein         1..402
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=45214
     Region          54..308
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mkkilllggs tqqipaieya neqgyytvlc dyladnpgqg yakkfycvst tdkdaileva
       61 knekvdgvva yasdpaapta ayvaeklglp tnpyksvktl afkdkfrdfl kenkfncpka
      121 kgfsslenak aeiaqftfpv mvkpvdssgs kgvskvekle dfeeaykial dnsrgkniiv
      181 eefieqdhdy miagdcfvid gkvkfwglln shrndkvnpy vpvgtsypiy isknrldlvk
      241 ketqrlfdsl dvefgafnie iiidkndkly fiemgprngg nmipdllyma tgedmiaati
      301 esamgnkygf nntiiqnkfl styvlhsdkd glfqtvqykn giedkilkev iykkngdrvq
      361 yfdgankaig ivffkfdtqe eqmdftnspe nwievvikqv nq
//
LOCUS       WP_392461790             281 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Pseudomonas].
ACCESSION   WP_392461790
VERSION     WP_392461790.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 281)
  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 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   3  (residues 1 to 281)
  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   4  (residues 1 to 281)
  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 281)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..281
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31050
     Region          22..273
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <149..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 msmplpeqth lwqapalgdv emlharyyqq rfaphvhegy vftviesgaq rfwhrgsehl
       61 apvgsmvlin pdelhtgata heagwryrgf ypehervtgv ldelelgrhg mpsfkdsvih
      121 dpalaiafsq lhqlseasas alqqqtawrq avlalvqrhg qcaepsapgh eplavarare
      181 llesqladpp slealagavn lspfhfarvf rqatglppha wlkqrrlara remlkhglaa
      241 sqvafdlgfa dqshlsrqfk qaygvtpgay rqacvhsalr a
//
LOCUS       WP_392462129             303 aa            linear   BCT 20-JAN-2025
DEFINITION  aldo/keto reductase [Streptococcus parasuis].
ACCESSION   WP_392462129
VERSION     WP_392462129.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus parasuis
  ORGANISM  Streptococcus parasuis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 303)
  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 303)
  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   3  (residues 1 to 303)
  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   4  (residues 1 to 303)
  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 10790928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus parasuis"
                     /db_xref="taxon:1501662"
     Protein         1..303
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /calculated_mol_wt=33978
     Region          4..303
                     /region_name="YdhF"
                     /note="Predicted oxidoreductase YdhF [General function
                     prediction only]; COG4989"
                     /db_xref="CDD:444013"
ORIGIN      
        1 mqelgqtglq vsrialgcmr maslnereta nvietvvqhg inffdhadiy gggeseirfa
       61 qgtklaglkr edlllqskcg irkgyfdfsk eyilesvdgi lkrldteyld vlalhrpdal
      121 meaeevaeaf yllkkagkvh yfgvsnqniy qmellqsyld qplavnqlql spahtplida
      181 glhvnmkdda atmrdgglid ycqlkkitiq awspflidlq rgifanhpdy allnqtigei
      241 aerynvshet ivvawilrhp akiqtivgsm npdrltkiaq asqitltrpe wyeiyksagn
      301 ilp
//
LOCUS       WP_392462610             273 aa            linear   BCT 20-JAN-2025
DEFINITION  LicD family protein [Streptococcus parasuis].
ACCESSION   WP_392462610
VERSION     WP_392462610.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus parasuis
  ORGANISM  Streptococcus parasuis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Kuchta,K., Knizewski,L., Wyrwicz,L.S., Rychlewski,L. and
            Ginalski,K.
  TITLE     Comprehensive classification of nucleotidyltransferase fold
            proteins: identification of novel families and their
            representatives in human
  JOURNAL   Nucleic Acids Res 37 (22), 7701-7714 (2009)
   PUBMED   19833706
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Streptococcus parasuis"
                     /db_xref="taxon:1501662"
     Protein         1..273
                     /product="LicD family protein"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=32453
     Region          1..265
                     /region_name="LicD"
                     /note="Phosphorylcholine metabolism protein LicD [Lipid
                     transport and metabolism]; COG3475"
                     /db_xref="CDD:442698"
ORIGIN      
        1 mrqitqeemr qiqldmldyi dqiardnhie yslgggsllg amrhkgfipw dddidlmler
       61 sqyerlmavl aedknpdfkl lhhsternlw pfaklyhtks yyisktdrih pwtglfidif
      121 pidklpntqe ernkffkkvr laaenlkctt fpnfasgsnh lfafarlilg mprfalyhgq
      181 skqkavevde vmstynatnv kfrgytdsry rlkecfpaei fdhyedvnfe hlvvrkikee
      241 kiylnqlyga symelppehk reshdyytwc wke
//
LOCUS       WP_392462880             299 aa            linear   BCT 20-JAN-2025
DEFINITION  aldo/keto reductase [Aeromonas dhakensis].
ACCESSION   WP_392462880
VERSION     WP_392462880.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 299)
  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 299)
  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   3  (residues 1 to 299)
  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   4  (residues 1 to 299)
  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 10790928
            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="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /calculated_mol_wt=33295
     Region          4..299
                     /region_name="YdhF"
                     /note="Predicted oxidoreductase YdhF [General function
                     prediction only]; COG4989"
                     /db_xref="CDD:444013"
ORIGIN      
        1 msvsrlplhp egptfsrlim gywrlmewql spsalldlmr yhldlgvtti dhadiyggyq
       61 ceqafgealr ldpslrnrme ivskcgialt akpehalnhy ntgkahiias aeaslqklgt
      121 dhldlllihr pdplmdadev adafitlkqa gkikhagvsn ftarqfellq srlpfplvtn
      181 qleisplnqs ttldgtldqc qqlrikpmaw sclgggrlfq apeyaplrae leqirhevga
      241 eqieqvvyaw vmmlpsqplp ligsgkreri aaavasqsiv lsrqqwfrir kaalgydvp
//
LOCUS       WP_392462928             369 aa            linear   BCT 20-JAN-2025
DEFINITION  protein-glutamate methylesterase/protein-glutamine glutaminase
            [Aeromonas dhakensis].
ACCESSION   WP_392462928
VERSION     WP_392462928.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 369)
  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   2  (residues 1 to 369)
  AUTHORS   Skerker,J.M., Prasol,M.S., Perchuk,B.S., Biondi,E.G. and Laub,M.T.
  TITLE     Two-component signal transduction pathways regulating growth and
            cell cycle progression in a bacterium: a system-level analysis
  JOURNAL   PLoS Biol 3 (10), e334 (2005)
   PUBMED   16176121
REFERENCE   3  (residues 1 to 369)
  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   4  (residues 1 to 369)
  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
REFERENCE   5  (residues 1 to 369)
  AUTHORS   Anand,G.S., Goudreau,P.N. and Stock,A.M.
  TITLE     Activation of methylesterase CheB: evidence of a dual role for the
            regulatory domain
  JOURNAL   Biochemistry 37 (40), 14038-14047 (1998)
   PUBMED   9760239
REFERENCE   6  (residues 1 to 369)
  AUTHORS   Volz,K.
  TITLE     Structural conservation in the CheY superfamily
  JOURNAL   Biochemistry 32 (44), 11741-11753 (1993)
   PUBMED   8218244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..369
                     /product="protein-glutamate
                     methylesterase/protein-glutamine glutaminase"
                     /EC_number="3.1.1.61"
                     /EC_number="3.5.1.44"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0008984 - protein-glutamate
                     methylesterase activity [Evidence IEA]"
                     /GO_function="GO:0050568 - protein-glutamine glutaminase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006482 - protein demethylation [Evidence
                     IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0018277 - protein deamination [Evidence
                     IEA]"
                     /calculated_mol_wt=39710
     Region          1..369
                     /region_name="PRK00742"
                     /note="chemotaxis-specific protein-glutamate
                     methyltransferase CheB"
                     /db_xref="CDD:234828"
ORIGIN      
        1 maikvlvvdd ssffrrrvse iitqdpmltv idtaqngrea vekaqqlrpd vitmdiempv
       61 mdgisavrei makyptpilm fsslthegak atldaldaga ldflpkkfed iardkdeavr
      121 llqqrvkeis rkrflmsapa rpkapepvar tplnaprpae rqaepqraap vaafkrsgks
      181 yqlvaigtst ggpvalqnvl tklpgdfphp illiqhmpat ftaafaarln glcqigvkea
      241 edgdvlkpgh aylapggkqm llegrgagar irivdgndkv nykpcvditf asaaktyadk
      301 vlaivltgmg adgrdgarll keqgstiwaq deascvvygm pqavakagia teslpldrva
      361 qrilvelgr
//
LOCUS       WP_392466778             377 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Arsenicicoccus cauae].
ACCESSION   WP_392466778
VERSION     WP_392466778.1
KEYWORDS    RefSeq.
SOURCE      Arsenicicoccus cauae
  ORGANISM  Arsenicicoccus cauae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Intrasporangiaceae; Arsenicicoccus.
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
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 377)
  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   5  (residues 1 to 377)
  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   6  (residues 1 to 377)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 377)
  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 11973053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Arsenicicoccus cauae"
                     /db_xref="taxon:2663847"
     Protein         1..377
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38086
     Region          <10..78
                     /region_name="COG3398"
                     /note="Predicted transcriptional regulator, contains two
                     HTH domains [Transcription]"
                     /db_xref="CDD:442625"
     Region          102..360
                     /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 mtsataptgl glvrgatdri vleslvdagr qtraeiaqat gvskptvsea vrrlgelgvv
       61 aeagrqegtr grsgiyyela agaglavalh agphlvvges rdvrgglvrr verpvgltvt
      121 adellgelag alsaltasdg trgassvaat tvsvadpveh rsgrlvhvpg spfvrgeacl
      181 rdvvggaaei dndvhwaava elhqgqtdtf lqlylgagig aalvadgrlv rgarglagea
      241 ayavtaagrt grrssprlld vlveegltvd ggtvvdvaav aalmrrgaaq gtaarvvgav
      301 gdvlcsaial vdpgrvvlsg pwgceprlvd alrthlaeaa vlpvevvtsv tgtqapldga
      361 rqrsvelara allsrvp
//
LOCUS       WP_392467855             118 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Pseudomonas sp. xss_2].
ACCESSION   WP_392467855
VERSION     WP_392467855.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. xss_2
  ORGANISM  Pseudomonas sp. xss_2
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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   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 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
REFERENCE   4  (residues 1 to 118)
  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 10009358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Pseudomonas sp. xss_2"
                     /db_xref="taxon:3367215"
     Protein         1..118
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13147
     Region          3..116
                     /region_name="HigA"
                     /note="Antitoxin component HigA of the HigAB
                     toxin-antitoxin module, contains an N-terminal HTH domain
                     [Defense mechanisms]; COG5499"
                     /db_xref="CDD:444250"
ORIGIN      
        1 mnikpirnde dlraafqrle aifqadagts eademevlvt lievyenkhy pihpanpvea
       61 ikfcmdqqgl tprdlerfig psgrvsevln gkrglslsmi krlhdglrip yesllagt
//
LOCUS       WP_392469382             408 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Sphingobacterium
            cellulitidis].
ACCESSION   WP_392469382
VERSION     WP_392469382.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 408)
  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 408)
  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 11417965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..408
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46476
     Region          1..298
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
ORIGIN      
        1 mrilhtadwh lgkkldffsr leeqkevlde icqiadredv dlvvvsgdly dtfnppveat
       61 ellyrtlkrl skngkrpvia iagnhdspdr idspdslare lgifffgqpn lkinpltvdg
      121 sfdiirvdeg fveiklpkyy ypirvlstaf aneirlkqyl gdedkasqlq evlkkkwldt
      181 anqycdsygv niltthlyml krgaevleep egekplrlgf advvysdsip gsiqytalgh
      241 lhkfheigqg tapviypgsp laysfsesgq kkqvvivdle pnkiaqyrtv slekgrplhr
      301 vrfkdideav rwlhdnkyal veltiesdnf lsssdlkrih gahegiihii pvvskkqein
      361 qpkslvnldq dmeslfkdyf kskygqepne elmalfhevs tntleked
//
LOCUS       WP_392469765             324 aa            linear   BCT 20-JAN-2025
DEFINITION  Ig-like domain-containing protein [Sphingobacterium cellulitidis].
ACCESSION   WP_392469765
VERSION     WP_392469765.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Fraser,J.S., Yu,Z., Maxwell,K.L. and Davidson,A.R.
  TITLE     Ig-like domains on bacteriophages: a tale of promiscuity and deceit
  JOURNAL   J Mol Biol 359 (2), 496-507 (2006)
   PUBMED   16631788
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Bork,P., Holm,L. and Sander,C.
  TITLE     The immunoglobulin fold. Structural classification, sequence
            patterns and common core
  JOURNAL   J Mol Biol 242 (4), 309-320 (1994)
   PUBMED   7932691
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475235
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..324
                     /product="Ig-like domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=36343
     Region          <76..>261
                     /region_name="YjdB"
                     /note="Uncharacterized conserved protein YjdB, contains
                     Ig-like domain [General function prediction only];
                     COG5492"
                     /db_xref="CDD:444243"
ORIGIN      
        1 mkllkstrpl iwlltfvfii sacsksesia pepekpkytk ieltstpiel fvgerfelqy
       61 ffspeilpqp evtwksskpe vieviggkis tlkagessis vqingtnlvs tktikvverp
      121 ivvnqivlev sktklnigdk ilinhkllpq nsvdinkhli ewsssdpsia tvekgnltav
      181 grgfvkitak lkdtdisstv qfeilpqikf aeigkdilap dgltlriisv dystsiqgtk
      241 satilylmtn ntssqkvieg afklykksgk aldqygffny lypgesrmrg ytfkeiatee
      301 fdyfeyrpsd ftkqydsflr llvk
//
LOCUS       WP_392470175             175 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Pseudomonas sp. zjy_14].
ACCESSION   WP_392470175
VERSION     WP_392470175.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. zjy_14
  ORGANISM  Pseudomonas sp. zjy_14
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 175)
  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 10789902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Pseudomonas sp. zjy_14"
                     /db_xref="taxon:3367264"
     Protein         1..175
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=19079
     Region          10..164
                     /region_name="YafK"
                     /note="Murein L,D-transpeptidase YafK [Cell
                     wall/membrane/envelope biogenesis]; COG3034"
                     /db_xref="CDD:442269"
ORIGIN      
        1 mknaikiftl ipvalsliac pkkaeittes adpcrehrsv vlvqlkkeql slckngatvk
       61 aydvalgsgg fgktragdek tpigtyplek prpstdkkfh tfikigyptp kqiaqgytgn
      121 dvgihgphky wawaggantw inwtngcvav ksnqdiidis qwveseqvrt vtlel
//
LOCUS       WP_392470971             291 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter sp. YQ_14].
ACCESSION   WP_392470971
VERSION     WP_392470971.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. YQ_14
  ORGANISM  Acinetobacter sp. YQ_14
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 291)
  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 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   3  (residues 1 to 291)
  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   4  (residues 1 to 291)
  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 291)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Acinetobacter sp. YQ_14"
                     /db_xref="taxon:3367236"
     Protein         1..291
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32882
     Region          24..175
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          202..284
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mmnqqqlipl flklvrkegf fvtaidgitl mrvdhntppi svlqeptlvf vlqgkkrgyi
       61 aketysfeqg eclivsvsmp fdcdtiasse qpmiavsmkl dadtvnella ktyfenyqft
      121 plttgmsviq ydetissvll rllntltseq dililgdqik rellyrviqh sgadalkglv
      181 vqgnlrpiyk iceyiqhhft ekltvemlae qanmstsafh kafkqvtqhs plqylkvvrl
      241 hkakqllqna dqsvaqaaya vgyqsssqfs refkkqfgfs pnqtevnidk e
//
LOCUS       WP_392471219             154 aa            linear   BCT 20-JAN-2025
DEFINITION  heteropolymeric bacterioferritin subunit Ftn [Acinetobacter sp.
            YQ_14].
ACCESSION   WP_392471219
VERSION     WP_392471219.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. YQ_14
  ORGANISM  Acinetobacter sp. YQ_14
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Yao,H., Alli,S., Liu,L., Soldano,A., Cooper,A., Fontenot,L.,
            Verdin,D., Battaile,K.P., Lovell,S. and Rivera,M.
  TITLE     The crystal structure of Acinetobacter baumannii bacterioferritin
            reveals a heteropolymer of bacterioferritin and ferritin subunits
  JOURNAL   Sci Rep 14 (1), 18242 (2024)
   PUBMED   39107474
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Walsh,B.J.C., Wang,J., Edmonds,K.A., Palmer,L.D., Zhang,Y.,
            Trinidad,J.C., Skaar,E.P. and Giedroc,D.P.
  TITLE     The Response of Acinetobacter baumannii to Hydrogen Sulfide Reveals
            Two Independent Persulfide-Sensing Systems and a Connection to
            Biofilm Regulation
  JOURNAL   mBio 11 (3), e01254-20 (2020)
   PUBMED   32576676
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: BlastRule
            Evidence Accession :: NBR016891
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Acinetobacter sp. YQ_14"
                     /db_xref="taxon:3367236"
     gene            1..154
                     /gene="ftn"
     Protein         1..154
                     /product="heteropolymeric bacterioferritin subunit Ftn"
                     /calculated_mol_wt=17823
     Region          3..154
                     /region_name="Bacterioferritin"
                     /note="ferritin-like diiron-binding domain; cd00907"
                     /db_xref="CDD:153099"
     Site            order(15,23,30,45,52,56)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:153099"
     Site            order(17..18,20..21,25,51,54,92..93,96,100,126..127)
                     /site_type="active"
                     /note="ferroxidase pore [active]"
                     /db_xref="CDD:153099"
     Site            order(18,25,51,54,93,100,127,130)
                     /site_type="other"
                     /note="ferroxidase diiron center [ion binding]"
                     /db_xref="CDD:153099"
ORIGIN      
        1 mrgnpevidy lnmliggela ardqylihsr myedwglgki yeridhemqe eashadaiir
       61 rvlflgaqpn mnredinvgt dvvsclkadl aleyhvrekl atgiklceek gdyisrdmlr
      121 qqlsdteedh tywlekqlrl ieliglqnyi qsqi
//
LOCUS       WP_392471547             229 aa            linear   BCT 20-JAN-2025
DEFINITION  Ig-like domain-containing protein [Sphingobacterium cellulitidis].
ACCESSION   WP_392471547
VERSION     WP_392471547.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Fraser,J.S., Yu,Z., Maxwell,K.L. and Davidson,A.R.
  TITLE     Ig-like domains on bacteriophages: a tale of promiscuity and deceit
  JOURNAL   J Mol Biol 359 (2), 496-507 (2006)
   PUBMED   16631788
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Bork,P., Holm,L. and Sander,C.
  TITLE     The immunoglobulin fold. Structural classification, sequence
            patterns and common core
  JOURNAL   J Mol Biol 242 (4), 309-320 (1994)
   PUBMED   7932691
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475235
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..229
                     /product="Ig-like domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=26393
     Region          <39..>166
                     /region_name="YjdB"
                     /note="Uncharacterized conserved protein YjdB, contains
                     Ig-like domain [General function prediction only];
                     COG5492"
                     /db_xref="CDD:444243"
ORIGIN      
        1 maidksfpfl iilfissiqs scvkkdelle dnklqeyrfd qkslelhvgn tiqitskgki
       61 sawksskkfv gtieddgtft ahhigktkis akiddknhsl eikvipnitd ipepvsfygk
      121 tknritslek rkviidkndv lsydtnsdli etmyylfqgg katyavlkfk mlektnldyl
      181 lkfyeeryey lgltknnhyf tdekkkrlia vsikppftal ysaykeked
//
LOCUS       WP_392471777             513 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HAL/PAL/TAL family ammonia-lyase [Acinetobacter].
ACCESSION   WP_392471777
VERSION     WP_392471777.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Turner,N.J.
  TITLE     Ammonia lyases and aminomutases as biocatalysts for the synthesis
            of alpha-amino and beta-amino acids
  JOURNAL   Curr Opin Chem Biol 15 (2), 234-240 (2011)
   PUBMED   21131229
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Louie,G.V., Bowman,M.E., Moffitt,M.C., Baiga,T.J., Moore,B.S. and
            Noel,J.P.
  TITLE     Structural determinants and modulation of substrate specificity in
            phenylalanine-tyrosine ammonia-lyases
  JOURNAL   Chem Biol 13 (12), 1327-1338 (2006)
   PUBMED   17185228
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Baedeker,M. and Schulz,G.E.
  TITLE     Autocatalytic peptide cyclization during chain folding of histidine
            ammonia-lyase
  JOURNAL   Structure 10 (1), 61-67 (2002)
   PUBMED   11796111
REFERENCE   4  (residues 1 to 513)
  AUTHORS   Schwede,T.F., Retey,J. and Schulz,G.E.
  TITLE     Crystal structure of histidine ammonia-lyase revealing a novel
            polypeptide modification as the catalytic electrophile
  JOURNAL   Biochemistry 38 (17), 5355-5361 (1999)
   PUBMED   10220322
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..513
                     /product="HAL/PAL/TAL family ammonia-lyase"
                     /EC_number="4.3.1.-"
                     /GO_function="GO:0016841 - ammonia-lyase activity
                     [Evidence IEA]"
                     /GO_process="GO:0170035 - L-amino acid catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56254
     Region          3..507
                     /region_name="HutH"
                     /note="Histidine ammonia-lyase [Amino acid transport and
                     metabolism]; COG2986"
                     /db_xref="CDD:442225"
ORIGIN      
        1 mvkptlvvge qalsiedvva varqeyqvvl pestawrdli qrgadfldql lldegviygv
       61 ttgygdsclv eipmhqvnel plhlsrfhgc glgenldlit aravvvtrlc slargysgvs
      121 ltllerlvwm lneniipvip segsvgasgd ltplsyiaga lvgerdvyaq gqivpiaqvy
      181 aekalqpitl rpkeglalmn gtavmtaiac lnykkaeqia lastlvtaln vlalegnpsh
      241 fdevlfaqkp hqgqqqiaqh lrewlnsevq tahqsprlqd ryslrcaphi vgvfedsktw
      301 lrqfieneln ssndnplidp vnlrvlhggh fygghiaqam dslkimiani adlmdrqiaq
      361 lvdhkmnhgl arnltgatte rlplnhgfka vqigvsawta ealkqtlaas ifsrstechn
      421 qdkvsmgtia ardatrvitl tqqvlaalcc asvqaihlkg mvtelsptlt afvewtlqsf
      481 alleedrplq telqqiidrf dnfellnqfq vna
//
LOCUS       WP_392471812             259 aa            linear   BCT 20-JAN-2025
DEFINITION  transglutaminase family protein [Acinetobacter sp. YQ_14].
ACCESSION   WP_392471812
VERSION     WP_392471812.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. YQ_14
  ORGANISM  Acinetobacter sp. YQ_14
            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 12090973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Acinetobacter sp. YQ_14"
                     /db_xref="taxon:3367236"
     Protein         1..259
                     /product="transglutaminase family protein"
                     /calculated_mol_wt=29782
     Region          3..79
                     /region_name="Bact_transglu_N"
                     /note="Bacterial transglutaminase-like N-terminal region;
                     pfam08379"
                     /db_xref="CDD:462455"
     Region          <129..212
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mklmvnhqth yrytqiarns vqsikmmpqs srhqtienwh isvpgeysck rdafnnlwit
       61 atqrhdyryl timaqgivel fdtelgffei dvspmlflqr tamthcdlmm fdfaqsivki
      121 kdrqhlills ekilqqmpyq pestsvttaa idafyagqgv cqdhahvfia mcralqipar
      181 yvsgylydqn qphlashawa eafienewyc fdisnqiftp qnhiyvavgr dyldvapvrg
      241 vreqggvesm msvvqvlac
//
LOCUS       WP_392476281             367 aa            linear   BCT 20-JAN-2025
DEFINITION  PDDEXK nuclease domain-containing protein [Salmonella enterica].
ACCESSION   WP_392476281
VERSION     WP_392476281.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 367)
  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 10008845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..367
                     /product="PDDEXK nuclease domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42239
     Region          1..345
                     /region_name="YhcG"
                     /note="Predicted nuclease of restriction endonuclease-like
                     (RecB) superfamily, DUF1016 family [General function
                     prediction only]; COG4804"
                     /db_xref="CDD:443832"
ORIGIN      
        1 mtnptlapqs deyqqihngi vqlldtartq tvrsintimt atywemgrri vefeqggear
       61 aaygeqlidr lsqdlsqryk rgfsasnlwq fkkfylyfqk ieilqtvsge slhlaqlaks
      121 fplpwsayvr llsvknpdar tfyeketlrn gwsvrqldrq iatqfyertl lshdksamlq
      181 qpapaepnil peqairdpfi leflnlkdey sesdledall shlmdfmlel gddfafvgrq
      241 rrlriddswf rvdllffhrr lrclllvdlk vgkfsysdag qmnmylnyak ehwtmpgenp
      301 pvglvlcagk gageahyalt glpntimase ykvqlpdekl ltdelirsqt mletqltrgg
      361 srttekn
//
LOCUS       WP_392477022             492 aa            linear   BCT 20-JAN-2025
DEFINITION  type I restriction-modification system subunit M [Nostoc sp. C110].
ACCESSION   WP_392477022
VERSION     WP_392477022.1
KEYWORDS    RefSeq.
SOURCE      Nostoc sp. C110
  ORGANISM  Nostoc sp. C110
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Nostoc.
REFERENCE   1  (residues 1 to 492)
  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   2  (residues 1 to 492)
  AUTHORS   Youell,J. and Firman,K.
  TITLE     Mechanistic insight into Type I restriction endonucleases
  JOURNAL   Front Biosci (Landmark Ed) 17 (6), 2122-2139 (2012)
   PUBMED   22652768
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Sistla,S. and Rao,D.N.
  TITLE     S-Adenosyl-L-methionine-dependent restriction enzymes
  JOURNAL   Crit Rev Biochem Mol Biol 39 (1), 1-19 (2004)
   PUBMED   15121719
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Murray,N.E.
  TITLE     Type I restriction systems: sophisticated molecular machines (a
            legacy of Bertani and Weigle)
  JOURNAL   Microbiol Mol Biol Rev 64 (2), 412-434 (2000)
   PUBMED   10839821
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114514
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Nostoc sp. C110"
                     /db_xref="taxon:3349876"
     Protein         1..492
                     /product="type I restriction-modification system subunit
                     M"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=55496
     Region          6..130
                     /region_name="HsdM_N"
                     /note="HsdM N-terminal domain; pfam12161"
                     /db_xref="CDD:463478"
     Region          142..394
                     /region_name="HsdM"
                     /note="Type I restriction-modification system, DNA
                     methylase subunit [Defense mechanisms]; COG0286"
                     /db_xref="CDD:440055"
ORIGIN      
        1 mitgemkskv drlwttfwnn gisnplsvie qisyllfikr lddlelgkek kaqrldrpvs
       61 nptfsayqqr crwsyfknlt dseemlrivr deafpfiktl gataaesayv rhmkdavfli
      121 anpallsnvv gqidqipmed rdtkgdlyey mlsklttagt ngqfrtprhi ikmmvdlmap
      181 gpreiicdpa cgtagflvaa aeylrelkds drnlvlnapg nwehfnqemf hgfdfdgtml
      241 rigsmnlmlh gienpkiear dslsedhagi teaftlilan ppfkgsleks tiakdltkvi
      301 sttktellfi alflrllkig graaviepdg vlfgsstahk kmrevlveeh kldgvismps
      361 gvfkpyagvs tavliftktg aggtdyvwfy dmeadglsld dkrqpveend ipdllqrwka
      421 rnpeqdtdrt gkaffvskee ikgngydlsi nrykeieyke vkyeppkvil qklrdledei
      481 radldtleel lg
//
LOCUS       WP_392477093             355 aa            linear   BCT 20-JAN-2025
DEFINITION  PDDEXK nuclease domain-containing protein [Nostoc sp. C110].
ACCESSION   WP_392477093
VERSION     WP_392477093.1
KEYWORDS    RefSeq.
SOURCE      Nostoc sp. C110
  ORGANISM  Nostoc sp. C110
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Nostoc.
REFERENCE   1  (residues 1 to 355)
  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 10008845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Nostoc sp. C110"
                     /db_xref="taxon:3349876"
     Protein         1..355
                     /product="PDDEXK nuclease domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40870
     Region          9..338
                     /region_name="YhcG"
                     /note="Predicted nuclease of restriction endonuclease-like
                     (RecB) superfamily, DUF1016 family [General function
                     prediction only]; COG4804"
                     /db_xref="CDD:443832"
ORIGIN      
        1 mtdslfpelt nyhtflnmlk qrvrtaqira alavnqelvv lywqigreil qrqqddgwgt
       61 kvierlakdl kqefpdikgf srtnllymra faeaypdesf vhqlggqipw rhncvlldrv
      121 kapeqrvwyi qqtiqngwsr ailemqiesr lyerqgsavt nfsqtlpkpq sdlaqqlikd
      181 pynfdfltlg keaqerdler alverirdfl lelgtgfsfv gsqyplevsg qeyrldllfy
      241 hltlrcyvii dlkmvefqpe fsgkmnfyvs avnailrhpd dqptigiilc ksknktvael
      301 alqgmtqpig vsthqigqev peqlkgilpt veqlemelnt vaaeleaqkd srldm
//
LOCUS       WP_392477337             339 aa            linear   BCT 20-JAN-2025
DEFINITION  PDDEXK nuclease domain-containing protein [Nostoc sp. C110].
ACCESSION   WP_392477337
VERSION     WP_392477337.1
KEYWORDS    RefSeq.
SOURCE      Nostoc sp. C110
  ORGANISM  Nostoc sp. C110
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Nostoc.
REFERENCE   1  (residues 1 to 339)
  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 10008845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Nostoc sp. C110"
                     /db_xref="taxon:3349876"
     Protein         1..339
                     /product="PDDEXK nuclease domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39349
     Region          1..335
                     /region_name="YhcG"
                     /note="Predicted nuclease of restriction endonuclease-like
                     (RecB) superfamily, DUF1016 family [General function
                     prediction only]; COG4804"
                     /db_xref="CDD:443832"
ORIGIN      
        1 msnpisdnyr hllmeiqqri rsaqyealka vnreminlyw digqiivtqq qgaswgksvv
       61 eqlakdlqte fpgisgfsaa nlwrmrlfye syvnneklap mvreigwshn lvivekckdd
      121 lerefyirmt rkfgwtknvl ihqienqtye ktllnqtnfd ktvpaeirnq lklavkdeyt
      181 fdfleladeh serqleqail trvepflqem ggifafigsq yrleideeey fidillyhrr
      241 lkclvaielk ignflpeyvg kmqfylavld dtvklpdenp sigiilcksk qrtiveyalk
      301 esnkpigvgt yqvvstlpqe lknqlpapeq vakllegve
//
LOCUS       WP_392478808             863 aa            linear   BCT 20-JAN-2025
DEFINITION  caspase family protein [Nostoc sp. C110].
ACCESSION   WP_392478808
VERSION     WP_392478808.1
KEYWORDS    RefSeq.
SOURCE      Nostoc sp. C110
  ORGANISM  Nostoc sp. C110
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Nostoc.
REFERENCE   1  (residues 1 to 863)
  AUTHORS   Van Opdenbosch,N. and Lamkanfi,M.
  TITLE     Caspases in Cell Death, Inflammation, and Disease
  JOURNAL   Immunity 50 (6), 1352-1364 (2019)
   PUBMED   31216460
REFERENCE   2  (residues 1 to 863)
  AUTHORS   Tsiatsiani,L., Van Breusegem,F., Gallois,P., Zavialov,A., Lam,E.
            and Bozhkov,P.V.
  TITLE     Metacaspases
  JOURNAL   Cell Death Differ 18 (8), 1279-1288 (2011)
   PUBMED   21597462
REFERENCE   3  (residues 1 to 863)
  AUTHORS   Zhang,J.H., Zhang,Y. and Herman,B.
  TITLE     Caspases, apoptosis and aging
  JOURNAL   Ageing Res Rev 2 (4), 357-366 (2003)
   PUBMED   14522240
REFERENCE   4  (residues 1 to 863)
  AUTHORS   Salvesen,G.S.
  TITLE     Caspases and apoptosis
  JOURNAL   Essays Biochem 38, 9-19 (2002)
   PUBMED   12463158
REFERENCE   5  (residues 1 to 863)
  AUTHORS   Villa,P., Kaufmann,S.H. and Earnshaw,W.C.
  TITLE     Caspases and caspase inhibitors
  JOURNAL   Trends Biochem Sci 22 (10), 388-393 (1997)
   PUBMED   9357314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..863
                     /organism="Nostoc sp. C110"
                     /db_xref="taxon:3349876"
     Protein         1..863
                     /product="caspase family protein"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=98131
     Region          1..238
                     /region_name="COG4249"
                     /note="Uncharacterized conserved protein, contains caspase
                     domain [General function prediction only]"
                     /db_xref="CDD:443391"
     Region          <355..>534
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
ORIGIN      
        1 mvkvalligv seyepglnpl pgavkdveam qqvllhpemg gftetdimvl knpqrqdmee
       61 aienlfahrq kddllvlffs ghgikddtgr lflatrttrk tprgdlirss avaasvvhes
      121 msrsrskrqv vildscfsga faeglsakdd gsvnireqlg gegravltss sstqysfeqq
      181 gsdlsiytry liegittgaa dldedgvvsi delheyasrk vreiqptmkp eiytsregfk
      241 irltkvpqgd pkqkyrkeva ryssrgdvsf vgrktldalr srlglseiea taiedemlav
      301 arqefkqklq qyerdfseal qqqvaltedd lnmlrlnlqq ilglrnedtm pieaqvkari
      361 eaykqhlqly rrslakamrq eyplsqptrh qlqqmqqewq lkdedlaaie nslraeveay
      421 rqklqqfeqa firavqqeyp lseakhnqlw qqqqllglka edidpitari taereayqqk
      481 lqqyeqvliq aiehqyplte eireelrryq hvleirdeev arieekvvrq ieanhpelnp
      541 dlrwkvretv hrsepptdqg qikglhpnal ssftntnlpd qlhkepvqks etlpykknks
      601 flietiskia nlenklfisi aamfvfgfli sliynnfikd ydyqptkses rdkaiaevin
      661 fqtdkpqytk gqnillnwti arplllaqvq iagsaddgta ygepitykfn qgnitdpklq
      721 klctqqnqql qcrniplvan ktgyfafeik afpnnesski sskkaeskte ilpkpfkivs
      781 ftingseqpn ivlnegesat lswrvegeni qvrllpygnd vkpvgsikla vnqafppeig
      841 lqvndisgkq qpqqrgfait vik
//
LOCUS       WP_392478975             349 aa            linear   BCT 20-JAN-2025
DEFINITION  PDDEXK nuclease domain-containing protein [Vibrio plantisponsor].
ACCESSION   WP_392478975
VERSION     WP_392478975.1
KEYWORDS    RefSeq.
SOURCE      Vibrio plantisponsor
  ORGANISM  Vibrio plantisponsor
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 349)
  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 10008845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Vibrio plantisponsor"
                     /db_xref="taxon:664643"
     Protein         1..349
                     /product="PDDEXK nuclease domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40829
     Region          9..327
                     /region_name="YhcG"
                     /note="Predicted nuclease of restriction endonuclease-like
                     (RecB) superfamily, DUF1016 family [General function
                     prediction only]; COG4804"
                     /db_xref="CDD:443832"
ORIGIN      
        1 msfeptehnl lsdikqvieq arsqvkqtvn aamvqaywqi grlivedeqq gqtraeygka
       61 qlkqlsdlla sdygkgfdvt nlrnmrrfyl afekretvsl elswshynal srienptare
      121 wyqqeavsqn wsvralerqi gtlyyerlla skdkalveqe aeqktqplat takeylrdpy
      181 ildflnlqdk tyqesdleqa iisnlqqfll elgkgfafve rqqrirfdde dfyidlvfyn
      241 fklkcfllvd lkigklkhqd vgqmdtyvrl yddqykgsdd nptiglvlcs ekseavvkys
      301 vlteqkqlfa akylpylpse eelkrelqre rqqaqqaltq qqksnndee
//
LOCUS       WP_392479613             155 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio plantisponsor].
ACCESSION   WP_392479613
VERSION     WP_392479613.1
KEYWORDS    RefSeq.
SOURCE      Vibrio plantisponsor
  ORGANISM  Vibrio plantisponsor
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 155)
  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 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   3  (residues 1 to 155)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 155)
  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   5  (residues 1 to 155)
  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   6  (residues 1 to 155)
  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 10007405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Vibrio plantisponsor"
                     /db_xref="taxon:664643"
     Protein         1..155
                     /product="AraC 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:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17324
     Region          <1..155
                     /region_name="SbmC"
                     /note="DNA gyrase inhibitor GyrI/SbmC [Replication,
                     recombination and repair]; COG3449"
                     /db_xref="CDD:442672"
ORIGIN      
        1 mqvriveftp rkvaiythqg apeqlmnsve nfvawrketg lspiaisdtf gipysdpnet
       61 dnkhfrfdia gsveedipdn rfgvvngmlt ggkcavlrhy gsldlisqtv yklyknwlpt
      121 sgeqpsgkpc ffhylniapd tdknalqtdv ylplk
//
LOCUS       WP_392482611              69 aa            linear   BCT 20-JAN-2025
DEFINITION  TOBE domain-containing protein [Nostoc sp. C110].
ACCESSION   WP_392482611
VERSION     WP_392482611.1
KEYWORDS    RefSeq.
SOURCE      Nostoc sp. C110
  ORGANISM  Nostoc sp. C110
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Nostoc.
REFERENCE   1  (residues 1 to 69)
  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 10007583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Nostoc sp. C110"
                     /db_xref="taxon:3349876"
     Protein         1..69
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=7106
     Region          <1..69
                     /region_name="MopI"
                     /note="Molybdopterin-binding protein MopI [Coenzyme
                     transport and metabolism]; COG3585"
                     /db_xref="CDD:442804"
ORIGIN      
        1 meisarnslk givkkvvpgt vnteiileia pgvelvsiit kssaeklglt egkeayavik
       61 ssdvivave
//
LOCUS       WP_392482930             373 aa            linear   BCT 20-JAN-2025
DEFINITION  THUMP domain-containing class I SAM-dependent RNA methyltransferase
            [Nostoc sp. C110].
ACCESSION   WP_392482930
VERSION     WP_392482930.1
KEYWORDS    RefSeq.
SOURCE      Nostoc sp. C110
  ORGANISM  Nostoc sp. C110
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Nostoc.
REFERENCE   1  (residues 1 to 373)
  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 373)
  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 373)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     THUMP--a predicted RNA-binding domain shared by 4-thiouridine,
            pseudouridine synthases and RNA methylases
  JOURNAL   Trends Biochem Sci 26 (4), 215-217 (2001)
   PUBMED   11295541
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Nostoc sp. C110"
                     /db_xref="taxon:3349876"
     Protein         1..373
                     /product="THUMP domain-containing 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:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=41577
     Region          1..370
                     /region_name="RlmL"
                     /note="23S rRNA G2445 N2-methylase RlmL [Translation,
                     ribosomal structure and biogenesis]; COG0116"
                     /db_xref="CDD:439886"
ORIGIN      
        1 mnyfatvarg letlaaqele qlgahsvepg fcgvafegdr tllyrvnlwa rlpfrilvdi
       61 defpcqnadd lyrgiqtidw vnyltpdmtl avnvtgknqh lnhshftslq vknaivdqqq
      121 eklgersnve lhepdvrinv hierdfctvk ldssgnslhr rgyrpavgaa plkeslaaal
      181 iqlsgwqpnq mfydplcgsg tlpleaslka lniapglfre sfgfenwldf dlsllekllq
      241 eakdsqldtl papiwgsdrd eniieqainn aqncgvdnhv wfsqmeladv vapadsgilf
      301 cnppygerlg rdsdlgafyk llgdvlkqrf kgwtafvlsg nkelsqsigl ksskriavyn
      361 galpcqlmky ely
//
LOCUS       WP_392482935             342 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Nostoc sp. C110].
ACCESSION   WP_392482935
VERSION     WP_392482935.1
KEYWORDS    RefSeq.
SOURCE      Nostoc sp. C110
  ORGANISM  Nostoc sp. C110
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Nostoc.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Nostoc sp. C110"
                     /db_xref="taxon:3349876"
     Protein         1..342
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37453
     Region          36..338
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mnikrrefit tcglatlatq ipaftaqgkp pspniirkps rlqvgdtvgl iapagivdak
       61 dieaaqqsls qlglkvklgk hildrygyla gkdsdraqdv nlmfsdrtik aiipmrggwg
      121 cnrilpllny slirshpkii igysdittll lainarskmi tfhgpvatst wnqftvdyfk
      181 rilfnaeavt mqnlnpsevr metiapgket gkliggnlsv lsamvgspyl pswnksilfv
      241 eeigedvyri drmltqlkta gilnqitgfi fgqctkcslg depsftlmqv lqqhilplgi
      301 pawygsmigh ikdkftlpig veveidaelg iirmlqsavs lv
//
LOCUS       WP_392483262             148 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Salmonella enterica].
ACCESSION   WP_392483262
VERSION     WP_392483262.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (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   2  (residues 1 to 148)
  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 148)
  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 148)
  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 10009358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..148
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16588
     Region          33..148
                     /region_name="HigA"
                     /note="Antitoxin component HigA of the HigAB
                     toxin-antitoxin module, contains an N-terminal HTH domain
                     [Defense mechanisms]; COG5499"
                     /db_xref="CDD:444250"
ORIGIN      
        1 mrthrqmdat sakkivdtfs davksvplmg edrndneyrr alalveflvd hndlenplfe
       61 llcariseye khapefkaln qhlektppgv svlrtlmdqy glkaadlane lgsksnvsni
      121 lngrraltvn hikaltqrfk lpadafie
//
LOCUS       WP_392484434             604 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sensor histidine kinase [Pseudomonas].
ACCESSION   WP_392484434
VERSION     WP_392484434.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 604)
  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 604)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20493667
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..604
                     /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=67212
     Region          39..268
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          230..590
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 miakptpprr prwrslalla lclapllwpl hhlaeryyqq elasqnrqtl dlyvanllgt
       61 lhryetlpqi lgdlpalrsv ladpfrleav tnanrllkgi vqqtgaevmy lmdvsgntla
      121 asnwdkhdsf vgrnfafrpy fneamaghlg rffgqgttsa krgyffaaav rdrerivgvl
      181 vvkvdldhte tlwgrtpeql lltdhngvvi ltsrpdwrfr atralsdaer qaiiaiqpyp
      241 tqapqplvlg pdawitqtrd iketgwqvsi laprmlvdrs vqtvmaigag tllvamllag
      301 lvmqrrrhyi dridfearar qelekrvaer tadleglntr lkravleren aqqeavraqd
      361 elvqagklsv lgtmsasish elnqplaair syaenaeill dhqrtedarg nlkligeltg
      421 rmasiiahlr afarrdrhap esvalqpald dalallakrr ramavelird lpeatlwvqa
      481 getrlrqvlg nllanaldal tekanprrlw lsaeqrddcv ylyirdngpg fsrqalehak
      541 epffttktrt qglglglaic eslmralgge lllanhpegg alltlqlrka apgatlpnse
      601 dpsa
//
LOCUS       WP_392485678             312 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Pseudomonas sp. CJQ_11].
ACCESSION   WP_392485678
VERSION     WP_392485678.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. CJQ_11
  ORGANISM  Pseudomonas sp. CJQ_11
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Pseudomonas sp. CJQ_11"
                     /db_xref="taxon:3367169"
     Protein         1..312
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=33169
     Region          22..308
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mkcvepsalp lrkaiapdac favvapagpa rldvhkatrw faergyrcrv ypgatqaegy
       61 lagadaqrlq dlhdafrdps idavlcmrgg ygsmrlldrl dfellqnhpk pligysdita
      121 lhaalyrhtg misfhgamln adllggkqtp tessllaqls ghlaagdpit hpaqfplntv
      181 ipglasgpll ggnlsmlgat lgtlaeldtq gcilfiedvn eplyrvdrll tqlrlagkle
      241 gikgvlvgdf agitaaalap llrdtfgplg vpvlagwrsg hcdpniclpl garvtldser
      301 qrlvleqalf qa
//
LOCUS       WP_392486196             366 aa            linear   BCT 20-JAN-2025
DEFINITION  GerAB/ArcD/ProY family transporter [Haloimpatiens sporogenes].
ACCESSION   WP_392486196
VERSION     WP_392486196.1
KEYWORDS    RefSeq.
SOURCE      Haloimpatiens sporogenes
  ORGANISM  Haloimpatiens sporogenes
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Haloimpatiens.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Haloimpatiens sporogenes"
                     /db_xref="taxon:3298609"
     Protein         1..366
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=41790
     Region          6..366
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 mdvesknnfi tkyqlfativ vtitgvgffs ypsamartvg tdgwivtils gfivyvlmyl
       61 ihkivrlndy gslhmilenn ygkifsiiia ivfsvlniml isvgmrvfae vikmyllekt
      121 pvefivmimi itgsilvrge ldvlikfnev sfwimfipiy lvmfllckgt dftnvlpvfn
      181 nsiykymegi altafsfegf eiaylvlphv kqkrnisktl fksvvfvvvf ysaitiltvc
      241 tfgvqqtksl iwstltmiks inipesfveq wegivmvfwi ifyittfvni yyfsadtlek
      301 tfkfgdikfs sillvpiiyl talypenlge vynlfndisf vlpifalafi iifplvisli
      361 krrggk
//
LOCUS       WP_392486705             310 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase family protein [Haloimpatiens
            sporogenes].
ACCESSION   WP_392486705
VERSION     WP_392486705.1
KEYWORDS    RefSeq.
SOURCE      Haloimpatiens sporogenes
  ORGANISM  Haloimpatiens sporogenes
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Haloimpatiens.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Vollmer,W., Joris,B., Charlier,P. and Foster,S.
  TITLE     Bacterial peptidoglycan (murein) hydrolases
  JOURNAL   FEMS Microbiol Rev 32 (2), 259-286 (2008)
   PUBMED   18266855
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436722
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Haloimpatiens sporogenes"
                     /db_xref="taxon:3298609"
     Protein         1..310
                     /product="N-acetylmuramoyl-L-alanine amidase family
                     protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34204
     Region          88..310
                     /region_name="AmiC"
                     /note="N-acetylmuramoyl-L-alanine amidase [Cell
                     wall/membrane/envelope biogenesis]; COG0860"
                     /db_xref="CDD:440621"
ORIGIN      
        1 mrntkkkvmp liilctlsll sffyynyskq knmatvpkte kkssaiknnk akdsskwkdk
       61 gkteeeikse ekskaeeksk vkeksensai ksekedakvs kaakkvvvid pghanrsnls
      121 keplapnsne mkikdgggaa gvttktpeyk inmqvslelk sflekkgyiv kltktkdses
      181 lgnverakig ndynaalvir ihadssnnre akgasmlvpa pintntkkiy eksnsygnti
      241 ltslvtevgm knrgviqrnd mtgfnwsqvp vvlvemgfls ntgeekllcs kdyqikiana
      301 lsngidkalr
//
LOCUS       WP_392488379             276 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: isocitrate lyase/PEP mutase family protein
            [unclassified Pseudomonas].
ACCESSION   WP_392488379
VERSION     WP_392488379.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789410
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..276
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29042
     Region          7..275
                     /region_name="PrpB"
                     /note="2-Methylisocitrate lyase and related enzymes, PEP
                     mutase family [Carbohydrate transport and metabolism];
                     COG2513"
                     /db_xref="CDD:442003"
ORIGIN      
        1 mdvqtlraea fkalherdga fvipnpwdag sakllaglgf ealattsagl afslgrpdae
       61 galslddtld nageivdata lpvaadleng fgdlpedcaq tilraaevgl vggsiedasg
      121 rsdapiydfg lavervraav qavrslpfpf tlcaraenll hgrmdlddti lrlqayaeag
      181 advlyapglr tveevravvq avaprpvnvl mgmagvqlnv nqlqdlgvrr isvgsslara
      241 algafhraal eirdegtfgy geqampfaql ndlfrr
//
LOCUS       WP_392488536             310 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: KpsF/GutQ family sugar-phosphate isomerase
            [unclassified Pseudomonas].
ACCESSION   WP_392488536
VERSION     WP_392488536.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Meredith,T.C. and Woodard,R.W.
  TITLE     Characterization of Escherichia coli D-arabinose 5-phosphate
            isomerase encoded by kpsF: implications for group 2 capsule
            biosynthesis
  JOURNAL   Biochem J 395 (2), 427-432 (2006)
   PUBMED   16390329
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Meredith,T.C. and Woodard,R.W.
  TITLE     Identification of GutQ from Escherichia coli as a D-arabinose
            5-phosphate isomerase
  JOURNAL   J Bacteriol 187 (20), 6936-6942 (2005)
   PUBMED   16199563
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002722
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..310
                     /product="KpsF/GutQ family sugar-phosphate isomerase"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33290
     Region          1..306
                     /region_name="GutQ"
                     /note="D-arabinose 5-phosphate isomerase GutQ
                     [Carbohydrate transport and metabolism, Cell
                     wall/membrane/envelope biogenesis]; COG0794"
                     /db_xref="CDD:440557"
ORIGIN      
        1 mnhlsiakea liaqaqavtq lsdrldgefq savelilgcq grtvvcgmgk sgligqkmva
       61 tfastgtpsf flhpaeafhg dlgmlkpidv lilisysget eeliklipsl ksfgnkiiam
      121 tgngkstlak hadiwldisv erevcpnnla pttstlatma mgdalavali eaiqfkpmdf
      181 aryhpggslg rklltrvrdv mhspapvvtp ttsfhdcllv mtrsrlgltv vmdeeklvgi
      241 vtdgdlrral lenegvvret vaqfmtpkph tiledsqlse aesymldnki ralavtdaeg
      301 svvgvveifd
//
LOCUS       WP_392492456             520 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type I restriction-modification system subunit M
            [unclassified Pseudomonas].
ACCESSION   WP_392492456
VERSION     WP_392492456.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 520)
  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   2  (residues 1 to 520)
  AUTHORS   Youell,J. and Firman,K.
  TITLE     Mechanistic insight into Type I restriction endonucleases
  JOURNAL   Front Biosci (Landmark Ed) 17 (6), 2122-2139 (2012)
   PUBMED   22652768
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Sistla,S. and Rao,D.N.
  TITLE     S-Adenosyl-L-methionine-dependent restriction enzymes
  JOURNAL   Crit Rev Biochem Mol Biol 39 (1), 1-19 (2004)
   PUBMED   15121719
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Murray,N.E.
  TITLE     Type I restriction systems: sophisticated molecular machines (a
            legacy of Bertani and Weigle)
  JOURNAL   Microbiol Mol Biol Rev 64 (2), 412-434 (2000)
   PUBMED   10839821
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114514
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..520
                     /product="type I restriction-modification system subunit
                     M"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=57612
     Region          7..135
                     /region_name="HsdM_N"
                     /note="HsdM N-terminal domain; pfam12161"
                     /db_xref="CDD:463478"
     Region          143..391
                     /region_name="HsdM"
                     /note="Type I restriction-modification system, DNA
                     methylase subunit [Defense mechanisms]; COG0286"
                     /db_xref="CDD:440055"
ORIGIN      
        1 mvtgdvekrl wavadqlwan tglrpgefsv pvlgliflry aekmyaaaee klgpigsggr
       61 rkvskddyla egviflpeka rfsylqtlte gdviglaine amkaveeenv dlkgalprny
      121 vqlgntvlle likllgpvdl sgdafgkvye yflgnfalke gqkggvfytp esivklivei
      181 iepfhgrifd pacgsggmfa qsadfvkrhh ktameeisif gtekeqvtvn lnkmnlavhg
      241 lsgdvriant yyedpheavt rdggrfdfvm anppfnvsgv dkerlegdlr fpfgvpktdn
      301 anylwiqlfy aslnkngrag fvmansagda rgseqvirqk liesgavdvi vsvgsnffyt
      361 vtlpctlwff drakerdaer adkvlfidar hiyrqidrah rdfkpeqief lanivrlyrg
      421 eapeldqgsa ellaerglgk gyvdvpglck vasreliesq gwslnpgryv gaaarevedv
      481 dfterleela eelevlnaes relelriadn iavifdgasa
//
LOCUS       WP_392492964             134 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Pseudomonas].
ACCESSION   WP_392492964
VERSION     WP_392492964.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (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   2  (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   3  (residues 1 to 134)
  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 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 10009358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..134
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14568
     Region          15..133
                     /region_name="HigA"
                     /note="Antitoxin component HigA of the HigAB
                     toxin-antitoxin module, contains an N-terminal HTH domain
                     [Defense mechanisms]; COG5499"
                     /db_xref="CDD:444250"
ORIGIN      
        1 mnalvktavd hwafvaplls tpkdeaaydt lvaaldelqe itgydeghpl dglvqcmanl
       61 isdfdkkhfp ipeatgvevl rsimeehgvs qrdlpeigsq stvsqllsgk rklnvrqira
      121 ladrfgvnpn vflg
//
LOCUS       WP_392494334             298 aa            linear   BCT 20-JAN-2025
DEFINITION  aldo/keto reductase [Leclercia sp. GLN_9].
ACCESSION   WP_392494334
VERSION     WP_392494334.1
KEYWORDS    RefSeq.
SOURCE      Leclercia sp. GLN_9
  ORGANISM  Leclercia sp. GLN_9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 298)
  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 298)
  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   3  (residues 1 to 298)
  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   4  (residues 1 to 298)
  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 10790928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Leclercia sp. GLN_9"
                     /db_xref="taxon:3367184"
     Protein         1..298
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /calculated_mol_wt=33357
     Region          3..298
                     /region_name="YdhF"
                     /note="Predicted oxidoreductase YdhF [General function
                     prediction only]; COG4989"
                     /db_xref="CDD:444013"
ORIGIN      
        1 mvqritlapq gpefsrfvmg ywrlmdwnms aqqlvsfiee hldlgvttvd hadiyggyqc
       61 eaafgealkr spalrqrmei vtkcgiatta kaehalghyi tdrdhiissa eqsltnlatd
      121 yldlllihrp dplmdadeva eaflalhqsg kvrhfgvsnf tpaqfallqs rlpftlatnq
      181 veispvhqpl lldgtldqlq qlrirpmaws clgggrlfnd eafqplrdel aqvaqelnae
      241 tieqviyawi lrlpsqplpi igsgkiervr salaaeqlam trqqwfrirk aalgydvp
//
LOCUS       WP_392494897             264 aa            linear   BCT 20-JAN-2025
DEFINITION  S1 family peptidase [Leclercia sp. GLN_9].
ACCESSION   WP_392494897
VERSION     WP_392494897.1
KEYWORDS    RefSeq.
SOURCE      Leclercia sp. GLN_9
  ORGANISM  Leclercia sp. GLN_9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Leclercia.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Querino Lima Afonso,M., da Fonseca,N.J. Jr., de Oliveira,L.C.,
            Lobo,F.P. and Bleicher,L.
  TITLE     Coevolved Positions Represent Key Functional Properties in the
            Trypsin-Like Serine Proteases Protein Family
  JOURNAL   J Chem Inf Model 60 (2), 1060-1068 (2020)
   PUBMED   31895561
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Waldner,B.J., Kraml,J., Kahler,U., Spinn,A., Schauperl,M.,
            Podewitz,M., Fuchs,J.E., Cruciani,G. and Liedl,K.R.
  TITLE     Electrostatic recognition in substrate binding to serine proteases
  JOURNAL   J Mol Recognit 31 (10), e2727 (2018)
   PUBMED   29785722
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Pelc,L.A., Chen,Z., Gohara,D.W., Vogt,A.D., Pozzi,N. and Di Cera,E.
  TITLE     Why Ser and not Thr brokers catalysis in the trypsin fold
  JOURNAL   Biochemistry 54 (7), 1457-1464 (2015)
   PUBMED   25664608
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Perona,J.J. and Craik,C.S.
  TITLE     Evolutionary divergence of substrate specificity within the
            chymotrypsin-like serine protease fold
  JOURNAL   J Biol Chem 272 (48), 29987-29990 (1997)
   PUBMED   9374470
REFERENCE   5  (residues 1 to 264)
  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 10595581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Leclercia sp. GLN_9"
                     /db_xref="taxon:3367184"
     Protein         1..264
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=28857
     Region          22..186
                     /region_name="Trypsin_2"
                     /note="Trypsin-like peptidase domain; pfam13365"
                     /db_xref="CDD:433149"
ORIGIN      
        1 mnsisqnink stvrivcdng tgtgfyfcfv nkdipdqfhp fivtnkhvie gakearlrlk
       61 lkpndqgidy fdlsiqnlsn tfighpdpnv dltifplsss yaelskrgle ldpfffcdas
      121 isgtrnltpv ediymtgypn glwdevnnkp itrkgitasd vnldwngkkq fmidmacfgg
      181 ssgspvyvmt egsfssgdgi aigkrfvflg vlfagpqfrv dgsidivevp tstvaisrtd
      241 immnlgivik aaellkfktl igia
//
LOCUS       WP_392495382              55 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Morganella].
ACCESSION   WP_392495382
VERSION     WP_392495382.1
KEYWORDS    RefSeq.
SOURCE      Morganella
  ORGANISM  Morganella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
REFERENCE   1  (residues 1 to 55)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 55)
  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 55)
  AUTHORS   Tyrrell,R., Verschueren,K.H., Dodson,E.J., Murshudov,G.N., Addy,C.
            and Wilkinson,A.J.
  TITLE     The structure of the cofactor-binding fragment of the LysR family
            member, CysB: a familiar fold with a surprising subunit arrangement
  JOURNAL   Structure 5 (8), 1017-1032 (1997)
   PUBMED   9309218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444001
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..55
                     /organism="Morganella"
                     /db_xref="taxon:581"
     Protein         1..55
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=5794
     Region          10..52
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
ORIGIN      
        1 mllsgklckf vsvvenrsik kaseqmnvta saisqgissl ekelgmklik ktvva
//
LOCUS       WP_392497257             279 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: FTR1 family iron permease [Morganella].
ACCESSION   WP_392497257
VERSION     WP_392497257.1
KEYWORDS    RefSeq.
SOURCE      Morganella
  ORGANISM  Morganella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Grosse,C., Scherer,J., Koch,D., Otto,M., Taudte,N. and Grass,G.
  TITLE     A new ferrous iron-uptake transporter, EfeU (YcdN), from
            Escherichia coli
  JOURNAL   Mol Microbiol 62 (1), 120-131 (2006)
   PUBMED   16987175
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Stearman,R., Yuan,D.S., Yamaguchi-Iwai,Y., Klausner,R.D. and
            Dancis,A.
  TITLE     A permease-oxidase complex involved in high-affinity iron uptake in
            yeast
  JOURNAL   Science 271 (5255), 1552-1557 (1996)
   PUBMED   8599111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430572
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Morganella"
                     /db_xref="taxon:581"
     Protein         1..279
                     /product="FTR1 family iron permease"
                     /GO_component="GO:0033573 - high-affinity iron permease
                     complex [Evidence IEA]"
                     /GO_function="GO:0005381 - iron ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0034755 - iron ion transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31093
     Region          1..278
                     /region_name="FTR1"
                     /note="High-affinity Fe2+/Pb2+ permease [Inorganic ion
                     transport and metabolism]; COG0672"
                     /db_xref="CDD:440436"
ORIGIN      
        1 mgqvlfvvwr esfeallvvg iiyawikqhp daaagrrylw ggvalgvals lflalliygv
       61 fnvlddsgqt yfmigmslfa aalivqmvyw mqqhsaslks gieqemndsa rqhswwgalf
      121 ivaiaiareg seivvflsgi vmglnadtlw sftgevvagi avaaltlwlf lftyrkiawk
      181 wffritgivl lflacslllk gteeivnllt ehdielndfl iyplwdttnl lddtsttgsf
      241 laslfgyraq piglsvitfv vywlviialf crkgkkhad
//
LOCUS       WP_392497480             167 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Pseudomonas sp. zbq_18].
ACCESSION   WP_392497480
VERSION     WP_392497480.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. zbq_18
  ORGANISM  Pseudomonas sp. zbq_18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 167)
  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 10789902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Pseudomonas sp. zbq_18"
                     /db_xref="taxon:3367251"
     Protein         1..167
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=18633
     Region          16..167
                     /region_name="YafK"
                     /note="Murein L,D-transpeptidase YafK [Cell
                     wall/membrane/envelope biogenesis]; COG3034"
                     /db_xref="CDD:442269"
ORIGIN      
        1 mrwllalllv tlatpslass aptlrgkaid kvlvvkserk lhlmgrgevl ksyrislgkv
       61 ptgakvsegd lrtpegfywi dwrktsdkfn lsmhisypna rdaanarkkg vsaggmimih
      121 gtplddeype wffstldwte gciamrnadm revwnlvqdg tlieirp
//
LOCUS       WP_392497521             274 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Pseudomonas sp.
            zbq_18].
ACCESSION   WP_392497521
VERSION     WP_392497521.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. zbq_18
  ORGANISM  Pseudomonas sp. zbq_18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789410
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Pseudomonas sp. zbq_18"
                     /db_xref="taxon:3367251"
     Protein         1..274
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28521
     Region          6..274
                     /region_name="PrpB"
                     /note="2-Methylisocitrate lyase and related enzymes, PEP
                     mutase family [Carbohydrate transport and metabolism];
                     COG2513"
                     /db_xref="CDD:442003"
ORIGIN      
        1 msaqrergea fqrlhqgegl lilpnpwdag sakmlahlgf qalattsagl afslgrcdae
       61 gavsrdeala naraivaatp lpvaadleng ygdspevcae tislaaeigl vggsiedasg
      121 raadpiypld lavariraaa eavraldvpf tltaraenfl ngradlddti rrlvayaeag
      181 advlyapglt treqiravvs avaprpvnvl vgspslhlsm aelidlgvkr vsvgsnlarv
      241 aygeffiaag elargsliam geampfdein elfr
//
LOCUS       WP_392497759             230 aa            linear   BCT 20-JAN-2025
DEFINITION  4'-phosphopantetheinyl transferase family protein [Pseudomonas sp.
            zbq_18].
ACCESSION   WP_392497759
VERSION     WP_392497759.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. zbq_18
  ORGANISM  Pseudomonas sp. zbq_18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459479
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Pseudomonas sp. zbq_18"
                     /db_xref="taxon:3367251"
     Protein         1..230
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=25067
     Region          32..230
                     /region_name="EntD"
                     /note="4'-phosphopantetheinyl transferase EntD
                     (siderophore biosynthesis) [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2977"
                     /db_xref="CDD:442216"
ORIGIN      
        1 mpamhmppfc qlhndlpall pgtclvqarf dpaqlqaedf grcnvppvrg vakrqaehla
       61 grlcarsalh glcgqalipg rdadgvpiwp agisgsishg hgqaaalval srdwrslgid
      121 leqqlppera trlaaeiltt nelqrsggls paefaqrvtl tfslkeslfk alfplvrrrf
      181 yfhdaellev dgeqarlrll ldlhhewpsg seldghyrsq adsllslvai
//
LOCUS       WP_392497908             262 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Pseudomonas sp.
            zbq_18].
ACCESSION   WP_392497908
VERSION     WP_392497908.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. zbq_18
  ORGANISM  Pseudomonas sp. zbq_18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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   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 262)
  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 10007860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Pseudomonas sp. zbq_18"
                     /db_xref="taxon:3367251"
     Protein         1..262
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28541
     Region          4..103
                     /region_name="CadC1"
                     /note="DNA-binding winged helix-turn-helix (wHTH) domain
                     [Transcription]; COG3710"
                     /db_xref="CDD:442924"
ORIGIN      
        1 mstyvinrli hfdneafvly aatapedslr igaiasrclt qlldakgeiv skrdlmngaw
       61 gafglevtdn slaqtirqlr valdklqpdh elivtvprig yklgeslvel ldqpppppla
      121 aahpastpap tetastrhad ssprwqprdl llglaalagw vllfllpgll rptalperpf
      181 aeqrmedidg vrihledmpa salqpdnrql asharqlaqa lgmngqvlhl yrfadqyrsl
      241 dllcqgtlta adsqclgvqa hd
//
LOCUS       WP_392498345             534 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Pseudomonas sp. zbq_18].
ACCESSION   WP_392498345
VERSION     WP_392498345.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. zbq_18
  ORGANISM  Pseudomonas sp. zbq_18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 534)
  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 11459492
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Pseudomonas sp. zbq_18"
                     /db_xref="taxon:3367251"
     Protein         1..534
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=58626
     Region          11..503
                     /region_name="YcbB"
                     /note="Murein L,D-transpeptidase YcbB/YkuD [Cell
                     wall/membrane/envelope biogenesis]; COG2989"
                     /db_xref="CDD:442228"
ORIGIN      
        1 mfkkrasyps ivlltlplva haievpvgql plqaapaplc aplessldds tklllndfyr
       61 lregrpawrd hdqrqhlreq lqqladdgld padyplrdgd ddcaelqasn sylqallhlr
      121 ggrlpasrqe tiwhapeepr adprlavlsi asatsdiasa faaarpqlaq yrllrsayav
      181 arlqpaghwq plpagpllkp ggndgrmpll rarlaaegyl aaplaegthf dpasvtalqs
      241 fqerhglkpd gilgpaslne lnvdaltrrg qlranlerlr rmaddlsqak vvinvaaael
      301 hviengselw rtrtqvgrpe ratpllasri vrltlnptwt vpptilredk lpairadlsy
      361 ldqhemsvyd rsgnrldpeq vdwnspgail lrqaagsrnp lgrvalrfdn pfsvylhdtp
      421 sqalfdkspr ffssgcvrve avdnllawll ppeeltavqs rlangktqsy rlstaaplli
      481 aywtveadas galrylpdiy nrdpaliaal aapsarhiag qdpaaytqea vtwk
//
LOCUS       WP_392498390             267 aa            linear   BCT 20-JAN-2025
DEFINITION  transglutaminase family protein [Pseudomonas sp. zbq_18].
ACCESSION   WP_392498390
VERSION     WP_392498390.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. zbq_18
  ORGANISM  Pseudomonas sp. zbq_18
            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 12090973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Pseudomonas sp. zbq_18"
                     /db_xref="taxon:3367251"
     Protein         1..267
                     /product="transglutaminase family protein"
                     /calculated_mol_wt=29802
     Region          3..79
                     /region_name="Bact_transglu_N"
                     /note="Bacterial transglutaminase-like N-terminal region;
                     pfam08379"
                     /db_xref="CDD:462455"
     Region          <105..214
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mrlsirhdtt ynyddqvras iqylrltpqd sarqhviswr ldlprpvraq rdpygnilhv
       61 ltldepheal vigargqvei dsrcesekdt rsplpylrft rltqsddalr hfaetgsggr
      121 rdrdglvalm hglheqmpyt pgatqvdsta aeafagragv cqdhthafla carslgvpsr
      181 yvsgylyted sghlashawa eawlgdgwys fdvtnqlarp erhlklavgl dyldacpvrg
      241 mrrggggeqm harvnvaalm qtqqqqq
//
LOCUS       WP_392498736             287 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Pseudomonas sp.
            zbq_18].
ACCESSION   WP_392498736
VERSION     WP_392498736.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. zbq_18
  ORGANISM  Pseudomonas sp. zbq_18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789410
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Pseudomonas sp. zbq_18"
                     /db_xref="taxon:3367251"
     Protein         1..287
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31120
     Region          8..286
                     /region_name="PrpB"
                     /note="2-Methylisocitrate lyase and related enzymes, PEP
                     mutase family [Carbohydrate transport and metabolism];
                     COG2513"
                     /db_xref="CDD:442003"
ORIGIN      
        1 mskashhdlr vrfrallnsn acyhtasvfd pmsariaadl gfevgilggs vaslqvlaap
       61 dfalitlsef aeqatrigrv arlpfiadad hgygnalnvm rtvmelerag vsaltiedtl
      121 lpaqfgrkst dlisvdegvg kiraalearf dpqlaiiart naavldvdev vsrtlayesa
      181 gadgicmvgi rdfdhleqia shlsvplmlv sygnpelrdd arlaqlgvri vvdghaayfa
      241 aikatydclr eqrgiaasdl natelthkyt qpedyivwar eymnvke
//
LOCUS       WP_392499222             381 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Pseudomonas sp. zbq_18].
ACCESSION   WP_392499222
VERSION     WP_392499222.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. zbq_18
  ORGANISM  Pseudomonas sp. zbq_18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 381)
  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 381)
  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 381)
  AUTHORS   ter Beek,J., 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 381)
  AUTHORS   Igarashi,K., Ito,K. and Kashiwagi,K.
  TITLE     Polyamine uptake systems in Escherichia coli
  JOURNAL   Res Microbiol 152 (3-4), 271-278 (2001)
   PUBMED   11421274
REFERENCE   5  (residues 1 to 381)
  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   6  (residues 1 to 381)
  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 11430824
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Pseudomonas sp. zbq_18"
                     /db_xref="taxon:3367251"
     Protein         1..381
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0019808 - polyamine binding [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:0015846 - polyamine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42076
     Region          18..378
                     /region_name="PotD"
                     /note="Spermidine/putrescine-binding periplasmic protein
                     [Amino acid transport and metabolism]; COG0687"
                     /db_xref="CDD:440451"
ORIGIN      
        1 mdrkdfikql rswqngsisr rdflgktglg mamavtaanm pgllfsnsaf agekgsigdr
       61 valatwpnyh nadnlaafae qtgarvqmnv fgsneemlak lqaggsgwdv fvptnytist
      121 yvelgliepl dlsrlpnfdp aafekrfmeq gvvdgklyav pknwgttgfv ydseqiksrp
      181 ttwkefwela kgeatgrvmv hdyqltaign alkafgysfn sldpkelada eklllevkph
      241 lfainsdyqp smrsgdawms mcwtgdgsql hrdmaqmqfv lgreggelws dffaipksve
      301 rrdaayafin flldpqvnkl eveahgypsg dkrvdallpk emledpimyp aaellsalef
      361 gaaatltspa raelmarfka a
//
LOCUS       WP_392499899             275 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. zbq_18].
ACCESSION   WP_392499899
VERSION     WP_392499899.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. zbq_18
  ORGANISM  Pseudomonas sp. zbq_18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (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   5  (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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Pseudomonas sp. zbq_18"
                     /db_xref="taxon:3367251"
     Protein         1..275
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30502
     Region          37..275
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <165..275
                     /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 mprintresh qqqafwrdpa lpfvesrrac hsracyrahs hptfsigavd agrsvfsgag
       61 eqpialhpgm lvfvpasrvh acnpapdasw syqmlhldaa wlqatraeya ttltdepiri
      121 ldesglyrqf crlndvlfst adtaeketal iefigdqdlt hlagihlplp dnvsrerlqp
      181 alrrlaktpg advpldelas lagmsryqli rafrrstglt phawqlnqri nlarehmrag
      241 adiatvaqdl gfadqahlqr vfkahtgvtp gryra
//
LOCUS       WP_392500692             221 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Photobacterium
            damselae].
ACCESSION   WP_392500692
VERSION     WP_392500692.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (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   2  (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   3  (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 10007860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..221
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=25056
     Region          8..92
                     /region_name="CadC1"
                     /note="DNA-binding winged helix-turn-helix (wHTH) domain
                     [Transcription]; COG3710"
                     /db_xref="CDD:442924"
ORIGIN      
        1 miiykhgndf fepqksayta deittklsas etkilqylid nngeivsret lleigwpeki
       61 vvpnslnvai anlrkafktk neiiitikga gftvakntfv kqqqrineee lrqeesetid
      121 llqvttsdtr teindrqesp hngvyiqrik vnwlractgv lvllavlwvs lwlsswqtpp
      181 cvafknqkvc gniellkpeq lpkdkegtly idmmgkihaq n
//
LOCUS       WP_392501912             302 aa            linear   BCT 20-JAN-2025
DEFINITION  aldo/keto reductase [Photobacterium damselae].
ACCESSION   WP_392501912
VERSION     WP_392501912.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 302)
  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 302)
  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   3  (residues 1 to 302)
  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   4  (residues 1 to 302)
  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 10790928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..302
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /calculated_mol_wt=34052
     Region          8..302
                     /region_name="YdhF"
                     /note="Predicted oxidoreductase YdhF [General function
                     prediction only]; COG4989"
                     /db_xref="CDD:444013"
ORIGIN      
        1 miskekcapn gpllsefiqg ywrlaswnms veeriafinq hlelgissvd hadiygdyrc
       61 etlfgealhr spslrsqlei itkcdiklcs ehypnrkinh ydtsfehits sveaslrnlq
      121 tdyidmllih rpdalmnade vahafsslkd qgkvlhfgvs nftpsqfsll qsrldfqlvt
      181 nqieinpmnf gvvddgtldl lqqlrirpma wsclaggelf ngqteqavrl rsellaiaqe
      241 vgaesvdqvi yawvrqlpsk plaiigsgki ervrsalasq kiqltreqwy riwvaskghg
      301 vp
//
LOCUS       WP_392502494             328 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase LdtE [Kluyvera intermedia].
ACCESSION   WP_392502494
VERSION     WP_392502494.1
KEYWORDS    RefSeq.
SOURCE      Kluyvera intermedia
  ORGANISM  Kluyvera intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Kluyvera.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Monton Silva,A., Otten,C., Biboy,J., Breukink,E., VanNieuwenhze,M.,
            Vollmer,W. and den Blaauwen,T.
  TITLE     The Fluorescent D-Amino Acid NADA as a Tool to Study the
            Conditional Activity of Transpeptidases in Escherichia coli
  JOURNAL   Front Microbiol 9, 2101 (2018)
   PUBMED   30233559
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Cava,F., de Pedro,M.A., Lam,H., Davis,B.M. and Waldor,M.K.
  TITLE     Distinct pathways for modification of the bacterial cell wall by
            non-canonical D-amino acids
  JOURNAL   EMBO J 30 (16), 3442-3453 (2011)
   PUBMED   21792174
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Magnet,S., Dubost,L., Marie,A., Arthur,M. and Gutmann,L.
  TITLE     Identification of the L,D-transpeptidases for peptidoglycan
            cross-linking in Escherichia coli
  JOURNAL   J Bacteriol 190 (13), 4782-4785 (2008)
   PUBMED   18456808
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF047955.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Kluyvera intermedia"
                     /db_xref="taxon:61648"
     gene            1..328
                     /gene="ldtE"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
     Protein         1..328
                     /product="L,D-transpeptidase LdtE"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=35236
     Region          1..300
                     /region_name="PRK10260"
                     /note="L,D-transpeptidase; Provisional"
                     /db_xref="CDD:182341"
ORIGIN      
        1 mkraslitls ilsalsafss awavdyplpp ansrlighnq tytvqegdkn lqaiarrfdt
       61 aamlileann tiasspmagt vvtipsqmll pdvpregivv nlaelrlyyf ppgeqmvqvf
      121 pigigqqgle tpemttrvgq kipnptwtpt agirarsler gvtlpavipa gpgnplglfa
      181 lrlaygngey lihgtnapds vglrvssgci rmnapdikal faqvrsgttv rvinepvkys
      241 vepngahyle vhrplspnea qdtqtmkitl ssdfkqfveq tgvseelvtk slarragypm
      301 mvsdskattt tsvlsaqnge assekmmq
//
LOCUS       WP_392503508             247 aa            linear   BCT 20-JAN-2025
DEFINITION  Ig-like domain-containing protein [Kluyvera intermedia].
ACCESSION   WP_392503508
VERSION     WP_392503508.1
KEYWORDS    RefSeq.
SOURCE      Kluyvera intermedia
  ORGANISM  Kluyvera intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Kluyvera.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Fraser,J.S., Yu,Z., Maxwell,K.L. and Davidson,A.R.
  TITLE     Ig-like domains on bacteriophages: a tale of promiscuity and deceit
  JOURNAL   J Mol Biol 359 (2), 496-507 (2006)
   PUBMED   16631788
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Halaby,D.M., Poupon,A. and Mornon,J.
  TITLE     The immunoglobulin fold family: sequence analysis and 3D structure
            comparisons
  JOURNAL   Protein Eng 12 (7), 563-571 (1999)
   PUBMED   10436082
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Smith,D.K. and Xue,H.
  TITLE     Sequence profiles of immunoglobulin and immunoglobulin-like domains
  JOURNAL   J Mol Biol 274 (4), 530-545 (1997)
   PUBMED   9417933
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Bork,P., Holm,L. and Sander,C.
  TITLE     The immunoglobulin fold. Structural classification, sequence
            patterns and common core
  JOURNAL   J Mol Biol 242 (4), 309-320 (1994)
   PUBMED   7932691
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475235
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Kluyvera intermedia"
                     /db_xref="taxon:61648"
     Protein         1..247
                     /product="Ig-like domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=25694
     Region          <4..>247
                     /region_name="YjdB"
                     /note="Uncharacterized conserved protein YjdB, contains
                     Ig-like domain [General function prediction only];
                     COG5492"
                     /db_xref="CDD:444243"
ORIGIN      
        1 maqcatsnek lfgraivlev adgcadtvpl eadwkalaag tsksfdfspn svtsdaddtq
       61 gfvenivtna dftlsfegev rkqdkldqyg vgkfikyftd eikaarqpsl wvrmqfgpvt
      121 fvgymiinal ssdggtndiv tfstefkvad astvevsenn vvavtgvtlt patstgaaag
      181 tstftvtvap agatnkeftv sstdpakata tkagnlvtvn rvasgsaqiv vntedgnfaa
      241 ihtvtit
//
LOCUS       WP_392504600             143 aa            linear   BCT 20-JAN-2025
DEFINITION  JAB domain-containing protein [Providencia stuartii].
ACCESSION   WP_392504600
VERSION     WP_392504600.1
KEYWORDS    RefSeq.
SOURCE      Providencia stuartii
  ORGANISM  Providencia stuartii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Providencia.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Attaiech,L., Granadel,C., Claverys,J.P. and Martin,B.
  TITLE     RadC, a misleading name?
  JOURNAL   J Bacteriol 190 (16), 5729-5732 (2008)
   PUBMED   18556794
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Ambroggio,X.I., Rees,D.C. and Deshaies,R.J.
  TITLE     JAMM: a metalloprotease-like zinc site in the proteasome and
            signalosome
  JOURNAL   PLoS Biol 2 (1), E2 (2004)
   PUBMED   14737182
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449512
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Providencia stuartii"
                     /db_xref="taxon:588"
     Protein         1..143
                     /product="JAB domain-containing protein"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=15837
     Region          <9..142
                     /region_name="RadC"
                     /note="DNA repair protein RadC, contains a
                     helix-hairpin-helix DNA-binding motif [Replication,
                     recombination and repair]; COG2003"
                     /db_xref="CDD:441606"
ORIGIN      
        1 mkqkihevre ylsqqlyrte qlsspkdted flavhlgdkd qevfavifln aqnqviqyae
       61 mfngtinyts ifpreiaklg lklnaaniic ahnhpsgttt psesdivatr tlkeamklld
      121 itlidhiiva ggktlslaer glv
//
LOCUS       WP_392506624             306 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas putida].
ACCESSION   WP_392506624
VERSION     WP_392506624.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 306)
  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 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   3  (residues 1 to 306)
  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   4  (residues 1 to 306)
  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 306)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..306
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34272
     Region          35..187
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          215..294
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mttatstept lelqrlelae linrhagepy gpasaiddly lvrhtenvrs vptlaqpalc
       61 ilaqgskslf lgdeqyaydp lhymvvsvtl plsavrldas penpslglrm dldpaeisql
      121 iaesgpmlvp nrpsgrglyv ertdaallda llrllrlldt prdiamlapl frreilyrll
      181 rgpqgyrlye ialansqthr vcqaitwlnn nyqqplried larevnlsts tlhhrfkavt
      241 smsplqyqkq lrlqearrlm lndgleaava ayrvgyenps qfsreysrly gappirdvar
      301 lratav
//
LOCUS       WP_392507314             283 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Naumannella halotolerans].
ACCESSION   WP_392507314
VERSION     WP_392507314.1
KEYWORDS    RefSeq.
SOURCE      Naumannella halotolerans
  ORGANISM  Naumannella halotolerans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Naumannella.
REFERENCE   1  (residues 1 to 283)
  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 283)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Naumannella halotolerans"
                     /db_xref="taxon:993414"
     Protein         1..283
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29413
     Region          2..283
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mpirptleli daaarqnvgi gafnvihles aealvagaed aglpvilqis encvkyhggq
       61 ltpilaatse iarqaavdva lhldhaenes laiagiesgf gsvmydgsrl pheanlattq
      121 rvvalaherg asveaelgev agkdlpgrsa hepgvltdpd qarafvaetg vdalavavgs
      181 rhamternav ldlelitrlr daagvplvlh gssgvddatl vaaiaagmtk invsthlnqv
      241 ftssirrslt edpglvdsrk ylgpariama aetarllrlf rga
//
LOCUS       WP_392507352             659 aa            linear   BCT 20-JAN-2025
DEFINITION  type I restriction-modification system subunit M [Klebsiella sp.
            zjy_5].
ACCESSION   WP_392507352
VERSION     WP_392507352.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella sp. zjy_5
  ORGANISM  Klebsiella sp. zjy_5
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 659)
  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   2  (residues 1 to 659)
  AUTHORS   Youell,J. and Firman,K.
  TITLE     Mechanistic insight into Type I restriction endonucleases
  JOURNAL   Front Biosci (Landmark Ed) 17 (6), 2122-2139 (2012)
   PUBMED   22652768
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 659)
  AUTHORS   Sistla,S. and Rao,D.N.
  TITLE     S-Adenosyl-L-methionine-dependent restriction enzymes
  JOURNAL   Crit Rev Biochem Mol Biol 39 (1), 1-19 (2004)
   PUBMED   15121719
REFERENCE   4  (residues 1 to 659)
  AUTHORS   Murray,N.E.
  TITLE     Type I restriction systems: sophisticated molecular machines (a
            legacy of Bertani and Weigle)
  JOURNAL   Microbiol Mol Biol Rev 64 (2), 412-434 (2000)
   PUBMED   10839821
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114514
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Klebsiella sp. zjy_5"
                     /db_xref="taxon:3367256"
     Protein         1..659
                     /product="type I restriction-modification system subunit
                     M"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=73249
     Region          9..136
                     /region_name="HsdM_N"
                     /note="HsdM N-terminal domain; pfam12161"
                     /db_xref="CDD:463478"
     Region          155..420
                     /region_name="HsdM"
                     /note="Type I restriction-modification system, DNA
                     methylase subunit [Defense mechanisms]; COG0286"
                     /db_xref="CDD:440055"
ORIGIN      
        1 mmttnissla sliwsvadll rgdfkqsqyg riilpftvlr rlecvlaptk aqvlatvest
       61 kalpdlardk lllnasgqaf yntsplelgk lgenyvgdnl dayvrafskd arevfehfnf
      121 easitlleda dllykvsrsf atvdlspeav dnyhmglvfe elirrfaess netagehftp
      181 rdivrlttsl vfsgdddala kpgvvrsiyd ptagtggfls cgmeylheln paarlatfgq
      241 elnpesyaic kadmlikgqd isniklgntl sddqlrfnrf dyclsnppfg vdwkkvekqv
      301 raeadqqgfn grfgpglprv sdgsllflmh liskmqqpgt dstgsrigii lngsplftgg
      361 agsgeseirr yilendllda lvalptdmfy ntgiatyvwv lsnhkpaerk gkvllinasd
      421 mhspmrkslg skrkylsdev lkeivslysr yedssiakif pstafgyrri tverplklal
      481 yphdterlan lqadkawakl ddslqsaila altnftddkl lsrdkfkkqf tkalgevklp
      541 apafkllvnh laeqddaaev cetkgepean pdlrdnenvp lgediheyfq revlphvpda
      601 widtgktdpl dgqvgivgye ipfnrhfyqy qpprdlaeid adldavarei mqllaevhs
//
LOCUS       WP_392508750             348 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Naumannella halotolerans].
ACCESSION   WP_392508750
VERSION     WP_392508750.1
KEYWORDS    RefSeq.
SOURCE      Naumannella halotolerans
  ORGANISM  Naumannella halotolerans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Naumannella.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Naumannella halotolerans"
                     /db_xref="taxon:993414"
     Protein         1..348
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37674
     Region          1..294
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mpdpttpell mvvdgnsllh rsfhalaasn arnragepiw airglltqlv vaaerigpqr
       61 iivgfddpdr nwrrerwphy kaqraeklps ldsqlllara vldelgvqvv cpeaqeaddv
      121 lasvsaragt eggqcvvvts drdafclins htrvlrving gvdaspvltp erlqlmigig
      181 pqqypdfaal rgdpsdnlpg vrgigpkrav tlltevgdge qifadaesgg elitaalsrt
      241 waqrladpta rqvwqhnrqv mqmrhdldlg pltdrgrlpl saaavrqvll dlglpatart
      301 aarvlaedpn aetesattds lgwqgraqwq garrslpalp vnlqptlf
//
LOCUS       WP_392508886             374 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Naumannella halotolerans].
ACCESSION   WP_392508886
VERSION     WP_392508886.1
KEYWORDS    RefSeq.
SOURCE      Naumannella halotolerans
  ORGANISM  Naumannella halotolerans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Naumannella.
REFERENCE   1  (residues 1 to 374)
  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 12830887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Naumannella halotolerans"
                     /db_xref="taxon:993414"
     Protein         1..374
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=40679
     Region          63..129
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          148..215
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          264..373
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(327..328,331,345..348,350)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkgnvcalav lasaalvftg capntpstdt avvapapavv esstptptpt qsptpsaspt
       61 pttepallak gdsgdevkdl qarlkqiaww ngkisgeydd qtvsaikgfq akrelpetge
      121 vdqktldalh dmtreptdde knnrltpgka ilkdgdsgdk vkdlqarlkq ldwftedvtg
      181 nygsvtvaav kgfqakreip etgevdqrtl dklnemttep tdeelnnkpk kedkddekss
      241 dseskqgeka eglpdecmtg kvmciskksn klwwlkdgvv sisfdvrfgt detptregtf
      301 yvdrmskdhv snmyhtpmpy amffsrgqav hyssdfaarg ynggshgcvn vrdkgkvael
      361 ysqvsigtkv yvys
//
LOCUS       WP_392508954             675 aa            linear   BCT 20-JAN-2025
DEFINITION  DNA gyrase/topoisomerase IV subunit B [Naumannella halotolerans].
ACCESSION   WP_392508954
VERSION     WP_392508954.1
KEYWORDS    RefSeq.
SOURCE      Naumannella halotolerans
  ORGANISM  Naumannella halotolerans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Naumannella.
REFERENCE   1  (residues 1 to 675)
  AUTHORS   Tari,L.W., Trzoss,M., Bensen,D.C., Li,X., Chen,Z., Lam,T.,
            Zhang,J., Creighton,C.J., Cunningham,M.L., Kwan,B., Stidham,M.,
            Shaw,K.J., Lightstone,F.C., Wong,S.E., Nguyen,T.B., Nix,J. and
            Finn,J.
  TITLE     Pyrrolopyrimidine inhibitors of DNA gyrase B (GyrB) and
            topoisomerase IV (ParE). Part I: Structure guided discovery and
            optimization of dual targeting agents with potent, broad-spectrum
            enzymatic activity
  JOURNAL   Bioorg Med Chem Lett 23 (5), 1529-1536 (2013)
   PUBMED   23352267
REFERENCE   2  (residues 1 to 675)
  AUTHORS   Gadelle,D., Filee,J., Buhler,C. and Forterre,P.
  TITLE     Phylogenomics of type II DNA topoisomerases
  JOURNAL   Bioessays 25 (3), 232-242 (2003)
   PUBMED   12596227
REFERENCE   3  (residues 1 to 675)
  AUTHORS   Wang,J.C.
  TITLE     Cellular roles of DNA topoisomerases: a molecular perspective
  JOURNAL   Nat Rev Mol Cell Biol 3 (6), 430-440 (2002)
   PUBMED   12042765
REFERENCE   4  (residues 1 to 675)
  AUTHORS   Champoux,J.J.
  TITLE     DNA topoisomerases: structure, function, and mechanism
  JOURNAL   Annu Rev Biochem 70, 369-413 (2001)
   PUBMED   11395412
REFERENCE   5  (residues 1 to 675)
  AUTHORS   Roca,J.
  TITLE     The mechanisms of DNA topoisomerases
  JOURNAL   Trends Biochem Sci 20 (4), 156-160 (1995)
   PUBMED   7770916
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..675
                     /organism="Naumannella halotolerans"
                     /db_xref="taxon:993414"
     Protein         1..675
                     /product="DNA gyrase/topoisomerase IV subunit B"
                     /EC_number="5.6.2.2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003918 - DNA topoisomerase type II
                     (double strand cut, ATP-hydrolyzing) activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006265 - DNA topological change [Evidence
                     IEA]"
                     /calculated_mol_wt=73554
     Region          3..675
                     /region_name="GyrB"
                     /note="DNA gyrase/topoisomerase IV, subunit B
                     [Replication, recombination and repair]; COG0187"
                     /db_xref="CDD:439957"
ORIGIN      
        1 mlvlegleav rkrpamyigs tdtrglmhcl weiidnavde aligygekit ialnadgslt
       61 vadtargipv dieprtglsg vevvytklha ggkfgtgsyn aagglhgvga svvnalsarl
      121 dvevdrnsat wgmsfhrgtp gtfdgpgpda rftpggslqk lkrakkgvtg trvtwwpdpl
      181 ifgpdmslap eelsnrarqt sflipglelq itdargaepv tethrhdggi sefceflapd
      241 qpvtevlrlq gndsftetvp mldeetgaml ptdvdrdvei dialrwgtgy dtvtrsfvni
      301 iatpkggthv ngyeraltkt vnkalsstrl lkngeeitkd daleglttvv tvrlaepqfe
      361 gqtkevlgtp avsrlvakvv eselggflss nkaadkqqsr vvlekvaaam rtrltaraqk
      421 eaqrrktale ssslpaklrd crsndvdrte lfivegdsal gtakdarsse fqalfpirgk
      481 ilntqrasig dmlknaecan liqvvgagsg rsfdldaary gkiifmadad adgahircll
      541 atlffrymrp lidagriyta vpplhrfelk npkkgqekyl ytysdneyqr taaeltkkgi
      601 rfddpqrykg lgemdasqla ettmdprhrl lrritvddga aaeqvfemlm gndvvprkef
      661 lvdgayrlda eqida
//
LOCUS       WP_392508890             552 aa            linear   BCT 20-JAN-2025
DEFINITION  peptide ABC transporter substrate-binding protein [Naumannella
            halotolerans].
ACCESSION   WP_392508890
VERSION     WP_392508890.1
KEYWORDS    RefSeq.
SOURCE      Naumannella halotolerans
  ORGANISM  Naumannella halotolerans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Naumannella.
REFERENCE   1  (residues 1 to 552)
  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 552)
  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 552)
  AUTHORS   ter Beek,J., 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 552)
  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 552)
  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 11467924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Naumannella halotolerans"
                     /db_xref="taxon:993414"
     Protein         1..552
                     /product="peptide 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=59980
     Region          42..544
                     /region_name="OppA"
                     /note="ABC-type oligopeptide transport system, periplasmic
                     component [Amino acid transport and metabolism]; COG4166"
                     /db_xref="CDD:443327"
ORIGIN      
        1 mtnrarsttr iaaglaalsl glaacsgggs sdgegdgged ltvtssisqd vdtllpmdan
       61 vgdniavldv iydglvrydp ettepypyla eeitttdnqv wtikikpgtt fhngepvdae
      121 afarawnyaa ygpnamgnny fferiegydd mqgeyeeadd gtvtvdeepa aeelsglevv
      181 dpqtlqvtlt apfvgfdtml gytgffpiaq aclddieact tkpigngpfq veewsqgqsl
      241 tatkyaeytg aetpnydrie wveyaggsew pdfqaglmdl aeapsanftq ayddpalqrv
      301 erptaaltyl sfplyddgpw tdiefrkals maidrqavid avlpgqrvpa dswvmpdgvp
      361 ggvagtcgea ctfnpeaaka aleaaggwpe getmtihlgq deteqelfqa igdqitlnlg
      421 ipyeldptpd ffdrrsnrdf sgpfrsnwfp dyplnenylg pvyasddaee gntnfgyyne
      481 dfnnaiadgd saatldeavt nyqeaerila edfptaplfy tnvvlfhsdr vsnvvidpfs
      541 grakmrllev tg
//
LOCUS       WP_392510315             294 aa            linear   BCT 20-JAN-2025
DEFINITION  heme/hemin ABC transporter substrate-binding protein [Pseudomonas
            sp. TYF_14].
ACCESSION   WP_392510315
VERSION     WP_392510315.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. TYF_14
  ORGANISM  Pseudomonas sp. TYF_14
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Naoe,Y., Nakamura,N., Rahman,M.M., Tosha,T., Nagatoishi,S.,
            Tsumoto,K., Shiro,Y. and Sugimoto,H.
  TITLE     Structural basis for binding and transfer of heme in bacterial
            heme-acquisition systems
  JOURNAL   Proteins 85 (12), 2217-2230 (2017)
   PUBMED   28913898
REFERENCE   2  (residues 1 to 294)
  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   3  (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   4  (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   5  (residues 1 to 294)
  AUTHORS   Ho,W.W., Li,H., Eakanunkul,S., Tong,Y., Wilks,A., Guo,M. and
            Poulos,T.L.
  TITLE     Holo- and apo-bound structures of bacterial periplasmic
            heme-binding proteins
  JOURNAL   J Biol Chem 282 (49), 35796-35802 (2007)
   PUBMED   17925389
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Pseudomonas sp. TYF_14"
                     /db_xref="taxon:3367193"
     Protein         1..294
                     /product="heme/hemin 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=30508
     Region          2..289
                     /region_name="ChuT"
                     /note="ABC-type hemin transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG4558"
                     /db_xref="CDD:443619"
ORIGIN      
        1 mmrrpaafla lcaglvlstq alaaelpqrw vsaggalsew italggeghl vgvdttsqhp
       61 aslkalpsvg yqrqlsaegi lslrpdvlvg teemgpppvl aqirkagvrv elfsskaelp
      121 avdenlrhlg qllgaeqqas alaadyrqrl dalqanvkla qagqqapgvl llvghagakp
      181 liagqgtagd wlldqaggrn laahpgyknf snealaaldp dvivfsdral adeqalqall
      241 kenpalaasr avrekrlvsl dptllvgglg prlpatlqsl aatfypaaqa sfaq
//
LOCUS       WP_392510884             279 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_392510884
VERSION     WP_392510884.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 279)
  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 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   3  (residues 1 to 279)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 279)
  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   5  (residues 1 to 279)
  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   6  (residues 1 to 279)
  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 10007405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..279
                     /product="AraC 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:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31369
     Region          3..279
                     /region_name="SbmC"
                     /note="DNA gyrase inhibitor GyrI/SbmC [Replication,
                     recombination and repair]; COG3449"
                     /db_xref="CDD:442672"
ORIGIN      
        1 mkrfetvlay idshlegdls vialsrianf safhfhrqft aymgvpvsry vqlmrlrraa
       61 hqlvaspatp ileaafgagf espeafaraf krafgmapsa fakapnwqaw savfnvphrs
      121 rsitmqiriv nfaethvaal ehqgppglvs esvarfrqwr mqsgqspvas srtfgipydn
      181 pdttpaqafr favcgeidet vqpndfgvhe rvipagrcav irhtgspdyi getiyplyrd
      241 wlpssneelr dhplffhyls vypetpleqw qtdiyvplk
//
LOCUS       WP_392511176             233 aa            linear   BCT 20-JAN-2025
DEFINITION  4'-phosphopantetheinyl transferase family protein [Pseudomonas sp.
            yb_2].
ACCESSION   WP_392511176
VERSION     WP_392511176.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. yb_2
  ORGANISM  Pseudomonas sp. yb_2
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459479
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Pseudomonas sp. yb_2"
                     /db_xref="taxon:3367218"
     Protein         1..233
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=25416
     Region          33..233
                     /region_name="EntD"
                     /note="4'-phosphopantetheinyl transferase EntD
                     (siderophore biosynthesis) [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2977"
                     /db_xref="CDD:442216"
ORIGIN      
        1 mntlpaccap lqhhwplprp lpgavlvsca fdpahlaadd fqragvlpsa sllrsvakrq
       61 aeylagrvca raalqhldgr dhvpgthedr spiwpagihg sithgkgwaa avvagknscq
      121 glgldqeall ddaraerlmg eiltpaeler ldrrqlgltv tltfslkesl fktlypltrq
      181 rfyfehaevl dwsaeglarl rlltdlspqw qqgaelqgqf clqdghllsl vsv
//
LOCUS       WP_392511897             263 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Photobacterium
            damselae].
ACCESSION   WP_392511897
VERSION     WP_392511897.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
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   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 263)
  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 263)
  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 11448557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..263
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30950
     Region          2..54
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
ORIGIN      
        1 mfsnilkqhr detgltqqel vdnlnayhsc ftkldvvtls rwengktlpp lkkqfivydy
       61 mnklpyiind isllnnsien seinlfetyk knkignissi akliicrnns dikinfntnk
      121 vdtinfiney ndnifiknet lmekiesitw iidndilgtl lhcnhnnslv iffmyaqtdc
      181 iyeyiyryly tkilesklen vvfyvfdddi yqlmkkigge tikstrlskc mvrrlvkfer
      241 idllsnketl gyyhyilgni dqt
//
LOCUS       WP_392513440             350 aa            linear   BCT 20-JAN-2025
DEFINITION  PDDEXK nuclease domain-containing protein [Photobacterium
            damselae].
ACCESSION   WP_392513440
VERSION     WP_392513440.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 350)
  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 10008845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..350
                     /product="PDDEXK nuclease domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40932
     Region          12..338
                     /region_name="YhcG"
                     /note="Predicted nuclease of restriction endonuclease-like
                     (RecB) superfamily, DUF1016 family [General function
                     prediction only]; COG4804"
                     /db_xref="CDD:443832"
ORIGIN      
        1 mttpslppst slldnirtll iegrkqvvla vnstmvhtyw qigrlivede qqgktrakyg
       61 kqvlkslses ltnefgkgfd trnlrnmrqf ylvfpiwnav rtelswthyr tltrienesa
      121 rhwymneaie qnwsaraler qigalyyerl lstqakqqdl qpvideanhk tselaltvkd
      181 ylrdpyifdf lglpnvslqe seleqalidn lqkfllelgk gfafverqqr ivtedgdffi
      241 dlvfynfhlk cfllidlkmh klshqdvgqm dmyvrmyeek krraddnpti glilctdnnr
      301 tvakysvlng seqlfaskym lelpseeelr hqlekerqhl laqrgqidnd
//
LOCUS       WP_392513669             285 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Salmonella
            enterica].
ACCESSION   WP_392513669
VERSION     WP_392513669.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
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   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 285)
  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 10007860
            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="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32399
     Region          32..142
                     /region_name="CadC1"
                     /note="DNA-binding winged helix-turn-helix (wHTH) domain
                     [Transcription]; COG3710"
                     /db_xref="CDD:442924"
ORIGIN      
        1 mscyaatasd ytqwclltls nyvmfwhgnn amlwiindni efnpemnrla slsrpdlnii
       61 lttpasrclr lllenapsvv sqqtffqkvw eedgmvvsan tlyqnisiir rglrtvgene
      121 dtliitvprr gfqiepgvsi mtirkdfaqa iekkgetppr msgrwfkhyv pvlwmtgtfa
      181 vgillgtisw qtvpdkdfyd rytlvettqg chffsrnedi esgsrfasyk smiletgmdc
      241 qkypwvyfps ssrtpavtal icqqpyktrg dtgcvtlffr gvthg
//
LOCUS       WP_392514462             312 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Pseudomonas sp. YQ_13].
ACCESSION   WP_392514462
VERSION     WP_392514462.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. YQ_13
  ORGANISM  Pseudomonas sp. YQ_13
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Pseudomonas sp. YQ_13"
                     /db_xref="taxon:3367235"
     Protein         1..312
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=33009
     Region          10..307
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mycaktfqpt lpaalpanac faivapagaa rldahnasqw fvdrgyrcci ypgalqaqgy
       61 lagpdqqrlq dlhaafadpa idailcmrgg ygsmrlldql dfelirrnpk pligysdita
      121 lhtaiyrhag lvtfhggmln adllgaklpp tessllaqls glvkageqva hpegfaldsv
      181 lpgvasgpll ggnlsmlgat mgtlaeldtq gcilfiedvn eplyrvdrll tqlrlagkle
      241 gikgvlvgdf agittaaltp lledtfaplg vpvlagwrsg hcdpnvclpl garvrldsvq
      301 qtlvleqdlf ra
//
LOCUS       WP_392515424             118 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Pseudomonas sp. FYR_7].
ACCESSION   WP_392515424
VERSION     WP_392515424.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. FYR_7
  ORGANISM  Pseudomonas sp. FYR_7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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   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 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
REFERENCE   4  (residues 1 to 118)
  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 10009358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Pseudomonas sp. FYR_7"
                     /db_xref="taxon:3367174"
     Protein         1..118
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13272
     Region          3..115
                     /region_name="HigA"
                     /note="Antitoxin component HigA of the HigAB
                     toxin-antitoxin module, contains an N-terminal HTH domain
                     [Defense mechanisms]; COG5499"
                     /db_xref="CDD:444250"
ORIGIN      
        1 mnikpirsde dlhaaflrle aifqaepgtp eademevlvt lievyenkyy piqsatplea
       61 ikfcmeqqsl tprdlepyig psgrvsevln gkrrlslsmi rrlheglrip yesllggt
//
LOCUS       WP_392516178             374 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Myroides odoratimimus].
ACCESSION   WP_392516178
VERSION     WP_392516178.1
KEYWORDS    RefSeq.
SOURCE      Myroides odoratimimus
  ORGANISM  Myroides odoratimimus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Myroides.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Myroides odoratimimus"
                     /db_xref="taxon:76832"
     Protein         1..374
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=42095
     Region          52..311
                     /region_name="AccC"
                     /note="Biotin carboxylase [Lipid transport and
                     metabolism]; COG0439"
                     /db_xref="CDD:440208"
ORIGIN      
        1 mkkvlilgtn agqadiieyf kelgwyvysc gfkktgpgve lsdefylvdt tniedlvqla
       61 kklkvdvvys vssdtnitsa tkvseilglp ilvnselinl fnkkdefrcf lnsneistvd
      121 fitidnined nakgllwsvf pcvvkpvdsq gqrgvqlvyk qedlysavke askwaldgkv
      181 iieefldgae istniivqng kilinefsdr ivfendffgl pkghgvpvsy inkeqlelaq
      241 syvvkivekl niidavlyiq mklkdgipki ieiaprldgc hiwrllkayk gfdlrllavk
      301 cllgepites dlgnnynkpa vlefyhlpan tkfdktgfdv nddvlynefr yhqgeeivsi
      361 ngrlevvgyc vytk
//
LOCUS       WP_392518664             312 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Pseudomonas sp. YQ_6].
ACCESSION   WP_392518664
VERSION     WP_392518664.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. YQ_6
  ORGANISM  Pseudomonas sp. YQ_6
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Pseudomonas sp. YQ_6"
                     /db_xref="taxon:3367230"
     Protein         1..312
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32958
     Region          10..307
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mycaktfqpt lpaalpanac faivapagaa rldahkvsqw fvdrgyrchi ypgalqaqgy
       61 lagpdqqrlq dlhaafadpa mdailcmrgg ygsmrlldql dfelirrnpk pligysdita
      121 lhtaiyrhag lvtfhggmln adllgaklpp tessllaqlg ghvrageqva hpagfalgcv
      181 lpgaasglll ggnlsmlgat mgtlaeldtq gcilfiedvn eplyrvdrll tqlrlagkle
      241 gikgvlvgdf agittaaltp lledtfaplg vpvlagwrsg hcdpnvclpl garvtldsvq
      301 qtlvleqdlf ra
//
LOCUS       WP_392518917             585 aa            linear   BCT 20-JAN-2025
DEFINITION  sensor histidine kinase [Pseudomonas sp. FYR_5].
ACCESSION   WP_392518917
VERSION     WP_392518917.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. FYR_5
  ORGANISM  Pseudomonas sp. FYR_5
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 585)
  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 585)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20493667
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Pseudomonas sp. FYR_5"
                     /db_xref="taxon:3367173"
     Protein         1..585
                     /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=64959
     Region          35..286
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          286..579
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mpfsfralrl glitllivlg talsagwamh qakrqamedd akrasqqlgl yanalhtlie
       61 ryralpavla ldpeliaalr gpidegvqna lnhklering aansstlell drtglaiaas
      121 nwrlpssyvg snygfrpyfk qtrsqgsgrf yavgvtsgvp gyflasavnd ehgrflgamv
      181 vklefpeler ewrqgndill vsdargitfi anqdgwryre lqplsgadra elaetrqydk
      241 qplvplqhqv ltrfapystl srvqgpegst eylweslple genwtlhllr kpqvaadgrn
      301 aalgaaavwl slvfavlfvs qrlrlarlrq rsrqelerqv eertrelrta qeglvqsakl
      361 aalgqmsaam aheinqpltt qrmqletlrl lldhgrhdea rqalepleqm ltrmaaltsh
      421 lktfarnspm glrerldlat vvdqalhlle arirseevev alylarpawv rgdairleqv
      481 linllhnald amidksykrl eiriepdgel wrlsvldsgg giaeadlpki fdpffttkpv
      541 geglglglai sygivheagg qlraenlpgg arlsltlprd lepvc
//
LOCUS       WP_392520285             349 aa            linear   BCT 20-JAN-2025
DEFINITION  quaternary amine ABC transporter ATP-binding protein [Pseudomonas
            putida].
ACCESSION   WP_392520285
VERSION     WP_392520285.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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   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   4  (residues 1 to 349)
  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 349)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..349
                     /product="quaternary amine ABC transporter ATP-binding
                     protein"
                     /EC_number="7.6.2.9"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis 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:0015697 - quaternary ammonium group
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38554
     Region          6..347
                     /region_name="ProV"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG4175"
                     /db_xref="CDD:443334"
ORIGIN      
        1 mssnykieik niykvfgaap anaiarikgg askgeilkqt gnvvglndvs maieaghihv
       61 imglsgsgks tlirhfnrli eptsgqvlvd gqdvlkfskk elehyrrhki smvfqrfglc
      121 phdtvldnaa fglkvqgvar aereekaryw leqvglagve rhyprqlsgg mqqrvglara
      181 lvndpdillm deafsaldpl iksemqdqll vlqkklnkti vfithdldea lkigdriail
      241 kdgelvqqgt pseilmqpad dyvkefiggv nrykairvsh llrkpalsmv saghhtsppp
      301 tsryvrlnqs leqvlpllmq sdeplavrnd dgklvgyldk pdvmaalnr
//
LOCUS       WP_392520486             516 aa            linear   BCT 20-JAN-2025
DEFINITION  type I restriction-modification system subunit M [Pseudomonas
            putida].
ACCESSION   WP_392520486
VERSION     WP_392520486.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 516)
  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   2  (residues 1 to 516)
  AUTHORS   Youell,J. and Firman,K.
  TITLE     Mechanistic insight into Type I restriction endonucleases
  JOURNAL   Front Biosci (Landmark Ed) 17 (6), 2122-2139 (2012)
   PUBMED   22652768
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Sistla,S. and Rao,D.N.
  TITLE     S-Adenosyl-L-methionine-dependent restriction enzymes
  JOURNAL   Crit Rev Biochem Mol Biol 39 (1), 1-19 (2004)
   PUBMED   15121719
REFERENCE   4  (residues 1 to 516)
  AUTHORS   Murray,N.E.
  TITLE     Type I restriction systems: sophisticated molecular machines (a
            legacy of Bertani and Weigle)
  JOURNAL   Microbiol Mol Biol Rev 64 (2), 412-434 (2000)
   PUBMED   10839821
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114514
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..516
                     /product="type I restriction-modification system subunit
                     M"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=57303
     Region          7..135
                     /region_name="HsdM_N"
                     /note="HsdM N-terminal domain; pfam12161"
                     /db_xref="CDD:463478"
     Region          143..391
                     /region_name="HsdM"
                     /note="Type I restriction-modification system, DNA
                     methylase subunit [Defense mechanisms]; COG0286"
                     /db_xref="CDD:440055"
ORIGIN      
        1 mvtgdvekrl wavadqlwan tglrpgefsv pvlgliflry aekmyaaaed klgpigsggr
       61 rkvskddyla egviflpeka rfsylqtlte gdviglaine amkaveeenv dlkgalprny
      121 vqlgnkvlle likllgpvdl sgdafgkvye yflgnfalke gqkggvfytp esivklivei
      181 iepfhgrifd pacgsggmfa qsadfvkrhh ktameeisif gtekeqvtvn lnkmnlavhg
      241 lsgdvriant yyedpheavt rdggrfdfvm anppfnvsgv dkerlegdlr fpfgvpktdn
      301 anylwiqlfy aslnkngrag fvmansagda rgseqvirqk liesgavdvi vsvgsnffyt
      361 vtlpctlwff drakerdaer adkvlfidar hiyrqidrah rdfkpeqief lanivrlyrg
      421 eapeldqgsa ellaerglsa syvdvpglck vasreliesq gwslnpgryv gaaardvedv
      481 dfterleela eefevltaea releavisqr fvqllg
//
LOCUS       WP_392520754             700 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Pseudomonas putida].
ACCESSION   WP_392520754
VERSION     WP_392520754.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 700)
  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 700)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
REFERENCE   3  (residues 1 to 700)
  AUTHORS   Linder,P., Lasko,P.F., Ashburner,M., Leroy,P., Nielsen,P.J.,
            Nishi,K., Schnier,J. and Slonimski,P.P.
  TITLE     Birth of the D-E-A-D box
  JOURNAL   Nature 337 (6203), 121-122 (1989)
   PUBMED   2563148
  REMARK    Erratum:[Nature 1989 Jul 20;340(6230):246]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423480
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..700
                     /product="ATP-dependent DNA helicase"
                     /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_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0032508 - DNA duplex unwinding [Evidence
                     IEA]"
                     /calculated_mol_wt=77140
     Region          <2..484
                     /region_name="RecD"
                     /note="ATPase/5#-3# helicase helicase subunit RecD of the
                     DNA repair enzyme RecBCD (exonuclease V) [Replication,
                     recombination and repair]; COG0507"
                     /db_xref="CDD:440273"
ORIGIN      
        1 meiqlteeqs aaldaiktfl ladsrdafvl rgsagtgktt liaklvktle emnlscslla
       61 ptgraarilg nkikqitgnp gyegstihra iytmthlevn egaetandpg vrmifplkee
      121 eslvslfvid essmvgdkan hgdfmqfgsg rllmdivtfa rmsrpgrskd hltkllfvgd
      181 paqlppvgen aspalsdayl seqfqlkvds fdlkkvmrqa qdsaildrat elrdamlaer
      241 fnkfslqpng qdieqvdark avdlivqglq tkasnvavvh snataleynr nirdrrwgda
      301 slpiqagetl linknstthl lsngdlvkvm evgadaqcvp vnlkgghhve lwfrnvtvaf
      361 rdadggiikt nclvlenllg sphrelaple qrallvdfrk rhpdlhpksa efrrtirndp
      421 yfnalqvkyg yamtchkaqg gewntvivdf esnagsrnas ffrwaytait raakkliivn
      481 ppnftpagdi awggssgtsa kpdkadlqel ttdpdwqrls ftpaiaplmq thqqlrlvwg
      541 aqgieieqlq hlqycerytl srngkraivq yyyngklqvg rsgsvpgals dsqlaedalt
      601 slgalaaksn teqpnqfiqe fligldvala sseiqrigqk pmpyrlrvsf adayrkgeid
      661 ftydgaftwt aaqevgspgs shglyeevqs lmtaqkeklq
//
LOCUS       WP_392523339             352 aa            linear   BCT 20-JAN-2025
DEFINITION  PDDEXK nuclease domain-containing protein [Pseudomonas sp. YQ_5].
ACCESSION   WP_392523339
VERSION     WP_392523339.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. YQ_5
  ORGANISM  Pseudomonas sp. YQ_5
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 352)
  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 10008845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Pseudomonas sp. YQ_5"
                     /db_xref="taxon:3367229"
     Protein         1..352
                     /product="PDDEXK nuclease domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40371
     Region          17..346
                     /region_name="YhcG"
                     /note="Predicted nuclease of restriction endonuclease-like
                     (RecB) superfamily, DUF1016 family [General function
                     prediction only]; COG4804"
                     /db_xref="CDD:443832"
ORIGIN      
        1 mnrrkvstps paapptllgd iralieasrq rvastvnael tllfwrigqr ihtevlagqr
       61 agygeeilpt laeqlardyg rgfgeknlrr mvkfattfpd elivatlsrq lswshfvlll
      121 alkepmqrdy yaqmagaerw svrtlrnrid smlyertals kkpgetiaqe latlrdaqrm
      181 spalvmrdpy ildflglrdt wqegdleaai iremesflle lgagftfvar qkriqidsed
      241 fyldllfynr rlrrlvavel kvgefkaayk gqmelylrwl dkherepeea splgiilctg
      301 kkseqielle ldksgihvae ylttlpprav lvdrlhqatq raqlqieqrk kd
//
LOCUS       WP_392524162             320 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Salmonella enterica].
ACCESSION   WP_392524162
VERSION     WP_392524162.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..320
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=35864
     Region          43..309
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 makshprwrl akkvltwlff iavvvllvvy akkvdwgdvw tvirdynrta llsavglviv
       61 syllygcydl lgrlycghkl akrqvmlvsf vcyafnltls twvggigmry rlysrlglpg
      121 stitrifsls ittnwlgyil lggiiftfgv vqlpdhwyid egtlrilgiv llliiavylw
      181 fcafakrrhm tikgqklvlp swkfalaqma issanwmamg aiiwllmgqd vnyffvlgvl
      241 lvcsiagviv hipagigvle avflallage htsqgtiiaa llayrvlyyf iplllalvcy
      301 lilesrakkl rakneramak
//
LOCUS       WP_392524608             310 aa            linear   BCT 20-JAN-2025
DEFINITION  KpsF/GutQ family sugar-phosphate isomerase [Pseudomonas sp. CJQ_7].
ACCESSION   WP_392524608
VERSION     WP_392524608.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. CJQ_7
  ORGANISM  Pseudomonas sp. CJQ_7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Meredith,T.C. and Woodard,R.W.
  TITLE     Characterization of Escherichia coli D-arabinose 5-phosphate
            isomerase encoded by kpsF: implications for group 2 capsule
            biosynthesis
  JOURNAL   Biochem J 395 (2), 427-432 (2006)
   PUBMED   16390329
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Meredith,T.C. and Woodard,R.W.
  TITLE     Identification of GutQ from Escherichia coli as a D-arabinose
            5-phosphate isomerase
  JOURNAL   J Bacteriol 187 (20), 6936-6942 (2005)
   PUBMED   16199563
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002722
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Pseudomonas sp. CJQ_7"
                     /db_xref="taxon:3367166"
     Protein         1..310
                     /product="KpsF/GutQ family sugar-phosphate isomerase"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32974
     Region          1..306
                     /region_name="GutQ"
                     /note="D-arabinose 5-phosphate isomerase GutQ
                     [Carbohydrate transport and metabolism, Cell
                     wall/membrane/envelope biogenesis]; COG0794"
                     /db_xref="CDD:440557"
ORIGIN      
        1 mnhltiakea liaqaqavtq lagrldgefq gavelilacq grtvvcgmgk sgligqkmva
       61 tfastgtpsf flhpaeafhg dlgmlksidv lilisysget eeliklipsl ksfgnkiiam
      121 tgngkstlak hadiwldisv drevcpnnla pttstlatma mgdalavali daiqfkpmdf
      181 aryhpggslg rklltrvrdv mrtpapvvtg ttsfhdcllv mtrsrlglav vidddklvgi
      241 vtdgdlrral ldnegiihet vahfmtanph tipqdaqlse aeaymldnki ralavingdg
      301 avvgvveifd
//
LOCUS       WP_392525178             267 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein, partial
            [Klebsiella sp. TYF_8].
ACCESSION   WP_392525178
VERSION     WP_392525178.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella sp. TYF_8
  ORGANISM  Klebsiella sp. TYF_8
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
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   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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Klebsiella sp. TYF_8"
                     /db_xref="taxon:3367188"
     Protein         1..>267
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          3..114
                     /region_name="CadC1"
                     /note="DNA-binding winged helix-turn-helix (wHTH) domain
                     [Transcription]; COG3710"
                     /db_xref="CDD:442924"
ORIGIN      
        1 matiyvient lrfnseahtl hsiksnerma laipaslcfd llirnqgriv tqaellqnaw
       61 gergmsvtpn tlyqnisllr kslnrfnvng tliqtipkrg fmiadeanir ieapgtpaek
      121 andiaaaein qinravtegh gahdegsqql hadpptaqdk gdvlsrtiig avrkrktgcl
      181 vagitsllii llhifinqsa ttdspfasyt littinscki frnddlrfde yyinflkehn
      241 iscsngrtiy itnhypssrt sliscry
//
LOCUS       WP_392525409             281 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Pseudomonas].
ACCESSION   WP_392525409
VERSION     WP_392525409.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 281)
  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 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   3  (residues 1 to 281)
  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   4  (residues 1 to 281)
  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 281)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..281
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31070
     Region          22..273
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <149..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 mspplreqth lwqapalgdv emlharyyqq rfaphvhegy vftviesgaq rfwhrgsehl
       61 apvgsmvlin pdelhtgata heagwryrgf ypehervtgv ldelelgrqg mpsfkdsvih
      121 dpalalafsq lhqlseasas alqqqtawrq avlalvqrhg qcaepsasgh eplavarare
      181 llesqladpp slealaaavn lspfhfarvf rqatglppha wlkqrrlara remlkhglaa
      241 sqvafdlgfa dqshlsrqfk qaygvtpgay rqacvhsalr a
//
LOCUS       WP_392527705             398 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Klebsiella sp. WSY_19].
ACCESSION   WP_392527705
VERSION     WP_392527705.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella sp. WSY_19
  ORGANISM  Klebsiella sp. WSY_19
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 398)
  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 398)
  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
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 398)
  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   5  (residues 1 to 398)
  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   6  (residues 1 to 398)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 398)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 398)
  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 20682457
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Klebsiella sp. WSY_19"
                     /db_xref="taxon:3367211"
     Protein         1..398
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44349
     Region          20..58
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          82..391
                     /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 mqrtglnnar vrqanksifl shlwrekqls ksqlsqltgl sipavsnila ellsegligh
       61 stekmskrgv nsgsyqipeh gawtlcmnit ptsieyqlad arllavdghq hlpidaptpq
      121 alleaivecw rrihrrypqh sinlalgvhg qvdpvtgvsq tmpqarwktp ieikylleeq
      181 lgvqvrvdnd cvmlalaekw qhqgiqpdfc vinvdygigs sfvindqiyr gslygsgqig
      241 htivnpdgka cdcgrygcle tvaslsalkk qarmwlktqp eaqrspeqlt tasliedweq
      301 gdvhirawvd saanaiglsl ynflnilnin qiwlygrsca fgeqwlesiv kqtgfnpfdh
      361 gdtprahatq igfgkltraq qlmgigylyv eeqlqtlr
//
LOCUS       WP_392527928             432 aa            linear   BCT 20-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Pseudomonas fluvialis].
ACCESSION   WP_392527928
VERSION     WP_392527928.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas fluvialis
  ORGANISM  Pseudomonas fluvialis
            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 10481000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Pseudomonas fluvialis"
                     /db_xref="taxon:1793966"
     Protein         1..432
                     /product="FAD-binding oxidoreductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=48108
     Region          21..148
                     /region_name="FAD_binding_4"
                     /note="FAD binding domain; pfam01565"
                     /db_xref="CDD:426326"
ORIGIN      
        1 mtpiqawgrl saephhlwpl qdaqainrap lqaarpalah gmgrsygdva lnpggnlwlt
       61 rgldhlisfd rqngrlrcea gvllrdiqql aiasgwilpv tpgtqlitvg gaiandvhgk
      121 nhhaqgsfgd hihalqlirt dgqqlecsrt qhvewlnatv gglgltglis qaelqlqpcs
      181 gpwlesetla yhsldeffql addseaewqh tvswidclar sgrglfmran pcahqqmppr
      241 drtplrmplt pplslvnsls lkafntlyfh whkqrharrl vhyvpffypl dnlqdwnrmy
      301 gprgfyqyqs viprqhgrea iaamlqaiaa sgagsflavl ktfgqrqapg llsfarpgvt
      361 laldfpnqgq stlrlferld sivreaggtl ypakdarmpr dlfeqgyprl deflsfrdpg
      421 issslsrrlm gy
//
LOCUS       WP_392527930             316 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Pseudomonas fluvialis].
ACCESSION   WP_392527930
VERSION     WP_392527930.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas fluvialis
  ORGANISM  Pseudomonas fluvialis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas fluvialis"
                     /db_xref="taxon:1793966"
     Protein         1..316
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33737
     Region          44..291
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mtdrlsagal rvprralalv vmvavlgygl mlghadrevl qqamrqlpea llwqvaglal
       61 csyllrfcrw qyflgalawp vawwrsleiy lgafaltlsp gklgelvrsl yllplgvplh
      121 aslaaflaer lldvlavall aclggllfvq fqvalgvllg llgvllwgct rglpvpllqa
      181 llrrlarrvp vwpvrlpfll sgwrllvgta lallawsaqg lalawlvegf gyalspwllm
      241 giyclsllag aasllpggig vteasmtgll vlaglgyeda llaalicrgl tlwlallvgl
      301 lamarlactr sasvls
//
LOCUS       WP_392531118             131 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Nostoc sp. C117].
ACCESSION   WP_392531118
VERSION     WP_392531118.1
KEYWORDS    RefSeq.
SOURCE      Nostoc sp. C117
  ORGANISM  Nostoc sp. C117
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Nostoc.
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   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 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
REFERENCE   4  (residues 1 to 131)
  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 10009358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Nostoc sp. C117"
                     /db_xref="taxon:3349875"
     Protein         1..131
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14590
     Region          1..130
                     /region_name="HigA"
                     /note="Antitoxin component HigA of the HigAB
                     toxin-antitoxin module, contains an N-terminal HTH domain
                     [Defense mechanisms]; COG5499"
                     /db_xref="CDD:444250"
ORIGIN      
        1 mtrtfnpesy gkllaeyqpk iittdaeneq aialaltleh rpnrtpeeem llqllvtlie
       61 qfeethypil qgtpnsmlvh lmdardttte alaevigsle ivlqivnggt isktqaetla
      121 dyfnvdinlf t
//
LOCUS       WP_392531371             144 aa            linear   BCT 20-JAN-2025
DEFINITION  ferritin-like domain-containing protein [Nostoc sp. C117].
ACCESSION   WP_392531371
VERSION     WP_392531371.1
KEYWORDS    RefSeq.
SOURCE      Nostoc sp. C117
  ORGANISM  Nostoc sp. C117
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Nostoc.
REFERENCE   1  (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   2  (residues 1 to 144)
  AUTHORS   Harrison,P.M. and Arosio,P.
  TITLE     The ferritins: molecular properties, iron storage function and
            cellular regulation
  JOURNAL   Biochim Biophys Acta 1275 (3), 161-203 (1996)
   PUBMED   8695634
REFERENCE   3  (residues 1 to 144)
  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 10005564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Nostoc sp. C117"
                     /db_xref="taxon:3349875"
     Protein         1..144
                     /product="ferritin-like domain-containing protein"
                     /EC_number="1.16.3.1"
                     /GO_function="GO:0004322 - ferroxidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008199 - ferric iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0015093 - ferrous iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=16206
     Region          5..141
                     /region_name="Bfr"
                     /note="Bacterioferritin (cytochrome b1) [Inorganic ion
                     transport and metabolism]; COG2193"
                     /db_xref="CDD:441796"
ORIGIN      
        1 mqeldqtkti dllnaimefe lagvvrythy slmvtgpnri pivaffkaqa sesllhaeqv
       61 geiltgldgh pslkiapmee tykhtvkdil aeslshekka ldlyknllet vtnasiylee
      121 fargmigqee mhnlelkkml rdfs
//
LOCUS       WP_392533733             302 aa            linear   BCT 20-JAN-2025
DEFINITION  caspase family protein [Nostoc sp. C117].
ACCESSION   WP_392533733
VERSION     WP_392533733.1
KEYWORDS    RefSeq.
SOURCE      Nostoc sp. C117
  ORGANISM  Nostoc sp. C117
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Nostoc.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Van Opdenbosch,N. and Lamkanfi,M.
  TITLE     Caspases in Cell Death, Inflammation, and Disease
  JOURNAL   Immunity 50 (6), 1352-1364 (2019)
   PUBMED   31216460
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Tsiatsiani,L., Van Breusegem,F., Gallois,P., Zavialov,A., Lam,E.
            and Bozhkov,P.V.
  TITLE     Metacaspases
  JOURNAL   Cell Death Differ 18 (8), 1279-1288 (2011)
   PUBMED   21597462
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Zhang,J.H., Zhang,Y. and Herman,B.
  TITLE     Caspases, apoptosis and aging
  JOURNAL   Ageing Res Rev 2 (4), 357-366 (2003)
   PUBMED   14522240
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Salvesen,G.S.
  TITLE     Caspases and apoptosis
  JOURNAL   Essays Biochem 38, 9-19 (2002)
   PUBMED   12463158
REFERENCE   5  (residues 1 to 302)
  AUTHORS   Villa,P., Kaufmann,S.H. and Earnshaw,W.C.
  TITLE     Caspases and caspase inhibitors
  JOURNAL   Trends Biochem Sci 22 (10), 388-393 (1997)
   PUBMED   9357314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Nostoc sp. C117"
                     /db_xref="taxon:3349875"
     Protein         1..302
                     /product="caspase family protein"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=34288
     Region          1..227
                     /region_name="COG4249"
                     /note="Uncharacterized conserved protein, contains caspase
                     domain [General function prediction only]"
                     /db_xref="CDD:443391"
ORIGIN      
        1 msrdalvvgi nkynfsglsa lrspandaea iakrlseagn fhvqrlpqfl npfeddvpqi
       61 spnqeiklad lekaleklfy pegrsipdta lfyfsghglr kdgrikegfl atsdtdpelg
      121 nwglrlkwlr elleespvrq qiiwldccys gellnftead pgdrgntrdr cfiaacrefe
      181 lahenvrtas svltsailrg fdladlsnqw vtnetlvtfl rqeletapqk fisnnlgcin
      241 lffrkettnk qpvqstvqtp sqpnqtakla eqlrawftal rydfekdein nenyfewiit
      301 gv
//
LOCUS       WP_392536072             327 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Nostoc sp. C117].
ACCESSION   WP_392536072
VERSION     WP_392536072.1
KEYWORDS    RefSeq.
SOURCE      Nostoc sp. C117
  ORGANISM  Nostoc sp. C117
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Nostoc.
REFERENCE   1  (residues 1 to 327)
  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 327)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 327)
  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   4  (residues 1 to 327)
  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 327)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Nostoc sp. C117"
                     /db_xref="taxon:3349875"
     Protein         1..327
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36683
     Region          50..202
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          230..309
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mnaaktsqkp drdlindpql krevdraqan rdelkeriag airydgtiep lkglhfnrss
       61 spsecvhsvs ipafcaiaqg skevllgsdr yqydpmhyll atvelpiisq ileaskeqpy
      121 lslrldldpt lvgsvmveag ypssrsradv kaidvsplna nlldavvrlv rlldspaeah
      181 vlaplikrei iyrllmgeqg nrlrhiavlg gytyhiarav erlrkdfnep ikiesiarel
      241 gmsvsgfhhh fksvtamspl qyqkqlrlqe arrlmlgekl datsaayrvg yddtshfnre
      301 ykrlfgappm rdverlreaa retassi
//
LOCUS       WP_392536548             285 aa            linear   BCT 20-JAN-2025
DEFINITION  LicD family protein [Legionella sp. 227].
ACCESSION   WP_392536548
VERSION     WP_392536548.1
KEYWORDS    RefSeq.
SOURCE      Legionella sp. 227
  ORGANISM  Legionella sp. 227
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Kuchta,K., Knizewski,L., Wyrwicz,L.S., Rychlewski,L. and
            Ginalski,K.
  TITLE     Comprehensive classification of nucleotidyltransferase fold
            proteins: identification of novel families and their
            representatives in human
  JOURNAL   Nucleic Acids Res 37 (22), 7701-7714 (2009)
   PUBMED   19833706
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Legionella sp. 227"
                     /db_xref="taxon:3367288"
     Protein         1..285
                     /product="LicD family protein"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=33198
     Region          21..270
                     /region_name="LicD"
                     /note="Phosphorylcholine metabolism protein LicD [Lipid
                     transport and metabolism]; COG3475"
                     /db_xref="CDD:442698"
ORIGIN      
        1 mtlaknsnpy sadtafqdgr lrqaqlkmlt mlevvdaicr khgldywlda gtllgavrhq
       61 gfipwdddvd iamprasyeq flrvapseip swmwlqtihs dpgyfnmatp lkirdrasrf
      121 iekhekgnep yvqgifidvf vydrmpvdpk qrkrykfyak klsrllstky skvkighypt
      181 lykliasffp kpllewslqk iihqanashs pyigrgyncv gknlikkeei yplqrvsfet
      241 kefniprnae afliqqygdy lqlppeeqrv mrhckeliph leeai
//
LOCUS       WP_392537796             251 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Legionella sp. 227].
ACCESSION   WP_392537796
VERSION     WP_392537796.1
KEYWORDS    RefSeq.
SOURCE      Legionella sp. 227
  ORGANISM  Legionella sp. 227
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 251)
  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 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   3  (residues 1 to 251)
  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   4  (residues 1 to 251)
  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 251)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Legionella sp. 227"
                     /db_xref="taxon:3367288"
     Protein         1..251
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28529
     Region          1..242
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <135..235
                     /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 mithhvdlrs yhtescshsh dfaqlvlpla gsmeleaghy sgvvnhqvgv fiapnerhcf
       61 sgsqenlflv vdvanqnnly rehnshafnl ttsikkliqf thyylaaneg dfltdslinq
      121 llvhfstksf speldrtvik aknwidfhfa dtvnlskvaq hchlsvsqlq rrfkqslgcs
      181 iaeywrfkkl nqakqllsaq hlsieaiafa vgyenlpafs rrfsqvfgvs psqwrtkals
      241 akkmremdns y
//
LOCUS       WP_392538100             299 aa            linear   BCT 20-JAN-2025
DEFINITION  S66 peptidase family protein [Legionella sp. 227].
ACCESSION   WP_392538100
VERSION     WP_392538100.1
KEYWORDS    RefSeq.
SOURCE      Legionella sp. 227
  ORGANISM  Legionella sp. 227
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Di Cera,E.
  TITLE     Serine proteases
  JOURNAL   IUBMB Life 61 (5), 510-515 (2009)
   PUBMED   19180666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Legionella sp. 227"
                     /db_xref="taxon:3367288"
     Protein         1..299
                     /product="S66 peptidase family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004180 - carboxypeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=33095
     Region          5..287
                     /region_name="LdcA"
                     /note="Muramoyltetrapeptide carboxypeptidase LdcA
                     (peptidoglycan recycling) [Cell wall/membrane/envelope
                     biogenesis]; COG1619"
                     /db_xref="CDD:441226"
ORIGIN      
        1 mknlpvltpg dwieiiapss rstdrqlsel kelleswgln civqqdifar dllcantdem
       61 rfkhlknale npktravicv rggygstrli pklaavhppe takifigisd itclhlylqq
      121 hwnwptihga aapdkfskes iasvrsilfr dapiafndlt pmntqaqker fiksqvtggn
      181 lamiqsgigt cwqidgreki illeeigerg yrvdrmlehl kqanifthaa aillgdfldg
      241 lepngtslid pvlqrfaesc aipvlriagi ghgpinypip lgtevhlqlg ahpqltcfr
//
LOCUS       WP_392539225             636 aa            linear   BCT 20-JAN-2025
DEFINITION  sensor histidine kinase [Pseudomonas sp. GLN_6].
ACCESSION   WP_392539225
VERSION     WP_392539225.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GLN_6
  ORGANISM  Pseudomonas sp. GLN_6
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 636)
  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 636)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20493667
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Pseudomonas sp. GLN_6"
                     /db_xref="taxon:3367183"
     Protein         1..636
                     /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=69756
     Region          51..304
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          270..596
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mqcstappra vppaltvkpr larvlllill llllvlgcgy agyylserng irdlaenger
       61 qlelnarave seitkytylp slleleynvg rllqtpttyr rqlvndyleg lnqrsgslai
      121 yvldrsgrvl atsnwrtpss ylgedlsfra yfqdaiegkp grfygigstt gepgyylahg
      181 lksgeriigv avvkvrldsl eqrwqrarlq ayvsdengii ilssnpnrrl kavhslgpnt
      241 rerlarslqy hwwaleelqp larrrlgdgl eqvsfaadqd geadagpity laqtrplddt
      301 pwhltlltpl qdqrsaalsh amlaavacal liflglalnq rrkviatrla arealeqann
      361 elerkiaert adlqasnqrl qaevrerqqa ettlrqaqde lvqagklavi gqmstsiahe
      421 lnqplaalrt lsgntvrflq rgaldvassn lqtigelvdr mgkitaslra farrsgdqge
      481 asleqavdaa llllqnhpgy aavqlhrdya hgpadvrlai eqtrleqilv nlianaldam
      541 seqterqlwl sgqddgeryr ltvrdngpgi aadvrvhlfe pffttkpgek glglgltlsa
      601 slaaaaagsl tvqhpdsggt afelnlakvt pgeptp
//
LOCUS       WP_392539237             458 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter large permease [Pseudomonas sp. GLN_6].
ACCESSION   WP_392539237
VERSION     WP_392539237.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GLN_6
  ORGANISM  Pseudomonas sp. GLN_6
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 458)
  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 458)
  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 458)
  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 458)
  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 10008688
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Pseudomonas sp. GLN_6"
                     /db_xref="taxon:3367183"
     Protein         1..458
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma 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=47996
     Region          3..457
                     /region_name="FcbT3"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, large permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4664"
                     /db_xref="CDD:443701"
ORIGIN      
        1 maelmaillf isicaalmag ypvaftlagv sllfagigvv tgtfdagyls alpnrlfgim
       61 nnqtmlavpl fvfmgvmlek srvaedlles msrlfgtlrg glaisvcmvg allaastgiv
      121 gatvvtmgll alptmlrrgy dpaiatgtla atgtlgqiip psivlvllgd vmssayqqaq
      181 lkmgifspkt vsvgdlfvga llpglllvgm yilyiigvai lqpkklpalp qeelgpiewg
      241 klinalvppl lligavlgsi lagyatptea aalgalgaml lafykgklnf gqlrevasgt
      301 teisamvfli ligaslfslv frgfggeali edvfaqlpgg vlgafflvmv vifllgfild
      361 fieitfvvvp ivgpvllamg ldpiwlgvmi alnlqtsflt ppfgfalfyl rgvtpasvpt
      421 stiykgvvpf iliqilllvi ayqfpglitw lpeqvygk
//
LOCUS       WP_392539594             236 aa            linear   BCT 20-JAN-2025
DEFINITION  4'-phosphopantetheinyl transferase family protein [Pseudomonas sp.
            GLN_6].
ACCESSION   WP_392539594
VERSION     WP_392539594.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GLN_6
  ORGANISM  Pseudomonas sp. GLN_6
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Lambalot,R.H., Gehring,A.M., Flugel,R.S., Zuber,P., LaCelle,M.,
            Marahiel,M.A., Reid,R., Khosla,C. and Walsh,C.T.
  TITLE     A new enzyme superfamily - the phosphopantetheinyl transferases
  JOURNAL   Chem Biol 3 (11), 923-936 (1996)
   PUBMED   8939709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459479
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Pseudomonas sp. GLN_6"
                     /db_xref="taxon:3367183"
     Protein         1..236
                     /product="4'-phosphopantetheinyl transferase family
                     protein"
                     /EC_number="2.7.8.7"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008897 - holo-[acyl-carrier-protein]
                     synthase activity [Evidence IEA]"
                     /calculated_mol_wt=25999
     Region          35..234
                     /region_name="EntD"
                     /note="4'-phosphopantetheinyl transferase EntD
                     (siderophore biosynthesis) [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2977"
                     /db_xref="CDD:442216"
ORIGIN      
        1 mnttylppcc splndhwplp hklpsvrlis ttfkpelldp adfsrcaiel vrgvakrqae
       61 ylagrlcare allrltgtaa vpacgedrap qwplgmvgsi thgsgwagai vgnnadwrgl
      121 gldieqimpa sraerlagei ltpaellrlq elpseqraqr isltfslkes lfkalypqvl
      181 qhfyfqdael lsvnadnkvr mrllvdlhad wpagselegq faefdgylls lvsipr
//
LOCUS       WP_392540357             441 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter large permease [Pseudomonas sp. GLN_6].
ACCESSION   WP_392540357
VERSION     WP_392540357.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GLN_6
  ORGANISM  Pseudomonas sp. GLN_6
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 441)
  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 441)
  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 441)
  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 441)
  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 10008688
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Pseudomonas sp. GLN_6"
                     /db_xref="taxon:3367183"
     Protein         1..441
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma 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=47766
     Region          3..440
                     /region_name="FcbT3"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, large permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4664"
                     /db_xref="CDD:443701"
ORIGIN      
        1 mdyeliallm fssmmllllt gkrvfgaigf vavaaalllw gdggsemafs aamklmkwyp
       61 lltlplfvfm gymlsesgla edlykmfhvw mgplngglai gtiglmvais amnglsvagm
      121 aigasialpe llrrgydkim vtgviqagss lgilippsvv lvlygmiarq pvgqlwlagv
      181 fpgllmaglf ilyiaircrl qpelgpalse eergqisrre kllllkagia plfiffcmtg
      241 lflmgitslv essavgaaaa tlmalvkgrl trsvmeetlr ktlgiscmfm wiilaalcfg
      301 avfdglgavk aieafflesl glgpwqvlil mqlsfiimgm flddtamlvi vaplyiplvg
      361 algfdlvwyg vlytitcqia ymtppfgynl flmramappe vslrdiyvsv tpfvlimvla
      421 lvlvmvfpqi alwlprwhyg g
//
LOCUS       WP_392540547             298 aa            linear   BCT 20-JAN-2025
DEFINITION  transglutaminase family protein [Pseudomonas sp. GLN_6].
ACCESSION   WP_392540547
VERSION     WP_392540547.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GLN_6
  ORGANISM  Pseudomonas sp. GLN_6
            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 12090973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Pseudomonas sp. GLN_6"
                     /db_xref="taxon:3367183"
     Protein         1..298
                     /product="transglutaminase family protein"
                     /calculated_mol_wt=33196
     Region          6..85
                     /region_name="Bact_transglu_N"
                     /note="Bacterial transglutaminase-like N-terminal region;
                     pfam08379"
                     /db_xref="CDD:462455"
     Region          <137..251
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mssafyqilh dthyryaapv slaqqlahlw pracpwqrnh eqqllvspqp cqrqdaldvf
       61 gnpltrlvfe rphdelmvsa rlkvevlard eldltqspaw eqactalrys ghallpdvle
      121 atrfrfespy vhlkqvfsdy aadcftpdrp llaavdglmq kifaefsfda aatqvatpll
      181 qvleerrgvc qdfahlmlac lrsmglsary vsgylltqpp pgqprligad ashawvsvfc
      241 peqgwvdfdp tnnirpaleh itlawgrdfa dvsplrgvil gggshdpevq vtvlplas
//
LOCUS       WP_392540534             299 aa            linear   BCT 20-JAN-2025
DEFINITION  heme/hemin ABC transporter substrate-binding protein [Pseudomonas
            sp. GLN_6].
ACCESSION   WP_392540534
VERSION     WP_392540534.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GLN_6
  ORGANISM  Pseudomonas sp. GLN_6
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Naoe,Y., Nakamura,N., Rahman,M.M., Tosha,T., Nagatoishi,S.,
            Tsumoto,K., Shiro,Y. and Sugimoto,H.
  TITLE     Structural basis for binding and transfer of heme in bacterial
            heme-acquisition systems
  JOURNAL   Proteins 85 (12), 2217-2230 (2017)
   PUBMED   28913898
REFERENCE   2  (residues 1 to 299)
  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   3  (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   4  (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   5  (residues 1 to 299)
  AUTHORS   Ho,W.W., Li,H., Eakanunkul,S., Tong,Y., Wilks,A., Guo,M. and
            Poulos,T.L.
  TITLE     Holo- and apo-bound structures of bacterial periplasmic
            heme-binding proteins
  JOURNAL   J Biol Chem 282 (49), 35796-35802 (2007)
   PUBMED   17925389
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Pseudomonas sp. GLN_6"
                     /db_xref="taxon:3367183"
     Protein         1..299
                     /product="heme/hemin 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=31307
     Region          1..289
                     /region_name="ChuT"
                     /note="ABC-type hemin transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG4558"
                     /db_xref="CDD:443619"
ORIGIN      
        1 mkrlssllal sasllscswl maaeplpqrw issggslsew vvalggesrl vgvdstsqhp
       61 eslralpsig yqrqlaaegm ltlrpdilig seemgpppvl aqlrgagvrv emlsskadlk
      121 slqaslqrig tllgepqrad qafaayqqrl qqqadwlvta krqqaapgvl lllghaggsp
      181 maggkdtsad wlieraggrn lashsgfkal steallaldp evviiadrsl sgdaareall
      241 qqnpalaatr aarnqrllml dptllvgglg prlpdglaal saafypasqp lvaeakptp
//
LOCUS       WP_392540928             317 aa            linear   BCT 20-JAN-2025
DEFINITION  lysylphosphatidylglycerol synthase transmembrane domain-containing
            protein [Pseudomonas sp. GLN_6].
ACCESSION   WP_392540928
VERSION     WP_392540928.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GLN_6
  ORGANISM  Pseudomonas sp. GLN_6
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Oku,Y., Kurokawa,K., Ichihashi,N. and Sekimizu,K.
  TITLE     Characterization of the Staphylococcus aureus mprF gene, involved
            in lysinylation of phosphatidylglycerol
  JOURNAL   Microbiology (Reading) 150 (Pt 1), 45-51 (2004)
   PUBMED   14702396
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kristian,S.A., Durr,M., Van Strijp,J.A., Neumeister,B. and
            Peschel,A.
  TITLE     MprF-mediated lysinylation of phospholipids in Staphylococcus
            aureus leads to protection against oxygen-independent neutrophil
            killing
  JOURNAL   Infect Immun 71 (1), 546-549 (2003)
   PUBMED   12496209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Pseudomonas sp. GLN_6"
                     /db_xref="taxon:3367183"
     Protein         1..317
                     /product="lysylphosphatidylglycerol synthase transmembrane
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=34670
     Region          39..284
                     /region_name="AglD2"
                     /note="Predicted membrane flippase AglD2/YbhN, UPF0104
                     family [Cell wall/membrane/envelope biogenesis]; COG0392"
                     /db_xref="CDD:440161"
ORIGIN      
        1 mkrsdlawtl vglgavllsc yllyhqvrti slneiadslr aiprldwlla aaatlgaysa
       61 lawydriala hlgkkiswrf islcsfttya lahnigasvf sgalvryray rskgmtpqei
      121 gilivfcsft fvlgtilasg cvlvlepdli hrvakvtplv seiigvllll lvalyvlgsw
      181 rhfkpwhwgk lhleyprlgi vgrqllagpl elacaaaiiy falpaennpg ylvvfgvfla
      241 sfslallsha pgglgvlevt flaampelpa advlaalivf rcfylllpfa lsllvvlgfe
      301 wtqwqsrrtn pdnpplp
//
LOCUS       WP_392541730             527 aa            linear   BCT 20-JAN-2025
DEFINITION  type I restriction-modification system subunit M [Pseudomonas sp.
            GLN_6].
ACCESSION   WP_392541730
VERSION     WP_392541730.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GLN_6
  ORGANISM  Pseudomonas sp. GLN_6
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 527)
  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   2  (residues 1 to 527)
  AUTHORS   Youell,J. and Firman,K.
  TITLE     Mechanistic insight into Type I restriction endonucleases
  JOURNAL   Front Biosci (Landmark Ed) 17 (6), 2122-2139 (2012)
   PUBMED   22652768
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Sistla,S. and Rao,D.N.
  TITLE     S-Adenosyl-L-methionine-dependent restriction enzymes
  JOURNAL   Crit Rev Biochem Mol Biol 39 (1), 1-19 (2004)
   PUBMED   15121719
REFERENCE   4  (residues 1 to 527)
  AUTHORS   Murray,N.E.
  TITLE     Type I restriction systems: sophisticated molecular machines (a
            legacy of Bertani and Weigle)
  JOURNAL   Microbiol Mol Biol Rev 64 (2), 412-434 (2000)
   PUBMED   10839821
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114514
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Pseudomonas sp. GLN_6"
                     /db_xref="taxon:3367183"
     Protein         1..527
                     /product="type I restriction-modification system subunit
                     M"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=59348
     Region          6..140
                     /region_name="HsdM_N"
                     /note="HsdM N-terminal domain; pfam12161"
                     /db_xref="CDD:463478"
     Region          149..413
                     /region_name="HsdM"
                     /note="Type I restriction-modification system, DNA
                     methylase subunit [Defense mechanisms]; COG0286"
                     /db_xref="CDD:440055"
ORIGIN      
        1 mltgkirndi dklwekfwtg gitnpltvie qisylmfarm ldmqedvaer kanrtgkpfd
       61 rlfpntpdgq llrwknfrnm sgkelhshlk qkvypffaql ggaegegger eglghiseym
      121 qdadleikne svltsavemv ndlpltqsdv kgdiyeylls klttagingq frtprhiida
      181 mieliapqpt evicdpscgt agflartmey lnrahsspeg tftdedgnlh ysgdllepyr
      241 qhinsqmfwg fdfdttmlrv ssmnmmlhgv nganiryqds lsksikehyp rqeqnffdvv
      301 lanppfkgsl detntnpdvl glvktkktel lfvahilrsl klggraaviv pdgvlfgssk
      361 ahqqlrqell dnnqlegivs lpsgvfkpya gvstailift kggstervwf ydlqadgysl
      421 ddkrtelkge gsndlpdaia qwhkyrqmve gnisastint lfgdkrkkaf vvpaediaan
      481 kydlsinryk eveyqqeqfe dpkvilqrlk gleqeiladl delegml
//
LOCUS       WP_392541536             372 aa            linear   BCT 20-JAN-2025
DEFINITION  protein-glutamate methylesterase/protein-glutamine glutaminase
            [Pseudomonas sp. GLN_6].
ACCESSION   WP_392541536
VERSION     WP_392541536.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GLN_6
  ORGANISM  Pseudomonas sp. GLN_6
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  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   2  (residues 1 to 372)
  AUTHORS   Skerker,J.M., Prasol,M.S., Perchuk,B.S., Biondi,E.G. and Laub,M.T.
  TITLE     Two-component signal transduction pathways regulating growth and
            cell cycle progression in a bacterium: a system-level analysis
  JOURNAL   PLoS Biol 3 (10), e334 (2005)
   PUBMED   16176121
REFERENCE   3  (residues 1 to 372)
  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   4  (residues 1 to 372)
  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
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Anand,G.S., Goudreau,P.N. and Stock,A.M.
  TITLE     Activation of methylesterase CheB: evidence of a dual role for the
            regulatory domain
  JOURNAL   Biochemistry 37 (40), 14038-14047 (1998)
   PUBMED   9760239
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Volz,K.
  TITLE     Structural conservation in the CheY superfamily
  JOURNAL   Biochemistry 32 (44), 11741-11753 (1993)
   PUBMED   8218244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11479194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas sp. GLN_6"
                     /db_xref="taxon:3367183"
     Protein         1..372
                     /product="protein-glutamate
                     methylesterase/protein-glutamine glutaminase"
                     /EC_number="3.1.1.61"
                     /EC_number="3.5.1.44"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0008984 - protein-glutamate
                     methylesterase activity [Evidence IEA]"
                     /GO_function="GO:0050568 - protein-glutamine glutaminase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006482 - protein demethylation [Evidence
                     IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0018277 - protein deamination [Evidence
                     IEA]"
                     /calculated_mol_wt=39428
     Region          1..372
                     /region_name="PRK00742"
                     /note="chemotaxis-specific protein-glutamate
                     methyltransferase CheB"
                     /db_xref="CDD:234828"
ORIGIN      
        1 mavkvlvvdd sgffrrrvse ilsadpniqv igtatngrea ieqaqalkpd vitmdyempm
       61 mdgitavrni mqrcptpvlm fsslthegar vtldaleaga vdflpknfed isrnpervkq
      121 llcekihtia rsnrrslnpp paapvvpats lskpavrpap tsapasrpav apapapvass
      181 aapkrksykl vaigtstggp valqrvltql pasfpapivl iqhmpaaftk afaerldklc
      241 risvkeaedg dvlrpglall apggkqmmvd argvvkilpg derlnykpcv ditfgsvaks
      301 ygdkvlavvl tgmgadgreg arllkqggsq vwaqdeascv iygmpmaivk anladaiypl
      361 ddigrhlaea ca
//
LOCUS       WP_392542834             552 aa            linear   BCT 20-JAN-2025
DEFINITION  peptide ABC transporter substrate-binding protein [Oryzobacter
            telluris].
ACCESSION   WP_392542834
VERSION     WP_392542834.1
KEYWORDS    RefSeq.
SOURCE      Oryzobacter telluris
  ORGANISM  Oryzobacter telluris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Intrasporangiaceae; Oryzobacter.
REFERENCE   1  (residues 1 to 552)
  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 552)
  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 552)
  AUTHORS   ter Beek,J., 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 552)
  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 552)
  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 11467924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Oryzobacter telluris"
                     /db_xref="taxon:3149179"
     Protein         1..552
                     /product="peptide 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=59135
     Region          22..552
                     /region_name="OppA"
                     /note="ABC-type oligopeptide transport system, periplasmic
                     component [Amino acid transport and metabolism]; COG4166"
                     /db_xref="CDD:443327"
ORIGIN      
        1 mrgttrtvav aalsavalla agcgnsgsgs dtettagskt ggeitirgcn pqnplvpsnt
       61 setcggnvld avfaklvhyd petakpandi aesiettdnq nftikikkgy kfhdgtevka
      121 knfvdawnya ayapnaqggg yfmtpiegyg dlqctgdged pcagagkaka dkltglavtd
      181 dytftiktte kvsnlpvrlg ytafaplpdv fftdpkafgd kpigtgpfkl dswtkeqsiv
      241 lskfadysge fkakvdkvtf kiyadadaay ndvlannldv tdeipasali ddkyksdlpe
      301 rnaqketgvi qyaefsptkv dpnvadpkir qaismaidrp tiikqifnnt rvpatgwvsp
      361 vvdgykaeqc gefckydpak akallaeagg ykgekltlsy nadaahkewt eatcnsikqa
      421 lgiecvatgv vdfstylkql edrkmkglfr lgwqmdypai enflapvfat gadsnymdys
      481 npafdkllve gaaatdpaas nakyqeaeal laqdmpaipl wygkttmgws dkvtgvkita
      541 fgtidlasis lk
//
LOCUS       WP_392543402             257 aa            linear   BCT 20-JAN-2025
DEFINITION  isocitrate lyase/PEP mutase family protein [Oryzobacter telluris].
ACCESSION   WP_392543402
VERSION     WP_392543402.1
KEYWORDS    RefSeq.
SOURCE      Oryzobacter telluris
  ORGANISM  Oryzobacter telluris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Intrasporangiaceae; Oryzobacter.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10616714
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Oryzobacter telluris"
                     /db_xref="taxon:3149179"
     Protein         1..257
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26147
     Region          10..244
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 mntldkatel qrlhavpell lvvnvwdvis arvvagtpgt talatashsi aasygypdge
       61 qiprdlmlea cgriaaatdl pvsadleagy gdpggtvara idlgivganl edqlkplgea
      121 vaaveaavaa geaagipfql nartdaflra gdrdpaevla daiergrayl dagaatffap
      181 gkldeptvaa lvealgpqkv tligvpgslp ldtlqrlgva rvsygpwsqn valtaladlt
      241 eavlaggalp egtrkln
//
LOCUS       WP_392546903             207 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Rhodopirellula sp. JB044].
ACCESSION   WP_392546903
VERSION     WP_392546903.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula sp. JB044
  ORGANISM  Rhodopirellula sp. JB044
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Rhodopirellula sp. JB044"
                     /db_xref="taxon:3342844"
     Protein         1..207
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22842
     Region          13..205
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 miaeafdrqp qrskqlildr lrgravkskg lpeidrsrlv rfddpvaqfr qtlefvgges
       61 hmvdtpeqvr eilmgidvfa gaeriastyp eaieptvqld rigdphllss ldwtvvrgef
      121 aiaengaiwi dggtlphrvm ifiaqylaiv vsrsqivdhm hdayarigtp epgfgvfvsg
      181 psktadieqs lvlgahgcrk lqvfltp
//
LOCUS       WP_392547040             277 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Rhodopirellula sp. JB044].
ACCESSION   WP_392547040
VERSION     WP_392547040.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula sp. JB044
  ORGANISM  Rhodopirellula sp. JB044
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 277)
  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 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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Rhodopirellula sp. JB044"
                     /db_xref="taxon:3342844"
     Protein         1..277
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32466
     Region          38..277
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <175..277
                     /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 miyekitade qasfrclewi dkdfdcphhf hpeveithiv asrgerlvgd rfdnyepgdl
       61 amfgpllphr yknwkcrksh srvvqfrlda lghgffelpe crairqlihd ssrglcfsda
      121 vrkdgcrmmt rlfktpvgpq risrlvelmd ilssdtereq mashdfmate nlesdkrler
      181 ilsyidahwq etiplaeiak vaglhpqsls ryfrrrlgrt fqdyvielrl sraardlles
      241 krtvsdiafh cgfnnlanfn rlflaryqms prqyrsr
//
LOCUS       WP_392547169             321 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Rhodopirellula sp. JB044].
ACCESSION   WP_392547169
VERSION     WP_392547169.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula sp. JB044
  ORGANISM  Rhodopirellula sp. JB044
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 321)
  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 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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Rhodopirellula sp. JB044"
                     /db_xref="taxon:3342844"
     Protein         1..321
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36225
     Region          55..311
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <200..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 mrdttlnqye gyyhylpvdd iamswgvylt glgsgrapag etyppkghpg lysfrwargr
       61 vlpefqmili tkgsgvfese ptgtlpiapg siitlfpgvw hryrpdfdvg wterwisfhg
      121 tmthrllelg lifpemavrk akrpsslska fdrilksvsd hsnqnsills fqamaligsv
      181 ientsdigev pgghtciynk evrdplvara ldliwthshq aftvqrfadr lsvsrrvler
      241 rfrneighsv lteitacrls rakrllvetd lgvkavafla gfpsdermrv tflekvnmsp
      301 sqyrseyleq rkpkvgrpsr s
//
LOCUS       WP_392547376             395 aa            linear   BCT 20-JAN-2025
DEFINITION  S1 family peptidase [Rhodopirellula sp. JB044].
ACCESSION   WP_392547376
VERSION     WP_392547376.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula sp. JB044
  ORGANISM  Rhodopirellula sp. JB044
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Querino Lima Afonso,M., da Fonseca,N.J. Jr., de Oliveira,L.C.,
            Lobo,F.P. and Bleicher,L.
  TITLE     Coevolved Positions Represent Key Functional Properties in the
            Trypsin-Like Serine Proteases Protein Family
  JOURNAL   J Chem Inf Model 60 (2), 1060-1068 (2020)
   PUBMED   31895561
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Waldner,B.J., Kraml,J., Kahler,U., Spinn,A., Schauperl,M.,
            Podewitz,M., Fuchs,J.E., Cruciani,G. and Liedl,K.R.
  TITLE     Electrostatic recognition in substrate binding to serine proteases
  JOURNAL   J Mol Recognit 31 (10), e2727 (2018)
   PUBMED   29785722
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Pelc,L.A., Chen,Z., Gohara,D.W., Vogt,A.D., Pozzi,N. and Di Cera,E.
  TITLE     Why Ser and not Thr brokers catalysis in the trypsin fold
  JOURNAL   Biochemistry 54 (7), 1457-1464 (2015)
   PUBMED   25664608
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Perona,J.J. and Craik,C.S.
  TITLE     Evolutionary divergence of substrate specificity within the
            chymotrypsin-like serine protease fold
  JOURNAL   J Biol Chem 272 (48), 29987-29990 (1997)
   PUBMED   9374470
REFERENCE   5  (residues 1 to 395)
  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 10595581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Rhodopirellula sp. JB044"
                     /db_xref="taxon:3342844"
     Protein         1..395
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42632
     Region          186..314
                     /region_name="Trypsin_2"
                     /note="Trypsin-like peptidase domain; pfam13365"
                     /db_xref="CDD:433149"
ORIGIN      
        1 mkltdlglaa llavslfasr clsdgprils slenatgple rrelkqflge yypdyqlpag
       61 kifaalnhdg ddkldgdelv afkdlleqid aeldttpedp gpgyplfssv asgiddskvd
      121 gavfhrhfdn leqhprpegf qiesvpmtsr lslpktvgrk tvvedlvkat vvlaggegdd
      181 yftsggvlvr sdglvltnfh vaeafssgmt altsdgksyr vvdfiagdrl advaliridg
      241 tdmptvevas tspeigddlv mmhhtenrfy tydrgylmrn pviegkqwme vslpfgpggs
      301 gcgifnqshe lvglvsivml gdgpslallg hglaeavdee ksgesdveqt dfldellwda
      361 tselesdgfe lvvrhavslp airrlfspva datpr
//
LOCUS       WP_392548995             534 aa            linear   BCT 20-JAN-2025
DEFINITION  Rne/Rng family ribonuclease [Rhodopirellula sp. JB044].
ACCESSION   WP_392548995
VERSION     WP_392548995.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula sp. JB044
  ORGANISM  Rhodopirellula sp. JB044
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Kime,L., Jourdan,S.S. and McDowall,K.J.
  TITLE     Identifying and characterizing substrates of the RNase E/G family
            of enzymes
  JOURNAL   Methods Enzymol 447, 215-241 (2008)
   PUBMED   19161846
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Callaghan,A.J., Marcaida,M.J., Stead,J.A., McDowall,K.J.,
            Scott,W.G. and Luisi,B.F.
  TITLE     Structure of Escherichia coli RNase E catalytic domain and
            implications for RNA turnover
  JOURNAL   Nature 437 (7062), 1187-1191 (2005)
   PUBMED   16237448
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Li,Z., Pandit,S. and Deutscher,M.P.
  TITLE     RNase G (CafA protein) and RNase E are both required for the 5'
            maturation of 16S ribosomal RNA
  JOURNAL   EMBO J 18 (10), 2878-2885 (1999)
   PUBMED   10329633
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Rhodopirellula sp. JB044"
                     /db_xref="taxon:3342844"
     Protein         1..534
                     /product="Rne/Rng family ribonuclease"
                     /EC_number="3.1.26.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004540 - RNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0006397 - mRNA processing [Evidence IEA]"
                     /calculated_mol_wt=60490
     Region          3..520
                     /region_name="CafA"
                     /note="Ribonuclease G or E [Translation, ribosomal
                     structure and biogenesis]; COG1530"
                     /db_xref="CDD:441139"
ORIGIN      
        1 mkremlinvl qpeesriavv edkvleelyv erksveafag niyrgkivnl epsiqaafvd
       61 fgvgrngflh isdvepqyfr qggydpeeim resdemaaas aarnresgrg nsrvfkggrp
      121 rikppiqeif krgdevlvqv ikegigtkgp tlstyisipg rylvlmpals rvgvsrkied
      181 eddrkrlkka lhacnppkgl gfivrtagag rsedelhrdm dyllrlwkai akrienttep
      241 geiyeesdli irtirdiysd didqilidee dsynkardfl ksvmprvvdr lklydgpvpl
      301 fhkynleeei vkinqrqvql kdggsividp tealvaidvn sgnfrgnasa denafrlnvs
      361 aakeiarqlr lrdlggvivn dfidmrkesy rrkvervlrd amakdrartk ilrtspfgli
      421 emtrqrirps lkrsiyqdcp cckgrglvkt pesmsievvr mlalavknkh ivrvtvrvnd
      481 avaaflnnkk rravtemeda gkmtvqilgs eglfpehlev dcrdnhgerv eids
//
LOCUS       WP_392551849              82 aa            linear   BCT 20-JAN-2025
DEFINITION  FeoA family protein [Orbus wheelerorum].
ACCESSION   WP_392551849
VERSION     WP_392551849.1
KEYWORDS    RefSeq.
SOURCE      Orbus wheelerorum
  ORGANISM  Orbus wheelerorum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Orbales; Orbaceae; Orbus.
REFERENCE   1  (residues 1 to 82)
  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 82)
  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 82)
  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 10004922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Orbus wheelerorum"
                     /db_xref="taxon:3074111"
     Protein         1..82
                     /product="FeoA family protein"
                     /GO_function="GO:0046914 - transition metal ion binding
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=8795
     Region          6..79
                     /region_name="FeoA"
                     /note="Fe2+ transport protein FeoA [Inorganic ion
                     transport and metabolism]; COG1918"
                     /db_xref="CDD:441522"
ORIGIN      
        1 mnipvltldr lpfgkeavia kllpeslpfr rkllamgitp gcqvsvirga plgdpleikm
       61 rgftlclrrk eaasiavvev ak
//
LOCUS       WP_392552489             408 aa            linear   BCT 20-JAN-2025
DEFINITION  bifunctional acetylornithine/succinyldiaminopimelate transaminase
            [Orbus wheelerorum].
ACCESSION   WP_392552489
VERSION     WP_392552489.1
KEYWORDS    RefSeq.
SOURCE      Orbus wheelerorum
  ORGANISM  Orbus wheelerorum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Orbales; Orbaceae; Orbus.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Ledwidge,R. and Blanchard,J.S.
  TITLE     The dual biosynthetic capability of N-acetylornithine
            aminotransferase in arginine and lysine biosynthesis
  JOURNAL   Biochemistry 38 (10), 3019-3024 (1999)
   PUBMED   10074354
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: BlastRule
            Evidence Accession :: NBR008112
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Orbus wheelerorum"
                     /db_xref="taxon:3074111"
     gene            1..408
                     /gene="argD"
                     /gene_synonym="dapC"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
     Protein         1..408
                     /product="bifunctional
                     acetylornithine/succinyldiaminopimelate transaminase"
                     /EC_number="2.6.1.11"
                     /EC_number="2.6.1.17"
                     /calculated_mol_wt=44275
     Region          5..406
                     /region_name="argD"
                     /note="acetylornithine/succinyldiaminopimelate
                     transaminase; PRK05093"
                     /db_xref="CDD:179933"
     Site            order(108..110,142..143,145,194,227,229..230,256)
                     /site_type="active"
                     /note="inhibitor-cofactor binding pocket [active]"
                     /db_xref="CDD:99735"
     Site            order(109..110,142..143,194,227,230,256)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99735"
     Site            256
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99735"
ORIGIN      
        1 mtyknnhlit rdifdkvilp vyapaqfipv kgkgsrvwdq dgeeyidfag giavnalghc
       61 hpnlvkalhe qseklwhvsn vftnepalql akklidhtfa drvffansga eaneaalkla
      121 rhyaiekysp yktkiisfth sfhgrtfftv svggqakysd gfgpkpadiv hvpfndldav
      181 kaiiddhtca vilepvqgeg gltcatpefl tgvralcdef nallifdevq cgmgrtgtlf
      241 tyeqygvtpd iltsakalgg gfpisamltt eavssvmhpg vhgttyggnp lacavgcaaf
      301 dtinsdevla giyakralfi aelekinqqf dlfsqykgkg lllgaelntk yqgkardfln
      361 tatqfkvmil nagtsvlrft pslvisdqei kegmarfasa vkkvisay
//
LOCUS       WP_392552944             152 aa            linear   BCT 20-JAN-2025
DEFINITION  JAB domain-containing protein [Orbus wheelerorum].
ACCESSION   WP_392552944
VERSION     WP_392552944.1
KEYWORDS    RefSeq.
SOURCE      Orbus wheelerorum
  ORGANISM  Orbus wheelerorum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Orbales; Orbaceae; Orbus.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Attaiech,L., Granadel,C., Claverys,J.P. and Martin,B.
  TITLE     RadC, a misleading name?
  JOURNAL   J Bacteriol 190 (16), 5729-5732 (2008)
   PUBMED   18556794
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Ambroggio,X.I., Rees,D.C. and Deshaies,R.J.
  TITLE     JAMM: a metalloprotease-like zinc site in the proteasome and
            signalosome
  JOURNAL   PLoS Biol 2 (1), E2 (2004)
   PUBMED   14737182
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449512
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Orbus wheelerorum"
                     /db_xref="taxon:3074111"
     Protein         1..152
                     /product="JAB domain-containing protein"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=16882
     Region          <14..152
                     /region_name="RadC"
                     /note="DNA repair protein RadC, contains a
                     helix-hairpin-helix DNA-binding motif [Replication,
                     recombination and repair]; COG2003"
                     /db_xref="CDD:441606"
ORIGIN      
        1 mtitvtnehd lniinqakai iaksihtgkk lcspndvkdy lilnlglldy eefcvlylnn
       61 qnqviafeel frgtinetsv ypreiakqvl cynavsvilv hnhpsgessp spadinltqk
      121 ieqalslidv qvldhfivak heivsmkklg li
//
LOCUS       WP_392554244             279 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Rhodopirellula sp. JB055].
ACCESSION   WP_392554244
VERSION     WP_392554244.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula sp. JB055
  ORGANISM  Rhodopirellula sp. JB055
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 279)
  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 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   3  (residues 1 to 279)
  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   4  (residues 1 to 279)
  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 279)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Rhodopirellula sp. JB055"
                     /db_xref="taxon:3342846"
     Protein         1..279
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31474
     Region          32..264
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <161..264
                     /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 mrspdsnptm sgaiiteval vdqvkrrerg afrseslpgh lihvctagev eqrsagvsqr
       61 fgagdaiwyh eneivqgkvl qppwkfftvn frapsllppp ldqrvcsvse stlermdrll
      121 svwrdrndse vkrhllvhai lleviadllp aqtqglridt paqlwweivs elrtnldgsi
      181 dlrllermsg rsqrsiarac rlatgmppmk rvkqirlsya rglvqlsdls mteiamrigy
      241 prvqefsrdy hanydvtpsa drkagpdyrd atrdeeasd
//
LOCUS       WP_392556960             165 aa            linear   BCT 20-JAN-2025
DEFINITION  response regulator [Rhodopirellula sp. JB055].
ACCESSION   WP_392556960
VERSION     WP_392556960.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula sp. JB055
  ORGANISM  Rhodopirellula sp. JB055
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 165)
  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 165)
  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 11467115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Rhodopirellula sp. JB055"
                     /db_xref="taxon:3342846"
     Protein         1..165
                     /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=17799
     Region          12..>131
                     /region_name="PleD"
                     /note="Two-component response regulator, PleD family,
                     consists of two REC domains and a diguanylate cyclase
                     (GGDEF) domain [Signal transduction mechanisms,
                     Transcription]; COG3706"
                     /db_xref="CDD:442920"
ORIGIN      
        1 mttvspnhla hprrcviadd vrvireqlgh wmqelgysvv hascgatalv elrreptdlv
       61 iadidmphvs glhllqtira dadnavaaip vivsssledg eigrmvtalg gsaylkkpvs
      121 kaqmmacvnf lsqdnqsapv ndhscsphsv sakfrriasd fqefd
//
LOCUS       WP_392557866             323 aa            linear   BCT 20-JAN-2025
DEFINITION  uracil-DNA glycosylase [Rhodopirellula sp. JB055].
ACCESSION   WP_392557866
VERSION     WP_392557866.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula sp. JB055
  ORGANISM  Rhodopirellula sp. JB055
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lee,D.H., Liu,Y., Lee,H.W., Xia,B., Brice,A.R., Park,S.H.,
            Balduf,H., Dominy,B.N. and Cao,W.
  TITLE     A structural determinant in the uracil DNA glycosylase superfamily
            for the removal of uracil from adenine/uracil base pairs
  JOURNAL   Nucleic Acids Res 43 (2), 1081-1089 (2015)
   PUBMED   25550433
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Zharkov,D.O., Mechetin,G.V. and Nevinsky,G.A.
  TITLE     Uracil-DNA glycosylase: Structural, thermodynamic and kinetic
            aspects of lesion search and recognition
  JOURNAL   Mutat Res 685 (1-2), 11-20 (2010)
   PUBMED   19909758
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Stivers,J.T. and Drohat,A.C.
  TITLE     Uracil DNA glycosylase: insights from a master catalyst
  JOURNAL   Arch Biochem Biophys 396 (1), 1-9 (2001)
   PUBMED   11716455
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Pearl,L.H.
  TITLE     Structure and function in the uracil-DNA glycosylase superfamily
  JOURNAL   Mutat Res 460 (3-4), 165-181 (2000)
   PUBMED   10946227
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The alpha/beta fold uracil DNA glycosylases: a common origin with
            diverse fates
  JOURNAL   Genome Biol 1 (4), RESEARCH0007 (2000)
   PUBMED   11178247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Rhodopirellula sp. JB055"
                     /db_xref="taxon:3342846"
     Protein         1..323
                     /product="uracil-DNA glycosylase"
                     /EC_number="3.2.2.27"
                     /GO_function="GO:0004844 - uracil DNA N-glycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=35266
     Region          135..321
                     /region_name="Udg4"
                     /note="Uracil-DNA glycosylase [Replication, recombination
                     and repair]; COG1573"
                     /db_xref="CDD:441181"
ORIGIN      
        1 mlelpcndrf fdakthprll mtslnndldp setsdatgel lahlrrvgvr fipqpnaesv
       61 eswqsrwrqa dvpadsnaas gstpavpapa vnaaaaspsa svatakklps apssrlqpve
      121 sftvsddpyp gtnlpiaere taladlastv agctqcslla kcrtqtvfge gnpaarfaff
      181 geapgadedr lgrpfigrag qlldkmvqac klerediyll ntvkcrppen rnpdpselen
      241 crgyyeqqlq ilrpeyivcl gaisahsllk tklsigrlrq rfhqyheskv lviyhpayll
      301 rnpeakkaaw adlqmlmrda gla
//
LOCUS       WP_392558752             535 aa            linear   BCT 20-JAN-2025
DEFINITION  complex I subunit 4 family protein [Orbus mooreae].
ACCESSION   WP_392558752
VERSION     WP_392558752.1
KEYWORDS    RefSeq.
SOURCE      Orbus mooreae
  ORGANISM  Orbus mooreae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Orbales; Orbaceae; Orbus.
REFERENCE   1  (residues 1 to 535)
  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 535)
  AUTHORS   Galemou Yoga,E., Angerer,H., Parey,K. and Zickermann,V.
  TITLE     Respiratory complex I - Mechanistic insights and advances in
            structure determination
  JOURNAL   Biochim Biophys Acta Bioenerg 1861 (3), 148153 (2020)
   PUBMED   31935361
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Friedrich,T. and Scheide,D.
  TITLE     The respiratory complex I of bacteria, archaea and eukarya and its
            module common with membrane-bound multisubunit hydrogenases
  JOURNAL   FEBS Lett 479 (1-2), 1-5 (2000)
   PUBMED   10940377
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Walker,J.E.
  TITLE     The NADH:ubiquinone oxidoreductase (complex I) of respiratory
            chains
  JOURNAL   Q Rev Biophys 25 (3), 253-324 (1992)
   PUBMED   1470679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Orbus mooreae"
                     /db_xref="taxon:3074107"
     Protein         1..535
                     /product="complex I subunit 4 family protein"
                     /GO_component="GO:0045271 - respiratory chain complex I
                     [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048039 - ubiquinone binding [Evidence
                     IEA]"
                     /GO_process="GO:0015990 - electron transport coupled
                     proton transport [Evidence IEA]"
                     /GO_process="GO:0042773 - ATP synthesis coupled electron
                     transport [Evidence IEA]"
                     /calculated_mol_wt=60458
     Region          56..524
                     /region_name="NuoM"
                     /note="NADH:ubiquinone oxidoreductase subunit 4 (chain M)
                     [Energy production and conversion]; COG1008"
                     /db_xref="CDD:440632"
ORIGIN      
        1 mllwlvflpl lggligwlle aslkrsftkm eqcrieqesr fflvnklkse lcyfsagwva
       61 lltmlivfvm mtilsidalt sfyqgqmwvk efdvnwipll gikfhlvldg lsilmgmlvs
      121 tivliailys rkerpsssgl fyfcllfmas aiimlfmamd lflwfflwea vaipfyflit
      181 lwgrrdssas lktngaskfl vytqitsllm llaiislalt nwqitnewtf dynvlmktpi
      241 ssyfefmlml gflaalvvri pllpfhnwfi dahieasttg simisgllvn tsiygllrfv
      301 fplfpnaslt ispfiiilsl ctlfymalsc fnqsdikrli ayahialmsf itavayngsl
      361 fayqgvvlli isislvivgl fiisglltef yltrninnfl glkshvkyls tltlfyllai
      421 lgipgtanfv gnfmtvfssy qnstymaifl iiglillsis iivrtqpify gvidkqqsnk
      481 ksvcfkdlfl ligilvilff iglypqwvld isspplnkiq qiissaqtnl ikgdv
//
LOCUS       WP_392561128             535 aa            linear   BCT 20-JAN-2025
DEFINITION  complex I subunit 4 family protein [Orbus sturtevantii].
ACCESSION   WP_392561128
VERSION     WP_392561128.1
KEYWORDS    RefSeq.
SOURCE      Orbus sturtevantii
  ORGANISM  Orbus sturtevantii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Orbales; Orbaceae; Orbus.
REFERENCE   1  (residues 1 to 535)
  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 535)
  AUTHORS   Galemou Yoga,E., Angerer,H., Parey,K. and Zickermann,V.
  TITLE     Respiratory complex I - Mechanistic insights and advances in
            structure determination
  JOURNAL   Biochim Biophys Acta Bioenerg 1861 (3), 148153 (2020)
   PUBMED   31935361
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Friedrich,T. and Scheide,D.
  TITLE     The respiratory complex I of bacteria, archaea and eukarya and its
            module common with membrane-bound multisubunit hydrogenases
  JOURNAL   FEBS Lett 479 (1-2), 1-5 (2000)
   PUBMED   10940377
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Walker,J.E.
  TITLE     The NADH:ubiquinone oxidoreductase (complex I) of respiratory
            chains
  JOURNAL   Q Rev Biophys 25 (3), 253-324 (1992)
   PUBMED   1470679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Orbus sturtevantii"
                     /db_xref="taxon:3074109"
     Protein         1..535
                     /product="complex I subunit 4 family protein"
                     /GO_component="GO:0045271 - respiratory chain complex I
                     [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048039 - ubiquinone binding [Evidence
                     IEA]"
                     /GO_process="GO:0015990 - electron transport coupled
                     proton transport [Evidence IEA]"
                     /GO_process="GO:0042773 - ATP synthesis coupled electron
                     transport [Evidence IEA]"
                     /calculated_mol_wt=59743
     Region          58..524
                     /region_name="NuoM"
                     /note="NADH:ubiquinone oxidoreductase subunit 4 (chain M)
                     [Energy production and conversion]; COG1008"
                     /db_xref="CDD:440632"
ORIGIN      
        1 mlfllvllpl fgglvgwlsd aflqgsftri gqcrighykr frflnklsde lcgygsswva
       61 llimlitlvi ifilgfdala sfyqgqdwvk sidlawiplf girfhlmldg lsilmnllii
      121 iiviigilys rkeapnspgl fyfcllfmts avmmsfmamd lflwfflwea vvipvyflit
      181 lwgrrdssaq ltingaskfl iytqissllm llsivslalt nwqltnqwtf dydiltktpi
      241 ssyvefllml gflaafivri plapfhswfi dahiessttg simisgllvn taiygllrfv
      301 iplfpnaslt isplmwglsl ltlfycaflc fsqsdikrli ayahvalmsf mtavvysasl
      361 layqgiilqi isvslvivgl fiisgllaer ystrnisqll glkaqvkyls tltlffifav
      421 lgvpgtanfv gnfmaivgsy snasyiaill ivglimlsis iiirihpify gvvdnslpak
      481 kaisikdlcl litilvilff iglypqwvld msypvvskiq hifssaqtnl iegdv
//
LOCUS       WP_392565851             542 aa            linear   BCT 20-JAN-2025
DEFINITION  complex I subunit 4 family protein [Utexia brackfieldae].
ACCESSION   WP_392565851
VERSION     WP_392565851.1
KEYWORDS    RefSeq.
SOURCE      Utexia brackfieldae
  ORGANISM  Utexia brackfieldae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Orbales; Orbaceae; Utexia.
REFERENCE   1  (residues 1 to 542)
  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 542)
  AUTHORS   Galemou Yoga,E., Angerer,H., Parey,K. and Zickermann,V.
  TITLE     Respiratory complex I - Mechanistic insights and advances in
            structure determination
  JOURNAL   Biochim Biophys Acta Bioenerg 1861 (3), 148153 (2020)
   PUBMED   31935361
REFERENCE   3  (residues 1 to 542)
  AUTHORS   Friedrich,T. and Scheide,D.
  TITLE     The respiratory complex I of bacteria, archaea and eukarya and its
            module common with membrane-bound multisubunit hydrogenases
  JOURNAL   FEBS Lett 479 (1-2), 1-5 (2000)
   PUBMED   10940377
REFERENCE   4  (residues 1 to 542)
  AUTHORS   Walker,J.E.
  TITLE     The NADH:ubiquinone oxidoreductase (complex I) of respiratory
            chains
  JOURNAL   Q Rev Biophys 25 (3), 253-324 (1992)
   PUBMED   1470679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Utexia brackfieldae"
                     /db_xref="taxon:3074108"
     Protein         1..542
                     /product="complex I subunit 4 family protein"
                     /GO_component="GO:0045271 - respiratory chain complex I
                     [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048039 - ubiquinone binding [Evidence
                     IEA]"
                     /GO_process="GO:0015990 - electron transport coupled
                     proton transport [Evidence IEA]"
                     /GO_process="GO:0042773 - ATP synthesis coupled electron
                     transport [Evidence IEA]"
                     /calculated_mol_wt=61233
     Region          1..526
                     /region_name="NuoM"
                     /note="NADH:ubiquinone oxidoreductase subunit 4 (chain M)
                     [Energy production and conversion]; COG1008"
                     /db_xref="CDD:440632"
ORIGIN      
        1 mlslliflpm iggilswlvs iffarrsnnl iltdeqtanl tktnsfiqwl kerwfcsgvq
       61 wiaiitmvie lmiilcywhe clqafysnsv wqkdlniewi pflgirfhlm ldglsiimvl
      121 lsvfltlmvi vysgkekhan iglyylcllw casgviglli avdlflfflf wemiaiplyf
      181 livlwgrrds naqlrfngas kfliftqlss llmlisvisl almnlslskn wtfdyfvltn
      241 tpisssaefl lmlgfffafi vrmpllpfhg wfidahiess ttgsmmisgl ltntaiygll
      301 rfvipmfpna siafapvvmg ialcslfyfa llaftqtdik kliayvhval msfltamiym
      361 gniltyqgii iqliaislti tglfmvsgll teryltrnik qfiglrgvvn ylpaftvffv
      421 laifgipgta nfvgnlmllf gsytkyamms vlfafglllv siallirmqp ifyglttskt
      481 vkisviykal akqdiamlml lvlilvaigv ypqmildtsy piinkiqyyl egsqmimike
      541 ga
//
LOCUS       WP_392566064             292 aa            linear   BCT 20-JAN-2025
DEFINITION  heme/hemin ABC transporter substrate-binding protein [Utexia
            brackfieldae].
ACCESSION   WP_392566064
VERSION     WP_392566064.1
KEYWORDS    RefSeq.
SOURCE      Utexia brackfieldae
  ORGANISM  Utexia brackfieldae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Orbales; Orbaceae; Utexia.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Naoe,Y., Nakamura,N., Rahman,M.M., Tosha,T., Nagatoishi,S.,
            Tsumoto,K., Shiro,Y. and Sugimoto,H.
  TITLE     Structural basis for binding and transfer of heme in bacterial
            heme-acquisition systems
  JOURNAL   Proteins 85 (12), 2217-2230 (2017)
   PUBMED   28913898
REFERENCE   2  (residues 1 to 292)
  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   3  (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   4  (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   5  (residues 1 to 292)
  AUTHORS   Ho,W.W., Li,H., Eakanunkul,S., Tong,Y., Wilks,A., Guo,M. and
            Poulos,T.L.
  TITLE     Holo- and apo-bound structures of bacterial periplasmic
            heme-binding proteins
  JOURNAL   J Biol Chem 282 (49), 35796-35802 (2007)
   PUBMED   17925389
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Utexia brackfieldae"
                     /db_xref="taxon:3074108"
     Protein         1..292
                     /product="heme/hemin 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=31288
     Region          23..283
                     /region_name="ChuT"
                     /note="ABC-type hemin transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG4558"
                     /db_xref="CDD:443619"
ORIGIN      
        1 mmksiyslgy iviglcglli syvvandriv tsggsiteiv yalqagdrvv gvdmsstypp
       61 hvkqlpqigy wkqlsiegll slkptifigw ddsgpaqise qlkqaniqtl ylkrvpntld
      121 lllsnvesig kaidqpveae qliaqiksqv aqttaqvkqy qhkptvlfll smagatqvag
      181 kntvvdsiiq laggeniaqh anyknysaea fitanpaili vttqslqaig gldnlanipg
      241 lthtqawqnr riiaidqali lgmgprvgea ltilaagfyp ssdtnidkpp sh
//
LOCUS       WP_392566222             407 aa            linear   BCT 20-JAN-2025
DEFINITION  bifunctional acetylornithine/succinyldiaminopimelate transaminase
            [Utexia brackfieldae].
ACCESSION   WP_392566222
VERSION     WP_392566222.1
KEYWORDS    RefSeq.
SOURCE      Utexia brackfieldae
  ORGANISM  Utexia brackfieldae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Orbales; Orbaceae; Utexia.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Ledwidge,R. and Blanchard,J.S.
  TITLE     The dual biosynthetic capability of N-acetylornithine
            aminotransferase in arginine and lysine biosynthesis
  JOURNAL   Biochemistry 38 (10), 3019-3024 (1999)
   PUBMED   10074354
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: BlastRule
            Evidence Accession :: NBR008112
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Utexia brackfieldae"
                     /db_xref="taxon:3074108"
     gene            1..407
                     /gene="argD"
                     /gene_synonym="dapC"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
     Protein         1..407
                     /product="bifunctional
                     acetylornithine/succinyldiaminopimelate transaminase"
                     /EC_number="2.6.1.11"
                     /EC_number="2.6.1.17"
                     /calculated_mol_wt=44063
     Region          4..406
                     /region_name="argD"
                     /note="acetylornithine/succinyldiaminopimelate
                     transaminase; PRK05093"
                     /db_xref="CDD:179933"
     Site            order(108..110,142..143,145,194,227,229..230,256)
                     /site_type="active"
                     /note="inhibitor-cofactor binding pocket [active]"
                     /db_xref="CDD:99735"
     Site            order(109..110,142..143,194,227,230,256)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99735"
     Site            256
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99735"
ORIGIN      
        1 mpqsidqsvn ralfdkvilp vyapapfipv kgegsrvwdq qhneyidfag giavnalghc
       61 hpklvsalka qshklwhvsn vftnepalkl aqrltentfa drvffansga eaneaafkla
      121 rryaietysp yktkiiafyq afhgrtlftv svggqakysd gfgpkpadii hvpfndlaav
      181 kavmddhtca vviepiqgeg gvtpatpefl qglrqlcdqf nallvfdevq cgmgrigslf
      241 aymdygvvpd iltsakalgg gfpisamltt hkvaqvmhpg vhgttyggnl lacavglavf
      301 dvintpevlk gvaarrnafi eqletinqqf kvftgyrgkg lllgaelspq yhdksshfla
      361 vaaefkvlil nagpnilrft pslvitdeei kdgmnrfaka vakivqa
//
LOCUS       WP_392567305             507 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Micromonospora echinofusca].
ACCESSION   WP_392567305
VERSION     WP_392567305.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 507)
  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 507)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..507
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=52988
     Region          243..411
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 mpslrgirtg asrfvrsrwa rramtvaalv avtsvgvivg vvlggrgesd vgpfrvafhv
       61 slaadggtev avpplgslfl dshegparlt arldsldqrr tealindpaa laragetapq
      121 dlrdalvrlg lrtlgvavla smllaavtfr svrrvawsgg lallitggtl gtaaatlrpq
      181 alaepryegl lanapaligd aqriaddygr yaeqlqrlvg nvgklyatvs slpiyqaspd
      241 ttrllhvsdl hlnpaawpvi ktvvdqydid avidtgditd wgsepettyv smishldvpy
      301 vyirgnhdsp rtaaavasqp navvldnsvt lvaglriagi adprftpdkr eeasgpwdes
      361 pttvegagel lattiralda pvdlalvhdp asapalngla pvvlaghthr revtvlpptg
      421 evttrlvvqg stggaglrgl egdeptplam svlylgpdrq lkayddirvg gtgtaqvsld
      481 rkvieappvg vpptsgaptp vvrpanr
//
LOCUS       WP_392568794             599 aa            linear   BCT 20-JAN-2025
DEFINITION  sensor histidine kinase [Stutzerimonas stutzeri].
ACCESSION   WP_392568794
VERSION     WP_392568794.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas stutzeri (Pseudomonas stutzeri)
  ORGANISM  Stutzerimonas stutzeri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
REFERENCE   1  (residues 1 to 599)
  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 599)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20493667
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Stutzerimonas stutzeri"
                     /db_xref="taxon:316"
     Protein         1..599
                     /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=66972
     Region          38..267
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          229..586
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mtppepprrp rwrnlalval llapllwplq elaeryyrne lteqnrqtld lyvanllgsl
       61 rryevlpril gdlptlrsal rqpaspaakd qanrlldqlr ketgadviyl mapdgntlaa
      121 snwndedsfv drnfafrpyf reamagklgr ffglgttsgk rgyyfgaavr dgdavlgvlv
      181 vkvdldhtet lwgttpeqlm vtdsfgvvil tskpewrfra sraldidere qiasdrpypt
      241 ltpqdltldi dtwliqsrel ketgwtvril apislverpv qtvvaigaat laalllllgl
      301 lmqrrrhyle rialdakarq qlerrvqert qdlealnsrl kqevlereqa qqelvraqde
      361 llqagklsal gtmsasishe lnqplgairs yadnarvlld qqrndeardn lkliseltar
      421 masiiahlra farrdrhape rvalqpsldd alallakrrq amgvelirdl peatlwvqag
      481 etrlrqilsn llanaldaln erppgrriwl raerqgdgvl ltlrdngpgf satalqrare
      541 pffttktsaq glglglaicd tltraldgql tmanhpegga qlslylrsad pgvafpsed
//
LOCUS       WP_392568824             549 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Stutzerimonas stutzeri].
ACCESSION   WP_392568824
VERSION     WP_392568824.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas stutzeri (Pseudomonas stutzeri)
  ORGANISM  Stutzerimonas stutzeri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
REFERENCE   1  (residues 1 to 549)
  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 11459492
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Stutzerimonas stutzeri"
                     /db_xref="taxon:316"
     Protein         1..549
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=61740
     Region          8..532
                     /region_name="YcbB"
                     /note="Murein L,D-transpeptidase YcbB/YkuD [Cell
                     wall/membrane/envelope biogenesis]; COG2989"
                     /db_xref="CDD:442228"
ORIGIN      
        1 mykkqaprli nmmllvpila iaqpaneppn pirtaletlp sacavpland pvarqqltel
       61 yhrhqftplw rsyaqldalq eqlqalvddg lnpaiyhpda irravqtstt dplhracadi
      121 latasyltal rhlaygrlpq dhlepvwrsp gaaapqpldd pllqiadegl aqlehafnka
      181 rpsleqyhnl rkaharlrae ppsqwlpipp getlrvgmsd prvtplrlrl asdgyllnap
      241 aqgsidtrfs qeveqalkaf qrqhglqpdg vlgvetlgal nvtssqrlnq lkinlerfrw
      301 lsrdieprsl lvdiaggrvi yfrdnrpqwe argqvgrdtr qtpaiksnvt rltlnptwtv
      361 pptilredkl priredlnyl aeqnmhvldy qgnvldpaqi dwsnpgnill rqaagphnpl
      421 grlvirfanp fsiylhdtps qglfarsqra fssgcvrves vmqlanlllt epererfnrl
      481 latgrthefg laqptpvllg ywtaeansag qahyrpdiyh rdtpllaalq dadrhdllrr
      541 ttlkeskrh
//
LOCUS       WP_392570180             274 aa            linear   BCT 20-JAN-2025
DEFINITION  aldo/keto reductase [Stutzerimonas stutzeri].
ACCESSION   WP_392570180
VERSION     WP_392570180.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas stutzeri (Pseudomonas stutzeri)
  ORGANISM  Stutzerimonas stutzeri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
REFERENCE   1  (residues 1 to 274)
  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 274)
  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   3  (residues 1 to 274)
  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   4  (residues 1 to 274)
  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 10790928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Stutzerimonas stutzeri"
                     /db_xref="taxon:316"
     Protein         1..274
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /calculated_mol_wt=30287
     Region          1..274
                     /region_name="YdhF"
                     /note="Predicted oxidoreductase YdhF [General function
                     prediction only]; COG4989"
                     /db_xref="CDD:444013"
ORIGIN      
        1 mmrlmqytel aqpqdllsfi ercverglsg fdhadiyggg eceahfgaal klspalrqqi
       61 qligkadivp aeqdrsrwqv khyntearyl ieavegtlkr lgverldgfl lhrpdpllri
      121 hevartlddl vssgkvgwlg vsnaellqcq vlarelplrc nqielslqaq dyawdgrlhg
      181 leaeglqvla wspmaggrfv ptlqtvleev gdalgatanq valawvrklp gcpvpilgsl
      241 rwerieealn gvhlqldtpt wfhlaeaarg hava
//
LOCUS       WP_392570778             273 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptosporangium
            sandarakinum].
ACCESSION   WP_392570778
VERSION     WP_392570778.1
KEYWORDS    RefSeq.
SOURCE      Streptosporangium sandarakinum
  ORGANISM  Streptosporangium sandarakinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Streptosporangium.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 273)
  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 273)
  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 273)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Streptosporangium sandarakinum"
                     /db_xref="taxon:1260955"
     Protein         1..273
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30659
     Region          17..68
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          90..267
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 msafseispd akpldvfgae vrryrkragl tqdrlaeitm fsqsligfie rgertpsrnf
       61 arlcddalra ggelvrlweh vtraasppwf rgwldverea htlhtweplv vpgllqteey
      121 aravlhgepg itdeqvekav earlerqgil srpqrpmlwv vldevvlqrp vggrdvmrrq
      181 lerlldsaes prigiqivpl elgstkgtsg afaiaqiqgr pdtvyiesai ngnvtdrpen
      241 veairarydt iraeanprha sielirkaek sws
//
LOCUS       WP_392571270             401 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptosporangium
            sandarakinum].
ACCESSION   WP_392571270
VERSION     WP_392571270.1
KEYWORDS    RefSeq.
SOURCE      Streptosporangium sandarakinum
  ORGANISM  Streptosporangium sandarakinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Streptosporangium.
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
REFERENCE   3  (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   4  (residues 1 to 401)
  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   5  (residues 1 to 401)
  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   6  (residues 1 to 401)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 401)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 401)
  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 20650276
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Streptosporangium sandarakinum"
                     /db_xref="taxon:1260955"
     Protein         1..401
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41651
     Region          24..72
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          88..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 mitstsdpqp adfadvratn lavvlrfvre hapcsradia astglnkatv sslvadlidr
       61 rlvretglte nrvgrpatml vldgspyaai gveinvdyvt avavdlsger llswrrsfqg
      121 pdvtvpqama vvaglvrrvt trmareerqv lgltvavpgl vgtdgvvrva pnlgwrdadl
      181 cgdlakalrd pgfpvqvdnd anlaalaehr fgpwagtadl vyltggigvg agvildgrlr
      241 rggrgyggei ghiqldplga ecrcgrrgcl eavagigavl ehaalspaev evaleetvrl
      301 artgdahtla vlagvgrdlg rgvsmianll npevvvlggy yvplapwllp eieaeargrv
      361 iapdvggcrv vasalgygaa alggaarvld lvdsgrlpri s
//
LOCUS       WP_392572339             276 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Streptosporangium
            sandarakinum].
ACCESSION   WP_392572339
VERSION     WP_392572339.1
KEYWORDS    RefSeq.
SOURCE      Streptosporangium sandarakinum
  ORGANISM  Streptosporangium sandarakinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Streptosporangium.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415139
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptosporangium sandarakinum"
                     /db_xref="taxon:1260955"
     Protein         1..276
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=30354
     Region          10..252
                     /region_name="LysX"
                     /note="Glutathione synthase, LysX or RimK-type ligase,
                     ATP-grasp superfamily [Amino acid transport and
                     metabolism, Coenzyme transport and metabolism,
                     Translation, ribosomal structure and biogenesis, Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG0189"
                     /db_xref="CDD:439959"
ORIGIN      
        1 msvsaayvtf adpdgmddek etalsawaea gitgrvvrwd dpeadwagfd avvvrspwdy
       61 idrreeflgw arrvervtrl lnpvavlern tdktymrdld apfipthwig pgetpdlpvl
      121 deyvvkpavs agardtirtr drgkaeahaa riaaegrtam vqpyldmvea egetsllyfg
      181 grfshavrrs aalaagsatd rqnsraelrd paadqvalae rvlgelpdll yarvdmvrla
      241 dgtpvliele ltepylflry apgaaerlar aladai
//
LOCUS       WP_392573958             458 aa            linear   BCT 20-JAN-2025
DEFINITION  alpha,alpha-trehalose-phosphate synthase (UDP-forming)
            [Kitasatospora papulosa].
ACCESSION   WP_392573958
VERSION     WP_392573958.1
KEYWORDS    RefSeq.
SOURCE      Kitasatospora papulosa
  ORGANISM  Kitasatospora papulosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Kitasatospora.
REFERENCE   1  (residues 1 to 458)
  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 458)
  AUTHORS   Eastmond,P.J. and Graham,I.A.
  TITLE     Trehalose metabolism: a regulatory role for trehalose-6-phosphate?
  JOURNAL   Curr Opin Plant Biol 6 (3), 231-235 (2003)
   PUBMED   12753972
REFERENCE   3  (residues 1 to 458)
  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   4  (residues 1 to 458)
  AUTHORS   Elbein,A.D., Pan,Y.T., Pastuszak,I. and Carroll,D.
  TITLE     New insights on trehalose: a multifunctional molecule
  JOURNAL   Glycobiology 13 (4), 17R-27R (2003)
   PUBMED   12626396
REFERENCE   5  (residues 1 to 458)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 929-939 (1997)
   PUBMED   9334165
  REMARK    Erratum:[Biochem J 1998 Feb 1;329(Pt 3):719]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Kitasatospora papulosa"
                     /db_xref="taxon:1464011"
     Protein         1..458
                     /product="alpha,alpha-trehalose-phosphate synthase
                     (UDP-forming)"
                     /EC_number="2.4.1.15"
                     /GO_function="GO:0003825 - alpha,alpha-trehalose-phosphate
                     synthase (UDP-forming) activity [Evidence IEA]"
                     /GO_process="GO:0005992 - trehalose biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50376
     Region          7..458
                     /region_name="OtsA"
                     /note="Trehalose-6-phosphate synthase, GT20 family
                     [Carbohydrate transport and metabolism]; COG0380"
                     /db_xref="CDD:440149"
ORIGIN      
        1 mvsehaaqvl vasnrgpvsy trrddgtlds krgggglvsg lsavddklwv caalsdgdre
       61 avrrgvsepg vrmldidaav hadayngian svlwfvhhmi yqtpvepvfd aefrrqwasy
      121 eaynqafaqa laeeagegaa vlvqdyhlsl vpgilrelrp dlrighfsht pwapvdyfrl
      181 lpddigeqll kgilgadraa fltrrwadaf igccteilgg tgrtrigvhg lgadaeflrr
      241 rsreadvder meilreqvga drrtivrvdr telsknivrg lhayrallee rpewrervvh
      301 iafaypsrqd lavyrdytae vqrvadgina eygtagwtpv llhvdddfar slaayrladv
      361 alvnpirdgm nlvakevpvv sdqggalvls reagayeelg edalvvnpyd vsataaalhe
      421 altmepgers arskrladaa talppqqwfl dqldalrs
//
LOCUS       WP_392574392             411 aa            linear   BCT 20-JAN-2025
DEFINITION  S1 family peptidase [Streptomyces yangpuensis].
ACCESSION   WP_392574392
VERSION     WP_392574392.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces yangpuensis
  ORGANISM  Streptomyces yangpuensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Querino Lima Afonso,M., da Fonseca,N.J. Jr., de Oliveira,L.C.,
            Lobo,F.P. and Bleicher,L.
  TITLE     Coevolved Positions Represent Key Functional Properties in the
            Trypsin-Like Serine Proteases Protein Family
  JOURNAL   J Chem Inf Model 60 (2), 1060-1068 (2020)
   PUBMED   31895561
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Waldner,B.J., Kraml,J., Kahler,U., Spinn,A., Schauperl,M.,
            Podewitz,M., Fuchs,J.E., Cruciani,G. and Liedl,K.R.
  TITLE     Electrostatic recognition in substrate binding to serine proteases
  JOURNAL   J Mol Recognit 31 (10), e2727 (2018)
   PUBMED   29785722
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Pelc,L.A., Chen,Z., Gohara,D.W., Vogt,A.D., Pozzi,N. and Di Cera,E.
  TITLE     Why Ser and not Thr brokers catalysis in the trypsin fold
  JOURNAL   Biochemistry 54 (7), 1457-1464 (2015)
   PUBMED   25664608
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Perona,J.J. and Craik,C.S.
  TITLE     Evolutionary divergence of substrate specificity within the
            chymotrypsin-like serine protease fold
  JOURNAL   J Biol Chem 272 (48), 29987-29990 (1997)
   PUBMED   9374470
REFERENCE   5  (residues 1 to 411)
  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 10595581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Streptomyces yangpuensis"
                     /db_xref="taxon:1648182"
     Protein         1..411
                     /product="S1 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=41960
     Region          198..374
                     /region_name="Trypsin_2"
                     /note="Trypsin-like peptidase domain; pfam13365"
                     /db_xref="CDD:433149"
ORIGIN      
        1 mrrrltvaaa aaallvsagp lpvagaegav avaagrwgth eaesfwtper masarplppg
       61 paepraaapq davapeppvd pvdpaapsdp sapgvpvpma pvapappfpp lppgepdepd
      121 epvrpvdpsp vttpspsasp ttpmpkptpt pvtlpapapv rpalpripaa gpgvgqdfgg
      181 lpvvgrmflv kgggsyfcta svvaspgrnl iisaahcltg adtqqvafvp qytrakprpf
      241 gmfpvlrtaa grskiwidqr yrtqgvnraa aldvafaqvg pgpkgfrvqd vvggnrlvtg
      301 agyaharatl ighpsaaarp rlcvnrttky tstdsripgs flriactgyp ggtsggpfll
      361 rldgrtgtgd vvgviggwkt ggdrpdvsys syfgadirkl yekavagaka s
//
LOCUS       WP_392575228             413 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces yangpuensis].
ACCESSION   WP_392575228
VERSION     WP_392575228.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces yangpuensis
  ORGANISM  Streptomyces yangpuensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 413)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Streptomyces yangpuensis"
                     /db_xref="taxon:1648182"
     Protein         1..413
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=42938
     Region          73..254
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          260..387
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mgrtrvnlqp irgrartglp alllgaallf ttacgggggg nnngsgsdna ggggktgtea
       61 skavvnvkpd dgakevatsg vlkitstggk lstvtvadtk gnavegklsp dgasweparh
      121 lasateykvh avakdeagre sakdtsfttl tptntfvghy tpedgatvgv gmpvsinftr
      181 gitnpeavek aitvtaepav aieghwfgnd rldfrpenyw aagtkvtvkl aldgvegrpg
      241 vygkqtrtvt ftigrsqvst vdaaahtmqv vrdgqvlkdv pitagapstt tyngqmvise
      301 kykvtrmnga tvgfggeydi sdvphamrls qsgtfvhgny waspgtfgsa nvshgcvglk
      361 dvrgagdskq paawffdesl igdviivkns kdkqiapdng lngwnmpwae wik
//
LOCUS       WP_392575412             406 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces yangpuensis].
ACCESSION   WP_392575412
VERSION     WP_392575412.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces yangpuensis
  ORGANISM  Streptomyces yangpuensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 406)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Streptomyces yangpuensis"
                     /db_xref="taxon:1648182"
     Protein         1..406
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43638
     Region          56..243
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          249..375
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mtrragagla avavwagllg glaactrdgk spveiqlpgr vrspdeairi tpddnakdvp
       61 adgrltvtvp egrlervvvt kvedaqaeev pgaiapdgls wsptpqagrl alaakytvda
      121 valdghnrrq arrttfttyv peerfigyfk penrstvgtg mivsfkfsra ierraevera
      181 iritaepave iaahwfgker ldfrpkqywk pgtkvtvrma lrdvegapgs ygiqsktvtf
      241 tvgrsqistv daaahtmevr rdgellstvp isagapkttt yngkmvvmel fdvtrmngqt
      301 vgfggeydip dvphamrltn sgtflhgnyw sspdtfgstn vshgcvglrd dkgggsdtpa
      361 gwffdrtlig dvievvnsqd ktvaadnglg gwnmswadwv agsala
//
LOCUS       WP_392576255             425 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptomyces yangpuensis].
ACCESSION   WP_392576255
VERSION     WP_392576255.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces yangpuensis
  ORGANISM  Streptomyces yangpuensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 425)
  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 16057555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Streptomyces yangpuensis"
                     /db_xref="taxon:1648182"
     Protein         1..425
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=44247
     Region          76..257
                     /region_name="Big_10"
                     /note="Bacterial Ig domain; pfam17964"
                     /db_xref="CDD:465591"
     Region          263..395
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mewrvrtdsk rrrrslaais vvlggvlvls acndggdkgg dpkssgeask sqadvdaaaa
       61 kdaskakiti spkdgatnvg lndaanvava dgtltkvelk tsegtavagd iaadgkswkp
      121 kgalkrstky alsatakdad gkeahenasf ttvspensfv asfvpeegqt vgvgmpvsit
      181 fnkaikdkka vqagitvsss sgqevvghwf saqrldfrpe qywqagstvt lklalegvqg
      241 apgvqgvqsk tvtfkigrsq vstvdaktkk mtvtrdgavi ktipisagap anptyngqmv
      301 isekfketrm ngatvgftda dgkgeydikd vphamrlsns gtflhgnywg adsifgsvnt
      361 shgcvglndv kgagdpnqpa awfydnslig dvvtvvnspd ktikpdngln gwnmswadwk
      421 agsaa
//
LOCUS       WP_392576317             517 aa            linear   BCT 20-JAN-2025
DEFINITION  complex I subunit 4 family protein [Streptomyces yangpuensis].
ACCESSION   WP_392576317
VERSION     WP_392576317.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces yangpuensis
  ORGANISM  Streptomyces yangpuensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 517)
  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 517)
  AUTHORS   Galemou Yoga,E., Angerer,H., Parey,K. and Zickermann,V.
  TITLE     Respiratory complex I - Mechanistic insights and advances in
            structure determination
  JOURNAL   Biochim Biophys Acta Bioenerg 1861 (3), 148153 (2020)
   PUBMED   31935361
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Friedrich,T. and Scheide,D.
  TITLE     The respiratory complex I of bacteria, archaea and eukarya and its
            module common with membrane-bound multisubunit hydrogenases
  JOURNAL   FEBS Lett 479 (1-2), 1-5 (2000)
   PUBMED   10940377
REFERENCE   4  (residues 1 to 517)
  AUTHORS   Walker,J.E.
  TITLE     The NADH:ubiquinone oxidoreductase (complex I) of respiratory
            chains
  JOURNAL   Q Rev Biophys 25 (3), 253-324 (1992)
   PUBMED   1470679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Streptomyces yangpuensis"
                     /db_xref="taxon:1648182"
     Protein         1..517
                     /product="complex I subunit 4 family protein"
                     /GO_component="GO:0045271 - respiratory chain complex I
                     [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0048039 - ubiquinone binding [Evidence
                     IEA]"
                     /GO_process="GO:0015990 - electron transport coupled
                     proton transport [Evidence IEA]"
                     /GO_process="GO:0042773 - ATP synthesis coupled electron
                     transport [Evidence IEA]"
                     /calculated_mol_wt=53787
     Region          4..514
                     /region_name="NuoM"
                     /note="NADH:ubiquinone oxidoreductase subunit 4 (chain M)
                     [Energy production and conversion]; COG1008"
                     /db_xref="CDD:440632"
ORIGIN      
        1 mqfllaflva apllgavaal lpappglkgr speqavlrhg vtvtgvilaa aialalgfdh
       61 daparfqatt diswipaldv rihlgvdgis lpllvmtall fflcalysyf klpagpspka
      121 fvalllvles gtlatfavld lllfflafem vlipmyflia rwggaqrqaa awkfilytll
      181 gsvvmllgll ligvtadtfd mvalasdngr elsrttqlla vlaigtglav ktpmwplhtw
      241 lpdahtaapt vgsvllagvl lkmgtygfvr illpvtpegm aafapylgaf avvgivygsl
      301 aclalarkgn kgdlkrliay ssvghmgfvl lgiasmtptg vngalfania hglitgllff
      361 lvgalkdryg tadldtlaga tgaalygrap rfgallafaa vaslglpgla gfwgemlalf
      421 gafdpaqglp rpafltytav gafgtlltaa yllvvvrrvc mgdpktgpel tvadvqhyel
      481 aawtplvalt vlaglwpall lgltdpavqq llaggns
//
LOCUS       WP_392576587             252 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Streptomyces yangpuensis].
ACCESSION   WP_392576587
VERSION     WP_392576587.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces yangpuensis
  ORGANISM  Streptomyces yangpuensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11440233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Streptomyces yangpuensis"
                     /db_xref="taxon:1648182"
     Protein         1..252
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=26888
     Region          22..252
                     /region_name="GCD1"
                     /note="NDP-sugar pyrophosphorylase, includes eIF-2Bgamma,
                     eIF-2Bepsilon, and LPS biosynthesis protein s
                     [Translation, ribosomal structure and biogenesis, Cell
                     wall/membrane/envelope biogenesis]; COG1208"
                     /db_xref="CDD:440821"
ORIGIN      
        1 mtddrrsass aaafpaapaq avvlaggqgs rlrpytddrp kpmveipgtg lpiighqlaw
       61 laaegvtdav vscghlagvl qewlaeaplp lrvttvveee plgrggglky aarhlpdpgg
      121 swyatngdvw trfslremaa fhaergavat lalarpripw gvvetnefgh vldfieapls
      181 pypvnagvyv fgpefaallp dlgdherttf prlarerrla gfplpqgayw raidtakdlt
      241 eaarelaaqt ap
//
LOCUS       WP_392576642             139 aa            linear   BCT 20-JAN-2025
DEFINITION  TOBE domain-containing protein [Streptomyces yangpuensis].
ACCESSION   WP_392576642
VERSION     WP_392576642.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces yangpuensis
  ORGANISM  Streptomyces yangpuensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 139)
  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 10007583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Streptomyces yangpuensis"
                     /db_xref="taxon:1648182"
     Protein         1..139
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13326
     Region          1..138
                     /region_name="MopI"
                     /note="Molybdopterin-binding protein MopI [Coenzyme
                     transport and metabolism]; COG3585"
                     /db_xref="CDD:442804"
ORIGIN      
        1 mslsirnqla gtvtavtvge amaavkvrle ggqditaait adavkdlgit tgsavtalvk
       61 atevalatga venisirnrl sgtvvdvaag pamaavrvdv ngggltaavt adavealgla
      121 agssvvalik steislata
//
LOCUS       WP_392576741             216 aa            linear   BCT 20-JAN-2025
DEFINITION  LutC/YkgG family protein [Streptomyces yangpuensis].
ACCESSION   WP_392576741
VERSION     WP_392576741.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces yangpuensis
  ORGANISM  Streptomyces yangpuensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Hwang,W.C., Bakolitsa,C., Punta,M., Coggill,P.C., Bateman,A.,
            Axelrod,H.L., Rawlings,N.D., Sedova,M., Peterson,S.N.,
            Eberhardt,R.Y., Aravind,L., Pascual,J. and Godzik,A.
  TITLE     LUD, a new protein domain associated with lactate utilization
  JOURNAL   BMC Bioinformatics 14, 341 (2013)
   PUBMED   24274019
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Streptomyces yangpuensis"
                     /db_xref="taxon:1648182"
     Protein         1..216
                     /product="LutC/YkgG family protein"
                     /GO_process="GO:0006089 - lactate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23473
     Region          2..214
                     /region_name="LutC"
                     /note="L-lactate utilization protein LutC, contains LUD
                     domain [Energy production and conversion]; COG1556"
                     /db_xref="CDD:441165"
ORIGIN      
        1 mtsrdrvlar irravpqpgp dpgpgadpgi prdylrvhap rtphervdll asnlteyrak
       61 vhrtdedglp pllmrlladr gsrtvlvppg lppywlsaad qtrvhdrrda taqdldrvds
      121 vvtgcalava etgtivldga pdqgrrritl ipdhhvcvir vpdqvvdsvp qaldrldpar
      181 tltwisgpsa tsdieldrve gvhgprtlev vllgaq
//
LOCUS       WP_003524483             322 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Enterocloster clostridioformis].
ACCESSION   WP_003524483
VERSION     WP_003524483.1
KEYWORDS    RefSeq.
SOURCE      Enterocloster clostridioformis
  ORGANISM  Enterocloster clostridioformis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Enterocloster.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Enterocloster clostridioformis"
                     /db_xref="taxon:1531"
     Protein         1..322
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36105
     Region          6..274
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 meklmdlhmh syysddgefs pgelvrqcgm ngirimsiad hnsvraneag rqaalragit
       61 yvsgieidct frgvnlhvlg ygiddtshdf tciednirsq aaaassqmlc atremgfevt
      121 aedmaglage hywkdrwtge mfaevllgre eykehplllp yrvggargdn pfvnfywdfy
      181 sqgkccyvkm eypqleevvd tihrnggyav lahpgvnlkd raelldpile agvdgieafs
      241 syhsqeqaaf yhkaacgrfr mitcgsdyhg ktkpsisigg hgctvpyeem vrqlgrilge
      301 merkersrgt rmkvpemndr ri
//
LOCUS       WP_003525056             244 aa            linear   BCT 20-JAN-2025
DEFINITION  3-deoxy-manno-octulosonate cytidylyltransferase [Enterocloster
            clostridioformis].
ACCESSION   WP_003525056
VERSION     WP_003525056.1
KEYWORDS    RefSeq.
SOURCE      Enterocloster clostridioformis
  ORGANISM  Enterocloster clostridioformis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Enterocloster.
REFERENCE   1  (residues 1 to 244)
  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 244)
  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 10118537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Enterocloster clostridioformis"
                     /db_xref="taxon:1531"
     Protein         1..244
                     /product="3-deoxy-manno-octulosonate cytidylyltransferase"
                     /EC_number="2.7.7.38"
                     /GO_function="GO:0008690 - 3-deoxy-manno-octulosonate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0033468 -
                     CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28139
     Region          2..238
                     /region_name="CMP-KDO-Synthetase"
                     /note="CMP-KDO synthetase catalyzes the activation of KDO
                     which is an essential component of the lipopolysaccharide;
                     cd02517"
                     /db_xref="CDD:133010"
     Site            order(8..10,49,76,96,98)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133010"
     Site            order(121,138,144..146,152..153,155..161,169,194..195,
                     198..200,207..210)
                     /site_type="active"
                     /note="oligomer interface [active]"
                     /db_xref="CDD:133010"
ORIGIN      
        1 mkvvgiipar ygstrlpgkp lkdicgkpml wwvynrvygi eqldevyvat ddtrieavck
       61 qyempviltr ndhrtgahrl qevsehisad fylqlngdep lidtraitaa ipekvpqnke
      121 ygtniitpmh epsqvldptn ikmifdsnmr alymsrgamp ypyksidfly ykhvgiigyn
      181 kkmldfykds fpgrlerieg idtlrfldyg kelqlfived ckclsvdtek dleevrrimg
      241 evne
//
LOCUS       WP_003526158             430 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Sinorhizobium meliloti].
ACCESSION   WP_003526158
VERSION     WP_003526158.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 430)
  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 430)
  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 430)
  AUTHORS   ter Beek,J., 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 430)
  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 430)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     Protein         1..430
                     /product="CmpA/NrtA family 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=46716
     Region          40..301
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mtktstsglt rrsllkttat aamvgaaktl lpsgafaqga gpettkavlg fialtdsapl
       61 viakekgffd kygmtevevv kqaswgttrd nlvlgsagag idgshiltpm pylistgkvt
      121 qnnqplpmvi larlnldaqa isvgaayadl kagldasvlk eafakkkaeg aaakvamtfp
      181 ggthdlwiry wlaaggidpd rdvetivvpp pqmvanmkvg tmdcfcvgep wneqlvnqki
      241 gytavntaei wtkhpeksfa mradwveknp raakalmmav qeaaqwcddm ankdelaklv
      301 gkrswfnvpa kdivdrlkge ydygngkvve nsphfmkfwr dhasypfqsh dawfltenir
      361 wgklapdtdi kgliakvnre diwreaakel gvtdipasts rgtetffdgk vfdpenpeay
      421 lkslaisria
//
LOCUS       WP_003525631             372 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Sinorhizobium].
ACCESSION   WP_003525631
VERSION     WP_003525631.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium
  ORGANISM  Sinorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group.
REFERENCE   1  (residues 1 to 372)
  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 372)
  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   3  (residues 1 to 372)
  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   4  (residues 1 to 372)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 372)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Sinorhizobium"
                     /db_xref="taxon:28105"
     Protein         1..372
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38917
     Region          27..358
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(99..101,122..123,172,224,248)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkksllsava ltamvafsgt awadilvgvg gpltgpnaaf gaqlqkgaeq aaedinaagg
       61 ingeqikvvl gddvsdpkqg vsvaqkfvad gvkfvvghfn sgvsipasei yaengilqvt
      121 pastnpqfte rglwntfrtc grddqqgava gayiaanfkd akvavihdkt pygqgladet
      181 kksmneagvt ealyegintg dkdfsaliak mkqagvsivy ygglhteagl imrqmkdqgl
      241 katmmsgdgi vsnelasiag davdgtlmtf apdprkspaa kdlvekfraa gfepeaytly
      301 ayaalqviae gakaagntdp qavaeaikak gpfktaigel gfdekgditr pdyvmytwkk
      361 gddgkfsyfq ne
//
LOCUS       WP_003528144             205 aa            linear   BCT 20-JAN-2025
DEFINITION  transcription termination/antitermination protein NusG
            [Sinorhizobium meliloti].
ACCESSION   WP_003528144
VERSION     WP_003528144.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Kang,J.Y., Mooney,R.A., Nedialkov,Y., Saba,J., Mishanina,T.V.,
            Artsimovitch,I., Landick,R. and Darst,S.A.
  TITLE     Structural Basis for Transcript Elongation Control by NusG Family
            Universal Regulators
  JOURNAL   Cell 173 (7), 1650-1662 (2018)
   PUBMED   29887376
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Liu,B. and Steitz,T.A.
  TITLE     Structural insights into NusG regulating transcription elongation
  JOURNAL   Nucleic Acids Res 45 (2), 968-974 (2017)
   PUBMED   27899640
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Steiner,T., Kaiser,J.T., Marinkovic,S., Huber,R. and Wahl,M.C.
  TITLE     Crystal structures of transcription factor NusG in light of its
            nucleic acid- and protein-binding activities
  JOURNAL   EMBO J 21 (17), 4641-4653 (2002)
   PUBMED   12198166
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415705
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..205
                     /gene="nusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
     Protein         1..205
                     /product="transcription termination/antitermination
                     protein NusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
                     /calculated_mol_wt=24133
     Region          5..>115
                     /region_name="NusG"
                     /note="Transcription termination/antitermination protein
                     NusG [Transcription]; COG0250"
                     /db_xref="CDD:440020"
ORIGIN      
        1 mnrsrwyair tapgyqrmaa vderlpenrr mesiierncr kdgfdifmps fytelkhhrt
       61 kqilqkrfpf lvgyafvnlp rlnfeelrrv dgvvcflrga nygplefpdv tiealyfaeh
      121 errqaflyeq hcrnenerqe qiqhlrgqlr kilpkgrkar vsmvdqaera idslspqike
      181 rvqkiiseln altgdaevan lrrav
//
LOCUS       WP_003528215             534 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Sinorhizobium meliloti].
ACCESSION   WP_003528215
VERSION     WP_003528215.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     Protein         1..534
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=54711
     Region          <59..>530
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
     Region          <384..533
                     /region_name="Peptidase_M10_C"
                     /note="Peptidase M10 serralysin C terminal; cl23859"
                     /db_xref="CDD:451582"
ORIGIN      
        1 matvtyhfpg glypsqynpp lsgvsvnptf gelvdmsesa rstttstevl yrldnglklk
       61 lvgtgfsfds sgdavggtit siqvllnngt tlvqtingln islelfqdaa aafdnaklen
      121 wlmsgadtin gsagdddisg rggndilngn dgddtitgge gddtydggag fdtlsfqday
      181 nasnafrgin lnastgtvid qfgfsetfqn feqyggtqfa dtmvgssadd ifmglggrdt
      241 inggagvdtv rydrdvdqga skgisinltt glatdsfgsq dtlssienvr atnfkdtivg
      301 nsdsnflraf agadtldgka gadrmrggag ddtyfvenag divdessdsg sgldivrssi
      361 sfslgnttsv kgnvenlslq gssaingtgn alnnvlvgng aantlngdag ndtiigglgn
      421 dtlvgstgld tfffntalna alnvdtingf svaddtirle ngiftaivgt gvltatqfvs
      481 nttglaadad driiyesdtg kllydsdgng aggsvhfatv dtnlaitagd fiit
//
LOCUS       WP_003529423             621 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sensor histidine kinase [Sinorhizobium].
ACCESSION   WP_003529423
VERSION     WP_003529423.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium
  ORGANISM  Sinorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group.
REFERENCE   1  (residues 1 to 621)
  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 621)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20493667
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Sinorhizobium"
                     /db_xref="taxon:28105"
     Protein         1..621
                     /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=66979
     Region          65..250
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          286..618
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mhnvrmvklp aeasdphalr srarrswlvf aavalvllaa glllardygr sqalaglagq
       61 sridaslkas llravverqr alplvladda airgallspd rpsldrinrk lealatsaea
      121 aviylidrsg vavaasnwqe ptsfvgndya frdyfrlavr dgmaehfamg tvsnrpglyi
      181 srrvdgpggp lgvivaklef dgveadwqas gkpayvtdrr givlitslps wrfmttkpia
      241 edrlapires lqfgdapllp lpfrkiearp dgsstldall pgdstaaflr vetmvpstnw
      301 rleqlsplka plaagareaq lltlaalvpl lalaalllrr rqvvamrsae erlarnalea
      361 sveertrdlr mardrletei adhrqttekl qavqqdlvqa nrlailgqva agvaheinqp
      421 vatirayadn artflhrgqt vtaaenmesi aeltervgai tdelrrfark ghfaagptam
      481 kevvegalml lrsrfagrmd airldlppdg lqalgnrirl eqvlinllqn aleaigdsed
      541 gaiqvrceea aggialtvad ngpgiaadvr eelftpfnts kedglglgla iskeivsdyg
      601 gtievesgps gttfavnlkk a
//
LOCUS       WP_003529514             280 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phytoene/squalene synthase family protein
            [Sinorhizobium].
ACCESSION   WP_003529514
VERSION     WP_003529514.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium
  ORGANISM  Sinorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Sinorhizobium"
                     /db_xref="taxon:28105"
     Protein         1..280
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30936
     Region          1..277
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mqqsddqila tlrdtdrdry lacllspaek rhslaalyaf yaeiarvrdm vkeplpgeir
       61 lqwwrdtlen eqsdgaghpl aeallrcire hhlpvrvlqd midarifdly ddpmqdraal
      121 egyagetasa liqlsslild pdnaarsada aghagvaqtv aglllllpvh vgrgqvylpa
      181 ellsatgldr etllagtdes aieravrafc glgrdhlaka regagaisgr nfsafipval
      241 aepvfdraea agarilrqsl qppqwqrqwr mwrasrrref
//
LOCUS       WP_003530737             204 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Sinorhizobium].
ACCESSION   WP_003530737
VERSION     WP_003530737.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium
  ORGANISM  Sinorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group.
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   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   3  (residues 1 to 204)
  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   4  (residues 1 to 204)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 204)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 204)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Sinorhizobium"
                     /db_xref="taxon:28105"
     Protein         1..204
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22389
     Region          11..193
                     /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"
ORIGIN      
        1 mssvhntpnf dgwralilhr phqnvdalfa qcarigiaae qawpdfsrdr saeefnvlli
       61 dadmghdeqf pwrqgeaplp mialigseap griawtiaqg adaqllkpig saglysalmv
      121 ashsfvrrra ldrdvaalkd rlarrqelae atallmlrkn cgaseayqhl rltamsrscs
      181 iedvaaaivq efenhglkna dhgr
//
LOCUS       WP_003534616             274 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Thomasclavelia ramosa].
ACCESSION   WP_003534616
VERSION     WP_003534616.1
KEYWORDS    RefSeq.
SOURCE      Thomasclavelia ramosa (Clostridium ramosum)
  ORGANISM  Thomasclavelia ramosa
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Coprobacillaceae; Thomasclavelia.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Thomasclavelia ramosa"
                     /db_xref="taxon:1547"
     Protein         1..274
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31613
     Region          1..248
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mvyadlhvht aysdgihsie etiklakekg ikviaitdhd tvfhfeevqk vcrqngleti
       61 rgvemscydy dvhkkvhvvg lglnnhpyhv eklcqktlqc rdeyhhelie ilnqkglnit
      121 yedakeyapy nivfkmhlfl aivhkypeyn dinkyrelfm setsldvdsk mgyidikegi
      181 kairedggia iiahpceykn ydeiekyvsy glqgieishp smesedyplt qelanrfhli
      241 rsggsdfhni hltaigdfgl tkeqfdelke emgr
//
LOCUS       WP_003533154             345 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Sinorhizobium meliloti].
ACCESSION   WP_003533154
VERSION     WP_003533154.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     Protein         1..345
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36774
     Region          63..307
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 matriygtny adiikqngyi aveiyaydgd ddiylnrtds yggynfvdag ygndlvvnsy
       61 eggndiylgg gndiyvadir ardtssydiv yggsgndrfe vegyasdyyg esgndtffsv
      121 gfnnyfnggt gtdtisyqfq ddwsaergkg vtidlgynya ttgsgrredl isienatgtn
      181 yghdditgsa vantlrglgg hdiieglggn dvldggsgdd dlyggsgadi lrggtgfdyl
      241 vggtgtdsfd fnsisesavg srrdvitdfh rsefdvidls tidadttwsg nqsftyiggn
      301 afsgeageln frsgiisgdv ngdgyadfqv rvngvtslrv ddffl
//
LOCUS       WP_003531513             409 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Sinorhizobium].
ACCESSION   WP_003531513
VERSION     WP_003531513.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium
  ORGANISM  Sinorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group.
REFERENCE   1  (residues 1 to 409)
  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 409)
  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
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 409)
  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   5  (residues 1 to 409)
  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   6  (residues 1 to 409)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 409)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 409)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Sinorhizobium"
                     /db_xref="taxon:28105"
     Protein         1..409
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43710
     Region          32..75
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          95..394
                     /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 msltdgpytg ppqpdvvdps gganqtrvra ynerlvmslv rrhgslskae iarrsglsaq
       61 tasvimrsle adgllvrgap vrgrvgqpsi pmrlnpdavy sfgvkigrrs adlvlmdflg
      121 tirlhlhqih typlpeeivs fivggigkle gqlgpgergr iagvgiatpf elwnwseevg
      181 apreemdrwr dfdlqaavas rirhpvflqn dgtsacgael afgvgasypd fvyfyigsfi
      241 gggvvinsal fsgrtgtaga vgplpvagkd gkstqllkia svfvlekllr ergidpeplw
      301 ysaddwidfg epleiwiqda aaalaqavvs avsvvdfsaa vidggfppwv rarllaatrk
      361 alqtldlqgv tvpdlvegtv gsharaigga slplfsryll dtnvlfkel
//
LOCUS       WP_003536426             511 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [Sinorhizobium].
ACCESSION   WP_003536426
VERSION     WP_003536426.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium
  ORGANISM  Sinorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Sinorhizobium"
                     /db_xref="taxon:28105"
     Protein         1..511
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=53136
     Region          13..511
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mletvreeld lpapssills pddnvvvata aiapgdrlag gvsavariep ghkaairrid
       61 vgepvvkygq aigratspia pgehvhshnl afdqgrlaig aavppeaase adkartflgy
      121 rradgraatr nyigivasvn csttvcraia deanrrilpk yegidgfvpi vhdqgcgmss
      181 tgdgmknlhr tlagyarhan fggvlmvglg cevnqltlyg qsgagaekrh fniqeaggsr
      241 rsveralgil deiakevaaa rrvpipvsei ivglqcggsd glsgitanpa lgaavdilaa
      301 aggtailset seiygaehll rsravnetva vkldgliaww edyvamhgas ldnnpspgnk
      361 rgglttilek slgavakggr spltavynya ervtepglvf mdtpgydpvs atgqvaggan
      421 viafttgrgs cfgcrpapsi kltsntalyr ameedmdidc gviasgetti adlgrgifel
      481 iietasgrkt kselfgygdn efvpwhlgat l
//
LOCUS       WP_003536193             596 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein/permease
            [Thomasclavelia].
ACCESSION   WP_003536193
VERSION     WP_003536193.1
KEYWORDS    RefSeq.
SOURCE      Thomasclavelia
  ORGANISM  Thomasclavelia
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Coprobacillaceae.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 596)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 596)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Thomasclavelia"
                     /db_xref="taxon:3025755"
     Protein         1..596
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=66453
     Region          1..577
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mllinktlir msegirgwia iitglkiltl vgtvmfakti ssflsdlyhp kmsqeqllaa
       61 iisaliascl iliadlltge aeyrcgakar inlrkeifek mlqldvgkie rigasntiss
      121 vgdgvelmqv yytkylpsll ycffapvylf fqlkdtsllv atilliisls lplvnnyfrk
      181 midqlkkeyw tsfqdltsyy leslkslvtl klfnqdrrrh dnlrrkadtf nqstmsimkm
      241 nfssflvsdg liylgvilav vigcsqlakg tidlaqavll lmlsysffss irqlmsathd
      301 alsgiaatik vdeilnldas rihkseaeta heiavkysqd tlaylqdysg iivkdivfny
      361 hqrrqvlkql sieipkgktt aivgksgcgk stlasmlmrf idpdqgylfl dgqsyfsltp
      421 eevrknivmv pqrvsifsgs leenlklaap nastsellnv lkqvhlyqwl qslpeglstd
      481 lgdsgaklsg gqrqkigiar allsgapyli fdeatssvdr dsedeiwqci nelgltrtli
      541 iishrlstiq radniivlnq grlveqgnhq allkyhgeyy qlvkeqeale aagkvg
//
LOCUS       WP_003534270             633 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Sinorhizobium meliloti].
ACCESSION   WP_003534270
VERSION     WP_003534270.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 633)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 633)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 633)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     Protein         1..633
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68748
     Region          1..633
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 madsldhapa qannlpqfla ltvgaigvvy gdigtsplya frealrpfgp ggvgrdevig
       61 lvslvlwtlt aivtikyvlf llradndgeg gtlsllalll kkgtkypvlm ffagvlgaal
      121 figdamitpa lsvlsavegl klvapalhdy vlpisvviil llfavqsrgt gavsvffgpi
      181 tliwflvmaa agiahigddl ailsafnply avgflwnagl vgfivlgaif ltvtgaealy
      241 adlghfgrhs iqaawftvvf palalnylgq galvlshpda isnpfflmfp twallpmvil
      301 ataatiiasq svitgafsli rqaihlgflp rfeicytset qtgqiylplv ntilltgvla
      361 lmlmfgssea lapaygvsit gamvidtila fefvrrqwgw avltataall pllslevvfl
      421 ganlfkvhhg gyvpiliagt litmmwtwrk gikllrekia rqdiplsrfi amverkseha
      481 pvdvpgtaif ltatpettpa vllhnikhnh vlhkhnvilt iktarvpyvp ekdrytitkl
      541 sdrfsllelr fgfmddqnvs ralarcrkeg fkfeimstsf ylgrrkliad aqfglprwqd
      601 klfiamadsa idpteyfhlp pnrvvelgeq vii
//
LOCUS       WP_003538145             178 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Thomasclavelia].
ACCESSION   WP_003538145
VERSION     WP_003538145.1
KEYWORDS    RefSeq.
SOURCE      Thomasclavelia
  ORGANISM  Thomasclavelia
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Coprobacillaceae.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Thomasclavelia"
                     /db_xref="taxon:3025755"
     Protein         1..178
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20076
     Region          3..175
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 msldqiikqr rsirkykkkp vsneqiqlli qaaveapswk nsqtaryhvi tsqpllnefk
       61 erclpefnqe nckdapvliv tsfipnrsgf erdgtpsnel angwgcydlg lhnqnillka
      121 telglgslvm girdidkikg lldiskeeii vsviaigisd ieperpkrkt veditrfy
//
LOCUS       WP_003536475             392 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Sinorhizobium].
ACCESSION   WP_003536475
VERSION     WP_003536475.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium
  ORGANISM  Sinorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Sinorhizobium"
                     /db_xref="taxon:28105"
     Protein         1..392
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=41813
     Region          3..390
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 meallvinag ssslkfqifg iataglerqv rakldgigtq prlkataadg telidrrlda
       61 tavsdlpaal svardwlatl rgfdlraigh rvvhggpdyv rpvlidttvl drlasyqdla
      121 plhqpnnlap irlameikpd vpqvacfdta fhrgraehtd cyalprtfye qgvrrygfhg
      181 isyeyiagrl revapevarg rvivahlgsg asmcalkdgr svettmgfta ldglpmgtrp
      241 gqldpgvvlh lltdqgmsaq avsdllyhrs glkglsgisn dmrellesdd prasfaidhf
      301 vhrcaldagm laaalgglda fvftagigen sapirarise glawlgaqfd paandagasv
      361 iskagsrval hivptdeelm iarhtlaiir as
//
LOCUS       WP_003536867             191 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Sinorhizobium].
ACCESSION   WP_003536867
VERSION     WP_003536867.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium
  ORGANISM  Sinorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group.
REFERENCE   1  (residues 1 to 191)
  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 191)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 191)
  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   4  (residues 1 to 191)
  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   5  (residues 1 to 191)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Sinorhizobium"
                     /db_xref="taxon:28105"
     Protein         1..191
                     /product="TRAP transporter small permease subunit"
                     /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=21115
     Region          4..171
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mkpllgfsrl idaiterigk avswlilvav lvsagnavir kmfnmssnaw leaqwylfga
       61 afmfaaaytl sqnehiridv vygmfsrrvq hwidlfghvf flmpfvvlml yylvpyvrms
      121 yvsgelsssa ggliiwpaka illigfvlla lqgvseiikk iaimtgnmdd ptpyvpahap
      181 lddavapear s
//
LOCUS       WP_003539612             296 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Thomasclavelia].
ACCESSION   WP_003539612
VERSION     WP_003539612.1
KEYWORDS    RefSeq.
SOURCE      Thomasclavelia
  ORGANISM  Thomasclavelia
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Coprobacillaceae.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Thomasclavelia"
                     /db_xref="taxon:3025755"
     Protein         1..296
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33408
     Region          4..270
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mekyidlhmh skysddgeft ptqlveqchk agikvmaiad hnsvkaidea keaaaklnik
       61 yipsveidct ykginlhvlg ygvdyhhadf vtleenvlnq elacskekvk ltnmlgfdvd
      121 qaaldalsdn gvytgemfge vllndqryne nsllkpyrsg gersdnpyvn fywdfyaqgk
      181 pcyteivypt lketidlikr hggtvvlahp gnnlkgkfei fdemvelgve gveafsnyhs
      241 petveyfyqa gkkhqilitc gsdyhgktkp aielgecrct idehdienql keykli
//
LOCUS       WP_003535950             371 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator
            [Thomasclavelia].
ACCESSION   WP_003535950
VERSION     WP_003535950.1
KEYWORDS    RefSeq.
SOURCE      Thomasclavelia
  ORGANISM  Thomasclavelia
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Coprobacillaceae.
REFERENCE   1  (residues 1 to 371)
  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 371)
  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
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 371)
  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   5  (residues 1 to 371)
  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   6  (residues 1 to 371)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 371)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 371)
  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 11973053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Thomasclavelia"
                     /db_xref="taxon:3025755"
     Protein         1..371
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41558
     Region          <11..57
                     /region_name="COG3398"
                     /note="Predicted transcriptional regulator, contains two
                     HTH domains [Transcription]"
                     /db_xref="CDD:442625"
     Region          77..361
                     /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 mvdysikkyn rkivyqliyq akqitkqeia erlklslptv ssnlleleqa dlikkedine
       61 stggrkplai sikeqsriai gvsilkegit fvaldlyaql irkqtvalvy dnsesyfkqy
      121 gqalnefidc lqikkenflg itiaiqgivs qdgkkviygp ilnnqgltle kfekssdlpv
      181 kmihdshaag laelnfsedn ndaiylslnh nlgsavfmag kvfqgnnyss tfehmtlven
      241 grqcycgkkg cfeaycneda llknhtnmtl eefykqlrqk dqtamqswnd yfhylalaih
      301 nltmvldapv iiggkiaslf enedldlltk lvsdldplkf tvpdikigqc lketaaigaa
      361 ltdikkfvae i
//
LOCUS       WP_003537907             396 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Thomasclavelia].
ACCESSION   WP_003537907
VERSION     WP_003537907.1
KEYWORDS    RefSeq.
SOURCE      Thomasclavelia
  ORGANISM  Thomasclavelia
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Coprobacillaceae.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Thomasclavelia"
                     /db_xref="taxon:3025755"
     Protein         1..396
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43100
     Region          3..395
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 makiisvnag ssslkfqlfe mddesvitsg vierigleds iftikyqgkk tvttnpikdh
       61 kvavqllldt liekgivkel neikgvghrv vqggsyfdss aiidedvvsk idelkslapl
      121 hnpahltgyy afkeaipeag avavfdtafh qtldpkcyiy pipykyytdy kvrkygahgt
      181 shfyvsqrai emlgnpehsk vivahlgagg sltavkdgks vntsmgftpl agimmgtrsg
      241 dvdpsvidyl ieevgmdmke vitmlnkesg llgisgvssd frdvqnaale gneraqlaid
      301 ifyrrviayi gryfialggv daicftagig ensffarkgi cdllkdalgi eldedanvng
      361 qgdrlistpn skvkvfvipt neelviardt krllnl
//
LOCUS       WP_003540161             466 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Desulfotomaculum nigrificans].
ACCESSION   WP_003540161
VERSION     WP_003540161.1
KEYWORDS    RefSeq.
SOURCE      Desulfotomaculum nigrificans
  ORGANISM  Desulfotomaculum nigrificans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfotomaculaceae; Desulfotomaculum.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 466)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Desulfotomaculum nigrificans"
                     /db_xref="taxon:1565"
     Protein         1..466
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=51901
     Region          <2..422
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mllreqllki rnrltqiftp dnllihllqg sslleklerm mssgsqiivl yvdiadfhqv
       61 vqihgealar qvlnllrsal nhkaaeflnc tgekavenlw gddflmicqq ktpltqqqvn
      121 kistvlrial eenlkpellk ltgnslklhl gcsvikgscr enhkqalyna lkeaqkvarg
      181 twsqqtlqlr eefselltak sfnilyqpiv slqsgeilgw ealtrgpsgs yffspsvifn
      241 faeevgllfp lekvcrelai knfgqgksnq klflnihpyt vndpnfvkge trklladssl
      301 sannlvfeit erqsihdfnq fnktlshyrs qgyqvavdda gagfsslqai aevrpeyiki
      361 dsslvrgint nrvkqallet fvtftekigc siiaegiete aeltalcsig vhygqgyfla
      421 rpsfpkpavs skslnkitsl sccnpadvwq kafpigkise pavqvd
//
LOCUS       WP_003542646             235 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Desulfotomaculum nigrificans].
ACCESSION   WP_003542646
VERSION     WP_003542646.1
KEYWORDS    RefSeq.
SOURCE      Desulfotomaculum nigrificans
  ORGANISM  Desulfotomaculum nigrificans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfotomaculaceae; Desulfotomaculum.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 235)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Desulfotomaculum nigrificans"
                     /db_xref="taxon:1565"
     Protein         1..235
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=26884
     Region          <6..227
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mnskylesil nidlithwyq pilnlntrei igyeallrys ngkfspenif nkaktaglln
       61 eldlqslima skqvssdvgv lfinvfpstl lkedflyvyd kylvkgipia ielsenepvk
      121 dwttlkkivk elkarqvkia vddlgigyss fqhwielepe fvkvdryfta nlsthmrkqk
      181 iikslvelfh gstqlilegi erpedlktav emginygqgf llgkpkpwkn qcedk
//
LOCUS       WP_003544102             637 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Desulfotomaculum nigrificans].
ACCESSION   WP_003544102
VERSION     WP_003544102.1
KEYWORDS    RefSeq.
SOURCE      Desulfotomaculum nigrificans
  ORGANISM  Desulfotomaculum nigrificans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfotomaculaceae; Desulfotomaculum.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Desulfotomaculum nigrificans"
                     /db_xref="taxon:1565"
     Protein         1..637
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=73302
     Region          58..513
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mefpkiqkei fnpisenvkk laelfpsavk dgqvdfdalk aelgqfetvs eklseryelg
       61 wagkedakrl antdiigrtl kyipedsknp dttenlyieg dnlevlkllr nsyynrikmi
      121 yidppyntgk dfiyrdnfkv seeenavseg eidllgerli vnqkssgryh snwlsmmypr
      181 lkvakdllte dgvifisidd nevdnlkkic nevfgednfv aciiwerays pvnlkkhfse
      241 nhdfvlcyak qidnlicngl krtdesidry knpdndprgp wkpadlsvgp aiqekryeii
      301 tpsgrsvfpp egrcwvytke ryeemladnr iwfgesgnnv psvkkflsev kntmtpmtiw
      361 kytevghsqd aakkliqlfd gksyfdypks vdlikrmiel yakqdsiimd ffsgsattah
      421 avmqlnaedg gnrkfimvql pepcdeksea ykagfknice igrerirrag ekikeenkdk
      481 egienldigf kvfrvadtni rwfseaiksd nitleegmms dkdrldfnpg ftdidvvyei
      541 llrhrdipls akveklyeig ertyifadtv vvcleenvte siidkiaaie pmpmkiifrd
      601 safgdditlk tntmlrleaq mkknsgnmkk ayrvefi
//
LOCUS       WP_003543039             398 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Desulfotomaculum nigrificans].
ACCESSION   WP_003543039
VERSION     WP_003543039.1
KEYWORDS    RefSeq.
SOURCE      Desulfotomaculum nigrificans
  ORGANISM  Desulfotomaculum nigrificans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfotomaculaceae; Desulfotomaculum.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Desulfotomaculum nigrificans"
                     /db_xref="taxon:1565"
     Protein         1..398
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43060
     Region          1..396
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mlilvvncgs ssikyklmdm eqetvllsgl aerigiagsr ikqesqagke lvleqdlpnh
       61 kvaletilkc itdqtygais dismikavgh rvvhggeefn ksvlindeli kvleelsdla
      121 plhnppnvvg iktcreilpg iphvavfdta fhqsipkhaf mygipyqyye kykirkygfh
      181 gtshkyvsgr aaeilgksve elkiivchlg ngssitavgn gvsvdttmgf tplaglpmgt
      241 rtgdidpaiv tflmekenls idetnnllnk qsgvlgisgi ssdfrdleda anqgnerael
      301 alsmfaysin kwigaftaal ggldvvvftg gigenskdmr arvlkglayt gleideeknn
      361 srgkeviisk pgspitamvv ptneelmiar etkvlatr
//
LOCUS       WP_003542960             179 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Rhizobium acaciae].
ACCESSION   WP_003542960
VERSION     WP_003542960.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium acaciae
  ORGANISM  Rhizobium acaciae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 179)
  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 179)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 179)
  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   4  (residues 1 to 179)
  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   5  (residues 1 to 179)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Rhizobium acaciae"
                     /db_xref="taxon:2989736"
     Protein         1..179
                     /product="TRAP transporter small permease subunit"
                     /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=19919
     Region          4..166
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 msvllaasrl idsisqfmgk iseymvlfcc lisagnaivr yafnyssngw leiqwylfaf
       61 vvmlgashal rnnehvrvdl iygsvsdrak iwidivglil fllpacvflt wicwpffals
      121 yrqgeisgna gglirwpvkl ilvagfalls lqglselvkr iaaltgyisi dtkyekplq
//
LOCUS       WP_003545104             130 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein [Rhizobium].
ACCESSION   WP_003545104
VERSION     WP_003545104.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..130
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=14789
     Region          22..98
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mlnqdtdatr rdpnvkdths liasdrvegt rvygadgrhi gsierliigk rdgrvayavl
       61 sfggflgigh dhyplpwekl nydtqldgyr idltkeqieg apsysddddt wyndngrrvy
      121 dyygvppywm
//
LOCUS       WP_003545118             292 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Desulfotomaculum nigrificans].
ACCESSION   WP_003545118
VERSION     WP_003545118.1
KEYWORDS    RefSeq.
SOURCE      Desulfotomaculum nigrificans
  ORGANISM  Desulfotomaculum nigrificans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfotomaculaceae; Desulfotomaculum.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Magnet,S., Arbeloa,A., Mainardi,J.L., Hugonnet,J.E., Fourgeaud,M.,
            Dubost,L., Marie,A., Delfosse,V., Mayer,C., Rice,L.B. and Arthur,M.
  TITLE     Specificity of L,D-transpeptidases from gram-positive bacteria
            producing different peptidoglycan chemotypes
  JOURNAL   J Biol Chem 282 (18), 13151-13159 (2007)
   PUBMED   17311917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18524800
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Desulfotomaculum nigrificans"
                     /db_xref="taxon:1565"
     Protein         1..292
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=32330
     Region          26..144
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
     Region          182..273
                     /region_name="Cu_amine_oxidN1"
                     /note="Copper amine oxidase N-terminal domain; pfam07833"
                     /db_xref="CDD:400265"
ORIGIN      
        1 mtlalylams llfspglaaa enskmiiink ktnqlgfyqn gvltnvfpva tgrrrsftpe
       61 gtfkvinkqv nppyykkhip ggspynplgp rwlglsapgg pygihgnnnp asigtyasng
      121 cirlhnkdil wlydqvpigt pviivwndvd lnngfidntp iklyfnnepv ilssenptfs
      181 rqdkpyvplk vicrlldydi kwnqqtgtid lvssnmtttl tpdsknayvn gqqlnltnpp
      241 vvmngityvt tstleeifsm kvswntanre lriiyqapvq ppandsqqen pv
//
LOCUS       WP_003545839             295 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Rhizobium acaciae].
ACCESSION   WP_003545839
VERSION     WP_003545839.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium acaciae
  ORGANISM  Rhizobium acaciae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Rhizobium acaciae"
                     /db_xref="taxon:2989736"
     Protein         1..295
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31734
     Region          19..260
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mtdiyefegk tlcntnsvlg egptydpdsn tvwwfnilgk elhelnlsta akkvhplpvm
       61 asvlaridag rqliateegl fvrdvasgnl tfyaalendr penrsndgrt hpsgalwigt
      121 mskraenqag aiyhvasgkv tkifngisip nsicfspdgt vgyytdsrin rlmrvmvdpl
      181 tglpsgepiv lvdsmddpgs idgsvvdadg ylwnarwgag vvdryspdgl risrykvpav
      241 qpscpafigv nadrlavtta wegldedars aqpsagalle lgidvkgvfd pvyvi
//
LOCUS       WP_003544042             221 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Desulfotomaculum nigrificans].
ACCESSION   WP_003544042
VERSION     WP_003544042.1
KEYWORDS    RefSeq.
SOURCE      Desulfotomaculum nigrificans
  ORGANISM  Desulfotomaculum nigrificans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfotomaculaceae; Desulfotomaculum.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 221)
  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   3  (residues 1 to 221)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Desulfotomaculum nigrificans"
                     /db_xref="taxon:1565"
     Protein         1..221
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25097
     Region          12..221
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 maveklkvgq kifisllnen eqylssvhdm ddrviyipvp faqnrplvls rgdkvnvkym
       61 geqcaytfva kaigrkvedq klpmyiltqp gesditrvql rqfvrvpvsl dvnyalppan
      121 nepptfekgf tvdlsaggmk latkqsirpg ttilvcftik arkqkqpeel kllgkvirse
      181 lvdpelntyh sgiqfiditr qqqdlimafl fermaqikrk r
//
LOCUS       WP_003546951             162 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Lactobacillus acidophilus].
ACCESSION   WP_003546951
VERSION     WP_003546951.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus acidophilus
  ORGANISM  Lactobacillus acidophilus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Lactobacillus acidophilus"
                     /db_xref="taxon:1579"
     Protein         1..162
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18010
     Region          2..153
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mvnsiftkrr atrqfltnsi sddkiqkiva afqtspcgmh qndvmnlvvv kdealrkeie
       61 katdnscyga pvlfiintkk enmfgerdas vaaenimlea adlglgsvyv mggaiklndy
      121 tdiqreldid pdfqttvvvp vgkiarepek edrssryqvt iy
//
LOCUS       WP_003545375             102 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Desulfotomaculum nigrificans].
ACCESSION   WP_003545375
VERSION     WP_003545375.1
KEYWORDS    RefSeq.
SOURCE      Desulfotomaculum nigrificans
  ORGANISM  Desulfotomaculum nigrificans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfotomaculaceae; Desulfotomaculum.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 102)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 102)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Desulfotomaculum nigrificans"
                     /db_xref="taxon:1565"
     Protein         1..102
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=10930
     Region          3..76
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mgtielrgfg slqkvmkekg fgfpeqveig egitgedlla kldilkeqve gifvngkver
       61 lshiinpgdr valippgvpg pyrvmlgivg dvgmesnkke nk
//
LOCUS       WP_003546683             394 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Lactobacillus acidophilus].
ACCESSION   WP_003546683
VERSION     WP_003546683.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus acidophilus
  ORGANISM  Lactobacillus acidophilus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Lactobacillus acidophilus"
                     /db_xref="taxon:1579"
     Protein         1..394
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43448
     Region          2..392
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkkvlainsg sssfkyklfs lpaekviakg madrvglana sfeikladgt dhvektdipd
       61 qeaavslllk flkefnvved lneivgvghr vvnggeyfkd stiinkenlq kiyelqdyap
      121 lhnpaegrgi eafmnvlpnv pqvavfdtty hysldpvhyl ysipykyyek ygvrrygahg
      181 tsirytapha akmlgkdlkd lklivchlgs gasitavkdg ksydtsmgfs piagvtmatr
      241 sgdidpsliq hlmhvehksm demihilnse sgllglsgis pdmrdiresd teraklarni
      301 finrivryvg aytaemggvd aiiftagige hdagvrkavm dafkflgvep dyeaneenge
      361 hfitkpgskv kamviptnee lmierdvvrl tnin
//
LOCUS       WP_003550506             379 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Rhizobium acaciae].
ACCESSION   WP_003550506
VERSION     WP_003550506.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium acaciae
  ORGANISM  Rhizobium acaciae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
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
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 379)
  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   5  (residues 1 to 379)
  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   6  (residues 1 to 379)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 379)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 379)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Rhizobium acaciae"
                     /db_xref="taxon:2989736"
     Protein         1..379
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40661
     Region          39..79
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          98..364
                     /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 mrylrsgprr lhtqemgalr akmvglrsge iadrnirvil eairrhgplt rmelgrhcgl
       61 tgpgitnilr rlaeeklvts nrrngvggga tatefalrpe gafsigvklr qrrgeavlid
      121 lsgqvhdrvy ieldpadrvs lvhaavrdmv drhatlpiig lgiaandwte dqsdqiaams
      181 tiarpyvene ctasllaert igssgreggl amiiidddvq agflirgipy sgvhgragsi
      241 gemltgpdnv qlntvvgfes lrsrigdqaf irllkgeeis spllsqwire aaghlldpii
      301 amagflapsv vmigsdlpqg viealihqls ierrdtstrp lltpwispmk pasfsgggva
      361 lgaallpfln tlllppasa
//
LOCUS       WP_003551799             388 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Lentilactobacillus
            hilgardii].
ACCESSION   WP_003551799
VERSION     WP_003551799.1
KEYWORDS    RefSeq.
SOURCE      Lentilactobacillus hilgardii
  ORGANISM  Lentilactobacillus hilgardii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lentilactobacillus.
REFERENCE   1  (residues 1 to 388)
  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 388)
  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
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 388)
  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   5  (residues 1 to 388)
  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   6  (residues 1 to 388)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 388)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 388)
  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 20650276
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Lentilactobacillus hilgardii"
                     /db_xref="taxon:1588"
     Protein         1..388
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43527
     Region          17..60
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          83..374
                     /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 mktitnkdlm rransklvlq eifnndyttr aaisrqlgln kstvssiyde lkeeqlveev
       61 gegaashvgg rkptniriya nygftinfdi syhnlhfman yldgsvieqa ettiyrknih
      121 eivaiiehqi dqyvdtvvsv kgllgiclsi hgivneqqei tyspfidfed vnlnerlsak
      181 yhvpvvlene snltavyvrd fmmkfdsknl vaigihkgig sgviinnrlf rgfrgqagev
      241 grtltknaqg qltpieqics edaiinrisd elgltglnry kvvemyrehn qnvvaaidef
      301 iqeissliyn ssmyfdtgai ylgsplmeaa peifdqvlik vqqlshseik lvrltdsdka
      361 tllgacsvit hyaldlvgyp lnffktkn
//
LOCUS       WP_003548456             303 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Lactobacillus
            acidophilus].
ACCESSION   WP_003548456
VERSION     WP_003548456.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus acidophilus
  ORGANISM  Lactobacillus acidophilus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 303)
  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 303)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10097223
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Lactobacillus acidophilus"
                     /db_xref="taxon:1579"
     Protein         1..303
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33340
     Region          7..283
                     /region_name="TBP_aldolase_IIB"
                     /note="Tagatose-1,6-bisphosphate (TBP) aldolase and
                     related Type B Class II aldolases. TBP aldolase is a
                     tetrameric class II aldolase that catalyzes the reversible
                     condensation of dihydroxyacetone phosphate with
                     glyceraldehyde 3-phsophate to produce tagatose 1; cd00947"
                     /db_xref="CDD:238477"
     Site            order(28..30,33,53,56..58,63,67,70..71,230..231,233..234,
                     237,241,244)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238477"
     Site            order(86..87,174..176,178,205..206,208,227,229..230)
                     /site_type="active"
                     /db_xref="CDD:238477"
     Site            order(87,175,205)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238477"
     Site            order(174,176,178,206,208)
                     /site_type="other"
                     /note="Na+ binding site [ion binding]"
                     /db_xref="CDD:238477"
ORIGIN      
        1 mayfvngnei frearkhhya vgayntnnle wtraelraae etrtplliqv stgaakymgg
       61 ykfvkdmved qmdsmnisvp vilnldhsdf esakecialg yssvmfdgha lpteenlakt
      121 keiiklaher gisveaeigk igenqgggel asvedakafv eagvdklacg ignihgvypa
      181 dwkglnfdrl keiaeavpet plvlhggsgi pedqikkaiq lgiskvnint efqlafqeat
      241 rkyieegkde dkankgydpr klllpgteai tdkmkemiaw lgtktiddel kdasfdrssl
      301 nee
//
LOCUS       WP_003552852             368 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [Rhizobium].
ACCESSION   WP_003552852
VERSION     WP_003552852.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 368)
  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 368)
  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 368)
  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 368)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..368
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40040
     Region          1..358
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mdrrsffkka gtagagavaa talaapaiaq enpkiawrmt ssfpksldti yggaediakh
       61 vaaatdgnft iqpfaageiv pglqavdava agtveaahtt syyfvgkdpt yaigtaipfg
      121 lnsrltnawy yegngnklmn efyatqgmya lpagntgaqm ggwfrkeint lddlkgvkmr
      181 iaglagrvme kvgvipqqia ggdiypalek gtidaaefvg pyddlklgfh kvakyyyypg
      241 wweggptvhg ffnlekwssl pkhyqaaltd acafantnml akydtknpta lkqlvaegat
      301 lrpfsqeime acfqaatgiy seisgtnqyf kkiyddqtaf krdaylwmql seytfdtfmm
      361 iqqragkl
//
LOCUS       WP_003553746             396 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Lentilactobacillus hilgardii].
ACCESSION   WP_003553746
VERSION     WP_003553746.1
KEYWORDS    RefSeq.
SOURCE      Lentilactobacillus hilgardii
  ORGANISM  Lentilactobacillus hilgardii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lentilactobacillus.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Lentilactobacillus hilgardii"
                     /db_xref="taxon:1588"
     Protein         1..396
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43450
     Region          6..394
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mgksiainag sstlkyklfq mpeetvlssg aidriglgss svsikyddgk kykdtldidn
       61 heqaiqlvld kllslniikd yseitgvghr ivaggedfkd sviidddvik kiegltefap
      121 lhepaailgi kafkkilpni isiavfdtsf httlpevnym yslpyeyyqn ykvrkygahg
      181 tsyryvsqra asilgkpled lklvilhlga gasidaikdg ksfdtsmgfs pvagitmatr
      241 sgdvdpsalq yvmgkagikn mddmvdilnh ksglvgvsgv sadmreiegv mhenhramla
      301 reifknriir yigsyvaemg gidalvftag igendimirq evsdklgyfg ikvdpkkndi
      361 rgeerdlsae gstvktllip tdeelmivrd ierlrk
//
LOCUS       WP_003552529             168 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Lentilactobacillus hilgardii].
ACCESSION   WP_003552529
VERSION     WP_003552529.1
KEYWORDS    RefSeq.
SOURCE      Lentilactobacillus hilgardii
  ORGANISM  Lentilactobacillus hilgardii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lentilactobacillus.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 168)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Lentilactobacillus hilgardii"
                     /db_xref="taxon:1588"
     Protein         1..168
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18670
     Region          1..149
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mtkkqdyqll lkqaqtlldg ekdivanmsn lvslifhslt dlngttfyrn inhelvlgpf
       61 qgkpacmhip fgkgvcgtva qtkrseivpd vtkfdghiac daaskseivv pafyhrafwg
      121 vldldsphln rfdsidehfl lqiaplifad ndepitdrqi vgnhlear
//
LOCUS       WP_003556388             408 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Rhizobium].
ACCESSION   WP_003556388
VERSION     WP_003556388.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 408)
  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 408)
  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
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 408)
  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   5  (residues 1 to 408)
  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   6  (residues 1 to 408)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 408)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 408)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..408
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43339
     Region          20..71
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          87..385
                     /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 mndtvsigss prrirqnniv aalqtiyahr slsradlark lgmnrsssge ivaelteggf
       61 vqesdesgkq rlehsragrp gimlelvpda affvgieigv ehisaavvdl saevracrki
      121 afdtmsstve eamargveli igamgkrmig rckglgisap ahirpdgtvt lapiigwrev
      181 plkeigrsaf laafpaavpi avendanafa igdsyrhgva gvtlfllmet gvgggimidg
      241 klfrgghgla geightlvpg sggqkfeqli grevlirqyr eaigrkhvdl qeflgdvhdr
      301 vpaavniaet wsrhlayall qacrlldpdr ivlggsvasl ypmvaarvav hmsegqsipf
      361 ptpeivvddd aefgsafgaa cmlhqrflsl eseefggedg apvqsats
//
LOCUS       WP_003553624             152 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Lentilactobacillus hilgardii].
ACCESSION   WP_003553624
VERSION     WP_003553624.1
KEYWORDS    RefSeq.
SOURCE      Lentilactobacillus hilgardii
  ORGANISM  Lentilactobacillus hilgardii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lentilactobacillus.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Lentilactobacillus hilgardii"
                     /db_xref="taxon:1588"
     Protein         1..152
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16666
     Region          6..152
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mqnvtelvnq qldallyeet dlvsnmanas allnqsldqi nwvgfyryip endelilgpf
       61 qgkvacmhik ngvgvcgtal tqkhslrvad vhqfaghiac dgdskseivi pifkdgqplg
      121 vldidspvle rfsakdeall ndfvnifikh vd
//
LOCUS       WP_003557450             312 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Rhizobium leguminosarum].
ACCESSION   WP_003557450
VERSION     WP_003557450.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 312)
  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 312)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 312)
  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   4  (residues 1 to 312)
  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 312)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..312
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34447
     Region          35..186
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          214..290
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mlpnpmkgdr glsrrgemve lagrlaprhg ynptalasvr ilrteavlhd ipvlyrpgav
       61 fvlqgskqgm legevflyde ehylavslpv pfrmtstasp erpllavyve fdmqmaaeia
      121 lqveehaelp gdeprslvss kiaddiedvl lrllmalqss vetdvlgagi lrelhyrvlv
      181 gpqggamiaa lqqkgrsgki iqslawlrkn ygleiavtdl ardvgmsvps yhvqfkaltg
      241 nspmqyvkam rlhearlmia rqtrtiaevs asvgyaspaq fsrdfkrhfg riasqeikwv
      301 qrhlgelgde hg
//
LOCUS       WP_003555649             310 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Rhizobium leguminosarum].
ACCESSION   WP_003555649
VERSION     WP_003555649.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
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
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..310
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=33423
     Region          1..307
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mirmenvtkr ygegaapsvd rltldvpegs tvaligpsgc gktttmrmin rlieptegri
       61 lvngedvtka dpvqlrrhig yviqnvglfp hmtiaeniaa vpnllgweqk riaartkell
      121 dlvgldpqem lkryprqlsg gqrqrigvar alaadpavll mdepfgaidp iararlqdef
      181 rqilkrvrkt vvlvthdlde airlgdriai mragkivqyd tpdailsgpv defvanfvgi
      241 draikrlslf svadaaltga psapaatvaa nvnlrdalsl mvaansdvla vvdgngtvtg
      301 hltrdtifsi
//
LOCUS       WP_003561808             407 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Rhizobium leguminosarum].
ACCESSION   WP_003561808
VERSION     WP_003561808.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 407)
  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 407)
  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
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 407)
  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   5  (residues 1 to 407)
  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   6  (residues 1 to 407)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 407)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..407
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44062
     Region          13..>62
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          78..374
                     /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 mltksstelv rqrnsvlvls vlrrhgalah teisdstgls satisaitte lekaqiieks
       61 ehqpasgrgr prvllrqrrd cgylivviis sdavqyslvd yagklidrfs eershdpaga
      121 arfvaavrag llrildrski sqekvllisi sskglvnste pvlvwspifg sdqidfesal
      181 rpewqakvil dnetllvaaa lgareemvkg adfrslaals lghsiglgiv rrgnqtgqei
      241 sapnfghmlh mangglcrcg trgcieayag fyailrsafe vpldtipakf vpvaeldkia
      301 akarqghrvp afafrqagla lgnglsrmls ltermpiait gpgtryydll rqgieeglgq
      361 shivrmegmp eirvvpdeqi lvfeghlnra lsvidqdivl sgvqsgd
//
LOCUS       WP_003553141             207 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Rhizobium].
ACCESSION   WP_003553141
VERSION     WP_003553141.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
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   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   3  (residues 1 to 207)
  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   4  (residues 1 to 207)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 207)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 207)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..207
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22779
     Region          12..196
                     /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"
ORIGIN      
        1 magpsrivqd lrrarvlvvh prdedgdvli ahlkrlgcev ratwplppal ppdvdtvflh
       61 vedvhvehal qiidlqqtai iaivtyespt alqaiidlna hgviskplrp lgiltqfala
      121 ryrhsyekrl agkvqkleet lksrrlveka vsalrvmngl deeaaykllr dqatskrvpm
      181 atiaesiiaa qdtmkslgls isaktqp
//
LOCUS       WP_003553772             193 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Rhizobium].
ACCESSION   WP_003553772
VERSION     WP_003553772.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 193)
  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 193)
  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   3  (residues 1 to 193)
  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   4  (residues 1 to 193)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 193)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..193
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=20874
     Region          9..191
                     /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"
ORIGIN      
        1 mretpnftgw qamvlhredg nterlirqlr llgihaalqw aplstaalpd lvivdadqgw
       61 ddllpwnget pacpvvallg seapgriawa lgqgagaiia kpiatsavyp alvmavsihq
      121 erkataeklk yleervrlrp lvhaaveklq aahgideesa yailrncamr rrlpmeqisa
      181 filagaeplp eag
//
LOCUS       WP_003557284             388 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Lentilactobacillus
            hilgardii].
ACCESSION   WP_003557284
VERSION     WP_003557284.1
KEYWORDS    RefSeq.
SOURCE      Lentilactobacillus hilgardii
  ORGANISM  Lentilactobacillus hilgardii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lentilactobacillus.
REFERENCE   1  (residues 1 to 388)
  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 388)
  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
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 388)
  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   5  (residues 1 to 388)
  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   6  (residues 1 to 388)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 388)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 388)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Lentilactobacillus hilgardii"
                     /db_xref="taxon:1588"
     Protein         1..388
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43474
     Region          <9..58
                     /region_name="COG3398"
                     /note="Predicted transcriptional regulator, contains two
                     HTH domains [Transcription]"
                     /db_xref="CDD:442625"
     Region          83..374
                     /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 mktitnkdlm rransklvlq eifnndyttr aeisrhlgln kstvssiyde lkeeqlveev
       61 gegaashvgg rkptniriya sygftinfdi syhnlhfman yldgsviaqa ettiyqknih
      121 eilaiiehqi nqyvdtvvsv kgllgiclsi hgivneqqei tyspfidfed vnlnerlsak
      181 yhvpvvlene snlaavyvrd fmmkfdsknl vaigihkgig sgviinnrlf rgfrgqagev
      241 grtltknaqg qltpieqics edaiinrisd elgltglnry kvvemyrehn hnvvaaidef
      301 iqeissliyn ssmyfdtgai ylgsplmeaa peifdqvlik vqqlshseik lvrltdsdka
      361 tllgacsvit hyaldlvgyp lnffktkd
//
LOCUS       WP_003563343             280 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Rhizobium hidalgonense].
ACCESSION   WP_003563343
VERSION     WP_003563343.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium hidalgonense
  ORGANISM  Rhizobium hidalgonense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 280)
  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 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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Rhizobium hidalgonense"
                     /db_xref="taxon:1538159"
     Protein         1..280
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31371
     Region          42..268
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <168..268
                     /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 mrtvslprgr qrlhamptss gyevrenepy dwdgrrrgqt pftvlqhtis gtgrlryqnr
       61 nyrlqggdtl lvlvphnhry wlekgdrwey fwismngeet lrihqlvlst agpvlklqps
      121 tidhladcsl rlvtgatspg aasaiayeaa malyddvfgs pafaaelslm qpvidhinan
      181 lekplpvsel agivglsrah fsrsfaeseg mppaefvlqq rlqravkllt kadflpvkev
      241 aimcgfddpn yfskvfrrvy gtnptefrtt gmyasigklr
//
LOCUS       WP_003561436             367 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Rhizobium leguminosarum].
ACCESSION   WP_003561436
VERSION     WP_003561436.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 367)
  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 367)
  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   3  (residues 1 to 367)
  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   4  (residues 1 to 367)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 367)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 367)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 367)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..367
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37411
     Region          25..358
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(98..100,121..122,171,223,247)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mtlktltatl vaslafapla haditiglia pltgpvaayg dqvkngaqta vdeinkkggi
       61 lgekvvlela ddagepkqgv saankvvgdg irfvvgpvts gvaipvsdvl aengvlmvtp
      121 tatapdltkr gltnvlrtcg rddqqaevaa kyvlknfkdk rvaivndkga ygkgladafk
      181 atlnaggite vvndaitpgd kdfsalttri ksekvdvvyf ggyhpeggll arqlhdlaan
      241 atiiggdgls ntefwaigtd avagtiftna sdatktpdsk aaadalaakn ipaeaftlna
      301 yaavevlkag iekagsaeda eavaaalkgg eeiptaigkv tygetgdlts qsfslykwea
      361 gkivaae
//
LOCUS       WP_003567104             305 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Rhizobium hidalgonense].
ACCESSION   WP_003567104
VERSION     WP_003567104.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium hidalgonense
  ORGANISM  Rhizobium hidalgonense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 305)
  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 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   3  (residues 1 to 305)
  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   4  (residues 1 to 305)
  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 305)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Rhizobium hidalgonense"
                     /db_xref="taxon:1538159"
     Protein         1..305
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33359
     Region          22..171
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          199..280
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mselekmrai amrhagrpsl klprlfaytl dhtteidpli ydpaaslviq gtqrmfigdk
       61 rfeygpgqsm ivaaeiaalg qvceasqdrp fvavglfldp allsdlvlem aampeppies
      121 gygvstasas llgawgrlle llerpteipv maqslehelm frllmgphgg llrqiagsds
      181 rlmhirkama wirdhyterl nfkavaalag msvsvfydrf kavaavsplq yqkyirlhea
      241 rrrmianqss aaeagfavgy esasqfsrey krlfgappgq dtgrakaglg ginrpralga
      301 rpdvd
//
LOCUS       WP_003565539             132 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Lacticaseibacillus paracasei].
ACCESSION   WP_003565539
VERSION     WP_003565539.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus paracasei
  ORGANISM  Lacticaseibacillus paracasei
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 132)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 132)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Lacticaseibacillus paracasei"
                     /db_xref="taxon:1597"
     Protein         1..132
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=14091
     Region          2..126
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(7..10,40..42,45,71,108,122)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mlklytdgat kgnpgpaalg ilvsglphqi qkhaalpams nheaefaaai agfelliqag
       61 lnttpvafys dsklviqaie kqyakhypdl agrlltligq fplvlpnwlp dranrgahml
      121 aqqglrqset ki
//
LOCUS       WP_003570663             314 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Rhizobium hidalgonense].
ACCESSION   WP_003570663
VERSION     WP_003570663.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium hidalgonense
  ORGANISM  Rhizobium hidalgonense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (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   2  (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   3  (residues 1 to 314)
  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   4  (residues 1 to 314)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Rhizobium hidalgonense"
                     /db_xref="taxon:1538159"
     Protein         1..314
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=34022
     Region          3..312
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 msmieisnvt krygaatvvd hvsmnvekge itvivgtsgs gkstlmrmin rlvpitegqi
       61 fvngqnvadv evtelrrkig yaiqghglfp hrtvaqniat vpqlldwdat rissrveell
      121 glfnldpatf aekyphqlsg gqqqrvgvar alaaepelll mdepfgaldp virgkaqddl
      181 laiqkqfgtt iilvthdmde afhlgnqiav msegrllqcs tpekiltepa dpfvqqltgt
      241 sdralklmsl lplkesmapa ksglsyslpq slslrdalae miwqgvdeaa vqdgerapvg
      301 sismtrllel grka
//
LOCUS       WP_003570023             202 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Rhizobium hidalgonense].
ACCESSION   WP_003570023
VERSION     WP_003570023.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium hidalgonense
  ORGANISM  Rhizobium hidalgonense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Rhizobium hidalgonense"
                     /db_xref="taxon:1538159"
     Protein         1..202
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=19997
     Region          86..163
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mtrkllttva agalfatafa paafsqttpq padpaaptta apadpaapkp pitpdvtkpa
       61 gdaaqapaaa ptadtaqagy iteqapdqvs antyigqsvy ngnnesigsv ndlilkkdgg
      121 fvaaivgvgg flgigeknva vpmekitvaq ntqdgsvklt tsetaeslka apefktlamq
      181 saekapaatg tdttatgstt pk
//
LOCUS       WP_003574930             400 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Rhizobium leguminosarum].
ACCESSION   WP_003574930
VERSION     WP_003574930.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 400)
  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 400)
  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
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   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   5  (residues 1 to 400)
  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   6  (residues 1 to 400)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 400)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 400)
  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 20283677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..400
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42790
     Region          16..>55
                     /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(29,31..33,42)
                     /site_type="other"
                     /note="non-specific DNA interactions [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            42..48
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            order(43..44,48)
                     /site_type="other"
                     /note="sequence specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238044"
     Site            43..44
                     /site_type="other"
                     /note="putative cAMP binding site [chemical binding]"
                     /db_xref="CDD:238044"
     Region          79..384
                     /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 mkaisgtnle qakshnrrvv ieavrtngpl sraaiarmta ltaqtvsniv eelershllv
       61 paeaqklarg qpiipysinp agaysiglel grqrasgvlt dlsgavcari erhvehpdpq
      121 rampalqaiv edlqqaftfd rhrllgvgma lpgryadggi tslspqnlpg wqdfpvghel
      181 eqrvklpvlv endataaaig erlhgvargl ssfvylflag gggigagmfl dghlykgsrn
      241 nageighiiv ephgklcscg krgcldryvs ptvayefmgi anaeeilpdd ldaliakgge
      301 gldawldqav qplrqtldfl elafdpqtiv lggsistslm rrlaerlepl hlpidpnrkg
      361 svprvmigmt gkdtailgaa alpifsetnp rfdvlqkpvg
//
LOCUS       WP_003567988             415 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Rhizobium
            hidalgonense].
ACCESSION   WP_003567988
VERSION     WP_003567988.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium hidalgonense
  ORGANISM  Rhizobium hidalgonense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 415)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 415)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Rhizobium hidalgonense"
                     /db_xref="taxon:1538159"
     Protein         1..415
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=45652
     Region          15..406
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 madfeihlnl hgrtrpigla rsnrvrgaet imfeydrawl edpdrfslep alalsrgafa
       61 ppaglatfgs igdsapdtwg rrlmqrserr maerdgravr tlaesdyllg vadetrlgal
      121 rfrwvgdeef qapiragvpa lielgrllqi terilrdeet dedlqlifap gsslggarpk
      181 asvidqhghl siakfpketd dysmetweev alqlaeqagi vtplhelidv agkkvmlsrr
      241 fdrdgtvrip flsamammga kdgergsype ivdalaehga qgktdahaly rrvafnvlis
      301 nvddhlrnhg flwlgkagws lspaydlnpv ptdvkarvlt tnidldegtc sldlleetag
      361 ffaltlaqar aiikevatst atwretakav garsaeinri asafehddlq ralal
//
LOCUS       WP_003571196             563 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Lacticaseibacillus
            paracasei].
ACCESSION   WP_003571196
VERSION     WP_003571196.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus paracasei
  ORGANISM  Lacticaseibacillus paracasei
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 563)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Lacticaseibacillus paracasei"
                     /db_xref="taxon:1597"
     Protein         1..563
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=61785
     Region          4..544
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mlgllkygrd qrwagvietv fdwlptllpi mialnfaakr pgnaliitvi lvliwlgyvi
       61 gyerhhrhaw amsakrelrd hyfealyqrn nagdataadn aviqrdlggl nnldmfystl
      121 fptliqaglt fllliglsvw ygswlaflpl acvfligfam mflgkkmsaq nkahlagflr
      181 mggrfmndls gmntlvmyna adryakkfad dseyfrqatm nllrtqlqvl fvingfvylt
      241 vfaggfvtal qlaagqlpaa gafatwfala mmmvnarqlg yffhvvksng palagilati
      301 akskttpatv kitdnrplkq lvlqdvaigy eadaplvsdi natlvpgkly glagengtgk
      361 stltqallgq ltplsgtima dntpvtalsn aqraavfgyv aandyifsgt ikenlllgnq
      421 fgdqwqqhld elglmhfvtd lqdgyatevg eggrllspgq rqqlafarml ladktvylld
      481 emtssidaan aaiilaaikr lsrqkivlfi shdlsamaea dvvwfihdhq lisadhaqly
      541 rdqpayrhlv dnpeamlkeg qps
//
LOCUS       WP_003576903             412 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Rhizobium leguminosarum].
ACCESSION   WP_003576903
VERSION     WP_003576903.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 412)
  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 412)
  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
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 412)
  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   5  (residues 1 to 412)
  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   6  (residues 1 to 412)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 412)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 412)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..412
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44720
     Region          29..>75
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          88..374
                     /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 mnqtlgarls pdltganved agehnravvl rcihrhapis raeiarqtgf tkpaiarivd
       61 rlldeglime arrrhglrgq paieleinpd acfaiginid rdhltilavd avgnvrarvh
      121 hekrfilpte fmqltsdais hfqrsrlidd arlagiglam pdwlgeisll gkpkayqewt
      181 efdvraalen ltqhpvfien eanaaalael dyglgaesss ffyiainacp ggglvldgng
      241 hrgamglsge igwlpiadss dgkaqkvqll geifslfsly dflarhdvkv svphdlltld
      301 ahgrrlvsqw lkemsahlav avkhiglvvd pdavlvggrl pirvvdellr yvhehldaed
      361 pnlpslhras lgedasamga aampmaaalm lasadaaqrt rsplknmdrl ns
//
LOCUS       WP_003580523             656 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Rhizobium leguminosarum].
ACCESSION   WP_003580523
VERSION     WP_003580523.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 656)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..656
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70276
     Region          21..617
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mrvrdkprqa rqirsrhlrl lvlslttlia isllsrlpaw sllelrsfdy lstvddprpp
       61 adgpvivaid epsladinaq wpwprslhaa lvnqlraaga rvigldiima epsnsdndaa
      121 iakavgpdvv lagdetliet pqasqlirat plpqltqaga vtgiasidls gdgmfrripg
      181 yedgfaamlm kaasgaanad lpagrliqsf gparsyptvs yyqaldpenl lppgyfkgrv
      241 vlvglslqna paidkggvda fatpytvhtg klvsgveiqa tiydniragl siaearlptv
      301 aacilisvll aattvwrstg wltivtsaaa llafaavsfa girlahvfvs plgptiayis
      361 vvfgqaafdy aeerrnkrqi irafaqyisp dlvkrlsndp sqlklggerr tlsvlfsdvr
      421 gfttiaetlk ddpeqltgli nrlltplsdv vmdhggtidk ymgdcimafw naplddpdha
      481 lhavraslam qaaisrlntq lereaatlgr kphvlkmgvg intgecivgn mgstrrfdys
      541 clgdsvnlas rlegasknyg valllgeeta rlvadtytvv eldriivkgr tvpspvftvv
      601 hkadaealta hqafieakya gtlvpldvvf drlaadipel sgyyaivrda ltegge
//
LOCUS       WP_003575348             103 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Rhizobium leguminosarum].
ACCESSION   WP_003575348
VERSION     WP_003575348.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..103
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=11341
     Region          1..>45
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mnevrlelll gkqvydlegk avgrleevka eargadlyvv eyhlgayslf erlsalaigr
       61 avltaigaar sgskkavpwd kldmrdlehl rvtcrettlq tln
//
LOCUS       WP_003576557             319 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Lacticaseibacillus paracasei].
ACCESSION   WP_003576557
VERSION     WP_003576557.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus paracasei
  ORGANISM  Lacticaseibacillus paracasei
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
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   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   4  (residues 1 to 319)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Lacticaseibacillus paracasei"
                     /db_xref="taxon:1597"
     Protein         1..319
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=34762
     Region          4..288
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 malislehvt keydgkpvvn dlslkvdqge lfvlvgtsgs gktttlkmin rlvdptsgvi
       61 efadkpltsy kmrdlrwdlg yvlqqialfp tmtvaqniav ipemkgwsrq kiraatdell
      121 ttvdlppaey rnrmpselsg gqqqrigilr alasrpkvvl mdepfsaldp isrtqlqdml
      181 lhlhralktt vifvthdmae amklgdrigv mrggkllqvd tpeeiatnpa ndfvadlfkg
      241 aqanqglqvt lsqlapfaad vsarhavggn ltlaealpll dahealrvns ehgafvvnth
      301 svvaylasaf vdqntetke
//
LOCUS       WP_003581918             401 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Rhizobium leguminosarum].
ACCESSION   WP_003581918
VERSION     WP_003581918.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
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
REFERENCE   3  (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   4  (residues 1 to 401)
  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   5  (residues 1 to 401)
  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   6  (residues 1 to 401)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 401)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 401)
  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 11513304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..401
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42360
     Region          22..78
                     /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; cd00092"
                     /db_xref="CDD:238044"
     Site            order(35,37..39,48)
                     /site_type="other"
                     /note="non-specific DNA interactions [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            48..54
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            order(49..50,54)
                     /site_type="other"
                     /note="sequence specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238044"
     Site            49..50
                     /site_type="other"
                     /note="putative cAMP binding site [chemical binding]"
                     /db_xref="CDD:238044"
     Region          85..382
                     /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 mndvrpirak sgtnhegtsa hnrrvmidal ringelsrad laratwltkq tvsniieele
       61 rdglvrsqep vrkgrgqpst pyrlvpegaf aiglqidrhv travavdlig svlvrdeagl
      121 ppggpsegak vildlvagvr sklagmvqqs ekrlvglgaa mpgpfgldgs gddpwmmeaw
      181 qkfplletla tgtgldvglq ndaaaaatae rmvgaahgld havclfvgyg igaglilnge
      241 lyrgangnag eigmallfad gkttplehra slaslyqhls adpadpdlha rindlvfkgd
      301 qsietwieaa avdlrwsihl ietvfdpqtv ilcgsapeal verliaaigp llpsiaerpg
      361 rmlprlqpgm adpwsvalga aagpisrafd phfaailkds l
//
LOCUS       WP_003581822             126 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Rhizobium leguminosarum].
ACCESSION   WP_003581822
VERSION     WP_003581822.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 126)
  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 126)
  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   3  (residues 1 to 126)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..126
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14348
     Region          17..118
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mphsnitpkt rdtakrlrre ltkaeaamwd mlrdlrpyga rfrretpigp yiadfawlsa
       61 rlivevdgds hetvggrghd lvrdaflrne gfkvlrfdna qvldgpdyvf ltiekhaapf
      121 lkerva
//
LOCUS       WP_003581194             319 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Lacticaseibacillus paracasei].
ACCESSION   WP_003581194
VERSION     WP_003581194.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus paracasei
  ORGANISM  Lacticaseibacillus paracasei
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
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   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   4  (residues 1 to 319)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Lacticaseibacillus paracasei"
                     /db_xref="taxon:1597"
     Protein         1..319
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=34802
     Region          4..288
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 malislehvt keydgkpvvn dlslkvdqge lfvlvgtsgs gktttlkmin rlvdptsgvi
       61 efadkpltsy kmrdlrwdlg yvlqqialfp tmtvaqniav ipemkgwprq kirtatdell
      121 ttvdlppaey rnrmpselsg gqqqrigilr alasrpkvvl mdepfsaldp isrtqlqdml
      181 lhlhralktt vifvthdmae amklgdrigv mrggkllqvd tpeeiatnpa ndfvadlfkg
      241 aqanqglqvt lsqlapfaad vsarhavggn ltlaealpll dahealrvns ehgafvvnth
      301 svvaylasaf vdqntetke
//
LOCUS       WP_003582409             279 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Rhizobium leguminosarum].
ACCESSION   WP_003582409
VERSION     WP_003582409.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 279)
  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 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   3  (residues 1 to 279)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 279)
  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   5  (residues 1 to 279)
  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   6  (residues 1 to 279)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..279
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30979
     Region          18..101
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          127..278
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mnaiaraiwf ieshfendls leeiseaagl sryhlsrvfg lvtghsisgy irgrrlsrav
       61 palvggssti levalcagyg sheaftrafr dqfgmtpdav rrqgharnlv llepirmepa
      121 hlndlepprf etlqpmlfag lqeiypyggn aaipslwqkf nahfghisgq kgnvaygict
      181 hidgeaekfr ymaaveisda gdlpadfatl klpgqryvvf nhrghvsgis atmnrifgtw
      241 wptsglehge ipdmferyde rfdpytgmgv teiwlpira
//
LOCUS       WP_003582594             196 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Rhizobium leguminosarum].
ACCESSION   WP_003582594
VERSION     WP_003582594.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..196
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21685
     Region          1..165
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlrrlydwtm slaarksaev wlaviafves svflvpadvl flpmalakpe rsyryaviat
       61 vasvlggiag walgfyayet varpvlefyg kldafeemka yvtyewilll lvtsglahlp
      121 pikivtilsg vihvnlglfi vsaivargar flflawllrr ygepirdfie krlgqivgig
      181 agavivlyvg yrsfah
//
LOCUS       WP_003576325             432 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Rhizobium leguminosarum].
ACCESSION   WP_003576325
VERSION     WP_003576325.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 432)
  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 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   3  (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   4  (residues 1 to 432)
  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 432)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..432
                     /product="CmpA/NrtA family 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=46612
     Region          40..301
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mtknstigit rrsmlkttat aaligavkta fpsgafaaga gpevkglklg fialtdsapl
       61 iiakekgffd khglpetdva kqaswgatrd nlvlggaang idgahilspl pylmhtgkvt
      121 qnnkpvpmai larlnldsqg isvskeyaet gvqldasklk aafekkkaeg keikaamtfp
      181 ggthdlwiry wlaaggidpn kdvstivvpp pqmvanmkvg nmdvfcvgep wneqlvnqgi
      241 gftaattgel wkghpekalg lraewieknp iaakallmav meaqqwcdsm dnkaemadil
      301 gkrqwfnvpt kdvlgrlkgd inygngreak atdlymkfwk dgasypfksh dtwfmtenir
      361 wgnlpattdt kalvnqvnre diwreaakdl gvaaadipas ssrgketffd gkvfdpenps
      421 ayldslsika vs
//
LOCUS       WP_003585657             341 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Agrobacterium].
ACCESSION   WP_003585657
VERSION     WP_003585657.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium
  ORGANISM  Agrobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Agrobacterium"
                     /db_xref="taxon:357"
     Protein         1..341
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37355
     Region          1..340
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mkirlenvvk tfdtfravrd vsldiesgel lallgpsgsg kttilrmvag leysdggqif
       61 fgeedatnip vrdrgvgfvf qhyalfphmt lneniafgmk vskvnrdraa iaarveellr
      121 lvkldglgdr fpaqisggqr qrvalarals vdpkvlllde pfgaldanvr rdlrrwlrei
      181 hdslgittif vthdqeeald ladrvvilnq geivqqgtpk evcrqpnsaf vmrflgdanr
      241 vagvarggkv yvgenelpfs yaqgdgavdi yarpgdlewe dlhegipasv ervldrager
      301 rviastdggd ilefdvppen dvaagdrgsv iirrakifpa p
//
LOCUS       WP_003585679             456 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Lacticaseibacillus paracasei].
ACCESSION   WP_003585679
VERSION     WP_003585679.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus paracasei
  ORGANISM  Lacticaseibacillus paracasei
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 456)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Lacticaseibacillus paracasei"
                     /db_xref="taxon:1597"
     Protein         1..456
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=50297
     Region          76..189
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          197..312
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          334..456
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(407..408,411,429..432,434)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkknkrwllv vgvlivlmgg fyiiqsmhyr dhflpnteil gvdvsgqtvn aankkltdqf
       61 dqrqytfvek nkkilkvkgd alglsqdfkk gltqilnkqn pwqwttsvfa gqktnaqedp
      121 tintaalkqf atstadklnq nrqepvnakl vtsgdqfkiq kevngdqida dklattvtsa
      181 ldnhrqviel tdaykkptvk asdrdlqtte rdmnklastk vslqiqsttv tvpqatvlsw
      241 vtndngkatv ssqaitnyvt alsqqystih ktrqfnsqqq gtvsvpagty gwsinisats
      301 amilasvkag qdlnkevshs gsgytttgdi gntyvevske kqhewyikdg kvvmdsdivt
      361 gkpgqdtpsg vfyvwskqrn atlrgknddg ssyaspvsyw mpidytgvgl hdspwqpkyg
      421 gdwykehgsh gcvnnppdfm aklyaavdeg tpvivy
//
LOCUS       WP_003582347             368 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Rhizobium
            leguminosarum].
ACCESSION   WP_003582347
VERSION     WP_003582347.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 368)
  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 368)
  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 368)
  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 368)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..368
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40132
     Region          1..358
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mdrrsffkka gtasagavaa talaapaiaq enpkiawrmt ssfpksldti yggaediakh
       61 vaaatdgnft iqpfaageiv pglqavdava agtveaahtt syyfvgkdpt yafgtaipfg
      121 lnsrltnawf yegngnklmn efyatqgmya lpagntgaqm ggwfrkeint lddlkgvkmr
      181 iaglagrvme kvgvipqqia ggdiypalek gtidaaefvg pyddlklgfh kvakyyyypg
      241 wweggptvhg ffnlekwssl pkhyqaaltd acafantnml akydmknpta lkqlvaegat
      301 lrpfsqeime acfqaatgiy seisgtnqyf kkiyedqtaf krdaylwmql seytfdtfmm
      361 iqqragkl
//
LOCUS       WP_003584008             500 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Rhizobium leguminosarum].
ACCESSION   WP_003584008
VERSION     WP_003584008.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..500
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=52082
     Region          7..500
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mdklpwiils agdnvavata aipqgstvag ietrekidpg hkvaiadipl gspvvkygqa
       61 igrttadvka gdhvhshnlh fendrlaata nsapeaatse dkartfmgyr radgraatrn
      121 yigiiasvnc sttvcraiad eanrtilphy dgidgfvpiv hdqgcgmsst gdgmnvlhrt
      181 lagytrhvnf ggvlmiglgc evnqltlygq sgagaskrhf niqdaggsrr averamgmlr
      241 eiaadvgrek rvpmsvgeii iglqcggsdg fsgitanpal gvaadllaaa ggtailsets
      301 eiygaehllr sravsdevak kldekiawwe dyvalhgasl dnnpspgnkr gglttileks
      361 lgavakggrs pltavygyae rvtapglvfm dtpgydpvsa tgqvagganm iafttgrgsc
      421 fgcrpapslk lssnsalyas meedmdidcg tiatgdatis gkgreifeli vdtasgkktk
      481 selfgygdne fvpwhlgatl
//
LOCUS       WP_003584219             432 aa            linear   BCT 20-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein
            [Lacticaseibacillus paracasei].
ACCESSION   WP_003584219
VERSION     WP_003584219.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus paracasei
  ORGANISM  Lacticaseibacillus paracasei
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 432)
  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 432)
  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 13086029
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Lacticaseibacillus paracasei"
                     /db_xref="taxon:1597"
     Protein         1..432
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=46937
     Region          32..219
                     /region_name="GH25_muramidase"
                     /note="Endo-N-acetylmuramidases (muramidases) are
                     lysozymes (also referred to as peptidoglycan hydrolases)
                     that degrade bacterial cell walls by catalyzing the
                     hydrolysis of 1,4-beta-linkages between N-acetylmuramic
                     acid and N-acetyl-D-glucosamine residues; cl10448"
                     /db_xref="CDD:447900"
     Site            order(36,58,90,92,124,126,152,174,202,213)
                     /site_type="active"
                     /db_xref="CDD:119373"
     Region          <224..431
                     /region_name="PRK06347"
                     /note="1,4-beta-N-acetylmuramoylhydrolase"
                     /db_xref="CDD:180536"
     Region          387..431
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
ORIGIN      
        1 mkfktklitl vvaflaaisf alpsqvnaak gdqgvdwsry qgdngvfgys tdkfgisqig
       61 gysgygtyeq ttyktqvasl iaagkrahty iwwqnidntd lakqvldhfl peiqtpkgsi
      121 valdyeagst ntatllwald yirdagytpm lygyksflms hidlsqiash yqlwlaeypd
      181 ynvttvpnyg yfpsfdnvgi fqftstyrsg gldgnvdltg itdsgyngst ttdsgktyvk
      241 pstdtpatna gqqannttls qikagdsvkv nfgttrwang vampswvqgk tytvqqvsgs
      301 svllggimsw inrsnvellt ttsvpsvssg stytvqsgds wwsiaykygm smytlasnng
      361 ktinsvihpg dvlrvsgasy ssvsshtyyt vrsgdsfwsi askygismyt laanngksiy
      421 sliypgesly ir
//
LOCUS       WP_003590247             179 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit [Rhizobium].
ACCESSION   WP_003590247
VERSION     WP_003590247.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 179)
  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 179)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 179)
  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   4  (residues 1 to 179)
  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   5  (residues 1 to 179)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..179
                     /product="TRAP transporter small permease subunit"
                     /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=19909
     Region          4..167
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 msgllaasrl idsvsrimgk lseymvlfcc lisagnaivr yafnyssngw leiqwylfaf
       61 vvmlgashal rnnehvrvdl iygavsdkak iwidifgliv flipvciflt wlcwpfftls
      121 yqqgeisgna gglirwpvkl ilvagfalls lqgvselikr iaaltghlki dmtyekplq
//
LOCUS       WP_003590472             401 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Rhizobium leguminosarum].
ACCESSION   WP_003590472
VERSION     WP_003590472.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
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
REFERENCE   3  (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   4  (residues 1 to 401)
  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   5  (residues 1 to 401)
  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   6  (residues 1 to 401)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 401)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 401)
  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 11513304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..401
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42249
     Region          22..78
                     /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; cd00092"
                     /db_xref="CDD:238044"
     Site            order(35,37..39,48)
                     /site_type="other"
                     /note="non-specific DNA interactions [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            48..54
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            order(49..50,54)
                     /site_type="other"
                     /note="sequence specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238044"
     Site            49..50
                     /site_type="other"
                     /note="putative cAMP binding site [chemical binding]"
                     /db_xref="CDD:238044"
     Region          85..382
                     /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 mndvrpirak sgtnhegtsa hnrrvmidal ringelsrad laratwltkq tvsniieele
       61 rdglvrsqep vrkgrgqpst pyglvpegaf aiglqidrhv travavdlig svlvraeagl
      121 ppggpstgak vildlvadvr sklagivqqs ekrmvglgva mpgpfgvags gddpwmmeaw
      181 qkfpllerla agtgldvglq ndaaaaatae rmvgaahgvd havclfvgyg igaglilnge
      241 lyrgangnag eigmallfad gkstplehra slaslyqhls adpadphlha rindlasrgd
      301 pniktwieaa avdlrwsihl ietvfdpqtv ilcgsapeal vkrliaaigp llpsiaerps
      361 rmlprlqpgm adpwsvaiga aagpigrafd prfaailkdf l
//
LOCUS       WP_003590558             160 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Lacticaseibacillus paracasei].
ACCESSION   WP_003590558
VERSION     WP_003590558.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus paracasei
  ORGANISM  Lacticaseibacillus paracasei
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Lacticaseibacillus paracasei"
                     /db_xref="taxon:1597"
     Protein         1..160
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17001
     Region          8..153
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mttldpiivd qldglltget dpitvlanas allndlmtdl nwagfylynd ktgqldlgpf
       61 qgkvacmhiq pgngvvgtsy aqnavlrvpn vhefaghiac dsasnaeivv pitvdnrvva
      121 imdidsptld rfsendeail tkfgetlaah ldtaalntvy
//
LOCUS       WP_003583513             297 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Lacticaseibacillus
            paracasei].
ACCESSION   WP_003583513
VERSION     WP_003583513.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus paracasei
  ORGANISM  Lacticaseibacillus paracasei
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 297)
  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 297)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10097223
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Lacticaseibacillus paracasei"
                     /db_xref="taxon:1597"
     Protein         1..297
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=32694
     Region          6..279
                     /region_name="TBP_aldolase_IIB"
                     /note="Tagatose-1,6-bisphosphate (TBP) aldolase and
                     related Type B Class II aldolases. TBP aldolase is a
                     tetrameric class II aldolase that catalyzes the reversible
                     condensation of dihydroxyacetone phosphate with
                     glyceraldehyde 3-phsophate to produce tagatose 1; cd00947"
                     /db_xref="CDD:238477"
     Site            order(27..29,32,53..54,56,60,64,67..68,141,232..233,
                     235..236,239,243,246)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238477"
     Site            order(81..82,177..179,181,207..208,210,229,231..232)
                     /site_type="active"
                     /db_xref="CDD:238477"
     Site            order(82,178,207)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238477"
     Site            order(177,179,181,208,210)
                     /site_type="other"
                     /note="Na+ binding site [ion binding]"
                     /db_xref="CDD:238477"
ORIGIN      
        1 mplvstkqlv ttayqnkfav gafnvgnsef vkniiavaek lespvileih pleyelmgsa
       61 ifkyireaal tatipvaihl dhgrnmadvl raiqdqansv midssglsfe enlkttkqvv
      121 evahsvgvsv eaelgsignr kftedqnmgr iytdsesakq fvtetgvddl avaigtvhgp
      181 ypsgendiri dilkqlnetl qmplvlhggs dnpdnkirea iqngiskvni stdikvpfyh
      241 giaktvadkp geyepwimmp yadeaqkkvi aekirlfgsd hksklyfeda krltpyf
//
LOCUS       WP_003591620             310 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Rhizobium leguminosarum].
ACCESSION   WP_003591620
VERSION     WP_003591620.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
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
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..310
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=33455
     Region          1..307
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mirmedvtkr yaegaapsvd rltlevpegs tvaligpsgc gktttmrmin rlieptegri
       61 lvngedvtka dpvqlrrhig yviqnvglfp hmtiaeniaa vpnllgweqk riaartqell
      121 dlvgldprem lkrfprqlsg gqrqrigvar alaadpavll mdepfgaidp iararlqdef
      181 rqilkrvrkt vvlvthdlde airlgdriai mragqivqyd kpdailshpa defvanfvgi
      241 draikrlslf svadaalaga psapaatvaa nanlrdalsl mvaansdvla vvdgngtvtg
      301 hltrdaifsi
//
LOCUS       WP_003591760             437 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Rhizobium leguminosarum].
ACCESSION   WP_003591760
VERSION     WP_003591760.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 437)
  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 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   3  (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   4  (residues 1 to 437)
  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 437)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..437
                     /product="CmpA/NrtA family 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=47158
     Region          46..306
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mkkisttgis tsgitrrsml kttataalig avktafpsga faggtgpevk gvklgfialt
       61 dsapliiake kgffdkhglp etdvakqasw gatrdnlvlg gaangidgah ilsplpylmh
      121 tgrvtqnnkp vpmailarln ldsqgisvak eyaetgvqld asklkatfek kkaegkevka
      181 amtfpggthd lwirywlaag gidpnkdvst ivvpppqmva nmkvgnmdvf cvgepwneql
      241 vnqgigftaa ttgelwkghp ekalelraew ieknpnaaka llmavmeaqq wcesmdnkae
      301 madilgkrqw fnvpskdvlg rlkgdinygn greakatdly mkfwkdgasy pfkshdtwfm
      361 tenirwgnlp attdvkalvn qvnredvwre aakdlgvaaa dipasssrgk etffdgkvfd
      421 penpsaylds lsikavs
//
LOCUS       WP_003592376             332 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Rhizobium leguminosarum].
ACCESSION   WP_003592376
VERSION     WP_003592376.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 332)
  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 332)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 332)
  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   4  (residues 1 to 332)
  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 332)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..332
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36359
     Region          <140..328
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          247..328
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 msenspapfs frfrgssfdn mvetlggafg afdaepvgra pdfnwgldfs andsavlltg
       61 yheaefqfni eptvdtaeyl sivvprsggm gvaygsrvae agkgklplyn nfepdsvlmy
      121 gqsnvidell inwsvilqti gqtfempfsg sldllpeldl stpvgrtign ltetiaigmr
      181 dngpllqspi amahmtqala dlvvrmvpnr lshfldkgpa liaprhvrka iefmqanidq
      241 pitmpkvaea agvssralet gfrafrgtsp avylltlrlr aarqelldpe skesmkgicl
      301 kwgffhfgrf savykstyge ypsdtrkrvc rl
//
LOCUS       WP_003590774             672 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Lacticaseibacillus
            paracasei].
ACCESSION   WP_003590774
VERSION     WP_003590774.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus paracasei
  ORGANISM  Lacticaseibacillus paracasei
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 672)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 672)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Lacticaseibacillus paracasei"
                     /db_xref="taxon:1597"
     Protein         1..672
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=77198
     Region          60..627
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mgfgdkiidl fmptkkerqp snhelavsep kpeiedftkl idrdslhslf pfsweqypty
       61 vqsgenfirv laiadypkrv ygnwlselkr kkgvidivqy idsasnnsmi tyykktiqnk
      121 eaqklntfdp ykkkilqnyi dsanmqldky ldnsttfvyq hmliylrans laelddlten
      181 vkntliklqm kplvpvkatf qafwstmpin enlmgdytyk esntevassm fpfddaeild
      241 lkprsdiegv nkdtnsliav dmldrnktln qnqviigtsg vgkttymiqk ilryaiqdyq
      301 lyiidpeney tkivealgga vlhltsnaks kinplqifse eilsadeavm nldllvkdki
      361 qrlkgffevl ktgitqvela ilddvvkqay vnsgvlkysr lkeikddqwp tlsnvydele
      421 kladkdedkf nrvkdfyyil gsythgsnsl fdghtnvnlk gkiisfdlkp lqseqevqsa
      481 aylntfqylw deitkdrhsr kklfvdefhf ltlhkaaatf fhqaykrfrk ynagaiagtq
      541 qiqdviegtt dtgqnigeai ignsytkvff gldgkgvddv itklrmtfsd kekkllerrr
      601 qgealmiygs qrafmrvelt eeelrlidpe ayqekynret aeqpdyqkrv vltpseidal
      661 ttteeeggal ne
//
LOCUS       WP_003593619             383 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Rhizobium].
ACCESSION   WP_003593619
VERSION     WP_003593619.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 383)
  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 383)
  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
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 383)
  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   5  (residues 1 to 383)
  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   6  (residues 1 to 383)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 383)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 383)
  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 20170230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..383
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42173
     Region          12..>67
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          92..379
                     /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 mayfpeplia prflregggv vssnerdmlr liwrhpglsr sevtghtdlt qqsvyriidq
       61 leergivsfg spkpgtgrgq psptlrlegr yayscgisvn tdvigiclmd isgkvlaess
      121 iilrersmaq sldlvrehla ehqrandlse daffgigfai agfhvsgtry naplplhews
      181 lielgplltd ffgkpvwvhn ggkagtvaes mfgagryirh faylsfnygf ggglvsngel
      241 lhngvgnage fsgiydaeen krrpalqyli enlnrngldi psisymrkhf dpkwpgvaew
      301 vdevtpaysr linaiwaifd pqgiifggqi psalaqmlid rteifdrpry gvprprpkli
      361 iseiasdasa mgaaiapfks ayy
//
LOCUS       WP_003594035             263 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Rhizobium
            leguminosarum].
ACCESSION   WP_003594035
VERSION     WP_003594035.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..263
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28686
     Region          20..112
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          178..251
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 maperrkdta llaaragryr eyapppalrr hfsrfwshal hdgppaqvti vpdgycdllw
       61 idsrlavagp drtaafptlr pgttvigarf apgaavpwlk tplsallgrs vpladigwkh
      121 taefearlgd cpdpadamal fgrlleeaar dadepaedaa mifaaadsgr pasrllgrls
      181 mserqlrrrc hhhfgygakt lerirrfqrf ldlcrrsgtm plahlaleag fadqahmtre
      241 vgelsgltpt ailgqlsmpk kpg
//
LOCUS       WP_003587665             301 aa            linear   BCT 20-JAN-2025
DEFINITION  uracil-DNA glycosylase [Rhizobium leguminosarum].
ACCESSION   WP_003587665
VERSION     WP_003587665.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Lee,D.H., Liu,Y., Lee,H.W., Xia,B., Brice,A.R., Park,S.H.,
            Balduf,H., Dominy,B.N. and Cao,W.
  TITLE     A structural determinant in the uracil DNA glycosylase superfamily
            for the removal of uracil from adenine/uracil base pairs
  JOURNAL   Nucleic Acids Res 43 (2), 1081-1089 (2015)
   PUBMED   25550433
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Zharkov,D.O., Mechetin,G.V. and Nevinsky,G.A.
  TITLE     Uracil-DNA glycosylase: Structural, thermodynamic and kinetic
            aspects of lesion search and recognition
  JOURNAL   Mutat Res 685 (1-2), 11-20 (2010)
   PUBMED   19909758
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Stivers,J.T. and Drohat,A.C.
  TITLE     Uracil DNA glycosylase: insights from a master catalyst
  JOURNAL   Arch Biochem Biophys 396 (1), 1-9 (2001)
   PUBMED   11716455
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Pearl,L.H.
  TITLE     Structure and function in the uracil-DNA glycosylase superfamily
  JOURNAL   Mutat Res 460 (3-4), 165-181 (2000)
   PUBMED   10946227
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The alpha/beta fold uracil DNA glycosylases: a common origin with
            diverse fates
  JOURNAL   Genome Biol 1 (4), RESEARCH0007 (2000)
   PUBMED   11178247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..301
                     /product="uracil-DNA glycosylase"
                     /EC_number="3.2.2.27"
                     /GO_function="GO:0004844 - uracil DNA N-glycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=32043
     Region          <44..>103
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          104..294
                     /region_name="Udg4"
                     /note="Uracil-DNA glycosylase [Replication, recombination
                     and repair]; COG1573"
                     /db_xref="CDD:441181"
ORIGIN      
        1 misandlspa elaallhfha dagvewllee eaidrfaefe amkaarrpat qaqpqpvaag
       61 eraapgenrt pprptaavrp apaeraasgp qpaipdgeav qqarfvaesa rslaelktai
      121 eafngcnlkh sarstifasg daesgimvig sapgaeddre gvpfsgksgq lfdkmlaaig
      181 ltrsailltq vipwrppgnr apsaaemdic rpfierqial aqpkailllg nfaarfffge
      241 ndtihglrgr wkeiaaadcv ipaiaslhpq dlltapvnkr lawndllafq aklkslsllr
      301 n
//
LOCUS       WP_003594557             346 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Rhizobium].
ACCESSION   WP_003594557
VERSION     WP_003594557.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..346
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38715
     Region          1..344
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mevrvqnirk efdrfpalhd vslgirsgel iallgpsgsg kttllrliag lesptegqif
       61 fgdedaskks vqqrnigfvf qhyalfrymt vldnvsfglr vrnsarrpak adirkralel
      121 ldlvqlsgle krypaqlsgg qrqrvalara mavepnvlll depfgaldaq vrkdlrkwlr
      181 eihdrtghtt vfvthdqdea leladrvvvm sqgaieqvgt pdevydnpns pfvfgfigqs
      241 nclqveisdg dirfegrslg lnaegepdgt aqlyfrphdv rlcesaenci agqpvssrrv
      301 agtrhieldi gndrphieie lppseadrld rhrvafkptr wklfrs
//
LOCUS       WP_003595764             563 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Lacticaseibacillus
            paracasei].
ACCESSION   WP_003595764
VERSION     WP_003595764.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus paracasei
  ORGANISM  Lacticaseibacillus paracasei
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 563)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Lacticaseibacillus paracasei"
                     /db_xref="taxon:1597"
     Protein         1..563
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=61812
     Region          4..544
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mlgllkygrd qrwagvietv fdwlptllpi mialnfaakr prnaliitvi lvliwlgyvi
       61 gyerhhrhaw amsakrelrd hyfealyqrn nagdataadn aviqrdlggl nnldmfystl
      121 fptliqaglt fllliglsvw ygswlaflpl acvfligfam mflgkkmsaq nkahlagflr
      181 mggrfmndls gmntlvmyna adryakkfad dseyfrqatm nllrtqlqvl fvingfvylt
      241 vfaggfvtal qlaagqlpaa gafatwfala mmmvnarqlg yffhvvksng palagilati
      301 akskttpatv kitdnrplkq lvlqdvaigy eadaplvsgv natlvpgkly glagengtgk
      361 stltqallgq ltplsgtima dntpvtalsn aqraavfgyv aandyifsgt ikenlllgnq
      421 fgdqwqqhld elglmhfvtd lqdgyatevg eggrllspgq rqqlafarml ladktvylld
      481 emtssidaan aaiilaaikr lsrqkivlfi shdlsamaea dvvwfihdhq lisadhaqly
      541 rdqpayrhlv dnpeamlkeg qps
//
LOCUS       WP_003597962             146 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein [Methylorubrum].
ACCESSION   WP_003597962
VERSION     WP_003597962.1
KEYWORDS    RefSeq.
SOURCE      Methylorubrum
  ORGANISM  Methylorubrum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Methylorubrum"
                     /db_xref="taxon:2282523"
     Protein         1..146
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=15445
     Region          33..112
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mptdlpeera yrkpgtleld ptsgegvatd etprliasdk vegtpvydst grhlgsvynf
       61 mvdkvsgqva yavlsfggfl gfgenhhplp wnaltysvel ggyvvdidpa dlegaptqgp
      121 genpfddpgf ggrlndhwgg rkapta
//
LOCUS       WP_003591792             684 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Rhizobium leguminosarum].
ACCESSION   WP_003591792
VERSION     WP_003591792.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 684)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 684)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..684
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=71318
     Region          1..684
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mtsrpldrll rpqtiavfgg rearrvieqc drmgfsgkiw pvhpkldevl grpcyrsvgd
       61 lpsapdaafv gvnrtltvei vrslsaagag gavcyasgfs eataeladga dlqqallsaa
      121 gnmpilgpnc yglingldga llwpdqhgmk riecgvailt qssniainlt mqtrglpiay
      181 mvtagnqaqt sladvacali edprvtavgl hvegfgdvsg lerlaaisrq skkpvvvlkv
      241 grseqakqaa vshtaslags davadavlar lgigrvqslp alletlkllh vagplpgrsi
      301 ssmscsggea slmadaavgr niefpglqpq qlprlrrvlg emvtlsnpld yhtfvwgdfa
      361 rqteafsamf eggyalnlvv ldfprgdrcd asewamtada vitaasatga lagllatlpe
      421 nmpepvadrl mangivafsg idetmvavev aagigqawqa ppppplldvp smdgeietlt
      481 eadgkaelaa cglpvprglq afspheaaeq aerlgfpvvl kglgiahkte agavalnlgd
      541 sqavsnaaak maanagylve kmidppvsel iigavrdpvf glsltlgagg ifveliedsi
      601 ilplpttkse irtaisrlrq akliygyrgr pkgdldaava aiaaaadyvv knaacleeld
      661 inplmvlpeg qgvaavdali rrrr
//
LOCUS       WP_003599992             319 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Lacticaseibacillus paracasei].
ACCESSION   WP_003599992
VERSION     WP_003599992.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus paracasei
  ORGANISM  Lacticaseibacillus paracasei
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
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   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   4  (residues 1 to 319)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Lacticaseibacillus paracasei"
                     /db_xref="taxon:1597"
     Protein         1..319
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=34778
     Region          4..288
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 malislehvt keydgkpvvn dlslkvdqge lfvlvgtsgs gktttlkmin rlvdptsgvi
       61 efadkpltsy kmrdlrwdlg yvlqqialfp tmtvaqniav ipemkgwsrq kirtatdell
      121 ttvdlppaey rnrmpselsg gqqqrigilr alasrpkvvl mdepfsaldp isrtqlqdml
      181 lhlhralkts vifvthdmae amklgdrigv mrggkllqvd tpeeiatnpa ndfvadlfkg
      241 aqanqglqvt lsqlapfaad vsarhavggn ltlaealpll dahealrvns ehgafvvnth
      301 svvaylasaf vdqntetke
//
LOCUS       WP_003601424             118 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Methylorubrum extorquens].
ACCESSION   WP_003601424
VERSION     WP_003601424.1
KEYWORDS    RefSeq.
SOURCE      Methylorubrum extorquens
  ORGANISM  Methylorubrum extorquens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylorubrum.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Methylorubrum extorquens"
                     /db_xref="taxon:408"
     Protein         1..118
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=13170
     Region          14..91
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 msdahttsap shpfiessrv egtavydang kqigiikrlv iekvngnvay avtsfrkfig
       61 gssdshtipw nylhydlglq gyrtniteeq lhnapefsrr ddhlisgqew ellaeyya
//
LOCUS       WP_003602107             160 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Lacticaseibacillus paracasei].
ACCESSION   WP_003602107
VERSION     WP_003602107.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus paracasei
  ORGANISM  Lacticaseibacillus paracasei
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Lacticaseibacillus paracasei"
                     /db_xref="taxon:1597"
     Protein         1..160
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17072
     Region          8..153
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mttldpiivd qldglltget npitvlanas allndlmtdl nwagfylynd ktgqldlgpf
       61 qgkvacmhiq pengvvgtsy aqnavlrvpn vhefaghiac dsasnaeivv pitvdnrvva
      121 imdidsptld rfsendeail tkfgetlaah ldtaalntvy
//
LOCUS       WP_003596732             778 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Methylorubrum extorquens].
ACCESSION   WP_003596732
VERSION     WP_003596732.1
KEYWORDS    RefSeq.
SOURCE      Methylorubrum extorquens
  ORGANISM  Methylorubrum extorquens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylorubrum.
REFERENCE   1  (residues 1 to 778)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Methylorubrum extorquens"
                     /db_xref="taxon:408"
     Protein         1..778
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=82541
     Region          54..778
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mshrrpgrca rtltfilats plaiaaaqaq ggnqavalee isvtsegngv pggapaasag
       61 tagpglppvs aptpldkpvg evvtsvgreg vidnraatsv adilrnspgv tvrqgngprd
      121 vvvsirgnna ratgvsrnmv vledgfpvtq adgssrfdlv dpraysridv frgpqspffg
      181 nfatggalnf vtrrgseing veygvdagsf gylnnyaafg gvsgpfeysl ftsdtrgngf
      241 lshnafdtqt inflgtyapt pddrftlkii nnevatdlpg rgslnqfrln pfqrgcataa
      301 aaapgcvtyn lllngrngat vpvtadegaf frgdrrtivg grwehdfdaf ttwrtqlvfd
      361 drqinqpfyt ssgrgdfpgf nfltdltrrg dlfglpatgy valayntlds nsltynrapy
      421 ggprlgalta dleatqanlg grarvelqls dqwiavagis aenttingrn itygfpaagg
      481 vtttlanidr sflnvapels llyrpntdwq frgrvatgya tpsasnltvt sagvpgnngq
      541 lqtqenlgfd vgadwtplpg vrfsvtgfye ffrnelvtqs pgagllsytf napasehrgv
      601 evgadwafap gwrataaytf ddqiytryve qlsagsltrr fdragnhipg vpanqllari
      661 gyeqatgpla glggyvetvf qddffidnan llkapgyaiv nlnvhyttel vgyakrlnlf
      721 fearnvldkt yvasaqnlan sisaasglqn gagvlanttg svfagaprnf vggmrlsf
//
LOCUS       WP_003602564              98 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein
            [Methylorubrum].
ACCESSION   WP_003602564
VERSION     WP_003602564.1
KEYWORDS    RefSeq.
SOURCE      Methylorubrum
  ORGANISM  Methylorubrum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Methylorubrum"
                     /db_xref="taxon:2282523"
     Protein         1..98
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10818
     Region          1..97
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mdrmeaitrl rdsadavrtm gatslylfgs targearads dldlfidydp asrfnafdlv
       61 gikllledrl gtaidvttrd glhprlrdri easalrvf
//
LOCUS       WP_003593589             657 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CHASE2 domain-containing protein [Rhizobium].
ACCESSION   WP_003593589
VERSION     WP_003593589.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 657)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 657)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..657
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..657
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70325
     Region          29..617
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mpvrdkprqa rqtgsrrlrl lvlslavlia isllsrlpaw sllelrsfdy lstvddprpp
       61 pggpvivaid epsladinaq wpwprslhae lvsqlraaga rvvgldiima epsnpdndaa
      121 iakavgpdvv lagdetliet pqasqlirat plpqltqaga vtgiasidls gdgmfrripg
      181 yqdgfaamlm ktasgaanad lpagrliqsf gparsyptvs yyqaldpenl lppgyfrdrv
      241 vlvglslqna peidkrgvda fatpytihtg klvsgveiqa tiydniragl siaearlpav
      301 aacilisvll aattvwrstg wltivtsaaa llafatvsfa girlahvfvs plgptvayis
      361 vvfgqaafdy aeerrnkrqi irafaqyisp dlvrrlsndp sqlklggerr tlsvlfsdvr
      421 gfttiaetlk ddpeqltgli nrlltplsdv vmdhggtidk ymgdcimafw naplddpdha
      481 lhavraslam qtaisrlnnq lereaaargg kphvlkmgvg intgecivgn mgstrrfdys
      541 clgdsvnlas rlegasknyg valllgeeta rlvaetyivi eldriivkgr tvpspvytvv
      601 hkadaealaa hqafieakya gtlapsnpaf drlaadipel aayyaivrda lvgdgge
//
LOCUS       WP_003594509             132 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Lacticaseibacillus paracasei].
ACCESSION   WP_003594509
VERSION     WP_003594509.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus paracasei
  ORGANISM  Lacticaseibacillus paracasei
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 132)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 132)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Lacticaseibacillus paracasei"
                     /db_xref="taxon:1597"
     Protein         1..132
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=14051
     Region          2..126
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(7..10,40..42,45,71,108,122)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mlklytdgat kgnpgpagig ilvsglphqi qkhaalpams nheaefaaai agfellsqag
       61 lnttpvafys dsklviqaie kqyakhypdl agrlltligq fplvlpnwlp dranrgahml
      121 aqqglrqset ki
//
LOCUS       WP_003604528             373 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Lacticaseibacillus paracasei].
ACCESSION   WP_003604528
VERSION     WP_003604528.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus paracasei
  ORGANISM  Lacticaseibacillus paracasei
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Lacticaseibacillus paracasei"
                     /db_xref="taxon:1597"
     Protein         1..373
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41905
     Region          1..265
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          260..349
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrfihtadwh igkklndfdl ledqqavfeq lvetaethkv daiviagdly dralpseaav
       61 svldnmlikl nrdhgypllv isgnhdsavr lrtgrawyaa tkmfvntqva eafapieldg
      121 vqffllpyfe pfavrdyfqd ktitnvaqai rpivakmktl fkpdmrhilv shffaagsdh
      181 sasetkvnvg gldavplddl aafdyvalgh lhnhhalhge pkiqysgall kyavseanqe
      241 kgvyivdtet mdrefvplkp khdlielkas yadltapayy qqqdrdayig idltdtqvip
      301 nvmaqlrqiy priislrren gvnaikplqe rqrdldpmsl lqtffkdmtq ddlsaaqikw
      361 akaglttakk eqa
//
LOCUS       WP_003597419             346 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Methylorubrum
            extorquens].
ACCESSION   WP_003597419
VERSION     WP_003597419.1
KEYWORDS    RefSeq.
SOURCE      Methylorubrum extorquens
  ORGANISM  Methylorubrum extorquens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylorubrum.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 346)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Methylorubrum extorquens"
                     /db_xref="taxon:408"
     Protein         1..346
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36722
     Region          13..344
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 misaiqsegr tvgariaaia thlpervltn ehlaelypdw ssdkildktg irerrvaaey
       61 etagdlafha aeklfaagdc vredidflil ctqapdyllp ttacllqdrl glgrhvgald
      121 vnlgcsgfvy glalatglia agaartvlll tadtyskfih egdksvrtlf gdgsaatlit
      181 asnesvigpf vfgtdgaggk dliveaggfr tprgpdtala eadshgnvrs rehlymngan
      241 vmsfslrevp rtfarllets gvtqsdvdhv vlhqanklml nalqrkmglp agkvphhyed
      301 igntvsstip fvlanlrdkg qmapgrrlvv igfgvglswa gasivc
//
LOCUS       WP_003606794             361 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Methylorubrum extorquens].
ACCESSION   WP_003606794
VERSION     WP_003606794.1
KEYWORDS    RefSeq.
SOURCE      Methylorubrum extorquens
  ORGANISM  Methylorubrum extorquens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylorubrum.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Methylorubrum extorquens"
                     /db_xref="taxon:408"
     Protein         1..361
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37498
     Region          3..204
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 matisgtngd nvlngtlqdd vilgllgndv itdpggfnri dgqdgndtit ggnnvdyiag
       61 gpgndtiygg ngsdqligei gndtiygqdg ddyaagnpgd dvlyggrgnd ffvgeqgadl
      121 vfgeegndfv aggedddtvy ggggndlvdg dlgndvlfgd agndvlfgdy gndrmsggtg
      181 tntldgalgi dtavfnfnfa qagvtsagtl ssiagqnsld tvkntevfaf adrsilqgdg
      241 nqavddlfyl srygdvyrng ndaeqhfsdy gwkegrnpna ffdtkgylaa yadvaaagin
      301 plehyltygw kegrdpsaqf dtkqylaang dvaaaglnpl lhyleygave gratfndgtf
      361 a
//
LOCUS       WP_003606038             456 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Lacticaseibacillus paracasei].
ACCESSION   WP_003606038
VERSION     WP_003606038.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus paracasei
  ORGANISM  Lacticaseibacillus paracasei
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 456)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Lacticaseibacillus paracasei"
                     /db_xref="taxon:1597"
     Protein         1..456
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=50283
     Region          76..189
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          197..312
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          334..456
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(407..408,411,429..432,434)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkknkrwllv vgvlvvlmgg fyiiqsmhyr dhflpnteil gvdvsgqtvn aankkltdqf
       61 dqrqytfvek nkkilkvkgd alglsqdfkk gltqilnkqn pwqwttsvfa gqktnaqedp
      121 tintaalkqf atstadklnq nrqepvnaql vtsgdqfkiq kevngdqida dklattvtsa
      181 ldnhrqviel tdaykkptvk asdrdlqtte rdmnklastk vslqiqsttv tvpqatvlsw
      241 vtndngkatv ssqaitnyvt alsqqystih ktrqfnsqqq gtvsvpagty gwsinisats
      301 amilasvkag qdlnkevshs gsgytttgdi gntyvevske kqhewyikdg kvvmdsdivt
      361 gkpgqdtpsg vfyvwskqrn atlrgknddg ssyaspvsyw mpidytgvgl hdspwqpkyg
      421 gdwykehgsh gcvnnppdfm aklyaavdeg tpvivy
//
LOCUS       WP_003607296             633 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup, partial [Methylorubrum extorquens].
ACCESSION   WP_003607296
VERSION     WP_003607296.1
KEYWORDS    RefSeq.
SOURCE      Methylorubrum extorquens
  ORGANISM  Methylorubrum extorquens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylorubrum.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 633)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 633)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 633)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Methylorubrum extorquens"
                     /db_xref="taxon:408"
     Protein         <1..633
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
     Region          8..633
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 asagavdasp qeahghaktg fwaltvgsvg vvygdigtsp lyafrealap srsdgillae
       61 evigtaslii walllivtik yvaillrmdn ngeggilslm aqarhalggs kivfmlgllg
      121 aslfygdsvi tpaisvlsav eglklvtpaf edyvlpitva iilglfavqs hgtarvatff
      181 gpamvvwfla maaaalphia gnpgvlaafn pwyavhyllg hgtgalvalg avflavtgae
      241 alfadlghfg rrpiqvawlg lvapclvlny lgqtalvlak pettdpfyql vpewglipmv
      301 llatlatvta sqavitgafs lsrqaiqlgm lprmeirhts eahsgqiylp qintllalgv
      361 vilaisfrss salasaygia vtgtmlltas mayvvlwkvv rlsplvsaai impfivlesl
      421 fllsnllklh eggyvplmla gglmlmmwtw vrgvtilfnk trktdvplve lvgmleksts
      481 yqrvkgtavf ltsdpeiapa allhnmkhnk viheknvvlt vetmdrprat qservriepv
      541 gfgfyrvvmr fgymetpnip rtltllkreg fkfdimstsf flsrrsirpa ahsgmplwqd
      601 rifitlakna ndatdffqip tgrvvevgtq vtv
//
LOCUS       WP_003603355             338 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Methylorubrum].
ACCESSION   WP_003603355
VERSION     WP_003603355.1
KEYWORDS    RefSeq.
SOURCE      Methylorubrum
  ORGANISM  Methylorubrum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae.
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
REFERENCE   4  (residues 1 to 338)
  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 338)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Methylorubrum"
                     /db_xref="taxon:2282523"
     Protein         1..338
                     /product="CmpA/NrtA family 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=34932
     Region          3..251
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mrirlgyvpl tdaapviaaa elgfaraegl eielarepsw atlrdrlalg hldaahmlgp
       61 laiasalgls gpearlsvpm alglngnavt vsnalwaama pesdglgdva aafsavarar
      121 agegrplvig tvhpfsshsy qlrlfaglsg ldldatvrlv vvpppetvda lrrgridgfc
      181 vgapwnsvav aaglgriaal gceiapdcpe kvlalpaega dftaplvrav hraglwcaap
      241 enrealsrll aeraeldada allartlsga livdrdgter anpdylrlda athrpdreha
      301 rwlvaqmaac gqvasggdaa draaalyrpd lfaaaigg
//
LOCUS       WP_003609759             127 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Weissella confusa].
ACCESSION   WP_003609759
VERSION     WP_003609759.1
KEYWORDS    RefSeq.
SOURCE      Weissella confusa
  ORGANISM  Weissella confusa
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Weissella.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Weissella confusa"
                     /db_xref="taxon:1583"
     Protein         1..127
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=13788
     Region          3..127
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(8..11,41..43,46,72,109,123)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mliklyadaa tqgnpgpsga gvvisadgkq tqlhhalgem snheaefraa ifafeqllpi
       61 aspddtvmfy idsklvadsi gksyakhype lidtlmalid rykivlttwi pdrenqgahk
      121 lalqaih
//
LOCUS       WP_003601768             295 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Methylorubrum].
ACCESSION   WP_003601768
VERSION     WP_003601768.1
KEYWORDS    RefSeq.
SOURCE      Methylorubrum
  ORGANISM  Methylorubrum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Methylorubrum"
                     /db_xref="taxon:2282523"
     Protein         1..295
                     /product="formate/nitrite transporter family protein"
                     /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=31990
     Region          58..288
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msqesrthgd pedegeakth gahtrekdna qvekahrpda lilheiirre geeemrrtwl
       61 alslsgfaag ltmgfslivp gvlkghlpha pwaelvtsag ysigflivvl grqqlftent
      121 vtpilpllte rtfgallrvv rlwgivlvan ilatiaiasv lahtdafkpe vreafaeisr
      181 htiedpfwtt vikavfagwl ialmvwilpa sgsaapfiii lmtwlvsmcg lahivagsvd
      241 ayylvaigei dfskyltgff vptllgnivg gvtlvsvlnf gqvapeiedh nrvga
//
LOCUS       WP_003609848             731 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor family protein
            [Methylosinus].
ACCESSION   WP_003609848
VERSION     WP_003609848.1
KEYWORDS    RefSeq.
SOURCE      Methylosinus
  ORGANISM  Methylosinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylocystaceae.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Methylosinus"
                     /db_xref="taxon:425"
     Protein         1..731
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=80118
     Region          27..731
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 msrslllrgv aagalslsaa fsfaqealpp idvgafassp stdkgsltap pvaeqrrrll
       61 qtagsvafvd aatpemetrh vadlrdalkd vpgvfvdtry gqelrlsmrg snltrdyhlr
      121 gfellqdgvp mnyadgggdf yeidpkyfrs ievykggnal tfgsstlgga infvsptaht
      181 aiapnmasid ggsfgsvrgq tqvsrvlgdf dflvngtfta sdgfrqhsqs dykqingnfg
      241 yrfsndietr fyfgvydvhq qlpgtltlsd arsnpslats pyiagagpng fganqarnvm
      301 nqrisnkttl qtdigridvd swfvhnylyh pifvvieqeg etwgfspklt tqleiaghkd
      361 elvvggriwg ggstdnwfvn yngmklnpgg gswtnwvams npgsdprirn nrmtslnlea
      421 ffenrfyvtp elamllgaki fsddrrysvi ggipfeplan hseqnyrgiv pkvglmfepq
      481 kdlqffaaft gsrdvpdfvd ltqgffppta gsnftplaaq kawtgeigsr gkwdrfawdv
      541 tyyhselqde llkfnanpgi gipattfnak rtmhqgvela asvdllrdvt apgagdllkl
      601 sqvwtwndfr fvgdvnygdn plagiprhvl rttlaysrpd glyvapavdw vpegsyvdym
      661 htlqtpgyll vgaqagmklp ygfsiyvdar nltdrhyisd vttiidargs tpaafypgyg
      721 rsvfaglkwa f
//
LOCUS       WP_003603354             430 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Methylorubrum].
ACCESSION   WP_003603354
VERSION     WP_003603354.1
KEYWORDS    RefSeq.
SOURCE      Methylorubrum
  ORGANISM  Methylorubrum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae.
REFERENCE   1  (residues 1 to 430)
  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 430)
  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 430)
  AUTHORS   ter Beek,J., 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 430)
  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 430)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Methylorubrum"
                     /db_xref="taxon:2282523"
     Protein         1..430
                     /product="CmpA/NrtA family 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=46571
     Region          40..301
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 msidhgnttr rgvlkgaaaa lalagaaraa lpagafaqga gpevkgaklg fialtdaapl
       61 fvakekgifa kyglpetevl kqaswgttrd nlvlgsegng idgahiltpm pylisagrvt
      121 qnnvpvpmyi marlnlngqc isiakehidh kigldtkpfk aaleakkasg kavkaamtfp
      181 ggthdlwiry wlaaggidpd kdietivvpp pqmvanmkvg tmdcfcvcep wneqlihqgi
      241 gytaittgel wkdhpekafa mraawvdkyp naakallmav meaqqwcdkp enrdemaaiv
      301 akrqwinvpv advvdrmkgk fdygtgrvve nsphimkfwg dnasypyqsh dlwfltedir
      361 wgkfdaqtdt kaliakvnre dlwreaakal gvaaiptsts rgvetlfdgk vfdpenpaay
      421 lnslgikkva
//
LOCUS       WP_003609976             219 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Weissella confusa].
ACCESSION   WP_003609976
VERSION     WP_003609976.1
KEYWORDS    RefSeq.
SOURCE      Weissella confusa
  ORGANISM  Weissella confusa
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Weissella.
REFERENCE   1  (residues 1 to 219)
  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   2  (residues 1 to 219)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Weissella confusa"
                     /db_xref="taxon:1583"
     Protein         1..219
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=23237
     Region          73..128
                     /region_name="SLBB"
                     /note="SLBB domain; pfam10531"
                     /db_xref="CDD:463136"
     Region          149..218
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mttfkalyyr fqhvifffgg lvavgigliv wwqcsqtkpv lprdvspsia adqssqmpss
       61 vsksvsstta kvvidvkgav yrpgvykfnn gpimadvlek aggtlptvdr trlnlaaplv
      121 ngqvlyvpng tedvpeqypl pgqatttsat ggdtssetin lntatlaelq klpgvgakra
      181 qdiidqretm ggfktvadlq evsgigektf aklepmvtv
//
LOCUS       WP_003608924             484 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [Methylosinus].
ACCESSION   WP_003608924
VERSION     WP_003608924.1
KEYWORDS    RefSeq.
SOURCE      Methylosinus
  ORGANISM  Methylosinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylocystaceae.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Methylosinus"
                     /db_xref="taxon:425"
     Protein         1..484
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52561
     Region          67..117
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          95..>483
                     /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 mrtktvnrkr dragaataig liilgpsala idagpalarl apqpyeiaag pmadalsrla
       61 desgahlvfd aaiarhvvtr gvhgkrtlee aldelltgts layrvdpegr avtivvaqng
      121 vtvsdagaet lptidigaes aratnatrga rsseprtpse gyvvtnsata tktdvplkqt
      181 pasvqvvpkq lirdqavtnl sgalenvsgv rsnndaiggy lfkirgfdsy dvyrnllnsg
      241 sayfsgsdma nverievlkg pasvlfgrge pgglinlvtk tplseprfvv eqqignydhy
      301 rtqwdfsapv aevpglawrl sgayqenrvf rqfdhasrvm vapvvtykps dwteltvdlq
      361 yygnqprvls gipvvgsapa nvplwrsyqe pndprdrtds fvgsyvfrqn ldenwkvtnr
      421 flysslwysq slvahsglsd dltkldryaq aqntavetys tnfdvqgkfe tfgarhiflf
      481 gldi
//
LOCUS       WP_003609542             183 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: transcription termination/antitermination protein
            NusG [Methylosinus].
ACCESSION   WP_003609542
VERSION     WP_003609542.1
KEYWORDS    RefSeq.
SOURCE      Methylosinus
  ORGANISM  Methylosinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylocystaceae.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Kang,J.Y., Mooney,R.A., Nedialkov,Y., Saba,J., Mishanina,T.V.,
            Artsimovitch,I., Landick,R. and Darst,S.A.
  TITLE     Structural Basis for Transcript Elongation Control by NusG Family
            Universal Regulators
  JOURNAL   Cell 173 (7), 1650-1662 (2018)
   PUBMED   29887376
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Liu,B. and Steitz,T.A.
  TITLE     Structural insights into NusG regulating transcription elongation
  JOURNAL   Nucleic Acids Res 45 (2), 968-974 (2017)
   PUBMED   27899640
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Steiner,T., Kaiser,J.T., Marinkovic,S., Huber,R. and Wahl,M.C.
  TITLE     Crystal structures of transcription factor NusG in light of its
            nucleic acid- and protein-binding activities
  JOURNAL   EMBO J 21 (17), 4641-4653 (2002)
   PUBMED   12198166
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415705
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Methylosinus"
                     /db_xref="taxon:425"
     gene            1..183
                     /gene="nusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
     Protein         1..183
                     /product="transcription termination/antitermination
                     protein NusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
                     /calculated_mol_wt=20180
     Region          18..183
                     /region_name="NusG"
                     /note="Transcription termination/antitermination protein
                     NusG [Transcription]; COG0250"
                     /db_xref="CDD:440020"
ORIGIN      
        1 miafrddpps rrddgptest rrwyvvqtrp qreagvvlql eaqnfraflp rvtrtirhar
       61 klrmvqapvf pgylfvsldl qrdrwrsvng tfgavglimg ddypaptphg vveqllscad
      121 argacrfdld laegqkvkvl agpfadaigs lvrlgdnerv qvlldimggr vpvtlersal
      181 aav
//
LOCUS       WP_003613186             403 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Lactobacillus delbrueckii].
ACCESSION   WP_003613186
VERSION     WP_003613186.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus delbrueckii
  ORGANISM  Lactobacillus delbrueckii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 403)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Lactobacillus delbrueckii"
                     /db_xref="taxon:1584"
     Protein         1..403
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=44060
     Region          145..249
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          <309..403
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(354..355,358,376..379,381)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mtsrkdyrkk ntqgskylii agvavivlac agiwghnayq qhqatvlaen kkqvaynkkh
       61 fnanvtiygv kvgkltvdqa vekiqakavn klvykdgkis avrdskltti skeqvqkyfd
      121 kqytqlptdq synyentalk kgksklkait aasvdysvag ktftlaakdy ltqvsyysga
      181 vhyddasklt aklnamdkev ktlgksykfk tpagstitvt nqsygwgiwt asakkavlsa
      241 yetgkktidg knhiygegyt tqglgygksn nglgnsyvvv siasqdmwvv vngkvvvtvs
      301 dvvtgtankg dnatptgvwy imykqkdatl rgqndngsny askvsywmpf tmsgcglhda
      361 swrtdwssta ylkggshgcv nirpseiksv wdavklhmpv ivy
//
LOCUS       WP_003614715             821 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [Methylosinus].
ACCESSION   WP_003614715
VERSION     WP_003614715.1
KEYWORDS    RefSeq.
SOURCE      Methylosinus
  ORGANISM  Methylosinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylocystaceae.
REFERENCE   1  (residues 1 to 821)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 821)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 821)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Methylosinus"
                     /db_xref="taxon:425"
     Protein         1..821
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89260
     Region          60..113
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          89..821
                     /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 mgstlamaam gvltigagaa dspaqasipa rerlgwiqky eippgsmata lntfayvsgl
       61 hiaydarvte rlttsgldga fstkdgldrl lrgsglayrf adngrsvsiv laqndtgvrt
      121 dasgatalpt idvgrearse rgaagvrgpg dratgysaps atsalktdtp ilqtpvavqv
      181 vtrqtmddqq aisiqealtt nassvsqnps astydsfnir gfstnygvyr nnlrrhlvst
      241 ldtsnlqsve ilkgpagmly grvepggiid lvvkrpletp yysfqeqags fgmtrtsvda
      301 tgpltpdrtw lyrisgnfmh adsyidyans qnvfiaptit fhpdeqfrln vdaefqdsil
      361 vdvyqtipai gtrpasvpis rylqdpavta nnptrhtrel igydwtfafd kdwsltnrll
      421 yeygyhgvtt tyfgsineat gdatrrlfmt ptyvgslstn ldlkgkfetg plrhdllvgg
      481 dfftenqdqy ngylgvspyv ksiniyapvy gsgvpykptp naftyarenw kglylqdmis
      541 afddrahlll ggrydwadav nsfssvsyvs aknaavtiyn eafsprigls iqpfpwlsfy
      601 gnysqsfgan ngvtggnipl apqrarqweg gvkaeffdkr ltatfayydi tktniptpdp
      661 lnprfstlig eaesegvefd ltgrlddnws vignfshdya vvtkdnnkan igrrlpsapl
      721 nagnlwlkyd ahgafeglsl gggvsivgsm qgdtandfql pdytlvnama syrfevegaa
      781 vtaqlnvknl tdaiyypasl nrttitvgap rtvlgsirve f
//
LOCUS       WP_003617817             671 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Novacetimonas hansenii].
ACCESSION   WP_003617817
VERSION     WP_003617817.1
KEYWORDS    RefSeq.
SOURCE      Novacetimonas hansenii
  ORGANISM  Novacetimonas hansenii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Novacetimonas.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 671)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 671)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 671)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 671)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Novacetimonas hansenii"
                     /db_xref="taxon:436"
     Protein         1..671
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=72974
     Region          47..671
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mtqatgpdap gtsttpahga qaadgkapdg kasapvpskv teygadqheh aanpvgfaal
       61 lgvlgvvfgd igtspiyalr stimvvsqhh riepweilgv lsliiwslll ivtvkyvili
      121 mradhngegg iislmsmaqr vattnrlrva lgmvgiggac lffgdgmitp aisvlsaveg
      181 levsfpaare lvipiallvl vglfsvqsyg tgkvgtifgp imlvwfsllg ilgltqivqh
      241 ptillavspt yavqfiiyhg wlsfialgsv vlsvtgaeal yadmghfgrq piryawlfcv
      301 lpclalnylg qgaliiahpt tlanpffllg phwlqvpmvi lstcatvias qagisggfsl
      361 crqiiqlgyl prmrithtna eeegqiylpe fnrflmtgal llvlsfrssd alasaygiav
      421 tgtfmctcvl amvvfrrlyh wsrlaaittf ggffvidttf fasnalkipq ggwvpvmlgi
      481 vltlmmttwk kgrllimnrq kqdsmpmnsf larlpqsrii rvpgtavymt atpdfvpacl
      541 lhnlkhnkvl hdhvlfvtvq tldqpeadrg hrvalqelap dmyriilryg fmetpnlpra
      601 ledlkasgle fdalqasyft srellvrssv pkmsrwrmsl fllmarnatp ateffrippd
      661 rvvelgvrla i
//
LOCUS       WP_003613606             841 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Methylosinus trichosporium].
ACCESSION   WP_003613606
VERSION     WP_003613606.1
KEYWORDS    RefSeq.
SOURCE      Methylosinus trichosporium
  ORGANISM  Methylosinus trichosporium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylocystaceae; Methylosinus.
REFERENCE   1  (residues 1 to 841)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 841)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 841)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..841
                     /organism="Methylosinus trichosporium"
                     /db_xref="taxon:426"
     Protein         1..841
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=92219
     Region          73..122
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          102..841
                     /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 magrnirtkf gsgegnmgsi lamalvalga gvsdspaeaa ispqeraglv qnyripsgpl
       61 psalnsfael nglqilydsa vtsrlrtigl egdfsvhdgl drllrgtgls wsisargdtv
      121 sillaqndrg tmndaasgat alptidvgae tknqqgaqtg prgpgdrhtg ynagsasatl
      181 kmdtpllktp lsvqvvtrqt mddrqeisvk dalitnvsgi qltpswfdtm lkirgfsnta
      241 stykngliey rmraldttnl qsidvmkgps amlygrvepg glvdlvvkrp ldtpyyslqq
      301 qvgsygltrt tldatgplta dktvlyrfng efyytdsyrn fvtdrnvfla ptitlhpieq
      361 frmnidfeyq rrdfvddyal ypavggapan ipasrylqep flntnapdrl dkkriaydwt
      421 ydfskdwslt nrlaytnagn gladtfggvf npvtgvltrs anffpgytdk nfttnldlkg
      481 kfvtgplqhs tlvgfdyfnt ftplytsyfn ilpstniyap iywtqmnryq npsfnqigqk
      541 wtgvygqdmi sflddsvhvl lggrydwaet santsrtsay aaqasyttyy nkafsprvgv
      601 ayqplpwvtv ygnfsrsfgl nstdvqgrpi apqraeqweg gvkaelldkr ltmslvyfdl
      661 vksnvaardp nnsantmlig karsqgiefd lngriddnws vianythddv rtlvgesvdp
      721 asqltkqrlv agyklpaspr nygnlwvkyd adgafagfsl gggisvvess lgdnansfvl
      781 pgytlldgmi ayttkiegyn vtaqlnvknl tdvayyptsd srttiqtgtp rtflgslrve
      841 f
//
LOCUS       WP_003615359             790 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: penicillin acylase family protein [Methylosinus].
ACCESSION   WP_003615359
VERSION     WP_003615359.1
KEYWORDS    RefSeq.
SOURCE      Methylosinus
  ORGANISM  Methylosinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylocystaceae.
REFERENCE   1  (residues 1 to 790)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 790)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 790)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Methylosinus"
                     /db_xref="taxon:425"
     Protein         1..790
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=85601
     Region          23..787
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkilrvatis lallilavaa tafgalrlal pvrsgthglp glaqsvtirf ddsgaphiaa
       61 anredafaal gyvtagdrlf qmdllrrksa grlaevfgpa llesdrfart mnfdrladai
      121 lerlpddekr aldayargvq qamrdavvkp wellalgydp epwrprdsil valtfahmss
      181 sieseraatv mraalpaavv efltpesdcy nealaprspe rcaagahppe elrpllragv
      241 rasrgaaivg vtapigsnaw avsrartadg railasdmhl flqqpnvwyr ahlaygdvai
      301 egltypgapl vvvgsngrva wgltnldadf tdlvrlrpag edgtkyatae gprdysirre
      361 risvrggeda lldiketvfg pvlpdrllgd etalrwtmld paatnldlmn mdravdvrsa
      421 lrilqgvgvp plnaivadag gsigwtligk ipkrrgfsgr faefwddggh gwdgyfsree
      481 lpvvvdppeg fivsanqrml gradfapeig hdysggvraw riaerlrsga fveadmaalq
      541 ldssaeyyry drdvalealr askiadaete dllraleafd graepsslgl rlvfefrsel
      601 keamlapile rcraldptfr yfwsnvdtsv ramidarrae sdreewngvv vaalrraaar
      661 ltaasgetsi aglrwgeenr vqmfhplsgv ssllapfldm pkaevagcpe cvrfhavsqs
      721 gngvganarl vaspgheddg lfqmaggqsg qpasphyadr hadwvagrsr plrarsfese
      781 lvlepakgap
//
LOCUS       WP_003619819             770 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Novacetimonas hansenii].
ACCESSION   WP_003619819
VERSION     WP_003619819.1
KEYWORDS    RefSeq.
SOURCE      Novacetimonas hansenii
  ORGANISM  Novacetimonas hansenii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Novacetimonas.
REFERENCE   1  (residues 1 to 770)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..770
                     /organism="Novacetimonas hansenii"
                     /db_xref="taxon:436"
     Protein         1..770
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=84289
     Region          90..769
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mkselslppt vpprlhplpy sdrgpvaeas nrltfalass lfgvlvashh aiaaasissd
       61 ditphriphh spphhaaggh davghhdeha assglnastv ehiavhhhsa athqaevylk
      121 tipggtsvid aatvlkgrna tnadafkyqa gvfaqapcgs ddlrisirgs giqtglnatr
      181 sgimflfddi plttpigtvn elqeplgiry teilrggngm dfgstqlgga inyvtqtgyn
      241 sqryqarvea gsfgyvkeql ssgsvigksd yyisvtnsyr agyqdntkst nfgvnfnygy
      301 kfndrvdtrl fvryrqtseg npfyltrdqi renpkqvqtg yaglgtqtie pgttfvadrt
      361 tihiddqskl vagfaylnap mnhelgstss lydidyatgm vdytrndnll ghnsdtdigi
      421 ytshdltati dnrvrvksay pdyaigtlvt rshlggsdtv lhvrnnteif hnfwltaaga
      481 lsytprsgsq typqtssfsq nalyfaprag fryvitpnve iygnvtrsvq spqdwqylsg
      541 avytsgiakg ltsgwvnlkp qtattfefgt nghfkgtews vsyyhsavhn ellsvmtpls
      601 elynnatygn asatthqgve tsfhstlykw qgniislrqa ytfqsfrfnh dstwghnyip
      661 giprhfyqge lhldmkngfy tsfdvevsss vlasydnqyk aapyhiynfd igylwpnkhr
      721 qvflslhnla nkhyatgvvp vystangqqp aamlsgdgfg ifggvsigfn
//
LOCUS       WP_003617751             801 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Novacetimonas hansenii].
ACCESSION   WP_003617751
VERSION     WP_003617751.1
KEYWORDS    RefSeq.
SOURCE      Novacetimonas hansenii
  ORGANISM  Novacetimonas hansenii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Novacetimonas.
REFERENCE   1  (residues 1 to 801)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 801)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 801)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..801
                     /organism="Novacetimonas hansenii"
                     /db_xref="taxon:436"
     Protein         1..801
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=87185
     Region          11..798
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mrnigcsrrq illggaaagf atfspmaraa rqrmvvaald glsapvevle dhwgvphvra
       61 gsipdaffan gflvardrlw eldfghrqal gqlaevfgpd fvdtdtanrl flfrgdaaae
      121 larfspqvqd carayvagin arlaqvranp dllppeftif gympmswdvl dliriraevt
      181 gntraeirra rlaargglsy dalctplepa heprvpggld vhavsqgdlg lfdvlqaspp
      241 lgrvrdagdt ehrrtnsgsn awviapsrta tqrpilandp hlsfgvpgpr yvihlsapgl
      301 dvigggtagm pgvmqghnaq iafgrtnfhi dqedlfilrt hpthpdryfh dgawkqmetv
      361 pthiavrgea grdvvlryaa qgpvvsadpa rrratavsat wlypgangll vniglnlahd
      421 wdsfrealrv htsptnftya dtagnigwqa agglpsrvdg hdgllpvpgd ghydwkglqp
      481 lemlpstfnp asgwfatsne mnlppgypaq errvsfewrd rfrhdrvahv leetpratia
      541 dcaalqhdtf srlaldmvgl lgavppdlmd vaallrgwdg hvhadsaaaa lyevwwtrle
      601 ralhtllipa rlhdllpgpi natvqktllh apdarfganp aqtrddmlvt alrgakselr
      661 drlgpvmaaw rwgtlhtitl dhalahvpai aarfpqlgga rtgtggdpyt vmarwynpls
      721 nghdpyvatg gasylmvcdv gewdhsvfln fpgqsgdprs ahyadfmpdw lrgrmqplpf
      781 sahrvraaav grtilqpaht p
//
LOCUS       WP_003619705             172 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Lactobacillus delbrueckii].
ACCESSION   WP_003619705
VERSION     WP_003619705.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus delbrueckii
  ORGANISM  Lactobacillus delbrueckii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Lactobacillus delbrueckii"
                     /db_xref="taxon:1584"
     Protein         1..172
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18618
     Region          3..163
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mkftkllksr ksirtytgkp adkkqvkkii eaaelapvac glyenyqlti indpkllkei
       61 dqeaammfgd leshplysvp tlilvsarkq dekayasagi iahnmvlaae nkglgacylf
      121 gaaaalaahp etvmkldlpa gfmpvcgvgi geteeeltir dqkldrigin ei
//
LOCUS       WP_003614731             395 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Lactobacillus].
ACCESSION   WP_003614731
VERSION     WP_003614731.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus
  ORGANISM  Lactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Lactobacillus"
                     /db_xref="taxon:1578"
     Protein         1..395
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42907
     Region          2..393
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mdkilainsg sssfkyklfs ladesvlasg lgdrigidgs tfsmkladgt kheaevdlpn
       61 qevavqtlld wlkeygviad vkeivgvghr ivnggelfpd saiidkdnih kvfdltnyap
      121 lhnpaeghgi qafmnilpdv pqvgvfdtsf hqsmdevhyi yslpyeyyek ykarkygahg
      181 tsvryvsgka aellgkdlkd lklvvchlgs gasvtavkdg kcydtsmgfs plagvtmgtr
      241 sgdvdpsvlq yimkkegitd fnemidilnh ksgllglsgi ssdmrdirns ddkraklada
      301 vfinrvvryv gsyiaemgga davvftagig ehddevregv mkslsfmgvd fddaankaan
      361 egfitkedsk lagliiptde elmierdvvr laklk
//
LOCUS       WP_003618035             307 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Novacetimonas].
ACCESSION   WP_003618035
VERSION     WP_003618035.1
KEYWORDS    RefSeq.
SOURCE      Novacetimonas
  ORGANISM  Novacetimonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Novacetimonas"
                     /db_xref="taxon:2919364"
     Protein         1..307
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32937
     Region          16..259
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mdtmtpqcaw dlkaqlgegp vwaeaeqaly fvdivgsaih rhvpatgaqa swkaphrpgf
       61 lvpvadgtfm cglqdglhvf dprtghfsaq avvepeqpgn rindgyvdpr grlwfgtmdd
      121 getspsgaly svtrqadgsl rivrqdegyv vtngpalspd grtlyhndsq qqsiyafdls
      181 ddgmlsnrrv farltdgypd gvvvdsagcl wvgvwgggri arflpdgqgl ppvivparnv
      241 tkiafggady rtvfvttark glsddvlatq pqtgglftfr vdvpgqpqat fpasglrelg
      301 relhtpa
//
LOCUS       WP_003623543             660 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Acetobacter pasteurianus].
ACCESSION   WP_003623543
VERSION     WP_003623543.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter pasteurianus
  ORGANISM  Acetobacter pasteurianus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 660)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 660)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 660)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 660)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Acetobacter pasteurianus"
                     /db_xref="taxon:438"
     Protein         1..660
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=72215
     Region          36..660
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mtdpanksag spptgdqphv asapeprrit efdadqpqha aapvgfaall gvlgvvygdi
       61 gtsplyafrs tvevisghhq vapweilgva slifwtlili vtvkyvilim radhngeggi
      121 laimslaqrv vinqrtrwil glvgivgacl ffgdgiitpa isvlsaiegv evsvpaahdf
      181 vipvailvii slfsvqwigt gkvgtifgpi mllwfgtlgv lglmeilhhp ailmalspty
      241 alefifyhgk lsflalgsvv lcvtgaealy admghfgrap iryawlffvl pmlvlnyfgq
      301 aalvisdpka lanpffllcp hwmqgpmvvl stfatviasq agisggfsic rqliqlgymp
      361 rlrithtnae eegqiylpdf nrflavgavl lvvafrssda lasaygiavt gtfictsila
      421 ivvfhrhfnw pawkvgaifg gfllldstff aanalkipdg gwvpvllgcv ltlmmttwkk
      481 grsliiarqr qdslpmgsfi arlpqsriir vpgmavfmts tpdfvppcll hnlrhnkilh
      541 dhvlfvtvqn ldqpeaergh rvaveelapd iyrivlrygf mempnipral eelkangvdf
      601 dalqasyfts relitrssvp rmsrwrmsif lfmlrnstss meffrippdr vvelgvkvai
//
LOCUS       WP_003623712             345 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Acetobacter
            pasteurianus].
ACCESSION   WP_003623712
VERSION     WP_003623712.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter pasteurianus
  ORGANISM  Acetobacter pasteurianus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Acetobacter pasteurianus"
                     /db_xref="taxon:438"
     Protein         1..345
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37905
     Region          1..>284
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msvnlhsftq yapgssrkil dninltvedg afialvgpsg agktsllrai gglspvyegq
       61 lliddlpigh sdlpkrktgf vfqnyalfrh msvarnisfg ldvlprkqrp draaitarvq
      121 dlleliqlph ladarpdqls ggqrqrvala ralatepkll lldepfgald pivrrtirrw
      181 lrelhdklgl ttilvthdhe ealdiadrlv vmqdgrivqd adattlntsp qtpfvmqflg
      241 etlefagkiq dgqfipedtd alpfpvsekn gkttvfirpc dvqfisgkga ahilsrsrnp
      301 nglyhyavqt tqraldittp mpteisegeq fgldishgki fanlp
//
LOCUS       WP_003625641             672 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: VirB4 family type IV secretion system protein
            [Lactobacillus].
ACCESSION   WP_003625641
VERSION     WP_003625641.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus
  ORGANISM  Lactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 672)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 672)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Lactobacillus"
                     /db_xref="taxon:1578"
     Protein         1..672
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=76990
     Region          60..627
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 msfgdkvidl fmptkkehnq gnsdqtgskp kpevedftkl idrdslhslf pfsweqypty
       61 vqsgenfirv laiadypkrv ygnwlselkr kkgvidivqy idsasnnsmi tyykktiqnk
      121 eaqklntfdp ykkkilqnyi dsanmqldky ldnsttfvyq hmliylrans laeldgltes
      181 vkntliklqm kplvpvkatf qafwstmpin enlmgdytyk esntevassm fpfddaeild
      241 lkprsdiegv nkdtnsliav dmldrnktln qnqviigtsg vgkttymiqk ilryaiqdyq
      301 lyiidpeney tkivealgga vlhltsnaky kinplqifse eilsadeavt nldllvkdki
      361 qrlkgffevl ktgitqvela ilddvvkqay vnsgvlkysr lkeikddqwp tlsnvydele
      421 kladkdadkf nrvkdfyyil gsythgsnsl fdghtnvnlk gkiisfdlkp lqseqevqsa
      481 aylntfqylw deitkdrhsr kklfvdefhf ltlhkaaatf fhqaykrfrk ynagaiagtq
      541 qiqdviegtt dtgqnigeai ignsytkvff gldgkgvddv itklrmtfsd kekkllerrr
      601 qgealmiygs qrafmrvelt eeelrlidpe ayqekyhret agqpdyqkrv vltpseidal
      661 ttteeeggtl ne
//
LOCUS       WP_003627252             224 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Lactobacillus helveticus].
ACCESSION   WP_003627252
VERSION     WP_003627252.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus helveticus
  ORGANISM  Lactobacillus helveticus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 224)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Lactobacillus helveticus"
                     /db_xref="taxon:1587"
     Protein         1..224
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24684
     Region          97..221
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkknivvvas iiiafgaiig lakacapksd vsqeavstqk iakqkknktk hkntkadsdi
       61 lrpykdpkdl rkagtwnkks etkkhpkisp tekdltlrvs legnrtyllr kgkviytmls
      121 tggiykkgks ltqtgtytiq agrgdsffny nlnegannwt swspdnvylf hsvptkgdgs
      181 ynmkeaaklg rtqgshgcir lsvpdskwlm dnipdgtkvv ikdh
//
LOCUS       WP_003628474             401 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Lactobacillus helveticus].
ACCESSION   WP_003628474
VERSION     WP_003628474.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus helveticus
  ORGANISM  Lactobacillus helveticus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 401)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Lactobacillus helveticus"
                     /db_xref="taxon:1587"
     Protein         1..401
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=44833
     Region          145..245
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          273..400
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(351..352,355,373..376,378)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mnedlkrknk rnnliiliig vlivigvvgg fgihnhrvas qaaaekyart hfnpnvkidg
       61 vkvgkltvak atakvnkkak nhvqlrnekl vysynttvpa ideaetkaff kkqqtktpsd
      121 qaynfttknl avakkklnal kkaeltykin gknyqlkakd llndvsyqdn kyrfgdtskl
      181 tekltqidke vstlhksykf tvpvgnkvkg ktitvenktw gwgvyvkkar rlilqafadg
      241 kttfdgadai ygvgystyah gygksnheig ntyavvslkq qevwlvrkgk lvahlddvvt
      301 gtmegskgdq tprgvwyihy kespstlrgt nndgssyasp vkywmpftls gcgfhdaswr
      361 tdwskkaylr ggshgcvnvk pseirkvwnn isknepviiy e
//
LOCUS       WP_003631067             345 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Acetobacter
            pasteurianus].
ACCESSION   WP_003631067
VERSION     WP_003631067.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter pasteurianus
  ORGANISM  Acetobacter pasteurianus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Acetobacter pasteurianus"
                     /db_xref="taxon:438"
     Protein         1..345
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37936
     Region          1..>284
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msvnlhsftq yapgssrkil dninltvedg afialvgpsg agktsllrai gglspvyagq
       61 lliddlpigh sdlpkrktgf vfqnyalfrh msvarnisfg ldvlprkqrp draaitarvq
      121 dlleliqlph ladarpdqls ggqrqrvala ralatepkll lldepfgald pivrrtirrw
      181 lrelhdklgl ttilvthdhe ealdiadrlv vmqdgrivqd adattlntsp qtpfvmqflg
      241 etlefagkiq dgqfipedtd alpfpvsekn gktivfirpc dvqfisgkgm ahilsrsrnp
      301 nglyhyavqt tqraldittp mpteisegeq fgldishgki fsnlp
//
LOCUS       WP_003626685             162 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Lactobacillus helveticus].
ACCESSION   WP_003626685
VERSION     WP_003626685.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus helveticus
  ORGANISM  Lactobacillus helveticus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Lactobacillus helveticus"
                     /db_xref="taxon:1587"
     Protein         1..162
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18001
     Region          5..153
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mvnpifenrr avrkyskeai sddkiqemia afqtapcgmh qadvmnlvvv kdeglrnkie
       61 kvtdnscyna pvlflintkk dsefgerdas vaaenimlea tdlslgsiyi mggaarlndf
      121 sdlqqelgid hefqttviva vgksavepek edrskryhvt iy
//
LOCUS       WP_003631719             236 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Legionella longbeachae].
ACCESSION   WP_003631719
VERSION     WP_003631719.1
KEYWORDS    RefSeq.
SOURCE      Legionella longbeachae
  ORGANISM  Legionella longbeachae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 236)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Legionella longbeachae"
                     /db_xref="taxon:450"
     Protein         1..236
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=25916
     Region          47..215
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mikllvllst iaatfptaas pitnieqeti tqpvqqleiq klsasaptln kgvielalra
       61 ytkayeegdv krrvltiidy svpsdeprmw ifdmnteslv fetyvahgrn sgsgkvpdtf
      121 sndmsskkss lgtyitedty igrkglslnl eglekglnsn aynrrvvvhg awyvepdfik
      181 kegragcswg cpaiaeslak pvinaikngs vvfayypdsy flshsnyist qdiamn
//
LOCUS       WP_003619922              81 aa            linear   BCT 20-JAN-2025
DEFINITION  acyl carrier protein [Lactobacillus delbrueckii].
ACCESSION   WP_003619922
VERSION     WP_003619922.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus delbrueckii
  ORGANISM  Lactobacillus delbrueckii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
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   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 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   4  (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 10011594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Lactobacillus delbrueckii"
                     /db_xref="taxon:1584"
     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=9060
     Region          3..78
                     /region_name="acpP"
                     /note="acyl carrier protein; Provisional; PRK00982"
                     /db_xref="CDD:179197"
ORIGIN      
        1 mseeeifatv kkiaveeldv eedqvtmean ikddleadsl dlfeivnele deydieldad
       61 entktvadvv alvqkqlaek d
//
LOCUS       WP_003632100             199 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Legionella longbeachae].
ACCESSION   WP_003632100
VERSION     WP_003632100.1
KEYWORDS    RefSeq.
SOURCE      Legionella longbeachae
  ORGANISM  Legionella longbeachae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Legionella longbeachae"
                     /db_xref="taxon:450"
     Protein         1..199
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22413
     Region          14..192
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mespelinry kidimealyh rravrnylsk nvdseiihql ldaavhapsa lheesrgfvv
       61 iqnkalldri sesakqltmd ekkkkidlqe ehilqvvqqn efnvfynapa liviystfkg
      121 kfvsadcwla aenlmlaalt yglgtcvigf svpalnlpew kkelgipkkm tavvpiilgw
      181 psdhtlptsh kpplilnwk
//
LOCUS       WP_003633547             394 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Lactobacillus helveticus].
ACCESSION   WP_003633547
VERSION     WP_003633547.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus helveticus
  ORGANISM  Lactobacillus helveticus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Lactobacillus helveticus"
                     /db_xref="taxon:1587"
     Protein         1..394
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43671
     Region          2..392
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkkvlainsg sssfkyklfs lpdekviasg madrvgldna sfeikladgt khvekteiad
       61 qeaavnllik flkqfnvvdd lheivgvghr vvnggeyfdd stiitkenlp kiyeledyap
      121 lhnpaeghgi eafmnvlpev pqvavfdtty hraldpvhyl yslpyeyyek ygvrkygahg
      181 tsirytapha akmlgkdlkd lkliichlgs gasitavkdg ksydtsmgfs piagitmatr
      241 cgdidpsliq hlmhvegksm demihilnhk sgllglsgis pdmrdisesd teraklarki
      301 finrivryvg syiaemggid aiiftagige hdmsvrkevm dafkymgvep dyeaneenge
      361 hfitkpdskv kvmviptnee liierdvvrl tnin
//
LOCUS       WP_003632075             321 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Legionella
            longbeachae].
ACCESSION   WP_003632075
VERSION     WP_003632075.1
KEYWORDS    RefSeq.
SOURCE      Legionella longbeachae
  ORGANISM  Legionella longbeachae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 321)
  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   2  (residues 1 to 321)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Legionella longbeachae"
                     /db_xref="taxon:450"
     Protein         1..321
                     /product="aminoglycoside 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=36817
     Region          52..237
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mtnahtewai silndlgyah dpikteiihd tawsqvcrfq tklgmvylkk vpaalslems
       61 viqllreefn apvpnifahn qelnsflmqd agiplhdvfm qefqpnllie amhdytmlql
      121 nstdriqlfl nlgvpdwrle klpklydqlm aeeelligdg ltlqelkqlk sldgklqflc
      181 eqlacfkiad tfghadfhdk nilfnpkthq ttlidlgevv ithpffsfvn clhratehlk
      241 lpvaqyrklk kacfknwlfl essvqifeii diinqcwtih avlgeyrlin siastavesl
      301 crqgrlsskl rmwiqqsath g
//
LOCUS       WP_003636060             391 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Legionella longbeachae].
ACCESSION   WP_003636060
VERSION     WP_003636060.1
KEYWORDS    RefSeq.
SOURCE      Legionella longbeachae
  ORGANISM  Legionella longbeachae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Legionella longbeachae"
                     /db_xref="taxon:450"
     Protein         1..391
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42924
     Region          3..390
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mnklilvins gsssikfslf acdkqclnly yhgqiqdlye spqinifnas qvlvlnqait
       61 tqgheaglkl lfnwlndlsd sitlaavghr vvhggtffsn ptlitddvmq kiaslmplap
      121 lhqphnleai qiinqlypsl aqiscfdttf hrtqkrlatl falpkslsde gilrygfhgl
      181 syeyiasvit eyigeignkr vitahlgnga smcamyqrks vatsmgftal dglmmgtrcg
      241 ridpgvllyl leqknysteq vtqllynesg llgvsglsnn vrellkhldd krvleaidlf
      301 cyraaleigs llmalggcda lvftagigeh aplirkkiga ylswlgikin deantrnati
      361 inesdstvlv gviptneelm iaqhvrsfln i
//
LOCUS       WP_003633506             739 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Legionella longbeachae].
ACCESSION   WP_003633506
VERSION     WP_003633506.1
KEYWORDS    RefSeq.
SOURCE      Legionella longbeachae
  ORGANISM  Legionella longbeachae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 739)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 739)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Legionella longbeachae"
                     /db_xref="taxon:450"
     Protein         1..739
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=83612
     Region          13..681
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mkaikirtiq lglgslclvf illlqseqpa flnringliy dylskmslhq kknfprvaii
       61 diddysvqqe grwpwprdki alllnnlknl gvkvvafdiv fsdveknyaq slkekvaqlp
      121 faqkdtqeqi ihllnqiepy vdndkifaat lsgnnavlgy llhydaqvkk gslpqpllnq
      181 dakpidatny ivpeflgyng ilplllkasp hagfvsnipd ldgvirhgsl lgnyanklya
      241 nialaavmqy ldtdqvklit hkshgkelld gitikdifip tnhkgqilip fwglpgtidy
      301 ysasdviqnk lspdelagsi vivgstmvll adlhqtplsq tfpgaeinan ivtailtqda
      361 lvefnwntvt gilaitalgg ilvilfpfcs pfilllfyff iitlisgisf llfnyqnlfi
      421 apalifllta llailnfsyd filekrqknk ikqlfgqyvp ptyvkkltdf senytmeget
      481 remtvffadi rdfttlsehl eakeikrlln efftpitdii fshkgtidky vgdmimafwg
      541 aplpdnehcy haisaaltin dnleeinkkl lkmnlpyiri gmglatglmd vgdmgsefrr
      601 sytvlgdtvn lasrlqdltk yyqisilvne stqmketpfl wrlvdqitvk grhiplkiye
      661 plgyrqdasp ellaelqeye qglksyygqe wenakeqflk llarnperhl yqiflsrieg
      721 fiqkpppkdw ngvfvhtqk
//
LOCUS       WP_003631693             224 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Legionella longbeachae].
ACCESSION   WP_003631693
VERSION     WP_003631693.1
KEYWORDS    RefSeq.
SOURCE      Legionella longbeachae
  ORGANISM  Legionella longbeachae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 224)
  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 224)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 224)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Legionella longbeachae"
                     /db_xref="taxon:450"
     Protein         1..224
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=25167
     Region          1..205
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Region          92..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(94..95,98..99,101,125,131..132,135..136,138..139,
                     161,164..165,168..169,172)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          123..155
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          160..188
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msvymteeeq lesikkwwkq ygnlitivls lilfgiagyr ylhwhqeklt qqasiayehm
       61 mvalsnhnik avrsyaneli hehsgsvyad vahmtlakiy vsknnlnkat qelqsvasns
      121 qmlalkqiak iriariyaae ksyanalkel gsiddntylp vinelkgdiy gatgqyqeai
      181 nsyklaldev ktngmgnlfl emktneitsk shsmisgdkk vrsa
//
LOCUS       WP_003640505             128 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ribonuclease HI family protein [Lactiplantibacillus].
ACCESSION   WP_003640505
VERSION     WP_003640505.1
KEYWORDS    RefSeq.
SOURCE      Lactiplantibacillus
  ORGANISM  Lactiplantibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 128)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 128)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Lactiplantibacillus"
                     /db_xref="taxon:2767842"
     Protein         1..128
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=13931
     Region          2..125
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(6..9,39..41,44,70,107,121)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mqlytdaatt pdnqrsaagi liidqgqqhq fkqvlpdsdn htaeflaaia gfktlldsyg
       61 pqvsvffytd sqivaesvak gysktfsvel atllhlqdqc qlvitqwiae sdnhgahqla
      121 qqglhlsd
//
LOCUS       WP_003640415             137 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-hydroxyacyl-ACP dehydratase FabZ family protein
            [Lactiplantibacillus].
ACCESSION   WP_003640415
VERSION     WP_003640415.1
KEYWORDS    RefSeq.
SOURCE      Lactiplantibacillus
  ORGANISM  Lactiplantibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 137)
  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 10101294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Lactiplantibacillus"
                     /db_xref="taxon:2767842"
     Protein         1..137
                     /product="3-hydroxyacyl-ACP dehydratase FabZ family
                     protein"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=14983
     Region          7..136
                     /region_name="FabZ"
                     /note="FabZ is a 17kD beta-hydroxyacyl-acyl carrier
                     protein (ACP) dehydratase that primarily catalyzes the
                     dehydration of beta-hydroxyacyl-ACP to trans-2-acyl-ACP,
                     the third step in the elongation phase of the bacterial/
                     plastid, type II, fatty-acid...; cd01288"
                     /db_xref="CDD:238615"
ORIGIN      
        1 mevtdlipqr fplqlldriv avqpgvsata eklvtinewf fqsqtltgrt mirpvlleil
       61 aqtgvvalls mpehhgnnvf fggirqadfk tdvrpgdrle amvtltklrr qigtghgvit
      121 cagrevvsad ltfvmqa
//
LOCUS       WP_003635412             617 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Legionella longbeachae].
ACCESSION   WP_003635412
VERSION     WP_003635412.1
KEYWORDS    RefSeq.
SOURCE      Legionella longbeachae
  ORGANISM  Legionella longbeachae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 617)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 617)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 617)
  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 617)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Legionella longbeachae"
                     /db_xref="taxon:450"
     Protein         1..617
                     /product="M4 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=68798
     Region          1..520
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mnklkiysfl ssafifsmts qaaskvfidg nnmhhyltkn nhslvgknsd yqfvlsnkvt
       61 lpngvikkky slyyreipvf namltsseln nvenhwygqm midikkdipn tiptvnfkev
      121 lkiakknaal kkndpitnes aqlyvrinen nkaeliylvs fnvegynvqr pysmvnahtg
      181 eiiaswnglt trdaegpggn qktgayyygr dygflnvsdt cqmtnqdvdt ydmnnqvtgg
      241 tiyqfacpsr ktdrpvhngk aingayspln dahyfagivl dmyrkwfsln plqskfqvrv
      301 hfatnyegaf wngqqmtfgd ggaytypfta idvmahevsh gvtefnsgll ykgqsggine
      361 afsdmageta eyyvnaplgk endwlggati mknqvamryf knptldgmsi dnaknynesm
      421 dvhhtsgvfn kafytlsttp swdirkafgt fllanqmywq peatfnsaac gvakaaadlg
      481 yeindvlasf svvgvdancn iddpetgtei eisngtiinn iklvagdehr ylikvpvlnk
      541 ypfsydllsi qvtdnqnnak nsaqlyvrye dgtlkkvlft gneyinikkp aagnyhilik
      601 giaantvnlt afygnlq
//
LOCUS       WP_003641555             397 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Lactiplantibacillus plantarum].
ACCESSION   WP_003641555
VERSION     WP_003641555.1
KEYWORDS    RefSeq.
SOURCE      Lactiplantibacillus plantarum
  ORGANISM  Lactiplantibacillus plantarum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactiplantibacillus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Lactiplantibacillus plantarum"
                     /db_xref="taxon:1590"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43326
     Region          3..395
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mgktiainag sstlkfklfe mpqerviaqg averigfkts pvnirygvdh hyqekavvad
       61 hlaavnivld eliklriids ydeitgvghr vvaggeqfhd svlitdqvlk qitdlaeyap
      121 lhnpanavgi rafkrvlphv pavavfdtaf hasmpavnyl yslpydyyqr ygarkfgahg
      181 tshryvavra akllgrplet lklitlhlga gssitaidhg qsldtsmgft plagitmatr
      241 sgdvdpslva ylmkklnisd pdeiltilnt qsgllglags admqeleary dedsqaqlai
      301 difvnrivky vgaylaelqg adalvitagi gerdarmrqr iadrltyfgv aidptknqvs
      361 gverdlsttd akirtllipt deelmiardv ervaqnq
//
LOCUS       WP_003641803             395 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase
            [Lactiplantibacillus].
ACCESSION   WP_003641803
VERSION     WP_003641803.1
KEYWORDS    RefSeq.
SOURCE      Lactiplantibacillus
  ORGANISM  Lactiplantibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Lactiplantibacillus"
                     /db_xref="taxon:2767842"
     Protein         1..395
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42761
     Region          2..393
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mqktliinag ssslkwqlfa mpaetvvasg lverismpgs iftikygdhq kfettvdnld
       61 qnhaaqmlla elqrlaiids lteitavahr vvaggetfkq avevtpavle aikglsdfap
      121 lhnpmeargi etmaqalptv kqyavfdsqf ftdlpemnai yslpyeltqk yhirrygehg
      181 ishgyltgra aellakpkdd lnlvtlhlgs gaslaavkng rafdtsmgft pltgvtmgtr
      241 agdvdpavlp flmkalkidd pneimmmlnn qsgllgisgi spdmreiraq eatnpqaqla
      301 veifvnrivk yagsyltelk radalifagg igehnatlrq qiidelsifg vtldpklnea
      361 gqeglisgad skikvmlipt neelamvrqv aalqn
//
LOCUS       WP_003642331             209 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Lactiplantibacillus].
ACCESSION   WP_003642331
VERSION     WP_003642331.1
KEYWORDS    RefSeq.
SOURCE      Lactiplantibacillus
  ORGANISM  Lactiplantibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 209)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Lactiplantibacillus"
                     /db_xref="taxon:2767842"
     Protein         1..209
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=23337
     Region          84..208
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(155,158,182..185,187)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mqrkstlill tsitlvigll avgtvkvvgd ahrpsqstvt tkkvvsktka kttakstvmr
       61 tpinwrqsse tvaypnvnry pdlwihvsla kqrlylmnhh hvlytmyass gvptadrktp
      121 rgtyhvqaer gkyfysasvd egayywvswl nhgeylfhst pvdaqghfik sdaadlgkrp
      181 sshgcihlsv adskwvynni kygtkvvid
//
LOCUS       WP_003642392             219 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Lactiplantibacillus plantarum].
ACCESSION   WP_003642392
VERSION     WP_003642392.1
KEYWORDS    RefSeq.
SOURCE      Lactiplantibacillus plantarum
  ORGANISM  Lactiplantibacillus plantarum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactiplantibacillus.
REFERENCE   1  (residues 1 to 219)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Lactiplantibacillus plantarum"
                     /db_xref="taxon:1590"
     Protein         1..219
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24047
     Region          95..219
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(165,168,192..195,197)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mklttkfily ltlsfsgivl lfgirsmvrn sfafeatraq aastshsnss htksktrkss
       61 vshktaaata tpvdwhgpse snhpypnvqn ypnlridvsv akqrvylkag nkllytmlat
      121 tgkpganatp kgdfviqper glhfynasln eganywvsfk dhgvylfhsv pvdasdhyia
      181 skaallgkrs dshgcvrlsi sdakwmyehi pvntpvhiq
//
LOCUS       WP_003645437             397 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase
            [Lactiplantibacillus].
ACCESSION   WP_003645437
VERSION     WP_003645437.1
KEYWORDS    RefSeq.
SOURCE      Lactiplantibacillus
  ORGANISM  Lactiplantibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Lactiplantibacillus"
                     /db_xref="taxon:2767842"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43344
     Region          3..395
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mgktiainag sstlkfklfe mpqerviaqg averigfkts pvnirygvdh hyqekavvad
       61 hlaavnivld eliklriids ydeitgvghr vvaggeqfhd svlitdqvlk qitdlaeyap
      121 lhnpanavgi rafkrvlphv pavavfdtaf hasmpavnyl yslpydyyqr ygarkfgahg
      181 tshryvavra akllgrplet lklitlhlga gssitaidhg qsldtsmgft plagitmatr
      241 sgdvdpslva ylmkklnisd pdemltilnt qsgllglags admqeleary dedsqaqlai
      301 difvnrivky vgaylaelqg adalvitagi gerdarmrqr iadrltyfgv aidptknqvs
      361 gverdlsttd akirtllipt deelmiardv ervaqnq
//
LOCUS       WP_003644040             625 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Lactiplantibacillus
            plantarum].
ACCESSION   WP_003644040
VERSION     WP_003644040.1
KEYWORDS    RefSeq.
SOURCE      Lactiplantibacillus plantarum
  ORGANISM  Lactiplantibacillus plantarum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactiplantibacillus.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Lactiplantibacillus plantarum"
                     /db_xref="taxon:1590"
     Protein         1..625
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=71021
     Region          60..506
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 megkklrpvn qfsddvrntt iqklqnvlpe vftegemvdf dklkeiltgk ldanidkysf
       61 nwngkkrsik lsqaptvatl kpnsskskkf ddtnnlyieg dnlevlkilq ksysdkvkli
      121 yvdppyntgk dfvykdnfed sldnyleqtg qvdsegnnfs vnpetngryh tdwlnmmypr
      181 lklarnllte dgvifisvdd aeqanlkkia deifgeknfl aqviwerays pvnlkknfse
      241 shdyilvygk nasiiesngl krsddandry snpdndprgd wkssdlsvgp aiekniyeiv
      301 tpsgrkttpp sgyswrlsre rfdeyvsdnr iwfgpngdav psikrflsev kqtivpmtiw
      361 kyedvghsqs asqylkrlfd dkayfsypkp vpliqrivel ysnpdsivld ffsgsattae
      421 avmrmnvedk gnrrfimvql peqlsekdva fkdgyktipe iaeerirrag dkiveenpll
      481 adkldigfkv felsksnikk wnaepkdlng qfellannfe egsksidvvy eimlkqgldl
      541 typiseikvg aavvydiafg amfvvlgdki tsevaghimk qiadeeaens vvvlqdekfi
      601 ndseklntie qlnasgiqyn dilsi
//
LOCUS       WP_003647579             320 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Lactobacillus gasseri].
ACCESSION   WP_003647579
VERSION     WP_003647579.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus gasseri
  ORGANISM  Lactobacillus gasseri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (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   2  (residues 1 to 320)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 320)
  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   4  (residues 1 to 320)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Lactobacillus gasseri"
                     /db_xref="taxon:1596"
     Protein         1..320
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=36653
     Region          2..250
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mmieyknisk kyqdqtilkd vsftvkkgdi fvlvgpsgsg kttllkmfnr lieptkgeil
       61 lddksikeyd lrklrektgy vlqtaslfpn ltvgenitiv leqegvsrte rrkrqkellk
      121 svdldpklyc drmpnelsgg eqqrvgiira laanpevvlm depfsaldpv vrkqlqdlll
      181 nlhdelnktv ifvthdmqea irlgntigvl hegileqvgk preilrhpat kfvreffagn
      241 rinqkldlet llkselgvdp rfypkvdtlv ryhvysvqdl ikdcsnypds lfiaetefge
      301 fliepkrvwn fflkwvagnd
//
LOCUS       WP_003635994             625 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Legionella longbeachae].
ACCESSION   WP_003635994
VERSION     WP_003635994.1
KEYWORDS    RefSeq.
SOURCE      Legionella longbeachae
  ORGANISM  Legionella longbeachae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 625)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Legionella longbeachae"
                     /db_xref="taxon:450"
     Protein         1..625
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=70687
     Region          3..621
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mmdesspekt nqfslsfaal gvvfgdigts plyafsqvit ylpisdynvy gilslifwsl
       61 fiivsfkylm ivfradndge ggimalagil rqkmkktgpw llfitligig liigdgiltp
      121 aisilsaveg leplsphlak yilpvtliil vllfklqrvg tgkigvcfap imliwfvtig
      181 tlgflqiiqn pevlmavnpy yaihffilhk dfalfilggi flvmtggeal fadlghfgkk
      241 sirigwftiv lpglflcyfg qgalvlmhpe disypfysls phwflpimvi lataativas
      301 qaiisaafsi lkqtallnli prikivytsk iekgqvylpf infilatgtc alvitfrsss
      361 sladaygiav nldmllttil vgiiayrcwh wnvlkliifp liliielgfl agnsskfltg
      421 gwipiliali gilvmytwhf gfeklrelhh rdalmdtfii delnqnkisr qpgtglyiid
      481 pydydgesll hhlrlnrifs ehmvflsvki enkpyipfen kfelitkakg fylihirfgf
      541 teninlpnil delfqrvqlp feinknklmy fieivfvemt rerlkgmclw qkhlfslmir
      601 navpdiqfyr lpynrtialg tyyqf
//
LOCUS       WP_003648903             160 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Lactobacillus paragasseri].
ACCESSION   WP_003648903
VERSION     WP_003648903.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus paragasseri
  ORGANISM  Lactobacillus paragasseri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Lactobacillus paragasseri"
                     /db_xref="taxon:2107999"
     Protein         1..160
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17755
     Region          1..151
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mnaifkrrav reytsekvde ekiqklisaf qaapcalhqt evmelsvitd pellkkiedn
       61 tnnscynapl vfmintkkds qfverdasva aenvmveavd lglasvyvmg gvialnklpe
      121 iqkelgmddg yetsvllpig ypaddgkped rsnrykvvrk
//
LOCUS       WP_003643965             236 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Lactiplantibacillus].
ACCESSION   WP_003643965
VERSION     WP_003643965.1
KEYWORDS    RefSeq.
SOURCE      Lactiplantibacillus
  ORGANISM  Lactiplantibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 236)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Lactiplantibacillus"
                     /db_xref="taxon:2767842"
     Protein         1..236
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=26980
     Region          <6..222
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mepiyryfvq pqlnllnntv ygyellikql tpdgwrlpes faaissqvts dlliattkil
       61 glkvrycavn isreqlmdtt vakaiiqsqv qlypaklvve lteerspkdy pdtmliphlr
      121 gfiehgmqis lddvgtgind fksiqeilpl aselkfalqn frsdikdpki qqklhfwrai
      181 sseyglrlil egiedaeddr lsshfdinlr qgyyygkpql lrlpgdpvnf eyptmn
//
LOCUS       WP_003641011             226 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Lactobacillaceae].
ACCESSION   WP_003641011
VERSION     WP_003641011.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillaceae
  ORGANISM  Lactobacillaceae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 226)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Lactobacillaceae"
                     /db_xref="taxon:33958"
     Protein         1..226
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=26027
     Region          <3..217
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 myryfiqpql dkfnnsligy emliryretd qdrwtlpesf dnipidvqvs llkatasela
       61 lkigsvsinf nrkqflnddi aaavidaqkk lfpvhvivev teepgedtft laamqqqidk
      121 ykanglqfsi ddvgtginvy dhikpllesa eeikfamqnf raedreneip iqlkfwrdia
      181 vqhdirlile gvendaedqm andlnislrq gyyygkphlf klkadh
//
LOCUS       WP_003650795             339 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            calcoaceticus].
ACCESSION   WP_003650795
VERSION     WP_003650795.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 339)
  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 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 339)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 339)
  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   5  (residues 1 to 339)
  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   6  (residues 1 to 339)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..339
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38990
     Region          27..211
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          91..336
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msiqlywdfp rsisairill migqqhgltp escienthis lndlsqpnfe vkaeqeflvi
       61 rnllklldpt lplsieaglr hhtttfgawg failssqtmk ealhfamryf qlssifcnle
      121 viqediytll ifdhsqlpdd lacflverdl itvisiqrdv lpiqfpvmsi nialpapvya
      181 nkfpeltgyp iqfnqprsci ifesslldlp lpqadpfira ryeeecqqlw trrsslgsys
      241 qkvrnillqq psqmpridem aahlqvnlrt lqrhlaiegv tyeqliddir kdlaedllkt
      301 tnltveevai qlgysevsaf srafkrwkgi sprnfrwqk
//
LOCUS       WP_003650965             343 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            calcoaceticus].
ACCESSION   WP_003650965
VERSION     WP_003650965.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 343)
  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 343)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 343)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 343)
  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   5  (residues 1 to 343)
  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   6  (residues 1 to 343)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..343
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39249
     Region          27..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <252..339
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msikeskirs dagifpwlty ltmkdmgldt daifssvnfl ehalnipdkn vrydnriqek
       61 fwavaekvsg nkdiglvvgg rmpvlrgdlf eyvflssstf gqglntaiky yhlftsafdv
      121 lklevkgeda yliglehsir hylecaisil laylkhvsne kfkplevwlt yregadaery
      181 qeiwgcpvyf nmpegcikfn adtlndssva anktlnkihe tiieesltqi ekhelvfkie
      241 ntlqdqlksg nfkiddiakt lnitskalrt dlkeigtsye kvlneyrqkl ardllentql
      301 ksdevvyllg fsepsafsra fkywtgetps qyrkrkskki itl
//
LOCUS       WP_003652299             392 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Lactobacillus gasseri].
ACCESSION   WP_003652299
VERSION     WP_003652299.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus gasseri
  ORGANISM  Lactobacillus gasseri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Lactobacillus gasseri"
                     /db_xref="taxon:1596"
     Protein         1..392
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43306
     Region          2..392
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkkvlainsg sssfkyklfs fpdekviasg madrvgmena vfkiklsngr eyiknmpihd
       61 qeeavkllie dlkkfhvved lreitgighr ivnggeifke svrvgdkelq eifdlgelap
      121 lhnipeangi kafmnivpnv pqvavfdtsy hqtldpihyl ysipyeyyed ygirkygahg
      181 isisyvapra akmlkknpnl vnlivchlgs gasvtavkrg ksydtsmgis pltgvtmgtr
      241 sgdfdpsalq rlmhktgmni deaidvlnyk sgllgisgvs snmrdliesk dkraklarki
      301 finrvvryvg ayaaelgrid avvftagvge hdpgiragim sslrylglep dfkanrtdge
      361 kfiskpksrv kaiivptnee lmiarevvrv vq
//
LOCUS       WP_003652452             342 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            calcoaceticus].
ACCESSION   WP_003652452
VERSION     WP_003652452.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 342)
  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 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 342)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 342)
  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   5  (residues 1 to 342)
  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   6  (residues 1 to 342)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..342
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39211
     Region          28..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          98..341
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mvvqsslskg tisialvhea lsaayakgln tqiilnkagi paellmspka rvpvttyaql
       61 wielanamnd effgmdshpm rrgsyklltk lvstaetlek alydilkffn filddlqgel
      121 irdqqkaylv irdreqpkrm ftyatflmlv hglmcwlvdq riglnnislr cpkpqdiqdy
      181 fvrfgedikf naeinqvefd ahyldikikk dkkalydfle qtpqnllvrf knenalslli
      241 rrhllklhpa qwpelkdvaq qlniseatvq rrlkheglsy qqikneircd iaverlsktn
      301 dsiqdisedl sfqdpsafhr afkkwtgvsp gayreaalhs ka
//
LOCUS       WP_003649859             196 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Lactobacillus].
ACCESSION   WP_003649859
VERSION     WP_003649859.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus
  ORGANISM  Lactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Lactobacillus"
                     /db_xref="taxon:1578"
     Protein         1..196
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=22429
     Region          36..196
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mdqqvlikkl aaehngtlth nqlinnniss yninlalksg llertrsgiy qesdttedif
       61 yslqqkykrg vysletalyl wdlsdqypfs ldmtfprgyn hanldldika hyqvktlqdi
      121 gitetksfng ntikvysper tlaeilrtvn midietvtna yktwaksnkk dinalmdfae
      181 kfkvvdkans ylevll
//
LOCUS       WP_003652719             340 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            calcoaceticus].
ACCESSION   WP_003652719
VERSION     WP_003652719.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 340)
  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 340)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 340)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 340)
  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   5  (residues 1 to 340)
  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   6  (residues 1 to 340)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..340
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38732
     Region          25..208
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          86..339
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkyawafers vhsvrlmadf avesgisyqt ileetgisqq qlldpnmvvt gqqelqvihn
       61 lveqlgdrpt lgldvgtryh fttfgplgma lmssasirea ldlaltyfsl tfaftrflvs
      121 dtdegiriei edegvppsvr qftlerdaaa litvqrdlvq dnfcqymaft fqpkaevqpy
      181 idlfgilpef gaaknfvlld phkvdqklqm andlilhtae eqcrqildrr qtqkkfinlv
      241 qqqlmrvrge mpsmdmvadr lhlnartlrr hlaqegmtfi qireevrqvl aeqyltlpka
      301 sieqiaewlg yaepasfiha ykrwhgktph avrlsgksst
//
LOCUS       WP_003653792             154 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Acinetobacter calcoaceticus].
ACCESSION   WP_003653792
VERSION     WP_003653792.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..154
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=15259
     Region          2..136
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mnaqkgftli elmivvaiig ilaaiaipqy qkytarsqit aglaeispgk tqfelalseg
       61 tansvnnspa aiglksttnn csavnvtang ttgtiactlq gsatitggil tltrsadvaa
      121 asgvnanvgg wtcsitkgtt dissaiapkg ctii
//
LOCUS       WP_003653920             625 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Acinetobacter calcoaceticus].
ACCESSION   WP_003653920
VERSION     WP_003653920.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 625)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..625
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68768
     Region          19..625
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mqntakkatl patalaalgv vfgdigtspl yalkesfhaa hglgikpenv lgilsiifwc
       61 lmliisikyv aivmradnng eggimallal nlrkakiadn kkiymiaigf igaslffgdg
      121 iitpaisvls aveglsiatd vfdpfimpia itiiialflv qkhgtafvgk ffgpitmvwf
      181 lslgllglhs viqtpvvlgm fsphwaiqfi yhnpvmtffv mgavvltvtg gealyadmgh
      241 fgpipirlaw fivvlpclvl nyagqgalll rdpaaiqnpf yllvpewaly pmiimatmat
      301 viasqavisg vfslarqaiq lgylprlsik htseseegqi yvpflnwlll iaiiililif
      361 ksssnlasay glavtltmlc dtilvavfiy sawkwslpkv llliipffvl esvlvgatsl
      421 kilsggwvpl ligaiavtil mtwkrgrelt faklehdtls ldlfvksign svhwvpgdav
      481 fmtgtpnvvp hamlhnikhn kvlhqrnilv tvviedvpyv epeeristet laehffriki
      541 fygfkdemnv pkalmqayeq lgleydlmhi sffisrdriv hsvgdgmspw reklfismqr
      601 ntspvsdfyq iptnrvvelg sqiei
//
LOCUS       WP_003654203             399 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Lactobacillus gasseri].
ACCESSION   WP_003654203
VERSION     WP_003654203.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus gasseri
  ORGANISM  Lactobacillus gasseri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Lactobacillus gasseri"
                     /db_xref="taxon:1596"
     Protein         1..399
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43766
     Region          2..396
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkkvlavnsg sssfkyklfs ldnekviasg madrvglpgs vftmtladgs qhdeqsdian
       61 qeeavqklls wlkeynvids ladiagvghr vvaggeeftd stvitddnlw kiynmsdyap
      121 lhnpaeadgi yafmkvlpnv pevavfdtsf hrsldpvqyl ysvpykyyek frarkygahg
      181 tsaryvsrrt adllkkpved lkmvlchlgs gasvtaikdg ksfdtsmgfs pvagitmstr
      241 sgdvdpsllq fimkkgnits fnevikmlnt ksgllglsgi spdmrdieka ikngdkqakl
      301 tkaifinriv ryigaymtem ggldvlvfta gigehdasvr kqimdgltwl gleydekank
      361 ankegiittp kskitamivp tneelmiard vvrlakldk
//
LOCUS       WP_003652793             308 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Acinetobacter
            calcoaceticus].
ACCESSION   WP_003652793
VERSION     WP_003652793.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 308)
  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   2  (residues 1 to 308)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..308
                     /product="aminoglycoside 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=35228
     Region          17..250
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mrnlegllnr lhadrlklvt hrdgasvykg qttqgdifvk ayklkvdndr yceilnelte
       61 fslapkvldk fewenysivv msalegrpvn nilkncsrie kllllksags tlgsfhrtin
      121 ssrlfemrfw qardsaskip ilwnehlelm iskwmsrvdp lkpdyqefsh elgelvlyck
      181 alheptqfsl lhcdyigrnl latscnkisg vldfeaarig davydlakmv wvdidfsdle
      241 lrnaflqgwe itygeevpqr eflcyvgiqc laaiawtdkn apiegntifr asairalriv
      301 lnelrtgf
//
LOCUS       WP_003653774             160 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acinetobacter calcoaceticus].
ACCESSION   WP_003653774
VERSION     WP_003653774.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..160
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=17345
     Region          8..105
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mnkyyilrfn qgvtlielmv vivivaifas iaipsyqsys rratasaakg eilklaeqle
       61 rhksknftyr gftttavtlp rggytieisd dttagnlltn gaangqtwvi katttdsrnf
      121 nfiaknsglr cqsltatavd ndcggtvtcn vcetnsenwq
//
LOCUS       WP_003651365             334 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            calcoaceticus].
ACCESSION   WP_003651365
VERSION     WP_003651365.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 334)
  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   5  (residues 1 to 334)
  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   6  (residues 1 to 334)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..334
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38216
     Region          23..197
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          123..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msknssdagi flwmtyqtmq kmgldaasif asvnlpnqpp dknirrdnst qnrfwtaaee
       61 isqdpdiglh vgkqmppfrg lvieylflss stfgeglqrt iryqalltdv fslsltlned
      121 qailsgfehs vrhylecgig vflnffkyit nnefrpnhit lpyqqgasae tyhemwecpv
      181 ilgqtkgaiv fpsvllnkts paaepellki hetlaeqqll tlekhqlihl ierllsngll
      241 esrqfdqkli aeqlnrnprt lradlqaint nyekilnqhr eklarrllan tqetidqivy
      301 ltgfsepsaf trafkrwtne tpsayrqrkq kqsn
//
LOCUS       WP_003652232              84 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Acinetobacter].
ACCESSION   WP_003652232
VERSION     WP_003652232.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 84)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 84)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 84)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 84)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..84
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8851
     Region          6..84
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mqqsiqikie afgaiekllp qnlslvcpnh ilvkdvldei vslhpestqa mekcacaigd
       61 nvitrqsals epctlvllsp vagg
//
LOCUS       WP_003655272             709 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Acinetobacter
            calcoaceticus].
ACCESSION   WP_003655272
VERSION     WP_003655272.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..709
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=78327
     Region          31..705
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 msllrldrlh ycilmsmgci ssplvwaddl aqditvlptl hveatrtdtt ylqtpasvfr
       61 vdapqadtss qvnltevvkg ipslqirnre nyaqdlqlsm rgfgarstfg vrgirlyvdg
      121 ipatmpdgqg qtsnidlssl dhvevltgpf sslygnssgg tiltstkegq gkdsielsys
      181 ggshdksrag lvlqggaksa nepsyvisss yfdtdgyreh sgaekvlnna klswnlddgs
      241 kinwvtnyvk ihaddpqglt hdqwnanpkq qvpflkqfnv rkdieqtqtg atwskpindk
      301 nelyamaylg nrqvtqyqsi pkstqdasvn haggvidfer nyygadfrwt gkellpnttv
      361 svgvaldtmd edrkgfenfn lvngqpsygv kgnlrrdedn tlwnidpylq aswqflptwr
      421 ldtgvrysnv hyksedryls ngddsdktdy dkvlpsaals wqilpelmay vsyakgfetp
      481 tftemayrpd glsgfnfdlt astsdtyetg lksqnhlgdf tlavfqtktk ddivsagnsn
      541 grstfrnadk tlregvefaw nkklwrdlta tasytyldat fdadipasgs vaqipsgnai
      601 pgiaknqaya slawqplhgl yggvdvqymd kvyvndtnsd aapsysvtsa nvgyawvmgd
      661 wkvnsfarvd nlfdknyags vivndgngry fepadgrnws aglrvikqf
//
LOCUS       WP_003651467             113 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Acinetobacter].
ACCESSION   WP_003651467
VERSION     WP_003651467.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 113)
  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   3  (residues 1 to 113)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 113)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..113
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12276
     Region          2..113
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mqpqmggiiq vnipdratlq asymgyvqgg glfvpskqkv kmgqeifila tlpeqsqkip
       61 ltgkviwish kqsgfkpqgf aiqlsgdkgi yykaeaervl agsmsldrps ytm
//
LOCUS       WP_003655936             335 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            calcoaceticus].
ACCESSION   WP_003655936
VERSION     WP_003655936.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 335)
  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 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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (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   5  (residues 1 to 335)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37876
     Region          23..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          251..328
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpqtatalas wvkaiqkale kagvdsqpll kqagldvqal ndpdaryslk ntanlwklav
       61 qatqdscfgl kvanqvnqnt fhvlghslit sttlkemflr iiryfrivtd ipelefygeg
      121 knhyfvihvp devqpesida fisvfirssr alqgsvfspl rielrrsepe dlenfksilk
      181 apivfnapkd mivfdtatie qpldggnpsl tqeydeiinr ylarfdkeni larvkvklie
      241 klstgdfqqq dvakslglsi rslqrklsae ntsyselldn trhelalsyi knsshnitei
      301 ayilgftdvs sftrafrrwt dlsplhyrek hlsls
//
LOCUS       WP_003655019             134 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Acinetobacter].
ACCESSION   WP_003655019
VERSION     WP_003655019.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 134)
  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   2  (residues 1 to 134)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..134
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15274
     Region          61..133
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mqlsmnlwks kyyifivlfw slisstliqa qsfdqnfkew kakqqmydqk lstqhsshsn
       61 apksstmtds sgqvhlnqan idelqklkgi gekkaqaive yrqknggfkn idefknvkgi
      121 gpaifeknkt rlsl
//
LOCUS       WP_003657550             166 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Moraxella].
ACCESSION   WP_003657550
VERSION     WP_003657550.1
KEYWORDS    RefSeq.
SOURCE      Moraxella
  ORGANISM  Moraxella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 166)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Moraxella"
                     /db_xref="taxon:475"
     Protein         1..166
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=18350
     Region          7..165
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cl49639"
                     /db_xref="CDD:483979"
     Site            order(104..105,126,139..142,144)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mtidrrivid tqsqcltlyq gnillrqfav stakngtgql egtgctplge hvigqkiggg
       61 lppnavfvar qftgelydvq lgqnfpnrdw ilgrilwleg qingynhgvd ktgalvdtkl
      121 ryiyihgtpd tepmgrpmsh gcvrmridei vwlfdkvevg dlvliq
//
LOCUS       WP_003659766             297 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Lacticaseibacillus
            paracasei].
ACCESSION   WP_003659766
VERSION     WP_003659766.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus paracasei
  ORGANISM  Lacticaseibacillus paracasei
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 297)
  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 297)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10097223
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Lacticaseibacillus paracasei"
                     /db_xref="taxon:1597"
     Protein         1..297
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=32730
     Region          6..279
                     /region_name="TBP_aldolase_IIB"
                     /note="Tagatose-1,6-bisphosphate (TBP) aldolase and
                     related Type B Class II aldolases. TBP aldolase is a
                     tetrameric class II aldolase that catalyzes the reversible
                     condensation of dihydroxyacetone phosphate with
                     glyceraldehyde 3-phsophate to produce tagatose 1; cd00947"
                     /db_xref="CDD:238477"
     Site            order(27..29,32,53..54,56,60,64,67..68,141,232..233,
                     235..236,239,243,246)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238477"
     Site            order(81..82,177..179,181,207..208,210,229,231..232)
                     /site_type="active"
                     /db_xref="CDD:238477"
     Site            order(82,178,207)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238477"
     Site            order(177,179,181,208,210)
                     /site_type="other"
                     /note="Na+ binding site [ion binding]"
                     /db_xref="CDD:238477"
ORIGIN      
        1 mplvstkqlv ttayqnkfav gafnvgnsef vkniiavaee lespvileih pleyelmgsa
       61 ifkyireaal tatipvaihl dhgrnmadvl raiqdqansv midssglpfe enlkttkqvv
      121 evahsvgvsv eaelgsignr kftedqnmgr iytdpesakq fvtetgvddl avaigtvhgp
      181 ypsgendiri dilkqlnetl qmplvlhggs dnpdnkirea iqngiskvni ltdikvpfyh
      241 giaktvankp geyepwimms yadeaqkkvi aekirlfgsd hksklyfeda krltpyf
//
LOCUS       WP_003663337             151 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Moraxella catarrhalis].
ACCESSION   WP_003663337
VERSION     WP_003663337.1
KEYWORDS    RefSeq.
SOURCE      Moraxella catarrhalis
  ORGANISM  Moraxella catarrhalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Moraxella catarrhalis"
                     /db_xref="taxon:480"
     Protein         1..151
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=16622
     Region          1..139
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkaqqgftli elmiviliig vlamfaipqy qkhtitaqvn rvmmetsqlr tavemcllqg
       61 lktkdckadt insdlmqdnk ptvtlpnneg ntestikavf sgnaasvlhn khltwkhipk
      121 dgwkcetdvd ddfrpkgcks stttsqatpe t
//
LOCUS       WP_003665490             256 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Limosilactobacillus reuteri].
ACCESSION   WP_003665490
VERSION     WP_003665490.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus reuteri
  ORGANISM  Limosilactobacillus reuteri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
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   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   4  (residues 1 to 256)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Limosilactobacillus reuteri"
                     /db_xref="taxon:1598"
     Protein         1..256
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=29198
     Region          6..>242
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mtepiiqfkh vekrfndqtv ipdlnftvnk gefitilgss gsgktttlkm ingliapsag
       61 eilidgqklr eldlvklrrh mgyvvqqigl fphmtigqni avvpkmlhwd kekinnrvke
      121 llslvqlnpa eymnrypqql sggqqqrvgv aralatnppy vlfdepfgal daltrmelqr
      181 evkkihesla ektfmfvthd inealflgqr vmimhegriv qfatpeeivr hpatefveql
      241 lgtirqnqdl wrqqyd
//
LOCUS       WP_003667715              81 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Limosilactobacillus reuteri].
ACCESSION   WP_003667715
VERSION     WP_003667715.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus reuteri
  ORGANISM  Limosilactobacillus reuteri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 81)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 81)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 81)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 81)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Limosilactobacillus reuteri"
                     /db_xref="taxon:1598"
     Protein         1..81
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8629
     Region          3..81
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 meinvklfaf lqdqlgpsit ldvtnpirvd allkqisqra pqltstlans rvainqefvn
       61 adtinleadt eiaiippvsg g
//
LOCUS       WP_003669341             151 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: pilin [Moraxella].
ACCESSION   WP_003669341
VERSION     WP_003669341.1
KEYWORDS    RefSeq.
SOURCE      Moraxella
  ORGANISM  Moraxella
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Moraxella"
                     /db_xref="taxon:475"
     Protein         1..151
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=16071
     Region          1..137
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkaqqgftli elmiviliig vlamfaipqy qkrvvtaqvn rvmmetsqlr tavemcllqg
       61 itdstkcdtt issdlikdkp iielaqqatg tstikanfnn taanalhnqs itwshtasgg
      121 whcattvdkd lapkgctssa tpqssspqss s
//
LOCUS       WP_003665068             461 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Limosilactobacillus reuteri].
ACCESSION   WP_003665068
VERSION     WP_003665068.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus reuteri
  ORGANISM  Limosilactobacillus reuteri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 461)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Limosilactobacillus reuteri"
                     /db_xref="taxon:1598"
     Protein         1..461
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=51075
     Region          337..461
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(412..413,416,434..437,439)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mhsyikywia gigalliimi agmtvhqknh fnknvtinnv avggltakqa fgkvkgtsga
       61 tkvyvdnklv hqtksmkanf snndeqkfnq alkkqftffp shkatnlsik pdnfdqnsln
      121 iaknkltnkv qqlntgrkap vdayavyqne kvsivpavkg nkydlqnavn qlnnqagstk
      181 initlhkeqp iaansktvkn eekqlnklkg kkvaylvqne kysfttnqii tratyqngky
      241 hfdttalnkq vkkinekhat ldkpfkfrth sgaeitttan gsygwkisek kagnsltkai
      301 idgrqevdge hdiegkgynt aglgynvtsn ngigdtyaev sladqrayfy kdgkcvletd
      361 ivsgtnnegn ktpkgvwyim yqqspsvlrg qnddgssyas kvnywspftl tgcgfhdasw
      421 rhnwsktayl sdgshgcinm qpsvagqafh dlkqnepvii y
//
LOCUS       WP_003670768             471 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Moraxella catarrhalis].
ACCESSION   WP_003670768
VERSION     WP_003670768.1
KEYWORDS    RefSeq.
SOURCE      Moraxella catarrhalis
  ORGANISM  Moraxella catarrhalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
REFERENCE   1  (residues 1 to 471)
  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 471)
  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 471)
  AUTHORS   ter Beek,J., 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 471)
  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 471)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Moraxella catarrhalis"
                     /db_xref="taxon:480"
     Protein         1..471
                     /product="CmpA/NrtA family 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=52571
     Region          106..344
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 msnifrpddt dkplnfgcrc gnhrsqsecd dklsldnrfe gvsdhsrieh tntdfieava
       61 ikalfpdept rraffktvgk ttalaaiasv lpiatlqeaa aidtlkpekk svdigflpil
      121 catplimadp lgyyaeqgik anllkragwa lvrdqmmnre ldaahflapm piainlglgs
      181 akqnmkvaai qntngqalvm alkhknnrnp knwkgmtfai pfehsihnyl lryflaehgl
      241 dpdkdvklrl ttppdmianl kagnidgffg pepfnqravw dkagyihtls rdiwnghpcc
      301 sfgtsqsfin dypqtflamy raiikanvma nkpsirkdls kllspanyln qpelvlrqsi
      361 mgrfadgvdt iqdvpdrmgf dvmpwhsvaa wmmtqmkrwg yitgninyqd ianqvfmltd
      421 akkqmqamgy tvkddepkit vmgkqfnatd pdayldsfai ghkstgrlhg i
//
LOCUS       WP_003671350             256 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Limosilactobacillus reuteri].
ACCESSION   WP_003671350
VERSION     WP_003671350.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus reuteri
  ORGANISM  Limosilactobacillus reuteri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
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   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   4  (residues 1 to 256)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Limosilactobacillus reuteri"
                     /db_xref="taxon:1598"
     Protein         1..256
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=29185
     Region          6..>242
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mtepiiqfkh vekrfndqtv ipdlnftvnk gefitilgss gsgktttlkm ingliapsag
       61 eilvdgqklr eldlvklrrh mgyvvqqigl fphmtigqni avvpkmlhwd keeinnrvke
      121 llslvqlnpa eymnrypqql sggqqqrvgv aralatnppy vlfdepfgal daltrmelqr
      181 evkkihesla ektfmfvthd inealflgqr vmimhegriv qfatpeeivr hpatefveql
      241 lgtirqnqdl wrqqyd
//
LOCUS       WP_003671354             537 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Moraxella catarrhalis].
ACCESSION   WP_003671354
VERSION     WP_003671354.1
KEYWORDS    RefSeq.
SOURCE      Moraxella catarrhalis
  ORGANISM  Moraxella catarrhalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Moraxella catarrhalis"
                     /db_xref="taxon:480"
     Protein         1..537
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=61158
     Region          2..>417
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mdfdttqnif iesdnlealk ilqksyagki kmiyidppyn tgndfiyhdd fsqskkeyei
       61 atgdrninge llksfkknsk dnghyhsnwl nmmlprlhla htllsddgvi fisiddneqa
      121 qlkllcdeif ggenfvatlp rqtsaqrpsq ekyisithdy llvyaknkny dfnsvierdl
      181 snikkdsngt yiegdtspil asstqgysag gdydiefngk ifkpedsrgn rrrwlwtker
      241 mnraielgii ietrttlrvr nyidkefqvg tnilvdknpn liltsndlin pnytnhkgta
      301 clrdllleny fdfskpldli kilakllngd nsiildffag sattahavmq lntedngnrq
      361 fimvqlpelt dekseaykag fktiseiske rirragakik aenpdktldt gfkvfklsds
      421 nfkawqiddd diakqlemyi dplkdnanei diiyelllkm glkltadikf dngvywltce
      481 nksyaivlns lsqdefnaii akkpakttvl dkaflndsek sniilqfkda glnfesi
//
LOCUS       WP_003671880             398 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase
            [Limosilactobacillus].
ACCESSION   WP_003671880
VERSION     WP_003671880.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus
  ORGANISM  Limosilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Limosilactobacillus"
                     /db_xref="taxon:2742598"
     Protein         1..398
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43480
     Region          2..394
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msktiavnag sstlkfklfd mpseevvaeg tierigekmg hakikygngq kheedkpfvd
       61 haaavnylld klielkivas ydeitavghr ivaggeffkd stiidddvis kidelseyap
      121 lhepaelvgi kafrkvlpna favavfdtsf hvdmpemnal ysvpydwyek ygarkygahg
      181 tshryvsara aemlgkpvee lklitmhiga gasitavkng ksfdtsmgft pvagitmatr
      241 sgdvdpslia fmqgklnlss demidilnhk sgllgisgis pdmrdilaaa ekgddraqla
      301 ldiyvnrivr yigayiaemg gadaivftag vgensvpvrk mitdkldyfg ikidqekndc
      361 hgverdlsad dakiktllip tneelmivrd ierlkknn
//
LOCUS       WP_003675334             461 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Limosilactobacillus reuteri].
ACCESSION   WP_003675334
VERSION     WP_003675334.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus reuteri
  ORGANISM  Limosilactobacillus reuteri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Magnet,S., Arbeloa,A., Mainardi,J.L., Hugonnet,J.E., Fourgeaud,M.,
            Dubost,L., Marie,A., Delfosse,V., Mayer,C., Rice,L.B. and Arthur,M.
  TITLE     Specificity of L,D-transpeptidases from gram-positive bacteria
            producing different peptidoglycan chemotypes
  JOURNAL   J Biol Chem 282 (18), 13151-13159 (2007)
   PUBMED   17311917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13392986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Limosilactobacillus reuteri"
                     /db_xref="taxon:1598"
     Protein         1..461
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=51182
     Region          <113..>227
                     /region_name="YoaR"
                     /note="Vancomycin resistance protein YoaR (function
                     unknown), contains peptidoglycan-binding and VanW domains
                     [Defense mechanisms]; COG2720"
                     /db_xref="CDD:442033"
     Region          337..461
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(412..413,416,434..437,439)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mhsyikywia gigalliimi agmtvhqknh fnknvtinnv avggltakqa fekvkgtsga
       61 tkvyvdnklv yqtksmkanf snndeqkfnq alkkqftflp shkatnlsik pdnfdqdsln
      121 iaknkltnkv qqlntgrkap vdayavyqne kvsivpavkg nkydlqnavn qlnnqagstk
      181 initlhkeqp iaansktvkn eekqlnrlkg kkvtylvqne kysfttnqii tratyqsgky
      241 hfdttalnkq ikkinekhat ldkpfkfkth sgaeitttan gsygwkisek kagnsltkai
      301 idgrqevdgk ydiegkgynt aglgynvtsn ngigdtyaev sladqrayfy kdgkcvletd
      361 ivsgtnnegn ktpkgvwyim yqqspsvlrg qnddgssyas kvnywspftl tgcgfhdasw
      421 rhnwsktayl sdgshgcinm qpsvagqafh dlkqnepvii y
//
LOCUS       WP_003677107             397 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Loigolactobacillus coryniformis].
ACCESSION   WP_003677107
VERSION     WP_003677107.1
KEYWORDS    RefSeq.
SOURCE      Loigolactobacillus coryniformis
  ORGANISM  Loigolactobacillus coryniformis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Loigolactobacillus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Loigolactobacillus coryniformis"
                     /db_xref="taxon:1610"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42965
     Region          3..396
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mskkvmainc gssslkfkly empaetvmie gavervgkdd aifsydyqgk khqtvqpvad
       61 hdvavhlvld tllaeqiiad yseiagvghr vsnggryysd atlinadvek ridqlsvlsp
      121 lhnpvnltgi qavsaalpda kevavfdtay hhtmpvvdki ygipykyyek dgirrygfhg
      181 pshqyialkt aelfpnnsqr iischignga sitaikdgks vvnsmgftpl aglmmgtrsg
      241 dvdpqiipyl eqqegmsaqd vkdmlnkksg llglsgisnd vrdlakiagd qsderherad
      301 lalkvfahqi qfyigayaae lngvdsivft agvgehsalv rqlacqnlgy lgvkidtakn
      361 aanalsieta dsttkvlvip tdeelmiard vvrvaql
//
LOCUS       WP_003672335             372 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Limosilactobacillus reuteri].
ACCESSION   WP_003672335
VERSION     WP_003672335.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus reuteri
  ORGANISM  Limosilactobacillus reuteri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Limosilactobacillus reuteri"
                     /db_xref="taxon:1598"
     Protein         1..372
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42170
     Region          1..264
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          260..346
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrflhtadwh igktlndfsl lddqlatfkq ieaiakdqqv daiviagdly drsvpneaav
       61 kllnqmlqdl nltdhfplla isgnhdsavr lstgtdwfay qsfflntdin naftpvtikn
      121 tqffllpffg iqevrnyfnd dkiknvndam grittemekh fapdkrhvlv ahffaagskr
      181 tadsetliev gglsavttdv lapfdyvalg hlhnrnalnd ekikysgspm kfsvseakqe
      241 kgvwivdtap fkaewvplsp ahdihllkgs ftelatkpee alredfydie ltdqeripdv
      301 lnklreyypk iislhrthqa kqvqlnlskk raqespldll adfysqtmgn dltdrqkkwa
      361 ekaltqimkg ee
//
LOCUS       WP_003678747             189 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Neisseria flavescens].
ACCESSION   WP_003678747
VERSION     WP_003678747.1
KEYWORDS    RefSeq.
SOURCE      Neisseria flavescens
  ORGANISM  Neisseria flavescens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Neisseria flavescens"
                     /db_xref="taxon:484"
     Protein         1..189
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20143
     Region          <31..>166
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mtiekamrir naqfelrhle qlqpsplaqa ttgtseddvy yvtlsddiii enpnsgddtv
       61 csnvsytlpn hvknlvltgt anifaagnns hniltgnegr nrlnsgrgdd tvygmggndn
      121 lnggdgndyl dggdgndain gdagddilvg gkgkdilkge agndtyslil phstnkqtee
      181 vnqhefyvq
//
LOCUS       WP_003679478             400 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Loigolactobacillus coryniformis].
ACCESSION   WP_003679478
VERSION     WP_003679478.1
KEYWORDS    RefSeq.
SOURCE      Loigolactobacillus coryniformis
  ORGANISM  Loigolactobacillus coryniformis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Loigolactobacillus.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Loigolactobacillus coryniformis"
                     /db_xref="taxon:1610"
     Protein         1..400
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43832
     Region          3..396
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mtkviainag ssslkwklfe tpaetvvaeg mvdrvglkds vftakygpde kerfkatldi
       61 kdqtaavdml lkkltdlkiv tdiaeitgvg hrvvaggeif kestvindev iqqiddlaey
      121 aplhnpaelq gikafckllp nalsvavfdt sfhqtmpavn ylysipyeyy ekygarkyga
      181 hgtshryvat raaeilgkpl nelklitlhl gagasitaid ggksidtsmg ftplagvtma
      241 trsgdidasl vaylmqklhl sdpedmidil nnksgifgis gvspdmrdle ktrdtnprsq
      301 lgidifvnri qkyigsyvae mggidalift agigendvim rkriidglsy fgakiddern
      361 nvhgvekiis tddsklkvll vptdeelmiv rdverlrreq
//
LOCUS       WP_003679924             388 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Loigolactobacillus coryniformis].
ACCESSION   WP_003679924
VERSION     WP_003679924.1
KEYWORDS    RefSeq.
SOURCE      Loigolactobacillus coryniformis
  ORGANISM  Loigolactobacillus coryniformis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Loigolactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Loigolactobacillus coryniformis"
                     /db_xref="taxon:1610"
     Protein         1..388
                     /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=43840
     Region          1..300
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mkkrivwidi vrgiaiifvi ighglqnsgi qqfawgaflv nfifafhlpv ffvasgylyk
       61 sksikkslks gfnnlllpyl fsvaiiilgs llakhklltn ifannwvslp smfirvayaa
      121 gqsmesvvsn qhygpippvg viwflpcmfi avvlfnllmr ladryqmaef srvslillvt
      181 algilihkri fmpwtadsal isqsffyfgy ivkkyrilet lsssyyvgsi siwllsaklg
      241 mfqlssgnap dylvgivagc gsslvifkas ilifkflgak klvlflqkig qgsllimcfh
      301 sldgtgfvfl ghlmsyfstr yaswllaiil ilyrliipml alviiphvpf arnfydnrry
      361 qffwqhsikg nksnlifspn skmkhhmf
//
LOCUS       WP_003678983             294 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Neisseria flavescens].
ACCESSION   WP_003678983
VERSION     WP_003678983.1
KEYWORDS    RefSeq.
SOURCE      Neisseria flavescens
  ORGANISM  Neisseria flavescens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 294)
  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 294)
  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 294)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Neisseria flavescens"
                     /db_xref="taxon:484"
     Protein         1..294
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32137
     Region          12..82
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          213..280
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 menndkinyd tqaaktlgde lrkhrtdaki diqdvasrlk lsteqidale kgeysgfpgl
       61 vfvsgylrsy arflkideqt iakhllsitp qledhvyavt rsantglsyt dtekqgfpkw
      121 ilgiaalala vggvyfwqsk ssfeneqani qnskdvadtm ktpalktdnv avsemtedgk
      181 keitnkpeva ndqaaseasa vaqeekpavk vekdelwikv qyrsnliitd kdgkvvfsri
      241 vpagseqrlr ggapynvwig iaagseanyg gtpieplkyr vageksasfv agkn
//
LOCUS       WP_003680423             320 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Loigolactobacillus
            coryniformis].
ACCESSION   WP_003680423
VERSION     WP_003680423.1
KEYWORDS    RefSeq.
SOURCE      Loigolactobacillus coryniformis
  ORGANISM  Loigolactobacillus coryniformis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Loigolactobacillus.
REFERENCE   1  (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   2  (residues 1 to 320)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 320)
  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   4  (residues 1 to 320)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Loigolactobacillus coryniformis"
                     /db_xref="taxon:1610"
     Protein         1..320
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=35508
     Region          7..315
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mttessiefr qvskqfgeny avkqlnltiq agelfvlvga sgsgktttlk minrleevts
       61 gtiyyhgqpl nelplrqlrl qmgyvlqqia lfpnmtvgqn islipemkrm pvteiktrvk
      121 dllnevgldp atyqqrlpsd lsggeqqrvg iirafagqpk vvlmdepfsa ldpisreqlq
      181 kltlkihqrl nstivfvthd mnealqlgdr igvmqhgqlv qvgtpdeiaq kpanefvskm
      241 fasaqtndiy gvylnrlkvl gylepltaad qqlpvfdsnq tigevlpalq thgavrinde
      301 malagkltke qllafminfn
//
LOCUS       WP_003671217             277 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Moraxella catarrhalis].
ACCESSION   WP_003671217
VERSION     WP_003671217.1
KEYWORDS    RefSeq.
SOURCE      Moraxella catarrhalis
  ORGANISM  Moraxella catarrhalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
REFERENCE   1  (residues 1 to 277)
  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 277)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 277)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Moraxella catarrhalis"
                     /db_xref="taxon:480"
     Protein         1..277
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=30300
     Region          12..229
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 midtpkndnn ftdqkslnal klhgekiiya vllvlavffg wqyyqknyak idtvaadayt
       61 sisvrderlv qaylnpqlde vakqalaeee kqlfgdidal vaahgntvya wqalmikarh
      121 qtnnndldga vttlgqatsi nldddgltai akirharaml angdtngals ianeamptaf
      181 easrqellgd iyhakneidn aksaytnawe vlrerqenra vlalklqslg vnvepieptp
      241 svvsipntqp vieggeifem iehdsavadt qnphtgn
//
LOCUS       WP_003681256             199 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Limosilactobacillus fermentum].
ACCESSION   WP_003681256
VERSION     WP_003681256.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus fermentum
  ORGANISM  Limosilactobacillus fermentum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 199)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Limosilactobacillus fermentum"
                     /db_xref="taxon:1613"
     Protein         1..199
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=22010
     Region          74..197
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(143,146,170..173,175)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mrsslkrgll avaltlvvai gfanllgnhr vdtaneasss stsetssvmr tpidwqksse
       61 tvaypdvnah pdlwikvskk kqrvylidng kilytmycst gtgkndtptg tyyiqaergt
      121 yfysqqsgeg ahywvswlnh geylfhsvpt desgnyklse akqlgkkaas hgcvrlsvpd
      181 akwfyenike gtkvvitnd
//
LOCUS       WP_003676778             264 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Neisseria cinerea].
ACCESSION   WP_003676778
VERSION     WP_003676778.1
KEYWORDS    RefSeq.
SOURCE      Neisseria cinerea
  ORGANISM  Neisseria cinerea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Neisseria cinerea"
                     /db_xref="taxon:483"
     Protein         1..264
                     /product="formate/nitrite transporter family protein"
                     /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=28528
     Region          8..259
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mdtrdlyphe ilqdainksr aksnfsvkml lilsflgggy vgfgylaflk vvsgipvewg
       61 glasllgacv fpiclicili gggelatgnm mlmtvgrmtk lvsmkklarn wvlvsignla
      121 galfmayflg hyvglaegaa aaktmaiaes kvnmdfgraf vsaiacnwmv cmgiwfyfga
      181 khtsgrilam wfpvmifvli gvqhfvanmf iipagifaga ditwgqffsn mvpvflgnvv
      241 ggssfvaasy lyafkhlikd dymi
//
LOCUS       WP_003682397             377 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Limosilactobacillus fermentum].
ACCESSION   WP_003682397
VERSION     WP_003682397.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus fermentum
  ORGANISM  Limosilactobacillus fermentum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Limosilactobacillus fermentum"
                     /db_xref="taxon:1613"
     Protein         1..377
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42138
     Region          1..265
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          260..352
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrflhtadwh vgkklngfdl laeqhdaflk inqlakdykv davvvagdly drsvpseeav
       61 eelnkdliqm nlkegwplla vsgnhdsavr latggdwfka tnffmhttva qaieepvtlg
      121 dtqffllpff glqevrnyfg dpeirdlkta marivtkmee efdpdrahvl vahffaagss
      181 htdsetqtev ggldavpvdl mapfdyvalg hlhnknalqa prvkyagspl kfsasevnld
      241 kgvwivdtqp fnlqwvplep lhdlvkltgs fdelatveya shyqeddffv ieltdtapip
      301 dlmnklrhyy pkiialsrvn kaadqsdlaa paqdlenkdp lallsdfyhq vtgeelsdnq
      361 rqwakdalla aqkeeeg
//
LOCUS       WP_003682804             334 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Limosilactobacillus
            fermentum].
ACCESSION   WP_003682804
VERSION     WP_003682804.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus fermentum
  ORGANISM  Limosilactobacillus fermentum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  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 334)
  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 334)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Limosilactobacillus fermentum"
                     /db_xref="taxon:1613"
     Protein         1..334
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35242
     Region          5..75
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          212..273
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mseneervnv gkklrearek kgltlddlqq atkiqkryli aiedekfdel pgdfyvrafv
       61 kqyadtvgld gntllkdydd dlpqtktaey snhlaqavet rtgnrqptvd rvdrarrylp
      121 tviiavvvvi ilgaiwatai vrnrqdaatk idsssvsvsg esskksssss ssskssssss
      181 kaakleftaa nrttssvtls ttssltkdtd mtikasgqaw tsvtvdgtsk lsktltdnst
      241 stvslpkgaq tvvltlgnas attvkigdqt ldltdsgkya ntrtvtikfg atttasssas
      301 ststsaasss vatttnstst tattntstqs sstr
//
LOCUS       WP_003682874             398 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Limosilactobacillus fermentum].
ACCESSION   WP_003682874
VERSION     WP_003682874.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus fermentum
  ORGANISM  Limosilactobacillus fermentum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Limosilactobacillus fermentum"
                     /db_xref="taxon:1613"
     Protein         1..398
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43465
     Region          2..394
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msktiavnag sstvkfklfd mpseevvaeg nierigmdmg hakikygdgq vseeekpfpn
       61 hgtavsylld qlinlgivke yheitavghr ivaggeffkd svvidddvmq kidelaeyap
      121 lhnpaelqgi kafkrvlpda favavfdtsf hsnmpemnal ysvpyewyek ygarkygahg
      181 tshryvasra aemlgkpled lklitfhiga gasitaikng ksfdtsmgfs plagvtmatr
      241 sgdvdpslva fvqsklgiss eemiellnhk sgllglsels admrdvqaaa ehgnkqcela
      301 leiyenrvlk yigsylaelg gadaivftag vgendkefrq aigdklayfg vkvdpekndv
      361 rgeerdvsad dakikvllip tneelmivhd ierlrkqa
//
LOCUS       WP_003682536             137 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Neisseria flavescens].
ACCESSION   WP_003682536
VERSION     WP_003682536.1
KEYWORDS    RefSeq.
SOURCE      Neisseria flavescens
  ORGANISM  Neisseria flavescens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Neisseria flavescens"
                     /db_xref="taxon:484"
     Protein         1..137
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14724
     Region          5..135
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mpllyaylal iasaftsatl lpgtseaaya afvyqypqha lggclcagla nglgsmvsyy
       61 mgrmfpakkr psekvlarik rwgiwpllfa wlpiigdalp laagwlrlna lhcaiiliag
      121 kllryamiyw gmsavag
//
LOCUS       WP_003683038             255 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Limosilactobacillus
            fermentum].
ACCESSION   WP_003683038
VERSION     WP_003683038.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus fermentum
  ORGANISM  Limosilactobacillus fermentum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
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   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   4  (residues 1 to 255)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Limosilactobacillus fermentum"
                     /db_xref="taxon:1613"
     Protein         1..255
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=28630
     Region          6..255
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mnqpeiefeh vvkrfgqttv ipdlsftink gefvtvlgas gsgktttlkm inglwqptsg
       61 tvkiggkklt ehnqvdlrrh igyvvqqial fphltikqni avvpkllgwe qakidqrvde
      121 lldlvklpsd qyadrypaql sggqqqrvgl aralaanpdf ilfdeplgal daltridlqk
      181 eiknlhasla dktfffvthd inealylgqr vmvmnrgrle qfaspetivq hpaspfveel
      241 lateernqel wrrlq
//
LOCUS       WP_003684838             255 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Limosilactobacillus
            fermentum].
ACCESSION   WP_003684838
VERSION     WP_003684838.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus fermentum
  ORGANISM  Limosilactobacillus fermentum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
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   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   4  (residues 1 to 255)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Limosilactobacillus fermentum"
                     /db_xref="taxon:1613"
     Protein         1..255
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=28746
     Region          6..255
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mnqpeiefeh vvkrfgqttv ipdlsftink gefvtvlgss gsgktttlkm inglwqptsg
       61 tvkiggkelt ehnqvdlrrh igyvvqqial fphltikqni avvpkllrwe qakidqrvde
      121 lldlvklpsd qyadrypaql sggqqqrvgl aralaanpdf ilfdeplgal daltridlqk
      181 eiknlhasla dktfffvthd inealylgqr vmvmnrgrle qfaspetivq hpaspfveel
      241 lateernqel wrrlq
//
LOCUS       WP_003686904             274 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Neisseria gonorrhoeae].
ACCESSION   WP_003686904
VERSION     WP_003686904.1
KEYWORDS    RefSeq.
SOURCE      Neisseria gonorrhoeae
  ORGANISM  Neisseria gonorrhoeae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Neisseria gonorrhoeae"
                     /db_xref="taxon:485"
     Protein         1..274
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29262
     Region          161..225
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mkwlftllav lniavfggtv gyklavkaag gvpenraven tppatpaagn aaasvedtaa
       61 llkpgdilse eqaeqlrlkk eaeqkklrek kqreekarre klaaekaqae rengaadalc
      121 aaqasltmde ddyhrikgll gkwshvasrs vekrtakakp adktyrvvlp vsadaenqaa
      181 elsakgfnpi pfdgalslgv gnsrenaqal qnrladagfg gahivehfae adrqddslsv
      241 srmtvlftgv naadadeirk itslygklnl ksck
//
LOCUS       WP_003687496             406 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Liquorilactobacillus mali].
ACCESSION   WP_003687496
VERSION     WP_003687496.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus mali
  ORGANISM  Liquorilactobacillus mali
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Liquorilactobacillus mali"
                     /db_xref="taxon:1618"
     Protein         1..406
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44992
     Region          2..394
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkkvlsinsg ssslkislfa mpseqrlaki mvdysnetnq lvtitlpnhe liaqhytgki
       61 tpvelaldll kkhqiittsq eitaighriv aggelfqhst kitpeviqkl esiselaplh
      121 npaniagild aelllpncpq iavfdtsfht dlppenflya lpleyyrkyk vrkygahgts
      181 hrfvaqqaak mlklplsklk litlhlgsga svtaikngks fdtsmgfspl tglmmstrcg
      241 dvdpsalvyl lkhhafsnmd ecmkvlnqhs gllgvsevsr dmreierest rnpqaelaik
      301 mfvkricdyi gaywlelgga dalvftggig endnhvreli cerlnclgik fesiqnqyhd
      361 spfdfatads qahllviptd eelmiardty eltstkqsfs ksavny
//
LOCUS       WP_003687905             358 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Neisseria
            gonorrhoeae].
ACCESSION   WP_003687905
VERSION     WP_003687905.1
KEYWORDS    RefSeq.
SOURCE      Neisseria gonorrhoeae
  ORGANISM  Neisseria gonorrhoeae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Neisseria gonorrhoeae"
                     /db_xref="taxon:485"
     Protein         1..358
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=40097
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msitiqnlnk krfgnfhalk ninlnvpagk lvsllgpsgc gkttllriia glenadggqi
       61 lfdgqdvtak hvrerkvgfv fqhyalfrhm nvfdnvafgl tvlpkperps kgqirakvee
      121 llklvqlshl aksyphqlsg gqrqrialar alavepklll ldepfgalda kvrkelrtwl
      181 rdihhnlgvt silvthdqee alevsdeivv mnhgkieqtg saeaiyrkpe nafvteflge
      241 adafegriek giwhyngfaw kldaqykwqe qtatgyirph ewqiaaehet pmiraeieki
      301 havgalthvl vkhgkqdvhi tlagsdaary piaegkklnl ipkqvyvfsq nelieysi
//
LOCUS       WP_003688732             319 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein
            [Lactobacillaceae].
ACCESSION   WP_003688732
VERSION     WP_003688732.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillaceae
  ORGANISM  Lactobacillaceae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales.
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   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   4  (residues 1 to 319)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Lactobacillaceae"
                     /db_xref="taxon:33958"
     Protein         1..319
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=34785
     Region          4..288
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 malislehvt keydgkpvvn dlslkvdqge lfvlvgtsgs gktttlkmin rlvdptsgvi
       61 efadkpltsy kmrdlrwdlg yvlqqialfp tmtvaqniav ipemkgwsrq kirtatdell
      121 ttvdlppaey rnrmpselsg gqqqrigilr alasrpkvvl mdepfsaldp isrtqlqdml
      181 lhlhralknt vifvthdmae amklgdrigv mrggkllqvd tpekiatnpa ndfvadlfkg
      241 aqanqglqvt lsqlapfaad vsarhavggn ltlaealpll dahealhvns ehgafvvnth
      301 svvaylasaf vdqntetke
//
LOCUS       WP_003687428             137 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Neisseria].
ACCESSION   WP_003687428
VERSION     WP_003687428.1
KEYWORDS    RefSeq.
SOURCE      Neisseria
  ORGANISM  Neisseria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Neisseria"
                     /db_xref="taxon:482"
     Protein         1..137
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14942
     Region          3..137
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mipsytyaal afsaftsatl lpgtseaafa lfvrnfpkha ygallcagla nglgsmvsyw
       61 mgrllpsrkm psektlnlir rfgiwllafa wlpvvgdalp ltagwlrlnp wtsglmlvig
      121 ktaryafilw gmqyyaa
//
LOCUS       WP_003681999             209 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Neisseria flavescens].
ACCESSION   WP_003681999
VERSION     WP_003681999.1
KEYWORDS    RefSeq.
SOURCE      Neisseria flavescens
  ORGANISM  Neisseria flavescens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 209)
  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 209)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 209)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Neisseria flavescens"
                     /db_xref="taxon:484"
     Protein         1..209
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23109
     Region          1..208
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Region          91..119
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(92,95..96,99..100,102,129,132..133,136..137,
                     139..140,162,165..166,169..170,173)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          127..157
                     /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"
ORIGIN      
        1 maahleeqqe ldnfkyfwkk tgrwifalli vaalgylgyt iyqgqkaskd qeaaavlaqm
       61 vekaqqktdp kainvdlael qknypdsist aqatlmvaat efdagrydva eghlnwvlkn
      121 qnaplvqala aqrlgvvllq qkkydaaina lntqveadfe plmletkgdv yvaqnktkea
      181 vqsyeaalsk mpqtavgrel lqmkidslk
//
LOCUS       WP_003689592             214 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein, partial [Neisseria
            gonorrhoeae].
ACCESSION   WP_003689592
VERSION     WP_003689592.1
KEYWORDS    RefSeq.
SOURCE      Neisseria gonorrhoeae
  ORGANISM  Neisseria gonorrhoeae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (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   2  (residues 1 to 214)
  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 214)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Neisseria gonorrhoeae"
                     /db_xref="taxon:485"
     Protein         1..>214
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          12..66
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msarlmgmaf ktgiprgqrf vlvklcdcan deglcypsqe tlaedtgfae tavrqhikwl
       61 kdnnfiksar rqrgrerksd iyrinvalle kcyaeaakrk aarqakmwee pldyepsdfe
      121 psdyepsdfe psdyepsdfd aknhqilsge psdfalrtir fcaknhqils gepsdfdgsl
      181 yvepsvepsg snargarapa gphpakpqta ppet
//
LOCUS       WP_003691391             395 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Liquorilactobacillus mali].
ACCESSION   WP_003691391
VERSION     WP_003691391.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus mali
  ORGANISM  Liquorilactobacillus mali
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Liquorilactobacillus mali"
                     /db_xref="taxon:1618"
     Protein         1..395
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43693
     Region          1..392
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkilavnags stlkwklfnm psakviakgq ierigldgai ettefaekki teqiqsdnhq
       61 eavtrllell reyhiveqld eikgvghrfv nggtvfsksv vvndevlakm eklkvlaplh
      121 npanimaira fkevlpeals vavfdtgfhh tmpeenviys ipyeyykkyh vqkfgahgis
      181 yrfvfnrlle ltskkkaktn tilmhlgsga sicavkdgrs idtsmgfspv sgitmqtrsg
      241 dvdpslliyl enqlgvsstr vldilnkesg ilgisgispd mrevfaqket nhradlavki
      301 finrivkyig syaaelgrvd slvftggige nvpfirrmvc aqlgifgvkl neecnenaia
      361 veqkissids avevwtiptn eelmiaedvy nlenn
//
LOCUS       WP_003692529             278 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Neisseria gonorrhoeae].
ACCESSION   WP_003692529
VERSION     WP_003692529.1
KEYWORDS    RefSeq.
SOURCE      Neisseria gonorrhoeae
  ORGANISM  Neisseria gonorrhoeae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Neisseria gonorrhoeae"
                     /db_xref="taxon:485"
     Protein         1..278
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29981
     Region          2..275
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 midlhchstv sdgmlppaev vrlahqngct llaltdhdht ggisearaea drlglrling
       61 veisvtwrgr tihvvgldfd eqdenlqnll advrkgrlkr leaiaaklek kgiggaydga
      121 lalaankemv srthvaefli knghvknkrq aftkylgdgk scavrhewat ladcvsavng
      181 aggmaviahp mrydlsatak rnlfeefknl ggagievhsg ncckndrlny alladrfgll
      241 asagsdfhrl ddfsggilga cpdlpenckp vrahfsrh
//
LOCUS       WP_003683308             133 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Limosilactobacillus fermentum].
ACCESSION   WP_003683308
VERSION     WP_003683308.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus fermentum
  ORGANISM  Limosilactobacillus fermentum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 133)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 133)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 133)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Limosilactobacillus fermentum"
                     /db_xref="taxon:1613"
     Protein         1..133
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=14421
     Region          2..126
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(7..10,40..42,45,71,108,122)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 miklysdaat kgnpgptglg wlivaggkqr qqsatlnrad nhhgefaaat aafddllany
       61 ghdqvvmfyt dsrlladaig kgyakhyqpe ldqllerida lptvvtqwvs esqnhgahsl
      121 anqalqrllk teh
//
LOCUS       WP_003686939             685 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Liquorilactobacillus mali].
ACCESSION   WP_003686939
VERSION     WP_003686939.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus mali
  ORGANISM  Liquorilactobacillus mali
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 685)
  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   3  (residues 1 to 685)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Liquorilactobacillus mali"
                     /db_xref="taxon:1618"
     Protein         1..685
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76657
     Region          1..677
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          173..252
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 mddnsvyrnl ffeesddnlq klnddvlele sepenidlin eifraahtlk gmsatmgynv
       61 mtklthkmen lfdffksgkl kvtseyisli fecldklsel vedlrndqel sedqisellk
      121 klinveesvn gtatekvqnt sdktgkltti lesnedadid vvkkakaqgy nafvvairid
      181 resmlkgpra fliiehleqe gdviytepta dllengefnt dfkliyltkn tkeqveanid
      241 inseidtfiv eefdsaksan snehkplaes vsakptestp kkpkssdkke kksstpskhp
      301 saarnqsirv dltrldlfln lvselvvyrn qlddankrsd amevkdsleq vsrltselqd
      361 lvlkirmqqv svvfsrfprm vrdlakeldk dmelivegee teldktvvse lseplihllr
      421 nsadhgiesa enrkkfgkpe kgtiklsayq egnqvnitle ddgmgidpqv mkesaeskgi
      481 dttgmtddel inlifhpgfs takkitnisg rgvgldavma kindlggsle mktelhvgtk
      541 fviklpltls iiqalmvrva nesfaipldv vervvviqek eiitsmdrev veyqeglipv
      601 irvdkvlglt neentkqfai vvksdkqyfa vlvneligqq eivikkidti iqklnkfqga
      661 tifgngsial ildvnaicqg klven
//
LOCUS       WP_003692205             654 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Ligilactobacillus ruminis].
ACCESSION   WP_003692205
VERSION     WP_003692205.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus ruminis
  ORGANISM  Ligilactobacillus ruminis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 654)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..654
                     /organism="Ligilactobacillus ruminis"
                     /db_xref="taxon:1623"
     Protein         1..654
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=75017
     Region          41..96
                     /region_name="TypeIII_RM_meth"
                     /note="Type III restriction/modification enzyme
                     methylation subunit; pfam12564"
                     /db_xref="CDD:432638"
     Region          177..644
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 maiesrimeh vrsvlerfdn kyiengilkk akviedldny drdlmsalld drlihdtyte
       61 kisdveifkv nqfiemfefk nywedsytry snkigltsgg kfidestdvv ldfpfkdtvl
      121 kagmskedve dagdaneqfl nevlakseid elfepkvfkn vrkydrsggg eqsslsdddn
      181 lvikgnnlia lhsikrryag kvkmiyidpp yntgsdsfey ndhfkrstwl tfmknrleia
      241 rellskdgli fvnidssrsn cksikgttme pylhilmdni fgesnyigtl dwkkkkqpsf
      301 lsriasvldh iivfakdekn idklsisttt dntkridnqs npkserlvka gvkymgkend
      361 lvikageyts rsmsvtydrd vvikngrtvs dvvitanwrt nqsnidqycn ddllyinssk
      421 tlrrfvtdee askgktmtdl lldsgqnqdg tnelialfgk kvfdtpkpek llchlikags
      481 nkgnivldff mgsattqava mkmgrrfigi eqmdyietis vprlqkvieg eqggiskdvg
      541 wqgggsfvya elmeknqgyl hdlqkatnvk elmrvydrmk enadldfrld lekfeeelpk
      601 lgsveerrre lvrildknql yynyanidda dvrdlitdsd yqfnksfynd kdge
//
LOCUS       WP_003693216             375 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Ligilactobacillus ruminis].
ACCESSION   WP_003693216
VERSION     WP_003693216.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus ruminis
  ORGANISM  Ligilactobacillus ruminis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Ligilactobacillus ruminis"
                     /db_xref="taxon:1623"
     Protein         1..375
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42421
     Region          1..250
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          259..346
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkflhtadwh vgrklhgydl steqadalrk lekiaidekv daiviagdiy drgmpsedsv
       61 rmvngalkkl nledgfplla isgnhdsaer lstgsewfea tsfylhtkle raaepiemsg
      121 vqfflmpyfe isaaknflgd etlktadqcv rrivslmker fkdgfkhvlv ghffavgslk
      181 sdsetpsevg gleavgidel ecfdyvalgh lhqhraskse kvkysgsllk ysvsetsdqk
      241 gvyvvdtdse iiaykplepl ndvrvvkglf enlikpenyr qipdddyvav eledrvpiid
      301 vmnrlkkyyp riielkrvng rvnhenngvk nleklsemdl fktfykdtvg edpdeeqckm
      361 meqalqdvrn ggenq
//
LOCUS       WP_003694588             401 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Ligilactobacillus ruminis].
ACCESSION   WP_003694588
VERSION     WP_003694588.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus ruminis
  ORGANISM  Ligilactobacillus ruminis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Ligilactobacillus ruminis"
                     /db_xref="taxon:1623"
     Protein         1..401
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43771
     Region          2..394
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mdkvlavnsg ssslkfklfe mpseaviasg lieriaipgs qttikygngk vykhqgtvkn
       61 hgeavnnlme llislgiiek yseitgvghr vvaggeyfsk svvvtdevir kiknitelap
      121 lhnpanligi qafkemlpda csvvvfdtaf hqtmpeenfl ysvpyewyek lgvrrygahg
      181 tshryvagea aklmgrplkd lklvtchlga gsslcaikng ksfdtsmgft pltgvtmatr
      241 sgdvdvsmia fvmdklgins isemiytlnk esglagisgv ssdmrdilsv shakhrarla
      301 idifvkdivk yigqyyfemg gidgivftag igensavirk mimerlsfmn itidneknee
      361 qdgatvisge dsaitmmkip tneelmiard vmelknkknk c
//
LOCUS       WP_003694690             175 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Neisseria gonorrhoeae].
ACCESSION   WP_003694690
VERSION     WP_003694690.1
KEYWORDS    RefSeq.
SOURCE      Neisseria gonorrhoeae
  ORGANISM  Neisseria gonorrhoeae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 175)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Neisseria gonorrhoeae"
                     /db_xref="taxon:485"
     Protein         1..175
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=19031
     Region          15..170
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 myanmgdmmh alhfsasdka alyrevlpqi esvvadeadw vanlantaav lkeafgwlwv
       61 gfyfvdtrsd elvlapfqgp lactripfgr gvcgqawakg etvvvkdvna hpdhiacssl
      121 srseivvplf sdgrcigvld adsehlaqfd eadalylgel akilerrfea srqaa
//
LOCUS       WP_003693678             129 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Neisseria gonorrhoeae].
ACCESSION   WP_003693678
VERSION     WP_003693678.1
KEYWORDS    RefSeq.
SOURCE      Neisseria gonorrhoeae
  ORGANISM  Neisseria gonorrhoeae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Neisseria gonorrhoeae"
                     /db_xref="taxon:485"
     Protein         1..129
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14216
     Region          1..122
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mknvqkgftl lelmiavail giltliayps yktyirrarl sevkstllvn aqnleryyrq
       61 kgtfktydtn klkqnkyfni tlskvspdhf tlqaapdtat negetctvtl ndggiiaasg
      121 tnqscpgfd
//
LOCUS       WP_003695153             244 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Ligilactobacillus ruminis].
ACCESSION   WP_003695153
VERSION     WP_003695153.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus ruminis
  ORGANISM  Ligilactobacillus ruminis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 244)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Ligilactobacillus ruminis"
                     /db_xref="taxon:1623"
     Protein         1..244
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=28428
     Region          94..228
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(182..183,195,198,204..205,207)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkkkniiywa valvlvlvta ystvhvhnar qvndvkmqse srkqaeedaq qkrfladqkk
       61 rlikpaswdk ptlsggypdi skyahakkke eriwievnlr kqrvyirrgp ytlytmyasv
      121 gknyrktkny qctpighfki ekrrgvsyyd ptrgygaryw tafkdeglyr fesvpfdeng
      181 kvikaeaekl gqkvtkkhni kaygsirlsv pdaqwieeni paktlvvids qddkrdawey
      241 lkvd
//
LOCUS       WP_003694423             152 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Ligilactobacillus].
ACCESSION   WP_003694423
VERSION     WP_003694423.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus
  ORGANISM  Ligilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Ligilactobacillus"
                     /db_xref="taxon:2767887"
     Protein         1..152
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16659
     Region          5..151
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mtdnllskql dallfnehnp vsnlanasal lysslkdinw agfylydeqt dsldlgpfqg
       61 kvacmhikng tgvcgtafsq rkalrvanvh efpghiacds asnseivipl ikdnqmigvl
      121 didspsknrf skedekalse fvevllkntk ws
//
LOCUS       WP_003695159             244 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Ligilactobacillus ruminis].
ACCESSION   WP_003695159
VERSION     WP_003695159.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus ruminis
  ORGANISM  Ligilactobacillus ruminis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 244)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Ligilactobacillus ruminis"
                     /db_xref="taxon:1623"
     Protein         1..244
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=27470
     Region          112..241
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(186,188,191,215..218,220)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mnnkqlpkhg knsnrnffaf lalvlvigaa giayvqhldd anrqkleska sskkkstsss
       61 hqnlfvkkks sstskiksss tteksvmrtp idwqkssetv dypdlnkven lwievrlrsn
      121 rtllkdgdkt iytmyssgge yhdvdgkqvs ytptgtyyie nergesffnn slnegaryyi
      181 swlnhgeylf htvptnaqge ydveeckklg kqpashgcir lsvpdaiwly nnlpvgtkvv
      241 indk
//
LOCUS       WP_003696929             390 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Ligilactobacillus ruminis].
ACCESSION   WP_003696929
VERSION     WP_003696929.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus ruminis
  ORGANISM  Ligilactobacillus ruminis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Ligilactobacillus ruminis"
                     /db_xref="taxon:1623"
     Protein         1..390
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43146
     Region          2..384
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msnillmnag sssvkwklfe letekvvakg lvermlmpgs kfeikygeqn fqetydnlty
       61 eraceliiek iqekgitsle kiacvghrvv aggekfrgat kidaekleei iemsdhaplh
      121 npmeakyiel mqrvmpdtpq yavfdstfft dmpemnaifs lpyeltkkyg irrygehgis
      181 hgyishrcae llekpledlk litlhlgsgs sisavkdgka ydssmgftpl tgvtmgtrcg
      241 dvdpsivpfl mkkldksaee ilqlfnsesg llgisgkspd mrdiranidd srcalareif
      301 inrivkyvgs yyvemggadv lvfaggigen dpslrrdvvs elaclgisld ealneknaeg
      361 listkdskak vmivptneel amvqaikekl
//
LOCUS       WP_003697385             451 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Ligilactobacillus ruminis].
ACCESSION   WP_003697385
VERSION     WP_003697385.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus ruminis
  ORGANISM  Ligilactobacillus ruminis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Ligilactobacillus ruminis"
                     /db_xref="taxon:1623"
     Protein         1..451
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=51592
     Region          1..441
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 miyidppynt gsdsfeyndh fkrstwltfm knrleiarel lskdglifvn idssrsncks
       61 ikgttmepyl hilmdnifge snyigtldwk kkkqpsflsr iasvldhiiv fakdeknidk
      121 lsistttdnt kridnqsnpk serlvkagvk ymgkendlvi kageytsrsm svtydrdvvi
      181 kngrtvsdvv itanwrtnqs nidqycnddl lyinssktlr rfvtdeeask gktmtdllld
      241 sgqnqdgtne lialfgkkvf dtpkpekllc hlikagsnkg nivldffmgs attqavamkm
      301 grrfigieqm dyietisvpr lqkviegeqg giskdvgwqg ggsfvyaelm eknqgylhdl
      361 qkatnvkelm rvydrmkena dldfrldlek feeelpklgs veerrrelvr ildknqlyyn
      421 yaniddadvr dlitdsdyqf nksfyndkdg e
//
LOCUS       WP_003701615             129 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Neisseria gonorrhoeae].
ACCESSION   WP_003701615
VERSION     WP_003701615.1
KEYWORDS    RefSeq.
SOURCE      Neisseria gonorrhoeae
  ORGANISM  Neisseria gonorrhoeae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Neisseria gonorrhoeae"
                     /db_xref="taxon:485"
     Protein         1..129
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14255
     Region          1..122
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mknvqkgftl lelmiavail giltliayps yktyirrarl sevkstllvn aqnleryyrq
       61 kgtfqtyekn klkqnkyfni tlskvspdhf tlqaapdtat negetcvvtl ndggiiaasg
      121 tnqscpgfd
//
LOCUS       WP_003701642             197 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein, partial [Neisseria
            gonorrhoeae].
ACCESSION   WP_003701642
VERSION     WP_003701642.1
KEYWORDS    RefSeq.
SOURCE      Neisseria gonorrhoeae
  ORGANISM  Neisseria gonorrhoeae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 197)
  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 197)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Neisseria gonorrhoeae"
                     /db_xref="taxon:485"
     Protein         1..>197
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          12..66
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msarlmgmaf ktgiprgqrf vlvklcdcan deglcypsqe tlaedtgfae tavrqhikwl
       61 kdnnfiksar rqrgrerksd iyrinvalle kcyaeaakrk aarqakmwee pldyepsdfe
      121 psdyepsdfe psdyepsdfd aknhqilsde psdfalrtvr fcaknhqils gepsdfdgsl
      181 yvepsvepsv epsveps
//
LOCUS       WP_003691837             681 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Ligilactobacillus ruminis].
ACCESSION   WP_003691837
VERSION     WP_003691837.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus ruminis
  ORGANISM  Ligilactobacillus ruminis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 681)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 681)
  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   3  (residues 1 to 681)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..681
                     /organism="Ligilactobacillus ruminis"
                     /db_xref="taxon:1623"
     Protein         1..681
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76262
     Region          3..681
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          175..254
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 maddnsvyrd lffeesddnl qtlndsilel eqepdnidli nsifrvahtl kgmsatmgyd
       61 vmtklthkme dmfdlfktgk mkintdhisl vfkcldklqe lvddlrddke leesqitdlw
      121 neldrvessa gageaeapap veehdegals tkferyddad tdvvndakag gmnaytiair
      181 ldkdtmlkgp rvflitehle kdgeiirtep sadlledgdf dtdfrmiylt kdsvddvkni
      241 iesnteidsy iveefkepaa eeekaeekte teekkteekp aeekkpaekk paaktqapah
      301 kaknqairvd ltrldrflnl vseivvyrnq ledatnresi geirdsleqv srltselqdl
      361 vlkirmqqvs vvfsrfprmv rdlsnqlnke mkleiigeet eldktvvsel seplihllrn
      421 sadhgiedpe trkklgkpev gtitlaayqe gnkvlitlsd dgkglkpdvi kasaekkgid
      481 ttgmtdrelq mlvfhpgfst akkitnisgr gvgldavqak iaelggsiem dskvdvgttf
      541 iiklpltlsi iqalmvqigk esfaipldvv ervvmvrekd imqtsnqevc kfqeglipii
      601 rtdkllqvps sssdkkyaii vkigkqyygv lvdkmvgqqe ivikkidpml qkikkyqgat
      661 ilgngsiali ldvnaicnsr q
//
LOCUS       WP_003702049             463 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Ligilactobacillus salivarius].
ACCESSION   WP_003702049
VERSION     WP_003702049.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus salivarius
  ORGANISM  Ligilactobacillus salivarius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 463)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Ligilactobacillus salivarius"
                     /db_xref="taxon:1624"
     Protein         1..463
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=51200
     Region          204..309
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          338..462
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(413..414,417,435..438,440)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mifinkgtkw laaglgavvl icggsffyqk qhfnrniein gvkvggmsva eatqklkttk
       61 lnnnvylgek llvkgsdptn stnavsqekv qeifdkqfsl fpssrsydyq akgdsdysyr
      121 knelraavks elerlnvsrt apkdayaelk ngsvhvinak kgnqydvnki mqeydkqfsd
      181 nqiklttvyt qpisadskqv qadkaklekl adqkvnytvq nktytlaakd vinsakivdg
      241 kyeydaanlk kkiddindsq stldknlkfk ttggseitld kgtygwalsp ikatrsitta
      301 fekgdsnlna ksdiygegyt englgyntts nsgignsyve vsisqqhvwv ykngtqvasl
      361 svvtgtndgn yntptglyyi mykqtnttlr gknadnsaya spvsrwapft ldgcgfhdad
      421 wrknwsstay ltdgshgcvn vrpaqisqiy dnveqyepvv iys
//
LOCUS       WP_003703620             398 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Ligilactobacillus salivarius].
ACCESSION   WP_003703620
VERSION     WP_003703620.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus salivarius
  ORGANISM  Ligilactobacillus salivarius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Ligilactobacillus salivarius"
                     /db_xref="taxon:1624"
     Protein         1..398
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43789
     Region          3..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mrkiivinsg ssslkfklfe spsknvlasg lierigldds iitikygdkk khrevqaikd
       61 htvavdlllq llkkldivtd lneisavghr vvaggeyfkk svpvdgnvik kiediielap
      121 lhnpanlvgi kvfkkllpna lsvvafdtaf hqtlpeenfm ystpydwyke ygvrrygahg
      181 ishryvslra aelmgkpved lklvtchlga gasitavkng ksfdtsmgft pltgiqmatr
      241 sgdvdvslva ymmkklkvks vseilymlnk esgflgvsgv sldmrdveaa aaknnkrael
      301 aiklfyndiv kyigqyymem egidgivfta gigenspetr eaimnklsfl gvtinkdens
      361 krgtegivsg kdssitvmri ptdeeymicc dvealmnk
//
LOCUS       WP_003694565              81 aa            linear   BCT 20-JAN-2025
DEFINITION  acyl carrier protein [Ligilactobacillus ruminis].
ACCESSION   WP_003694565
VERSION     WP_003694565.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus ruminis
  ORGANISM  Ligilactobacillus ruminis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
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   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 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   4  (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 10011594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Ligilactobacillus ruminis"
                     /db_xref="taxon:1623"
     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=9000
     Region          3..77
                     /region_name="acpP"
                     /note="acyl carrier protein; Provisional; PRK00982"
                     /db_xref="CDD:179197"
ORIGIN      
        1 mtkeevlakv qeiaaeqldv dkeeivltan ikddldadsl dvfeimnele dsfdiqldad
       61 esiqtigdvv dyvqkqldak d
//
LOCUS       WP_003704057             246 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Ligilactobacillus salivarius].
ACCESSION   WP_003704057
VERSION     WP_003704057.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus salivarius
  ORGANISM  Ligilactobacillus salivarius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 246)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Ligilactobacillus salivarius"
                     /db_xref="taxon:1624"
     Protein         1..246
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=27940
     Region          93..230
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkknnliywi vaiilvgiag wsavhmhhle sknavkvsre mkisssisrh ikkitkeqkk
       61 amrkkvdwnk psmtkaypdv skyknvkksn rirlvvssak qrvyvmsgpy vlytmytslg
      121 knynsktpny qvtpvgkfkl eetrgdkfyd atrqlgglhw tsfkgkgmyh fqsvpvdeng
      181 kviekdakhl gntkitkknn ikaygsiwlt vpdaewiqkn lpvgtkvliy gedassdnfi
      241 adnakh
//
LOCUS       WP_003705680             463 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Ligilactobacillus salivarius].
ACCESSION   WP_003705680
VERSION     WP_003705680.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus salivarius
  ORGANISM  Ligilactobacillus salivarius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 463)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Ligilactobacillus salivarius"
                     /db_xref="taxon:1624"
     Protein         1..463
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=51249
     Region          204..309
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          338..462
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(413..414,417,435..438,440)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mifikkgtkw laaglgavil icggsffyqk qhfnrniein gvkvggmsva katqklkttk
       61 lnnnvylgek llvkgsdptn stnavsqekv qeifnkqfsl fpsgrsydyq akgdsdysyr
      121 knelraavks elerlnvsrt apkdayaelk ngsvhvinak kgnqydvnki mqeydkqfsd
      181 nqiklttayt qpisadskqv qadkaklekl adqkvnytvq nktytlaakd vinsakivdg
      241 kyeynaanlk kkiddindsq stldknlkfk ttggseitld kgtygwalsp ikatrsitta
      301 fekgdsnlna ksdiygegyt englgyntts nsgignsyve vsisqqhvwv ykngtqvasl
      361 nvvtgtndgn yntptglyyi mykqtnttlr gknadnsaya spvsrwapft ldgcgfhdan
      421 wrknwsstay lndgshgcvn vrpsqinqiy dnveqyepvv iys
//
LOCUS       WP_003706470             149 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Ligilactobacillus salivarius].
ACCESSION   WP_003706470
VERSION     WP_003706470.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus salivarius
  ORGANISM  Ligilactobacillus salivarius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 149)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Ligilactobacillus salivarius"
                     /db_xref="taxon:1624"
     Protein         1..149
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16249
     Region          5..149
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mtnsllsqql dalltnetnf ianlsnasal lyqslsdinw agfylydetn delhlgpfqg
       61 kvacmhikng sgvcgtalqq qkvlrvdnvh efaghiacds asnseivvpl ikddkiigvl
      121 didspslsrf sledevelve fsktllkhi
//
LOCUS       WP_003704681             309 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Ligilactobacillus
            salivarius].
ACCESSION   WP_003704681
VERSION     WP_003704681.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus salivarius
  ORGANISM  Ligilactobacillus salivarius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
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   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 309)
  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 309)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Ligilactobacillus salivarius"
                     /db_xref="taxon:1624"
     Protein         1..309
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33524
     Region          1..69
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          226..291
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mtdigktlqn arnekhytld dlqqitkiqk ryliaieenn fdalpgdfyv rafirqyadt
       61 vgikadklls eldeqagkkk veeteeepte aktrteavrr qqqsstpsqv sqsfdkfmhy
      121 lptiiivgvv viiigsiyfv vagnkkeanq aasstnvsis sdvssskkss kkessseevs
      181 sssskkesss ssessskssk gqkitntavs gsrftyslts pakknkikft skggsawssi
      241 svngtanwqg tlqngashtv tlpegttsfn islgnsnvtn itingkkfdf lkenstltvr
      301 qitvnvane
//
LOCUS       WP_003709293             147 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Neisseria lactamica].
ACCESSION   WP_003709293
VERSION     WP_003709293.1
KEYWORDS    RefSeq.
SOURCE      Neisseria lactamica
  ORGANISM  Neisseria lactamica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Neisseria lactamica"
                     /db_xref="taxon:486"
     Protein         1..147
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=15290
     Region          1..146
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkaiqkgftl ielmiviaiv gilaavalpa yqdytaraqm sealtlaegq kaavveyysd
       61 ngtfpttnas agianastik gkyvqkvevn gdatsatits tmnasgvnkd isgktlllvg
      121 kqnsgsfewt ckagtvdtkf lpsscrk
//
LOCUS       WP_003706738             410 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Ligilactobacillus salivarius].
ACCESSION   WP_003706738
VERSION     WP_003706738.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus salivarius
  ORGANISM  Ligilactobacillus salivarius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Ligilactobacillus salivarius"
                     /db_xref="taxon:1624"
     Protein         1..410
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=46601
     Region          69..408
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mkelelrvaa vllnqpnlle anyvdpnwfe nfnircvida lctldpners llnvfnevqn
       61 ksaikysdli klqgmsitsa nlssdlksih kayaernlel gmqayqnskt kqeldnlsna
      121 iteltrvdee edtgeldeai eelkvrlttn qpvgiksypk ldellaggly gsmlftigar
      181 psvgktayav nlayqilerd pevqvdfftl emnkremlnr fisrqakvss mrlknpsnel
      241 tlaitrlisd ginwvrnhkl riydrilnls givnvirkna akskpnkyva ivdyiglvkv
      301 nsrqdrwiqv gqitrelkil aneynipiva laqlnrgves rqvkepmlsd lresgsieqd
      361 snvvaflyrp deddrsvvkl sikknregql gdisyyfegq ymlfkevdae
//
LOCUS       WP_003710616             149 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Neisseria lactamica].
ACCESSION   WP_003710616
VERSION     WP_003710616.1
KEYWORDS    RefSeq.
SOURCE      Neisseria lactamica
  ORGANISM  Neisseria lactamica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Neisseria lactamica"
                     /db_xref="taxon:486"
     Protein         1..149
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=16706
     Region          1..103
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mtdnrgftlv elisvvlils vlalivypsy rnyvekakin avraallena hfmekfylqn
       61 grfkqtstkw pslpikeaeg fcirlngiar galdskfmlk avaidkdknp fiikmnensv
      121 tfickksass cddgldyfkg ndkdckllk
//
LOCUS       WP_003712538             137 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Neisseria lactamica].
ACCESSION   WP_003712538
VERSION     WP_003712538.1
KEYWORDS    RefSeq.
SOURCE      Neisseria lactamica
  ORGANISM  Neisseria lactamica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Neisseria lactamica"
                     /db_xref="taxon:486"
     Protein         1..137
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15027
     Region          3..137
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mipsytyaal afsaftsatl lpgtseaafv lfvrrfpeha ygallcagla nglgsmvsyw
       61 mgrllpsrkm psektlnlmr rfgiwllpfa wlpvvgdalp laagwlrlnp wtsglmlvig
      121 ktaryafilw gmqyyaa
//
LOCUS       WP_003713175             102 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Limosilactobacillus oris].
ACCESSION   WP_003713175
VERSION     WP_003713175.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus oris
  ORGANISM  Limosilactobacillus oris
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Limosilactobacillus oris"
                     /db_xref="taxon:1632"
     Protein         1..102
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11467
     Region          3..101
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(8..9,27..28,36,39,41..42,44,47..48,50,58,63,70)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(27,58..59,61,82)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 makmdeqfiq dvlntvdlip fgrvasygqi aqiicrprna rlvgkilgky ggrgkhpchr
       61 vvtasgrlvp gwfdqrpmll aegvpfkden hvdirrcrwr gi
//
LOCUS       WP_003712855             537 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Neisseria lactamica].
ACCESSION   WP_003712855
VERSION     WP_003712855.1
KEYWORDS    RefSeq.
SOURCE      Neisseria lactamica
  ORGANISM  Neisseria lactamica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Neisseria lactamica"
                     /db_xref="taxon:486"
     Protein         1..537
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=60723
     Region          1..>412
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mfieaenlea lkilqksyag svkmiyidpp yntgndsfiy pdkfsesree yarrvgdtdd
       61 agylkrdgvf qgawrkngkd sghyhsnwls mmlprlhlak tllredgvif isiddneqaq
      121 lkllcdevfg aenfvsniiw ekrytrsnna rmfttlteqi vcyrksdnlq elkeprneka
      181 dstytnpdnd prgvwtsvsc vnpatkeqrp nlsyeiqnph tgevikhptn awkfehskyl
      241 syqednrlyw gkngenkypr lkkfltemdg gmvpvdlwkh detgttdaas kelesmigkg
      301 iftfpkppsl ikrmlkiasn kkdsiildff sgsgttahav mqlnaedggs rrficvqlpe
      361 etdekseark agfdtiaeia kerirragrq isdglqsgqn vdtgfkvfkl aesgfkqwrq
      421 sgqadtealq relslnidsv lsetpsenll celmlrlglk ltckvslsdg vyfvededtg
      481 glyafllerv nqdlidavla khpvkavvld rlfegddalk gntvlqmkda gvmfecv
//
LOCUS       WP_003709710             371 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Ligilactobacillus salivarius].
ACCESSION   WP_003709710
VERSION     WP_003709710.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus salivarius
  ORGANISM  Ligilactobacillus salivarius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Ligilactobacillus salivarius"
                     /db_xref="taxon:1624"
     Protein         1..371
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42531
     Region          1..263
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          259..349
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkflhtadwh igkklhnfdl nyeeddafkq ieriaeeekv daiiiagdly drslpseeav
       61 ksvneklkrl nlvdkypllv isgnhdsatr lntgsewfka tnlflntkis gafepveied
      121 tqffllpyfe pqevrnyfdr qnlknvqeam qlivekikek fkpnmkhvlv ahffaagstq
      181 tdsetnvmvg gldaiptsyl ndfdyvalgh lhdarasqae tikysgspvk fsvseatsqk
      241 gvwivdteki apkfvplvpv heinvledsf dnlispsvye kyskedyyai rltdtkvipd
      301 vinklrnyyp kilelrrvge iqelkveenk erdltdpmkl vsdfftevtg ekltsnqqkw
      361 venalkdvnk k
//
LOCUS       WP_003714364             398 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Limosilactobacillus oris].
ACCESSION   WP_003714364
VERSION     WP_003714364.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus oris
  ORGANISM  Limosilactobacillus oris
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Limosilactobacillus oris"
                     /db_xref="taxon:1632"
     Protein         1..398
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43196
     Region          6..393
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msksiavnag sstlkfklfd mpseevvaeg tierigekmg hakikyagqk heddqpfadh
       61 gaaikylldq lialgivkny deitavghrv vaggeyfkds aiidddviak idslaeyapl
      121 hdpaelmgik afrkalpnaf aiavfdtsfh aempkknaly sipyewyeky garkygahgt
      181 shryvaaqaa kmlkkpledl klitmhigag asitavkngk sfdtsmgftp lagitmatrs
      241 gdvdpslvaf veekaglssd emidalnhks gllgiselsp dmrdilaaad kgnekaqlal
      301 diyvnrikry igayiaemdg vdaivftagv gensapvrkl vtdnldcfgi kidqeknqch
      361 gverdlsaad akvktllipt neelmivrdi erlkkean
//
LOCUS       WP_003714658             148 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: pilin [Neisseria].
ACCESSION   WP_003714658
VERSION     WP_003714658.1
KEYWORDS    RefSeq.
SOURCE      Neisseria
  ORGANISM  Neisseria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Neisseria"
                     /db_xref="taxon:482"
     Protein         1..148
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=15332
     Region          1..146
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkaiqkgftl ielmiviaiv gilaavalpa yqdytaraqm sealtlaegq ksavveyysd
       61 ngtfpntnas agianasdik gkyvasvnvs gtaslakita tmnssgvnnd ikgstlvleg
      121 kqnsgsfewt ckagtvkekf lpsscrak
//
LOCUS       WP_003709501             129 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Neisseria lactamica].
ACCESSION   WP_003709501
VERSION     WP_003709501.1
KEYWORDS    RefSeq.
SOURCE      Neisseria lactamica
  ORGANISM  Neisseria lactamica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Neisseria lactamica"
                     /db_xref="taxon:486"
     Protein         1..129
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14322
     Region          1..121
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mknvqkgftl lelliavail siltliayps ykaytrrirl sevkstllmn aqnleryyrq
       61 kgtfdnydpk klkqnkyfni tlskvtpdhf tlqavpdpat negetcivtl ndggtlsaag
      121 ngqscpdfd
//
LOCUS       WP_003714994             398 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Limosilactobacillus oris].
ACCESSION   WP_003714994
VERSION     WP_003714994.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus oris
  ORGANISM  Limosilactobacillus oris
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Limosilactobacillus oris"
                     /db_xref="taxon:1632"
     Protein         1..398
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43224
     Region          6..393
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msksiavnag sstlkfklfd mpseevvaeg tierigekmg hakikyagqk heddqpfadh
       61 gaaikylldq lialgivkny deitavghrv vaggeyfkds aiidddviak idslaeyapl
      121 hdpaelmgik afrkalpnaf aiavfdtsfh aempkknaly sipyewyeky garkygahgt
      181 shryvaaqaa kmlkkpledl klitmhigag asitavkngk sfdtsmgftp lagitmatrs
      241 gdvdpslvaf veekvglssd emidalnhks gllgiselsp dmrdilaaad kgnekaqlal
      301 diyvnrikry igayiaemdg vdaivftagv gensapvrkl vtdnldcfgi kidqeknqch
      361 gverdlsaad akvktllipt neelmivrdi erlkkean
//
LOCUS       WP_003715624             236 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein
            [Limosilactobacillus oris].
ACCESSION   WP_003715624
VERSION     WP_003715624.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus oris
  ORGANISM  Limosilactobacillus oris
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (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   2  (residues 1 to 236)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 236)
  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 236)
  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 236)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Limosilactobacillus oris"
                     /db_xref="taxon:1632"
     Protein         1..236
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26768
     Region          146..235
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(165,184..185,203,206,214..215,227,232)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 makefllmsq saelvdqlta tckkarwqlt qittptglvv aleqrpvtgi wwdlshvsld
       61 ttiatmtlvr hqltgpimil vpevtdriqr klfhaqvddv lalpvdersf rarveqrlwl
      121 yrhvqfakpa paeapeknav iaandwtidq anytvkkagq pveltpkefq llsylinhhn
      181 qvlsreqlvs gvwgydllas srivdihish lrdkleddph kpahlltvrg fgykfv
//
LOCUS       WP_003716169             155 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Limosilactobacillus oris].
ACCESSION   WP_003716169
VERSION     WP_003716169.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus oris
  ORGANISM  Limosilactobacillus oris
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 155)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Limosilactobacillus oris"
                     /db_xref="taxon:1632"
     Protein         1..155
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16215
     Region          16..135
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mknnqlllnq ltsllageps plailanasa linqsvsqln wagfylydqa nnelvlgpfq
       61 gqvacmhikm gtgvcgtaaq tqttqvvadv sqypgyiscd aaarselvvp lvksngelyg
      121 vldldapvpd rfddqlvacm taaaaiimka ideaa
//
LOCUS       WP_003717234             462 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Limosilactobacillus vaginalis].
ACCESSION   WP_003717234
VERSION     WP_003717234.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus vaginalis
  ORGANISM  Limosilactobacillus vaginalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 462)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Limosilactobacillus vaginalis"
                     /db_xref="taxon:1633"
     Protein         1..462
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=51606
     Region          337..462
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(413..414,417,435..438,440)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mrfqlkhwll viiallvivl ginwwhqahh fnkkvtingi nvgglttkqa lekvkttkns
       61 nqvylndhli ydgsdtdyvf tsadeakvkn vfhkqftffp srkpyslelk pgkqdlsqye
      121 tkkatvqsil qrenrgrqap vdayaelrdd kvtvhkgqkg tkideqrilh qlssqatnsk
      181 iyltakqqqp lspdsktvqn ekkqlqklig kkvsykvekq tyhlttgdvi tsatykdgqy
      241 hfntsvidkk ikqinkkqat lgkafkfktp dgkeitttrd gsygwkisae ragkslanai
      301 atgkssvdak adiygigynr rgtgygvten ggigntyavi siadqhawfy kngkcvddvd
      361 vvtgkmsnka dqtpkgvwyi mykqspsvlk gtsdngskys skvqywaqft dsgcgfhdas
      421 wrhnwsktay lndgsngcan mhpsdaagay nslevnepvi iy
//
LOCUS       WP_003716464             256 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Limosilactobacillus
            vaginalis].
ACCESSION   WP_003716464
VERSION     WP_003716464.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus vaginalis
  ORGANISM  Limosilactobacillus vaginalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
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   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   4  (residues 1 to 256)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Limosilactobacillus vaginalis"
                     /db_xref="taxon:1633"
     Protein         1..256
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=28894
     Region          6..>242
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mtkpviqfkh vqkqfgknvv ipdlsfeinq gefvtilgss gsgktttlkm vnglwkpnag
       61 eilidgqkis dldlvqlrrh mgyvvqqigl fphmtiaeni avvpkmlqwe qskidqrvke
      121 llalvqldpa kyanrypsql sggqqqrvgv aralavnppy vlfdepfgal daltrielqk
      181 evkrihesla nkifmfvthd ineafflgqr vmimhegrie qfatpgeiis hpatpfvkel
      241 lgtvqqnqel wrqyhd
//
LOCUS       WP_003718689              98 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Listeria ivanovii].
ACCESSION   WP_003718689
VERSION     WP_003718689.1
KEYWORDS    RefSeq.
SOURCE      Listeria ivanovii
  ORGANISM  Listeria ivanovii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Listeria ivanovii"
                     /db_xref="taxon:1638"
     Protein         1..98
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11122
     Region          1..98
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(6..7,25..26,34,37,39..40,42,45..46,48,56,61,68)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(25,56..57,59,80)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mvpvdfedrv yevvrqiplg kvttygqiay kigfpknsrl vgatlkhskr dkitpchrvv
       61 naagrlvpnw deqrellmse gvqlkanghv dlktyfwq
//
LOCUS       WP_003718723             266 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Listeria].
ACCESSION   WP_003718723
VERSION     WP_003718723.1
KEYWORDS    RefSeq.
SOURCE      Listeria
  ORGANISM  Listeria
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Listeria"
                     /db_xref="taxon:1637"
     Protein         1..266
                     /product="formate/nitrite transporter family protein"
                     /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=28836
     Region          10..243
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mdvessplmq kidystrkki dlvnnsilry ivramlaclf ltlgtavavm igdkvdhfap
       61 glgkivyafm fswslvmiiy mnaelgtsnm mymttgvyqk iikpgkalqi lflciicnll
      121 ggilagylvs ltsafqnlpa dhflftavtg klekapleif vegifanivv ntavlctlrm
      181 kddagkviam ifiififafl gfehvianfs sfslaffasg gtlaamtvgn vsvnlvlall
      241 gnfvggglvi glgyawlnrt ksiykd
//
LOCUS       WP_003719376             397 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Listeria ivanovii].
ACCESSION   WP_003719376
VERSION     WP_003719376.1
KEYWORDS    RefSeq.
SOURCE      Listeria ivanovii
  ORGANISM  Listeria ivanovii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Listeria ivanovii"
                     /db_xref="taxon:1638"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42964
     Region          2..388
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mqkmmainag ssslkfqife mpgeevlvkg lieriglpga ifnmsfqnek ikevckinnh
       61 geavetlleq lkahqvinnl seiagvghrv ahggedfvks cvvtdevvqg ieavtslapl
      121 hnpaniigik tfrellpeai svavfdtafh qtipeenfly alpyelyekh hirkygfhgt
      181 shqyvagkaa evlgkplekl kiischlgng asvcaiedgk svntsmgftp naglmmgtrs
      241 gtidatiipy lvdelgysld evvqmmsses gvlgvsgiss dfrdievaae egntraqltl
      301 rmftgqicny igayasamng cdallftagv gensplirkm vteqlsylgv tcdvtknnag
      361 dmiisendqa vkvciiptne elmiardvek yakqptr
//
LOCUS       WP_003719889             166 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Listeria ivanovii].
ACCESSION   WP_003719889
VERSION     WP_003719889.1
KEYWORDS    RefSeq.
SOURCE      Listeria ivanovii
  ORGANISM  Listeria ivanovii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 166)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Listeria ivanovii"
                     /db_xref="taxon:1638"
     Protein         1..166
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18144
     Region          8..157
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mieiakmtgs keenyalalk qvqamitget nlianlsnvs silnqaltni nwvgfylfek
       61 eknelvlgpf qglpacirip lgkgvcgsaa ldqktyived vhqfpghiac daasnseivl
      121 plvkneqlig vldidspsts hfdkvdqlwl ekirdaivhe lpnemn
//
LOCUS       WP_003708068             116 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Neisseria].
ACCESSION   WP_003708068
VERSION     WP_003708068.1
KEYWORDS    RefSeq.
SOURCE      Neisseria
  ORGANISM  Neisseria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 116)
  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   3  (residues 1 to 116)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 116)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Neisseria"
                     /db_xref="taxon:482"
     Protein         1..116
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12767
     Region          1..116
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 msdgqnipvk mmslklqems llyksympfl eygglfvqtd dvlsigedil laveilnypk
       61 lflptqvawi npartsskpk gvglaftkhe nclklkdqie velgsvlgsg kptftm
//
LOCUS       WP_003720201             132 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Listeria ivanovii].
ACCESSION   WP_003720201
VERSION     WP_003720201.1
KEYWORDS    RefSeq.
SOURCE      Listeria ivanovii
  ORGANISM  Listeria ivanovii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 132)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 132)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Listeria ivanovii"
                     /db_xref="taxon:1638"
     Protein         1..132
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=14418
     Region          2..125
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(6..9,39..41,44,68,107,121)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mevfvdgasa gnpgpsgagi vlkadgiheq laiplavmtn heaefiaikl gleaalkkqa
       61 tfirlysdsk vaieaiqkrh aknplfkhhl deilqmsdpl alffvewrhv sqnkqadqla
      121 rqaikkqkqs gk
//
LOCUS       WP_003721314             334 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Listeria monocytogenes].
ACCESSION   WP_003721314
VERSION     WP_003721314.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 334)
  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 334)
  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
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  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   5  (residues 1 to 334)
  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   6  (residues 1 to 334)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 334)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 334)
  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 20283862
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..334
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37878
     Region          <18..75
                     /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(24,26..28,37)
                     /site_type="other"
                     /note="non-specific DNA interactions [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            37..43
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            order(38..39,43)
                     /site_type="other"
                     /note="sequence specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238044"
     Site            38..39
                     /site_type="other"
                     /note="putative cAMP binding site [chemical binding]"
                     /db_xref="CDD:238044"
     Region          <134..307
                     /region_name="ASKHA_ATPase_ROK"
                     /note="ATPase-like domain of the ROK (Repressor, ORF,
                     Kinase) domain family; cd23763"
                     /db_xref="CDD:466849"
ORIGIN      
        1 maiprdlkel nkkniksilr qqgamtkaei aevtglsvvt vnklirdlve neeileqdns
       61 vatggrravs yeinpnfqqv lvislqekwk kitysfsvyn llgepefved msgedldita
      121 lkrntkdiic afpkiscvvi gvpgieiggk lramdfplll nvqlretlea evnlpvlvet
      181 dtnaailgyk nrpvkeeniv glyyperfpp gagllmngei lkgqnglage ikhmplqvdw
      241 dnfdfsvdei kahirkmvll tmsfydpeti vlytnfyfgq kdfmeelkee lkqvypyavl
      301 peivlsrkft tdyrigllaf gidylennmt dwri
//
LOCUS       WP_003721566             397 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Listeria monocytogenes].
ACCESSION   WP_003721566
VERSION     WP_003721566.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43024
     Region          3..388
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mhkimainag ssslkfqift mpgeevlvkg lieriglpda ifnmsfqnek iketrainnh
       61 geaveilleq lkahqvindl neitgvghrv ahggedfvts cvvtdevvkg ieavtnlapl
      121 hnpaniigik tfrellpnav svavfdtafh qtipeenfly alpyelyekh hirkygfhgt
      181 shkyvagkaa evlekplekl kiischlgng asvcaieagk svntsmgftp naglmmgtrs
      241 gtidatiipy lvdelgysld evmhmmsses gvlgvsgiss dfrdieiaak egnsralltl
      301 rmftgqicny igayasamng cdallftagv gensslirqm vteqlsylgv tchvtknnag
      361 dmiisnddea vkvciiptne elmiardvek yakqtis
//
LOCUS       WP_003719944             374 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Listeria ivanovii].
ACCESSION   WP_003719944
VERSION     WP_003719944.1
KEYWORDS    RefSeq.
SOURCE      Listeria ivanovii
  ORGANISM  Listeria ivanovii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Listeria ivanovii"
                     /db_xref="taxon:1638"
     Protein         1..374
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42212
     Region          1..266
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          262..346
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkflhtadlh lgkivsgvsm lteqefilae itkiaqeekv dalivagdly dravppadav
       61 kvlndilvkw nvelgipifa isgnhdsaer lsfgtqwyas sklymkgkcs adfeaipfmd
      121 aeiwlvpyhe paiireafkd hsirsfedam qavtkqirak wnpakaqilv ghafvsggip
      181 sdserqlaig nvdrvstncf dgftytalgh lhhphainhp tifysgsplk ysfsevndkk
      241 svriveiegn slvrveerll tpkhdmriis gtlaeltenl vetpddffqv nlmdegalid
      301 pmgklrqfyp nilhlerkkq qlkesqasfe evmkkddlel fdqffeyang teltneqkqk
      361 ltevfelark eeae
//
LOCUS       WP_003721758             249 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Listeria monocytogenes].
ACCESSION   WP_003721758
VERSION     WP_003721758.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 249)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..249
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=28527
     Region          6..241
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mdissteiwd airrnsylly yqpkvdaktn kiigfeglvr lktattilap idffddivll
       61 natremqdfv aetaikqinq lggrfsisin ipahyvasst ymtflhdyvk ehlkypecle
      121 ieiiergeit elaiadknlr kikdlgvkvs mddfgkgyss laylrslpid ivktdmsfia
      181 llktdrkqqi iiraivnlch dlggkvvteg vedmeqvekl remkvdyfqg yyfsrplpme
      241 dikekysfv
//
LOCUS       WP_003724512             297 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Listeria
            monocytogenes].
ACCESSION   WP_003724512
VERSION     WP_003724512.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
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
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..297
                     /product="aminoglycoside 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=34448
     Region          14..232
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mdvtqlkmlh nakviseink gfsvdrkyqv detylvrvfp idllqereqe fkiiqaldsq
       61 tpfvpkaydf gfieregymi isylrgedae igmtrlshse qlkagfsage ilrevhkipl
      121 aipkmnwldf qtvkferkvk elkeleitas fltdtekfvn eniarlknrp iclqhgdfhp
      181 aniilnnkkf vglidfnrle fgdplfdlak igffttevsi pfargnilgy idkeevtdfw
      241 nlyalytamh itsavnwaak nesrnfkklm dyaaktvash dnfqrivpnw mneeefk
//
LOCUS       WP_003724943             235 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Listeria].
ACCESSION   WP_003724943
VERSION     WP_003724943.1
KEYWORDS    RefSeq.
SOURCE      Listeria
  ORGANISM  Listeria
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 235)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Listeria"
                     /db_xref="taxon:1637"
     Protein         1..235
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=27101
     Region          6..235
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mglmkfqlfi qpkldvlqgn iveyeillrd dsavprfpls eleavladee lylafsewfs
       61 eafldvlkky pndrfainia pqqlfyietl hwldklkses hritvemted ifdvpghkrh
      121 lnandknafi lnkikvihgl gyhiaiddvs cglnslervm sylpyiieik fslihfknip
      181 ledlllfika wanfaqknkl dfvvegietk etmtlleshg vsifqgylvn kpfpv
//
LOCUS       WP_003712180             429 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Neisseria
            lactamica].
ACCESSION   WP_003712180
VERSION     WP_003712180.1
KEYWORDS    RefSeq.
SOURCE      Neisseria lactamica
  ORGANISM  Neisseria lactamica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Neisseria lactamica"
                     /db_xref="taxon:486"
     Protein         1..429
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=49081
     Region          19..407
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mmksiltvsg nrmrkprith ldvwanderi gtlekgamyr faydnpnssl lglhyqdrsk
       61 vyisnnmpyi faqyfpegfl aahitskyaf hdapfednem lrlailgret lgrihvrcnd
      121 plfnewidgl emknprilte rdllginarq vfqqymaeif hhgrfvnvsg iqqkmsldai
      181 rrntkqtasy iakgfdpsey pclaaneflc mqtikqagip vaqtslseds svllvrrfdv
      241 geqgyflgme dftslrqysv edkykgsyaa iaqiirqisg rpdedlihff nqlaascilk
      301 ngdvylknfs vlyhdeydvr lapaydvldt siygvgtqgt fdayddtlal nltdlgkkty
      361 pskntlldfa ekycdlgred asfmmdtivq akeqvlvkys dvlrdngwla qqwhfipden
      421 eeglpftfr
//
LOCUS       WP_003730510             571 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Listeria
            monocytogenes].
ACCESSION   WP_003730510
VERSION     WP_003730510.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 571)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..571
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=63812
     Region          2..552
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 midkrlfqlv ekkslillil frvlglglmi slwfnfaqql tqyleggsva wlrlvgivll
       61 vlvgkailtk laekqiyqas aelrlsmrra vmakafrlgn segqlpastl tqltvdgieq
      121 leiyysrflp qlfycliasl mifgslvgfa wqpaivllic mpmipvvima vmkiakrils
      181 gywsdytnlg skfhenlsgl silkaydqdk ykqeeivsda erfrkatmsl lsmqlnsiti
      241 mdiisysgaa lgigmslimf tngdisltgm lmflllsaef fipmrqlgsl fhvamngisa
      301 csklfaylel keqvygeiel ekslerievr dltftyekek naalhevsas fnqgsfsalv
      361 gksgsgkstf vrvllnqlpg yqgeiiwndv plsdlngeti rkqgvlvdnh gylyansiqe
      421 nllignshas etdlwnvleq vsladfvrnl peqlntllee ngsnlsggqr qrlllarall
      481 reaklyvfde itsgvdlese kiilgvlqkl aqekivlfis hrlynvlaad qvlvfeagkl
      541 vevaspeqlq qeshyfknyf leeeallkgg a
//
LOCUS       WP_003720240             227 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Listeria ivanovii].
ACCESSION   WP_003720240
VERSION     WP_003720240.1
KEYWORDS    RefSeq.
SOURCE      Listeria ivanovii
  ORGANISM  Listeria ivanovii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 227)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Listeria ivanovii"
                     /db_xref="taxon:1638"
     Protein         1..227
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=26595
     Region          <6..226
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mkkpsvseii gqnlfdtiye pivaventqv fgyesltrlq tnhwnaisdf ikkaeqdglq
       61 kafelltlhn avkcfhknsd iplfvnisyd aflenqeelq eilldnrkiv fefretsklp
      121 qermndldeq lllfqkkhqt kfaiddfgsg yadlhrvfah hsdfvktdrl llrdlfqsdg
      181 kkiffeqlnn yvkkhhksfi vegvetkeql tflqdigvpy aqvyyfh
//
LOCUS       WP_003730599             309 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Listeria
            monocytogenes].
ACCESSION   WP_003730599
VERSION     WP_003730599.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
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   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 309)
  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 309)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..309
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34002
     Region          1..69
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          157..>272
                     /region_name="PRK06347"
                     /note="1,4-beta-N-acetylmuramoylhydrolase"
                     /db_xref="CDD:180536"
     Region          224..289
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mtelgdklkq arrekglsld dlqqvtkiqk rylvaieegn yavmpgkfya rafikqyaea
       61 vgldsatlfd efesevpetp qqevvnnept rvqskrnpmp aqsvgnqgna rnrffdilpk
      121 ilialfivfi lfivwfflln kqdnstekvk tdtnnptvkv edstkskdts kdtekkdttt
      181 eedkstetkd ktedtakeve vtkgetsgna ttytvkntdk mtlslsatgd swigvsdang
      241 stiqnvtlst qnpsteidlg dnktvsivig nspvttvkin gkqlelapdl vkqvltinle
      301 asdtssdae
//
LOCUS       WP_003730828             133 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ribonuclease HI family protein [Listeria].
ACCESSION   WP_003730828
VERSION     WP_003730828.1
KEYWORDS    RefSeq.
SOURCE      Listeria
  ORGANISM  Listeria
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 133)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 133)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 133)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Listeria"
                     /db_xref="taxon:1637"
     Protein         1..133
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=14580
     Region          2..125
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(6..9,39..41,44,68,107,121)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mevfvdgasa gnpgpsgagi vlkaegiyeq faiplavmtn heaefiaikl gleeaikkqa
       61 tlirlysdsk vaieaihkrh aknplfkphl eailemadtf elffaewrnv sqnkqadqla
      121 rqaikkqkqp gvk
//
LOCUS       WP_003730956             571 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Listeria
            monocytogenes].
ACCESSION   WP_003730956
VERSION     WP_003730956.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 571)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..571
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=63973
     Region          2..552
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 midkrlfqlv ekkslvllil frvlslglmi glwlvfaqql thyleaqsvd wlwligtvlv
       61 vlvgkailtk laekqiyqas aelrlsmrra vmekafrlgn negqlpastl tqlavdgieq
      121 leiyysrflp qlfycliasl mifgslvgfa wqpaivllic mpmipivima vmkiakrils
      181 gywsdytnlg tkfhenlsgl silkayeqdk ykqeeivsda erfrkatmsl lsmqlnsiti
      241 mdiisysgaa lgigmslimf tngnismtgm lmflllsaef fipmrqlgsl fhvamngisa
      301 csklfaylel keqvygseel akplekmevr hltytyeegk akalqdisvn fnkgsfsalv
      361 gksgsgkstf vrvllnqlpg yqgeivwndv plaslsgeti rkqavlvdnh gylyansire
      421 nllignpaan dsdlwnvleq vsltdfvrkl peqlnenlee ngsnlsggqr qrlllarall
      481 cqaevyvfde itsgvdlese kiillvlqkl akekivlfis hrlynvldad qvlvfdagkl
      541 levasperlq qesnyfknyf leeeallkgg a
//
LOCUS       WP_003732444             343 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Listeria monocytogenes].
ACCESSION   WP_003732444
VERSION     WP_003732444.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..343
                     /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=40340
     Region          4..276
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mtqsalkres yfdnakfili flvvfghflq tfiadyagvr vlyiyiytfh mpafvlisgf
       61 faksfgkpgy lkktmkklil pyvffqliys ifyyfllskd nlsiqlldpe wslwfllslf
      121 fwnvmlfifa kikpwksisi alfvglvagy fdiiggylsl srtfvffpff lvgyflkkeh
      181 fyylkthfvm ilggifivll lsfitfhpnl ndkwflgskp yanfvevksl glfirglvyl
      241 isfgsiaaff sfiprkrlff tkwgkntlyv yllhgffikf fregsqtdfq yspstflllf
      301 vvtfvltvll ssrlvkifvq pvielrvsml rdvfsrltkr esy
//
LOCUS       WP_003725366             328 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Listeria monocytogenes].
ACCESSION   WP_003725366
VERSION     WP_003725366.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
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   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   4  (residues 1 to 328)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..328
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=36614
     Region          1..318
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mirfdnvskk ysddktaavn nvtldikdge ffvfigpsgc gktttlkmin rliplttgti
       61 yinekrisdy dihelrwdig yvlqqialfp hmtieeniai vpelkkwske kihdritell
      121 dsvgldpesy rhrkpaelsg geqqrvgvvr alaadpgiil mdepfsaldp isrqrlqqdi
      181 salqkkikkt ivfvthdmqe alalgdricv mqggeivqva tpqeimknpe ndfvkdflas
      241 ghafntpile anftvkdlie adlfysyqts dgtlgissae pvenlvrria eeqsipvtde
      301 agnfigtvsn khvmqflarh lessgelv
//
LOCUS       WP_003733226             374 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Listeria monocytogenes].
ACCESSION   WP_003733226
VERSION     WP_003733226.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..374
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42190
     Region          1..266
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          262..349
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkflhtadlh lgkivsgvsm laeqeyiltq itqiaeeeqv dalilagdly dravppadav
       61 kvlndilvkw nvelgipifa isgnhdsaer lafgsqwyes sklymkgkct sqfdgipfmd
      121 aevwlvpyhe paiirqafad nsirsfedam qavtkqirsk wdtskaqilv ghafvsggip
      181 sdserqlaig nvdrvstdcf dgftytalgh lhhphairhp sifysgsplk ysfseandhk
      241 svrivelegk elisvterfl tpkhdmriis gtlaeltenl venpddffqv nlmdegalid
      301 pmgklrqfyp nilhlerkkq tlketqdsfe eimkkddlel fgqffehvng teltetqkqk
      361 ladvfeqark edae
//
LOCUS       WP_003734764             571 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Listeria
            monocytogenes].
ACCESSION   WP_003734764
VERSION     WP_003734764.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 571)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..571
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=63963
     Region          2..552
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 midkrlfqlv ekkslvllil frvlslglmi glwfvfaqql thylegqsvd wlwligtvlv
       61 vlvgkailtk laekqiyqas aelrlsmrra vmekafrlgn negqlpastl tqlavdgieq
      121 leiyysrflp qlfycliasl mifgslvgfa wqpaivllic mpmipivima vmkiakrils
      181 gywsdytnlg tkfhenlsgl silkayeqdk ykqeeivsda erfrkatmsl lsmqlnsiti
      241 mdiisysgaa lgigmslimf tngnismtgm lmflllsaef fipmrqlgsl fhvamngisa
      301 csklfaylel keqvygseel akplekmevr hltytyeegk akalqdisvn fnkgsfsalv
      361 gksgsgkstf vrvllnqlpg yqgeivwndv plaslsgeti rkqavlvdnh gylyansire
      421 nllignpaan dsdlwnvleq vsladfvrkl peqlnenlee ngsnlsggqr qrlllarall
      481 cqaevyvfde itsgvdlese kiillvlqkl akekivlfis hrlynvldad qvlvfdagkl
      541 levasperlq qesnyfknyf leeeallkgg a
//
LOCUS       WP_003738275             266 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Listeria
            monocytogenes].
ACCESSION   WP_003738275
VERSION     WP_003738275.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..266
                     /product="formate/nitrite transporter family protein"
                     /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=28811
     Region          10..243
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mdvensplmq kidystrkki dlvnnsilry ivramlaclf ltlgtavavm igdkvdhfap
       61 glgkityafm fswslvmiiy mnaelgtsnm mymttgvyqk ivkpgkalqi lllcivcnll
      121 ggilagylvs ltsvfhnlpa dhflftavsg klekaplqif vegifanivv ntavlctlrm
      181 kddagkviam ifiififafl gfehvianfs sfslaffasg gtlaamtagn vtvnlvlall
      241 gnfvggglvi glgyawlnrt ksiykd
//
LOCUS       WP_003738926             327 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Listeria monocytogenes].
ACCESSION   WP_003738926
VERSION     WP_003738926.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
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
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..327
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=36514
     Region          1..317
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mirfdnvskk ysddktavnn vtldikdgef fvfigpsgcg ktttlkminr liplttgtiy
       61 inekrisdyd ihelrwdigy vlqqialfph mtieeniaiv pelkkwskek ihdritelld
      121 svgldpesyr hrkpaelsgg eqqrvgvvra laadpgiilm depfsaldpi srqrlqqdis
      181 alqkkikkti vfvthdmqea lalgdricvm qggeivqvat pqeimknpen dfvkdflasg
      241 hafntpilea sftvndliea dlfyayqtsd gtlgisakep veslvrriae eqsipvtdea
      301 gnfigtvsnk hvmqflarhl estgelv
//
LOCUS       WP_003730258             618 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Listeria monocytogenes].
ACCESSION   WP_003730258
VERSION     WP_003730258.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 618)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 618)
  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   3  (residues 1 to 618)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..618
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..618
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=68551
     Region          5..614
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          137..211
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 mttnmldlfi eeasehlqal ndnllqlekd ptngqlvsei frsahtfkgm satmgfqqva
       61 dlthamenvl devrnnrlav tehlvdiift ctshletmvs diqhggqgaa disktvadle
      121 allhpeqetd lavektyriq iqieeaailk avravmcler laemgiiset lpdreaiele
      181 efeqsfevvl esaqtkeeie avildiseie kvtvteevee vqviepikka akqttkrlen
      241 ktirvqleki eklmnvfees vieraridei aektnnkelm ehlgrfssis keiqngllnm
      301 rmvpvdsvfn rfpkmvrtla kelgkkidlv iegadtevdk ivideigdpl vhlirnsvdh
      361 gaetvevrrk ngknetatin lkafhsgnnv vieiaddgag inkrkvleka iaknvvtrae
      421 stkmtdaeif dllfdsgfst adqvsdlsgr gvgldvvrnt ilkiggkisv essenagstf
      481 rieipltlsi iqsmlvatse rryavplanv aeaitinpad iqhvhgkdli nyretiievl
      541 dlgecfhetp lndtdellll vvknakrtfg liikdiigqr eivlktlggf fsesqiafsg
      601 atilgdgrvv lilnletf
//
LOCUS       WP_003739453             297 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Listeria
            monocytogenes].
ACCESSION   WP_003739453
VERSION     WP_003739453.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
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
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..297
                     /product="aminoglycoside 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=34389
     Region          14..232
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mdvarlkmlh nakviseikk gfsinkkyqv detylvrvfp idllqerkqe fkiiqalnsq
       61 tpfvpkaydf gfieregymi isylqgedae sgmthlshse qfkagfsage ilrevhkipl
      121 dipkmnwldf qtakfkrkve elkeleitas flteteqfvy enltrlknrp vclqhgdfhp
      181 aniilknnkf vglidfnrle fgdplfdlak igffttevsi pfargsilgy idkeevtdfw
      241 nlyalytamh itsavnwaak nesrnfkklm dyaaktaash dnfqkivpsw mneeefk
//
LOCUS       WP_003730593             284 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Listeria monocytogenes].
ACCESSION   WP_003730593
VERSION     WP_003730593.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 284)
  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 284)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10097223
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..284
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=30727
     Region          5..281
                     /region_name="TBP_aldolase_IIB"
                     /note="Tagatose-1,6-bisphosphate (TBP) aldolase and
                     related Type B Class II aldolases. TBP aldolase is a
                     tetrameric class II aldolase that catalyzes the reversible
                     condensation of dihydroxyacetone phosphate with
                     glyceraldehyde 3-phsophate to produce tagatose 1; cd00947"
                     /db_xref="CDD:238477"
     Site            order(26..28,31,51,54,56..57,61,65,68..69,142,233..234,
                     236..237,240,244,247)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238477"
     Site            order(82..83,177..179,181,208..209,211,230,232..233)
                     /site_type="active"
                     /db_xref="CDD:238477"
     Site            order(83,178,208)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238477"
     Site            order(177,179,181,209,211)
                     /site_type="other"
                     /note="Na+ binding site [ion binding]"
                     /db_xref="CDD:238477"
ORIGIN      
        1 myvsmkgmle rankkyyavm aincfnleta raaidaaqel rapiiidllq dhltshlgsr
       61 fltkpiikma eeasvevain ldhghdvaiv kqcladgfss vmmdasshpy eenvaitkkm
      121 vefaevycas veaevgsiga vtgdnytnqe mytnpkvaid fakrtgidal aisygsshgd
      181 ypegftpafq fnivreikaa tnmplvlhgg sgcgaenire svrlginkin vgsdfmkaqa
      241 nqlkanlean paknyvdlih etikagketv knyiqlsgst gksl
//
LOCUS       WP_003740719             282 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Neisseria mucosa].
ACCESSION   WP_003740719
VERSION     WP_003740719.1
KEYWORDS    RefSeq.
SOURCE      Neisseria mucosa
  ORGANISM  Neisseria mucosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
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
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Neisseria mucosa"
                     /db_xref="taxon:488"
     Protein         1..282
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=31674
     Region          10..>246
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mmqpehtpli efknvskryd nhaavnelnl tiyqgeffvl vggsgsgkst tlrminalte
       61 ptdgnvyfng rrikdydirg lrhrigyvlq qialfptmtv rqnielmpdi lgwdkpkrts
      121 rvnellelvg mppetylnry phelsggeqq rigilraiaa kpdillmdep fsaldplara
      181 slqetvslih kklgttivfv thdmseaakl acrigvmhqg rlvqvdtpqd iqnhpaddyv
      241 rslfgaaqpe ntastdevin lyrsldadgk arvrehwake en
//
LOCUS       WP_003743744             332 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Neisseria].
ACCESSION   WP_003743744
VERSION     WP_003743744.1
KEYWORDS    RefSeq.
SOURCE      Neisseria
  ORGANISM  Neisseria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae.
REFERENCE   1  (residues 1 to 332)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Neisseria"
                     /db_xref="taxon:482"
     Protein         1..332
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=35225
     Region          34..161
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(121..122,125,138..141,143)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkkilfstsl aaltayatan tpvpdvspvs qgqhvvinip qqrlflytdg qltkiypvav
       61 gkamtqtnlg ehkigakafn ptwhipksiq kergdgvksv ppgpnnplgp vfvrlgdpkf
      121 slgihgtnap asvpgvrshg cvrmkspdal efaktiatga pasviyqlas lnedanknlw
      181 laayrdpynk knldtdalkk siaawakahg ktinatrida ilkartgaan cltcakgvkl
      241 rtplkslawm sgssafskpk vmpkpapvkd evlpagseie idaedtptpk aaseysprkp
      301 kaaeytpppa astpsypkyd lpadgdptsl lf
//
LOCUS       WP_003743776              96 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Neisseriaceae].
ACCESSION   WP_003743776
VERSION     WP_003743776.1
KEYWORDS    RefSeq.
SOURCE      Neisseriaceae
  ORGANISM  Neisseriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales.
REFERENCE   1  (residues 1 to 96)
  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   2  (residues 1 to 96)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Neisseriaceae"
                     /db_xref="taxon:481"
     Protein         1..96
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9845
     Region          13..80
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkkflfaals vltaslslaa vnintaspse lealpgigpa kakaiadyrq qhgafksvee
       61 lknvkgigeg ifsklkaeat vapapantka knvvqk
//
LOCUS       WP_003743777             154 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Neisseriaceae].
ACCESSION   WP_003743777
VERSION     WP_003743777.1
KEYWORDS    RefSeq.
SOURCE      Neisseriaceae
  ORGANISM  Neisseriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Neisseriaceae"
                     /db_xref="taxon:481"
     Protein         1..154
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=17188
     Region          7..106
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mnkenckgys ltqlifviai igiltaiayp syqkylrdse mrqalaalve saqfmerfyq
       61 qngsfkktst awpdlpnsrs lenfciyphg largaldgkf tlkavaldkn keprvikine
      121 slttficest asscddvtkn yfsgadkncs vyrl
//
LOCUS       WP_003745428             185 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase, partial [Neisseria mucosa].
ACCESSION   WP_003745428
VERSION     WP_003745428.1
KEYWORDS    RefSeq.
SOURCE      Neisseria mucosa
  ORGANISM  Neisseria mucosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Neisseria mucosa"
                     /db_xref="taxon:488"
     Protein         <1..>185
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
     Region          1..>185
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 dnlevlkhlk nayansvkmi yidppyntgs dgfvyqddrk ftpeelarla nidedeaari
       61 ldftdkgsns hsawltfmyp rlyiarellk ddgvifisid dneaaqlkll cdevfgegnf
      121 veqiiwekkf spqndakyfs enhdylicya kniteleikl lprtegtnar yknidndprg
      181 awtsg
//
LOCUS       WP_003745783              98 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Listeria seeligeri].
ACCESSION   WP_003745783
VERSION     WP_003745783.1
KEYWORDS    RefSeq.
SOURCE      Listeria seeligeri
  ORGANISM  Listeria seeligeri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Listeria seeligeri"
                     /db_xref="taxon:1640"
     Protein         1..98
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11169
     Region          1..98
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(6..7,25..26,34,37,39..40,42,45..46,48,56,61,68)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(25,56..57,59,80)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mipadfedrv yevvrqiprg kvttygqiay kigfpknsrl vgatlknskr nkitpchrvv
       61 naagrlvpnw eeqrelllse gvqfkanghv dlkiyfwq
//
LOCUS       WP_003746078             522 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA, partial [Listeria seeligeri].
ACCESSION   WP_003746078
VERSION     WP_003746078.1
KEYWORDS    RefSeq.
SOURCE      Listeria seeligeri
  ORGANISM  Listeria seeligeri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 522)
  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   3  (residues 1 to 522)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Listeria seeligeri"
                     /db_xref="taxon:1640"
     Protein         1..>522
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          5..522
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          135..214
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 mttnmldlfi eeasehlqal ndnllqlekd ptngglvsei frsahtfkgm satmgfqqva
       61 dlthamenvl devrnnrlvv tehlvdiift ctshletmvs diqhggqgaa ditktvadle
      121 allspeqees teatyqisik iedaailkav ravmclerla eigiisdttp dreaieleef
      181 eqtfevvles tqtkeeieav lldiseiekv tvkeeveetq ivepikktak qttkrlenkt
      241 irvqlekiek lmnvfeesvi erarideiae ktnnkelmeh lgrfssiske iqngllnmrm
      301 vpvdsvfnrf pkmvrtlake lgkkidlvie gadtevdkiv ideigdplvh lirnsvdhga
      361 etvevrrkng knetatinlk afhsgnnvvi eiaddgagin krkvlekaia knvvtraest
      421 kmtdteifdl lfdsgfstad qvsdlsgrgv gldvvrntil kiggkisves senagstfri
      481 eipltlsiiq smlvataeyr yavplanvae aitidradiq hv
//
LOCUS       WP_003747641             328 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Listeria seeligeri].
ACCESSION   WP_003747641
VERSION     WP_003747641.1
KEYWORDS    RefSeq.
SOURCE      Listeria seeligeri
  ORGANISM  Listeria seeligeri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
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   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   4  (residues 1 to 328)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Listeria seeligeri"
                     /db_xref="taxon:1640"
     Protein         1..328
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=36721
     Region          1..318
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mirfdnvskk ynedkiavnn vtldikdgef fvfigpsgcg ktttlkminr liplttgtiy
       61 inekrisdyd ihelrwdigy vlqqialfph mtieeniaiv pelkkwdkdk ihdritelld
      121 svgldpesyr hrkpaelsgg eqqrvgvvra laadpgiilm depfsaldpi srqrlqqdis
      181 alqkkikkti vfvthdmqea lalgdricvm qdgeivqvat pqeiiknpen dfvkdflasg
      241 hafntpileg sftvndlida dlfyayqtsd gslgisltdp venlvrrvae eqsipvldea
      301 tgefvgtitn khvmqflarh lessgelv
//
LOCUS       WP_003748913             293 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Listeria
            seeligeri].
ACCESSION   WP_003748913
VERSION     WP_003748913.1
KEYWORDS    RefSeq.
SOURCE      Listeria seeligeri
  ORGANISM  Listeria seeligeri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 293)
  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   2  (residues 1 to 293)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Listeria seeligeri"
                     /db_xref="taxon:1640"
     Protein         1..293
                     /product="aminoglycoside 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=33751
     Region          14..230
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mdlraiemlk nakvikeike gfsidqkyqv dnsylvrvfp enmweerkve feaiqklspl
       61 apkvpraldf gllqgkgymv idyvlgedae sgmthlskae qfqagvsaga vlrkihkmdi
      121 natelnwydf qkekyyrkls klkksnievv flqelesfie nnldlmkgre irlqqgdfhp
      181 aniilknhqf sgiidfnrle fgdplldlak igffttnssi afakgnilgy igkeditdfw
      241 klyalytamh ivfalswase ndtrnlekle syaiktvssh dnfrklipkw mtn
//
LOCUS       WP_003750781             116 aa            linear   BCT 20-JAN-2025
DEFINITION  PilZ domain-containing protein [Neisseria polysaccharea].
ACCESSION   WP_003750781
VERSION     WP_003750781.1
KEYWORDS    RefSeq.
SOURCE      Neisseria polysaccharea
  ORGANISM  Neisseria polysaccharea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 116)
  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   3  (residues 1 to 116)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 116)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Neisseria polysaccharea"
                     /db_xref="taxon:489"
     Protein         1..116
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12689
     Region          1..116
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 msdgqnipak mmslqlkdmn llyssympfl ehgglfvqtd dvfsigddil laveilnfpk
       61 lflptkvawi npartsskpk gvglaftkhe nclklkdqie velgsvlgsg kptftm
//
LOCUS       WP_003744201             143 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Neisseriaceae].
ACCESSION   WP_003744201
VERSION     WP_003744201.1
KEYWORDS    RefSeq.
SOURCE      Neisseriaceae
  ORGANISM  Neisseriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Neisseriaceae"
                     /db_xref="taxon:481"
     Protein         1..143
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=16390
     Region          1..134
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkntlqkgft lvellivivi lailatlayp syerfirksr lenvrselli naqnlerfya
       61 qnrtfenfpa tdlvqneyft iqffnyrntq kgkknpsasg flleakpndg yksketcsvy
      121 ldsdgifwas nadcpgyehi dqk
//
LOCUS       WP_003742675             282 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Neisseria mucosa].
ACCESSION   WP_003742675
VERSION     WP_003742675.1
KEYWORDS    RefSeq.
SOURCE      Neisseria mucosa
  ORGANISM  Neisseria mucosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Neisseria mucosa"
                     /db_xref="taxon:488"
     Protein         1..282
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29437
     Region          12..242
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mgtdkkdtiy gtsgedviyg gdgadviygg dgndtlqggn ngdslygqgg kdylqggdgn
       61 dylnggadad imrggdgndv yfvdhkgdev ieygnlnggi dtvrsvidyt ltdnvehlfl
      121 qgsgnlngtg nalnndingn sgdnhlygla gddclvgkdg ndyldggign dvliggtgnd
      181 tyffdkgygr dtiqdesgnd tlqfgkgisa sdvllsksgn nltvsvgnsd svtiddwfsg
      241 nnhkienfkf adgstyevtg hgdyyslsav nsiqqqtqvp ni
//
LOCUS       WP_003755889             327 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Listeria grayi].
ACCESSION   WP_003755889
VERSION     WP_003755889.1
KEYWORDS    RefSeq.
SOURCE      Listeria grayi
  ORGANISM  Listeria grayi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
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
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Listeria grayi"
                     /db_xref="taxon:1641"
     Protein         1..327
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=36933
     Region          1..317
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mikfedvskt ykdgleavkn inleikdgef fvfigpsgcg ktttlkminr lnkltkgtiy
       61 idgkrisdyd ihelrwnigy vlqqialfph mtieeniaiv pelkkwdkkk iqeritelld
      121 svglepekyr hrkpaelsgg eqqrvgvvra laadpdiilm depfsaldpi srqklqqdis
      181 dlqkrikkti vfvthdmqea ialgdriclm qdgevvqidt peeilrhpen efvrnfldsg
      241 nahsqsvlgs sytvqdllde nlhlsyqtdd gslyvnasds ldsliqtlad tksipvkdad
      301 gnfiatvtnq hvlrflsivm erqgehv
//
LOCUS       WP_003757071             162 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Neisseria sicca].
ACCESSION   WP_003757071
VERSION     WP_003757071.1
KEYWORDS    RefSeq.
SOURCE      Neisseria sicca
  ORGANISM  Neisseria sicca
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Neisseria sicca"
                     /db_xref="taxon:490"
     Protein         1..162
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=16287
     Region          1..159
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkaiqkgftl ielmivvaii gilaaialpm ygdytaraqa tegyellggm ktplveavaa
       61 tsndvacngt aatgtaaatd pawfksavls gkyvagvkae hagqddaatc tltatfkaas
      121 agvndkvagk tismkltpat gawecdttlg dnvapaacrk ks
//
LOCUS       WP_003750509             288 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Neisseria polysaccharea].
ACCESSION   WP_003750509
VERSION     WP_003750509.1
KEYWORDS    RefSeq.
SOURCE      Neisseria polysaccharea
  ORGANISM  Neisseria polysaccharea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Neisseria polysaccharea"
                     /db_xref="taxon:489"
     Protein         1..288
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30718
     Region          175..239
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mkwlfillva iniavfggtv gykltlkqag kipeaqnaan nlqvqpvapt mpvvrnipas
       61 gsavqaases dtgvllgasd ilteeqaeql rlkkeaeqkk lkekkqreek arreklaaek
      121 aqaerengaa dalcaaqasl tmdeddyhri kgllgkwshv asrsvekrta kakpadktyr
      181 vvlpvsadae nqaaelsakg fnpipfdgal slgvgnsren aqalqnrlag agfggahive
      241 raaetsrqdd slsvsrmtvl ftgvnaadad eirkitspyg klslksck
//
LOCUS       WP_003752352             166 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Listeria seeligeri].
ACCESSION   WP_003752352
VERSION     WP_003752352.1
KEYWORDS    RefSeq.
SOURCE      Listeria seeligeri
  ORGANISM  Listeria seeligeri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 166)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Listeria seeligeri"
                     /db_xref="taxon:1640"
     Protein         1..166
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18109
     Region          8..157
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mievtkmtgt keenyalalk qvqamiagep nvianlsnvs silnqaltni nwvgfylfek
       61 etnqlvlgpf qglpacirip lgkgvcgsaa anqktylved vhqfpghiac daasnseivl
      121 pivkneqlig vldidspsts rfdevdqlwl ekirdaivhe fpnemn
//
LOCUS       WP_003759183             357 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Neisseria
            sicca].
ACCESSION   WP_003759183
VERSION     WP_003759183.1
KEYWORDS    RefSeq.
SOURCE      Neisseria sicca
  ORGANISM  Neisseria sicca
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Neisseria sicca"
                     /db_xref="taxon:490"
     Protein         1..357
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39959
     Region          1..347
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msitiqnlnk hfgafhalkn inlnvptgkl vsllgpsgcg kttllriiag lenadggnil
       61 fdgqdvtakh vrerkvgfvf qhyalfrhmn vfdnvafglt vlpkserpsk eqirtkveel
      121 lklvqlshla ksyphqlsgg qrqrialara lavepkllll depfgaldak vrkelrtwlr
      181 dihhnlgvts ilvthdqeea levsdeivvm nhgkieqtgs aeaiyrkpen afvteflget
      241 dafegriekg iwhyngfawk ldaqykwqeq tatgyirphe wqlaaehetp miraeiekih
      301 avgalthvlv khgkqdvhit lagsdasrld lsagrelalv pkqvyvfsqn elieysi
//
LOCUS       WP_003759821             232 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Listeria].
ACCESSION   WP_003759821
VERSION     WP_003759821.1
KEYWORDS    RefSeq.
SOURCE      Listeria
  ORGANISM  Listeria
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 232)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Listeria"
                     /db_xref="taxon:1637"
     Protein         1..232
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=26895
     Region          3..232
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mkfqlyiqpk ldilqgnive yeillrddse vprfplsele avladeelyl tfcewfsdaf
       61 fdvlkkypnd rfainiapqq lfymetlhml dklrseshri tiemtedifd vpahkrhlna
      121 ddkdafilnk ikiihglgyh vaiddvgcgl nslervlsyl pyiielkfsl ihfnnidled
      181 lllfikawan fahknnldfv vegietketm aileshgvsi fqgylvnkpf pv
//
LOCUS       WP_003761343             270 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Listeria innocua].
ACCESSION   WP_003761343
VERSION     WP_003761343.1
KEYWORDS    RefSeq.
SOURCE      Listeria innocua
  ORGANISM  Listeria innocua
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Listeria innocua"
                     /db_xref="taxon:1642"
     Protein         1..270
                     /product="formate/nitrite transporter family protein"
                     /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=29469
     Region          3..257
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mgyyspqevt eitiekgtqk ansstltlvl lgflggafis lgyllyirav gtmphewgsf
       61 atligaslfp vglvcillgg gelitgnmma iaiawydkki sfqqllrnwa ivsvmnlvga
      121 ffvayffghf vgltegdflp ktlatagaki ndsfwvafvs gigcnwfvgi avwlcyaakd
      181 fagkilgiwf pvmafvaigf qhvvanmfii paaifagyys wadfiwnvip vylgnvvgga
      241 vfvslfyfla ykknapkkvk eeihqpieen
//
LOCUS       WP_003766158             290 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Neisseria sicca].
ACCESSION   WP_003766158
VERSION     WP_003766158.1
KEYWORDS    RefSeq.
SOURCE      Neisseria sicca
  ORGANISM  Neisseria sicca
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
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   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 290)
  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 290)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Neisseria sicca"
                     /db_xref="taxon:490"
     Protein         1..290
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31711
     Region          12..81
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          209..276
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 menqkkneyd iqaakslgde lgqlrhksgw didevarrlk lsaeqieale kgdysffsgl
       61 vfvmgylrsy arllkideat itgrlkaisa peedhvylvd rkknaglnyq dgekvgfpkw
      121 vlgmaalill gggiyvwqsk snheneqqva qnsdavrnsm qtpdlkkenv avsnmvengk
      181 qeisnaekaa ssvaaseaaa sapevkvdsd elwikvqyrs nliitdkkgt mifsriipag
      241 serrfkggap ynvwigiatg aqanyggtti nlaeyrvage ksasfvagkk
//
LOCUS       WP_003766162             270 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Listeria].
ACCESSION   WP_003766162
VERSION     WP_003766162.1
KEYWORDS    RefSeq.
SOURCE      Listeria
  ORGANISM  Listeria
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Listeria"
                     /db_xref="taxon:1637"
     Protein         1..270
                     /product="formate/nitrite transporter family protein"
                     /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=29499
     Region          3..257
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mgyyspqevt eitiekgtqk ansstltlvl lgflggafis lgyllyirav gtmphewgsf
       61 atfigaslfp vglvcillgg gelitgnmma vaiawydkki sfqqllrnwa ivsvmnlvga
      121 ffvayffghf vgltegdflp ktlatagaki ndpfwvafvs gigcnwfvgi avwlcyaakd
      181 fagkilgiwf pvmafvaigf qhvvanmfii paaifagyys wadfiwnvip vylgnvvgga
      241 vfvslfyfla ykknapkkvk eeihqpieen
//
LOCUS       WP_003768227             357 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Neisseria
            sicca].
ACCESSION   WP_003768227
VERSION     WP_003768227.1
KEYWORDS    RefSeq.
SOURCE      Neisseria sicca
  ORGANISM  Neisseria sicca
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Neisseria sicca"
                     /db_xref="taxon:490"
     Protein         1..357
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=40005
     Region          1..347
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msitiqnlnk hfgsfhalkn inlnvptgkl vsllgpsgcg kttllriiag lenadggnil
       61 fdgqdvttkh vrerkvgfvf qhyalfrhmn vfdnvafglt vlpkserpsk eqirtkveel
      121 lklvqlshla ksyphqlsgg qrqrialara lavepkllll depfgaldak vrkelrtwlr
      181 dihhnlgvts ilvthdqeea levsdeivvm nhgkieqtgs aeaiyrkpen afvteflget
      241 dafegriekg iwhyngfawk ldaqykwqeq tatgyirphe wqiaaehetp miraeiekih
      301 avgalthvlv khgkqdvhit lagsdasrld lsagrelalv pkqvyvfsqn elieysi
//
LOCUS       WP_003770135             274 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Neisseria elongata].
ACCESSION   WP_003770135
VERSION     WP_003770135.1
KEYWORDS    RefSeq.
SOURCE      Neisseria elongata
  ORGANISM  Neisseria elongata
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
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   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   4  (residues 1 to 274)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Neisseria elongata"
                     /db_xref="taxon:495"
     Protein         1..274
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=30725
     Region          9..>243
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mqdsltsfie frgagkqydg kyavrdldlt iyqgeffvlv ggsgsgkstt lrminaliep
       61 tdgnvyllgk rikdydirql rhqigyvlqq ialfptmtva enielmpdvl gwpkaerkar
      121 vnellelvel dpahyrdryp helsggeqqr igilraiaak pqlllmdepf saldplvrtv
      181 lqdqiamihq kfgttivfvt hdmqeaakla crigvmhngk lvqigtpeei kkqpandyvq
      241 slfstaaapd aqriihqflr ldkqgqeavr ravl
//
LOCUS       WP_003771452             397 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Listeria innocua].
ACCESSION   WP_003771452
VERSION     WP_003771452.1
KEYWORDS    RefSeq.
SOURCE      Listeria innocua
  ORGANISM  Listeria innocua
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Listeria innocua"
                     /db_xref="taxon:1642"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43051
     Region          3..388
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mhkimainag ssslkfqift mpgeevlvkg lieriglpda ifnmsfqhek iketrainnh
       61 geaveilleq lkehqvindl neitgvghrv ahggeafvss civtddvvkg iedvtslapl
      121 hnpaniigik tfrellpnav svavfdtafh qtipeenfly alpyelyekh hirkygfhgt
      181 shkyvagkaa evlekplekl kiischlgng asvcaieagk svntsmgftp naglmmgtrs
      241 gtidatiipy lvdelgysld evthmmsses gvlgvsgiss dfrdieiaak egnsralltl
      301 rmftgqicny igayasamng cdallftagv gensplirkm vteqlsylgv tcnvtknnag
      361 dmiisnddea vkvciiptne elmiardvek ytkqtis
//
LOCUS       WP_003771813             327 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Listeria].
ACCESSION   WP_003771813
VERSION     WP_003771813.1
KEYWORDS    RefSeq.
SOURCE      Listeria
  ORGANISM  Listeria
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae.
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
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Listeria"
                     /db_xref="taxon:1637"
     Protein         1..327
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=36648
     Region          1..317
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mirfdnvskk ysddktavnn vtldikdgef fvfigpsgcg ktttlkminr liplttgtiy
       61 inekrisdyd ihelrwdigy vlqqialfph mtieeniaiv pelkkwskek ihdritelld
      121 svgldaesyr hrkpaelsgg eqqrvgvvra laadpgiilm depfsaldpi srqrlqqdis
      181 tlqkkikkti vfvthdmqea lalgdricvm qdgeivqvat pqeivknpen dfvkdflasg
      241 hafntpiles sftvndliea dlfyayqasd gtmgissnep venlvrriae eqsvpvkdet
      301 gqfigtitnk hvmqflarhl essgelv
//
LOCUS       WP_003771892             200 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Listeria innocua].
ACCESSION   WP_003771892
VERSION     WP_003771892.1
KEYWORDS    RefSeq.
SOURCE      Listeria innocua
  ORGANISM  Listeria innocua
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 200)
  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   2  (residues 1 to 200)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Listeria innocua"
                     /db_xref="taxon:1642"
     Protein         1..200
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21958
     Region          <54..>99
                     /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"
     Region          80..199
                     /region_name="comE"
                     /note="comEA protein; TIGR01259"
                     /db_xref="CDD:213597"
ORIGIN      
        1 mmellkkhkn yfligiailc agviyisipt sqtdkvtanq alnteekpqk egkknvthiy
       61 idikgavrtp gvyklpvdar vqdvvkvagg ltedadnskl nlaeklkdem siyvykngea
      121 gseevvkddi essetdkkvn insatkvdlq qvpgigdska taiieyreke glfqtiedlk
      181 nvtgigektv eklkeyldvn
//
LOCUS       WP_003772307             356 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Neisseria
            elongata].
ACCESSION   WP_003772307
VERSION     WP_003772307.1
KEYWORDS    RefSeq.
SOURCE      Neisseria elongata
  ORGANISM  Neisseria elongata
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Neisseria elongata"
                     /db_xref="taxon:495"
     Protein         1..356
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39940
     Region          1..346
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msitienlnk hfgafhalkn inltaptgkl tsllgpsgcg kttllriiag lenaddgkil
       61 fdgqdvtakh vrerkvgfvf qhyalfrhmn ifdnvafglt vlprsqrpse kqirskveel
      121 lklvqlphla ksyphqlsgg qrqrialara lavepkllll depfgaldak vrkelrtwlr
      181 dihhelgits ilvthdqeea levsdqivvm nhgkieqvgn aatlyrqpnn afvteflgnt
      241 dafegciekg ewrygefawp ldrqyrwqeq havgyirphe wetnaqnpml agtiatihvs
      301 galthltltl pegrqvhvdf atsetgrlnl higcelklsp rqvyvfgqse lidyai
//
LOCUS       WP_003772572             249 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Listeria innocua].
ACCESSION   WP_003772572
VERSION     WP_003772572.1
KEYWORDS    RefSeq.
SOURCE      Listeria innocua
  ORGANISM  Listeria innocua
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 249)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Listeria innocua"
                     /db_xref="taxon:1642"
     Protein         1..249
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=28415
     Region          6..238
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mdissteiwd airrnsflly yqpkvdaktn eligfeglir lktattilap adffediall
       61 natremqdfv aetaieqinq lggrfsisin ipahyvvssn ymtflydyvk ehlkypecle
      121 ieiiergeit elavadknlr kikklgvtvs mddfgkgyss laylrslpid ivktdmsfia
      181 llktdrkqqi iiqaivnlch dlggkvvteg vedieqvktl remkvdyfqg yyfsrplpmk
      241 eikekysiv
//
LOCUS       WP_003774595             209 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Neisseria elongata].
ACCESSION   WP_003774595
VERSION     WP_003774595.1
KEYWORDS    RefSeq.
SOURCE      Neisseria elongata
  ORGANISM  Neisseria elongata
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 209)
  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 209)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 209)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Neisseria elongata"
                     /db_xref="taxon:495"
     Protein         1..209
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23298
     Region          1..208
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 maahlddqqe lenfkyfwrs kgrwlfvvll laslvylgwv lyqghiktkn eeaatalagl
       61 vekaktsqdk qslqadlsil qqnypesiss aqatmmvaad lfdqgqyeaa ekqlnwvlqn
      121 qqipfvrala iqrlatvqlq qkkydaalat lqmpvdaafe aliletqgdv lyaqgknkea
      181 lavyeqalak tvqdapglql lqlkadelr
//
LOCUS       WP_003776339             397 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Alloiococcus otitis].
ACCESSION   WP_003776339
VERSION     WP_003776339.1
KEYWORDS    RefSeq.
SOURCE      Alloiococcus otitis
  ORGANISM  Alloiococcus otitis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Carnobacteriaceae; Alloiococcus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Alloiococcus otitis"
                     /db_xref="taxon:1652"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42942
     Region          2..395
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msktisinag ssslkwklfe mpdevvvasg iveriglpds iftikygdgq kyettadiqd
       61 hevavemlle qltelniies fdeitgvghr vvaggekfse stlidddviq aiedlaefap
      121 lhnpanatgi kafkkvlpdi tsvavfdtsf htsmpkknyl ysipmqyyek hnarrygahg
      181 tshryvsnra aeiigqpied lkivtahlgn gasitavdgg ksvdtsmgft plagvtmgtr
      241 sgdidpsllp fimrkegiad inemvrilnn esglkglsgv ssdmrdiesa aaegnedaqv
      301 aldifndrvr kyigqyaatm ngidvlvfta gigenaanvr qavadglsfl glkvdpdknd
      361 vrgeeriist ddskvkvlli ptdeelmiar dvealkd
//
LOCUS       WP_003776706             389 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein, partial [Neisseria macacae].
ACCESSION   WP_003776706
VERSION     WP_003776706.1
KEYWORDS    RefSeq.
SOURCE      Neisseria macacae
  ORGANISM  Neisseria macacae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Neisseria macacae"
                     /db_xref="taxon:496"
     Protein         <1..389
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
     Region          65..313
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 yisvrdnlli gngtradtyg rekgsidfee ehgaiknvkv enniiadnls dtaitktlpi
       61 sngkgialsg nniignaavs apsavdhpek vtsitrqels nipdqnyyya nettgfksvs
      121 vtyitgtags dsikgtdgid hidgksgddn iyagggndtv fvsggtnfis ggdgddivrg
      181 gdgrdtvngd sgndvifgng gddhlnggag ndtlfggenn dvfygesgkd vlyggsgddl
      241 lfgglnddil yggagndtyv fcfgeghdti sdnhgnnalq fgqgiavkdl hihastdang
      301 sidwkitian sggkitidnq ylkgsntaav gefrfdegtf tvetlldkls asgqtggfet
      361 vnsgvgsfsy ssdtanvqhy davtqptil
//
LOCUS       WP_003777813             267 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Alloiococcus otitis].
ACCESSION   WP_003777813
VERSION     WP_003777813.1
KEYWORDS    RefSeq.
SOURCE      Alloiococcus otitis
  ORGANISM  Alloiococcus otitis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Carnobacteriaceae; Alloiococcus.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Alloiococcus otitis"
                     /db_xref="taxon:1652"
     Protein         1..267
                     /product="formate/nitrite transporter family protein"
                     /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=29325
     Region          14..255
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 meerletksd fikkvaastr kkeelfdqsk ahyfvramya gamlvfatag gayaadalnk
       61 inpnlgkfgf afifafglvw ilylhhelvt snmmyltasc yhkiitppka lsillfctlg
      121 niagavlagl ligntspfqa ltadsfiltv ldgkltkevg lifleaiaan ifvniailgf
      181 iltksemaki fmvltaiflf vylsyehvva nfaitgiawf tnvgvsyslg hilftwlvaw
      241 lgnyvgggli mglvygwynd dqlsyrd
//
LOCUS       WP_003775953             192 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Neisseria].
ACCESSION   WP_003775953
VERSION     WP_003775953.1
KEYWORDS    RefSeq.
SOURCE      Neisseria
  ORGANISM  Neisseria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Neisseria"
                     /db_xref="taxon:482"
     Protein         1..192
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20942
     Region          2..188
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mtrrliigis gasgfqygvk alqllrahdv ethlvvskga emtraletgy tkeevyalad
       61 vvysvnhige riasgsfktd gmliapcsmr tlasvahgfg dnlltraadv vlkerrrlvl
      121 mvreaplnla hienmrrvte mggiifppip amyqqpqtid diithsvaha ldmfgieteg
      181 vprwnggqte ad
//
LOCUS       WP_003778776             357 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Neisseria].
ACCESSION   WP_003778776
VERSION     WP_003778776.1
KEYWORDS    RefSeq.
SOURCE      Neisseria
  ORGANISM  Neisseria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Neisseria"
                     /db_xref="taxon:482"
     Protein         1..357
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39972
     Region          1..347
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msitiqnlnk hfgnfhalkn inlnvptgkl vsllgpsgcg kttllriiag lenadggnil
       61 fdgqdvtakh vrerkvgfvf qhyalfrhmn vfdnvafglt vlpkserpsk eqirakveel
      121 lklvqlshla ksyphqlsgg qrqrialara lavepkllll depfgaldak vrkelrtwlr
      181 dihhnlgvts ilvthdqeea levsdeivvm nhgkieqtgs aeaiyrkpen afvteflget
      241 dafegriekg iwhyngfawk ldaqykwqeq tatgyirphe wqlaaehetp miraeiekih
      301 avgalthvlv khgkqdvhit lagsdasrld lsagrelalv pkqvyvfsqn elieysi
//
LOCUS       WP_003776639             136 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Neisseria].
ACCESSION   WP_003776639
VERSION     WP_003776639.1
KEYWORDS    RefSeq.
SOURCE      Neisseria
  ORGANISM  Neisseria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Neisseria"
                     /db_xref="taxon:482"
     Protein         1..136
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14660
     Region          5..136
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mpliyaylgl aasaftsati lpgtseaafa afiynypeqa ygawlcagla nglgsmvsyw
       61 mgrlipskkr ssektlrllr rwgtlpllfa wlpvigdalp iaagwlrlnp ytsalmlltg
      121 kilrygiila gikgmm
//
LOCUS       WP_003779491             162 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Neisseria macacae].
ACCESSION   WP_003779491
VERSION     WP_003779491.1
KEYWORDS    RefSeq.
SOURCE      Neisseria macacae
  ORGANISM  Neisseria macacae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Neisseria macacae"
                     /db_xref="taxon:496"
     Protein         1..162
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=18165
     Region          17..130
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkcpvyfskg ggmkeiqrgf slsqlvftiv mvgiltsiay psyqkyvent klqevraamm
       61 enarflerfy qkngsfkqss tqwpdlpike igdfcikvqg dakgtpdgrf tlkavarsdq
      121 npkvlkines fvtvscette stcedktqhf antdksckif es
//
LOCUS       WP_003779864             263 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Neisseria].
ACCESSION   WP_003779864
VERSION     WP_003779864.1
KEYWORDS    RefSeq.
SOURCE      Neisseria
  ORGANISM  Neisseria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Neisseria"
                     /db_xref="taxon:482"
     Protein         1..263
                     /product="formate/nitrite transporter family protein"
                     /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=28038
     Region          8..259
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 masrdlypqe ilqvvldksc akaqssvstl avlsvlaggy igfgylaylk vvsgiphewg
       61 glatllgaam fpialicill gggelvtsnm mimslgrlag ristkmllrn wvvvclgnla
      121 gtlamafflg hyvgmtegsv aektiavaea kvhmdfgraf vsavacnwmv cmgawlhfaa
      181 khtagrmlai wfpvmifvln gfqhlvanmf iipagilaga ditwgqfffn mipvflgnvl
      241 ggasfvgasy lytykdtlkd cae
//
LOCUS       WP_003774390             239 aa            linear   BCT 20-JAN-2025
DEFINITION  YaaA family protein [Erysipelothrix rhusiopathiae].
ACCESSION   WP_003774390
VERSION     WP_003774390.1
KEYWORDS    RefSeq.
SOURCE      Erysipelothrix rhusiopathiae
  ORGANISM  Erysipelothrix rhusiopathiae
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Erysipelotrichaceae; Erysipelothrix.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Prahlad,J., Yuan,Y., Lin,J., Chang,C.W., Iwata-Reuyl,D., Liu,Y., de
            Crecy-Lagard,V. and Wilson,M.A.
  TITLE     The DUF328 family member YaaA is a DNA-binding protein with a novel
            fold
  JOURNAL   J Biol Chem 295 (41), 14236-14247 (2020)
   PUBMED   32796037
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Liu,Y., Bauer,S.C. and Imlay,J.A.
  TITLE     The YaaA protein of the Escherichia coli OxyR regulon lessens
            hydrogen peroxide toxicity by diminishing the amount of
            intracellular unincorporated iron
  JOURNAL   J Bacteriol 193 (9), 2186-2196 (2011)
   PUBMED   21378183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006857
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Erysipelothrix rhusiopathiae"
                     /db_xref="taxon:1648"
     Protein         1..239
                     /product="YaaA family protein"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=27649
     Region          2..236
                     /region_name="YaaA"
                     /note="DNA-binding protein YaaA associated with the
                     oxidative stress response [Replication, recombination and
                     repair]; COG3022"
                     /db_xref="CDD:442258"
ORIGIN      
        1 miilvsptkt qkensqdyie nslfpeiksk llaslqaltr deikasmhvs dkiadtvyqn
       61 yqsfsestpa ilsyqgssfk nmnrelwshe dyqeaqkrly ifsalyglsk cssavgryrl
      121 dflmklnmdl yqiwkqpitd ylnnlnqplv nlasseyssm idmntlsvpm itldfkeqig
      181 dsyktkstyv kiargkmvsy liqnriqsfn dikkitfddy tfntelstde tyiftrkes
//
LOCUS       WP_003781174             159 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Kingella denitrificans].
ACCESSION   WP_003781174
VERSION     WP_003781174.1
KEYWORDS    RefSeq.
SOURCE      Kingella denitrificans
  ORGANISM  Kingella denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Kingella denitrificans"
                     /db_xref="taxon:502"
     Protein         1..159
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=17530
     Region          1..102
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mnqftkktta rgftlielmv siallailai iaypsfatyv qntrienara smldaihsle
       61 rqyaqkpqfs taninditne yydlefhnin dssyyltakp ksgvfsdsvl asvpmniyyd
      121 sitatfsrcs esglntavqe aqtkkpsttn sntgcrpls
//
LOCUS       WP_003782271             209 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Actinomyces naeslundii].
ACCESSION   WP_003782271
VERSION     WP_003782271.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces naeslundii
  ORGANISM  Actinomyces naeslundii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 209)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Actinomyces naeslundii"
                     /db_xref="taxon:1655"
     Protein         1..209
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=21131
     Region          119..207
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 msvsnydype defdvgeddg pvpvgvhraq vprwrswvpl laiiiivpal awgavtlfln
       61 gsggsspsga asstqqaksg qankqasgdk taeaskpsas asagasasas gnidfntgvt
      121 vangtetsgl akgagdkltn ggftavevvp giyentepak stvyfsspes rpaaeevgkk
      181 lgisnvvegt aentqgstia vilrddykp
//
LOCUS       WP_003782358              97 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [Actinomyces].
ACCESSION   WP_003782358
VERSION     WP_003782358.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces
  ORGANISM  Actinomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Actinomyces"
                     /db_xref="taxon:1654"
     Protein         1..97
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10732
     Region          6..94
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mtidtkalae acarfgvarl rvfgsvltdh fdphtsdidf lvdfqagrnd rfadffglqd
       61 eltrifgrki dlvvaesvkn pyfkssvlrg aedvyaa
//
LOCUS       WP_003784382             170 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Kingella denitrificans].
ACCESSION   WP_003784382
VERSION     WP_003784382.1
KEYWORDS    RefSeq.
SOURCE      Kingella denitrificans
  ORGANISM  Kingella denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 170)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Kingella denitrificans"
                     /db_xref="taxon:502"
     Protein         1..170
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18699
     Region          12..166
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mtptptlpeh ftkaeryqai lpqiegllra nadlwtanla ninallaetf gwfwvgfylv
       61 dntgtelqls tfqgpvactr iahnkgvcgq awaqgktliv pnvhehpghi acssrsqsei
      121 vvplrnrrgh iigvldidse qlnqfdetda qylqqicaml peiltapeia
//
LOCUS       WP_003785984             156 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Kingella kingae].
ACCESSION   WP_003785984
VERSION     WP_003785984.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..156
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=17065
     Region          1..107
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mktfiqttqr gftlvelmvs iavlailami aypsystyme rvridnarat mmdtiqfaer
       61 yyatnktfaq ldtakikaag iandkydley vavgannyll katpkadlys akkrasspln
      121 vlyssqsgvf vrcndsdfai aavaepkgtt ncepls
//
LOCUS       WP_003777066             922 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Neisseria].
ACCESSION   WP_003777066
VERSION     WP_003777066.1
KEYWORDS    RefSeq.
SOURCE      Neisseria
  ORGANISM  Neisseria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae.
REFERENCE   1  (residues 1 to 922)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 922)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 922)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..922
                     /organism="Neisseria"
                     /db_xref="taxon:482"
     Protein         1..922
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=97501
     Region          <33..201
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          255..462
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          426..674
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mdtkqvfrai vseeaaahsa slekssepkv fqgtkgndvy yathtadniv ekanegqdtv
       61 ysnvsytlpn nvenlvltgs dniygagnns dnvlvgnsgn nrlysgrgnd tvyggaghdn
      121 inggegddql fgdegndild gaagndvlqg gegndtylfg eksgndtvid rqgsnsirfl
      181 dglsaddltv tavrnaeggq dwriavkhtq svltisnqyq egsnmpsvqr fvfangtlnl
      241 nqfikatqaq veirdnager iegtdgndal ngtvgndvid gkagadmmrg gigddtyyvd
      301 nakdvvvens gegndtviss vsytasthve nvtltgnani yaagnnsnnt ltgnsghnrl
      361 nsgrgndtvy gmggndning gdgndyldgg dgndtingda gddtliggag kdmlkggtgn
      421 dtyiygsddt iidnqgnntl kfsddlrvsd ikvnvidnad gsknweitsa ngsatiqnqv
      481 dakghisinq fqflgenyta etllkavntg kadqgikneg tpnddvivgs kfndelssgt
      541 dgrdviygmd gddiirdegt tywgnewssd dklyggngnd klyarvgady ldggagddyl
      601 eggdgrdtyv fgkgyghdti fdfgfdidee fnptsisnav kftggltldd lnisvtpgyd
      661 ktgidytpdp fdytinprln gntwtvsikg sndvltiknq mgsqgaisef qfdngtyste
      721 qiiehfglkv shvrkdgtii qylnddsdtf eqrlyegsnr iihgtdngdt vsvsgnyggk
      781 ttfiggsgdd tvkvghdsti dagagndtis ggsyantitf gkgsghdkls lnasgedntv
      841 lfsgnltlkd idleinkagn nkenwvvklk gsddtltvld avhssdggdt vdafkfaasg
      901 etysmsqflt alghdtahqg vl
//
LOCUS       WP_003788484             586 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Kingella kingae].
ACCESSION   WP_003788484
VERSION     WP_003788484.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..586
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=66868
     Region          81..484
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 madkvpkkak kfvlnaitas qpasqpasqp asqlytkltr krqeiffnqt lafdeidrlf
       61 dakafskfsr ytadgkqpvg eikrhsdgfl kgvpaenlii kgnnlialhs lakqfkgkvk
      121 liyidvpfnt endsfvyndk fthstwltfm knrleiakkl lsddgiicvh tdnteaayvq
      181 vlldeifirn nflnhititt naasgfkatg qtifstsnhi fvyarnrvns qlnklylskq
      241 ydenykyfll npdehfsnwk fstileqlsi elklsekemk shiteqellf kisefadknr
      301 drvfrtaais ggalkkrqki inhsknnkgi vfqhenedvt gfyilngeqm vfwentyrni
      361 dgnfipatii idvwtdisft giaseggvkl kngkkpekli kriielttne ndivldyhlg
      421 sgttaavahk mnrqyigieq mdyietlave rlkkvingeq ggiskavnwq gggefvyael
      481 apfnetakqq ilacesagcl kalfedlceh yflkynvsvn efnqiinepe fqtlpldeqk
      541 qmvlemldln qmyvsysemn daqfsgclnd edkalnrqfy qdgeke
//
LOCUS       WP_003790041             382 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Schaalia dentiphila].
ACCESSION   WP_003790041
VERSION     WP_003790041.1
KEYWORDS    RefSeq.
SOURCE      Schaalia dentiphila
  ORGANISM  Schaalia dentiphila
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 382)
  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 382)
  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
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 382)
  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   5  (residues 1 to 382)
  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   6  (residues 1 to 382)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 382)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 382)
  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 11973053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Schaalia dentiphila"
                     /db_xref="taxon:3050224"
     Protein         1..382
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38716
     Region          <10..49
                     /region_name="COG3398"
                     /note="Predicted transcriptional regulator, contains two
                     HTH domains [Transcription]"
                     /db_xref="CDD:442625"
     Region          78..367
                     /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 mathdvdetv ltligsgqad trpaivkqtg lapstvsaav srlveagvia eaehsvstgg
       61 rrarrlvtsd gagalalvel gahhglialt dptrgvgqas sllidiaegp qavldavide
      121 vsrqeesagv rvggialavp gpvdaersrv irparmpgwd ginvaeavte qcglpalien
      181 daragaiges vyrrrlqgvt pidtliyvka gsaiggaylv dgvpqvgqgg lagdishipv
      241 eaaagrpckc gnvgcletia sadsiradla aaglvyenna qllaaardgi pevatairqa
      301 gtllghcvah lvsflapqgv ivggalsavd aftagvraal hqsclpsime hlviessrsg
      361 reaalwglst ltpskisken rs
//
LOCUS       WP_003783297             267 aa            linear   BCT 20-JAN-2025
DEFINITION  YaaA family protein [Actinomyces naeslundii].
ACCESSION   WP_003783297
VERSION     WP_003783297.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces naeslundii
  ORGANISM  Actinomyces naeslundii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Prahlad,J., Yuan,Y., Lin,J., Chang,C.W., Iwata-Reuyl,D., Liu,Y., de
            Crecy-Lagard,V. and Wilson,M.A.
  TITLE     The DUF328 family member YaaA is a DNA-binding protein with a novel
            fold
  JOURNAL   J Biol Chem 295 (41), 14236-14247 (2020)
   PUBMED   32796037
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Liu,Y., Bauer,S.C. and Imlay,J.A.
  TITLE     The YaaA protein of the Escherichia coli OxyR regulon lessens
            hydrogen peroxide toxicity by diminishing the amount of
            intracellular unincorporated iron
  JOURNAL   J Bacteriol 193 (9), 2186-2196 (2011)
   PUBMED   21378183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006857
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Actinomyces naeslundii"
                     /db_xref="taxon:1655"
     Protein         1..267
                     /product="YaaA family protein"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=27795
     Region          2..241
                     /region_name="YaaA"
                     /note="DNA-binding protein YaaA associated with the
                     oxidative stress response [Replication, recombination and
                     repair]; COG3022"
                     /db_xref="CDD:442258"
ORIGIN      
        1 mlillppseg ktapssgpsl alaslldaer ltaprrtvms alaevsrgpd aasvlglgpr
       61 saeqtrtnlw letspcapah qlftgvlyea akldsiaaqt tgrgtlerhc vifsglwgvl
      121 spidpvpdhr lsmgtslpgp grlpsfwkph lapvlkdrga pglvvdcrsa dyaaawkpsa
      181 sdgveimtvr vvrvandgsr kvvshmakqa rglltgalls avaagtlspd ahaddvaala
      241 arlnsvddve vseadrqgrl vltlvtr
//
LOCUS       WP_003786171             281 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Kingella kingae].
ACCESSION   WP_003786171
VERSION     WP_003786171.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..281
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30268
     Region          2..275
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 midlhchstv sdgalppdev valaaqngct mlaltdhdht gglaiarata qqhgirfing
       61 veisvtwrgr gvhivgldfd ehesslqtll arlrlgridr ieqigaklak hgiagaaega
      121 lalatnremv srthmadwlv qqglvrnkqa aftkylgdgk cgfvrhqwad laetvqainq
      181 agglaviahp mrydmsatar rqlfeefkql ggvgievhsg gcslgdrlny amlaerygll
      241 ssvgsdfhra ndysggtlga cpelppicda iwtrfrnhsi i
//
LOCUS       WP_003791263             440 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Schaalia dentiphila].
ACCESSION   WP_003791263
VERSION     WP_003791263.1
KEYWORDS    RefSeq.
SOURCE      Schaalia dentiphila
  ORGANISM  Schaalia dentiphila
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 440)
  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 440)
  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
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 440)
  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   5  (residues 1 to 440)
  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   6  (residues 1 to 440)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 440)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 440)
  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 20650276
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Schaalia dentiphila"
                     /db_xref="taxon:3050224"
     Protein         1..440
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44945
     Region          49..90
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          114..430
                     /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 mptrsdsand agrisrgpva sprpsergmg aqnrgvksen vrasnmstvl rnilaspgev
       61 traglsqrtg mtratisrlv ddlvgaglvr elepgdgggr grpanrltpa egsavalgve
      121 vdvasldvtl vdiagrelgh rrierdfads apeetmalaa reahallegt lpdgalflgt
      181 gvglpglvsp trlalapnlg wrdiphdqll apladlnpvv vaneadlaay avaytrpgva
      241 ggpstfvyvs gevgvgagvi vdhrpmsgar awsgeighmc adpngplcrc gargcleaym
      301 gvralaehvg aptgsgarei lrcaglvdea gvkasgslgv gaeqerarav laeagvalgr
      361 vlsgvinamd iphvvlggav aelsgalldp areeietrtl qapwsspive vlpdsasltv
      421 rgaafrvlds lvddpaafls
//
LOCUS       WP_003791686             166 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Kingella kingae].
ACCESSION   WP_003791686
VERSION     WP_003791686.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 166)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..166
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18439
     Region          8..163
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mhethiapna skteryqtiv paieallssd rdlfiaglan vnallketfg wlwvgfylvd
       61 eqrtelqlsa fqgpvactri ahgrgvcgqa waqnrtivvp dvnqhpdhia cssrsqseiv
      121 vplynqrqqi igvldadaeq inqfdeidae ylqqicqvit knllaq
//
LOCUS       WP_003791731             156 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Kingella kingae].
ACCESSION   WP_003791731
VERSION     WP_003791731.1
KEYWORDS    RefSeq.
SOURCE      Kingella kingae
  ORGANISM  Kingella kingae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Kingella kingae"
                     /db_xref="taxon:504"
     Protein         1..156
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=15801
     Region          1..145
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mktmqkgftl ielmiviaii gilaaialpa yqdytkrsrv seglslagga ksalteyyas
       61 nnewpadnaa agiatsitgn avksvvasrs atgaagkgli tvtfnnkvtd gatlimegeg
      121 ndagsvkwtc tggslvtkyr psecrgtgta nsstgs
//
LOCUS       WP_003791810             338 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Schaalia dentiphila].
ACCESSION   WP_003791810
VERSION     WP_003791810.1
KEYWORDS    RefSeq.
SOURCE      Schaalia dentiphila
  ORGANISM  Schaalia dentiphila
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 338)
  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 338)
  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   3  (residues 1 to 338)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Schaalia dentiphila"
                     /db_xref="taxon:3050224"
     Protein         1..338
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37541
     Region          226..336
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mkqedrgnda pfilnavera iirvprsshh gltkipaavn iagktyldla rltdidtrql
       61 pqvvlaarlf hlththramv itgqcalwvh gygsdpvlpp itvatrssir pisipsttig
      121 phsfpsvtvk pthvhhlpra dnargllien leaaqitvar tspnqraafa qicvignaft
      181 hfdnfrlrds rrhekywkel lsaeltrlgn gargrsqaqw iithadagca spgearvlye
      241 lcaadltgmr tqvevhtrgr ryfidcafpa ekvgiefdgr akygddarsi hsslsrerer
      301 qrhleaegwh iirvgwhdle hpdeliaqvr aalaarlg
//
LOCUS       WP_003792294             118 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Schaalia dentiphila].
ACCESSION   WP_003792294
VERSION     WP_003792294.1
KEYWORDS    RefSeq.
SOURCE      Schaalia dentiphila
  ORGANISM  Schaalia dentiphila
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Schaalia dentiphila"
                     /db_xref="taxon:3050224"
     Protein         1..118
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=13001
     Region          1..92
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(24,51..52,54)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mgeelveavl rvveeipegr vatygmiara vgtgprvvgr imhdwgggvp wwrvvsvhgt
       61 fpttvrgegf seweregiph dptrgkvlik ecvveqdwln avarpiienm qnnaelsd
//
LOCUS       WP_003792614             405 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Schaalia dentiphila].
ACCESSION   WP_003792614
VERSION     WP_003792614.1
KEYWORDS    RefSeq.
SOURCE      Schaalia dentiphila
  ORGANISM  Schaalia dentiphila
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 405)
  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 405)
  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
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 405)
  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   5  (residues 1 to 405)
  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   6  (residues 1 to 405)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 405)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 405)
  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 11513089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Schaalia dentiphila"
                     /db_xref="taxon:3050224"
     Protein         1..405
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41889
     Region          4..>59
                     /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"
     Region          74..355
                     /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 mhyptrrplp tledrivahl akapatrsql cealdtsrtn lgralttlld egsvtpvrtn
       61 apgrgrptql ltlnssaahc vglnvtrtsc agvmlsragt vlaavhiisp aspslqlsle
      121 qtcealaasa arqgidtstv ravgvgvpip mgrnarlssd ayptmeelse ltrrwwaplp
      181 ivdntvrmaa laealwgaga dmssfiylrl sggvggcvvs dfrlvggagg lagelghmtv
      241 gandspcacg krgcletlas vpalceragv adiaqlraav lsgdtrarea leratqavgy
      301 vlgsaallin praiivagei vdafpslrsd iaaamhreli pvmewdidvv gaslgplgaa
      361 qasayiaarp feedtaaarl peegsplevg passmevrtd hggrp
//
LOCUS       WP_003784096            1531 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Kingella denitrificans].
ACCESSION   WP_003784096
VERSION     WP_003784096.1
KEYWORDS    RefSeq.
SOURCE      Kingella denitrificans
  ORGANISM  Kingella denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 1531)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 1531)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 1531)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1531
                     /organism="Kingella denitrificans"
                     /db_xref="taxon:502"
     Protein         1..1531
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=164444
     Region          630..663
                     /region_name="HemolysinCabind"
                     /note="RTX calcium-binding nonapeptide repeat (4 copies);
                     pfam00353"
                     /db_xref="CDD:459777"
     Region          <773..>940
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          902..936
                     /region_name="HemolysinCabind"
                     /note="RTX calcium-binding nonapeptide repeat (4 copies);
                     pfam00353"
                     /db_xref="CDD:459777"
     Region          <1037..>1126
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          1197..1446
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mimsnidisd ytllaeasya dfslsydkes gtypeklkdk ngkevgtkqa itelgkpgmv
       61 dkiintatfn sednskstte qfaeyltdky evaahwkdrg dfftsadkdq ssgfsgtlfk
      121 skiseqyvla lrgteggkdl fitdggdivn dglahhqivd mynfwqqita qkgkpydvmy
      181 vetlgqiydv alekineakl dgavgfftds stvkmikkir sdklykmgde rrfglgihvd
      241 kvtttghslg ghlsaafsrl fpdkvehsym vngagfgaks npisylfsns qdnissvfsa
      301 ldgadhfdka kitnligdkn idvvannwfi glsqpgktpe lfieeagigk ifghaagsms
      361 dtmqaaslff amdgklnqtd lsealktlnp vfkavtndde etlekvvyqi gkllgdkvpg
      421 qaatrnelye riaslkallt gkkdvgeled aqggkyqfvs latdagswkd dvsqnsdkgt
      481 alryalreln pfavvgadyt ahnrhgnlnl ysienpygmt ntylqhraam lawknainta
      541 nvsysddfga infnyteiis aiaaaatspl aplttaiasa isllpadlkg dwtyedksgn
      601 lsfhidgknl tdlsnhyvrf gsdtidelkg gdledylfgg gnidtldgge gddymeggqg
      661 ldtyiikdhd tvfdsdmqgk ilfdnggkpi qidrfesdge qnpviwhspd rqftavrygk
      721 dlivstksdk sdkvtvkdff kiakdngkgg ltglgieldk aellkpgmqn kltgianryn
      781 nfhansggyt eiiggslsdt vfatssgiwa emgdgndrvy gsmsadmidg gdgndilngs
      841 sfvpagtdkp qaeldkdadi iiggnghdli igmagddtiy tgkkdehket kptgmrgdwa
      901 lghlgddtiy gsrgqdflqg gegsdiihgg adddvilgds firfssrtvl ekgvipdaiv
      961 vpkyeystig venlpgkaig fthnaqtdkl iaeyavsips pqsfewslsi dkekgdyvld
     1021 tpkgiplsnd qhlvekngaa dylyggtgnd liigqtgddf lfgekgndil wgddnrdlsv
     1081 agndyldgge gndtlygglg ndtltggtgs ntldggegfd tyvitgeefa qttatpaekk
     1141 shniirdsdg qgkilvqdid lgslhwqlnk gtgkwsargq eialaqngnd llvqnkdgit
     1201 vatvsnfqng hlgitlpgfa aqtdkpqsep aptpqpvqpq pvqpqpvqpq pvqpqpvqpq
     1261 pvqpqpvqpq pvqpqpvqpq pvqpqpvqpq pvqpapatqt vieggsgnet fhadvsgslv
     1321 karggndwvh gsdgddtlig gagndvlygq aghdelyged gddrlyggeg ddklaggrgs
     1381 dylaggagsd ryvfernfgk dfvmnldtsp dstdtlritd gytpddftfk rdgdnlvite
     1441 kadsgneitv hkhfsadyrg ayaidrivfd nqkvldtqav nalvrqdaal anaanhmvqa
     1501 magfgagsga tagnlmqnaa hqplllaass v
//
LOCUS       WP_003793052             533 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Schaalia dentiphila].
ACCESSION   WP_003793052
VERSION     WP_003793052.1
KEYWORDS    RefSeq.
SOURCE      Schaalia dentiphila
  ORGANISM  Schaalia dentiphila
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Schaalia dentiphila"
                     /db_xref="taxon:3050224"
     Protein         1..533
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=56020
     Region          24..532
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mkraivvvcs waaalclaaa ylaigwgidd iaghnawstw wigvlgalgs gvfawavsal
       61 gaaqmnqmep alrhsmirqv falgpsqrtn eragrvvnsa tdgvervaay kgiflapmia
      121 slttpilvvi lvamtiepas ggflaiaipl vpicvmgfrk afkpvssryr hasrqlaake
      181 ldaiqglgdl almnagkdmg krlaeaaeev rskvmsylag nqlillvids vfslgmitga
      241 itlaliryqq gaisvgegis lvllssimld pldrigqffy igmggiaank eikkfikqtp
      301 pvtdakgvka paippqrgei rlsgvsfsyt edtpvlqgan ltltqgehva lagpsgagks
      361 tisallqgfl rptrgrvsln gvdlasapls wvraqtavve qstylfsgtl rdnlllaapa
      421 atddqlieal raahlgefvd tlpggldarv garglavsgg eaqriaiara flknasimil
      481 deptahvdla sereilasle tvcagrttlt ishrdatikg adrvatlqeg tir
//
LOCUS       WP_003794581             447 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Kingella oralis].
ACCESSION   WP_003794581
VERSION     WP_003794581.1
KEYWORDS    RefSeq.
SOURCE      Kingella oralis
  ORGANISM  Kingella oralis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 447)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 447)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Kingella oralis"
                     /db_xref="taxon:505"
     Protein         1..447
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=50308
     Region          52..429
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mqpenltlqi fhhqqwhdaa elsfdasfvc thldylndya fcqdengdfl cwekddsyal
       61 glnypvnimg yqnqpftlld diipagasrr ywvqhlgiar qpenqqnytl lqrgtiapig
      121 nvrikqavph eaatrhfqaa eainrqadfl eyaqehgaia ggatgaggea pklllrqtps
      181 gevwidnqqd gksadayylv kyprnqrtpi dcdilraefy fyhelaalgf atintrqmkl
      241 eegehypslw lprfdveqaq gqtvrlames vysllergag sylnhgetlr aivrkiqhsh
      301 lvqaqgfqld agawisqwlq rdllniafgn sdnhgrntaf irragsiefa pvydfapmka
      361 dpegiirstt wgaplengge ydfsaiaqsf adladpdall aelqstaekl ldlkhrlhqr
      421 gvpsrilema glgydylpek lkrwgll
//
LOCUS       WP_003795387             270 aa            linear   BCT 20-JAN-2025
DEFINITION  YaaA family protein [Schaalia odontolytica].
ACCESSION   WP_003795387
VERSION     WP_003795387.1
KEYWORDS    RefSeq.
SOURCE      Schaalia odontolytica
  ORGANISM  Schaalia odontolytica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Prahlad,J., Yuan,Y., Lin,J., Chang,C.W., Iwata-Reuyl,D., Liu,Y., de
            Crecy-Lagard,V. and Wilson,M.A.
  TITLE     The DUF328 family member YaaA is a DNA-binding protein with a novel
            fold
  JOURNAL   J Biol Chem 295 (41), 14236-14247 (2020)
   PUBMED   32796037
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Liu,Y., Bauer,S.C. and Imlay,J.A.
  TITLE     The YaaA protein of the Escherichia coli OxyR regulon lessens
            hydrogen peroxide toxicity by diminishing the amount of
            intracellular unincorporated iron
  JOURNAL   J Bacteriol 193 (9), 2186-2196 (2011)
   PUBMED   21378183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006857
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Schaalia odontolytica"
                     /db_xref="taxon:1660"
     Protein         1..270
                     /product="YaaA family protein"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=28374
     Region          2..219
                     /region_name="YaaA"
                     /note="DNA-binding protein YaaA associated with the
                     oxidative stress response [Replication, recombination and
                     repair]; COG3022"
                     /db_xref="CDD:442258"
ORIGIN      
        1 mliwlppseg knapsqgpsl dlnalsrasl ttsrrtvcdt ltalgdgpva aavlkvgari
       61 dlsvntalds apcatasslf tgvlyeaiee capsawsgag aahvsifsgl fgvlspsdvi
      121 pdhrlamgvs lpdlgvlstw waprldeals peaseriivd grsgpyraac kapwarvwel
      181 rveretdgkr svishdakrw rgaitgllla sdgylaeets aaekaleeaa yslslgdakg
      241 hehrvtdvey gaekqtkngg strtvtlvth
//
LOCUS       WP_003796124             151 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Kingella oralis].
ACCESSION   WP_003796124
VERSION     WP_003796124.1
KEYWORDS    RefSeq.
SOURCE      Kingella oralis
  ORGANISM  Kingella oralis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Kingella oralis"
                     /db_xref="taxon:505"
     Protein         1..151
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=16847
     Region          1..102
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkakgftlve llvviviiav lavvayplyt nyvknarlse ahqammdnaq alerhyanha
       61 nfkksstqwv dlpitqtpyf cirmlgnprg teseaaysmk avsfdknrea rvlihahdgt
      121 slvcessktt cdetpffnna mrvdsdcrpy p
//
LOCUS       WP_003797276             338 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Schaalia odontolytica].
ACCESSION   WP_003797276
VERSION     WP_003797276.1
KEYWORDS    RefSeq.
SOURCE      Schaalia odontolytica
  ORGANISM  Schaalia odontolytica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 338)
  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 338)
  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   3  (residues 1 to 338)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Schaalia odontolytica"
                     /db_xref="taxon:1660"
     Protein         1..338
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37394
     Region          226..336
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 msqevggnda pfilnavera iirvprsshh gltkiptavk iagrtyldls altdidmsql
       61 peivlaarly hlalthqtlv atgqcalwah gygcdptlpp itvsassair pivlpaiaig
      121 thtfapvkvk prhvchlpai sdirgllven lesaqitaar tsrnrraaft qmcmnahtyt
      181 hfdnfhmkas rnneeswkff lerelkqlgn rargrsqaqw iithadagca spgearvlye
      241 lcaagltgmr tqvevhtrgr ryfidcafta ekvgiefdgr akygddarsi hsslsrerer
      301 qrhleaegwh iirvgwhdld hpdelvvqvr galaarla
//
LOCUS       WP_003797474             349 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Arthrobacter
            globiformis].
ACCESSION   WP_003797474
VERSION     WP_003797474.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter globiformis
  ORGANISM  Arthrobacter globiformis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Arthrobacter globiformis"
                     /db_xref="taxon:1665"
     Protein         1..349
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=36051
     Region          15..344
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mtftlnaalh arnfdvslsl gpaetvavlg pngagkstll giiaglirpd sghavlgdkt
       61 lfnldagnsh clpphtrgta llaqepllfp hmnvlenvaf gpraaganra salqtarhwl
      121 aeveasefad rrpgqlsggq aqrvavaral atdpelllld epmaaldiha apmlrrllkr
      181 vlasrraiii thdvldalml adraivvegg riteagptrg vlekprskfa aglagmnllp
      241 giitgrglts dgglditahp edgavpgqdg vavfsptavs vflsaehgsp rnsfavtvtd
      301 lephgdqirv hagglsadit paasadlglt pgmtvyfvik ataiavypa
//
LOCUS       WP_003797942             166 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Kingella oralis].
ACCESSION   WP_003797942
VERSION     WP_003797942.1
KEYWORDS    RefSeq.
SOURCE      Kingella oralis
  ORGANISM  Kingella oralis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 166)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Kingella oralis"
                     /db_xref="taxon:505"
     Protein         1..166
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18046
     Region          33..162
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 myaiqttsas kanqyqqllp qlqaliaada diliatlanv cavlkeqfnw fwvgfylvnd
       61 srselilapf qgplactriq kgrgvcgqaw vqnqtlvvpd vnrhpdhiac ssqsqseivv
      121 plhngsgevv gvldidhtel aafdatdahy lqqlcallsr qlfqaa
//
LOCUS       WP_003799584             205 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Alcaligenes].
ACCESSION   WP_003799584
VERSION     WP_003799584.1
KEYWORDS    RefSeq.
SOURCE      Alcaligenes
  ORGANISM  Alcaligenes
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 205)
  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 205)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 205)
  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   4  (residues 1 to 205)
  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   5  (residues 1 to 205)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Alcaligenes"
                     /db_xref="taxon:507"
     Protein         1..205
                     /product="TRAP transporter small permease subunit"
                     /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=22651
     Region          3..171
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mkfflrlssl idrlntvvgk svtwltlivv lvsainavvr kvygissnqw lelqwylfga
       61 ifllaagytf fvnehvrvda vaerfpprvq vwidifgvif fllpatllif wlsipffeqs
      121 yvlneqssnt gglarwpvkl lipvgfalla lagishlikc igflrgacpn pllkngglsa
      181 eeelakeile iarandatis vskgq
//
LOCUS       WP_003800911             201 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Arthrobacter].
ACCESSION   WP_003800911
VERSION     WP_003800911.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter
  ORGANISM  Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 201)
  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 201)
  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   3  (residues 1 to 201)
  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   4  (residues 1 to 201)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 201)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 201)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Arthrobacter"
                     /db_xref="taxon:1663"
     Protein         1..201
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22299
     Region          13..199
                     /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"
ORIGIN      
        1 mseptesnkt sqparrvvva edetlirldi ieilrgegyd vigeadngek avqlaeelkp
       61 dlvlmdvkmp vmdgisaaek ivkariapvv lltafsqkel verardagam ayvvkpftpa
      121 dlipaleial srheeikale sevtdlqeqf atrklverak sllttkmglt epeafrwiqk
      181 tsmdrrlsmr evaetiinqv n
//
LOCUS       WP_003801344             282 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Alcaligenes ammonioxydans].
ACCESSION   WP_003801344
VERSION     WP_003801344.1
KEYWORDS    RefSeq.
SOURCE      Alcaligenes ammonioxydans
  ORGANISM  Alcaligenes ammonioxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Alcaligenes.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Alcaligenes ammonioxydans"
                     /db_xref="taxon:2582914"
     Protein         1..282
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30736
     Region          7..281
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 msvqaclpvd lhchsiysdg vlspaelaer ahangvklwa ltdhdeiggl kqarhhaerl
       61 gmgfvdgvei svtwanktih ivglgvnpdh eplhqalqdv ragrgqrarq mgerlaelgf
      121 pdayegavpf aanpelisrt hfarflvqqg ycadmneafr ryladgkpaa vetvwaslee
      181 avgwiresgg kaiiahpgry elddtrshal ysqflelggv gievltgshs aqeysvytqv
      241 arsygfevsc gsdfhgpreg ridlgglppl psglkpvwhe wl
//
LOCUS       WP_003802101             181 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Alcaligenes].
ACCESSION   WP_003802101
VERSION     WP_003802101.1
KEYWORDS    RefSeq.
SOURCE      Alcaligenes
  ORGANISM  Alcaligenes
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Alcaligenes"
                     /db_xref="taxon:507"
     Protein         1..181
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=19748
     Region          16..179
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mqawtsdlia wllntlslpe vglsaifivs lvsatllplg sepavfayin lapdmfwpav
       61 lvatvgntag gaisyatgla aekayeawre khpqstdede tkprnkaagr whelgqrwli
      121 rmgppallls wlpvvgdplc avagwlrlpf wpsvfymavg klgryitmta gllwifpklg
      181 w
//
LOCUS       WP_003798210             132 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Kingella oralis].
ACCESSION   WP_003798210
VERSION     WP_003798210.1
KEYWORDS    RefSeq.
SOURCE      Kingella oralis
  ORGANISM  Kingella oralis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 132)
  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   2  (residues 1 to 132)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Kingella oralis"
                     /db_xref="taxon:505"
     Protein         1..132
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13856
     Region          36..101
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mhtlkiecgf cfkslygdfi mlkklflavl aslsfsfala avdlntatve qlstlkgika
       61 kkataiveyr qkngafksvd dlknvpgigq ktvdklrsel tvgaaapaaq pkaapkpaas
      121 kadktnkada ak
//
LOCUS       WP_003787338             388 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Actinomyces].
ACCESSION   WP_003787338
VERSION     WP_003787338.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces
  ORGANISM  Actinomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 388)
  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 388)
  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
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 388)
  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   5  (residues 1 to 388)
  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   6  (residues 1 to 388)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 388)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 388)
  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 15726307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Actinomyces"
                     /db_xref="taxon:1654"
     Protein         1..388
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39823
     Region          4..>69
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          80..364
                     /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 mdylatlaps tleerivqvl asgpatrgel carldvsrtv lgraltelrq dgavrvvsyr
       61 srsegrgrpv eqlglaeria cavgldvsrt sasgiildrk gevlasvltp lsfdgwrepl
      121 delcqalkka addagvdmsy vsrigvglpv pvgqgtgpgt algedlfstv eqivspywsg
      181 sllvdntirm talaearwga gqgapeqiyv hlgggvgacv ivadrigggs tgyagelghi
      241 tvpggdrpcq cgkngcletl asapavteia gaadledlrr mldahapdav galaeasrav
      301 aqacamavll mspsrivlgg elvtacpelv pqiaadiagr lvpgtswgve vvaarldglg
      361 caqgaaaaad syvtacleea krhqrsya
//
LOCUS       WP_003799322             289 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Arthrobacter globiformis].
ACCESSION   WP_003799322
VERSION     WP_003799322.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter globiformis
  ORGANISM  Arthrobacter globiformis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 289)
  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 289)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Arthrobacter globiformis"
                     /db_xref="taxon:1665"
     Protein         1..289
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29700
     Region          1..258
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mraqldelvv salkrgsavp aftcydftta lavvsaaeeg qrgvillvap ktaatanglr
       61 lisalrglad dasvpvavql dhatdldvis aavaagadsv ladgsalpye dnialvcavr
      121 saleaqghae vvleaelggl agdedrafgt egdgagneva gltdsaqved fvartgaqll
      181 avavgnvhgk ykgeprlrwd vlqdiavrth iplvlhgasg ipadelakap amnvgkvnfn
      241 telrtgvlat leeqlpahrs dgenlqgllt rwnaaakdfg tstlailsr
//
LOCUS       WP_003804987             193 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Alcaligenes].
ACCESSION   WP_003804987
VERSION     WP_003804987.1
KEYWORDS    RefSeq.
SOURCE      Alcaligenes
  ORGANISM  Alcaligenes
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Alcaligenes"
                     /db_xref="taxon:507"
     Protein         1..193
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21220
     Region          4..190
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mrakrrlvig mtgatgavyt vrllqvlqsc pdvethlvis psgvlniqye ldidkneiqs
       61 ladqvhnfrd vgatlasgsf ptagmvvvpc smrtlaavah glsdnlitra advtlkerrr
      121 lvmlvretpf nlahlrnmta vtemggiifp pmpafylrpk siddivdhtv mrvlelfdiq
      181 vpgerwdgtq kpn
//
LOCUS       WP_003808103             204 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit [Bordetella].
ACCESSION   WP_003808103
VERSION     WP_003808103.1
KEYWORDS    RefSeq.
SOURCE      Bordetella
  ORGANISM  Bordetella
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 204)
  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 204)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 204)
  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   4  (residues 1 to 204)
  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   5  (residues 1 to 204)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Bordetella"
                     /db_xref="taxon:517"
     Protein         1..204
                     /product="TRAP transporter small permease subunit"
                     /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=21794
     Region          4..169
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mtrllellcg alraitnrac laagwalial svvialnvla rkifsfslqg vdeyggycla
       61 icasigfsqa aydrahiris vltdllpqrl racsdvfala lltsvaltla vkatgvayds
      121 ysmqalatsa lrtplaipqa mwaaalcwfg lvlatqllhs llllarrdwg ginrnygnps
      181 vdeevaeelr sanermagkl egah
//
LOCUS       WP_003808518             577 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase [Pseudomonadota].
ACCESSION   WP_003808518
VERSION     WP_003808518.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonadota (proteobacteria)
  ORGANISM  Pseudomonadota
            Bacteria; Pseudomonadati.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Pseudomonadota"
                     /db_xref="taxon:1224"
     Protein         1..577
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=64212
     Region          7..508
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mskqkleltw igkekrpkle prilledpdk syhakrrvte ndifdnrlif gdnllalkal
       61 eyeftgrvrc iyidppyntg safaqyedgl ehsiwlglir erltllrnll skdgscwiql
      121 ddneaqyckv ladeifgrdn fianvvwnks yavrsnaqff ssahehilvy akdrahlrln
      181 qfgrsakqte rysnpdndpr gpwqsvtmti slvggargrq yaktgvseni fevkspsgkv
      241 flpppnrcws rnpsgfkkld aegriywgts genaprlkmy lseaaegvmp ttlwadgaef
      301 ghnqdgirel raldvgdfpt pkpeklisqv islasdpgdi vldsfagsgt tgavahkmgr
      361 rwlmvelgeh chthilprlr kvidgedggg vtesvgwegg ggfryyslap sliindrwgn
      421 pvinpeynaa qlaealakle gfsyapsevq wwqhghsser dfiyvttqnl sadqlqalsd
      481 evgsdrsllv ccaafhgvta akanerwpnl tlkkipkmvl arcewghddy slnvanlpma
      541 kpdpvetsaa aeankkaksr kvpaansnqg glfgene
//
LOCUS       WP_003804466             255 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Arthrobacter globiformis].
ACCESSION   WP_003804466
VERSION     WP_003804466.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter globiformis
  ORGANISM  Arthrobacter globiformis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Arthrobacter globiformis"
                     /db_xref="taxon:1665"
     Protein         1..255
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=26262
     Region          93..233
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mhqapprkrn wfaagalaav ilattacggv isatrqpssd avpggstgna pgyavkaadl
       61 latlpvkgra pktgydrekf gpawsdtdhn gcdtrndila rdltkttfkp gtkncivltg
      121 tladpytats iaftrgskts savqidhvva lsdawqkgaq rlskaqrtaf andplnllaa
      181 sgpanqqksd gdaatwlpgs rayrcpyvar qisvkakykl wvtqaertam asvlaqcggt
      241 vaggtaaggt aagtk
//
LOCUS       WP_003809537             254 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Bifidobacterium].
ACCESSION   WP_003809537
VERSION     WP_003809537.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 254)
  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 254)
  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   3  (residues 1 to 254)
  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   4  (residues 1 to 254)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 254)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..254
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=28098
     Region          36..248
                     /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"
ORIGIN      
        1 maaekttepd evltdeelqa aaapepdsan nneahkrtvv vaedesvnrm dlvamledng
       61 yevvgeaang eeaveltrkf rpsvvcmdvk mprmdgieaa giicdeniap vvmltafsqs
      121 dlvkkatgag amayvtkpye eskllpalev amgrfaeind lldnverses klqeteeqlk
      181 kaeeqlkkae etleerklvd rakgllmdka dfseqgafrw iqktsmdqri pkkrlamaii
      241 akygeqksea eder
//
LOCUS       WP_003809774             238 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Bordetella].
ACCESSION   WP_003809774
VERSION     WP_003809774.1
KEYWORDS    RefSeq.
SOURCE      Bordetella
  ORGANISM  Bordetella
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 238)
  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   3  (residues 1 to 238)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Bordetella"
                     /db_xref="taxon:517"
     Protein         1..238
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25604
     Region          42..235
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mpdahdpylv sgrfeianll qtlqarqcll lmripgrpfn svtsvlhvda qagqvvldaa
       61 qddtlnqrla dagdvafdts ldnisisfaa arvtrcefea rpallvdlpe tltrvqrrdt
      121 friavpvaqp atwvreagga eplalcdisp gglaladpqq tldpapgkiy rgvlalpelg
      181 afaaairvvh hldevlakgk tsrrigcafv eldkgtgiri qayvnalqrd qiarqrgl
//
LOCUS       WP_003810940             300 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Bifidobacterium adolescentis].
ACCESSION   WP_003810940
VERSION     WP_003810940.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium adolescentis
  ORGANISM  Bifidobacterium adolescentis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Bifidobacterium adolescentis"
                     /db_xref="taxon:1680"
     Protein         1..300
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32406
     Region          15..267
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mshvsyaepp aqgwdihcht vfsdgtetpr tlvaqarklg lhgvaiadhd ttagwdeate
       61 aseeiglpll lgteitavde dvsvhmlafq ydpsnehmss mfantraarl hrtkrmverl
      121 sqdfpitwdd vlaqvkeger ttigrphiad alvaagvyet rsdafadavs akskyyiptp
      181 spstheviaa vkgaggvvva ahagdpqrnr rllsdeqlda miadgldgle vwhrgnppeq
      241 rerlltiaar hdllvtggsd whgkgkpngl genltdddtv reilhrgvdl sdrvgsshaa
//
LOCUS       WP_003805437             312 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Arthrobacter globiformis].
ACCESSION   WP_003805437
VERSION     WP_003805437.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter globiformis
  ORGANISM  Arthrobacter globiformis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Arthrobacter globiformis"
                     /db_xref="taxon:1665"
     Protein         1..312
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33523
     Region          3..304
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mvnrlmlldt aslyfrafyg lpdtirrpdg tpvnavrgll dmiarlttdy gathlvacwd
       61 ddwrpqwrvd liptykahrv aevvagaadv evvpdaletq iplirhvldl agiavvgvpe
      121 headdvvgty ashadlpvdv vtgdrdlfqv vddarqvrvi ytargmknle vmtdavvvak
      181 yrvlpaqyad yatlrgdasd glpgvagige ktaaallleh gtldgllaaa adpegrvsgp
      241 vrsklaaaad ylnvapavvn vvrnlelpsl deagaelhpv tgaareeler lstewnlggs
      301 vrrllealdr rt
//
LOCUS       WP_003811985             616 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Bifidobacterium bifidum].
ACCESSION   WP_003811985
VERSION     WP_003811985.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium bifidum
  ORGANISM  Bifidobacterium bifidum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 616)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Bifidobacterium bifidum"
                     /db_xref="taxon:1681"
     Protein         1..616
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=65725
     Region          492..607
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(560..561,564,580..583,585)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 maneytgddn qedertqavf plddqmdipp lnmpvlhdgs tfdaepsgla glvqetqakr
       61 qadaasaqtq esqetqafdp laelddeaap epqpaapats sfapqrpaad dvatvafaav
      121 amnpaddaal gkgvsaaktk npkrgmiiaf siigallvll vaaffgtnwy fqdrvapgvr
      181 fgnvsvmgkt eseltgivnq avsdsaitvt dsegnnvkag ldklgvtvnv kqtvrnllda
      241 ksgnmftrin pfakqdvrls attdnyklst ylteqlveeq dravasnisy danskkfivt
      301 egnegkeadp sdviaavkka vsqpgeaqkl svmysdvamp itvetatsaa ndankrltss
      361 lvignskgkt ftlpadeiak wiqvkpdiqk gtitlaydqd aiktylsqnl akkldqdmvv
      421 eknitntdgt vltvtqkgvd gvavqstdet aaqvldalna grgaeltatv kvtdhktesr
      481 kvdytspngd phmvinlseq kvyaykgstl vktfivstgk pstptdngtf fvhtkyqsqt
      541 mrgegyvtpn vpwvtyynqg egfhgapwnt agiasgtpks hgctnmhved akwvydflpi
      601 gamvqivgtt ptsavr
//
LOCUS       WP_003806260             266 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Arthrobacter
            globiformis].
ACCESSION   WP_003806260
VERSION     WP_003806260.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter globiformis
  ORGANISM  Arthrobacter globiformis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 266)
  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 266)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Arthrobacter globiformis"
                     /db_xref="taxon:1665"
     Protein         1..266
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28441
     Region          1..249
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mtytvncsil ltelpllerp aaakaagfda vefwwpfess vpsdsettaf eraitdagvq
       61 lsglnfnagn mpggdrglvs wvgregefkd nidvvagige rlgctafnal ygnrqeefsp
      121 eeqdelaarn laaaaegvar iggtvllepv sgaprypllk aqhaldviar vkaesgaqni
      181 klladfyhla vngddvaavi ekhakdfghi qiadnpgrga pgtgelplge wiarsrelgy
      241 dgyigleyke pqetafswai rehaan
//
LOCUS       WP_003812132             293 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Bifidobacterium bifidum].
ACCESSION   WP_003812132
VERSION     WP_003812132.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium bifidum
  ORGANISM  Bifidobacterium bifidum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Bifidobacterium bifidum"
                     /db_xref="taxon:1681"
     Protein         1..293
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31615
     Region          16..268
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mtrlalaaap prsgwdihch tvysdgtqtp aslvelsrhi glhgasisdh dttsgwadae
       61 aaareegmrl lrgteitacd gpvsvhmlay qynpndrhts dlfartrqar lkrtkamvar
      121 lgedypiswq svleqvhege rttigrphia dalvaagvyr trseafadav satskyyipt
      181 psptthevla avaaaggvvi iahpgavnrn vtllsdsqie tlieegldgl evwhrdnppq
      241 qrerlyaiaq ahqllvtggs dwhgagkpnh lgenltddet vaeivrrgai plv
//
LOCUS       WP_003812637             364 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [Bordetella].
ACCESSION   WP_003812637
VERSION     WP_003812637.1
KEYWORDS    RefSeq.
SOURCE      Bordetella
  ORGANISM  Bordetella
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 364)
  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 364)
  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 364)
  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 364)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Bordetella"
                     /db_xref="taxon:517"
     Protein         1..364
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39836
     Region          1..356
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mqrrsflkqa tlgaaaggaa laapalaqds ptihwrlass fprsadaift ggenlakyvs
       61 eatdgkfsir afpageivpa lqvldavqng tiecghtasy yyfgkdpalc fdgavpfgln
      121 trqmnawmrh gdglkltrel fqkynvvnfp cgytgtqmgg wfrneiksvd dlkglkfras
      181 afagavlsrl gvvpqqiagg diypalekgt idaaewigpy ddeklgfhkv aknyyfpgww
      241 egtlqvslyv nqdvynqlpk hyqaalaqaa aaatndmiak ydaenpaalr rlvaegaqlk
      301 afpksvmeac ytqaqavyke fsekdpmfkr vydsmvafrd neipwfrvae gsydgfmatv
      361 argk
//
LOCUS       WP_003812773             409 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Bifidobacterium].
ACCESSION   WP_003812773
VERSION     WP_003812773.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..409
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44091
     Region          3..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 maktvlvins gsssikyqlv dlesgeglas glvekigepv dghykheyng ekheleepih
       61 dheqglrrvl gffkeygpdl seagivavgh rvvqggslfp kpalvtdkti navkdlavla
      121 plhngpeakg aevmrallpd vpqifvfdss fffqlpkaas tyalnkeiad qyhirrygah
      181 gtshefissv vpgvigkpae glkqivlhig ngasasaevs gkpvetsmgl tpleglmmgg
      241 rtgdidpavv fhlirnahmn vdeldtlfnk rsgmmgmtgf gdlrevhrlv aegnedakla
      301 ldvyvhrivs yignytyqmg gcdvitftag vgenddivrk mvcdklapfg vkldeeknak
      361 rskepriist pdssviiavi ptneelaiar ksaeiaenga dtygntftk
//
LOCUS       WP_003812942             636 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Bordetella bronchiseptica].
ACCESSION   WP_003812942
VERSION     WP_003812942.1
KEYWORDS    RefSeq.
SOURCE      Bordetella bronchiseptica
  ORGANISM  Bordetella bronchiseptica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 636)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 636)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 636)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 636)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 636)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Bordetella bronchiseptica"
                     /db_xref="taxon:518"
     Protein         1..636
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=69488
     Region          1..636
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mthtaagapr daktaihaps srmalmlgal gvvygdigts plytlracln tiddlqpahv
       61 lgvlsilfwl lmivvslkyv tlvlradnrg eggtlallel avrgregrar wllivlgifg
      121 aalfygdsmi tpaisvlsal egisivshtl epwvvpvalv vlvalfaiqs hgtgavgklf
      181 gpimalwfat lavlggyqiw ltpevlaaln pvwalrfiae fpvmsflllg avvlaltgae
      241 alyadmghfg rpairrawfa mvlpaltlcy fgqgalllrd paairnpffl mapewglaal
      301 vglatvatvv asqavisgaf svtrqavqlg fwprmqilht savekgqiyl pqvnalllca
      361 vlvlvllfrn senlaaaygf avtgtmltts vlafavlprd stggkrvlwm vllgallvid
      421 illfganifk iheggwlpll vgvvvftlmm twrrgrrlla dmqardrqpl refmtqleaf
      481 pparvqgtai fmtmnagnvp pallhnlkhn kvlhdhvlfl sirvadvpyv sederfdmhk
      541 isasswqasi nygfkedpdv pdalrqvaea ypeidlepmr tsfylsrqtv vaarrpamar
      601 wrralfafma rnstrstrff kippnrvvem gmqvel
//
LOCUS       WP_003813014             313 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Bifidobacterium
            bifidum].
ACCESSION   WP_003813014
VERSION     WP_003813014.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium bifidum
  ORGANISM  Bifidobacterium bifidum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (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   2  (residues 1 to 313)
  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 313)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Bifidobacterium bifidum"
                     /db_xref="taxon:1681"
     Protein         1..313
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34442
     Region          17..70
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msiqaltwvi ygvasdikha dfrtllvlad hadpqgmgay psrstisrlt gysvrtvsya
       61 lkslessgli srgdqrivsn lggykptvwn lnmsrgakta plknaetpvq hdctpavqtd
      121 ctpavqtdct pavqtgvqkt rtgvqtgvqh dctrtiskee pyiepresna rarkpipipa
      181 dwkpseehra ladrlgidcd ieadkfrdra ldsgarsadw nakyrnwlvk gkergfatpk
      241 dsnarrrftw gseevkrvlg piscegtdty melackvadl lnqgldpnml rrqlanvpdn
      301 vlaeqlfeqe aaa
//
LOCUS       WP_003814468             814 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Bordetella bronchiseptica].
ACCESSION   WP_003814468
VERSION     WP_003814468.1
KEYWORDS    RefSeq.
SOURCE      Bordetella bronchiseptica
  ORGANISM  Bordetella bronchiseptica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 814)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 814)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 814)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..814
                     /organism="Bordetella bronchiseptica"
                     /db_xref="taxon:518"
     Protein         1..814
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89487
     Region          76..125
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          129..814
                     /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 mvitfnlfsv khsmrarpsa atralhsssr prrlipallg alaclgtgvq aapidvdipp
       61 qnlaqalhql grqanlqvly sqdlvdgqrs pavqgrmepa ealerllkgr nirysiqhnt
      121 vtltpmplta tlpaisvvga lpdsdtyvat gttagtktdt plieipqsis vvtaaqireq
      181 npqtlgdavr ytpgivvqeg fnrtddpfii rgfdvrtnpg vmfrdglkip lphysamsep
      241 yalerievvk gpasvlygqa spggivnvvs krptdsplre lqlsggshsn rqlagdfggr
      301 iddegrltyr ltglarnadt midhvpddry ylapaltwri spdtsltlla symknktinn
      361 agyplegtvk ynpngriprh rftgepdwsk wdqevanvgy qfahrfndtw qfkqnlgyaq
      421 srnrvnhayw wtwvpgsdfs taergayrrd ddahgvsidn qfeatwqsgr frhntlfgld
      481 ytetsftrkq yagynnlapi dffdpaygsd vllpakpdty tnekrsqlgl ylqdqikfdd
      541 klvvvlsgry dnadgstlnk lsgvntrtgd naftwrtgll yladnglapy isystsfqpq
      601 agttspargt tpfdptkgkq weagvkyqpn gsnsfitasv feltrtnvpt tdpanpvysv
      661 qegevrsrgl elsatanlas gwnliaayty tdaeitksns ntlgntpeav prnmaslwsd
      721 ytvpsgalag lnigagvrym gstynntnaa kvgdytvfda alrydfgars pslkgwtadl
      781 tvrnlfdkdy vasctyacfy gegrtvlgrv tykw
//
LOCUS       WP_003811818             276 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SPOR domain-containing protein [Bordetella].
ACCESSION   WP_003811818
VERSION     WP_003811818.1
KEYWORDS    RefSeq.
SOURCE      Bordetella
  ORGANISM  Bordetella
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Bordetella"
                     /db_xref="taxon:517"
     Protein         1..276
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28369
     Region          199..273
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mglftskdsa setqssrprp svsseaqaae lrararrrla gavalvlaav ivlpmildse
       61 pvpvdsdipi rvpdrnsafq ptvndpqaaa pqpeqpapqa pagtpeagap qppalasapp
      121 qtpppgqtpa qpqtppaaqp patppqqaat ppaapkpeak pepkpakpaa parsddgara
      181 iallegrspp paqpkpaang nfvlqvasyt tqadaqarrg klhqagvtna fveqasingk
      241 qqyrlrvgpf psreaaqaaq arlrtlgydn gfiaaq
//
LOCUS       WP_003815535             710 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Bordetella bronchiseptica].
ACCESSION   WP_003815535
VERSION     WP_003815535.1
KEYWORDS    RefSeq.
SOURCE      Bordetella bronchiseptica
  ORGANISM  Bordetella bronchiseptica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Bordetella bronchiseptica"
                     /db_xref="taxon:518"
     Protein         1..710
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73050
     Region          27..706
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mtqdldmaer svaapqwega araaavlear svaivgasad pgkiagrpla ymlsrgfvgk
       61 lfpvnptraq vqgvksypsl aaigepvdla ivgtpaalve gviregiaag vrafvvfssg
      121 fsetgeagaa lqrrlgelar ahgvtilgpn clgvansatg liasfttale etpirpggfa
      181 lvsqsgalga ywmdiclrsg lgfskwittg necdmdaaaa iaylagdadt rviglyiedi
      241 rdtaafrral rvaaeagkpv iaikagrsqa gaaaaashtg alagddalyd aclrqhgalr
      301 vdslgemmda arlylfdsvp qgrrvavmsv sggagvliad eaerrglalp plagstaaal
      361 apvlpsfvqa anpldltgnv vqdtasigra leavardpgn daivlfvglm hsiasaftda
      421 iaqarqrthr piiviwigak eesvaaleqa ripvfrdipp avaavgaavr lralreaala
      481 malpaaappa apgarveala ecdgkallre lgvagvpagm lvsaaapdrl paplaypvva
      541 klqaasllhk sdiggvvlni gsdaqlreav hrlagiaqah gieargvlve pmqpfdhell
      601 lglrrdprfg atltlgrggv eveldadvas qllplsagdi qamleslraa rlfkgfrgrg
      661 avdlaalssq iadlcrifla qpdlaevein plavrgdraw vldavvsrya
//
LOCUS       WP_003815961             674 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter permease [Bordetella].
ACCESSION   WP_003815961
VERSION     WP_003815961.1
KEYWORDS    RefSeq.
SOURCE      Bordetella
  ORGANISM  Bordetella
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 674)
  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 674)
  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 674)
  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 674)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..674
                     /organism="Bordetella"
                     /db_xref="taxon:517"
     Protein         1..674
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=72080
     Region          5..666
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mqidhdktqq ltekydseir frpldktatw ivsillvtls ifhyytagfg llreathrgv
       61 hlafvlslif lvfgfskahy qrepkstllr pggvplydwa iaivlalsvl yipyifedla
      121 frvgnplpmd vamgtilivg llegtrramg wplpiiamvf layaafgpyf pgllqhagnn
      181 wpqivnhmyl tsqgiygvav gvvatyvfhf vlfgvlatri glgqlfldva stiagryagg
      241 pakvsvfgsa mfgmlsgssv anavtvgslt ipamirigyp rhfaagveaa sstggqitpp
      301 imgaaaflmi eflgipyqqi aiagifpafl yffgmfmqvh feakreglrg lteeempalk
      361 asfkkrwptl lplimligvl asgrtpylaa fagitgcivv gllnpmqrlr lrdlyeafet
      421 gakyalavga aagtvglvig vvtltgvgfk isyivisaaq aiaggvgtii pdvvantqtl
      481 tliaalvmtg ivcilmgcgi pttanyiimv avaaptlvql gvqpiaahff vfyfgiladi
      541 tppvalaaya aagmagsdpf ktgntafrlg itklivpfvf vfspsllisv qgftwydfft
      601 tlvgcmvglv llsaafsrym lvemkswerw vctlgallti lpgltsglvg laicipvflr
      661 qlaqlkleng akaa
//
LOCUS       WP_003816740             209 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Bordetella
            bronchiseptica].
ACCESSION   WP_003816740
VERSION     WP_003816740.1
KEYWORDS    RefSeq.
SOURCE      Bordetella bronchiseptica
  ORGANISM  Bordetella bronchiseptica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 209)
  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 209)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 209)
  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   4  (residues 1 to 209)
  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   5  (residues 1 to 209)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Bordetella bronchiseptica"
                     /db_xref="taxon:518"
     Protein         1..209
                     /product="TRAP transporter small permease subunit"
                     /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=23181
     Region          3..171
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mrallalsrg idalnlrvgr avtwvtllvv lvsagnavvr kvfhsssnaw lelqwymfga
       61 mflltagytl lknehvrvdi lssrlprhkq iwieifgvvf fllpactlim vlswpvfmds
      121 ylsgeqssns gglirwpvkl lipvgfallv laglshlikc igflrgqcpd ptaregsksa
      181 eellaeeiar ealereasvq eqrnnhegr
//
LOCUS       WP_003817309             293 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Bifidobacterium].
ACCESSION   WP_003817309
VERSION     WP_003817309.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..293
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31587
     Region          16..268
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mtrlalaaap pksgwdihch tvysdgtqtp aslvelsrhi glhgasisdh dttsgwadae
       61 aaareegmrl lrgteitacd gpvsvhmlay qynpndrhts dlfartrqar lkrtkamvar
      121 lgedypiswq svleqvhege rttigrphia dalvaagvyr trseafadav satskyyipt
      181 psptthevla avaaaggvvi iahpgavnrn vtllsdsqie tlieegldgl evwhrdnppq
      241 qrerlyaiaq ahqllvtggs dwhgagkpnh lgenltddet vaeivrrgai plv
//
LOCUS       WP_003817684             178 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Bordetella bronchiseptica].
ACCESSION   WP_003817684
VERSION     WP_003817684.1
KEYWORDS    RefSeq.
SOURCE      Bordetella bronchiseptica
  ORGANISM  Bordetella bronchiseptica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Bordetella bronchiseptica"
                     /db_xref="taxon:518"
     Protein         1..178
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=19594
     Region          16..174
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 meqslldavh wllallalpk vglsavflvs llsatllplg seaavygfvk lapdmfwptv
       61 lvatvgntag gaisyymglw ahraverwra rhpherqdgf qsrlggrwna rariwlhrmg
      121 ppalllswlp avgdplcava gwlrlsfwpc vaymaigkfl ryalltgall walpelhm
//
LOCUS       WP_003815695             713 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate--CoA ligase family protein [Bordetella].
ACCESSION   WP_003815695
VERSION     WP_003815695.1
KEYWORDS    RefSeq.
SOURCE      Bordetella
  ORGANISM  Bordetella
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 713)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Bordetella"
                     /db_xref="taxon:517"
     Protein         1..713
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=75177
     Region          17..712
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mdnasvspgf trpprlsvar ivapgsiavv gasddlkkfg griihyvtrn gyrgtvipvn
       61 prraevaglp avpsiahlgp vdvailalpv dmieqaigec aaagvgacvi vsagfaelgd
      121 egvarqdriv riareagmrl vgpncmgiin phhrmaltss lvveqgellp gniglisqsg
      181 almvsmydra creqirfsac vslgnqcdle icdffeymid dpltrvitmy vegfvdtgrf
      241 aelarraqra gkpvlltktg rtaagaeaar shtaslagny ralealceat gvtivddpdg
      301 mlqlaailar fgrcaaegvg ivspsggaig igvdrlsdvg irlgrldaas qqllgtvmnp
      361 shafnpvdlg nrtteemsql rtivqaynqa pdigvifvil ttsphfeqvt lalgqamaqa
      421 ggkpvlflvt pggvadncrt llqdlglpyv drmddairil rhyvpkadal pardaprpas
      481 wpmpegagrm lgarpgepev kallraygip laqerfcrta eqaveaarai gfpvvlkavs
      541 aqlvhksdig avklrladda avrrawaeie qalssqvdga vldgclvaem vtaqsellvg
      601 aindaqfgpm imvgfggvtv elvpdtqlav apvdteqama llrrlkqwpl ldgyrgmpka
      661 dvaavaevvs rvswliadlr dqvaeldinp lliragdgkp igvdaraaml gpg
//
LOCUS       WP_003818340             164 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Bordetella bronchiseptica].
ACCESSION   WP_003818340
VERSION     WP_003818340.1
KEYWORDS    RefSeq.
SOURCE      Bordetella bronchiseptica
  ORGANISM  Bordetella bronchiseptica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Bordetella bronchiseptica"
                     /db_xref="taxon:518"
     Protein         1..164
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17379
     Region          29..156
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfdatpistv skpvfyaela aqahallage hdrianaanf salvyralpd inwagfyfhd
       61 gqelvlgpfq gkpacvrial srgvcgaaas qrrtqvvpdv hafpghiacd aasraeivvp
      121 llhkgsllgv wdvdsplpgr fddedragme alcevflhsl gsad
//
LOCUS       WP_003813609             825 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [Bordetella].
ACCESSION   WP_003813609
VERSION     WP_003813609.1
KEYWORDS    RefSeq.
SOURCE      Bordetella
  ORGANISM  Bordetella
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Bordetella"
                     /db_xref="taxon:517"
     Protein         1..825
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89743
     Region          65..115
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          93..825
                     /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 mfsrsqkhps wrlspcvlaa alcavavgsa dtaraqapaa saqhyeiaag pladaltrfa
       61 rragvvlsfd palvqgrsta glqgvygvrd gfaallagsg lqaragggnn wslaalprgg
      121 daqtlapvtv lglegalapt vgyvasasls gtktdtplie tpqsisvvtr dqiteqgaqt
      181 lnqvlrytag vatetrgata trldqfsvrg fsaatyldgm rvfggrdalp qvdayrlerv
      241 dvlkgpasvl ygqggpggvv nqvskrplde plreievqag nfdfrrvnmd fsgpvdedrr
      301 flyrvtgaay msdgqvdhtr erryfvspsf twrpsadttl tvltnfqrdp dmgsygsisa
      361 mrtllsapdg rrlgpnhydg dadfeksdrr syslgyqleh rfndtfkasq nlrfqhaegv
      421 yrsiygasnn nygyldkdyr ysqrglaisd vdvdaftidn nlqarfdtga lahtvlvgfd
      481 yqrvqtdtls gygsappldv fdpdyhmgie rppftsdqtq ynyqtglylq dqirldrlsl
      541 llggrydwsr thtgtdnlan gshsssalaa eaftgrvgai ynfdngvapy asysesfepq
      601 tgtgwnntpf kptegkqyev gvkyqppgsa tlltlaafdi rrknlpttdp dpthmcgvsr
      661 csiqagevrt rgieleakte plrglsliaa ysyldneyek aypnttgldl kgkkpvavpa
      721 hqasawaryq lqegplaglg mgagvryigs syanetntlk vpsvtlvdmm ldydlgrasp
      781 alkgmqvaln vsnlfdkeyi gsclsdswcw ygyqrsikas lryrw
//
LOCUS       WP_003819402             174 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Bordetella
            bronchiseptica].
ACCESSION   WP_003819402
VERSION     WP_003819402.1
KEYWORDS    RefSeq.
SOURCE      Bordetella bronchiseptica
  ORGANISM  Bordetella bronchiseptica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Bordetella bronchiseptica"
                     /db_xref="taxon:518"
     Protein         1..174
                     /product="TRAP transporter small permease subunit"
                     /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=19535
     Region          1..166
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 merliqvldl fsdrmgrlas mvmlpvllvt favvvlryvf gigliwlqds yvwltsvffi
       61 cmagntflhd rhvrvelfys rmnarkqalv nalgvllllw ptlfvtvqqs wrpiarswrf
      121 leaspnaggl sfayvhkslv yvfclvlflq glslllksar tlagargvap easp
//
LOCUS       WP_003820145             706 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Bordetella bronchiseptica].
ACCESSION   WP_003820145
VERSION     WP_003820145.1
KEYWORDS    RefSeq.
SOURCE      Bordetella bronchiseptica
  ORGANISM  Bordetella bronchiseptica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Bordetella bronchiseptica"
                     /db_xref="taxon:518"
     Protein         1..706
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73687
     Region          18..706
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mstladnapr magagdwida alaprsvaiv gasdnpekig grpikymlqh gyqgrilpin
       61 pgrdrvqgia awhsldavnv pidmllvcva geaavqavrd garlgvrvcv vissgfaetg
      121 epgrqaqehm kaaaaaagmr llgpntqgla nfsngalatf atllgevapa dgpvavisqs
      181 gamsmvpyah lraegigvry svatgnecdl nvadfteavl rdpgvrlill ymeslpapat
      241 laraaalars rqvpvlalka gvspqglqaa qshtgaiate dkaldawfrq hgilrvpdar
      301 slvmgaqlll rcghlpgnrl ailsnsgaac vtgadaaerh glqvpplpae traridavlp
      361 gfasslnpid ltaallsnnh lfgqvlpila saracdalfi tlpmsgkgyd tdqfardaaa
      421 ftaetglpvv vscplaasrr ifaqaglatf ehdedalaal gqlarlsglr etalrlarpa
      481 phapaapvpr tagllseads leqieaigir tapwrlclda dsmgsalgsl pgpwavkacs
      541 aqiphkseyg lvhlgiadeq raralfpvlr qevlgmgksf dgvivasivk prrefmigar
      601 wdsqfgcivi vgdggkyvea mpdvatlvyp fdqahaeecl rklrvaalfd gvrgenplpv
      661 qelahaatrl gawlhaqqga vasvdinpli agpdgrlyaa dalvei
//
LOCUS       WP_003820520             238 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Bifidobacterium bifidum].
ACCESSION   WP_003820520
VERSION     WP_003820520.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium bifidum
  ORGANISM  Bifidobacterium bifidum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 238)
  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   2  (residues 1 to 238)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Bifidobacterium bifidum"
                     /db_xref="taxon:1681"
     Protein         1..238
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=24525
     Region          <107..>190
                     /region_name="MSCRAMM_ClfA"
                     /note="MSCRAMM family adhesin clumping factor ClfA;
                     NF033609"
                     /db_xref="CDD:468110"
     Region          171..237
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mpshgeshte khadvadftt pavepisrlm gvrpddgmrg qsakrdvprl rfrpfhavtv
       61 mlvlttalca sltmllqqsl ryvsaqshna amqnaggket giaetlpggs dgsdsvngdg
      121 snsggtgsdq ensggagdae sqgdgvessa gsqaaqngrs sqqgsdgsdd gatadtridl
      181 ntataeqlds ipgvgpvtaq rildhrrsig rftsvdqlld vsgigaktlt kirpwvrv
//
LOCUS       WP_003821757             265 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Eikenella corrodens].
ACCESSION   WP_003821757
VERSION     WP_003821757.1
KEYWORDS    RefSeq.
SOURCE      Eikenella corrodens
  ORGANISM  Eikenella corrodens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Eikenella.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Eikenella corrodens"
                     /db_xref="taxon:539"
     Protein         1..265
                     /product="formate/nitrite transporter family protein"
                     /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=29158
     Region          7..262
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 maqsvfveki eqachkkewl ferskskyal rsliagmllt ltpatgviaa dvlntvhpsl
       61 grfafpfffs wglvyilfln telttsnmmy ltagtflkki kwekaliill yctafnligs
      121 iftawlfnqt safahisadg ylanmvghkl erpnglvlae gifanlfvnv avvaylllke
      181 qaakiaavfa avymfvflan ehvaanfasf alvgfnqiad svshfealni lrhcsvafva
      241 nwigggllig vpyaflnede geyvd
//
LOCUS       WP_003817981             860 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Bordetella bronchiseptica].
ACCESSION   WP_003817981
VERSION     WP_003817981.1
KEYWORDS    RefSeq.
SOURCE      Bordetella bronchiseptica
  ORGANISM  Bordetella bronchiseptica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 860)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 860)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 860)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..860
                     /organism="Bordetella bronchiseptica"
                     /db_xref="taxon:518"
     Protein         1..860
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=95562
     Region          73..115
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          100..860
                     /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 mqvrtgdmpl araarmrthw raaalaaila hawlppgvas aqpaqaleqp lsfdmapqpl
       61 gqalielnrr talsiafdpr qvehfqapai rgvmtseqal rqalsgsnla yslrgqvatv
      121 rqqevaqlmp vtvsgdnlpa yiadtptsia tktslpprqt pftinqasqe limergdani
      181 ydtlegfagv tttsgngdig qsmsrsinvr gfstggagql lingqrtyss asaarspdsl
      241 ervellrgpa alyygaaepg givnytykrp qaqaaytivg rtdskgsygs mvdmtgplnq
      301 ddtllyrlvg sythtvddqd hifqepksvl aaltyapssr fdttltyerm emeavpeqen
      361 nmrisnrnsp yygqyypvpr dffwgslndr avtetdtllw darwrpserf nlsayanyqe
      421 skqwwqntrv ngagngpdad gnvqryvsgr qardrnwsfg ldlsgkaytg afrhdwltga
      481 gyghtqtrss grqvaadsrp gqpytpgpln ifdpdygnwh yqdriwedpl aaatkrndln
      541 lyfqdmlhlp dektrlllam gwaqfdsrpp dnaqrnkisk wsprialmhd ltpsttvyas
      601 ygesfypnel nlldmsgsyi tkpqegkqye igfkqdlfds ramltaalfr idkknmpmsa
      661 qpdgqcdpla apapgtpgti dgsgdcrtsl sglersqgle lelsglitdw waaslsyayl
      721 kteyvdtedp fsqgrskpnm pahnlalwnk frvyqdpvyg tahvavglra wskshnawrd
      781 pavgtyynpy srtdynpgyg ivdvgvfyan tlangmdlkl qlniknlfnk tyydrnrfan
      841 gttivwgner ramlnaqlsf
//
LOCUS       WP_003823100             209 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Eikenella corrodens].
ACCESSION   WP_003823100
VERSION     WP_003823100.1
KEYWORDS    RefSeq.
SOURCE      Eikenella corrodens
  ORGANISM  Eikenella corrodens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Eikenella.
REFERENCE   1  (residues 1 to 209)
  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 209)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 209)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Eikenella corrodens"
                     /db_xref="taxon:539"
     Protein         1..209
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23551
     Region          4..208
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Region          91..119
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(92,95..96,99..100,102,129,132..133,136..137,
                     139..140,159,165..166,169..170,173)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          127..153
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          158..189
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mavydlkdqe eienfkyfwr swgrwlfall vvaaigyfgw vmysshqrsv nneavavfdq
       61 waenqqankp aeaaklltql qsqyptsisa aqatlmqaga afdqgkydea ighlnwvlky
      121 hqeplirama iqrlatvqlq qqkyddaiat lgmntdeaya gilletkgdv yaaqgkrsea
      181 aaaykqamdk lpqddqgref iqlkidqmn
//
LOCUS       WP_003818607             340 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Bifidobacterium bifidum].
ACCESSION   WP_003818607
VERSION     WP_003818607.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium bifidum
  ORGANISM  Bifidobacterium bifidum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Bifidobacterium bifidum"
                     /db_xref="taxon:1681"
     Protein         1..340
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35744
     Region          211..340
                     /region_name="COG3942"
                     /note="Surface antigen [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443142"
ORIGIN      
        1 mrhaahkank gsvqrtspsa lfrssrgsht aravravraa ngdavalaid pvlaaklnev
       61 apmtrraire takaaqrksy mmssaslaal vgtaatalaf sniqqssnsr lladdpattt
      121 tqlarvtgst vsrsesrtel gpiasdqtaa aatsgaadak tsntiadaks vqttnngnwe
      181 lndknsaidv sqlsrslann pqvavlvdqd agklpegfnp nhatgdsgla yafsqctwwa
      241 ylrrhqlglp vgsyfgngqd wansarahgy wvdntprhkg dvmvfragqe gassvyghva
      301 ivesinadgt vtisecgasl ngkpvsrtls nvndfqyihy
//
LOCUS       WP_003823279             310 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase, partial [Eikenella corrodens].
ACCESSION   WP_003823279
VERSION     WP_003823279.1
KEYWORDS    RefSeq.
SOURCE      Eikenella corrodens
  ORGANISM  Eikenella corrodens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Eikenella.
REFERENCE   1  (residues 1 to 310)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Eikenella corrodens"
                     /db_xref="taxon:539"
     Protein         1..>310
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
     Region          34..163
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(125..126,129,142..145,147)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkklallcll aaagtaaann tplpdfspva agqhvvinip qmrlflyeng qlknvypvav
       61 gknrtrtplg nyhigskayn ptwsipasir reraaaglpe issippgpsn plgpvfvrlg
      121 pprlglgihg tnapasvpgi rshgcvrmhs nnalqfarnv rtgasaaviy qlaslnadtn
      181 nhlwlaayad pyqqrnlntt alrqsidaws qangltanpa rinsvlrsrn grlvcitcqn
      241 anarvqgklq svawqngaae lsrpqavdas eplqadeilp egsavealtd gagstetpip
      301 papalpraaa
//
LOCUS       WP_003824035             156 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Eikenella].
ACCESSION   WP_003824035
VERSION     WP_003824035.1
KEYWORDS    RefSeq.
SOURCE      Eikenella
  ORGANISM  Eikenella
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Eikenella"
                     /db_xref="taxon:538"
     Protein         1..156
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=17469
     Region          1..108
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mnglfvstrr gftlmelmii iaivailaai aypsyqsfvr ksrleeanaa llensramer
       61 fyarnrtfka tsttwpalav sqtqhfcikf qgnargvlgd kytikavafd vskeprvlli
      121 nqdqtvricq ssrsrcdnke vfsggnnidq ecellh
//
LOCUS       WP_003825838             148 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Bifidobacterium angulatum].
ACCESSION   WP_003825838
VERSION     WP_003825838.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium angulatum
  ORGANISM  Bifidobacterium angulatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Bifidobacterium angulatum"
                     /db_xref="taxon:1683"
     Protein         1..148
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15615
     Region          9..132
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mksvqnalkr rangekgftl vellvvviii gilaavavpi ylnqrkaawn stiqsdvkna
       61 slvvetamts nngkfdstwa ktykgntgki gdntvtvskd vtitisdlgg nayevsgqdt
      121 ndgtkkytyn sstgetkeea kaaapakp
//
LOCUS       WP_003827234             283 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: class II fructose-bisphosphate aldolase
            [Citrobacter].
ACCESSION   WP_003827234
VERSION     WP_003827234.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 283)
  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 283)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10097223
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..283
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29894
     Region          5..281
                     /region_name="TBP_aldolase_IIB"
                     /note="Tagatose-1,6-bisphosphate (TBP) aldolase and
                     related Type B Class II aldolases. TBP aldolase is a
                     tetrameric class II aldolase that catalyzes the reversible
                     condensation of dihydroxyacetone phosphate with
                     glyceraldehyde 3-phsophate to produce tagatose 1; cd00947"
                     /db_xref="CDD:238477"
     Site            order(26..28,31,51,54..56,60,64,67..68,141,233..234,
                     236..237,240,244,247)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238477"
     Site            order(81..82,177..179,181,208..209,211,230,232..233)
                     /site_type="active"
                     /db_xref="CDD:238477"
     Site            order(82,178,208)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238477"
     Site            order(177,179,181,209,211)
                     /site_type="other"
                     /note="Na+ binding site [ion binding]"
                     /db_xref="CDD:238477"
ORIGIN      
        1 mfadmksmvt kawreqyall aincmnlesa raavrvaekh rapiilnlyq ghlehfpapi
       61 aaavvktlae easvpvalal dhgkdpvrir qafragfsgl midasafale enirqtravv
      121 elaasvslcv egelghlada pcydhaanad lmtqaadvep fiqqtgidll avsvgtahgm
      181 yapgitpaid flrleeiarl stvplalhgg sgtpfdqlqr cptfgvakin vgaavfeagk
      241 aallhtlcrd tsgelvdala lmeqaceeai ipylqasgai gka
//
LOCUS       WP_003819569             184 aa            linear   BCT 20-JAN-2025
DEFINITION  16S rRNA (cytidine(1402)-2'-O)-methyltransferase, partial
            [Bifidobacterium bifidum].
ACCESSION   WP_003819569
VERSION     WP_003819569.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium bifidum
  ORGANISM  Bifidobacterium bifidum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Zhao,M., Zhang,H., Liu,G., Wang,L., Wang,J., Gao,Z., Dong,Y.,
            Zhang,L. and Gong,Y.
  TITLE     Structural Insights into the Methylation of C1402 in 16S rRNA by
            Methyltransferase RsmI
  JOURNAL   PLoS One 11 (10), e0163816 (2016)
   PUBMED   27711192
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Kimura,S. and Suzuki,T.
  TITLE     Fine-tuning of the ribosomal decoding center by conserved
            methyl-modifications in the Escherichia coli 16S rRNA
  JOURNAL   Nucleic Acids Res 38 (4), 1341-1352 (2010)
   PUBMED   19965768
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Kozbial,P.Z. and Mushegian,A.R.
  TITLE     Natural history of S-adenosylmethionine-binding proteins
  JOURNAL   BMC Struct Biol 5, 19 (2005)
   PUBMED   16225687
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001055
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Bifidobacterium bifidum"
                     /db_xref="taxon:1681"
     gene            <1..184
                     /gene="rsmI"
                     /GO_function="GO:0070677 - rRNA
                     (cytosine-2'-O-)-methyltransferase activity [Evidence
                     IEA]"
     Protein         <1..184
                     /product="16S rRNA
                     (cytidine(1402)-2'-O)-methyltransferase"
                     /EC_number="2.1.1.198"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0070677 - rRNA
                     (cytosine-2'-O-)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0000451 - rRNA 2'-O-methylation [Evidence
                     IEA]"
     Region          <1..117
                     /region_name="RsmI"
                     /note="16S rRNA C1402 (ribose-2'-O) methylase RsmI
                     [Translation, ribosomal structure and biogenesis];
                     COG0313"
                     /db_xref="CDD:440082"
ORIGIN      
        1 vtcapgpsav ldalalsglp tdrfcyegfl prkhservqh lrmlqserrt ivfyetphri
       61 adsmddllda fgpnramalc reltkdyeei rrgmvgtirq gvvdnpprge mvlviggasd
      121 eeaeaaapat lsiddlavla idraledgvr ikdaiaqvva ehplpdgslp nrkqvytavl
      181 amks
//
LOCUS       WP_003822730             202 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein, partial [Bifidobacterium bifidum].
ACCESSION   WP_003822730
VERSION     WP_003822730.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium bifidum
  ORGANISM  Bifidobacterium bifidum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Bifidobacterium bifidum"
                     /db_xref="taxon:1681"
     Protein         <1..202
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
     Region          73..202
                     /region_name="COG3942"
                     /note="Surface antigen [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443142"
ORIGIN      
        1 elgpiasdqt aaaatsgaad aktsntiada ksvqttnngn welndknsai dvsqlsrsla
       61 nnpqvavlvd qdagklpegf npnhatgdsg layafsqctw waylrrhqlg lpvgsyfgng
      121 qdwansarah gywvdntprh kgdvmvfrag qegassvygh vaivesinad gtvtisecga
      181 slngkpvsrt fsnvndfqyi hy
//
LOCUS       WP_003821433             825 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Bordetella bronchiseptica].
ACCESSION   WP_003821433
VERSION     WP_003821433.1
KEYWORDS    RefSeq.
SOURCE      Bordetella bronchiseptica
  ORGANISM  Bordetella bronchiseptica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Bordetella bronchiseptica"
                     /db_xref="taxon:518"
     Protein         1..825
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89744
     Region          65..115
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          93..825
                     /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 mfsrsqkhps wrlspcvlaa alcavavgsa dtaraqapaa saqhyeiaag pladaltrfa
       61 rragvvlsfd palvqgrsta glqgvygvrd gfaallagsg lqaragggnn wslaalprgg
      121 daqtlapvtv lglegalapt vgyvasasls gtktdtplie tpqsisvvtr dqiteqgaqt
      181 lnqvlrytag vatetrgata trldqfsvrg fsaatyldgm rvfggrdalp qvdayrlerv
      241 dvlkgpasvl ygqggpggvv nqvskrplde plreievqag nfdfrrvnmd fsgpvdedrr
      301 flyrvtgaay msdgqvdhtr erryfispsf twrpsadttl tvltnfqrdp dmgsygsisa
      361 mrtllsapdg rrlgpnhydg dadfeksdrr syslgyqleh rfndtfkasq nlrfqhaegv
      421 yrsiygasns nygyldkdyr ysqrglaisd vdvdaftidn nlqarfdtga lahtvlvgfd
      481 yqrvqtdtls aygsappldv fdpdyhmgie rppftsdqtq ynyqtglylq dqirldrlsl
      541 llggrydwsr thtgtdnlan gshsssalaa eaftgrvgai ynfdngvapy asysesfepq
      601 tgtgwnntpf kptegkqyev gvkyqppgsa tlltlaafdi rrknlpttdp dpthmcgvsr
      661 csiqagevrt rgieleakte plrglsliaa ysyldneyek aypnttgldl kgkkpvavpa
      721 hqasawaryq lqegplaglg mgagvryigs syanetntlk vpsvtlvdmm ldydlgrasp
      781 alkgmqvaln vsnlfdkeyi gsclsdswcw ygyqrsikas lryrw
//
LOCUS       WP_003825073             225 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Bifidobacterium
            angulatum].
ACCESSION   WP_003825073
VERSION     WP_003825073.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium angulatum
  ORGANISM  Bifidobacterium angulatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 225)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Bifidobacterium angulatum"
                     /db_xref="taxon:1683"
     Protein         1..225
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=23519
     Region          142..223
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mtstggngie syamdefdnp pkgpagvhrg rrsaaarytp fvvvvvvaal cgflawgvls
       61 gefnkvhwpw spassqtssk tstttakkka aekkaaakka aekkqqeeaa kkqqeeeaak
      121 kqqeeeaakq qqeqaaqvdr slsvrvingt gisgyaatkq svlnqagyan vaaanpsgtl
      181 pdatvvwyqn dadkataedv analgisnvq qtsglgasiv villn
//
LOCUS       WP_003828934             262 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Bifidobacterium].
ACCESSION   WP_003828934
VERSION     WP_003828934.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 262)
  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 262)
  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   3  (residues 1 to 262)
  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   4  (residues 1 to 262)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 262)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..262
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=29037
     Region          43..256
                     /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"
ORIGIN      
        1 maarkkseep sidvdevltd eelkavaeed gepaecktkp engprtvvva edeavnrmdl
       61 vamledngye vvgqaangee aveltrkfrp dvvcmdvkmp rmdgiaaagi icdeniapvv
      121 mltafsqtdl vkkatgagam ayvtkpyees kllptlevam grfaeindll dnverserkl
      181 qettdqlket eeklkkaedt leerklvdra kgllmdkadf seqgafrwiq ktsmdqripk
      241 krlaqaiiak ygdpkpsetd er
//
LOCUS       WP_003828955             409 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Bifidobacterium].
ACCESSION   WP_003828955
VERSION     WP_003828955.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..409
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44038
     Region          3..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 maktvlvins gsssikyqlv dlesgeglas glvekigepv dghykheyng ekheleepih
       61 dheqglkrvl gffeeygpkl sdagivavgh rvvqggsifp kpalvtdkti nqvkdlavla
      121 plhngpeakg aevmrsllpd vpqifvfdss fffqlpkaas tyalnkeiad qyhirrygah
      181 gtsheyissv vpdvigkpae glkqivlhig ngasasaevs gkpvetsmgl tpleglmmgg
      241 rtgdidpavv fhlirnahmn vdeldalfnk rsgmmgmtgf gdlrevhrlv gegnedakla
      301 ldvyvhrivs yignytyqmg gcdvitftag vgenddivrk mvcdklapfg vkldeeknat
      361 rskepriist pdssviiavi ptneelaiar ksaaiaeagt dtygntfak
//
LOCUS       WP_003816638             381 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Bifidobacterium
            bifidum].
ACCESSION   WP_003816638
VERSION     WP_003816638.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium bifidum
  ORGANISM  Bifidobacterium bifidum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 381)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Bifidobacterium bifidum"
                     /db_xref="taxon:1681"
     Protein         1..381
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=41786
     Region          8..375
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mtplldvdrv rvllagntvg mltmspsrtl afaydktwlt hgfsispisl plrdgvfvaq
       61 rdplngmfgv fddsmpdgwg rlltdrmlrq hgidpysvgp larlsivghg gmgaleyepa
      121 stidddlqsf pdldslaeec lnvmsadfsn dldqlfvlgg ssggarpkil ttingeewli
      181 kfpssvdapd igemeyhisn lartcgidmp eirlfpsrrc agyfgvkrfd ripltngeig
      241 kvhmvsaggl letshrianl dyallmrltm rmtggikece rlyrlmcfnv fignrddhak
      301 nfsylhdaes gawslspayd ltenpginge httavngkgr gitvedmadi gmkagiprtr
      361 cisiarnmre riadagftvr n
//
LOCUS       WP_003829535             174 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Bifidobacterium breve].
ACCESSION   WP_003829535
VERSION     WP_003829535.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium breve
  ORGANISM  Bifidobacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (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   2  (residues 1 to 174)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Bifidobacterium breve"
                     /db_xref="taxon:1685"
     Protein         1..174
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18448
     Region          104..172
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 migvrstdaa dgavhrlrdk prltfnvhqa lavvlllvaa lgisltlliq qsmhlaalsn
       61 vavetpnnan atqqrpqsss dsdemtdvep dpeqlpetqt densavtvdd glvdintagl
      121 aelqtitgvg pvtaqriidy rktigryasv dqllgvkgig sktlekirgq vtvr
//
LOCUS       WP_003830687             287 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Bifidobacterium breve].
ACCESSION   WP_003830687
VERSION     WP_003830687.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium breve
  ORGANISM  Bifidobacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
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   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 287)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Bifidobacterium breve"
                     /db_xref="taxon:1685"
     Protein         1..287
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30632
     Region          16..68
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
     Region          <67..>271
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
ORIGIN      
        1 msnialswaf kchvgnasak avlvyladra dddgtaaypk iativnvtel sertvraalk
       61 tlqergfirr gdqryarlgk ggrnrlpqyc qivwdlaves dpstlewike thtaehdpkt
      121 mgntvdpaas timengeskd vtpenagtkp ipstanlagl endpepalqi shlqhcesct
      181 pstanlagll ykdktlqvnp pskpsfpsap tghlpasgat aaekikpnns arttprspkr
      241 pdgssprsvc sarcsawprp hrpkptarps sactagsstr erngppl
//
LOCUS       WP_003831534             382 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator
            [Bifidobacterium].
ACCESSION   WP_003831534
VERSION     WP_003831534.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 382)
  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 382)
  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
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 382)
  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   5  (residues 1 to 382)
  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   6  (residues 1 to 382)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 382)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 382)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..382
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41596
     Region          16..70
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          82..362
                     /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 mkpmpstavk qanrqaiidh lyrhgpstkq hlqmtlglsl ptitanlrdl edeglvgrge
       61 ptestggrka qthvfaaksh aaigvrmrad gvtlvavdly geviarkrkr vsyrntsdyy
      121 dmvgdfvtef agrvvrsgsq vlgiafsiqg ivspdgsait fgqivgntgl tlekltrhie
      181 fpalmihdsd asamaelwfd psisdavciy lerrpggavi ahgtlyqgpn lsngtvehmc
      241 lvpggkpcyc gqrgcmdpyc spealledge gmpgffsvls qgerghrkrf dewmgyvaqa
      301 ivnirsviag dviiggeaaq yldddmltel khraeslspf ttdftlkksi ciedqntiga
      361 alrfvrdyvd gicgrmrplp rr
//
LOCUS       WP_003831930             410 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Citrobacter
            portucalensis].
ACCESSION   WP_003831930
VERSION     WP_003831930.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 410)
  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 410)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..410
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47634
     Region          1..405
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mslprlslmd arhlhlaaqg llkktrrrat padilatisr msllqidtin ivarspylvl
       61 fsrlgdyspq wlddslqqge lmeywaheac flprsdfmli rhrmlapenm gwkykvawmk
      121 ehaheieqll qhiqhngpvr sadfehprkg tsgwwewkpq krhleglfta gkvmvverrn
      181 fqrvydlthr vmphwdderd plsqedaesa mldnsarslg ifreqwlady yrlkrpalkn
      241 wcneraeqrq iipvdveglg alwlhshlqp lleqalagkl tathsavlsp fdpvvwdrkr
      301 aeqlfdfsyr lecytpapkr qygyfvlpll hrgqlvgrmd akmhrktgvl dvislwlqdg
      361 vkpgvtlqkg lfqaiddfar wqqatrvtlg rypeglfada rhgweidpal
//
LOCUS       WP_003833062             209 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Bifidobacterium breve].
ACCESSION   WP_003833062
VERSION     WP_003833062.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium breve
  ORGANISM  Bifidobacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 209)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Bifidobacterium breve"
                     /db_xref="taxon:1685"
     Protein         1..209
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=22329
     Region          82..166
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mtqqiderqa rkayvrhrqt ivfsisgvvl aailvvailf nfhvfglgqi ntpatapnyg
       61 naapcavkgd dgkatyvang tvgvrvmngt ehsqfaaavs kaleargfvm qeatnysstn
      121 verttiyfgk nainqaytva gnftdaamvm naredqlidv vlgatfndlk deksspqegk
      181 kitdftgcva adkmtnlpad tqhtaypaq
//
LOCUS       WP_003832782             423 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Bifidobacterium breve].
ACCESSION   WP_003832782
VERSION     WP_003832782.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium breve
  ORGANISM  Bifidobacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 423)
  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 423)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Bifidobacterium breve"
                     /db_xref="taxon:1685"
     Protein         1..423
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46491
     Region          15..71
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msgpaeqwaw qlqderlsls ekfvlvylar rayyddgcga wpsvntiaah chctrrsvlr
       61 alkrlqelgy lregdqelaa rnprshepip rghrskvwdv vmkgaqtepe ditdpgetda
      121 gkdvpakpst aepsrskeca rgdmaspdav spdavspdtm spqgdpagev tscpkrgdmv
      181 spnrqvitna plvpygdipl ageqpeeers erdapdwrla lppkgvrdpl wtpgaedade
      241 rvrsralqev rvltlihdrv aaidpksarp asmrdrrkvh ellterslae vetildwayg
      301 nprwiswlvd gtmveryfaq vsldmrakqa rgpqrsgsht tvaeltpvhd pdrpvavssg
      361 lawrvpvygg gilsvalcqa hldgeagqae cpvcaydrrn qathaigldq aehaeeshee
      421 aks
//
LOCUS       WP_003833782             165 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Citrobacter].
ACCESSION   WP_003833782
VERSION     WP_003833782.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..165
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17870
     Region          1..153
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mnkielytdl nrdfqalmag etsflatlan tsallyerla evnwagfyll eddtlvlgpf
       61 qgkiacvrip vgrgvcgtav aqnqvqried vhafdghiac daasnaeivl piavdnqiig
      121 vldidstafg rfteedeqgl rtlvaqletv lattdykkff arvag
//
LOCUS       WP_003835108             560 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Bifidobacterium catenulatum].
ACCESSION   WP_003835108
VERSION     WP_003835108.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium catenulatum
  ORGANISM  Bifidobacterium catenulatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Magnet,S., Arbeloa,A., Mainardi,J.L., Hugonnet,J.E., Fourgeaud,M.,
            Dubost,L., Marie,A., Delfosse,V., Mayer,C., Rice,L.B. and Arthur,M.
  TITLE     Specificity of L,D-transpeptidases from gram-positive bacteria
            producing different peptidoglycan chemotypes
  JOURNAL   J Biol Chem 282 (18), 13151-13159 (2007)
   PUBMED   17311917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19799648
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Bifidobacterium catenulatum"
                     /db_xref="taxon:1686"
     Protein         1..560
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=60010
     Region          62..>262
                     /region_name="YoaR"
                     /note="Vancomycin resistance protein YoaR (function
                     unknown), contains peptidoglycan-binding and VanW domains
                     [Defense mechanisms]; COG2720"
                     /db_xref="CDD:442033"
     Region          405..558
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mslndmdspe sdnrkfafpn mgddpkvisq vsldsfaeta dsiddgaals vnvskkrhll
       61 wlwivlavml lfgavagggy wffqshalpg vtlwgrsmtg qsrdhivqei sdtaesltvp
      121 vsyegtskkv tlkdlgvaid aesiaenvmn akrddsffqk yafwaredvd vepfddsqas
      181 aqtvggmlgv qsasatnpsl qlnadgtafd vtpgqqgtgi dvteivkeak nvlesfgkqt
      241 aqtvtlentv tdpvitddqa neakasadaw iakpvsikig dhkvaefgaq aiasaitlgp
      301 dseklgdnqi rngsliidgd klqqyyndsi ksnfhadrvd gdvivnsvgd vlqtnvdghd
      361 gitvsdggdt nvgrdaaeaf akgsdsvsiq gtcdaqnekk ttrtvvvsls shtvtaieng
      421 qtvrvmhmsa gqgndyqtgq cqpsgdlctp tycdpnsydn ctpdgdfkvw lkyqsqdmsg
      481 tltlsdgnte kwdvkdvgfv nyfsktgcai hriatqsafn dssiqamgkn tshgcvgvgw
      541 dqaewfynwc lmgttvhvqa
//
LOCUS       WP_003835703             231 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Citrobacter freundii].
ACCESSION   WP_003835703
VERSION     WP_003835703.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 231)
  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   3  (residues 1 to 231)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..231
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26756
     Region          32..221
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 msfglakedk feiiatlree lhkktklevl censsvitql ekvdferfvi swhediapek
       61 vqyfilhses givkfsarfe qtpsagaevg lsylipdlif faqqrqnqrf sfmkgydffc
      121 fgrykngeny sfkiknisqg gcalivkdvn arflykdavi knasldfdtf gslqldlkvi
      181 dvvlinefde dnqlyschqi scefdfknrr eetevekiii kflmsnkirs l
//
LOCUS       WP_003838527             350 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Bifidobacterium dentium].
ACCESSION   WP_003838527
VERSION     WP_003838527.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium dentium
  ORGANISM  Bifidobacterium dentium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Bifidobacterium dentium"
                     /db_xref="taxon:1689"
     Protein         1..350
                     /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=39061
     Region          1..284
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mqrirffdia kgiailavil ghsaieanvf iphhtaqlvv avcfsfhmpl ffilsgyfmh
       61 persfrwake arqllctyav tgvavlvgvt cmatvnhegr aymlrrwgea vlygsgdisd
      121 rtlwpvelri gaiwfllalf wahlllhafa klpytpvwvv ssfaigyisa ryvwlpwslq
      181 sgmcavafvy vgylakrydl mghvkrfpwl wgvagviwvv aivrfggmsm ainnygtrpv
      241 qavigslagt lcvvgiskll dhvpalgral swtgqsslai lcvhlveddv lpwqmylgvl
      301 hnllphiplt vtsfvvrlpi dlafaallyy vpvvnewfyp qlakrrqaaa
//
LOCUS       WP_003838698             740 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Citrobacter freundii].
ACCESSION   WP_003838698
VERSION     WP_003838698.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 740)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 740)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..740
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=83898
     Region          490..736
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mmillrkten infintfrdy fcvgiaffal qliaghlskq edvagitlhf ydltlplisa
       61 llvlyrqkal pilgafflya lysyslssvf tltaqllaal isqtlyffst gkrgavsfgr
      121 sqlttlrivw lvccnallfi sidhwlqsnt asapitnlft lqtlinlqwl mnscltgipf
      181 cylllrsvqn pawcilyirq vktliksgpp ilyqvlwlvl llcimsaliv irediliftd
      241 ysllwllpvm lwgvicigha fispvwvtml illgyyinsy ispdnynnyl hslvisstiv
      301 fvfsltivvt gvlvvrnrky lrrlkqlfrs epntglpnfq alqmdirkha teclcyirct
      361 elntleqthg iefrfefvka lsayvrklik dtgniyyapg hgiilrlnta pdiptlykdl
      421 nsfrfiwkdy qlglscgvay tteknliknl sqaikhlntq syislmqgqp lllspqvpgd
      481 kivsqavirh mlqkaidrks felmaqpvvs tmlvvqpivs ttgltryhei lirikmvdgk
      541 lifpdtilpv aceagllpal ditvieqtfr fiqsrqksdp nshfsinltp dslnkidfld
      601 nvftlfrkys iapkriifei iesdiidnan vtdvlralrk agskiaiddf gtgassysrl
      661 rtldadilki dgsfirnilt defsrcavrs fcevaklknm evvaefvene eiekmlitmg
      721 igwlqgyhig kpvpielael
//
LOCUS       WP_003838959             523 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Bifidobacterium dentium].
ACCESSION   WP_003838959
VERSION     WP_003838959.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium dentium
  ORGANISM  Bifidobacterium dentium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 523)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Bifidobacterium dentium"
                     /db_xref="taxon:1689"
     Protein         1..523
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=56167
     Region          390..514
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(474..475,479,487..490,492)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 msdereqala gddtatiapl pvapavftpi eeiampevkr knkwpliitl ivmgvmllaa
       61 vsgffvarwy fqdkaapgvt fagssvagqt reqlkdtvsd avksttitik dndgntdtak
      121 ltdlgvtvni nktvsnllaa khdddgvlaa inavnpfdkn evplaaqtne ldlttyvtdk
      181 fvdederava stisydsdeq afttvegreg rtpetdkvlt avrnainvpg gnstasisyk
      241 nvdmpvsvsa aqratdeana rlnnkivldn gkdktfelpv dvvaswikpn adldkgtisl
      301 tydeqaigny leqevpnqln qdkvsqedav dsngtvlvti vkgvdglkvk nvsaltpkvv
      361 nalqggqgat ipvesdvdaf dtvqkkseyr ivvdrasqta tvyqndqavr tfpvctgtag
      421 khetdlgtyy iylkynvqdm tglnddgsry lskgvkwvgy fnggegfhta swngygiahg
      481 dpvhygshgc vnmyeadakw iydncpegtv vqvvgampsg avr
//
LOCUS       WP_003843284             335 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Bifidobacterium dentium].
ACCESSION   WP_003843284
VERSION     WP_003843284.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium dentium
  ORGANISM  Bifidobacterium dentium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Bifidobacterium dentium"
                     /db_xref="taxon:1689"
     Protein         1..335
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37982
     Region          169..333
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mketikkmlp sklieriqri ktyhslcsay kkeakrfais yaapactskt qiesllifyv
       61 hqiekgfsfd ayqygrgkna lhniallike laavdvdwrn nivykdavla lgeyrhrhma
      121 agrdisymtt lfpqdinaai iessktkypn islsyadkkd ndtvpfsvlv errhairsys
      181 dkpvcrkele qairlslrtp svcnrqpari riftdidiit qalkiqggfg gynmppalml
      241 itadlqafmg inernegyvd gglfsmslly sletcglaac plntmfndla atetrrllhv
      301 pdnevfvmyi avghfretsr icrsqrfgld rilmn
//
LOCUS       WP_003836528             228 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Bifidobacterium
            catenulatum].
ACCESSION   WP_003836528
VERSION     WP_003836528.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium catenulatum
  ORGANISM  Bifidobacterium catenulatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 228)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Bifidobacterium catenulatum"
                     /db_xref="taxon:1686"
     Protein         1..228
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=23999
     Region          147..226
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 makqdketyd syekdvydnp pagpmgvhrg arsaasramp yviviivall agllfwgvys
       61 geinnlkmpw ssqespttss aeksksgesk sksqsdsasg nktdasnags stdsqqndqn
      121 tdqntdqnae qadnataqqv vntgtevrvv natnitgyaq skadvlvqag ytsvsasnpt
      181 gnvpsqtvvw yqnetdrata envaqtlgis nvqqsdglvt pivvvlld
//
LOCUS       WP_003844522             283 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Citrobacter freundii].
ACCESSION   WP_003844522
VERSION     WP_003844522.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 283)
  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 283)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10097223
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..283
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=30018
     Region          5..281
                     /region_name="TBP_aldolase_IIB"
                     /note="Tagatose-1,6-bisphosphate (TBP) aldolase and
                     related Type B Class II aldolases. TBP aldolase is a
                     tetrameric class II aldolase that catalyzes the reversible
                     condensation of dihydroxyacetone phosphate with
                     glyceraldehyde 3-phsophate to produce tagatose 1; cd00947"
                     /db_xref="CDD:238477"
     Site            order(26..28,31,51,54..56,60,64,67..68,141,233..234,
                     236..237,240,244,247)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238477"
     Site            order(81..82,177..179,181,208..209,211,230,232..233)
                     /site_type="active"
                     /db_xref="CDD:238477"
     Site            order(82,178,208)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238477"
     Site            order(177,179,181,209,211)
                     /site_type="other"
                     /note="Na+ binding site [ion binding]"
                     /db_xref="CDD:238477"
ORIGIN      
        1 mfadmksmvt kawreqyall aincmnlesa raavrvaekh rapiilnlyq ghlehfpapi
       61 aaavvktlae easvpvalal dhgkdpvrir qafragfsgl midasafale enirqtravv
      121 elaasvslcv egelghlada prydhvtnvd lmtqaadvep fiqqtgidll avsvgtahgm
      181 yapgitpaid flrleeiarl stvplalhgg sgtpfdqlqr cptfgvakin vgaavfeagk
      241 aallhslcrd tsgelvnala lmeqaceeai ipylqasgai gka
//
LOCUS       WP_003846998             410 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Citrobacter].
ACCESSION   WP_003846998
VERSION     WP_003846998.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 410)
  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 410)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..410
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47582
     Region          1..405
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mslphlsltd arhlhlaaqg llkktrrrat padilatisr msllqidtin ivarspylvl
       61 fsrlgdyspq wlddslqqge lmeywaheac flprsdfmli rhrmlapenm gwkykaawmk
      121 ehaheieqll qhiqhngpvr sadfehprkg ssgwwewkpq krhleglfta gkvmvverrn
      181 fqrvydlthr vmphwdderd plsqedaesv mldnsarslg ifreqwlady yrlkrpalkn
      241 wcneraeqqq iipvdveglg tlwlhshlqp lleqalagkl tathsavlsp fdpvvwdrkr
      301 aeqlfdfsyr lecytpapkr qygyfvlpll hrgqlvgrmd akmhrktgvl dvislwlqdg
      361 vkpgvtlqkg lfqaiddfar wqlatrvtlg rypeglfada rhgweidpah
//
LOCUS       WP_003847748             237 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Corynebacterium
            ammoniagenes].
ACCESSION   WP_003847748
VERSION     WP_003847748.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium ammoniagenes
  ORGANISM  Corynebacterium ammoniagenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 237)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Corynebacterium ammoniagenes"
                     /db_xref="taxon:1697"
     Protein         1..237
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=24688
     Region          147..236
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mtnetvdnse neatqsadkg aaagttlplr gfamvliava vmfglwalya ftqddssdqa
       61 sqntseqtds agsnqageqe pgtvgadtae qstdvappad dadkpeqdae krdeakpape
      121 rpeareadtk gastsggsgn aapaaplkin vlnnsmtqgl aadvadrlra dgrelgevgn
      181 fseeilpett vffpkgkada eqvarelade ydgvarensn ilpdetrdgi tiilten
//
LOCUS       WP_003843036             212 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LytR C-terminal domain-containing protein
            [Bifidobacterium].
ACCESSION   WP_003843036
VERSION     WP_003843036.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 212)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..212
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=23255
     Region          83..167
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mtqaiderea rkqyvrrrqk vvfsiigaim avvmvisllf ffhvgglgtv ktatvqpnyg
       61 qqvpcavneq dgskgkyven rnitvrvlng tkfigfakav sgalenrefn tqtpdnytss
      121 kvertiiffg knainqaytv nsnftdammv mddrtdqlid ivvgatfdnl qdtkkvpaag
      181 kqiesfegcv aadkltdlpk adqhdpvnpp eg
//
LOCUS       WP_003848328             261 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Corynebacterium
            ammoniagenes].
ACCESSION   WP_003848328
VERSION     WP_003848328.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium ammoniagenes
  ORGANISM  Corynebacterium ammoniagenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Corynebacterium ammoniagenes"
                     /db_xref="taxon:1697"
     Protein         1..261
                     /product="formate/nitrite transporter family protein"
                     /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=27345
     Region          2..258
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mslnesieag vskklvlfdq dqprfavrgi lagaylalgt afagvagqvt enlapgtgsi
       61 vfaalfglgl fsivilgael atgsmmffcy gaatkqhswg kgvwmvfltt iynligvvii
      121 gaalgmsakf admdpthlls tisigkvekp idgmlvegmv anfvvnmaii ggilakevvs
      181 kffvivpiia ifvglstehv ianfcvmvia lfssdpipaa mtvgsisinw vvvwignfig
      241 ggllmggvya wlnkgpkeyr d
//
LOCUS       WP_003848469             302 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pantoea].
ACCESSION   WP_003848469
VERSION     WP_003848469.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 302)
  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 302)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 302)
  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   4  (residues 1 to 302)
  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 302)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..302
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33651
     Region          27..179
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          207..288
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mahdalchrl aqqvvtlmth ghdrlcpven vsliyanqyr prtpmmyqpg ivilfqgskt
       61 gylgstvfqy daskylmltv plpvecetwa speipiaglc lnvdtaslqd llieigdddq
      121 fqpqpqtsgi hsawltepml caaerlldvm tqprdarvlg phivreiiyy vltgpiggal
      181 lslvsrqtqf sliaralrri enhyaenlsv dalaaevnms vsafhhnfka vtqtsplqyl
      241 kryrlhqarl lmlhdglkas aaavrvgyes psqfsrefkr yfgvtpgeev nrvrqtvads
      301 sl
//
LOCUS       WP_003848696             205 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Pantoea eucalypti].
ACCESSION   WP_003848696
VERSION     WP_003848696.1
KEYWORDS    RefSeq.
SOURCE      Pantoea eucalypti
  ORGANISM  Pantoea eucalypti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 205)
  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 205)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 205)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Pantoea eucalypti"
                     /db_xref="taxon:470933"
     Protein         1..205
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=21924
     Region          1..204
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 mevysneneq tdalrnffas ngkalaigvv igiaalggwr ywsshqddta ksvsaqyqql
       61 tsamqagkpe tleavnrfas ensntygala amdlakqyvd agqldkaasl lqnglkdtkd
      121 anlqavinlr lariqlqqnq adaalktldg vkgdgwtaiv adirgeallt kgdkqgarda
      181 wskgvesdas palkqmmqmk mnnls
//
LOCUS       WP_003850027             276 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Corynebacterium diphtheriae].
ACCESSION   WP_003850027
VERSION     WP_003850027.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium diphtheriae
  ORGANISM  Corynebacterium diphtheriae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
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   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   4  (residues 1 to 276)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Corynebacterium diphtheriae"
                     /db_xref="taxon:1717"
     Protein         1..276
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=29830
     Region          1..269
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 miefesvskr ygkrgekava dfslfipkgk ttvlvgssgs gkttllrmin rmveptegrv
       61 ivrgkdvaet dpvqlrrsig yviqsagllp hrtviqnial vptlnkepka eierrakqal
      121 advdlepsla nrypgelsgg qqqrvgvara lasdpdillm depfgavdpi vrrslqkqli
      181 dlqsrlrktv vmvthdidea fcvgdhivvl ekggkiaqqg spahifahpa ndfvasflgs
      241 dqenrslyte lidghtvvvd tfgrplgtlg dgatcg
//
LOCUS       WP_003840973             249 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Bifidobacterium dentium].
ACCESSION   WP_003840973
VERSION     WP_003840973.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium dentium
  ORGANISM  Bifidobacterium dentium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Bifidobacterium dentium"
                     /db_xref="taxon:1689"
     Protein         1..249
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=27223
     Region          98..237
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mprrrnathf rkkrfnaegp verilcllvi aavvgitigl ilpktsptvg eitgeytatg
       61 saaetlerlt vddnpskagy drtafgyrqt dadgngcdvr edvlardltd vryqsaggck
      121 vqsgtlndpy tgktihfrrg rdtssavqid hvvalenawq sgarewsrak ryeygndmyn
      181 llavdgpanq ekgsasaayw lptngdyrcd yvarqigvkd kygltvtike kramlsvlhg
      241 cpaqsipes
//
LOCUS       WP_003851038             196 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Corynebacterium diphtheriae].
ACCESSION   WP_003851038
VERSION     WP_003851038.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium diphtheriae
  ORGANISM  Corynebacterium diphtheriae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Corynebacterium diphtheriae"
                     /db_xref="taxon:1717"
     Protein         1..196
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=22360
     Region          <106..172
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mkrifftllv amtcfavyls iphgwyfhdl revshrvtvi gyersqfgdg walqssgcst
       61 rdevlaatli dahltvdcsl trgygddpys lrpiavhpgr drepieldhv yplsaawdmg
      121 afawdkerri afandplnlv aaskqqnrqk sdklpsewlp sarkqrcwyv nrladvarky
      181 dlplssadlr vmrrqc
//
LOCUS       WP_003852110             376 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Pantoea].
ACCESSION   WP_003852110
VERSION     WP_003852110.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 376)
  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 376)
  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
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 376)
  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   5  (residues 1 to 376)
  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   6  (residues 1 to 376)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 376)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 376)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..376
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41354
     Region          13..70
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          79..371
                     /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 mvhgysaghd velnrsekli lelvrrndgi srsslvsqti lnqssvhriv dtltengfls
       61 lgespsqgrg kpspslslna narygygisi nsdsvaasli nfrggiteyc vldthprdpa
      121 rtllnikhhy ldtlkqygis pekvcgvgys magflydsrk yfnppeplkn wmgidlrrei
      181 tmlfdrpvwi ennattaaha eaflgaglky dtfgylsfny gfgggiving kpfqgafgna
      241 geisriftpe egklrpalgi lidrlrhggi eikdirdlnh kfdpawpiaq qwveevtpnl
      301 hramdamnav idpaaiilgg eiprklgemf lamprtcsgk rwdisaeypd illsaiegds
      361 salgaaltpl retyfn
//
LOCUS       WP_003845416             229 aa            linear   BCT 20-JAN-2025
DEFINITION  YaaA family protein [Corynebacterium ammoniagenes].
ACCESSION   WP_003845416
VERSION     WP_003845416.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium ammoniagenes
  ORGANISM  Corynebacterium ammoniagenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Prahlad,J., Yuan,Y., Lin,J., Chang,C.W., Iwata-Reuyl,D., Liu,Y., de
            Crecy-Lagard,V. and Wilson,M.A.
  TITLE     The DUF328 family member YaaA is a DNA-binding protein with a novel
            fold
  JOURNAL   J Biol Chem 295 (41), 14236-14247 (2020)
   PUBMED   32796037
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Liu,Y., Bauer,S.C. and Imlay,J.A.
  TITLE     The YaaA protein of the Escherichia coli OxyR regulon lessens
            hydrogen peroxide toxicity by diminishing the amount of
            intracellular unincorporated iron
  JOURNAL   J Bacteriol 193 (9), 2186-2196 (2011)
   PUBMED   21378183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006857
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Corynebacterium ammoniagenes"
                     /db_xref="taxon:1697"
     Protein         1..229
                     /product="YaaA family protein"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=25211
     Region          2..219
                     /region_name="YaaA"
                     /note="DNA-binding protein YaaA associated with the
                     oxidative stress response [Replication, recombination and
                     repair]; COG3022"
                     /db_xref="CDD:442258"
ORIGIN      
        1 mliilppset kafggdgdpl dlaslsfpsl hdnrqniidi lrqydvdeam kvlkisealr
       61 aeaeenskll tgptmpalyr ytgvlydald aktlsdkawd qlaigsalfg vvrprdmipf
      121 yrlsggtkly datmksrwgn sitkaleaed dfiidlrsgt yqalgrvksa vtvrvenseg
      181 kvishfnkfh kgqlaraiag kdlhsiedim dtpgfrftev ngtqltmvv
//
LOCUS       WP_003854405             249 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Corynebacterium glutamicum].
ACCESSION   WP_003854405
VERSION     WP_003854405.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium glutamicum
  ORGANISM  Corynebacterium glutamicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 249)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Corynebacterium glutamicum"
                     /db_xref="taxon:1718"
     Protein         1..249
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=26151
     Region          143..249
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 maknsrirys asikrgaaai ltaaatsval iavpatasaq dlatgssqiq tdaregawat
       61 rntiqdqlas igpaalpvra avdnaingmf pglvdekvaa eqeaaraeae reaaaareae
      121 aarvaaeeaa rfdrgscpai advcvdidgg rtwlqengqv tygavpvssg gvgqetprgt
      181 fyinrkvkde isyefgnapm pyamyftyng hafhqgnvat tsagcvrlnt qdaiyyfnnv
      241 gigdmvyiy
//
LOCUS       WP_003855431             193 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Corynebacterium glutamicum].
ACCESSION   WP_003855431
VERSION     WP_003855431.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium glutamicum
  ORGANISM  Corynebacterium glutamicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Corynebacterium glutamicum"
                     /db_xref="taxon:1718"
     Protein         1..193
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20988
     Region          5..184
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mslsvveait nrratrkytd eaptpelidk ivnlaleaps afnaqqreiv vitdpaqkqk
       61 lyeashqkqf ltapvtfiav arvenepedl eeilgterae rvagfingrs lqqareatlr
      121 daslaaafli laaqaeglst spttgwdeek vkaaigiggr ddraialvia agfpneqpeh
      181 pgrlqnrrid nsy
//
LOCUS       WP_003858222             409 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Enterobacter].
ACCESSION   WP_003858222
VERSION     WP_003858222.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 409)
  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 409)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Enterobacter"
                     /db_xref="taxon:547"
     Protein         1..409
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47254
     Region          1..405
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mslpqlslaa arnlhlaaqg llkkprrraq padilstvqr msllqidtin ivarspylvl
       61 fsrlgnyppq wldnalsqge lmeywaheac flprsdfalv rhrmlapdkm gwkyrqewmv
      121 ehadeieqli ahiqkngpvr sadfehprkg asgwwewkph krhleglfts gkvmvverrn
      181 fqrvydlthr vmphwddtrd llsqevaeai mlgnsarslg iflpqwlady yrlrqpqlkp
      241 lletwqreqr vmpvsveslg emwlhadlfp llaqaqegkl qathsavlsp fdpvvwdrkr
      301 aeqlfdfsyr lecytpaprr qygyfvlpll hkgqlvgrmd akmhrktgml eiialwleeg
      361 ikvtaglekg lttalsefar wqgaheivlg rvpvelfatc rdgwetdtp
//
LOCUS       WP_003858253             628 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Corynebacterium glutamicum].
ACCESSION   WP_003858253
VERSION     WP_003858253.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium glutamicum
  ORGANISM  Corynebacterium glutamicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 628)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 628)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 628)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 628)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 628)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 628)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..628
                     /organism="Corynebacterium glutamicum"
                     /db_xref="taxon:1718"
     Protein         1..628
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68828
     Region          5..628
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mlnrmksarp ksvapksgqa lltlgalgvv fgdigtsply slhtafsmqh nkvevtpenv
       61 ygiismvlwt itlivtvkyv mlvtradnqg qggilalval lknrghwgkf vavagmlgaa
      121 lfygdvvitp aisvlsateg ltvispsfer filpvslavl iaifaiqplg tekvgkafgp
      181 imllwfvtla glgipqiiah peilqslsph walglivaep fqafvllgav vltvtgaeal
      241 yadmghfgar pirvawfcvv mpaliltylg qgalvinqpe avrnpmfyla peglriplvi
      301 latiatvias qavisgaysl tkqavnlkll prmvirhtsr keegqiympl vngllfvsvm
      361 vvvlvfrsse slasayglav tgtlvlvsvl yliyvhttww ktalfivfig ipevllfasn
      421 ttkihdggwl plliaavliv vmrtwewgsd rvnqeraele lpmdkflekl dqphniglrk
      481 vaevavfphg tsdtvplslv rcvkdlklly reivivqivq ehvphvppae raemevlhha
      541 pirvvrvdlh lgyfdeqnlp dhlhaidptw dnatyflsal tlrsrlpgki agwrdrlyls
      601 mernqasrte sfklqpskti tvgtelhl
//
LOCUS       WP_003860622             249 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Corynebacterium].
ACCESSION   WP_003860622
VERSION     WP_003860622.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 249)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..249
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=26125
     Region          143..249
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 maknsrirys asikrgaaai ltaaatsval iavpatasaq dlatgssqiq tdaregawat
       61 rntiqdqlas igpaalpvra avddaingmf pglvdekvaa eqeaaraqae reaaaareae
      121 aarvaaeeaa rfdrgscpas advcvdidgg rtwlqengqv tygavpvssg gvgqetprgt
      181 fyinrkvkde isyefgnapm pyamyftyng hafhqgnvat tsagcvrlnt qdaiyyfnnv
      241 gigdmvyiy
//
LOCUS       WP_003861257             180 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease family protein [Corynebacterium].
ACCESSION   WP_003861257
VERSION     WP_003861257.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..180
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=19822
     Region          <69..>138
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mknfirvlia fsvflciytv aphigrgpgd lapvtaipqr atvlgydras mfggwlggvr
       61 egivdeagdt dpysgnrldl ssaevdhilp lsaawdlgah rwsagerisf andplnlvlv
      121 skaenqeksd qlpsewlpsd rharcwyver lfavanayel plpeddirvs rkqcgfakpw
//
LOCUS       WP_003847669             303 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Corynebacterium
            ammoniagenes].
ACCESSION   WP_003847669
VERSION     WP_003847669.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium ammoniagenes
  ORGANISM  Corynebacterium ammoniagenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Corynebacterium ammoniagenes"
                     /db_xref="taxon:1697"
     Protein         1..303
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33511
     Region          17..289
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 msgaweqqpa kllhhydrta qhaahqiirr ysnsfslasn llrghvktdi rnlyavvria
       61 deivdgagyg agldtsqcqq llddyerqvl aaphqrlhsd pvlhayaisa rrcefkdeyl
      121 saffasmrrd lspqsgnkqq efddyiygsa evigllclqa flvgqnptpd argvmehgar
      181 tlgaafqkin flrdiandtq flgrtyfpql eeqelddalk aelvadirsd ltvarssisy
      241 lpanarigvi aateifaelt ndidrisaae llstrvslsp arkvivlarv priaaqrkgg
      301 srs
//
LOCUS       WP_003863249             193 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Corynebacterium].
ACCESSION   WP_003863249
VERSION     WP_003863249.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..193
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21151
     Region          5..184
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mslsvveait nrratrkytd eaptpelidk ivdlaleaps afnaqqreiv vitdptqkqk
       61 lyeashqkqf ltapvtfiav arvenepedl eeilgterae rvagfingrs iqqtreatlr
      121 daslaaafli laaqaeglst spttgwdeek vkeaiglggr edraialvia tgfpneqpeh
      181 pgrlqnrrid nsy
//
LOCUS       WP_003863608             628 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Corynebacterium].
ACCESSION   WP_003863608
VERSION     WP_003863608.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 628)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 628)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 628)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 628)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 628)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 628)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..628
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..628
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=69004
     Region          5..628
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mlnrmksarp ksvapksgqa lltlgalgvv fgdigtsply slhtafsmqh nkvevtpenv
       61 ygiismvlwt itlivtvkyv mlvtradnqg qggilalval lknrghwgkf vavagmlgaa
      121 lfygdvlitp aisvlsateg ltvispsfer filpvslavl iaifaiqplg tekvgkafgp
      181 imllwfvtla glgipqiivh peilqslsph walrlivaep fqafvllgav vltvtgaeal
      241 yadmghfgar pirvawfcvv mpaliltylg qgalvinqpe avrnpmfyla peglriplvi
      301 latiatvias qavisgaysl tkqavnlkll prmvirhtsr keegqiympl vngllfvsvm
      361 vvvlvfrsse slasayglav tgtlvlvsvl ylvyahttww ktalfivfig ipevllfasn
      421 ttkihdggwl plliaavliv vmrtwewgsd rvnqeraele lpmdkflekl dqphniglrk
      481 vaevavfphg tsdtvplslv rcvkdlklly reivivrivq ehvphvppee raemevlhha
      541 pirvvrvdlh lgyfdeqnlp enlhaidptw dnatyflsal tlrsrlpgki agwrdrlyls
      601 mernqasrte sfklqpskti tvgtelhl
//
LOCUS       WP_003862897             221 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LytR C-terminal domain-containing protein
            [Corynebacterium].
ACCESSION   WP_003862897
VERSION     WP_003862897.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 221)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..221
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=22361
     Region          131..218
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mtsdmqnspq hsatpseekq gglpmrglam iliavavlla awalwsmqgk ddtsttsagq
       61 tqstetnagt iaessgssds eqasaepgts eetsaeqpaa dgeaanaagt aasggassan
      121 gnstpvntly vlnnstvpql aarvadslsg dyqkvesgnl pdtiipqntv yftagnteae
      181 kaareladrv sgvamersda lptetegkda lvlvlvqdva l
//
LOCUS       WP_003863157             290 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Enterobacter].
ACCESSION   WP_003863157
VERSION     WP_003863157.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Enterobacter"
                     /db_xref="taxon:547"
     Protein         1..290
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32751
     Region          14..255
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 maepqlllny tghlpecptw saeekalywa dilegeihry hlptaehsvl sfheevgcfa
       61 lrerggfiva mrnaiwltdk hgllqrkvcd npsnpqlarf ndggtdhqgr fyagtfwgpg
      121 dyngallmri dndltpkviq cdihghngla fspdkrwmft sdtpngviyr tpldeqgepg
      181 kreefrrfse gdgipdgaam deegcywsal fdgwriarfs pqgeqleeyr lpvrcptmvc
      241 fggddmktlf itttrenmea eelakyplsg aiftlpvnva gmkksrfieh
//
LOCUS       WP_003862489             299 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Enterobacter].
ACCESSION   WP_003862489
VERSION     WP_003862489.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 299)
  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 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   3  (residues 1 to 299)
  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   4  (residues 1 to 299)
  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 299)
  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 12071874
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_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          28..171
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          207..288
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mnrdaicrql tsqiktlidn gndsaellpd irllygtqpg trtpvmyqpg ivflfsghki
       61 gyinervfry dtneyllltv plpfecetfa teevplagir vnvdilqlqe llmdigedel
      121 frpsmaasgi nsatlseeil caierlldvm erpldarilg kqiireilyh vllgpgggal
      181 lalvsrqthf slisrvlkri esqytenlsv dqlaaeanms vsafhhnfks vtstsplqyl
      241 ktyrlhkarm lmihdgmkas aaamrvgyes asqfsrefkr yfgvtpgeda srirtmqga
//
LOCUS       WP_003865363             210 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Holdemanella
            biformis].
ACCESSION   WP_003865363
VERSION     WP_003865363.1
KEYWORDS    RefSeq.
SOURCE      Holdemanella biformis
  ORGANISM  Holdemanella biformis
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Erysipelotrichaceae; Holdemanella.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 210)
  AUTHORS   ter Beek,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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Holdemanella biformis"
                     /db_xref="taxon:1735"
     Protein         1..210
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=23886
     Region          2..>199
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mlevqiykkl aefdldvsfq vddyilglmg asgsgksmtl kciagietpd qgrivlngrv
       61 lfdsekkinv piqkrnvgym fqsyalfpnm nvyenisvgl rarkvkdvdi vvqkvmqqfr
      121 ifelasrypk qlsggqrqrv alarlmayep dvllldepfs aldedlkedl lqelkselqi
      181 skpvifvshd keevnylcdl kykikqgeii
//
LOCUS       WP_003868185             386 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [Thermoanaerobacter].
ACCESSION   WP_003868185
VERSION     WP_003868185.1
KEYWORDS    RefSeq.
SOURCE      Thermoanaerobacter
  ORGANISM  Thermoanaerobacter
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Thermoanaerobacter"
                     /db_xref="taxon:1754"
     Protein         1..386
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=40740
     Region          <1..382
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mkimgyvrpd grvgirnhil iipssvcase vamriashve gavalanqhg ccqigadlel
       61 taktlvglgk npnvaaalvv glgcegvpte kvaeeiaatg krveyiiiqd cggtlkaeei
      121 gtriarqmaq eaallkreev disnlilave cggsdttsgl asnpvagyvs dklielggts
      181 mfsetteiig aehllakrav srevadklle ivrrceekak tmgvdmrggq ptpgnieggi
      241 stieeksmga iykggtkpiq gildyaeppa ekgglyimdt pgqdiesitg mtaggaqvvi
      301 fttgrgtptg spiapvikit anpdtykkme dnidfnagti vqgdetirea gerlfkemie
      361 vvngkltkae vlkhrefgiy klistf
//
LOCUS       WP_003865177             297 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Holdemanella biformis].
ACCESSION   WP_003865177
VERSION     WP_003865177.1
KEYWORDS    RefSeq.
SOURCE      Holdemanella biformis
  ORGANISM  Holdemanella biformis
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Erysipelotrichaceae; Holdemanella.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Holdemanella biformis"
                     /db_xref="taxon:1735"
     Protein         1..297
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33759
     Region          3..269
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mnrfdlhmhs cyssdgqftp kelieiakek glktialsdh dcisgvkemi rlgneagiev
       61 ipaiecstsi gytdvhllgy gidldndyfq nllektqvks rnafstrcdr lrakygveid
      121 eeailkeang knpwfvmcth mfndpryqdi pdfkdyipgg krsdpapvnf fwdkcqygsd
      181 lfvyvpmpdf lesvqkihea gglaivahpf ttfykndeml killesgvdg ieaysnyhtp
      241 eqnvyyenla kehhllitcg sdfhgekkps iqmgeyglek dgslwleqfk eklkaar
//
LOCUS       WP_003875037             238 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Mycobacterium avium].
ACCESSION   WP_003875037
VERSION     WP_003875037.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium avium
  ORGANISM  Mycobacterium avium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Mycobacterium avium"
                     /db_xref="taxon:1764"
     Protein         1..238
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=25588
     Region          90..231
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mnvnrkvllw laaaaalavl vayqavgsst rhtaeyaara dvptvqpgtd vlagiavlpv
       61 rqhrydylrs afgdawdddn dapmghngcd trddilnrdl vdktyvsvkr cpdavatgtl
      121 hdpytnktia fqrgpkvges vqidhivpla yawdmgayaw pgperrrfan dpanllavdg
      181 qanqdkgdaa paqwmppnaa fhcqyamqfi avlrgyalpv dqastgvlrq aaatcpag
//
LOCUS       WP_003876692             280 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Mycobacterium avium].
ACCESSION   WP_003876692
VERSION     WP_003876692.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium avium
  ORGANISM  Mycobacterium avium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 280)
  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 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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Mycobacterium avium"
                     /db_xref="taxon:1764"
     Protein         1..280
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30667
     Region          <49..248
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          164..247
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mvgyrtldvp egvhrgmpss mltfivsldd gveaadtata lpaarptpli lgglhlrash
       61 vrqrrgqagv qlavhplasr alfglpsaei pvadydatav lgrdivdlhh rvaeahrwpd
      121 vfalvaqyli darrrrdgat vrpevlhawh llqrsrglmp vtaladavgv ttrhlatlfr
      181 revghspktv amlmrfqhat gliaesarrh grvdlarvaa dtgysdqahl srefvrfagv
      241 ppqrwlaeef rniqdgghsl gsqwehdcfe sdrlvdtasp
//
LOCUS       WP_003877334              94 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Mycobacterium avium].
ACCESSION   WP_003877334
VERSION     WP_003877334.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium avium
  ORGANISM  Mycobacterium avium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 94)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 94)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 94)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 94)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Mycobacterium avium"
                     /db_xref="taxon:1764"
     Protein         1..94
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=9675
     Region          12..94
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mgrvpvqang isvtvryfaa araaagaese tvvvvvrpgt tvgelverla vrgsrlaevl
       61 srcsylcdgi avrdetqslr sgdtidvlpp fsgg
//
LOCUS       WP_003879662             349 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Mycolicibacterium].
ACCESSION   WP_003879662
VERSION     WP_003879662.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium
  ORGANISM  Mycolicibacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Mycolicibacterium"
                     /db_xref="taxon:1866885"
     Protein         1..349
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37400
     Region          5..328
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mtdaivvrga nkhygdfaal dnidfevpsg sltallgpsg sgkstllrai agldqpdsgt
       61 itingrdvtg ippqrrgigf vfqhyaafkh ltvrdnvafg lkirkrpkae vkekvdnlle
      121 vvglagfqtr ypnqlsggqr qrmalarala vdpqvlllde pfgaldakvr ddlrtwlrrl
      181 hdevhvttvl vthdqaeald vadriavlnk grieqvgspt evydepanaf vmsflgavse
      241 lngilvrphd irvgrnpela vaagdgtaea tgvlratidr ivmlgfevrv eltsaathvp
      301 ftaqitrgda ealglregdt vyvratrvpq iaggaqvpas nedepltvs
//
LOCUS       WP_003866481             412 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Cutibacterium
            namnetense].
ACCESSION   WP_003866481
VERSION     WP_003866481.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium namnetense
  ORGANISM  Cutibacterium namnetense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (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   2  (residues 1 to 412)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Cutibacterium namnetense"
                     /db_xref="taxon:1574624"
     Protein         1..412
                     /product="aminoglycoside 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=44859
     Region          160..357
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mrrpawlggp gkdadgavll tgpgagellk tavehaggdl idwhldhvdt npgqsttaty
       61 qawvqwpagk rqelfgmsar asgpvvtdsr adiyvdgsre vavwrypddp dlpglsraay
      121 pehmaaiisd ldlvgarvsa qqinlrmigy rprrravlcv evsnrrfyvk vlrdgifqat
      181 larhdlltra svpsptvagv tednllflte lpgcplskal felgtpctae slvdlldqlp
      241 pqvcdlprrs pwsesvdhyc rmvaaalpdq serlermaqt iaqgladvpa gnepthgdfh
      301 egqihvwngq vcgildvdti gpgrraddla clvahlstvq rmnafqadrm rqiltawvpv
      361 fdsrvdpiel rlrsaavais latgpyrsqe dnwqaetlst vdaaealidq vv
//
LOCUS       WP_003874017             426 aa            linear   BCT 20-JAN-2025
DEFINITION  DNA polymerase domain-containing protein [Mycobacterium avium].
ACCESSION   WP_003874017
VERSION     WP_003874017.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium avium
  ORGANISM  Mycobacterium avium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Zhu,H., Nandakumar,J., Aniukwu,J., Wang,L.K., Glickman,M.S.,
            Lima,C.D. and Shuman,S.
  TITLE     Atomic structure and nonhomologous end-joining function of the
            polymerase component of bacterial DNA ligase D
  JOURNAL   Proc Natl Acad Sci U S A 103 (6), 1711-1716 (2006)
   PUBMED   16446439
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Zhu,H. and Shuman,S.
  TITLE     A primer-dependent polymerase function of pseudomonas aeruginosa
            ATP-dependent DNA ligase (LigD)
  JOURNAL   J Biol Chem 280 (1), 418-427 (2005)
   PUBMED   15520014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Mycobacterium avium"
                     /db_xref="taxon:1764"
     Protein         1..426
                     /product="DNA polymerase domain-containing protein"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=47286
     Region          4..312
                     /region_name="LigD"
                     /note="Eukaryotic-type DNA primase [Replication,
                     recombination and repair]; COG3285"
                     /db_xref="CDD:442515"
ORIGIN      
        1 mnhmtrpvsl evagrrvtit hpdkvvfpra gggettgsaa gphtkldlvr yylsvadgal
       61 rgvagrpmil krfvkgitqe avfqkrapan rpdwvdvael ryargtsaae avihdaagla
      121 wlinlgcvdl nphpvladdl dhpdelrvdl dpmpgvswrr ivdvalvare vledygltpw
      181 pktsgsrgfh iyariarrwe frqvrlaaqt vareverrap eaatsrwwke eregvfvdfn
      241 qnakdrtvas aysvratpda rvstplrwde vagcrpepft idtvparlae igdpwagmdd
      301 avgdldrllv laeelgpper apkgagtrsg grrrssmpli evartktrde amaaldvwrd
      361 rhpeaaarlq padvlvdgmr gpssiwyrir inlqhipedq rppqeeliad yspwqgyggr
      421 qkpswg
//
LOCUS       WP_003874381             215 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Mycobacterium avium].
ACCESSION   WP_003874381
VERSION     WP_003874381.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium avium
  ORGANISM  Mycobacterium avium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Mycobacterium avium"
                     /db_xref="taxon:1764"
     Protein         1..215
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23882
     Region          7..210
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mtlnlsvdev ltttrsvrkr ldfdkpvpre vlmeclelal qaptgsnaqg wqwvfvedad
       61 kkktiadiyl anaraylslp aaeypegdtr germpkvkds avylaehmhe apvllipcle
      121 grvenaplgl sasfwaslfp aawsfclalr srglgtcwtt lhlindgekq aaellgiphd
      181 rysqgglfpi aytkgtdfrp akrlpaeqvt hwdsw
//
LOCUS       WP_003886125             344 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Mycolicibacterium phlei].
ACCESSION   WP_003886125
VERSION     WP_003886125.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium phlei (Mycobacterium phlei)
  ORGANISM  Mycolicibacterium phlei
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Mycolicibacterium phlei"
                     /db_xref="taxon:1771"
     Protein         1..344
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38456
     Region          171..325
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mtatprshtr tgrpelpvll lrvwraiwlr atstphgrer ryvkrgirey krsaasgaap
       61 yllrrnvhri ekgltmrpvr dtfatdyirp tvdafraglr tgtlrpghpe fnwiysvlrt
      121 yfdvtasssh raivsareaf gdaastidve tpdsgphpai plqptvkidd lealavgrrs
      181 vrwftsepva rdlvdravav gaesptacnr qpyrfeifdd pvstakvaai pmgtdgydhq
      241 ipgliviigd laaffdprdr hliyidscla amgviyalea qgvntccinw pdlperevem
      301 rkllglkpse rvvmliaygy adpdamvpys akrlideirt yrtl
//
LOCUS       WP_003886662             288 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Mycolicibacterium phlei].
ACCESSION   WP_003886662
VERSION     WP_003886662.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium phlei (Mycobacterium phlei)
  ORGANISM  Mycolicibacterium phlei
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 288)
  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 288)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 288)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 288)
  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   5  (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   6  (residues 1 to 288)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Mycolicibacterium phlei"
                     /db_xref="taxon:1771"
     Protein         1..288
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31262
     Region          19..101
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          126..286
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 midalnrlvg eieahlgedi didafaasvg tteyhlrrmf sslagmpvse yvrrrrmtva
       61 aadvvggedf ltiavrygyg steafgrafk svhgvshgqv rrdggplrsq pqlrfrltve
      121 gstpvdariv drpafrligh aarvpliyeg vnphierhia aipaeeherl kglsdtepag
      181 llqvsadvdp dyregselty llgvavsvdt avpddldvid vpagpwvvfr tsgahpealq
      241 sayaasatew fpsnpwrlrp gpsivavldr apdfstatcd lwmpvera
//
LOCUS       WP_003887517             408 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein
            [Mycolicibacterium phlei].
ACCESSION   WP_003887517
VERSION     WP_003887517.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium phlei (Mycobacterium phlei)
  ORGANISM  Mycolicibacterium phlei
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 408)
  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 408)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Mycolicibacterium phlei"
                     /db_xref="taxon:1771"
     Protein         1..408
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45757
     Region          1..404
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 masrltadqa rrvavaaqgf aeprlrgpvt rahlrrlisr iqvlqldsvs vavrahyapv
       61 fsrlgpydrd lldraawshs araprmlvey waheaalmav edwpllrwrm reythgrwgt
      121 eivkrnarlv devvaavtel gpatagqiee ylgaeqrgrk gpwwdrsdtk wvtealfasg
      181 vlttatrvgf arhydlaerv lppdvlarev deddavrelv lraagalgvg teqdlrdyfr
      241 lspaqvkpai aklvadgele pvqvdgwkgt aylragqavl rrdrgtallc pfdpliffrp
      301 rvarlfgfey rleiytpapk rrwgyyvwpf lldgelvarv dlkadrsada lrvvgafvep
      361 greptrvaea lvgelqamag wlglgdvtvg rrgdlapvlr rvwgrrtr
//
LOCUS       WP_003888311             290 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Mycolicibacterium phlei].
ACCESSION   WP_003888311
VERSION     WP_003888311.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium phlei (Mycobacterium phlei)
  ORGANISM  Mycolicibacterium phlei
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 290)
  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 290)
  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   3  (residues 1 to 290)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Mycolicibacterium phlei"
                     /db_xref="taxon:1771"
     Protein         1..290
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32068
     Region          172..279
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mrpfvgteal aagvvtryql ktryraifrn vyvaaehdvs pvdkaigawl wsgrrataag
       61 lsaaalhgtr wisskspael nqpsrhktpg illhsdtlae devcvlrgvp attpartafd
      121 lgrrggveta viridaliha trlkteaves viaqhrgarg lvqlrtvlkl sdpgaespqe
      181 trtrlvltea glrpthtqie vydgydqigr idmgyprwkv gveydgiqhw tdpwvrnrdi
      241 hrqadfdrlg wrivrvnadm vryrrdlivs rtraaleaag adlsasnvsl
//
LOCUS       WP_003879878             138 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein, partial [Mycolicibacterium fortuitum].
ACCESSION   WP_003879878
VERSION     WP_003879878.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium fortuitum (Mycobacterium fortuitum)
  ORGANISM  Mycolicibacterium fortuitum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Mycolicibacterium fortuitum"
                     /db_xref="taxon:1766"
     Protein         1..>138
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
     Region          11..>137
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mledflrdhd gvitlahakq aglsqdavnr rvrsgkwlrc srgvyfaddr pftdaarira
       61 avwsagpnav asglaaawwh evtkyppdtv evtiprtghh pkqhgvklrr rdldphdive
      121 rrglrvtalp ltvveaaa
//
LOCUS       WP_003889834             221 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Mycolicibacterium phlei].
ACCESSION   WP_003889834
VERSION     WP_003889834.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium phlei (Mycobacterium phlei)
  ORGANISM  Mycolicibacterium phlei
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Mycolicibacterium phlei"
                     /db_xref="taxon:1771"
     Protein         1..221
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24584
     Region          8..200
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mrqptndvwe tlatarairr ftdepvddav ldrcleaatw apnganaqlw rfivldspeq
       61 ravvaqaaql alqaiekiyg msrpadndts raarnnraty elhdragelt svlftayrne
      121 faseflqggs ifpamqnfyl aaraqglgac ftswtsygge klireavgvp dewvlaghiv
      181 vgwprgqhgp vrrrpisevv frnhwdpera diiygagark r
//
LOCUS       WP_003889939             276 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Mycolicibacterium
            phlei].
ACCESSION   WP_003889939
VERSION     WP_003889939.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium phlei (Mycobacterium phlei)
  ORGANISM  Mycolicibacterium phlei
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Mycolicibacterium phlei"
                     /db_xref="taxon:1771"
     Protein         1..276
                     /product="formate/nitrite transporter family protein"
                     /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=29643
     Region          24..246
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msntrqrrlg dsdspiedel etafrrmvde gtqrlhrtwr evlvtgffgg tevavgvlay
       61 lsvlhsgqnq lvaglafsig flalllgrse lftegflvpv ttvaagragp gqlaklwsgt
      121 lvanlvggwv lmalimaafp klheqtiesa ehfvfaplsv esvalavlgg mvitlmtrmq
      181 hgtdstvgki aaavagafvl aglglfhsil dsllifgalc tgaapfgyld wlawfwytal
      241 anmvgglalv tllrllrskd rieeererad kddpvr
//
LOCUS       WP_003891669             392 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Mycolicibacterium smegmatis].
ACCESSION   WP_003891669
VERSION     WP_003891669.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium smegmatis (Mycobacterium smegmatis)
  ORGANISM  Mycolicibacterium smegmatis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 392)
  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 392)
  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
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 392)
  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   5  (residues 1 to 392)
  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   6  (residues 1 to 392)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 392)
  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 15726307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Mycolicibacterium smegmatis"
                     /db_xref="taxon:1772"
     Protein         1..392
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40621
     Region          2..>67
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          73..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 mpppatlvsp tpgevfalir drrattrgel grltglsrta vtarvaalea gglvierdqa
       61 stggrpaaql tfnvdagvvf saaigrsrtq lavcnldgti lastdidqep giapddlmpd
      121 lvkrldtlld esgrrgvrif gvglslpgtv dqrtgaslds pnmsgwdgvp lapyftsltd
      181 apvvidndan aiavaerrgg ygeyddmlvv kastglaagi imggqlqrga vqaagefghs
      241 ktaaaagvhc rcgdtgclea iaggwalvra lqrdgravnh lrdvvalaht gdpearrmir
      301 esgrhigevl aaavnllnpa vlviagdmvg aydlfvaglr etlygnatal atrtlqivps
      361 ihrerssmvg catnvldrvl spdavdaamy gd
//
LOCUS       WP_003892619             627 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Mycolicibacterium smegmatis].
ACCESSION   WP_003892619
VERSION     WP_003892619.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium smegmatis (Mycobacterium smegmatis)
  ORGANISM  Mycolicibacterium smegmatis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 627)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Mycolicibacterium smegmatis"
                     /db_xref="taxon:1772"
     Protein         1..627
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=69814
     Region          58..>457
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mtspdltevn idrlaelfpn vitetldadg npkkavdfdl lrqelsdhvv egpqeryrld
       61 wpgkreaafa anapiaktlr pireesvnfd ttknlfiegd nlealkllqe sylgkvkliy
      121 idppyntgnd fvysddfaes tkeylersgq sddngvklva ntesngrfhs dwlsmmyprl
      181 klarnlladd glmfvsidds eaaglshiag eifgrdnvva aiawekrytr snnangfysv
      241 kdtillcrrs isagrikevr gdgaadiysn pdnddrgvwt sssyvnpatk earpnlaypi
      301 trpsdgaiie hpthawkfse geherhirdn rlwwgkdgta qyprlkvfls elsegmvpid
      361 lwshedagtt daggaevkel fdgaavfdfp kptrllrkil giyvppwnsw addfivldff
      421 agsssmahav laqngadggk rrfvmvqlpe pcppksiaas qgyeniaqls rerirragrr
      481 iledaplmae sldvgfralr vdstnmadvl rspddtvqqt lgtlessvks nrsgddllfq
      541 vlldwglelt mpltveqleg revfvvddda liacfdsdvs pelvrtiakr eplravfrds
      601 gfasddarin aeqifreisp atdikai
//
LOCUS       WP_003892898             232 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Mycolicibacterium smegmatis].
ACCESSION   WP_003892898
VERSION     WP_003892898.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium smegmatis (Mycobacterium smegmatis)
  ORGANISM  Mycolicibacterium smegmatis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Mycolicibacterium smegmatis"
                     /db_xref="taxon:1772"
     Protein         1..232
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25886
     Region          12..216
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mvegdkrlgl tadevltttr avrkrldysr pvprelvtec vriatqapsg rnrqrwdfvv
       61 vddprlrsrv aeiwrrglfa gvpgtggrhe isrmtspeew rriaagldhl aahlheapml
      121 lipcvrvasr relatvrgqa gawgsvlpav wsfmlaarer glgtawttch lsyelemael
      181 lgidadhvvq aaltpvaftr gtefrpgpra dhrdflhwnt wdgrsragrk tg
//
LOCUS       WP_003893769             234 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Mycolicibacterium smegmatis].
ACCESSION   WP_003893769
VERSION     WP_003893769.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium smegmatis (Mycobacterium smegmatis)
  ORGANISM  Mycolicibacterium smegmatis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Mycolicibacterium smegmatis"
                     /db_xref="taxon:1772"
     Protein         1..234
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=25522
     Region          86..208
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mtrrrtwwla llvalavfva yqtisvsser smvadadvpt vapgadvlag vavvparmrg
       61 hdyrrvafgd awtddndapg ghngcdtrnd ildrdlvdkt ytsisrcpta vatgvlhdpy
      121 tnltipftrg nktgaavqie hivplayawd qgarywpqqm rvrfandpan lvavqgqanq
      181 dkgdkepalw mppnaafhcq yamqfievmr gyalpvdaps vpvlrqaadt cprg
//
LOCUS       WP_003894756             172 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Mycolicibacterium
            smegmatis].
ACCESSION   WP_003894756
VERSION     WP_003894756.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium smegmatis (Mycobacterium smegmatis)
  ORGANISM  Mycolicibacterium smegmatis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 172)
  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 172)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 172)
  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   4  (residues 1 to 172)
  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   5  (residues 1 to 172)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Mycolicibacterium smegmatis"
                     /db_xref="taxon:1772"
     Protein         1..172
                     /product="TRAP transporter small permease subunit"
                     /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=18639
     Region          9..170
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mtedvtlpra vtviargtsi vagllllgvi lltvadvvsr nardrsivgt vdiatmllva
       61 iaflglasae adgrhvvvel fesrfgprtr lvlsvirtvl lialallltw glsevlfsai
      121 ergettndil rlptwpaklv llasfamffv vavwkelltf malrterqgd nr
//
LOCUS       WP_003869345             326 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Thermoanaerobacter
            ethanolicus].
ACCESSION   WP_003869345
VERSION     WP_003869345.1
KEYWORDS    RefSeq.
SOURCE      Thermoanaerobacter ethanolicus
  ORGANISM  Thermoanaerobacter ethanolicus
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Thermoanaerobacter.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 326)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Thermoanaerobacter ethanolicus"
                     /db_xref="taxon:1757"
     Protein         1..326
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35171
     Region          2..326
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mrrariigvg syhpknlitn eelskrigep isinfenkvg ilqryitgpd estadlayea
       61 airalemadi sakdidliil stdtpeyitp ptsaivqgrl gainagffdi nascagfags
      121 lavaskmima ddslnkvlvi gaynmskfid yntpglsaif adgggavvlt sieenagfla
      181 skfigdgtqy dflgiydgga knplrkdnpk dqlltsfkpl ppdrnlkmwp plvkevvera
      241 gykvedidhi fftqinksvi levmdtlgld rskattimek ygytgsaclp malddavknn
      301 rikrgdlivf vgsgvgfsma asafiy
//
LOCUS       WP_003896873             277 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Mycolicibacterium
            smegmatis].
ACCESSION   WP_003896873
VERSION     WP_003896873.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium smegmatis (Mycobacterium smegmatis)
  ORGANISM  Mycolicibacterium smegmatis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 277)
  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 277)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Mycolicibacterium smegmatis"
                     /db_xref="taxon:1772"
     Protein         1..277
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29426
     Region          1..270
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mpaspytvnc silltelpll qrpeaaraag fdavefwwpf aeatpsdrev defvsaisda
       61 gvqltglnfa agdmpggerg ilshpgrsad frasvdiave iakrlgtkaf nalygnrrdd
      121 agvdeqdaaa venliyasea treidavvli epvsgsplyp lklaadavav idrvaaqsdg
      181 tannlrllad vyhmsvngdd vpaaleghad lighvqiada pgrgepgtgs lplagyleql
      241 agygyrgyvg leykasredp fdwlplehrs vhvradr
//
LOCUS       WP_003898311             415 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Mycolicibacterium smegmatis].
ACCESSION   WP_003898311
VERSION     WP_003898311.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium smegmatis (Mycobacterium smegmatis)
  ORGANISM  Mycolicibacterium smegmatis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 415)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Mycolicibacterium smegmatis"
                     /db_xref="taxon:1772"
     Protein         1..415
                     /product="amidohydrolase family protein"
                     /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=44221
     Region          9..410
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mpesvpassa hqpatydlvi hrahvfdghq ahtglrdvgv nggqiadvsa eplrgetevd
       61 aaegwvlpgl idthvhfydv aavtdpasmr tfeeneladr lksflrhgit tiksvgdptd
      121 evlrtrsria agtlrgprfl atgcgitgrd ghpastvfan npwarqrftr evdsaaqmqd
      181 vvhhladrkv daikllsega cacatspeyl wrnpafptav eltrlspell kagidtaher
      241 glrvtvhttq qaaareaiea gadglehgvt vepitdhalv dlmlerdtty tptlwiddaa
      301 hpdtrgnlkk vadagvtivm gsdtfsgrgl fgantleeae lmvaagmtpl qslvagtsaa
      361 arqcvrpdlg avapgkradl vvltadptrd ignlrnlamt ildgeivvdn rqgtt
//
LOCUS       WP_003891142             171 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein
            [Mycolicibacterium phlei].
ACCESSION   WP_003891142
VERSION     WP_003891142.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium phlei (Mycobacterium phlei)
  ORGANISM  Mycolicibacterium phlei
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
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   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
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   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Mycolicibacterium phlei"
                     /db_xref="taxon:1771"
     Protein         1..171
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18537
     Region          74..161
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(93,112..113,132,135,143..144,153,158)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 myqsaslphs pdpvqvvlvf dippesplla srtadladey grliataipg vrartavitt
       61 ptapvapsqr etglcvyrga revridgqpv rltyrefell cclaaspgrt vsraeliatv
      121 wrdnppgdsl rtvdthvrrl raklgrfagv lttvrgsgyr fdprpdvyva a
//
LOCUS       WP_003893713             315 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Mycolicibacterium
            smegmatis].
ACCESSION   WP_003893713
VERSION     WP_003893713.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium smegmatis (Mycobacterium smegmatis)
  ORGANISM  Mycolicibacterium smegmatis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Mycolicibacterium smegmatis"
                     /db_xref="taxon:1772"
     Protein         1..315
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35075
     Region          16..299
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mirnefaaag iddpmlreay rrcreinaah grtfflatrl lapdqrpavh alygfaryad
       61 dildefdptl dtaararqlq lladqffara ehpgdpvlta vghtvarygi aaelfedflr
      121 smrmdlsvtd yadraaleey mrgsaeaigl qllpilgtvt apeeaaphaa algrafqltn
      181 flrdvdedll rdrvylpade lavhgvdrdl lmwchhnqht dsrvrkalqa qheiarrtyr
      241 yaaegiamla prsrpcvata mqlyseildc ieesdfaifr rratvgtrrr iqvagaglih
      301 awrarshaaa vpgaa
//
LOCUS       WP_003910402             205 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Mycobacterium tuberculosis complex].
ACCESSION   WP_003910402
VERSION     WP_003910402.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium tuberculosis complex
  ORGANISM  Mycobacterium tuberculosis complex
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 205)
  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 205)
  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   3  (residues 1 to 205)
  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   4  (residues 1 to 205)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 205)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Mycobacterium tuberculosis complex"
                     /db_xref="taxon:77643"
     Protein         1..205
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22520
     Region          13..204
                     /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"
ORIGIN      
        1 mtgpttdada avprrvliae dealirmdla emlreegyei vgeagdgqea velaelhkpd
       61 lvimdvkmpr rdgidaasei askriapivv ltafsqrdlv erardagaia ylvkpfsisd
      121 lipaielavs rfreitaleg evatlserle trklverakg llqtkhgmte pdafkwiqra
      181 amdrrttmkr vaevvletlg tpkdt
//
LOCUS       WP_003910464             369 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Mycobacterium tuberculosis].
ACCESSION   WP_003910464
VERSION     WP_003910464.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium tuberculosis (Mycobacterium tuberculosis variant
            tuberculosis)
  ORGANISM  Mycobacterium tuberculosis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
REFERENCE   1  (residues 1 to 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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..369
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38509
     Region          5..359
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msklqlravv adrrldvefs vsagevlavl gpngagksta lhviagllrp daglvrlgdr
       61 vltdteagvn vathdrrvgl llqdpllfph lsvaknvafg pqcrrgmfgs grartrasal
      121 rwlrevnaeq fadrkprqls ggqaqrvaia ralaaepdvl lldepltgld vaaaagirsv
      181 lrsvvarsgc avvltthdll dvftladrvl vlesgtiaei gpvadvltap rsrfgariag
      241 vnlvngtigp dgslrtqsga hwygtpvqdl ptgheaiavf pptavavype pphgsprniv
      301 gltvaevdtr gpmvlvrghd qpggapglaa citvdaatel rvapgsrvwf svkaqevalh
      361 paphqhass
//
LOCUS       WP_003895408             366 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Mycolicibacterium
            smegmatis].
ACCESSION   WP_003895408
VERSION     WP_003895408.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium smegmatis (Mycobacterium smegmatis)
  ORGANISM  Mycolicibacterium smegmatis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 366)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Mycolicibacterium smegmatis"
                     /db_xref="taxon:1772"
     Protein         1..366
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39226
     Region          19..353
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mgphwlvmda adeasspfrt riaaagrclp ktrlttselm setrhnthid lerltgirer
       61 rvslgeddsy slatkaaldc lekadrsads vevvincsit kfhggltqyl eptmssdvah
      121 aigardamtf disnacagml tgvmvlntwi rqglvargmv vsgeyisqlg qnaakhirtv
      181 lskelasltl gdagaallle rvpaggsgit lagfttiady srlclaypkg rdpgarmftd
      241 sraihraait ntpvllrevl dtagisiddi dhvithqtsa raikkgmavm aaefgdhprh
      301 davitvdryg ntastthtva lieelearri epgetvalia lasgleigii lltvdedlvk
      361 rygndh
//
LOCUS       WP_003910078             397 aa            linear   BCT 20-JAN-2025
DEFINITION  DNA polymerase domain-containing protein [Mycobacterium
            tuberculosis].
ACCESSION   WP_003910078
VERSION     WP_003910078.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium tuberculosis (Mycobacterium tuberculosis variant
            tuberculosis)
  ORGANISM  Mycobacterium tuberculosis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Zhu,H., Nandakumar,J., Aniukwu,J., Wang,L.K., Glickman,M.S.,
            Lima,C.D. and Shuman,S.
  TITLE     Atomic structure and nonhomologous end-joining function of the
            polymerase component of bacterial DNA ligase D
  JOURNAL   Proc Natl Acad Sci U S A 103 (6), 1711-1716 (2006)
   PUBMED   16446439
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Zhu,H. and Shuman,S.
  TITLE     A primer-dependent polymerase function of pseudomonas aeruginosa
            ATP-dependent DNA ligase (LigD)
  JOURNAL   J Biol Chem 280 (1), 418-427 (2005)
   PUBMED   15520014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..397
                     /product="DNA polymerase domain-containing protein"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=43970
     Region          4..302
                     /region_name="LigD"
                     /note="Eukaryotic-type DNA primase [Replication,
                     recombination and repair]; COG3285"
                     /db_xref="CDD:442515"
ORIGIN      
        1 msrmaapvsl dvhgrqvivt hpgrvvfpah ndrkgytkfd lvryylavae gamrgvagrp
       61 milkrfvkgi faeavfqkra panrpdwvdv aelhyasgrs aaeavihdaa glawvinlgc
      121 vdlnphpvla gdldhpdelr vdldpmpgva wqrvvevalv vrevledygl tawpktsgsr
      181 gfhvyariap cwsfpqvrla aqtvarever rlpdaatsrw wkeeregvfv dfnqnakdrt
      241 vasaysvrat pdarvstplh weevpgcdpa vftmatvpsr ladigdpwag mddavgrldr
      301 llmlaeelgp pqkaqsakpl ieiaraktra eamaaldiwr drypgaaall rpadvlvdgm
      361 rgpssiwyri rinlqhvpad qrppqeelia dyspwpr
//
LOCUS       WP_003920138             234 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Mycobacterium xenopi].
ACCESSION   WP_003920138
VERSION     WP_003920138.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium xenopi
  ORGANISM  Mycobacterium xenopi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Mycobacterium xenopi"
                     /db_xref="taxon:1789"
     Protein         1..234
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25880
     Region          3..201
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdiyealytt rmmrrlrpdp ipldtqaril daavrapngg ntqrwhfvav ddpqlkrefa
       61 qlfrrarale yekfqtgtgp mvapapdadp aahaetmrri kgagdyladh feeiplllfv
      121 faiddlggan iypaiwsall aaraegvggv mtmvlrnftd svnellgvpv eegwtmsaml
      181 algyprgkwg vaanrrpvhd vssrnrwgvp fgvevpqplw pperdmatgl talr
//
LOCUS       WP_003920370             206 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Mycobacterium xenopi].
ACCESSION   WP_003920370
VERSION     WP_003920370.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium xenopi
  ORGANISM  Mycobacterium xenopi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 206)
  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 206)
  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   3  (residues 1 to 206)
  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   4  (residues 1 to 206)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 206)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 206)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Mycobacterium xenopi"
                     /db_xref="taxon:1789"
     Protein         1..206
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22796
     Region          13..200
                     /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"
ORIGIN      
        1 mtgsttdvda asprrvliae dealirmdla emlreegydi vgeagdgqea velaerlkpd
       61 lvimdvkmpr rdgidaasei askriapivv ltafsqrdlv erardagama ylvkpftvsd
      121 lipaielavs rfseitaler evatladrle trklierakg llqtkqgmte peafkwiqra
      181 amdrrttmkr vaevvletld ptreqt
//
LOCUS       WP_003920637             209 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Mycobacterium xenopi].
ACCESSION   WP_003920637
VERSION     WP_003920637.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium xenopi
  ORGANISM  Mycobacterium xenopi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Mycobacterium xenopi"
                     /db_xref="taxon:1789"
     Protein         1..209
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23157
     Region          6..201
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdiasvdell tttravrkrl dvtrpvprev ildcvrlamq aptasnaqdw rwlvvtaadk
       61 raaiaeiyrs vggeylahaa dteadpqtrr vyrsalalte mlaqvpvhvi pclrrrfdet
      121 drlvaasawa siipaawsfl lalrsrglgs vwttmhlake qqvaelldip atvtqvalfp
      181 vaytigtdfr pasrpppqtv tfwntwgeh
//
LOCUS       WP_003922092             236 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Mycobacterium xenopi].
ACCESSION   WP_003922092
VERSION     WP_003922092.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium xenopi
  ORGANISM  Mycobacterium xenopi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Mycobacterium xenopi"
                     /db_xref="taxon:1789"
     Protein         1..236
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=25574
     Region          88..229
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mnkkallwls vvaaiavvva yqvtssagdr akefaaradv ptlqpgtdvl agitvvpari
       61 hrydyrraaf gdawdddnda pgghngcdtr ddilnrdltd ktyvsikrcp davatgtlhd
      121 pytnatihfq rgarvgqsvq idhivplala wdmgaynwpy pqrlrfandp anllavsgqa
      181 nedkadsqpa lwmppntafw cqyavqyvav lrgyalpvdq psadvlhraa atcptg
//
LOCUS       WP_003922740              90 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Mycobacterium xenopi].
ACCESSION   WP_003922740
VERSION     WP_003922740.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium xenopi
  ORGANISM  Mycobacterium xenopi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 90)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 90)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 90)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 90)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Mycobacterium xenopi"
                     /db_xref="taxon:1789"
     Protein         1..90
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=9103
     Region          10..90
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mardepgvvr vtvryfaaar aaagadsetv svrpgatvad lvdglaakda rlakvlsrcs
       61 ylcdgiavrd antalrsget idvlppfagg
//
LOCUS       WP_003926479             216 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Mycolicibacterium
            thermoresistibile].
ACCESSION   WP_003926479
VERSION     WP_003926479.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium thermoresistibile (Mycobacterium
            thermoresistibile)
  ORGANISM  Mycolicibacterium thermoresistibile
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Mycolicibacterium thermoresistibile"
                     /db_xref="taxon:1797"
     Protein         1..216
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23368
     Region          3..201
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 melveamrtt gtcryfrpdp vpdevlyqaf dharfapqgg nrqpvrwivv rdparkaalq
       61 dlylplwkny lsgiadgtvn vgalpktvrd adyfaehlae apaivvacae ldglhptdtd
      121 lgrlsivgga svyptvqnfc lalrnlgvgs alttllcqve pevrellaip egvataahia
      181 igyprdpfpa kltrlpvedv vaaetydqpf fapttv
//
LOCUS       WP_003926629             153 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Mycolicibacterium
            thermoresistibile].
ACCESSION   WP_003926629
VERSION     WP_003926629.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium thermoresistibile (Mycobacterium
            thermoresistibile)
  ORGANISM  Mycolicibacterium thermoresistibile
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 153)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Mycolicibacterium thermoresistibile"
                     /db_xref="taxon:1797"
     Protein         1..153
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=15868
     Region          68..152
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mnqressgip lraivmvllf lgvvfllvaf qamgsendsd gadapvagnl tttttttspe
       61 aepgrpevrv ynlsdvtgaa astadrlrea ewdvadvgdm elegvevttv ffgdapgeee
      121 aanevgqlld apvqprtpel aeqppgiiva vtg
//
LOCUS       WP_003926894             309 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Mycolicibacterium
            thermoresistibile].
ACCESSION   WP_003926894
VERSION     WP_003926894.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium thermoresistibile (Mycobacterium
            thermoresistibile)
  ORGANISM  Mycolicibacterium thermoresistibile
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 309)
  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   2  (residues 1 to 309)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Mycolicibacterium thermoresistibile"
                     /db_xref="taxon:1797"
     Protein         1..309
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30739
     Region          238..307
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mrtelpaarl yrrlgaghhp dsgsgrtdtg edrgedrgee rgedrgeegt aanesgtapd
       61 avlskwlpdn tdgasggwla airadpgrag avalvavgvt avlitifalv rdetppvmsa
      121 nlppvemvss asaapgpqtt aapdepvvvs vvglvhkpgl vrlapgarva daltaaggav
      181 ggadliglnm arrvtdgeqi ivgiaavpge paalgssist gagdpagapa sgagestapd
      241 pggaaggsvn lntatveqld tlpgigpvta eaivawrdrn grfdsvdqll evdgigparl
      301 dklrdrvhv
//
LOCUS       WP_003928661             235 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Mycolicibacterium vaccae].
ACCESSION   WP_003928661
VERSION     WP_003928661.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium vaccae (Mycobacterium vaccae)
  ORGANISM  Mycolicibacterium vaccae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Mycolicibacterium vaccae"
                     /db_xref="taxon:1810"
     Protein         1..235
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=25154
     Region          87..217
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mnrrqtlwla lsvllaviva yqvsatspap seyiadadip tvapaadvla gvieiparvr
       61 gndyrraafg eswtddtsap ggrngcdtrn dildrdlidk tyvaisrcpr avatgtlrdp
      121 ytnatvpfvr gnqtgaavqi dhivplalaw dlgarhwped irerfandpa nliavsggan
      181 qdkgdkppaa wmppndafhc qyaiqfiavl rgyglpvdap svpvlreaad tcprg
//
LOCUS       WP_003924401             410 aa            linear   BCT 20-JAN-2025
DEFINITION  DNA polymerase domain-containing protein [Mycolicibacterium
            thermoresistibile].
ACCESSION   WP_003924401
VERSION     WP_003924401.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium thermoresistibile (Mycobacterium
            thermoresistibile)
  ORGANISM  Mycolicibacterium thermoresistibile
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Zhu,H., Nandakumar,J., Aniukwu,J., Wang,L.K., Glickman,M.S.,
            Lima,C.D. and Shuman,S.
  TITLE     Atomic structure and nonhomologous end-joining function of the
            polymerase component of bacterial DNA ligase D
  JOURNAL   Proc Natl Acad Sci U S A 103 (6), 1711-1716 (2006)
   PUBMED   16446439
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Zhu,H. and Shuman,S.
  TITLE     A primer-dependent polymerase function of pseudomonas aeruginosa
            ATP-dependent DNA ligase (LigD)
  JOURNAL   J Biol Chem 280 (1), 418-427 (2005)
   PUBMED   15520014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Mycolicibacterium thermoresistibile"
                     /db_xref="taxon:1797"
     Protein         1..410
                     /product="DNA polymerase domain-containing protein"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=45989
     Region          1..295
                     /region_name="LigD"
                     /note="Eukaryotic-type DNA primase [Replication,
                     recombination and repair]; COG3285"
                     /db_xref="CDD:442515"
ORIGIN      
        1 maesrtvevd grrvvvsnpn kvvfpqlglt ksdlvdyyls vaepalrgvr nrpmilkrfv
       61 kgiteeavfq krapakrpdf vdtaelryas gtsaaeavih daaglvwavn lgcvdlnphp
      121 vraddlahpd elrvdldpmp gvgwrqiidv awvarevled hgltawpkts gsrgfhiyar
      181 ierrwpfkqv rlaaqavare verrapesat arwwkeerhg vfvdfnqnay drtvasaysv
      241 ratpdarvst plrwdevsrc dpaeftiatv pgrvadigdp wepmddhags ldalltlaed
      301 lgpperaprg vsrgtgrrqs skplieiart rtrdeamaal dtwrdrypav aeklqpadil
      361 vdgmrgpssi wyririnleh vpeaerppqe plladydpwq nysghqqrrs
//
LOCUS       WP_003931914             209 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Mycolicibacterium
            vaccae].
ACCESSION   WP_003931914
VERSION     WP_003931914.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium vaccae (Mycobacterium vaccae)
  ORGANISM  Mycolicibacterium vaccae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
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   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   3  (residues 1 to 209)
  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   4  (residues 1 to 209)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 209)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 209)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Mycolicibacterium vaccae"
                     /db_xref="taxon:1810"
     Protein         1..209
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22889
     Region          15..206
                     /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"
ORIGIN      
        1 mssasaspsd avvtprrvlv aedealirld laemlreegy evvgeagdgq eavelaeslr
       61 pdlvimdvkm prrdgidaas eiaskriapi viltafsqre lverardaga maylvkpfsi
      121 tdlipaiela vsrfsemael ekevanlsdr letrklvera kgllqskqgm tepeafkwiq
      181 raamdrrttm krvaevvlet ldppaepta
//
LOCUS       WP_003935876              94 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Rhodococcus].
ACCESSION   WP_003935876
VERSION     WP_003935876.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..94
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10038
     Region          5..93
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(22,49..50,52,74)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(22..23,31,32,34..35,37,40..41,49,54,61)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 msiidavrea vvaippgsva sygdigrrig agprqvgram slldddvpww rvvyadgtta
       61 schggrapal lleegtavtg krvdmqrarh rwrd
//
LOCUS       WP_003934850             350 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: DNA polymerase domain-containing protein
            [Rhodococcus].
ACCESSION   WP_003934850
VERSION     WP_003934850.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Zhu,H., Nandakumar,J., Aniukwu,J., Wang,L.K., Glickman,M.S.,
            Lima,C.D. and Shuman,S.
  TITLE     Atomic structure and nonhomologous end-joining function of the
            polymerase component of bacterial DNA ligase D
  JOURNAL   Proc Natl Acad Sci U S A 103 (6), 1711-1716 (2006)
   PUBMED   16446439
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Zhu,H. and Shuman,S.
  TITLE     A primer-dependent polymerase function of pseudomonas aeruginosa
            ATP-dependent DNA ligase (LigD)
  JOURNAL   J Biol Chem 280 (1), 418-427 (2005)
   PUBMED   15520014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..350
                     /product="DNA polymerase domain-containing protein"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=38623
     Region          6..311
                     /region_name="LigD"
                     /note="Eukaryotic-type DNA primase [Replication,
                     recombination and repair]; COG3285"
                     /db_xref="CDD:442515"
ORIGIN      
        1 mpdakrspav eldvggvpvr lsnpdkvyfp rlgeagskrr lveyyrtvat agsapllqal
       61 qerpthlqrf pdgiegeeiy qkrvparrpd hvatcevtfp sgrtadvlrv raaadvvwaa
      121 nlgtvtfhpw avrcgdvdrp delridldpq pgtafddara valevlrpll delglvgfpk
      181 tsggrglhvy vrivpewdfv gvrragialm reverrsggr attawwkeer gqrifldfnq
      241 nardktiasa ysvrrtpiat vstpltwdel vdadpddfti atvpgllerr gdpmaamdet
      301 aqtldvllem aerdaaaglg dlpyppthpk mpgepkrvqp srdtdrkrpg
//
LOCUS       WP_003923796             275 aa            linear   BCT 20-JAN-2025
DEFINITION  phosphonate ABC transporter ATP-binding protein [Mycolicibacterium
            thermoresistibile].
ACCESSION   WP_003923796
VERSION     WP_003923796.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium thermoresistibile (Mycobacterium
            thermoresistibile)
  ORGANISM  Mycolicibacterium thermoresistibile
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
REFERENCE   2  (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   3  (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   4  (residues 1 to 275)
  AUTHORS   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Mycolicibacterium thermoresistibile"
                     /db_xref="taxon:1797"
     Protein         1..275
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=29412
     Region          27..275
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mtapatgapt appdptaart atpgtstaie vtdlrvrfrr crtdalagvn ltvrqgetva
       61 ligtngagks tllrslvrlv epvggritlg dtdvtaasrr elrtlrrdvg fvfqrfhlvp
      121 rltafhnvvh gamgrrgtrc aspltapgev rreamraler vgladhadrr vdtlsggqqq
      181 rvavarmlmq rprivladep vasldpssan tvlelltsva teggvtvvma lhqidlalry
      241 adrviglrng tldfdqpars cdtarldpif aradt
//
LOCUS       WP_003937094             203 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Rhodococcus ruber].
ACCESSION   WP_003937094
VERSION     WP_003937094.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus ruber
  ORGANISM  Rhodococcus ruber
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Rhodococcus ruber"
                     /db_xref="taxon:1830"
     Protein         1..203
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22044
     Region          93..178
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 mrtrrdgaag rerrprglfa gvaaglvlvv laavlmlgav psrylpwdta dfpdvdtsal
       61 tppqtrivel ladehrtqrp gtfysegaee pwcanfvswi mreagrplan phsghwripg
      121 vytlqeyyes agrfepadgg yqpvvgdvvl yenelwvgqh tnivvavdgd tattvggnel
      181 grirvhtvdv tsdsavvgfg rle
//
LOCUS       WP_003937346              98 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Rhodococcus].
ACCESSION   WP_003937346
VERSION     WP_003937346.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..98
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10444
     Region          9..98
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(27,55..56,58,80)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(27..28,36,38,40..41,43,46..47,55,60,65)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mpatseadve rvrelvasvp egrvttygdv aaaaglsspr tvgwimrtds adlpwhrvvp
       61 asgrpaahla hrqlarlsqe gvpirdgrvd laaarhrf
//
LOCUS       WP_003937405             180 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Rhodococcus ruber].
ACCESSION   WP_003937405
VERSION     WP_003937405.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus ruber
  ORGANISM  Rhodococcus ruber
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 180)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Rhodococcus ruber"
                     /db_xref="taxon:1830"
     Protein         1..180
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=17333
     Region          93..179
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 msttsessgp plralamvli slailfaglg laslgnsdse gsapepatep aaapattsat
       61 saplaatpar tttagatttv sattsspvaa aapvrvlnns nvtglaaqta glledegftv
      121 aetgnysdgv iastsvyygt gpgerqtaea vaealgvtaq prfagiedsa pgvivivtsp
//
LOCUS       WP_003937942             123 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Rhodococcus ruber].
ACCESSION   WP_003937942
VERSION     WP_003937942.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus ruber
  ORGANISM  Rhodococcus ruber
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Rhodococcus ruber"
                     /db_xref="taxon:1830"
     Protein         1..123
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11687
     Region          <15..>104
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mnlsvsssnp alvpdtnvsf ggsgatrtmt vagmdkatgp aaltvtvsdg tatgtivvty
       61 aagghgddtl tgtdgadilf gqngtdtvng lggndllcgg rgndtlaatt attpsaaara
      121 tth
//
LOCUS       WP_003939201             239 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease family protein [Rhodococcus].
ACCESSION   WP_003939201
VERSION     WP_003939201.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..239
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=25597
     Region          95..235
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 maaansagrr rlwllayvla fvvfvvlqqt yggdeagpgp aptpapssaa aaetvellks
       61 lavrapdpsg gydraqfgpa wtddvtvagg rngcdtrndv lkrdlvnikl apvtkectve
      121 agtlydpytg reiyfrrgvd tssavqidhv valsdawqkg arlldaqtrk nlandprnlq
      181 avdgptnqgk gdkdaaqwlp pnseyrctyv srqievkaey glwitpdekd amagvlatc
//
LOCUS       WP_003943124             198 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CHAP domain-containing protein [Rhodococcus].
ACCESSION   WP_003943124
VERSION     WP_003943124.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..198
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21479
     Region          87..172
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 mspaesnrrr rivlwiagvl gvvivvgvvv vavapsrylp wdtaefpavd asaltsdqgr
       61 vlellqsehe qdrpgtfysd gideewcadf vswimreagr plsnpnsgsw ripgvytlqe
      121 yyqgigayae ngsgytpnvg dvviydssrw vgqhtnivva vdgnsaitvg gnefgkvrvh
      181 dldwqsdsav vgfgklhp
//
LOCUS       WP_003943809             259 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Rhodococcus].
ACCESSION   WP_003943809
VERSION     WP_003943809.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..259
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28085
     Region          4..94
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          158..237
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mgwytpqsva pdlsdilvcg wtacaegehl lvpdacmdvl wirgvgirvc gpetaawsft
       61 lppgtrsvgv rfrpgsaspm lrtsaselrd sradlsdvtd arterillnr lensedheqv
      121 silesavrsw vsssfrhdpv inhvrtalse hswnvsslad aaaltsrqlq rrcndafgyg
      181 patlrsilrl qrfmalarsr palglaesaa hcgfsdqahl trecrrissl tpaallrtqa
      241 pdwhgsdtvv alaegdava
//
LOCUS       WP_003943863             246 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Actinomycetes].
ACCESSION   WP_003943863
VERSION     WP_003943863.1
KEYWORDS    RefSeq.
SOURCE      Actinomycetes (high G+C Gram-positive bacteria)
  ORGANISM  Actinomycetes
            Bacteria; Bacillati; Actinomycetota.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 246)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Actinomycetes"
                     /db_xref="taxon:1760"
     Protein         1..246
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=26560
     Region          3..240
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mvrelreald dhqfevlyqp qvnlnssaii syeallrwrh plrgliepqd fmrsaessgl
       61 iipiglqale micaqtaswp ehmmvavnfs prqlatphaa heilgaldss qtplsriive
      121 vtelgvvgrh aaetlhvlhn egirialddf gagfasfsal selpldilki dqsltwavsa
      181 agragdrafm vmesiadiar klgldsiaeg vetaehaanv lragcdmgqg yyfgkplpas
      241 svvtpv
//
LOCUS       WP_003945084             381 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Rhodococcus].
ACCESSION   WP_003945084
VERSION     WP_003945084.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 381)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 381)
  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   4  (residues 1 to 381)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            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="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=40401
     Region          1..301
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mitfegvtkq ypdgttavdr ldltieaesf tvfvgpsgcg kttsmrminr mitptsgkif
       61 vdgrdiaqtd avklrlgigy viqnagllph rtvidnvatv pvlrgesrra arkaalgvle
      121 rvgldislat rypgqlsggq qqrvgvaral aadppillmd epfsavdpvv redlqtemlr
      181 lqselkktiv fvthdideav klgdhiavfg pggrlqqvaa prdvlaapat dfvagfvgrd
      241 rgyrglsfra adevplhpvr tavenelkal rlelgewvlv vtdngtpqgw idvtgveglr
      301 sgrtlaqsts aggslfspgg dlrqaldaai sspsgigvav dgegaviggi lgsevvakla
      361 dqrrredeer nrvaftegfg s
//
LOCUS       WP_003948014             588 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LytR C-terminal domain-containing protein
            [Streptomyces].
ACCESSION   WP_003948014
VERSION     WP_003948014.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 588)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..588
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=61606
     Region          497..584
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mndrrhasdp yggeyaseqy gpvsydeygr pipqqppqgh dpyagqqqgy gydpygqggp
       61 gtgqqppvpa dpyagqqqgy gyeqqgydpy gqggpgtgqq ppvpadpyag qqqgygyeqq
      121 gydpygqggp gtgqqprvpq qqtrqdgdgp egygdqgygg pdeggapdyk teqfsfieep
      181 deesedvidw laftesrter reeakrrgrs rmialvvvla lvlaggvgyl wyagklpgts
      241 spassggaad tagpqkrdvv mvhlhdtrte ktstlllvdn ttsergatvl lpnslsltge
      301 dgnattlads vdddgstgtr eavdqllgts vegtwrldtp ylnnlvelvg nieldadanv
      361 papkkgdspl vtkgadrtlg gpaavayaty qakgepqtaq lqrfgqvfqa vlrklssdpq
      421 aatvtvetla qildpslnek dlgaflarla drakggdhtt ellpvgqdgr paqeatdkiv
      481 kqilggsvse gaqgdatrvg lqdatgaqgr aekaraslvn ggyayvgrgs gdtaratssv
      541 tyekagdkae avevartlgl pdsavtqgst pgnvdvsvvl ggdyqpge
//
LOCUS       WP_003946990             386 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces albidoflavus].
ACCESSION   WP_003946990
VERSION     WP_003946990.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 386)
  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 386)
  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
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 386)
  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   5  (residues 1 to 386)
  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   6  (residues 1 to 386)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 386)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     Protein         1..386
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39246
     Site            order(14,27..29,38..41,43..44,47..48,50..51,64..66,71..73)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Region          15..67
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Site            order(27,30,80)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
     Region          76..381
                     /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 mpasprtarv indrlaldhl lregpltaar lkeltglsrp tvadlvdrlt gaglirivge
       61 sgadrrgpna rlyglvaera hlaaldvrts glalvvtdll gtplaearlp idgalgivpa
      121 veravsllda tlaevgvdel qsvcvgapgl vdpatgelrd stglpgwhrr lvralqghrs
      181 arvlvenetn laavaerrhg aaqdhdtfvl lwlghgvgaa vvldgtlrrg agggageigf
      241 lpvpltsslp satdcgggfh slagaaavhe larrhgipvt garddadgre epasatavra
      301 afeagtagel fldeladrva lgaaavaavl dpgcvvlage tgeaggeala arvgkrlaal
      361 splrtdvrpt rlggstvltg alftaq
//
LOCUS       WP_003950701             292 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Streptomyces].
ACCESSION   WP_003950701
VERSION     WP_003950701.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            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="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30523
     Region          1..258
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mridlhthst asdgtdtpaa lvraaaaqgl dvvaltdhdt trghaeaaaa lpegltlvpg
       61 aelscrltgp dgpmgvhmla ylfdpdepel lrqrelvrdd rvpraramvd klralgvdvt
      121 weqvariagd gsvgrphlae alvelgvvas vsdafteewl adggrayapk heldpfeavr
      181 lvkaaggvtv lahpraakrg hvvpeeavar laeagldgve adhaehgpad rarvralaae
      241 lgllvtgssd yhgtrkdial gahttdpeiy geitrratga fpvpgaggrp ra
//
LOCUS       WP_003941291             233 aa            linear   ENV 20-JAN-2025
DEFINITION  HNH endonuclease family protein [uncultured Rhodococcus sp.].
ACCESSION   WP_003941291
VERSION     WP_003941291.1
KEYWORDS    ENV; RefSeq.
SOURCE      uncultured Rhodococcus sp.
  ORGANISM  uncultured Rhodococcus sp.
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus; environmental samples.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="uncultured Rhodococcus sp."
                     /db_xref="taxon:194249"
                     /environmental_sample
     Protein         1..233
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=24957
     Region          90..229
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mvarlsails tlvlvclvas cgwfgderle sapgsptrse leellsrtai vdtrphpggy
       61 qrgcgngqac vfgpawsddq dapgghdgcd trnnvlaqdl sdvvfkpgtr dcvvlsgamt
      121 dpysgdrief ersqaksvqi dhvfplaaaw dfganswtpa lrmrfandms lnllavngpd
      181 nqskgdstps ewlppdpayr cfyagkyltv aisyglpvsr adhsaltdla trc
//
LOCUS       WP_003931452             274 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Mycolicibacterium
            vaccae].
ACCESSION   WP_003931452
VERSION     WP_003931452.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium vaccae (Mycobacterium vaccae)
  ORGANISM  Mycolicibacterium vaccae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Mycolicibacterium vaccae"
                     /db_xref="taxon:1810"
     Protein         1..274
                     /product="formate/nitrite transporter family protein"
                     /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=29086
     Region          2..265
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msyvppkela griidageak avmstrdtli raymagailg laaafavtit vktgqpllga
       61 vlfpvgfcml yllgfdlltg vftlvplawl drrpgvtlga mlrnwglvfi gnfagamtta
      121 vlmaiyftfg fsiepdavgq algaigegrt lgyaeygaag mltlfvrgvl cnwmvstgvv
      181 gammsdslpg kviamlmpim lffylgfehs ivnmflfpsg lmlggdftva dylvwneipt
      241 llgnlvgglt fvgliiyath artaptrqli ktpd
//
LOCUS       WP_003957996             301 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Streptomyces clavuligerus].
ACCESSION   WP_003957996
VERSION     WP_003957996.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces clavuligerus
  ORGANISM  Streptomyces clavuligerus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Streptomyces clavuligerus"
                     /db_xref="taxon:1901"
     Protein         1..301
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32119
     Region          1..295
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mlldtaslyf rayfgvpdtv rapdgtpvna vrgllefigr lvqdhrpddl vacwdndwrp
       61 hwrvelipsy kahrvavete agpdeeeapd tltpqvpvia evlealgiar vgadgyeadd
      121 vigtltarat gpvdivtgdr dlfqlvddar grrvlyplkg vgtlqttdeg wlrerygvdg
      181 pgyadlallr gdpsdglpgv pgigektaak lldafgdlag imaavddpas rltpaqrrrl
      241 deargyvava pkvvrvatda plppfdpalp saprdpaala algerwglgg alqrllttlr
      301 g
//
LOCUS       WP_003963554             103 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Escherichia coli].
ACCESSION   WP_003963554
VERSION     WP_003963554.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..103
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11315
     Region          2..103
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(7..8,26..27,35,38,40..41,43,46..47,49,57,62,69)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(26,57..58,60,84)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mekedsfpqr vwqivaaipe gyvttygdva klagspraar qvggvlkrlp egstlpwhrg
       61 vnrhgtislt gpdlqrqrqa llaegvmvsg sgqidlqryr wny
//
LOCUS       WP_003960499             391 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces clavuligerus].
ACCESSION   WP_003960499
VERSION     WP_003960499.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces clavuligerus
  ORGANISM  Streptomyces clavuligerus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 391)
  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 391)
  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
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 391)
  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   5  (residues 1 to 391)
  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   6  (residues 1 to 391)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 391)
  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 11513089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Streptomyces clavuligerus"
                     /db_xref="taxon:1901"
     Protein         1..391
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40310
     Region          10..75
                     /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(17,20,69)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
     Region          65..374
                     /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 mndraaldll lahgplsrtr igkltglskp tasqllarle saglvvatgt tegrpgpnaq
       61 lyavngraaf aagidvtplr iraavadltg rtvgefelpt pgrraenavr rvvaalegaa
      121 eaagittadv hrlvigtpga fdpstgrlry ashlpgwhsp dlleeldaal pmpvgyendv
      181 nlvavaeqrl gvardhenfv llwneeglga avviggrlhr gstggagevg flpvpgtplv
      241 rgvtkansgg fqelagaqvl prlahelgve pvgqghyvqv agalvaraae adsgpyrafl
      301 dtyatglatg laslvavldp elvvlsgeai aaggeplrar vqaelaelaa srprlvigsv
      361 rdhpvlrgal esalaatrde ifdttaqrra p
//
LOCUS       WP_003965841             266 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Streptomyces].
ACCESSION   WP_003965841
VERSION     WP_003965841.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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
REFERENCE   2  (residues 1 to 266)
  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 266)
  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 266)
  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 11444466
            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="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28300
     Region          9..79
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          191..244
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 msignspedd rpsigralqq ariaagltve evssstrvri pivhaieqdd fsrcggdvya
       61 rghirtlara vgldpeplve eydadhggrp aptpaaplfe aerirseprr pnwtaamvaa
      121 ivavigfvgf tlfsgedeps ntaqiaegsq pdktaakpta tkpadpkpvp sesaiaaapr
      181 dkvtvklsad rgkswisakd hngrqlfdgl llqgesktfq dkeridlvlg dagaidlfvn
      241 gkqvedrfgp gqverlsytk gdpeag
//
LOCUS       WP_003967056             265 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Streptomyces].
ACCESSION   WP_003967056
VERSION     WP_003967056.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..265
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26877
     Region          <112..263
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mirhrltara avvallatgl aaspavaapt pagaptgtga gakarvgadw akqsitftag
       61 agqvndlhvv pmdqgdgvrr igfrdsvplq pgdhctyltp gdetyvvcel ptgasrpdri
      121 dvflgdgdde iatsdpgvat vsggpgddml hahtahtvrg dagndmvmgr vvldggdgmd
      181 hlmavdgdqr lyggrgddmi eayegndivy agpgddhvmg gegddilfgg tgddmvhged
      241 gndlivggpg kdsvdggpgr nivlr
//
LOCUS       WP_003967139             742 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate--CoA ligase family protein [Streptomyces].
ACCESSION   WP_003967139
VERSION     WP_003967139.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 742)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..742
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=78416
     Region          52..738
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mlgsthgtlt tdfrarvvac geephaavvs lptasarggl dvsgrplhlp vpdldrffrp
       61 rsvavvgasd aegrpntgit rqllawadrv garlhpvhpt rpavfgrdcf psvadvpepv
      121 dlavllvadp lpvieelgea kvpfavafas gfaetgeaga aaqtrlaaav ersgvrllgp
      181 ntnlnaferf redldgpaia litqsghqgr plhalqelgi rlshwaptgn eadletadfl
      241 ayfaqlpevg aiacyveglr dgrsfllaad raarakvpvv avkvgrteag artaashtgk
      301 ltgaddvvda amrqfgvvrv dgldelqdta allararppr aegvavysis ggtgahfadl
      361 ataagltlpa lsqekraelh twipeylnva npidngghpv gdwrgrkiid ailadpsvgv
      421 licpitgpfp pmsdrlaqdl adaaeatdkl vcvvwgspvg tedayrttll gssrlatfrt
      481 arncvtavka yldhhrftar yrspfedapr tpspsfrkaq gllrpgqqls ehaakqllra
      541 ygirvpreql vtsaaaavra agpvgypvvm kasgprlahk telglvkvgl tsasqvrday
      601 reltdiarye svdldgvlvc qmidrgvemm vgvthdalfg ptvtvglggv lvevlhdaav
      661 rvppfgeqea rdmlgelrgr allegvrggp pvdvdalvev vlrvqrmale lgddlteldi
      721 nplvvlgrgq gavaldalav cr
//
LOCUS       WP_003967255             233 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease family protein [unclassified
            Streptomyces].
ACCESSION   WP_003967255
VERSION     WP_003967255.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..233
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=24646
     Region          <128..214
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mvnkyltrgl salplplalv vpllllpplp aaqaapaapv aevttladav gqlkmaeenr
       61 agyttssfrh wnagedatdg cdtraevlls eavvaptvgs gcgltggrwt shldgqevtg
      121 agsldvahlv algeawdsga sawterrrea yandqgadas laavtarinr rkadkdpadw
      181 mppspdvqcr ytgewvstkl rwqltvddre lealkvyaeg pcedtvvhya pav
//
LOCUS       WP_003968919             376 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Streptomyces].
ACCESSION   WP_003968919
VERSION     WP_003968919.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 376)
  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 376)
  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
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 376)
  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   5  (residues 1 to 376)
  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   6  (residues 1 to 376)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 376)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 376)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..376
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37989
     Region          37..>65
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          86..360
                     /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 mngsrtktqa ganlpalrhh naalvldllr aagaegisrl elaegtgltp qavskitarl
       61 redglavgag lrpstggkpr tvlrlvpdaq favglhldrd gltavlvdla grpvavtrap
      121 ldlgapadrv ladaadavrd lcaaephkpv lgvgvavpgp ldhrdgvlrr vtgfpqwdgy
      181 plraalaert glpvtldkdt naaalavala ldeprgdfay lhlgtglgag lvlggevhrg
      241 artgagefgh qtlqldgplc gcggrgciev lclaaeargd raeaarvlga gaanlvgllg
      301 idrvvlggrt vaadedayvr gvravieera arggagtgvt vtvarggdrp vaegaahlvl
      361 apvfgrvger vggarg
//
LOCUS       WP_003968387             273 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Streptomyces].
ACCESSION   WP_003968387
VERSION     WP_003968387.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 273)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..273
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29922
     Region          21..270
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          25..129
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
ORIGIN      
        1 maagprrdtr givdapdlfa hvrfrrrepa aalrpylehy wlidwdltep yaahvvphps
       61 vnlvfqryea gdgprersgy aevagvdpgl farklagrgr vcgvqfrpgg frpfapgrpv
      121 sawtglrsda aaalrlpppv rgvldpdden arvtaldafl laleprpdpq atlamavvdr
      181 vrtdrtvlrv drlardagls arslqrlfsa yvgvgpkwvi lryriheale ragsdpavdw
      241 arlaadlgys dqahlvrdft atvgvpptaf apr
//
LOCUS       WP_003969127             407 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Streptomyces].
ACCESSION   WP_003969127
VERSION     WP_003969127.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 407)
  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 407)
  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
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 407)
  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   5  (residues 1 to 407)
  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   6  (residues 1 to 407)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 407)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..407
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42249
     Region          22..>65
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          85..395
                     /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 magttpgapg tpgtprvlra mndraaldll lehgplsrtr igkltglskp tasqllarle
       61 aaglvvatgt segrpgpnaq lytvnaraah vagldvngrr ivaavadvtg rtvgefelat
      121 pgrradsvvr qvadaldgav kdagltradv hrivigtpga fdpgtgrlry ashlpgwhss
      181 tlldelaafl pmpveyendv nlvavaeqrl gaarghedfv llwneeglga alvingrlhr
      241 gftggagevg flpvpgtplv rqvvkansgg fqelagaqav prlakalgvd tpqqpyakva
      301 adllaraada yerdpaltel lrqyaqrlat glasvtavld pglivlsgga vaaggeilrs
      361 liqselaela asrprlvvge idrtpvlrga leraladtrd evfdtsr
//
LOCUS       WP_003971164             378 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: aminoglycoside phosphotransferase family protein
            [Streptomyces].
ACCESSION   WP_003971164
VERSION     WP_003971164.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 378)
  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   2  (residues 1 to 378)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..378
                     /product="aminoglycoside 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=40446
     Region          97..307
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mytasssvsa pprplrpmga gggpylapha gapvqgpgra rraagpgagp lsgridlsgp
       61 qgaqvrmaia svqricpefn pvqvlrrsgr svlivgttgr atavakclld hspawterfr
      121 heiaayrafv rhrppvrvpr liaadpenct lviermpgrv aaltrhpaea ppradiraal
      181 gaiarvnawr pppglfeapl dyasriaryh elglftdrdl gdlqkllhgl ahaggrqgmg
      241 qfchgdalls nillsptgpv lvdwehagwy lpgydlatlw avlgdapvar rqisqlaqar
      301 gpaardaflv nlmlvltrei rnyetavqrt mreapaagpg gdrpgaissg eeqrlllrrl
      361 hddcamarra vraavgtr
//
LOCUS       WP_003972996             254 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-deoxy-manno-octulosonate cytidylyltransferase
            [Streptomyces].
ACCESSION   WP_003972996
VERSION     WP_003972996.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 254)
  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 254)
  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 10118537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..254
                     /product="3-deoxy-manno-octulosonate cytidylyltransferase"
                     /EC_number="2.7.7.38"
                     /GO_function="GO:0008690 - 3-deoxy-manno-octulosonate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0033468 -
                     CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27936
     Region          15..249
                     /region_name="CMP-KDO-Synthetase"
                     /note="CMP-KDO synthetase catalyzes the activation of KDO
                     which is an essential component of the lipopolysaccharide;
                     cd02517"
                     /db_xref="CDD:133010"
     Site            order(21..23,62,88,108,110)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133010"
     Site            order(134,151,157..159,165..166,168..174,206..207,
                     210..212,219..222)
                     /site_type="active"
                     /note="oligomer interface [active]"
                     /db_xref="CDD:133010"
ORIGIN      
        1 maattarqtg aeprrhiavi pcrwgasrfp gkplallgdk pllwhvhqrc leakrldgai
       61 vatdderiea acrelgidci rtgehltgtd rvaevaerlp adgyinvqgd epfisptain
      121 dvsealeftp pgtfavnayt klvdvgavld hnvvkvvvta rgealmfsrq pipyprgdrp
      181 kylrqlglyg ftgealqhfr qlqqgplera egvemlrfve yghavrmvpv lddgvavdtp
      241 edlaraerll dqrn
//
LOCUS       WP_003973551             683 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: M4 family metallopeptidase [Streptomyces].
ACCESSION   WP_003973551
VERSION     WP_003973551.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 683)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 683)
  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 683)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..683
                     /product="M4 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=71090
     Region          65..673
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mssstphrrt shttshtsrr tahrraaava lagvaaliat avqsgtataa pdpspakgne
       61 lvrlspaqra elirdadatk aktadelglg akeklvvrdv akdrdgtlht ryertydglp
      121 vlggdlvvat dagkteqvvk atakalrpat vtpkisaaka esqavsaaka agaeqpdadr
      181 aprkviwaas gtpvlayetv vgglqedgtp nelhvitdaa tgaklyeyqg vengtgntly
      241 sgtvtlgtaq sgssytltdt argnhktynl nrgtsgtgtl fsgsddvwgn gsasnaetaa
      301 adahygaalt wdyyknvhgr sgirgdgvga ysrvhygnny vnafwqdscf cmtygdgsgn
      361 anpltsidva ahemshgvts vtaglnysge sgglneatsd ifatavefya nnssdvgdyl
      421 igeeidingd gtplrymdkp skdgaskdsw ysgiggvdvh yssgpanhff yllsegsgtk
      481 tingvtynsp tsdglpvtgi grakaekiwf ralttkftst tnyagartgt laaagelygt
      541 dsaeytavan awaginvgar pgggdpgdgt tfesttnvni pdygsavtss ltvsgrtgna
      601 psnlqvgvdi ehtwrgdlqi dlvapdgsty rlknsgydpa edvhetytvn assesangtw
      661 klrvqdqgpa dtgyidawrl tfp
//
LOCUS       WP_003974920             204 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LytR C-terminal domain-containing protein
            [Streptomyces].
ACCESSION   WP_003974920
VERSION     WP_003974920.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 204)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..204
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=20592
     Region          84..174
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mggqykitgd kyprmrparr rgrfavvava cvtvlgvlgw gtlqlidvft ggdkasaaga
       61 agcattaras aspaavvlpk pgqvtvnvln attrgglaqk tadelkkrgf rvgdvsnapk
      121 eydkkvagtg lllgpttslk tsltvlgtql pgaehradaa rkgaavdlii gngfkglakp
      181 adadtalael aaprstpaae kkgc
//
LOCUS       WP_003959552             278 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            clavuligerus].
ACCESSION   WP_003959552
VERSION     WP_003959552.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces clavuligerus
  ORGANISM  Streptomyces clavuligerus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Streptomyces clavuligerus"
                     /db_xref="taxon:1901"
     Protein         1..278
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=30282
     Region          1..252
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 meirvlgplv aqlehrsvvp saakprqvla llalhpgrvv tvstlldelw gdapprtapa
       61 tlqtyirqlr rmladaldpa gvrgpkdvlc tryggyaldv tsavdatefq rlcvagqtal
      121 regrdldasq llhralglwr gpaladvqig ralevetlrl eetrlcaldg rieadlrlgr
      181 haallgelta laaqhplhet vhaqlmlaly rcgrpshals ayhrlrrsli relalepspr
      241 lqrlhqaile adpsleppyp vghggrpara dwlvtasa
//
LOCUS       WP_003970196             302 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 5'-3' exonuclease [Streptomyces].
ACCESSION   WP_003970196
VERSION     WP_003970196.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..302
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32509
     Region          1..296
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mlldtaslyf rayfgvpdsv rapdgtpvna vrglldfigr lvqdhrpddl vacwdndwrp
       61 qwrvdlipty kahrvaeetp agqtdeeevp dtlspqvpii edvlaalgia rvgvtpyead
      121 dvigtlagra tgpvdivtgd rdlyqlvdda rqvrvlyplk gvgtlqvtde awlrekygvd
      181 gagyvdlall rgdpsdglpg vpgigektaa klldaygdld gimaavddpk akltpsqrkr
      241 ldearayvav apkvvrvagd vplpdfdpal preprdpaal dalaeqwglg galqrlltal
      301 qh
//
LOCUS       WP_003977569             384 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Streptomyces].
ACCESSION   WP_003977569
VERSION     WP_003977569.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 384)
  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 384)
  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
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 384)
  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   5  (residues 1 to 384)
  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   6  (residues 1 to 384)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 384)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 384)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..384
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40088
     Region          20..71
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          84..368
                     /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 magltggdps llrrinsavv lhalratdaa tlteitrvtg lsrptvegvv eglieaglvv
       61 eaaadegtar rqgrparrfr frveaghllg leigphrvaa llsgldgrvi gaqakdvden
      121 apaderlerl rtavaellrr agvargslra vgaatpgive adgtvrlgta lpgwtglglg
      181 erlsrsfkcp vlvendanaa avaehwkgta tecddivfvl aglspgagal iggrlhrgyg
      241 gaageigalh llgrdvtpet llsttdqplh pldeqavakv faearegder araaverfiq
      301 rlvhdvaala laldpemvvi ggwaagldgv leplrrelar yclrpprval sllgeaavat
      361 galrlaldhv eeqlfavega tarr
//
LOCUS       WP_003978066             429 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Streptomyces].
ACCESSION   WP_003978066
VERSION     WP_003978066.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 429)
  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 429)
  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
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 429)
  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   5  (residues 1 to 429)
  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   6  (residues 1 to 429)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 429)
  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 20283677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..429
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45080
     Region          1..60
                     /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            4..5
                     /site_type="active"
                     /note="putative switch regulator [active]"
                     /db_xref="CDD:238044"
     Site            order(29,31..33,42)
                     /site_type="other"
                     /note="non-specific DNA interactions [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            42..48
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            order(43..44,48)
                     /site_type="other"
                     /note="sequence specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238044"
     Site            43..44
                     /site_type="other"
                     /note="putative cAMP binding site [chemical binding]"
                     /db_xref="CDD:238044"
     Region          80..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 magrngrtvr dlrranrtav lqrlyfdgpl srfelgpatg lssgsvsnvv adlvadglve
       61 eagsvdsdgg rprtllrvap asghmigvdv getrvrvelf dltltelara erplapqrhd
      121 vdvivghvrd giaevlatag lpperllgag igvpgiveht adrgavvhgq tigwdavple
      181 allragsplp dtvpwlidng aktlgqaemw fgagrgarna vvvlfgsgvg aslvtpeaeq
      241 gravewghlt vrvrgrrcrc galgcleaya gaesllarwr eeggrvpegt deetaltaml
      301 aaaypadgaa adpvalavle etaeylgagl sdlinlfqpe riliggwagl qlgarflpav
      361 rrhavsyalr hparkvtvdl grlgpdavtv gaailpladf farggrrpep apeypvpawr
      421 taleeraph
//
LOCUS       WP_003972418             642 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: molybdopterin oxidoreductase family protein
            [Streptomyces].
ACCESSION   WP_003972418
VERSION     WP_003972418.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 642)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 642)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..642
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=70623
     Region          13..636
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mrkrdrtpkt ytrlthplvr dsreaplrra tweealdrta rgltaargaf gmfscaratn
       61 emnyvaqkfa rvvmgthnvd scnrtchaps vaglsaafgs gggtssyeei ehtdvivmwg
      121 snarfahpif fqhvlkgirg garmyvvdpr rtstaewaes wlgpnvgtdi plahavgrei
      181 ihaglaneaf ierattgydd ykalvepwtl slaekvtgvp aaairelaha yaraeraqlc
      241 wtlgitehhn gtdnvralin lslltghvgr ygsglqplrg qnnvqgggdm gaipnrlpgf
      301 qdvldpevrr kfetawdtvv ephhgltlte mfeamdegtl ravycigenp aqseadaeqa
      361 vrrlraldfl vvqdifltkt aeladvvlpa tagwaetegt ttnserrvqr vrravsppge
      421 aredidilcd laarlghdwk yadaeavwne lrslspdhhg mtyarleehq giqwpcpstq
      481 eleptylhgr lwaqdpasrg rlapfgivrh dppvdltdeq ypirlttgrr ldsyntgvqs
      541 ggyasplrrg esvelcpeda erygvvvgee vrvtsrrgsl lapvwvdtal rpglafmsfh
      601 fpdevdtnql tieancpiag taefkasair iekvsasgpa lr
//
LOCUS       WP_003981250             290 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Streptomyces].
ACCESSION   WP_003981250
VERSION     WP_003981250.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 290)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 290)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..290
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32280
     Region          19..102
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          126..284
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mlerlneale hieshldrqi evsrlariam tseyhfrrmf salagvslse yirrrrltva
       61 gaevlagert lleiavrygy gsgeafaraf ravhgvgpge arrtgaalhs qprmsfrlii
      121 egsssmryrv vekeqfhvig kkarvplvhq gvnpaiadfi rgigqetldr italsdqqpe
      181 glvavcddld psraegteld yyhgvvsqlp apddldtlvv pagtwavfen sgpfpealqf
      241 lwrdvftqwf psnpyqsrpg peilrtrlsq dssqadaelw ipverlndag
//
LOCUS       WP_003982427             378 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Streptomyces].
ACCESSION   WP_003982427
VERSION     WP_003982427.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 378)
  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 378)
  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
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 378)
  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   5  (residues 1 to 378)
  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   6  (residues 1 to 378)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 378)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 378)
  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 11513089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..378
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38609
     Region          2..74
                     /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(2..3,17..19,28..31,33..34,37..38,40..41,47,54..55,
                     60..62)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(17,20,69)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
     Region          65..367
                     /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 mndraaldll vaqgpltrtq igaltglskp tasqllgrle aaglvrttgn vtgrpgpnaq
       61 lyevnpdaay vaalavdqcg itaavadvtg rvlgeervgt daveedappk taqlvasavd
      121 galdkagltr erlhgavigt pgaldpqtgv lryaphlpgw haralkdela gvlgvpivie
      181 ndvnlaavae qhggaaqdfd dfvlvwadeg vgaaivlggq vlrgatggag eigymplpga
      241 plarggdrda arpdagggfq rlvgspsive lareyggadv rtvdealddd rvraevarrl
      301 atglaavvav vdprlvvlsg evaqvggepl relveeeftg lalprpeiri sniegnpilt
      361 galhtalaea rnavfdta
//
LOCUS       WP_003984551             212 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Streptomyces].
ACCESSION   WP_003984551
VERSION     WP_003984551.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..212
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22916
     Region          19..205
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 msdgpatldi dglltrtptv rrrldltrpv arpllaqclr lalhapnggn rqnwwflvid
       61 dpetkagiaq yykaasdayl daappaamse ravagvrhla dhlhqvpalv lagtrgrlph
      121 daplarqssf fgsvypavws fmlaarsrgl gtalttvhla herevaalvg ipademtqva
      181 lvavghttge sgfrptprqp ldevvswnrw qq
//
LOCUS       WP_003973552             549 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: M4 family metallopeptidase [Streptomyces].
ACCESSION   WP_003973552
VERSION     WP_003973552.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 549)
  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 549)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..549
                     /product="M4 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=56869
     Region          47..548
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 msslfachkr ttlalatavt agamlttglt agnaaadsaa psalpgapvl lsgsarsali
       61 qeqqagaagt aremglgake klvvkdvvkd rdgsvhtrye rtydglpvlg gdlvvhrses
      121 gatrgvtkat eaavkvatvt pkvkaakaeq qalsaakdag ssktaadsap rkviwaaqgk
      181 pvlayetvvg glqddgtpne lhvitdaatg aklyeyqgik tgsgkslysg tvelgttrsg
      241 ssyqlydtgr gghktynlar ktsgtgtlft daddtwgtga assdpqdqta avdaaygaqv
      301 twdfykesfg rsgikndgka aysrvhygsn yvnafwsdsc fcmtygdgtg ntnpltsldv
      361 aghemshgvt sntaglnysg esgglneats difgtgveyf anssadkgdy ligeriding
      421 dgtplrymde pskdgaskdy wdsglggvdv hyssgpanhf ffllsegsga rtvdgvdyds
      481 ptsdgstvtg igrdkalqiw ykalteymts ttdyadarta tlsaasdlyg adsteyktvg
      541 aawtainvs
//
LOCUS       WP_003983472             356 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Streptomyces sp. SID5471].
ACCESSION   WP_003983472
VERSION     WP_003983472.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. SID5471
  ORGANISM  Streptomyces sp. SID5471
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 356)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Streptomyces sp. SID5471"
                     /db_xref="taxon:2690298"
     Protein         1..356
                     /product="amidohydrolase family protein"
                     /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=37006
     Region          <4..344
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mfgaesnlqq alafgvttel dmfmgppedt ralcrlager hdladlrsag llasapgghp
       61 avtmptlptv agpgqadafv aarqaegahf ikimvddgvn hgrslpalep atvtaladaa
      121 rrrgllsvah vsavwsarra ldsgvdvlth lpleaaldda fvrraaearr vviptlamle
      181 vsaprsatgv trsladgpri aaflsdhara aitegreglc vehplpahrf rhalssvarl
      241 hragvpvlag tdanhrpgra cpvvhgaglh aelallveag ltpaealtaa taapaarfgl
      301 sdrgviapgr radlvlvagd pttditatrs ieavwrggvr fdreayrerv asrtaa
//
LOCUS       WP_003986372             534 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: M4 family metallopeptidase [Streptomyces].
ACCESSION   WP_003986372
VERSION     WP_003986372.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 534)
  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 534)
  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 11461404
            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="M4 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=55945
     Region          37..534
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mtstprkhsl raaalvasaa mvavafqtgs ataqpdaatg alalsgqqrv aaiksaqada
       61 agtaqkiglg gqekliardv ikdadgtvht ryertyeglp vlggdlvvhe kkngtrtvdk
      121 atqaeiavpt tdaaqpaaaa kksalsasaa ekntkaeakn aprkviwaas gkpvlayetv
      181 vtgvqkdgtp selhvvtdak tgkklfqdet ietgtgtssy sgtvpltttk sgstynltdg
      241 argghktydl nqgtsgtgtl ftdaddkwgg grqtaavdah ygaavtwdyy knvhgrngir
      301 ndgkaaysrv hygnsyvnaf wqdscfcmty gdgqnnsnpl taldvaahem shgvtaatak
      361 lnysgesggl neatsdifgt aaefyannav dkgdyligek idingdgtpl rymdkpskdg
      421 askdywsssl gnvdvhyssg panhwfylvs egsgskting vnynsptydn skvtgigrak
      481 aekiwyralt tyftsttkya gartgtlkaa adlyganste yktvaaawtg invk
//
LOCUS       WP_003978962              77 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Streptomyces].
ACCESSION   WP_003978962
VERSION     WP_003978962.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 77)
  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 77)
  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 77)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 77)
  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   5  (residues 1 to 77)
  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 10164212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..77
                     /product="winged 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=8259
     Region          12..73
                     /region_name="WHTH_GntR"
                     /note="Winged helix-turn-helix (WHTH) DNA-binding domain
                     of the GntR family of transcriptional regulators; cd07377"
                     /db_xref="CDD:153418"
     Site            order(33,35..36,44..48,50..51,54,64..65,67..70)
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:153418"
ORIGIN      
        1 meidralphw pqvaaeirrr iqngtyrpge rlpgtvaiaa efdvsqstat ravaslrpeg
       61 lvrvvsgrgy fvaegan
//
LOCUS       WP_003956626             217 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Streptomyces
            clavuligerus].
ACCESSION   WP_003956626
VERSION     WP_003956626.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces clavuligerus
  ORGANISM  Streptomyces clavuligerus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  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 217)
  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   3  (residues 1 to 217)
  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   4  (residues 1 to 217)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 217)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 217)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Streptomyces clavuligerus"
                     /db_xref="taxon:1901"
     Protein         1..217
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=23781
     Region          24..213
                     /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"
ORIGIN      
        1 mtapdspqpv adddvshipp lttrvviaed ealirldlke mleeegyavv geagdgqrav
       61 elarehrpdl vildvkmpvl dgisaaeqia aesiapvlml tafsqrdlve rardagamay
      121 lvkpfsksdv vpaiemavsr ftelkaleke vadlslrlet rklvdraksv lmteyglnep
      181 aafrwiqkts mdrrlsmqqv aeaviqdsee kkaakgq
//
LOCUS       WP_003989905             214 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease family protein [Streptomyces].
ACCESSION   WP_003989905
VERSION     WP_003989905.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..214
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=23062
     Region          <116..209
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mpkfyarrrl svlagltgli asaglingpa asaalptpvs aatarsylss ltvatedrtg
       61 ydrdlfphwi tqsgacntre vvlkrdgtnv qqdsscaats gswyspydga twsaasdvdi
      121 dhlvplaeaw dsgadswtts rrqsfandlt rpqliavtdn vnqakgdqdp atwmpsrtay
      181 rctyvrawvq vkyyyglsvd saeksaltny lasc
//
LOCUS       WP_003993686             296 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            viridochromogenes].
ACCESSION   WP_003993686
VERSION     WP_003993686.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces viridochromogenes
  ORGANISM  Streptomyces viridochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 296)
  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 296)
  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 296)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces viridochromogenes"
                     /db_xref="taxon:1938"
     Protein         1..296
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33007
     Region          37..90
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          113..291
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mdvvgvegea aagsagarav pagewereph psdslrtfga vvqalrehag lsrvdlgarv
       61 qyskhtvesv elgrrmpdea fveraeealg ntgalrkaar hltrgeagla awfrrwarle
      121 reavslctye crlvpgllqs eayaravfeg tiplrtdeel evqlaarmer qvmmrerptv
      181 pfsfiveehv frrqfgdaea mrglmdhvle ltaprnvtlq vvpvearlha cldgplqile
      241 tsegrrlgys egqqngrlis dpkemillcq rydtlrsqal nptesrdlle rlrgel
//
LOCUS       WP_003993717             403 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces
            viridochromogenes].
ACCESSION   WP_003993717
VERSION     WP_003993717.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces viridochromogenes
  ORGANISM  Streptomyces viridochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  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 403)
  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
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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   5  (residues 1 to 403)
  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   6  (residues 1 to 403)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 403)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces viridochromogenes"
                     /db_xref="taxon:1938"
     Protein         1..403
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41000
     Region          14..77
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          77..379
                     /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 metpgsqssl hranlervvr avrlagsltq aeiarttgls aatvsnivre lkdggtvevt
       61 ptsaggrrar svslsgdagi vigvdfghth lrvavgnlah qvlaeesepl dvdassaqgf
      121 draeqlvsrl ieatgvdrsk iagvglgvpg pidvesgtlg stailpgwtg tkpaeelrgr
      181 lgvpvhvdnd anlgalgemv wgsgrgvrdl ayikvasgvg aglvingkiy rgpggtagei
      241 ghitldesgp vcrcgnrgcl etftaaryvl pllqsshgtd ltmegvvrlg regdpgcrrv
      301 iadvgrhigs gvanlcnlln psrvvlggdl aeagelvlgp iresvgryai psaarhlsvl
      361 pgalggraev lgalalalse mgdstlldgt apgtlqtatp aft
//
LOCUS       WP_003993910             422 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces
            viridochromogenes].
ACCESSION   WP_003993910
VERSION     WP_003993910.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces viridochromogenes
  ORGANISM  Streptomyces viridochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  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 422)
  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
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 422)
  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   5  (residues 1 to 422)
  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   6  (residues 1 to 422)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 422)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces viridochromogenes"
                     /db_xref="taxon:1938"
     Protein         1..422
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43810
     Region          16..59
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          79..393
                     /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 mghpvkrtsr dirtanryev lrqiiaespt srqelaaatg lslatvatlv gelldlgmit
       61 evgfedsagg rprglvavna sggaligvdi aetyvhvelf dlglnvlara dedvrasesl
      121 peqvvghvat avgsvvtqag iegarvlgvg vsvpgqvdra tgiseyapnw dwhsvplldl
      181 ltehiayplh ldnplrasav aelwfgaarg rsnavvvnlg tgvgaglvlg gglhrgvsns
      241 agewghttmv ldgrlcrcgn hgcveayvga rgimmnlrel spdsallhpe dqtatidala
      301 rgvaagdpva rrvvhetary lgagvadlvn lfnpeivvls swvgialgep llhevreavt
      361 rhalprplaa teivlspipt dpvclgaatf alegalqaag qkngtrtapa rsrtrtaatp
      421 ps
//
LOCUS       WP_003995582             373 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces
            viridochromogenes].
ACCESSION   WP_003995582
VERSION     WP_003995582.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces viridochromogenes
  ORGANISM  Streptomyces viridochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 373)
  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 373)
  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
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 373)
  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   5  (residues 1 to 373)
  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   6  (residues 1 to 373)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 373)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 373)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Streptomyces viridochromogenes"
                     /db_xref="taxon:1938"
     Protein         1..373
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37348
     Region          2..62
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          70..357
                     /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 mdlsesarav favlaaagsa trpqlaslag lskptvssav aelesarlaa hsgtasggtg
       61 rsaavyglgp aagavlavdl gpaltrvrgc aldgtllaqa tgtreeaadv vrealvalpa
      121 gaplrtvvva vgdvtareke garmrpatak agpvfdamav alppgvpvhl ennvncaala
      181 elhegaargr rtfgylrigv giglgivvgg qvlrgangaa gelarlpypw ddgreprhea
      241 leeyigarsl lrraaeawpd edgpcprtae qlfalagegr aaaravigrh atdvgrlaaa
      301 vtavldpgli vlggstgadp qvlpgvrael arlswptevv sstvgdlgtv vgaarlavtr
      361 gvqtvteaag akd
//
LOCUS       WP_003997070             399 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Streptomyces].
ACCESSION   WP_003997070
VERSION     WP_003997070.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 399)
  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   5  (residues 1 to 399)
  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   6  (residues 1 to 399)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 399)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..399
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40598
     Region          14..77
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          77..379
                     /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 metpgsqssl hranlervvr avrlagsltq aeiarttgls aatvsnivre lkdggtvevt
       61 ptsaggrrar svslsgdagi vigvdfghth lrvavgnlah qvlaeesepl dvdasstqgf
      121 draeelvnrl iaatgvdrsk iagvglgvpg pidvesgtlg stailpgwtg tkpaeelrgr
      181 lgvpvhvdnd anlgalgelv wgsgrgvrdl ayikvasgvg aglvisgkiy rgpggtagei
      241 ghitldesgp vcrcgnrgcl etfaaaryvl pllqsshgtd ltmegvvrla rdgdpgcrrv
      301 iadvgrhigs gvanlcnlln psrvvlggdl aeagelvlgp iresvgryai psaarqlsvl
      361 pgalggraev lgalalalse mgdstlldst lhaatpaft
//
LOCUS       WP_003986039             285 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Streptomyces].
ACCESSION   WP_003986039
VERSION     WP_003986039.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..285
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29662
     Region          15..256
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mtrawevava aparlgegpt wdaragrliw vdilsarvht vdpatgrrtv lateqhvgaa
       61 kprrggglvv nlrdgvgtyd adgafawlhr epvagrrgnd aavapdgalw agtmaydeap
      121 grgtltriap dgsatrvlsd vtvsngtgws pdgrrmyyid tptrrvdvfd vtdeglvtgr
      181 rpfveieepa etagypdgla vdaeggvwva mfegaqvrhy tpggvlervl pmpvarptac
      241 afggaaltdl yvttarggpg aaplggsllv vpdagrglaq pefag
//
LOCUS       WP_003998201             275 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            viridochromogenes].
ACCESSION   WP_003998201
VERSION     WP_003998201.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces viridochromogenes
  ORGANISM  Streptomyces viridochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (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
REFERENCE   4  (residues 1 to 275)
  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 18542080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Streptomyces viridochromogenes"
                     /db_xref="taxon:1938"
     Protein         1..275
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30958
     Region          15..71
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
     Region          95..270
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mnskklprkk nlstmrmvgk qmqaarkaag ftqsslgkav ladeetiasi eqgrrpllle
       61 laqaldelld tkgtlaagve nmpeidqfpl faeqymvher eaislcwydn avlpgllqtr
      121 dyaravlrer vppydedele aktegrierq eilhrkcppm msfivwepvl yielggpkvh
      181 rdqlrhlrec aelpglalqf lpmrtsahag ldgpftllet pdhqhlayte sqrgsqwvsg
      241 pdevsilark yamlrsqamt pqeskslldr lvgdk
//
LOCUS       WP_003982235             548 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: M4 family metallopeptidase [Streptomyces].
ACCESSION   WP_003982235
VERSION     WP_003982235.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 548)
  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 548)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..548
                     /product="M4 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=56616
     Region          44..548
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 msphisrrar itgvslaaag aliaaavtag tagasptaps gtttgaaaas pvkmtashra
       61 ellrdasatk aqtaqqlglg aqeklvvkdv ikdadgttht rydrtfaglp vlggdlivhr
      121 akggavkstt kansakiavt sttpkvapka aaqaaqgtak sfgakqaaav tpkkvvwaas
      181 gtpvlaydtv vggfqkdgtp nqlhvitdan tgkklfqyqg iengagtsay sgsveigtkk
      241 ggdgyeltdd srgghstfnl ngsesgegkl ftnkddkwgn gkaddpetaa vdaaygaqvt
      301 wdyyknvhgr agikgdgkga tsrvhygqny snafwddscf cmtygdgagn kkpltsidva
      361 ahemshgvts atanltysge sgglneatsd ifgtsveffa knkedagdyl igekidiagd
      421 gkplrymdkp skdgqsldsw tpeagnvdvh yssgianhff yllsegsgak eiggvkydsp
      481 tadgkkvegi grdkaekiwf kalttymtsn tdykgareat vkaatdlfgk dsaevkgvea
      541 awtgvavk
//
LOCUS       WP_003999003             274 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            viridochromogenes].
ACCESSION   WP_003999003
VERSION     WP_003999003.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces viridochromogenes
  ORGANISM  Streptomyces viridochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 274)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Streptomyces viridochromogenes"
                     /db_xref="taxon:1938"
     Protein         1..274
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30258
     Region          20..272
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          24..126
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
ORIGIN      
        1 meaprhdtrg ivdpsgllsr vrfrrhepae plrryvewyw lidwdlpapy ashivphpsv
       61 nltfqwdgad eetvppygev tgialglytr kltgrgrvcg vkfrpggfrp yapqapashw
      121 tgrvlpaqdv fpratadtar cvvspaadea rvaaldtfll sqpcvpdpqa dlamdlvqri
      181 radrtvrrvg dfargaglsv ralqrlfsay vgvspkwvil ryrihealel agtrrdvdwa
      241 llaadlgyad qahlvrdfta tvgvpptaya qgvt
//
LOCUS       WP_003999467             369 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Streptomyces viridochromogenes].
ACCESSION   WP_003999467
VERSION     WP_003999467.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces viridochromogenes
  ORGANISM  Streptomyces viridochromogenes
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Streptomyces viridochromogenes"
                     /db_xref="taxon:1938"
     Protein         1..369
                     /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=40822
     Region          32..300
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 msngipnava qfrspesaak pessrpasad ggrdaffdna kyllivlvav ahawelvess
       61 ratkalyvlv ytfhmpafiv isgylsrtfa arprqlrrlv ggiavpyvvf etayslfkry
      121 addahdhpis lldpwlltwf laalfiwrlt tplwqqlrhp lavaltiavl asvtpgvggd
      181 lnlqrvlqfl pffvlglclk pdhfrllgrr airlaaiplf agalafaywa atrmrtewff
      241 rrssaqeige pwwtgvvmtf alfacslllt aaflawvprr rtwftvlgag ticgyllhgf
      301 ltkgaqysgl vdanawlhdp agkvvltvva agavtvlctp pvrrvlrpvt epdlawafrr
      361 dpaertarg
//
LOCUS       WP_003999497             118 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Streptomyces
            viridochromogenes].
ACCESSION   WP_003999497
VERSION     WP_003999497.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces viridochromogenes
  ORGANISM  Streptomyces viridochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Streptomyces viridochromogenes"
                     /db_xref="taxon:1938"
     Protein         1..118
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=13202
     Region          1..71
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 miraadvrew rehdvvdpkg rkigtleavy vdtatdepam atvrtglptr qrlvfvplde
       61 avlgpgyvrv thakgtvrka psigtddvlp aereetifry ydmayrpgeh gerqlarr
//
LOCUS       WP_004000185             225 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Streptomyces viridochromogenes].
ACCESSION   WP_004000185
VERSION     WP_004000185.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces viridochromogenes
  ORGANISM  Streptomyces viridochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Streptomyces viridochromogenes"
                     /db_xref="taxon:1938"
     Protein         1..225
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=24220
     Region          <118..210
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 miknlrraai aavllvvpfl asaparahgr aaetytlpma aavqllplaa evrdgyqrts
       61 fkhwnagkhp adgcntraet llseavdrpd vlrgcrlsgg rwwsyydarw vtsasaldvd
      121 hmvplaeawd sgasqwtatr reayandlda vtslvavsaa snrskadqdp aewlppavgv
      181 lcryvsewta tklrwgltad atelealtql adacpgttvt yepap
//
LOCUS       WP_004003267             371 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Streptomyces viridochromogenes].
ACCESSION   WP_004003267
VERSION     WP_004003267.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces viridochromogenes
  ORGANISM  Streptomyces viridochromogenes
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Streptomyces viridochromogenes"
                     /db_xref="taxon:1938"
     Protein         1..371
                     /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=41576
     Region          27..298
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 msqpivttge avdtapatgt tsppaparqr daffdnakyl aivlvaagha weplrdgsrt
       61 vsalymvvya fhmpafivvs gyfsrgfdar pdrfrrlvtq lvvpyvvfet aytlftrwtd
      121 qepdrpisll dplyltwfla alfvwrlttp lwrwvrlplp laltlaalat lspsigddld
      181 lqrtlqflpy fvlglslrpe hfrlvrrrav riaavpvfgc afavaywavp rmtgawfyhr
      241 dsaeelgapa wygvvmtpvl fvcslllvac flswvpgrrm wctvlgagtl ygyllhgfva
      301 qgagfwgwyd pvwihrplga vvvtvvaaav vtllctppvr ralrfavepd lrwlfrretv
      361 epardraavr g
//
LOCUS       WP_004003487             296 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            viridochromogenes].
ACCESSION   WP_004003487
VERSION     WP_004003487.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces viridochromogenes
  ORGANISM  Streptomyces viridochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 296)
  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 296)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces viridochromogenes"
                     /db_xref="taxon:1938"
     Protein         1..296
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32364
     Region          17..66
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mssearewvw eysssrgtar lvllsiadrv adeqcvswas lsslakrtra svstvreaid
       61 rlvqageleq lddftgpqrs tvyrlplaak avaetaeede dadqapeeap evaptlrvsa
      121 lrrygirpre vpesparvrk pavpesgrsr rkparrrtgf rhvdvpetgt qnrsepdlnr
      181 ryssggaavl saaewqvdpa thawarqqgh ldrlgeqglq aadakwrahr agfnprrada
      241 waadwrswva rehaptrpnl yavpgkstaa pggmtraeah taallaalde ptgteg
//
LOCUS       WP_004004527             301 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Rothia dentocariosa].
ACCESSION   WP_004004527
VERSION     WP_004004527.1
KEYWORDS    RefSeq.
SOURCE      Rothia dentocariosa
  ORGANISM  Rothia dentocariosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Rothia.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Rothia dentocariosa"
                     /db_xref="taxon:2047"
     Protein         1..301
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=33039
     Region          150..286
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mtkskrpptp nlrdfkkiad vdprkilppd mdpknkrfly talailviiv liiaviyigr
       61 hsqggllgsp sapssatgdg eeqnvktesl eevknphdav dpatayapnl stakkelaal
      121 pvkeraskag ytreqfgaaw ddvdhngcnt rddilrrdlt nirfkagtra ctvqtgtldd
      181 pytgrtiefk rgkksssavq idhvvalsna wqtgaqdige ekrrelandp enlvaadgpa
      241 nmqksdadas dwlpgntayr ctyvarqvhv kakyrlwvta dekrvmenvl nsckdtnpvk
      301 k
//
LOCUS       WP_004004567             204 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator [Rothia].
ACCESSION   WP_004004567
VERSION     WP_004004567.1
KEYWORDS    RefSeq.
SOURCE      Rothia
  ORGANISM  Rothia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
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   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   3  (residues 1 to 204)
  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   4  (residues 1 to 204)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 204)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 204)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Rothia"
                     /db_xref="taxon:32207"
     Protein         1..204
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22917
     Region          16..204
                     /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"
ORIGIN      
        1 msektahehe gdqvsartvv vaedealirl diveilkdqg fevvaetdng ktaielakkh
       61 hpdlvlmdvk mpimdgitaa eeigkekiap vvlltafsqk elvdraveag amayvvkpft
      121 pndlfpaiev alsryeqlrt lekevttird qfetrklvdr aksllitkmn ltepeafrwi
      181 qktsmdrrls mrevsdtiik qlse
//
LOCUS       WP_004005316              88 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Rothia].
ACCESSION   WP_004005316
VERSION     WP_004005316.1
KEYWORDS    RefSeq.
SOURCE      Rothia
  ORGANISM  Rothia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 88)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 88)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Rothia"
                     /db_xref="taxon:32207"
     Protein         1..88
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=9162
     Region          1..88
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mqihffaaar aasgvaetqv sltdlveptl ralveklgea ftgktasgmt laqvmhqcsf
       61 lidgtrseld tvltdnarvd vlppfagg
//
LOCUS       WP_003988464             332 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Streptomyces
            viridochromogenes].
ACCESSION   WP_003988464
VERSION     WP_003988464.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces viridochromogenes
  ORGANISM  Streptomyces viridochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 332)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Streptomyces viridochromogenes"
                     /db_xref="taxon:1938"
     Protein         1..332
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35207
     Region          4..306
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mteqpigils tgshlpkeev tnaeiaarvg vptewieert gilerryaap deatsdlgih
       61 aaanalegag leadevdyli vststpdspq pptafhvqrg lgahkavcfd vnvvcsgfvy
      121 alaiarslir erpgsralvv gadiysrild ftdrrtavlm adgagaavvg avdepygftg
      181 felasrgdah qlirveaggs rlpasertvq ngdhyfrmeg ravrdfvldn fpslldalca
      241 rtdtsredia hfvphqpngv mlaqlverag ltsahthrtl drygnagnaa iaitldeahr
      301 qghlhpgdlv llggfgggms mgaglirwgv ta
//
LOCUS       WP_003994174             639 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Streptomyces
            viridochromogenes].
ACCESSION   WP_003994174
VERSION     WP_003994174.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces viridochromogenes
  ORGANISM  Streptomyces viridochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 639)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 639)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Streptomyces viridochromogenes"
                     /db_xref="taxon:1938"
     Protein         1..639
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=70351
     Region          11..632
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mrkrepktyt rlthplvrds rdeplrrasw eealdraarg largrgafgm fscaratnem
       61 nyvaqkfarv vmgtnnvdsc nrtchapsva glsaafgsgg gtssyeeieh tdvivmwgsn
      121 arfahpiffq halkgirnga rmyavdprrt staewaeswl glnvgtdipm ahaigreiih
      181 aglaneafie rattgfeeyr alvepwtlsl aekvtgvpaa airqlahaya raeraqlcwt
      241 lgitehhngt dnvralinls lltghvgryg sglqplrgqn nvqgggdmga ipnrlpgfqd
      301 lldpevrlkf eaawdaviqp hyglnltemf eamedgslka vycvgenpaq seadseqavr
      361 rlrsldflvv qdifltktae ladvvlpata gwaetdgttt nserrvqrvr kavtppgear
      421 edidiicdla arlghdwkya daetvwnelr svspdhygmt ydrleehqgi qwpcpsterl
      481 eptylhgrlw dpdpagrgrl apfgivqhdp pvdltdeqyp irlttgrrld syntgvqsgg
      541 yasplrrgey velcpedaer ygvvvgervq vtsrrgsvta pvwvdtalrp glafmtmhfp
      601 devdtnalti eancpiagaa efkasairie klpiativg
//
LOCUS       WP_004005590             183 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LytR C-terminal domain-containing protein [Rothia].
ACCESSION   WP_004005590
VERSION     WP_004005590.1
KEYWORDS    RefSeq.
SOURCE      Rothia
  ORGANISM  Rothia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 183)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Rothia"
                     /db_xref="taxon:32207"
     Protein         1..183
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=18876
     Region          97..182
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 msqyphdefd didentarrg tyrgviddps kspkgiipvv vagilslvig gamyinhprs
       61 sspeaaarak sysapaspse ssspsasase qakdanvavy nasapggsaa kasaalegyt
      121 itetanwsgt ppqsstvyyk deakksqaea iaktlnittv qessdtsilg endivvvlat
      181 dys
//
LOCUS       WP_004005906             653 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Rothia dentocariosa].
ACCESSION   WP_004005906
VERSION     WP_004005906.1
KEYWORDS    RefSeq.
SOURCE      Rothia dentocariosa
  ORGANISM  Rothia dentocariosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Rothia.
REFERENCE   1  (residues 1 to 653)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..653
                     /organism="Rothia dentocariosa"
                     /db_xref="taxon:2047"
     Protein         1..653
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=73005
     Region          3..497
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mpelnwvgkd kvithhldvp yrvldrqysy dehgqhqedn gsqnmiihgd nlealkallp
       61 ryegkvdcvy idppyntgne gwvyndavnd prikkwlgev vgkegedlsr hdkwlcmmyp
      121 rlrllqrlla ptgaifvsid dneaahlkam cdeifgarcf vadiswqrty strndskgip
      181 aevehlfvfs kqpgwnpnkl ertaemddky snpdgdrtaw tssdafapga athqgmvyai
      241 qhpftgelvy pargrcwtfe qaevlrilsg wtdyelrdld daderarvcg vatdevkpgv
      301 lgivlakpld qaradaqavy ergqwprfyf tkggqggvrr ktyldsvgga lptnfwsyev
      361 aghtdeakke iraifdgrva fdtpkptrli erilavatde nslvldsfag sgttahalln
      421 lnkadggnrr filvelgdya gsvtaervrr titgykdvre eqvvlfdhkl tlatlkkgad
      481 lvaeattvyq ealdqdyskv srpkvvtqvs gksatasvqv vatrihnhdv sgtggdfsfy
      541 elgpallvdg linpdidvsk vreyvwftet gqafsssssa hpyflgrydd asfffvfepd
      601 rvtsldrdyl asippecaas syviyadtcl lsdeelrsln itfkkiprdi trl
//
LOCUS       WP_004006835             202 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Mobiluncus].
ACCESSION   WP_004006835
VERSION     WP_004006835.1
KEYWORDS    RefSeq.
SOURCE      Mobiluncus
  ORGANISM  Mobiluncus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 202)
  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 202)
  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   3  (residues 1 to 202)
  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   4  (residues 1 to 202)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 202)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 202)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Mobiluncus"
                     /db_xref="taxon:2050"
     Protein         1..202
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22450
     Region          15..201
                     /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"
ORIGIN      
        1 maktasavkd tkvhrrviva edealirldi vetmkendfe vvgeaadgee avtlalelep
       61 dlivmdvkmp kldgiaaaek imketpcaiv mltafsdkel ierakdagtm aylvkpfdpk
      121 dllpaveval srhqellsle dsiadlqdrl ttrkqvdrak gllmekmelt epeafrwiqk
      181 tsmdrrlsmr evadavidql gd
//
LOCUS       WP_004008966             394 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Mobiluncus curtisii].
ACCESSION   WP_004008966
VERSION     WP_004008966.1
KEYWORDS    RefSeq.
SOURCE      Mobiluncus curtisii
  ORGANISM  Mobiluncus curtisii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Mobiluncus.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Mobiluncus curtisii"
                     /db_xref="taxon:2051"
     Protein         1..394
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=43812
     Region          8..>358
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mddfregnwl lradaavglr alhqagqrvq miyidppynt gntfayhdrr akdewlammh
       61 pllatareil tpdglifisi dfnqlcelkl emdrtfgten lignfvwvsn lkgrqlgagp
      121 agtheyilty ardatqvgkl rgrtellqkl mpavyhlpqr qvkhdargey vtknelyntn
      181 skfnevtaps mvfdilyhpq tgavrtsevg aadpelaaag wicahphpna kpglryhawr
      241 wsrakverdy adlefqvrgr gahrhlkiyt kirnfhetal kdlvigpsti sgqrelqrlg
      301 lgglfetpkp tkllqvliea atspgdtvld ffagsgttgq aahtagrrfv liqleepfss
      361 aksapasehg ldtiadltaa rlqaahvpfr ettl
//
LOCUS       WP_004001473             734 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Streptomyces
            viridochromogenes].
ACCESSION   WP_004001473
VERSION     WP_004001473.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces viridochromogenes
  ORGANISM  Streptomyces viridochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 734)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 734)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="Streptomyces viridochromogenes"
                     /db_xref="taxon:1938"
     Protein         1..734
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=78208
     Region          2..731
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mpnsatpthc pycalqcgmn ltptqdggva vverpdfpvn kgalcgkgrt aasvlasnvr
       61 ltsplvrsgg tlvpatwdea ldrvaeglgr trtehgpdac gvfggggltn ekayglgkfa
      121 rivlgtsqid yngrfcmssa aaagmkafgl drglpfpled ipktgcvilv gsnlaetmpp
      181 slrffnelke nggtlividp rrtrtaeqad lhlmprpgtd lalalgllhl vvaegrvdee
      241 yvqertvgwe earaaamahw peyveritgv pvpqlretvr lfcepehamv ltargpeqqs
      301 kgtdtvgawi nlclatgrag rplsgygclt gqgngqggre hgqkadqlpg yrklddpaar
      361 rhvaevwgvd pdslpgpgrs ayelldalgt diralllmgs npvvsapraa hieeriksld
      421 flavcdvvls etaaladvvl pvtqwaeetg tttnlegrvl lrrraitppe gvrsdlevmh
      481 elaarlggdr glekgfptdp eevfeelrra saggaadysg ityrrlieen gvfwpcpatt
      541 dgaqgvpdds eesedaslda aavvaddpaq ddeatgavhp gtprlfldrf atpdgrarfv
      601 pvshravaee pddeypvllt tgrvvaqyqs gaqtrrvdel naaapgpfve lhprlaarlg
      661 aaegdpvavv srrgravapa rittgirpdt vfmpfhwpge grantltnpa ldptsrmpef
      721 kacavrveav esrg
//
LOCUS       WP_004009737             250 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase, partial [Escherichia coli].
ACCESSION   WP_004009737
VERSION     WP_004009737.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>250
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
     Region          4..>250
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mrqdieasvi gglliggltp tasdvlatle peafsiplyr kafevirkqa rnrnlidalm
       61 vaeacgeehf tsilmtsknc psaanlkgya gmvadnyhrr lvleimdemr epiqsgtida
      121 ssqamdelvk rlsairkprd evkpvrlgei itdytdtldr rlrngeesdt lktgieelda
      181 itggmnaedl viiaarpgmg ktelalkiae gvasrvipgs dvrrgvlifs memsalqiae
      241 rsianagrmp
//
LOCUS       WP_004010042             580 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Mobiluncus curtisii].
ACCESSION   WP_004010042
VERSION     WP_004010042.1
KEYWORDS    RefSeq.
SOURCE      Mobiluncus curtisii
  ORGANISM  Mobiluncus curtisii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Mobiluncus.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 580)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 580)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Mobiluncus curtisii"
                     /db_xref="taxon:2051"
     Protein         1..580
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=63223
     Region          6..565
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mpngeilklg ragwipmcaa slfgllhsav tlslawvmsr ifatlysgey shlvvllgvl
       61 avlllvrpai algkellvsl igktvkidvr lkllqhlnni gpfglsskrt geaealvtdg
      121 velledyygr yipqiavtvv taitvlillf qldslvafig aivvvltptl pkawnkvltr
      181 rgyrhweqys qmnaevvdam qgmttlqlfn gveerrekiv ftsqqllstt lsqmrislle
      241 salsswvvyg gpvmvlalgv rqaaqgniav dslfwcmflg velfrpfqdl svnwhagyhg
      301 ystaqkalsl lkaptpddss lpqehrprtt eiqfndvsyr yssalqdavs dinleipege
      361 tlglvgqsgc gkstmlglll rfgdpnrgni riggvdlral srddrcslit lvpqepvifd
      421 gtiadnlrac asnasdellk slclslgled iapidtlldf rvdergsgvs ggqrqrvaia
      481 rallretpil lldeatsald aeterltwra idnhrnklas kgrsltiiss ahrlesvraa
      541 drivvlsagk iveignhdsl mhqggtyaml vatseelvqs
//
LOCUS       WP_004010885             295 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Mobiluncus holmesii].
ACCESSION   WP_004010885
VERSION     WP_004010885.1
KEYWORDS    RefSeq.
SOURCE      Mobiluncus holmesii
  ORGANISM  Mobiluncus holmesii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Mobiluncus.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Mobiluncus holmesii"
                     /db_xref="taxon:144178"
     Protein         1..295
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=32377
     Region          142..285
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mskldkigqg ftpeenpgle petpqvapwd gwfgkssnrn qrgrslalva favvavtglg
       61 tqfvgddgwf fgllggdrth stsqsgnage rtrdaagktt gtlardvldk levrdkdpfh
      121 dfdrerlfgk gwldldgndc ntrnevlard lenvqyraat pttpahcvvq sgvlhdkytg
      181 etidfrrsqe tsdavqidhv valgnvwrtg gqqlsqqere aiandplnle avkgqvnqdk
      241 qsqdaaawlp pardyrcayv arqiavkaky glwvtpaekq ammgvlkecp repip
//
LOCUS       WP_004010406             403 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Mobiluncus holmesii].
ACCESSION   WP_004010406
VERSION     WP_004010406.1
KEYWORDS    RefSeq.
SOURCE      Mobiluncus holmesii
  ORGANISM  Mobiluncus holmesii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Mobiluncus.
REFERENCE   1  (residues 1 to 403)
  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 403)
  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
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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   5  (residues 1 to 403)
  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   6  (residues 1 to 403)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 403)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Mobiluncus holmesii"
                     /db_xref="taxon:144178"
     Protein         1..403
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42473
     Region          23..76
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          83..380
                     /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 mgfvtmenll gpgspsslrv anqkrvlsai idaggisqae isrrtglapa tvsnivrelt
       61 eaeilrlaea asgrrgntia fapeigyamg vslereqvrv givtldhdiv dtqviplppe
      121 anatinkems valfdsmmaa kglenaqiva gcivvadavr sdgrmsnyts mipglnginl
      181 ediaqevspf piltendana galaehmwgv akdvddfvyv eassgigagi maggkilygt
      241 ggisgeighf pipshhelck cggsgclemi asvsaimasl rsleipvhtl rdlyrlieeg
      301 dvrvtrriqe agraigyvla qvcnilnpkm iviggelsfa gesflnqire tinqfalpdc
      361 aadttlrlsa lgssaplrga makavsmvdl dvilqrflad esn
//
LOCUS       WP_004004120             579 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Streptomyces
            viridochromogenes].
ACCESSION   WP_004004120
VERSION     WP_004004120.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces viridochromogenes
  ORGANISM  Streptomyces viridochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 579)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 579)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Streptomyces viridochromogenes"
                     /db_xref="taxon:1938"
     Protein         1..579
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=60658
     Region          3..561
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mivhpelrra agharrplla atllqgavtl thlaqavlla valadlarga tdrlplllga
       61 vlgvvagrav lgtwqrrtat ragaqvrvdl rdellarlgq lgpthlttar agavrttlvd
      121 gvegvdayvs rylpqllitl tvpplllaal aaieprallg lvpalllala gprawdrlla
      181 krgkehwdty eglgadylea lqgmpalraa gavsrtrerl eersaalhra tvaklrvslv
      241 dtgltdlaiq ggvvaaalla cwsavtgstt atgtylvlll asecfrpvrd lsrewhagyl
      301 gvsaadglaa lrtaapavpd tgtaqahwps ppelrfenve fsydgtdtpa lsgvtftaet
      361 grttaivgps gagkstllal llrhrdpqqg rimiggrdva eyaldslrqg iavvsqetyl
      421 fhatiadnlr larpaatdde lvraartagi hdeiaalpdg yatvlgerga tlsggqrqrl
      481 alarallada pvlvldeats avderreadi vrelldaagg rtvlvvahrl aavrhadriv
      541 vldgghvdav gehaalveag gvyaelvkag rtheeglaa
//
LOCUS       WP_004012017             645 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Mobiluncus mulieris].
ACCESSION   WP_004012017
VERSION     WP_004012017.1
KEYWORDS    RefSeq.
SOURCE      Mobiluncus mulieris
  ORGANISM  Mobiluncus mulieris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Mobiluncus.
REFERENCE   1  (residues 1 to 645)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..645
                     /organism="Mobiluncus mulieris"
                     /db_xref="taxon:2052"
     Protein         1..645
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=73023
     Region          57..534
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 madiekmdle skdliddrle klqdllpeaf sesgidfdkl rlllgdevde gseryaftwp
       61 gktdairqsq tvstatlrpc peksrsrdgk dgsfdsdniy iegdnlevlk llqrgyhgkv
      121 kmiyidppyn tghdfvyhds fgntienyke qaglagqsna etsgryhsdw csmmyprlkl
      181 arellsddgv ifisisnvel srlitmcsdi ygesnfidlf iwektqhfgr qklnsysnad
      241 yivcfakklv dkgvkellve kvknelqdap lynasnnlnt llfpagtvkf nmpdgiynet
      301 sseeytllds vkiidsrnen efrlrfrsrw snetvqreld kgttfwvktd kfairaiygt
      361 gktanesprq iiftntsnpk atfnrfgdri dtsenaskev qnlignafsy pkpvslikyl
      421 isllwtdgdf ddnplvmdff sgsgttaqav mdinlyatng narftlvqlp ekaaedrrtl
      481 cdigeerirr agdkiksdld esnrqlmlge epkqlpdigf rvftlddsgi ekpqpgklmh
      541 evvkpnrtel divfemmlkw gleltlpvek sdaadypvws vacdelvccm spgltieale
      601 aiadmepkrv lildsilndt lklnavqifk haserigtdi elrtv
//
LOCUS       WP_004012240             381 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Mobiluncus mulieris].
ACCESSION   WP_004012240
VERSION     WP_004012240.1
KEYWORDS    RefSeq.
SOURCE      Mobiluncus mulieris
  ORGANISM  Mobiluncus mulieris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Mobiluncus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Mobiluncus mulieris"
                     /db_xref="taxon:2052"
     Protein         1..381
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=43793
     Region          8..>292
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mekaqrlelt wynkdkalip tetgkygytw vdpadpryce thtlvfdeyv tgsqtpkndk
       61 sryteradle pqddnllilg esgdvlealt rvpelaekyv gkvkliyidp pfntaqtfan
      121 yednlehsvw ltmmrdrlvn lkkllredgs iwvhlddvev hrmrllldei fgsenfisev
      181 iwqkayggnn ssvefvsstd tvlvyskkrn nlqlnslprt pkmdsrysnp dndirgrwkg
      241 dnafgegagk pgksqhpgvy giqhpvtgkm vyprpgyhwv neqikmlqif kdwgeyvtgd
      301 ftfeekvnre kvcgpgviir edirplvwld wteekglary aqgnlpvyyp tsngyggfnl
      361 krylidmtsg ktpsiffrgk m
//
LOCUS       WP_004012812             293 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Mobiluncus mulieris].
ACCESSION   WP_004012812
VERSION     WP_004012812.1
KEYWORDS    RefSeq.
SOURCE      Mobiluncus mulieris
  ORGANISM  Mobiluncus mulieris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Mobiluncus.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Mobiluncus mulieris"
                     /db_xref="taxon:2052"
     Protein         1..293
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31331
     Region          3..261
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 melhidphvh salsdgtdap rdlllrarev gldvvgavdh dtfdhwasfh eahaellaag
       61 anppavllgs eistsvglqp vhllvylpdp srghlravlq nvhderlvrl qrmvenistd
      121 ypitwaevia evpgltpgrp hlgdalvkkg yfatrseafd rvlgphspyy vsrpvvdtfe
      181 vvaagladgg vpviahpfaa krgkrplqad tvrdlaragv agievyhrel gaaprdlalg
      241 laeelglfvs ggsdyhgrgk pnvlgenlmp ssslepilqr gatpllgelp trn
//
LOCUS       WP_004012553             303 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Mobiluncus mulieris].
ACCESSION   WP_004012553
VERSION     WP_004012553.1
KEYWORDS    RefSeq.
SOURCE      Mobiluncus mulieris
  ORGANISM  Mobiluncus mulieris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Mobiluncus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Mobiluncus mulieris"
                     /db_xref="taxon:2052"
     Protein         1..303
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=32581
     Region          <25..>110
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          133..272
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mkqksnvvfa lalafslaal lgscaneagt gepeqnetne ssqpsqpvet psiepaphet
       61 psdpgetppa eeaphetetp appaptgdap satvqeamnq letlpvkgra pktgyarsqf
      121 gkrwkdidhn gcdtrndiln rdlsaktyrp gthdcvvltg tlqepytgtq vsfdkkkaas
      181 avqidhvval sdawqkgaqq ltaeqreqla ndplnllavd grenqrksdg daatwlppnk
      241 afrcryvslq vnvktkyhlw vtsaekdait rvlskcsgav gwqnstpatq vgadnrltrn
      301 fsg
//
LOCUS       WP_004013006             626 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Mobiluncus mulieris].
ACCESSION   WP_004013006
VERSION     WP_004013006.1
KEYWORDS    RefSeq.
SOURCE      Mobiluncus mulieris
  ORGANISM  Mobiluncus mulieris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Mobiluncus.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Mobiluncus mulieris"
                     /db_xref="taxon:2052"
     Protein         1..626
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=70663
     Region          58..597
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mnrearehne avrpnsaeie rlrlafpeyf daqdafrldr feqmlkseai nlsregyelr
       61 flgktyakyq aglesetviv pdmehnaqpe nresenlyiv gdnldalghl vksyagmvkc
      121 iyidppyntg sdgfvyqddf gftarqlvdk igisedearr vldmrgkssh sawltfmypr
      181 lalakellsd dgvifisidd neqanlkllc deifgeqnfv asfvivrseg gglakqavig
      241 hdylptyakn idkfiplgrp kdirgkiink dgvdywietd wlrkefgkyg tcyyeeivry
      301 lgvekkreid agiesgdyvl vpkgqftivg rlrrvdtdts kfytvlkrld gegyakylnk
      361 lgvanlsslq ldsffsfpkp velvksvvqg ctilskndsd ivldffsgss ttadavmqln
      421 aedggnrryi mvqlpeiinp kdnrhskaay qagyrtidei grerikraaa kikvetgvni
      481 dygfklfrle tpaaktldel deftpnpaea lagdyvskfn ldgtpgrdvv latwlnqdgf
      541 gllakpqkll lkgytldvye dsayliepgi tsedvqelvr lletnellln rivvfpysvi
      601 fsvmhelkkn lsvlksgqsv evierf
//
LOCUS       WP_004013470             279 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Mobiluncus mulieris].
ACCESSION   WP_004013470
VERSION     WP_004013470.1
KEYWORDS    RefSeq.
SOURCE      Mobiluncus mulieris
  ORGANISM  Mobiluncus mulieris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Mobiluncus.
REFERENCE   1  (residues 1 to 279)
  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 279)
  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   3  (residues 1 to 279)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Mobiluncus mulieris"
                     /db_xref="taxon:2052"
     Protein         1..279
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31934
     Region          171..271
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mikdsyagie ttgslrakgv nwrqlkklvf tgelkeirrg wyayehadpg aiaaikhggq
       61 lgcisgcnvh glwippqyqr slhicvkswr naqpnlaesg vithrgadsr llsirsvedc
      121 lvdvmkhhda etalvmlesa vnmglityrd gealiarqsa qkrkllrhfa pgaesgsetr
      181 vrlwfnrrnl pvrtqerirs vgrvdllvgk sfivecdsra hhtqdenyhk drerdftsee
      241 lgyqvlrlsy ahiwrewdkt qkrlagiiek rkyrrepqv
//
LOCUS       WP_004008692             435 aa            linear   BCT 20-JAN-2025
DEFINITION  ferrochelatase [Mobiluncus curtisii].
ACCESSION   WP_004008692
VERSION     WP_004008692.1
KEYWORDS    RefSeq.
SOURCE      Mobiluncus curtisii
  ORGANISM  Mobiluncus curtisii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Mobiluncus.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Ferreira,G.C.
  TITLE     Ferrochelatase
  JOURNAL   Int J Biochem Cell Biol 31 (10), 995-1000 (1999)
   PUBMED   10582332
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Ferreira,G.C., Franco,R., Lloyd,S.G., Moura,I., Moura,J.J. and
            Huynh,B.H.
  TITLE     Structure and function of ferrochelatase
  JOURNAL   J Bioenerg Biomembr 27 (2), 221-229 (1995)
   PUBMED   7592569
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Taketani,S.
  TITLE     Molecular and genetic characterization of ferrochelatase
  JOURNAL   Tohoku J Exp Med 171 (1), 1-20 (1993)
   PUBMED   8122254
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Cole,S.P. and Marks,G.S.
  TITLE     Ferrochelatase and N-alkylated porphyrins
  JOURNAL   Mol Cell Biochem 64 (2), 127-137 (1984)
   PUBMED   6390167
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11477763
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Mobiluncus curtisii"
                     /db_xref="taxon:2051"
     Protein         1..435
                     /product="ferrochelatase"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0004325 - ferrochelatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47280
     Region          5..392
                     /region_name="hemH"
                     /note="ferrochelatase; Reviewed; PRK00035"
                     /db_xref="CDD:234585"
ORIGIN      
        1 msnlapydal llvsyggpng pedvlpflrn atggagipds rleqvgghyr lfggvspina
       61 rnaallsslh qrlgdeliya ignrnwhpyf seslidlvdr garriltlft taytcysgcr
      121 qyrenlaqal adlraarpei adqvtldrar pfantpgfvs anaraiaaaa rdlnltpdsa
      181 qspespsepv hlvyvthsip ldmarhsgpc hgahgatads dpnqkpalfd drfdtpvsrp
      241 svpmhqrqtd fspvalnalp avtreqnalg qgwtylaqhl avaqavqrhl saqgldlpws
      301 lafcsrsgsp hqawlepdin dhlrdlaaag vrrvivapfg fisdhmevvf dldteasata
      361 qelgleyrra atadsdpefl nelanlvyer aafargehps qsvepdtypp laetcgpncc
      421 qyprpahphl hhpnh
//
LOCUS       WP_004014795             578 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Mobiluncus mulieris].
ACCESSION   WP_004014795
VERSION     WP_004014795.1
KEYWORDS    RefSeq.
SOURCE      Mobiluncus mulieris
  ORGANISM  Mobiluncus mulieris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Mobiluncus.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 578)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 578)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Mobiluncus mulieris"
                     /db_xref="taxon:2052"
     Protein         1..578
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=62135
     Region          7..562
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mftnqirimr aggvtawlll psilagliss atyigaavln allftellts rnletiiyli
       61 sgvaimlilr pladvagqll qnraglklkt rlrgalldkl dkrgpmragl grsgkiqsvl
      121 tdgveaiepy fikyftqlvv tlvtaialti gmglisplia ivlllcgisi vaiprlwdka
      181 laergqshwi ayedlnadfi dammgmstlk sfgaadrygk rlqdqstsll qttlnqlrls
      241 lgetglsggm kvlgpalglt iaifqighqq melsqlfvit mlsieifrpf ntlsscwhea
      301 ffgisalpam naifsaadat ppaklteqts ktcgnisfqn vsytylgane lalngvsftv
      361 paqqitaivg lsgsgkstal glmmgfdqps sgtislagnn prqiditram tlvpqdpiif
      421 pgtvreills snpsatekem ldaltwahav nlhqenadda ssvlnlrvfe hatnlsggqk
      481 qrlaiarali rdtpililde stsaldsdte ysvlddirqa kpeltmlivt hridtaartd
      541 hvivlgngei lcqgfpaela knpdsawskl lhtqiveg
//
LOCUS       WP_004014829             399 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Mobiluncus mulieris].
ACCESSION   WP_004014829
VERSION     WP_004014829.1
KEYWORDS    RefSeq.
SOURCE      Mobiluncus mulieris
  ORGANISM  Mobiluncus mulieris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Mobiluncus.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 399)
  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   5  (residues 1 to 399)
  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   6  (residues 1 to 399)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 399)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Mobiluncus mulieris"
                     /db_xref="taxon:2052"
     Protein         1..399
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41730
     Region          20..73
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          80..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 mttetftgpg spsslrmanq krvlaaiida ggisqaeisr rtglapatvs nivrqlidag
       61 ilhlaetasg rrgntiafap digyamgvsi erelvrvgiv tldhtivdsq alqlppgfst
      121 algqekavem fdsmmeahgl knsqivagcv vvanavradg tlshfiamip gwndvnlekq
      181 aqaispfpil tendanagam aehmwgvaqd vadfiyveas ygigagimse grilhgsggi
      241 ageighlpvp gynnlckcgg tgclesvasl ssiiaslqdi glqvdtledl ykllengdir
      301 airqlrkaas amgyilaqic nilnpqmivi ggalshagel ylnqvretin dvalpdsasd
      361 melrlstlgs sgplrgamak avslanldai lqkfladev
//
LOCUS       WP_004016547             487 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Mobiluncus mulieris].
ACCESSION   WP_004016547
VERSION     WP_004016547.1
KEYWORDS    RefSeq.
SOURCE      Mobiluncus mulieris
  ORGANISM  Mobiluncus mulieris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Mobiluncus.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Mobiluncus mulieris"
                     /db_xref="taxon:2052"
     Protein         1..487
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=54977
     Region          2..376
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mykdkfgdti enykqqaslt gqsnadtsgr yhsdwcsmmy prlklarell sddgvifisi
       61 ddnenrnlri icdevfgean fvsqliwera yspkndakyv snshdyvlvy aksiehfvig
      121 rlprtaeana ryknpdndpr gvwkpsdlsv ktysaesdyp ittpsgrive ppagrcwrls
      181 rnafrerlqd nriwfgpdgd svpcikrflt elkfdgmapt simfykevgh sqegakelvt
      241 lfdgkgyfdg pkptkllqrl itlanladgd vvldffsgsa stahalfsqe letntsyhfv
      301 lvqlpeptdt srdafkdgya tlcdigeeri rragnkikae ldesnrqlml geepkqlpdi
      361 gfrvfqldes sierpepgql mndvvkskrt eldivfemml kwgleltmpv eksdaagypv
      421 wsvacnelvc cmspgltiea ieaiaemkpr rvlildsild dtlklnavqi fkhaserigt
      481 dielrtv
//
LOCUS       WP_004018972             362 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Gordonia
            terrae].
ACCESSION   WP_004018972
VERSION     WP_004018972.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..362
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37908
     Region          5..352
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mtgvdlevsi dltvpalrve hrfaagttta vvgpngagks tmlrvvagll rrddrcrlal
       61 gdrvfsdttt fvppsrrgia llsqdarlfp hltvadnvgf apaaqrlars eirerverwl
      121 satevadlad rkphqlsggq aqrvaiaral aaqprillld epfraldvdv asrlrallrt
      181 lladrdrtti mvthdpvdal glcddimvle dgrvvesgsa rdvltrptsr faaslsglnl
      241 fvgildadda vvdpsgnrvv gsagddgpqp gagaaatfsp ravavyleap hgsprttlaa
      301 gvrdiaprgd havvtaevgk qlvaaevtwa avadlglvtg lavylvvkas evrisavgpg
      361 sl
//
LOCUS       WP_004019045             318 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Gordonia terrae].
ACCESSION   WP_004019045
VERSION     WP_004019045.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            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="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33221
     Region          1..308
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mlldgaslwf rsffalpekm tspdgrpvna vrgfvdtian lvvrerpsrl vvcldldwrp
       61 efrtdlipty kahrvavpdg gtdvegrevd veevpdtltp qvdmimavla aagiatsgav
      121 gceaddvigt laydeandpv ivvsgdrdll qvvaddpvpv rvlyvgrgla kaemmgpvev
      181 aekygvpvdr agigyaemsm lrgdpsdglp gvagigekta akliteygsl daleaaaadp
      241 sssvptrsrk sllasvdylq aarivvsvrt dadtidsgsd vlpaepadpa alaelveelg
      301 igasvgrlak algwpqag
//
LOCUS       WP_004013543             439 aa            linear   BCT 20-JAN-2025
DEFINITION  ferrochelatase [Mobiluncus mulieris].
ACCESSION   WP_004013543
VERSION     WP_004013543.1
KEYWORDS    RefSeq.
SOURCE      Mobiluncus mulieris
  ORGANISM  Mobiluncus mulieris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Mobiluncus.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Ferreira,G.C.
  TITLE     Ferrochelatase
  JOURNAL   Int J Biochem Cell Biol 31 (10), 995-1000 (1999)
   PUBMED   10582332
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Ferreira,G.C., Franco,R., Lloyd,S.G., Moura,I., Moura,J.J. and
            Huynh,B.H.
  TITLE     Structure and function of ferrochelatase
  JOURNAL   J Bioenerg Biomembr 27 (2), 221-229 (1995)
   PUBMED   7592569
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Taketani,S.
  TITLE     Molecular and genetic characterization of ferrochelatase
  JOURNAL   Tohoku J Exp Med 171 (1), 1-20 (1993)
   PUBMED   8122254
REFERENCE   4  (residues 1 to 439)
  AUTHORS   Cole,S.P. and Marks,G.S.
  TITLE     Ferrochelatase and N-alkylated porphyrins
  JOURNAL   Mol Cell Biochem 64 (2), 127-137 (1984)
   PUBMED   6390167
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11477763
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Mobiluncus mulieris"
                     /db_xref="taxon:2052"
     Protein         1..439
                     /product="ferrochelatase"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0004325 - ferrochelatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48003
     Region          5..403
                     /region_name="hemH"
                     /note="ferrochelatase; Reviewed; PRK00035"
                     /db_xref="CDD:234585"
ORIGIN      
        1 mydvspydal mlvsyggpnr pedvlpflrn atggagipds rlrqvgrhye lfggrspinr
       61 rnqellaalr hrlgdnliyg ignrnwhpyf tetledlarr garriltlft aaytsysgcr
      121 qyrenlaaal asfqekhpei eltldrvrpf antpgfvaan vaavhealaq ladsqsspag
      181 tvppkthlvy vthsiplema rnsggrvsei dvvdenggls asrmaprepe atpgdtkath
      241 kpalfddrph peghstprhp eldpdtitgl aqvtkqqdcl gtgwtylaqh laianainrq
      301 lragglqlpw slafcsrsgs phqqwlepdi ndhlsdlqvs girnvvvapi gfisdhmevv
      361 fdldteavqt arevglnyvr aataesypgf ldqladlvae raalargehp elivepgtyp
      421 algencgvdc cryprhlhg
//
LOCUS       WP_004019738             781 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Gordonia terrae].
ACCESSION   WP_004019738
VERSION     WP_004019738.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 781)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 781)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 781)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            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="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=83978
     Region          13..756
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mdmtathsga gpdveilrdg hgiphvrgad paavlygqgr acgedrrwqi efmrlraegr
       61 taevfgascv ewdtfarraq ldaaarrifd assartrdlv aayaagvnst lddpdtsaaa
      121 pelealahrp qpwrpwtpis vfimhhvlfg rfttklfrlh acrtlgldal rfwdfetret
      181 dptmpampde afldeilait rpvspeqpsp avdlgdpmsg snawgvsaer sstgapivag
      241 dphrflelpg iyqqfhlast gpldafdmag fafagvpgvp hfcqgddiaw gitnamgdyq
      301 dlflerltrd etgtllvevp ggsrvparvs tetilvrgae pvatqvittp ngavvfggpe
      361 dsfamsirsp llsedvsfda pldllfastv adveaalvnw vepvnravia hadgtvathv
      421 agrvpvrape nywlpvpgwd eryqwrgyer gslgdpdfda tlrstgitvt anqrmsdvpa
      481 lqpltsecve pfradriaar lddldsvspa dcadihsdvr leqatvvqel lsrvradnaa
      541 aedvrqrlva wdrsmaadst daylyaefrt qlvlgvantd ilaplrgphg fpavfqpwfv
      601 peprlatalt svvantagig idieavavaa ldavvarvag fgstptwgsv hrlapihgfd
      661 lvgaspqypd lfatlrptpl plagdaesvf anaaavgthl citgaaaryv wdladrsasr
      721 wivplgvsgd prsehfqdqa aqwatgelve vvrdwdtlha maaaastpta atsterepcp
      781 r
//
LOCUS       WP_004019502             367 aa            linear   BCT 20-JAN-2025
DEFINITION  bifunctional L-1,2-propanediol dehydrogenase/glycerol dehydrogenase
            [Escherichia coli].
ACCESSION   WP_004019502
VERSION     WP_004019502.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Gonzalez,R., Murarka,A., Dharmadi,Y. and Yazdani,S.S.
  TITLE     A new model for the anaerobic fermentation of glycerol in enteric
            bacteria: trunk and auxiliary pathways in Escherichia coli
  JOURNAL   Metab Eng 10 (5), 234-245 (2008)
   PUBMED   18632294
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Subedi,K.P., Kim,I., Kim,J., Min,B. and Park,C.
  TITLE     Role of GldA in dihydroxyacetone and methylglyoxal metabolism of
            Escherichia coli K12
  JOURNAL   FEMS Microbiol Lett 279 (2), 180-187 (2008)
   PUBMED   18179582
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Truniger,V. and Boos,W.
  TITLE     Mapping and cloning of gldA, the structural gene of the Escherichia
            coli glycerol dehydrogenase
  JOURNAL   J Bacteriol 176 (6), 1796-1800 (1994)
   PUBMED   8132480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF047954.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..367
                     /gene="gldA"
     Protein         1..367
                     /product="bifunctional L-1,2-propanediol
                     dehydrogenase/glycerol dehydrogenase"
                     /EC_number="1.1.1.6"
                     /EC_number="1.1.1.75"
                     /GO_function="GO:0008888 - glycerol dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_function="GO:0019147 - (R)-aminopropanol dehydrogenase
                     activity [Evidence IEA]"
                     /GO_process="GO:0019588 - anaerobic glycerol catabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0051596 - methylglyoxal catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38611
     Region          1..366
                     /region_name="gldA"
                     /note="glycerol dehydrogenase; Provisional; PRK09423"
                     /db_xref="CDD:181843"
     Site            order(9..11,13..14,205,208,231..232,235)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:341449"
     Site            order(37,93..95,98,101,116..117,119,138..139,156,164,171,
                     175,254,258,271)
                     /site_type="active"
                     /db_xref="CDD:341449"
     Site            order(171,254,271)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:341449"
ORIGIN      
        1 mdriiqspgk yiqgadvinr lgeylkplae rwlvvgdkfv lgfaqstvek sfkdaglvve
       61 iapfggecsq neidrlrgia etaqcgailg igggktldta kalahfmgvp vaiaptiast
      121 dapcsalsvi ytdegefdry lllpnnpnmv ivdtkivaga parllaagig dalatwfear
      181 acsrsgattm aggkctqaal alaelcyntl leegekamla aeqhvvtpal ervieantyl
      241 sgvgfesggl aaahavhngl taipdthhyy hgekvafgtl tqlvlenapv eeietvaals
      301 havglpitla qldikedvpa kmrivaeaac aegetihnmp ggatpdqvya allvadqygq
      361 rflqewe
//
LOCUS       WP_004020351             312 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phytoene/squalene synthase family protein [Gordonia].
ACCESSION   WP_004020351
VERSION     WP_004020351.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..312
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33925
     Region          18..278
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mmhlpghtqv vpphrrydev aeacaamvir sysssfglas rllpprirrd iqniyalvrv
       61 adeivdaprp eqglvdrsne ldqleeqtsv alvtgsssnl vvhafaqtar rvgidldlvg
      121 pffdsmrsdl tqvqhdfdsl atyiygsaev vglmclrafl adepksaaqy dhlapgaqrl
      181 gaafqkinfl rdfgedsdgl grrylvgldp ddpadaawal wlddidldlt aaaaaiphlp
      241 agsrvavcta hdlfaeltar lressatear rtrvrvpnag kakiaaaava rrgmprtpra
      301 davglyrrkt nv
//
LOCUS       WP_004021138             396 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Gordonia terrae].
ACCESSION   WP_004021138
VERSION     WP_004021138.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..396
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42241
     Region          1..269
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          259..>315
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrivhtsdwh lgrtfhgvel ladqrralih laelvaaesa davivagdvy drsvpsadav
       61 rvydeglaei aaagaqivvt sgnhdsptrl gagsgfaaag glhlrtsiad idrpvllada
      121 hgdvaiygip ylepdtarrh lgvesagght avldaamtrv rtdlaarrar svvvahafvs
      181 gaaasgsers isvggvetvp aetfsgadyv alghlhspqr vtdtvrysgs llpysfgert
      241 hrkaalvidl dadgvaevrp helpvvrels sltgvlgdll tdqqydaaqd hyvevtltdp
      301 vrptdamrrl rerfpfavhv qwerphsgsg vdyrsrvrgr sdaeivasfi sdvrdeptkg
      361 ervlleralr avvgepesda aeltlfdiea ivaesa
//
LOCUS       WP_004021368             401 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Gordonia terrae].
ACCESSION   WP_004021368
VERSION     WP_004021368.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 401)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..401
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=43396
     Region          <92..396
                     /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 mltlgssvia vsvdpyhrav vaygyeaaas aserfieqvl mpispqarfh rrsdfywiiy
       61 lpwtgagdde lgrnalieaa rtklgahtvs dgdrswfldv cmgvavgdeq laasseddlv
      121 rhadaalcia lssrravafa tptmqrhira evdlagwltr sverdfsvfy qpivavpdrr
      181 vvgyesllrw htesgvlapd aflsvaegis llapigrhai geairdlsgt isdevgpgtf
      241 vslnlsgqql wddglvsyvh glidghgvep srvwvevred qairvdtsas raidalhdlg
      301 cticiddlga gfsalryvrd lpvdvlkvdr tliaqladss pdravvraig emaaatgvkm
      361 vaegieseev lpileefgfd yaqgylfgrp aplvdlfgsd r
//
LOCUS       WP_004022814             161 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Gordonia terrae].
ACCESSION   WP_004022814
VERSION     WP_004022814.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 161)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..161
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=16317
     Region          72..155
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mnadrepnrl plragammlf avavvfiglg whsaatagnd sptteaattv sstptstsps
       61 tsavstgkrl cvinagqvag lasdvtellq akgyqmaepg nytaggfsen tifheddtdk
      121 aqadevaeal ggtvaveerp tsftrcrggi pvvvvtavsg a
//
LOCUS       WP_004016185             285 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Mobiluncus mulieris].
ACCESSION   WP_004016185
VERSION     WP_004016185.1
KEYWORDS    RefSeq.
SOURCE      Mobiluncus mulieris
  ORGANISM  Mobiluncus mulieris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Mobiluncus.
REFERENCE   1  (residues 1 to 285)
  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 285)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Mobiluncus mulieris"
                     /db_xref="taxon:2052"
     Protein         1..285
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29838
     Region          1..274
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mladirklag daaarhvglg afnvvllehg eaqvaaaesc glpvilqlsq navkyhhgrl
       61 rpigsavlrl aeearvpvva hldhaedidl ckaavdlgft simydgskla daenrrstae
      121 itqwchdrgv sveaelgevg gkngvhdpsa rtnpddaahf vtdtgvdlla vavgsshamt
      181 srdaaldndl iariaaavpv plvlhgssgv sdagmraair agmtkinvst hlnvvytemv
      241 rrdlaagpel vdprkysrgg naavqaever llrmystpva aavds
//
LOCUS       WP_004024333             305 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Mycoplasmopsis agalactiae].
ACCESSION   WP_004024333
VERSION     WP_004024333.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis agalactiae (Mycoplasma agalactiae)
  ORGANISM  Mycoplasmopsis agalactiae
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Mycoplasmopsis agalactiae"
                     /db_xref="taxon:2110"
     Protein         1..305
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34762
     Region          1..292
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mnsenklmll vdgnflifqs fyasynkynp nsvlvakdgt ttngvhvffq tlfklikfyn
       61 pshmfiafda kgktkrheey ydykagreka peiifeqfdl akkilsamni kwfekvgyea
      121 ddliatvakh nsqfnnyiys kdkdllqlvn ennsiikvik kvgnfteykl etinefaniy
      181 ginpnqipdy kglagdssdk lkgvagigpk kaisllnefg tleaiyenin kitgktkeyl
      241 endcesahfc kklailnsdv emdtniddyq iilnqdkaie ilkefgfdsv ldtyvnvllp
      301 kyklt
//
LOCUS       WP_004026030             528 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Ureaplasma urealyticum].
ACCESSION   WP_004026030
VERSION     WP_004026030.1
KEYWORDS    RefSeq.
SOURCE      Ureaplasma urealyticum
  ORGANISM  Ureaplasma urealyticum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Mycoplasmoidaceae; Ureaplasma.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Ureaplasma urealyticum"
                     /db_xref="taxon:2130"
     Protein         1..528
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=61511
     Region          87..>446
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mikdldsylk didemskssl nedqkqlikk ilektdpqdl dnvfqlliqr vkigfsfdva
       61 psvhqtqiai lakneqlsfm ndahnlfknd tnsliigeny dvlknllvle reretsgrda
      121 yydviyidpp ynteasktdg nnfsekddva askfvyrdkf srngwlnmmn erlklaknll
      181 kndgvifvsi ddneqaylkv lmdeifgeen ftcnfvwekn yapknnnkfv svnhdyilcy
      241 cknkilknkf nrnqrteknn rlyfykddrg fykssdltkk gsnniydiiw dgkkylcpkn
      301 sswlyneekm yelikqnrif lpenennrpf lkkylnevdd vislsilkye vvnhtdgskk
      361 qldsildnhn fntpkpieli kyliniastn narildffag sgttghavla lnkedggnrt
      421 ftivtnnene igtnvcyerl yrinngfgtk netdfdwink nkpylnnlnv ydlkyfdtnp
      481 ikidnneike aftkmlvdfn dasqsnlfds nqrellinls tlksinnk
//
LOCUS       WP_004027078             529 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Ureaplasma urealyticum].
ACCESSION   WP_004027078
VERSION     WP_004027078.1
KEYWORDS    RefSeq.
SOURCE      Ureaplasma urealyticum
  ORGANISM  Ureaplasma urealyticum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Mycoplasmoidaceae; Ureaplasma.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Ureaplasma urealyticum"
                     /db_xref="taxon:2130"
     Protein         1..529
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=61423
     Region          87..>447
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mikdldsylk didemskssl nedqkqlikk ilektdpqdl dnvfqlliqr vkigfsfdva
       61 psvhqtqiai lakneqlsfm ndahnlfknd tnsliigeny dvlknllvle rereretsgr
      121 dayydviyid ppynteaskt dgnnfsekdd vvaskfvyrd kfsrngwlnm mnerlklakn
      181 llkndgvifv siddneqayl kvlmdeifge enfvtnfiwq kksggglnkl iyegheyilc
      241 ysknnynfcl seknkkmsgf ikykdknnns ffinsdiirn nfgkkdnkfe hrnkayedls
      301 kedkekwnlk ldnknyilvp fkkepgkhlv akifnderkt tysiiklpft fvsgiwtkdg
      361 nnevdslnid fqnpkpiqli mhlldlhsnk narvldffag sgttghavle lnkedggnrt
      421 ftlvtnnenq igtnvcyerl yrinngvgtk neadfdwink neaylnnlnv ydlkyfntnp
      481 ikidnneike aftkmlvdfn ntsqsslfen nqrellinls tlkpiekke
//
LOCUS       WP_004028311             401 aa            linear   BCT 20-JAN-2025
DEFINITION  prolipoprotein diacylglyceryl transferase [Spiroplasma melliferum].
ACCESSION   WP_004028311
VERSION     WP_004028311.1
KEYWORDS    RefSeq.
SOURCE      Spiroplasma melliferum
  ORGANISM  Spiroplasma melliferum
            Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Entomoplasmatales;
            Spiroplasmataceae; Spiroplasma.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002130
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Spiroplasma melliferum"
                     /db_xref="taxon:2134"
     Protein         1..401
                     /product="prolipoprotein diacylglyceryl transferase"
                     /EC_number="2.5.1.145"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008961 -
                     phosphatidylglycerol-prolipoprotein diacylglyceryl
                     transferase activity [Evidence IEA]"
                     /GO_process="GO:0009249 - protein lipoylation [Evidence
                     IEA]"
                     /GO_process="GO:0042158 - lipoprotein biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47576
     Region          16..>222
                     /region_name="Lgt"
                     /note="Prolipoprotein diacylglyceryltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0682"
                     /db_xref="CDD:440446"
ORIGIN      
        1 mnlatwiahd tygnwfrpyw flifcgfait iilswvnfrk rdiptqgfyw gifvitpial
       61 lgasffgkyd vknpiffftl fafwepgmsi hgglifglit gwiwfgfesr khnislwvya
      121 dlivpnilla qaigrwgnff nhellgapia reqlmwlpsf irdnlfkwyv ptpvpnnfhp
      181 teaigingnp vnptdfnnvq yfqpiflyes lanillwfli vialplifry syywrfkkee
      241 pdfmqlswkg vwakwyydik pdpmlvnnls qqvnlkkvyf knkhkmtkkq vikahwkyyg
      301 arlkqiftad vrelekienp hrlkilrcgi ktgmyiagyn liriiletqr ddhdlflknm
      361 rtldyvilsl mivigiilil faqwiavikw rkggwlyekq y
//
LOCUS       WP_004029026             287 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Spiroplasma
            melliferum].
ACCESSION   WP_004029026
VERSION     WP_004029026.1
KEYWORDS    RefSeq.
SOURCE      Spiroplasma melliferum
  ORGANISM  Spiroplasma melliferum
            Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Entomoplasmatales;
            Spiroplasmataceae; Spiroplasma.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Spiroplasma melliferum"
                     /db_xref="taxon:2134"
     Protein         1..287
                     /product="formate/nitrite transporter family protein"
                     /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=31644
     Region          15..282
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msdeikkeek vdnsdsysne dsfvniykya lkkgnspfyk tflmglaagl figfgyiaai
       61 tatkgnwdni piglkslvfg lvftvaitmi vflggemfts nslalivvfk kqlnvgrfvs
      121 nlfivlsgnf lgclvmaglt awggflnhtp dsvtdfynna ailidgkleh twwenfgsai
      181 lcnflvagsi yaahttksai akffvvnlii mafaisgfsh vvansylwfl qpflkifgts
      241 ggwadfgkfa ynvqlptlfg nflsggiflp flyyfiyrkd vkdqlvl
//
LOCUS       WP_004026202             486 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Ureaplasma urealyticum].
ACCESSION   WP_004026202
VERSION     WP_004026202.1
KEYWORDS    RefSeq.
SOURCE      Ureaplasma urealyticum
  ORGANISM  Ureaplasma urealyticum
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Mycoplasmoidaceae; Ureaplasma.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Ureaplasma urealyticum"
                     /db_xref="taxon:2130"
     Protein         1..486
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=55534
     Region          17..478
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mstkdlndai ldlfclvinn ndfwkdvilr leakdfpekv qqnifntian lneqkykise
       61 snilnglgny vivdeqdqny llhknylvqi lertdylvdl kdcieiikna siknkldlfa
      121 neilstqisl tnakdqfkem hekfleilas rtedtienme lianryfekl nkignsgiip
      181 gviktkydni dkftngykpg elvviaarpg igkttfclnv mvnnvneiie ynqniqpnqk
      241 ekiivmfsle itkeqilqkf isiktgisnr evienkyria kgydtrsfam qaineikswp
      301 ifvddrpnis ivdieaklyd lkkrydialv vldylqlvsa gnanknmtrt qevgrvssal
      361 kviakeinap viaiaqlsrk aeerdvssna nmknnplvkt idnspklsdl resgsieqda
      421 dvvaflhwdr kqrnamqndn qetrmrddli eakfiveknr ngstgetdii fsklnskfir
      481 attske
//
LOCUS       WP_004024975             367 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Malacoplasma
            iowae].
ACCESSION   WP_004024975
VERSION     WP_004024975.1
KEYWORDS    RefSeq.
SOURCE      Malacoplasma iowae (Mycoplasma iowae)
  ORGANISM  Malacoplasma iowae
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Mycoplasmoidaceae; Malacoplasma.
REFERENCE   1  (residues 1 to 367)
  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   2  (residues 1 to 367)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Malacoplasma iowae"
                     /db_xref="taxon:2116"
     Protein         1..367
                     /product="aminoglycoside 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=44068
     Region          28..236
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 msinfsnlsk ninfinfski srgnnkelky ivkdsemnry lfkinsiihl dnkvnefrfa
       61 kriehlpfek seivdlcvfn qnryicsiyk widgkiledq iknypsnkqy sfgfkagrsl
      121 klihdlpird eelkqveelp vrkiieyyhq nkrfendnii idfilknnsk ikdekicflh
      181 ghysiknfii knndeislid ynqcyfgdyv qdfskneiyn syyseqfaqg iidgyfynrk
      241 ipdtfwlkya yyaayncitl flwaskqevi stkikikemi qnvlnqfnnf esiipnwykk
      301 nvlskerqkf inspytleki lgtpkkenkn dskikyfdem yddndddlld ekmmdsfkef
      361 lknvakk
//
LOCUS       WP_004023638             701 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Gordonia terrae].
ACCESSION   WP_004023638
VERSION     WP_004023638.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            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="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72222
     Region          1..697
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mtseslssmf rpssvalvga sdkstfsrya yenlvdfgms drtyvvnrrg advhgrrsvt
       61 scqeigervd iallmvpqaa tlaalhdaaa agisnvvvls sgygesgeag qraqreltat
      121 aarlgitllg pnmlgfanfv dravvtaipr lpqkagsval lsqsgassia mmdfarmsga
      181 dlsylvtlgn eamittghvl dylvddeate aiavfietir dpatfaaaar raaaagkpiv
      241 alkagssdla artaqahtga lvgddkvtsa vlrelgvirv nsiedmltta gtaaalgrlp
      301 rsgasavsis ggacdiladr aqdadmefpe fapqtlqkia avmpnygtth nplditgaav
      361 idpslwtsti eavgndpsvg svmvvstipt adtsgsahql rtleaiaagi aksaapgilv
      421 nqvvqeitpy srdlldavgv raaitglsqa vdtvshlqww savvdqvnat cdvdlpepyd
      481 gepragvwse hqartllasa gvnvvpselt ttaadavsaa arlggpvalk ivsaqilhks
      541 dvggvalgve geeavhsayt avraagesva datidgvlvs pmryggtell vgvvrdeqwg
      601 lvlavgfggv lvellgdaal atlpvtqakv tqmlrslrgr rllegvrgap padlealssq
      661 iarianlass lgdelqslev nplrvdgslv ealdaviewr g
//
LOCUS       WP_004034101              75 aa            linear   BCT 20-JAN-2025
DEFINITION  acyl carrier protein [Clostridium sp. MD294].
ACCESSION   WP_004034101
VERSION     WP_004034101.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. MD294
  ORGANISM  Clostridium sp. MD294
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
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   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 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   4  (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 10011594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Clostridium sp. MD294"
                     /db_xref="taxon:97138"
     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=8462
     Region          1..74
                     /region_name="acpP"
                     /note="acyl carrier protein; Provisional; PRK00982"
                     /db_xref="CDD:179197"
ORIGIN      
        1 mevlerikei iaeqtgkdia eitpetsvme dleadsldlf qiindiedef dvkiedteki
       61 ktvadvvkiv eenqq
//
LOCUS       WP_004016901             417 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Mobiluncus
            mulieris].
ACCESSION   WP_004016901
VERSION     WP_004016901.1
KEYWORDS    RefSeq.
SOURCE      Mobiluncus mulieris
  ORGANISM  Mobiluncus mulieris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Mobiluncus.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 417)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Mobiluncus mulieris"
                     /db_xref="taxon:2052"
     Protein         1..417
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=45025
     Region          4..401
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mgmaaqsiav wvwltgatrp vvagrlapsp egrysfvygk syldhplaya lqpglpleer
       61 efiappglem hgvfrdalpd gwgqnvidyq hggqpqslet ymlesgsnrf gnldfqasls
      121 qyvprledtd vqaleadiql llsqrrlsra aglalvhgts iggakpkiat areiiklsts
      181 dtgmsirrea fatllatrmg veaakvrlts lngrdalvvq rfdrdatggr ipvlslltls
      241 geseltaryt syrqlysqlv qhgggvsdga ggvsdtgdfg nsvgekifrr iaanimlgnn
      301 ddharnhavf wdgahmrltp afdiepvrga swdsnqaisf gadgqresrl dvliaasccy
      361 glskadgqhi ieqilaaard aftevfdete lspeltagmf hpsiwenhpl pspatds
//
LOCUS       WP_004044871             394 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Lactobacillus intestinalis].
ACCESSION   WP_004044871
VERSION     WP_004044871.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus intestinalis
  ORGANISM  Lactobacillus intestinalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Lactobacillus intestinalis"
                     /db_xref="taxon:151781"
     Protein         1..394
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43524
     Region          2..392
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkkvlainsg sssfkyklfs lpdeevlaeg ladrvgldds tfsikltdgd khveeveipd
       61 qetavklllk alkkynvied lneiagvghr ivaggeyfkd saiitkdnlq kifdlkeyap
      121 lhnpaegegi kafmkvlpkv pevgvfdtaf hesldpvhyl ysvpydwyek yrarkygahg
      181 tsvryvanrt akllnkdlkd lklvvchlgs gasitavkdg ksydtsmgft plagitmgtr
      241 sgdvdpsllq fvmhkkdisi demidilnhd sgllgisgvs pdmrdlkhnp dkraqlarei
      301 finriiryvg ayitemggad aivftagige hdarvraavm kafefmglvp dleankvnge
      361 ktitkpeski ramivptnee lmierdvvrl ahld
//
LOCUS       WP_004047741             125 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Ligilactobacillus murinus].
ACCESSION   WP_004047741
VERSION     WP_004047741.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus murinus
  ORGANISM  Ligilactobacillus murinus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 125)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 125)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Ligilactobacillus murinus"
                     /db_xref="taxon:1622"
     Protein         1..125
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=13933
     Region          2..124
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(7..10,38..40,43,69,106,120)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mvklytdaat nqthsaagil viadqkqyqf kqkitasnnh qaefeaailg feylsrnfpn
       61 aqnvffhsds kividsldkr ysksfapela klltlhekfp lvidqwipdk qntgahslal
      121 qalka
//
LOCUS       WP_004048922              98 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Ligilactobacillus murinus].
ACCESSION   WP_004048922
VERSION     WP_004048922.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus murinus
  ORGANISM  Ligilactobacillus murinus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 98)
  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   2  (residues 1 to 98)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Ligilactobacillus murinus"
                     /db_xref="taxon:1622"
     Protein         1..98
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10381
     Region          28..97
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 miyvpkqgat tndqtavapa dpqtslsanv sgangskvnl ntatkeqlmq vdgigdkkat
       61 kiieyrqqhg sfkqlselkd isgigdktyq klskslti
//
LOCUS       WP_004049905             252 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Ligilactobacillus
            murinus].
ACCESSION   WP_004049905
VERSION     WP_004049905.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus murinus
  ORGANISM  Ligilactobacillus murinus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Ligilactobacillus murinus"
                     /db_xref="taxon:1622"
     Protein         1..252
                     /product="formate/nitrite transporter family protein"
                     /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=26695
     Region          9..252
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 myteqikavq gaaskklafl hqnplgyfll smlagmyigf gillaftvsg qlqgapttkl
       61 lmgtvfgval slviiagsel ftgnnfilav galtkqntwl qasylwvicw lgnacgaill
      121 ailynatglq vdgvakalta tavvkttvgp lsllmrgilc nilvclalws sfqtkndaak
      181 limvfwclla ffttgfehsv anmtlltaal ikpagavltv gawlynlfwv slgnmlgaic
      241 flavpyviaa kk
//
LOCUS       WP_004050581             398 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Ligilactobacillus murinus].
ACCESSION   WP_004050581
VERSION     WP_004050581.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus murinus
  ORGANISM  Ligilactobacillus murinus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Ligilactobacillus murinus"
                     /db_xref="taxon:1622"
     Protein         1..398
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43885
     Region          3..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mekimiinsg ssslkfklfn nethetlasg iierigihgs kikvkygagq kyeldheitn
       61 hlqgiellln vlkelnliad lseikgighr vvaggeyfsq pvivdndvia kikelaqlap
      121 lhnpanlngi kafrkylpns lsvavfdtaf hqtlpqenym ystpyewyek ygvrrygahg
      181 isheyvarka aelmgrpfed lklitchlga gasitaikyg rsfdtsmgft plsgiqmatr
      241 agdvdislan yimkkldiqs msdmvyllne ksgflgvsgv sadmrdveda aatgnerakl
      301 aiklfynsil ryvgqyiaem ggvdgivftg gigenspets eaimkrlaym gvtinetenk
      361 krgaqtiisg pdstvtvmri ptdeeymiaq hvwrllen
//
LOCUS       WP_004051092             370 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Ligilactobacillus murinus].
ACCESSION   WP_004051092
VERSION     WP_004051092.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus murinus
  ORGANISM  Ligilactobacillus murinus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Ligilactobacillus murinus"
                     /db_xref="taxon:1622"
     Protein         1..370
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41997
     Region          1..249
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          259..342
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkflhtadwh igkrlheypl vkeqhdalaq iaqiaqkeqv davvvagdly drslpseeav
       61 tlvnqalrdl nltadlpllv isgnhdsavr latgqewfkq tklylhtrls eaftpiefed
      121 tqffllpyfe lqearnyfad esisdltsam klvvaklktk fdpakkqvlv ahffaagslr
      181 sdsetkievg gldsvptklf sdfdhvalgh lhdkraldlp tikysgsllk ysvaeansqk
      241 gvwivetepf sckwislapl ndiccleasy aelttklyqt vaqddyvaie ltdeheiidv
      301 mnklrkyypr ivelkrkkrl vhtkqaekie sksplelftd ffvqatgrkp tqlqqkwake
      361 sllelekege
//
LOCUS       WP_004038778             804 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Clostridium sp. MD294].
ACCESSION   WP_004038778
VERSION     WP_004038778.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. MD294
  ORGANISM  Clostridium sp. MD294
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 804)
  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 804)
  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 804)
  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   4  (residues 1 to 804)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..804
                     /organism="Clostridium sp. MD294"
                     /db_xref="taxon:97138"
     Protein         1..804
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=90849
     Region          25..>75
                     /region_name="clpX"
                     /note="ATP-dependent Clp protease ATP-binding subunit
                     ClpX; PRK05342"
                     /db_xref="CDD:235422"
     Region          69..804
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mpqtkelnyk qlknicspsd fsfqtteeis sldggvigqe ravkafdfgl tvkmqgynif
       61 mtgpsgtgkt tyakistkki aatepvpydw cyvyhfqnpr tplalrfkag mgkqfkedms
      121 elvqifktei qkvfrsedye keksvilkkf dekkdiymke msdmakengf qlrssnsgiy
      181 fmpiidgkti neeeydklee eqqeaidkas nvvqekagti mrdlreleke ckkqtddldy
      241 kvgmfaighh vnsvqekyke ytrvisyind vkedvlenis qffeeeeevd esiasllplf
      301 skksseditq kykvnlivdh setegapvvv hfnptyynlv geveydsefg nlttdfmkik
      361 aglfhkangg ylilqaqdil snpqsweair rviktkeiam dnlreqmgai vapvlkpepv
      421 padfkiilig seyyydvlse fddefdkffk ikaefdyemk rndenivkla qfikkfseke
      481 htahftadav cavieyssrt aerqdklstr fnrltevmge aaawaklsgd tlitakhikk
      541 aieqkeqrlk myeeklgeml dekvimidte gskigqingl avldmgsyaf gnpcritatt
      601 ymgesgiini ekeaqlsgqt hdkgiqiltg flgqtyaqef plslscrvcf eqnyngidgd
      661 sasstelyci lsslaevpir qdlavtgsin qrgeiqaigg vtykiegffd lckkrgltgt
      721 qgviipetni kdlvlkdevi eavkqgafhi yaistleegi allmdmeagq knkngkypan
      781 svhgkvmkkl kayykgasge kiek
//
LOCUS       WP_004056513             134 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein
            [Hominisplanchenecus murintestinalis].
ACCESSION   WP_004056513
VERSION     WP_004056513.1
KEYWORDS    RefSeq.
SOURCE      Hominisplanchenecus murintestinalis
  ORGANISM  Hominisplanchenecus murintestinalis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Hominisplanchenecus.
REFERENCE   1  (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   2  (residues 1 to 134)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 134)
  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 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   5  (residues 1 to 134)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Hominisplanchenecus murintestinalis"
                     /db_xref="taxon:2941517"
     Protein         1..134
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14672
     Region          41..130
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(60,79..80,98,101,109..110,122,127)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mlmfndteek avekaiaala dmipleamqp phspaltfpg leirlhqrrv lkdgsdiplt
       61 rleygtlcyl aaspgrvftk aqifeavwsm esescqsnva nvicnlrkki epdsgkptyi
      121 ktvlgvgykf asge
//
LOCUS       WP_004069740             124 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Schaedlerella
            arabinosiphila].
ACCESSION   WP_004069740
VERSION     WP_004069740.1
KEYWORDS    RefSeq.
SOURCE      Schaedlerella arabinosiphila
  ORGANISM  Schaedlerella arabinosiphila
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Schaedlerella.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Schaedlerella arabinosiphila"
                     /db_xref="taxon:2044587"
     Protein         1..124
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14171
     Region          44..121
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mlttvdsfvs hnednlwdfe vvsdvkyenv nrvhplkqrd valliqdvkn dphitgiivf
       61 gsavrfdchs msdldvlivr ddqqiridas lsniqseldl ifhsklgerl kkeiqrtgvv
      121 vfrr
//
LOCUS       WP_004071219             706 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Schaedlerella arabinosiphila].
ACCESSION   WP_004071219
VERSION     WP_004071219.1
KEYWORDS    RefSeq.
SOURCE      Schaedlerella arabinosiphila
  ORGANISM  Schaedlerella arabinosiphila
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Schaedlerella.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 706)
  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   3  (residues 1 to 706)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Schaedlerella arabinosiphila"
                     /db_xref="taxon:2044587"
     Protein         1..706
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=77081
     Region          1..705
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          177..260
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 mdnmlemyly etntlmeqld ellieaekns dfttndvnei frimhtikgs sammefstlm
       61 eiahhiedlf fyirengmds ldeshkndlf nlmfqstdal rgevekiend eplstnidsi
      121 iksinsflek isssgekssa ddsaeaasap aappadkeai aainqelagc pdsklpyfik
      181 ihfeegsgme nlrafmiita lkeidipfey ypsdvetnsd taesiidngf fvalssqedv
      241 dsavgilkeq nsiqayevie nvhakaeapk qeapapaaqk sadaapapvp aeaaqkgspa
      301 paaasthsap vkqslisvnl skldslvavv geivitesmv tsspdlqnlk ldnfmksarq
      361 lrkltddlqd iamslrmvpv sgtfqkmnrv vrdmkkklnk dvrltlvgen tevdktivds
      421 isdpimhivr nsvdhgieet reeriaagkd pqgevilaas htgseviiti tddgrgmdte
      481 kilakaerng iltkpaseys kkeilsllml pgfstneevt efsgrgvgmd vvkknvesvg
      541 gtisissefg qgsvttlkip ltmaitdgme isvgkslfti pianirqslk iqrdevilda
      601 ggneivkclg efypiirvhe lynietektn iedgiliwve sadksfclfv dellgeqqvv
      661 vkplpsylns fniknsgigg ctllgdgnis lildignlya ayhtqy
//
LOCUS       WP_004071813             640 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Desulfobacter postgatei].
ACCESSION   WP_004071813
VERSION     WP_004071813.1
KEYWORDS    RefSeq.
SOURCE      Desulfobacter postgatei
  ORGANISM  Desulfobacter postgatei
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfobacteraceae; Desulfobacter.
REFERENCE   1  (residues 1 to 640)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Desulfobacter postgatei"
                     /db_xref="taxon:2293"
     Protein         1..640
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=72976
     Region          54..572
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mekmdgktmd ivaenvgklk elfpeafteg kvdfdalkev lgtfvddrde rysftwngks
       61 karmiaqtps tgtlrpckee svdwdttqni fiegdnlevl kllqksyhkk mkmiyidppy
      121 ntgkdfvykd nfkdniknyk eitgqvdgeg rnlsnnpets gryhtdwlnm myprlklarn
      181 llkddgvifi siddseasnl ikicdevfge enfiadliwq kkfsrandas yfstmhdhil
      241 cyakrtklnn ngdswelkll prgdeipdgy tnpdddhrgp wtsvvlsaks gtekliyeit
      301 tpsgrkclpp dgrfwgvnrd rfselvednr iwfgkdgsgi prlktflsev qdglrpntiw
      361 fhqevghnqe grqevkklfd dkgyfdgpkp vrlldriiqi snlsssdivl dffagsattg
      421 havvnhnacn etsfkyilvq lpevcdekse afkagyktia eiskerirra gakikeenpe
      481 yegdlgfkvf kldatnikpw evdfdltert ledyisnikt drreedvlye vllkygldlt
      541 lpidewimdn gklimkdehh sqlstvnsql vysigmgali iclsdaisle vvegiaelkd
      601 elnpeimrvv fkdsgfkddv vktnavqilk qagivdvrsl
//
LOCUS       WP_004073144             693 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Desulfobacter postgatei].
ACCESSION   WP_004073144
VERSION     WP_004073144.1
KEYWORDS    RefSeq.
SOURCE      Desulfobacter postgatei
  ORGANISM  Desulfobacter postgatei
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfobacteraceae; Desulfobacter.
REFERENCE   1  (residues 1 to 693)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 693)
  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   3  (residues 1 to 693)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..693
                     /organism="Desulfobacter postgatei"
                     /db_xref="taxon:2293"
     Protein         1..693
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76973
     Region          176..693
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msyeniiatt erlaselils dpaqpdsikt llpilksiha qckaqnllse aaqilkvrhi
       61 vdaiikdgpr vksnllsnle mvvtdfstkl knmgekesnt lfvrkrfqsd dqpqngeyne
      121 lerklnelsm liaglcpgkd peikeiignv edlidisani kpstfydisk rckqymenll
      181 dsarsgdfii nhsatdaile svdllkhlid svkqglvsgy rqeddhidvd ilrdklkniq
      241 ifltkgekep lgeilvrknn lkkhdidqal eiqkrhpekk igeiliedkk iasaqvasal
      301 meqsavkkrv dsqvkvstqk lddlvdyage lviaqsmlrq qtmknsalsq tvgqlgqivn
      361 nmqniaismr mipikatfmk mirlvrdlsr ksgkqinlsm tgeeteidrn mvdalyepmv
      421 hmirnacdhg iesiqertan nkppqgnidl rayhkggniv ieieddgkgl drakilkkat
      481 atglitgdeq mtdaqvfsli lspgfstarq itdisgrgvg mdvvkagiek frghlniese
      541 kgvgsrfiit lpltlaiidg mlvrvddery viptiaiqka frpgpgeyft vegkgqmikd
      601 rgrlvplirl neifktsndv ksveqslvvv veskeerraf lidellgkde yviknlggnm
      661 ddirgiagga iladgkvgli ldvhgifsiv skk
//
LOCUS       WP_004073331             447 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Desulfobacter postgatei].
ACCESSION   WP_004073331
VERSION     WP_004073331.1
KEYWORDS    RefSeq.
SOURCE      Desulfobacter postgatei
  ORGANISM  Desulfobacter postgatei
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfobacteraceae; Desulfobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Desulfobacter postgatei"
                     /db_xref="taxon:2293"
     Protein         1..447
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=49301
     Region          74..201
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mnielsdnfy fskgsalvsv ivlvlvmill tmpscqvaqa syshpglvrf qsriidyrsr
       61 inprfkkkvr trtrliivht selelestlr vvsrgkrfkn grttpgghan yviarngrvy
      121 rildkkyrad haglsmwdgr sdvsdisvgi efvgyhdapl ttsqytsaem lllilkrayg
      181 lqdkdilths qiaygrpnpw fsnnhrgrkr caknfdrtra glgptwpfdp dvragrltpd
      241 pmlaqvfyst skavvhkgnt afqvlksdvi skqnsawaia gedynasstv yvlpggntla
      301 gdrvasslgw drlpvgtkvl lnqqtaqvrq eakdiikiis gpmtarchag eayhaastiy
      361 flpsdrilrg caisnwddlp sgtrlvvgyk gpfiitkdkt aygiagakfk dpgtvyhipg
      421 rgpvqgnrip dfkdlpkgtg vylptag
//
LOCUS       WP_004073370             308 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Desulfobacter postgatei].
ACCESSION   WP_004073370
VERSION     WP_004073370.1
KEYWORDS    RefSeq.
SOURCE      Desulfobacter postgatei
  ORGANISM  Desulfobacter postgatei
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfobacteraceae; Desulfobacter.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Desulfobacter postgatei"
                     /db_xref="taxon:2293"
     Protein         1..308
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33269
     Region          6..280
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mahifadlhn httasdgdfs pgdlvalaag mgikvlgvtd hdtldgleaa ldagkiqgve
       61 vfpgveisvr fkrafftgtl hvltyfssam lkdsgfvtrf ktllaggrge rlvrarieki
      121 nevfgpgges pllsrdltfe eiaaysdnvs rrhfamalae rlgisdkdti triignnspa
      181 ylpsgvdleq vkgfiksepv vavlahpaag sfpgeghyke vlppleivtr llsevldagv
      241 kglevhypgh spehqvllls waekydllvt ggsdchdsak rplgtagvne qefkrlrqmv
      301 lceekknr
//
LOCUS       WP_004074683             735 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Desulfobacter postgatei].
ACCESSION   WP_004074683
VERSION     WP_004074683.1
KEYWORDS    RefSeq.
SOURCE      Desulfobacter postgatei
  ORGANISM  Desulfobacter postgatei
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfobacteraceae; Desulfobacter.
REFERENCE   1  (residues 1 to 735)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 735)
  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   3  (residues 1 to 735)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..735
                     /organism="Desulfobacter postgatei"
                     /db_xref="taxon:2293"
     Protein         1..735
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=81397
     Region          148..731
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mtyetiistd eyselsvkln elsiliagfc pgeipdlglm lnnlddlini akgidpatfy
       61 diskrcknyv ekmilknldd tkpveegval lksilcylkk gepftfdyad vlemleenls
      121 gdvkeqtaqv ekkdandniq napekisddd meiltdfise aqenldtiev slielehdpv
      181 ntdiindifr pfhtikgvag flsltkintl ahatenllds arsgdfiinh tvtdiilasv
      241 dtlkalldkv kqgiqtgyre sdddidvdsl rsrlkqlqis ltkgekeplg eilvrkkels
      301 qsdldqalei qnkhsvkklg eilveekkvk pkqvasalme qsclkkkidv qvrvstqkld
      361 dlvdyagelv iaqsmlrqqt kedaivsktv sqlgqivnhm qniamsmrmi piqatfmkmi
      421 rlvrdlsrks gkeihlsmtg edteidrnvv dalyepmvhm irnacdhgie atsersktgk
      481 paqgnihlca yhkggniiie ieddgkgldk dkilekakst glikgdeqmt dtqvfdlimq
      541 pgfstakeit disgrgvgmd vvkdgiekfr ghlniaskkg kgtkfiislp ltlaiidgml
      601 igvddqryvi ptiaiqkafk prqgeyftvk gkgemvkdrg nliplirlne iygtsnnkks
      661 idvclvvvve skeekkaili dellgkdeyv ikslgnsmnd iqgiaggail adgkvglild
      721 vdgifsivaq rplei
//
LOCUS       WP_004074913              99 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Desulfobacter postgatei].
ACCESSION   WP_004074913
VERSION     WP_004074913.1
KEYWORDS    RefSeq.
SOURCE      Desulfobacter postgatei
  ORGANISM  Desulfobacter postgatei
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfobacteraceae; Desulfobacter.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Desulfobacter postgatei"
                     /db_xref="taxon:2293"
     Protein         1..99
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11140
     Region          8..98
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mpqidrnlik rieahkdiik ekffvesmsi fgsiskgtak sdsdidilir fkttpglfgf
       61 idlkqylevi vgrpvdlvte nalkkqlrdd ilrdavhva
//
LOCUS       WP_004074931              99 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Desulfobacter postgatei].
ACCESSION   WP_004074931
VERSION     WP_004074931.1
KEYWORDS    RefSeq.
SOURCE      Desulfobacter postgatei
  ORGANISM  Desulfobacter postgatei
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfobacteraceae; Desulfobacter.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Desulfobacter postgatei"
                     /db_xref="taxon:2293"
     Protein         1..99
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11010
     Region          6..98
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mtqidhniik tieahkdiik ekfsvesmsi fgsiskgtak sdsdidilir ykttpglfgf
       61 idlkqylevi vgrpvdlvte nalkkqlrda ilrdavhvv
//
LOCUS       WP_004080064             368 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Thermotoga].
ACCESSION   WP_004080064
VERSION     WP_004080064.1
KEYWORDS    RefSeq.
SOURCE      Thermotoga
  ORGANISM  Thermotoga
            Bacteria; Thermotogati; Thermotogota; Thermotogae; Thermotogales;
            Thermotogaceae.
REFERENCE   1  (residues 1 to 368)
  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 368)
  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
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 368)
  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   5  (residues 1 to 368)
  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   6  (residues 1 to 368)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 368)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 368)
  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 11513089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Thermotoga"
                     /db_xref="taxon:2335"
     Protein         1..368
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40756
     Region          3..>61
                     /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(3..4,8..10,23..25,34..37,39..40,43..44,46..47,
                     53..55,60..61)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Region          75..363
                     /region_name="ASKHA_NBD_ROK_TM1224-like"
                     /note="nucleotide-binding domain (NBD) of Thermotoga
                     maritima N-acetylglucosamine kinase (TM1224) and similar
                     proteins; cd24059"
                     /db_xref="CDD:466909"
ORIGIN      
        1 mpksvraeni srilkrimks pvsrvelaee lgltkttvge iakiflekgi vveekdspkg
       61 vgrptkslki spncayvlgi evtrdeiaac lidasmnila heahplpsqs dreetlnvmy
      121 riidrakdmm eklgsklsal tvaapgpidt ergiiidprn fplsqiplan llkekygiev
      181 wvendadmga vgekwytkrd dsfawiltgk gigagiiidg elyrgengya geigytrvfn
      241 gneyvfledv cnenvvlkhv lsmgfsslae ardsgdvrvk eyfddiaryf sigllnlihl
      301 fgiskivigg ffkelgenfl kkikieveth llykhsvdms fskvqepvia fgaavhalen
      361 ylervtts
//
LOCUS       WP_004081150             132 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Thermotoga maritima].
ACCESSION   WP_004081150
VERSION     WP_004081150.1
KEYWORDS    RefSeq.
SOURCE      Thermotoga maritima
  ORGANISM  Thermotoga maritima
            Bacteria; Thermotogati; Thermotogota; Thermotogae; Thermotogales;
            Thermotogaceae; Thermotoga.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Thermotoga maritima"
                     /db_xref="taxon:2336"
     Protein         1..132
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15133
     Region          25..119
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 myeeyirawv erkkkeeekm kllahkalee arkvtgvlre kygakrvvlf gslakylrga
       61 geftersdid laveglpkee yfrvlseinr lsefevdlid legcpaflrs lieregmeie
      121 egtdsltdsg dr
//
LOCUS       WP_004082202             382 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase family protein [Thermotoga].
ACCESSION   WP_004082202
VERSION     WP_004082202.1
KEYWORDS    RefSeq.
SOURCE      Thermotoga
  ORGANISM  Thermotoga
            Bacteria; Thermotogati; Thermotogota; Thermotogae; Thermotogales;
            Thermotogaceae.
REFERENCE   1  (residues 1 to 382)
  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 18888537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Thermotoga"
                     /db_xref="taxon:2335"
     Protein         1..382
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=43480
     Region          199..241
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
     Region          253..370
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mlfqtlladh llelksvsed hvtlsvkkly egeittflly spagfvfpek vknsdytfev
       61 dfegpffpiv egvnsfgkrm yrvapqvlrv plekpetrvi sdikngevlv yvfiqspegv
      121 vpvslnlegk rfrffnlegk wicvfksfle dgaheleitf ngpygytfsl kkeiyvikrv
      181 avpmrgedga fdytvfaehv vkrgetlwsi anqygvrvgd ivlinrledp drivagqvlk
      241 igrvyfrenp vtivvnlfss klalyydgvl lkvypvalgr sdatppgryw vlrkeidpal
      301 ywfgeyispr tplnglgtry lqlsdptyai hgtskpweig krishgcirm fnrdveeida
      361 fagvgtevvv vkedkefper iy
//
LOCUS       WP_004082420             794 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: Lon protease family protein [Thermotoga].
ACCESSION   WP_004082420
VERSION     WP_004082420.1
KEYWORDS    RefSeq.
SOURCE      Thermotoga
  ORGANISM  Thermotoga
            Bacteria; Thermotogati; Thermotogota; Thermotogae; Thermotogales;
            Thermotogaceae.
REFERENCE   1  (residues 1 to 794)
  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 794)
  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 794)
  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   4  (residues 1 to 794)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..794
                     /organism="Thermotoga"
                     /db_xref="taxon:2335"
     Protein         1..794
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=90133
     Region          1..780
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mirklrpdei nsfdldflnf qtteevppne gfigqkrake aietgirire kgynifvtgm
       61 tgtgrrtfvq mmlqdvakkl pvpndwgyvy nfenpyepka isfkagqgrr fkkrledlin
      121 evvealnksf eseefarkis emeekyalmr kqlwesleak aselgfvvql tpagvvmlpv
      181 vdgkplppea vnalpdqair eieerqmklk hlvdgtlyri rkldiefrks leefhkrtal
      241 faidplfvev esefenegvk eflesvkkdi venlldflrm darerkeiym rkyslnlivd
      301 nsdltgapvi yetnptysnl fgkieyyvrg gflhtdfsmi rpgsvhkang gfliveaerl
      361 lsqpyawynl krvlmesqis venlehtlgv sstitlkpek ipldlkvvii gtpylyelly
      421 eldpdfrklf rikaefdwei prnelnvqky vsfissvcre knlphfdrga vkrviwyamr
      481 nagnstklsa vfgdivnliv esgelarleg sevttsdhvl kayqamenrr nlleekydem
      541 iktfdlmiev tgskvgqing ltvldlgdhs fgvpvkitak vylgrpgvvd iqreadlsgk
      601 ihskavlile gflgsryaqd fplsvsasis feqvyseveg dsaslaeala llsaiskvpi
      661 kqgiavtgsi nqhgevqpvg givekvegfy racktrgfdg eqgviipkan aknlvlkdei
      721 iqamkkglfh iwtvetidda ieivmgmkag rvtktgkfer nsvnylvyre lkkmkklldg
      781 vpeerkkkkr kgkk
//
LOCUS       WP_004083151             139 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Schaedlerella
            arabinosiphila].
ACCESSION   WP_004083151
VERSION     WP_004083151.1
KEYWORDS    RefSeq.
SOURCE      Schaedlerella arabinosiphila
  ORGANISM  Schaedlerella arabinosiphila
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Schaedlerella.
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   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
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   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Schaedlerella arabinosiphila"
                     /db_xref="taxon:2044587"
     Protein         1..139
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16305
     Region          45..134
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(64,83..84,102,105,113..114,126,131)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mdlllirlek idndfyesli kfisdhgysp kvvvrntdil sfhgleiiss khqvllhdke
       61 ikmtkkefyi lellarnkgq vftkdqiydq vwgesyfsds kniiayinki rkkiepdpah
      121 piyiltvwgi gykfnekie
//
LOCUS       WP_004085424             634 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Xylella fastidiosa].
ACCESSION   WP_004085424
VERSION     WP_004085424.1
KEYWORDS    RefSeq.
SOURCE      Xylella fastidiosa
  ORGANISM  Xylella fastidiosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xylella.
REFERENCE   1  (residues 1 to 634)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 634)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 634)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 634)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 634)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 634)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Xylella fastidiosa"
                     /db_xref="taxon:2371"
     Protein         1..634
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=69456
     Region          1..634
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mstsshsgdc aavssnsnst iilsaigvvf gdigtsplyt lkeafspnyg lapnhdtvlg
       61 ilslifwamm lvvtikyviv imrvdndgeg gimaltaltq rtmpfgsrsi yivgilgifg
      121 tslffgdgii tpaisvlsav eglevaephm kafvvpitla vlillflcqr fgtervgktf
      181 gpitflwfia igvvgvynil qapevlyain pwwglhffle hgwhsmfvlg avvlavtgge
      241 alyadmghfg akairhawmy vvlpmlalny lgqgalvlsn ptaignpfyq sipdwglypm
      301 ialataaavi asqalitgsy slssqamqlg yiprmnvrht sqstigqiyv ptvnwtlltl
      361 viltvigfgd stsmasaygv avtgtmmitt vlmiiyaran prvprlmlwm iaivfiavdg
      421 affyaniikf mdgawfplll gvviftfmrt wlrgrkllhe emrkdginld nflpglmlap
      481 pvkvpgtavf ltadstvvph almhnlkhnk vlhernvflt vktlkipyaa nserlkiepi
      541 sngfyrvhir fgfmetpdvp lalmcskdha eidfdpmhtt ffvsretvip sanrgmpiwr
      601 dklfvlmhrn aapanaffri pgnrlvelga qvei
//
LOCUS       WP_004089779             212 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Xylella fastidiosa].
ACCESSION   WP_004089779
VERSION     WP_004089779.1
KEYWORDS    RefSeq.
SOURCE      Xylella fastidiosa
  ORGANISM  Xylella fastidiosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xylella.
REFERENCE   1  (residues 1 to 212)
  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 212)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 212)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Xylella fastidiosa"
                     /db_xref="taxon:2371"
     Protein         1..212
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22767
     Region          7..200
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 maigdlhdeq ehgerirswl rkngvgllcg vllgfvfiaa wqwreakqvd qftsaaqqfa
       61 vfgkllqake lgnaaqalak lngapsglya elgalqlaka qseagntaea ikilrtlpvd
      121 sqfkliadqr larllvatgk adeankllat rnddvsfeiq gdallvlgkr eqareryaka
      181 lamgdsaapq rrileiklmd vggtlptpvg pi
//
LOCUS       WP_004090242             313 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Escherichia coli].
ACCESSION   WP_004090242
VERSION     WP_004090242.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (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   2  (residues 1 to 313)
  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 313)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..313
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34761
     Region          17..70
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mstkltgyvw dgcaasgmkl ssvaimarla dfsndegvcw psietiarqi gagmstvrta
       61 iarleaegwl trkarrqgnr nasnvyqlnv aklqaaafsq lsdsdpsksd asksdpskfd
      121 asksgkkagf hpsesggdps vkskhdpsdk ktsrpdasqp dtqtaeqefl trhpdavvfs
      181 pkkrqwgtqd dltcaqclwk kiialyeqaa ecdgevvrpk epnwtawane irlmcvqdgr
      241 thkqicemys rvsrdpfwcr nvlspsklre kwdelslrls psvstytekr edpyfkasyd
      301 nvdysqipag frg
//
LOCUS       WP_004090636             348 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Xylella
            fastidiosa].
ACCESSION   WP_004090636
VERSION     WP_004090636.1
KEYWORDS    RefSeq.
SOURCE      Xylella fastidiosa
  ORGANISM  Xylella fastidiosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xylella.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Xylella fastidiosa"
                     /db_xref="taxon:2371"
     Protein         1..348
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38640
     Region          1..344
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mgiriqelrk qfedftalag idldirqgel lallgpsgsg kttllriiag lehadagrvl
       61 fgdedattms vqarrvgfvf qhyalfkhms vyenvafglr vrrgkarwpe sqisarvfel
      121 lslvqldgle qrypmklsgg qrqrvalara laieprvlll depfgaldaq vrrdlrrwlr
      181 eihdrtgltt vfvthdqeea leladrvail nqggieqvas pdevynrpss pfvysfvgav
      241 nrlpgcvgad glevagivls cppqlsgwga vdlyvrpedl vldaqegwsa ivlwsqrsgp
      301 rmrvrarleh saheveiels satdeyvegq klrliprhyg vffsesgs
//
LOCUS       WP_004093365             411 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Acetonema longum].
ACCESSION   WP_004093365
VERSION     WP_004093365.1
KEYWORDS    RefSeq.
SOURCE      Acetonema longum
  ORGANISM  Acetonema longum
            Bacteria; Bacillati; Bacillota; Negativicutes; Acetonemataceae;
            Acetonema.
REFERENCE   1  (residues 1 to 411)
  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 411)
  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
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 411)
  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   5  (residues 1 to 411)
  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   6  (residues 1 to 411)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 411)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 411)
  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 20283051
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Acetonema longum"
                     /db_xref="taxon:2374"
     Protein         1..411
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44278
     Region          21..>60
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          117..393
                     /region_name="ASKHA_ATPase_ROK_BsXylR-like"
                     /note="ATPase-like domain of Bacillus subtilis xylose
                     repressor (XylR) and similar proteins; cd24076"
                     /db_xref="CDD:466926"
ORIGIN      
        1 mqeftpvspr ptgpgineap vidiirrhgp vsradiaklt gltpptvtni agklldsgli
       61 keyrmgessg grpplllkin sgisqviimn irsevimgya idpelqvhfe vtnsikgmke
      121 aavldlmlqm idqcrkaata pvaaigvvvr gpvrlregiv vfalnigwkn lplktileek
      181 fqlpafiend akvltmgeyh ygsmkdtanm illkvshgig agimingrly rgmngsagev
      241 ghttvdvagp lcrcgnygcl ealasedalv elvvkamkeg qpscvddlad gdpdrvtvdt
      301 vyqaadmgds lalqmldrva rylgigianl vnifnpeliv isgciakaqs hiedtlnriv
      361 rerafescss ilkihfsert tentlkgaad mvfteitkta wlvqgktasr l
//
LOCUS       WP_004093507             186 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Acetonema longum].
ACCESSION   WP_004093507
VERSION     WP_004093507.1
KEYWORDS    RefSeq.
SOURCE      Acetonema longum
  ORGANISM  Acetonema longum
            Bacteria; Bacillati; Bacillota; Negativicutes; Acetonemataceae;
            Acetonema.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Acetonema longum"
                     /db_xref="taxon:2374"
     Protein         1..186
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=20238
     Region          2..141
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mgltvvtfte sfisplmpdl ilvplcladp anaiyyaala ttasvaggfi gygigmwlgp
       61 gvlsrfpaar tamekveays trevawvifl avmsplpykv isitagalrv nfpmfilisf
      121 agrakrfmie gvliyyfgsa aielireysl attavivgis liwsavwwrr rvkkhellat
      181 kqglkp
//
LOCUS       WP_004094587             191 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Acetonema longum].
ACCESSION   WP_004094587
VERSION     WP_004094587.1
KEYWORDS    RefSeq.
SOURCE      Acetonema longum
  ORGANISM  Acetonema longum
            Bacteria; Bacillati; Bacillota; Negativicutes; Acetonemataceae;
            Acetonema.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Acetonema longum"
                     /db_xref="taxon:2374"
     Protein         1..191
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20853
     Region          3..189
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mkpkriivai tgasgailgi rileelrrle vethlvlsqw aertirmetd ytveqvrsla
       61 gvchpvddla asissgsfht dgmviapcsm ktlaaiacgf synlisraad vaikekrrlv
      121 lvpretplss ihlqnmlals nngvvllppc vgfytrpdtv eaivnhltgk ildvlgfehq
      181 lfprwtgtpe k
//
LOCUS       WP_004096226             311 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Hafnia].
ACCESSION   WP_004096226
VERSION     WP_004096226.1
KEYWORDS    RefSeq.
SOURCE      Hafnia
  ORGANISM  Hafnia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Hafniaceae.
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
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Hafnia"
                     /db_xref="taxon:568"
     Protein         1..311
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=34566
     Region          1..310
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mihfkhvnks fagrpavedl slhiaegeft vligtsgsgk sttlkminrl idhdsgeltf
       61 agqnissfep ealrrrmgya iqsiglfphw tveqniatvp qllkwptari rervtelmem
      121 lsldvaefrh ryphqlsggq qqrvgvaral aadpevllmd epfgaldpvt rttlqqeiar
      181 ihtllgrtiv lvthdideal sladrivlmd agkviqqgtp qellnhpvne fvrqffghsd
      241 vgikllgldv vasrvrrgel slgepircdl nlrdamslfi yrqvdrlpvi deagqpvgvl
      301 yfsdlvkkae a
//
LOCUS       WP_004097128             259 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Acetonema longum].
ACCESSION   WP_004097128
VERSION     WP_004097128.1
KEYWORDS    RefSeq.
SOURCE      Acetonema longum
  ORGANISM  Acetonema longum
            Bacteria; Bacillati; Bacillota; Negativicutes; Acetonemataceae;
            Acetonema.
REFERENCE   1  (residues 1 to 259)
  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 259)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Acetonema longum"
                     /db_xref="taxon:2374"
     Protein         1..259
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29008
     Region          1..257
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mkksvcieti fteaplaerf alvkeagfdy vefwtwkdkd ittikelclq yslkvasfsg
       61 dqdyslinpd esekyisfvk esiktaqyln cknlvihsna lgeggvvlng ypeipdskkf
      121 atifkvlkdl apiaerekvt lvlealnskl dhagnflnnt idpasliklv nspyikvlyd
      181 vyhmqimegn iidtlkryld vigyihiadv pgrhepgtge inyvnvmdal kalkydkvag
      241 yelfplkssk eainaiksl
//
LOCUS       WP_004098011             274 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Klebsiella].
ACCESSION   WP_004098011
VERSION     WP_004098011.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 274)
  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 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   3  (residues 1 to 274)
  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   4  (residues 1 to 274)
  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 274)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..274
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31623
     Region          16..274
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <158..270
                     /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 mqgvpeqfsd erdsarfrhl aqlpgvelyh ahisryafep htheafgiga ielgaerfry
       61 rgsqhvasvn sivtmnpdel htgeaetadg wryrmiyldp dtleevtgvr hwwfsevvrq
      121 dplrsrqign liyglwhtdd plaqqgllld lidtfrpfah haaalpearh rfervrdylh
      181 dnymrtvtld elaqvaalsp yhfqrqfkah fhvtphqmlm airlwrakaf lthgmpaadv
      241 alaagltdqs hltraftrry gitpvryqkq vlpr
//
LOCUS       WP_004098440             193 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Acetonema longum].
ACCESSION   WP_004098440
VERSION     WP_004098440.1
KEYWORDS    RefSeq.
SOURCE      Acetonema longum
  ORGANISM  Acetonema longum
            Bacteria; Bacillati; Bacillota; Negativicutes; Acetonemataceae;
            Acetonema.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Acetonema longum"
                     /db_xref="taxon:2374"
     Protein         1..193
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21200
     Region          4..188
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mndilenilt rrsirafkkd qipeedlnti lvagsyapng mglqdwkfta iqnattlkkv
       61 neairqtlls ipivpeihpy vmsliekakd enadflyhap tfiivsnlkd ngnsmpdsal
      121 aignmmlaah sigigscwln qlpglthlpl irelltdldv pehhivygsv vmgyaagesk
      181 paaprknvih iir
//
LOCUS       WP_004099584             103 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Klebsiella].
ACCESSION   WP_004099584
VERSION     WP_004099584.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..103
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11250
     Region          5..101
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(7..8,26..27,35,38,40..41,43,46..47,49,57,62,69)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(26,57..58,60,84)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mdshdtfpqr vwqivasipe gcvatygdva qlagspraar qvggvlkrlp egstlpwhrv
       61 vnrhgdislt gpdlqrqrqa llaegvqvsg sghidlqhyr wiy
//
LOCUS       WP_004071745             404 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Desulfobacter
            postgatei].
ACCESSION   WP_004071745
VERSION     WP_004071745.1
KEYWORDS    RefSeq.
SOURCE      Desulfobacter postgatei
  ORGANISM  Desulfobacter postgatei
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfobacteraceae; Desulfobacter.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 404)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Desulfobacter postgatei"
                     /db_xref="taxon:2293"
     Protein         1..404
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44592
     Region          27..397
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mlklnavlsl pggghllcge iftttpdarg riqgsfrytk eylstpdafp ldpvhlplgt
       61 aeieadrpqg vhgvfedalp ddwgrallsa kyhipraeqt vpnllkflgt sglgalsfys
      121 gkenayvdps aaihnlsgiv eaalnfdagl pvdgndlkal ficgsspgga rpkaliktnd
      181 grqwiakfpk lndryhveai eagtlcladn aglnvpnffi qkagkrsvll verfdmtasl
      241 grnhmismqt lldadgyynl sysdmfliin kfsskprkdt dalfrqmvfn aaisntddhl
      301 knfamlhtef gfclspaydl lpdiyhnreh rlsfpqgagt lppdrkiler ighvykvsnp
      361 vriigdiyqs vscwqdvfee ydvpqkdiqr lepaisrgls riqp
//
LOCUS       WP_004100463             373 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Thermosipho africanus].
ACCESSION   WP_004100463
VERSION     WP_004100463.1
KEYWORDS    RefSeq.
SOURCE      Thermosipho africanus
  ORGANISM  Thermosipho africanus
            Bacteria; Thermotogati; Thermotogota; Thermotogae; Thermotogales;
            Fervidobacteriaceae; Thermosipho.
REFERENCE   1  (residues 1 to 373)
  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 373)
  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
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 373)
  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   5  (residues 1 to 373)
  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   6  (residues 1 to 373)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 373)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 373)
  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 11513089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Thermosipho africanus"
                     /db_xref="taxon:2421"
     Protein         1..373
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42680
     Region          10..>50
                     /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"
     Region          68..365
                     /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 mklnnskkil lnllfkneay rnqlqkslkv tpstlsyild nlkkkgyitv lksesetvgr
       61 pkhiikmdkn fwksigirig resvnltvfn gyfeeeekis ikltkndign eniskileki
      121 ikkvssldki kaigialsgn idkdkanski lklenfnphy iikkllpnti vsllndveai
      181 ateefvkhgg kkilvinygt gigacfyesr giyekserki ielghfyvgt nekcycgatg
      241 cletiasdya nlkrykfsnl kiedfilnee lynndldelr nlhktyekka qeiynesfky
      301 laifltnifk lfnpekiils gegvtkwfsn elerkihsis nfpvsityrg lknniefgaa
      361 vdalreyilr snl
//
LOCUS       WP_004101408             680 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Thermosipho africanus].
ACCESSION   WP_004101408
VERSION     WP_004101408.1
KEYWORDS    RefSeq.
SOURCE      Thermosipho africanus
  ORGANISM  Thermosipho africanus
            Bacteria; Thermotogati; Thermotogota; Thermotogae; Thermotogales;
            Fervidobacteriaceae; Thermosipho.
REFERENCE   1  (residues 1 to 680)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 680)
  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   3  (residues 1 to 680)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Thermosipho africanus"
                     /db_xref="taxon:2421"
     Protein         1..680
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76615
     Region          1..680
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          192..269
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 msyeeylsvf idegreyvqq lndalldlek npedmeyinv afralhtlkg magtmgfenm
       61 aklchrmeny ldavrsgkvs idsdkldylf ngldliekml ekiasegsee ieedvsglve
      121 ifeklaqgen vgkkeskpag tvetsqtnnd sekseskekp eneadymyee deallhvvne
      181 akkkgydviy tkvilaenvq lksarmymvf hgieelggei iksvpsvedi enekfdreve
      241 lyviakvepl klqeklsais evekvivkkv eikhksevke kekeekkeek heekkknvki
      301 tqtvrvdiek ldtlmnlmge lviarsriid ilkkynikev deslaqlsri tldlqnivmk
      361 vrmvpisyvf nrfprmvrdi sknlgkeinf vmkgedteld rtfveeigdp lvhlirnald
      421 hgietkeeri akgkppvgtl ilsarhegnn vvieveddgr gldrekilkk aierglvdev
      481 kasglpdekv yeflfmpgfs tkeqvselsg rgvgmdvvkn tveslngtvh ieskkglgtk
      541 viiklpltla iiqallvkvd kyiyaipisv idstlivlpe eiqmvqnkev ivkrgevipi
      601 iklwdvlgmk hneeldelnv vvvkvanrky giavdtligq edivikslgk lfadvkefsg
      661 gatlgdgsia liidtlnlve
//
LOCUS       WP_004099869             385 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Klebsiella].
ACCESSION   WP_004099869
VERSION     WP_004099869.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 385)
  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 385)
  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   3  (residues 1 to 385)
  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   4  (residues 1 to 385)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 385)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 385)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 385)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..385
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40548
     Region          33..368
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(108..110,131..132,181,233,257)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mktvkisals aaillsgfas saawsaaset viiglagplt gpsarigkdl engaqlaidd
       61 inkqhptigg kavtfklqse ddqsdprtav avaqrlvdsg vagvvghwnt gtsipaarvy
      121 hdagiaqvap vatghaytkq gfdtsfrvmg hdddggqfag qyavqtlkak riaviddrta
      181 fgqgladefi ksleaqgiki vdrqyvddkt vdfsavltai rsknadliff ggvdsqaapl
      241 arrikqlgmn atlmgaggfv sqtflqlaqk egdgvvalep glpvermpgg kafeqayqsr
      301 yhthielhap faydatrvlv aamekadsvd padylpalra inyagvtgqi afdkegnlks
      361 ptftvykvvd gkwqpqtvlg gattk
//
LOCUS       WP_004104314             726 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Klebsiella].
ACCESSION   WP_004104314
VERSION     WP_004104314.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 726)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 726)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 726)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..726
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..726
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=82886
     Region          159..725
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 midhfnikik ktllallvcf iaiplsrfis pqtiidgnqi ylawlplslm yavlfifgry
       61 avaplviafa itnawiidlt ftqavillfc qlfsvflsca ivryqlgrrw ragltakhmg
      121 vrvfwggffa pillkitmyl agrffsfpla issyfgnmsv iytvidiqsl isaalifttf
      181 fyyplrmiis pryarvfwrn lchswqvreq rvftlywfva laaillvlct pydsvfiagy
      241 lvplifilyf igisrlahtl iriswsvsaf llvaynqnfl hgvqteysls fvlsvlicft
      301 iclfymadiy arsermkfrw rdqaeedplt glpnlrales hlqrnpavai sslriqnldf
      361 lsrhygmmmr veskrqiack lqpllsqger ifqlpgsell lvlngpepea rlnhivstln
      421 hkkfswnnqt ldlefgaswg gysgtesdih pmlgqlswls eqagaarrvl aldaaqeqis
      481 dqtseqvrll aqikqalner glvlyaqpir daagkgyyev lcrmrcgnni itpdkfippi
      541 aqfnlsqrfd mqvletlfss lrhhqgqhfs vnllpytlmq kdsatqiisl fkrynlsaea
      601 itievteeqa fsdvetsmyn iqqlrefgca iaiddfgtgy anyerlkslq adilkidgcf
      661 vrdietdpld aimvksiiem akvkkmkvva eyvetpeqre kllqlgvdyl qgylvgkpqp
      721 lselrt
//
LOCUS       WP_004105968             495 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [Klebsiella].
ACCESSION   WP_004105968
VERSION     WP_004105968.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..495
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=53958
     Region          1..495
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mqyikihsqd nvavaladma agtvvtidgd tvtlaqdiar ghkftlrgia kgdnvikygl
       61 pighaladia pgehihshnt rtnlsdlday syqpdliepa aqpadrdiqi yrrangevgv
      121 rnelwilptv gcvnamarqm qnrflketnd aedidgvhlf shtygcsqlg ddhintrtml
      181 qnmvrhpnag avlvvglgce nnqvdafret lgefdpdrvh fmicqhqdde veaglehlrq
      241 lydvmrhdkr epgklselkf glecggsdgl sgitanpmlg rfsdyliang gttvltevpe
      301 mfgaeqllms hcrdeetfgk lvtmvndfkq yfiahdqpiy enpspgnkag gittledksl
      361 gctqkagssq vvdvlryger lkvhglnlls apgndavats alagagchmv lfstgrgtpy
      421 ggfvptvkia tnselaakkk hwidfdagql ihgkampqll eefvdtivaf angkqtcner
      481 ndfrelaifk sgvtl
//
LOCUS       WP_004106743             224 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LytR C-terminal domain-containing protein
            [Gardnerella].
ACCESSION   WP_004106743
VERSION     WP_004106743.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella
  ORGANISM  Gardnerella
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 224)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Gardnerella"
                     /db_xref="taxon:2701"
     Protein         1..224
                     /product="LytR C-terminal domain-containing protein"
                     /function="Transcription / DNA replication, recombination,
                     and repair / Chromatin structure and dynamics"
                     /calculated_mol_wt=23728
     Region          141..222
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 marnnqnvsy tpdafdeppe gpvgvhrgnp awyavilpyf valiiaavvg vlvwaiasge
       61 ishlplpwnh qqqssqsasp tkpsenkksa ksdedkssed edddddnnks eenksdkkda
      121 ddskdnsand skaqtsldks vavkvlnatk isghaaagad klkqagyanv tagnptgkvp
      181 sesvvwykdd sqkaaaedia ktlgisaven ekeivspivv vlck
//
LOCUS       WP_004107489             718 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Rhizobium freirei].
ACCESSION   WP_004107489
VERSION     WP_004107489.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium freirei
  ORGANISM  Rhizobium freirei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 718)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 718)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..718
                     /organism="Rhizobium freirei"
                     /db_xref="taxon:1353277"
     Protein         1..718
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=75210
     Region          17..717
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mtveifsrlp stlpggsmer llrprsvaiv gasdkpralg asvlsnldrs gyagaihlin
       61 pkrteigdrp clasiddlpe gvdaavlavp raavlpaiea larrrvgaav ifsagfaegg
      121 eegladqrei ariaaeagmv iegpnclgmv nhvdripltf ietvsealgd rpgiaivsqs
      181 gamaavlgvt fasralglsy sistgneags gvedyveflv edastrviam iveqfrkpar
      241 flaaarkaya kgkrivllhp grssaarqsa athtgalagd hqvmrakvar agvilaetle
      301 elgdiaeial rcpelpaggp avlgesgafk altldlceel gldlppinde tapalravlp
      361 pfvgvsnpld ltaqglvepd lydrtlttlf ddarfasiva ciiqtdpvts giklppilka
      421 vrerkptkpl ifagldegap ipadyiaqlr algivyfpst erafralkri defatrdlta
      481 satppvriad lpsqggvvpe yrakqiltpl gipfpegrla atleqalaaa atigypvvlk
      541 aqspdlshks daggiiiglt daaslkkgwi klhadvaghr pgltldgili eamgkrgiel
      601 iigarndpdw gpvilagfgg vtaeilkdvr iltpdlpeda iirelyrlkn apllrgfrgs
      661 ppldvgaaar iiatlgrlll aeaaiqeidl npvviypdgq gavaldalml tapangrt
//
LOCUS       WP_004109811             296 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Rhizobium freirei].
ACCESSION   WP_004109811
VERSION     WP_004109811.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium freirei
  ORGANISM  Rhizobium freirei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Rhizobium freirei"
                     /db_xref="taxon:1353277"
     Protein         1..296
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32168
     Region          19..261
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mtdihdfqgn ilcntssvlg egptydpdtd tvwwfnilgk elhelhlptg kkkvhelpmm
       61 asvlarvdae rqmiateegl flrdiasgel sfyaaietdk pgnrsndgrt hisgslwigt
      121 mgkraemqag aiyhvaaggk vtkifdqisi pnsicfspdg tigyftdtrv sqlmrvlvdp
      181 etglpagepi vmvdsmedpg gldgsvcdad gyiwnarwgs gfvdkyspdg lrieryrvpa
      241 mqpscpafig knadrlavtt aweglddear smqpqagall elgptvrgvf dppykl
//
LOCUS       WP_004110176             208 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LytR C-terminal domain-containing protein
            [Gardnerella].
ACCESSION   WP_004110176
VERSION     WP_004110176.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella
  ORGANISM  Gardnerella
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 208)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Gardnerella"
                     /db_xref="taxon:2701"
     Protein         1..208
                     /product="LytR C-terminal domain-containing protein"
                     /function="Amino acid transport and metabolism"
                     /calculated_mol_wt=22823
     Region          83..167
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mtqeyderia rkafmyqrkr svlttvgvgl gvtfifallv qfhafginsv rapkdnpnyg
       61 vpapcaiigk egakapyvdn ravairvlng tkfrglarav gealnargfn ltevnnnkss
      121 nikrtiiyfg knaineaytv nanftdaimr mddrkdklvd ivlgstfnnl rpkvdvpaag
      181 atihevqgci radlmknipk adqhkevk
//
LOCUS       WP_004110274             146 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Rhizobium freirei].
ACCESSION   WP_004110274
VERSION     WP_004110274.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium freirei
  ORGANISM  Rhizobium freirei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Rhizobium freirei"
                     /db_xref="taxon:1353277"
     Protein         1..146
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15728
     Region          19..141
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mfdlaayfgl flaafaaati lpmqseavlv gmlltesypa aalvavaslg nvfgslvnwg
       61 lgrwierfrh rrwfpvgesa maraqswyrr ygrwsllasw lpvvgdpitv vagalreplp
      121 tflllvaiak vgryavlala atslas
//
LOCUS       WP_004110852             348 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Rhizobium
            freirei].
ACCESSION   WP_004110852
VERSION     WP_004110852.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium freirei
  ORGANISM  Rhizobium freirei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Rhizobium freirei"
                     /db_xref="taxon:1353277"
     Protein         1..348
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39100
     Region          1..344
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mevrvqnlrk efgrfpalnd vsldirssel iallgpsgsg kttllrliag letptdgrif
       61 fgeddasrkt vqqrnigfvf qhyalfrhmt vldnisfglk vrsasrrppr deirrralel
      121 lelvqlngle krypaqlsgg qrqrvalara mavepnvlll depfgaldaq vrkdlrkwlr
      181 eihdrtghtt vfvthdqeea leladrvvvl nkgtveqvgt pdeiydapns pfvygfigqs
      241 nrvkvriasg eiwfddkplg lstphepdge adlyfrphdi elrdgdggai agllvasrrv
      301 agtrhleini gseyepieie lppnkadald rnriafrptr wklfrssl
//
LOCUS       WP_004110897             408 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Rhizobium freirei].
ACCESSION   WP_004110897
VERSION     WP_004110897.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium freirei
  ORGANISM  Rhizobium freirei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 408)
  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 408)
  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
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 408)
  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   5  (residues 1 to 408)
  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   6  (residues 1 to 408)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 408)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 408)
  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 20283677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Rhizobium freirei"
                     /db_xref="taxon:1353277"
     Protein         1..408
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43579
     Region          16..>55
                     /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(29,31..33,42)
                     /site_type="other"
                     /note="non-specific DNA interactions [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            42..48
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            order(43..44,48)
                     /site_type="other"
                     /note="sequence specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238044"
     Site            43..44
                     /site_type="other"
                     /note="putative cAMP binding site [chemical binding]"
                     /db_xref="CDD:238044"
     Region          79..384
                     /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 mktisgtnle qakshnrrvv ieairtngpl sraaiarlta lttqtvsniv eelarshlli
       61 pmeaqkiarg qpiipytinp sgaysiglel grqraagvlt dlsgtvcari drhvdrpgpt
      121 eampvfaaiv rdlqeafsfd rdrllgvgia lpgryadggv tslsplnlpg wqnfpvarel
      181 erliglpvlv endatagaig erlygvargl gsfvylflag dggigagmfl dghlykgsra
      241 nageighiiv ephgrlctcg krgcldryvs psvayeclgi edaqeldpdd ldamiaansr
      301 glqtwleqav qplrqtidfl elafdpqtiv lggsappslm tglaervepl hipvnpmeer
      361 kiprlmvgat gkdtailgaa alpifsetnp qfdvlqkpii hraaeqag
//
LOCUS       WP_004111128             685 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Rhizobium freirei].
ACCESSION   WP_004111128
VERSION     WP_004111128.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium freirei
  ORGANISM  Rhizobium freirei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 685)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Rhizobium freirei"
                     /db_xref="taxon:1353277"
     Protein         1..685
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=71804
     Region          1..685
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mtqrsldrli rpktiavfgg rearrvieqc dlmgfageiw pvhptqesvl grrcyrsvae
       61 lpdapdaafv gvnrtltvdi vrelaargag gavcyasgfs eavaeladga dlqralveaa
      121 ggmpivgpnc ygmingldga llwpdqhgiv rsergvailt qssniainls mqrrglpisy
      181 lmtagnqaqt glsdlaqavl adprvtavgl hiegfgdira lealamrard lkkpvvalkv
      241 gkseqaqrat vshtaslags davadavldr lgigrvttlp elvetlkllh aagpldsnai
      301 ssmscsggea slmadaavgr nvafralkae qlpalraslg tmvtlsnpld yhtfvwgdla
      361 rqteafsamf aggyalnliv ldfpredrcd gadwmitvsa vaaaakqtga ragilatlpe
      421 nmpeaiaqql ieagivpfcg isealaaaei asgianawer prplpllsar aeageietls
      481 eaaakaelaa tglavplgkt aataseaadc aqqlgfpval kalgvehksd vgavklnlwd
      541 rnavqdaaes mshvargflv ermvdrplae livgavrdpv vgltltvgag gilvelleds
      601 ivlplpvtka eildrisrlk vrkliegyrg nagtsleiva davvsaaeyv vknasrleel
      661 dinplmvlpd srgvvaadal irrrr
//
LOCUS       WP_004111841             276 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Klebsiella oxytoca].
ACCESSION   WP_004111841
VERSION     WP_004111841.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella oxytoca
  ORGANISM  Klebsiella oxytoca
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Klebsiella oxytoca"
                     /db_xref="taxon:571"
     Protein         1..276
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=30730
     Region          43..189
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkrcragvll alllagcase kgiidhdgyq ldtrhpaqaa yprikvlvih ytaddfdvsl
       61 atltdnqvss hylipekppl hggkpriwql vpeedlawha gvsfwrgstr indtsigiel
      121 enrgwqktag vksftpfnpa qidaliplak diiaryqilp qnvvahadia pqrkddpgpl
      181 fpwhrlaeqg igawpdarrv afylqgrpsy epvdtaelld vlarygyqvt pemtpaqqkr
      241 vimafqmhfr parwdgvada qtlaiaeall ekygrg
//
LOCUS       WP_004112086             529 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Gardnerella vaginalis].
ACCESSION   WP_004112086
VERSION     WP_004112086.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella vaginalis
  ORGANISM  Gardnerella vaginalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Gardnerella.
REFERENCE   1  (residues 1 to 529)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Gardnerella vaginalis"
                     /db_xref="taxon:2702"
     Protein         1..529
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=59213
     Region          395..519
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(469..470,473,492..495,497)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mselehnnpd afesenidni annidvnsvd nynidnndin qtavlknrhk snksalvlly
       61 slvifvillv caflgtqayf hdrvapgvhf agssqivgaq laavsknvdn avdstkieik
      121 ddrgktinan fedlyvkvdk satvknimrs khdnaftmlm pwvqktvalq atrndmdmda
      181 yiikkfvndk drampytaky dsgsesyvve dgvpgrtvit lpvreavkks lenpgktvkv
      241 tiesrrieap ikrdvakktv dqlnniltkk itlsngdskd ftipksaias wikvnadeqr
      301 kqisftvdre avntwlskel aknlnqqkid qedtyskkgq fimttlkgvn gvevryskdv
      361 ankvvdaiek ctdakitvpt nvvkfavekk ivemrivvdk ttqtvsvykd dqlirtmpvc
      421 tgsngyyetp ngtfhiylry dvqamqgfnr dgsryylpgi twvsyfnggi sfhtarwndv
      481 giaqgypakh gshgcinmye qdskwvydnc prgtivqvvg eqpdgpvrq
//
LOCUS       WP_004112340             295 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Gardnerella vaginalis].
ACCESSION   WP_004112340
VERSION     WP_004112340.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella vaginalis
  ORGANISM  Gardnerella vaginalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Gardnerella.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Gardnerella vaginalis"
                     /db_xref="taxon:2702"
     Protein         1..295
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32075
     Region          24..276
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mtvtstsadi dffanpdenn sgwdlhchtf ysdgtksped lvneaktigl kgvaitdhdt
       61 tagwsdfkea aniadfpvif gseitsvegn isvhmlayry npndeciiem fdltrkrrln
      121 rtrkmvelms hdfpitwqdv laqagkgnlt tigrphiada lvaagvfetr sqafagpvap
      181 hgpyyiptps psvdevikvi khaggvsvia hpadysrnpv ilsdsqiayy aslgldglev
      241 yhrgnsltqr qrlfglakdl dllvtggsdw hgsgkpnslg eettsdevvs kilnr
//
LOCUS       WP_004112928             349 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Rhizobium].
ACCESSION   WP_004112928
VERSION     WP_004112928.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 349)
  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 349)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 349)
  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   4  (residues 1 to 349)
  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 349)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..349
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38960
     Region          77..328
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          245..326
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mfqsssphlt fkrggssfdg mietlgtafg eykaalvspv ddfqwsldfs tcdyatvikg
       61 fhqhefefqi qptinavqhl sivlprsggm gvtyasreat arpgklllyn nlepesvvmy
      121 grsnvidell ldwnvilqtl dqtfetpfsg sldllpelet stsagqmigs laetvirglr
      181 dpsvrspiam ahvtqaladl ivrfvphkls hlldrkpymi aprhvrraie ymeanisqpi
      241 rmpmvakaag vstralqlgf rafrettpaa ylamlrlraa rvelldpang httreiclkw
      301 gflhfgrfsa mykasygesp shtrkrvrgm qprsrrqpqt vvghsilrr
//
LOCUS       WP_004114053             193 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Gardnerella vaginalis].
ACCESSION   WP_004114053
VERSION     WP_004114053.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella vaginalis
  ORGANISM  Gardnerella vaginalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Gardnerella.
REFERENCE   1  (residues 1 to 193)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Gardnerella vaginalis"
                     /db_xref="taxon:2702"
     Protein         1..193
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=21027
     Region          69..149
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 myqkkrfvlt tvgicvgaaf llavlvqchv fgiaapktpe idpnygvqap cptknkdenk
       61 atyidnravp irvlngtkfr gfaravgegl rnrgfnliev gnseksvkrt tiyfgkksin
      121 eaytlaanfk dailrmddrq dklidvvlgv tfnnlkpktd vpaagative ikgcadfnsm
      181 knlpksanhn pvq
//
LOCUS       WP_004114499             290 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Klebsiella oxytoca].
ACCESSION   WP_004114499
VERSION     WP_004114499.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella oxytoca
  ORGANISM  Klebsiella oxytoca
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Klebsiella oxytoca"
                     /db_xref="taxon:571"
     Protein         1..290
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32542
     Region          14..255
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 maepqplfdy tghlpecptw seaeqalywa dimeceihry dvqtgdhqvl qfpeepgcfa
       61 lrekggfiva lrsgiwltdv hgllqrkvcd npsnpqlarf ndggtdrdgr fyagtfwgpg
      121 dfngallmrv dndlspqviq cdihgangla fsedkrwmyt sdtpnaviyr tpldeqgevg
      181 krevfrrfqp gegipdgaai dtegcywsam fdgwriarfs ptgeqleeyr lpvrcptmvc
      241 fggadmktly itttrenmda eelakyplsg aiftlpvtva gmkklpfter
//
LOCUS       WP_004115225             292 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Klebsiella].
ACCESSION   WP_004115225
VERSION     WP_004115225.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..292
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32284
     Region          13..255
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mrievlldlk trlgespvwd veqqrlwwvd sldgrlfacn aqggaikswd vrqkigsfal
       61 rqngegavva lqngvhlldf asgeltllhh peadrpfnrl ndgkvdrqgr flfgsmdmre
      121 eepsgalyrl dadlslhvlk kniivsnapc wspsgetfyf adtwtgeica wdyntatgdl
      181 sgervfcrvd sseggaadga tvdsegylwn alvyagklvr ytpegkvdri iempvkkvts
      241 vmfggenldv lyvtsmaqpp lprfpednql rgslfalydl gvtgvaerrf ag
//
LOCUS       WP_004083059             355 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Schaedlerella
            arabinosiphila].
ACCESSION   WP_004083059
VERSION     WP_004083059.1
KEYWORDS    RefSeq.
SOURCE      Schaedlerella arabinosiphila
  ORGANISM  Schaedlerella arabinosiphila
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Schaedlerella.
REFERENCE   1  (residues 1 to 355)
  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 355)
  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
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 355)
  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   5  (residues 1 to 355)
  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   6  (residues 1 to 355)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 355)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 355)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Schaedlerella arabinosiphila"
                     /db_xref="taxon:2044587"
     Protein         1..355
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39496
     Region          16..64
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          78..345
                     /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 mkryigledm shincasvlr viqssggisr kqisditgls wggmtkivnk lmeheyivee
       61 kngafagngr tpgllrvntk khlaagadin htglrawvtd fsgglqktyf renhfrnree
      121 llenilsffe mifqddknee iqavgiamqg rvdsekgisi hfpecenwrd vplvsilker
      181 fhteiylehd pdcmlffeme smdaenvill ridqsigmav alggailrgt gilelphsiv
      241 ipggkpckcg lrgcleayia pcmqdgkiqk qaleemvspl avaiynsicm fhaeaviltg
      301 dlmkyhgmfe grlllelhkm qkdtrtairf sedtetavkg aaliaarqav nairl
//
LOCUS       WP_004116650             245 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Gardnerella vaginalis].
ACCESSION   WP_004116650
VERSION     WP_004116650.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella vaginalis
  ORGANISM  Gardnerella vaginalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Gardnerella.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Gardnerella vaginalis"
                     /db_xref="taxon:2702"
     Protein         1..245
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=26903
     Region          94..233
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mqydhnthys snpiskrias fiwlislaii igiviglvlp kinhdvgeit geyaadgdaa
       61 allnklkvsk shpsgynrsv fgyrttdvdk ngcdvredvl ardlkqvrfk ysgsckvasg
      121 llhdpytgln infvrgrkts alvqidhvva lenawqsgaw kwshakrlkf gndmlnllav
      181 qgaanqekgs asaaywlpsn ksfrcdyvar qiavkykydl svtsaekrsm asilhgcsaq
      241 klpns
//
LOCUS       WP_004116889             413 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Rhizobium freirei].
ACCESSION   WP_004116889
VERSION     WP_004116889.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium freirei
  ORGANISM  Rhizobium freirei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 413)
  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 413)
  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
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 413)
  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   5  (residues 1 to 413)
  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   6  (residues 1 to 413)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 413)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 413)
  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 15726307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Rhizobium freirei"
                     /db_xref="taxon:1353277"
     Protein         1..413
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44790
     Region          18..>76
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          78..374
                     /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 mlaksstelv rqknsalvls alrrhgplah telsdftkls satvsvitad leraqiieka
       61 eqqaasgrgr prvlfsqrrn cgylivvvis sdavqyslvd yagrlidrfs eersqeasgv
      121 gpfvadlrda lrriaarsql ahdkvlmisi sskglvdtse pvlrwspifg rdeidfaavl
      181 rdewpakiil gnetllvasa lgrqeennkg sdframaals lghsiglgiv rrgeegghqv
      241 sapnfghmmh vpggglcrcg argcieayag fyamlrtafd vpldtipakf vpiaeldkia
      301 vsarhggrrn mlafrqagla lgnglsrvls lhermpivit gpgvryydll iegiteglae
      361 shvvrmegmp elrvivdept lvfeghlnha fsiidndivr rtasvvelrg qag
//
LOCUS       WP_004116979             529 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Gardnerella vaginalis].
ACCESSION   WP_004116979
VERSION     WP_004116979.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella vaginalis
  ORGANISM  Gardnerella vaginalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Gardnerella.
REFERENCE   1  (residues 1 to 529)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Gardnerella vaginalis"
                     /db_xref="taxon:2702"
     Protein         1..529
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=59168
     Region          395..519
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(469..470,473,492..495,497)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mselehnnpd afesenidni annidvnsvd nynidnndin qtavlknrhk snksalvlly
       61 slvifvillv caflgtqayf hdrvapgvhf agssqivgaq laavsknvdn avdstkieik
      121 ddrgktinan fedlyvkvdk satvknimrs khdnaftmlm pwvqktvalq atrndmdmda
      181 yiikkfvndk drampytaky dsgsesyvve dgvpgrtvit lpvreavkks lenpgktvkv
      241 tiesrrieap ikrdvakktv dqlnniltkk itlsngdskd ftipksaias wikvnadeqr
      301 kqisftvdre avdtwlskel aknlnqqkid qedtyskkgq fimttlkgvn gvevryskdv
      361 ankvvdaiek gtdakitvpt nvvkfavekk ivemrivvdk ttqtvsvykd dqlirtmpvc
      421 tgsngyyetp ngtfhiylry dvqamqgfnr dgsryylpgi twvsyfnggi sfhtarwndv
      481 giaqgypakh gshgcinmye qdskwvydnc prgtivqvvg eqpdgpvrq
//
LOCUS       WP_004118029             227 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Gardnerella vaginalis].
ACCESSION   WP_004118029
VERSION     WP_004118029.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella vaginalis
  ORGANISM  Gardnerella vaginalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Gardnerella.
REFERENCE   1  (residues 1 to 227)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Gardnerella vaginalis"
                     /db_xref="taxon:2702"
     Protein         1..227
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=24168
     Region          144..225
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mannsqnvsf ttddfdnppe gpvgvhrgnr awyavlfpyv vvlvvavvlg llawalmsge
       61 innirmpwsa nnsaiskssn gnkngkides ksksdkadgd dsdedkdpee tnksdkkqdk
      121 edknsskdsn anndsstadi nktvqvkvvn atkiqghaaq eagklkqagy anveaanpkg
      181 nvpsdsvvwy kgdenraaaq diaktlgisn veatseittt ivvvlck
//
LOCUS       WP_004118204            1356 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Rhizobium].
ACCESSION   WP_004118204
VERSION     WP_004118204.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 1356)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 1356)
  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 1356)
  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 1356)
  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 18568555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1356
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..1356
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=149730
     Region          16..67
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          <478..978
                     /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 mstllnppas neaitpaqcr aarallawsq qelasrarva tstvadferg hrnpiqqnae
       61 airgvleaeg iafraggavi gptlpafadr kdaglpirwv datdlsqwae rrdgqgslpt
      121 llaklaranr pillrfpsde gvqhagwdgv teaseaseyi plgvtgweig tqrdriaska
      181 dddykkrsen plglipaelt fifvtprhwp qkemwaqkkr aeniwkdvra ydgdnlvhwi
      241 elypavglwl aialgkrpag aldlreywle walatqwqlp selvlcdrde satrilrwlr
      301 gpssvlavkg espaevsgfv yaainqlpan laeyylcrsl vvansetarl igdsatplvi
      361 vvldpepgpa qalakkghhv laaygqdass sgdaivlerp arenikivle gvgvpsemag
      421 rmardssrsl gilrrlmpss pgrvpawakg lpsqsliaal laggwdesse gdksvlsrla
      481 dmpyepfaas laglagnfds plrkvgsvwk iasprdawgl laadispshm erfaavaldv
      541 lsaadpryem paeerwyasv rgvhpefskn lrngvgevli ilalfgklas svpsaelqpd
      601 liiqrllsga drqrwwslsr dfqllaeasp ssflsaldda lgqddspvav lfghdtsplf
      661 gaehlstllw aletlawspd ylgraasilg aldeldpggr ytnrpgsslr ttfllwapqt
      721 hatleqrlrv ldrlrarfpk aawklllgil ptehdsfspt paplwrdfst ptseivtfel
      781 iergalaitd rlladasadi srwvalldrw gnlgarreea lnklkalvpf iaddvgrnal
      841 rsklrailhs hrsfrdaawa lpeeelapfe eiynaitpvd liaeiswlfd tsvalpnpig
      901 trwhedtqrq lqgerrsvve ailtnmgldg lfalanavqe kgylgqaiae aevgnprrgh
      961 eiivraltre gvvglgvarg miitmypmqa dqwvtdlvde mqqigakqes llaillalpp
     1021 ssrawsllre lganfeeqyw krvpilwing eredtefavs klmdvgrarh vvhlvglrlh
     1081 tgltfgsdll vrllieaalq paefdadhnd ttmfqhyvae ilsvldnrdd vpatemlkle
     1141 wiylpvleys qrpakliire lasnpqlfid vicaiykpse dsrvveetva nqeqvtnrar
     1201 qasnllrlwn vvpgtrpdgt idlailedwv qrarqlaksa gredisdqki gevlacapsg
     1261 qdgiwpteav reliesvrnk nieiglmigr rnlrgvttrl prdggaqehd lartfsewsr
     1321 atalewprts avlekiatsy dyearshdnd aekldw
//
LOCUS       WP_004118575             236 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Enterobacterales].
ACCESSION   WP_004118575
VERSION     WP_004118575.1
KEYWORDS    RefSeq.
SOURCE      Enterobacterales
  ORGANISM  Enterobacterales
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  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   3  (residues 1 to 236)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Enterobacterales"
                     /db_xref="taxon:91347"
     Protein         1..236
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27518
     Region          44..205
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 msegvsknsr yeiiailrde lriqsklyfy cndikhqstl kkiegnffyi kpstshpglp
       61 kesifyfiih splgkieftt nnritdksns nnllcfiipe slsilqrrts prinvryesq
      121 fycsgryrsg tiykyhlndi seggcsfisl eplhsfirng nelensvlnl geygqilfnl
      181 kikhiseenn rkqcdatsfr vscmfyyese ekkekiekii vkliidrkii nrrslv
//
LOCUS       WP_004122015             194 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Rhizobium freirei].
ACCESSION   WP_004122015
VERSION     WP_004122015.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium freirei
  ORGANISM  Rhizobium freirei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Rhizobium freirei"
                     /db_xref="taxon:1353277"
     Protein         1..194
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20981
     Region          3..189
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mskdrfivai tgatghaygi rlletlrelg lethlvmsrs aivalayetd lklkdvhala
       61 dhvhgnddva apissgsfrt rgmiiapctt ktlgeiasga cgtlvsraad vvlkerrrlv
      121 lmlretplhl ghlrnmvtit eigaivmppv pafypkpkti demidhtigr aldlfdidtg
      181 qvkrwkeppa digg
//
LOCUS       WP_004104618             290 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Klebsiella oxytoca].
ACCESSION   WP_004104618
VERSION     WP_004104618.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella oxytoca
  ORGANISM  Klebsiella oxytoca
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Klebsiella oxytoca"
                     /db_xref="taxon:571"
     Protein         1..290
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32538
     Region          14..255
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 maepqplfdy tghlpecptw seaeqalywa dimeceihry dvqtgdhqvl qfpeepgcfa
       61 lrekggfiva lrsgiwltdv hgllqrkvcd npsnpqlarf ndggtdrdgr fyagtfwgpg
      121 dfngallmri dndlspqviq cdihgangla fsedkrwmyt sdtpnaviyr tpldeqgevg
      181 krevfrrfqp gegipdgaai dtegcywsal fdgwriarfs ptgeqleeyr lpvrcptmvc
      241 fggadmktly itttrenmda eelakyplsg aiftlpvtva gmkklpfter
//
LOCUS       WP_004126154             531 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [Klebsiella].
ACCESSION   WP_004126154
VERSION     WP_004126154.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..531
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=57019
     Region          2..527
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mqtilkidpt dnlivalqdl rkeqqvnwnd eayilrsdvk akhkfatedi apgdivslyg
       61 vpvgkatrpi trgeaitten ikhyaapvsl ddvapydwqq pdvsawqqrt fkgivredgr
      121 vatanywlvi plvfcenrnv qrvtdalnda lgyannglkn farqvtsaga lndtrhlpfp
      181 hldgircitv nsgcggatsd smtmcdvlaa ysdhpnvlgm tvfalgceka rivdfnaala
      241 krnpnfskpi iyfrqqdwss eekmmqdalt etynaireap vaerqdvpls hlkigvkcga
      301 sdgfsgisan pamgevsdrl valggasgla efpelcgaeg divqrcatre lkekflslmk
      361 nyehvanffg ttiadnpspg niadglitda iksagaakkg grapvsavcd yaepmgesgl
      421 slvctpgndv davtglvaag cnvvifstgl gtptgnpivp vlkvstnsal akkmpdiidy
      481 dcgpiiegtp ladiadglfe kiiatasgtw rtkadaleqf dfmlwkrsle l
//
LOCUS       WP_004126526             267 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Klebsiella].
ACCESSION   WP_004126526
VERSION     WP_004126526.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 267)
  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 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   3  (residues 1 to 267)
  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   4  (residues 1 to 267)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..267
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30445
     Region          17..259
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <161..259
                     /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 mlelsmslpi kvqngglfis rgvgshparr lhsweiifve kgtltirenn eifsvnagds
       61 lllwpqrlhv gigqfpadlk fywlhfevms gegdtllsip qhmrvndpqy iislfrqflr
      121 eqenihrsva lelilllilq qisaaageqp adspgnalaw raqqiirtrf hlplsastla
      181 qelhcnvdyl grvyrhvfrl tltealhrqr vraaekllis dslsltevam kcgfndvgyf
      241 rkifrkhtsl tpaawkrryc kehinsa
//
LOCUS       WP_004126737             283 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: class II fructose-bisphosphate aldolase [Klebsiella].
ACCESSION   WP_004126737
VERSION     WP_004126737.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 283)
  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 283)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10097223
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..283
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=30094
     Region          5..281
                     /region_name="TBP_aldolase_IIB"
                     /note="Tagatose-1,6-bisphosphate (TBP) aldolase and
                     related Type B Class II aldolases. TBP aldolase is a
                     tetrameric class II aldolase that catalyzes the reversible
                     condensation of dihydroxyacetone phosphate with
                     glyceraldehyde 3-phsophate to produce tagatose 1; cd00947"
                     /db_xref="CDD:238477"
     Site            order(26..28,31,51,54..56,60,64,67..68,141,233..234,
                     236..237,240,244,247)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238477"
     Site            order(81..82,177..179,181,208..209,211,230,232..233)
                     /site_type="active"
                     /db_xref="CDD:238477"
     Site            order(82,178,208)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238477"
     Site            order(177,179,181,209,211)
                     /site_type="other"
                     /note="Na+ binding site [ion binding]"
                     /db_xref="CDD:238477"
ORIGIN      
        1 mfadmksmvi kawreryall aincmnlesa raavrvaekh rapiilnlyq ghlshfpatt
       61 aaavvrvlae easvpvtlsl dhgkdpikir qafragfsgl midasafala enirqtrevv
      121 elaasvglcv egelghlada prydqasnad lmtqpedvpp fieqtgidll avsvgtahgm
      181 yapgvkpmld fdrlaqiqra ssvplalhgg sgtpfeqlqr cpefgvakin vgaavfeagk
      241 aallhtlchd stieladals vmeqasadai vpylrasgsi nka
//
LOCUS       WP_004130054             338 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [Rhizobium].
ACCESSION   WP_004130054
VERSION     WP_004130054.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 338)
  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 338)
  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 338)
  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 338)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..338
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=37410
     Region          4..336
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mirmnrrtli mssvamtaal aaprimrass pefsfkfani mpvdhplntr mteasdkisq
       61 qtdgrvsiqv fpasqlgtda dmlsqlrsgg ldllaqtgli aatlvppaai tgvgfaypdy
      121 aqvwksvdge lgrsirtafe kvnliafekm wdngfrqtts igkpiksped lkgfkirvpp
      181 aplwtslfks lgaaptsipw getysalqth vadglenpla giyfakmyev qkylsrtnhm
      241 wdgfwilanr dnfemlpedl rdivvteinr saivqradve klnselqael tskglefidv
      301 dvskfratlq assfysdwkg rfgeeawall estsgkli
//
LOCUS       WP_004130282             341 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CHAP domain-containing protein [Gardnerella].
ACCESSION   WP_004130282
VERSION     WP_004130282.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella
  ORGANISM  Gardnerella
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Gardnerella"
                     /db_xref="taxon:2701"
     Protein         1..341
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37033
     Region          208..341
                     /region_name="COG3942"
                     /note="Surface antigen [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443142"
ORIGIN      
        1 mkhaehgaka kgrfnspfml ftsvrgshas snnhhafssn nsaavlanng avvslenvdl
       61 envnqefavs lsrrqlrlar vakerknrmi vsaslfalvg aaltsmalnk pnsidslask
      121 syssklsfvd dssaqaasrs smresinran kylnfssava glesdlsafs tksshkskwd
      181 lgsnsdfkvs emsksaannp nvavfldsda kivpsgfnpn hdsgdsgnay efsqctwwvy
      241 vrrhqlglpv gsnmgdgwmw gwtarklgyw vdntprhvgd imvfgrgqag vnrayghvai
      301 vekinqdgsi etsessaeyh grtysrvvsa kdasafefih y
//
LOCUS       WP_004131039             296 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Gardnerella].
ACCESSION   WP_004131039
VERSION     WP_004131039.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella
  ORGANISM  Gardnerella
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 296)
  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   2  (residues 1 to 296)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Gardnerella"
                     /db_xref="taxon:2701"
     Protein         1..296
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33191
     Region          231..294
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mhktsrnvle rfeaisglnn yvseeisdis dsyreaknlq htkddlnild yktcvldset
       61 keralalkdl aananssslk vddfnkrnea rmknhvrlai kpahvlaiml ilvvclscsl
      121 tmlisqyaty skvyaynase ksknhsnkqv dfynksdakd dgkndskdes nnkskdgikd
      181 esnnkskvsa nhkselkkde esvesvgknq dlieknksey sqnrskniqn ksecininsa
      241 gseelqaikg igpkmaqril dmrkkvrvfn rvedlmqvng igpktfakik smicvg
//
LOCUS       WP_004131729             506 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Gardnerella].
ACCESSION   WP_004131729
VERSION     WP_004131729.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella
  ORGANISM  Gardnerella
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 506)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Gardnerella"
                     /db_xref="taxon:2701"
     Protein         1..506
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=56241
     Region          373..497
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(447..448,451,470..473,475)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 msesqennms vfesddteqf evskkrvkgn ksalvllysf iiflilvvaa fvgsqayfhn
       61 rvapgvhfag ssevsgaqie kvtdavnrai entkieikdd sgkssvetlk dlsvsvdksa
      121 tvqnvmrakh nnvftmlmpw lqenvglkak ldnesmdayi vkkfvsekdr ampytakfds
      181 ssnsyvvedg vpgrtiitlp vreaikrvle npgktvkvtv gsrkveapik rdvaqktvdq
      241 lnnllskkit ldngdskdft lskavlaswi kidadcakkk isykvdssaa nawlskelak
      301 nlnqqkvdqe dtynkqgkfi lttlkgengi evkyskdfan kvvqaveksa daklsvptnv
      361 vkfgiekktv dmrvvvnksn qtisvykddq llktfpvcsg sngyyetpng tyfiylryrv
      421 qdmrgfnrng sryflpgitw vsyfnggisf htalwnnvgi sqgypakygs hgcinmyeqd
      481 akwvfencpr gtvvevvgeq pdgpvr
//
LOCUS       WP_004118626             286 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Rhizobium freirei].
ACCESSION   WP_004118626
VERSION     WP_004118626.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium freirei
  ORGANISM  Rhizobium freirei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Rhizobium freirei"
                     /db_xref="taxon:1353277"
     Protein         1..286
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31059
     Region          12..282
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mtttaaprgn rdiclatlrd tdrdrylacl lapeekrpal valytfnael arirdlvhep
       61 lpgevrmhyw rdllegqahg sseanpiaae lltaieqyrl prqtlidmid arifdlyddp
      121 metrgnlegy agetasaliq laslvlsade akrsadaagh agvaqaiagl lllmplhrhr
      181 gqlylpleil tatgldrdsf lagkdkaris vaieafaglg rehlarataa gaipqavfpa
      241 flpatlaepv lkkaqklgag lfdqspalpq wrrqmrmaia sitkki
//
LOCUS       WP_004122259             118 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Rhizobium freirei].
ACCESSION   WP_004122259
VERSION     WP_004122259.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium freirei
  ORGANISM  Rhizobium freirei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 118)
  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 118)
  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   3  (residues 1 to 118)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Rhizobium freirei"
                     /db_xref="taxon:1353277"
     Protein         1..118
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=13621
     Region          16..114
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mrrnvpdrlr hfaktmrhda tkaenmlwqa lrrsqlegfk frrqvpidgy ildfvcfkar
       61 livevdgaqh aestkdlard ahfskqgfri vrvwnhevtt nlegvcltil aelknsge
//
LOCUS       WP_004133381             418 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Klebsiella].
ACCESSION   WP_004133381
VERSION     WP_004133381.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 418)
  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 418)
  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 418)
  AUTHORS   ter Beek,J., 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 418)
  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 418)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..418
                     /product="CmpA/NrtA family 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=46040
     Region          38..289
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mgdkfsisrr rllqtgaalg gamllpgimq aawaagsdkp eqttvrvgfi pltdcaplai
       61 aslkgfdkky gitlvpskea swaavrdklv ageldaahil ygmlyglelg iaskpqaman
      121 lmtlnrngqa itlsselqeq gvtdlsglkk rigqhapgsy tfahtfptgt hamwlyywla
      181 sgginpfadi rtvvvpppqm vmnmrignms gfcvgepwna raindrigft aatsqdiwpe
      241 hpekilgtrs ewvtrhpnta ralvaalmea qrwieasadn tretarllar rawlntkeqy
      301 ltgrmlgeyd ngigrrwqda hpmrfyeqge vsfpwlsdgm wfltqfrrwg llksapdyla
      361 vaqrinridv wkeaaqavgg isaptqamrs stlidgkvwn gvdpegyars faiqrkga
//
LOCUS       WP_004134357             614 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Gardnerella greenwoodii].
ACCESSION   WP_004134357
VERSION     WP_004134357.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella greenwoodii
  ORGANISM  Gardnerella greenwoodii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Gardnerella.
REFERENCE   1  (residues 1 to 614)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..614
                     /organism="Gardnerella greenwoodii"
                     /db_xref="taxon:2914925"
     Protein         1..614
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=67498
     Region          479..603
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(553..554,557,576..579,581)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mtdmqhnpeg edpfnqmpgh tpddasddtv afaqveqnqv dnqsadndek tlaenlgeva
       61 deyedqdsfd sglsvqeili nnsadstetd tfkavtpdsk stpenggsrn skdgnrggrg
      121 angaktgsan hgnrsalall ysllvfvili avaffalqwy fhdrvspgvn fgdvsvarnl
      181 tgykedsvkr vvsdavdass lvikddrgns itadlgelgv kinqpntvra imqakhnnlf
      241 trimpwiqqt vslqakvdhs amdsyvltrf vrerdravpy sakfdknses yvvedgipgr
      301 tietlsvrea vkkllahpgk slkvsvtsrk tqapikrdaa qklvdelnkl lskkitfnng
      361 dgkdftvpkt vlaswitvka dttrrklsyt vdtdkadefl sqalpkelnq qkvnqedain
      421 kdgkfifttm kgsngveity aksaaekave alrkgndfkl tlpakitkft vekklvemri
      481 vvdkstqtas vykndelvkt fpvctgrtga ddstpgtffi ylryasqdmr grngdgssyf
      541 spnvrwvsyy hagegfhtas wnydgiatgd aanhgshgci nmyeqdarwi yencprgtiv
      601 qivgttpdgp vrek
//
LOCUS       WP_004135288             229 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Gardnerella greenwoodii].
ACCESSION   WP_004135288
VERSION     WP_004135288.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella greenwoodii
  ORGANISM  Gardnerella greenwoodii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Gardnerella.
REFERENCE   1  (residues 1 to 229)
  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   2  (residues 1 to 229)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Gardnerella greenwoodii"
                     /db_xref="taxon:2914925"
     Protein         1..229
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=25465
     Region          167..226
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 meyyepgskv pepktylpnr riasslaefs ndafsennie nnfnsfdeti rnikssprfh
       61 mkpvhtlaim fvlvvalcas ltmlisqslt yqrvqnsqse slqkiednad yskrsfddle
      121 dsnskknnen sesdygnens dnsesnessk snessevses nksgtlrini ntatvdqlqs
      181 lkgigpktaa riiahrkrvg gfksledllq ikgigpktln kfrgnvdvk
//
LOCUS       WP_004137932             746 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor family protein [Klebsiella].
ACCESSION   WP_004137932
VERSION     WP_004137932.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 746)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..746
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..746
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=82846
     Region          9..746
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mknfnysgia lavvsallsg aslaaessdv geinvkgqsl ggglmvqeds gkarstltke
       61 amekapgasn aidmlkytpg mnvnsndasg lsgidytmrg mnsdqiglsm dgipindsgn
      121 yavypnllgd aenleqifvt qgsseadgph igssggnigl vtkrpskefg gfvkqtlgsh
      181 nlsktfarle tgeyngfsnw lsyshteakk wrgegrnysd kfemnslyed gngnssnlim
      241 kynrqdnsny ntlskaqfee dprqdysttp vynskgqlsk yyklnrnpfe tftlsftqrl
      301 qlrdnlaltv qpyyywgngg sftgqtasvl sntsdtagqy dlsnltsnty yrpswtqtwr
      361 pgvttklkwd indehsldig ywyerarqsq tqpfisiqdd gnpanvsgkp ggsdqvkdan
      421 gntvqgrnqy tvtpahkvwl qdswfvtpdw tlvgglayqy verkgdnkgs lysaaekrqa
      481 tyheflpnfs isykpdsenq lfynltrnmr tppnyvlynv gdsistkpel swnhelgwrf
      541 qredmllsat lfymrytdrq isttnadgdy emmnigsves kglelewsgk lpynfnyyts
      601 ytythseqkd divsngghpl ptagktvpnv pknmlnaslg yddglyygsf ggkyvssfyg
      661 dltndekigg rtvfdvaagv hlpvdkkivk satlrfgidn lfdkqyltsv rsttfnaaay
      721 dgvkastpyy nvgeertfsv sleatf
//
LOCUS       WP_004137661             283 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: class II fructose-bisphosphate aldolase [Klebsiella].
ACCESSION   WP_004137661
VERSION     WP_004137661.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 283)
  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 283)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10097223
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..283
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29970
     Region          5..281
                     /region_name="TBP_aldolase_IIB"
                     /note="Tagatose-1,6-bisphosphate (TBP) aldolase and
                     related Type B Class II aldolases. TBP aldolase is a
                     tetrameric class II aldolase that catalyzes the reversible
                     condensation of dihydroxyacetone phosphate with
                     glyceraldehyde 3-phsophate to produce tagatose 1; cd00947"
                     /db_xref="CDD:238477"
     Site            order(26..28,31,51,54..56,60,64,67..68,141,233..234,
                     236..237,240,244,247)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238477"
     Site            order(81..82,177..179,181,208..209,211,230,232..233)
                     /site_type="active"
                     /db_xref="CDD:238477"
     Site            order(82,178,208)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238477"
     Site            order(177,179,181,209,211)
                     /site_type="other"
                     /note="Na+ binding site [ion binding]"
                     /db_xref="CDD:238477"
ORIGIN      
        1 mfadmksmvi kawreryall aincmnlesa raavrvaekh rapiilnlyq ghlshfpatt
       61 aaavvrvlae easvpvtlsl dhgkdpikir qafragfsgl midasafala enirqtrava
      121 elaasvglcv egelghlada prydqasnad lmtqpqdvsp fieqtgidll avsvgtahgm
      181 yapgvtpmld fdrlaqiqra ssvplalhgg sgtpfeqlqr cpefgvakin vgaavfeagk
      241 aallhtlchd stieladals vmeqasadai vpylrasgsi nka
//
LOCUS       WP_004122710             387 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Klebsiella].
ACCESSION   WP_004122710
VERSION     WP_004122710.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 387)
  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 387)
  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   3  (residues 1 to 387)
  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   4  (residues 1 to 387)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 387)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 387)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 387)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..387
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41762
     Region          33..356
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(106..108,129..130,179,232,256)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mnkhimvlkv frsslialsl lgstsllake tvkiafigpl tggasatglg grnsaqlavn
       61 qhnadpaaky tfelikfdde ckpatgvqvv tkaatnnsii aaighycsav aavtvntyhr
      121 fglplvvwga vlpeitygnn ykeihrvngt minegklaae yvknsgfkri aviydttdyg
      181 kgqskyflqy lkenpqasvv ssfgvdisqq dfsaeltavq ksnpdiiyfg gltpqgvalr
      241 aqmqrmgisk pmmgvsgiln sgfidgvgke aaegvvsfhn gapidkysqg aaflkaynma
      301 gfkeepdayg pfaysaatli mdavekvgpd rkkvrdvlnh tagykslvgt infddhrqnl
      361 tnayqyvvqd gkwvywpdsk yghaiek
//
LOCUS       WP_004140954             147 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Cardiobacterium hominis].
ACCESSION   WP_004140954
VERSION     WP_004140954.1
KEYWORDS    RefSeq.
SOURCE      Cardiobacterium hominis
  ORGANISM  Cardiobacterium hominis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cardiobacteriales; Cardiobacteriaceae; Cardiobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Cardiobacterium hominis"
                     /db_xref="taxon:2718"
     Protein         1..147
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=15640
     Region          7..147
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mgvkvkrniq qgftlielmv viaiigvlaa ialpayqiyv traqmgeafn lvdaqknavv
       61 etrtnkgdwp snnteagmgd ptkisgkyve kvevtsggvi tatmkssgia atiqhktltl
      121 tptetngsyt wecssnvgkm ylpavcr
//
LOCUS       WP_004141683             425 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Cardiobacterium
            hominis].
ACCESSION   WP_004141683
VERSION     WP_004141683.1
KEYWORDS    RefSeq.
SOURCE      Cardiobacterium hominis
  ORGANISM  Cardiobacterium hominis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cardiobacteriales; Cardiobacteriaceae; Cardiobacterium.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 425)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Cardiobacterium hominis"
                     /db_xref="taxon:2718"
     Protein         1..425
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=46910
     Region          6..415
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mtpyeatrrl avsriladgr kvavgtlaqn rdgvyfayda aylqqygnls pyhlradgsv
       61 qlaarglphg lhgvfadclp dgwgmllqdr hfrqqgilpa qvtaldrlaf igdrgmgalg
      121 feplwqpqap penrdyaalg laaqavfdgq tedvlqelir vgssggarpk aqiwmapdep
      181 rhcrtvaqpg deawlvkyts rhlpplghee glceaaylql aeraglqpca wrlldapaks
      241 gakrwlalkr fdctaqgryh lhsasgllha dyrlpsldys dllkmskqlc rapaigrlqf
      301 araifnllla nhddhgknwa flqddrgdwq papfydatfs phprgehmta fggygkappl
      361 ktmqqlaaha gfprwpeaqk iiqqiadtaa tfgatalalg vkkstvrevq qhlnhiwqen
      421 rqlla
//
LOCUS       WP_004141788             409 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Klebsiella
            pneumoniae].
ACCESSION   WP_004141788
VERSION     WP_004141788.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 409)
  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 409)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..409
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47343
     Region          1..405
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 msvlqlslne arhlhlaaqg llkkprrrar pkdilstiqq msllqidtin vvarspylvl
       61 fsrlgsypqh wldeslrnge lmeywaheac flprsdfalv rhrmlnpdnm gwkyhrawme
      121 ehagsiaelv ahigqngpvr sadfthprks asgwwewkph krhleglfta gevmvverrn
      181 fhrvydltrr vmpdwdderd alsredaeai mlrnsarslg ifraqwlvdy yrlrqpalpg
      241 llaawqeegl vvpvnvealg emwlhheala qletapggkl tashsavlsp fdpvvwdrkr
      301 aeqlfnfsyr lecytpapkr qygyfvlpll hqgklvgrmd skihrksrel eifalwleeg
      361 gkitrgleqg lrraindfar wqsaerilcr rlpeglfvgq eqgweidad
//
LOCUS       WP_004125490             495 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [Klebsiella].
ACCESSION   WP_004125490
VERSION     WP_004125490.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..495
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=53897
     Region          1..495
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mqyikihshd nvavaladma agsvvtidgd tvtlaqdiar ghkftlrgia kgdnvikygl
       61 pighaladia pgehihshnt rtnlsdlday syqpdlsepa aqpadrdiqi yrrangevgv
      121 rnelwilptv gcvnamarqm qnrflketnd aegidgvhlf shtygcsqlg ddhintrtml
      181 qnmvrhpnag avlvvglgce nnqvdafret lgefdpervh fmvcqhqdde veaglehlrq
      241 lydvmrhdrr epgklselkf glecggsdgl sgitanpmlg rfsdyliang gttvltevpe
      301 mfgaeqllms hcrdeetfgk lvtmvndfkq yfiahdqpiy enpspgnkag gittledksl
      361 gctqkagssq vvdvlryger lkvhglnlls apgndavats alagagchmv lfstgrgtpy
      421 ggfvptvkia tnselaakkk hwidfdagql ihgkampqll eefvdtivaf angkqtcner
      481 ndfrelaifk sgvtl
//
LOCUS       WP_004141903             276 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Klebsiella pneumoniae].
ACCESSION   WP_004141903
VERSION     WP_004141903.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..276
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=31173
     Region          43..189
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkrmmrivll allltgcage kgiidrdgyq ldtrhpaqat yprikvlvih ytadnfdvsl
       61 atltdkevss hylipeqppr yqhkpriwql vpeedlawha gvsywrgstr indtsigiel
      121 enrgwqktag vksftpfhpe qiaaliplar diiaryhiap qnvvahadia pqrkddpgpl
      181 fpwqqlaqqg igawpdeqrv afylngrpas epvdpeivld llsrygyqvt pemtpaqkkr
      241 viiafqmhfr pqrwdgvada qteaiaeall ekygqg
//
LOCUS       WP_004142687             103 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Klebsiella].
ACCESSION   WP_004142687
VERSION     WP_004142687.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..103
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11343
     Region          5..101
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(7..8,26..27,35,38,40..41,43,46..47,49,57,62,69)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(26,57..58,60,84)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 maphdtfpqr vwhivasipe gyvttygeva rlagspraar qvggvlkrlp egstlpwhrv
       61 vnrhgdislt gpdlqrqrqa llaegvqvsg sghidlqhyr wvy
//
LOCUS       WP_004142790             363 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Cardiobacterium hominis].
ACCESSION   WP_004142790
VERSION     WP_004142790.1
KEYWORDS    RefSeq.
SOURCE      Cardiobacterium hominis
  ORGANISM  Cardiobacterium hominis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cardiobacteriales; Cardiobacteriaceae; Cardiobacterium.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Cardiobacterium hominis"
                     /db_xref="taxon:2718"
     Protein         1..363
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=40701
     Region          1..350
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqirelhk tygdypalhp tdltiengem aallgpsgsg kttllrliag lesadggqir
       61 lngrdvthvp vrerhigfvf qhyalfkhlt vadniafglt iqprrerpak arirekvaql
      121 ldmvqladmg srypaqlsgg qqqrvalara latepevilf depfgaldvq vrhdlrlwlk
      181 tlqrelrftg vfvthdreea leladrivvm rhgaiaqnad pqqlyaapad aqvfnfmsdt
      241 rrfparvenh ilhsgrgwak aeypiadgdg elalrvqdle lsghppghvq lpviiehstl
      301 lganyrltvk nqgwggdsrw qlplpaqtwl rqplhhgqrv ylkprrlyfl rtngavealf
      361 ral
//
LOCUS       WP_004144723             192 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Klebsiella].
ACCESSION   WP_004144723
VERSION     WP_004144723.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..192
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20818
     Region          4..188
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mtpriiigis gasgfqygvk alellrplai evhlvvskga ektceletdy rldevmalad
       61 vvhpinhlga sissgsfktl gmlvapcsmr slgaiahclt dnlltraadv vlkerrrlvl
      121 laretplnlg hirnmaavte mggiifppvp alyqrpqsad diithsvnra ldlfdlevnn
      181 iprwgegell yt
//
LOCUS       WP_004146562             122 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein, partial
            [Klebsiella pneumoniae].
ACCESSION   WP_004146562
VERSION     WP_004146562.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 122)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 122)
  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 122)
  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 122)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         <1..122
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          44..117
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(51,70..71,89,92,100..101,112,117)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 tltalgarlr qdrpaappae aigtppavsp gswrlhedkl ispdartlel tqqeyrlvel
       61 lmrnrnevcs kldlhaclfs hesepdlhri dvvvsrlrhk arqqgihlpv raifgkglaf
      121 is
//
LOCUS       WP_004135026             233 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Klebsiella].
ACCESSION   WP_004135026
VERSION     WP_004135026.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 233)
  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   3  (residues 1 to 233)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..233
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26825
     Region          27..231
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mtegtiktsk yeiiaifree lrkqaeievf vnnkstitql arvdfaefhi lttskiptgh
       61 kvkfilhsds gkiefcstlk ksyaggegkc rkvaftlpec iqvvqrrrdp rfrlrhehef
      121 fchgrhknge nylfeikdis dggcalmtks pnlkflshna ilknailala eygevtvdlv
      181 iknvvmvtld dneesdsyyq iscqfkfrhl dnkkriekvl ldlimeakrk krv
//
LOCUS       WP_004147404             241 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Stenotrophomonas].
ACCESSION   WP_004147404
VERSION     WP_004147404.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 241)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..241
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=25842
     Region          46..215
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mtasrlcrla afgllatsas apalaqtpal atsaddlaal lsrsapkadr hvlqlaaham
       61 rcalqrpelg ingdrlsvid ysrpsteprl wvfdlahqrl lfeewvahgr nsgenrtehf
      121 snrdgsfmss lgaftaqety mggngyslrl aglepgfndr areraivihg apyvnpataq
      181 lqgrlgrslg cpavrlsvak plidalrggt mvfayypdqd wlkhsqllgg ecggqgtlat
      241 r
//
LOCUS       WP_004149224             309 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Klebsiella].
ACCESSION   WP_004149224
VERSION     WP_004149224.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..309
                     /product="formate/nitrite transporter family protein"
                     /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=33913
     Region          37..288
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mdeldnnklk aeddereves eenqrgeeie vnedrlpsra maihehirqe gekemerdal
       61 allwsaiaag lsmgasllak gifhvklegi pggfllenlg ytfgfiivim arqqlftent
      121 vtavlpvmhn ptlgnvgllm rlwsvvlagn ligtavaawa fnympifdep trqafvsiae
      181 dvmknsptem fanaiisgwl vatmvwmfpv agaakivvii lmtwlialad tthivvgsve
      241 ilylvfngnl pwsdfiwpfa lptlagnicg gtfifallsh aqirndmssk rkaearaqaa
      301 ekgkkadra
//
LOCUS       WP_004151472             616 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase
            [Enterobacterales].
ACCESSION   WP_004151472
VERSION     WP_004151472.1
KEYWORDS    RefSeq.
SOURCE      Enterobacterales
  ORGANISM  Enterobacterales
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Enterobacterales"
                     /db_xref="taxon:91347"
     Protein         1..616
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=70458
     Region          58..503
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mnkispempe lqsmditadn itklkslfpe afsegsidfd vlkqllganv dekeerygln
       61 whgkrqarql altpsrgtlr pckdesvdwh ntknlmiegd nlevlkllqk syagkikliy
      121 idppyntgqd fiysddyrdn lskylnftgq vingnkistn tetsgrfhts wlnmmyprlk
      181 laknllhsdg fifvsidshe vsnlkiimdd ifgeecyrnt iavrrgiknv qaqfedvsal
      241 sqgheyilly sknslsrlpk lsqshleqkp gkwdtfwrgt drptmryelf gitpekgqwr
      301 weknrtaeai enyrfflekk sqqmslddwf fdnltstnkk lnfvrknded vvqyyvppsd
      361 gkilsdnwmd islsgnetif dtekntdlle riinwicrss ndivldffag sgttghavlk
      421 snsknnsnih ymliqlpeps nksefmtise ltkyrliesg kkvkdgnpdw ngdvgfrvfk
      481 ldtsnirpwe ataeslseqi dayvspileg rseedlltel mlkrgidlsv nietrqfdgl
      541 tvscvdggkl ftcfakqipa ssveeltkgi idwhkslkvg kdtvcyfldd afennvaktn
      601 lcaileqhgl tnlhsl
//
LOCUS       WP_004151497             188 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Stenotrophomonas maltophilia].
ACCESSION   WP_004151497
VERSION     WP_004151497.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas maltophilia
  ORGANISM  Stenotrophomonas maltophilia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas; Stenotrophomonas
            maltophilia 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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Stenotrophomonas maltophilia"
                     /db_xref="taxon:40324"
     Protein         1..188
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /function="Negative regulator of beta-lactamase
                     expression"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=21042
     Region          16..186
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mpnpllpglq lqplpyqdrl plrdpatlem vvihctelpd lamareyger vlydsgagns
       61 ghfyidrdgs vlqyvaperv ahhvrgmnah tlgielvntg rypywfdsrq qamdepytea
      121 qlqaleqlll alvarypslr riaghdqldl eqvpasddpa lmvarkrdpg plfpwarvla
      181 kvplqgle
//
LOCUS       WP_004154035             160 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Stenotrophomonas].
ACCESSION   WP_004154035
VERSION     WP_004154035.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..160
                     /product="GAF domain-containing protein"
                     /function="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16991
     Region          8..159
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfanasltgs kpeqyaqlle qarglvyaes drianaanls alvyhalpdl nwvgfylydg
       61 kelvvgpfqg lpacvripld kgvcgaaasq rvtqrvddvd afpghiacds asrselvvpl
      121 lrgdeligvf didspkvgrf daedqaglea iarvfvealg
//
LOCUS       WP_004156743             280 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Magnetospirillum
            molischianum].
ACCESSION   WP_004156743
VERSION     WP_004156743.1
KEYWORDS    RefSeq.
SOURCE      Magnetospirillum molischianum
  ORGANISM  Magnetospirillum molischianum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Rhodospirillaceae; Magnetospirillum.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Magnetospirillum molischianum"
                     /db_xref="taxon:1083"
     Protein         1..280
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30437
     Region          6..278
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mpdrkpalsy aasllrcddr erfltvlfap adcredlfal yalnvelsri reqarepmag
       61 lirlqwwrda llagqggagh plvaplreai rryhldpdll dglliarerd fdpdppadpd
      121 daeklaaagp vglgllalai lgankksgea ernavcavss awgvlghlrs iayhaalgrv
      181 tlpasllpkd gavailagra tgeslskatr tmaeraerhl iharsvnvmr ealpalltav
      241 qaktyaaalr rsnwnpfepr iarnrsrpla lawtvwrghl
//
LOCUS       WP_004157423             697 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Microcystis aeruginosa].
ACCESSION   WP_004157423
VERSION     WP_004157423.1
KEYWORDS    RefSeq.
SOURCE      Microcystis aeruginosa
  ORGANISM  Microcystis aeruginosa
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Microcystaceae; Microcystis.
REFERENCE   1  (residues 1 to 697)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 697)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 697)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Microcystis aeruginosa"
                     /db_xref="taxon:1126"
     Protein         1..697
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=71816
     Region          <208..>697
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 maisqevyas lnilyasqap sasdislwqt npsltslswe etvlvfansd aaketyplla
       61 apgaatdatr kqyvlevfnn ayglqeadld paeidywvew lsltnsdgsp adsdgngipn
      121 ildfpivlnq fqppaiqqal lnraevaldf aqqffqagia tfdqalydas wnvistvtad
      181 pasvtaaell taqavkdtig ggtgttftll dngavltaaa nskvapegkf lstandkvsa
      241 ltflngsfiq dpstsdndvl taqivgfvgp nienietiqf sgaagasval vgiskakqvq
      301 vvkgdltiid annyaidlva gyasnltlqe tvggkdltvn lkgttagasi tadlfdkskv
      361 nlvvkadsvl snadttkdtl sldqtesnfv itgdknltid gnitlvdgtn rldatdftgk
      421 ltlnlgknsf ikqivggksd dtftltadnn qidgvalngn ngndtltvkv gasaaaldkv
      481 tnvetiifke atvadttitt vdtlvgngat ltvdassftt ksltfkgaae tngsfkitgg
      541 akaddltggd radtltgggg ldnltgglgn dqfvlnqata gndvtitdfn iiagnndifa
      601 lsnaafagap avgaaltvsa vagatnsant ilvdtfanlt vdqtatglvr fgydttnnkl
      661 fydadgnfsa griliansan alslalglna snftiva
//
LOCUS       WP_004155918             133 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Erwinia amylovora].
ACCESSION   WP_004155918
VERSION     WP_004155918.1
KEYWORDS    RefSeq.
SOURCE      Erwinia amylovora
  ORGANISM  Erwinia amylovora
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Erwinia.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Erwinia amylovora"
                     /db_xref="taxon:552"
     Protein         1..133
                     /product="YqaA family protein"
                     /function="Predicted membrane protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14339
     Region          1..131
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mltssffsat llpgsseavl vglmladkis vsalvitaal gntlggltni vigrfipqkn
       61 qgrwhgtavl wlrrlgpaal lfswlpvigd llcvvagwlr fpwlpmvifl aigktlryil
      121 laaatlqgme wwh
//
LOCUS       WP_004157890             166 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Erwinia amylovora].
ACCESSION   WP_004157890
VERSION     WP_004157890.1
KEYWORDS    RefSeq.
SOURCE      Erwinia amylovora
  ORGANISM  Erwinia amylovora
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Erwinia.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 166)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Erwinia amylovora"
                     /db_xref="taxon:552"
     Protein         1..166
                     /product="GAF domain-containing protein"
                     /function="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18022
     Region          1..153
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mtkaefytel nrdmkallsg etsflavmgn csallyerle gvnwagfyll teentlvlap
       61 fqgkvacvri pigrgvcgta lsekrvqrvd dvhafpghia cdaasnaeiv lplvvnghvi
      121 gvldidsvey nrfdsedekg lkaltdglcd vlsgtdvekf ihmnrt
//
LOCUS       WP_004158916              96 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Microcystis aeruginosa].
ACCESSION   WP_004158916
VERSION     WP_004158916.1
KEYWORDS    RefSeq.
SOURCE      Microcystis aeruginosa
  ORGANISM  Microcystis aeruginosa
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Microcystaceae; Microcystis.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Microcystis aeruginosa"
                     /db_xref="taxon:1126"
     Protein         1..96
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10789
     Region          1..94
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mkrdkvlaii aahreqlqgl gvksltlfgs vardqarpds dvdflvefnr dvglfefiel
       61 rlyledilgc svdlgtedal rehlrepvlk dviyaf
//
LOCUS       WP_004159483             125 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [Microcystis].
ACCESSION   WP_004159483
VERSION     WP_004159483.1
KEYWORDS    RefSeq.
SOURCE      Microcystis
  ORGANISM  Microcystis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Microcystaceae.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Microcystis"
                     /db_xref="taxon:1125"
     Protein         1..125
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14372
     Region          29..118
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mimsvnnpyl eywqkrqkeq qeynqklaqe arknlppvid ylkenfpitk iilfgslvkg
       61 kfqetsdidl avagippesf fqalgkvnli sarwidlkpi edlephflkr vlqtgeclya
      121 sdecq
//
LOCUS       WP_004159450             440 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Microcystis aeruginosa].
ACCESSION   WP_004159450
VERSION     WP_004159450.1
KEYWORDS    RefSeq.
SOURCE      Microcystis aeruginosa
  ORGANISM  Microcystis aeruginosa
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Microcystaceae; Microcystis.
REFERENCE   1  (residues 1 to 440)
  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 440)
  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 440)
  AUTHORS   ter Beek,J., 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 440)
  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 440)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Microcystis aeruginosa"
                     /db_xref="taxon:1126"
     Protein         1..440
                     /product="CmpA/NrtA family ABC transporter
                     substrate-binding protein"
                     /function="16.1 : Circulate"
                     /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=47606
     Region          51..310
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 msklsrrrfi ftagatavgt ailhgcatpn ntatspspag spaaspaasg etpevttakl
       61 gfialtdaap liiakekglf akhgmpdvqv mkqaswaatr dnlelgsagn gidgshilsp
      121 mpylmtlgki tkqpvpmyil arlntngqai siskshadlk ldldssklke tltkaksagk
      181 emkaavtfpg gnhdlfmryw lsaggidpnn dislivvppp qmvanmkvgt mdafcvgepw
      241 naqivskglg ytalitgefw kdhpekafal radwvdknpk aakaltmavl eaqqwcndpa
      301 nvkemceiis grewlkidpa dilgrmqgni dfgdgrkien spvamkfwad nasypykshd
      361 twfvtedirw gyipadtdik alvdkvnred iwreaakaln vpadqiptst srgvetffdg
      421 vtfdpenpqa yldslkikki
//
LOCUS       WP_004159488             117 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [Microcystis].
ACCESSION   WP_004159488
VERSION     WP_004159488.1
KEYWORDS    RefSeq.
SOURCE      Microcystis
  ORGANISM  Microcystis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Microcystaceae.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Microcystis"
                     /db_xref="taxon:1125"
     Protein         1..117
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13507
     Region          24..113
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 msafptpeld kilkekdiqr eqqrqtllak tqqwlhenav kyginrayif gsvtrpykfh
       61 pgsdvdiave ninpalhfea isilsyylgr evdiillknc hfahrireeg ilwttdn
//
LOCUS       WP_004141763             210 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Cardiobacterium hominis].
ACCESSION   WP_004141763
VERSION     WP_004141763.1
KEYWORDS    RefSeq.
SOURCE      Cardiobacterium hominis
  ORGANISM  Cardiobacterium hominis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cardiobacteriales; Cardiobacteriaceae; Cardiobacterium.
REFERENCE   1  (residues 1 to 210)
  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 210)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 210)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Cardiobacterium hominis"
                     /db_xref="taxon:2718"
     Protein         1..210
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22656
     Region          4..198
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 mipttdrtde etvelirewl qqygltiiag lvlglgaigg yrywqnqqet qrlnesaqld
       61 tllqaleknd lqaaaapyda llkessdita laalnmasay qkadkkedaq talklaaasp
      121 dplvaqsarw qqalfqveng dydaalqsad alknsayapq aaalqglile kqnklpealq
      181 awqrsqelap spataaeina lqahlavken
//
LOCUS       WP_004160765             174 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Microcystis aeruginosa].
ACCESSION   WP_004160765
VERSION     WP_004160765.1
KEYWORDS    RefSeq.
SOURCE      Microcystis aeruginosa
  ORGANISM  Microcystis aeruginosa
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Microcystaceae; Microcystis.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Microcystis aeruginosa"
                     /db_xref="taxon:1126"
     Protein         1..174
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=17952
     Region          15..128
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mnstfkfkfi qalnkkngnk gftliellvv viiigvlaai alpnllsqia kgrqaeartn
       61 lgtvnraqqa nrletgsfat ftanagtvst gslpvsiepq yynytgptva dtlsavtgaa
      121 aisdftndir dysaavaqnt agvfrsiice adsptasvaa atsaascstg srir
//
LOCUS       WP_004174930             723 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Klebsiella].
ACCESSION   WP_004174930
VERSION     WP_004174930.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 723)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 723)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 723)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..723
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..723
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=82035
     Region          160..723
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mldkininik ktllafiicl vaiplarfis pqtiidgnli yiawlpisvm fsvififgry
       61 aiaplilafa itnsfliklt lpqafillfc qlfavfvsca ilrlmvgkrw rcgptakhmg
      121 arifwggffa pvllkitmyl agqyfafpla itsyfgsmpl iytvidiqsl isaalifttf
      181 lyypmrmiis pryarrfwqq eclpwlapqy rsftlywfia laviltllca pyqsefiagy
      241 lvpvifivyf igisrighal lriswsvsaf llvvynknfl qgvqseysls fvlsvlisft
      301 iclfymadiy arsdrnkrrw rsqaeedplt glpnlrales hlqscpqqai cslridnldf
      361 lsrhyglmmg vdckrqiira lqpllgaadk vfqvpgseli lvldgpepss rlnhmvavln
      421 hkkfswhnqp ldlefgaawg rddgqgegly qmlgqlswls eqagserrvl aldeeqdlvv
      481 dqtteqvrll mrvkqvlkdr almlyaqpiq npegegyhei ltrmrcgdsv impdrfipli
      541 vqfnlsqrfd mlvletlfsm lhkhpgqrfs vnllpatlmq knsagqiial fqrysvspel
      601 itievteeqa fsnadtsrqn lealrafgca iaiddfgtgy anyerlkhlq adiikidgcf
      661 vrdiltdpld aimvksivem arakqmsvva eyvesepqka rllelgvnyl qgyligkpqp
      721 lge
//
LOCUS       WP_004175561             418 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Klebsiella].
ACCESSION   WP_004175561
VERSION     WP_004175561.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 418)
  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 418)
  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 418)
  AUTHORS   ter Beek,J., 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 418)
  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 418)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..418
                     /product="CmpA/NrtA family 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=45863
     Region          38..289
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mgdkfsisrr rllqagaalg gamllpgvmq aawaggsdkp eqtrvrvgfi pltdcaplai
       61 aaakgfdqky gitlvaskea swaavrdklv ageldaahil ygllyglelg iaskpqaman
      121 lmtlnrngqa itlsselqek gvtdlgglkr lidrsapgsy tfahtfptgt hamwlyywla
      181 sagidpfndv rtvvvpppqm vmnmrignms gfcvgepwna raindrigft aatsqdiwpe
      241 hpekvlgtrr dwvernpnta ralvaalmea qrwiaaspen tretarllar rgwlntkeqy
      301 ltgrmlgeyd nglgrrwqda hpmrfwagge vsfpwlsdgm wfltqfrrwg llkqapdyla
      361 vasrinridv wqaaaqavgg isapaarmrs stlmdgtvwn gsdpegyarh fsiqrkga
//
LOCUS       WP_004177520              91 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Nitrosospira].
ACCESSION   WP_004177520
VERSION     WP_004177520.1
KEYWORDS    RefSeq.
SOURCE      Nitrosospira
  ORGANISM  Nitrosospira
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae.
REFERENCE   1  (residues 1 to 91)
  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   2  (residues 1 to 91)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Nitrosospira"
                     /db_xref="taxon:35798"
     Protein         1..91
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9720
     Region          17..>65
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkkllitlvt mlaftgaaha vvnintatqa elqtlpgiss arakaiieyr tkagafratd
       61 dlikvddtid mrdlrkdvti tgptlirpva k
//
LOCUS       WP_004178530             730 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Nitrosospira lacus].
ACCESSION   WP_004178530
VERSION     WP_004178530.1
KEYWORDS    RefSeq.
SOURCE      Nitrosospira lacus
  ORGANISM  Nitrosospira lacus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosospira.
REFERENCE   1  (residues 1 to 730)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Nitrosospira lacus"
                     /db_xref="taxon:1288494"
     Protein         1..730
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=78744
     Region          37..728
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mktplpdgcr vaslvtlafa sgfssaqpps qqtsypvass snaqptlnpv vvtgtrvdqs
       61 sfllpmsidv vespvirdgr plvnlseals rvpglviqnr qnyaqdlqis srgfgarstf
      121 girgirmivd dipatmpdgq gqaatinlgs vkrievlrgp fsaiygnapg gviqayteeg
      181 ppgtelsaml lggsygttra elklggtlga tgatgtgpfn yvvdisrfet hgyrdhsaaa
      241 ryqasaklty rfthdatltl vtnelhqggt qdplgltraq msvdprqadk sattfntrks
      301 idntqgglvy ehklspsnti kligyagtre ilqflaiprg aqipitssgg vvdlerqfgg
      361 lglrwthrts gprpltltmg idydsskerr kgfenfagtv lgvrgdlrrn enntvtsfgq
      421 yaqaewqfvp swilsagvrh tevkfksedf fsgtgnpdds ggmtfhnvnp vlgllykats
      481 slnlyvstgs gfetptfael ayrpdggsgl nfalrpsrsl nmeaglkwlp tgntrvnlal
      541 fqafvsgeil patnsggrat fqnaadttrr gvelsldsrf grdlsaflsy tyldavfqda
      601 ytyrptaaps rvtvaagnfl pgvprntaya eltwrrgqpg fsaaveaiyr drifvndint
      661 eaakqyaman lrlayshqfg gwkftefvrv dniadtkysg svivnegngr fyepapgrny
      721 mvgvsasytf
//
LOCUS       WP_004179177             409 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Klebsiella].
ACCESSION   WP_004179177
VERSION     WP_004179177.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 409)
  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 409)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..409
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47288
     Region          1..405
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 msvlqlslne arhlhlaaqg llkkprrrar pkdilstiqq msllqidtin vvarspylvl
       61 fsrlgsypqh wldeslrnge lmeywaheac flprsdfalv rhrmlnpdnm gwkyhrawme
      121 ehagsiaelv ahigqngpvr sadfthprkg asgwwewkph krhleglfta gevmvverrn
      181 fhrvydltrr vmpdwdderd alshedaeai mlrnsarslg ifraqwlady yrlrqpalpg
      241 llaawqeegl vvpvnvealg emwlhhkala qletapggkl tashsavlsp fdpvvwdrkr
      301 aeqlfnfsyr lecytpapkr qygyfvlpll hqgklvgrmd skihrksrel eifalwleeg
      361 vkitrgleqg lrraindfah wqsaerilcr rlpeglfvgq eqgweidad
//
LOCUS       WP_004183189             103 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Klebsiella pneumoniae].
ACCESSION   WP_004183189
VERSION     WP_004183189.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..103
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11369
     Region          5..101
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(7..8,26..27,35,38,40..41,43,46..47,49,57,62,69)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(26,57..58,60,84)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mapydtfpqr vwhivasipe gyvttygeva rlagspraar qvggvlkrlp egstlpwhrv
       61 vnrhgdislt gpdlqrqrqa llaegvqvsg sghidlqhyr wvy
//
LOCUS       WP_004185094             206 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Klebsiella pneumoniae].
ACCESSION   WP_004185094
VERSION     WP_004185094.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 206)
  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 206)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 206)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..206
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22231
     Region          1..204
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 metfnnendq vdalkrffae ngkalavgvi lgigalvgwr ywtshqqdta rdaslayeka
       61 tsalksntpe vlsgaekfaa dnkntygafa slelaqhfve qndlpnaekq lqqglaaasd
      121 dnlksvismr larvqlqmkq vdaalktlds ikgegwtaiv adlrgeills kgdkqgaraa
      181 weagvksdas palsemmrmk mnnlsi
//
LOCUS       WP_004185652             299 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Klebsiella pneumoniae].
ACCESSION   WP_004185652
VERSION     WP_004185652.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 299)
  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 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   3  (residues 1 to 299)
  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   4  (residues 1 to 299)
  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 299)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..299
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33493
     Region          28..179
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          207..288
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqhaeicrtl tgkinllkdk hemlssllpd vrllygtqpg prtpvmyqpg ivflfsghki
       61 gyinertfry dtneyllltv plpfecetfa tpevplagmr lnvdilqlqe llmdigedpl
      121 fqpavassgi nsavlsedil caaerlldvm erpldarilg kqivreilyy vltgpcggal
      181 lalvsrqthf slisrvlkhi esqytenlsv drlaaeanms vsafhhnfka vtstsplqyl
      241 knyrlhkarm lmihdgmkas aaamrvgyes psqfsrefkr yfgltpgeda arirtmqgm
//
LOCUS       WP_004188108             191 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Streptococcus
            sanguinis].
ACCESSION   WP_004188108
VERSION     WP_004188108.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sanguinis
  ORGANISM  Streptococcus sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 191)
  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 191)
  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   3  (residues 1 to 191)
  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   4  (residues 1 to 191)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 191)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Streptococcus sanguinis"
                     /db_xref="taxon:1305"
     Protein         1..191
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21443
     Region          1..190
                     /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"
ORIGIN      
        1 mkgrilivdd dpiirldirn ileaadyevv aeasdgfeai dlcqkyrcdl vmmdiklpll
       61 dgltagkkil edalaysvil lsaysdehyv qkaktngisa ylvkpldaks lipmvevcie
      121 kgrqlqqmsn emvklskkid driviekakg llmardhlse peafkrirti smqkrvpmie
      181 iakllvlqdd v
//
LOCUS       WP_004188202             290 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [pseudomallei
            group].
ACCESSION   WP_004188202
VERSION     WP_004188202.1
KEYWORDS    RefSeq.
SOURCE      pseudomallei group
  ORGANISM  pseudomallei group
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 290)
  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 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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="pseudomallei group"
                     /db_xref="taxon:111527"
     Protein         1..290
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31435
     Region          43..281
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <183..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 mmtllavppe klsaasaast aagptpaagn gacasppssg aalegdddgf aamlahfaql
       61 epvfdalpdv affvkdvrar yalvnrtlaq rcgykdkrdl ygkaadevfp rrfgrsyveq
      121 dltiiaggrq ltdqlelhly sgrqpgwclt ckeplrnaqg rivgiaglsr dlrahesshp
      181 aysriadvvr yihahyvqpl nlkhlagmag msvaqleryf hkvfhltprq mllkarldaa
      241 tallvthdkv tdvaalcgyt dhsaftrqfk atvgvtptey rlmlqegrga
//
LOCUS       WP_004189725             105 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Burkholderia].
ACCESSION   WP_004189725
VERSION     WP_004189725.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (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   2  (residues 1 to 105)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..105
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10288
     Region          22..78
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mlkkllataa lcaaaahgwa avdvnaandd alrgirgigp akakaivder sahgpfkdaa
       61 dlarrvkgmg gktverlqae glaigaarap aaagapqkaa aagkk
//
LOCUS       WP_004190127             292 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Klebsiella].
ACCESSION   WP_004190127
VERSION     WP_004190127.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..292
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32334
     Region          13..255
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mrievlldlk trlgespvwd veqqrlwwvd sldgrlfacn aqggaikswd vrqkigsfal
       61 rqsgegavva lqngvhlldf asgeltllhh peadrpfnrl ndgkvdrqgr flfgsmdmre
      121 eepsgalyrl dpdlslhvlk kdiivsnapc wspsgetfyf adtwtgeica wdyntatgdl
      181 sgervfchvd rseggaadga tvdsegylwn alvyagklvr ytpegkvdri iempvkkvts
      241 vmfggenldv lyvtsmaqpp lprfpednql rgslfaiydl gvtgvaerrf ag
//
LOCUS       WP_004190629             350 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [pseudomallei
            group].
ACCESSION   WP_004190629
VERSION     WP_004190629.1
KEYWORDS    RefSeq.
SOURCE      pseudomallei group
  ORGANISM  pseudomallei group
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 350)
  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 350)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 350)
  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   4  (residues 1 to 350)
  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 350)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="pseudomallei group"
                     /db_xref="taxon:111527"
     Protein         1..350
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39166
     Region          33..216
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          264..342
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtrrstkdnl glrrptipva ylrhlltvfe ergidardar agtglrddvl gepdariaps
       61 qwgrlvlnai rlsgdegigf elglrlrmsv hgflgyaalt aadlrasllv naryfrmrnr
      121 qyrlhyaerd dgatlslhgv qaspvlqhha mfeivltgia qnvgtvagra dppielqfaw
      181 pepdyyaryr drlppvrfgc aanavwvsrd aldwplplad dvahrqalaq vereyadvrh
      241 eegdlvarvr aeltltahgy pgpdalarrl lmstrtlrrr lldagcgyra lvdearlrda
      301 rrllrasdld lktiaarlqf ndpanftraf rkwtgltpsa yreagggder
//
LOCUS       WP_004175366             805 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Nitrosospira lacus].
ACCESSION   WP_004175366
VERSION     WP_004175366.1
KEYWORDS    RefSeq.
SOURCE      Nitrosospira lacus
  ORGANISM  Nitrosospira lacus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosospira.
REFERENCE   1  (residues 1 to 805)
  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 805)
  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 805)
  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   4  (residues 1 to 805)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..805
                     /organism="Nitrosospira lacus"
                     /db_xref="taxon:1288494"
     Protein         1..805
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89447
     Region          86..803
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mpisnlfpad lrltidpdsl gfsdssellq yplpwigqer aemaarfglg mdqpdynlfv
       61 lgevgsgrss llrqtmvaaa amrstppdlc ylhnfdaper plalrlpagq grllrqllar
      121 ltksllmeip qrlggqdfkv gserikkayk aeeakaytel tafaeshdft ihregghivf
      181 tllgekghil tedevltlpk arrveieqae qelhaeitry fekirpmerv mnealaalqr
      241 qvvkpllese sqeiraglrk qikdsvklgs yleqvmedvl gnlelfkvsd tdeegrqeel
      301 ervmsryrvn lvvdndglng apvivednpl fhslfgsiey qsendvlatd ftriragsll
      361 rahggflmlh lrdlladalv weklrrllrs drlqieepgt aftsitavsl vpeavdvevk
      421 ivligsrqqy ydlqeadpef arrfrvkvdf aesflasaet rrasaifvah acrelglphf
      481 taaavaclle dshrqvddql rqsaifarae alvmesaalc qaraghrvda edveaalrar
      541 vlrhdypeqr lqesiaegdv litlngekvg qlnsltqvdl gdyrfgfpvr vtartfaged
      601 gllniereve msgpihdkgv filqnylsal fvhaaplaln asivfeqeyn gmegdsasca
      661 elyvllssls dlplkqgiav tgavnqhgev lpvggvneki egyfsvceta gldgshgvli
      721 parnrrhlml erkvveavag nlfhiytaeh asegvqlltg fpagmadetg nyphdsvlgr
      781 ahqtllayrr acqesqrpkv rrkrs
//
LOCUS       WP_004146835             411 aa            linear   BCT 20-JAN-2025
DEFINITION  TerD family protein [Stenotrophomonas maltophilia].
ACCESSION   WP_004146835
VERSION     WP_004146835.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas maltophilia
  ORGANISM  Stenotrophomonas maltophilia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas; Stenotrophomonas
            maltophilia 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 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Stenotrophomonas maltophilia"
                     /db_xref="taxon:40324"
     Protein         1..411
                     /product="TerD family protein"
                     /function="Uncharacterized protein involved in stress
                     response"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=43717
     Region          28..411
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mtslmaggnc vlpgddfevr vrwisakasl sevdvsafvl gntgkvasds dmvfygqttd
       61 ssgavrlket nragsagare alldidlrkl rgesekvait stlmdaqakg vsfkdlqslv
      121 isiyhggseq isfdvpvagk seaalivgef ykrngqwkfr avgqgfnggl kplaegfgvs
      181 ieaepksppp paapapspat ppppptapvn lskitltkaq pkinlakqgg afgeikinln
      241 wnkrtaskgl lagifgggsg idldlrclfe lkdgskgavq algrvfgdfd rapfirlmgd
      301 drtganndge wmringarwd dikriivfts iyegvtnwge tdgvvtvfvp gnapievkld
      361 egashsrnca ivllenigge isvkrevqyf asepdidqrf gwglrwsags k
//
LOCUS       WP_004192434             351 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [pseudomallei group].
ACCESSION   WP_004192434
VERSION     WP_004192434.1
KEYWORDS    RefSeq.
SOURCE      pseudomallei group
  ORGANISM  pseudomallei group
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="pseudomallei group"
                     /db_xref="taxon:111527"
     Protein         1..351
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38090
     Region          1..350
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mgitvrnlhk rfgefaaldd vsldfpagel vallgpsgcg kttllrviag lehadsgqvv
       61 lqgldvasvg arerqvgfvf qhyalfrhmt vfenvafglr vkprrerpse aairakvhel
      121 lslvqldwla qrypselsgg qrqrialara lavepkvlll depfgaldak vrkelrgwlr
      181 rlhddlhist ifvthdqeea levadrivvl nhgrveqvgs pqavydhprs afvyeflgaa
      241 nrldgtvsgn gfvahgaaqa iavdadfagp arayvrphdl elaapharaq giaadvrrvv
      301 plggsvrvel aarsgevlea eldrnawral aldvgdalta vpravrvfpa r
//
LOCUS       WP_004185114             365 aa            linear   BCT 20-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Streptococcus
            sanguinis].
ACCESSION   WP_004185114
VERSION     WP_004185114.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sanguinis
  ORGANISM  Streptococcus sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 365)
  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 365)
  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 11443421
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Streptococcus sanguinis"
                     /db_xref="taxon:1305"
     Protein         1..365
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=38225
     Region          <4..95
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          51..95
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
ORIGIN      
        1 mkmnkkllla stvalsalpl lttraeeqpq nwtartveqi kaditsnenq qtytvqygdt
       61 lgniaqamni dlvelakinq ianadlifpg tvltvttngq neiasveiqs yqagnnagyv
      121 tesytadeif gteqaapatp aqpaetpapa veeavaapad qapapaeeap apvaevasea
      181 apaaeenaaa pveaapqpav aaspeapaea asevtelgqd qvsqataave pttynapavt
      241 daasvttnnp aneglqpqta alkeeiaaky gitefslyrp gdsgdhgkgl aadfivgent
      301 elgnrvaadv tsnmtergis yviwqqqfya pfesiygpan twnqmpdrgs vtenhydhvh
      361 vsmne
//
LOCUS       WP_004199750             616 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Klebsiella pneumoniae].
ACCESSION   WP_004199750
VERSION     WP_004199750.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..616
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=70504
     Region          58..538
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mikitsdmte lqsmnitedn isklkslfpe afsegsidfd vlkqllganv dekeerygln
       61 whgkrqarql altpsrgtlr pckdesvdwd ntknlmiegd nlevlkllqk syagkvkliy
      121 idppyntgqd fiysddyrdn lskylnftgq vingnkistn tetsgrfhts wlsmmyprlk
      181 laknllhsdg fifvsidshe vsnlkiimdd ifgeecyrnt iavrrgiknv qaqfedvsal
      241 sqgheyilly sknslsrlpk lsqshleqkp gkwdtfwrgt drptmryelf gitpekgqwr
      301 weknrtteai enyrfflekk sqqmslddwf fdnltstnkk lnfvrknded vvqyyvppsd
      361 gkilsdnwmd islsgnetif dtekntdlle riinwicrss ndivldffag sgttghavlk
      421 snsknnsnih ymliqlpeps nksefmtisd ltkyrliesg kkvkdgnpdw ngdvgfrvfk
      481 ldtsnirpwe asaetlsqql dayvspileg rseedlltel mlkrgidlsv nvetrqfdel
      541 tvscvdggkl ftcftrqipa ssvevltkgi idwhkslkag kdtvcyfldd afennvaktn
      601 lcaileqhgl tnlhsl
//
LOCUS       WP_004200476             424 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Burkholderia].
ACCESSION   WP_004200476
VERSION     WP_004200476.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 424)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..424
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=46280
     Region          35..254
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 msmididpps fqsprpiagd dgnrrtvlyg dytvfsvfqp vfsvshrrai gyhaslrahd
       61 sqsnqvpshe vftqaarrgd llelgrlaes lhlgnfhtfd shdewlflsl hpaalmdtvy
      121 gdallanlka lglppqrvvl evpeqagget prfaaivdgl rkagflialg gfgakhsnid
      181 rvwhlhpdiv tldrgilaqa sehshlervl pglvsllhes gqlvlmggit terealiale
      241 cdvdfvqgqy fagpsvepvq pqaaagvmdt lsaalrlrva ertraqqarl apyvaallqa
      301 sallregrdl teaskellel peaarcflld asgrqigdnv lprvhasqra krfspllhse
      361 gaswerrpyf ieamrvpgra hftppylsin eahlcvtasi atpavqgmqv lcvdinweaa
      421 ahrd
//
LOCUS       WP_004203282             402 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Klebsiella].
ACCESSION   WP_004203282
VERSION     WP_004203282.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 402)
  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 402)
  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
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 402)
  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   5  (residues 1 to 402)
  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   6  (residues 1 to 402)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 402)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 402)
  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 15726307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..402
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43196
     Region          16..>132
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          79..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 mktsgtnleh arvhnrrvii eavrlhgelt raelarltal tpqtvsniva eleqmdllts
       61 hqprrasgrg qpavpvslnp asawsigihl dhqtlivvlv dltgevhfrr lilvqkpqpg
      121 atfarlaevl deiralpald wsrvlgmgvv mpgpfgvegi sstgpttlng wegvdvaael
      181 grlsglpvtl endatvaaig erfhgvarql nsfvylyigt glgagiftdg hvytghahna
      241 gevghivvap ngrpcycgne gcleryvslq aayefcgldp yralpedlls vdaalfdqwi
      301 tsilaplrqa inllecvfda etvvvggmmp apllervlar lpplyqsvrg rylpaqrvkm
      361 gmtgtdtaal gaaalpifde fnpqfqvlmk avntnalfgk ak
//
LOCUS       WP_004192617             365 aa            linear   BCT 20-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Streptococcus
            sanguinis].
ACCESSION   WP_004192617
VERSION     WP_004192617.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sanguinis
  ORGANISM  Streptococcus sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 365)
  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 365)
  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 11443421
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Streptococcus sanguinis"
                     /db_xref="taxon:1305"
     Protein         1..365
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=37941
     Region          <4..95
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          51..95
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
ORIGIN      
        1 mkmnkkllla stvalsalpl lttraeeqpq nwtartveqi kaditsnenq qtytvqygdt
       61 lgniaqamni dlvdlakinq ianadlifpg tvltittngh neitsveiqs yqagnnaglv
      121 tedytaseif gteqaapaap aqaaetpapa veeavaapae aapapaeeap apvaevasea
      181 apaaeanaaa pveatpqpav aaspvapaea apevtelgqd qvsqataave pttynapavt
      241 daasvatnns anaglqpqta alkeeiaaky gitefslyrp gdsgdhgkgl aadfivgent
      301 elgnqvaadv tsnmtergis yviwqqqfya pfesiygpan twnqmpdrgs vtenhydhvh
      361 vsmne
//
LOCUS       WP_004208492             286 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Sphingobium].
ACCESSION   WP_004208492
VERSION     WP_004208492.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..286
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31350
     Region          16..257
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mtawrkierg eirdtlgegt lwsarenavy wvdilapaln rlslddgqvs rwampeplgw
       61 vaeraqggfi ggfqsgfasf tldplaitpi hdpephlpgn rmndgkadkd griwcgtmdm
      121 aegqdvgaly rldpdgsvtv mddgyrvpng pafsacgeyl yhsdtgrrim yrfrrgpdgt
      181 ihdrqpfitf teadghpdgm tvdaegylwv ahwggsrisr fspegkldra ielparqvtn
      241 itfagpdldr mfvssaaigl pesdydgaff evecgvkglp tnlygg
//
LOCUS       WP_004209681             276 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Klebsiella].
ACCESSION   WP_004209681
VERSION     WP_004209681.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..276
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=31143
     Region          43..189
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkrmmrivll allltgcage kgiidrdgyq ldtrhpaqaa yprikvlvih ytadnfdvsl
       61 atltdkevss hylipeqppr yqhkpriwql vpeedlawha gvsywrgstr indtsigiel
      121 enrgwqktag vksftpfhpe qiaaliplar diiaryhiap qnvvahadia pqrkddpgpl
      181 fpwqqlaqqg igawpdeqrv afylngrpas epvdpeivld llsrygyqvt pemtpaqkkr
      241 viiafqmhfr pqrwdgvada qteaiaeall ekygqg
//
LOCUS       WP_004212182             161 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Sphingobium].
ACCESSION   WP_004212182
VERSION     WP_004212182.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 161)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..161
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16944
     Region          8..160
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mydfapaada dkatlyadll saadaltrde pdavanmanl saliwqflpd lnwagfyrmv
       61 edelvlgpfq gkaaciripl grgvcgtaaq tretqlvadv hafpghiacd aasaseivvp
      121 vvhdgrligv ldldsprpar fdsadqqgle alvarvagri g
//
LOCUS       WP_004209851             486 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: amidohydrolase family protein [Sphingobium].
ACCESSION   WP_004209851
VERSION     WP_004209851.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 486)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..486
                     /product="amidohydrolase family protein"
                     /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=51879
     Region          29..463
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mktllaalla atallplpaa aktaparadl lirhatlvdv ehgrlvpdqa vatrgdriva
       61 vgndatiaaa wragknvear grylipglwd mhvhfgggpe lieenkallp lyiangittv
      121 rdasgdlpyd vlrwrgeiad grlfgptlls sgpkiegikp vwkgtletgs eadvdqaiak
      181 lkelnvnfvk itdstlkpdl flyavrkarg aglrasghip maltvgqaie agissiehid
      241 yahkagvkde aritadfaag ridraqasaq ldagfdeata maayrdmaar gvfvtptlsi
      301 srtvayldqn dhsadpelay igprlrktyd wrieraakat pdqiaqrhai yehnaailpl
      361 lqqagvtima gtdagflnsf dypgfalhqe lalyvdrglt paqalasatr agpawfglld
      421 rygavaegkq admvlltanp ledihatkai davilrgtlq drarldalla etkakvaawn
      481 aaatrp
//
LOCUS       WP_004206117             495 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [Klebsiella].
ACCESSION   WP_004206117
VERSION     WP_004206117.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..495
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=53843
     Region          1..495
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mqyikihsqd nvavaladmt agsvvtidnd pvtlgqdivr ghkfalraia kgenvvkygl
       61 pighaladia pgehvhahnt rtnlsdlday ryqpeqvaqp pqpadrdvqi yrrangdvgv
      121 rnelwilptv gcvnamarqm qnrflkeang aedidgvhlf shtygcsqlg ddhlntrtml
      181 qnmvrhpnag avlvvglgce nnqveafret lgeydpqrvh fmvcqhqdde veagvahlhq
      241 lydvmrqdkr qpgklselkf glecggsdgl sgitanpmlg rfsdyviang gttvltevpe
      301 mfgaeqllms hcrdeatfdk lvtmvndfkq yfiahdqpiy enpspgnkag gittledksl
      361 gctqkagssq vvdvlryger lkvhglnlls apgndavats alagagchmv lfstgrgtpy
      421 ggfvptvkia tnselaakkk hwidfdagql ihgkampqll eefvdtivaf angkptcneq
      481 ndfrelaifk sgvtl
//
LOCUS       WP_004212504             193 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Sphingobium].
ACCESSION   WP_004212504
VERSION     WP_004212504.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 193)
  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 193)
  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   3  (residues 1 to 193)
  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   4  (residues 1 to 193)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 193)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..193
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=20922
     Region          1..191
                     /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"
ORIGIN      
        1 mriviiddsg lratvleegl reagyddihi vpprgafvar lermapdvvl mdlgspsrdt
       61 leemltvsra larpiamfvd qsddamigaa idagvsayvv dglrkervkp vlelavrrfn
      121 afarmqseld eartaladrk iidraksilm nqrslseqda yallrssamn qgkkivdvaq
      181 alitasdllg ggi
//
LOCUS       WP_004213337             317 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Klebsiella pneumoniae].
ACCESSION   WP_004213337
VERSION     WP_004213337.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (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   2  (residues 1 to 317)
  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 317)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..317
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34588
     Region          17..70
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mstkltgyvw dacassgmkl ssvaimarla dfsndegvcw psiatisrqi gagestvrta
       61 iaalekegwl trtqrrngnr nasnvyqlnv sklqkaafsh lsvsdtsksd asksdaskid
      121 pskfdasesi nktgfdpses ggdpsvkstt dpsdinpscp dasqpdeqgs adeflsrhpd
      181 avvysaakrq wgsqddltca efiwgkiism ydlaaesdge vvrpkepnwt awanevrlmv
      241 mqdgrthkqi cslfkrankd sfwcknvlsp sklrekwdel slklsaplns srqessisra
      301 sfdgvdyslp ensgfrt
//
LOCUS       WP_004214074             309 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Klebsiella pneumoniae].
ACCESSION   WP_004214074
VERSION     WP_004214074.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..309
                     /product="formate/nitrite transporter family protein"
                     /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=33822
     Region          37..288
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mdeldnnklk aeddgreves eenqrgeeie vnedrlpsra maihehirqe gekemerdal
       61 allwsaiaag lsmgasllak gifhvklegi pggfllenlg ytfgfiivim arqqlftent
      121 vtavlpvmhn ptlgnvgllm rlwsvvlagn ligtavaawa fnympifdep trqafvsiae
      181 dvmknsptem fanaiisgwl vatmvwmfpv agaakivvii lmtwlialad tthivvgsve
      241 ilylvfngnl pwsdfiwpfa lptlagnicg gtfifallsh aqirndmssk rkaeahaqaa
      301 ekgkkadra
//
LOCUS       WP_004216865             363 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Klebsiella pneumoniae].
ACCESSION   WP_004216865
VERSION     WP_004216865.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..363
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41647
     Region          191..343
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mkqfinkilg kkltgklrli kescnaqlvh tcsktrflss lyyfafnssf krenqsvlhg
       61 khlykesltq vgrssallrr nihrlekgli mrprreifak dyiletveqf krcvalntie
      121 rnemewaydv lteyfdsiii ngeksvekay hifskassvy lernrslskd fkfipysres
      181 slqsnisyee lkklflqrrs vrwfdqdkkv eaqslmdaie laslapsacn rqpfkfyftv
      241 dqnkareiak ipmgtagfad nivalivivg dlsyypyerd rhviyidasl aamqlmlale
      301 tlglsscpvn wpdiesfevk mekklgltkn lrpiillpvg yadltglips sskksssela
      361 vqi
//
LOCUS       WP_004217836             555 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase family protein [Bifidobacterium].
ACCESSION   WP_004217836
VERSION     WP_004217836.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 555)
  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 19384773
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..555
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=59005
     Region          <23..>120
                     /region_name="PknB_PASTA_kin"
                     /note="Stk1 family PASTA domain-containing Ser/Thr kinase;
                     NF033483"
                     /db_xref="CDD:468045"
     Region          137..252
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          413..553
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mtfpsgnggf ssngasnqvp sdasdmrdfe stqvftpmqd vplppqlpqq hdsnagmngp
       61 aagkrhhvwp wivlalvvvl agacaglvaf fntralpgtt lwgvdvsgkt qqqiaqaisn
      121 evdgtkipvs yegktgsvtl adlgvkvdaq qiaqeavdak rhenvfarya pwakhdvnpa
      181 idakdanpea ldeqlgtnsv kpvdaklqvg ddgstiavie gteghgadpt etaneavrvv
      241 qslgaqepkt vevqlktisp aittdeanka kstldklmaq kpgvyigker faaftpsmil
      301 aattidpngn gtlpqgqirn gnvvydatal qkaydeqikp nikstkedre vivnnngtei
      361 evikeghdgv tlddgadani gtkaidafgk gngtvsvsgk ldpmkvketk rhvvvdlsdh
      421 tvtalengna vktmhmsagq gndyatgkcq asgdmctpeg dfeiwlkyps qnmsgtltls
      481 dgkketwdvk nvgfvnyfsk sgcaihriat qtpytdaqiq algentshgc vgigwdmaew
      541 fynwcvdgts vhvqq
//
LOCUS       WP_004218335             242 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease family protein [Bifidobacterium].
ACCESSION   WP_004218335
VERSION     WP_004218335.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..242
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=26233
     Region          91..227
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 marrfkrkyg vtplerilii lliavvvgat lgvilprinn giaeitgryt atgtaaetln
       61 klavvdrpng dgydrdlfgf retdddgngc dvredilard ltdvayvtrn gckvksgvln
      121 dpytgkvihf trgqntsaav qidhvvalqn awqsgakdwn arkrmqfand pynllavdgp
      181 anqgkgsasa aywlptnasy rcdyvarqig vkdkyglsvt ssekramqsv lhgcpgqeip
      241 ad
//
LOCUS       WP_004218679             401 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator
            [Bifidobacterium].
ACCESSION   WP_004218679
VERSION     WP_004218679.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
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
REFERENCE   3  (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   4  (residues 1 to 401)
  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   5  (residues 1 to 401)
  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   6  (residues 1 to 401)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 401)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 401)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..401
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42795
     Region          11..74
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          79..375
                     /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 mnsrttteqq tlseynrart lqylhhhgia sraqiakalh ltpaalskis nhllasgaiv
       61 etgalegkgn rrsiglavna rafqvlgvkf arslieiglf dlagkpsfir elptventti
      121 pqaieslhae irrllaehph ilaigmavpg pylrdrghta vvssmgqwrq vnfraefeha
      181 fdvpviieqd aragalaqyl fdpnpanenl ayyllgegig lgvidhgtvi ngslgaatei
      241 ghvsidvngk acdcgnvgcl erycsavaih eamlgngmla tdsrlthrea caelfaraqs
      301 gdgqarelve rigtfvgygc vticnafnps rivigdivaq agepllqrvr evvgervipe
      361 itqstqiels alptdaavtg aaavaityil dhpsqffasg t
//
LOCUS       WP_004218991             208 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LytR C-terminal domain-containing protein
            [Bifidobacterium].
ACCESSION   WP_004218991
VERSION     WP_004218991.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 208)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..208
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=22461
     Region          83..167
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 maenndaree rreyvhrrqt ivfavvgavl vvalfisslf lfhvgglgev kttaegadhg
       61 vvapcvspae dgskpkylds ksvttrvlng tkfsgfanav gralqnrefv vqsidnydna
      121 kverttivfg knaipqaytl aanfpdaqlq mddrqdklvd vilgatfqnl tktdelpktg
      181 seipniegck pandmkdlpk apehtsvg
//
LOCUS       WP_004209930             122 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: endonuclease domain-containing protein [Sphingobium].
ACCESSION   WP_004209930
VERSION     WP_004209930.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 122)
  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 122)
  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   3  (residues 1 to 122)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..122
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=13740
     Region          18..116
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mrnyrdlpsg avdqaralrr nateaekrlw ralreqlptv kfrrqvphga yvadflcfsg
       61 klvvevdgas haesaeqdav rtryfetqgy qilrfwnhev mentegvvav iaarlspsps
      121 ha
//
LOCUS       WP_004220707             162 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Bifidobacterium pseudocatenulatum].
ACCESSION   WP_004220707
VERSION     WP_004220707.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium pseudocatenulatum
  ORGANISM  Bifidobacterium pseudocatenulatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Bifidobacterium pseudocatenulatum"
                     /db_xref="taxon:28026"
     Protein         1..162
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=16884
     Region          23..135
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mraatfpegk kdsimksvrn alnrrakgek gftlvellvv viiigilaai svpiylnqrk
       61 sawnsqtesd vknaslvvet astanngklp seingatatc sksqntgctl ggntitvteg
      121 vtlkitgkad nsytiegene nsgtaiflyd sangvvsktg tk
//
LOCUS       WP_004221728             560 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase family protein [Bifidobacterium].
ACCESSION   WP_004221728
VERSION     WP_004221728.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 560)
  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 19384773
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..560
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=59996
     Region          54..>87
                     /region_name="fliL"
                     /note="flagellar basal body-associated protein FliL;
                     Reviewed; cl00681"
                     /db_xref="CDD:469875"
     Region          129..234
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          405..558
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mslndmdspe sgngkfafpn mgdepkvisq vsldsfaeta dsiddgaalt vnaskkrhll
       61 wlwivlavml llgavagggy wffqshalpg vtlwgksmtg qsrdhiiqei sdtaesltvp
      121 vsyegtskkv tlkdlgvaid aesiaenvmn akrddsffqk yafwtredvd vesfddsrvs
      181 aqtvgdmlgv qsvsatnpsl qlnadgtafd vtpgqqgtgi dvtdivkeak nvlesfgkqt
      241 aqmvtlknkv tdpaitddqa neakasadaw iakpvaikig dhkvaefgaq siasaitlgp
      301 dseklgdnqt rngsliidgd klqqyyndsi ksnfhadrvd gdvivnsvgd vlqtnvaghd
      361 gitvtdgsdt nvgrdaaeaf akgsdsvsiq gtcdpqnekk ttrtvvvsls shtvtaieng
      421 qtvrvmhmsa gqgndyqtgq cqpsgdlctp tycdpnsydn ctpdgdfkvw lkyqsqdmsg
      481 tltlsdgnte kwdvkdvgfv nyfsktgcai hriatqsafn dssiqamgkn tshgcvgvgw
      541 dqaewfynwc lmgttvhvqa
//
LOCUS       WP_004219915             313 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CHAP domain-containing protein [Bifidobacterium].
ACCESSION   WP_004219915
VERSION     WP_004219915.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..313
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32825
     Region          180..313
                     /region_name="COG3942"
                     /note="Surface antigen [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443142"
ORIGIN      
        1 mrhaahkaak vsnerfsvak alftssrgsh takavrmvql angggavvgl epavaeklne
       61 vapmsrramr eaaraagrrs afmasaslaa lvgtaatama vgqqnasemt fadnattttq
      121 mkrvsddaas rsesrsdlda lastsnsgdw qlgetsssmd tnllsksiad npnvavlmdq
      181 dagllpsgfn pnhgtgdtgn dypygqctww aytrraqlgl pagshfgdar swgdsaralg
      241 ywvdntarhv gdivvfapgq mgadsyyghv aivegvnadg sikisesnvr glgvisdrtf
      301 taqeasqlty ihy
//
LOCUS       WP_004220507             426 aa            linear   BCT 20-JAN-2025
DEFINITION  galactokinase [Blautia hansenii].
ACCESSION   WP_004220507
VERSION     WP_004220507.1
KEYWORDS    RefSeq.
SOURCE      Blautia hansenii
  ORGANISM  Blautia hansenii
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Blautia.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   McAuley,M., Kristiansson,H., Huang,M., Pey,A.L. and Timson,D.J.
  TITLE     Galactokinase promiscuity: a question of flexibility?
  JOURNAL   Biochem Soc Trans 44 (1), 116-122 (2016)
   PUBMED   26862196
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Holden,H.M., Thoden,J.B., Timson,D.J. and Reece,R.J.
  TITLE     Galactokinase: structure, function and role in type II galactosemia
  JOURNAL   Cell Mol Life Sci 61 (19-20), 2471-2484 (2004)
   PUBMED   15526155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Blautia hansenii"
                     /db_xref="taxon:1322"
     Protein         1..426
                     /product="galactokinase"
                     /EC_number="2.7.1.6"
                     /GO_function="GO:0004335 - galactokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0005534 - galactose binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0046835 - carbohydrate phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=47079
     Region          36..411
                     /region_name="GalK"
                     /note="Galactokinase [Carbohydrate transport and
                     metabolism]; COG0153"
                     /db_xref="CDD:439923"
ORIGIN      
        1 mknsgilkee llqgkysqll keiyldesml eyqnkryada itefeklyge kevevysapg
       61 rsevcgnhtd hqlgmvlats inldaiavvs ktegdliriv segydmvevd vndleekyee
      121 egttaalirg vvakvkeegy rvggfeayvt sdvligagls ssaafeiivg tifsglfnem
      181 sispvflaqa gqfaenvyfg kpcglmdqma csvgglihid fknpeepvve kvpadfeayk
      241 yslcivdtka shadltedya qipaemkkva affkqdvlre vdekefysqi pglrsilgdr
      301 pvlralhffe eekrvqaqve alkqgdfkef lslveksgns sfkylqniyt trneqsqams
      361 ialgvsesil gnhgvcrvhg ggfagtiqif vensfveeyr kamdkvfgsg schvlkvrqh
      421 ggmqvl
//
LOCUS       WP_004228909             123 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Streptococcus criceti].
ACCESSION   WP_004228909
VERSION     WP_004228909.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus criceti
  ORGANISM  Streptococcus criceti
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Streptococcus criceti"
                     /db_xref="taxon:1333"
     Protein         1..123
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=13820
     Region          14..105
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(27,62..63,65,90)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 msqstfippd kyakairqip ygkvvtladl raylgqsdsv pvfsgiatli vawseedesi
       61 pywrvlksgg evnakypggl eaqkvlleae ghriiqkgkt kmkyyvkdyq eqsylfdvkr
      121 nlm
//
LOCUS       WP_004227704             293 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Lysinibacillus].
ACCESSION   WP_004227704
VERSION     WP_004227704.1
KEYWORDS    RefSeq.
SOURCE      Lysinibacillus
  ORGANISM  Lysinibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 293)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Lysinibacillus"
                     /db_xref="taxon:400634"
     Protein         1..293
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=34070
     Region          <32..273
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mesavgqsik tsnifsffky lygqhqsssl ymkrlkalkq iiqhndlhty fqpivdlqsk
       61 qtigfealnr plpstlfnsv dqfyefvgqt dcvflfecfc rnlslqrfke rlhkdlvnkn
      121 flvflnihpn vlldkkyhsg etlqllkelg ikpqqvvfel tersavidfm efervlshyr
      181 sqgyriavdd vgsgynslkt liylkpefik ldrsliqfid qnneqqqlvt llmkyaeqan
      241 tkiiaegier qeeldylhri gihyaqgyai gkpakeiymg kirvgdhedr gsh
//
LOCUS       WP_004229383             191 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Enterobacterales].
ACCESSION   WP_004229383
VERSION     WP_004229383.1
KEYWORDS    RefSeq.
SOURCE      Enterobacterales
  ORGANISM  Enterobacterales
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 191)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Enterobacterales"
                     /db_xref="taxon:91347"
     Protein         1..191
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=20952
     Region          <1..172
                     /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 mrwrhprlgl lppgqflpla esfglmpeig awvlgeacrq mhkwqgpawq pfrlainvsa
       61 sqvgptfdde vkrvladmal paelleielt esvafgnpal fasfdalrai gvrfaaddfg
      121 tgysclqhlk ccpittlkid qsfvarlpdd ardqtivrav iqlahglgmd vifrrrlhql
      181 igrngccaas s
//
LOCUS       WP_004224019             409 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Klebsiella].
ACCESSION   WP_004224019
VERSION     WP_004224019.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 409)
  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 409)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..409
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47322
     Region          1..405
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 msvlqlslne arhlhlaaqg llkkprrrar pkdilstiqq msllqidtin vvarspylvl
       61 fsrlgsypqh wldeslrnge lmeywaheac flprsdfalv rhrmlnpdnm gwkyhrawme
      121 ehagsiaelv ahigqngpvr sadfthprkg asgwwewkph krhleglfta gevmvverrn
      181 fhrvydltrr vmpdwdderd alsredaeai mlrnsarslg ifraqwlady yrlrqpalpg
      241 llaawqeegl vvpvnvealg emwlhheala qletapggkl tashsavlsp fdpvvwdrkr
      301 aeqlfnfsyr lecytpapkr qygyfvlpll hqgklvgrmd skihrksrel evfalwleeg
      361 vkitrgleqg lrraindfvh wqsaerilcr rlpeglfvgq eqgweidad
//
LOCUS       WP_004229417             318 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Lysinibacillus capsici].
ACCESSION   WP_004229417
VERSION     WP_004229417.1
KEYWORDS    RefSeq.
SOURCE      Lysinibacillus capsici
  ORGANISM  Lysinibacillus capsici
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lysinibacillus.
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
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Lysinibacillus capsici"
                     /db_xref="taxon:2115968"
     Protein         1..318
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=35670
     Region          1..306
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mitfdnvskq ydnnqiavka lnveikkgef fviigpsgcg kttllkminr lipltagtiw
       61 indkrisdyn ihelrwsigy vlqqialfph mtieeniavv pelkkwsktr ihqrvdella
      121 lvglepakyr qrkpkelsgg eqqrvgvvra laadpeiilm depfsaldpi srtklqddll
      181 emqrtiqkti vfvshdmqea lklgdrlcim kdgeivqigt pqqllqnpvn dfvqqfiggk
      241 qldqlftihd vlqpitvtnd fghtipvdap fpmileklae hdllgveeng kligmvtras
      301 tlrylaadsk krghghgg
//
LOCUS       WP_004229512             165 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Streptococcus criceti].
ACCESSION   WP_004229512
VERSION     WP_004229512.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus criceti
  ORGANISM  Streptococcus criceti
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Streptococcus criceti"
                     /db_xref="taxon:1333"
     Protein         1..165
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18003
     Region          <38..156
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mtmtqkksmy dlllaqleal legetnalan lanasalike alpnsvfvgf ylfdgqelil
       61 gpfqgkvscv hialgkgvcg esaqknqtli vddvtqhany iscdsaamse ivvpiyrddq
      121 llgvldldss ltgdydetdr vylerfvail lektdwnfam fgvkn
//
LOCUS       WP_004229779             680 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Lysinibacillus capsici].
ACCESSION   WP_004229779
VERSION     WP_004229779.1
KEYWORDS    RefSeq.
SOURCE      Lysinibacillus capsici
  ORGANISM  Lysinibacillus capsici
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lysinibacillus.
REFERENCE   1  (residues 1 to 680)
  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 680)
  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 680)
  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 680)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Lysinibacillus capsici"
                     /db_xref="taxon:2115968"
     Protein         1..680
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=73171
     Region          18..664
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mttqekskke kkveefeqis aeeqqailek ydiesnvrti sgvmkhvify gllafslfql
       61 ytaifgqfpa qiqrtihlgf gltlifllfp arkkapkhki awfdyilall aiavgsywsm
      121 nytelvnrng sitqvdfivg liavvlvlea arravglpit iiaiafliya yygpyfpafm
      181 ahrgqdlesi vnlmyfttdg ifgtpisvsa tfifvfllfg aflvktgvgq yfndlavala
      241 gkliggpakv avfssalqgt isgssvanvv tsgsytipmm kklgyrkefa gaveaaastg
      301 gqlmppimga aaflmvefig rgitywdiak aaaipallyf tgiwimthfe akrvglkglr
      361 ddqmpnrqev fkkiylllpi vaiiilmltg tpvmhaalyg iiisigvtmf nketrlkpkd
      421 vidalvegar talgvvaata cagiivgvvv ktglglslan slvalaggsi iltlifvmia
      481 slilgmgapt tanyvitsti aapaivalls pntpqelvpv vvllsahffv fyfgiiadit
      541 ppvalaafaa sgisggdpik tgvnsaklai aafiipymiv fspallmidt tipqilwvvf
      601 taitgmvaig agvigywyrk lfwferiili aagllliype kfsdwvglgi fivmfviqfl
      661 shkkgnhpdn mngktgvsvs
//
LOCUS       WP_004236460             110 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Morganella].
ACCESSION   WP_004236460
VERSION     WP_004236460.1
KEYWORDS    RefSeq.
SOURCE      Morganella
  ORGANISM  Morganella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
REFERENCE   1  (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   2  (residues 1 to 110)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Morganella"
                     /db_xref="taxon:581"
     Protein         1..110
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11733
     Region          41..108
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mktkwtsall ltsalltggf fstsalaqaa ppadsaqvqq svaqetnris intataeela
       61 relsgvgpkk aqriveyrte ngpftsaeql kdvygigeri ftmnsdkiel
//
LOCUS       WP_004237106             287 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Morganella].
ACCESSION   WP_004237106
VERSION     WP_004237106.1
KEYWORDS    RefSeq.
SOURCE      Morganella
  ORGANISM  Morganella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
REFERENCE   1  (residues 1 to 287)
  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 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   3  (residues 1 to 287)
  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   4  (residues 1 to 287)
  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 287)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Morganella"
                     /db_xref="taxon:581"
     Protein         1..287
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33359
     Region          42..287
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          206..285
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mathditltd qipvlteetd tlltgestla dhngvpltfg nayltlmicr agyahmslnf
       61 ksqpvragdi lvlaedtial lkkrsrgfrv ffclipasfs aeiayvlpnp lflflheypr
      121 ciplpeeksl ltmwlaqmqd itrnspvyrh imqrnhlqnl flriaermpp dapaaiqkys
      181 rketlcwqfw elicrhsreh rdvqyyarrl nitpfylsql tgtffnhspk slinrrvipe
      241 iktllrystl sveqiadklh fddpsylcry frretgislt tyrrqns
//
LOCUS       WP_004237757             713 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor family protein [Morganella].
ACCESSION   WP_004237757
VERSION     WP_004237757.1
KEYWORDS    RefSeq.
SOURCE      Morganella
  ORGANISM  Morganella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Morganella"
                     /db_xref="taxon:581"
     Protein         1..713
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=78136
     Region          18..713
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mtdscnascr parltplala lavisggsia atadtedpvv vvgnwldntd nsdtllnhgg
       61 artiktkkqi desgaetiad alrgipgvqv rdsngtggsd vslnvgirgl parlsprsti
      121 lldgiplaaa pygqpqlsms plslgsissi dvmrgatsvr ygpqnvggvi nfvtkpipet
      181 fsgsasvktq gartgglktl tdasvggske dgsagallly sglhgqgyrk nndntdiddi
      241 ilktryafsd tdellanfhy yhaqsgmpgg lteaqykadp yqsvrpfdrf egnrqdmsfk
      301 yrhqeddkqf elltwfsksy rgsyiesegt nasagksrlv syprhytaya iepsysqlfr
      361 fdnqsheitl gyrylnetad ekayrsgwyp tgsqssrpqt dsyyqhtsgg teahaiyidd
      421 tinvgnwtvi pglryeniki hlddgfrnqf rsksyseplp alsviyhidd qwklfanags
      481 sfgslqyfql ntggagndpa nglsaekahn yeagtrfddg llsaemtlfy idfndqlqyi
      541 enstgwtnlg atthqgvela lnydlsetak wldgvsiyst ytytkavskr gnfadkdlpf
      601 ysrqlftaga ryetgnwvwn lntyaqskqq spgtgknyit egsadgrygi ipgymmwdar
      661 aeyhfgpqws dltlaagvkn lfdqasftrs tdnnygiyag qprtffaqas vkf
//
LOCUS       WP_004238421             278 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Morganella].
ACCESSION   WP_004238421
VERSION     WP_004238421.1
KEYWORDS    RefSeq.
SOURCE      Morganella
  ORGANISM  Morganella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
REFERENCE   1  (residues 1 to 278)
  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 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   3  (residues 1 to 278)
  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   4  (residues 1 to 278)
  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 278)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Morganella"
                     /db_xref="taxon:581"
     Protein         1..278
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31749
     Region          31..278
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <168..278
                     /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 mqsdghcreq adyfhlddfy glgmisaryy qqkfsrhthe gfcigvideg vqqffrtgsn
       61 hyaptgdiil vnsdeihtgs saletgwayr aiyptpemld almqdlksad rgfvpwfsha
      121 vvhdpglaaq lrllfdvllk pdnrllkgsl llstlawlit rhnkkgfrpa eitpagqrlq
      181 hiaemmnshp etdysldela amanlspwyf lrqfrlrygm pphawliqar lrkarqllqn
      241 gdrpadvslq cgftdqshft rhfkramgvs pgkfmqrr
//
LOCUS       WP_004238856             385 aa            linear   BCT 20-JAN-2025
DEFINITION  TerD family protein [Morganella morganii].
ACCESSION   WP_004238856
VERSION     WP_004238856.1
KEYWORDS    RefSeq.
SOURCE      Morganella morganii (Proteus morganii)
  ORGANISM  Morganella morganii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Morganella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Morganella morganii"
                     /db_xref="taxon:582"
     Protein         1..385
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=42197
     Region          1..385
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mnmtpganap vplktlrimv lsgaaadasa frlyadgkvq gdpdmvfygq pqnddntisw
       61 qqngsntvft vdvsrlrqdv qkvafvvtcd ggqtvaglcs levqveadre kllsgivdta
      121 grqeaalilg elyrrnnewk frfvaqgfng glkplaehfg vdvaaesapa papkpaeski
      181 slskislske kpsislskrd nfgeirinln whrdvqnsns ggflsnvfgg gnkgidldlg
      241 afvelqngqk sviqalgnaf gdyrrepfiq lqgddrtgav segewlhing gewkhirqil
      301 iyafiyqgvp swdktdgvvt vfvpeqppve trltegddrr tmcaiarlvn engaikverl
      361 nrffknqsdm deafgwgfrw kagsk
//
LOCUS       WP_004240313             283 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Morganella morganii].
ACCESSION   WP_004240313
VERSION     WP_004240313.1
KEYWORDS    RefSeq.
SOURCE      Morganella morganii (Proteus morganii)
  ORGANISM  Morganella morganii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Morganella.
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   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 283)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Morganella morganii"
                     /db_xref="taxon:582"
     Protein         1..283
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31102
     Region          <29..70
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msnkiqgyvw dacavsgvkg tklmimvrla dfssdegisy psvetlsrqi gagvstirda
       61 cnelekdgwl tkkqrrngnr nasnlyflnv dkletialqe iaklkkqren naishppvsd
      121 gsesdrsenr nsgrfdppds gvkggfhppe sggdpsvnsk hdpsvnsked pkpatqkktt
      181 vkfdplsvrp envsepvwqd wvkfrkeikk pltetscrqi akklaghpdp dsvlcdsian
      241 gwqgifpert agrkpakpst hfgfsdknye srsaawvngg khv
//
LOCUS       WP_004241062             458 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Morganella morganii].
ACCESSION   WP_004241062
VERSION     WP_004241062.1
KEYWORDS    RefSeq.
SOURCE      Morganella morganii (Proteus morganii)
  ORGANISM  Morganella morganii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Morganella.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Morganella morganii"
                     /db_xref="taxon:582"
     Protein         1..458
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=50274
     Region          10..424
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 menkftdyla eksviggvli andeteeiai samesltedd ftsaahriif kamrrmmnsg
       61 vrvdlillsg eldqsgesgv tggfaylaec akntpsital payvqkikdl tnarktlavl
      121 hggiskitaa gvsnltdvvg evqssissmd tgsvvetqhi mdgvtesini lesmlngdiw
      181 khktqfglqd idssfggfnn tdfivvggrp gmgktmfsta itktiglkqr kpvvfyslem
      241 ptwqiseria fhhgrvdkqs llgddkakin qeeawaklsn algdiqespi yindrpsmsi
      301 heiradarkm hkktgglgvi ivdylqkmkm tnpenmnqsv geiatglknl akelkcpvva
      361 laqlnrnleq rvnkrpvnad lresgvieqe advifmiyrd ekynpqtdlk gvtevictks
      421 rhapgaekty yftnthggld qadltrints gyqddiec
//
LOCUS       WP_004242179             165 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Streptococcus].
ACCESSION   WP_004242179
VERSION     WP_004242179.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus
  ORGANISM  Streptococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Streptococcus"
                     /db_xref="taxon:1301"
     Protein         1..165
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18346
     Region          4..156
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mlksekqsry qmlneelsfl leaetnvlan lsnasallks rfpntvfagf ylfdgkelil
       61 gpfqggvsci rialgkgvcg eaahfqetvl vgdvrtypny iscdslakse ivvpmikngq
      121 llgvldldss eiddydvidr nyleqfvail lektewdftm feeka
//
LOCUS       WP_004242632             655 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter permease [Proteus].
ACCESSION   WP_004242632
VERSION     WP_004242632.1
KEYWORDS    RefSeq.
SOURCE      Proteus
  ORGANISM  Proteus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
REFERENCE   1  (residues 1 to 655)
  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 655)
  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 655)
  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 655)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Proteus"
                     /db_xref="taxon:583"
     Protein         1..655
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=69866
     Region          18..644
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mtnndhltpv eppaldkeas sgtrhltgiy lkitttlaif islyaiysna lsntqefyrn
       61 tiflsgilil gfilfpfskr fstakfngwd ylfialtlis ygyfffnyvd lhvvrksipn
      121 tmdyamailg iivlfeaarr ttgyfipsla tfaiiyalfg qyfmgifgha gfsverllyr
      181 lfmtsegifg itlstastai vvfilfgsfl svsgatalfn dlalamagrr rggpaqvavi
      241 ssaltgslsg savanvattg tftiplmkni gltsrfagav eatastggmi mppimgaaaf
      301 imagflgisy ttiviaaiip allyyaalim aidieakkqg lkglskenip qvkavlkarg
      361 llllpliivi gtllmgktpi yagflgilti ivaswltpdk tvrmtltkva dalaeaargs
      421 vqvtiacaai gviicvvtmt gigatlafni vsmtdntlwm illvvmlvci vlsmglpsta
      481 lyivvavtvs pilikagvmp laahffvfwf galsnitppv alasytaasi aradpmqtsw
      541 davrlalpgf iipfilvynp allmqgdnls visiglmvis alvgiyalsi atanfwiikt
      601 twferiafaa aailmikpgl ytdllgmali lltgafhllr skkqlvnvgq vsgen
//
LOCUS       WP_004240315             456 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Morganella morganii].
ACCESSION   WP_004240315
VERSION     WP_004240315.1
KEYWORDS    RefSeq.
SOURCE      Morganella morganii (Proteus morganii)
  ORGANISM  Morganella morganii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Morganella.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Morganella morganii"
                     /db_xref="taxon:582"
     Protein         1..456
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=50372
     Region          6..425
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mfseqeleaa viggllagga tqdaydvlat lpddafsvgy fsrvyreikk qaltsaiidp
       61 vfiadalggn gdfahimelt rktisyanlk gyaekvrnya avrkitalin kfqkeitdaa
      121 thdqaesviq kfsseftlit sekeslvpvh lnelidgyvd vlekrnrgeg sgmmirtgie
      181 alddkiggfn ptdlifiggr pgmgktelal tmmekmttag dsvlmfsmem anmqiaermi
      241 agaaqlpvsk mrncdlddes warissaiah lidrdihiid asnltidqic aiserhkrky
      301 patkgifidy lglikkpkae rndlaiaais agmkglakhi htpvvalsql srdvdkrpln
      361 qrrpvaadlr dsgsleqdad yifltyrdvv ynpnspakny aeiiieknrh getgtvyqef
      421 knghylptdq isaaevsrmq qqaeapkrrr yadkaf
//
LOCUS       WP_004244334             274 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Proteus].
ACCESSION   WP_004244334
VERSION     WP_004244334.1
KEYWORDS    RefSeq.
SOURCE      Proteus
  ORGANISM  Proteus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Proteus"
                     /db_xref="taxon:583"
     Protein         1..274
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31531
     Region          1..250
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 miyadlhvht nhsdgvceik dvlenafrng iktiaitdhd ttnhydeiyr egerlglniv
       61 kgvemscydf dvykkvhvvg lwlnektpnv dklcdntlnc rdqfhrelil slnqqgydic
      121 yedakkfsky nivfkmnifq alrekypeem tkerykqlfg sktkietdlk mgyipvdegi
      181 aailqdggip ilahpcvydn ydeiekyvqf glkgleishs rmkpidyelt qnyankfgll
      241 ksggsdfhdp allkfgdfgl nqtqfetlkk dank
//
LOCUS       WP_004244721             303 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase, partial [Proteus mirabilis].
ACCESSION   WP_004244721
VERSION     WP_004244721.1
KEYWORDS    RefSeq.
SOURCE      Proteus mirabilis
  ORGANISM  Proteus mirabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Proteus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Proteus mirabilis"
                     /db_xref="taxon:584"
     Protein         1..>303
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
     Region          7..>303
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mnqvpnnlma eqnvigglll dpqsdnaqsi fsqlkpedfy arhhqiiylt lremytqrmp
       61 idimtvtdfl askgrinqsg gfaylaemar etpsianima yakkirecsa qrfviektve
      121 iqklmmtpse lsfvgkieqa qrlldeatsf gkmgkktglr riddvlddvf tdicdrqdnp
      181 ekhrglktgf kdfdhllspk qivigslfvi garpkmgktt vltemaknvs qqgkpvllfs
      241 memtdkqlve rtlaqqtqin sdkfyqklee hewdrlcsai grlkdepniw vddtpgmslq
      301 hir
//
LOCUS       WP_004245608             390 aa            linear   BCT 20-JAN-2025
DEFINITION  TerD family protein [Proteus mirabilis].
ACCESSION   WP_004245608
VERSION     WP_004245608.1
KEYWORDS    RefSeq.
SOURCE      Proteus mirabilis
  ORGANISM  Proteus mirabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Proteus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Proteus mirabilis"
                     /db_xref="taxon:584"
     Protein         1..390
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=42303
     Region          1..390
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mtltpggnis vpdqtlmvri hsgslvdvsa frlyasgkvn gdadmvfygq ttnddrtiiy
       61 atagnstsft vdltrlrpdv driaftatce gqqtithlqh lsiqvdannn vvanghvdid
      121 grteaalilg elyrrngswk frfiaqgfng glkplaeyfg vdiadpepap apapapapap
      181 apapssvkls kvsltkekpa isltkkddfg kirinldwhr esksggsgll gglfggnkgi
      241 dldigafvel qdgyksviqa lgngfgdfnr mpyvelqgdd rtgdvaggew ifingrewkn
      301 ikqvliftfi yegvpnwskt dgvvtihvpe qppietrltd gnngramcai arlvnengsi
      361 kverlneffk ghrdmdnayg wgfrwtagsk
//
LOCUS       WP_004249444             380 aa            linear   BCT 20-JAN-2025
DEFINITION  TerD family protein [Proteus mirabilis].
ACCESSION   WP_004249444
VERSION     WP_004249444.1
KEYWORDS    RefSeq.
SOURCE      Proteus mirabilis
  ORGANISM  Proteus mirabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Proteus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Proteus mirabilis"
                     /db_xref="taxon:584"
     Protein         1..380
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=41446
     Region          1..380
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mtltpggnis vpdqtlmvri hsgspvdvsa frlyasgkvn gdadmvfygq ttnddrtiiy
       61 atagnstsft vdltrlrpdv driaftatce gqqtiahlqh lsiqvdannn vvanghvdid
      121 grteaalilg elyrrngswk frfiaqgfng glkplaeyfg vdiadpepap apapssvnls
      181 kvsltkekpa isltkkddfg kirinldwhr eskssgsgll gglfggnkgi dldigafvel
      241 qdgyksviqa lgngfgdfnr mpyvelqgdd rtgdvaggew ifingrewkn ikqvliftfi
      301 yegvpnwskt dgvvtihvpe qppietrltd gnngramcai arlinengsi kverlneffk
      361 ghrdmdnayg wgfrwtagsk
//
LOCUS       WP_004252808             332 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein [Thauera].
ACCESSION   WP_004252808
VERSION     WP_004252808.1
KEYWORDS    RefSeq.
SOURCE      Thauera
  ORGANISM  Thauera
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae.
REFERENCE   1  (residues 1 to 332)
  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 332)
  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 332)
  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 332)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Thauera"
                     /db_xref="taxon:33057"
     Protein         1..332
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=36887
     Region          10..331
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mtpkkswkki avasvmaalf sgavqaaefk ftfahvlves tpnakaavkf keeveknsng
       61 rieinirpaa qlggdveiie qtqmglvhia ipptgnlanf epkmylfdlp flmpdndamk
      121 rvldgevgre lldtldksnl ygvnfwgagf rhmtnnvrpi tqpddlknik mrtlqapail
      181 atyrayganp tamaftevyn glqqgvvegq enpfaniysm rfhevqkhlt ltrhayhtya
      241 avmnkaawns lpddlkkvvr dafdvgrdya rqitdaedar ivaeikdkid ireltpegra
      301 afvekskpiy kefearvtpa llqkamkaaa gs
//
LOCUS       WP_004248588             728 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Thauera sp. 27].
ACCESSION   WP_004248588
VERSION     WP_004248588.1
KEYWORDS    RefSeq.
SOURCE      Thauera sp. 27
  ORGANISM  Thauera sp. 27
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 728)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..728
                     /organism="Thauera sp. 27"
                     /db_xref="taxon:305700"
     Protein         1..728
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=78736
     Region          34..726
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mtatpravsa paprpiarll rlgipgalag facvagaqda atadqsavtl npvvvtgsrv
       61 etnsfdlpfs vdavdmranq agnlgvnase alagvpglvi qnrqnyaqdl qisvrgfgar
      121 aafgvrgvkl iadgipasnp dgqgqaatfn ldtaerievm rgpfstvygn haggviqlfs
      181 rtgegaprmr asvlggswgt tkigvglege qsgvgfivda srfdtdgyrd hsktrrdqgf
      241 aklsfrpded stltlvangl rqpdtqdplg vtwasyqrnp ravedvakqy ntrksihhlq
      301 ggatyerrfg edrlqlsayt grrsvtqyqs iprivqipta dnperarhag gvvdfdrdfy
      361 glgarwiaqr slgdgeltlt vgldydrsed drrgyenfig ttlgvkgnlr rkeidtitst
      421 dpyiqalwkq gpwqwsagvr hsrvafkvdd ryivgingdd sgsarysett palgvvyals
      481 pvtnvyasag lgfetptlne lsyspadgsf nlglkpstsr qaelgiktfv gdstrvnaav
      541 frietedeiv vagssggrtt fknagktlrq glemalesel ahnltarasf tylkaeydea
      601 fttrigmadv tipagnrlpg ipklsayael awkpieavtl ageliyrdkl evhdrnidra
      661 apsytlfnlr lsaeqqqgpw tfgqllridn vfdrkhvgsv ivgdsngryy epgperswya
      721 gasasyhf
//
LOCUS       WP_004253822             394 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Thauera].
ACCESSION   WP_004253822
VERSION     WP_004253822.1
KEYWORDS    RefSeq.
SOURCE      Thauera
  ORGANISM  Thauera
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Thauera"
                     /db_xref="taxon:33057"
     Protein         1..394
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=41536
     Region          2..393
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkavlvlnag ssslkfalyp ingelatepa fsgqvegiga tpeitlktas gariqeavrt
       61 sgsqseqhrd alnhvfgllt qhnpdleiva aghrvvhggd hysaptrlde avlrtldtfv
      121 plaplhqphn lravravgtl mpdvpqvgcf dtafhrtqpa vaqafalprr isaegvkryg
      181 fhglsydyva rqlpdiiger akgavviahl gngasmcalr dgrsvastmg ftaveglmmg
      241 trtgsldpgv mlylmeqkam dakaltnlly kesgllgvsg isqdmrtlla sgapeakeav
      301 dlfcyriare lgslaaaagg ldalvftggi gehaaavrek vaelsawlgv kidaaanadh
      361 arridaadsr vavavvptne ermiarytve tlgl
//
LOCUS       WP_004253911             160 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Providencia].
ACCESSION   WP_004253911
VERSION     WP_004253911.1
KEYWORDS    RefSeq.
SOURCE      Providencia
  ORGANISM  Providencia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Providencia"
                     /db_xref="taxon:586"
     Protein         1..160
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17408
     Region          1..152
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mdkkkyylel sdnlsallag eydliatlan tsallyeyle gvnwagfyls ngqelvlgpf
       61 qgkvacvrip fgkgvcgtaf snnqvqried vhafpghiac daasnaeivf plvvsgqiig
      121 vldidspnis qfdqedekgl qhlvnqlcqh lamcsmpkyh
//
LOCUS       WP_004255860             269 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Thauera].
ACCESSION   WP_004255860
VERSION     WP_004255860.1
KEYWORDS    RefSeq.
SOURCE      Thauera
  ORGANISM  Thauera
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 269)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Thauera"
                     /db_xref="taxon:33057"
     Protein         1..269
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=29695
     Region          33..250
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mpnaqalspc srdaqtpvgg cnrcrglapl dfdfsmafqp ivdirsdkvw awealvrgpq
       61 gegagsilsr itednryqfd qhcriraiel ahglgiparl sinflpnavy epracirati
      121 eaanrvgfpl drlqfeitev eevrsdghlr riveeyraig fgtaiddfga gyaglnllth
      181 fqpdvlkidm nlvrnidqdr trrlivrnlv qlagelpctl iaegietlde arcladlgit
      241 lhqgyayarp gfeslpqpdt allekvkaa
//
LOCUS       WP_004257869             685 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Providencia rettgeri].
ACCESSION   WP_004257869
VERSION     WP_004257869.1
KEYWORDS    RefSeq.
SOURCE      Providencia rettgeri
  ORGANISM  Providencia rettgeri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Providencia.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Providencia rettgeri"
                     /db_xref="taxon:587"
     Protein         1..685
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=76324
     Region          17..685
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 msyrlkrhql ahcialtlgi gtlatpigfa apavtsdkli vtsstgqsrl spseqqekgk
       61 lekvaggtnl vvieketrla tlqdaldyqp glviqnffgg idqprlnirg sgvqsaplar
      121 gvlllqdglp atdadgsfhi stlemrdarm vsvrrgansl npqsnslgge ldvlsytgrn
      181 eqgrlryeyg shgreglqta fggvsddgvf dgrvnftydh fdgyrkhsas qrktlrsnfg
      241 yvtnnfenrt wlswtdlrfd vagpvseevl nnnptdvypm vwlrdphrnv eqfrvanrsd
      301 wqvdnqaiga gvwhirthdn fttpayyrfs rshseglqft ynietepvty rtalawdqmt
      361 lqtelmqnrk gtpadktkig kydgraenly gsvgvdlhit ptvtvnldvk gtharrdvek
      421 rqshlsldqs wtfwtpkagv iwrptesqry fanisaseep atfweiinss ngkltklspq
      481 kaityeigge gdvtdglkwn lalyrsqikd eyittydsag tvvgvfnyaa ktrhqgleag
      541 ltgrvgagpg dinyrvswty ndfrfmggey ngnyiagipr nivaaevlye igdwsfgpni
      601 hwaptdmavd hqnnldiqkr khyavlglkg sykpteqwsv ylsmdnltde ryattsvanq
      661 tvtakdstlf pgmgfnmngg vtynf
//
LOCUS       WP_004260352             365 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Thauera].
ACCESSION   WP_004260352
VERSION     WP_004260352.1
KEYWORDS    RefSeq.
SOURCE      Thauera
  ORGANISM  Thauera
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Thauera"
                     /db_xref="taxon:33057"
     Protein         1..365
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=40002
     Region          1..352
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvrnihk rfgafnaldd isldfptgel vallgpsgcg kttllriiag leqadagqvl
       61 ldgedasgth vrdrqvgfvf qhyalfrhmt vfdnvafgmr mkprgqrpse kqiadkvhel
      121 lnlvqldwla drfpsqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 klhddlhits ifvthdqeea levadrvvlm nhghveqigt peevyrhpat pfvygflgsv
      241 nffhgrvege glrvgddhlq hgvsglgqga evvafarphe ldivvdggag egvaarvsri
      301 lafgvtarve ldgingatgq hfeveltrdr vaqlalhegq avrllpsrls lfeqphaara
      361 agaar
//
LOCUS       WP_004261466             165 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Streptococcus oralis].
ACCESSION   WP_004261466
VERSION     WP_004261466.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus oralis
  ORGANISM  Streptococcus oralis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Streptococcus oralis"
                     /db_xref="taxon:1303"
     Protein         1..165
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18239
     Region          3..156
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mlesekqsry qmlneeltfl legetnvlan lsnasallks rfpntvfagf ylfdgkelvl
       61 gpfqggvsci rialgkgvcg eaahfqetvl vgdvtnypny iscdsrakse ivvpmvkngq
      121 llgvldldss eiddydamdr dyleqfvail lektewdftm fgeka
//
LOCUS       WP_004251790             461 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: replicative DNA helicase [Proteus].
ACCESSION   WP_004251790
VERSION     WP_004251790.1
KEYWORDS    RefSeq.
SOURCE      Proteus
  ORGANISM  Proteus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Proteus"
                     /db_xref="taxon:583"
     Protein         1..461
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=52470
     Region          7..428
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mnqvpnnlma eqnvigglll dpqsdnaqsi fsllkpedfy arhhqiiylt lremytqrmp
       61 idimtvtdcl askgrinqsg gfaylaemar etpsianima yakkirecsa qrfviektve
      121 iqklmmapse lgftdkieqa qrlldeatsf gkmgrktglr riddvlddvf tdicdrqdnp
      181 ekhrglktgf kdfdrllspk qivigslfvi garpkmgktt vltemaknvs qqgkpvllfs
      241 memtdkqlve rtlaqqtqin sdkfyqklee hewdrlcsai grlkdepniw vddtpgmslq
      301 hirsesrkik rkvgdigfig vdyltlmqag kadrndiayg eitkglkila kelntvvvll
      361 vqlnrglenr adkrpvpsds rdtgqieqdc dywlgiyrda vyhdnvdetl temilrlnrh
      421 gktgtvyvdq qglsitpvdq ymaayraqpk repkryceks f
//
LOCUS       WP_004264057             707 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor family protein [Providencia].
ACCESSION   WP_004264057
VERSION     WP_004264057.1
KEYWORDS    RefSeq.
SOURCE      Providencia
  ORGANISM  Providencia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Providencia"
                     /db_xref="taxon:586"
     Protein         1..707
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=78306
     Region          13..707
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mnlktsklli plaisaalap yhvfaadnpk ndqitvtgnw lentedgevv fnhpgartvk
       61 tqqqikesgs etiadalkgi pgvqvresng tggsdvslnv gvrgltsrls prstilldgm
      121 plaaapygqp qlsmsplslg siesidvirg gasvrygpqn vggvinfvtk pipkdfsggv
      181 slqtqgaktg glktlvdasv ggskaddsag aillysglhg qgyrksndnt diddlilktr
      241 yaitdndell anfhyyhams gmpggltqaq ynadpfqstr pydrfegnrq dmslkykhee
      301 ddkqfelmtw fsksyrgsyi esdhkdkane rrlvsyprhy tayaiepsys qlfrfndish
      361 evtvgyryln etadekayrs nwyqagtqss rpstndyyqh tsggteahai ylddtidvgn
      421 wtvipgirye ninihlndsf knqnrskrys eplpalaviy hiddewklfa nastsfgslq
      481 yfqlntkgvg nspanglsae kahnyevgtk ydntalslea tlfyidfddq llyventtgw
      541 tnlgatthqg velaarynls elsdkldgis vystytytka vskkgdfahk dlpfysrqvf
      601 tagsryetgn wvwnlntyaq stqespgtss hyvtkpsadg rygtipgymv wdargeyhfg
      661 kslsdltlsa giknlfdqty ftrstdnnyg iyvgqprtyy vqasvkf
//
LOCUS       WP_004264699             737 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Thauera sp. 63].
ACCESSION   WP_004264699
VERSION     WP_004264699.1
KEYWORDS    RefSeq.
SOURCE      Thauera sp. 63
  ORGANISM  Thauera sp. 63
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 737)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 737)
  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   3  (residues 1 to 737)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Thauera sp. 63"
                     /db_xref="taxon:497321"
     Protein         1..737
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=78676
     Region          1..723
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdeitsvfvt esreqlaale sallqlednp ddsdtlnaif rsahtikgga gviecyyiva
       61 fthvvenvld klrnreitld sdlialllac gdhmghllgv lvsgangpde dlaaegeall
      121 krlqrdpgta espsgppaai appiessggs avetdcwhis lrfgpdvlrn gmdplsflry
      181 lstigrierl etmadampna demdpescyl gfeisfssta dkaaiervfd fvrdectlni
      241 lpphsrltdy ialisalped tmrlgeilvk vgaltqgeld sglaeqsapq paedapdeat
      301 vaepqplgei lvehkavqpe lveaavakqk qvtekkaaea rliriqadkl dclidlvgel
      361 viagasvsll agktglgeli eatsltgrlv esirdaalql rmvqigetfn rfhrvvrdts
      421 remgkevelv isggeteldk smvekigdpl mhlvrnamdh glelpsvrea ngkaargrle
      481 ltachdsgsi vievaddgag lnrdrilaka lergivqpgq amtdteifnl ifepgfstae
      541 kvtnisgrgv gmdvvrrniq glrgsvdvss epgkgsrfai rlpltlaiid gflvgvgnaa
      601 yvipldsvve cielavdgsg rdyvnlrgev lplvrlrqlf aisgeaparq nvvvvqyagv
      661 ksgivvdqlm gefqtvikpl gsifrnirgi ggstilgsge valildvqal vkrcanneaq
      721 lipsssgpra lptgaqp
//
LOCUS       WP_004266435             175 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Treponema phagedenis].
ACCESSION   WP_004266435
VERSION     WP_004266435.1
KEYWORDS    RefSeq.
SOURCE      Treponema phagedenis
  ORGANISM  Treponema phagedenis
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Treponema phagedenis"
                     /db_xref="taxon:162"
     Protein         1..175
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19568
     Region          3..171
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mnfqeilerr qscrsfdfek kiedqklqrv ldaarlapsa cnaqpyelfv aqgavaeava
       61 ktraigmnkf meqcntfiil sedsynllak igaqiqskhy ksidigiaaa hivlaaaaeg
      121 letciigafs ekklqeilht hnkitliiai gygseqnilr ekqrkpfnel ikylr
//
LOCUS       WP_004268559             363 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator
            [Bifidobacterium].
ACCESSION   WP_004268559
VERSION     WP_004268559.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 363)
  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 363)
  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
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 363)
  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   5  (residues 1 to 363)
  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   6  (residues 1 to 363)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 363)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 363)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..363
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39614
     Region          14..53
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          73..308
                     /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 mesttvkrhn relilrelfa apsmtkrqia datrlsmpti tenlrelaad glivpaeara
       61 stggrkaqtw qfnarhrtai gvalrptevv cmavdlrgnv iaehkvtmar rndnayyera
      121 ahtistfaqs lpspigvcfa lpssaarhci cvaedwnaat esyqgisril tlpcsriarn
      181 vayatvelhn hpllrnavcl ylgeyinsai vmdgvaregn lehmqldasg dicrcgsrgc
      241 levlcssrql teegeslpgf fgvleqgern hhvrmdrwlg slahavnnir tfvpadvilc
      301 gpiadyldds eiaqlerltt caehvnpsar npqvmrgccv eyqdavgaaq slipashdgi
      361 psd
//
LOCUS       WP_004268820              96 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [Microcystis].
ACCESSION   WP_004268820
VERSION     WP_004268820.1
KEYWORDS    RefSeq.
SOURCE      Microcystis
  ORGANISM  Microcystis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Microcystaceae.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Microcystis"
                     /db_xref="taxon:1125"
     Protein         1..96
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10780
     Region          1..93
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mkrdevlail eahrkqlqtl gvkslslfgs vardeahsds dvdflvefnq eggffqllqv
       61 qyyledilgc svdlgtqdtl rehlrepvle dvinaf
//
LOCUS       WP_004269146             116 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Nitrosococcus oceani].
ACCESSION   WP_004269146
VERSION     WP_004269146.1
KEYWORDS    RefSeq.
SOURCE      Nitrosococcus oceani
  ORGANISM  Nitrosococcus oceani
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Nitrosococcus.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Nitrosococcus oceani"
                     /db_xref="taxon:1229"
     Protein         1..116
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13080
     Region          25..112
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mntkplnsth ngnkdplkka pqwdiaeaqr ivrekleaik adiylfgsra dgtmgrysdi
       61 digidphepl ptgllaeire aleesqiiyh vdlvdlsqvs ktfrrrvlek gvqwkd
//
LOCUS       WP_004270911             397 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Latilactobacillus curvatus].
ACCESSION   WP_004270911
VERSION     WP_004270911.1
KEYWORDS    RefSeq.
SOURCE      Latilactobacillus curvatus
  ORGANISM  Latilactobacillus curvatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Latilactobacillus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Latilactobacillus curvatus"
                     /db_xref="taxon:28038"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43792
     Region          2..394
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mskvlainag sstlkwklfi mpeeqvvaqg mvdrlglsds vftvkygdgq kfsmtqdikt
       61 qdvavdlllk kliefkiine yseisgighr vvaggedfks salideaslk rieelseyap
      121 lhnpaeagvi rafrkilhdv pqvavfdtsf httmpeenyl yslpleyyhk ygarkygahg
      181 tshryvshra aemlgkplee lkmitmhlgs gvsvtaikdg ksldtsmgft plagvtmstr
      241 sgdidaslva flmeklnikd paemidilnt ksgiygisgl spdmrdlekt reerpesqla
      301 idifvnrlik yvgsyvaimg gldvlvitag mgegdilmrq riadrlsffg vkvdpernnv
      361 maqervisad dsrvkvllvp tneevmiard vveighv
//
LOCUS       WP_004271694             356 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Nitrospirillum viridazoti].
ACCESSION   WP_004271694
VERSION     WP_004271694.1
KEYWORDS    RefSeq.
SOURCE      Nitrospirillum viridazoti
  ORGANISM  Nitrospirillum viridazoti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Nitrospirillum.
REFERENCE   1  (residues 1 to 356)
  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 356)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 356)
  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   4  (residues 1 to 356)
  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 356)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Nitrospirillum viridazoti"
                     /db_xref="taxon:3144925"
     Protein         1..356
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39476
     Region          42..221
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          277..351
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpktaaaspn dadaamidqp tirvlfltal lnvlsevddr idpllrdygf frsqldkpye
       61 rvplhryval lehaaakfqr pdlglemgqs fgladlgpfh allrasgtlr galdcltlfq
      121 srlqsktsfd sqigpdrtty syriedpriw prqqdaefal sgyanlvrql tsakwspaev
      181 hlehpitgrd afltrffrap vlgnqvanal iirnedldkp lvsvlspede klksvlerhl
      241 ldlmgpaaap ggglvaltkd iiarrlgrar vdcalaaael klserslrrr lmeegtsfra
      301 llqearqera rrilaaadlp lsvaaeqlgy sdtatfsraf kdwtgispgr yskntr
//
LOCUS       WP_004271891             409 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Nitrospirillum viridazoti].
ACCESSION   WP_004271891
VERSION     WP_004271891.1
KEYWORDS    RefSeq.
SOURCE      Nitrospirillum viridazoti
  ORGANISM  Nitrospirillum viridazoti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Nitrospirillum.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Nitrospirillum viridazoti"
                     /db_xref="taxon:3144925"
     Protein         1..409
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43501
     Region          9..405
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mrrrkisnai ivinagsssi kfslfadetr qlelflkgqi eglrtdnahf iarhpagdvv
       61 gerrwtgtea gafdhdaatr flmgfinthl eghkveavgh rivhgggdft apaaldaavl
      121 drlatfvpla plhqrhnlap arsilastpg lfqvgcfdta fhatqpplaq afalpaeitd
      181 rgvrrygfhg lsyeyiashl gelgldgakv ivahlgngas lcamdggrsv astmgftave
      241 glpmgtrcgt ldpgvllylm demhmgprdl ekllyqrsgl lgvsgissdm rtletspepr
      301 aklavdlfty rigreigsla aalggldalv ftagigehsa gvreavchha awlgveldga
      361 anarpedarp edgatrisap gsrvaawivp tdeeqmiarh trrlltgat
//
LOCUS       WP_004272941             188 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Nitrospirillum viridazoti].
ACCESSION   WP_004272941
VERSION     WP_004272941.1
KEYWORDS    RefSeq.
SOURCE      Nitrospirillum viridazoti
  ORGANISM  Nitrospirillum viridazoti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Nitrospirillum.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Nitrospirillum viridazoti"
                     /db_xref="taxon:3144925"
     Protein         1..188
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20364
     Region          3..183
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdlfdalhnr ravraysesg vaanqirsvi eaavdapsgm nrqpwsfivv mdrprlrlws
       61 dhakafllrs ldeqpelkpm eshladpafn ifydapalia icatvpdama qqdcclaaen
      121 lmlaayghgl atcwiglsha wlnsadgkda lalpptmpvv apiiighprd dappkpprna
      181 ahiswigd
//
LOCUS       WP_004271133              86 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: zinc ribbon domain-containing protein
            [Latilactobacillus].
ACCESSION   WP_004271133
VERSION     WP_004271133.1
KEYWORDS    RefSeq.
SOURCE      Latilactobacillus
  ORGANISM  Latilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
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 10577258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Latilactobacillus"
                     /db_xref="taxon:2767885"
     Protein         1..86
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=9850
     Region          4..85
                     /region_name="Zn_ribbon_2"
                     /note="Putative zinc ribbon domain; pfam12674"
                     /db_xref="CDD:463667"
ORIGIN      
        1 mekfcqscgm pltaqnqgse qdgtksnqyc qlcyvdgqwt eptitfeqml ekgiagirad
       61 qttgkmkqwf liksypmmlk kmrrwa
//
LOCUS       WP_004274219             369 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Nitrospirillum viridazoti].
ACCESSION   WP_004274219
VERSION     WP_004274219.1
KEYWORDS    RefSeq.
SOURCE      Nitrospirillum viridazoti
  ORGANISM  Nitrospirillum viridazoti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Nitrospirillum.
REFERENCE   1  (residues 1 to 369)
  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 369)
  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   3  (residues 1 to 369)
  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   4  (residues 1 to 369)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 369)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 369)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 369)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Nitrospirillum viridazoti"
                     /db_xref="taxon:3144925"
     Protein         1..369
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38918
     Region          29..360
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(102..104,125..126,175,227,251)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mvrmkgrvaa vaimvaaglg agaaraeikl glgapltgpn avvgeqlrrg seqaikdlna
       61 kggvlgeqiv liqaddasnp sqgvaaankl itqgvvavig hynsavsiaa akvyseegvv
      121 qispgstnpq ltemgshttf rtcgrddqqg evaaqyiakn fpkarigilq dqttygrgla
      181 datraalakq glkevvyeav tvgdrdmssv itrmkdaqvd fvyfgglhte agllvrqmae
      241 kglkakfmag dgivsnefwn itgamgngvl ntfgadyrqq pvaaevvksf raqnyepeay
      301 tlysyaavqa waqavttaks tdpakvadal hkgsfqtvig plsfnakgdr ttadytvyqw
      361 rdgsytevk
//
LOCUS       WP_004274774              79 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Campylobacter upsaliensis].
ACCESSION   WP_004274774
VERSION     WP_004274774.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter upsaliensis
  ORGANISM  Campylobacter upsaliensis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 79)
  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   2  (residues 1 to 79)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Campylobacter upsaliensis"
                     /db_xref="taxon:28080"
     Protein         1..79
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8801
     Region          9..76
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkkifflmfa lasflfaavn lntatleelk slkgigetka kaildyrkeq nftsieelkk
       61 vkgigdktfe eikdsivve
//
LOCUS       WP_004274804             200 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Campylobacter upsaliensis].
ACCESSION   WP_004274804
VERSION     WP_004274804.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter upsaliensis
  ORGANISM  Campylobacter upsaliensis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Campylobacter upsaliensis"
                     /db_xref="taxon:28080"
     Protein         1..200
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22945
     Region          3..196
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mslelfktry scrnfkketi edeilkeile varlspsslg lepwkflvik dakkreelsl
       61 ianhqshvkn aaaiviivsr ldfaeyfeek lkkrkmseee iqkrimlykp flqsmdertk
      121 iaysreqahi alagilyaan tlniatctig gfdsaklnay lnldikkels tlmialgysd
      181 deeipaksrf dfdevvrfld
//
LOCUS       WP_004276041             650 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Campylobacter upsaliensis].
ACCESSION   WP_004276041
VERSION     WP_004276041.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter upsaliensis
  ORGANISM  Campylobacter upsaliensis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 650)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..650
                     /organism="Campylobacter upsaliensis"
                     /db_xref="taxon:28080"
     Protein         1..650
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=75917
     Region          161..648
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mknellqdle nrfetlkyir nlaqsydekl fcylleqsty kdefknrffi mrnntyifkl
       61 ndfltfldlr nlsgsftsyt nkiglgfktk sflktnnevv lnfaykdgvi kggqskdedk
      121 kneiffneil akdeidvlfa rkalqnfeli gdlkenlnna nllikgnnll clhslkkkfa
      181 nqvkliyidp pyntgndsfn yndnfnhstw lcfmknrlei areflrddgv ifiqcddneq
      241 aylkvlcdei fngggggnnf vgcvavkmtp ssgvkrrfan ikfiknkeyl liykkreini
      301 nplydvinny dphysiyfng kefttinqkm kesgiklsgi pkelyfsipe tkhflqihkn
      361 yvfrdhppsk wslneiekhk piferkekqn srnyvykihn pnneeefell fdsvsgfrrl
      421 eplewkmnde neiislrgdf wdckydgdmg ninkegftkf gqgqkperli mdiikattqe
      481 ndlvmdffag sgttlavamk mkrrfigieq mdyiesitke rlkkvvsgeq ggiskavnwq
      541 ggggfiyael mplnaiyker iknindekml dsiykdlesk afldyridld silkdkefke
      601 ldlekkkevl lsildsnmdy vlygdiedkd yaissevikl nkifygddnv
//
LOCUS       WP_004276374             386 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Campylobacter upsaliensis].
ACCESSION   WP_004276374
VERSION     WP_004276374.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter upsaliensis
  ORGANISM  Campylobacter upsaliensis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Campylobacter upsaliensis"
                     /db_xref="taxon:28080"
     Protein         1..386
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=45419
     Region          234..376
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mqkaqiikle fsnkkdsvlm felqnnrgkd ltnmeklksy layqiytysd kdsaetklne
       61 mtsvfkeiyr vvvndikqln edailgyfni atskfgfayr enddslnykk elkdikdsea
      121 klawideyvk glknaffdfn tfteskseyk dyllhlnvad typfvikayq lfrndeekle
      181 rvfkalevia frdklvstra kirdklngal knfdsvekle sgiknicdke wywtdekvke
      241 alspeqytle kiapyifmry enalrnkntr tkgyiftlqe iqkpqiehia pqtkndekva
      301 sgyceydeef kkfylncign lmliaqshni signnpfadk lqsyekspia qhreikefan
      361 gevwdkdsid krhkkleefv lktwsl
//
LOCUS       WP_004277710             368 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Campylobacter upsaliensis].
ACCESSION   WP_004277710
VERSION     WP_004277710.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter upsaliensis
  ORGANISM  Campylobacter upsaliensis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Campylobacter upsaliensis"
                     /db_xref="taxon:28080"
     Protein         1..368
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=42908
     Region          28..>348
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 miqmfqklpd sksilqdtyk yrlsgnfnad nlliyddnln amrflaqeld yqnsidliyi
       61 dppfgtnnif klgstmsaek dskiaykdkf slesylefly crlvwirklm sekgslylhi
      121 dskmghyvki lcdevfgren finditrikc npknfkrkay gnikdmilfy akssqyiwne
      181 ikdevlesdl kkrfnkkddk gyyttiplha pgitqngesg qewngikppn grhwrcslke
      241 ldrlqelgli ewsrnnnprk kvyrdkckgk kiqdiwefkd sqnpayptek nramlrriia
      301 mssnedsrvm dcfcggggfl qealnlgrkf igidegieai klnqkwlkas enhlfshdia
      361 liekltcq
//
LOCUS       WP_004278490             335 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004278490
VERSION     WP_004278490.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 335)
  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 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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 335)
  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   5  (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   6  (residues 1 to 335)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38392
     Region          22..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <146..335
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msqltdasvv lrlgyqairr aglpteellt kagvalnqve andrtplsaq yafwvaaeev
       61 skdpdiglhl gehlplyrgq viehlfvsse nfgeglkral ayqrlisdaf aaklvieddr
      121 cyltngeqpf aeslvnrhft ecamsgvlrf fkfiteghfe piyidfnfyk gapddeyfrv
      181 yecpvslgqk etrlyfdpti leyplwqaep ellqlheqla ieklqelary dlvgevrrai
      241 gstlesgett letvaaqlni tprrlrtqls eahtsfqqil sdyrcrlakr llastnesve
      301 rivyltgfse pstfyrafkr wtnetpveyr krkqr
//
LOCUS       WP_004279078             353 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Acinetobacter].
ACCESSION   WP_004279078
VERSION     WP_004279078.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..353
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39607
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvqniek hfgafhalkn isldfpdgql vallgpsgcg kttllriiag lesadggqvi
       61 legqdatnvh vrerevgfvf qhyalfrhmt vfdniafglr vrprktrpse aeikkrvtrl
      121 ldlvqlgfla drypaqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 tlhdelhits ifvthdqeea levadqivvm nkgnveqigs prevyetpkt pfvfdflgqa
      241 nrfegqnhgg liqlgedriq fegaknaaqg evilfarpde lrihaqphdn aiqatfirel
      301 wiagkvvael ndrqgnliei lltpdearah qfrpnqtvwl savnlhlfen qva
//
LOCUS       WP_004280421             342 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004280421
VERSION     WP_004280421.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 342)
  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 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 342)
  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   4  (residues 1 to 342)
  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 342)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..342
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38675
     Region          32..209
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          256..337
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mktiaprqdq gipgvyglll ldvisrwgyn neslfqpfsl tseqladpdf riptpvanel
       61 vkyalkltge ptlgyhlgtq mrisihgfig yaimtannit dalvlanrfi qlrlpflqlf
      121 fstfgakatv qlqtdiqlep lrteisialm iglismakai tgvtdatgei dfdfkkpegf
      181 erfmakfpth qfrfeqphli lsfdksylmn klvhadpias qiainqcete lsalgerhri
      241 amrvrdilth aeqhylsies vadrlhmsdr tlkrqlaaeg tsfstlvdev ryrhatslls
      301 rtdftleqia delgysdvan fsrafkrwsg rspsnwrkdp yl
//
LOCUS       WP_004280697             713 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Leptospira mayottensis].
ACCESSION   WP_004280697
VERSION     WP_004280697.1
KEYWORDS    RefSeq.
SOURCE      Leptospira mayottensis
  ORGANISM  Leptospira mayottensis
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 713)
  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   3  (residues 1 to 713)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Leptospira mayottensis"
                     /db_xref="taxon:1137606"
     Protein         1..713
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=80092
     Region          1..703
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdlsevratf iseseellss mesnllilek dseneegihs vfraihtikg tsgmfgyepi
       61 ekfthevetl ldrirsrkqi ltkegieflf lacdhirhlv esvedtdtli ldpktsrkqa
      121 dlmslakkll senfsndlkk dsaskssqts sgnlnvpsns aywqitlipn qhlfesgmdp
      181 ytfikylaqs gnikhifvyp esipnwqefh pehsylgfei syasptegee ihstfqflke
      241 esylkilppk csldffeqnc kdfplgreay lyaleiqkvl ngdelqrlrn ifvhttedvy
      301 splnvatien gkesetikiq tktlrvdssk idtlialvge litqeanlsr riidtedtql
      361 iesseslyrl vseirefals lrmvpiadlf ekykrvvrdl skelnkqvel eifggeteld
      421 rsviekiadp ivhilrnald hgietseeri lkgkpaagkl qiqashgtgs ilieikddgk
      481 gldgekivek aiskgliakd qtlseseiys lifqpgfsta ehvtnlsgrg vgmdvvlkni
      541 eslrgtvqiq takdqgssfh irlpltlaii dgflvrasgl ffivpmqmvr etveskvvln
      601 gsfsgtmnlr dellpilhls sflsletntf ykenililey edksfgivvn dlqgeiqsvi
      661 rpmaeifksi kcfsgtsilg sgeiafildv pglynsirdq eqsknkelvv ksg
//
LOCUS       WP_004280363             338 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Acinetobacter lwoffii].
ACCESSION   WP_004280363
VERSION     WP_004280363.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter lwoffii
  ORGANISM  Acinetobacter lwoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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
REFERENCE   4  (residues 1 to 338)
  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 338)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Acinetobacter lwoffii"
                     /db_xref="taxon:28090"
     Protein         1..338
                     /product="CmpA/NrtA family 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=38249
     Region          2..242
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mstlekteln igyiplldcv ailwaekqgy faeqgltinl ireaswsslr drlaygflda
       61 ahclsamlpa aalgtdqlqv alqtplvlsv nqafislrqd lcyelgiqpe ddeqstskkl
      121 vqalqknhpi nlayvykysi hhyclkewla ltdlqlakni qlmtspppsm vkgiaeqvfd
      181 gfcvgepwni qaklegysfi vaasqnvipk vadkvlamtq ewaeqhpftv eavvkavqka
      241 qddlkqrsdl sdvwnmlvdy qiiqfecsaq rhvydfhkik niirnfvges aepkvddfiw
      301 llqqmqkwen ldlseddqlq iaqqcihslq nqhadiig
//
LOCUS       WP_004281196             135 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acinetobacter lwoffii].
ACCESSION   WP_004281196
VERSION     WP_004281196.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter lwoffii
  ORGANISM  Acinetobacter lwoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Acinetobacter lwoffii"
                     /db_xref="taxon:28090"
     Protein         1..135
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14741
     Region          1..121
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mmkvikgftl ielmivvvil aivaaialps yqayvrkgne klalqqiadl slelekeksr
       61 nfsyegmngk svlakagtkh vytttvtael rkwsikscvn qaledaslyk nyasnsqgat
      121 cewsdtsctv pvncq
//
LOCUS       WP_004281453             273 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter lwoffii].
ACCESSION   WP_004281453
VERSION     WP_004281453.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter lwoffii
  ORGANISM  Acinetobacter lwoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 273)
  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 273)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 273)
  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   4  (residues 1 to 273)
  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 273)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Acinetobacter lwoffii"
                     /db_xref="taxon:28090"
     Protein         1..273
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31118
     Region          18..269
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          190..268
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mhkkiqadsa slkqlpthdl ikaplwisfr edpaqsvypl hghawgefvy afhgvmevni
       61 nhinyvtpsp hgiwlppnle hrglnrtavs hgtlyvhesl csqlptqpgi llsaplvtal
      121 fthlkqlhqq dhpafedsae yqrllqvlld qlqqaqlvss ylphsehall kqildylhqh
      181 ladqsslqql aervnltert larysqkelg mslhewrqrl kvmqamslln sghsvesiaf
      241 dlgyanasaf inmfkrwmgs tpdqfrkryt vnd
//
LOCUS       WP_004281645             262 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Acinetobacter lwoffii].
ACCESSION   WP_004281645
VERSION     WP_004281645.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter lwoffii
  ORGANISM  Acinetobacter lwoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 262)
  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 262)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Acinetobacter lwoffii"
                     /db_xref="taxon:28090"
     Protein         1..262
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29395
     Region          1..257
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 miklavnlsm iftevplier falaraqgfn hveiqfpyel tigqiqnqls thqlnlclin
       61 vpagdlmqgg hglagipgqe iefrhaveqa iqyatalnvp rvnilagkqp ldcdllpcln
      121 tlasnlkmac smliehqiep vfemingtdm prfliqnvaq aqemleavhh palkmqydcy
      181 hmammgedvl etlqeniasi ghiqfadcpg rhqpntgsiq yhdifqwlkh sqyqgyvaae
      241 ykpsghsnds fdwkaeffpe hd
//
LOCUS       WP_004282132             429 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [Acinetobacter].
ACCESSION   WP_004282132
VERSION     WP_004282132.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..429
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=49114
     Region          3..418
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mntvavlklt lhhgivgyla gfqsgknilv ftdsfrsdqq rptlslltsp lypqvdkile
       61 ktyvthqrlh pllsnllpeg alreliaqsl kvhidnefql laalghdlpg aliatpldpe
      121 eipdeikfkl qisnpdqilk qeirtdnkfs lagvqmkfsm kakdgrftlv qatessllgd
      181 wiiktpssrh afvplneysm mslakmvgid vpeirlvdma llqnlpplnl pqeqyafaik
      241 rfdrqstadt telihiedfa qifgaypqqk ysttnyeqig kiiyqfsdnk ildiqqfasr
      301 llvnillang dahlknwsmi yqdkrtprls paydilmtsv yienelhfal nlaknkdwyl
      361 aemkhfeqwa ekvgvpwrvi ekqlhaimdk arsvwpalll dlpmisvhke klrehwkklh
      421 pdfqiltdd
//
LOCUS       WP_004284058             566 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Neisseria weaveri].
ACCESSION   WP_004284058
VERSION     WP_004284058.1
KEYWORDS    RefSeq.
SOURCE      Neisseria weaveri
  ORGANISM  Neisseria weaveri
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Neisseria weaveri"
                     /db_xref="taxon:28091"
     Protein         1..566
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=64140
     Region          7..474
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mknqkleltw igkhkrpkle arilleeadk syhakvrsek dvfdnrlifg dnllalkale
       61 qeftgkvkcv fidppyntgs afthyddgle hsiwlglmrd rleiikrlls ddgslwitid
      121 dneahylkvl cdeifgrgnf vanvvwqkky aatndskqfs svhdhllvya klsdnwrpnl
      181 vprseelnsk yvnwdndprg pwyptnlsvk tysaandyei ispaglsfrp pptrswvvsk
      241 qkyeelladg ritfgkkgds rpykktflse vqqgvvpiti wehefaghni gaksemramf
      301 gnrndlfdtp kpelllsrvm hiatnpgdlv ldsfagsgtt gavahkmgrr wimvelgehc
      361 hthiiprlqk vidgtdqggi skavnwqggg gfryyrlapt liindrwgnp iinpdynpem
      421 laealakleg ftyrpsethw wqhgyssecd fiyvttqsls aeqlqalsde vgegcsllic
      481 csawrgltat qaaerfpnlt lkkipkmila rcewghddys lnvanlpfae aeplpektdd
      541 qklpvkakkg krlpeeqegl fdgeeq
//
LOCUS       WP_004281070              86 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: zinc ribbon domain-containing protein
            [Acinetobacter].
ACCESSION   WP_004281070
VERSION     WP_004281070.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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 12181465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..86
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=9488
     Region          19..>67
                     /region_name="zinc_ribbon_15"
                     /note="zinc-ribbon family; pfam17032"
                     /db_xref="CDD:465334"
ORIGIN      
        1 mffifgvgpk tktieksqfl cpvcrtrsgy elkqqrnyfs lffiplipls kpksafvtcs
       61 ncgtampstv ldhaqpepgr nsnlea
//
LOCUS       WP_004284769             101 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Neisseria weaveri].
ACCESSION   WP_004284769
VERSION     WP_004284769.1
KEYWORDS    RefSeq.
SOURCE      Neisseria weaveri
  ORGANISM  Neisseria weaveri
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 101)
  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   2  (residues 1 to 101)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Neisseria weaveri"
                     /db_xref="taxon:28091"
     Protein         1..101
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10414
     Region          9..80
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkryllglag vllsalslaa vnintataee lkalpgigpa kaeaivayrs angpfkaved
       61 lkkvkgigeg vygrlkdeat vaevkkkeak plakkdgskk p
//
LOCUS       WP_004286282            1085 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Neisseria weaveri].
ACCESSION   WP_004286282
VERSION     WP_004286282.1
KEYWORDS    RefSeq.
SOURCE      Neisseria weaveri
  ORGANISM  Neisseria weaveri
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 1085)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 1085)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 1085)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1085
                     /organism="Neisseria weaveri"
                     /db_xref="taxon:28091"
     Protein         1..1085
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=115850
     Region          29..226
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          283..514
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          436..659
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mrnndttfls ankhadavlt makatepktf tgssdddvyy vnnradkiie npnqgkdsvy
       61 sssdyvlptn venltlvgnq niygsgnnsd ntligntghn rlnsgrgndt vyghdgndni
      121 nggegndsly gdsgddning eegndylfgg egndtlnggk gddmlsggag edtyifkags
      181 gfdtiidhqg vntvrldeni tledlnisst tdaegnisli iklnedsqlt vknqytkssy
      241 kpavqsfmvg sktydayeia qkanisitap aehnpldirg skagetlngt egndklygye
      301 gddtlygnkg hdeinggsga dtmyggagnd lyyvdnkndk viekngegvd evkswvshtl
      361 ntnvenlilm gnanifgsgn nsdnilkgna gnnrlnsgrg ndtvygdggd dtlnggeghd
      421 qlhgddghdy lngeegndal yggagndtyv fgrgydsdti tdslgsntvr fdnsvtlqnl
      481 slqsikndkg gtdwlisisd tadnlsisnq fssdgktsis sfivegktyt aqaffdalnq
      541 peaglvlsgt dednvltgta gndkidggsd grdklygkdg ddvivehsrt yyggtwadrd
      601 dyldggagnd slhadtgsdy ldggtgndfm eggdgsdtyi fgkgyghdvi fdytltsdfe
      661 ylnthsnrnr vsfvdgitpd dleisiykgy hlpdtllnsp ldkfytthpv tngdtwiikv
      721 kntddtltil nqkpvmgaia vfefanqsyt aseffelkhk glsgeeitaq nasqiytidk
      781 dghanfygts dqdnfhfgqy reeytaaysl esisayggng ndkvhvgreg eqanisfygg
      841 ngddslsvts annpikvfdg gkgndkldgy nshietivfr agdghdtivn qhyagisnvt
      901 psnplheskp eihftggltl ndldirytgd ktvitvkdtg dtvtlgvnsg dlhlpdysip
      961 altvssirfd sgetysledl iqnhplptgl adlggntvtp esaaipagyt asvnkakiss
     1021 lktaenglsd dglfentake naldnainqm taapasgnss sdhvvyania sdsfvtmnee
     1081 piali
//
LOCUS       WP_004287085             212 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Francisella philomiragia].
ACCESSION   WP_004287085
VERSION     WP_004287085.1
KEYWORDS    RefSeq.
SOURCE      Francisella philomiragia
  ORGANISM  Francisella philomiragia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Francisellaceae; Francisella.
REFERENCE   1  (residues 1 to 212)
  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 212)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 212)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Francisella philomiragia"
                     /db_xref="taxon:28110"
     Protein         1..212
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23530
     Region          30..210
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Region          127..160
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          164..192
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mknlskkqsq alytivgiiv vaiictiilq fynsdnekrm feasdiyqra lianenpksp
       61 tsvkiakfee vtknypdtsf gifaswqlad lymaptdldt ksfnvnlsnl pkaidvlqqs
      121 vqsnpndslt ditkvrlakl yissnnpdka isilqsissl nsnaypltll geaysekkdk
      181 dkaldawkka lqdpnssaef kqiitqlinn ak
//
LOCUS       WP_004289221             246 aa            linear   BCT 20-JAN-2025
DEFINITION  3-deoxy-manno-octulosonate cytidylyltransferase [Campylobacter
            coli].
ACCESSION   WP_004289221
VERSION     WP_004289221.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter coli (Campylobacter hyoilei)
  ORGANISM  Campylobacter coli
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 246)
  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 246)
  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 10118537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Campylobacter coli"
                     /db_xref="taxon:195"
     Protein         1..246
                     /product="3-deoxy-manno-octulosonate cytidylyltransferase"
                     /EC_number="2.7.7.38"
                     /GO_function="GO:0008690 - 3-deoxy-manno-octulosonate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0033468 -
                     CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28331
     Region          2..230
                     /region_name="CMP-KDO-Synthetase"
                     /note="CMP-KDO synthetase catalyzes the activation of KDO
                     which is an essential component of the lipopolysaccharide;
                     cd02517"
                     /db_xref="CDD:133010"
     Site            order(8..10,49,75,95,97)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133010"
     Site            order(118,135,141..143,149..150,152..158,166,191..192,
                     195..197,204..207)
                     /site_type="active"
                     /note="oligomer interface [active]"
                     /db_xref="CDD:133010"
ORIGIN      
        1 mkilgiipar ygstrfpgkp ladilgkpmi wwvynqakka kkltdlivat dderimracd
       61 qfdipnimtn ihengisrvh evsqkikadl yvqingdepl iesriierii prvigrdfva
      121 nlicqikspn elldlsniki ifdknkkaiy msrtpiptpy kslefeyykh igvlaytksm
      181 ldffalskps kyekieglei lrfveygkdf ycievknfks lsvdtpkdle kiknnlknkk
      241 kalkci
//
LOCUS       WP_004289727             103 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Bacteroides eggerthii].
ACCESSION   WP_004289727
VERSION     WP_004289727.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides eggerthii
  ORGANISM  Bacteroides eggerthii
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Bacteroides eggerthii"
                     /db_xref="taxon:28111"
     Protein         1..103
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11530
     Region          6..100
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(6..7,25..26,34,37,39..40,42,45..46,48,56,61,68)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(25,56..57,59,80)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mnhsvflqdv ysvvaaiptg cvvtygqiay lvgrpqcsrm vgqamhnvpe dlhlpchrvv
       61 nsqgrlvpgw teqrallene gvrfkangfv dmkksqwefm keq
//
LOCUS       WP_004290770             188 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Bacteroides eggerthii].
ACCESSION   WP_004290770
VERSION     WP_004290770.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides eggerthii
  ORGANISM  Bacteroides eggerthii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Bacteroides eggerthii"
                     /db_xref="taxon:28111"
     Protein         1..188
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20922
     Region          5..178
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mlnevlenik srrsvrtyte qqvsaenlnl ileaatyaps gmnyqtwhft aiqdadilre
       61 lnekikgafa ksdeprlqer ghsetyccyy haptliivsn eptqwwasmd cacamqnifl
      121 aakslgigsc winqlgqtcd dpdvraflmk lgvpenhrvy gcaalgyape gapmkdkkla
      181 egtvtvir
//
LOCUS       WP_004291598             215 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Bacteroides eggerthii].
ACCESSION   WP_004291598
VERSION     WP_004291598.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides eggerthii
  ORGANISM  Bacteroides eggerthii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Bacteroides eggerthii"
                     /db_xref="taxon:28111"
     Protein         1..215
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23517
     Region          40..206
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mkslkfmllg agllmlsacg pqaqkesest vteksnsdav ietimsrrsi rkykpeavnr
       61 dtmkiilncg inapngqnkq swavrvvdsp eflngvsevf kqknpqaagd pnfknmfrna
      121 ptvvfighdt sydcsqidcg llgenmvlaa wsmgigsccl asptrfiadt peaaeylkrl
      181 efpegyklly ciafgypdea paakprdtak vkyid
//
LOCUS       WP_004294431             432 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [Bacteroidales].
ACCESSION   WP_004294431
VERSION     WP_004294431.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidales
  ORGANISM  Bacteroidales
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Bacteroidales"
                     /db_xref="taxon:171549"
     Protein         1..432
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48412
     Region          3..418
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 miesldvilw dkkvgtlvan reghrskacf yfdsdyvrdg ydiaplrapv kgvaaqrglp
       61 vypdeerlfg glpsfiadsl pdhwgntvfn ewakvhhirm rdlsaldrla yigrrgmgal
      121 efvpptaeel etpfkvkiad lyqlarqafe eagrfnvpvs gnlmveslfk vgtsaggrrp
      181 kavvnvnfee gqcysgqvat pypgytpmiv kfdehqkmpt trieysyylm avdaglqmmp
      241 srllegeqta hflterfdrr ngkkvhiqtl aamnpsadsy ealfevacri gvppgelrql
      301 frsmvlnvlg gnvddhnknf sflmgndggw hvapaydytf svdpdapyyv nrhsmtvnnk
      361 tegiaaedlm evarrygika aepfiekaig ivsrypeygr eagvgeewik tiekeitarv
      421 ecvsdnrtgr lk
//
LOCUS       WP_004296698             159 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Bacteroides].
ACCESSION   WP_004296698
VERSION     WP_004296698.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..159
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17245
     Region          1..157
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdafidstiq lliewglpgl fisallagsi vpfsselvlv alvklglppi aclisatlgn
       61 tvggmtcyym grlgkiswie kyfkvkkekv dkmvkflqgk galmafftfl paigeviaia
      121 lgfmrsntwl tivsmfvgkl iryilllyal esawdaiag
//
LOCUS       WP_004296945             370 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Bacteroides].
ACCESSION   WP_004296945
VERSION     WP_004296945.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 370)
  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 370)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 370)
  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   4  (residues 1 to 370)
  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 370)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..370
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42677
     Region          126..367
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <306..362
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mgithlsiel tldlialiig iiliirakdn ypklywgiia tgigimfswe nigwltivtd
       61 tpeynftell niekmlkwya lanivalfpi aslspgylnh friftflllp iititvgisy
      121 lgfngnitpi hsideiipni hqidvklrvc ifllsvftpl vlliypmmnn ktyrrinnnm
      181 ylfigflfvf lgiyilftln inefvfnlfg imaivftvlf siqylryenp fsnhinmihn
      241 akntestiml qagkpsptlp lfstieaylq eqhpytdqry niellaksln kqehdisaai
      301 ksqgftgfre yinylrleyf rqlaaenpks nvkelmfacg ftsratfyrn fsekygvsps
      361 kfienqrveq
//
LOCUS       WP_004298370             359 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Thauera].
ACCESSION   WP_004298370
VERSION     WP_004298370.1
KEYWORDS    RefSeq.
SOURCE      Thauera
  ORGANISM  Thauera
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae.
REFERENCE   1  (residues 1 to 359)
  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 359)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 359)
  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   4  (residues 1 to 359)
  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 359)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Thauera"
                     /db_xref="taxon:33057"
     Protein         1..359
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39579
     Region          9..193
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          236..318
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mlaglqrrgl dgapllarag idlaetdtri pveryallyn lcvealedea fgllpepmrp
       61 gsfeflcral lgaptlgeal lrairflriv lpafrielrv dgaraellld dggslgpgld
      121 aparvfayew llrllhgvas wfvgrglald avafpyarpa haddyalvyt ehssfdapql
      181 aarlqanlla lplrrdeaal vgflegapgk ittlyrrdre mvfrvrdilr dalpqnlsle
      241 evaerlhvsp rtlhrrlede gsgfrnikea trrdiayarl aktrqpiari aaelgyadps
      301 tfyrafvaws gmspeqfrhr lagndglpaa sagpdrrpap tprvtagrqr srefgptea
//
LOCUS       WP_004298633             142 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Thauera aminoaromatica].
ACCESSION   WP_004298633
VERSION     WP_004298633.1
KEYWORDS    RefSeq.
SOURCE      Thauera aminoaromatica
  ORGANISM  Thauera aminoaromatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Thauera aminoaromatica"
                     /db_xref="taxon:164330"
     Protein         1..142
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15137
     Region          1..133
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mnhasrtrgf tlielmivva iigilasial paysdyirrs kiveatsvls dlrvrmeqfy
       61 qdnrsyvstg ttcgvamptq qfftmsctgt sttytltatg ksgtdvagft ytlnqqnvra
      121 ttggsfgtst tcwvgkrggg cl
//
LOCUS       WP_004287035             433 aa            linear   BCT 20-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Francisella
            philomiragia].
ACCESSION   WP_004287035
VERSION     WP_004287035.1
KEYWORDS    RefSeq.
SOURCE      Francisella philomiragia
  ORGANISM  Francisella philomiragia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Francisellaceae; Francisella.
REFERENCE   1  (residues 1 to 433)
  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 433)
  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 18525164
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Francisella philomiragia"
                     /db_xref="taxon:28110"
     Protein         1..433
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=48369
     Region          <26..83
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          <334..405
                     /region_name="FimV"
                     /note="Type IV pilus assembly protein FimV [Cell motility,
                     Extracellular structures]; COG3170"
                     /db_xref="CDD:442403"
ORIGIN      
        1 mfkginrvia vgcalamavp vfameiytvk sndylykiak shsingvsts eltdaikgin
       61 kseipgivdn rikvgdklai pttkgevedg ltltrnqmiq gsynqpssvs ttpklgdqtm
      121 vssdsesdss sapnvlsedk iptlisgeen tqqsyksnld sqinptdiqe nesyeessfs
      181 flgslfkfiv yvivlavvii vgrrfwetrs tkkeqeleii srkkrdhlms rispvvsgne
      241 fyssrkshns pqeefdffnn snkasssaqt gvnledsenn nqdnldineg defaeiandl
      301 yadrdnnivv ktergvvfet stdesllsns gdseiqeida kqqaeqelqy vnelveqfld
      361 sekyveasit iqdsleknpn nidlryklle vyaqagdeia fegevhfiks knivsmfdpl
      421 hqkiaklrdk yfe
//
LOCUS       WP_004298984             589 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Streptococcus suis].
ACCESSION   WP_004298984
VERSION     WP_004298984.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..589
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=66358
     Region          26..562
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mrpaidfekl rqflsrdive gresyeftwv gkrgaiaeag kpttqtlrpd leesvdfdks
       61 enifitgdnl evlkvlqesy lgkidmiyid ppyntgkdfv ysdkfqmsee elaeemdlrd
      121 edglqrvglt knekssaryh sdwlnmmypr lvlarnllkd sgvifisidd neqanlkaic
      181 deifgeenfv anfvwekgre ggndssllrs hyenilsycv nnkakgiinl dpkdtsrhiv
      241 dlpeknlvag iifeknigep fqlinlskqk dylvkiplvd gtviewssya pqssintwit
      301 egkvfvgtkr vpyvksylkd elqgqkpsni inqkygttka gtievrnyfg drkifpyakp
      361 ssllkrllti gssnssfild ffagsattad avmqlnaedg gnrkyilctl deqvadksaa
      421 keagyetidq isrerirraa kkiqeehpet vgkqdfgfra ykldtsnfkd vsqtpdsfnq
      481 eslfdsvsni kdgrtdldll fqimltwgme lslpiaktqi dgtdiynvad galiacfade
      541 isesvirqia keeplravfk desfansaak inlgqifkev apntkvkvv
//
LOCUS       WP_004300016             298 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Bacteroides].
ACCESSION   WP_004300016
VERSION     WP_004300016.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 298)
  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 12122938
            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="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34912
     Region          218..295
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mekkiplnig leilenpdiv rfnefrfisp hfgfvnsfak iesnlitidq pyrikegria
       61 vikqgyarvl inlieetfqp dklllivpns ilqiievspd fdmqmvamda eflsiagkdn
      121 ffthlsqlqk nlilsltshe ydlfksyfal iwnilqeptf rreaiqylli sllcnieylv
      181 knnnqkeqsc qthqeeifqr fislvnaysk kernvsfyad klcltpryln tiirqtsqqt
      241 vmdwinqsii leakvllkhs nllvyqisde lnfpnpsffs kffkrmtgmt pheyqfsk
//
LOCUS       WP_004300049             147 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Thauera aminoaromatica].
ACCESSION   WP_004300049
VERSION     WP_004300049.1
KEYWORDS    RefSeq.
SOURCE      Thauera aminoaromatica
  ORGANISM  Thauera aminoaromatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Thauera aminoaromatica"
                     /db_xref="taxon:164330"
     Protein         1..147
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=16219
     Region          30..109
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mndeerdnyg mykaiapttl gpdmetgpgp hlmgadtlig nevvnhdden vgeikeimle
       61 vhngriayav lsfggflgmg eklfavpwsa lkldtenkrf vlnvakdrls eapgfdkgkw
      121 pnmadpawss tihsyygtqq hrdelth
//
LOCUS       WP_004300403             189 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Bacteroides].
ACCESSION   WP_004300403
VERSION     WP_004300403.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..189
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20997
     Region          6..179
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mktnevleni karrsvrayt gqqvleedlq aileaatyap sgmhletwhf taiqnmdklt
       61 elnerikgaf aksddsrlqe rghsktyccy yhaptlvivs neptqwwagm dcacaienmf
      121 laaqslgigs cwinqlgttc ddpevrefit algvpanhkv ygcvalgypd skipikekkv
      181 kantitivr
//
LOCUS       WP_004300985             112 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Bacteroides].
ACCESSION   WP_004300985
VERSION     WP_004300985.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..112
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12295
     Region          12..109
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(15..16,34..35,43,46,48..49,51,54..55,57,65,70,77)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(34,65..66,68,89)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mkdykvdkas lsasfcqevy qvvreipvgk vstyggiaal lgmpqcsrmv gralkqipdd
       61 lsvpchrvvn asgrlvpgwt eqkqllleeg isfkqngcvd lkkhlwnysv se
//
LOCUS       WP_004303833             496 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [Bacteroides].
ACCESSION   WP_004303833
VERSION     WP_004303833.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..496
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54184
     Region          4..496
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 metkylrinp adnvavaivn lpagehlsvd gieitlnedi paghkfalkn faegenviky
       61 gypigharma kkqgdwmnet niktnlagll dytynpiqvs ldiphkdltf kgyrrkngdv
      121 gvrneiwiip tvgcvngiig qlaeglrret egkgvdaiva fphnygcsql gddhentkki
      181 lrdmvlhpna gavlvvglgc ennqpdvfre flgefdedrv kfmvtqkvgd eyeegmeilr
      241 dlyakaskde rtdvplselr vglkcggsdg fsgitanpll gmfsdfliaq ggtsvltevp
      301 emfgaetilm nrckneelfe qtvhlindfk eyflshgepv genpspgnka ggistleeka
      361 lgctqkcgks yvsgvmpyge rlqkkglnll sapgndlvaa ttlaasgchm vlfttgrgtp
      421 fgtfvptmki stnstlaknk pgwidfnagv ivenepmekt cerfidyiik vasgefvnne
      481 kkgyreiaif ktgvtl
//
LOCUS       WP_004304651             675 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Campylobacter jejuni].
ACCESSION   WP_004304651
VERSION     WP_004304651.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter jejuni
  ORGANISM  Campylobacter jejuni
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 675)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..675
                     /organism="Campylobacter jejuni"
                     /db_xref="taxon:197"
     Protein         1..675
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=78633
     Region          166..628
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mlkdkllqdl eehfetlgqv rnlaqnyder lfnylleesk ykeefknrff ifnkkvlifk
       61 inefltfldl knlsgsftsy ankiglankt ksllktnnev vlnfafkdgi ikggqskdeq
      121 ktqeiffnei lahdeidvlf dkkalqnfel igeiknlqey lknnpnllik gnnllvlhsl
      181 kklyankikl iyidppyntg ndsfgyndkf khstwltfmk nrleiarefl rddgvifvqc
      241 ddneqaylkv lmdeifgrdn fvnsiavklk niagasggge dkrfkkniey iliygksyek
      301 leqfksvyds relyshisfc kenniswkyt sallnggekk liattldgdg neikiferin
      361 ydiksigqmi kdfkmnekei fyhyvnkifr ttmpqssirv rvleklkeln lspylisiey
      421 tpksgrnkgv vyeqfyngek lnlfawlkdv veikdkqifk kelagtlwdf afamtnltke
      481 gdtqfsnakk peallqriie istnendivm dffagsgttl avahkmkrkw igieqmdyie
      541 titkerlkkv iegeqggisk ainwqgggnf vyaelmplna iykekiqnln dekeldniyq
      601 elktkafldy rvdineilkd kefenldles kkeilklvld snmdyllygd ikdedyalsk
      661 eiiklnkify gdenv
//
LOCUS       WP_004304815              89 aa            linear   BCT 20-JAN-2025
DEFINITION  zinc ribbon domain-containing protein [Bacteroides ovatus].
ACCESSION   WP_004304815
VERSION     WP_004304815.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 89)
  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 10577258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..89
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10519
     Region          5..88
                     /region_name="Zn_ribbon_2"
                     /note="Putative zinc ribbon domain; pfam12674"
                     /db_xref="CDD:463667"
ORIGIN      
        1 meqkfcqscg mpiddstfgk eadgskneey chycyadghf tkectmdemi elnlnyldef
       61 nkdsevkytv eearktmkey fpqlkrwkq
//
LOCUS       WP_004306103             208 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Bacteroides].
ACCESSION   WP_004306103
VERSION     WP_004306103.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..208
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23847
     Region          3..190
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 melyevlekr rtyrdfsdre vsdeivkrii gaafkaptnd hlrqlefivv rdreniakvi
       61 tplvknmeaf kelvfevddt ddedkmamfa dalpkqqkml mqsgllilpf frqkqspllk
      121 pveqsslnyf asawcalenm llaatneglg tvfhipvsde aekikeivga pegyeftcll
      181 tmgypaenaf lpkqkeinie drihmniw
//
LOCUS       WP_004292874             275 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Thauera sp. 63].
ACCESSION   WP_004292874
VERSION     WP_004292874.1
KEYWORDS    RefSeq.
SOURCE      Thauera sp. 63
  ORGANISM  Thauera sp. 63
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Thauera sp. 63"
                     /db_xref="taxon:497321"
     Protein         1..275
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29122
     Region          164..227
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 msttrllviv lillnalafa gvkgwiagta prteperitn qlnperirls ggvgredada
       61 tpqmppsapa eavaapepsp ppvaeaqpat eeagistaas tpdsdalaaa astaapatdv
      121 ppappppalv cqawaglsee eanaltrrlr rggfeaerrr setpaswwvr mppqgsrdqa
      181 erraqelrdl gvrdlfivqe agpsqyaisl glfktearaq qllgqlrtrg vrnagvearm
      241 stsyliqarl tdesvravea dvrgisarrt acngr
//
LOCUS       WP_004306924             265 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Bacteroides].
ACCESSION   WP_004306924
VERSION     WP_004306924.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
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   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 12122938
            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="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29982
     Region          19..127
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          191..265
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mvkgkvifed eekieikypc felkdiveyy feiktpdnsi npfslialpn aniivsvyls
       61 dksqtfkvhr gqgmsdtsgd kisgsltdai avihapgthe fsikfkpgvl ysclsedipt
      121 lvdnslplqk ylnqkiidel klktsfdgrv lfvenwllsn mkifssdfkl kavtkaiyyi
      181 nnshdyklnv vskevgvsnp tlnryfkevl gvspkqcfka lrfktalkny rakgsydlyd
      241 elgytdfshf vkeaknlank ppsel
//
LOCUS       WP_004307078             112 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Bacteroides].
ACCESSION   WP_004307078
VERSION     WP_004307078.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..112
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12267
     Region          12..109
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(15..16,34..35,43,46,48..49,51,54..55,57,65,70,77)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(34,65..66,68,89)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mkdykvdkas lsasfcqevy qvvreipvgk vstyggiaal lgmsqcsrmv gralkqipdd
       61 lsapchrvvn asgrlvpgwt eqkqllleeg isfkqngcvd lkkhlwnysv pe
//
LOCUS       WP_004307264             325 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Bacteroides].
ACCESSION   WP_004307264
VERSION     WP_004307264.1
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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..325
                     /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=37346
     Region          6..277
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 maeismqkss lriewidvck glgiflvvig htsiaqisqt vynwiysfhm pmfymlsgmm
       61 lndskysdfr syikrrlktl iipffclntl vwlivkglni shiqtdftel ltgclamyfi
      121 ralfvselwy ffinklasnw vlklfiifll ivlsdyfrgv pseyigltrn eaigvilpsm
      181 plfyyavghv irnmalnlnt heikywlvss vmivliiisc llqpvsygyf hilpafcgii
      241 ilgllsills rlsvtllnst vcfigrntli ivafhqiiyn smkiltkyls lstvqdatlr
      301 llllaltlyf lirsfnkyap wlvgr
//
LOCUS       WP_004312658             375 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Bacteroidales].
ACCESSION   WP_004312658
VERSION     WP_004312658.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidales
  ORGANISM  Bacteroidales
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia.
REFERENCE   1  (residues 1 to 375)
  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 375)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 375)
  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   4  (residues 1 to 375)
  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 375)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bacteroidales"
                     /db_xref="taxon:171549"
     Protein         1..375
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43127
     Region          121..374
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          291..371
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mkslfilqlv ccvitamlal qlamaslqvr wkvwryeisr wilvasmlff svhyllqmih
       61 glraqgtdvg aafnilfytp vafaitlsii niestgnkvr ryclrgmmay iliaivfvig
      121 mfksqslhig nmlyvmlglf vasmayfili irketkarkq klmenfgidl ipyvrysqas
      181 iillyfaagl lpvailfntl lyiigplill sviffvhtfi amgyyitpke vipeendaea
      241 kvteaedmkd gknthgtnil tanrkmeiel alkkwceegf ykdyevniys latklgykkn
      301 elteyfnqse ytnfrtwlsd irfneavrmm kanpeysida istecgfssh twiyrifkqk
      361 tgmspsqwrk qfasi
//
LOCUS       WP_004307848             149 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SPOR domain-containing protein [Bacteroidaceae].
ACCESSION   WP_004307848
VERSION     WP_004307848.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidaceae
  ORGANISM  Bacteroidaceae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Bacteroidaceae"
                     /db_xref="taxon:815"
     Protein         1..149
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16606
     Region          63..131
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mrklalltll lvlavvgvqa qgivkslern vpgqgkvtih qdpriealig merpatgeqk
       61 viktsgfriq ayagnntrqa kndayhvasr vkeyfpeltv ytsfnpprwl crvgdfrsie
      121 eadammrrlk stgvfkevsi vrdqinipl
//
LOCUS       WP_004320675              89 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: zinc ribbon domain-containing protein [Bacteroides].
ACCESSION   WP_004320675
VERSION     WP_004320675.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 89)
  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 10577258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..89
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10535
     Region          5..88
                     /region_name="Zn_ribbon_2"
                     /note="Putative zinc ribbon domain; pfam12674"
                     /db_xref="CDD:463667"
ORIGIN      
        1 meqkfcqscg mpiddstfgk etdgsknedy chycyadghf tkectmdemi elnlnyldef
       61 nkdsevkytv eearktmkey fpqlkrwkq
//
LOCUS       WP_004321562             112 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Bacteroides].
ACCESSION   WP_004321562
VERSION     WP_004321562.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..112
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12293
     Region          12..109
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(15..16,34..35,43,46,48..49,51,54..55,57,65,70,77)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(34,65..66,68,89)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mkdykvdkas lsasfcqevy qvvreipvgk vstyggiaal lgmpqcsrmv gralkqvpdd
       61 lstpchrvvn asgrlvpgwt eqkqllleeg isfkqngcvd lkkhlwnysv pe
//
LOCUS       WP_004321902             263 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Thauera aminoaromatica].
ACCESSION   WP_004321902
VERSION     WP_004321902.1
KEYWORDS    RefSeq.
SOURCE      Thauera aminoaromatica
  ORGANISM  Thauera aminoaromatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 263)
  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   3  (residues 1 to 263)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Thauera aminoaromatica"
                     /db_xref="taxon:164330"
     Protein         1..263
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28386
     Region          48..259
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 maelstpspa spapldggrg delekftlrg arqilqllqd lithrglita htggghsfmt
       61 avlkvdeerg rvvldpspdp qanrralaap rltcvtqldg iriqfplvgl gegqdkgrpa
      121 lfaplpaeml rlqrrefyrl qvplahelsc llkaedlark pvevsarvid igaggvavvv
      181 ptgaaefvig gtlpacrlal pdgepieldl evrnlnrqtq rngteqlrvg lrfaalpraa
      241 dtriqryifk teralnakar ggl
//
LOCUS       WP_004312710             588 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LysM peptidoglycan-binding domain-containing protein
            [Bacteroides].
ACCESSION   WP_004312710
VERSION     WP_004312710.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 588)
  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 588)
  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 15193204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..588
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=67521
     Region          <23..76
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          <67..131
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          161..202
                     /region_name="LysM"
                     /note="Lysin motif; smart00257"
                     /db_xref="CDD:197609"
ORIGIN      
        1 mkpinriflf llfisvsyai syaqenqsyf lhtiekgqsl ysiskmynvt tsdiirlnpg
       61 cdekiyagqt ikiptgkesq kgetfhtiqa getlyklttm ynvsakdice anpglsaenf
      121 rigqvilipq kkeeqtdavv qtpteqstiq gpvvprckdm hkvkrketif svsreygise
      181 qelidanpel kkgmkkgqfl cipypaattv qptqkedpya vppsnselfr knketpqkls
      241 tikaalllpf qedkrmveyy egflmavdsl krtgvsldly vydsgkdist lntilaknem
      301 ksmniifgpm hqnqikplsd faekndirlv ipfskkgeev fnnpavyqin tpqsylysev
      361 yehftrqfpn ahvifiesan sdkekaefis glkqelknkg ismksvsesa tkeilkttlr
      421 ndkenifipt sgnnviliki lpqltllvre npvekihlfg ypewqtytkd ylesffeldt
      481 yfyssfytnt lfpaavqftn nyhrwyskdl vsewpnyaml gfdtgffflk glsrygsele
      541 nnltkmnltp iqtgfkfqrv nnwggfinkk vffirftknf elvkldfe
//
LOCUS       WP_004324580             137 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Thauera aminoaromatica].
ACCESSION   WP_004324580
VERSION     WP_004324580.1
KEYWORDS    RefSeq.
SOURCE      Thauera aminoaromatica
  ORGANISM  Thauera aminoaromatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Thauera aminoaromatica"
                     /db_xref="taxon:164330"
     Protein         1..137
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=13720
     Region          9..137
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlnedptlla glaasaflaa tllpggseav faallalrpe ltpaallvat aantaggmst
       61 yalgrllprk esgahartll rwgslallls wvpligdalc aaagalrlna faclawmalg
      121 kglryaaiaw alpsaga
//
LOCUS       WP_004325250             429 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Bacteroides
            ovatus].
ACCESSION   WP_004325250
VERSION     WP_004325250.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..429
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48415
     Region          3..416
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 miesldvilw dkkvgtlvas rerhrnkacf yfdsdyvrdg ydiaplrapv kgvaaqrglp
       61 vypdedrifg glpsfiadsl pdhwgntvfn ewakahrirv rdlsaldrla yigrrgmgal
      121 efvpptaeel etpfkvevad lyqlarqafe eagrfnvlms gdlmveslfk vgtsaggrrp
      181 kavinvnfee gqcysgqvat pypgytpmii kfdehlkmpt trieysyylm avdaglqmmp
      241 crllesghat hflterfdrr knkkvhiqtl aamnpsansy edlfdtacri gvppaelrql
      301 fralvlnvlg gnvddhnknf sflmdddgrw hvapaydytf sidpdapyyv nrhsmtvnnk
      361 tegiavedll nvarkygika aepfiekaag ivlrypeygr kagvseewik iiekeisarv
      421 eglnenrik
//
LOCUS       WP_004317903             588 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LysM peptidoglycan-binding domain-containing protein
            [Bacteroides].
ACCESSION   WP_004317903
VERSION     WP_004317903.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 588)
  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 588)
  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 15193204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..588
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=67153
     Region          <23..76
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          <67..131
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          161..202
                     /region_name="LysM"
                     /note="Lysin motif; smart00257"
                     /db_xref="CDD:197609"
ORIGIN      
        1 mkpinriflf llfisvsyai syaqenqsyf lhtiekgqsl ysiskmynvt tsdiirlnpg
       61 cdekiyagqt ikiptgkesq kgetfhtiqa getlyklttm ynvsakdice anpglsaenf
      121 rigqvilipq kkeeqtatat qtpteqttiq gpvvpkckdm hkvkrketif svsreygise
      181 qeliaanpel kkgmkkgqfl cipypaattv qptqkedpya ippsnselfr ksketpqkls
      241 tikaalllpf qedkrmveyy egflmavdsl krtgisldly vydcgkevst lntilaknem
      301 ksmniifgpm hqnqikplsd faekndirlv ipfsqkgeev fnnpavyqin tpqsylysev
      361 yehftrqfpn anvifiepas vdkekaefis glkqelkskg ipmrtvsesa tketlkaalr
      421 sdkenifipt sgnnvlliki lpqltllvre npaenihlfg ypewqtytrd hlenffeldv
      481 yfyssfytnt lfpaavqftn ayhkwyskdl askypnyaml gfdtgffflk glslygsele
      541 nnlpkmnltp iqtgfkferv nnwggfinkk vffirftknf elvkldfe
//
LOCUS       WP_004327102             348 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Bacteroides].
ACCESSION   WP_004327102
VERSION     WP_004327102.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 348)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..348
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=39379
     Region          213..346
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mhcinnmngi asgliiascv fysctsctge ispvheqqtd slsqdtivqp evkpvnkklt
       61 aeqieiskdl lydqytledt ypykdttrqf qwdkikerla lleniqlqps twailqnykn
      121 rngeaplvrs fkrnaygrva dtlgieryqs vplylltdtl vperygqdge ltrfiedgek
      181 fikaepmftg dewmipkkyv kvigdtivfn kavfvdrhnq niaslersgk gqwvvrsmnp
      241 sttgrhlppy aqetplgmfv lqekkvkmvf lkdgsketgg yapyasrftd gayihgvpvn
      301 aprktqieys pslgttprsh mcvrnatsha kfiydwapvn gtiifvle
//
LOCUS       WP_004327621             159 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Thauera].
ACCESSION   WP_004327621
VERSION     WP_004327621.1
KEYWORDS    RefSeq.
SOURCE      Thauera
  ORGANISM  Thauera
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae.
REFERENCE   1  (residues 1 to 159)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Thauera"
                     /db_xref="taxon:33057"
     Protein         1..159
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=17374
     Region          5..159
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cl49639"
                     /db_xref="CDD:483979"
     Site            order(101,115,118,131..134,136)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mhlrvdlgrq clelfgadga cirryavstg ergagersgs lctprgrhri rarigagapa
       61 gavfrgrrpt gevwtaefaa ahpgrdwils rilwlcgeep grnrggevdt mrryiylhgt
      121 gddqpmgvar shgcvrmrnh diielfelvp agtvveive
//
LOCUS       WP_004328184             308 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Alistipes].
ACCESSION   WP_004328184
VERSION     WP_004328184.1
KEYWORDS    RefSeq.
SOURCE      Alistipes
  ORGANISM  Alistipes
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Rikenellaceae.
REFERENCE   1  (residues 1 to 308)
  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 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   3  (residues 1 to 308)
  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   4  (residues 1 to 308)
  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 308)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Alistipes"
                     /db_xref="taxon:239759"
     Protein         1..308
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35343
     Region          38..284
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <179..286
                     /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 mnepydsqta npsiekyvva snngiethkf trcvigyilh gekyvyyddk cykfsqgdlf
       61 flgmgchytk nipeeghpye qilvrftpee lqrillhlni tyklnitnnh lcekcrtlnh
      121 aampawssir rffnhtndyl tedsflhdpp aenikiteli ylivshgdcc ikskllgnvd
      181 aardnlqqtv yasifsdisv eeiakrcnrs ltsfkkeffr iygtsphqwl irqrliharl
      241 llistdkaia eigtacafpn tshfiklfrk qygmtpatyr nrhrgpeelq ptpqaeaavr
      301 etavsvta
//
LOCUS       WP_004328383             151 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Alistipes].
ACCESSION   WP_004328383
VERSION     WP_004328383.1
KEYWORDS    RefSeq.
SOURCE      Alistipes
  ORGANISM  Alistipes
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Rikenellaceae.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 151)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Alistipes"
                     /db_xref="taxon:239759"
     Protein         1..151
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17132
     Region          2..150
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 msaklakydr lyeqikgyvq ttddiwarla tmeavlhhkm qtffwtgvya liddelivrs
       61 yqgpvacqkl rhhtgvcwaa vstgetvivp dverfpghia cnsksrseiv lpirdregrv
      121 facldvdsdr ldafdredee glkkilsllf d
//
LOCUS       WP_004330816             242 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Porphyromonas asaccharolytica].
ACCESSION   WP_004330816
VERSION     WP_004330816.1
KEYWORDS    RefSeq.
SOURCE      Porphyromonas asaccharolytica
  ORGANISM  Porphyromonas asaccharolytica
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Porphyromonadaceae; Porphyromonas.
REFERENCE   1  (residues 1 to 242)
  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   2  (residues 1 to 242)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Porphyromonas asaccharolytica"
                     /db_xref="taxon:28123"
     Protein         1..242
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=27390
     Region          110..172
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mnsfkrgrte twvliavsli ilaaigkvlw dnnyqaqsla plagqtiseq ivslptdsiq
       61 rrasgtyapp lqpdksqkdv sgasqgiels adyvgapeqq kyssqpklre gqridlnsad
      121 tltlqqvpgi gpsfarrivk yrdqlggyyt vlqlqeiygm epdryqrikp ffyigirnys
      181 tpfdalrsds ipshpylnyr qqaalarsir kngtidswhr imsleefnrd dsvrlshyfh
      241 fk
//
LOCUS       WP_004330986             140 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Porphyromonas asaccharolytica].
ACCESSION   WP_004330986
VERSION     WP_004330986.1
KEYWORDS    RefSeq.
SOURCE      Porphyromonas asaccharolytica
  ORGANISM  Porphyromonas asaccharolytica
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Porphyromonadaceae; Porphyromonas.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Porphyromonas asaccharolytica"
                     /db_xref="taxon:28123"
     Protein         1..140
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15667
     Region          56..123
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mtilsgslva qeraqeqdif thittqssgg qvtitqpnwl rsvvgksfht psgiitgyri
       61 qvytsnmrga kqeayrlasq lrgaapelss yvtysapfwr lslgdyasrh eaqqqlnalr
      121 ashprlmrea yivrekirvr
//
LOCUS       WP_004331292             338 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Porphyromonas asaccharolytica].
ACCESSION   WP_004331292
VERSION     WP_004331292.1
KEYWORDS    RefSeq.
SOURCE      Porphyromonas asaccharolytica
  ORGANISM  Porphyromonas asaccharolytica
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Porphyromonadaceae; Porphyromonas.
REFERENCE   1  (residues 1 to 338)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Porphyromonas asaccharolytica"
                     /db_xref="taxon:28123"
     Protein         1..338
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=37908
     Region          202..337
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mknimtflpl altlllacqp stessaevtp tdtiaiadti vaepqpelta dqividrelt
       61 fdkytledsy eykektrtiq wdkiqaqllr ieqlqaepqq wgvlqnykna ngeapltkaw
      121 srdsyklvsd slgveryqsv plyapsdtlt pelygrdgtl iamtdtlgsk fwqgrvespe
      181 aewyvprryv qllkpdvtfs hvvvvdrknq hivvlerqsp ahylvrsinp attgrhkpph
      241 aketplgifl lqqkkpkmfy tsdgssriag fapwasrftc gayihgvpvn npkgkiveys
      301 pslgttprsh mcvrnassha kfvydncptl atlivvie
//
LOCUS       WP_004332664             817 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Thauera linaloolentis].
ACCESSION   WP_004332664
VERSION     WP_004332664.1
KEYWORDS    RefSeq.
SOURCE      Thauera linaloolentis
  ORGANISM  Thauera linaloolentis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 817)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 817)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 817)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Thauera linaloolentis"
                     /db_xref="taxon:76112"
     Protein         1..817
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88425
     Region          68..118
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          95..817
                     /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 mscpprsirr tmtpaaralf vaflgasavl alptspahaa eagatvdidi pagsldqaln
       61 rlgrqtgiql avnaeltagr qspgvsghhs veaalrrlla gtgleavrdg sgeytlrklp
      121 pavsgeatlt avtvtaagfg attentgayt tgsastatkm nlslretpqs vsvltrqqid
      181 dqnlttldda vqqitgltmq kgyytgdsgs fsargfpvan llldgvptsa gangtfnadn
      241 daldiydrve vvrgatgltt gagtpsaain lvrkrptaet qgrvtlsags wdnyramvda
      301 ggplnqagtl rgrvvatvqd adkfydvahd rnhqlygile adltpgttat lgfhyrkvdn
      361 dgllpglptn pdgsflsglr rsanpandfd ywkqtdktlf aelthrfand wqlkaaalwk
      421 rpeqdmlfsg lyrnggvlrq stqhyrldne qdsydlalng pfslfgrthe lmlgasyrsr
      481 dnlnwggwae yswtaagpav dpydwdssav pkpaidmtrw aidnttrqka vyaatrlnla
      541 dplkliagar inwyenenhl tgasykvdhe ltpylgaiyd vndnhsayas wteifepqgs
      601 ydssgklldp itgtnyeigl kgeyfggrln aslaaflikq qnratddlag pnpcpgsawg
      661 ycqrasgeve skgveleigg altpdwqlma gytyvsakyt kdadrsnigk pfdsdlprhq
      721 lklsssyrlp gelarwrigg nlyaqnrika sddsrirhsg ytvvglhtay sldkqteirl
      781 nvhnlfdkry yqnigwstgg nvfgvprsft ltamysf
//
LOCUS       WP_004332670             827 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Thauera linaloolentis].
ACCESSION   WP_004332670
VERSION     WP_004332670.1
KEYWORDS    RefSeq.
SOURCE      Thauera linaloolentis
  ORGANISM  Thauera linaloolentis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 827)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 827)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 827)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..827
                     /organism="Thauera linaloolentis"
                     /db_xref="taxon:76112"
     Protein         1..827
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89481
     Region          86..136
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          115..827
                     /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 mntvrpfhps hhqsrplrpa apdhaaafrl halalgcvia lgtlaiappa haqqnggtea
       61 ravlafdqpa qplgeainal arharvqivf aasategfta palrgsytpr qaldrllags
      121 glvathaggs fiiqtrphap eatlkavtvs aqhdrsgtte gtgsytqrgp sgtatglals
      181 lretpqsvsv mtrqrmddfk letltdvleq apgvtvsrqn dmttfnvrga tvnlqtdgar
      241 rtsagwgwnt hivhtlddla eidrvevlkg ssglingdga ygatvnlirk rptrefqasv
      301 tagagswdny rldtdvggpl nadaslrgrl vaahkesktf ngketdssml ygtleydlgp
      361 dtlasagltw rqreqrgagg ttpiqgfdgn gnavprmard ynigapwagy eqdslnafar
      421 lehrfangwt gklqithdgi etpkmhigsl ryalpavtgq fglykdiesr dqslivdlqg
      481 pfqlfgrehk lllgagasrs rttllrggpp daalppgvey aqggsvipqp ddalstysnd
      541 kfsskrryly aasqlsladp vklivgtrvs nyeqkdvtdi gwynydlnek gvvtpyaglv
      601 vdvardisvy asyasiyqvq sakdanertl dpeegltyev gakgeffdkr lnasasyfwm
      661 rtdntaeeig lndrgdsiyr avmgtirrgy elelsgelar gwqaqgsyvq nssdldsssa
      721 tpkhqfklgs twqftggalr gltvgaatrw qsaisvqrgn arlgqdaywl ldlmaryqid
      781 erlsisanln naldkkyfag vtnfnaqglf ytwgaprsft aslrydf
//
LOCUS       WP_004332718             845 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Thauera linaloolentis].
ACCESSION   WP_004332718
VERSION     WP_004332718.1
KEYWORDS    RefSeq.
SOURCE      Thauera linaloolentis
  ORGANISM  Thauera linaloolentis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 845)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 845)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 845)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..845
                     /organism="Thauera linaloolentis"
                     /db_xref="taxon:76112"
     Protein         1..845
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=92174
     Region          74..125
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          104..844
                     /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 mkqparssgt ahhssrlrmh alartlrhva lgaalastll pvalhaqqee sraytipags
       61 ltdvlnrfgv esglllsfst elttgrqspg lqgryttaaa lhellrqsgl eavpqprggy
      121 llrqapasgn aelptrlaav rvlarragdg ttedsgayts rvtsiasktd mafreipqsv
      181 svltraqidd qklvdindal klmpgvtvnr mndnsfnfys rgfqitsmqv dggaplalga
      241 ytysplqdma fydrvevmrg asgllggmgd pggiinlark kplaeartvl elsagswdhy
      301 ramadfsrpl tedghirgra vvlyenrdyh ldhrsterpa fygvveadlg ddtlltlggs
      361 fnrrketggg sglpryadgr aldlkrstsl tqpwaykdsd etevfaqlah tfangwalkl
      421 nlthsetdte antafvggpv dpatglgvwa gghyeyenqq dlvdlnlsgn fklfgrthel
      481 lvgadwqrvt srwvastfpg hwsdpadvld sggnwnpdrd vslrnhlryg pwgqeqvggy
      541 avlrlhptdr lhvvagvras rydfdqrvss assasapwtt tsdlpftlkt kitpyggviy
      601 dlndawsayl syagiykpqs lmlagpppgs gsldpvkgks yeaglkgely ggrlnatfsv
      661 fnvertgtal ldarypsnyd awagnccylp qgkvtsrgvd veiggellpg wqialgytyn
      721 rtrdenagnt fstitprhll klstaytlpg dwsrwkvggs ahvqsrtlvs gsatingadr
      781 aydfreggya vvnamvqyrl dpqwtlalnv nnlfdreyye rigdttngnw fgtprsamlt
      841 ltwrq
//
LOCUS       WP_004332731             804 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Thauera linaloolentis].
ACCESSION   WP_004332731
VERSION     WP_004332731.1
KEYWORDS    RefSeq.
SOURCE      Thauera linaloolentis
  ORGANISM  Thauera linaloolentis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 804)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 804)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 804)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..804
                     /organism="Thauera linaloolentis"
                     /db_xref="taxon:76112"
     Protein         1..804
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86965
     Region          66..117
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          93..804
                     /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 mahpfpshpr plvhalraal lglalagpta almstsaqaq taprnyhipa gpldralttf
       61 aaqanitlsf dasqtrnlha palnggytpd aglarllags gleaihrgeg nyvlrkatsp
      121 aaappdtqls avvisgkapg aitegtglyt tyssssstrl nlapqetpqs ltvvtrqqie
      181 drnvttltel ldtvpgvhva kegvgdeiyg yyargfeirn feidgvptnd glqlfsqnla
      241 iydrveivrg atglisgmgn paatinlirk rptlkpqasl sveagnwsrr gaafdvsgkl
      301 ndsgsvrgrl vgdakrsgnw ldrykeesgt lygiaeadld datlltagfs hqrtdidspl
      361 rsglpgfyad ggrtrlsrst naapgwsynd qkttsafvsv erewsngwsg kaeytytevd
      421 ydfvatylng alqrdgsgls llptrwkgkp tqhnldlylt gafrlfgreh eliggltlsr
      481 yktsgpsygg wqydyasspa gaidnlftwd gsnaapafta sggsstktrn naaylssrlh
      541 lsddlklilg trvvrweqde rnwgddgsas leslrenvvv pyvgavyaln kewsayasat
      601 kifnpqsswv kdesdstldp legtgyeigi kgghfggrlq ssaalfhtrq dnlpvwtgvg
      661 liysaeqdtt skgielevng eltegwqlaa gyahtrttda dgerlntflp rnslklytry
      721 rlpgalrglt vggglrwqsk tgsydvwqgs qtiaslmary qidrhlsvsl nvdnlfdrty
      781 yswpgsysny aaprstmlsm kyaf
//
LOCUS       WP_004334275             195 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Porphyromonas endodontalis].
ACCESSION   WP_004334275
VERSION     WP_004334275.1
KEYWORDS    RefSeq.
SOURCE      Porphyromonas endodontalis
  ORGANISM  Porphyromonas endodontalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Porphyromonadaceae; Porphyromonas.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Porphyromonas endodontalis"
                     /db_xref="taxon:28124"
     Protein         1..195
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22003
     Region          7..161
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mmekkqllel lesnrsyrrf dssvqlseke irswiealry tasaknaqpl kyrivtdkaq
       61 vdavfallhw aaylpdwqgp slkerpvafv iqvldrtisa ssrfdegiql ealtlmarss
      121 gyggcilaaf dsakmsdlls ldtdrytpit vvalgkpiee vviealptpd gdiryyrted
      181 kvhhvpkrtm dqlii
//
LOCUS       WP_004315208             358 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-oxoacyl-ACP synthase III family protein
            [Bacteroides].
ACCESSION   WP_004315208
VERSION     WP_004315208.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 358)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..358
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39897
     Region          9..341
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mdfrfknkki tgilsilpsk eiyfdneley ynfseskatk lkltmgynkr rifdkelcvs
       61 dicvqgmeyl fatgklckkd idamilvtqs qdyflpptcn liqgrlglgv dvlcmdivqg
      121 cagyilgliq afmlleqqni nkvvlfnadi lsrkvsrydr qispmlgdac sitiveksda
      181 pcdilcnynv dggramsvni paggwrepst sqsaileedk dgnrrsrndm vedgsqifnl
      241 iqlnvpkmih hvldaagtsk seidyymvhq pnrfmiqkla dkisvprdrm psnivenygn
      301 ssgvtipvni vhnlgsllis gkkklllagf gvglawgati ldignldfce mfevnnee
//
LOCUS       WP_004334820             495 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Pseudoalteromonas distincta].
ACCESSION   WP_004334820
VERSION     WP_004334820.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas distincta
  ORGANISM  Pseudoalteromonas distincta
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Pseudoalteromonas distincta"
                     /db_xref="taxon:77608"
     Protein         1..495
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54201
     Region          1..495
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mkpliklhpt ddvaiamrni tageilpvdg eeilvnenid kghkvalrdi nkqenvikyg
       61 apigfaleni qkggwvhthc vkttlndeld yqyipefieq seatpspevn iyrrqngeig
      121 irneiwlipt vgcvngminq mikefklrhp qleidgiyaf phqfgcsqlg ddldttrill
      181 qnmalhpnag galvvglgce nnqlpafrdg lgdydegrik flitqqadde ieegvalleq
      241 iyaqvkqdkr qpgtlsevkf glecggsdgl sgitanpmlg yfsdyliaqg gttvltevpe
      301 mfgaetllms rckdeetfnk lvsmvnnfkg yykahnqpiy enpspgnkkg gittledksl
      361 gctqkagtsk vqavlhyger lqipglnlld apgndpiats algaagchmv lfttgrgtpy
      421 ggfvptlkia tnselankkk rwidfdagvl indasmeqvq gefvellvni vngqptcnei
      481 ndirevaiwk kgvtl
//
LOCUS       WP_004337091             158 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Prevotella bivia].
ACCESSION   WP_004337091
VERSION     WP_004337091.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 158)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..158
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17641
     Region          1..150
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mdltekyeal lpqfkglisd etnivgilan vsallqstfa drffwtgfyl kqndttltlg
       61 pfqgtvacys ipfgkgvcgt twkegktliv ddvekfpghi acsslsrsei vvplydskhn
      121 fygvldidst evgtfnevdk kyleqmmeil mieieyll
//
LOCUS       WP_004337479             292 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Prevotella bivia].
ACCESSION   WP_004337479
VERSION     WP_004337479.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 292)
  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 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 292)
  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   4  (residues 1 to 292)
  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 292)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..292
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33562
     Region          <93..292
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          213..292
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mtdsfeeitv sraktkyagg gyiedefilf demsnvpmpk gfvrfqsvlf avctkgsady
       61 klntnsihie agdaiivtsg qvlsdvhlsd dcrgfgfmvs ldffhyilsg mtnlsslflf
      121 srthpvfrit leqiddileh ckrarkrlfd hthpfrreli acllramiyd fgniiysaqh
      181 lattkltrae ilfnefikcv qdnfrterrv awyakslnit skylsevvks iskrtpsdwi
      241 dyyvilelrv llrssdlsvk eisdqlnfan qsfmgkyfre hvgispskfr ks
//
LOCUS       WP_004337693             371 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Thauera linaloolentis].
ACCESSION   WP_004337693
VERSION     WP_004337693.1
KEYWORDS    RefSeq.
SOURCE      Thauera linaloolentis
  ORGANISM  Thauera linaloolentis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
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   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   3  (residues 1 to 371)
  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   4  (residues 1 to 371)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 371)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 371)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Thauera linaloolentis"
                     /db_xref="taxon:76112"
     Protein         1..371
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39251
     Region          24..359
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(100..102,123..124,173,225,249)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkktllalal vsagfaaqaq tvvkighagp ltgpiahfgk dgengarlal edanakglvi
       61 ggqtvkfelv seddqgdprt attaaqrltd agvkgvight tsgasipasr vyeqagvpvi
      121 tpsstspklt qqnykttyrv iandlqqgea makyaidtlk vkkfaviddr taygqglada
      181 faesikklgg eivgreftnd katdftailt kikartpdai fyggmdsqga pmlrqlrqlg
      241 ipatflggdg nctsemlkla gdamnekvfc tqagipltqm pggneflsrf rqrfnadvli
      301 yapyaydaas alvegmkaad stdpakylpa mqkvdfkgvt ghiafdargd vreggvslyn
      361 yangkwepvk q
//
LOCUS       WP_004337690             371 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Thauera linaloolentis].
ACCESSION   WP_004337690
VERSION     WP_004337690.1
KEYWORDS    RefSeq.
SOURCE      Thauera linaloolentis
  ORGANISM  Thauera linaloolentis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
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   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   3  (residues 1 to 371)
  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   4  (residues 1 to 371)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 371)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 371)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Thauera linaloolentis"
                     /db_xref="taxon:76112"
     Protein         1..371
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38807
     Region          25..363
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(102..104,125..126,175,227,251)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkktivalav mgiglgaaha qqvvklgnaa pltgtishlg kdlengtrma vetvnaqgga
       61 diggkkvkfe ligeddqadp rtgttvaqrl vdagvkgvvg hlnsgtsipa sriydqggip
      121 qvspastnpk ltqqnfkgvf rtiandvqqg galgdfavkt lgaarvaivd drtaygqgla
      181 detdkavkaa gaqvvareft tdkatdfnai ltkiraanpd viffggmdaq agpmlrqikq
      241 lginakfmtg dggcspemik lagdainstt ycsmaglpie kmpggakfre dykkrfngev
      301 qiyapyayda amaiikamek agsvepakyl pelkasnfdg vtgnvsfder gdlkegavtv
      361 yqfkdgnwva l
//
LOCUS       WP_004338171             401 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Prevotella bivia].
ACCESSION   WP_004338171
VERSION     WP_004338171.1
KEYWORDS    RefSeq.
SOURCE      Prevotella bivia
  ORGANISM  Prevotella bivia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Prevotella bivia"
                     /db_xref="taxon:28125"
     Protein         1..401
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44125
     Region          1..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mnilvlncgs ssikyklynm edesvlaqgg aerigldeaf vkvtlsdgsk kkimhdmpdh
       61 kegvkfvfel lldkeigaik sldeidavgh rvvqggdlfe ksclvtkdve dgierlidla
      121 pvhnlghlrg iravdalmpn tpqvtvfdna fhstmpqyay myavpyefye kyhvrrygfh
      181 gtshryvsqr vcdmlgvdik dqkiitchig ngasvaaikg gkvidtsmgl tpleglmmgs
      241 rsgdidasvv tylmdktgkk pqemadflnk esgvlgitgi ssdmreiesa yekgderatl
      301 alqmynyrik kyigayaaam ggvdiivwta gvgenqtstr meacsglefl gvkmdaernn
      361 vrgketiisa edskvkvvli ptdeeiviar dtqeivknlk k
//
LOCUS       WP_004340231             158 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Segatella buccae].
ACCESSION   WP_004340231
VERSION     WP_004340231.1
KEYWORDS    RefSeq.
SOURCE      Segatella buccae (Prevotella buccae)
  ORGANISM  Segatella buccae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 158)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Segatella buccae"
                     /db_xref="taxon:28126"
     Protein         1..158
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16960
     Region          2..157
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mnmttkesry etlvaqvaal iegetcrmsv lanvtaalhd afpeiffwvg fymvedgelr
       61 lgpfqgpvac mhiacgkgvc gtawaekrtl vvpdvedfpg hiacsslsrs eivvpvfgrg
      121 gsvkavidvd scslgafdev darylekiak nlskelal
//
LOCUS       WP_004340301             827 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Thauera linaloolentis].
ACCESSION   WP_004340301
VERSION     WP_004340301.1
KEYWORDS    RefSeq.
SOURCE      Thauera linaloolentis
  ORGANISM  Thauera linaloolentis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 827)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 827)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 827)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..827
                     /organism="Thauera linaloolentis"
                     /db_xref="taxon:76112"
     Protein         1..827
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89531
     Region          74..124
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          101..827
                     /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 mphnrpfpvr tplasairlm lcgallagga iqaparaqla epagsapasa graydiaags
       61 ldqvlgrfgr eagvmiaidp eltqdvrsag lrgthttasg laailavhrl eavpganggy
      121 rlrrlppaad trlapvtvta qaerggtteg tgsyttgsmn tatkmplsir etpqsvtvmt
      181 aqriedqglt slsdvvqatp gltvtkwgge ryrftsrgfq vnnlmvdglp iqyeeaalst
      241 gamsmydrve vmrgaaglme gegtpggsin lmrkrptref qgsltgsvgs wdnylgsldv
      301 ggpineagtl rgravvshqd kksfiddyen krtlvygile adltpattat lgfsysnedn
      361 pgvdwngigt wpdgsflpis rstrmspswa ywdkksttvf advehrfdng wkaklaatsi
      421 dsemdmmgty lanqtaapsy nlvggspayr yardqysida haagpvrlwg gthelvfgas
      481 hrknkwkdeg aptdftpvsf npldwsprsv pkptitgswn lwtrdaereq tgiygsgrfk
      541 lsdpltliag arvdwykqti aqqwggsayg asdfkvdhef tpylgavydl nvqhsiyasw
      601 trifnpqdyy tadgglldpq tgsnyevgik geyfggrlna saaifqidle nlpdglpvsq
      661 catgltscyr sagevrsrgv efelngelap gwqmatsyty asakrlseas aydpigsysi
      721 gkryatnipr hlfklatsyr lpgelsrwkv ggslhvqdgv kspwgvkqgg yaiagmhasy
      781 avtrqldlsl nvnnlfdrky ystigsysda nffgdprnfl ltakyrf
//
LOCUS       WP_004341818             810 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Thauera linaloolentis].
ACCESSION   WP_004341818
VERSION     WP_004341818.1
KEYWORDS    RefSeq.
SOURCE      Thauera linaloolentis
  ORGANISM  Thauera linaloolentis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 810)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 810)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Thauera linaloolentis"
                     /db_xref="taxon:76112"
     Protein         1..810
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88694
     Region          61..111
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          88..810
                     /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 mphrtlprls llalavaqlt lapalaaepa aaanaavqrs ydipagplea alnrfgreag
       61 itlsfstdla aglrspglqg shdpagglar llqgtglaae argdgsytly rlpmsvgeat
      121 lapvtvmeqn vrdgttedtg syttgsmsta trmnlsiret pqsisvltrq rmddqametl
      181 edvventpgi ilskaggerp aiyargfwlq kmtydglaga ydgdyvgspn lamydrveiv
      241 rgatgltsga gtpsaainmv rkkptrdfql nltgsigswd nyrtevdaag plnqqgslrg
      301 ravlsyqdkd sfidvvnnks slvyatlead lgprtmlsvg gsyqkddnrn twggvpwaad
      361 gsdlhlprss yfgydweywd kenkevfiel qhrfandwnl rltgrkgwsd maylgthltn
      421 yntwaqpgae ydayldtssy einvsgpfal lgrqhelvlg tsfqesdrll aggqgilrnt
      481 gidiynwdsg slarpafdls mlrnnylieq rsayattrln phddlkiilg trldwyqydt
      541 dtswmgnatt sgykvtrnvt kyagviydln ehhsvyasyt difepqsqsg fsgelldpil
      601 gknyeigikg eyfggalnas aalfridqvn raalaqnqag cpinncyeas gkvrsegvel
      661 evsgalnpnl nlaagytytd atyvrndtnt aqegtrfdta fpehlfklgt tyrlhgalnq
      721 wrvgagiqwq seiykegvna gtpfrieqka yavanitlgy qasknvdlql nvdnlfdkry
      781 yhslgshpgw ggvarygtpr nfmltarykf
//
LOCUS       WP_004334620             182 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Porphyromonas endodontalis].
ACCESSION   WP_004334620
VERSION     WP_004334620.1
KEYWORDS    RefSeq.
SOURCE      Porphyromonas endodontalis
  ORGANISM  Porphyromonas endodontalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Porphyromonadaceae; Porphyromonas.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Porphyromonas endodontalis"
                     /db_xref="taxon:28124"
     Protein         1..182
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20146
     Region          98..164
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mvrysisntt sgrtlfrgma lvlfislvsc iqgyaqteke slshgangif ealsaqregq
       61 gtiditqped iknqvglvhq kqarhseger sgvhtqqgfr iqaytgnlak skeeayrrak
      121 vvnaanpalg cyvtykspfw rlsvgdfrtr eeaqkamqdl kraipaiape lyivrdnirv
      181 sn
//
LOCUS       WP_004342328             380 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Segatella
            buccae].
ACCESSION   WP_004342328
VERSION     WP_004342328.1
KEYWORDS    RefSeq.
SOURCE      Segatella buccae (Prevotella buccae)
  ORGANISM  Segatella buccae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 380)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 380)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Segatella buccae"
                     /db_xref="taxon:28126"
     Protein         1..380
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42904
     Region          5..365
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mkefdslkvm yhdrlvgrlt mgtndtclfq yekewldsgf sisplklplr adlfeadylp
       61 fqgnfgvfed smpggygeyv lqkelekrgv nykalnplqr lsivgssgmg alcyipdnki
      121 tmprgsvdld evqqsaldvl sgktdenagr lyvdsgnsgg vrpkmllqde grnwlvkfrh
      181 tydpiasgvi efmynqaake agitvprfkl fkgryfgeer fdlspdgkri hmvtasglln
      241 eginppkmdy kallaltgyi tqdhieveqq frrmvfnyya enfddharnf sflyvdgkwk
      301 lspaydmthd splgqhattv gykanpteed fieagasvqi trqlctdiid evkpigqrlv
      361 krlkesclse kksgnekvkk
//
LOCUS       WP_004342878             360 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Thauera linaloolentis].
ACCESSION   WP_004342878
VERSION     WP_004342878.1
KEYWORDS    RefSeq.
SOURCE      Thauera linaloolentis
  ORGANISM  Thauera linaloolentis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 360)
  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 360)
  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 360)
  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 360)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Thauera linaloolentis"
                     /db_xref="taxon:76112"
     Protein         1..360
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39959
     Region          1..354
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 merrkflqga gmagilaags apaivqaqqq irwrlassfp ksletvygas eafakyvsda
       61 tggkfvisvh pggelvpafg vvdaiqqgti dcahtapyyf fgkdesfald ctipfgmtsr
      121 amsawmfegn gmklmrefya qfniinfpmg nsgaqmggwy rkeikslkdf dglkfrvggf
      181 ggrvlaklgv vpqniaagei yqalekgtid aaewigpydd lrlglhkvak nyyypawweg
      241 stqfslyind kqwnglsaey kaiieqasra ahltcqaryd arnptalkql vaegaklsrf
      301 pkdfmdaafk asrevyaeln dknpnwkkiy pdysrfladq vqweavaesn ysqylasqkl
//
LOCUS       WP_004343763             419 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein [Thauera
            linaloolentis].
ACCESSION   WP_004343763
VERSION     WP_004343763.1
KEYWORDS    RefSeq.
SOURCE      Thauera linaloolentis
  ORGANISM  Thauera linaloolentis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 419)
  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 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   3  (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   4  (residues 1 to 419)
  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 419)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Thauera linaloolentis"
                     /db_xref="taxon:76112"
     Protein         1..419
                     /product="CmpA/NrtA family 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=44656
     Region          43..294
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 metlktetpe lsrrgfikag aaagaaallp glfpggawaa gsdapekkei rvgfipltdc
       61 asvvmaavkk fdekygiriv pskeaswasv rdklvsgeld aahvlyglvy gvhlgiggpk
      121 kdmamlmnln hngqaitlsk alreagaadg aglgkvvaas spgtytfaqt fptgthamwl
      181 yywlaahgih pfrdiksivv pppqmvanmr vgnmhgycvg epwnqravid gigftaaatq
      241 diwpghpeki lgtsadwvak hpnaaralta avldasrwid asdvnrseta rtiaarsyvn
      301 tdvaviegrm lgdyddgagr qwkdahgmkf fgdgavnfpw lsdgmwfltq hrrwgllerd
      361 vdylatarai nhidiykqaa taagvavpag emrsatlidg vvwdgsnpaa yaagfkika
//
LOCUS       WP_004343861             791 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Thauera linaloolentis].
ACCESSION   WP_004343861
VERSION     WP_004343861.1
KEYWORDS    RefSeq.
SOURCE      Thauera linaloolentis
  ORGANISM  Thauera linaloolentis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 791)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 791)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Thauera linaloolentis"
                     /db_xref="taxon:76112"
     Protein         1..791
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=85310
     Region          47..97
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          76..791
                     /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 mklrktllaa avlslgmhaa aasaapfdlp aqsldqalge farqaglqll aspsltqglq
       61 grpvtratsv sdalvqllag tglhgrvegg aliieragge avlpavsvta qglggahdas
      121 pvatrsygst ktdtaiveip qsvsvvtrqq mdemgaqsve qsvgylagvg tgiygkdsrv
      181 deiwvrgfrt gsfannmyvd glrppgssag aaalstrfds yglervevlr gpssvlygqv
      241 tpgglvnirs krppqeaqhq vglqtdsegl iranvdiggp lddertwlyr lvssasrtdt
      301 evdhvelerf ffnpsltwqp sartsvtllv nhqrdrggat wqrlpvvgty ldsphgkvsr
      361 sffqgepdfd rydrdqtavg ysleqfiges vklrqnvryi evdmnydsvs rrslgadgrt
      421 ltgnaeshen hskgfsadtn llyaletgav ahmllggfdy qkvdielasa tgtvgpldly
      481 apvygspvvi gertpnsesg riqsgvylqd qmfwnkwtlt aglrhdwart rtvslrsntr
      541 tsesteattg rlgvtylfdn gvapyasyst sfvpssgedy hgkafdpveg kqielgvkyq
      601 ppgsrnlvta slyemtqsni ltpdpdptht cngglcrvqt gegrvrgfel egtyaltral
      661 tlsgsytymd tevtesnstd lgkrlahvpk emmaarfdwr aarglhlglg arytgssygd
      721 nantlknasr tlvdaslryd laeldqslrg lrlsvsasnl ldkeyvtcng ltsfcfygag
      781 rlvsatlsyd w
//
LOCUS       WP_004344951             295 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Pseudomonas].
ACCESSION   WP_004344951
VERSION     WP_004344951.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            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="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32112
     Region          3..278
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mrvdlhchst asdgvlapaa lvqrahekgv gllaltdhdt leglpeahqa aarlgielvn
       61 gvelsctwgg atihvlgygf dldaaplrqa tealhrgrwa raeeidrrla akgmpgaleg
      121 araiqqalgd sgnaparphf aeflvqggwv kdradafrkw lgagklgdvk qhwptleevv
      181 gclrearawi slahpyhydf trtkrrrlva dflqagghai evvngvqpae qvgtlsilar
      241 efglmvtsgs dfhapgdwse lgmyravped lpamwprfar hfrdierhse akgae
//
LOCUS       WP_004346389              67 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase, partial [Thauera linaloolentis].
ACCESSION   WP_004346389
VERSION     WP_004346389.1
KEYWORDS    RefSeq.
SOURCE      Thauera linaloolentis
  ORGANISM  Thauera linaloolentis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 67)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Thauera linaloolentis"
                     /db_xref="taxon:76112"
     Protein         1..>67
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
     Region          2..>55
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mhirvdigrq clglfgddga cirrypvsta lngageeags qrtprgrhri rarigagapa
       61 gavfrgr
//
LOCUS       WP_004347228             278 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptococcus parauberis].
ACCESSION   WP_004347228
VERSION     WP_004347228.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus parauberis
  ORGANISM  Streptococcus parauberis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 278)
  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 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   3  (residues 1 to 278)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 278)
  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   5  (residues 1 to 278)
  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   6  (residues 1 to 278)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Streptococcus parauberis"
                     /db_xref="taxon:1348"
     Protein         1..278
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31821
     Region          30..102
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          125..276
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mmhqfnktid ylestltsev elkkfqnisg ysyplfsrif silseitlae ylrnrkltla
       61 vddllntdqk vidialkyny dsadafsfaf kkfhgnspse vrkgknyklf pkmklalkvi
      121 ggsqmnikie tkpsfkvagv lkenidsnqc pstwdelysk ysfeqlesfg ngqslgvcye
      181 nevndkinym agynvlddak arnlgldile vkeseyavvp vkgsvpdsih qawkylleef
      241 fpengykhsg lpdfevyten dihdpnyeme lwvpivkq
//
LOCUS       WP_004348669             400 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Hoylesella buccalis].
ACCESSION   WP_004348669
VERSION     WP_004348669.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella buccalis (Prevotella buccalis)
  ORGANISM  Hoylesella buccalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 400)
  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 400)
  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
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   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   5  (residues 1 to 400)
  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   6  (residues 1 to 400)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 400)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 400)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Hoylesella buccalis"
                     /db_xref="taxon:28127"
     Protein         1..400
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44127
     Region          20..71
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          79..394
                     /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 mktilkleyl hrkpdnykti lkylmlhdgc tipeiskhig isvptttkii tnlmskgfvv
       61 skgkrdqthg rlptvyglst dsgyflgidp sydslamalc dfsgnivfek nkipfqlent
      121 qqcldtlldl vneyigsldi qkesilhasm nvsgrvnpft gvsysifdfl nqplakyisd
      181 qigiptcien dtramtfgey lvgccksakn vlfvnaswgi aigiivggki yygksgfsge
      241 fghvkaydne vlcrcgkkgc letevsgmal lretvknvlk gkrsilsdkv lkenkeltls
      301 dvlyaiqked tlcietlqki adqlgrnlag minifnpdml iiggdlsqtg dyitqpvqma
      361 ikkyslnivn edsevvtstl reragvvgac mvaryqvvrd
//
LOCUS       WP_004348724             282 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: aminoglycoside phosphotransferase family protein
            [Pseudomonas].
ACCESSION   WP_004348724
VERSION     WP_004348724.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 282)
  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   2  (residues 1 to 282)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            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="aminoglycoside 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=30814
     Region          11..242
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 maacpelada tfailasgwh stavevggrw vfkfprgaea eaallreaav lrlvrpavsl
       61 pvpapqvfag pplfshhekl pggyllgedy rrldeparqa vgdalgrfya elhrlpparm
      121 ravgalpvrp wesptamrrr alpllpaawr eraerlvrey aklpadplgs ifgffdghgw
      181 nmafdseagr lngvydfada gigplhqefi ysafidadlt erivaayerf sgrrlerrri
      241 alltaahrls elaeladepr hlpdmlagal dglalaeaqg la
//
LOCUS       WP_004349288             131 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Hoylesella buccalis].
ACCESSION   WP_004349288
VERSION     WP_004349288.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella buccalis (Prevotella buccalis)
  ORGANISM  Hoylesella buccalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 131)
  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 131)
  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   3  (residues 1 to 131)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Hoylesella buccalis"
                     /db_xref="taxon:28127"
     Protein         1..131
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15452
     Region          28..128
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mhnkkhdfgy ataapdryqm lkeyakqlrk nmteaetilw eelrqldgyh frrqhpindy
       61 iadficlsah liievdgkyh dvpqqqtedd trtdalskmg ytvvrftnee iitdvdrvvd
      121 eiynildeqd e
//
LOCUS       WP_004347431             207 aa            linear   BCT 20-JAN-2025
DEFINITION  RHS repeat-associated core domain-containing protein [Hoylesella
            buccalis].
ACCESSION   WP_004347431
VERSION     WP_004347431.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella buccalis (Prevotella buccalis)
  ORGANISM  Hoylesella buccalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 207)
  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 12859901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Hoylesella buccalis"
                     /db_xref="taxon:28127"
     Protein         1..207
                     /product="RHS repeat-associated core domain-containing
                     protein"
                     /calculated_mol_wt=23130
     Region          <23..159
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
     Region          <23..83
                     /region_name="Rhs_assc_core"
                     /note="RHS repeat-associated core domain; TIGR03696"
                     /db_xref="CDD:274730"
ORIGIN      
        1 mngkvieers mnytsykdyi kipflfqgqy ydeeiklayn rfryydpqmg ryisedpirf
       61 asgkialfay vsdtngwldv fglktysihg nskkspkpnh vyviydrgte evykfgisgg
      121 rirkdtkssr aesqvralna aggnyeskiv rkgstrskal nveqgrvnvy sisaqnagnt
      181 giglsgqsri anapiapegn lrpnpqi
//
LOCUS       WP_004351890             674 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter permease [Pseudomonas].
ACCESSION   WP_004351890
VERSION     WP_004351890.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 674)
  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 674)
  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 674)
  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 674)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..674
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..674
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=71949
     Region          15..671
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 msdhqnglhl eaenwpralf avalafsvfq vvtaafplis tqvlramhvg llllvvhisy
       61 pafgigrpwq plawllgmag lgtavyqwvf egdliqrsge ltqadmvvgv vlivlvfeaa
      121 rrvmgialpi icalflaygl fgehlpgdla hrgygfdqiv nqlsfgtegl ygtptyvsat
      181 yiylfilfga fleqagmirl ftdfamglfg hrvggpakvs vfssalmgti tgsgvanvvt
      241 tgqftiplmk rfgykpafag gveatasmgs qlmppvmgav afimaetinv pyveiakaal
      301 ipallyfgsv ywmvhlearr adlkglprdq cpsawgavre rwfllipllv liallfsgrt
      361 plfsgtigla ltaivilgsa iilrvsslgl riafwvalgl lcagffrlgi gvifvviaal
      421 alacwfvrgg retlricvra laegarhaip vgiactlvgv iigvisltgi attfasyvld
      481 lgrenlllsl vltmvtclvl gmgiptipny iitssiaapa llelgvpliv shmfvfyfgi
      541 ladltppval acfaaapiak erglkisfwa vrialagfvv pfmavyspal mlqeggwgat
      601 lyvtckavla iglwgmasig ylqgplawwe rlvafaagas lvlalpisde lgfvlgalvi
      661 gwhlwrqrar eava
//
LOCUS       WP_004337328             193 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Thauera
            linaloolentis].
ACCESSION   WP_004337328
VERSION     WP_004337328.1
KEYWORDS    RefSeq.
SOURCE      Thauera linaloolentis
  ORGANISM  Thauera linaloolentis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 193)
  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 193)
  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 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   4  (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   5  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10164212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Thauera linaloolentis"
                     /db_xref="taxon:76112"
     Protein         1..193
                     /product="winged 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=20729
     Region          1..>80
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
     Region          9..>164
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mndddllrpr alyeaiadsv rerifthela pgaaldeaal aqgygvsrtp vrealkvlah
       61 eglvqleprr gccvarldah dvddlltvld lleihlleer agaaghvpas tpptghganr
      121 yaadvivrlr eklrlalgpa fsdseamlfe riraeldaal aahdkagsar lyrrfatarr
      181 klacgthacv aaa
//
LOCUS       WP_004353322             715 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate--CoA ligase family protein [Pseudomonas].
ACCESSION   WP_004353322
VERSION     WP_004353322.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 715)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..715
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=75173
     Region          15..713
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 msanhsqqli daprfasltp lieprsvavi gassdptrig grpiaymlrh gyagqilpvn
       61 pnraeiqglp afasvaelpq apdvaivavp apqvletvra lgrqgarsai vfssgfsevg
      121 eagaamqdav vaaareygmr llgpnalgaf nsnlgyyaff stslergvpl pgrvgiatqs
      181 gaygahllgm arqcrlgtpi cvatgneadv tlgdsigwlv espeidvvma yaesirnvds
      241 flaaleaahr agkpvilhkv grsalgsraa lshtaslagd dkvldavlgd yavirartte
      301 elmdiaylat rriypvgnsl gmitvsggag iivsdvaeev glpmppmpdm aqerlkarls
      361 faspinpvdc taqalndltl vrdftesmvv dggyrsllaf ftqagtaasi garlaeqfrr
      421 ikeahperlf vvsvmgegee lapyeeagfa lfedptravv aiqamgrlge afarplrlrr
      481 pagglqlpas tpgeaeakrl laragiesaa eavlgsaeea vafaegigyp vvlklasadi
      541 qhkseiggvl lgvsdadavr agfqlllrra aekapqarld gvlvarqlqg gvecfmgiqr
      601 dplfgpvalf glggifvevl qdvvfrrcpf evdeaeamir sirgapllfg argrpradva
      661 alarllsnls rfaweagerl rsvdlnpvia lpegqgawav davleveeva dgars
//
LOCUS       WP_004354502             150 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Prevotella denticola].
ACCESSION   WP_004354502
VERSION     WP_004354502.1
KEYWORDS    RefSeq.
SOURCE      Prevotella denticola
  ORGANISM  Prevotella denticola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Prevotella denticola"
                     /db_xref="taxon:28129"
     Protein         1..150
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16412
     Region          2..150
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdvlthllld ygywgmllsa flagsffpfs seavmlglla agldpvlllv ygsignvmgg
       61 mfnyglgrlg klewleryfh vkktsidray rfmgghgawm gffaflpilg saitivlglt
      121 ranillsvls itigkvlrya vliwgadfff
//
LOCUS       WP_004354788             813 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Thauera phenylacetica].
ACCESSION   WP_004354788
VERSION     WP_004354788.1
KEYWORDS    RefSeq.
SOURCE      Thauera phenylacetica
  ORGANISM  Thauera phenylacetica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 813)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 813)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 813)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..813
                     /organism="Thauera phenylacetica"
                     /db_xref="taxon:164400"
     Protein         1..813
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86725
     Region          76..125
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          103..813
                     /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 mtkptfsprp qrlalavhaa mmalpmtatg vaifaapsaa haqataqapa qamhefdipa
       61 gplstaltra aaqsgvplta daaltagkta palkgrmtlr ealaqllags glaagtegas
      121 ivikavppap ggakeavlpv vtvragadtd gstasgylvk sasvgalgek slkdtpysie
      181 vysrelmenk qarsladltk adasislqqd nivtennsla irglgpdsat gqkidglnsr
      241 vrandlpleh lerveilkga ggflygfgap ggtinyvlkr ptdepvrsls tqimdsgltl
      301 ihgdlggrfg aqdafgyrvn lvneegatyi ndgksrrhsg slaldwritp dlvwradalv
      361 gehvrkggyw avipnadgaa snwttatple pidgsrrlap tftrygsrhk tygtdlawqf
      421 asdwklslsh risengreft qpaifantng dyslryydla trfesrqsqg visgklstgp
      481 vvhelvmgas hnvtqsfsgp yqasnlanag nlgnpadaas pfpgfasydd aneefgfmrr
      541 relfvsdtlh lgsdwdlivg lrrgrlevkd taynrtattp tlaavfrptq glslygsyve
      601 aleegatape taanayevfa plkskqyevg akaegrnwsa taalfrlqrg ltyttsdnvf
      661 tqdgearyqg leisgkfrls prwlvtastm wldatnqkte ggaldgkriq gvareqtsvy
      721 geysvaglpl tltagaryvg krpvdadnqw hvgsvtllda garyetkwgt kpvslrlsid
      781 nltnkaywvs qsessnlqqg aprtiklgaq ief
//
LOCUS       WP_004354806             820 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Thauera phenylacetica].
ACCESSION   WP_004354806
VERSION     WP_004354806.1
KEYWORDS    RefSeq.
SOURCE      Thauera phenylacetica
  ORGANISM  Thauera phenylacetica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 820)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 820)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 820)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..820
                     /organism="Thauera phenylacetica"
                     /db_xref="taxon:164400"
     Protein         1..820
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87419
     Region          95..139
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          118..820
                     /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 mtnraiharr raatpqaths thlrptplvv alhlalmggt lmasgwstva haqgsgtaas
       61 saeaapkryd ipagpvgtvv arfagasgvl lagaselvqg rnspglsgty tldaaikall
      121 agsgldavrq angsyalrqa apaavptpas pahtaaeavl pvvtvragad ttrtglaaeg
      181 ywvtssgvag fterpikdtp fsvksvssel mlnrgvgdlg kldqidasvs nsysnwypgq
      241 firgfslvnd tnyrrnglaf qqpytvglen kervdvlkgl sglqagfssp ggvinyvikr
      301 pediselhlt vnqfgnakmh vdvgrmltdd vgvrlnaave dernqidhvh gprsfvsgav
      361 awkitpntsf dfdieheqrk ktfqpnltln tdgkipamps pstflgqqwa sfnvdstams
      421 gklehrfssd wssslaighh ilkrdntwlg fdsiapngda dvnlwhspnd kgeatgvrfa
      481 tngkfatagl qhdlafgyeh trvkfawnaa wvsafgstni ynpvalvrps gtydsggdtd
      541 lrrdgffind vvalgekwdi hlggrygvve dqasyadsay ektaftptva lvfkprpdls
      601 ayvsytegle tggtaptgtt nvnqimpplv skqveaglkg eigqlawets ifrisrpaey
      661 tngantyvqt geqlhqglef svsgkvtrev tlfggamwld aklketgdpa tagkrptgaa
      721 nqrvaltaey apaalsgwtf aanlthtgsr avdaantaia pgyelfglgl rhqrkiagkd
      781 vtfrlnvdnl fnkrywakvd ndalevgvpr tvwgglsvaf
//
LOCUS       WP_004355996             402 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Pseudomonadota].
ACCESSION   WP_004355996
VERSION     WP_004355996.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonadota (proteobacteria)
  ORGANISM  Pseudomonadota
            Bacteria; Pseudomonadati.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Pseudomonadota"
                     /db_xref="taxon:1224"
     Protein         1..402
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43534
     Region          7..399
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msnsqpslil vlncgsssik favfpvdadp lprtplwngk vqgiggpapn fgesgvepfp
       61 veldaehpht aalqfiqeri skrldgrrvt tvahrvvhgg srywaptlvt qqmlddlrsy
      121 iplaplhqpf plkamgllle qrpdivqvac fdtafhhslp kveqilplpy sawerglrry
      181 gfhglsydym shalperhgd largrtivah lgsgaslcam qnlesvattm gfsaldglmm
      241 gtrtgsldpg allylmever lsleevgstl ynqsgllgvs gisaeprvvv khendpgeag
      301 erarialaly vrrivreiga ltavlggldl lvftagvgeh nafvrervcr dlaflgikld
      361 adantinapv isttgsrvrv aleptneewv aarctqklmi ag
//
LOCUS       WP_004356473             139 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Thauera phenylacetica].
ACCESSION   WP_004356473
VERSION     WP_004356473.1
KEYWORDS    RefSeq.
SOURCE      Thauera phenylacetica
  ORGANISM  Thauera phenylacetica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Thauera phenylacetica"
                     /db_xref="taxon:164400"
     Protein         1..139
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14829
     Region          1..131
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mqrqpqagft lielmvtvai igilasialp ayndyltkgr ipqatsglan grvlleqwfq
       61 dnrtyakvrd vsppcpantq yftfsgcpse sattytltat gagamsgfvy tineanvmts
      121 ttswgnktnc wvvsknggc
//
LOCUS       WP_004357138             222 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Prevotella disiens].
ACCESSION   WP_004357138
VERSION     WP_004357138.1
KEYWORDS    RefSeq.
SOURCE      Prevotella disiens
  ORGANISM  Prevotella disiens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Prevotella disiens"
                     /db_xref="taxon:28130"
     Protein         1..222
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24872
     Region          126..201
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mkkflttivv vllstlavsa qgtvtvthss didalvngnk kttktnknkp qqpqqtikkp
       61 nvttpgtqrv vpyiapptsn ssgetyqrtk lvrkkvrkpi idpvdgtetk hmvmkrvakg
      121 vkkvrgfrvl aysggntrka rqeaeklgqk akeilvtepi yvhfysprwm cqvgnftnya
      181 qakkvmrklr kegfthanii rtmvtiqttk vlddnpnfdn ey
//
LOCUS       WP_004359660             248 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Thauera phenylacetica].
ACCESSION   WP_004359660
VERSION     WP_004359660.1
KEYWORDS    RefSeq.
SOURCE      Thauera phenylacetica
  ORGANISM  Thauera phenylacetica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  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   3  (residues 1 to 248)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Thauera phenylacetica"
                     /db_xref="taxon:164400"
     Protein         1..248
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27116
     Region          56..246
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 msedtnnddl gregpadehd egeaqrgftf edmrlavgdr lqiectartg vrrafvrvvg
       61 yvdgisllvs tpvsggrrve lvendpvivr vfsrqsafaf rasvlracrl pldyvhlsfp
      121 tviqgsvirk atrvrtqfpv qvsteagsaa gegtmlnlsa tgalihthaa lgeqgsivrl
      181 rfdadlhgvq seldiaaeir nvqqapdaes egieyhygvd fhalgaedrm kikslvyqti
      241 ieqprrii
//
LOCUS       WP_004359733              96 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Thauera phenylacetica].
ACCESSION   WP_004359733
VERSION     WP_004359733.1
KEYWORDS    RefSeq.
SOURCE      Thauera phenylacetica
  ORGANISM  Thauera phenylacetica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Thauera phenylacetica"
                     /db_xref="taxon:164400"
     Protein         1..96
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10691
     Region          1..96
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mdrdlalqkl tqskpelhrr fgvvdlalfg stlrgearad sdvdvlvrfd gpatsaryfg
       61 vqfyledllg apvdlvtdka lreelrhive reavhv
//
LOCUS       WP_004359806             150 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Prevotella].
ACCESSION   WP_004359806
VERSION     WP_004359806.1
KEYWORDS    RefSeq.
SOURCE      Prevotella
  ORGANISM  Prevotella
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Prevotella"
                     /db_xref="taxon:838"
     Protein         1..150
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16269
     Region          11..150
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mesltqllvd ygywgmflsa flagsflpfs seavmlglla agvdpvlllv ygsignvlgg
       61 mlnyglgrlg klewleryfr vkkesldray rfmgghgawm gffaflpilg saitivlglt
      121 ranivlsvls itigkvlrya vliwgassff
//
LOCUS       WP_004359778             295 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Pseudomonas].
ACCESSION   WP_004359778
VERSION     WP_004359778.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            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="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32169
     Region          3..278
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mrvdlhchst asdgvlapaa lvqrahekgv gllaltdhdt leglpeahqa aarlgielvn
       61 gielsctwgg atihvlgygf dldaaplrqa tealhrgrwa raeeidrrla akgmpgaleg
      121 araiqralgd sgnaparphf aeflvrggwv kdradafrkw lgagklgdvk qhwptleevv
      181 gclrearawi slahpyhydf trtkrrrlva dflqagghai evvngvqpae qvgtlsilar
      241 efglmvtags dfhapgdwse lgmyravpee lpamwprfar hfrdterhse akgae
//
LOCUS       WP_004361145             133 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Thauera phenylacetica].
ACCESSION   WP_004361145
VERSION     WP_004361145.1
KEYWORDS    RefSeq.
SOURCE      Thauera phenylacetica
  ORGANISM  Thauera phenylacetica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Thauera phenylacetica"
                     /db_xref="taxon:164400"
     Protein         1..133
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=13538
     Region          1..130
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkkmqqgftl ielmivvaii gilaavalpa ysdyqakakv aaglaeisag ktafeerrnn
       61 aetvasaadi glqtttgnct iaatattitc tlanapsqvn tkvitwtrna tsgawscatt
      121 apakyapktc pga
//
LOCUS       WP_004362673             332 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Prevotella nigrescens].
ACCESSION   WP_004362673
VERSION     WP_004362673.1
KEYWORDS    RefSeq.
SOURCE      Prevotella nigrescens
  ORGANISM  Prevotella nigrescens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 332)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Prevotella nigrescens"
                     /db_xref="taxon:28133"
     Protein         1..332
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36366
     Region          2..332
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mayikaltyy lpkkeltnee lvkdfpewsv ekvaqkvgvn trhiageket acdmaekaar
       61 klfkeyninp etvdfillct qspdyflpst acilqarlgi sktagafdyn lgcsgciygm
      121 aiakgliaag iaknillvts etytkylhps dksnrsifgd gaaaclistn gfaeignftl
      181 gtdgtgannl ivrtgaarhk dttgkrtide eghtnfddyl ymnggnvfnf tldvvppmie
      241 dilkgnnltk eqidyyvfhq ankfmlntir kvcrlskenf yinleetgnt vsstiliglk
      301 dcldkslvkk gdtvmlagfg vglswggtil kf
//
LOCUS       WP_004363567             594 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Prevotella nigrescens].
ACCESSION   WP_004363567
VERSION     WP_004363567.1
KEYWORDS    RefSeq.
SOURCE      Prevotella nigrescens
  ORGANISM  Prevotella nigrescens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 594)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Prevotella nigrescens"
                     /db_xref="taxon:28133"
     Protein         1..594
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=68932
     Region          498..577
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mklfvydlll hpphslktvl ctlyiligga svafadvnta tvhsemsrmp akerlvylrn
       61 acdnaigkdd ekqydllkiy iaeaqkqast vdemyglkrl mcyyynydkd kqlhkelpda
      121 mnkmiaygyt dyyyelwslm ieqhfyteki iqalseakel fddakkrkng yglavannll
      181 geiyadmydg iislrhfaia veyakklkpn nrlliliysn ytdalynerq ysqmlkvaqe
      241 weeklkehae nikkegksls pltpwyaycy laiadaqmqm gnydaansyl qkvastinsq
      301 tirvksayyh sisqfwackk dyekaleysn mclkisasik damgmnslli dhayilnsag
      361 rykeasqlys slmekrdsle enymrnqlne msvnyqlene ranrnqanmn laislsalli
      421 siligvlyyi ytrklrqrer imfktvqrfk lterlnlasl etlseekltm eerlfietcq
      481 mmdrdkpyrd pdfnrdlmat llntnrtylg sairkyadgl tisefitryr lryaaallvg
      541 rpdmnindtg lmagfnsrst ynrlfrnffg vsptsfrdir iqsadeqsse addv
//
LOCUS       WP_004362972             401 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Prevotella nigrescens].
ACCESSION   WP_004362972
VERSION     WP_004362972.1
KEYWORDS    RefSeq.
SOURCE      Prevotella nigrescens
  ORGANISM  Prevotella nigrescens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Prevotella nigrescens"
                     /db_xref="taxon:28133"
     Protein         1..401
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43954
     Region          1..396
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkilvlncgs ssikyklydm adesvlaqgg aervgldeaf vkvtlkdgsk ekimhdmpdh
       61 kegvkfvfql lldpkygalk sldeidavgh rivqggdlfe kscivtkeve egiesliela
      121 pvhnlghlrg ikavdalmph tpqvtvfdna fhstmepyaf lyavpyemye kyhvrrygfh
      181 gtshryvshr aceflgvdyk sqkiitchig ngasmaaikd gkvvdtsmgl tpleglmmgs
      241 rsgdidasav tyimeklgka pqemadylnk esgvlgitgi ssdmreieaa eaagnerail
      301 alkmysyrik kyigayaaam ggvdmivwta gvgenqiglr idackglefl gikmdaeknn
      361 crgvervisa ddskvkvlli ptdeeiviar dtqelvlear k
//
LOCUS       WP_004365622             347 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Thauera phenylacetica].
ACCESSION   WP_004365622
VERSION     WP_004365622.1
KEYWORDS    RefSeq.
SOURCE      Thauera phenylacetica
  ORGANISM  Thauera phenylacetica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 347)
  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 347)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 347)
  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   4  (residues 1 to 347)
  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 347)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Thauera phenylacetica"
                     /db_xref="taxon:164400"
     Protein         1..347
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37937
     Region          34..216
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          260..341
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkilapspae ltrgraatpi afiraiaagy rlrgmdpasa laqaqippal lddpdarvta
       61 aqmelmsgva mqelddealg wfsrrlpwgs ygmlcraslg sptlevalkr wcrhhrllte
      121 divfalaqrg gtatihvteh aalgelrefc lvstlryllg yacwvvdsri alieaafpfp
      181 apahadayay lfagparfsa esasiafdar ylalpvrrde kalqtmlqra lpltvlqyrr
      241 drllvhsvtq llaanpgaah taedvaahln lsvrtlhrql keegvslqrl knearrehai
      301 rlllqsgkpv kqiaaavgfd seksfarafr ewtgvapsgf rtkgegl
//
LOCUS       WP_004366729             401 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Prevotella nigrescens].
ACCESSION   WP_004366729
VERSION     WP_004366729.1
KEYWORDS    RefSeq.
SOURCE      Prevotella nigrescens
  ORGANISM  Prevotella nigrescens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Prevotella nigrescens"
                     /db_xref="taxon:28133"
     Protein         1..401
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43968
     Region          1..396
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkilvlncgs ssikyklydm adesvlaqgg aervgldeaf vkvtlkdgsk ekimhdmpdh
       61 kegvkfvfql lldpkygalk sldeidavgh rivqggdlfe kscivtkeve egiesliela
      121 pvhnlghlrg ikavdalmph tpqvtvfdna fhstmepyaf lyavpyemye kyhvrrygfh
      181 gtshryvshr aceflgvdyk sqkiitchig ngasmaaikd gkvvdtsmgl tpleglmmgs
      241 rsgdidasav tyimeklgka pqemadylnk esgvlgitgi ssdmreieaa eaagnerail
      301 alkmysyrik kyigayaaam ggvdmivwta gvgenqiglr idackglefl gikmdaeknn
      361 crgveriisa ddskvkvlli ptdeeiviar dtqelvlear k
//
LOCUS       WP_004368042             198 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Thauera phenylacetica].
ACCESSION   WP_004368042
VERSION     WP_004368042.1
KEYWORDS    RefSeq.
SOURCE      Thauera phenylacetica
  ORGANISM  Thauera phenylacetica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 198)
  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 198)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 198)
  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   4  (residues 1 to 198)
  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   5  (residues 1 to 198)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Thauera phenylacetica"
                     /db_xref="taxon:164400"
     Protein         1..198
                     /product="TRAP transporter small permease subunit"
                     /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=21648
     Region          4..171
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mhsllrlsrl idwinervgr avmwlvlvav visagnalvr klfntssnal leiqwylfaa
       61 ifmlaagytf lrnehvridi ltsrlsargq nivdilgilf fllpmavlil wlswpivmts
      121 lasgemsqns gglirwpvkm llplglgllv lqalselvkr iafltghgpn plqkksagaa
      181 tadlveaika qrggraep
//
LOCUS       WP_004368540             687 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Hoylesella oralis].
ACCESSION   WP_004368540
VERSION     WP_004368540.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella oralis
  ORGANISM  Hoylesella oralis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 687)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Hoylesella oralis"
                     /db_xref="taxon:28134"
     Protein         1..687
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=74357
     Region          4..687
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 minrqllhpe sivviggsnn vhkpggaivr nlingkyqgt lrivnpkede iqgikafhdv
       61 kelpptdlai lvvaarfcpe yvevlasekd vrafiiisag fgeetpegge mekrilqtce
      121 kygaaligpn cigvlnnwyh gvftkpiphl spsgadfisg sgatavfile savikglqfn
      181 svwsigngkq igiedvlqhm denfdadrds kvkllyieni anpdrllfha sslirkgcri
      241 aaikagtses gsraasshtg aiassdsave alfrkagivr cfsreelttv gciftlpplt
      301 grnfaivtha ggpgvmltda lskgglnvpk leggaveelk aqlmpgsavt npidilatgt
      361 peqlgiaidy cerrfdnida ifvifgspgl vklyetydtl dkkikecrkp ifpilpclnt
      421 agpevaeflr kghvnfsdev tlataltqim ktpkpaspei ellgvdvpki reiiasieed
      481 gyvppetvhr llncagipmv pekvsadktq lidfanrigy pvvakvvgpi hksdvggval
      541 dirsskhlel eyermmkidg atsvmiqkmi kgtelfigak yeprfghvvl cglggifvev
      601 lkdvssglap lsnseaismi rslrgykilk gprgqkgine qkyaeiiqrl stllrfatei
      661 kemdinplla denevtavda rilirke
//
LOCUS       WP_004351109             267 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phosphonate ABC transporter ATP-binding protein
            [Pseudomonas].
ACCESSION   WP_004351109
VERSION     WP_004351109.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
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   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            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="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=28561
     Region          3..247
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mslsldgvdl vhadgqrala dirlrlaage rvaligpsga gktsllrvla sqwrpsagrv
       61 ellgeepwal saaarqrlra riglvhqapp lpprqrvvsa vlagrlgqwp lwkslvslvy
      121 pldrasahda lqrldlgdkl fqrcdqlsgg qlqrvgiarv lyqraelila depvsamdpv
      181 laghtlalln reaaargstl laslhavdla lqhfprvigl ragriafdlp agevdraald
      241 alyaneqlqa ertspagepa vvhiprc
//
LOCUS       WP_004369820             157 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Hoylesella oralis].
ACCESSION   WP_004369820
VERSION     WP_004369820.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella oralis
  ORGANISM  Hoylesella oralis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Hoylesella oralis"
                     /db_xref="taxon:28134"
     Protein         1..157
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17174
     Region          6..155
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mdkqekqeiy nlllsqikal vegetntvgv lanvssalhh afdtffwtgf ylrqgdtlrl
       61 gpfqgtvacy tipvgkgvcg tackeastiv vpdvekfegh iacssqsrse ivvplfdgnr
      121 qvvcvldids tepaafddid rewlekiaet valslyr
//
LOCUS       WP_004372348             137 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: pilin [Pseudomonas].
ACCESSION   WP_004372348
VERSION     WP_004372348.1
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 11471942
            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="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=13878
     Region          1..129
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mrqkgftlie llivvaiigi latiglpmyt thqakakfta glaeisalka gyedtlnqgt
       61 vptvaliggt sptancridv tgdvatgigs isceildapa pvlgksitlt rnategwkcv
      121 ttaeakyvak gcgvtga
//
LOCUS       WP_004372644             809 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Thauera phenylacetica].
ACCESSION   WP_004372644
VERSION     WP_004372644.1
KEYWORDS    RefSeq.
SOURCE      Thauera phenylacetica
  ORGANISM  Thauera phenylacetica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 809)
  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 809)
  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 809)
  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   4  (residues 1 to 809)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..809
                     /organism="Thauera phenylacetica"
                     /db_xref="taxon:164400"
     Protein         1..809
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=87802
     Region          68..799
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 madlvplpat alrkrcdpac fsfdttesla dhagdlgqer aveairfgla mghtgyhvfv
       61 lgdagsgkha ttfrllrera asepvppdlc ylhnfdealk prlltlpagr gaalrtcmqt
      121 firdlgpalg aaldsdahve rveslqsahk areegalrel gqacnaegis llqtpegfvf
      181 aptkdgepls peafealped erkaievrig ewsdrledll ndfpgwrksv residraere
      241 vlgpavahll revreahedl pavlafldav erdvidsavr gtmldeedde apepeentry
      301 hryqvkllvd hsasqgapvv fennpgygnl igriehvvqq gnqvshfnli ragalhrang
      361 gylvldaerl lsqpfawegl krslrageir ieppaeaqgw sgaltlepea vpsalkvvli
      421 gdrevyyllm ehdpefadlf kvaadfnddi lrtpenecey arlmallarg akllpversg
      481 varlveeasr laddsgrlsl ntralsdlmr eadfharqkg laattraeve dalaararra
      541 nryptrvles ildgttlist tgeragqing lvvielageh fghpvritat vrmgegdvvd
      601 ieretelgga ihskgvlils aflaaryarh qplslsaslv feqsyapveg dsaslaelca
      661 llsaltqvpi qqrfaitgsv nqfgevqvig gvnekiegff dlcsargldg tqgvvipaas
      721 irhlmlredv vqaaaegrfh ihavktvdea mtvltgveag epdakgvipk gtlnhkiatv
      781 laemtaarha ysdaegaaga rqhrrrhgv
//
LOCUS       WP_004373639             287 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Prevotellaceae].
ACCESSION   WP_004373639
VERSION     WP_004373639.1
KEYWORDS    RefSeq.
SOURCE      Prevotellaceae
  ORGANISM  Prevotellaceae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Prevotellaceae"
                     /db_xref="taxon:171552"
     Protein         1..287
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33074
     Region          208..286
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mkeltigfll etnkgshide dlllvnniad lprsnepgrl dflffgmcts gvgkyslnti
       61 dyvvlpkdil ivtpgdvtdn yslsadfkgi giimsknfyr evilnvhels slflfarnhp
      121 vceletdevn tvanyfsiik qkldnkahlf rvetvklllq aliydlsnai yriqkndkhh
      181 ssrlekiffd yvklvenhfr serrvgwyak qlnitpkyls eavkaishrt pnewidyyti
      241 helrimlkst aksikeiave lnfpnqsfmg kyfkdhvgvs pseyrkv
//
LOCUS       WP_004373972             342 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Ectopseudomonas
            hydrolytica].
ACCESSION   WP_004373972
VERSION     WP_004373972.1
KEYWORDS    RefSeq.
SOURCE      Ectopseudomonas hydrolytica
  ORGANISM  Ectopseudomonas hydrolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Ectopseudomonas.
REFERENCE   1  (residues 1 to 342)
  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 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 342)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 342)
  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   5  (residues 1 to 342)
  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   6  (residues 1 to 342)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Ectopseudomonas hydrolytica"
                     /db_xref="taxon:2493633"
     Protein         1..342
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37736
     Region          59..209
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          91..331
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 madsefvalt hsstlrrlly ealtalgldp tdtyrrayag aalaapllea redhdsaprf
       61 wqalegisgd vdiglhlgev mqprpmdvvg ylllaardlr qglqafvrfq hilsggfaar
      121 leeqgeqarl iidlnyrgvg slrqqmecla vllakmlaaa agelpllgvd frhraprrla
      181 ehrrllgvep rfsqphdali lpramlarps rsasprlfev lsaeaekqla elvenqllar
      241 vrywlelnlg yapctlecca aalgsrrgal qralseqgss fralhdevrr lcalrlldqg
      301 lsvrevarac gfaelspfyr afrrwqggtp rglvsrhgat ge
//
LOCUS       WP_004374364             346 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Pseudomonas].
ACCESSION   WP_004374364
VERSION     WP_004374364.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..346
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38076
     Region          71..312
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mpvthlagal crptdctlrt snsqhiatrf nehssvshpr dlgrvqvaer wsrikecnyv
       61 pvkvantrad lgeslvwder sgvlyfvdis ggringltpd geveclyesa arigalaltd
      121 rgnlifteda svalfdvptr kvsqhsasvh prstyrfndg acdpqgrfvt glmdealsdn
      181 tgalfrfdwq lsdqvihddm glptglawsq dghtvyfvds aaraiyraey liegrlgavt
      241 lfaetpaelg rpdglaldre gglwvcqyhg scllrydrhg yltdqvlmpv pcptsccfgg
      301 pgmntlyist arydmtpedl hhypdagdly airpetggva rhsfke
//
LOCUS       WP_004374532             158 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Segatella oris].
ACCESSION   WP_004374532
VERSION     WP_004374532.1
KEYWORDS    RefSeq.
SOURCE      Segatella oris (Prevotella oris)
  ORGANISM  Segatella oris
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 158)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Segatella oris"
                     /db_xref="taxon:28135"
     Protein         1..158
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17416
     Region          4..157
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 miisakeqty qtlcrqiecl isgeknitsv lanvasalhf afperffwtg fylvcceelq
       61 lgpfqgpvac mhiargsgvc gtawaenrtl ivddvetfpg hiacsslsrs eivvplhrsd
      121 gsvwavmdid skqlsafdsa daynlekien ilrkqlee
//
LOCUS       WP_004374561             129 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Segatella oris].
ACCESSION   WP_004374561
VERSION     WP_004374561.1
KEYWORDS    RefSeq.
SOURCE      Segatella oris (Prevotella oris)
  ORGANISM  Segatella oris
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 129)
  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 129)
  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   3  (residues 1 to 129)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Segatella oris"
                     /db_xref="taxon:28135"
     Protein         1..129
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15358
     Region          28..122
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mdkktvfiyh tsspdrygll kelakekrkk mtyaetllwe klklfpkpih frrqhiigdf
       61 ivdfvylekh lvievdgeyh ntpkqslddq lrteslnrqg fqvirftneq vvthiedvth
      121 qiyksinnk
//
LOCUS       WP_004374680             751 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Segatella oris].
ACCESSION   WP_004374680
VERSION     WP_004374680.1
KEYWORDS    RefSeq.
SOURCE      Segatella oris (Prevotella oris)
  ORGANISM  Segatella oris
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 751)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..751
                     /organism="Segatella oris"
                     /db_xref="taxon:28135"
     Protein         1..751
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=84347
     Region          11..751
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mhyinkmlpl lfalttvdgy aqaqqdslkn sksaltdsvh kltevvvrsn qmlgskfear
       61 nrtgsayyis peeiskfgyt dinrmlksvp gvnvyeedgy glrpnislrg tkaerseris
      121 lmedgvlaap apyaapaayy fpnagrmyai evlkgssqvq ygpfttggai nmvstpipsk
      181 fsarlnssyg syntlksyis vgnrfkhtgf lveylryqsd gfrkdepner tgfkrndlia
      241 kfsaqtnkde gvnhvfelkf gfanetsdet ylglsekdfa rrpyfryaga qkdnlktrht
      301 qwvatyliks gnnlkittnl yynyffrnwy klnelragit kaerrsidav ltdpetnqdy
      361 fdivtgkkdy igealmlran kriyhsrgiq skgeyrtmlw ggyltaelgm ryhadsedry
      421 qqddaysiqn grmslflagq pgsqanritt ahafsgywmg kwskgiftlt agmryedvel
      481 lnrnytkadp rrtgmvriet pnharavlpg lgfnvkllpv lslfggihkg fappsatlnq
      541 kaessvnves glrlttqklr ceaiafvnny snmlgsdlaa qggqgtleqf nvgkaivngl
      601 ellcsyrplp nhfafqipiq lsytytntkm kndfvssawg svtygdeipy iykhafnaqi
      661 sfehkwiean fgaryngdmr ttpghgriae rekipahlil daslkghink kitltlnain
      721 ltnkkylvsr hpsglraghp fgiygglqvq l
//
LOCUS       WP_004374908             193 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Thauera phenylacetica].
ACCESSION   WP_004374908
VERSION     WP_004374908.1
KEYWORDS    RefSeq.
SOURCE      Thauera phenylacetica
  ORGANISM  Thauera phenylacetica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Thauera phenylacetica"
                     /db_xref="taxon:164400"
     Protein         1..193
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21366
     Region          3..164
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mkifsplyer amvwsrhrra pwflgglsfa essffpippd vmlapmclan phrawwfalv
       61 ttltsvaggl fgyligyyaf dliepwlrgs nywsayeqav awfdawgfwa ifiagfspip
      121 ykvftiaagv asmallpftl aslvgrgarf flvaglmawg germegalrk yvdrigwatv
      181 aavvvgvlvy rag
//
LOCUS       WP_004376017             498 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Segatella oris].
ACCESSION   WP_004376017
VERSION     WP_004376017.1
KEYWORDS    RefSeq.
SOURCE      Segatella oris (Prevotella oris)
  ORGANISM  Segatella oris
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Segatella oris"
                     /db_xref="taxon:28135"
     Protein         1..498
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54858
     Region          5..498
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mkqtaylqin kgdnvvvclr pinageeiki gnhavqalrn tpaghkillc dtpkdkpiik
       61 ygypigrake nlkagewvne nniqtnlsgt leyeyrpaik plsieqedrt fkgfmrknge
      121 vgirneiwiv ptvgcvngia erlaqkleqe tqlkgvdaih awhhnygcsq lgddhentrk
      181 vlrdiclhpn agavlvlslg cennqpedfm kmlgdydrer irllvtqrve gdeieegmki
      241 lrklyktaaq dkreevpvsk lriglkcggs dgfsgitanp lvgefsdwli aqggttilte
      301 vpemfgaeti lmnrcqtpel fqktvhlinn fkeyflshge pvgenpspgn kaggistled
      361 kalgctqkcg hapvsgvley aerlktngln llsapgndlv astalaasgc qmvlfttgrg
      421 tpfgtfvptm kistnsqlfk skqnwidfna gelmegvdml tlrnlfidri iatangekvk
      481 nemngyreia ifkngvtl
//
LOCUS       WP_004378995             268 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Segatella oulorum].
ACCESSION   WP_004378995
VERSION     WP_004378995.1
KEYWORDS    RefSeq.
SOURCE      Segatella oulorum
  ORGANISM  Segatella oulorum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 268)
  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 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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Segatella oulorum"
                     /db_xref="taxon:28136"
     Protein         1..268
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30872
     Region          49..268
                     /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 msnhtvvads nfnrigneel kdyavyalck agcctftynt vqfeikandl lvireqqlmq
       61 hiktdiafdv lvlyihfpfv ekstpdvnfd vrsellltan palqlnqkef eratddmhvi
      121 iersddhehh fqkdvlstcc llflldifdv qnriygsshv svrsshlvta fmemlksgey
      181 kqhrevsyya dklfvtskhl savcrmvtgr tanywinhfv klaihqqlrs erlsvvevse
      241 mfnfsspahf sryvqaqlge pptairek
//
LOCUS       WP_004379149             301 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Segatella oulorum].
ACCESSION   WP_004379149
VERSION     WP_004379149.1
KEYWORDS    RefSeq.
SOURCE      Segatella oulorum
  ORGANISM  Segatella oulorum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 301)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Segatella oulorum"
                     /db_xref="taxon:28136"
     Protein         1..301
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34998
     Region          220..296
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mekviktydi syfaflnqpa vyaddnyfvv apaeqypelt gnirigclli lfclqgnvql
       61 slnnetfhla tgdciicppy aiisrleiae ntitsmvgys iesvasmlig gedmwhlfal
      121 lakkpiinnt qryiyqrmdy flsilryrts nndkyqkelc yhlfamlffd vlndfhlpqe
      181 qpkahtpsnr khyraeiiyk dflilltkdn glhrdvkyfs dklfispkyl sytvkrfegk
      241 paqevllera vnrvkselky tdtplqavsd lfqfenytaf ckfvkknlgv saleyrmgrh
      301 r
//
LOCUS       WP_004379234             352 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Segatella oulorum].
ACCESSION   WP_004379234
VERSION     WP_004379234.1
KEYWORDS    RefSeq.
SOURCE      Segatella oulorum
  ORGANISM  Segatella oulorum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 352)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Segatella oulorum"
                     /db_xref="taxon:28136"
     Protein         1..352
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38211
     Region          7..340
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 maflkvknvs irgvacavpk dvkeikdlpf fapgeaekvi althversri vpkgmccsdl
       61 cqaaaeklld slgweretve alifvslsrd yitpatanil qeklhlpksc mafdiplacs
      121 gyvyglsvis slmssgnikr alllvgetts vlqspldktl wplhgdagsa taleykegva
      181 pmffdlmsdg sgagaimhey ggtrnpmned slrmreredg iirkgyhgym dgmsvfsfsv
      241 keppaaikal ceyngidlns idylllhqan kymdekigkk lkipsekipy slmqygntss
      301 tsipmtivvg igdklsqeqa dvimcgfgag lswaaayikl nhivslplie lg
//
LOCUS       WP_004380634             174 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Segatella oulorum].
ACCESSION   WP_004380634
VERSION     WP_004380634.1
KEYWORDS    RefSeq.
SOURCE      Segatella oulorum
  ORGANISM  Segatella oulorum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Segatella oulorum"
                     /db_xref="taxon:28136"
     Protein         1..174
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19423
     Region          5..166
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdnevlkalc errsirsfka eqitdeelqt vlesgtwapt gkglqspyiv avqnakqlew
       61 lrkenarlme vssdpyygap tivlvfapke wpnnvkdgsl vlgnmmlaah slglgscwin
      121 reekmfetae gqqlmrdwgl pealmgigal vlgypsshpk tvkprkadyy riik
//
LOCUS       WP_004381195             167 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein, partial [Thauera phenylacetica].
ACCESSION   WP_004381195
VERSION     WP_004381195.1
KEYWORDS    RefSeq.
SOURCE      Thauera phenylacetica
  ORGANISM  Thauera phenylacetica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Thauera.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Thauera phenylacetica"
                     /db_xref="taxon:164400"
     Protein         <1..167
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
     Region          57..123
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 aavepppaep avvpapspap palchawgdl saseadrlaq rlrrigitaa rsrsetpeaw
       61 wvrippqrnr seaerrvvel nllgvsdtfi vqesgpnqna vslglfkten rarillgqlr
      121 akgvdnagie prmstsyriq anvpanelri vesaapglra rrqactr
//
LOCUS       WP_004382382             132 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Prevotella veroralis].
ACCESSION   WP_004382382
VERSION     WP_004382382.1
KEYWORDS    RefSeq.
SOURCE      Prevotella veroralis
  ORGANISM  Prevotella veroralis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 132)
  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 132)
  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   3  (residues 1 to 132)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Prevotella veroralis"
                     /db_xref="taxon:28137"
     Protein         1..132
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15475
     Region          31..125
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 msedrrkkkl gyetsspdry hilkdyaken rkkmtlaesi lwnelrgmrg dchfrrqhpi
       61 gdfivdfvcl shnlvievdg ayhnesqqmi ddamrtecln dmgfnvlrft ndeicteldn
      121 vteqindfin ke
//
LOCUS       WP_004382993             368 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Prevotella veroralis].
ACCESSION   WP_004382993
VERSION     WP_004382993.1
KEYWORDS    RefSeq.
SOURCE      Prevotella veroralis
  ORGANISM  Prevotella veroralis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 368)
  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 368)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 368)
  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   4  (residues 1 to 368)
  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 368)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Prevotella veroralis"
                     /db_xref="taxon:28137"
     Protein         1..368
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42461
     Region          133..363
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          278..358
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mmnqqidllk silfaewttl vtfgicllvl qkqkkpayql ytrarqllai nflifamepf
       61 lywlkeeeiy sipypetisl slylivtvll smiylpfvqp dyitrkrvlh niiflagcls
      121 flcigaiigg tfrlishitv tvvlltmvil lgirfysyyr kaqqkmanfy adnfkqsiaw
      181 larsvtlvia lgfpsyipsi lphwgieiyk alcllsiiym flsftnymfn anfvvlnitl
      241 pqknvrldkg tieklqrctl rwqktpaalt knitindvsr qlgtnrtyls lylntylnlt
      301 fsewigqirl kqakillasn aimsmeqvae atgftsssaf shyfkahegl spirwrrqtr
      361 hkktdqsd
//
LOCUS       WP_004383825             229 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Prevotella veroralis].
ACCESSION   WP_004383825
VERSION     WP_004383825.1
KEYWORDS    RefSeq.
SOURCE      Prevotella veroralis
  ORGANISM  Prevotella veroralis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Prevotella veroralis"
                     /db_xref="taxon:28137"
     Protein         1..229
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25816
     Region          141..216
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mkrlltiivl ilttitsaha qstvtvtqst didalvngkk takkankesk kvesqreqsr
       61 qsigskiktp dtkqlsvpkl ndhkpeiarp dnntlqpvrq vgtklvkrlv rrphdptfdd
      121 iddgkqivtk rvkkgikkvr gfrvqvysgg ntriahqqad kagqtakqlf pdqpiyvhfy
      181 aprwmclign ftnyntakkv mrkmrkegyp qanvirmmvs irtstvidn
//
LOCUS       WP_004387005             416 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Cronobacter sakazakii].
ACCESSION   WP_004387005
VERSION     WP_004387005.1
KEYWORDS    RefSeq.
SOURCE      Cronobacter sakazakii
  ORGANISM  Cronobacter sakazakii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Cronobacter.
REFERENCE   1  (residues 1 to 416)
  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 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   3  (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   4  (residues 1 to 416)
  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 416)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Cronobacter sakazakii"
                     /db_xref="taxon:28141"
     Protein         1..416
                     /product="CmpA/NrtA family 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=45563
     Region          39..290
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 msdssfslsr rrllqagaal sgamllpglm gsvwaagsdk peldtvrvgf ipltdcapvv
       61 maalkgfdkk ygirilpske aswaavrdkl vsgeldaaha lygliyglel giagkaqpma
      121 tlmtlnqngq aislsadlle kgvttpdalq krvaasepga ytfahtfptg thamwlyywl
      181 aaagihpfnd vrtvvvpppq mvmnmrignm vgfcvgepwn araindrigf taatsqsifp
      241 dhpekvlgtr rlwveqnpht araltaavle aarwidasdd nrretaqvla kraylntkvq
      301 yltprmlgey ddgagkrwkd dhamrffrdg evsypwhsdg mwfltqfrrw gllktdpdya
      361 aiaarinrtd iyqqaaaavg gvalpastrr tsrlmdgsvw dgrdpaayaa rfamkr
//
LOCUS       WP_004388654             313 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Cronobacter sakazakii].
ACCESSION   WP_004388654
VERSION     WP_004388654.1
KEYWORDS    RefSeq.
SOURCE      Cronobacter sakazakii
  ORGANISM  Cronobacter sakazakii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Cronobacter.
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
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Cronobacter sakazakii"
                     /db_xref="taxon:28141"
     Protein         1..313
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=34509
     Region          1..309
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 miefkqvskf ynggaavkdl sltfaegafs vligtsgsgk sttlkminrl vehdageirf
       61 ageeirqfsp ealrrrmgya iqsvglfphw tvaqnvatvp qllkwpkari qarvdellal
      121 lgltpdafrd ryphqlsggq qqrvgvaral aadpevllmd epfgaldpvt rsalqqemrr
      181 ihqllgrtiv lvthdideal glaehlvlmd ngevvqqgtp lalltaprnd fvrdffgrse
      241 lgvrllslkq vrdfiepgmv dgapvaetlt lreamsvfve rqcealsvvd angahrgvlr
      301 frhlvnqrea rge
//
LOCUS       WP_004396663             302 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Vibrio].
ACCESSION   WP_004396663
VERSION     WP_004396663.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 302)
  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 302)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 302)
  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   4  (residues 1 to 302)
  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 302)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..302
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33416
     Region          34..188
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          217..296
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mvnqteekpd laqlmqnyvd kyalhhlegc tdtaipgvwf yrssqgnsrq pfiyqsgivi
       61 lgqgqkrihl ganavdygpn dylvvgvpmp leceavakqn qpllgltidi dhslllkqva
      121 aleengfkpp vdannpcglk svqmnhtmln sckrlmnali dgleaellgg slleemafra
      181 ltsleghvlf elahheghya riakalskvh rdyatsltvn tlaeeanmsv safhqafrgv
      241 tmesplqylk kvrlnkakel iqiegkrvnd aarlvgyssp sqfsreykrh fnhtprgala
      301 kv
//
LOCUS       WP_004396847             270 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio metschnikovii].
ACCESSION   WP_004396847
VERSION     WP_004396847.1
KEYWORDS    RefSeq.
SOURCE      Vibrio metschnikovii
  ORGANISM  Vibrio metschnikovii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 270)
  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 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   3  (residues 1 to 270)
  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   4  (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   5  (residues 1 to 270)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Vibrio metschnikovii"
                     /db_xref="taxon:28172"
     Protein         1..270
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30014
     Region          17..270
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <173..267
                     /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 msqylvnnpe rakllsprpa elitlpaymd chdhsytqiv iglkgqadfe vsgignivgp
       61 gqgcvvtsst vhafgatvgq sdilvlnlpl pqgddpltlq rinelarsdi yfqldkqiqk
      121 liqmlvlemh aspddlllsr acsdtvlall lrhisafevh rkearfdlda idryieqhls
      181 rrisvaqlag svylgesqfh qlfkeqlgit phqyvlskrv dmakqlleqs rftlgqvael
      241 agfsnqsaft htfsrlqgis psqykkqcsr
//
LOCUS       WP_004397072             190 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Thermoanaerobacter].
ACCESSION   WP_004397072
VERSION     WP_004397072.1
KEYWORDS    RefSeq.
SOURCE      Thermoanaerobacter
  ORGANISM  Thermoanaerobacter
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae.
REFERENCE   1  (residues 1 to 190)
  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 190)
  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   3  (residues 1 to 190)
  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   4  (residues 1 to 190)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 190)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 190)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Thermoanaerobacter"
                     /db_xref="taxon:1754"
     Protein         1..190
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21777
     Region          1..188
                     /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"
ORIGIN      
        1 msqwrivlad ssdlsrqfik nvllanghlv yeardggsai rlcralapdl viadlnlani
       61 ngfevgriin eddiapvilm tstlqrdfle eirkysvfsy llkpvdrgvl lstvefvien
      121 ykkfrsmkee iqklkhelea rkkiekakgy imkakglsee eaykimrkms mdmsipmeii
      181 aemilqeyke
//
LOCUS       WP_004397556             631 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Pseudomonas syringae].
ACCESSION   WP_004397556
VERSION     WP_004397556.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 631)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 631)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 631)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 631)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 631)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 631)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..631
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68329
     Region          1..631
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msqtnshaqa ggtakpigll iaavgvvygd igtsplytlk evfqggygve vthdailgvl
       61 slifwsliwv vsfkymafvl radnqgeggi malmalarra sakhpklqmm mvvfglfgaa
      121 lfygdsmitp avsvlsameg lelafdgldh wivpmalvvl vglfliqrhg tarigvlfgp
      181 vmvvwflvlg algvygimqs pevlkavnpa wglnffiihp gigvailgav vlaltgaeal
      241 yadmghfgrk pisrawfilv lpalllnyfg qgalvlgnpe avrnpfylla pswallplig
      301 lstmatiias qavisgafsm tlqaiqlgyi prmhiqhtss daqgqiyiga vnwalmvgvi
      361 mlvigfessg alasaygvav tgtmlcttil vstvmlmlwk wppllavpll iclllvdglf
      421 faanvpkifq ggafpvlaga vlfilmttwk rgkqllaeri degglplpif igsirvqpph
      481 rvqgtavflt arsdavphal lhnmlhnqvl heqvvlltvv yedtprvpsa qrfevesyge
      541 gfyrvilhfg fidepdvpaa ltlchlaeld fspmrttyfl sretvipski dgmarwreal
      601 fafmlknang nlrffklpfn rvielgtqve m
//
LOCUS       WP_004398192             175 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit [Vibrio].
ACCESSION   WP_004398192
VERSION     WP_004398192.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 175)
  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 175)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 175)
  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   4  (residues 1 to 175)
  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   5  (residues 1 to 175)
  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 10008692
            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="TRAP transporter small permease subunit"
                     /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=19922
     Region          10..166
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mdlseqqepl nyldrlvvkv ghtisflflv salvifyevi qryvfdsptf wvhettvmig
       61 allfvyggsh cvakdkhirv viiydavspk vrrwldviiy amccvstgml awaawqvllr
      121 avfapngdir fettgsawdp afpafikitl flilclmfiq fvfrlinklt rgshv
//
LOCUS       WP_004398726             374 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Vibrio nigripulchritudo].
ACCESSION   WP_004398726
VERSION     WP_004398726.1
KEYWORDS    RefSeq.
SOURCE      Vibrio nigripulchritudo
  ORGANISM  Vibrio nigripulchritudo
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 374)
  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 374)
  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
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 374)
  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   5  (residues 1 to 374)
  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   6  (residues 1 to 374)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 374)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 374)
  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 20170230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Vibrio nigripulchritudo"
                     /db_xref="taxon:28173"
     Protein         1..374
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41390
     Region          <9..109
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          94..366
                     /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 mlspikplql nltegqkrvl avirqhgtlp rtkiaeltgf gtgsvttlck elltlqliqe
       61 servkggrgq pakpvslspy aaftfgvafh iaridlalan ftgevldrve ifydesqpve
      121 etiilirdai skmtakhrll narilgigvs mpgphlcdgk rvrtinqmah wqdvdladaf
      181 ghhfeypvwi dndckvaavg eyysglwddi ehlvlieigh giggavimng klhsgrhnns
      241 geigtyfnrs eaprpclrel iielqesgld vvkledipdi ehpivaswik rsaerlmpal
      301 lltlswfdpe civiggsspk aisdalikem dlatewekrf dypvaeiaps kvgtylssyg
      361 asmypffqtl syqt
//
LOCUS       WP_004400141             309 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Vibrio
            nigripulchritudo].
ACCESSION   WP_004400141
VERSION     WP_004400141.1
KEYWORDS    RefSeq.
SOURCE      Vibrio nigripulchritudo
  ORGANISM  Vibrio nigripulchritudo
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Vibrio nigripulchritudo"
                     /db_xref="taxon:28173"
     Protein         1..309
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33517
     Region          14..264
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mdkfnavspe rfsvgesplw daknqrvvfv diigkllvsv sldgtcetik tedfptacar
       61 vaqsdkhwiv afangvalld ktsgkttpvc qpdsmvgnrl negkcdpqgr fwvssmqtnl
      121 hadgsgkamt resgalfsvd dlgnssqwtd ynigltntma wspdrstfyf gdsmnnviwa
      181 fdydeqsgev snqsvffegy pngdpdgsci ddegylwncr fggseiiria pdgsldkvvk
      241 lpvtnptsct fggaegktlf itsaqfslsd eqlaknpleg allsaemevg gnaenayqms
      301 dqlrkrigi
//
LOCUS       WP_004400424             384 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Vibrio
            nigripulchritudo].
ACCESSION   WP_004400424
VERSION     WP_004400424.1
KEYWORDS    RefSeq.
SOURCE      Vibrio nigripulchritudo
  ORGANISM  Vibrio nigripulchritudo
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 384)
  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 384)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Vibrio nigripulchritudo"
                     /db_xref="taxon:28173"
     Protein         1..384
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43912
     Region          1..373
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mmslskpqar klallsqglp pkspkshspa htlnvmeqig yvqidtisvv qrahhhvlws
       61 rnpkyrpehl dkliadkkvv eywshaasfl pmknyrytlp rkvaiksgeq ahwykkdhkl
      121 mnhvitriqe egpllakdfe skgtkingwg akpakraley lfmqgdlmip errgfqkvyd
      181 ltervlpsdi dvsvpspqeh arflvlnylk ahglgsipef vyllknvkte vtsaiqqlne
      241 dgvivevdve gnsfwvlses lslldarlnr kqakilspfd nlliqrkras tlfnfdylie
      301 cyvpegkrqy gyfclpilwn galvaradck vdkktatlnv lhlflepslk kkadfleale
      361 qelasfsafn qcehfkicki secr
//
LOCUS       WP_004401858             381 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator
            [Thermoanaerobacter].
ACCESSION   WP_004401858
VERSION     WP_004401858.1
KEYWORDS    RefSeq.
SOURCE      Thermoanaerobacter
  ORGANISM  Thermoanaerobacter
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae.
REFERENCE   1  (residues 1 to 381)
  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 381)
  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
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 381)
  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   5  (residues 1 to 381)
  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   6  (residues 1 to 381)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 381)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 381)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Thermoanaerobacter"
                     /db_xref="taxon:1754"
     Protein         1..381
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41707
     Region          20..59
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          80..369
                     /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 mkdytkgtsg likninkanv ldvikkmqpi srievskvlk mskstisaiv delieeglvi
       61 engygekgtv grkpiqlsfn pdarfvigis vestnsigil tnlegkilkk ikwetgikeq
      121 afngivkgik elteedknii gigiglpgit diqkgivdap glkwsnfdlk krlseifdyn
      181 iyldnsvnya algerwigcc reienfvlin igngigsgiy vngtllrgns yaagevgyma
      241 igedafervy syedygyfer kaslsslves vskslsyakt megvvkeykk qnpacvqavs
      301 qfiknlsmgi anivsilnpe aiiiggdiln yeidirqelk ekvkrivpfd fdikvaqlge
      361 dasaigavad vllntnnlil l
//
LOCUS       WP_004402955             478 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein [Vibrio
            nigripulchritudo].
ACCESSION   WP_004402955
VERSION     WP_004402955.1
KEYWORDS    RefSeq.
SOURCE      Vibrio nigripulchritudo
  ORGANISM  Vibrio nigripulchritudo
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 478)
  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 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   3  (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   4  (residues 1 to 478)
  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 478)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Vibrio nigripulchritudo"
                     /db_xref="taxon:28173"
     Protein         1..478
                     /product="CmpA/NrtA family 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=53148
     Region          51..332
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mkcrktiank ttekwnavrn rmaslslksr tlkslalavl lgsnsvvaev gepeledlkf
       61 gfikltdmap lavayekgff edeglyvtle aqanwkvlld rvidgeldga hmlagqplga
      121 tigigtqadv itafsmdlng naitvsndiw aqmkpnlekq adgkpvhpik adalkpvves
      181 yldkgkpfnm gmvfpvsthn yelrywlaag gihpgyyapk tgdnsgqvea dvllsvtppp
      241 qmpatmeagt ikgycvgepw nqqavfkgig vpvvtdyeiw knnpekvfgv saawakkypn
      301 thirvvkami raahwldekq nanrmeavki lakshyvgad adviansmtg tfeyekgdkr
      361 svpdfnvffr ynatypyysd aiwyltqmrr wgqipsekpd dwyaniakkv yrpdiyqqaa
      421 esliedgilk asdfpdfnte dgyrdpqthf iddvvydgkq pnaylkkfsi glkgseei
//
LOCUS       WP_004402956              69 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Vibrio
            nigripulchritudo].
ACCESSION   WP_004402956
VERSION     WP_004402956.1
KEYWORDS    RefSeq.
SOURCE      Vibrio nigripulchritudo
  ORGANISM  Vibrio nigripulchritudo
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 69)
  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 69)
  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   3  (residues 1 to 69)
  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   4  (residues 1 to 69)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 69)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 69)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Vibrio nigripulchritudo"
                     /db_xref="taxon:28173"
     Protein         1..69
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=7759
     Region          <1..69
                     /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"
ORIGIN      
        1 mlaiekevqa ltqklddrkw iekakgtlmk mhhideeeay kalrnsamks sqpigqvakn
       61 lmltfdsis
//
LOCUS       WP_004405005             431 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Pseudomonas
            syringae].
ACCESSION   WP_004405005
VERSION     WP_004405005.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 431)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 431)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..431
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47781
     Region          16..413
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mleqvnviye gwgerwqwgt lvsttaltgr plivfeysne arqrglelss ytlpldggrl
       61 rrdfpdhqly lpgpvydslp dgwgmllmdr lfrrrgltta rigplerlay igssamgamt
      121 fepvapegqe sdvhipleql aadvkqvlrg nggeflqall lvggspqgar pkalvyrdpe
      181 tggfttaatp gfeawlikfp akeehaevca iemvyaeclr mcgietpdtq yfnlpdglaa
      241 faskrfdrrd glripmqsla aftganyqsp gvldyvnflr atqmctndvr emaraferav
      301 fnvafnnrdd hpknfayims qdgqwklspa ydvtfcegag gyhqmdvmge aleisraqml
      361 rlaeeaemsp daatgvidgm cdvasrftai aenlcpqvit rdtlrmiqsr idqnvarlhh
      421 sqadgghgrf s
//
LOCUS       WP_004405387             406 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Vibrio
            nigripulchritudo].
ACCESSION   WP_004405387
VERSION     WP_004405387.1
KEYWORDS    RefSeq.
SOURCE      Vibrio nigripulchritudo
  ORGANISM  Vibrio nigripulchritudo
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 406)
  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 406)
  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 406)
  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 406)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Vibrio nigripulchritudo"
                     /db_xref="taxon:28173"
     Protein         1..406
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=45025
     Region          52..388
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mrdekltrrg fmkvsaryga tstllaagal gagatlsqla naaeqtakkr yavkpkfqlk
       61 fgasgfnekn ldiqksgqlf fakdleartn gairvefigs nqicgqtnci kktqqgivdi
      121 ysastqnsag gapylnvldy aymfpsraaq yhffyskkse allreplrkr hnvqflfthc
      181 elrgiqlglk wqdkptvtsv dqlagtknrv tgtqlgriam elmnlnpvpi aweetldglk
      241 qglidgaetw mgavayagma pvvsqcvdlk ffcgtehtam nlsvfdklgs elqdavmesa
      301 ylaqiytqgm neaglydivg atnpqkpgti faennvrvat lsdaelrkae emcspefnpk
      361 pweawrerln kwsgghdtyq eiydiareip kdmapvnvep qrwwqs
//
LOCUS       WP_004405952             269 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Vibrio
            nigripulchritudo].
ACCESSION   WP_004405952
VERSION     WP_004405952.1
KEYWORDS    RefSeq.
SOURCE      Vibrio nigripulchritudo
  ORGANISM  Vibrio nigripulchritudo
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (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   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Vibrio nigripulchritudo"
                     /db_xref="taxon:28173"
     Protein         1..269
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30777
     Region          20..>93
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          <69..258
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          184..259
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 massnyhpiq gnvhiqdgyq tlvppepvsq ivqsfwqlnv pfgryvyhsi pdncvdwitr
       61 vdnpqesvfi ppflsanpfq legpvsyfgv rfqllgyqal tvhpleswas evqglsvldl
      121 lpsdysgavq rflvenqdfy srcgaitqwl trvaspsvid srlanflnfs qatagsvals
      181 dvhcrelgis srqlrrvvrh hlgvsprefq qvmrfqhaik qlentqeena wadfyydqsh
      241 firdcqrfmg mtylqfrnms vlynseesd
//
LOCUS       WP_004408534             331 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Vibrio
            nigripulchritudo].
ACCESSION   WP_004408534
VERSION     WP_004408534.1
KEYWORDS    RefSeq.
SOURCE      Vibrio nigripulchritudo
  ORGANISM  Vibrio nigripulchritudo
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 331)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Vibrio nigripulchritudo"
                     /db_xref="taxon:28173"
     Protein         1..331
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35875
     Region          1..331
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mafrivssdi ylpeypwsae dfdvylgltk gtsnkkfave kryiasrqes aifmatqail
       61 kclrqspfsl sdidlliyas gthhqslpyd aaavlaelka ppsitsldin stclsflsal
      121 dyaqcvfaak rhqrvlivts elgsgitlnk fkkpkpevat lfsdgaaayl leaselsygl
      181 hgamfethhe gyeccqikgg gshinphkvs haeylaacqf emdgkslfrh ivnvmpeflk
      241 rgianaglsq sdiayflphq ashhgmaklp kltgfsaeki vnnfrelgnq vaaslpinlh
      301 llrlekagsg ekvllagsaa glslgmgvie l
//
LOCUS       WP_004408732             705 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Vibrio nigripulchritudo].
ACCESSION   WP_004408732
VERSION     WP_004408732.1
KEYWORDS    RefSeq.
SOURCE      Vibrio nigripulchritudo
  ORGANISM  Vibrio nigripulchritudo
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 705)
  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 705)
  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 705)
  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 705)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..705
                     /organism="Vibrio nigripulchritudo"
                     /db_xref="taxon:28173"
     Protein         1..705
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=75648
     Region          2..689
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 medkkdvdla qfelpirtdf pwlttlitav givlaglhiw fntlatlpel wvsathfagf
       61 svvcallypa rkswkksrfa laidmvvaaa avscliyipl aedalydrgv kfvtsdwvfs
      121 iisivvvlei irrtigwfip vlivisltyv vwwgqwvpgv fhfpglsaet llyrsfysse
      181 gmfgtisris wsyvfmfilf gaflvrsgag dfiidvsraa ankviggpgf vavmgsglmg
      241 svsgssvant vstgvitipl mqragfpsrf aagveaaast ggqlmppvmg agafimasyt
      301 qipyvdivav sivpamiyfl svaffvriea krsgvhqvds nsepvlkvla sgwhyliplv
      361 vlvyllvsgf tptyaagisi vsvvvaswls pnkmgikaif ealaqgsrnm attavlltgi
      421 glvinvistt gvgntfslmi newasgslli mlllialasl ilgmglpvta ayivlgtlsa
      481 palynliaqd qlldmlalgq lpeeakaifm laapdqlaal nspmsveqaq slialvpadf
      541 lptlleqaig mekvglalla ahliifwlsq dsnvtppvcl tafaaatiar tppmrtglta
      601 wkiakglyiv pvimaytalv swdpvaviti gifsvfgvya liaalegyle stlswwmril
      661 vaalgvvmmw peislavrlv alasfvalfy hsyrtenksy tlktd
//
LOCUS       WP_004395839             204 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Vibrio].
ACCESSION   WP_004395839
VERSION     WP_004395839.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 204)
  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 204)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 204)
  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 11459477
            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="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22243
     Region          1..202
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 melydteeqq veaikdwwke ngkavllgav lglgglfgwr yyqhstttgq ettsetyska
       61 ianfsakgaq aesdlqhfid nhqkseyavl aamqlakaqa dagqldeala qlewakkstk
      121 daaltpviaf riarlqaeqq qfdaalaelt titeaswaar vaelrgdial rkgdkdaaya
      181 aysqaqqssn asqtlqlkld dlar
//
LOCUS       WP_004410491             191 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Pseudomonas syringae].
ACCESSION   WP_004410491
VERSION     WP_004410491.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 191)
  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 191)
  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   3  (residues 1 to 191)
  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   4  (residues 1 to 191)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 191)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..191
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21384
     Region          1..191
                     /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"
ORIGIN      
        1 mlrillindt akkvgrlrsa lieagfdvid esgliidlpa rveavrpdvi lidtespgrd
       61 vmeqvvlvsr dqprpivmft dehdpgvmrq aiksgvsayi vegiqaqrlq pildvamarf
      121 esdqalraql hardqqlaer krielakgll mkmkdcneee aytlmrrqam srqqklvqva
      181 eqiiamsell g
//
LOCUS       WP_004411103             287 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Pseudomonas].
ACCESSION   WP_004411103
VERSION     WP_004411103.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..287
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30830
     Region          1..278
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mnvdlhchst asdgalspta lvarahengv rvlsltdhdt legleearaa ahslgmqlvn
       61 gvelsctwgg atihilgygf dtqapaltea isrlhegrwl raeeisrkla ikgmpgaleg
      121 araiqqelgd sgnaparphf adfmvrsgfv kdraeafrkw lgagklgdvk qhwptledtv
      181 atlrasgawv slahpshydf trskrrklvg dfvqagghai evvngmqpad qvgtlailar
      241 efgllvsags dfhgpgtwge igtyrpvped lpplwcrfkh eqptasv
//
LOCUS       WP_004411400             256 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Vibrio orientalis].
ACCESSION   WP_004411400
VERSION     WP_004411400.1
KEYWORDS    RefSeq.
SOURCE      Vibrio orientalis
  ORGANISM  Vibrio orientalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 256)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Vibrio orientalis"
                     /db_xref="taxon:28175"
     Protein         1..256
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=29297
     Region          <6..242
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mqlvyeqlal yyqpkmsvsk ekivgaeali rwtnsngevk lpmsflplfe kyglirnldd
       61 fvihraldql viwnycgidi sisvnvsgef fvrddfeerl eslgkqydak iielleieil
      121 esselsgrkk vceniikcke lgfkislddf gtgyssldyl tkfdfnlvki drelikhtpf
      181 ckatsivlkg vvdicrslgf ktlaegvetr eqliclseyg fdliqgyyva kpmctlefer
      241 wilkeidcst iisksi
//
LOCUS       WP_004411501             193 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Vibrio orientalis].
ACCESSION   WP_004411501
VERSION     WP_004411501.1
KEYWORDS    RefSeq.
SOURCE      Vibrio orientalis
  ORGANISM  Vibrio orientalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 193)
  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 193)
  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   3  (residues 1 to 193)
  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   4  (residues 1 to 193)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 193)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Vibrio orientalis"
                     /db_xref="taxon:28175"
     Protein         1..193
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21935
     Region          10..193
                     /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"
ORIGIN      
        1 mykklsqnpi vvcsdraeeq qrlsaelsrd fdnvsscqls qlelildaqv qasvvigwlq
       61 psaelrliie lcrqrnhpll vvlkrlnsnd mnrlpevkdy allpadsqfp lvpwieqayi
      121 trqsisales eierlsirld erkliekakg llmkihqvde eaayaamrks amqssqtlaq
      181 varnllqtle vlr
//
LOCUS       WP_004411502             457 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein [Vibrio
            orientalis].
ACCESSION   WP_004411502
VERSION     WP_004411502.1
KEYWORDS    RefSeq.
SOURCE      Vibrio orientalis
  ORGANISM  Vibrio orientalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 457)
  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 457)
  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 457)
  AUTHORS   ter Beek,J., 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 457)
  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 457)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Vibrio orientalis"
                     /db_xref="taxon:28175"
     Protein         1..457
                     /product="CmpA/NrtA family 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=50893
     Region          38..311
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mkwtsvfkqt llgaalassv yvpsafaelg epeleelkfg fikltdmapl avayekgffe
       61 deglyvtlea qanwkvlldr vidgeldgah mlsgqplgat igigtkaevv tafsmdlngn
      121 aitvsnktwq qmklhiatqp dgkpvrpika dalkpvvesy ldqgkpfnmg mvfpvsthny
      181 elrywlaagg ihpgyyapqs gdnsgqvnae vllsvtpppq mpatmeagti egycvgepwn
      241 qqavfkgiga pvvtdyeiwk nnpekvfgvs kswaekypnt hirvvkalir aahwldendn
      301 anrieaskll akseyvgadf eviansmtgt feyekgdvrd vpdfnvffrh natypyysda
      361 iwyltqmrrw gqiseektdd wymniakevy rpdiyqqaae alvedgvltg ndfpdftqed
      421 gfrapqthfi ddivydgrtp nayiekfaig lkgkekv
//
LOCUS       WP_004411829             297 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio orientalis].
ACCESSION   WP_004411829
VERSION     WP_004411829.1
KEYWORDS    RefSeq.
SOURCE      Vibrio orientalis
  ORGANISM  Vibrio orientalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 297)
  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 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   3  (residues 1 to 297)
  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   4  (residues 1 to 297)
  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 297)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Vibrio orientalis"
                     /db_xref="taxon:28175"
     Protein         1..297
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33133
     Region          27..181
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          210..290
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msladvmqky velkqlhnle gisktqidgv vfyrsskgnn rqpfvyqsgv ivlgqghkni
       61 ylgdkpvryg sedylvvgvp mplecesfpe ngepllglsi sidpqllhrl vnkleslhcy
      121 kphaercvga glgavkmddg mldvctrimk alccpveaei lsdslleela yralmssegq
      181 vlfdlarhdg hyarvakale flhnnyhetv tvqhlaqqan msvsafhqaf rdvtlespiq
      241 yikkvrlnka reliqlegvr vgvaarsvgy nstsqfsrey krhfnqtpte inttvng
//
LOCUS       WP_004412858             687 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Vibrio orientalis].
ACCESSION   WP_004412858
VERSION     WP_004412858.1
KEYWORDS    RefSeq.
SOURCE      Vibrio orientalis
  ORGANISM  Vibrio orientalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 687)
  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   3  (residues 1 to 687)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Vibrio orientalis"
                     /db_xref="taxon:28175"
     Protein         1..687
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=75899
     Region          4..681
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 maldmeqlrk mfyeecrenl evleevllnl dlahiedesi ntifraahsi kggagtfnll
       61 disefthnve ayldlvrnqe rtltadsidl llksgdcihs mlegheqgtd vnldlkqevs
      121 qklaellgsd ssepevvdce sedvletssn adqvwnisfa phqdmffsgn dplrilrels
      181 elddscqini dtsalpelqe ieselcflsw hatisgaldl dlikeifewv edecdltiel
      241 sqpdieqpae dsqqttspvt tventetkpv pesaakstkv aksdssvssi rvdidkvdsl
      301 inlvgelvit qsmlteignd fsidkleklk sgldqllqns kdlqenvlni rmlpmsfafs
      361 rfprlvrdls srlekqvdlq ikgeqteldk tvlerivdpl vhlvrngidh gieqpeqrle
      421 ngksemgvie lnayhqggai vieirddgag lncdklwnka lekgvlspds rreeysdkqi
      481 mnlifapgfs taeevsdisg rgvgmdvvrr nieelgghie veselgkgsr ftislpltla
      541 ildgqlvrva gevyvipllt ivesiqidpq ciklasggie lyrlreenip ilrlqeelem
      601 gssggldqri lcfveaagnr vgllldelld qqqvviksle snyskvagis gatilgdgsv
      661 sliidvqgli tnflnrtsds snkglaa
//
LOCUS       WP_004413270             266 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Vibrio orientalis].
ACCESSION   WP_004413270
VERSION     WP_004413270.1
KEYWORDS    RefSeq.
SOURCE      Vibrio orientalis
  ORGANISM  Vibrio orientalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 266)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Vibrio orientalis"
                     /db_xref="taxon:28175"
     Protein         1..266
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=30327
     Region          <35..261
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 melasiysvq mdyiqslvry qregfvygfy qgktfysvfq pivdragkvl afeglvriwd
       61 dqgnsvnpgd yfssmppgda anvvatllcg klhsinlaht vyrhsklfin vspsvftlla
      121 nhrqsiehlm hrlrclrlvs dqivyeitef eetdlegilq gkayleeygi vtalddygar
      181 ystrkralki rapylkidrs yvgdenfvre avavarsiga ktiaegietr eqfemcresg
      241 vdyfqgywia kpmtsqrlqr yqplal
//
LOCUS       WP_004415085             703 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Pseudomonas syringae].
ACCESSION   WP_004415085
VERSION     WP_004415085.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 703)
  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   3  (residues 1 to 703)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..703
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=75791
     Region          3..693
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msinldqaqq tfivearell qameesllql esepgdqdai gavfraahti kgsaglfglt
       61 pivsfthive dvldrlregs vsvdaeliav llksgdhmle lidvvasrsq qmqqpalere
      121 aalrqalqvf qapasagaad sasaavvsdd epsaevlwhi slrfgvdvfr ngmdplsflr
      181 ylntlgqmvq vttvtdsipa veawdpesch lgfeidfrsa aghaainevf dfvredcave
      241 itpvnetpdh veptgtelvs qpehspmvas gellgdqrav prtpatatat averpssgse
      301 qknkdgryvr vnadkldeli nlvgelvias agasllaksc dndplqeass tvsglveqil
      361 dgalhlrmip igdtfnrfrr vvrdvsqelg kdidliinga eteldktvve kigdplmhll
      421 rnsmdhgies aearraagkp akghlslnay hdsgsiviei addgaglnre rildkaqqrg
      481 lvaagasltd qeiynlifep gfstaeavtn lsgrgvgmdv vkrnitllrg tvdldsqpgq
      541 gtivrirlpl tlaiingflv gidqstyvip ldmvqeciel dehnrqltrd sgyldlrgev
      601 lplvylrdhf nhegpaarrq nvvvvryaeh kaglvvdell gefqtvikpl gklfgalrgi
      661 sgstilgsga valildipal lnqivhmear stqapqsllp tsr
//
LOCUS       WP_004415891             376 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Pseudomonas syringae].
ACCESSION   WP_004415891
VERSION     WP_004415891.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 376)
  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 376)
  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
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 376)
  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   5  (residues 1 to 376)
  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   6  (residues 1 to 376)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 376)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 376)
  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 18624027
            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="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41405
     Region          15..83
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          81..355
                     /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 mpldldtplh shqplslner klldilrrrg aitratvste mdlaqqsvhr lieelisrgl
       61 lrsgervkng rgqpspriel vneavyaigv sintdsavvc vadlgcnvle qvtlrtppls
      121 rnstldslek tiermlqrng ieaqrvvgmg faiagfflen rqinapeplr dwslmdlqpv
      181 leerfgmpvw lennattaai geslvgvgaw asnfiylsfn fgfgagvvin gkpyfgshgn
      241 ageitlynde esinrpalry lledlhqsgv qvdsiedlrl rfdpdwpgvn twltrvkptl
      301 drlinalagl fdpqavvfgg qlppelgkrl iaattfwgth rynsppprpq lllsetngda
      361 aalgaalvpl kerffv
//
LOCUS       WP_004415734             271 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Pseudomonas syringae].
ACCESSION   WP_004415734
VERSION     WP_004415734.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..271
                     /product="formate/nitrite transporter family protein"
                     /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=28286
     Region          5..251
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mslntpqqia eiavesgvkk ahlglpslmi lgflagafia lgflldihvs tmiphewasl
       61 gnllgavvfp vglilvvlag gelltgnmms lpmalfagri glgqlvrnwv lvtlanliga
      121 lfvaycfghv vgltegafma ktvaianakv gasfeqafis gigcnwlvcl avwlsyaskd
      181 vigkvvgmwf pvmafvaigf qhivanmfvi paaifagsls waqfgdnfvp vflgnavgga
      241 vfvglayhla ffnaatkpve msrtsgaqtp e
//
LOCUS       WP_004417682             306 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Vibrio orientalis].
ACCESSION   WP_004417682
VERSION     WP_004417682.1
KEYWORDS    RefSeq.
SOURCE      Vibrio orientalis
  ORGANISM  Vibrio orientalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Vibrio orientalis"
                     /db_xref="taxon:28175"
     Protein         1..306
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33960
     Region          71..143
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mdidmaakpk qffskrwsli allalpvmpt palaqeflcd atqayanelp vldkacpigk
       61 glwgnskprg sestfwiqcg vfgkplslek akalykhigt dvwikpeakg wrcligpytn
      121 faevkqdlak vktekgykea firevvrgap vkaaplpvkt kksskpaaqs ttvipapikq
      181 pakpavvatp epkkaqqeia irlattlngv eykvpyvmfs ddqfymehsl pwnrmdyeea
      241 yktcyrlgmg matveqwqal lksgemekgq wpmhlpywgs nkvglftsgk tnqlkgtsll
      301 nvmcvk
//
LOCUS       WP_004418357             788 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas syringae].
ACCESSION   WP_004418357
VERSION     WP_004418357.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 788)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 788)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 788)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..788
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..788
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=85627
     Region          48..90
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          74..787
                     /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 mlrpfppslt alvalglsaa avaapvqldl paqplskslt qlsqesglqi saddsliask
       61 qapavrgsle paqalsrllg sgldaqvqgn avkvfqpasn gpmtlgnvei saqtgiagma
      121 ttegsgsytt gsmssatrlp lsiretpqsv svitrqried qgmndlndvv kyapgvtlrk
      181 fgsdrqqfla rgfaidnlmy dglptivstf tldtisgadl amydrvevvr gatglmtgag
      241 spsatlnlir krptttpqvs vttsagswdr yrtevdasnr lndsgtlrgr vvaayetgns
      301 fvderdkerq tfygvleadl sesttwtiga srqrddatsd wgslpsgpng enldlprstf
      361 lsndwaywdr hnvslftdlt hhfdngwssk laatriwaes dmysnyltan gtgygqaagq
      421 ydttdvqtsl dgslsgpfql fgrehelmlg vsrreekfdq kggfygstpi dihhfnpnvi
      481 akpdlatrta yvsqntatee gvyaaarfnp idplhlivgs rvswydyqnr sanngdykvi
      541 revtpyagvv ydlndtysay asyteifkpq nqldvgggvl dpmtgesyei glkgeyfdgs
      601 lnaslavfdm tqenrayaiv nppaacqqqn rvcyeaagev rsrgidaeit gqltpdwqas
      661 asytlvlsqy vkdrtndkgd lfapnqpkhl fkaatsyhlp gnlnkwrvga dvlaqsetyn
      721 rvgnghsvqd ayavvglmag yrfdehwdar vnlnnvfdek ywqgiplatg sgvygdprnl
      781 mvslkwsl
//
LOCUS       WP_004418576             346 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas syringae].
ACCESSION   WP_004418576
VERSION     WP_004418576.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 346)
  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 346)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 346)
  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   4  (residues 1 to 346)
  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 346)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..346
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38578
     Region          30..212
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          257..339
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mptltlrlgd lsvgfiqslt davnsfdrnp dalleqygld pirlsqarar lsiprymrlg
       61 haaiqltgqp glglrmgqls rfaqaglagi taaqapnvre aartlirfep lygsnyrgqs
      121 sfhedaagaw mrfysispyn aynrfvvdsi lagwlaqlst lagtelraqr veiefeapdy
      181 aaqyavlsdn pvvfgaatnq lrldqtslal rnpdhcpstw rhllllcege leqqtrtrsl
      241 reriiqllgp llnggsepdl eevaarlklp twtlrrklae egtcfravln dtrrdlamty
      301 irdtelafge iayllgfasa eafqrafkrw ngqtpgefrr sqrqsa
//
LOCUS       WP_004418635             143 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Vibrio orientalis].
ACCESSION   WP_004418635
VERSION     WP_004418635.1
KEYWORDS    RefSeq.
SOURCE      Vibrio orientalis
  ORGANISM  Vibrio orientalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Vibrio orientalis"
                     /db_xref="taxon:28175"
     Protein         1..143
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15629
     Region          8..142
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mirenncklr nkkvrgmtli elmlvvaiia ilasiaypsy qrhllkahri tvlgdlakiq
       61 lelernyngs yasaaqavlp ggvchfctrd qrqfelsvss altsytitat akgsqtgdkc
      121 kgssyskltl nsiglhtpnn cwq
//
LOCUS       WP_004419489             811 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas sp. Lz4W].
ACCESSION   WP_004419489
VERSION     WP_004419489.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. Lz4W
  ORGANISM  Pseudomonas sp. Lz4W
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 811)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 811)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 811)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..811
                     /organism="Pseudomonas sp. Lz4W"
                     /db_xref="taxon:1206777"
     Protein         1..811
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88832
     Region          61..109
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          92..811
                     /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 msrsldtflr pgllavaial sipltstcvi aaeqaptars ynlpagplaa tlnqiasqsg
       61 itlaidpalv agktsapvqg sfeastalre alrdsglqlv pgsagsfsli aipegvvale
      121 attisgqssy espwgpvdgy laqrtaagtk tdtslleapr sisvatrsqm qdravqnldd
      181 avrympgvta ssygsdsrae wlkvrgfept qfldglplpk gtyampklet wdlervallr
      241 gpassvygqt pagglldmvs rrpedsashe vqmqigsyqr kqisfdstgp iddegrflyr
      301 vsgvvrdsnt aidhnedkry niapsltwni dedtkltfls qfnrddtgit sqflplqgtk
      361 vstsagkvky henlgdpkwe fydktyyalg yafehrlndv wqfrqnlryt ksdlafqgit
      421 aggyygsvad dgtverganv vdedisqfav dnnfqadfdt gaikhtvlig ldhqrvntny
      481 kwdygaapas niinpiygqd fsnvkyttyn dynqktrdtg lylqdqmald nwrltlggrq
      541 dwlhtdttfy neknardtrd dsaftgnaal syvfdsgftp yvsyaesfqa epggfagksf
      601 kpgtgkqyel glkyqppgsd mlftaavydl trknivlsdt lgvsrplgea nvrgleleav
      661 gnvnenlklt aaytyantkm tkvsdpldkn rplpltpehq asiwadytwh kgalegfgvg
      721 fgaryigetd niaigsmayv pdasyghtda ytvydaavhy dlgkmnkslq gatvsvnann
      781 vfdkqylstc dgfycyygdr rnimasvnyk w
//
LOCUS       WP_004422476             192 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Metapseudomonas
            furukawaii].
ACCESSION   WP_004422476
VERSION     WP_004422476.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas furukawaii
  ORGANISM  Metapseudomonas furukawaii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 192)
  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 192)
  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   3  (residues 1 to 192)
  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   4  (residues 1 to 192)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 192)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Metapseudomonas furukawaii"
                     /db_xref="taxon:1149133"
     Protein         1..192
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21525
     Region          1..192
                     /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"
ORIGIN      
        1 mlrillindt akkvgrlkaa lveagfevid esgltidlpa rveavrpdvv lidtespgrd
       61 vmeqvvlvsr dqprpivmft dehdpkvmrq aiqagvsayi vegiqvdrlq pildvamarf
      121 esdqalraql nardqqlaer krielakgll mkmkncneee aytlmrrqam srqqkliqva
      181 eqiiamhdml gp
//
LOCUS       WP_004422646             256 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Metapseudomonas furukawaii].
ACCESSION   WP_004422646
VERSION     WP_004422646.1
KEYWORDS    RefSeq.
SOURCE      Metapseudomonas furukawaii
  ORGANISM  Metapseudomonas furukawaii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Metapseudomonas.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 256)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Metapseudomonas furukawaii"
                     /db_xref="taxon:1149133"
     Protein         1..256
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=27873
     Region          27..244
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mgmpsdsdvp tvtpcahcre geslgfdfsm afqpivdlrd nslfayealv rtakgggaae
       61 vlgrvnednr yafdqacrvk avelasrlai pcqvsinflp navysaatci ratleaarrf
      121 gfptnrlife itegeelvdk ahlksiiaey rkqgfktaid dfgagysgln llaefqpdli
      181 kldmalirni drdpvrdaiv rgilgvcqal sieviaegve tpeelaclrg lgvnlfqgyl
      241 farpgfeqlp pvnwpa
//
LOCUS       WP_004420204             292 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Mycoplasmopsis bovigenitalium].
ACCESSION   WP_004420204
VERSION     WP_004420204.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis bovigenitalium (Mycoplasma bovigenitalium Freundt
            1955)
  ORGANISM  Mycoplasmopsis bovigenitalium
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Mycoplasmopsis bovigenitalium"
                     /db_xref="taxon:2112"
     Protein         1..292
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33395
     Region          1..259
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mnklllidgn fmmfqsfyas yypekaitmk ddnnrstnav hvffmslfnl infvkpthif
       61 iafdahgktk rhelypeyka grkqtpieif dqfiitkeil dslniswfek vgdegddiia
      121 tvanqnknik kiiysrdqdl lqlvdnntsv lhksgagfiy yspwnfeqkf kikphlipdf
      181 kglagdksdn ikgvigigei ganklinkyg sieniyqnin ningsiknkl ikgkndamfc
      241 krlatlnknv einfdfndfs vaniafkngf vkmsefklns vikkwkkltn es
//
LOCUS       WP_004422945             330 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Ectopseudomonas oleovorans].
ACCESSION   WP_004422945
VERSION     WP_004422945.1
KEYWORDS    RefSeq.
SOURCE      Ectopseudomonas oleovorans
  ORGANISM  Ectopseudomonas oleovorans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Ectopseudomonas.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 330)
  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 330)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Ectopseudomonas oleovorans"
                     /db_xref="taxon:301"
     Protein         1..330
                     /product="AraC family transcriptional regulator"
                     /function="AraC-type DNA-binding domain-containing
                     proteins"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36913
     Region          26..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          247..329
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mlharlttlh vvslilqrfa eqpelrsqll agsgigaadl dnadaritrv qelqvcanal
       61 alradlgldl grslhvssyg llgyaalsaa tfgdawrlll qypallgtyf rldmqvegel
      121 awicasgyrd aealevfnve mclaslklig dellrqplsl egaeftyarp dyvshyaqsf
      181 pcplrfeaqr nafafpaall errlpladsv thgdmvercr rlnaefssrq awlervrqll
      241 aaqlaeppgl enlaqqmhcs prtlrrhlqe lgtsyqglld elrferakal lgeeqwpvyr
      301 iaevlgfset asfrhafqrw sgvppsrfra
//
LOCUS       WP_004423646             282 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Metamycoplasma auris].
ACCESSION   WP_004423646
VERSION     WP_004423646.1
KEYWORDS    RefSeq.
SOURCE      Metamycoplasma auris (Mycoplasma auris)
  ORGANISM  Metamycoplasma auris
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Metamycoplasma.
REFERENCE   1  (residues 1 to 282)
  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 282)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10097223
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Metamycoplasma auris"
                     /db_xref="taxon:51363"
     Protein         1..282
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=31523
     Region          5..280
                     /region_name="TBP_aldolase_IIB"
                     /note="Tagatose-1,6-bisphosphate (TBP) aldolase and
                     related Type B Class II aldolases. TBP aldolase is a
                     tetrameric class II aldolase that catalyzes the reversible
                     condensation of dihydroxyacetone phosphate with
                     glyceraldehyde 3-phsophate to produce tagatose 1; cd00947"
                     /db_xref="CDD:238477"
     Site            order(26..28,31,51,54..56,61,65,68..69,143,231..232,
                     234..235,238,242,245)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238477"
     Site            order(84..85,176..178,180,206..207,209,228,230..231)
                     /site_type="active"
                     /db_xref="CDD:238477"
     Site            order(85,177,206)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238477"
     Site            order(176,178,180,207,209)
                     /site_type="other"
                     /note="Na+ binding site [ion binding]"
                     /db_xref="CDD:238477"
ORIGIN      
        1 mlvnakeiiq nayknkkvvf hininnlewt kqillaanyk nvpiilgvsp saakyfggyn
       61 vcyslvksli kdlkikipvc lhldhgsyfd cleaikakfs simfdgsklp feknlelskk
      121 lseickkknl sieceigrig gaedgvisei sytnlneaka fkkigidmla vgignihgey
      181 psdwkglnfs llkelnetln mpfvlhggsg isdtdlkkci slgvskinin telqianara
      241 lesfiktndi menknynprr lyklpneaiy nkvieildkf ke
//
LOCUS       WP_004423773             246 aa            linear   BCT 20-JAN-2025
DEFINITION  phosphonate ABC transporter ATP-binding protein [Metamycoplasma
            auris].
ACCESSION   WP_004423773
VERSION     WP_004423773.1
KEYWORDS    RefSeq.
SOURCE      Metamycoplasma auris (Mycoplasma auris)
  ORGANISM  Metamycoplasma auris
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Metamycoplasma.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
REFERENCE   2  (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   3  (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   4  (residues 1 to 246)
  AUTHORS   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 246)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Metamycoplasma auris"
                     /db_xref="taxon:51363"
     Protein         1..246
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=28430
     Region          4..245
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mqnihfknys asyfkdknav lkdisldikk gqmiafigks gagkttifna llkqletksg
       61 hlcinnknid kikkrewkki iqkvgylsqe tnliehlnvy enilhfypky knkffsffhi
      121 ltkkqknevf kilenlgild kiytrvsdls ggqkqrveia klllkevdii ladeptssld
      181 iktskeimgl ldeinkkyqt tilinihdln imqsffnkyc fikdgcliks gnpknlsqke
      241 iedlyk
//
LOCUS       WP_004421970             244 aa            linear   BCT 20-JAN-2025
DEFINITION  16S rRNA (cytidine(1402)-2'-O)-methyltransferase [Leptospira
            noguchii].
ACCESSION   WP_004421970
VERSION     WP_004421970.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Zhao,M., Zhang,H., Liu,G., Wang,L., Wang,J., Gao,Z., Dong,Y.,
            Zhang,L. and Gong,Y.
  TITLE     Structural Insights into the Methylation of C1402 in 16S rRNA by
            Methyltransferase RsmI
  JOURNAL   PLoS One 11 (10), e0163816 (2016)
   PUBMED   27711192
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Kimura,S. and Suzuki,T.
  TITLE     Fine-tuning of the ribosomal decoding center by conserved
            methyl-modifications in the Escherichia coli 16S rRNA
  JOURNAL   Nucleic Acids Res 38 (4), 1341-1352 (2010)
   PUBMED   19965768
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Kozbial,P.Z. and Mushegian,A.R.
  TITLE     Natural history of S-adenosylmethionine-binding proteins
  JOURNAL   BMC Struct Biol 5, 19 (2005)
   PUBMED   16225687
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001055
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     gene            1..244
                     /gene="rsmI"
                     /GO_function="GO:0070677 - rRNA
                     (cytosine-2'-O-)-methyltransferase activity [Evidence
                     IEA]"
     Protein         1..244
                     /product="16S rRNA
                     (cytidine(1402)-2'-O)-methyltransferase"
                     /EC_number="2.1.1.198"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0070677 - rRNA
                     (cytosine-2'-O-)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0000451 - rRNA 2'-O-methylation [Evidence
                     IEA]"
                     /calculated_mol_wt=27431
     Region          9..228
                     /region_name="RsmI"
                     /note="16S rRNA C1402 (ribose-2'-O) methylase RsmI
                     [Translation, ribosomal structure and biogenesis];
                     COG0313"
                     /db_xref="CDD:440082"
ORIGIN      
        1 mkiefqktlv lvsvslgnpg dlttrakyll ehsdiligee pgitskllks isiskqfflc
       61 nehttpeeir slgeavinag ltvlvsdagt pgiedpgrel vqevlkrggn vrsapgpiaf
      121 gaalsisgfk ispftfcgff srdsaerkke liyylkpght ivfyetpyry kavlrdldwv
      181 fkkikddrei ffcldltlds efqfrgklen llkildtlpk gnpvivisqr kekwdrfskt
      241 kklr
//
LOCUS       WP_004424623             146 aa            linear   BCT 20-JAN-2025
DEFINITION  division/cell wall cluster transcriptional repressor MraZ
            [Metamycoplasma auris].
ACCESSION   WP_004424623
VERSION     WP_004424623.1
KEYWORDS    RefSeq.
SOURCE      Metamycoplasma auris (Mycoplasma auris)
  ORGANISM  Metamycoplasma auris
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Metamycoplasma.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Chen,S., Jancrick,J., Yokota,H., Kim,R. and Kim,S.H.
  TITLE     Crystal structure of a protein associated with cell division from
            Mycoplasma pneumoniae (GI: 13508053): a novel fold with a conserved
            sequence motif
  JOURNAL   Proteins 55 (4), 785-791 (2004)
   PUBMED   15146477
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449500
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Metamycoplasma auris"
                     /db_xref="taxon:51363"
     Protein         1..146
                     /product="division/cell wall cluster transcriptional
                     repressor MraZ"
                     /GO_function="GO:0000976 - transcription cis-regulatory
                     region 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=16858
     Region          1..139
                     /region_name="MraZ"
                     /note="DNA-binding transcriptional regulator and inhibitor
                     of RsmH methyltransferase activity [Translation, ribosomal
                     structure and biogenesis]; COG2001"
                     /db_xref="CDD:441604"
ORIGIN      
        1 mfgkyernld dkyrvvipsk ilselgneff vtigfdkqli lrdknefekl rtkleennsl
       61 nkdfrelnrf ifantelvnp dksnrinipk ylaekaaikk nvvfigagni cevfakeiyd
      121 akesqfenet sindlaqklf evgvkl
//
LOCUS       WP_004426099             406 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Leptospira noguchii].
ACCESSION   WP_004426099
VERSION     WP_004426099.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 406)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     Protein         1..406
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47637
     Region          289..369
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mntyiesfln rvysskilsn fedkiflkss lqkwieknif ptfliffsly lmiwnrtipe
       61 ilmsedlykf klisiicgis iysflllrli ilgifevqis yhyifknait aiilsfaflm
      121 yfekpfsmmi tgelfcfgic iytllessyl ifsrpykkey yflfpilggi gfgilgnfig
      181 tafynvewns isyyfyaffi ftlyllkrri ktqneeatlq dsvlslnset qeiieqpysi
      241 ledeilelve pleeknllke ddlkraeeri ngfireklya ddsirlidls aylgvslhqa
      301 sfylnkyknm gfsdfinqnr mndairllve krnmnlldia fecgfnsyts fhrackkwtg
      361 hspkglrrnt iqsntsnehf kistdsqkie ilnknsesne lnnavv
//
LOCUS       WP_004426197             574 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Leptospira noguchii].
ACCESSION   WP_004426197
VERSION     WP_004426197.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 574)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     Protein         1..574
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=65605
     Region          43..560
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mgnsefvqnt nlnikpvili vddeviilgs ikyaiqlsfg nrfdiemaed adsameilar
       61 ckseqidvpl vicdqvlrgk sgdelliqih qeypqiykvm ltgyasaksl gnalnkanly
      121 ryltkpwdse dliltiseav kayfqnrkva elsskleety lfnretlfpn fenlkrridr
      181 rlienensil aliriesfgs iaenfgiety rkmlfeflsv ldcfiggyng eifhiydnmi
      241 avltkieedr fysllsavri flrsecievd gisfqvkisi gvssdqsdvy dkarlammta
      301 snnpsveyip ysettnkvdr iyanlklgkk fnsalnagni ipyfqgiydn klnritkyec
      361 larimegdqi ynpamfipia kstgiirllt plmvektfky fskhpeysfs inisesdldk
      421 ksfplwvmnr llhyrispdr vifeilendh wngngssnst rslqelkeig ckiaiddfgv
      481 ersnferlie iqpdfikidg kfiqgihenq tsyrlaaait emahtigakv vaefvsneee
      541 leavkslsid ysqgyylmep aedilyketi lnlv
//
LOCUS       WP_004426416             484 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Leptospira noguchii].
ACCESSION   WP_004426416
VERSION     WP_004426416.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 484)
  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 484)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     Protein         1..484
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=56983
     Region          27..77
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mndnqrvfrv qkdrnftivk nhfiddarls mkatailllv lrypdnwrms vktlskfksd
       61 kessiasgfk elvtfgyaef rkgkdpvtgr fnsgwyffee sqkpevqyki kttenkrien
      121 qselflkevk esnrkenkvl dleqrerpql enqvvvnstl pstkeqkpsi qifssqiqnt
      181 treynqpsqt rleeqkelle eleikfkrek nqaldspqae kplldfplle npilenrplp
      241 ntiyqglskq vlfkqilnts reygppakth ieeqkqssek vnphfhfpds wlikfqeyyf
      301 kehgsemgqp dselkalnkl yelskgdwkv ieskiqvliq lrkqdskfwy eqslspesit
      361 kfwsrlferk vkptdknrmr nehqnksiga ekrtepkyne sskltpdkpi eikdldpykc
      421 flgwgksklf kqqleyyeqn sdplkyegtk kilfekfvne vypglvsdse vkktsienrk
      481 gsaa
//
LOCUS       WP_004426570             356 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Leptospira
            noguchii].
ACCESSION   WP_004426570
VERSION     WP_004426570.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     Protein         1..356
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=40100
     Region          1..352
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mgievknlvk rfgnftaidd lsldvpsgel vallgpsgsg kttllriiag ledadkgqvi
       61 fegrevgkkn akdrgvgfvf qhyalfrhmt ifeniafgle vrkrserpsk dkirdkvmsl
      121 lklvqlenfh nrypselsgg qrqrialara laieprflll depfgaldak vrkelrnwlr
      181 rlhdeihvts vfvthdqeea levsdkvvil rsgkieqvgt pdevynhpkn sfvfhflgdv
      241 nlfhgrvqgg qtqlgeikvd apehseiena savgyvrpyd veilrepiea qtipaeiqyi
      301 hstgrnvkvd lkrldtgtil esqlnssefq slnllpgetv hirfkkvkvy vedyti
//
LOCUS       WP_004417503             431 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Pseudomonas
            syringae].
ACCESSION   WP_004417503
VERSION     WP_004417503.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 431)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 431)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..431
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47967
     Region          16..413
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mleqvnvfye gwgerwqwgt lvsttaltgr plivfeysne arqrglelss ytlplegarl
       61 rrdfpdhqly lpgpvydslp dgwgmllmdr lfrrrgltta rigplerlay igssamgamt
      121 fepvaperqe sdvhipleql aadvkqvlrg nggeflqall lvggspqgar pkalvyrdpe
      181 tggfttaatp gfeawlikfp akeehaevca iemvyaeclr mcgietpdtr yinlpdglaa
      241 faskrfdrrd glripmqsla aftganyqsp gvldyvnflr atqmctndvr emaraferav
      301 fnvafnnrdd hpknfayims qdgqwklspa ydvtfcegag gyhqmdvmge aleisraqml
      361 rlaeeaemsp daatgvidsm cdvasrftai aenlcpqvit rdtlrmiqsr idqnvarlhh
      421 sqadgghgrf s
//
LOCUS       WP_004429005             371 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Leptospira noguchii].
ACCESSION   WP_004429005
VERSION     WP_004429005.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 371)
  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 371)
  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 371)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     Protein         1..371
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=41429
     Region          3..71
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          282..345
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mnqkrvgqil reareekkls vkdvaretni svkyilalet edysqfpget ftmgflknyg
       61 gylkldtgql inlyrgekie esqapleelt rptasyytki nvdknkifti asvliilisa
      121 yliidsfigp ssdedsvees gkkldipeni dflsrsipen rsesfiltpd kgvsfsvsnq
      181 qcklfidsve kggavntavl afnvypeltv ykfrlsegqe kilsytipei sslrrnvrii
      241 sqavtensak vlvtlseeeq rqennnpvdn tktlgdvpiq vtlvfnkpsy aefiidgqmg
      301 frglvqtget rsleakdrle lkvgdgsave miqngkpkit lgrpgklvkk ifvktqnpyd
      361 stqsiikelg e
//
LOCUS       WP_004429377             387 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Leptospira noguchii].
ACCESSION   WP_004429377
VERSION     WP_004429377.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 387)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     Protein         1..387
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44621
     Region          284..363
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mqeveyysla atlylmiaaf gifkknkqkn igapvlfflm acafwsftat vfisenvlak
       61 klaqyfyayf smatafffmn fvtntkkkdl pyiysdfttl rklllrsfas taaivvlwdl
      121 fdefkipnis eivslgillf fiylffqtlv llyssknkdi llkilpsigl llvikltevf
      181 ryfegskvme pihtfhyyfl ilspiilsec isiissdiqk tqnkflldds tknevdknls
      241 qrdsiqekks lledlniekv esklaelmqn ekvhldeelr lpslasemgl svhhlsafln
      301 ehmgmnfntf inhhrikeak vmlleepdrs ilsigmavgf ssssafhraf lketkkspka
      361 freenlpnyk skedemenld pryshsi
//
LOCUS       WP_004279739             875 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Acinetobacter lwoffii].
ACCESSION   WP_004279739
VERSION     WP_004279739.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter lwoffii
  ORGANISM  Acinetobacter lwoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 875)
  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 875)
  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 875)
  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   4  (residues 1 to 875)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..875
                     /organism="Acinetobacter lwoffii"
                     /db_xref="taxon:28090"
     Protein         1..875
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=98323
     Region          106..832
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mtqrldqins siasntsttp qkirsdllis afeqseiknt ldhtrltstq lthipnleki
       61 pastkrikpl nnflgqdrar asveagialp ysgynifavg taglgkrtmv krllqqhakt
      121 metpndwvyv nnfqnqrqpi alelpsgqgp kfqamlnqsw qtilkqlerr ftaetyhnri
      181 emirqetgde qqqalieltk egaeldlkli srhdehcfvp vhliddklqe msqedlnals
      241 nqdraelatn mrymdkkler lglhlgdled dardrvqiln rdiakqvvlp rveqilskfk
      301 hvqglehylk yyaediinnv eivleqeedd ftpalfsrvp aryqanviit hkpnsgvpvi
      361 fedfpthynl lghveqltqn gtittdftli rpgtlhkang gflmleaeql leqpyawqgl
      421 kralksghlk lsslehmitl tgsisiepas iplnikvill aepeiyyeil elepelgsif
      481 kiradftdtl qrndnneqay mqliadyvqs dkllpfdrsa laalltdssr qaedqsslsl
      541 haltlgdlir eahhhafqag dkmvsekhin taldhrkyrl gylrelywqd ltrgtqliet
      601 rghrlgqina lsvihyadve fglpsrltas vyqgggdild iersvelggs lhakgvllms
      661 sflkahfgre qtlhfsaala feqsygqvdg dsatvaelsa llsaisqlpi dqswaitgsm
      721 nqlgqvqpvg gvnakiegff dacklqgltg kqgviiprqn mqhlmlrkdv tiaveegqfh
      781 ihaidtidqa leilmarpvg tldkkgrysk nsiyaavmaq ldywqaiedg aelvevpkkk
      841 kkkkkkkdkk qivepqteve adastvekpd aaten
//
LOCUS       WP_004430680             463 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase family protein [Agrobacterium].
ACCESSION   WP_004430680
VERSION     WP_004430680.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium
  ORGANISM  Agrobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 463)
  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 11465564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Agrobacterium"
                     /db_xref="taxon:357"
     Protein         1..463
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=50085
     Region          184..>221
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          331..461
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mkqflnaalg ltvalvavfa plqagaqqry gdqqqtmlvt pdgrvldfmp ergdivisrd
       61 amgrtvfydq ygnllatemp sgyqqrqqar qrdttyyppa pggqyrepqr dygyqdngsv
      121 rdyreyrgdg sddnfytgsv papgavesgp lgqpmpgest taavpqpdhl ierhtpvttp
      181 vnrsrqeiva lqtfldregi spgvidgkmg dnvnkaiaaw qdmtgekldp nnsddilerl
      241 rasggmpivd ytitaadaag pyvasipddy aaksqlpals ftstsealae rfhmdenylk
      301 elnpgidfsv pgtiikvvnp getkkgqvar ivahkgikqv faygqdgnli aaypatigst
      361 dtpspsgtht verialnpgy tynpkinfkq gqndkilqip pgpngpvgtv wialskptyg
      421 ihgtpepski gktnshgcir ltnwdatela kmvrpgvvve fae
//
LOCUS       WP_004431743              76 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Schinkia azotoformans].
ACCESSION   WP_004431743
VERSION     WP_004431743.1
KEYWORDS    RefSeq.
SOURCE      Schinkia azotoformans
  ORGANISM  Schinkia azotoformans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Calidifontibacillus/Schinkia group; Schinkia.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 76)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 76)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 76)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Schinkia azotoformans"
                     /db_xref="taxon:1454"
     Protein         1..76
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8114
     Region          1..76
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 minillfahl geaigepsvt wtelpitvgd lkqkitqryn lplqsvmvav neeyaedqle
       61 lkagdvvali ppvsgg
//
LOCUS       WP_004432692             425 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Leptospira noguchii].
ACCESSION   WP_004432692
VERSION     WP_004432692.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 425)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     Protein         1..425
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=49542
     Region          19..248
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mlysqdtsnl lsygennyqp hyqpilevtn cniigyevlg rfyfpekney rslgyqfhnp
       61 eldairliqi drlirekair hlkdsglrtk lflnmmpnfl smihtgdvld lkrihvlnli
      121 ekydippsev vleitedkfd gniekllsiv nvfkdygfki avddlgvgfs nlerigyihp
      181 dimkvdikim reslnrrsfk nvlsaiadms qklgsdllfe gieteeelhl alsmganllq
      241 gfyfsrpqve fqdkkqftrt lrdtlekfsg lrfmelleef qkgqsvidsl geklealrhn
      301 gkedlplvlh lmlselptei lsvfacdifg yqitptyfrv hpgeewdsdl teignnyawr
      361 pffirhkakv vqnsakwtvt epmydmdlhk qvviftytlr dnyilvikmd weteglgqki
      421 edrrq
//
LOCUS       WP_004433676             234 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Bacillus methanolicus].
ACCESSION   WP_004433676
VERSION     WP_004433676.1
KEYWORDS    RefSeq.
SOURCE      Bacillus methanolicus
  ORGANISM  Bacillus methanolicus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 234)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Bacillus methanolicus"
                     /db_xref="taxon:1471"
     Protein         1..234
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=27207
     Region          <3..230
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mpinsiirnd effhhyqpiy diqnwkvvgy eglfrtegls tpeitfdiak rkkklyelds
       61 rsihkaslty lkagysdryr nlflnvfpst itnpkfhtfi dqiindnefk sqqlifeine
      121 nedvkfdilk ksishlknlg fliaiddfgk gyssiksive lqpdfikldr ffiedlrnse
      181 qkkdliryll hfchkfnskl iaegvednes lailkslgvq yaqgfllgrp alls
//
LOCUS       WP_004433754             348 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Bacillus methanolicus].
ACCESSION   WP_004433754
VERSION     WP_004433754.1
KEYWORDS    RefSeq.
SOURCE      Bacillus methanolicus
  ORGANISM  Bacillus methanolicus
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Bacillus methanolicus"
                     /db_xref="taxon:1471"
     Protein         1..348
                     /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=41078
     Region          1..272
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mkqrnyyfdn akfiliffvv fghllrsfie nnetiytiyk viytfhmpaf ivvsgffakg
       61 fyqkgyvkki akklilpymt fqiiysifyy flyeqselkm dpfdphwslw flislffwni
      121 mlllfakyka avsitaalii glligyvdsv snylslsrtf vffpffllgy ylrkehisal
      181 lrvkfrlfsl aafiivfigf ylypemnyew llgskpygel geasfnamlt rlglyilsvi
      241 mvfsffafvp rkqyfftslg knslyvyllh gffvrafres eipklfhepe nflllagisl
      301 lltivlssqi aisfaqplie fklsrlkllq awfisivkfy rkklnnei
//
LOCUS       WP_004425093             114 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Ectopseudomonas
            oleovorans].
ACCESSION   WP_004425093
VERSION     WP_004425093.1
KEYWORDS    RefSeq.
SOURCE      Ectopseudomonas oleovorans
  ORGANISM  Ectopseudomonas oleovorans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Ectopseudomonas.
REFERENCE   1  (residues 1 to 114)
  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 114)
  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   3  (residues 1 to 114)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Ectopseudomonas oleovorans"
                     /db_xref="taxon:301"
     Protein         1..114
                     /product="endonuclease domain-containing protein"
                     /function="Very-short-patch-repair endonuclease
                     [Replication, recombination, and repair]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=13760
     Region          14..108
                     /region_name="Endonuclease_DUF559"
                     /note="Putative endonuclease; cd01038"
                     /db_xref="CDD:411708"
     Site            order(18,47,64,71)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:411708"
ORIGIN      
        1 mtlldnakrl rhemtdaeqr lwyylrahrf lglkfkrqkp igpyivdfic terwlvield
       61 ggqhqlqtey dqqrerylet rgyrvlrfwn hqvlaetkav leqirleige qdgl
//
LOCUS       WP_004433913             286 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Bacillus methanolicus].
ACCESSION   WP_004433913
VERSION     WP_004433913.1
KEYWORDS    RefSeq.
SOURCE      Bacillus methanolicus
  ORGANISM  Bacillus methanolicus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 286)
  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 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   3  (residues 1 to 286)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 286)
  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   5  (residues 1 to 286)
  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   6  (residues 1 to 286)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Bacillus methanolicus"
                     /db_xref="taxon:1471"
     Protein         1..286
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32419
     Region          21..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..286
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 malveslqka idymedhlld nitiediakq pnispshfqr ifmiltdisv geylrrrrlt
       61 laaqelsstn skiidiafky gydtpesfsk afrkqhgvtp searkgigki qsynrltiqv
      121 nlkgaepmky riverdafqv vgvkrefpcg aedagipgip efwseaneng tvnkliqlns
      181 gqikgllgli enfneekntv nywiaaehsg evpdefssle lpaskwvvfe vrgpipsami
      241 ntwkqiysew fpsnryeqae iapfeayids dlyspnsyne iwvaik
//
LOCUS       WP_004435256             574 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Leptospira noguchii].
ACCESSION   WP_004435256
VERSION     WP_004435256.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 574)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     Protein         1..574
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=65595
     Region          43..560
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mgnsefvqnt nlnikpvili vddeviilgs ikyaiqlsfg nrfdiemaed adsameilar
       61 ckseqidvpl vicdqvlrgk sgdelliqih qeypqiykvm ltgyasaksl gnalnkanly
      121 ryltkpwdse dliltiseav kayfqnrkva elsskleety lfnretlfpn fenlkrridr
      181 rlienensil aliriesfgs iaenfgiety rkmlfeflsv ldcfiggyng eifhiydnmi
      241 avltkieedr fysllsavri flrsecievd gisfqvkisi gvssdqsdvy dkarlammta
      301 snnssveyip ysettnkvdr iyanlklgkk fnsalnagni ipyfqgiydn klnritkyec
      361 larimegdqi ynpamfipia kstgiirllt plmvektfky fskhpeysfs inisesdldk
      421 ksfplwvmnr llhyrispdr vifeilendh wngngssnst rslqelkeig ckiaiddfgv
      481 ersnferlie iqpdfikidg kfiqgihenq tsyrlaaait emahtigakv vaefvsneee
      541 leavkslsid ysqgyylmep aedilyketi lnlv
//
LOCUS       WP_004435321             220 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Bacillus methanolicus].
ACCESSION   WP_004435321
VERSION     WP_004435321.1
KEYWORDS    RefSeq.
SOURCE      Bacillus methanolicus
  ORGANISM  Bacillus methanolicus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 220)
  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   3  (residues 1 to 220)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Bacillus methanolicus"
                     /db_xref="taxon:1471"
     Protein         1..220
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25047
     Region          10..217
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mlkigdtlml epkysnsfet ykcrlverig ndlyidypvn titkrtvfll dgtqlkvtfv
       61 gayssvylfe sevmgrvkqk ipmlilsypg kknlikiqrr qyvrvetpad vaihplngef
      121 qpftavtedi saggaaaila gnneilregm iveaifvlpf qsgeyhyksf ksrvvrivdv
      181 senrkkislq fmeisgqdrq lllrfcferq lemkkkglsc
//
LOCUS       WP_004435506             296 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Leptospira noguchii].
ACCESSION   WP_004435506
VERSION     WP_004435506.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 296)
  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 296)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     Protein         1..296
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33254
     Region          21..77
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mgehypyikf fadiiesgvw anlssaaktl ylvllkfsdq hfkpvwpste vllkftgfkt
       61 kksiiqgkrd liqagllqvt pgtghtssry yfcfnypgsk ippqgynfgn pgggrketqg
      121 vgengsqgsg evapnhinit itnnqhqepg krkkevslde lekeygsttl teafsiakgr
      181 gmetnlryvq gicknltktk dssmpefnqn qgtydekett wngflrwsrd rlakssietl
      241 ekirvepdgr tlcildpvte slrmiiakyf teeirppilv ifsakneenr itstkh
//
LOCUS       WP_004436277             357 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Bacillus
            methanolicus].
ACCESSION   WP_004436277
VERSION     WP_004436277.1
KEYWORDS    RefSeq.
SOURCE      Bacillus methanolicus
  ORGANISM  Bacillus methanolicus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Bacillus methanolicus"
                     /db_xref="taxon:1471"
     Protein         1..357
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=40610
     Region          1..352
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msikiqnisk sfgsfkaldd ihihiktgel vallgpsgsg kttllriiag leaadqgsil
       61 fgnedithir tkerkvgfvf qhyalfrhms vfdnvayglk vrprksrpsk keieervyel
      121 lrlvkleaya nryptqlsgg qrqrvalara lavepkvlll depfgaldak vrkdlrrwlr
      181 rlhdnfqits ifvthdqeea ldvadrvvim negrieqigs peevydhpns pfvydflgnv
      241 nlfrgrlhkg klhqgnfqid apefsdaenk taigyvrphd isiekeensk dgvsavikhi
      301 hvvgpivhle lkrndteeyl eaeltkdlyn nlqlktgekv fvkpkqlrvf ipedyti
//
LOCUS       WP_004439004             410 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator
            [Hyphomicrobiales].
ACCESSION   WP_004439004
VERSION     WP_004439004.1
KEYWORDS    RefSeq.
SOURCE      Hyphomicrobiales
  ORGANISM  Hyphomicrobiales
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria.
REFERENCE   1  (residues 1 to 410)
  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 410)
  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
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 410)
  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   5  (residues 1 to 410)
  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   6  (residues 1 to 410)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 410)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Hyphomicrobiales"
                     /db_xref="taxon:356"
     Protein         1..410
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44461
     Region          31..74
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          94..393
                     /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 mrqsvetaqq appttmdmsg ganqigvray nerlvlslvr rhgglskaei arlcglsaqt
       61 vsvimrslek dgllirgerl rgrvgqpstp mrlnpdavfs fgvkigrrsv dlvlmdfvgh
      121 irlklrrtyp yplpewilpf viegmaeles klspaerqki agvgiaapfe lwnwaqevga
      181 pqiemerwrd vdiragiaen vsypvflqnd atsacgaelv fgagqnytdf lyvfigsfig
      241 ggvvlnsalf sgktgtagai gplpvqgedg ntvqllkias ifvlenmlre rgidprplwf
      301 spdewidfge pleswigkta aalaqaviaa asiidfssvi idggfpdwvr trivaatrea
      361 lkrhdlqgvt lpeivegavg sqaraiggas lplfsrylid qnvlfkdttg
//
LOCUS       WP_004439140             600 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sensor histidine kinase [Agrobacterium].
ACCESSION   WP_004439140
VERSION     WP_004439140.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium
  ORGANISM  Agrobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 600)
  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 600)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20493667
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Agrobacterium"
                     /db_xref="taxon:357"
     Protein         1..600
                     /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=65947
     Region          26..272
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          250..589
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mmlglglgyg avtkgsgvia esyfgemseq grttlrlavs alggllnrye plpaliadhd
       61 dieelvahpk dealrqranv ylksintlle ssdiyiitld getiaasnyd gptsfvgenf
      121 syrpyfqdaa kglqsrffal gttshkrgyy fsapilfnae ikgvivfkvd iegieasfgd
      181 genrilvsdp egiifmtgtp qwlysglmpl tperlartea srryanatlk elplkhgsfg
      241 shqlmtitqn egdreymvls qpmadagwtv svlmdtgslr tqvktamiai ilclclaaal
      301 iaamlqrrrr lrerlthqae aqaelerrve ertadlarvn qeieheiaer rqtekqlrkm
      361 qndlvqagkl aalgqmsaal sheinqplaa aknyaenasl lvergrldev renlrrisgl
      421 idrmasisrh lrnfarkpne kmtavsletv lrdtleivga rlkaanavld vnlgpvplav
      481 kagpvrlqqv lvniisnaad avegredrri aleavqhgqt vsvfirdrgp gvppaisdri
      541 fdpffttkgv grglglglsi syniikdfgg qlrvrnheeg gaefeielpa aawrmeaaae
//
LOCUS       WP_004426786             838 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Leptospira noguchii].
ACCESSION   WP_004426786
VERSION     WP_004426786.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 838)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 838)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 838)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..838
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     Protein         1..838
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=95082
     Region          37..838
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkrilqivln fwnqipiwir kslitilvlv vlikvlfvfl ifwkaprlsg elkipgltqp
       61 vsvirdsygv phirsedsss ayfalgyvca sdrlfqmeil rraakgelse vlgaelvptd
      121 iflrqvllrr taekmlqese kanpqilkel dsfleginyf lkteslpief tilgytpkpf
      181 drldvmsals llsfsfaeal rndalytile rklpnrnvse lfprhdaeep fsiqedqpsy
      241 spkkltenqk vflplakesk fsksgelsdl esiiqktnri lkelpslsgs nswvigpsrs
      301 ttggailand phigysnpgt wyevhlkagd hetygyhlpi fpfplvahnv qkawaltmle
      361 nddmdfyeei lhptkpnfvk ekgnwvpvqv lkesiqvkge epreitiqvt shgpilskpi
      421 qgytgpvvsl ywvfhhlsvp lletihslgh cssltecsti vsnlpapgln vsyadkngni
      481 awwsvgrfpi rkkktntrki lngasgeddv igyipfdqnp klinppegvi ltanhlptye
      541 lkgygkpegy wqesdrgrri hellsqkknw tvddmkkiqt dvhsfsarsi vplisleiee
      601 dknwsgvfke aldiyrkfdg entldssgat ifhtlnqfvm lnlwmdefge snlqifgqta
      661 erwnayksil anpksdfwdd lttpgiketr reilirsfaq tvrylskehg gppstwkwkd
      721 ahkikfehpm gkvpalnlif nqgpfsvasg esvinlmnqk einpkmtprv gpskrriidl
      781 tnpenswsvl ptgnsgnlgs pfygdqielf lngehrkirf tqsqiekdsk yiikmipk
//
LOCUS       WP_004438438             179 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Rhizobium/Agrobacterium group].
ACCESSION   WP_004438438
VERSION     WP_004438438.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium/Agrobacterium group
  ORGANISM  Rhizobium/Agrobacterium group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae.
REFERENCE   1  (residues 1 to 179)
  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 179)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 179)
  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   4  (residues 1 to 179)
  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   5  (residues 1 to 179)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Rhizobium/Agrobacterium group"
                     /db_xref="taxon:227290"
     Protein         1..179
                     /product="TRAP transporter small permease subunit"
                     /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=19844
     Region          4..166
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mksllkisal idsasealgk vagylvlicc lvsagnamvr yalnyssngw leiqwymfaf
       61 ivligasytl rmnehvrvdi iygaisprsr iwvdiigivl fllpgclyla wlswpmftls
      121 wnqgemssna gglirwpvkl iifagfallv lqgfselikr igalnglyal dtkyekplq
//
LOCUS       WP_004440252             407 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Rhizobium/Agrobacterium group].
ACCESSION   WP_004440252
VERSION     WP_004440252.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium/Agrobacterium group
  ORGANISM  Rhizobium/Agrobacterium group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae.
REFERENCE   1  (residues 1 to 407)
  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 407)
  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 407)
  AUTHORS   ter Beek,J., 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 407)
  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 407)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Rhizobium/Agrobacterium group"
                     /db_xref="taxon:227290"
     Protein         1..407
                     /product="CmpA/NrtA family 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=43301
     Region          2..263
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mperhsvkag fsptvdcavl ivaaekgfaa degielelvr kqsargvlsv lgedgvqiah
       61 lpapvpvgsa vglhdmpani igvftlslgg sattvspgfy delyreglkl pdpaafgram
      121 arvcaarraa genppvfave diastsfyal ryllgscgvl lgrdmeivea lpkampglle
      181 sgdvdalcsa epagsaavlg gagrivttga liwhnapeki lavkrdwada nasllegllr
      241 alyragewca npanieelag ilaaphymnv sgefllpalt gyistsqkdm qrfqeffvts
      301 akaanfpwqs qalwffsqml rwgeipagcr fdaavveaar nayrpdifrk amkplfvpvp
      361 ganlklegtl repvhvgasr tglvlgpdcf fdgrvfdpet ldmddei
//
LOCUS       WP_004440339             398 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Hyphomicrobiales].
ACCESSION   WP_004440339
VERSION     WP_004440339.1
KEYWORDS    RefSeq.
SOURCE      Hyphomicrobiales
  ORGANISM  Hyphomicrobiales
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 398)
  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 398)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Hyphomicrobiales"
                     /db_xref="taxon:356"
     Protein         1..398
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46042
     Region          1..396
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mtikvsneaa rriflarqgl ssppgkalsk dgllqlitdl gfvqvdsigt verahhqiif
       61 srnqtyrrnh lttllekdra lfehwthdas ilptefypyw khrfrrrepi iqerwrkwhg
      121 egfdaafget leriaatgpv larelkeegh qsggwwnwhp sktaleylwh tgklaiagrv
      181 nfqkvydlae rvipgehhet evehaefvdw acrealkrlg fathgeiaaf fdlvtpqear
      241 dwvknhrdel cevsllasdg dtarqsyafa dftadltdvp epssrvrvls pfdpllrdrn
      301 rterlfgfyy rievfvpepk rqygyyvfpl legdrligri dmkaerkgst ldvrrlwlep
      361 gvrasagrle kldaelsrla kftgvesvny legwreen
//
LOCUS       WP_004440794             465 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Leptospira noguchii].
ACCESSION   WP_004440794
VERSION     WP_004440794.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 465)
  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 465)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     Protein         1..465
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=54579
     Region          27..77
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mnenqrvfrv pkdrnytkvk nhfiddtrls lkatsillla lrypddwkms vktiarlksd
       61 kessitsglk elvtfgyaey rkkrskagef esgwyffees qkpevqlnik ptknnglenq
      121 relfeeekpl ldypqpenpl lenpvtvnpn venqplpnti dqrlskqelf tqklntsrey
      181 sqpakahvee qkqilleies kneetplldy pqsenpvvvn pnvenqplpn tidqrlskqe
      241 lssqklntsr eygppakthv eeqsskkvnp rfhfpdswli nfqnyylkeh gsemgqpdse
      301 lkalnslyei skgnwnviet kiqtliqlrk qdskfwceqs lspesiskfw srlferkekq
      361 yeknrmrnek rnepkynesk nmtdkpieik dldpykcflv wgktkllkqq lefyeqnpdp
      421 lkyegtkkil fekfvnevyp glvsnsevkk stienrkent qgiva
//
LOCUS       WP_004441250             195 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Hyphomicrobiales].
ACCESSION   WP_004441250
VERSION     WP_004441250.1
KEYWORDS    RefSeq.
SOURCE      Hyphomicrobiales
  ORGANISM  Hyphomicrobiales
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Hyphomicrobiales"
                     /db_xref="taxon:356"
     Protein         1..195
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21104
     Region          1..165
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlkniyawtm alaarktavw wlaivafves svfvvpadvl flpmvlakpk kamfyalvat
       61 vasvlggiag wflghyafes iarpilefyg kldsfehlkn svdyetivll lvtsglahlp
      121 pikvvtilsg aanislglfi lsavvtrgar ffilagllqr ygesvrhfie krlgaitaaa
      181 aaaliaiyav yvfvr
//
LOCUS       WP_004442062             283 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Clostridium botulinum].
ACCESSION   WP_004442062
VERSION     WP_004442062.1
KEYWORDS    RefSeq.
SOURCE      Clostridium botulinum
  ORGANISM  Clostridium botulinum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium; Clostridium botulinum group.
REFERENCE   1  (residues 1 to 283)
  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 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   3  (residues 1 to 283)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 283)
  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   5  (residues 1 to 283)
  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   6  (residues 1 to 283)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Clostridium botulinum"
                     /db_xref="taxon:1491"
     Protein         1..283
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32234
     Region          28..100
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          127..281
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 memleklnes iqyiesnlng eiqyekaaqi accsvyhyqr mfsyiagipl seyirnrrlt
       61 kaafdlqagd kvvdvalryg yesptafnra frkmhyvsps vaqkegiflk ayppisfkit
      121 ikgvgemkys iikneeiriv gvkapltkni denfkfvpkl weksaedgsi dnivslmned
      181 sngmlgvsvc mdsldnweyy iatktdkdap kgmheyiipa gtwavfpgeg pmpksiqeie
      241 kriitewfpt sgyeyadapd ielylnqdpt nakfevwipi rkk
//
LOCUS       WP_004442210             710 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Leptospira noguchii].
ACCESSION   WP_004442210
VERSION     WP_004442210.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 710)
  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   3  (residues 1 to 710)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     Protein         1..710
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79672
     Region          1..699
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdlseirdtf iseseellss mesnllilek dsnnnegihs vfrtihtikg tsgmfgyepi
       61 ekfthdvetl ldrirsgkqi ltkegieflf lacdhirrlv rdvgdtlild aqtsknqinl
      121 lslakklile dssnsqkdev lqnqsvsigh lnssstswqi tlipnihlfe sgldpstfik
      181 ylsqsgkvkh ifvypesipn wpefnpehsh lgfeisyesp sngeeihstf qflkegsylk
      241 ilspgcnlnl fmenyndfpl gkkaylnale iqkvftaeei qklsytsenl nsplttqteq
      301 tftfienqke sdfikiqtkt lrvdsskidt lislvgelit qeanlsrkis dsenlqlies
      361 seslyrlvte irefalslrm ipisdlfeky krvvrdlske lnkqveleii ggeteldrsv
      421 iekisdpivh ilrnaldhgi etseermkkg kpatgqlkiq ashgtgsili einddgkgld
      481 cdkilekais kglitrdqnl seseiyslif qpgfstaeev tnlsgrgvgm dvvlrniesl
      541 rgsvqihtlk dhgssfqirl pltlaiidgf lvkasnlyfi vpmqmvretv eskvilngss
      601 sgtmnlrgel lpvlhlsefl cleyssfgke nilileyedk sfgiivndlh gevqsvirpm
      661 aeifknikcf sgtsilgsge iafildvpgl ynsirdqeqn knkdlatktg
//
LOCUS       WP_004446404             821 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Leptospira noguchii].
ACCESSION   WP_004446404
VERSION     WP_004446404.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 821)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     Protein         1..821
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=92443
     Region          52..821
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mkhrsalply iflfllftwe tsaqpeetnk pilsesssng eetekekwnq gtisvigkrk
       61 tdlkripgsa tviekefleq tkpvdsmevl rripgasiry qdtglilnlg frgvnndlgr
      121 kvliledgvf tslnpysape qyytpnidrm erievvkgsg ailfgpstig gvvnfitkrp
      181 pknpvfsvsa qggsygffss qvsyggtfgn tgidisilrk qgdgfrdhqs frihefsfks
      241 vtdlnekhtl tskflataqd anmtylgltt aqfwnhpssn faeqdnrkle rysgdighew
      301 kladhsklvt kvysaytern warqnylrnt gsnfsaipsn viksydtepf vnrpgdtvym
      361 ldsvghrnrs yrfvgvesry qqdyqflgik nqldtglryh yetadikyld gpptpdytmf
      421 gngfnnpptg vvsseyslak sgnvrdhevn ntksiagfaq nsfkfqnsfs vipgiryemf
      481 tqnrtilrqq tidpatnqpd pnspsqevdk gskhtyhvvi pglgltydir knanwfkdlt
      541 wfagahkgfs ppryqdalnn sgiinridpe ysynyetgfr gditkylnaq ityfhlnyin
      601 qiiitsstsg ndsassakng grtyskgvet nvtfdpaqlf dvsfklpidl iytradarmn
      661 qysidtskit adqsfldfvv tqkdkngnyv pyvsrdtatl aigfihpkgf yvraeyqyfs
      721 sqyhddsntr tvywadsitd plgkkilqyl niasnssget gvipayelin cslgykdpvk
      781 rwslfitgkn ladvryisgr lpegiqvgpf rqinvgasfe l
//
LOCUS       WP_004449445             821 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Leptospira noguchii].
ACCESSION   WP_004449445
VERSION     WP_004449445.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 821)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     Protein         1..821
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=92392
     Region          52..821
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mkhrsalplc iflfllfswe asaqpeetnk pilsesssng eetekekwnq gtisvigkrk
       61 tdlkripgsa tviekefleq tkpvdsmevl rripgasiry qdtglilnlg frgvnndlgr
      121 kvliledgvf tslnpysape qyytpnidrm erievvkgsg ailfgpstig gvvnfitkrp
      181 pknpvfsvsa qggsygffss qvsyggtfgn tgidisilrk qgdgfrdhqs frihefsfks
      241 vtdlnekhtl tskflataqd anmtylgltt aqfwnhpssn faeqdnrkle rysgdighew
      301 kladhsklvt kvysaytern warqnylrnt gsnfstippn viksydtepf vnrpgdtvym
      361 ldsvghrnrs yrfvgvesry qqdyqflgik nqldtglryh yetadikyld gpptpdyamf
      421 gngfnnpptg vvsseyslak sgnvrdhevn ntksiagfaq nsfkfqnrfs vipgiryemf
      481 tqnrtilrqq tidpatnqpd pnspsqevdk gskhtyhvvi pglgltydir knanwfkdlt
      541 wfagahkgfs ppryqdalnn sgivnridpe ysynyetgfr gditkylnaq ityfhlnyin
      601 qiiitsstsg ndsassakng grtyskgvet nvtfdpaqlf dasfklpidl iytradarmn
      661 qysidtskit adqsfldfvv tqkdkngnyv pyvsrdtatl aigfihpkgf yvraeyqyfs
      721 sqyhddsntr tvywadsitd plgkkvlqyl nitsnssget gvipayelin cslgykdpvk
      781 rwslfitgkn ladvryisgr lpegiqvgpf rqinvgasfe l
//
LOCUS       WP_004449738             574 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Leptospira noguchii].
ACCESSION   WP_004449738
VERSION     WP_004449738.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 574)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     Protein         1..574
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=65542
     Region          43..560
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mgnsefvqnt nlnikpvili vddeviilgs ikyaiqlsfg nrfdiemaed adsameilar
       61 ckseqidvpl vicdqvlrgk sgdelliqih qeypqiykvm ltgyasaksl gnalnkanly
      121 ryltkpwdse dliltiseav kayfqnrkva elsskleety lfnretlfpn fenlkrridr
      181 rlienensil aliriesfgs iaenfgiety rkmlfeflsv ldcfiggyng eifhiydnmi
      241 avltkieedr fysllsavri flrsecievd gisfqvkisi gvssdqsdvy dkarlammta
      301 snnssveyip ysettnkvdr iyanlklgkk fnsalnagni ipyfqgiydn klnritkyec
      361 larimegdqi ynpamfipia kstgiirllt plmvektfky fskhpeysfs inisesdldk
      421 ksfplwvmnr llhyrispdr vifeilendh wngngssnst cslqelkeig ckiaiddfgv
      481 ersnferlie iqpdfikidg kfiqgihenq tsyrlaaait emahtigakv vaefvsneee
      541 leavkslsid ysqgyylmep aedilyketi lnlv
//
LOCUS       WP_004449970              91 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein, partial [Leptospira
            noguchii].
ACCESSION   WP_004449970
VERSION     WP_004449970.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 91)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     Protein         <1..91
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          1..78
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 telglsthqa syylnqylnm sfteflqfhr inevknmiri klnynllnia fecgfnsass
       61 fhracvkftg ksprdlrqel lsnietqrkv e
//
LOCUS       WP_004450419             206 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Leptospira noguchii].
ACCESSION   WP_004450419
VERSION     WP_004450419.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     Protein         1..206
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22812
     Region          73..201
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mtskecsten eevtgkepdr vvrklfrqtl vgivilllgv vflarvfpep vlvvsqkfie
       61 itgvfgvgvg imladslhvf ippdvflmla vvgklnsilv ivsasvgsli ggtvsyltgr
      121 illpkmeris tfvkrheqkl ehylhrygfw avvlaaltpl pyswvslaag amkmkyslff
      181 kgclfriprf ivfyyliqfg wvgggi
//
LOCUS       WP_004451648              99 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein, partial
            [Leptospira noguchii].
ACCESSION   WP_004451648
VERSION     WP_004451648.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            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   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 99)
  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 99)
  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 99)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     Protein         <1..99
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          1..88
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(18,37..38,56,59,67..68,80,85)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 idpvrrrvtl kdnivnisrk efdilqlmaa spgkvfsrem ileavwgmew dgfermidsh
       61 vkrirsklek nsaqpewiet iwgigyrftd nydnivipd
//
LOCUS       WP_004452112             258 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Clostridium botulinum].
ACCESSION   WP_004452112
VERSION     WP_004452112.1
KEYWORDS    RefSeq.
SOURCE      Clostridium botulinum
  ORGANISM  Clostridium botulinum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium; Clostridium botulinum group.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Clostridium botulinum"
                     /db_xref="taxon:1491"
     Protein         1..258
                     /product="formate/nitrite transporter family protein"
                     /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=27780
     Region          2..249
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 myseeinkis nvaenkrdll rnnrvgylis salagiyvgi gtiliftlgg nlesvnssyv
       61 klimglsfgi alslvimags elftgnnmvm aigtlnkktt wkdalsiwgn sfagnligsm
      121 llalifvntg lakgsvgkfi lktaetkmtl qpmelflrgl lcnilvclav wcslkmkeea
      181 gklimifwcl fafissgfeh svanmtllsi alfiphgvgi svngmaynli fvtlgniigg
      241 alfvgaayyk isensfkr
//
LOCUS       WP_004452979             392 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Leptospira noguchii].
ACCESSION   WP_004452979
VERSION     WP_004452979.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 392)
  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 392)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 392)
  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   4  (residues 1 to 392)
  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 392)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     Protein         1..392
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45630
     Region          120..372
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          294..372
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mdffpdlnfl dyliflkeal nryleylysa sivisfltgl sgfykatksr lnlvrgiflm
       61 sacfliighs kafafmtsnp ngilnlemri ffsyyygfav caslsstfyv mylfgslqnp
      121 lrlslysfls fpviflislm iedlisivyf gksvlftlqf sagifnfhyv iknkmkkiyl
      181 nypiqnftlc talivhsigm wlgmqnlmil alsftgffii yffileynhp efwkvsfsse
      241 qleiksedsk tqtlqtspkn lverldisri eekiqkfved reyldeeirl sdfsayigls
      301 lhqasyylnn ykdlsftdfl sfhrleeakr mieqrpdinl levalasgfn spssfrracl
      361 kftgkppkef rnyvlhhqmt psmtlefqnq lg
//
LOCUS       WP_004455029             710 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Leptospira noguchii].
ACCESSION   WP_004455029
VERSION     WP_004455029.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 710)
  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   3  (residues 1 to 710)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     Protein         1..710
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79484
     Region          1..699
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdlseirdtf iseseellss mesnllilek dsnnnegihs vfrtihtikg tsgmfgyepi
       61 ekfthdvetl ldrirsgkqi ltkegieflf lacdhirrlv revgdtlild aqtsknqinl
      121 lslakklile dssnsqkdev lqnqsvsigh lnssstswqi tlipnihlfe sgldpstfik
      181 ylsqsgkvkn ifvypesipn wpefnpehsh lgfeisyesp sngeeihstf qflkegsylk
      241 ilspgcslnl fmenyndfpl gkkaylnale iqqvltaeei qklsytsenl niplttqteq
      301 tftsienqke sdfikiqtkt lrvdsskidt lislvgelit qeanlsrkis dsenlqlies
      361 seslyrlvte irefalslrm ipisdlfeky krvvrdlske lnkqveleii ggeteldrsv
      421 iekisdpivh ilrnaldhgi etseerirkg kpatgqlkiq ashgtgsili einddgkgld
      481 cdkilekais kglitrdqnl seseiyslif qpgfstaeev tnlsgrgvgm dvvlrniesl
      541 rgsvqiqtlk dqgssfqirl pltlaiidgf lvkasslyfi vpmqmvretv eskvilngss
      601 sgtmnlrgel lpvlhlsefl clesnsfgke nilileyedk sfgiivndlh gevqsvirpm
      661 aeifknikcf sgtsilgsge iafildvpgl ynsirdqeqn knkdlatktg
//
LOCUS       WP_004455108             352 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Clostridium
            pasteurianum].
ACCESSION   WP_004455108
VERSION     WP_004455108.1
KEYWORDS    RefSeq.
SOURCE      Clostridium pasteurianum
  ORGANISM  Clostridium pasteurianum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Clostridium pasteurianum"
                     /db_xref="taxon:1501"
     Protein         1..352
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39101
     Region          1..331
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 myvevknlnk ifgdykaskn vsfgiergkl igllgpsgsg kttilriiag lesadsgevy
       61 idgklvndip agkrgigfvf qnyalfrnmt vyqnvafgls ikkvnkneik krvlelielv
      121 glkglekryp sqlsggqkqr vafaralapn pqlllldepf aaidakvrke lrtwlkqtih
      181 klgitsifvt hdqeeaveva deiiitnlgt veqkgepvei ykkpetafva kfigesniie
      241 kfdklkafkd iqkgskaiir pefvqigkeg evqyvsasdr gvvtdisfag snwiitakig
      301 dievtgirsl eqshfkvgde vlvlihrlyv fhenkveive nklkidpmpv yi
//
LOCUS       WP_004455890             352 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Clostridium perfringens].
ACCESSION   WP_004455890
VERSION     WP_004455890.1
KEYWORDS    RefSeq.
SOURCE      Clostridium perfringens
  ORGANISM  Clostridium perfringens
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Clostridium perfringens"
                     /db_xref="taxon:1502"
     Protein         1..352
                     /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=41069
     Region          8..283
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mntvlkqrkr ldyldiakgl liisvvlchs pfenayylyw fhmpaffiis gmlykrgmni
       61 keqaikffvp yaifslidis fnyimyyhgn fslgdlihei ikyayggkat wgvfwfipvm
      121 fvtkvvfdql nkrltskkla fvcilsyila hiysmsfips svtditenqf vfwnldtvli
      181 tfpyyalgyy itklniqrvf ketstlilss igvvamfiln ssigiyyyln ikysyykdpi
      241 fdilmpvtit ifilslsyqi skfkykklft iiganslvim ylhkqvatlf mdvfnygyim
      301 ftiigvclpl lmmvlinksi vskflfngdl tfyrkikdik diepkdiiid nk
//
LOCUS       WP_004456039             479 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Leptospira noguchii].
ACCESSION   WP_004456039
VERSION     WP_004456039.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 479)
  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 479)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     Protein         1..479
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=56320
     Region          28..77
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mndnqrvfrv qkdrnftvvk nhfiddprls mkatailllv lrypdnwrms vktmakfksd
       61 kdssiasgfk elvtfgyaef rkgkdpvtgr fnsgwyffee sqkpevqyki kttenkriek
      121 qselflkevk esnrkenkvl dleqrerpql enqvvvnstl pstkeqkpsi qvfssqiqnt
      181 treydqpsqa rieeqrelle eleikfkrek nqaldspqae kplldfplle npilenrplp
      241 ntidqglskq vlfkqilnts reygppakth ieeqkqssek vnphfhfpes wlmkfqeyyl
      301 kehgsemgqp dselkalnkl yelskgdwnv ieskiqtliq lrkqdsqfwy eqslspesit
      361 kfwsrlfvrk vkptdknrmr nehqnksigt epkynesksi pdkpieikdl dpykcflgwg
      421 ksklfkqqle yyeqnsdplk yegtkkilye kfvnevypgl vsdsevkkts ienrkgsaa
//
LOCUS       WP_004456574             368 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Leptospira noguchii].
ACCESSION   WP_004456574
VERSION     WP_004456574.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 368)
  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 368)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 368)
  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   4  (residues 1 to 368)
  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 368)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     Protein         1..368
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42078
     Region          102..353
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          270..349
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mnildsilnq eillslirfg agfalvlgig nwirarkqid ylvssvlilt aifqfidesm
       61 lnmipqtwlr kllflidiva laasgtlifl istmsfkrys klpliyywnl igplilslpi
      121 atfyeqhgnk elefflfaad lyvfvyfvia vanifidkky esstmsfkti lslvilislc
      181 ipleilgivf enkslillss vhttftvify yfltlirpnl ldiissesgk nfvkrsllhd
      241 vdinalekrl ihiikeeriy ldedirlpdv seelgisvhq lsfflnnhlg mnfnnyinqf
      301 rveeaksmli ndpsrsvvsv giavgfnsns sfykaflket gmspkqfret qtkvihfqss
      361 stdiqfrn
//
LOCUS       WP_004456805             406 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Leptospira noguchii].
ACCESSION   WP_004456805
VERSION     WP_004456805.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 406)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     Protein         1..406
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47636
     Region          289..369
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mntyiesfln rvysskilsn fedkiflkss lqkwieknif ptfliffsly lmiwnrtipe
       61 ilmsedlykf klisiicgis iysflllrli ilgifevqis yhyifknait aiilsfaflm
      121 yfekpfsmmi tgelfcfgic iytllessyl ifsrpykkey yflfpilggi gfgilgnfig
      181 tafynvewns isyyfyaffi ftlyllkrri ktqneeatlq dsvlslnset qeiieqpysi
      241 ledeilelve pleeknllke ddlkraeeri ngfireklya ddsirlidls aylgvslhqa
      301 sfylnkyknm gfsdfinqnr mndairllve krnmnlldia fecgfnsyts fhrackkwtg
      361 hspkglrrnt iqsntsnehf kistnsqkie ilnknsesne lnnavv
//
LOCUS       WP_004457977             245 aa            linear   BCT 20-JAN-2025
DEFINITION  16S rRNA (cytidine(1402)-2'-O)-methyltransferase [Leptospira
            santarosai].
ACCESSION   WP_004457977
VERSION     WP_004457977.1
KEYWORDS    RefSeq.
SOURCE      Leptospira santarosai
  ORGANISM  Leptospira santarosai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Zhao,M., Zhang,H., Liu,G., Wang,L., Wang,J., Gao,Z., Dong,Y.,
            Zhang,L. and Gong,Y.
  TITLE     Structural Insights into the Methylation of C1402 in 16S rRNA by
            Methyltransferase RsmI
  JOURNAL   PLoS One 11 (10), e0163816 (2016)
   PUBMED   27711192
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Kimura,S. and Suzuki,T.
  TITLE     Fine-tuning of the ribosomal decoding center by conserved
            methyl-modifications in the Escherichia coli 16S rRNA
  JOURNAL   Nucleic Acids Res 38 (4), 1341-1352 (2010)
   PUBMED   19965768
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Kozbial,P.Z. and Mushegian,A.R.
  TITLE     Natural history of S-adenosylmethionine-binding proteins
  JOURNAL   BMC Struct Biol 5, 19 (2005)
   PUBMED   16225687
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001055
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Leptospira santarosai"
                     /db_xref="taxon:28183"
     gene            1..245
                     /gene="rsmI"
                     /GO_function="GO:0070677 - rRNA
                     (cytosine-2'-O-)-methyltransferase activity [Evidence
                     IEA]"
     Protein         1..245
                     /product="16S rRNA
                     (cytidine(1402)-2'-O)-methyltransferase"
                     /EC_number="2.1.1.198"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0070677 - rRNA
                     (cytosine-2'-O-)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0000451 - rRNA 2'-O-methylation [Evidence
                     IEA]"
                     /calculated_mol_wt=26862
     Region          9..229
                     /region_name="RsmI"
                     /note="16S rRNA C1402 (ribose-2'-O) methylase RsmI
                     [Translation, ribosomal structure and biogenesis];
                     COG0313"
                     /db_xref="CDD:440082"
ORIGIN      
        1 mkeelqgtlv lvsislgnsd dltararnll eycdvligee vrttstllks lsiskrfllc
       61 nehttpeeir slaqtvmdsg lsvlisdagt pgiedpgkel vgevlrkggk vrsapgpiaf
      121 gaalsisgfk tspftfcgfl srdsserkae lsrylkpght vvfyetpyry ksvlqdlnlv
      181 fkktkderei ffcldltles efqfrgkige llkildtlpk gnpvivvspr kgksnlkvgl
      241 rsssk
//
LOCUS       WP_004441906             281 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phytoene/squalene synthase family protein
            [Agrobacterium].
ACCESSION   WP_004441906
VERSION     WP_004441906.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium
  ORGANISM  Agrobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Agrobacterium"
                     /db_xref="taxon:357"
     Protein         1..281
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30737
     Region          3..277
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 maptenldvc latlrdtdrd rylacllspa drrnalaaly afnaeiarir dsvrealpge
       61 vrmqwwrdll egsphgdsqs hpvasallet ieryrlprsv lsnmiearif dlyddpfedr
      121 nalegyaget asaliqlasl vlspeeaaas aeaaghagva qamagmmllm plhrrrgqvy
      181 ipadmlsaag ldretflegt drqrigiaie lfaahaldhi ekarrarisg nvfaaylpva
      241 isgpvitaar kagagvfege vqlsqlrrqw llakasflkr f
//
LOCUS       WP_004458087             352 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Clostridium perfringens].
ACCESSION   WP_004458087
VERSION     WP_004458087.1
KEYWORDS    RefSeq.
SOURCE      Clostridium perfringens
  ORGANISM  Clostridium perfringens
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Clostridium perfringens"
                     /db_xref="taxon:1502"
     Protein         1..352
                     /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=41083
     Region          8..283
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mntvlkqrkr ldyldiakgl liisvvlchs pfenayylyw fhmpaffiis gmlykrgmni
       61 keqaikffvp yaifslidis fnyimyyhgn fslgdlihei ikyayggkat wgvfwfipvm
      121 fvtkvvfdql nkrltskkla fvcilsyila hiysmsfips svteitenqf vfwnldtvli
      181 tfpyyalgyy itklniqrvf ketstlilss igvvamfiln ssigiyyyln ikysyykdpi
      241 fdilmpvtit ifilslsyqi skfkykklft iiganslvim ylhkqvatlf mdvfnygyim
      301 ftiigvclpl lmmvlinksi vskflfngdl tfyrkikdik diepkdiiid nk
//
LOCUS       WP_004460222             632 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Clostridium
            perfringens].
ACCESSION   WP_004460222
VERSION     WP_004460222.1
KEYWORDS    RefSeq.
SOURCE      Clostridium perfringens
  ORGANISM  Clostridium perfringens
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Clostridium perfringens"
                     /db_xref="taxon:1502"
     Protein         1..632
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=72681
     Region          33..628
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mplfkkeefn pyllnkiqpv ggikfnnrni vkgdgyeaci riydfpswvn dfwldnlldi
       61 kdvistidie tedrlkalnd inksisenqt rmydlksnid iieasnnvat lqnlvmdmtv
      121 rdeiikliti ryfinarteq eleekikyvl deiemrgyrg kvllneqeye wkslflsste
      181 qkylrnkrkg hpipsatlgg gyplnfveln dpygmfmgtt ltngvrgnii ldlfaktqtr
      241 ksynslvvgt mgagkstllk kvvknhtiig ntvrildvag efrslvldlg gkivsldgss
      301 giinplhiya tiidentnev lieqsymqhi sklsimykll apnsqddelr efeklivtfy
      361 kdygidreka teykaeeypt lsefykyikd nyfedddnvk knlsrfrqkr iediastien
      421 lvvtygkifd ghssimdltk enlisfevrt lssmdskifn aqmfnvltml wnnsliqglk
      481 ekrayderek kiyeavkyvl lideahkfin sdnimgvdfl ekfgrearky fagyifatqs
      541 irdvvpdinn sevakkiktl feltqykfim qqdnnakevl dkiflgqltq sevdaipllg
      601 tgetilsiss dknlkfkvei sdkedylfkg ga
//
LOCUS       WP_004455367             369 aa            linear   BCT 20-JAN-2025
DEFINITION  GerAB/ArcD/ProY family transporter [Clostridium pasteurianum].
ACCESSION   WP_004455367
VERSION     WP_004455367.1
KEYWORDS    RefSeq.
SOURCE      Clostridium pasteurianum
  ORGANISM  Clostridium pasteurianum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Clostridium pasteurianum"
                     /db_xref="taxon:1501"
     Protein         1..369
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=42268
     Region          2..358
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 mkekitsyef lilmflvpyg taslffmasd tkndvwiali fyslvsipiq miyislfnky
       61 pndspvtylp kifgkyigfi lsilyiwffa ydasrdlrdf ieltasfsli rlpmyitgav
      121 fvtaiiynvy kgienignma qiaflivafs sfcilllayi tdpniriqsi lpiihsgfvs
      181 lvtsgwklsm fpygefvvmt mfypfvlqrs klrkavifss ileglflavn nilfivtlgf
      241 efantndypl letlrwihig dflnrldiif lvvltlggff kisiliyaaa lgieqlfnfk
      301 hwgilcsilg vlilitslim ardnpehlni gwniglkyif pqfvilipla alithyiklf
      361 lqkknrnye
//
LOCUS       WP_004463838             123 aa            linear   BCT 20-JAN-2025
DEFINITION  zinc ribbon domain-containing protein [Acetivibrio thermocellus].
ACCESSION   WP_004463838
VERSION     WP_004463838.1
KEYWORDS    RefSeq.
SOURCE      Acetivibrio thermocellus
  ORGANISM  Acetivibrio thermocellus
            Bacteria; Bacillati; Bacillota; Clostridia; Acetivibrionales;
            Acetivibrionaceae; Acetivibrio.
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 12181465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Acetivibrio thermocellus"
                     /db_xref="taxon:1515"
     Protein         1..123
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14635
     Region          22..120
                     /region_name="zinc_ribbon_15"
                     /note="zinc-ribbon family; pfam17032"
                     /db_xref="CDD:465334"
ORIGIN      
        1 mfffaifgiq dknkhigncn nivcpscgrl smyevykyyk yfhifflpif kwdvryivkt
       61 sccgclyeld plvgkefekn psteireenl qridryspfk ycsncrtevp veysycpycg
      121 erl
//
LOCUS       WP_004464646             204 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Leptospira].
ACCESSION   WP_004464646
VERSION     WP_004464646.1
KEYWORDS    RefSeq.
SOURCE      Leptospira
  ORGANISM  Leptospira
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            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="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=22859
     Region          1..197
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mklvlgmaga sgsiyaerfi kalftiegtt fficspaslr vfreemeckv ssskelldfi
       61 iskykiqntp hrfeirnfad igadiasgsn swkgmvilpc smktiasina gmtenliert
      121 advtlkerrt lllvpretpy nrihlknmle lhdaggiilp aspgfyqmpk tledlgdfig
      181 erifrllgve mnlyprwapr dhge
//
LOCUS       WP_004455222             838 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Leptospira noguchii].
ACCESSION   WP_004455222
VERSION     WP_004455222.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 838)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 838)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 838)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..838
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     Protein         1..838
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=95158
     Region          37..838
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkrilltvln fwnqipiwir kslitilvlv vlikvlfvfl ifwkaprlsg elkipgltqp
       61 vsvirdsygv phirsedsss ayfalgyvca sdrlfqmeil rraakgelse vlgaelvptd
      121 iflrqvllrr taekmlqese kvnpqilkel dsfleginyf lkteslpief tilgytpkqf
      181 drldvmsals llsfsfaeal rndtlytile rklpnrnvse lfprhdaeep fsiqedqpsy
      241 spkkltenqk vflplakesk fsksdelsdl epiiqktnri lkelpslsgs nswvigpsrs
      301 ttggailand phigysnpgt wyevhlkagd hetygyhlpi fpfplvahnv qkawaltmle
      361 nddmdfyeei lhptkpnfvk ekgnwvpvqv lkesiqvkge epreitiqvt shgpilskpi
      421 qgytgpvvsl ywvfhhlsvp lletihslgr cssltacsti vsnlpapgln vsyadkngni
      481 awwsvgrfpi rkkktntrki lngasgeddv igyipfdqnp klinppegvi ltanhlptye
      541 lkgygkpegy wqesdrgrri hellsqkknw tvddmkkiqt dvhsfsarsi vplisleiee
      601 dknwsgvfke aldiyrkfdg entldssgat ifhtlnqfvm lnlwmdefge snlqifgqta
      661 erwnayksil anpksdfwdd lttpgiketr reilirsfaq tvrylskehg gppstwkwkn
      721 ahkikfehpm gkvpaldlif nqgpfavasg esvinlmnqk einpkmtprv gpskrriidl
      781 tnpenswsvl ptgnsgnlgs pfygdqielf lngehrkirf tqsqiekdsk yiikmipk
//
LOCUS       WP_004468596             337 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Leptospira santarosai].
ACCESSION   WP_004468596
VERSION     WP_004468596.1
KEYWORDS    RefSeq.
SOURCE      Leptospira santarosai
  ORGANISM  Leptospira santarosai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 337)
  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 337)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Leptospira santarosai"
                     /db_xref="taxon:28183"
     Protein         1..337
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38766
     Region          85..325
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          248..328
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 myeriinkfn iqqknllple svfvvisfqy ilkeffgtqs lvvsnfdfnf rlkivsiifg
       61 lqlfpflqir pilksilnlk snlsiqsifl flvvtgytll ivsndvfsfa lygslfvflv
      121 slgisaetff lvknhklpar fyaisvipff mgliffgnav lvltfdlnfy ffpffsytvi
      181 qllasilhfn sdkihlrmns fvsdptivpa dkhllkhvsl adiekklncf iqekkhtdfk
      241 sshlpdfaky lgislhqasy ylnqykglrf tdfinqyrie eallilsdns qpvnlkktal
      301 acgfssytpf fsafkkvtgi tptdfvnqkn lnisfrf
//
LOCUS       WP_004457695             507 aa            linear   BCT 20-JAN-2025
DEFINITION  response regulator transcription factor [Clostridium perfringens].
ACCESSION   WP_004457695
VERSION     WP_004457695.1
KEYWORDS    RefSeq.
SOURCE      Clostridium perfringens
  ORGANISM  Clostridium perfringens
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 507)
  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 507)
  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   3  (residues 1 to 507)
  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   4  (residues 1 to 507)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 507)
  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   6  (residues 1 to 507)
  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   7  (residues 1 to 507)
  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 14435958
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Clostridium perfringens"
                     /db_xref="taxon:1502"
     Protein         1..507
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=58713
     Region          4..124
                     /region_name="REC_YesN-like"
                     /note="phosphoacceptor receiver (REC) domain of YesN and
                     related helix-turn-helix containing response regulators;
                     cd17536"
                     /db_xref="CDD:381091"
     Site            order(9..12,15..17,20,106..107)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381091"
     Region          419..502
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mykvmladde nlilqgleni ieweelglei vnkasngqea idkfkenpvd ivvtdinmpq
       61 vtglellkel kkinsdvkfi ilsgyddfsy akkaielgve nyilkpidee elektlknti
      121 nkikqekeen ksslgkhnil iklikgklaq geieenkegf ymnlnserys lciintrsry
      181 dseemlhniv nvikentknn feiiytldee lilinswdea lskkeikkyy dklkeqiine
      241 ygidvflsvg epvcdlykis ssykeannlk kyvltlgynk cittedvkdi nekninfsev
      301 ldklnkriia kdiegaekii eetvedkkln prniydlsvk ilflldgive efkvekqytg
      361 nslgeeival csedtredik tllcseirev ielmhpttik yspviqqiis yvnenyyeev
      421 slktlaqkyh intsylgqvf tkevgcsfse ylnktknmka kelilntnmk indiakkvgy
      481 ldtsyfyrkf kkyygvcpst lrnikny
//
LOCUS       WP_004470719             204 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Leptospira santarosai].
ACCESSION   WP_004470719
VERSION     WP_004470719.1
KEYWORDS    RefSeq.
SOURCE      Leptospira santarosai
  ORGANISM  Leptospira santarosai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Leptospira santarosai"
                     /db_xref="taxon:28183"
     Protein         1..204
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=22887
     Region          1..197
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mklvlgmaga sgsiyaerfi kalftiegtt fficspaslr vfreemeckv ssskelldfi
       61 iskykiqntp hrfeirnfad igadiasgsn swkgmvilpc smktiasina gmtenliert
      121 advtlkerrt lllvpretpy nrihlknmle lhdaggiilp aspgfyqmpk tledlgdfig
      181 erifrllgve mnlyprwvpr dhge
//
LOCUS       WP_004471490             343 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Leptospira santarosai].
ACCESSION   WP_004471490
VERSION     WP_004471490.1
KEYWORDS    RefSeq.
SOURCE      Leptospira santarosai
  ORGANISM  Leptospira santarosai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 343)
  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 343)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 343)
  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   4  (residues 1 to 343)
  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 343)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Leptospira santarosai"
                     /db_xref="taxon:28183"
     Protein         1..343
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40138
     Region          85..321
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <260..321
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 myeqqktinp fftleknefp ileiiiislh filidvsygl wdlvisnldk hyrlifvsil
       61 fgiqlfpfll lrpiiksklk igsqfsiskn iliiavsipv flvlfqdals lalygsicif
      121 llslflavet fflvkkhrls frfywislip ismalicign vafilkynsd fndypfvsng
      181 inlfivslly frrynfrlfe lsnstgdndl lkkssladie tkidlfikek ryldikfnym
      241 sefskyleip syhaslyink yrgrsyrefi nqlrieevil nlsnnfqsrn iikiafasgf
      301 ssysafirsf kknigitpsq yivqnnlkid pdlrfihemk ded
//
LOCUS       WP_004473393             296 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Leptospira santarosai].
ACCESSION   WP_004473393
VERSION     WP_004473393.1
KEYWORDS    RefSeq.
SOURCE      Leptospira santarosai
  ORGANISM  Leptospira santarosai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 296)
  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 296)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Leptospira santarosai"
                     /db_xref="taxon:28183"
     Protein         1..296
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32835
     Region          21..77
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mgehypyikf fadiiesgvw adlssaaktl ylvllkfsdq hfkpvwpste illkltgfkt
       61 kksiiqgkkd liqagllqvt pgtghtssry yfcfnypgsk ippqgyifgt sgggilgtpg
      121 vsegrspgfg egnpnhinit itnnqnqeps kkanltlndl ekkygssvls ealsiaktrg
      181 meanlkyvqg icknlertdn nptmpefnpn rrssyekdat wkgfllwskd rltrssievl
      241 ekirvepdgr tlcildsvpe slqmiiakyf teeisppilv ifsakseenr iastkn
//
LOCUS       WP_004475463             846 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Leptospira santarosai].
ACCESSION   WP_004475463
VERSION     WP_004475463.1
KEYWORDS    RefSeq.
SOURCE      Leptospira santarosai
  ORGANISM  Leptospira santarosai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 846)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 846)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 846)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..846
                     /organism="Leptospira santarosai"
                     /db_xref="taxon:28183"
     Protein         1..846
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=95876
     Region          20..846
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mknimhtiss fwnrtptwgr rsvvafftlv vlikiifafl ifwkaprlsg eltvpglakp
       61 vsvvrdtygv phiqsedsts ayfalgyvsa sdrlfqmeil rraargelse vlgadlisad
      121 iflrqillrr taekmlkdae kgnpqilkel dsflagvnff leketlpief tilgyqpkpf
      181 drldvlsals llsfsfseal rndslytile rklpnrnvke lfprhdaedp fsirenqpsy
      241 spkrltesek nffpdrtgad rfsaskpetl sglelddfgs virrtnqilg elplflgsns
      301 wvigpsrttt ggavlandph igygnpgtwy evhlktgdye tygyhlpifp fpiiahnakk
      361 awaltmlend dmdfyeeiph ptkpnfvkek gnwvpvqvfk elipvkgeea reitiqvtsh
      421 gpilskpiag ytgpvvslyw vfhhlpapll etiyslgrcs tlqecydvvs llpapglnvs
      481 yadasgniaw wgvgrfpirr nktntrkiln gasgedevig ylpfsqnpkl vnppegiilt
      541 anhlptyelk gygkpegywq esdrgrriye llsqkkewsv ddmkkvqtdi hsfsartmvp
      601 lisleleedr nwtgvfreal dvyrmfdgen tldssgatif htlnqfvmln lwmdefgesn
      661 lqvfgqtaer wnsyksilvn pksdfwddls tsdlretrrd ilirsfaqtv rylskelggs
      721 psswkwgrvh eitfehpmgk vpllglifnq gpfpvvsges vinlmnqkei npkmtprvgp
      781 skrriidlvh penswsvlpt gnsgnigspf ygdqiqmfln gehrairftq sqiekdskyv
      841 lkfvpq
//
LOCUS       WP_004477015             296 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Leptospira santarosai].
ACCESSION   WP_004477015
VERSION     WP_004477015.1
KEYWORDS    RefSeq.
SOURCE      Leptospira santarosai
  ORGANISM  Leptospira santarosai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 296)
  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 296)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Leptospira santarosai"
                     /db_xref="taxon:28183"
     Protein         1..296
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32787
     Region          21..77
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mgehypyikf fadiiesgvw aglssaaktl ylvllkfsdq hfkpvwpste illkltgfkt
       61 kksiiqgkkd liqagllqvt pgtghtssry yfcfnypgsk ippqgyifgt sgggilgtpg
      121 vsegrspgfg egnpnhinit itnnqnqepp kkanltlndl ekkygssvls ealsiaktrg
      181 meanlkyvqg icknlertdn nptmpefnpn rrssyekdat wkgfllwskd rltrssievl
      241 ekirvepdgr tlcildsvpe slqmiiakyf teeisppilv ifsakseenr iastkn
//
LOCUS       WP_004480080             846 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Leptospira santarosai].
ACCESSION   WP_004480080
VERSION     WP_004480080.1
KEYWORDS    RefSeq.
SOURCE      Leptospira santarosai
  ORGANISM  Leptospira santarosai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 846)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 846)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 846)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..846
                     /organism="Leptospira santarosai"
                     /db_xref="taxon:28183"
     Protein         1..846
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=95827
     Region          20..846
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mknimhtiss fwnrtptwgr rsvvafftlv vlikiifafl ifwkaprlsg eltvpglakp
       61 vsvvrdtygv phiqsedsts ayfalgyvsa sdrlfqmeil rraargelse vlgadlisad
      121 iflrqillrr taekmlkdae kgnpqilkel dsflagvnff leketlpief tilgyqpkpf
      181 drldvlsals llsfsfseal rndslytile rklpnrnvke lfprhdaedp fsirenqpsy
      241 spkrltesek nffpdrtgad rfsaskpetl sglelddfgs virrtnqilg elplflgsns
      301 wvigpsrttt ggavlandph igygnpgtwy evhlktgdye tygyhlpifp fpiiahnakk
      361 awaltmlend dmdfyeeiph ptkpnfvkek gnwvpvqvfk elipvkgeea reitiqvtsh
      421 gpilskpiag ytgpvvslyw vfhhlpapll etiyslgrcs tlqecydvvs llpapglnvs
      481 yadasgniaw wgvgrfpirr nktntrkiln gasgedevig ylpfsqnpkl vnppegiilt
      541 anhlptnelk gygkpegywq esdrgrriye llsqkkewsv ddmkkvqtdi hsfsartmvp
      601 lisleleedr nwtgvfreal dvyrmfdgen tldssgatif htlnqfvmln lwmdefgesn
      661 lqvfgqtaer wnsyksilvn pksdfwddls tsdlretrrd ilirsfaqtv rylskelggs
      721 psswkwgrvh eitfehpmgk vpllglifnq gpfpvvsges vinlmnqkei npkmtprvgp
      781 skrriidlvh penswsvlpt gnsgnigspf ygdqiqmfln gehrairftq sqiekdskyv
      841 lkfvpq
//
LOCUS       WP_004480929             337 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Leptospira santarosai].
ACCESSION   WP_004480929
VERSION     WP_004480929.1
KEYWORDS    RefSeq.
SOURCE      Leptospira santarosai
  ORGANISM  Leptospira santarosai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 337)
  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 337)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Leptospira santarosai"
                     /db_xref="taxon:28183"
     Protein         1..337
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38832
     Region          85..325
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          248..328
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 myekiinkfn iqqknllple svfvvisfqy ilkeffgtqs lvvsnfdfnf rlkivsiifg
       61 lqlfpflqir pilksilnlk snlsiqsifl flvvtgytll ivsndvfsfa lygslfvflv
      121 slgisaetff lvknhklpar fyaisvipff mgliffgnaf lvltfdlnfy ffpffsytvi
      181 qllasvlhfn sdkihlrmns fvfdptivpa dkhllkhvsl adiekklncf iqekkhtdfk
      241 sshlpdfaky lgislhqasy ylnqykglrf tdfinqyrie eallilsdns qpvnlkktal
      301 acgfssytpf fsafkkvtgi tptdfvnqkn lnisfrf
//
LOCUS       WP_004481794             296 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Leptospira santarosai].
ACCESSION   WP_004481794
VERSION     WP_004481794.1
KEYWORDS    RefSeq.
SOURCE      Leptospira santarosai
  ORGANISM  Leptospira santarosai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 296)
  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 296)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Leptospira santarosai"
                     /db_xref="taxon:28183"
     Protein         1..296
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32765
     Region          21..77
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mgehypyikf fadiiesgvw aglssaaktl ylvllkfsdq hfkpvwpste illkltgfkt
       61 kksiiqgkkd liqagllqvt pgtghtssry yfcfnypgsk ippqgyifgt sgggilgtpg
      121 vsegrspgfg egnpnhinit itnnqnqeps kkanltlndl ekkygssvls ealsiaktrg
      181 meanlkyvqg icknlertdn nptmpefnpn rrssyekdat wkgfllwskd rltrssievl
      241 ekirvepdgr tlcildsvpe slqmiiakyf teeisppilv ifsakseenr tastkn
//
LOCUS       WP_004482483             702 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Leptospira santarosai].
ACCESSION   WP_004482483
VERSION     WP_004482483.1
KEYWORDS    RefSeq.
SOURCE      Leptospira santarosai
  ORGANISM  Leptospira santarosai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 702)
  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   3  (residues 1 to 702)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Leptospira santarosai"
                     /db_xref="taxon:28183"
     Protein         1..702
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=78755
     Region          1..692
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdlseiratf iseseellss mesnllilek dsengegihs vfraihtikg tsgmfayepi
       61 ekfthevetf ldrirsgkqi ltkegieflf lacdhirrlv esvedtlvld pktsrkqtdl
      121 islakkllnd fseeedskss psdhtnvpsg sshwqitlip nrhlfesgmd pytfikylar
      181 sgnikrvfvy pesvpdwref hpehsylgfe isydspgege eilstfqflk eesylkilpp
      241 kcgldlfeqn cksfpfgrea ylsaleiqkv lnkdelqklr nvsvhtteev rsssnevqng
      301 kesetlkvqt ktlrvdsski dtlialvgel itqeanlsrk iintedtqli esseslyrlv
      361 seirefalsl rmvpiadlfe kykrvvrdls kelnkqvele ifggeteldr sviekiadpi
      421 vhilrnaldh gietseerir kgksavgklq iqashgtgsi lieikddgkg ldgekiveka
      481 iskglvtkeq vlseseiysl ifqpgfstae hvtnlsgrgv gmdvvlknie slrgtvqiqt
      541 vkdrgssfhi rlpltlaiid gflvkasglf fivpmqmvre tveskvvlng sssgtmnlrd
      601 ellpilhlsg flslntnkfd kenilileye dksfgivvnd lqgeiqsvir pmakifksvk
      661 cfsgtsilgs geiafildvh glynsirdqe qsknrelavn sg
//
LOCUS       WP_004484359             296 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Leptospira santarosai].
ACCESSION   WP_004484359
VERSION     WP_004484359.1
KEYWORDS    RefSeq.
SOURCE      Leptospira santarosai
  ORGANISM  Leptospira santarosai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 296)
  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 296)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Leptospira santarosai"
                     /db_xref="taxon:28183"
     Protein         1..296
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32859
     Region          21..77
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mgehypyikf fadiiesgvw aglssaaktl ylvllkfsdq hfkpvwpste illkltgfkt
       61 kksiiqgkkd liqagllqvt pgtghtssry yfcfnypgsk ippqgyifgt sgggilgtpg
      121 vseerspgfg egnpnhinit itnnqnqepp kkanltlndl ekkygssvls ealsiaktrg
      181 meanlkyvqg icknlertdn nptmpefnpn rrssyekdat wkgfllwskd rltrssievl
      241 ekirvepdgr tlcildsvpe slqmiiakyf teeisppilv ifsakseenr iastkn
//
LOCUS       WP_004484677             337 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Leptospira santarosai].
ACCESSION   WP_004484677
VERSION     WP_004484677.1
KEYWORDS    RefSeq.
SOURCE      Leptospira santarosai
  ORGANISM  Leptospira santarosai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 337)
  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 337)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Leptospira santarosai"
                     /db_xref="taxon:28183"
     Protein         1..337
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38772
     Region          85..325
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          248..328
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 myekiinkfn iqqknllple svfvvisfqy ilkeffgtqs lvvsnfdfnf rlkivsiifg
       61 lqlfpflqir pilksilnlk snlsiqsifl flvvtgytll ivsndvfsfa lygslfvflv
      121 slgisaetff lvknhklpar fyaisvipff mgliffgnaf lvltfdlnfy ffpffsytvi
      181 qllasvlhfn sdkihlrmns fvsdptivpa dkhllkhvsl adiekklncf iqekkhtdfk
      241 sshlpdfaky lgislhqasy ylnqykglrf tdfinqyrie eallilsdns qpvnlkktal
      301 acgfssytpf fsafkkvtgi tptdfvnqkn lnisfrf
//
LOCUS       WP_004484894             332 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Leptospira
            santarosai].
ACCESSION   WP_004484894
VERSION     WP_004484894.1
KEYWORDS    RefSeq.
SOURCE      Leptospira santarosai
  ORGANISM  Leptospira santarosai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 332)
  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   2  (residues 1 to 332)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Leptospira santarosai"
                     /db_xref="taxon:28183"
     Protein         1..332
                     /product="aminoglycoside 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=39203
     Region          8..301
                     /region_name="COG3178"
                     /note="Predicted phosphotransferase,
                     aminoglycoside/choline kinase (APH/ChoK) family [General
                     function prediction only]"
                     /db_xref="CDD:442411"
ORIGIN      
        1 msnpvsltdq elkfldfsgk hpqkihpins easdrkyfrv fypdktlilc kdlrfqydfv
       61 eiadflgqeq fvvpeilkkd lihflilmtd ggekdltsva ddleyrewlv ksieilvglq
      121 ktnpippvss refdfekfef estftysnyl klqkefrikt qlrsevkifi eecsaflaey
      181 pvkvfchrdf hgrnllinse nricmidfqd armgtpfydl ssilydayrp ipfgmrqgly
      241 qlflklseqd fpkfkecyyi qclqrsykal gsyfylvadk kmdkyrvsvl naldnlleiv
      301 qvglfpdqly vffyllkeel lsnslfmkgi kr
//
LOCUS       WP_004484976              98 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [Leptospira].
ACCESSION   WP_004484976
VERSION     WP_004484976.1
KEYWORDS    RefSeq.
SOURCE      Leptospira
  ORGANISM  Leptospira
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Leptospira"
                     /db_xref="taxon:171"
     Protein         1..98
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10997
     Region          1..96
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mnsvevqdil iehkqellsl gvqklllfgs varnearegs dvdilvqfhs gkknfdsfmd
       61 lsfrledlln thvdlltees ltkdlrdsil seailiei
//
LOCUS       WP_004489458             803 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Leptospira santarosai].
ACCESSION   WP_004489458
VERSION     WP_004489458.1
KEYWORDS    RefSeq.
SOURCE      Leptospira santarosai
  ORGANISM  Leptospira santarosai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 803)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="Leptospira santarosai"
                     /db_xref="taxon:28183"
     Protein         1..803
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=90041
     Region          40..803
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 meqksilpfc iflffllswe vlsqpeqnps sngeepenaa isvigkrktd lkripgsaiv
       61 iekefleqtk pvdsmevlrr vpgasiryqd tglilnlgfr gvnndlgrkv liledgifts
      121 lnpysapeqy ytpnidrmer ievvkgsgai lfgpstiggv vnfitkrpsk epilsvsaqg
      181 gsygffasqi syggtfgntg idisflrkqg ngfrdhqnfr lhefsfkstt dlnekhvlts
      241 kflatvqdan mtylglttaq fwnhsssnfa eqdnrklqry sgdighewkf adhsklvtkv
      301 yaayternwa rqnylrntgp nfgaipgnvi ktydtepfvn rpgdtvymld svghrnrsyr
      361 fvgaesryqr dyqffgiknq ldaglryhye tadikyldgp stpdyaifgn gldkpptgas
      421 sseyslaksg nirdhevnqt ksvagfaqns fkfydrlsvi pgvryetftq nrtilrqqsl
      481 dpvtnqplan spsqevdkgs khtyhvvipg lgltydlhkd vtwfagahkg fsppryqdal
      541 nnsgvvnrid peysynyetg frgditnyln aqvsyfdlny inqiiitsst sgndsassak
      601 nggrtysrgl etnvtfdpak lfnasfklpi dliytradak mnqysidatk fapnqslldf
      661 ivtqkdkngn yvpyvsrdta tlalgfihsk gfysrveyqy fsaqyhddsn trtvywadli
      721 tdplgkkvlq ylnitsnssg etgvipaygl infslgykdp ikrwslfvtg knladvryis
      781 grlpegiqvg pfrqinvgvt lel
//
LOCUS       WP_004490212             296 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Leptospira santarosai].
ACCESSION   WP_004490212
VERSION     WP_004490212.1
KEYWORDS    RefSeq.
SOURCE      Leptospira santarosai
  ORGANISM  Leptospira santarosai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 296)
  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 296)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Leptospira santarosai"
                     /db_xref="taxon:28183"
     Protein         1..296
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32894
     Region          21..77
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mgehypyikf fadiiesgvw anlssaaktl ylvllkfsdq hfkpvwpste illkltgfkt
       61 kksiiqgkkd liqagllqvt pgtghtssry yfcfnypgsk ippqgyifgt sgggilgtpg
      121 vseerspgfg egnpnhinit itnnqnqeps kkanltlndl ekkygssvls ealsiaktrg
      181 meanlkyvqg icknlertdn nptmpefnpn rrssyekdat wkgfllwskd rltrssievl
      241 ekirvepdgr tlcildsvpe slqmiiakyf teeisppilv ifsakseenr tastkn
//
LOCUS       WP_004490259             846 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Leptospira santarosai].
ACCESSION   WP_004490259
VERSION     WP_004490259.1
KEYWORDS    RefSeq.
SOURCE      Leptospira santarosai
  ORGANISM  Leptospira santarosai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 846)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 846)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 846)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..846
                     /organism="Leptospira santarosai"
                     /db_xref="taxon:28183"
     Protein         1..846
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=95877
     Region          20..846
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mknimhtiss fwnrtptwgr rsvvafftlv vlikiifafl ifwkaprlsg eltvpglakp
       61 vsvvrdtygv phiqsedsts ayfalgyvsa sdrlfqmeil rraargelse vlgadlisad
      121 iflrqillrr taekmlkdae kgnpqilkel dsflagvnff leketlpief tilgyqpkpf
      181 drldvlsals llsfsfseal rndslytile rklpnrnvke lfprhdaedp fsirenqpsy
      241 spkrltesek nffpdrtgan rfsaskpetl sglelddfgs virrtnqilg elplflgsns
      301 wvigpsrttt ggavlandph igygnpgtwy evhlktgdye tygyhlpifp fpiiahnakk
      361 awaltmlend dmdfyeeiph ptkpnfvkek gnwvpvqvfk elipvkgeea reitiqvtsh
      421 gpilskpiag ytgpvvslyw vfhhlpapll etiyslgrcs tlqecydvvs llpapglnvs
      481 yadasgniaw wgvgrfpirr nktntrkiln gasgedevig ylpfsqnpkl vnppegiilt
      541 anhlptyelk gygkpegywq esdrgrriye llsqkkewsv ddmkkvqtdi hsfsartmvp
      601 lisleleedr nwtgvfreal dvyrmfdgen tldssgatif htlnqfvmln lwmdefgesn
      661 lqvfgqtaer wnsyksilvn pksdfwddls tsdlretrrd ilirsftqtv rylskelggs
      721 psswkwgrvh eitfehpmgk vpllglifnq gpfpvvsges vinlmnqkei npkmtprigp
      781 skrriidlah penswsvlpt gnsgnigspf ygdqiqmfln gehrairftq sqiekdsnyv
      841 lkfvpq
//
LOCUS       WP_004491227             846 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Leptospira santarosai].
ACCESSION   WP_004491227
VERSION     WP_004491227.1
KEYWORDS    RefSeq.
SOURCE      Leptospira santarosai
  ORGANISM  Leptospira santarosai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 846)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 846)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 846)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..846
                     /organism="Leptospira santarosai"
                     /db_xref="taxon:28183"
     Protein         1..846
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=95847
     Region          20..846
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mknimhtiss fwnrtptwgr rsvvafftlv vlikiifafl ifwkaprlsg eltvpglakp
       61 vsvvrdtygv phiqsedsts ayfalgyvsa sdrlfqmeil rraargelse vlgadlisad
      121 iflrqillrr taekmlkdae kgnpqilkel dsflagvnff leketlpief tilgyqpkpf
      181 drldvlsals llsfsfseal rndslytile rklpnrnvke lfprhdaedp fsirenqpsy
      241 spkrltesek nffpdrtgan rfsaskpetl sglelddfgs virrtnqilg elplflgsns
      301 wvigpsrttt ggavlandph igygnpgtwy evhlktgdye tygyhlpifp fpiiahnakk
      361 awaltmlend dmdfyeeiph ptkpnfvkek gnwvpvqvfk elipvkgeea reitiqvtsh
      421 gpilskpiag ytgpvvslyw vfhhlpapll etiyslgrcs tlqecydvvs llpapglnvs
      481 yadasgniaw wgvgrfpirr nktntrkiln gasgedevig ylpfsqnpkl vnppegiilt
      541 anhlptyelk gygkpegywq esdrgrriye llsqkkewsv ddmkkvqtdi hsfsartmvp
      601 lisleleedr nwtgvfreal dvyrmfdgen tldssgatif htlnqfvmln lwmdefgesn
      661 lqvfgqtaer wnsyksilvn pksdfwddls tsdlretrrd ilirsfaqtv rylskelggs
      721 psswkwgrvh eitfehpmgk vpllglifnq gpfpvvsges vinlmnqkei npkmtprvgp
      781 skrriidlah penswsvlpt gnsgnigspf ygdqiqmfln gehrairftq sqiekdskyv
      841 lkfvpq
//
LOCUS       WP_004491123             296 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Leptospira santarosai].
ACCESSION   WP_004491123
VERSION     WP_004491123.1
KEYWORDS    RefSeq.
SOURCE      Leptospira santarosai
  ORGANISM  Leptospira santarosai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 296)
  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 296)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Leptospira santarosai"
                     /db_xref="taxon:28183"
     Protein         1..296
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32837
     Region          21..77
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mgehypyikf fadiiesgvw aglssaaktl ylvllkfsdq hfkpvwpste illkltgfkt
       61 kksiiqgkkd liqagllqvt pgtghtssry yfcfnypgsk ippqgyifgt sgggilgtpg
      121 vseerspgfg egnpnhinit itnnqnqeps kkanltlndl ekkygssvls ealsiaktrg
      181 meanlkyvqg icknlertdn nptmpefnpn rrssyekdat wkgfllwskd rltrssievl
      241 ekirvepdgr tlcildsvpe slqmiiakyf teeisppilv ifsakseenr tastkn
//
LOCUS       WP_004493850             846 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Leptospira santarosai].
ACCESSION   WP_004493850
VERSION     WP_004493850.1
KEYWORDS    RefSeq.
SOURCE      Leptospira santarosai
  ORGANISM  Leptospira santarosai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 846)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 846)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 846)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..846
                     /organism="Leptospira santarosai"
                     /db_xref="taxon:28183"
     Protein         1..846
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=95771
     Region          20..846
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mknimhtiss fwnrtptwgr rsvvafftla vlikiifafl ifwkaprlsg eltvpglakp
       61 vsvvrdtygv phiqsedsts ayfalgyvsa sdrlfqmeil rraargelse vlgadlisad
      121 iflrqillrr taekmlkdae kgnpqilkel dsflagvnff leketlpief tilgyqpkpf
      181 drldvlsals llsfsfseal rndslytile rklpnrnvke lfprhdaedp fsirenqpsy
      241 spkrltesek nffpdrtgad rfsaskpetl sglelddfgs virrtnqilg elplflgsns
      301 wvigpsrttt ggavlandph igygnpgtwy evhlktgdye tygyhlpifp fpiiahnakk
      361 awaltmlend dmdfyeeiph ptkpnfvkek gnwvpvqvfk elipvkgeea reitiqvtsh
      421 gpilskpiag ytgpvvslyw vfhhlpapll etiyslgrcs tlqecydvvs llpapglnvs
      481 yadasgniaw wgvgrfpirr nktntrkiln gasgedevig ylpfsqnpkl vnppegiilt
      541 anhlptnelk gygkpegywq esdrgrriye llsqkkewsv ddmkkvqtdi hsfsartmvp
      601 lisleleedr nwtgvfreal dvyrmfdgen tldssgatif htlnqfvmln lwmdefgesn
      661 lqvfgqtaer wnsyksilvn pksdfwddls tsdlretrrd ilirsfaqtv rylskelggs
      721 psswkwgrvh eitfehpmgk vpllglifnq gpfpvvsges vinlmnqkei npkmtprvgp
      781 skrriidlah penswsvlpt gnsgnigspf ygdqikmfln gehrairftq sqiekdskyv
      841 lkfvpq
//
LOCUS       WP_004496331             135 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Leptospira].
ACCESSION   WP_004496331
VERSION     WP_004496331.1
KEYWORDS    RefSeq.
SOURCE      Leptospira
  ORGANISM  Leptospira
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Leptospira"
                     /db_xref="taxon:171"
     Protein         1..135
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=14890
     Region          11..110
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(12..13,31..32,40,43,45..46,48,51..52,54,64,69,75)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(31,64..65,67,93)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mnsykdnsei sffkevyalv kkvpkgkvts ygriaallgk praaravgya lnalskgqeq
       61 kvpwqrvins qgkisfrgdt grsilqkkml edegikfgsa etidlkvfgw pdtisgkpah
      121 kkrknlsgnr vlpkr
//
LOCUS       WP_004464038             245 aa            linear   BCT 20-JAN-2025
DEFINITION  16S rRNA (cytidine(1402)-2'-O)-methyltransferase [Leptospira
            santarosai].
ACCESSION   WP_004464038
VERSION     WP_004464038.1
KEYWORDS    RefSeq.
SOURCE      Leptospira santarosai
  ORGANISM  Leptospira santarosai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Zhao,M., Zhang,H., Liu,G., Wang,L., Wang,J., Gao,Z., Dong,Y.,
            Zhang,L. and Gong,Y.
  TITLE     Structural Insights into the Methylation of C1402 in 16S rRNA by
            Methyltransferase RsmI
  JOURNAL   PLoS One 11 (10), e0163816 (2016)
   PUBMED   27711192
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Kimura,S. and Suzuki,T.
  TITLE     Fine-tuning of the ribosomal decoding center by conserved
            methyl-modifications in the Escherichia coli 16S rRNA
  JOURNAL   Nucleic Acids Res 38 (4), 1341-1352 (2010)
   PUBMED   19965768
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Kozbial,P.Z. and Mushegian,A.R.
  TITLE     Natural history of S-adenosylmethionine-binding proteins
  JOURNAL   BMC Struct Biol 5, 19 (2005)
   PUBMED   16225687
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001055
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Leptospira santarosai"
                     /db_xref="taxon:28183"
     gene            1..245
                     /gene="rsmI"
                     /GO_function="GO:0070677 - rRNA
                     (cytosine-2'-O-)-methyltransferase activity [Evidence
                     IEA]"
     Protein         1..245
                     /product="16S rRNA
                     (cytidine(1402)-2'-O)-methyltransferase"
                     /EC_number="2.1.1.198"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0070677 - rRNA
                     (cytosine-2'-O-)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0000451 - rRNA 2'-O-methylation [Evidence
                     IEA]"
                     /calculated_mol_wt=26846
     Region          9..229
                     /region_name="RsmI"
                     /note="16S rRNA C1402 (ribose-2'-O) methylase RsmI
                     [Translation, ribosomal structure and biogenesis];
                     COG0313"
                     /db_xref="CDD:440082"
ORIGIN      
        1 mkeelqgtlv lvsislgnsd dltararnll eycdvligee vrttstllks lsiskrfllc
       61 nehttpeeir slaqtvmdsg lsvlisdagt pgiedpgkel vgevlrrggk vrsapgpiaf
      121 gaalsisgfk tspftfcgfl srdsserkae lsrylkpght vvfyetpyry ksvlqdlnlv
      181 fkktkderei ffcldltles efqfrgkige llkildtlpk gnpvvvvspr kgksnlkvgl
      241 rgssk
//
LOCUS       WP_004497181             838 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Leptospira weilii].
ACCESSION   WP_004497181
VERSION     WP_004497181.1
KEYWORDS    RefSeq.
SOURCE      Leptospira weilii
  ORGANISM  Leptospira weilii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 838)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 838)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 838)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..838
                     /organism="Leptospira weilii"
                     /db_xref="taxon:28184"
     Protein         1..838
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=95272
     Region          20..838
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkhlsnrlfs fwkklplwtr rsleiifvli ffvklgfvfl ifwkaprlsg eltvpgltkp
       61 vsvvrdsygv phirsedsss ayfalgyvsa sdrlfqmeil rraargelse vlgaelvptd
      121 iflrqvllrr taekmlqesv kgnpqilkel dsfleginyf lkteslpief tilgyqpkpf
      181 drldvlsals llsfsfaeal rndslytile rklpnrniae lfprhdaedp fsirenqpsy
      241 spkrlteark nsfllaekse faksnelsdf asvirrtnqi leelplflgs nswvispsrs
      301 ttggailand phigygnpgt wyevhlmags yetygyhlpi fpfpiiahna kkawaltmle
      361 nddmdfyeev lhptkpnfvk ekgnwvpvqv fkelipvkge eareitiqvt shgpilskpi
      421 agysgpvvsl ywifhhipap vletvyslgr csslqecsev vsklpapgln isyadangni
      481 awwsvgrfpi rknktntrki lngasgeddv igylpfeqnp klinppegii ltanhlptye
      541 lkgygkpegy wqesdrgrri yellsqkkew svedmkkiqt dvhsfsarti vplislelel
      601 dknwsgvfre aldvyrkfdg entldsagat ifhtlnqfvm lnlwmdefge snlqvfgqsa
      661 erwnsyksil anpksdfwdd lstpdlqetr rdilirsfaq tvrylskefg gspsswkwek
      721 aheitfehpm gkvpflglif nqgpfpvasg eaavnlmnqk einpkmtprv gpskrrivdl
      781 ihpenswsvl ptgnsgnlgs pfygdqiqmf lngehrpirf tqsqiekdsk yvlkfvpr
//
LOCUS       WP_004497687             356 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Leptospira].
ACCESSION   WP_004497687
VERSION     WP_004497687.1
KEYWORDS    RefSeq.
SOURCE      Leptospira
  ORGANISM  Leptospira
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Leptospira"
                     /db_xref="taxon:171"
     Protein         1..356
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=40044
     Region          1..352
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mgievknlvk rfenftaidr lslevpagel vallgpsgsg kttllriiag ledadegqvi
       61 feglevskkn akdrgvgfvf qhyalfrhmt ifeniafgle vrkrserpsk eairnkvmsl
      121 lklvqlenfh nrypselsgg qrqrialara laieprflll depfgaldak vrkelrnwlr
      181 rlhdeihits vfvthdqeea levsdkvvil nsgkieqvgt pdevynhpin sfvfhflgdv
      241 nlfhgrvqgg qtqlgeikvd tpehseiesa savgyvrpyd veilrapiea qtipaeiqyi
      301 hstgrtvkid lkrldtgsil esqlnssefq slnllpgetv hirfkkvkvy vedyti
//
LOCUS       WP_004492522             846 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Leptospira santarosai].
ACCESSION   WP_004492522
VERSION     WP_004492522.1
KEYWORDS    RefSeq.
SOURCE      Leptospira santarosai
  ORGANISM  Leptospira santarosai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 846)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 846)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 846)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..846
                     /organism="Leptospira santarosai"
                     /db_xref="taxon:28183"
     Protein         1..846
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=95846
     Region          20..846
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mknimhtiss fwnrtptwgr rsvvafftlv vlikiifafl ifwkaprlsg eltvpglakp
       61 vsvvrdtygv phiqsedsts ayfalgyvsa sdrlfqmeil rraargelse vlgadlisad
      121 iflrrillrr taekmlkdae kgnpqilkel dsflagvnff leketlpief tilgyqpkpf
      181 drldvlsals llsfsfseal rndslytile rklpnrnvke lfprhdaedp fsirenqpsy
      241 spkrltesek nffpdrtgad rfsaskpetl sglelddfgs virrtnqilg elplflgsns
      301 wvigpsrttt ggavlandph igygnpgtwy evhlktgdye tygyhlpifp fpiiahnakk
      361 awaltmlend dmdfyeeiph ptkpnfvkek gnwvpvqvfk elipvkgeea reitiqvtsh
      421 gpilskpiag ytgpvvslyw vfhhlpapll etiyslgrcs tlqecydvvs llpapglnvs
      481 yadasgniaw wgvgrfpirr nktntrkiln gasgedevig ylpfsqnpkl vnppegiilt
      541 anhlptyelk gygkpegywq esdrgrriye llsqkkewsv ddmkkvqtdi hsfsartmvp
      601 lisleleedr nwtgvfreal dvyrmfdgen tldssgaaif htlnqfvmln lwmdefgesn
      661 lqvfgqtaer wnsyksilvn pksdfwddls tsdlretrrd ilirsfaqtv rylskelggs
      721 psswkwgrvh eitfehpmgk vpllglifnq gpfpvvsges vinlmnqkei npkmtprvgp
      781 skrriidlah penswsvlpt gnsgnigspf ygdqiqmfln gehrairftq sqiekdskyv
      841 lkfvpq
//
LOCUS       WP_004499389             356 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Leptospira
            weilii].
ACCESSION   WP_004499389
VERSION     WP_004499389.1
KEYWORDS    RefSeq.
SOURCE      Leptospira weilii
  ORGANISM  Leptospira weilii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Leptospira weilii"
                     /db_xref="taxon:28184"
     Protein         1..356
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=40030
     Region          1..352
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mgievknlvk rfenftainr lslevpagel vallgpsgsg kttllriiag ledadegqvi
       61 feglevskkn akdrgvgfvf qhyalfrhmt ifeniafgle vrkrserpsk eairdkvmsl
      121 lklvqlenfh nrypselsgg qrqrialara laieprflll depfgaldak vrkelrnwlr
      181 rlhdeihits vfvthdqeea levsdkvvil nsgkieqvgt pdevynhpin sfvfhflgdv
      241 nlfhgrvqgg qtqlgeikvd tpehseiesa savgyvrpyd veilrapiea qtipaeiqyi
      301 hstgrtvkvd lkrldtgsil esqlnssefq slnllpgetv hirfkkvkvy vedyti
//
LOCUS       WP_004494613             245 aa            linear   BCT 20-JAN-2025
DEFINITION  16S rRNA (cytidine(1402)-2'-O)-methyltransferase [Leptospira
            santarosai].
ACCESSION   WP_004494613
VERSION     WP_004494613.1
KEYWORDS    RefSeq.
SOURCE      Leptospira santarosai
  ORGANISM  Leptospira santarosai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Zhao,M., Zhang,H., Liu,G., Wang,L., Wang,J., Gao,Z., Dong,Y.,
            Zhang,L. and Gong,Y.
  TITLE     Structural Insights into the Methylation of C1402 in 16S rRNA by
            Methyltransferase RsmI
  JOURNAL   PLoS One 11 (10), e0163816 (2016)
   PUBMED   27711192
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Kimura,S. and Suzuki,T.
  TITLE     Fine-tuning of the ribosomal decoding center by conserved
            methyl-modifications in the Escherichia coli 16S rRNA
  JOURNAL   Nucleic Acids Res 38 (4), 1341-1352 (2010)
   PUBMED   19965768
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Kozbial,P.Z. and Mushegian,A.R.
  TITLE     Natural history of S-adenosylmethionine-binding proteins
  JOURNAL   BMC Struct Biol 5, 19 (2005)
   PUBMED   16225687
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001055
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Leptospira santarosai"
                     /db_xref="taxon:28183"
     gene            1..245
                     /gene="rsmI"
                     /GO_function="GO:0070677 - rRNA
                     (cytosine-2'-O-)-methyltransferase activity [Evidence
                     IEA]"
     Protein         1..245
                     /product="16S rRNA
                     (cytidine(1402)-2'-O)-methyltransferase"
                     /EC_number="2.1.1.198"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0070677 - rRNA
                     (cytosine-2'-O-)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0000451 - rRNA 2'-O-methylation [Evidence
                     IEA]"
                     /calculated_mol_wt=26879
     Region          9..229
                     /region_name="RsmI"
                     /note="16S rRNA C1402 (ribose-2'-O) methylase RsmI
                     [Translation, ribosomal structure and biogenesis];
                     COG0313"
                     /db_xref="CDD:440082"
ORIGIN      
        1 mkeelqgtlv lvsislgnsd dltararnll eycdvligee vrttstllks fsiskrfllc
       61 nehttpeeir slaqtvmnsg lsvlisdagt pgiedpgkel vgevlrrggk vrsapgpiaf
      121 gaalsisgfk tspftfcgfl srdsserkae lsrylkpght vvfyetpyry ksvlqdlnlv
      181 fkktkderei ffcldltles efqfrgkige llkildtlpk gnpvvvvspr kgksnlkvgl
      241 rgssk
//
LOCUS       WP_004499844             807 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Leptospira weilii].
ACCESSION   WP_004499844
VERSION     WP_004499844.1
KEYWORDS    RefSeq.
SOURCE      Leptospira weilii
  ORGANISM  Leptospira weilii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 807)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..807
                     /organism="Leptospira weilii"
                     /db_xref="taxon:28184"
     Protein         1..807
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=90551
     Region          44..807
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 meqksipslc iflffllswg ifaqseenpt qrpssngees eraaisvigk rkvdlkripg
       61 saiviekefl eqtkpvdsme vlrrvpgasi ryqdtgliln lgfrgvnndl grkvliledg
      121 iftslnpysa peqyytpnid rmerievikg sgailfgpst iggvvnfitk rpskepilsv
      181 saqggsygff ssqvsyggtf gntgidisfl rkqgngfrdh qdfrlhefsf ksitdlnekh
      241 iltskflata qdanmtylgl ttaqfwnhss snfaeqdnrk lqrysgdigh ewkltdhskl
      301 vtkvyaayte rnwarqnylr ntgsnfgaip dnviktydte pfvnrpgdtv ymldsvghrn
      361 rsyrfvgaes ryqqdyqffg iknqldaglr yhyetadiky ldgpptpdya ifgngfdkpp
      421 tgaasseysl sksgnirdhe vnhtksiagf aqnslkfydr fsvipgirye sfsqnrtilr
      481 qqsldpatnq plpnspsqev dkgskhtyhv vipglgltyd lnkdvtwfag ahkgfsppry
      541 qdalnnsgvv nridpeysyn yetgfrgdit nylnaqvsyf dlnyinqiii tsstsgndsa
      601 ssaknggrty srgletnvtf dpaklfeasf klpidliytr adarmnqysv dvakitpnqs
      661 lldfivaqkd kngnyvpyvs rdtvtlalgf ihqkgfysrv eyqyfsaqyh ddsntrtvsw
      721 adlitdplgk kvlqylnits nssgetgvip ayglinfslg ykdpiqrwnl fvtgknladv
      781 ryisgrlpeg iqvgpfrqin vgvtfel
//
LOCUS       WP_004500282             206 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Leptospira weilii].
ACCESSION   WP_004500282
VERSION     WP_004500282.1
KEYWORDS    RefSeq.
SOURCE      Leptospira weilii
  ORGANISM  Leptospira weilii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Leptospira weilii"
                     /db_xref="taxon:28184"
     Protein         1..206
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22579
     Region          73..201
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mtskecsten kevsgkepdr vvrklfrqtl vgiavlvlgv vflarvfpep vlavsgrfid
       61 itgvfgvgig illadslhvf ippdvflmia vagklnsilv ivsasigsli ggtvsyltgr
      121 illpkiegva sfvkrheqkl ehylhrygfw avvlaaltpl pyswvslaag tmkmryllff
      181 qgclfriprf ivfyyliqfg wvgggm
//
LOCUS       WP_004501044             838 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Leptospira weilii].
ACCESSION   WP_004501044
VERSION     WP_004501044.1
KEYWORDS    RefSeq.
SOURCE      Leptospira weilii
  ORGANISM  Leptospira weilii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 838)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 838)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 838)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..838
                     /organism="Leptospira weilii"
                     /db_xref="taxon:28184"
     Protein         1..838
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=95279
     Region          20..838
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkhlsnrlfs fwkklplwtr rsleiifvli ffvklgfvfl ifwkaprlsg eltvpgltkp
       61 vsvvrdsygv phirsedsss ayfalgyvsa sdrlfqmeil rraargelse vlgaelvptd
      121 iflrqvllrr taekmlqesv kgnpqilkel dsfleginyf lkteslpief tilgyqpkpf
      181 drldvlsals llsfsfaeal rndslytile rklpnrniae lfprhdaedp fsirenqpsy
      241 spkrlteark nsfllaekse faksnelsdf asvirrtnqi leelplflgs nswvispsrs
      301 ttggailand phigygnpgt wyevhlmags yetygyhlpi fpfpiiahna kkawaltmle
      361 nddmdfyeev lhptkpnfvk ekgnwvpvqv fkelipvkge eareitiqvt shgpilskpi
      421 agysgpvvsl ywifhhipap vletvyslgr csslqecsev vsklpapgln isyadangni
      481 awwsvgrfpi rknktntrki lngasgeddv igylpfeqnp klinppegii ltanhlptye
      541 lkgygkpegy wqesdrgrri yellsrkknw svddmkkiqt dihsfsarsi vplislelel
      601 dknwsgvfre aldvyrkfdg entldsagat ifhtlnqfvm lnlwmdefge snlqvfgqsa
      661 erwnsyksil anpksdfwdd lstpdlqetr rdilirsfaq tvrylskefg gspsswkwek
      721 aheitfehpm gkvpllglif nqgpfpvvsg eaavnlmnqk einpkmtprv gpskrriidl
      781 ihpenswsvl ptgnsgnlgs pfygdqiqmf lngehrpirf tqsqiekdsk yvlkfvpr
//
LOCUS       WP_004502419             532 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Leptospira weilii].
ACCESSION   WP_004502419
VERSION     WP_004502419.1
KEYWORDS    RefSeq.
SOURCE      Leptospira weilii
  ORGANISM  Leptospira weilii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 532)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Leptospira weilii"
                     /db_xref="taxon:28184"
     Protein         1..532
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=60951
     Region          285..519
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 miseysdlfv enkihssdif syslynfegk elysepsyns llnsdlklkk averfidygn
       61 rhsnisglrk fkndrniqlm vrsendriyk vdfeinpkgs yilvhiestt rnlscsekhr
      121 iqrfrslkhd lvrtlklekt yfylvnieiy nhpslhkyet qiyeavfldl haefltitnn
      181 qnvgfristn qiffayqink pgvdinwips slisymknti qienyefhlk lsiggfhtse
      241 tdtsplnilk glktnlrkvi dspfsryatq nqndssnlia tylslrnsvh kkelllyyqp
      301 ivssetkglh slealsrwnh svkgmispdi fiplaeesgl issigawviq nalldlsqiq
      361 kneslssnsl isinispfql knpefadnli syfsklnllp nsvvlemtes ryeeaaliie
      421 qmailkrfgf qiaiddfgig nsnfsrieki ecdyvkldks lvigvdtnqs krsilkaisq
      481 vllslgkktv fegienaele siaidyganf lqgfhygkpa qitdlssfrf qf
//
LOCUS       WP_004503606             255 aa            linear   BCT 20-JAN-2025
DEFINITION  3-deoxy-manno-octulosonate cytidylyltransferase [Leptospira
            weilii].
ACCESSION   WP_004503606
VERSION     WP_004503606.1
KEYWORDS    RefSeq.
SOURCE      Leptospira weilii
  ORGANISM  Leptospira weilii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 255)
  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 255)
  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 10118537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Leptospira weilii"
                     /db_xref="taxon:28184"
     Protein         1..255
                     /product="3-deoxy-manno-octulosonate cytidylyltransferase"
                     /EC_number="2.7.7.38"
                     /GO_function="GO:0008690 - 3-deoxy-manno-octulosonate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0033468 -
                     CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29172
     Region          2..243
                     /region_name="CMP-KDO-Synthetase"
                     /note="CMP-KDO synthetase catalyzes the activation of KDO
                     which is an essential component of the lipopolysaccharide;
                     cd02517"
                     /db_xref="CDD:133010"
     Site            order(8..10,49,76,101,103)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133010"
     Site            order(126,143,149..151,157..158,160..166,176,201..202,
                     205..207,214..217)
                     /site_type="active"
                     /note="oligomer interface [active]"
                     /db_xref="CDD:133010"
ORIGIN      
        1 mrtigivpar maasrfpgkp mfpilgkpmi ehvfnrakly qgwdeliiat cdeeisnfak
       61 sknfpvvmtg shhiraldrv aeagtmftqk lvdddivvcv qgdepmlapd mmeaviaplk
      121 mdesipatvl amhiveeeiw rnpdtvkiih nekgevlyts rmalpyckgk fspelgarri
      181 ygifafrwky lqeftkhpet rlekleacds nrildmsftq yiapypyvks ysvdspsdiv
      241 lvenhmkhdk yfqmy
//
LOCUS       WP_004504264             807 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Leptospira weilii].
ACCESSION   WP_004504264
VERSION     WP_004504264.1
KEYWORDS    RefSeq.
SOURCE      Leptospira weilii
  ORGANISM  Leptospira weilii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 807)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..807
                     /organism="Leptospira weilii"
                     /db_xref="taxon:28184"
     Protein         1..807
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=90581
     Region          44..807
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 meqksipslc iflffllswg ifaqseenpt qrpssngees eraaisvigk rkvdlkripg
       61 saiviekefl eqtkpvdsme vlrrvpgasi ryqdtgliln lgfrgvnndl grkvliledg
      121 iftslnpysa peqyytpnid rmerievikg sgailfgpst iggvvnfitk rpskepilsv
      181 saqggsygff ssqvsyggtf gntgidisfl rkqgngfrdh qdfrlhefsf ksitdlnekh
      241 iltskflata qdanmtylgl ttaqfwnhss snfaeqdnrk lqrysgdigh ewkltdhskl
      301 vtkvyaayte rnwarqnylr ntgpnfgaip gnviktydte pfvnrpgdtv ymldsvghrn
      361 rsyrfvgaes ryqqdyqffg iknqldaglr yhyetadiky ldgpptpdya ifgngfdkpp
      421 tgaasseysl sksgnirdhe vnhtksiagf aqnslkfydr fsvipgirye sfsqnrtilr
      481 qqsldpatnq plpnspsqev dkgskhtyhv vipglgltyd lnkdvtwfag ahkgfsppry
      541 qdalnnsgvv nridpeysyn yetgfrgdit nylnaqvsyf dlnyinqiii tsstsgndsa
      601 ssaknggrty srgletnvtf dpaklfeasf klpidliytr adarmnqysi daskitpnqs
      661 lldfivaqkd kngnyvpyvs rdtvtlalgf ihqkgfysrv eyqyfsaqyh ddsntrtvyw
      721 adlitdplgk kvlqylnits nssgetgvip ayglinfslg ykdpiqrwnl fvtgknladv
      781 ryisgrlpeg iqvgpfrqin vgvtfel
//
LOCUS       WP_004508668             129 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Leptospira weilii].
ACCESSION   WP_004508668
VERSION     WP_004508668.1
KEYWORDS    RefSeq.
SOURCE      Leptospira weilii
  ORGANISM  Leptospira weilii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 129)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Leptospira weilii"
                     /db_xref="taxon:28184"
     Protein         1..129
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=14413
     Region          4..128
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(7..10,41..43,46,70,110,124)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 misifcdgas kgnpgpssig ivaykgdkee friserigea tnnvaewasl kkgleecirr
       61 kfdtihaymd selvvrqvsg kykvkhpnll eykkevdklv sslqnfqith vpreknsvad
      121 klaneafqk
//
LOCUS       WP_004509153             184 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Aliarcobacter butzleri].
ACCESSION   WP_004509153
VERSION     WP_004509153.1
KEYWORDS    RefSeq.
SOURCE      Aliarcobacter butzleri (Arcobacter butzleri)
  ORGANISM  Aliarcobacter butzleri
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Arcobacteraceae; Aliarcobacter.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Aliarcobacter butzleri"
                     /db_xref="taxon:28197"
     Protein         1..184
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20485
     Region          1..184
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mkitvaisga sgvslalnfi kqipkdfevf vvfsksskra lklennistk elfkdeknit
       61 ifkdsdigas iasgsfkvdk miilpcsqnt lakcavgiad slitraftvm lkekreivia
      121 prempfntis lknmlilskl gvtiappilg yysnqqsled menfligkwf dllkidntly
      181 krwk
//
LOCUS       WP_004509520             162 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Aliarcobacter butzleri].
ACCESSION   WP_004509520
VERSION     WP_004509520.1
KEYWORDS    RefSeq.
SOURCE      Aliarcobacter butzleri (Arcobacter butzleri)
  ORGANISM  Aliarcobacter butzleri
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Arcobacteraceae; Aliarcobacter.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 162)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Aliarcobacter butzleri"
                     /db_xref="taxon:28197"
     Protein         1..162
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=18742
     Region          <2..162
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mpfefslnis ykdiiepdfl efiksmlnkh kitnrvvfei ledesiknyd llinfieeik
       61 tlgckvaidd fgtgysnfeh llkmnvnylk idasliknit kdensrkitk tivefaksln
      121 lktiaefven keifdmakdl gvdysqgyyf sapiekpnin ef
//
LOCUS       WP_004509685             771 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Aliarcobacter butzleri].
ACCESSION   WP_004509685
VERSION     WP_004509685.1
KEYWORDS    RefSeq.
SOURCE      Aliarcobacter butzleri (Arcobacter butzleri)
  ORGANISM  Aliarcobacter butzleri
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Arcobacteraceae; Aliarcobacter.
REFERENCE   1  (residues 1 to 771)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 771)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 771)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..771
                     /organism="Aliarcobacter butzleri"
                     /db_xref="taxon:28197"
     Protein         1..771
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86541
     Region          46..95
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          79..771
                     /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 msllkkslia pslaillatn lysanytvdt tnatkaieki selsnipfiv dtnilngknt
       61 nkihnvqnld ealklmfegt gleavvknnt ivikkiegkg tvlepisvne sykngtaeng
      121 ylseditgvg lwgkrslqdt pysmtvipkd lientqandm aqifkmnplt qdggdqmsgn
      181 yynvirgfss nnaivngipl adwysfttme dlervetisg atgflygggr vggavnyvtk
      241 kptledkrsi tlgnyggeqy ythidlsgqi dekkvfgyri nalyqdgdsv anvgkeqkfv
      301 slafdykptd nftmdlnyah reldrknqkp ffnigantfr pildiskgyt snlnsieekn
      361 drvttslkwn lndiftlrss flyeetdrev vgetliytrn dglydallyr ypkggqghks
      421 yagnlyldsk fetfnidhll tigysqnyqn ykrdknwwqp rywldgvnle qikntviprn
      481 pnehggripf skteykntli gddivfndqw salvgfnyat venwsswggs ydkseltptl
      541 slmykpfedl ttyvtymesl etgeivadty snageildpl vskqyeigak yslnesillt
      601 salfriekan qysnnetpmp kyvqdgeqvh qgieltftgk vtddltlfgg gtlmdlsiek
      661 sndkslegkk ptnaatkmak lyaeynipqi sgltltggay ytgekygddl ntdkipsytl
      721 ydaglryktk ldkypttfll nvanltgkdy wasssylgdp rsvafsmkme f
//
LOCUS       WP_004509986             348 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Aliarcobacter butzleri].
ACCESSION   WP_004509986
VERSION     WP_004509986.1
KEYWORDS    RefSeq.
SOURCE      Aliarcobacter butzleri (Arcobacter butzleri)
  ORGANISM  Aliarcobacter butzleri
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Arcobacteraceae; Aliarcobacter.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Aliarcobacter butzleri"
                     /db_xref="taxon:28197"
     Protein         1..348
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39068
     Region          1..342
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mkievknltk nfgnfvalen inldivdgel lallgpsgsg kttllrmiag letvddkdsg
       61 kilfngvnva kkdigerdig fvfqhyalfr hmtvfeniaf glrvkpkkqr lsnkeieekv
      121 nkllkliqld gfasrfpwql sggqrqrval aralavepkv llldepfgal dakvrtdlrr
      181 wlkelqeelg ittilvthdq eealevanri vviskgkieq vgtpeevfhn pknefvinfl
      241 gnvnlfhgrv ddgklnleds sdnkylirph eleiisvndk eailqakvky iqlagsfvki
      301 dlshlndetk tlmveishse fkekniqkgd ivgirprtlr tfedgagi
//
LOCUS       WP_004510562             404 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Aliarcobacter butzleri].
ACCESSION   WP_004510562
VERSION     WP_004510562.1
KEYWORDS    RefSeq.
SOURCE      Aliarcobacter butzleri (Arcobacter butzleri)
  ORGANISM  Aliarcobacter butzleri
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Arcobacteraceae; Aliarcobacter.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Aliarcobacter butzleri"
                     /db_xref="taxon:28197"
     Protein         1..404
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43452
     Region          1..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mlvfvlnags sslkyqlmnp vikkvlasgl cerigidgvl kheygengqk ltlnvpmpth
       61 keaieavltt ltagegkvin sindidaigh rtvhggeefs gsvmitpevi dtmkklspla
      121 plhnpanilg ieicqqlmpg kpnvgvfdta fhqtmpdyay myalpyemyt khgirkygfh
      181 gtshffvsne argmldkkhn triivchlgn gssvsavlng rcidtsmglt piqglmmgtr
      241 sgdvgagalq ymmsqenlti dqaidimnkk sgilgisgks sdlrevlqgm qdgdercrla
      301 vdmvaynikk yvgsyvaald gidalcftgg igenaalire kvcagldsmg lvidpvknnk
      361 rsnvardiat ngsasrifvi ptneeyvian dtykivsgqa stcq
//
LOCUS       WP_004510564             396 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Aliarcobacter butzleri].
ACCESSION   WP_004510564
VERSION     WP_004510564.1
KEYWORDS    RefSeq.
SOURCE      Aliarcobacter butzleri (Arcobacter butzleri)
  ORGANISM  Aliarcobacter butzleri
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Arcobacteraceae; Aliarcobacter.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Aliarcobacter butzleri"
                     /db_xref="taxon:28197"
     Protein         1..396
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43600
     Region          1..395
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mlvfvlnags sslkyqlina kthelkasgl verigidgil kheigenkkl tfetpipthk
       61 eaielvlril tndetkvins ideiqaighr vvhggehfkg svivnddvlk kieeliplap
      121 lhnpanilgi kicmqilpkv pnvttfdtaf hqtmpienfl yavpysdyte hhlrkygfhg
      181 tshyyvsnea vkilnkkdsk iivchlgngs svcavrdgks istsmgltpl eglvmgtrsg
      241 didagvipyl mekkglshtq iidylnkksg ilgvsgissd lrevikaand gdkrskiaii
      301 mlcdrikkyl csyaglmhgv daicftagig ensdlirekv ceglqfmgie idteknkvre
      361 kgireintka sktkifvipt neelviaqdt fnlvkk
//
LOCUS       WP_004511869             293 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Geobacter metallireducens].
ACCESSION   WP_004511869
VERSION     WP_004511869.1
KEYWORDS    RefSeq.
SOURCE      Geobacter metallireducens
  ORGANISM  Geobacter metallireducens
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Geobacterales; Geobacteraceae; Geobacter.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Geobacter metallireducens"
                     /db_xref="taxon:28232"
     Protein         1..293
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32173
     Region          2..258
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mmstidlhvh snysdgihpp adlvkmaaer glvaiaiadh dtvdgideal iagarlgvev
       61 vpavelsaeh gryrdmhilg yhldhrdprl vdmlaefrin reirgraivd kinqrladgr
      121 kpllsydevl nlaegavgrp higrmlierg yarnmedafr rylipcnvpk ryipagdait
      181 eirraggvav lahpitvsdd rqvlrgivse lvalgldgie vfnnmcykdd mlfleflcre
      241 sgllmtggsd fhgfeddvei gsgrgglavs hrlaeavknl aesrritppg srt
//
LOCUS       WP_004511941             343 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Geobacter].
ACCESSION   WP_004511941
VERSION     WP_004511941.1
KEYWORDS    RefSeq.
SOURCE      Geobacter
  ORGANISM  Geobacter
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Geobacterales; Geobacteraceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Geobacter"
                     /db_xref="taxon:28231"
     Protein         1..343
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37974
     Region          1..338
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msieivsvnk afgsftalnd vnltvpsgel tallgpsgsg kttllriiag letpdagsir
       61 fdgeettdrh vrerqvgfvf qhyalfrhmt vaenvafglt vkprkerpsk keirervfel
      121 lrlvqlegla drypsqlsgg qrqrvalara lavepkvlll depfgaldak vrvelrrwlr
      181 rlhdeihvts vfvthdqeea levadrivvm nkgrieqvgt paevydqpan pfvfdflgsv
      241 nlfhcraeqg qaraaapels vgyvrshdie vertptvaav eaevrhvqav gpavrvellv
      301 rgtgktveae lsrdgaerla lgigetvyar prkmqrfvgd yqi
//
LOCUS       WP_004511966             192 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Geobacter metallireducens].
ACCESSION   WP_004511966
VERSION     WP_004511966.1
KEYWORDS    RefSeq.
SOURCE      Geobacter metallireducens
  ORGANISM  Geobacter metallireducens
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Geobacterales; Geobacteraceae; Geobacter.
REFERENCE   1  (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   2  (residues 1 to 192)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Geobacter metallireducens"
                     /db_xref="taxon:28232"
     Protein         1..192
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=20988
     Region          116..186
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mrerahlial wtlavlastv lvtkgrglpl teggstafll drsngvrvkv tgiqgksgvy
       61 clpedavlks viimayrglt anaskssdfa trlkdgdwvm ferdasepvk islktmpate
      121 rillgipldp atmtesewel lpgigptlar rivfdrqyng gfrsirdler vsgigkvtvd
      181 kleryfpntv th
//
LOCUS       WP_004512316             147 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Geobacter metallireducens].
ACCESSION   WP_004512316
VERSION     WP_004512316.1
KEYWORDS    RefSeq.
SOURCE      Geobacter metallireducens
  ORGANISM  Geobacter metallireducens
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Geobacterales; Geobacteraceae; Geobacter.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Geobacter metallireducens"
                     /db_xref="taxon:28232"
     Protein         1..147
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16127
     Region          5..147
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 meqlltthsl palfglsfla stlvpigsew llvtlllkhh dpalavgvat vgnwlgactt
       61 yaigmwggpf lvrrvlride aterradrly grygswsllf swlpvigdpl clvggilrvr
      121 firfsllvgs gklaryafia witvrgm
//
LOCUS       WP_004512396              89 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Geobacter metallireducens].
ACCESSION   WP_004512396
VERSION     WP_004512396.1
KEYWORDS    RefSeq.
SOURCE      Geobacter metallireducens
  ORGANISM  Geobacter metallireducens
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Geobacterales; Geobacteraceae; Geobacter.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Geobacter metallireducens"
                     /db_xref="taxon:28232"
     Protein         1..89
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10098
     Region          9..88
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mairqeqyek ikelaqsyga triilfrsav dnpeaardid iacdgvrgwk lyelaarlee
       61 elhtpfdvvp ltpptrftel vekrgrvll
//
LOCUS       WP_004512734             404 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Geobacter metallireducens].
ACCESSION   WP_004512734
VERSION     WP_004512734.1
KEYWORDS    RefSeq.
SOURCE      Geobacter metallireducens
  ORGANISM  Geobacter metallireducens
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Geobacterales; Geobacteraceae; Geobacter.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Geobacter metallireducens"
                     /db_xref="taxon:28232"
     Protein         1..404
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43870
     Region          1..400
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 miililncrg fsihfqlfdw strtilargd vdrielgdsf ivmevpgrdp yhldsdcssf
       61 gaavalilst lthplegpld rveqiaavgh rvahggerft ssvtineeii aavrgfeela
      121 plhipanlag iegamatlpr tphvavfdsa fhqtmplhay iyplpwewye khgvrrygfh
      181 gaphcyaaqr gaallgrdpa acnlvtvhig ngtslcaveg grsidtsmgl tplegtmmgt
      241 rcgsidpgip pfmmqeeqla prdmdrilnq rsgaagitgl kldraaflar aaegnercll
      301 alemeayrlk khiggyaaal grldavvfst asgegewlvr ektladmeif girldrernr
      361 aarsvereer isaddspvav yvvhteeemv yaeevaalln gagg
//
LOCUS       WP_004513730             167 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Geobacter metallireducens].
ACCESSION   WP_004513730
VERSION     WP_004513730.1
KEYWORDS    RefSeq.
SOURCE      Geobacter metallireducens
  ORGANISM  Geobacter metallireducens
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Geobacterales; Geobacteraceae; Geobacter.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Geobacter metallireducens"
                     /db_xref="taxon:28232"
     Protein         1..167
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18370
     Region          3..163
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mevleaiygr rsvrqytsep vtreevleiv qagswapsgl nnqpwrfaiv sddekrrala
       61 gftkyrhile gapvsiavfc draamyndtk dhqsvgaclq nmllaahalg lgavwlgeil
      121 ksadkvrell alpeslelma vvavgrpaef trtgdrkdld elivgey
//
LOCUS       WP_004498318             129 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ribonuclease HI family protein [Leptospira].
ACCESSION   WP_004498318
VERSION     WP_004498318.1
KEYWORDS    RefSeq.
SOURCE      Leptospira
  ORGANISM  Leptospira
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 129)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Leptospira"
                     /db_xref="taxon:171"
     Protein         1..129
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=14500
     Region          4..128
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(7..10,41..43,46,70,110,124)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 misifcdgas kgnpgpssig ivaykddkee friseriget tnnvaewasl kkgleecirr
       61 kfdtihvymd selvvrqvgg kykvkhpnll eykkevdklv sslqnfqith vpreknsvad
      121 klaneafqk
//
LOCUS       WP_004514067             520 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Geobacter metallireducens].
ACCESSION   WP_004514067
VERSION     WP_004514067.1
KEYWORDS    RefSeq.
SOURCE      Geobacter metallireducens
  ORGANISM  Geobacter metallireducens
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Geobacterales; Geobacteraceae; Geobacter.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Geobacter metallireducens"
                     /db_xref="taxon:28232"
     Protein         1..520
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=58137
     Region          3..427
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mpfldwvnkt qavsstadvp yhllqfrtah gdagadnlli qgdnlkalka llpfyrgrvk
       61 ciyidppynt qsafahyddk lehsqwlsmm yprlvllrel lkedgslwis cddneahyik
      121 vivdeifgrl nfiidvswqk rdgppndrki gaihehilvw gkgksgnskk tlaeeafnlm
      181 prtekansqy dvfkepdgpd ergpfrkidt tangkggrfv tslfypiknp ytaeevwprq
      241 gtcwrhskee merlqaekrl ywgvngtakt pmrklfldea kqgmttpsiw sdtglnqhas
      301 seieklfgek aafetpkpea llqriihiat npgdlvldsf lgsgttaava hkmgrrwigi
      361 emgehavthc lprlekvigg epggiskavd wqggggfrfh slgepvfdad ggihpavrfp
      421 alaaylwhfe tgeparqtft tpllgthggt awyllyngil gdrrpqggnv ltsavlahld
      481 eayphhgprv iygettrlge arlreagitf kqipydikar
//
LOCUS       WP_004519697             140 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Neisseria].
ACCESSION   WP_004519697
VERSION     WP_004519697.1
KEYWORDS    RefSeq.
SOURCE      Neisseria
  ORGANISM  Neisseria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Neisseria"
                     /db_xref="taxon:482"
     Protein         1..140
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15842
     Region          1..124
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkhqqgftli ellivvliaa ilatiaypsy qnyirqtrla svrtqmlhna qqleryytqk
       61 stfvgfpten lqqnqyfnis fsegtdsmpd psdsgyilka vpnretnade tctvyyndsg
      121 iiwansdkqn cpgyeipkse
//
LOCUS       WP_004520647             137 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Neisseria].
ACCESSION   WP_004520647
VERSION     WP_004520647.1
KEYWORDS    RefSeq.
SOURCE      Neisseria
  ORGANISM  Neisseria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Neisseria"
                     /db_xref="taxon:482"
     Protein         1..137
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14821
     Region          3..135
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mpplyaylal iasaftsatl lpgtseaaya afvyqypqha lgaclcagla nglgsmvsyy
       61 mgrmfpakkr psekvlariq rwgiwpllfa wlpiigdalp latgwlrlna lhcaiiliag
      121 kllryamiyw gmnivag
//
LOCUS       WP_004520655             264 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Neisseria].
ACCESSION   WP_004520655
VERSION     WP_004520655.1
KEYWORDS    RefSeq.
SOURCE      Neisseria
  ORGANISM  Neisseria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Neisseria"
                     /db_xref="taxon:482"
     Protein         1..264
                     /product="formate/nitrite transporter family protein"
                     /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=28397
     Region          8..256
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mdtrdlfphe ilqdaigksc aksefsikml vilsflgggy vgfgylaclr visgipaewn
       61 glaallgasv fpialicili gggelatgnm mimalgrltg rvstyklvrn wlivslgnla
      121 gavamayflg hyvglaegpa aaktiaiaea kvnmdfgraf vsaiacnwmv cmgiwfyfga
      181 rhtsgrilam wfpvmifvli gfqhfvanmf iipagiwaga nvswgqffyn mipvflgnvl
      241 ggssfvaasy lfaykhllkd dfsi
//
LOCUS       WP_004521045             132 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein, partial [Neisseria subflava].
ACCESSION   WP_004521045
VERSION     WP_004521045.1
KEYWORDS    RefSeq.
SOURCE      Neisseria subflava
  ORGANISM  Neisseria subflava
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Neisseria subflava"
                     /db_xref="taxon:28449"
     Protein         <1..132
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
     Region          <1..83
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 ilataaftvy resvrsanlr aahaallena rfmeqfyakk gsfkltstkw pelpvkeagg
       61 fcirmsgqak gilegkftlk avaldreaep rvlrlneslt avvcgkmkgk gsctdgeeif
      121 rgndaecrpf tg
//
LOCUS       WP_004522740             796 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Burkholderia pseudomallei].
ACCESSION   WP_004522740
VERSION     WP_004522740.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 796)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..796
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=85566
     Region          37..795
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mastrnrtrr hlkilsglil ccallalvla aaylraslpq ldgelrapvl gapmtaerda
       61 lgvptitard rfdaaygigy lhaqdrffqm dmlrrsgage lselfgpial gvdrdhrlyr
      121 fralaaaava hlppddlrll qrytqgvndg laalrarpfe yallrmqpqr wrpedsllvi
      181 wamyfdlqgr lasrefarhw lqahstpeql afllppssrf dapldvpgia aaaapvsata
      241 pawlrdarpa tsvngvsidg qsavgsnnwa lagsrtasga aivgddmhls fglpniwyra
      301 mfklgggagl aarvvgvtlp glpavvvgsn griawgftng yadclellpl erdardpsrf
      361 rlggawqrar etvetirvhg aapveltvld ttagpvreig gkayaahwia qasgaanlaf
      421 akmieatgve eaigiaagag lpaqnvvigd stgrigwtva galpdrrapg eagargdgap
      481 swraalppda hprivdpagg qlwtannrql agdayrligd ggadlgarar qlrdgltale
      541 rpderaayrl dlddralfms lwrdralrvl deaalaghpa raefrrllvs gwtgrasvds
      601 vgytlargyl yrlydvlfgs ldarlkqqqh dadyalanrr wpvviarlld eqppgwlpad
      661 aaswrdvqla aidrtidals angapladaa wgrrntlria hpfarsvplv grwltapadp
      721 vpgdanmprv aaprfgqser lvvspgrees glfnmpggqs ghplspffla gheawvkgep
      781 lpllpgpteh tlrfvr
//
LOCUS       WP_004526573             340 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia pseudomallei].
ACCESSION   WP_004526573
VERSION     WP_004526573.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 340)
  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 340)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 340)
  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   4  (residues 1 to 340)
  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 340)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..340
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37293
     Region          28..212
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          255..337
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtaklahwdf vrpvattrvl vdvgveqgla vgqclggsgv cadlldkpda tvaavqelri
       61 vrnlmrllgp dfplgieigr ryhataygvw gfalmssatf gdavsvglry lqltstfcei
      121 rptlrgddat lviddrdlpg dvrdvlveit vaalitlqfd ldaanlpvkr lalkmkppsy
      181 agrfrtlfda tpefgaahna ltvdarcldl klpqrnaltr rrcedecrrv lerhrrsegw
      241 agrvrrqlag dpargptmdv laaelgvspr tlrrrlaneg tdyetvadel rqalaealla
      301 tttltlaevs erlgysepsa farafrrwkg mspseyrcaa
//
LOCUS       WP_004527950             325 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia pseudomallei].
ACCESSION   WP_004527950
VERSION     WP_004527950.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 325)
  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 325)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 325)
  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   4  (residues 1 to 325)
  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 325)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..325
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35639
     Region          50..202
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          230..309
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mdqrhtrles aahapprpda qtlapreaar relaalierf apadgahpsa ipalsffrcs
       61 spvdlgcsvt raafvfaaqg akrvtvagqa yeydhqqclv tsvdlpmlsq vtrasagapy
      121 lcvkialdvq riaelsaemr mpppeavptg egivvgalse plfdaalrlv rlldtpadip
      181 ilapliekel lyrlltsglg arlrhiavag sqtyriarai ewlrhhytep lrvetlaqqv
      241 nmsvsslhhh fkhvttlspl qyqkqlrlhe arrlllgqhg dvgsvalrvg ydspsqfsre
      301 ysrlfgappl rdvvqrrrng tgvqe
//
LOCUS       WP_004528047             311 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Burkholderia
            pseudomallei].
ACCESSION   WP_004528047
VERSION     WP_004528047.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..311
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32897
     Region          26..273
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 messnrpart heasaatllv dcrnalgega twcdaahaly wvdiegarlw rwraagahgg
       61 ercdswempe riaccaltgd pdvllvglas rlaffdtrrr altpivdvep drptrlndgr
      121 cdragafvfg tkdesggasp raiggyyrln adlslqrlal ppaaiangia fspdgsamyf
      181 cdsptreiqv cdyrpggdvd rvrsfvrlad ahgepdgstv dasggvwnaq wggarvvryd
      241 aqgvetdria vptpqpscvt ldaagrlyvt sarvglddga lagnsgaggv fvahtrdpgg
      301 atprfalarh a
//
LOCUS       WP_004511713             811 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Geobacter metallireducens].
ACCESSION   WP_004511713
VERSION     WP_004511713.1
KEYWORDS    RefSeq.
SOURCE      Geobacter metallireducens
  ORGANISM  Geobacter metallireducens
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Geobacterales; Geobacteraceae; Geobacter.
REFERENCE   1  (residues 1 to 811)
  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 811)
  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 811)
  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   4  (residues 1 to 811)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..811
                     /organism="Geobacter metallireducens"
                     /db_xref="taxon:28232"
     Protein         1..811
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=90608
     Region          8..805
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mplpsqrkll peqlrwtcdp gqfdftttdd lpelegtlgq aralasidfg ldiresgfnl
       61 fltgeagtgr tstiknilkk kaktepipsd wvyvnnfksp dlpialalpa gkgtelsldm
      121 delittvrsi ipkaldskey ennkativea yqeknnelfg qleaeaqekg falqrtvsgl
      181 vmvpqkeern ytqeeyeals dqekgkleeg gqelteklnd vlrqvrdnek qtkeslaqld
      241 rdlgnasvgh hidplrekyg espkvleyln tvqediianl edfkpqqqvq spipglklpr
      301 qepsferyqv nvfvdnhdae gapvvfepnp tysnlfgrte himqmggtat tnftmikpga
      361 lhransgyli vdarevlvnp yswdalkrci rsaeikfedp leqyrfitiv smkpeaiplq
      421 akiimigspw iyyllyhlep dyrkffkvkv dfdsriartp evlkdyalfv sthcknekll
      481 pfdrsgvagl ieysarlved qeklssqfme iadlireasy wagkdgggpv thahvanaie
      541 qkvyrsnrie ermqelfddg tilvdvdgam pgqinglsvi slgdhtfgrp srvtarvylg
      601 ragmvniere vklsgpihdk gvliltgylg gkfahdkpls fsasicfeqn yegvegdsas
      661 stelycllsa fsgvpirqgi avtgsvnqhg miqpiggvnf kiegfyavck akgltgeqgv
      721 iipksnerhl mlndevvqav rdgkfhiwsv etidqgiell tgvaagerqe dgtypeesin
      781 hlvdkrlrem iesmkmfgas dkdekkqege k
//
LOCUS       WP_004528280             881 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia pseudomallei].
ACCESSION   WP_004528280
VERSION     WP_004528280.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 881)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 881)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 881)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..881
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..881
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=94425
     Region          129..179
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          158..881
                     /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 mdsicnrrpr rahagvcadt anapaglpea aqpaarlgag rprdaaaprc arqatshtsh
       61 ashtlhapcm pqfaprrvva rvaaaalfsa caapgvsgaa epaaatrgyd ipagpldaal
      121 trfxreagil lsfpgelttg lrspglhgra dpaaaldrll tgtglvalrq psggytlarl
      181 pgpaaagada alaadttlpt vavrasgpha dsyrppreaa glrsdaplae vpqavaivaq
      241 qvlrdqrprn lddalanvsg itqgntlgst qdtvmkrgfg dnrdgsvmrn gmpivqgrsl
      301 nattdsvevl kgpasllygi mdpggvinvv tkqpqlarrh aisalgstyg ggrnggeltf
      361 dstgaigesr vayrlivdqt neqywrnyge hretlvapsl awygrdtqmv lsyeyrrflm
      421 pfdrgtaldp rtnaplaipa rrrldepfnd mrgesnlaql aidhqlapdw kvhvgysynr
      481 etydanqiri tavdplkgtl trsndathgs rstdsygiay vdgrvtlagm rhdvqfgvdg
      541 eyrqvyradm lrqpiktpfs ylnptyglvp pstsvsasds dqsdtlhtas lffqdsihls
      601 erwmlvggar wvrysqlagr grpfqvntnl sgtkwlprag ivykwndals lygsytqslk
      661 ptskiapmag gyvidgstap eegaswelga kldmpgglag tlaffdidkk hvlvsqydda
      721 tnqtawrtsg rarsrgield vsgrigarwn viasyayida kttedplyag nrlwnvarht
      781 aslaavydvg tvlggddlri gaagryvgar pgdsansftl payatadafa tydtrlgkqk
      841 lqfqlnvknl fnrtyypssv nrffvsvgda rqvsllttlq f
//
LOCUS       WP_004530299             255 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Burkholderia].
ACCESSION   WP_004530299
VERSION     WP_004530299.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 255)
  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 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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (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   5  (residues 1 to 255)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..255
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27704
     Region          18..251
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <154..251
                     /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 mtrlaapsls lrrygavqas dvhdfhqivl gvdgamtmtv dgvderidrr cawlipagar
       61 hdyagladns qlvldlppgs lavperlfer artmaidpgl ttlvgelasr iargpladaa
      121 sarrlhwqaa arlcgalvge ldgapsqpav gldfaridgw lrahlaqplr iadlaahcgf
      181 gmrrfhqlfc eafgetphry lqrlrldaav mllgdpkrsl tdiasevgfa dqsafthaft
      241 krfglapgrw rsdrh
//
LOCUS       WP_004530696             163 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Burkholderia pseudomallei].
ACCESSION   WP_004530696
VERSION     WP_004530696.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..163
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=17348
     Region          24..103
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mntpqqgttr iigkgrasaa gpgpdvmaas tldgdkvytt dgddvgkike imldvrtgrv
       61 ayavlssggl lgigdkllai pwsaltldtd rkcflvtvss eriknapgfd kshwptmadp
      121 nwaaslhqyy gsapywsdve eelgidapph easpdrperg grh
//
LOCUS       WP_004531039             314 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Burkholderia].
ACCESSION   WP_004531039
VERSION     WP_004531039.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 314)
  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 314)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 314)
  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   4  (residues 1 to 314)
  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 314)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..314
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_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          35..186
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          214..295
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msfeplfadg garlqrrila lfgqlapneg ythaaidgvr firsnrpvpr mpvlydpsiv
       61 vvcqgrkrgy vgersfvyda qqylvlsvpl pfecetfatp depflaisir idlaviaela
      121 illdethgas vseprgiyst pldapladav lrllealasp adtrvlgpai mreigyrvlt
      181 gaqgdairaa laqqhhfgrv aralrrihad lsgeldvetl aseagmslav fhaqfksvta
      241 tspmqyvkat rlhharlmmv qdglnagaaa arvgyasasq fsrefkrlfg rspsdevrwv
      301 qaggrqpval eage
//
LOCUS       WP_004531297             790 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Burkholderia pseudomallei].
ACCESSION   WP_004531297
VERSION     WP_004531297.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 790)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 790)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 790)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..790
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=84688
     Region          33..790
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 masrtnrlpr wlkilpgvil lgallvaaga alflraslpr ldgdvraptl ggpmtierda
       61 agvptvaard rfdaaygigy lhaqdrffqm dylrrtgage laellgpaal dfdrehrlfr
      121 fraraaaafa qlppderrll erytqgvndg laalrarpfe yallgeppar wrpedsllvi
      181 wamyfqvqgt lasrdiarnw ltahatqqqr afllpsssgf dapldaprid eapaplpdaa
      241 pdwfraagdg aakrasldfr ssvgsnnwai agsrsargaa ivgddmhlvl glpntwyraa
      301 ftypggaapv rravgvtlag lpaivagsng hvawgltvgy adcldlvple rdgddsrafr
      361 msgarqiarr yvesirvrgg asvsltvlet tvgpvreigg rpyavhwvaq spgavnlgla
      421 rladavdvdg amrvantlgi paenivvgdr agrigwtiag alpdrraprg gegaawrsll
      481 ppdayprvvd psggqlwtan srqlaggayr ligdggtdlg aratqlrdgl talgrtdeqa
      541 ayrialddra lfiaqwrdra lrvlddaala ghpsraefrr llehgwtgra svdsvgytla
      601 rgflyrlydv tfdglnarlk qvdagadyel anlrwpavva rlldaqppgw lpagasswrd
      661 vqliaidrti aaltadgapl araswgarnt lriahpfags lpllggwlta paaqmpgdsh
      721 mprvaapdfg qsermvvspg heefgifnmp ggqsghplsp fflaghdawv raeptpflpg
      781 varhtlrfap
//
LOCUS       WP_004531788             901 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia pseudomallei].
ACCESSION   WP_004531788
VERSION     WP_004531788.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 901)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 901)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 901)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..901
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..901
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=96492
     Region          149..199
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          178..901
                     /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 mgnegcippi vnessimdsi cnrrprraha gvcadtahap aglpeaaqpa arlgagrprd
       61 aaaprcarqa tshtshasht lhapcmpqfa pqfaprrvva rvaaaalfsa caapgvsgaa
      121 epaaatrgyd ipagpldaal trfgreagil lsfpgelttg lrspglhgra dpaaaldrll
      181 tgtglvalrq psggytlarl pgpaaagada alaadttlpt vavrasgpha dsyrppreaa
      241 glrsdaplae vpqavaivaq qvlrdqrprn lddalanvsg itqgntlgst qdtvmkrgfg
      301 dnrdgsvmrn gmpivqgrsl nattdsvevl kgpasllygi mdpggvinvv tkqpqlagrh
      361 aisalgstyg ggrnggeltf dstgaigesr vayrlivdqt neqywrnyge hretlvapsl
      421 awygrdtqmv lsyeyrrflm pfdrgtaldp rtnaplaipa rrrldepfnd mrgesnlaql
      481 aidhqlapdw kvhvgysynr etydanqiri tavdplkgtl trsndathgs rstdsygiay
      541 vdgrvtlagm rhdvqfgvdg eyrqvyradm lrqpiktpfs ylnptyglvp pstsvsasds
      601 dqsdtlhtas lffqdsihls erwmlvggar wvrysqlagr grpfqvntnl sgtkwlprag
      661 ivykwndals lygsytqslk ptskiapmag gyvidgstap eegaswelga kldmpgglag
      721 tlaffdidkk hvlvsqydda tnqtawrtsg rarsrgield vsgrigarwn viasyayida
      781 kttedplyag nrlwnvarht aslaavydvg tvlggddlri gaagryvgar pgdsansftl
      841 payatadafa tydtrlgkqk lqfqlnvknl fnrtyypssv nrffvsvgda rqvsllttlq
      901 f
//
LOCUS       WP_004533413             344 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Burkholderia].
ACCESSION   WP_004533413
VERSION     WP_004533413.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..344
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=37412
     Region          58..225
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 maeeqqakii negrrgflar ssawpvgmlm lplagcgdgd gvvpsahaqd tpppsgagyt
       61 idrsiqspnq dsrvrtlvlh ytaqtladsi asltspqrqv sahylvpdaa ddgrrfkvfe
      121 lvpqarrawh agvsywqgdr mlnagsvgie ivnlgfpped enlplmnrrw ypypdaqvav
      181 fgalaadvva qhqvlphkvv ghsdvapgrk tdpgplfpwk klydqykiga wpeaeavdyy
      241 rvnrpfagdv aslqskllay gydtpqtgtl daqtvnvvsa fqmhfrpsry dgvpdvetva
      301 ildallekyf nrgrainkqt lpgataptge kgsdawplap apsr
//
LOCUS       WP_004533837             837 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Burkholderia pseudomallei].
ACCESSION   WP_004533837
VERSION     WP_004533837.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 837)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 837)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 837)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..837
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=92042
     Region          52..835
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 msirhatrsv alcsmlalas tlgctsgahd apaahaprta qtahatavaa giaglrepvr
       61 ivrdsvgvsh iyarnthdlf faqgynaard rlwqldlwrr qgegkmaeqf gprfaaqdra
      121 arlflyrgdl eaeyasyhpe akqilqafad ginayvreak adpakmppef rltgaepgew
      181 rpessliriy gitrnvtgev alarqvaavg lskalslnaf eppvrqtaip agvdvglidk
      241 riladyllar nglpfraedf prsplgaaqr dalaarlnaa rltladdsan plapryesnn
      301 wvvagartas gkpllandph rrigmpslry mvhlhapgwn vigagepalp gvsvghndrv
      361 afgltifafg deedlyvydt rpghpdeyry rgrwekmriv eetvavrgqa nrverlaftr
      421 hgpvlyedaa hrkayalraa ylefpgtaay laslrldqar dwpsfvagmr rhyvpgenmv
      481 yadvdgnigw fggalapirr eadwsgalpv pgdgryewag ltegealphv lnpaagyiat
      541 anaydlpdgy ryvdrsahvw aepfrqrrld evlrgasglt vadmqrlqyd drslpaqaml
      601 gfasqlkade pgtrdalarl arwsgdmaid svpatiyefw mrevmrrvrd vevpaaarda
      661 fpklevrqvl rylqqpdgaf gadpvagrda lllaalrdgl anaraklgen vdawrwgrlh
      721 haqfdhqlag vlpefgafgt eryavggndd tvhrgtyrps dfrqtsgasy rqvidvadwd
      781 rsmiqntpgq sgdprspfha nllkgwasge ywpmafsdra vdalahdtli lepapar
//
LOCUS       WP_004513217              74 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Geobacter].
ACCESSION   WP_004513217
VERSION     WP_004513217.1
KEYWORDS    RefSeq.
SOURCE      Geobacter
  ORGANISM  Geobacter
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Geobacterales; Geobacteraceae.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 74)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 74)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 74)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Geobacter"
                     /db_xref="taxon:28231"
     Protein         1..74
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=7989
     Region          3..74
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 meitvklfam frvgrfaagt ykyrdgitpa diagelkipe kdvgivlvns rhakldhrlf
       61 egdtlslfpl vggg
//
LOCUS       WP_004535025             277 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia pseudomallei].
ACCESSION   WP_004535025
VERSION     WP_004535025.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 277)
  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 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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..277
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30175
     Region          1..257
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          170..246
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mpayrrlhap hprlrdivnc yfvevgragp mlypatpsas itvfasgasv htngiahtet
       61 lmcrpqrsav watllpgtty vsvvfrpgqi rrvmprgasa ayddgsplda vfpraavral
      121 vdgvrgaptl ghavaaledw lmaqahvaee fdaggillpp acvdapreal aaqfsrsprq
      181 lerlfidtfg asqremrsll ryartlsrli aadfalpals dmaidcgyyd haqmtrafrr
      241 yagmapvqla aavrdarqas mtmyryelad krillda
//
LOCUS       WP_004535450             790 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Burkholderia pseudomallei].
ACCESSION   WP_004535450
VERSION     WP_004535450.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 790)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 790)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 790)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..790
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=84678
     Region          33..790
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 masrtnrlpr wlkilpgvil lgallvaaga alflraslpr ldgdvraptl ggpmtierda
       61 agvptvaard rfdaaygigy lhaqdrffqm dylrrtgage laellgpaal dfdrehrlfr
      121 fraraaaafa qlppderrll erytqgvndg laalrarpfe yallgeppar wrpedsllvi
      181 wamyfqvqgt lasrdiarnw ltahatqqqr afllpsssgf dapldaprid eapaplpdaa
      241 pdwfraagdg aakrasldfr ssvgsnnwai agsrsargaa ivgddmhlvl glpntwyraa
      301 ftysggaapv rravgvtlag lpaivagsng hvawgltvgy adcldlvple rdgddsrafr
      361 msgarqiarr yvesirvrgg asvsltvlet tvgpvreigg rpyavhwvaq spgavnlgla
      421 rladavdvdg amrvantlgi paenivvgdr agrigwtiag alpdrraprg gegaawrsll
      481 ppdayprvvd psggqlwtan srqlaggayr ligdggtdlg aratqlrdgl talgrtdeqa
      541 ayrialddra lfiaqwrdra lrvlddaala ghpsraefrr llehgwtgra svdsvgytla
      601 rgflyrlydv tfdglnarlk qvdagadyel anlrwpavva rlldaqppgw lpagasswrd
      661 vqliaidrti aaltadgapl araswgarnt lriahpfags lpllggwlta paaqmpgdsh
      721 mprvaapdfg qsermvvspg heefgifnmp ggqsghplsp fflaghdawv raeptpflpg
      781 varhtlrfap
//
LOCUS       WP_004535630             796 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Burkholderia pseudomallei].
ACCESSION   WP_004535630
VERSION     WP_004535630.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 796)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..796
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=85565
     Region          37..795
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mastrnrtrr hlkilsglil fcallalvla aaylraslpr ldgelrapvl gapmtaerda
       61 lgvptitard rfdaaygigy lhaqdrffqm dmlrrsgage lselfgpial gvdrdhrlyr
      121 fralaaaava hlppddlrll qrytqgvndg laalrarpfe yallrmqpqr wrpedsllvi
      181 wamyfdlqgr lasrefarhw lqahstpeql afllpsssrf dapldasgia aaaapvsata
      241 pawlrdarsa tsvngvsidg qsavgsnnwa lagsrtasga aivgddmhls fglpniwyra
      301 mfklgggagr aarvvgvtlp glpavvvgsn griawgftng yadclellpl erdardpsrf
      361 rlggawqrar etvetirvhg aapveltvld ttagpvreig gkayaahwia qasgaanlaf
      421 akmieatgve eaigiaagag lpaqnvvigd stgrigwtva galpdrrapg eagargdgap
      481 swraalppda hprivdpagg qlwtannrql agdayrligd ggadlgarar qlrdgltale
      541 rpderaayrl dlddralfms lwrdralrvl deaalaghpa raefrrllas gwtgrasvds
      601 vgytlargyl yrlydvlfgg ldarlkqqqh dadyalanrr wpvviarlld eqppgwlpad
      661 aaswrdvqla aidrtidals angapladaa wgrrntlria hpfarsvplv grwltapadp
      721 vpgdanmprv aaprfgqser lvvspgrees glfnmpggqs ghplspffla gheawvkgep
      781 lpllpgpteh tlrfvr
//
LOCUS       WP_004537036             881 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia pseudomallei].
ACCESSION   WP_004537036
VERSION     WP_004537036.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 881)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 881)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 881)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..881
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..881
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=94482
     Region          129..179
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          158..881
                     /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 mdsicnrrpr rahagvcadt anapaglpea aqpaarlgag rprdaaaprc arqatshtsh
       61 ashtlhapcm pqfaprrvva rvaaaalfsa caapgvsgaa epaaatrgyd ipagpldaal
      121 trfgreagil lsfpgelttg lrspglhgra dpaaaldrll tgtglvalrq psggytlarl
      181 pgpaaagada alaadttlpt vavrasgpha dsyrppreaa glrsdaplae vpqavaivaq
      241 qvlrdqrprn lddalanvsg itqgntlgst qdtvmkrgfg dnrdgsvmrn gmpivqgrsl
      301 nattdsvevl kgpasllygi mdpggvinvv tkqpqlarrh aisalgstyg ggrnggeltf
      361 dstgaigesr vayrlivdqt neqywrnyge hretlvapsl awygrdtqmv lsyeyrrflm
      421 pfdrgtaldp rtnaplaipa rrrldepfnd mrgesnlaql aidhqlapdw kvhvgysynr
      481 etydanqiri tavdplkgtl trsndathgs rstdsygiay vdgrvtlagm rhdvqfgvdg
      541 eyrqvyradm lrqpiktpfs ylnptyglvp pstsvsasds dqsdtlhtas lffqdsihls
      601 erwmlvggar wvrysqlagr grpfqvntnl sgtkwlprag ivykwndals lygsytqslk
      661 ptskiapmag gyvidgstap eegaswelga kldmpgglag tlaffdidkk hvlvsqydda
      721 tnqtawrtsg rarsrgield vsgrigarwn viasyayida kttedplyag nrlwnvarht
      781 aslaavydvg tvlggddlri gaagryvgar pgdsansftl payatadafa tydtrlgkqk
      841 lqfqlnvknl fnrtyypssv nrffvsvgda rqvsllttlq f
//
LOCUS       WP_004535836             277 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia pseudomallei].
ACCESSION   WP_004535836
VERSION     WP_004535836.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 277)
  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 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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..277
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_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          1..257
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          170..246
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mpayrrlhap hprlrdivnc yfvelgragp mlypatpsas itvfasgasv htngiahaet
       61 lmcrpqrsav watllpgtty vsvvfrpgqi rrvmprgasa ayddgsplda vfpraavral
      121 vdgvrgaptl ghavaaledw lmaqahvaee fdaggillpp acvdapreal aaqfsrsprq
      181 lerlfidtfg asqremrsll ryartlsrli aadfalpals dmaidcgyyd haqmtrafrr
      241 yagmapvqla aavrdarqas mtmyryelad krillda
//
LOCUS       WP_004537801             429 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Burkholderia pseudomallei].
ACCESSION   WP_004537801
VERSION     WP_004537801.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..429
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=47552
     Region          37..259
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mtiaqqerpv aaspyrfeve mtsglervaa hhhdltltsv fqpifslshm ravgyeallr
       61 ahdaldrpvs pldvfgeaar hgeatqvdrl aqalhlenfa rfgaerewlf lnvhpgvltd
      121 pfqaaalfan lrrldiaprr ivlevleqra edierladav refrehgfli alddfgaghs
      181 nieriwqlnp divkldriml shaqhraglt ailhglvtll heagklvlie gieteheaqi
      241 alacdadfvq ghffgrpapg lpdsaaasac igelteryrq qteaaerrda qrlapyqraf
      301 eraaerlaag epldevcwnf laldhaarcf lldergrqag rnvvlradra shetrflpla
      361 daqganwlrr pyfraaiaep grvqatrpyl sinealpcvt lsiavrvnda lcvlcgdidw
      421 idadaaaga
//
LOCUS       WP_004537901             796 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Burkholderia pseudomallei].
ACCESSION   WP_004537901
VERSION     WP_004537901.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 796)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..796
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=85556
     Region          37..795
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mastrnrtrr hlkilsglil fcallalvla aaylraslpr ldgelrapvl gapmtaerda
       61 lgvptitard rfdaaygigy lhaqdrffqm dmlrrsgage lselfgpial gvdrdhrlyr
      121 fralaaaava hlppddlrll qrytqgvndg laalrarpfe yallrmqpqr wrpedsllvi
      181 wamyfdlqgr lasrefarhw lqahstpeql afllpsssrf dapldapgia aaaapvsata
      241 pawlrdarpa tsvngvsidg qsavgsnnwa lagsrtasga aivgddmhls fglpniwyra
      301 mfklgggagp aarvvgvtlp glpavvvgsn griawgftng yadclellpl erdardpsrf
      361 rlggawqrar etvetirvhg aapveltvld ttagpvreig gkayaahwia qasgaanlaf
      421 akmieatgve eaigiaagag lpaqnvvigd stgrigwtva galpdrrapg eagargdgap
      481 swraalppda hprivdpagg qlwtannrql agdayrligd ggadlgarar qlrdgltale
      541 rpderaayrl dlddralfms lwrdralrvl deaalaghpa raefrrllas gwtgrasvds
      601 vgytlargyl yrlydvlfgs ldarlkqqqh dadyalanrr wpvviarlld eqppgwlpad
      661 aaswrdvqla aidrtidals angapladaa wgrrntlria hpfarsvplv grwltapadp
      721 vpgdanmprv aaprfgqser lvvspgrees glfnmpggqs ghplspffla gheawvkgep
      781 lpllpgpteh tlrfvr
//
LOCUS       WP_004539032             311 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Burkholderia
            pseudomallei].
ACCESSION   WP_004539032
VERSION     WP_004539032.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..311
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32951
     Region          26..273
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 messnrpart heasaatllv dcrnalgega twcdaahaly wvdiegarlw rwraagahgg
       61 ercdswempe riacfaltgd pdvllvglas rlaffdtrrr altpivdvep drptrlndgr
      121 cdragafvfg tkdesggasp raiggyyrln adlslqrlal ppaaiangia fspdgsamyf
      181 cdsptreiqv cdyrpggdvd rvrsfvrlad ahgepdgstv dasggvwnaq wggarvvryd
      241 aqgvetdria vptpqpscvt ldaagrlyvt sarvglddga lagnpgaggv fvahtrhpgg
      301 atprfalard a
//
LOCUS       WP_004539686             202 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Burkholderia pseudomallei].
ACCESSION   WP_004539686
VERSION     WP_004539686.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 202)
  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   2  (residues 1 to 202)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..202
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19175
     Region          24..80
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mlkkllmlvv alslsltaal aaavevntad qaalesvkgl gpvkskaiid erakngpfkd
       61 addlanrvkg lgaksvahle aagltiggst tpptgakakt gtakpaatat papapapapt
      121 tssatpapsa atpapatatp stpasapaak ksrsskkqdk aaaasaaaqa sapaaasttk
      181 akgskkskkn kaatpasaas ga
//
LOCUS       WP_004539941             105 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Burkholderia pseudomallei].
ACCESSION   WP_004539941
VERSION     WP_004539941.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (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   2  (residues 1 to 105)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..105
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10304
     Region          22..78
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mlkkllataa lcaaaahgwa avdvnaandd alrgirgigp akakaivder sahgpfkdaa
       61 dlarrvkgmg gktverlqae glaigaaral aaagapqkaa aagkk
//
LOCUS       WP_004540842             325 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia pseudomallei].
ACCESSION   WP_004540842
VERSION     WP_004540842.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 325)
  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 325)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 325)
  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   4  (residues 1 to 325)
  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 325)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..325
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35691
     Region          50..202
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          230..309
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mdqrhtrles aahapprpda qtlaprkaar relaalierf apadgahpsa ipalsffrcs
       61 spvdlgcsvt raafvfaaqg akrvtvagqa yeydhqqrlv tsvdlpmlsq vtrasagapy
      121 lcvkialdvq riaelsaemr mpppeavptg egivvgalse plfdaalrlv rlldtpadip
      181 ilapliekel lyrlltsglg arlrhiavag sqtyriarai ewlrhhytep lrvetlaqqv
      241 nmsvsslhhh fkhvttlspl qyqkqlrlhe arrlllgqhg dvgsvalrvg ydspsqfsre
      301 ysrlfgappl rdvvqrrrng tgvqe
//
LOCUS       WP_004542824             890 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia pseudomallei].
ACCESSION   WP_004542824
VERSION     WP_004542824.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 890)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 890)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 890)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..890
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..890
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=95445
     Region          138..188
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          167..890
                     /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 mdsicnrrph rahagvcadt anapaglpea aqpaarlgag rprdaaaprc arqatshtsh
       61 ashtlhapcm pqfapqfapr rvaprrvvar vaaaalfsac aapgvsgaae paaatrgydi
      121 pagsldaalt rfgreagill sfpgelttgl rspglhgrad paaaldrllt gtglvalrqp
      181 sggytlarlp gpaaagadaa laadttlptv avrasgphad syrppreaag lrsdaplaev
      241 pqavaivaqq vlrdqrprnl ddalanvsgi tqgntlgstq dtvmkrgfgd nrdgsvmrng
      301 mpivqgrsln attdsvevlk gpasllygim dpggvinvvt kqpqlarrha isalgstygg
      361 grnggeltfd stgaigesrv ayrlivdqtn eqywrnygeh retlvapsla wygrdtqvvl
      421 syeyrrflmp fdrgtaldpr tnaplaipar rrldepfndm rgesnlaqla idhqlapdwk
      481 vhvgysynre tydanqirit avdplkgtlt rsndathgsr stdsygiayv dgrvtlagmr
      541 hdvqfgvdge yrqvyradml rqpiktpfsy lnptyglvpp stsvsasdsd qsdtlhtasl
      601 ffqdsihlse rwmlvggarw vrysqlagrg rpfqvntnls gtkwlpragi vykwndalsl
      661 ygsytqslkp tskiapmagg yvidgstape egaswelgak ldmpgglagt laffdidkkh
      721 vlvsqyddat nqtawrtsgr arsrgieldv sgrigarwnv iasyayidak ttedplyagn
      781 rlwnvarhta slaavydvgt vlggddlrig aagryvgarp gdsansftlp ayatadafat
      841 ydtrlgkqkl qfqlnvknlf nrtyypssvn rffvsvgdar qvsllttlqf
//
LOCUS       WP_004546516             837 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Burkholderia pseudomallei].
ACCESSION   WP_004546516
VERSION     WP_004546516.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 837)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 837)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 837)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..837
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=92000
     Region          52..835
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 msirhatrsv alcsmlalas tlgctsgahd apaahaprta qtahatavaa giaglrepvr
       61 ivrdsvgvsh iyarnthdlf faqgynaard rlwqldlwrr qgegkmaeqf gprfaaqdra
      121 arlflyrgdl eaeyasyhpe akqilqafad ginayvreak adpakmppef rltgaepgew
      181 rpessliriy gitrnvtgev alarqvaavg lskalslnaf eppvrqtaip agvdvglidk
      241 riladyllar nglpfraedf prsplgaaqr dalaarlnaa rltladdsan plapryesnn
      301 wvvagartas gkpllandph rrigmpslry mvhlhapgwn vigagepalp gvsvghndrv
      361 afgltifafg deedlyvydt rpghpdeyry rgrwekmriv eetvavrgqa nrverlaftr
      421 hgpvlyedaa hrkayalraa yleypgtaay laslrldqar dwpsfvagmr rhyvpgenmv
      481 yadvdgnigw fggalapirr eadwsgalpv pgdgryewag ltegealphv lnpaagyiat
      541 anaydlpdgy ryvdrsahvw aepfrqrrld evlrgasglt vadmqrlqyd drslpaqaml
      601 gfasqlkade pgtrdalarl arwsgdmaid svpatiyefw mrevmrrvrd vevpaaarda
      661 fpklevrqvl rylqqpdgaf gadpvagrda lllaalrdgl anaraklgen vdawrwgrlh
      721 haqfdhqlag vlpafgafgt eryavggndd tvhrgtyrps dfrqtsgasy rqvidvadwd
      781 rsmiqntpgq sgdprspfha nllkgwasge ywpmafsdra vdalahdtli lepapar
//
LOCUS       WP_004548050             796 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Burkholderia pseudomallei].
ACCESSION   WP_004548050
VERSION     WP_004548050.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 796)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..796
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=85537
     Region          37..795
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mastrnrtrr hlkilsglil fcallalvla aaylraslpq ldgelrapvl gapmtaerda
       61 lgvptitard rfdaaygigy lhaqdrffqm dmlrrsgage lselfgpial gvdrdhrlyr
      121 fralaaaava hlppddlrll qrytqgvndg laalrarpfe yallrmqpqr wrpedsllvi
      181 wamyfdlqgr lasrefarhw lqahstpeql afllpsssrf dapldasgia aaaapvsata
      241 pawlrdarsa tsvngvsidg qsavgsnnwa lagsrtasga aivgddmhls fglpniwyra
      301 mfklgggagr aarvvgvtlp glpavvvgsn griawgftng yadclellpl erdardpsrf
      361 rlggawqrar etvetirvhg aapveltvld ttagpvreig gkayaahwia qasgaanlaf
      421 akmieatgve eaigiaagag lpaqnvvigd stgrigwtva galpdrrapg eagargdgap
      481 swraalppda hprivdpagg qlwtannrql agdayrligd ggadlgarar qlrdgltale
      541 rpderaayrl dlddralfms lwrdralrvl deaalaghpa raefrrllas gwtgrasvds
      601 vgytlargyl yrlydvlfgg ldarlkqqqh dadyalanrr wpvviarlld eqppgwlpad
      661 aaswrdvqla aidrtidals angapladaa wgrrntlria hpfarsvplv grwltapadp
      721 vpgdanmprv aaprfgqser lvvspgrees glfnmpggqs ghplspffla gheawvkgep
      781 lpllpgpteh tlrfvr
//
LOCUS       WP_004547568             353 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Burkholderia].
ACCESSION   WP_004547568
VERSION     WP_004547568.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 353)
  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 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   3  (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   4  (residues 1 to 353)
  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 353)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..353
                     /product="CmpA/NrtA family 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=37686
     Region          14..260
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mntarikaaa admperarlr igfvalsdaa plvaaqrlel garygltlel crqpswasir
       61 dkllsgelda ahalyglvyg vqlgiggpra dlavpmvlnr ngqaitfsnr ladayrasge
      121 lkaalatlgr rpvfaqtfpt gthamwlyhw lashgvdplh dvrsvvippp emvgalaage
      181 ldglcvgepw navaeargag rtvaatsevw pdhpekalac rrefvalypn aarllvrtll
      241 dacawlddpa hrmqaarwla qpdtigvpve qiaprllgdy gagpfaqppa pirfhahgta
      301 nrpaasdglw flsqyrrwgm lsgdvddaai angvahtaly deavvlggar rge
//
LOCUS       WP_004548488             296 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Burkholderia
            pseudomallei].
ACCESSION   WP_004548488
VERSION     WP_004548488.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..296
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32171
     Region          17..266
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mehefkwvca vplasgcgeg avwaeaeqal ywtdvtrfll lrltprdgcv ktwlfdepvv
       61 alsltdrvgr llvalgshli lwtaatderv nygvwlngwp qvrfnegrsg pdgsfwvgsm
      121 rnnvntdgsl reaggsdgil mrvgpgtqts iqggelgian tlcwtpdhsr lifgdtlanm
      181 lyiadyrdgv lsnrhpfftg ferglpdgsa idaegfvwnc rfgggcivri spegkmdrvi
      241 eaptsnpttc afggpdyrtl yvtsasihte pgdrlaggvf alrtevpglp sfafqy
//
LOCUS       WP_004548591             837 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Burkholderia pseudomallei].
ACCESSION   WP_004548591
VERSION     WP_004548591.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 837)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 837)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 837)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..837
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=91982
     Region          52..835
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 msirhatrsv alcsmlalas tlgctsgahd apaahaprta qtahatavaa giaglrepvr
       61 ivrdsvgvsh iyarnthdlf faqgynaard rlwqldlwrr qgegkmaeqf gprfaaqdra
      121 arlflyrgdl eaeyasyhpe akqilqafad ginayvreak adpakmppef rltgaepgew
      181 rpessliriy gitrnvtgev alarqvaavg lskalslnaf eppvrqtaip agvdvglidk
      241 riladyllar nglpfraedf prsplgaaqr dalaarlnaa rltladdsan plapryesnn
      301 wvvagartas gkpllandph rrigmpslry mvhlhapgwn vigagepalp gvsvghndrv
      361 afgltifafg deedlyvydt rpghpdeyry rgrwekmriv eetvavrgqa nrverlaftr
      421 hgpvlyedaa hrkayalraa yleypgtaay laslrldqar dwpsfvagmr rhyvpgenmv
      481 yadvdgnigw fggalapirr eadwsgalpv pgdgryewag ltegealphv lnpaagyiat
      541 anaydlpdgy ryvdrsahvw aepfrqrrld evlrgasglt vadmqrlqyd drslpaqaml
      601 gfasqlkade pgtrdalarl arwsgdmaid svpatiyefw mrevirrvrd vevpaaarda
      661 fpklevrqvl rylqqpdgaf gadpvagrda lllaalrdgl anaraklgen vdawrwgrlh
      721 haqfdhqlag vlpafgafgt eryavggndd tvhrgtyrps dfrqtsgasy rqvidvadwd
      781 rsmiqntpgq sgdprspfha nllkgwasge ywpmafsdra vdalahdtli lepapar
//
LOCUS       WP_004549745             368 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Burkholderia
            pseudomallei].
ACCESSION   WP_004549745
VERSION     WP_004549745.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 368)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..368
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40260
     Region          4..331
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 msynvrmasl acnlpsrllr nddaafdeve pipsewwqfw giesryvidp hageselama
       61 ertarqalar agvdaaeldl vlfnitspfv taadgarrfa prlsrtlrer lgarraldad
      121 vemecasfvl qmqlaanlik qgrvkralvc ssermsavvd yaskssttfg dgaaaavlva
      181 dahdphgadw lnavyrsdat hyalatmqwr ypkppadrdd aerqaerfga yftlkpeaqe
      241 qiarfmpeai pdiverllgk tglrtddida mvfhqpseil vrawaqrlgl apdqyvirla
      301 dcaclvsaav plalyesirr gvvkpgsqvv iagagagwgf gaqlwrwget vvtdagspvd
      361 aterehaa
//
LOCUS       WP_004550333             429 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Burkholderia].
ACCESSION   WP_004550333
VERSION     WP_004550333.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..429
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=47524
     Region          37..259
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mtiaqqerpv aaspyrfeae mtsglervaa hhhdltltsv fqpifslshm ravgyeallr
       61 ahdaldrpvs pldvfgeaar hgeatqvdrl aqalhlenfa rfgaerewlf lnvhpgvltd
      121 pfqaaalfan lrrldiaprr ivlevleqra edierladav refrehgfli alddfgaghs
      181 nieriwqlnp divkldriml shaqhraglt ailhglvtll heagklvlie gieteheaqi
      241 alacdadfvq ghffgrpapg lpdsaaasac igelteryrq qteaaerrda qrlapyqraf
      301 eraaerlaag epldevcwnf laldhaarcf lldergrqag rnvvlradra shetrflpla
      361 daqganwlrr pyfraaiaep grvqatrpyl sinealpcvt lsiavrvnda lcvlcgdidw
      421 idadaaaga
//
LOCUS       WP_004550651             340 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia pseudomallei].
ACCESSION   WP_004550651
VERSION     WP_004550651.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 340)
  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 340)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 340)
  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   4  (residues 1 to 340)
  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 340)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..340
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37378
     Region          28..212
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          255..337
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtaklahwdf vrpvattrvl vdvgveqgla vgqclggsgv cadlldkpda tvaaaqelri
       61 vrnlmrllgp dfplgieigr ryhataygvw gfalmssatf gdavsvglry lqltstfcei
      121 rptlrgddat lmiddrdlpg dvrdvlveit vaalitlqfd ldaanlpvkr lalkmkppsy
      181 agrfrtlfda tpefgaahna ltvdvrcldl klpqrnaltr rrcedecrrv lerhrrsegw
      241 agrvrrqlag dpargptmdv laaelgvspr tlrrrlaneg tdyetvadel rqalaealla
      301 tttltlaevs erlgysepsa farafrrwkg mspseyrraa
//
LOCUS       WP_004550696             347 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia pseudomallei].
ACCESSION   WP_004550696
VERSION     WP_004550696.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 347)
  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 347)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 347)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 347)
  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   5  (residues 1 to 347)
  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   6  (residues 1 to 347)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..347
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38761
     Region          33..220
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <182..346
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 matsvpdptr qlnkatvssa yalfmlmlae ergiadadll ahtgvtrtkl eepnaritpl
       61 qqaaivfnll gmtndpsiai eiglrssltk sgligfglms catlgeaiql girylptrvp
      121 ffsvrftefe htvqidilea fplgrlrqfa venfmvetai lfnslltpsh dktmkanael
      181 cfewpeppyf aryrdrlprc hfgapanqir ceaalldepi ktanahtaqm ivqqceaela
      241 rlgyaesive rvrnllirgs hgypsldala relhlsertl krklsdygtt ysalldeirl
      301 rdalrllegt tltveeiaar vgytdranfs rafrrwtgts psdrrrt
//
LOCUS       WP_004551177             150 aa            linear   BCT 20-JAN-2025
DEFINITION  RHS repeat-associated core domain-containing protein, partial
            [Burkholderia pseudomallei].
ACCESSION   WP_004551177
VERSION     WP_004551177.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 150)
  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 10264210
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         <1..150
                     /product="RHS repeat-associated core domain-containing
                     protein"
     Region          1..32
                     /region_name="RHS"
                     /note="RHS protein; pfam03527"
                     /db_xref="CDD:427349"
     Region          24..101
                     /region_name="Rhs_assc_core"
                     /note="RHS repeat-associated core domain; TIGR03696"
                     /db_xref="CDD:274730"
ORIGIN      
        1 hvdaagtava mtddagalaw agrysawgri lpptslkvqi dqplrfaghy addevrlhln
       61 gtryydpdtg rylspdrsae pgtspyryvs npqtacnptg ravtlarpra gkrlgssvkr
      121 tfdlgepaag lvaklddvvd galiqlgqev
//
LOCUS       WP_004551653             894 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia pseudomallei].
ACCESSION   WP_004551653
VERSION     WP_004551653.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 894)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 894)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 894)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..894
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..894
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=95893
     Region          142..192
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          171..894
                     /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 mdsicnrrpr rahagvcadt ahapaglpea aqpaarlgag rprdaaaprc arqatshtsh
       61 tshtshtsha shtlhapcmp qfapqfaprr vvarvaaaal fsacaapgvs gaaepaaatr
      121 gydipagpld aaltrfgrea gillsfpgel ttglrspglh gradpaaald rlltgtglva
      181 lrqpsggytl arlpgpaaag adaalaadtt lptvavrasg phadsyrppr eaaglrsdap
      241 laevpqavai vaqqvlrdqr prnlddalan vsgitqgntl gstqdtvmkr gfgdnrdgsv
      301 mrngmpivqg rslnattdsv evlkgpasll ygimdpggvi nvvtkqpqla rrhaisalgs
      361 tygggrngge ltfdstgaig esrvayrliv dqtneqywrn ygehretlva pslawygrdt
      421 qvvlsyeyrr flmpfdrgta ldprtnapla iparrrldep fndmrgesnl aqlaidhqla
      481 pdwkvhvgys ynretydanq iritavdplk gtltrsndat hgsrstdsyg iayvdgrvtl
      541 agmrhdvqfg vdgeyrqvyr admlrqpikt pfsylnptyg lvppstsvsa sdsdqsdtlh
      601 taslffqdsi hlserwmlvg garwvrysql agrgrpfqvn tnlsgtkwlp ragivykwnd
      661 alslygsytq slkptskiap maggyvidgs tapeegaswe lgakldmpgg lagtlaffdi
      721 dkkhvlvsqy ddatnqtawr tsgrarsrgi eldvsgriga rwnviasyay idakttedpl
      781 yagnrlwnva rhtaslaavy dvgtvlggdd lrigaagryv garpgdsans ftlpayatad
      841 afatydtrlg kqklqfqlnv knlfnrtyyp ssvnrffvsv gdarqvsllt tlqf
//
LOCUS       WP_004553602             342 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Burkholderia pseudomallei].
ACCESSION   WP_004553602
VERSION     WP_004553602.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..342
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=37282
     Region          56..223
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 maeeqqakii negrrgflar ssawpvgmlm lplagcgdgv vpsahaqdtp ppsgagytid
       61 rsiqspnqds rvrtlvlhyt aqtladsias ltspqrqvsa hylvpdladd grrfkvfelv
      121 pqarrawhag vsywqgdrml nagsvgieiv nlgfppeden lplmnrrwyp ypdaqvavfg
      181 alaadvvaqh qvlphkvvgh sdvapgrktd pgplfpwkkl ydqykigawp eaeavdyyrv
      241 nrpfagdvas lqskllaygy dtpqtgtlda qtvnvvsafq mhfrpsrydg vpdvetvail
      301 dallekyfnr grainkqtlp gataptgekg sdawplapap sr
//
LOCUS       WP_004553831             296 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Burkholderia
            pseudomallei].
ACCESSION   WP_004553831
VERSION     WP_004553831.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..296
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32127
     Region          17..266
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mehefkwvca vplasgcgeg avwaeaeqal ywtdvtrfll lrltprdgcv ktwlfdepvv
       61 alsltdrvgr llvalgshli lwtaatderv nygvwldgwp qvrfnegrsg pdgsfwvgsm
      121 rnnvntdgsl reaggsdgil mrvgpgtqts iqggglgian tlcwtpdhsr lifgdtlanm
      181 lyiadyrdgv lsnrhpfftg ferglpdgsa idaegfvwnc rfgggcivri spegkmdrvi
      241 eaptnnpttc afggpdyrtl yvtsasihte pgdrlaggvf alrtevpglp sfafqy
//
LOCUS       WP_004556130             888 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia pseudomallei].
ACCESSION   WP_004556130
VERSION     WP_004556130.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 888)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 888)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 888)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..888
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..888
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=95233
     Region          136..186
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          165..888
                     /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 mdsicnrrpr rahagvcadt anapaglpea aqpaarlgag rprdaaaprc arqatshtsh
       61 tshashtlha pcmpqfapqf aprrvvarva aaalfsacaa pgvsgaaepa aatraydipa
      121 gpldaaltrf greagillsf pgelttglrs pglhgradpa aaldrlltgt glvalrqpsg
      181 gytlarlpgp aaagadaala adttlptvav rasgphadsy rppreaaglr sdaplaevpq
      241 avaivaqqvl rdqrprnldd alanvsgitq gntlgstqdt vmkrgfgdnr dgsvmrngmp
      301 ivqgrslnat tdsvevlkgp asllygimdp ggvinvvtkq pqlarrhais algstygggr
      361 nggeltfdst gaigesrvay rlivdqtneq ywrnygehre tlvapslawy grdtqvvlsy
      421 eyrrflmpfd rgtaldprtn aplaiparrr ldepfndmrg esnlaqlaid hqlapdwkvh
      481 vgysynrety danqiritav dplkgtltrs ndathgsrst dsygiayvdg rvtlagmrhd
      541 vqfgvdgeyr qvyradmlrq piktpfsyln ptyglvppst svsasdsdqs dtlhtaslff
      601 qdsihlserw mlvggarwvr ysqlagrgrp fqvntnlsgt kwlpragivy kwndalslyg
      661 sytqslkpts kiapmaggyv idgstapeeg aswelgakld mpgglagtla ffdidkkhvl
      721 vsqyddatnq tawrtsgrar srgieldvsg rigarwnvia syayidaktt edplyagnrl
      781 wnvarhtasl aavydvgtvl ggddlrigaa gryvgarpgd sansftlpay atadafatyd
      841 trlgkqklqf qlnvknlfnr tyypssvnrf fvsvgdarqv sllttlqf
//
LOCUS       WP_004559211             209 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein, partial [Amycolatopsis
            vancoresmycina].
ACCESSION   WP_004559211
VERSION     WP_004559211.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis vancoresmycina
  ORGANISM  Amycolatopsis vancoresmycina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Amycolatopsis vancoresmycina"
                     /db_xref="taxon:208444"
     Protein         <1..209
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
     Region          <114..199
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 shrapfegva vppavvrrlv aaggahgvea rpvheiavva rllhfaaetf redgayqrel
       61 slwtirdepa hrhgvgipms ripagsvpwa glvrrateip eppelerrla getlllfvtv
      121 ddsrfdhvra gyamehawla avdlglaaav ltqplhlaqv rsalcedlgl tgfpqallri
      181 gyaaeadpps prravdevlq rgprpaslq
//
LOCUS       WP_004561096             385 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Amycolatopsis
            vancoresmycina].
ACCESSION   WP_004561096
VERSION     WP_004561096.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis vancoresmycina
  ORGANISM  Amycolatopsis vancoresmycina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 385)
  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 385)
  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
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 385)
  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   5  (residues 1 to 385)
  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   6  (residues 1 to 385)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 385)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 385)
  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 20650276
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Amycolatopsis vancoresmycina"
                     /db_xref="taxon:208444"
     Protein         1..385
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38945
     Region          18..57
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          83..372
                     /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 mtqavrheem rarnlevvlg avgrggpltr aalaevtglt kstvsklvgd lvdagllaei
       61 gparpgergr pgvavvlsga rvaslglein vdylavrvld ltggvrfaar rerdnrgsrp
      121 kkvlgelqal atealteahr lglevagavl avsgpvgdgv lfsapnlgwq dvrpadllrl
      181 pvpveldnea nlaaqgelwy gdgerdflyv sgeigigagl vvggtlfsga tglagelghv
      241 vvapegvqcr cggsgclety agqeallaag kapsvpalla alergdgpal aacaaaghal
      301 gialtsavnl ldldrivlgg vftplypwls gpvsevlsar lgglrgtppv ltasrlggda
      361 atlgaagrvi hrvladpapf vtras
//
LOCUS       WP_004563952             586 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Ligilactobacillus salivarius].
ACCESSION   WP_004563952
VERSION     WP_004563952.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus salivarius
  ORGANISM  Ligilactobacillus salivarius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Ligilactobacillus salivarius"
                     /db_xref="taxon:1624"
     Protein         1..586
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=67742
     Region          92..>468
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mtekfierpl knekdkamqy lnslleqark dnrsedienl eeltrllhtk kyglvweeha
       61 efveeemktk ipvfvedtnr kivgnpetad ynfllegdnl hslhllekth tgkidviyid
      121 ppyntgnkdf tyndkivgqe dsflhskwls fmesrlkiar nllsddgvia vsidyhegyq
      181 lkllmdeifg eenfatdlhv etsaiaghrr isamngtvvk ttefvfiytk tphtkiinhk
      241 fydkidgfdt hyskflnpet gflenfsatl qntklvaeif dqyklkpslk nldklikvek
      301 rlktwlysde isgnlfrldt klkanvvefk pglnywknky vvsnengtqy tafrysdrig
      361 qtdgykpsfs erairgnlwk gfssdggnls keggvnlkng kkplrlikql ikalgtsksi
      421 vvldffagsg ttghavaqln kedggnrkyi lctnnennic eeitykrltn iqedlphnlk
      481 yfktdfvdkt kfpdftlene llnyvtplve lefgvdisdp svqvilteer leellrnnkl
      541 keratlfihp difldskeqk qlkelnitlq eipdyffgke lwqsny
//
LOCUS       WP_004564927             353 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease family protein [Actinomyces].
ACCESSION   WP_004564927
VERSION     WP_004564927.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces
  ORGANISM  Actinomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Actinomyces"
                     /db_xref="taxon:1654"
     Protein         1..353
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=37524
     Region          107..>219
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mnasgrllar ltvlgalsas gmtaalpvha ddaspepsqr saatelaalh eapwdrrgdf
       61 ilslkaslev lselpedapa ahswaeggsr tgwfgeawtd vdgdgcdtrn eilardleda
      121 dfsradglqs reegrgrgag vcpdatvwag vlqdpytgrr vtftrgqets aavqidhvvp
      181 lnylyahgaw qwdertrllv andplnlvav egeanqakga cgpascpigs tetgswrptg
      241 pggwwpanss yrctyarrfv svaaayrlgl pqadkaalst tlnsclaggd gtaslperaa
      301 rsakevgsvv whspryaala algalvlgwg lilrgrrrgr aasrrrrrsm srh
//
LOCUS       WP_004564267             397 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Ligilactobacillus salivarius].
ACCESSION   WP_004564267
VERSION     WP_004564267.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus salivarius
  ORGANISM  Ligilactobacillus salivarius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Ligilactobacillus salivarius"
                     /db_xref="taxon:1624"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43703
     Region          2..396
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkkiivinsg ssslkfklfe spsknvlasg lierigldds iitikynnkk yrevqtikdh
       61 taavdlllql lkklnivtdl neisavghrv vaggeyfkks vpidssviek iediielapl
      121 hnpanlvgik vfkkllpnal svaafdtafh qtlpkenfmy stpyewykny gvrrygahgi
      181 shryvslraa klmgkpvedl klvtchlgag asitavkngk sfdtsmgftp ltgiqmatrs
      241 gdvdvslvay mmkklkvksv seilymlnke sgflgvsgvs ldmrdveaaa aknnkraela
      301 iklfyndivk yigqyymeme gidgivftag igenspetre aimnklsflg vtinkdensk
      361 rgtegivsgk dssitvmrip tdeeymiccd vealmnk
//
LOCUS       WP_004565586             386 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Schaalia odontolytica].
ACCESSION   WP_004565586
VERSION     WP_004565586.1
KEYWORDS    RefSeq.
SOURCE      Schaalia odontolytica
  ORGANISM  Schaalia odontolytica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 386)
  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 386)
  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
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 386)
  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   5  (residues 1 to 386)
  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   6  (residues 1 to 386)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 386)
  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 15726307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Schaalia odontolytica"
                     /db_xref="taxon:1660"
     Protein         1..386
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40381
     Region          17..>75
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          79..359
                     /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 msathgpdri relnslaild ylrsvdeatv sqiaqetgls rtsvgatiad ceelgwvasl
       61 ppapsitgrp akryrfqsea gvvvgldiga nhidvmatnl igaslasara dvspdepapq
      121 rlgaalalld silegqgvvr erltvisval tgpvdaegrs pygtplpgwd svdisrelrd
      181 rygcavfven dckcalaaea wtgqaqdlss aayimagari gasfmidgtv crgaggaage
      241 vgalkalkws stpavflths rlpadiathr aaqwvcdqar egdreaikia rsfgrnlavg
      301 asalvltvdp ealivgggis asadvwmdaf tqrltelvlr vpdvrtsnlg sqavvlgavr
      361 rglnhiealt lgdtlrgpqv lfdeqh
//
LOCUS       WP_004565953             164 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Bordetella].
ACCESSION   WP_004565953
VERSION     WP_004565953.1
KEYWORDS    RefSeq.
SOURCE      Bordetella
  ORGANISM  Bordetella
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Bordetella"
                     /db_xref="taxon:517"
     Protein         1..164
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17370
     Region          29..156
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfdatpistv skpvfyaela aqarallage hdrianaanf salvyqalpd inwagfyfhd
       61 gqelvlgpfq gkpacvrial srgvcgaaas qrrtqvvpdv hafpghiacd aasraeivvp
      121 llhkgsllgv wdvdsplpgr fddedragme alcevflhsl gsad
//
LOCUS       WP_004566389             275 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Bordetella bronchiseptica].
ACCESSION   WP_004566389
VERSION     WP_004566389.1
KEYWORDS    RefSeq.
SOURCE      Bordetella bronchiseptica
  ORGANISM  Bordetella bronchiseptica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Bordetella bronchiseptica"
                     /db_xref="taxon:518"
     Protein         1..275
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=29798
     Region          41..193
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mpwitraapi acllalagca argpagldld tsitavsqss rvravvlhyt stgnenslki
       61 lserkvsahy litdtprprv yrlmdetraa whagisawyg qstmnstsig ielvnpgwtn
      121 gegnwtrggh gdtdsrhwap ysdaqietli vllrdivarh giapenivgh sdiapqrkvd
      181 pgplfpwqrl aqaglgrwyd eagaaahlar lqtegvpdia wfqgqlarlg yatpqsgvld
      241 tatrnvlaaf qmhyrparhd gqpdaetaai mlalr
//
LOCUS       WP_004566829             266 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Corynebacterium
            diphtheriae].
ACCESSION   WP_004566829
VERSION     WP_004566829.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium diphtheriae
  ORGANISM  Corynebacterium diphtheriae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Corynebacterium diphtheriae"
                     /db_xref="taxon:1717"
     Protein         1..266
                     /product="formate/nitrite transporter family protein"
                     /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=28580
     Region          16..259
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mathnptlnd kifgsvakke allktnfhry fthcilagvy ltlgtafsah vgqkvenlap
       61 glgsvtfamf ffvglativi lnaelvtsnm mymsygvvgk kipwhkaalv livcvignlv
      121 gaviigyllg qsaaysgltp esfvsvtldh klekhsmglf veamlanfvv nmaivgcali
      181 kdiagkliwl mfvigmfvgl glehvvanfs lvtlvgfgse vhseyftagy ilhnwgidff
      241 gnlvggglci ggvyawlnrg senyrd
//
LOCUS       WP_004568145             238 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Bordetella bronchiseptica].
ACCESSION   WP_004568145
VERSION     WP_004568145.1
KEYWORDS    RefSeq.
SOURCE      Bordetella bronchiseptica
  ORGANISM  Bordetella bronchiseptica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 238)
  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   3  (residues 1 to 238)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Bordetella bronchiseptica"
                     /db_xref="taxon:518"
     Protein         1..238
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25589
     Region          42..235
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mpdahdpylv sgrfeianll qtlqarqcll lmripgrpfn svtsvlhvda qagqvvldaa
       61 qddtlnqrla dagdvafdts ldnisisfaa arvtrcefea rpallvdlpe tltrvqrrdt
      121 friavpvaqp atwvreagga eplalcdisp gglaladplq tldpapgkiy rgvlalpelg
      181 afaaairvvh hldevlakgk tsrrigcafv eldkgtgiri qayvnalqrd qiarqrgl
//
LOCUS       WP_004568437             577 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Bordetella bronchiseptica].
ACCESSION   WP_004568437
VERSION     WP_004568437.1
KEYWORDS    RefSeq.
SOURCE      Bordetella bronchiseptica
  ORGANISM  Bordetella bronchiseptica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Bordetella bronchiseptica"
                     /db_xref="taxon:518"
     Protein         1..577
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=64270
     Region          7..508
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mskqkleltw igkekrpkle prilledpek syhakrrvte ndifdnrlif gdnllalkal
       61 eyeftgrvrc iyidppyntg safaqyedgl ehsiwlglir erltllrnll skdgscwiql
      121 ddneaqyckv ladeifgrdn fianvvwnks yavrsnaqff ssahehilvy akdrahlrln
      181 qfgrsakqte rysnpdndpr gpwqsvtmti slvggargrq yaktgvseni fevkspsgkv
      241 flpppnrcws rnpsgfkkld aegriywgts genaprlkmy lseaaegvmp ttlwadgvef
      301 ghnqdgirel raldvgdfpt pkpeklisqv islasdpgdi vldsfagsgt tgavahkmgr
      361 rwlmvelgeh chthilprlr kvidgedggg vtesvgwegg ggfryyslap slivndrwgn
      421 pvinpeynaa qlaealakle gfsyapsevq wwqhghsser dfiyvttqnl sadqlqalsd
      481 evgsdrsllv ccaafhgvta akanerwpnl tlkkipkmvl arcewghddy slnvanlpma
      541 kpdpvetsaa aeankktksr kvpaansnqg glfgene
//
LOCUS       WP_004570493             268 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Polaribacter irgensii].
ACCESSION   WP_004570493
VERSION     WP_004570493.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter irgensii
  ORGANISM  Polaribacter irgensii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 268)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Polaribacter irgensii"
                     /db_xref="taxon:531"
     Protein         1..268
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31185
     Region          12..110
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          <172..254
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkltyfeiqk tahlieefyh isysnktipy nttiipygvs sltfvycdgq rvstennete
       61 lknlvlagqf fksyqfsane vgfscgisfk pttlhkltnl niskftnkhv lfeqvhknis
      121 aklefifknn snnliqlfqn lenllfelpl ienkntiavd taidfihqkq gllsvqellq
      181 impfgqktle tqfkkivglt pakyirihrf inlmkqyenk kvnlkdliym ydyydeshft
      241 kdfksftska pkdffeedfs iivaalkk
//
LOCUS       WP_004566201             204 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Bordetella
            bronchiseptica].
ACCESSION   WP_004566201
VERSION     WP_004566201.1
KEYWORDS    RefSeq.
SOURCE      Bordetella bronchiseptica
  ORGANISM  Bordetella bronchiseptica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 204)
  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 204)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 204)
  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   4  (residues 1 to 204)
  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   5  (residues 1 to 204)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Bordetella bronchiseptica"
                     /db_xref="taxon:518"
     Protein         1..204
                     /product="TRAP transporter small permease subunit"
                     /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=21880
     Region          4..169
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mtrllellcr glraitnrac laagwalvvl svvialnvla rkifsfslqg vdeyggycla
       61 icasigfsqa aydrahiris vltdllpprl racsdvfala lltsvaltla vkatgvayds
      121 ysmqalatsa lrtplaipqa mwaaalcwfg mvlatqllhs llllarrdwg ginrnygnps
      181 vdeevaeelr sanermagkl egah
//
LOCUS       WP_004558602             682 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Amycolatopsis
            vancoresmycina].
ACCESSION   WP_004558602
VERSION     WP_004558602.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis vancoresmycina
  ORGANISM  Amycolatopsis vancoresmycina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 682)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 682)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 682)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Amycolatopsis vancoresmycina"
                     /db_xref="taxon:208444"
     Protein         1..682
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=72877
     Region          1..680
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mpqvdthcpy calqcgmsln gtrvtprdfp vnagglcqkg wtsgsllpsp krlttpmlrv
       61 ngalepvswn faldhvarkl retqeahgpd gvaifggggl tnekayllgk farvalgtsq
      121 idyngrfcms saaaagikaf gadrgmpfpv tdlknadvvl laganpaetm ppftqhlrgs
      181 dlivvdprrt ptaelaslhl apapgtdlal algilhavve gghlnqsyvd ertsgfaemw
      241 riaaswwper aervtgvsaa dmrlaaekla garnayvlta rgteqhatgt atvgawinla
      301 lslglpgrqg sgygcltgqg ngqggrehgq kadqlpgyrk lddpaareyv agvwgvdaes
      361 lpgpgrsate llealgqdng pkalmvfgsn vvvsaprsqr vqdrlseldf lvvadfvlse
      421 taaladvvlp vtqwaeedgt ltnlegrill rrkaltpppg vrsdldvlng lahrlgqpeg
      481 rfpadaetvf eelriaskgg iadysgvsyd rlragealhw pvpaddhpgt prmfldafah
      541 pdgrarftpv ehtgpaelpd eefplqattg rvlqhyqsga qtrlvqelnd vvpeafvevh
      601 pdtakragle egdparirsr rgemtakvrf vqslkpdlvf lpfhfpgeqr anlftnpald
      661 pvsrmpefkv cavslstvdg aa
//
LOCUS       WP_004573073             400 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Acetonema longum].
ACCESSION   WP_004573073
VERSION     WP_004573073.1
KEYWORDS    RefSeq.
SOURCE      Acetonema longum
  ORGANISM  Acetonema longum
            Bacteria; Bacillati; Bacillota; Negativicutes; Acetonemataceae;
            Acetonema.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Acetonema longum"
                     /db_xref="taxon:2374"
     Protein         1..400
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43184
     Region          1..393
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkvlvvncgs ssikyqlfnm mdetvlakgl veriglegsv lthqpdgkdk vviqedipnh
       61 svgiklvlna ltdgkhgvit smkeivaigh rvvhagekfa dsvlitpdvm naleecidma
      121 plhnppnilg inacaelmpg vpqvgvfdta fhqtmpkhaf lyglpyeaye kyglrrygfh
      181 gtshkyvsqq aaeimdqhlt nlriitchlg ngasiaaiky grsidtsmgf tpleglvmgt
      241 rsgeidpaii pylmkkegmt pdqidsylnk ksgvlgisgv ssdfrdiega adtgneraql
      301 aidifayrvk kyigsyvaam ggvdaivfta glgenspdir dkicnglefl gtridpaknk
      361 irgkaqeisv dgakvkifvi ptneelviar dtrvicggli
//
LOCUS       WP_004573528             275 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Acetonema longum].
ACCESSION   WP_004573528
VERSION     WP_004573528.1
KEYWORDS    RefSeq.
SOURCE      Acetonema longum
  ORGANISM  Acetonema longum
            Bacteria; Bacillati; Bacillota; Negativicutes; Acetonemataceae;
            Acetonema.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Acetonema longum"
                     /db_xref="taxon:2374"
     Protein         1..275
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30168
     Region          5..248
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 msiekadlhi httasdglyt pqeiidsalq aglshisitd hdtldgllsl nadshvqklk
       61 vipgiefstd lpahevhilg yyidirskpl rqqldvlted rrlrvnkile klallgypis
      121 qeqvlrtamg atsvgrphva kvlvergyfs svaevfsqil sagkpayvph fkltpeqvir
      181 liiqakgvpv lahpglignd alvsaiiqkg irglevyhpm hskgeiakyl slarqhnllv
      241 tggsdfhgip arypaslgqf yipadvvyql qtyre
//
LOCUS       WP_004574033             236 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease family protein [Gardnerella].
ACCESSION   WP_004574033
VERSION     WP_004574033.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella
  ORGANISM  Gardnerella
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Gardnerella"
                     /db_xref="taxon:2701"
     Protein         1..236
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=26703
     Region          86..222
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mrnrcnkrqf lalfwmllfa vlcgivigll lpkinsnvgk itgeyeasge aaqalkklri
       61 skpyrygyer qvfgyrttdd dgngcdvred vlardlqnvk ykyagscqvr fgllhdpytg
      121 kdinfvrgrk tsaliqidhv valqnawesg awkwnrakrl kfgndmmnll avegaanqek
      181 gsasaaywlp snktfrceyv arqiavkyky gltvtreekq smesvlhncs aqklpk
//
LOCUS       WP_004573540             257 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Acetonema longum].
ACCESSION   WP_004573540
VERSION     WP_004573540.1
KEYWORDS    RefSeq.
SOURCE      Acetonema longum
  ORGANISM  Acetonema longum
            Bacteria; Bacillati; Bacillota; Negativicutes; Acetonemataceae;
            Acetonema.
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
REFERENCE   2  (residues 1 to 257)
  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 257)
  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 257)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Acetonema longum"
                     /db_xref="taxon:2374"
     Protein         1..257
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=27613
     Region          1..69
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          184..249
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mpslgemlra erekkgltlk dienatnira lyleaieqgn ysvspgevfl kgfirnyanf
       61 lglngaefve lyrqsrqtpp dpelqatgtg semvtpvses ssedaikkwl fiaafivivg
      121 ggttwwlmgd stggeqlpgq peppvppqvq tapvapvqps qaatpttppa avqpkpaakp
      181 ivvvatfstr swtrvtadgk lvfegtpqrg eiltweaqka melrfgnaaa veltyngqfl
      241 gvqgrngqvv vknftar
//
LOCUS       WP_004576218             813 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: penicillin acylase family protein [Pseudomonas].
ACCESSION   WP_004576218
VERSION     WP_004576218.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 813)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 813)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 813)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..813
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..813
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=88751
     Region          12..813
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 maapafppfr lrfataatll gmlglagcqt ggyqdsvppt sgvqplkgla qnvsvrrnam
       61 gapliesssf hdalfslgyv hagdrieqmv amrllaqgrl aelagseald idrlmraanl
      121 kqsaaqqyad asprlkrffe vyargvnayl fryrdklpag lassgyrpey wkpedsalif
      181 clyafsqsvn lqeelsaltl aqkagsdkla wllpgapdep laemevdklk glnlasqlpg
      241 lpalaaasqk ladldllgsp gsanlalgpq rsrsgkslla sdsraawals pvqintskyq
      301 vaglslpglp ivlagyngkl awsssavmad nqdlflerlr rqgnqlsyla dgkwlparar
      361 setyfvrgqr pvrevmydtr hgtllaqpen aslglalnlp qfkgdrslda lfdltraknv
      421 erafdstrev taaavnfvfa epehigwqvs grypnrregq gllpspgwdg rydwdgyadp
      481 mlhpydqdpp agwirhanqr slprgygmql sstwyypera erlaqlagng rhdsrslmal
      541 qndqvtllan klkqmfdapg maqplkqaid alpagqrdka rdtlarlkaf dgrlspvsad
      601 aalyelflqe varqtflddl gpeagpawqa fvsnarlsfs aqadhllgrd dspfwddrnt
      661 pqkedkpail arslagamea giaqlgadrr twqwgqlhqy rwpapayhgl gdaisrapla
      721 aggdfttlal tpfawgsdfd thlpasarmi vdfgqaeplq iltssgqsgn pasahyrdgl
      781 dawfkgrfms lplqqqnfgr aygnqrltlv pgr
//
LOCUS       WP_004576447             404 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Pseudomonas putida].
ACCESSION   WP_004576447
VERSION     WP_004576447.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 404)
  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 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   3  (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   4  (residues 1 to 404)
  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 404)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..404
                     /product="CmpA/NrtA family 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=43729
     Region          17..268
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mntvpratpl awvngsdape ktslnigyma ltdcasvvva atqgfaqqhg ltlnlkrqgs
       61 wagqrdklvs geldaahcly glvyavhlgi ggvpasdmav lmglnqnaqa inlspalqrk
      121 gvtnpealar lvhqhgarlt faqtfptgth amwlyywlas qgihplrdvd svvvppaqma
      181 ahlqagridg fcvgepwaad avakgqgftl atsqsiwpdh pekvlacarv faeqypnsar
      241 alikailtas rfieqspenr rstaqllsas ayldtpldsi aprllghyed glgnqwqdph
      301 alrlfdqgra nlpylsdgmw fmtqfrrwgl lredpdylgv arqvqqlqly seaahslgia
      361 cpgqpmrssl lidgsrwdgs dpfgyarsfs lhalgdlpda rvga
//
LOCUS       WP_004580184             363 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Marinobacter
            nanhaiticus].
ACCESSION   WP_004580184
VERSION     WP_004580184.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter nanhaiticus
  ORGANISM  Marinobacter nanhaiticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 363)
  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 363)
  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 363)
  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 363)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Marinobacter nanhaiticus"
                     /db_xref="taxon:1305740"
     Protein         1..363
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39561
     Region          3..362
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 msmnrrkflg aalasttaga tlaapalvra qesksfnfkm tnayppgspf yvqgpgsptd
       61 fcnkvkamsg grlnishfaa gelipalegf navaqgtvem naanayfwag nipaaqfftt
      121 vpfgmntqgm mawlyqgdgl klwhelyeph gliafpmgnt gvqmtgwfre piesvkdldg
      181 lkmripglag kvyselgvsv rllpggeifp alergvidaa efvgpfqdrr lglhnaakyy
      241 yttgwheptn vtellinkev wdslpkdlqm miqmaaqasv leslswsean nadalkdlve
      301 negviaqplp epivsrlkev tddtlasman adpqmkkvyd symtfkkkha swaalsekpl
      361 lnl
//
LOCUS       WP_004574679             146 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Gardnerella pickettii].
ACCESSION   WP_004574679
VERSION     WP_004574679.1
KEYWORDS    RefSeq.
SOURCE      Gardnerella pickettii
  ORGANISM  Gardnerella pickettii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Gardnerella.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Gardnerella pickettii"
                     /db_xref="taxon:2914924"
     Protein         1..146
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16082
     Region          38..124
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 maisataanp aksakyaeis kstkstklty pptltplvvq klcapiarkl gvkslylfgs
       61 vaqgtanrns dvdfiyemqd esnleretsr ivrkqelmrs ladclgrkid lvnksyvtqp
      121 ladedaeiqr rafvttintk pifqiv
//
LOCUS       WP_004580891              98 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Marinobacter nanhaiticus].
ACCESSION   WP_004580891
VERSION     WP_004580891.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter nanhaiticus
  ORGANISM  Marinobacter nanhaiticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 98)
  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   2  (residues 1 to 98)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Marinobacter nanhaiticus"
                     /db_xref="taxon:1305740"
     Protein         1..98
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10005
     Region          36..96
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkllisaffv ittlfsgfal adatapaepa ataaaqvnin tadaktlakl dgigeskaqa
       61 iidfrdangp fasvadltkv kgigertleq nqavitvq
//
LOCUS       WP_004581037             280 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Marinobacter
            nanhaiticus].
ACCESSION   WP_004581037
VERSION     WP_004581037.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter nanhaiticus
  ORGANISM  Marinobacter nanhaiticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Marinobacter nanhaiticus"
                     /db_xref="taxon:1305740"
     Protein         1..280
                     /product="formate/nitrite transporter family protein"
                     /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=30179
     Region          2..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msylapsefv tkmvdagesk iymstrdtli raymagaila laaafavtva vetgvfliga
       61 vlfpigfcml ylmgfdlltg vfmltplall dkrpgvninq ilrnwgwvfl gnfagaltva
      121 fmmafiftyg fntdpgpvga kiagvgeart lgyaeyglag witifirgml cnwmvsmgvv
      181 gamvstsvsg kvlamwmpim lfffmgfehs vvnmflfpsg iimggnfsim dyfiwneipt
      241 vlgnlvggla ftgltlytth vrtaakrkia prasseraaa
//
LOCUS       WP_004581255             244 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Marinobacter nanhaiticus].
ACCESSION   WP_004581255
VERSION     WP_004581255.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter nanhaiticus
  ORGANISM  Marinobacter nanhaiticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 244)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Marinobacter nanhaiticus"
                     /db_xref="taxon:1305740"
     Protein         1..244
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=26487
     Region          44..211
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mlnsrfprvl avamgvlfsv svvsnttasp fdqtlyskls vsapnisrdv lksalqasqc
       61 avssglekpk rlavidfslp ssekrlwifd lengalvlrd lvahgknsgl nqasafsnie
      121 gshqssiglf qaretyrgkh gyslrldgle egindlarqr aivihgadyv dtawvrnygr
      181 igrshgcpav sqkvirqvvd slkggqfvft yypdqrwlqs sdylncgstq magtasnags
      241 neri
//
LOCUS       WP_004581727             607 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Marinobacter nanhaiticus].
ACCESSION   WP_004581727
VERSION     WP_004581727.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter nanhaiticus
  ORGANISM  Marinobacter nanhaiticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Marinobacter nanhaiticus"
                     /db_xref="taxon:1305740"
     Protein         1..607
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=69165
     Region          3..>404
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mptlefkgkq fvyshhlgvp frelkvisdk slpaknqeps lddnliiqgd nlealkallp
       61 thagkvdcif idppyntgne gwcyndnvrs plmrewlkks anpvdkedle rhdkwlcmmw
      121 prlqllkell sergsiwitl ddneaqrckm mldeifgeen fvasciwhkm dspkntaryf
      181 sedhdyllvy tkniafweln hlprtdemis ryqnpdndpr gpwllsdlda rnkyskglys
      241 ittpkgrviq gppkgkywri seekfkemdq dgriwwgadg nadpnikrfl sevrdgvvpq
      301 tiwnwkdvgs trhakteilk vfsdtderei fvtpkpkalv arvlaiatdk nslvldsfag
      361 sattahavle ankkddgnrr filiecedya dtltaervrr vingypytgt qreelhreni
      421 twstfekkhs kvldhvasie nlqgheydki skqikdgvlt vtgerkvkgt apglggsfty
      481 ctlgepidie slltgtglpt fdalaryvfy tatgqslakv gepapdgfig etdlfrvhlf
      541 yqpdrewlrs neaalnaerv taieqnskgg kraivfavak fmsqkeltar riefcqlpya
      601 vhrilgd
//
LOCUS       WP_004582128             197 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Marinobacter nanhaiticus].
ACCESSION   WP_004582128
VERSION     WP_004582128.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter nanhaiticus
  ORGANISM  Marinobacter nanhaiticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 197)
  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 197)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 197)
  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   4  (residues 1 to 197)
  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   5  (residues 1 to 197)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Marinobacter nanhaiticus"
                     /db_xref="taxon:1305740"
     Protein         1..197
                     /product="TRAP transporter small permease subunit"
                     /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=22067
     Region          29..192
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mtvstdtdrl elepapqgls geylphtsls raldsviqgf grlsawlwpi lmmiiivnvv
       61 sryvfaqgfi eleelqwhiy sagflfalsy allwdshvrv dlirerisyr aqawielfgl
      121 lfilapfigl llyfavpyvi dswtmneass apgglsqrwi vkstlpiglg llliaafsrl
      181 vrllaflfga eaqhghq
//
LOCUS       WP_004582750             344 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Marinobacter nanhaiticus].
ACCESSION   WP_004582750
VERSION     WP_004582750.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter nanhaiticus
  ORGANISM  Marinobacter nanhaiticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 344)
  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 344)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 344)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 344)
  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   5  (residues 1 to 344)
  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   6  (residues 1 to 344)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Marinobacter nanhaiticus"
                     /db_xref="taxon:1305740"
     Protein         1..344
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39328
     Region          23..207
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          92..339
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 manltvsghf vraalcgael qqldtsamlr raaispellr asgarvssaq fsrlmqviwq
       61 dmadefmgmg prrcrpgtfa tmcallnecs tlesvlirah qfsnlfdhpv cmrheprgkd
      121 rkqvalvlev dgeihdpkhf fresilviwh rlcswligqa ialdearfay pypphgdeyr
      181 hifhcpltfe aertelifda rflsapvird rpemkqflkt spadllarpd eghsytgrir
      241 gligrdfsrp vpdfewiase lhvspqtlrr rlkqentsfq eikdllrrdl aiyhlgkker
      301 aindiahlvg ftepstfhra fkkwtgmtpg awreseapri qdgd
//
LOCUS       WP_004587755              99 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Pseudoalteromonas].
ACCESSION   WP_004587755
VERSION     WP_004587755.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            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="MoaD/ThiS family protein"
                     /calculated_mol_wt=10771
     Region          19..99
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mvagsetnln dtdaaaghvn vlffgqlker lkcdkltvei atplsikafk hmlveqnphw
       61 qswleerdvl calnqtmsss delvkagdel affppvtgg
//
LOCUS       WP_004588368             140 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Pseudoalteromonas].
ACCESSION   WP_004588368
VERSION     WP_004588368.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..140
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15031
     Region          1..138
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mnkqargftl ielmiavaiv gilasialpn yteyvkrssr aeaaaallda ankqeqyfvd
       61 nreytetfsd lgiqetteng hfklsidvgd ddntftitak pitgavkgdt dckelsitdi
      121 glkgaegtkg dsdvgycwgr
//
LOCUS       WP_004589477             647 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_004589477
VERSION     WP_004589477.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 647)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..647
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=72853
     Region          <226..644
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 magfkklifi qilswlvcva agsyfisvsf nnavseaqts aqtsvtryin sltsdelspe
       61 sikkaigdgk afssfilrdy qgaevfsvns ptqlpmfaef iqssfnsvrp qfavndaadi
      121 kveftlnier laqqlqtslf ivifisaflv iipiilmksi fhslnknism tvadvidiyi
      181 nqnqigddld taldaskmkk lgkdlvpsfn rlshflknkn ddiqnaalsi kqeaykdvit
      241 elgnrnmfve yyekhiense rstfgslalv rcselqtinq srgyqkgddy vkgvadiikh
      301 isgtytgsqv frlnssdfai vlpntplkea erfgenlqsr ftqyqqnqel ssvantgivg
      361 yekgkplgel lsvvdnamsm aqskqvnawh vqretdlvnn vsagfgnqnw rkvinevies
      421 krvhlvmqni mplgksikay aeiqvrfkte dnqvlptasf lamaekldma ieidrliids
      481 slekiksrnl sekffglnvt assahndqfv iwlerrllkd thiasklvfe vsefglqqni
      541 kaskrfidmv hrvgarvtve rfgvgltsfk ffrdlkpdfi kmdasytrgl eddknnqyfm
      601 rlmvdlahri gvsvfaegve sqeekhivet lcldgvqgyy iekpkdi
//
LOCUS       WP_004597143             385 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Rickettsia prowazekii].
ACCESSION   WP_004597143
VERSION     WP_004597143.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia prowazekii
  ORGANISM  Rickettsia prowazekii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; typhus
            group.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Rickettsia prowazekii"
                     /db_xref="taxon:782"
     Protein         1..385
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43230
     Region          3..385
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkdviliana gssslkisif aiqnkrvndk iynifleknn nkilfyinqq kesttsikdd
       61 piemminlfe ewwkkqsaln liatghrivh ggknfnkpvv vnkkvikelr vliplsplhq
      121 pynlqvldlf fqkykaishi icfdtsfhct nspitkafgl pkqyydkgim rygfhglsyq
      181 yvsshfkeit medlppkaii ahlgsgsslc aiknglslts smgfsvldgv mmatrpgnld
      241 pgvvlylinn ekmtineite llykksgllg msgessdmrt liasnshdsk favdlfvyri
      301 vleigkliaa legidclift agvgqnspvi remiskklsw lgikidyekn qknehristk
      361 gskikvfvvp tneeliiaee vmkfl
//
LOCUS       WP_004600727             357 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Corynebacterium otitidis].
ACCESSION   WP_004600727
VERSION     WP_004600727.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium otitidis
  ORGANISM  Corynebacterium otitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
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   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   4  (residues 1 to 357)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Corynebacterium otitidis"
                     /db_xref="taxon:29321"
     Protein         1..357
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=38115
     Region          1..293
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mitfdnvtkv hpngttavkd lnltveegsi tvfvgpsgcg kttslrmink mtdpsegrvi
       61 vngediadvd pvshrlgigy viqhagllph rsvldnvaqv lrlkkvpkdk araaardaie
      121 rvrlapelad rypaqlsggq qqrvgvaral aadppillmd epfsavdpvt rddlqnevlr
      181 iqkdlkktvv ivthdideal rlgdkiavfa rggvvqqyaa petlltrpan eeveqfigrd
      241 rgfralsfqp alrfpdgrei sveplgeaad garqapegwr lavgadgsae swvaedgdtf
      301 pvgtvasleg gslrstldsv lsspgpfglv vdgedrpvgt vasqdvfelv ddkagvr
//
LOCUS       WP_004600988             396 aa            linear   BCT 20-JAN-2025
DEFINITION  galactokinase [Corynebacterium otitidis].
ACCESSION   WP_004600988
VERSION     WP_004600988.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium otitidis
  ORGANISM  Corynebacterium otitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   McAuley,M., Kristiansson,H., Huang,M., Pey,A.L. and Timson,D.J.
  TITLE     Galactokinase promiscuity: a question of flexibility?
  JOURNAL   Biochem Soc Trans 44 (1), 116-122 (2016)
   PUBMED   26862196
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Holden,H.M., Thoden,J.B., Timson,D.J. and Reece,R.J.
  TITLE     Galactokinase: structure, function and role in type II galactosemia
  JOURNAL   Cell Mol Life Sci 61 (19-20), 2471-2484 (2004)
   PUBMED   15526155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Corynebacterium otitidis"
                     /db_xref="taxon:29321"
     Protein         1..396
                     /product="galactokinase"
                     /EC_number="2.7.1.6"
                     /GO_function="GO:0004335 - galactokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0005534 - galactose binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0046835 - carbohydrate phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=39324
     Region          19..396
                     /region_name="GalK"
                     /note="Galactokinase [Carbohydrate transport and
                     metabolism]; COG0153"
                     /db_xref="CDD:439923"
ORIGIN      
        1 mlagpprgde slaadaaalf raehgqapag vwaapgrvnl igehvdyaag vclptalphc
       61 tavaaaprgd grvsavslap ggrrlaesca ldevgagrpa gwlgyvagtl aalgaggcdl
      121 aivsdvpvga glsssaaltc atalaaagla gnddpdeedr rrllaaavra enhvvgantg
      181 gldqaaslla eaghavaldf agdtarlvpf dpgaaglsvl vadtrvahdh aaggygsrrg
      241 lvddvarrla aeglgfrdpg aleaavrlag pelgeelvea rvrhvveeta raaratqlaa
      301 agrlaelgel maeshrslrd ffevstgeld savdaalgag aagarltggg fggsaialcp
      361 dpeavvsaia evakrrgype prfflappsa garria
//
LOCUS       WP_004575710             812 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: Lon protease family protein [Pseudomonas].
ACCESSION   WP_004575710
VERSION     WP_004575710.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 812)
  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 812)
  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 812)
  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   4  (residues 1 to 812)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..812
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..812
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89547
     Region          2..800
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mpdpvaarlr lapealtrrf speqfaftht ddlepfrgvl gqeravealq fgvamprpgy
       61 nvyvmgepgt grfsfvkryl kaegkrqqtp adwvyvnhfd dtrepralel psgsaaefis
      121 dmgglidnll stfpavfehp syqqkkgaid rafnqrydra ldvierasle kdvalyrdas
      181 nvaftpmadg kaldeaefaq lpeevreqfh edialleerl neelaslpqw kresnnqlrq
      241 lneetitlal qpllaplsek yaenaavcay lqsvqlnllr tlveqlvdds ksdavarkll
      301 eeqyapslvv ghhadggapv vfephptydn lfgrieystd qgalytsyrq lrpgalhran
      361 ggflileaek mlgepfvwda lkralqsrkl kmespigelg rvatvslqpq viplnvklvi
      421 igsrqlyyal qdhdpdfqem frvlvdfded mpmvdenleq faqllrtrtn eegmapltsd
      481 avarlatysa rlaenqsrls arigdlfqlv seadfirqla sdemtdaghi eralkakatr
      541 tgrvsqrvld dmlagiilid tegaaigkcn gltvlevgds afgmparisa tvypggsgiv
      601 dierevnlgq pihskgvmil tgylgsryaq efplaisasi aleqsygyvd gdsaslgeac
      661 tlisalsrtp lkqcfaitgs inqfgevqav ggvnekiegf frlcearglt geqgviipra
      721 nvatlmlder vlqavengmf hvyavsqade alsllvgeea gvlddkglft egsvnarvve
      781 rlreiaemis eediekaeke rleeviaqak pa
//
LOCUS       WP_004601261             208 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Corynebacterium
            otitidis].
ACCESSION   WP_004601261
VERSION     WP_004601261.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium otitidis
  ORGANISM  Corynebacterium otitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 208)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Corynebacterium otitidis"
                     /db_xref="taxon:29321"
     Protein         1..208
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=21596
     Region          117..206
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mthennddrq qrqlplrgla lvlvavalll glwavyawts dddtpaadqa asstssssst
       61 sttssetpde dkdsrepegg deaeepaehr epeggggsge gprdqgesrp ggddlvvnvl
      121 nnstvgnlak dtadrlretg apigevgnlp eerlrltett vfftegnaaa edaarrlada
      181 lggvarphdg aldeavrgpe dvtvvlag
//
LOCUS       WP_004601432             261 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Corynebacterium
            otitidis].
ACCESSION   WP_004601432
VERSION     WP_004601432.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium otitidis
  ORGANISM  Corynebacterium otitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Corynebacterium otitidis"
                     /db_xref="taxon:29321"
     Protein         1..261
                     /product="formate/nitrite transporter family protein"
                     /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=27198
     Region          2..217
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mslndsiess vykkidlfry dfgryavrsl lagayltvgp ifatvagniv dsiapgtgpl
       61 vfallfglgf ftilvlgael atgnmmffcy gavqgrcgwl rslgvlvvnt llnlvgvviv
      121 agllglssal sdagpnhllf evvdgklskd gpelfvdaii anfvvnmafv aslyakdivn
      181 kffavvptia ifvglglenv iadfslista lfsgaelpgs vtpgnvavaw glvflgnllg
      241 gglligggyg wlnlgresyr d
//
LOCUS       WP_004601573             261 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Corynebacterium
            otitidis].
ACCESSION   WP_004601573
VERSION     WP_004601573.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium otitidis
  ORGANISM  Corynebacterium otitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Corynebacterium otitidis"
                     /db_xref="taxon:29321"
     Protein         1..261
                     /product="formate/nitrite transporter family protein"
                     /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=27022
     Region          2..256
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mslndsiaaa vakkdqlfyq dfarfairai lagaylaigt gfgvvagdav aqyapalgpv
       61 vfalffglgl fciillgael atgdmmyffy gatqrkvswl ksagvivaat llnlvgvliv
      121 alilgysakl sgagpdhllv sltegkleks pgqllaegil anfvvnmgvl gstfakdvvg
      181 kfvvivpiia mfvglglehv ianfclmltt lfaadplpds ltlgavltnw givwvgnvig
      241 gglligavys tlnkgesayr d
//
LOCUS       WP_004608701             397 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Thomasclavelia spiroformis].
ACCESSION   WP_004608701
VERSION     WP_004608701.1
KEYWORDS    RefSeq.
SOURCE      Thomasclavelia spiroformis
  ORGANISM  Thomasclavelia spiroformis
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Coprobacillaceae; Thomasclavelia.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Thomasclavelia spiroformis"
                     /db_xref="taxon:29348"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43624
     Region          3..395
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mvkvmainag ssslkfqlin mpseevitsg iverigleeg nfemkyngek ftkqcpisdh
       61 svavqlllda lvdhhvvenl heidacghri vhggeyfnds ikvdedvvak veelaelapl
      121 hnpahiigyn afknalpgve hvfvfdtafh qtldqeryly plpmeyykdl kvrkygahgt
      181 shkyvsqvan emlgkpensk iivchlgnga sisavqngvc idtsmgftpl agvmmgtrcg
      241 dvdpsimpyl cnklnktade mleiynkksg mlgvsgissd srdiedafyk gderarltss
      301 lyariaskfi gsyfvemggl daiaftagvg enasylrrli vddiadalgv vlddkanetr
      361 skenrfisse sskvkvmvip tneevmiard tirvldl
//
LOCUS       WP_004609628             482 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Thomasclavelia spiroformis].
ACCESSION   WP_004609628
VERSION     WP_004609628.1
KEYWORDS    RefSeq.
SOURCE      Thomasclavelia spiroformis
  ORGANISM  Thomasclavelia spiroformis
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Coprobacillaceae; Thomasclavelia.
REFERENCE   1  (residues 1 to 482)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Thomasclavelia spiroformis"
                     /db_xref="taxon:29348"
     Protein         1..482
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=54188
     Region          88..201
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          354..481
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(431..432,435,454..457,459)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mntgdviagk rkkrrirkef ivilslilli ifiyfigsiy fndkflrgty inaldvsglt
       61 ideankelak tiddytlelr frdgnveqls gedlqvkyne nnnvkdvlek qnsfewiqaf
      121 fskqnhtvnn lalvdenvlk eklaslqhlq tatqippeda kieyvdnkfv iknevmgsti
      181 dlekasqaii lafsegskvl dldksncyve pnvkasdeli qqqcqaanqy asaiityktr
      241 sgdvvldgne litwlsidet gkyyrddsvf kkkatefvss lakkinsvge trtfvgannr
      301 titvsggnyg vrlqnskevt gllkdiyank vgvrtpitvg keasidnggl gntfveidlk
      361 gqhmwyhkdg qiilesdivs gtyndpdrrt pagtyylynk ernrvlrgtk lpdgtwpyet
      421 pvsywmpfnk giglhdsssw rskwggtiym nsgshgcinl ptniaaqlyn nieincpvvc
      481 yy
//
LOCUS       WP_004609878             148 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Thomasclavelia spiroformis].
ACCESSION   WP_004609878
VERSION     WP_004609878.1
KEYWORDS    RefSeq.
SOURCE      Thomasclavelia spiroformis
  ORGANISM  Thomasclavelia spiroformis
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Coprobacillaceae; Thomasclavelia.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 148)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Thomasclavelia spiroformis"
                     /db_xref="taxon:29348"
     Protein         1..148
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16457
     Region          4..145
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mkekqldsll eninyeisil antsafikqe fedvswagfy lnqnkqlilg pfqgliacts
       61 ipfnkgvcga catsrkticv envhefpghi acdsasnsei vipiiidddl ygvldldsts
      121 fnrfkkddqi ileklvatlv khlkrfkc
//
LOCUS       WP_004612884             219 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Coprococcus].
ACCESSION   WP_004612884
VERSION     WP_004612884.1
KEYWORDS    RefSeq.
SOURCE      Coprococcus
  ORGANISM  Coprococcus
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Coprococcus"
                     /db_xref="taxon:33042"
     Protein         1..219
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24833
     Region          1..165
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mfidmhmhes tfskdsflkl demvelaker glgaicitdh ddmglkeyak eysektgfpi
       61 fvgieffslq gdivalgiee ypkervdaqk fidivkeqgg icfsahpfrn nnrgleenlr
      121 ivkgldgvev lngstlpean kkaadyarel glvtvgssdc hipgkigffa tyfpeevrtm
      181 edlirvfksg kckpayywng eykiwdmetp ihkpfeier
//
LOCUS       WP_004615970             279 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Ruminiclostridium
            papyrosolvens].
ACCESSION   WP_004615970
VERSION     WP_004615970.1
KEYWORDS    RefSeq.
SOURCE      Ruminiclostridium papyrosolvens
  ORGANISM  Ruminiclostridium papyrosolvens
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Ruminiclostridium.
REFERENCE   1  (residues 1 to 279)
  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 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   3  (residues 1 to 279)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 279)
  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   5  (residues 1 to 279)
  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   6  (residues 1 to 279)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Ruminiclostridium papyrosolvens"
                     /db_xref="taxon:29362"
     Protein         1..279
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32339
     Region          25..102
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..276
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mdwvrslnya idyievhlse nivcddiaqs afyssfhfqr tfslltgmtv seyvrnrrls
       61 laaqellnyd skvidvalky gydtpesfak afrrfhgvlp sqakkhgtel kafnrltlki
      121 vleggsvmdy kiekkdsfrv vtktrkftee nriisipmfw seycedglhq kvcgmfgicl
      181 pgepdckefe ygigceekyv kqipegfiti dipsytwavf kcvgampdsi qnmwrriyse
      241 wlpqskyeli pgydielyte gdiksedyis eiwipviek
//
LOCUS       WP_004617894             375 aa            linear   BCT 20-JAN-2025
DEFINITION  GerAB/ArcD/ProY family transporter [Ruminiclostridium
            papyrosolvens].
ACCESSION   WP_004617894
VERSION     WP_004617894.1
KEYWORDS    RefSeq.
SOURCE      Ruminiclostridium papyrosolvens
  ORGANISM  Ruminiclostridium papyrosolvens
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Ruminiclostridium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Ruminiclostridium papyrosolvens"
                     /db_xref="taxon:29362"
     Protein         1..375
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=42970
     Region          2..357
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 mekisknqlf climmgqigs tnlwalgiea krdawivdii stiagmglvw lytsiyskyp
       61 dknivgitqs ilgktlgwpl gfiyfmlyaf natrttsefa dlinvtflqd tpnlviqiif
      121 ylaiiyvlfl gietlgriae iifsvvifli iaiyimiias kqidfkellp vfqdgykpil
      181 kafypiginf pfglvyvffq fwkyngsvkt vkkttywala ltgvnltvsl iimvtsmgin
      241 ytsnatipfl eviklinigd iitnldaigv ilvfmggfyl tilfyysavi ifaelfhikd
      301 yrwvlvplai fimwysrvye pnypfhvkyl lpqfwqqfvp lsnvvpimll iifylkkycn
      361 kdlniknkeg sregi
//
LOCUS       WP_004619196             231 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CHAP domain-containing protein [Caulobacter].
ACCESSION   WP_004619196
VERSION     WP_004619196.1
KEYWORDS    RefSeq.
SOURCE      Caulobacter
  ORGANISM  Caulobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Caulobacter"
                     /db_xref="taxon:75"
     Protein         1..231
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24508
     Region          24..106
                     /region_name="COG3942"
                     /note="Surface antigen [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443142"
ORIGIN      
        1 mtkrtrtllg slaaaamisl vpmsganadg ywqcvpfarl msgiqifgda rtwwsqaagk
       61 ydtgsvpkig svlsfkptar mnlghvafvs qvltdrviqv thanwsiieg drgqiekdvt
      121 vvdvspngdw tqvkvwydpi rdlgttvypt ngfiypdaqa ikiamatski amaqnavvsa
      181 akqaanqvas svraspldii sqaadstdri aalieaatgg gsdnnkqnpp r
//
LOCUS       WP_004619241             290 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Ruminiclostridium
            papyrosolvens].
ACCESSION   WP_004619241
VERSION     WP_004619241.1
KEYWORDS    RefSeq.
SOURCE      Ruminiclostridium papyrosolvens
  ORGANISM  Ruminiclostridium papyrosolvens
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Ruminiclostridium.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 290)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 290)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Ruminiclostridium papyrosolvens"
                     /db_xref="taxon:29362"
     Protein         1..290
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33721
     Region          21..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..288
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mnwldkmnea icyvednlag eidfdevark accstyhfqr mfsfitevpl seyirrrrlt
       61 laafelqnss vkvielafky gyespdaftr afqnlhgvtp tsardmgvql kayprisfhi
      121 sikgdvemny rieekesfsv fgidtilskv dgecykripe fwlksiedgt verilkaadd
      181 gkqnmmlnaa myghendgty hymlchripq kgipegfvql dipkltwaif pteehtedkt
      241 sekvqaiwer iypewfpssg yqhadapefe myykvgdnky iveiwipvyk
//
LOCUS       WP_004620142             661 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Caulobacter].
ACCESSION   WP_004620142
VERSION     WP_004620142.1
KEYWORDS    RefSeq.
SOURCE      Caulobacter
  ORGANISM  Caulobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae.
REFERENCE   1  (residues 1 to 661)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 661)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 661)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 661)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 661)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 661)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..661
                     /organism="Caulobacter"
                     /db_xref="taxon:75"
     Protein         1..661
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=70847
     Region          22..661
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 magkeplavs dsspttsqtp vsaqaaphgh atgrfwplal gsvgvvfgdi gtsplyafrd
       61 alaeaardgl vrseilgvls lalwalilvv tvkyvlflmr asnngeggvl slmalaqqga
      121 rgrtrmifal gaigaalfyg dgvitpavsv lsaveglksv rgfsgwfgtq evivvslvil
      181 talftfqakg takvagifgp imvawflcig amglwhiree psvlaaispt yavgflahhg
      241 ltgfmvmgav fltvtgaeal tadmghfgrg piqvswiala lpmlalnyfg qaalaskala
      301 vaqaahqtlp nadwfflmap hqwrfglvlf sglatviasq avitgafslt qqaiqlgllp
      361 rmeikitstt eagqiyvapi nwmlfigvvl vvlsfrsssa lahaygisvt gtmvvttmla
      421 yivvrhvwkw slaaslaliv plfaldltff vanllkvltg gwaplalgag lclmmsifvs
      481 aterlrdkls kdglpfadfr emiarrptas tpgtavflts dpdttppalm hslkhfkvlh
      541 erniilkvvn etspyvqedk rietqalder fwlvtlhygy mespnipkal aacrkqglkf
      601 dimstsffvs rraivpsvap dalptwkrkl ftfltrnaad pttffhlppg rvvelgtqvs
      661 l
//
LOCUS       WP_004621279             189 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Eubacteriales].
ACCESSION   WP_004621279
VERSION     WP_004621279.1
KEYWORDS    RefSeq.
SOURCE      Eubacteriales
  ORGANISM  Eubacteriales
            Bacteria; Bacillati; Bacillota; Clostridia.
REFERENCE   1  (residues 1 to 189)
  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 189)
  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   3  (residues 1 to 189)
  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   4  (residues 1 to 189)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 189)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 189)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Eubacteriales"
                     /db_xref="taxon:186802"
     Protein         1..189
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21385
     Region          1..189
                     /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"
ORIGIN      
        1 msaggilivc skpelikeir almlqqgyss aeyslsasaa rrkldffepe lilvnsplqd
       61 elgidfildi adntdagiiv lakhehledm qyrlekvgal ilpkpinkmt llqtarfaaq
      121 srkslmglkt inedlekkmk drkiiekakw ilvekmnmte pqahryiqkr amdtrtsqlk
      181 vaeeiiqsf
//
LOCUS       WP_004621537             243 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Caulobacter].
ACCESSION   WP_004621537
VERSION     WP_004621537.1
KEYWORDS    RefSeq.
SOURCE      Caulobacter
  ORGANISM  Caulobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae.
REFERENCE   1  (residues 1 to 243)
  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 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   3  (residues 1 to 243)
  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   4  (residues 1 to 243)
  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 243)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Caulobacter"
                     /db_xref="taxon:75"
     Protein         1..243
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25858
     Region          1..243
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <140..241
                     /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 mghdltapae lsfrrygeda pphahvfdqi vlprrgvlem eidgrggrvd pgraavvapg
       61 arhafaasge nlfvvadigg almepfehlr drpfapvtga vrglldylag etpgaieagv
      121 arlwtplllr glsaappkvd prlvramami earydqsltv rdlaaeagms psrffarfae
      181 aygttphgal sdarlraaqr llsdtrlsia eiavrtghgd qsgltkrmka algvtpgawr
      241 kgr
//
LOCUS       WP_004622139             202 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Caulobacter].
ACCESSION   WP_004622139
VERSION     WP_004622139.1
KEYWORDS    RefSeq.
SOURCE      Caulobacter
  ORGANISM  Caulobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Caulobacter"
                     /db_xref="taxon:75"
     Protein         1..202
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21575
     Region          1..162
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlrrlydwvm glaasrhapl slfavsfaes sffpippdvm lapmvlakpe kawryallct
       61 iasvlggmlg waigyflrdf glwmmsitgh aggleqfqcw ygkygvwvil akgltpipyk
      121 lvtiasglaa fsfpifvaas avtraarffl vafvvkrfgp ammpvierrl alfaailigl
      181 lviglgashf lgggghggac ga
//
LOCUS       WP_004622623             397 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Ruminiclostridium papyrosolvens].
ACCESSION   WP_004622623
VERSION     WP_004622623.1
KEYWORDS    RefSeq.
SOURCE      Ruminiclostridium papyrosolvens
  ORGANISM  Ruminiclostridium papyrosolvens
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Ruminiclostridium.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Ruminiclostridium papyrosolvens"
                     /db_xref="taxon:29362"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42903
     Region          1..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkvlvinags sslkyqlidm tnetvlakgl cdrigidnsf ikqsrgseea vvlnkelknh
       61 kdaieavisa ltddkigvik nmseisavgh rivhggekfn ssvviddsvm aavrecidia
      121 plhnppniig ieacqqimpn ipmvavfdtt fhssmpdyay lyalpyelye kygirkygfh
      181 gtshkyvaer aaamlgkpls elkiitchlg ngssicavnk gksvdtsmgf tplqglamgt
      241 rsgtidpevv tflmekenld vkgisnllnk ksgvlgisgv ssdfrdlhaa adsgnsrael
      301 aieifsygvk kfigeyiavm ngvdaivfta gvgennsvvr nmivsdmdff gvkideeknk
      361 lrgqeidist adasvrtlvi ptneelaiak etvkfik
//
LOCUS       WP_004620410             304 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Ruminiclostridium
            papyrosolvens].
ACCESSION   WP_004620410
VERSION     WP_004620410.1
KEYWORDS    RefSeq.
SOURCE      Ruminiclostridium papyrosolvens
  ORGANISM  Ruminiclostridium papyrosolvens
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Ruminiclostridium.
REFERENCE   1  (residues 1 to 304)
  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 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   3  (residues 1 to 304)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 304)
  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   5  (residues 1 to 304)
  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   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Ruminiclostridium papyrosolvens"
                     /db_xref="taxon:29362"
     Protein         1..304
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35096
     Region          21..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          150..302
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mpaweqiqvt inyieghlnq eitiaalaek aglsqfyyqr lfhrlvkkpv aeyirlrrma
       61 kaadillnkk lrildialel gfethehfsr tfkntygmtp neyrknpkil nhmtktelll
      121 nyvlidegvp litdgiviei nrkhfdldvt yigfteklpl eygaglgidp gvdvlgnlwe
      181 eihsyknqlq gmvvgseevg vmlpcsengf ynyfagvrad vdnsemqsei aqwiqprgey
      241 ivcsfeaenf hflvtdalyk aqqylfstwl pnhniqteaf cleyyethtp ettkmeiwlk
      301 ikea
//
LOCUS       WP_004623494             167 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Ruminiclostridium cellobioparum].
ACCESSION   WP_004623494
VERSION     WP_004623494.1
KEYWORDS    RefSeq.
SOURCE      Ruminiclostridium cellobioparum
  ORGANISM  Ruminiclostridium cellobioparum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Ruminiclostridium.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 167)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Ruminiclostridium cellobioparum"
                     /db_xref="taxon:29355"
     Protein         1..167
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17984
     Region          9..162
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mkdinvscpe ekaemykllh sqmkallege hdmtanlana sallnevldn inwvgfyllk
       61 ndelilgpfq gkvacvriaa gkgvcgtavs enktqlvedv hrfpghiacd sasnseivip
      121 lrcegkvvgv ldidspligr fdtedasgle klagvieeac dwmqngk
//
LOCUS       WP_004624655             659 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Caulobacter].
ACCESSION   WP_004624655
VERSION     WP_004624655.1
KEYWORDS    RefSeq.
SOURCE      Caulobacter
  ORGANISM  Caulobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 659)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 659)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 659)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 659)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Caulobacter"
                     /db_xref="taxon:75"
     Protein         1..659
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=70959
     Region          28..659
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 maseassasn lddapppsei prqdgsgahg aghdpkghgf lalalgsigv vfgdigtspl
       61 yalrealahs ratassehav lgvvslvlwt mtlfvtikyv iffmradnkg eggtlalmal
      121 aqkalggggr krsvavfflg vvgaalfygd giitpaisvl saveglkdap hvgralspyi
      181 lpisagilia lflvqakgth rmaslfgpft aawflilgal galhladdps ifravnpwyg
      241 vrfllengfl gfvilgsvfl vvtgaealya dmghfgkrpi qaswlclvfp clalnylgqg
      301 alvlhhpaar hnpfwemvpg faywpvlima tiatviasqa vitgafsmtq qavqlgllpr
      361 ieikrtsetq agqifvpavn qfllvgvlal lfmfqsshkl asaygiavtg amfvdtllay
      421 vvirriwkwn laqtglllip laaldsvfia snmlkipdga wlplafggvl vlvmwtwtrg
      481 aailtaktrr dsvplidlme ilraraphra pgtaifltsd pemtpvalmh nlkhnkvlhe
      541 rnviltvrta etprvleddr vriekvnddf kkvvvtygfm espnipkala vcrkqglkfd
      601 imatsfflgr rsivpsansg mplwqdrlfi ylmknaanpt dffkippgrv velgaqvtv
//
LOCUS       WP_004627398             285 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Ruminiclostridium
            cellobioparum].
ACCESSION   WP_004627398
VERSION     WP_004627398.1
KEYWORDS    RefSeq.
SOURCE      Ruminiclostridium cellobioparum
  ORGANISM  Ruminiclostridium cellobioparum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Ruminiclostridium.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Ruminiclostridium cellobioparum"
                     /db_xref="taxon:29355"
     Protein         1..285
                     /product="formate/nitrite transporter family protein"
                     /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=30914
     Region          11..281
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mpdndtyknf nilapdqiae qtvengykka ntrvsrlfvl gilagafiaf asegsnaaiy
       61 nipwagvgkt lagaifttgl mmvivagsel ftgntlmvaa laqkritlgs mlknwitvya
      121 gnfmgavlia wlvfmsgqld ftggllggft iktaaykvsl sfskafimgi lcnwlvslav
      181 wmaygtkdma grllaiffpi wlfitsgfeh cvanmyyipa gilaksnpew vknaislgvt
      241 pekishltwg sffthnlipv tlgnlvggvv ftgmaywfvy lfrkn
//
LOCUS       WP_004628665             381 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Ralstonia].
ACCESSION   WP_004628665
VERSION     WP_004628665.1
KEYWORDS    RefSeq.
SOURCE      Ralstonia
  ORGANISM  Ralstonia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 381)
  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 381)
  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   3  (residues 1 to 381)
  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   4  (residues 1 to 381)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 381)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 381)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Ralstonia"
                     /db_xref="taxon:48736"
     Protein         1..381
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39983
     Region          30..367
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(106..108,128..129,178,230,254)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mklkqlclaa alctlaggam taasaqevik lgfaapmsgp qaqygtdmkn gatlaveefn
       61 atkpkiagkd vkfqlmaedd qadpktgtav aqklvdsgik gmlghfnsgt sipasrvynq
      121 agiaqiamat apeytkqgyk ttfrmmtsdt qqgsvvgtfa vkklgyknia ivddrtaygq
      181 gladefekaa kaagativrr eftndkasdf kailtqiksk npdavfygga egqsapllkq
      241 mrelgmkstl msgemsktdd fiklagpqaa egmvaslagl pleqmpggag ykaryekrfg
      301 tpvqtyspya ydgamalmka mvaagssdpa kylpilaatn tqgvtakhya yddkgdlkdg
      361 gitvykvtgg kwtplesvgg k
//
LOCUS       WP_004629325             403 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Ruminiclostridium
            cellobioparum].
ACCESSION   WP_004629325
VERSION     WP_004629325.1
KEYWORDS    RefSeq.
SOURCE      Ruminiclostridium cellobioparum
  ORGANISM  Ruminiclostridium cellobioparum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Ruminiclostridium.
REFERENCE   1  (residues 1 to 403)
  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 403)
  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
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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   5  (residues 1 to 403)
  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   6  (residues 1 to 403)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 403)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Ruminiclostridium cellobioparum"
                     /db_xref="taxon:29355"
     Protein         1..403
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43907
     Region          20..59
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          84..391
                     /region_name="ASKHA_ATPase_ROK_BsXylR-like"
                     /note="ATPase-like domain of Bacillus subtilis xylose
                     repressor (XylR) and similar proteins; cd24076"
                     /db_xref="CDD:466926"
ORIGIN      
        1 mklgktgnnk flkqfnetsl lelirlnkqi skadlaqltg lsptacgviv snllekgyir
       61 eagigiskgg rrpnlyelnp ksyysigvdi dvdyirfilm ditgnveyrd missrfdqsv
      121 sesiafiekk vrqiiernai redrllgvgv svpgmvdnvt hevifapnlg wervdlesmm
      181 sgmgnfpiyv dneaicsais enwigccteq rdfvcinmks gigssifadg nlyrgcsgsa
      241 geighimvdh ngpkcacgny gcletlvssr smvekaqklv rqgliadfsd eldinsinsi
      301 dfiidavkag nesarvilve aagylglava nlintinpsr ivlgkelvkf sedilehmrn
      361 ialakalkyp asrveilase lgedssalga aivplkklfg hrl
//
LOCUS       WP_004629421             305 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Ruminiclostridium
            cellobioparum].
ACCESSION   WP_004629421
VERSION     WP_004629421.1
KEYWORDS    RefSeq.
SOURCE      Ruminiclostridium cellobioparum
  ORGANISM  Ruminiclostridium cellobioparum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Ruminiclostridium.
REFERENCE   1  (residues 1 to 305)
  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   2  (residues 1 to 305)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Ruminiclostridium cellobioparum"
                     /db_xref="taxon:29355"
     Protein         1..305
                     /product="aminoglycoside 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=35899
     Region          44..260
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mdtkeskyvs yikerypqmd iskvecnftd gmhgdivivn ekdvfkfary dwsagyiene
       61 vniikligrd fsiyvpkaep vekgiarfny ikgeplyrnt lfqlgnrmqe mvaeqlamfl
      121 kqlhsiplka eriknlsecq atmsqeewlt kfeeierkvf pycdsyskey yrqifrpllq
      181 dekfmdyqpv lihgdlmpyh iifnkntnri sgiidfglsg lgdpaydvgi lldnygetfv
      241 krmsryyksi isyldrarfy afvnnllwae svsdmlvtrd ftnfripakd rdimpigtrw
      301 fdikg
//
LOCUS       WP_004629827             237 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Ruminiclostridium cellobioparum].
ACCESSION   WP_004629827
VERSION     WP_004629827.1
KEYWORDS    RefSeq.
SOURCE      Ruminiclostridium cellobioparum
  ORGANISM  Ruminiclostridium cellobioparum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Ruminiclostridium.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (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   3  (residues 1 to 237)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Ruminiclostridium cellobioparum"
                     /db_xref="taxon:29355"
     Protein         1..237
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27183
     Region          24..229
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mnakdikvgt kleveipeyd rkadesttsy isqladvidd kticivspms egrlkflsrn
       61 ltiiiyylne rqellyfkgq vkghrksgal dvfdveivse fnkiqrrrfy rldvvlncly
      121 rvidhqpist dnyqfddlsn telttaytkn isgsgfcmil eeplnsgavl disidlegsa
      181 tirvfaqvir nsseknkkfe agmhyikisp rdsdvltryi fekqrqilkn tmqaklk
//
LOCUS       WP_004630101             397 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Ruminiclostridium cellobioparum].
ACCESSION   WP_004630101
VERSION     WP_004630101.1
KEYWORDS    RefSeq.
SOURCE      Ruminiclostridium cellobioparum
  ORGANISM  Ruminiclostridium cellobioparum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Ruminiclostridium.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Ruminiclostridium cellobioparum"
                     /db_xref="taxon:29355"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42884
     Region          1..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkvlvinags sslkyqlidm tneavlakgl cdrigiensf ikqskgdeea vviskvlknh
       61 kdaiaaviaa ltdekigvik smseisavgh rivhggekfn ssavinekvm davrecidia
      121 plhnppnivg ieacqqimpd vpmvgvfdtt fhstmpdyay lyaipyelye kygirkygfh
      181 gtshkyvser aadllgkpls elkiitchlg ngssicavdk gksvdtsmgf tplqglamgt
      241 rsgtidpevv tylmekedlt vkgistllnk ksgvlgvsgv ssdfrdlhta aeegnkraql
      301 aleifaygvk kfigeyiavm ngvdaivfta gigennstir tqildnmdfl gikidpdknk
      361 irgqeidisa pgatvktfvi ptneelaiar etvrllk
//
LOCUS       WP_004630238             375 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Ruminiclostridium
            cellobioparum].
ACCESSION   WP_004630238
VERSION     WP_004630238.1
KEYWORDS    RefSeq.
SOURCE      Ruminiclostridium cellobioparum
  ORGANISM  Ruminiclostridium cellobioparum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Ruminiclostridium.
REFERENCE   1  (residues 1 to 375)
  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 375)
  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
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 375)
  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   5  (residues 1 to 375)
  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   6  (residues 1 to 375)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 375)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 375)
  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 11973032
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Ruminiclostridium cellobioparum"
                     /db_xref="taxon:29355"
     Protein         1..375
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41671
     Region          <16..>73
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
     Region          78..366
                     /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 mttgrvnsie vkkinrnaiy nflymrepis iqeiayslnm slptvtqnik elyerglvie
       61 tglfestggr kakaisynst akyavgldit rnhvgivmid lsakvirnyr klfpfvnske
      121 yfkgvghlvn sfildckiep enilgvgial pailsddsrs vsyaqvidfe ggsitafeef
      181 ipyrctfsnd anaagfaerw gdktdesvay lslnnsvggs iiigkniyng qnqrggefgh
      241 mtiapagrtc ycgqkgcvda ycsakilsds tngniaeffr llrlgkepqk siweeyvsyl
      301 vvainnlrml fdckvilggy agaymdeyld elrqkvsryn tfevdgtylh vckykletta
      361 vgaallhved fikni
//
LOCUS       WP_004624277              89 aa            linear   BCT 20-JAN-2025
DEFINITION  zinc ribbon domain-containing protein [Ruminiclostridium
            cellobioparum].
ACCESSION   WP_004624277
VERSION     WP_004624277.1
KEYWORDS    RefSeq.
SOURCE      Ruminiclostridium cellobioparum
  ORGANISM  Ruminiclostridium cellobioparum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Ruminiclostridium.
REFERENCE   1  (residues 1 to 89)
  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 10577258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Ruminiclostridium cellobioparum"
                     /db_xref="taxon:29355"
     Protein         1..89
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10164
     Region          8..88
                     /region_name="Zn_ribbon_2"
                     /note="Putative zinc ribbon domain; pfam12674"
                     /db_xref="CDD:463667"
ORIGIN      
        1 mdntqmkfcq scamplesee lqgtnadgsr ngdychycfv ngnfakeetm eemiescvpf
       61 vskgnpwpde etarksmlel fpqlkrwkk
//
LOCUS       WP_004624361             387 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Ruminiclostridium cellobioparum].
ACCESSION   WP_004624361
VERSION     WP_004624361.1
KEYWORDS    RefSeq.
SOURCE      Ruminiclostridium cellobioparum
  ORGANISM  Ruminiclostridium cellobioparum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Ruminiclostridium.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Ruminiclostridium cellobioparum"
                     /db_xref="taxon:29355"
     Protein         1..387
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43343
     Region          1..275
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          271..360
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkiihtgdwh igkivnefsm leeqkyileq lvsvverekp dalilagdif drsippveav
       61 elvdevfnml llemqvpvla iagnhdsaer lsfasriltn nglhiagifd gnvprisled
      121 ksgpvnfyll pytdprnirh iyddnqisth ddamkkvmdr igqafnssqr nimvthgyit
      181 qmgrpaeyts eserplsigg tefvnsdyfg mfdytalghl hapqkagydn vrysgsllky
      241 sfsevrqkkg vtvvelgekg naihrhidli prrdmriikg pvnelispev yksanaedyi
      301 yavltdrgel idpisklrav ypnimglsre sgsrkegskt sasqgykskt klelfrefyd
      361 siqgeplgqe aeevmakiig evekegg
//
LOCUS       WP_004631602             145 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Ralstonia].
ACCESSION   WP_004631602
VERSION     WP_004631602.1
KEYWORDS    RefSeq.
SOURCE      Ralstonia
  ORGANISM  Ralstonia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Ralstonia"
                     /db_xref="taxon:48736"
     Protein         1..145
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15310
     Region          6..144
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 maskprcqra raargftlie lmitvaivgi laiiaypsyv qyivrsnraa aesfmqevaa
       61 aqerflldnr ayapdlttlq yasnvpanvs pnytftlsas svppsyqlaa tpqgsqqand
      121 aacgtltltn tgakvastga sncwk
//
LOCUS       WP_004632261              76 aa            linear   BCT 20-JAN-2025
DEFINITION  acyl carrier protein [Gemella morbillorum].
ACCESSION   WP_004632261
VERSION     WP_004632261.1
KEYWORDS    RefSeq.
SOURCE      Gemella morbillorum
  ORGANISM  Gemella morbillorum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Gemellaceae;
            Gemella.
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   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 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   4  (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 10011594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Gemella morbillorum"
                     /db_xref="taxon:29391"
     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=8643
     Region          1..76
                     /region_name="acpP"
                     /note="acyl carrier protein; Provisional; PRK00982"
                     /db_xref="CDD:179197"
ORIGIN      
        1 maileevkei itryvkvepe kitlesklne dldadsidia dvvmdieeky gfefsdedae
       61 nivaikdlvk vieerk
//
LOCUS       WP_004632526             271 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Ralstonia].
ACCESSION   WP_004632526
VERSION     WP_004632526.1
KEYWORDS    RefSeq.
SOURCE      Ralstonia
  ORGANISM  Ralstonia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 271)
  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 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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Ralstonia"
                     /db_xref="taxon:48736"
     Protein         1..271
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31006
     Region          21..262
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          183..261
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 madtvytafr eadlrvpkga pfyfrydhfe petdiephth pwgqinrisl glmevvvdgr
       61 rltapaeyvi wvpanqphsa sirqatdfls lymaeplaqr lppmaclipq tplvralfed
      121 fatrrvtgma dewdlrqfel lvetlvragh adsylpdstd rqlepilqai rldpadtitl
      181 qqwaervhgt ertlarrfqt elgmsfvqwr nrvrllralv wlkedrsvqd ialalgygtp
      241 safiamfrkq vgvsperyrr qmcgeaerpa a
//
LOCUS       WP_004633581             156 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein [Ralstonia].
ACCESSION   WP_004633581
VERSION     WP_004633581.1
KEYWORDS    RefSeq.
SOURCE      Ralstonia
  ORGANISM  Ralstonia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Ralstonia"
                     /db_xref="taxon:48736"
     Protein         1..156
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=16612
     Region          41..120
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mqttttgtal gtgtgtgvgt tagvrmriig radsdsagpg pelmaadtle gdrvvnlnge
       61 dlgkitdiml dvqrgriaya vmsvggflgi gdklfavpws amsldvdrkc fvldankdrl
      121 eaapgfdkds wptmadptwa qsvheyygsr pyweey
//
LOCUS       WP_004634689             207 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Ralstonia].
ACCESSION   WP_004634689
VERSION     WP_004634689.1
KEYWORDS    RefSeq.
SOURCE      Ralstonia
  ORGANISM  Ralstonia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Ralstonia"
                     /db_xref="taxon:48736"
     Protein         1..207
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=22081
     Region          15..204
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mtptpnataq tppvrriiva itgasgaiyg vrllqvlegl retagveshl lmspaglmnv
       61 qhelhmaree vealahvvhn vrdigatias gsfaaeamvv apcsmktlaa vahglsdnli
      121 araadvtlke rrrlilmvre tplnlahlrn mtavtemggi vfppvpgfyq rpktiddlvd
      181 htvgrvldli glpqtlapgw rglrstd
//
LOCUS       WP_004637856             159 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Acinetobacter haemolyticus].
ACCESSION   WP_004637856
VERSION     WP_004637856.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter haemolyticus
  ORGANISM  Acinetobacter haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Acinetobacter haemolyticus"
                     /db_xref="taxon:29430"
     Protein         1..159
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17668
     Region          10..159
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 maeelvlqqg hkaeqyqsii pqiqtivege sdmianlani caalkqqfdw lwigfylvkq
       61 nelvlgpfqg piactriakg rgvcgtaweq qqvmivpdvd qfpghiacss asrseivlpi
      121 mkngecigvl didseelnqf demdaeylqq lmlmiekiv
//
LOCUS       WP_004637951             141 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Acinetobacter].
ACCESSION   WP_004637951
VERSION     WP_004637951.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 141)
  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   2  (residues 1 to 141)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..141
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15951
     Region          71..140
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mklpqlrski nfllliilgf gvishlnakq fdqsyiqwka qqqkhdqqla rqddqyylsr
       61 ptqqqnvkpv sssvnisgdk islnqanlqq lqslsgvgek kaqaiieyrq khgafkalde
      121 lmnvkgigpk lleknrsrli l
//
LOCUS       WP_004638512             333 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter haemolyticus].
ACCESSION   WP_004638512
VERSION     WP_004638512.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter haemolyticus
  ORGANISM  Acinetobacter haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 333)
  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   6  (residues 1 to 333)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Acinetobacter haemolyticus"
                     /db_xref="taxon:29430"
     Protein         1..333
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38102
     Region          25..201
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          86..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mvtnkasdag iflwmvyqtm hkmnldaaai fasvhlpdqp pdksvrrdns tqrrfwdaae
       61 kisvdsdigl hvggnvppfr gqvieylfls sptfgeglqr tiryqalltd amsfklehhd
      121 nevaiisgln hpvrhyleca igillnffky isedaftpse iwlpydkgak qdeykkiwgc
      181 nvrlgqtegr lffdaklldh pspayepell kvhehhaasq lellhkhqli heiekilasg
      241 llessefdqn ivasrldrsa rslradlqfl ntsyekviaq yrerlarrll sqtqesidqi
      301 vyltgfseps afsrafkrwt getptayrqr kqq
//
LOCUS       WP_004638917             196 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Acinetobacter].
ACCESSION   WP_004638917
VERSION     WP_004638917.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 196)
  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 196)
  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   3  (residues 1 to 196)
  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   4  (residues 1 to 196)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 196)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..196
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22440
     Region          1..191
                     /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"
ORIGIN      
        1 mpklkivlid ddqaraeyik tcliehdfdv vacftldhln ifklehlqad villdmdhph
       61 rdviescvsn fdlptvlftk ntdkntikqa idagitayiv dgiepsrlht ildisieqyk
      121 khkklegdlr daktkladrk diekakvllm qlhdlsedta fqllrknams hrmtigemar
      181 rlldaqqlln nqlkde
//
LOCUS       WP_004638928             365 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Acinetobacter calcoaceticus].
ACCESSION   WP_004638928
VERSION     WP_004638928.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..365
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39574
     Region          <73..>277
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          283..357
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 msmnnkqrwm ggvvllgggv llaalllkgn eeikqvevqp pastspktqt klkqategqm
       61 vqlqplavdv etekrlleeq rrsrekavae qearaaefla mqqqaeadaa rkaaaeyaai
      121 narrtaaqes sdnippelvg eakaknqqtn vankttdtlk ieadkkaaea krqaeaakka
      181 aeakrqaevd kkvsdakrqa eadkkaadak rqaeadkkaa eakrqaeadk kaaeakrqae
      241 adkkateakr qaeadkkasd akrkaeadkk adaekarell engdkkwmvq valaanqana
      301 dsvvsklrak gykvttsqts kgirimvgpa kdrdtadaar kkitsdssln mksawvidwv
      361 pldqr
//
LOCUS       WP_004639681             140 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acinetobacter calcoaceticus].
ACCESSION   WP_004639681
VERSION     WP_004639681.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..140
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15464
     Region          1..123
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkkyegftli elmivvaiia ilaalaypsy tqykirgnra dvqsemmqta qrlqsyyain
       61 hhytnatldn gltskdypts navyrialnv ndqtwmltat pktttiqsgn gavilnsegq
      121 kcwtkgqsct tsttsnwdgh
//
LOCUS       WP_004639683             187 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acinetobacter calcoaceticus].
ACCESSION   WP_004639683
VERSION     WP_004639683.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..187
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=20594
     Region          3..>103
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mlkqraftli elmvavviia ilaaiaypsy tryiekkdla vakqeaqria telerfkakn
       61 fsykgfdaty lynagtvipy dkttgslllp ldatsttaky tltlldstqh lplsilkdsd
      121 dketadsakv qglnwvitve rakdssgepk qannydllin sdgfrcmtkv knvvsgytnc
      181 gsssetw
//
LOCUS       WP_004640219             365 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter haemolyticus].
ACCESSION   WP_004640219
VERSION     WP_004640219.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter haemolyticus
  ORGANISM  Acinetobacter haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 365)
  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 365)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 365)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 365)
  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   5  (residues 1 to 365)
  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   6  (residues 1 to 365)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Acinetobacter haemolyticus"
                     /db_xref="taxon:29430"
     Protein         1..365
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42126
     Region          54..232
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <227..361
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mrypkgsnkr yfggqngqmp taithsiclq rfvpptilas lihyaeqkkw nykqwfeasg
       61 ldfiqiqqtn hlirfdqlcn vvrqaistyq qpclglklgs seglismgil gfamqscktv
      121 aealeialry hrisgsvlnl afriqgeice levttpkles dlkafffdel fsstiaclna
      181 mlgdhddvms lelsylptdn qqeyrnifgc svqfnsdkni mrfktsmlqr rlknyspany
      241 ataiqiceqa siqidlfnqs nfvdlldhli eqhlperfem qqaaqqlhis erhlrrqlll
      301 egwsfqkirq tvlerkakql leqnlsmsei slqlgfselr efrrafkrwt gqapsvykqt
      361 yeish
//
LOCUS       WP_004640913             391 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Acinetobacter].
ACCESSION   WP_004640913
VERSION     WP_004640913.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            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="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42350
     Region          5..388
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 maisvlvinc gsssikyali serredriyg laenlgaada rikgitigge plelsipyad
       61 hakaletlla rlanynpqai ghrvvhggtm thaerltqdt idrirhavpl aplhnpanli
      121 gieatlalfp hlpqvavfdt afhqtmpera yryalpqfly sdyqvrrygf hgtshayvse
      181 raselagqkn qggwlsahlg ngsstcaiwn gesidtsmgm tplegvvmgt rsgdvdpslp
      241 lflsnnlgwd iqkidnmlnk esgllglsdl sndmrtlvea senghegatl aievfcyrla
      301 kslsalscgl prldgliftg gigenaanir ektvaylphf glqfsveknn slargtegri
      361 dhgtgpqiwv iptdeegria ketrqvlgql n
//
LOCUS       WP_004641255             159 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acinetobacter haemolyticus].
ACCESSION   WP_004641255
VERSION     WP_004641255.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter haemolyticus
  ORGANISM  Acinetobacter haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Acinetobacter haemolyticus"
                     /db_xref="taxon:29430"
     Protein         1..159
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=17711
     Region          1..138
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkvmnrrsgf tlielmitvt iiailaviai psydiyirka dlstaqqemh kiaalleqhr
       61 trnfsyegfi lrdpvrnegp yadvdnatkt mlllplnass gkqkftlilt vdsqtwslka
      121 esqnprnysl lmtstglkck tktpanitnq scglaseew
//
LOCUS       WP_004641267             165 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Acinetobacter].
ACCESSION   WP_004641267
VERSION     WP_004641267.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..165
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=17821
     Region          1..112
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mqnnrltsaq gftlvelmiv vvivaifaai aipsyqeyvr raiaaqaqqe mqristeler
       61 skarnfnylg fpstvvlpvg atgaaiqyti tvsdgadvsr sltdsaatgq swvmrgiwkt
      121 aettnvdnfs flmtssgvrc knktkanita tnvdnatcgt greew
//
LOCUS       WP_004641298             168 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin, partial [Acinetobacter haemolyticus].
ACCESSION   WP_004641298
VERSION     WP_004641298.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter haemolyticus
  ORGANISM  Acinetobacter haemolyticus
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Acinetobacter haemolyticus"
                     /db_xref="taxon:29430"
     Protein         <1..168
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
     Region          1..167
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 gftlielmiv vaiigilaai aipayqsyti rtkvtegltl asaakaavae tfatrnsgav
       61 apyagtgpsa pgsygyeyta gqnvasiqia gignveapaa gdgiititya gqlntalvsp
      121 illtpgsgav sdvtgllaaa msqaapvvwg ctiatpasfk yvpancry
//
LOCUS       WP_004643031             358 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            calcoaceticus].
ACCESSION   WP_004643031
VERSION     WP_004643031.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 358)
  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 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   3  (residues 1 to 358)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 358)
  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   5  (residues 1 to 358)
  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   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..358
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41371
     Region          34..220
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <195..350
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtagvlhkki rdnsgskvli glvihflehv nffginreel llqgeliddk lsdsnqcval
       61 yhfermityt yntcknpvia ldffqkmdst aygvlghlvp lssnlkqaid tlkefqplig
      121 cigdisiqlr sdtvywkwdc rsddpifnrc aneynlawwv slirlvrneq fsvlkavhfk
      181 hslakpelqn yyneffgcsv yfdqpetall llpkslnmal rtgnaglyes vrifasklle
      241 qqkaeknftq qvksqiylll hkdklsrenv aeqlgvnvrt lsrklqqdgn lsystlldqv
      301 rfelainyle vhhehsvlfi skalgfytsh sfiswfkskt nltpmqyrkn knteypqy
//
LOCUS       WP_004643565             872 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Acinetobacter calcoaceticus].
ACCESSION   WP_004643565
VERSION     WP_004643565.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 872)
  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 872)
  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 872)
  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   4  (residues 1 to 872)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..872
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..872
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=97919
     Region          109..830
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mtqkldqvti stlslaktnt tnvtvnafps afeqpdikmt ldktvlkpeq lthipdfeki
       61 pastkrikpl nnflgqdrak asveagislp ysgynifavg taglgkrtmi krllqqhakt
      121 mptpddwvyv ynfkqarqpi alrfpagqgt kfqqaheqtw qiilkqlerr fsaetyhnri
      181 erirqetgdv qqqalveltk egeeldlkli srnekhgfvp vqvkddqvqe ltqndidaln
      241 skqraeiaan irymdkkldr lglhlgdled dardkvsvln rdiatqvvmp rmdlilnkyg
      301 qvkgledylk qyaqdiivnv elileqdedd yapsmfnrvp aryqanviva nkpnsgapvi
      361 fedfpthynl lghveqlthn gtiitdftli rpgslhqang gflmleaeql leqpyawqgl
      421 kralksgqlk lsslehmltl tgsisiepaa ipldikvilm aepeiyyeil eiepelgsvf
      481 kiradftdtl qrnetneqay mqliadyvqa dkllpfdrsa laalltdssr qaedqsslsl
      541 hastlgdlir eahhhafkae dkivteqhin lalqhrqyrl gylrelywqd lsrgtqliet
      601 sgyrlgqina lsvihyadve fglpsrltas vyqgggdild iersvelggs lhakgvllms
      661 sflkahfgre qilhfsaala feqsygqvdg dsatvaelsa lisaisqipi dqswaitgsm
      721 nqlgqvqpig gvnakiegfy dacklqgftg kqgviiprqn mqhlmlrqdv idavrsgqfh
      781 ihaidtidqa leilmarpvg aldkkgkysk nsiyaavmeq leywqaiedg aeieeepkkk
      841 kknkkkikkh eeltandlpq enaeevatlk qk
//
LOCUS       WP_004643423             277 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            calcoaceticus].
ACCESSION   WP_004643423
VERSION     WP_004643423.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 277)
  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 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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..277
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31966
     Region          30..270
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <166..270
                     /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 mgnwvdiskd tntgietira hftghaydph whssyligvt esgiqqfhcr kkqinshagq
       61 vfmlepeeih dghapasdgf tyqmlylhpd wlkqriqglf hnspdhyelv idaplksdeq
      121 laiitsqafq hlhykemniv kdnsldllih hiaqgkwlkk ahqsssahtp riayqirdil
      181 hdhlfedigl edmarmigld ryhihrifka tfhlaphqyl iqlrltrard llarsispaq
      241 vasdlcfadq shlsrwfkrc ygltpaayrk ictnlqd
//
LOCUS       WP_004644598             142 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Acinetobacter].
ACCESSION   WP_004644598
VERSION     WP_004644598.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..142
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15916
     Region          1..135
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mmayvllfls afgaatllpl qsetvlagff llgrhselll ilvatvgnvl gscvnwwlgi
       61 klevykdkrw fpvsekhllk aqilyakygs pmlllswvpv isdpitlvsg vlkekfttfi
      121 ilvftakflr yivvymiyle va
//
LOCUS       WP_004645633             353 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Acinetobacter].
ACCESSION   WP_004645633
VERSION     WP_004645633.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..353
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39598
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvqniek hfgafhalkn isldfpdgql vallgpsgcg kttllriiag lesadggqvi
       61 legqdatnvh vrerevgfvf qhyalfrhmt vfdniafglr vrprktrpse aeikkrvtrl
      121 ldlvqlgfla drypaqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 tlhdelhits ifvthdqeea levadqivvm nkgnveqigs prevyetpkt pfvfdflgqa
      241 nrfegqnnag iiqlgedriq fegaknaaqg evilfarpde lrihaqphdn aiqatfirel
      301 wiagkvvael ndrqgnliei lltpdearah qfrpnqtvwl savnlhlfen qva
//
LOCUS       WP_004645647             264 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Acinetobacter].
ACCESSION   WP_004645647
VERSION     WP_004645647.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..264
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29990
     Region          36..261
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mpnqnsetss qttdssnpek kryyepasqd idvdnfrkvi esrrsvrkft kkpipvevld
       61 acldlallap nssnlqpwtf yvvqnsskkk hlvkacmsql aaktaseliv ciartdride
      121 makrnvnefp fpeappaikk yykyipynyk tgylnafgnf kkvafkvart ldkqmpvsaf
      181 spadaklwat kttalacenl vlalraygfd scmmegfdep mvreilklnd eqypvmviga
      241 geraedgvff pqyrfdrelf iqkv
//
LOCUS       WP_004646283             113 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Acinetobacter].
ACCESSION   WP_004646283
VERSION     WP_004646283.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..113
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12704
     Region          6..108
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(30,61..62,64,91)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(30..31,39,42,44..45,47,50..51,53,61,66,73)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mtqtssasqe maemilavvn qipyakvaty gqiarlaglp kharlvgrvl shldsdtdip
       61 wyrvinaqak isvkqldehg qniqqqklmq egiflkgdrl dlkryqwdcl vki
//
LOCUS       WP_004636239             892 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: VirB4 family type IV secretion system protein
            [Ralstonia].
ACCESSION   WP_004636239
VERSION     WP_004636239.1
KEYWORDS    RefSeq.
SOURCE      Ralstonia
  ORGANISM  Ralstonia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 892)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 892)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..892
                     /organism="Ralstonia"
                     /db_xref="taxon:48736"
     Protein         1..892
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=101312
     Region          285..860
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mlnnptlspf dresltqiee rlagrrrsta elvpwlfkys dfmiankdsa lmvsfeftap
       61 dsnsismtvm relyehvaas lgnlsrypis lwwtvhrrld sryvtlpmpd kvaqmvdddr
      121 hanflaegny vnrhfvtfsl lpqvgldafa srvmhgvthd dlsipsalwe avratfsdqy
      181 qfaytqsele aavetfesil hgfaadnphi kmrrlagkrl ggfmhavcsp psdhiteldi
      241 petpaldqam cdteitpghd ylhfysngrq rygiatgipg krdywpsnas pktlddllki
      301 kgeltishcf rvsspsaakr fidsirkyhe gqrfdvrqll aatlrgtdmd akpgrqnktr
      361 lkaaeeantr agkvemleei ygfynftvia yspvfeetpa skglageqay kkavathnav
      421 edvlraaqfi pvretlhams afattipgmw recarwafld teavsrllpl rgvsrgsmfn
      481 ahlskqmrtr ipalaaftte ygtpfwftay lmdlghmlic grsgfgktif mllcatlfrk
      541 ypnarligfd mnlsmriptv lqggrylqfa adantvaeee ratcnpyvll ghlrhlkflv
      601 dwtvllasqr gyrpttddrk aiekairaaa trdpqfwrlr fvhaslpngp lkneldqwvg
      661 eavdalyfdn eqdgfddtqw tsiatdkilk dhavarpfls yatyriqdei eqrrlrgvia
      721 ptvvmlpeiw sllddnqfak qigewivtmr kllgcvwmda qtpeqvansp iwpairdnvl
      781 irvfvpvkdf kpdtkkayee kfgltqtqqd aikklkakrd yfitedggis rsvsvplppr
      841 teailrselq aqilfdrhmr sgepdwkery ieeataqiea dklnlddedr ha
//
LOCUS       WP_004647283             336 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004647283
VERSION     WP_004647283.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 336)
  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   6  (residues 1 to 336)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..336
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38944
     Region          27..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          82..336
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mlvlknyvgs vygglghlll dyyqlkqlev pekllaiqnl erfdfalwrd llttldqqlq
       61 rpalgleiaq lveakhlgii gylalssetl geafmryhdy hrliydggpl qlqwegdyvs
      121 igwvevpfhl ntqltdeiai almtefvkan vknphgvqly evhfqhaipk nialyeqyfg
      181 ckvrfsqarn qvlmhvsels rplkqgdqtl qkllmqqaka llekfpystl vdqqlqqail
      241 iglqknlfqi khiaeqmnfs vrqlqrhlqk qgktyqqcmq eircmlamqy lkdphlslqe
      301 tamllgyseq safqrafkqw tqltpqqwrq qnmpaa
//
LOCUS       WP_004647476             140 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Acinetobacter].
ACCESSION   WP_004647476
VERSION     WP_004647476.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 140)
  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   2  (residues 1 to 140)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..140
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15240
     Region          69..138
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkktpyrigp twinlllscw lgfisigtah atatdymewk tqqqqhdarl kkkaaatass
       61 esnhylakpa lsassaanki slnnatveql qqlngigqkk aeaiiehrqk ngkfksieei
      121 qlvkgigpal faknkaklal
//
LOCUS       WP_004647524             140 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Acinetobacter].
ACCESSION   WP_004647524
VERSION     WP_004647524.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..140
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15503
     Region          13..140
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mslfllflsa lgaatllplq seavllgllv qnkqhvvlli avaslgnilg scvnwylglk
       61 iehyknkkwf pvskdkmlka qatyqkygyw slllswvpii gdpitliagl lkenfarfll
      121 ivsvakigry lfvyaafavf
//
LOCUS       WP_004647812             429 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [Acinetobacter].
ACCESSION   WP_004647812
VERSION     WP_004647812.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..429
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=49120
     Region          3..418
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mntvavlklt lhhavvgyla gfqsgknilv ftdsfrfdqq rqtlslltsp lypqadkile
       61 ktyvthqrlh pllsnllpeg alreliaqsl kvhidnefql laalghdlpg aliatpldpe
      121 eipdeikfkl qisnpdqilk qeirtdnkfs lagvqmkfsm kakdgrftla qaiessllgd
      181 wiiktpssrh gfvplneysm mslaktvgid vpeirlvdma llqdlpplnl pqeqyafaik
      241 rfdrqstadt ielihiedfa qifgayphqk ysttnyeqig kiiyqfsdnk ildiqqfasr
      301 llvnillang dahlknwsmi yhdksaprls paydilmtsv yienerhfal nlaknkdwyl
      361 aemkhfeqwa ekvgvpwrvi ekqlhaimdk arsvwpvlll dlpmisvhke klrehwkklh
      421 pdfqiltdd
//
LOCUS       WP_004647896             426 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Acinetobacter
            bohemicus].
ACCESSION   WP_004647896
VERSION     WP_004647896.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter bohemicus
  ORGANISM  Acinetobacter bohemicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 426)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 426)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 426)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Acinetobacter bohemicus"
                     /db_xref="taxon:1435036"
     Protein         1..426
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48872
     Region          3..415
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mntvavlklt lhhgvvgyla gfqsgknilv ftdsfrfdqq retlslltsp lypqadkvle
       61 ktyvthqrlh pllsnllpeg alreliaqih idnefqllat lghdlpgali atpldpeeip
      121 deikfklqis npdqilkqei qtdnkfslag vqmkfsmkak dgrftlaqat essllgdwii
      181 ktpssrhafv plneysmmtl aktvgidvpe ihlvdmtllq dlpplnlpqe qyafaikrfd
      241 rqntanttel ihiedfaqif gayphqkyst tnyeqigkii yqfsdnkifd iqqfasrlli
      301 nillangdah lknwsmiyqd krtprlspay dilmtsvyie nerhfalnla knkdwylaem
      361 khfeqwakkv gvpwrviekq lheimdkars vwpallldlp mgsahkeklr ehwqklhpnf
      421 qiland
//
LOCUS       WP_004648225             112 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Acinetobacter bohemicus].
ACCESSION   WP_004648225
VERSION     WP_004648225.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter bohemicus
  ORGANISM  Acinetobacter bohemicus
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Acinetobacter bohemicus"
                     /db_xref="taxon:1435036"
     Protein         1..112
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12510
     Region          8..108
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(31,62..63,65,92)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(31..32,40,43,45..46,48,51..52,54,62,67,74)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mpqycstssd elarqilqvv alipygkvas ygqiaklagl pkharlvgyv lkhldqatei
       61 pwhrvinsqg kislskldhc gdniqrlkll eegvmviadk inlkqyqwmn el
//
LOCUS       WP_004648369             460 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Acinetobacter bohemicus].
ACCESSION   WP_004648369
VERSION     WP_004648369.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter bohemicus
  ORGANISM  Acinetobacter bohemicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 460)
  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 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   3  (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   4  (residues 1 to 460)
  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 460)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Acinetobacter bohemicus"
                     /db_xref="taxon:1435036"
     Protein         1..460
                     /product="CmpA/NrtA family 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=51241
     Region          39..319
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mkkillnkvf lilylvglsf llascqkepd qetaasplai ekttltigfv kltdmaplai
       61 avekgffkde glnvtleaqp swgvlyervq kdeldaahml aamplasfid pssnktpiit
      121 pftlsyngaa itvsnsvwne mkknvpmehn lpkhpisans lrpviaqykq qqkvfklgmt
      181 fptgthnyml rywlaaggih pgtydpahnn tsgnigsdvd ltvipppemi stmvegvtsg
      241 ysvgepwnqk avkkgfgvsv itsdaiweng adkvfgltqk faqqnptttl klvkaliras
      301 hwldenndtn rkeateiiaq dnyirvdkdi iansmtgvfe yepgdvrpak sfhtffkgqy
      361 gipyysdavw wltqmrrwgq istsqtdqwy letakqvyrp dlytqaaqal idegkmqvtq
      421 fptlksnafi kapqtspldq vvfdahqpnr flaafkigyk
//
LOCUS       WP_004648398             506 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Acinetobacter bohemicus].
ACCESSION   WP_004648398
VERSION     WP_004648398.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter bohemicus
  ORGANISM  Acinetobacter bohemicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Acinetobacter bohemicus"
                     /db_xref="taxon:1435036"
     Protein         1..506
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54121
     Region          7..506
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mtnlfhilql hpndniaiak ihlapqsivs eqtvtleeip aahkvaleni fqgdailryg
       61 qiigfatqdi ragehvhvhn lamadfdrdy afgenvipvi aasqsrtflg ikradgrvat
      121 rnyvgvistv ncsatvvkkv aqyfdrpemm ekypnvdgvv alshsfgcci dhhgeglkql
      181 rrtiagymeh pnfaaviivg lgceanqlkp llqsknaeya skiqslvmqe eggtqktidk
      241 aialveeilp eanqiarepl plshlcvalq cggsdgysgi tanpalgvav dhlvahggta
      301 ilsetpeiyg aehlltrrav ntevghklvd lihsweayad rekgsidnnp tpgnkagglt
      361 tilekslgav aksgstplkg vyryaetidt hglvfmdapg ydpmgatgqi agganlvaft
      421 tgrgscfgak pspsikiatn tamydrmldd mdincgnime gtssvaekgq eifemfirva
      481 sgeqskseal giggeefvpw migaqm
//
LOCUS       WP_004648752             113 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Acinetobacter].
ACCESSION   WP_004648752
VERSION     WP_004648752.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 113)
  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   3  (residues 1 to 113)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 113)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..113
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12309
     Region          2..113
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mqprmggiiq vnipdkdtly asympyvvgg glfvptkqpi klgeevfvla tlpeqsqkip
       61 ltgkviwisq kqngiklqgf gmqlsgekgi yykseaekll agiksegrss ytm
//
LOCUS       WP_004649069             831 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Acinetobacter bohemicus].
ACCESSION   WP_004649069
VERSION     WP_004649069.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter bohemicus
  ORGANISM  Acinetobacter bohemicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 831)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 831)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 831)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..831
                     /organism="Acinetobacter bohemicus"
                     /db_xref="taxon:1435036"
     Protein         1..831
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90649
     Region          61..112
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          121..831
                     /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 mkdyqakstl amairavlwg mplvvtsfts taiyaanvhp isiahtsldq alkqlaiqtg
       61 iiisydtasl skinstalkg nysvdqalal llqphqlnsv ktasggysiq aktnpaksqi
      121 pnqhqanegs vtgtdsaqla tisltanqgk slttegsgsy takattastg ltlslketpq
      181 svsvmtrqqm ddqnltqitd vanqvagltv nqsgnvgsds spiyargksv dsylldgvkl
      241 lstyssifqs qdtalfdrve vvrgstglmt gagtasasin mvrkkplpdf kasvsadvgs
      301 wnsyrtdldv ssplndsgsv rgrtvfayqn sdsyidrfne erkiaygvve tdltentqas
      361 lglsyqqiyi tgqargglpa fnsdgtrtnw srsdsaapnw sysdrattsi fadvnhqlsd
      421 hwklktslah iitesdelvg yasggtpnkd tgsgvslyst hwaykpiqnl fnitlngsfd
      481 llgqthdlvv gstltkssns qpyftnwwid gwsgtieniy ewdgntpsrp ynpavgwtke
      541 nntsssifaa ahfklnddla llvgsrlenw klkkennnyk entittttrq ennkiipyig
      601 lvydfndyws aytsytnifs pqdrktlagd yidplegnst eigikgaffd dqlnigaaiy
      661 etqednlava ipdnpngskv lapdgsqayr aesgtktrgf eleatgklsd vwqisssfsr
      721 nlskdskgnl lnpnipsnta kifttytlpy ldeaitiggg irwqseihsv drkftqseys
      781 vvdlmarykm tnnltanlnl nnifdkkyyl ttgnsyygap tnfrvglkyd w
//
LOCUS       WP_004649250             395 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Acinetobacter
            bohemicus].
ACCESSION   WP_004649250
VERSION     WP_004649250.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter bohemicus
  ORGANISM  Acinetobacter bohemicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 395)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 395)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Acinetobacter bohemicus"
                     /db_xref="taxon:1435036"
     Protein         1..395
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44391
     Region          8..385
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mntqtnlstk itvcanqael giltygsvhh yqptqetqhv sltmtqrgmd gyssralhpi
       61 faqnlpegfn rrliaeklsr yakvndmyll alqgdqgigm lsykselnlp eadslslgei
      121 lsyrsneplf pqllekyylr tslagmqpkv sipnaitvqt ditvqqrdli vksfdsefpl
      181 ltvnefvcmq aarqcglepp kaylsenlet yvverfdssn dgtklgyedf ttlmkksndp
      241 nakytgsyet llkatyiytg saaevekmyk yivfnclign gdahlknfal qysadmknif
      301 vsppfditht liyqsidnkm alklagskaf pylshlikla essqfrirnp keiiesfsen
      361 ildylrtsne vqlfdglrts iehsisniit sspnt
//
LOCUS       WP_004649618             396 aa            linear   BCT 20-JAN-2025
DEFINITION  TerD family protein [Acinetobacter bohemicus].
ACCESSION   WP_004649618
VERSION     WP_004649618.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter bohemicus
  ORGANISM  Acinetobacter bohemicus
            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 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Acinetobacter bohemicus"
                     /db_xref="taxon:1435036"
     Protein         1..396
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=44080
     Region          22..395
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mqlvaggnia laseiieili kttvpmpiel dltayllakd tqkvrgdqdm ifygqpqtpn
       61 qsvvlvqsss ndpyltqlki ntglldpeiq kvtlcatlne pnnfsriapi qvellsahqt
      121 ianaliqtqa ktekalilae vykhndkwkf rfidqgfngg lkplaenfgv vieetpsnis
      181 ptptptptps ksnlnlskik ldknnsrinl tkkgagfgki svnlnwnksg aksesffqtl
      241 trsnsidldl gamvqlkdgs idlvqplgnr fghfdqvpyi kldaddrtga singenlhin
      301 gnqwdrieri viytyiyega aqwaatdgvv tirlpdqpei evrltegnql ntcaivelkn
      361 ingeiqanre vryfkdqqfl dqfyrfgfrw tqgskd
//
LOCUS       WP_004649897             336 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter bohemicus].
ACCESSION   WP_004649897
VERSION     WP_004649897.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter bohemicus
  ORGANISM  Acinetobacter bohemicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 336)
  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   6  (residues 1 to 336)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Acinetobacter bohemicus"
                     /db_xref="taxon:1435036"
     Protein         1..336
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38543
     Region          22..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          100..336
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mgqltdasvv lrlgyqairr sglpteeilt kagvalnqve tndrtplsaq yafwvaaeev
       61 srdpdiglhl gehlplyrgq viehlfisse nfgeglkral ayqrlisdaf haklvledgr
      121 cyltngeqga wvdhlvnrhf secamsgilr ffkfitegrf npiyidfnfs qgafddeyfr
      181 vyecpvslgq ketrlyfdpa ileyqlwqae pellqlheql aleklqelar ydlvgevrra
      241 igstlesget tletvathln itprrlrtql seantsfqqi lsdyrcrlak kllantaesv
      301 erivyltgfs epstfyrafk rwtnetpvey rkrkqr
//
LOCUS       WP_004650245             264 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Acinetobacter bohemicus].
ACCESSION   WP_004650245
VERSION     WP_004650245.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter bohemicus
  ORGANISM  Acinetobacter bohemicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acinetobacter bohemicus"
                     /db_xref="taxon:1435036"
     Protein         1..264
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29585
     Region          1..257
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 miklainlsm iftevplier falaqaqgfk hveiqfpyel sieqiqsqlt mhdltlclin
       61 lpagdlmqgg dglagvpgme lefhrgleha iqyatalnvp svnilagkqp ldsdllpcln
      121 tlssnlklac hrlsahhiqp vfeminstdm prflvqniaq aqemleavqh palkmqydcy
      181 hmammgedvl ealkenihdi ghiqfadcpg rhepdtaqih faeifqwlnq saysgyiaae
      241 yrpqahsshs fawkdkyfak hpqs
//
LOCUS       WP_004651663              83 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Acinetobacter].
ACCESSION   WP_004651663
VERSION     WP_004651663.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..83
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8691
     Region          5..83
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 msqikikiea fgaverqlpq nleiicslns titdvlaqvg qaypaafami ercacavged
       61 iisrqtqlns dstlvllspv agg
//
LOCUS       WP_004651924             106 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Acinetobacter proteolyticus].
ACCESSION   WP_004651924
VERSION     WP_004651924.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter proteolyticus
  ORGANISM  Acinetobacter proteolyticus
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Acinetobacter proteolyticus"
                     /db_xref="taxon:1776741"
     Protein         1..106
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11804
     Region          3..106
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(8..9,27..28,36,39,41..42,44,47..48,50,58,63,70)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(27,58..59,61,88)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mvqdtnelhr qilevialip ygkvasygqi aklaglpkhp rlvgyvlkhl dkdseipwyr
       61 vinsqgkisv trinekgenv qqslleaegv fllngkvslk ifgwqp
//
LOCUS       WP_004652114             718 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Acinetobacter
            proteolyticus].
ACCESSION   WP_004652114
VERSION     WP_004652114.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter proteolyticus
  ORGANISM  Acinetobacter proteolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 718)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..718
                     /organism="Acinetobacter proteolyticus"
                     /db_xref="taxon:1776741"
     Protein         1..718
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=78650
     Region          31..718
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mtcsisapld fskfkpsals caitaliscv atttfaddsq snstqtleti siqaegnwle
       61 qanakkvlnh pgartvvdqq slevrgttsv kealrtvpgv qasensgtsg sdaslsigvr
      121 gltsrfsprs qlmidgvpla vapygqpqls lapttlgnme sidvvrgags vrfgpqnvgg
      181 iinfntrsip esfaasvgmt tevaengnlk vnpnlffgtt ldnglglall ysgvngdgyr
      241 dqndyanind lrlkaryald dyssieanlh ryeakvdmpg gltpaqyaqn pyqslrnhdy
      301 megnrndisl kynykkdnna fevlayhlds yrdagversg sslyqiaprd ykvtaiepry
      361 shafqlgdtl nevsvgyryl ketssesvdr anynrdtgps nfygwtkadg dteahavyvd
      421 nrtdlgawsi tpglrferik tnenmyklnr dysvlngvna sksydavlps favmykandq
      481 wnifanygks faplqysqma ntnargaylt mdglnpekad nyeigthyld dylsleftlf
      541 yidfadqlkr ddatqtysnl gatkhkgael gfkynlgain ddlanvsmya nttytkatas
      601 agqdsgneld fysnwignag vdykrdqwtf ntnvyaqsrq taagnndgtg rygnipgygi
      661 vgvraaydfa dtslsglkvg lgvknlfnhd yytrsadqvg giyagpsrty ylqtsfdf
//
LOCUS       WP_004652760             338 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            proteolyticus].
ACCESSION   WP_004652760
VERSION     WP_004652760.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter proteolyticus
  ORGANISM  Acinetobacter proteolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 338)
  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   5  (residues 1 to 338)
  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   6  (residues 1 to 338)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Acinetobacter proteolyticus"
                     /db_xref="taxon:1776741"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38957
     Region          43..201
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <178..331
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mvlsnpnqvk lvsssmlnll nyfcvennlk nakylndykt selipmgewi elledinqkk
       61 pkptlgleis kyvqpkhlgi lgyiasscen ilevlnvfik yqrlfceakp akmsisdqfi
      121 virwgadpyl knnhlidell mgvfytfldq lvhpnrievq kisfsaektk ffynyenffg
      181 cpvefesedv eiyismtsld lavsnadpvl ndilikqanl llakrpkldl fdeliqktii
      241 qavskgnisv eevanklglp arifqlklkq qgytfkerln qvrrdlafdy ladlnlsild
      301 ismllayqeq tsfirafktw tgmsplqyrk kkilnhrs
//
LOCUS       WP_004652939             331 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            proteolyticus].
ACCESSION   WP_004652939
VERSION     WP_004652939.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter proteolyticus
  ORGANISM  Acinetobacter proteolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 331)
  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   6  (residues 1 to 331)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Acinetobacter proteolyticus"
                     /db_xref="taxon:1776741"
     Protein         1..331
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37737
     Region          41..200
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <163..331
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mteipsipsv lleliakylq qnnisnfqfn elskqyahqp rmplhkwwnl lehiyqqhpt
       61 pvlghfigql aephhihilg ylalsspnli gflncfrnfq pllqnsasfs ivqkedrfcm
      121 cwtpvvhkns qlsnevllsg vlstirkilq qpeicplkie fsatapvdit pyaavygcpv
      181 sfdsdvlrlw lpleilhlpi psrdphlkkl ldqqaeallk sipnpdtflk dlqllivnml
      241 kigepsaeni akqmnlslrs fyrklsgynl qysdlvksir lelaksylvk selslteial
      301 llgyaeqsaf srafkqweni spseyrkshl s
//
LOCUS       WP_004653281              83 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Acinetobacter proteolyticus].
ACCESSION   WP_004653281
VERSION     WP_004653281.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter proteolyticus
  ORGANISM  Acinetobacter proteolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Acinetobacter proteolyticus"
                     /db_xref="taxon:1776741"
     Protein         1..83
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8922
     Region          6..83
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mqtieikiea fgaierllpk plafefaadr mvndvlahiv tlypevdham ekcacaiged
       61 iitrqtplen sctlvllspv agg
//
LOCUS       WP_004653586             292 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            proteolyticus].
ACCESSION   WP_004653586
VERSION     WP_004653586.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter proteolyticus
  ORGANISM  Acinetobacter proteolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 292)
  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 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 292)
  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   4  (residues 1 to 292)
  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 292)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Acinetobacter proteolyticus"
                     /db_xref="taxon:1776741"
     Protein         1..292
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32896
     Region          24..175
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          202..283
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mmndqtlinl flklipkegf fataidgitl mrvdhntppi avlqeptlvf vlqgqkrgyi
       61 gtetysfkqs eclivsvsmp fdcdtiaspe apmiaismkl eadtvnella ktyfenyqfk
      121 plttgmsviq ydqtisnvli rllntlrseq dvlilgdqik rellyrviqh sgadaltglv
      181 aqgnlrpiyk iceyiqhhft ekltvemlae qanmstsafh kafkqvtqyp plqylkvvrl
      241 hkakqllqna dqsvaqaaya vgyqsssqfs refkkqfgfp pkhadtntqm es
//
LOCUS       WP_004653986             352 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            proteolyticus].
ACCESSION   WP_004653986
VERSION     WP_004653986.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter proteolyticus
  ORGANISM  Acinetobacter proteolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 352)
  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 352)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 352)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 352)
  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   5  (residues 1 to 352)
  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   6  (residues 1 to 352)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Acinetobacter proteolyticus"
                     /db_xref="taxon:1776741"
     Protein         1..352
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40580
     Region          41..212
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          102..340
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mnknlnldln sakdtisnal irealsvaas rglnivnian ragisaellt sskarvpvaq
       61 caqlwvelae smndeflgmd thpmrrgsys llaklafnae tleqaiheil kflslvlddi
      121 rgelvqrgak aylilhdreh pkrmftysty lmlvhslmcw lsdqrigfhk msfrchppve
      181 iqdyrvrfce niqfnaeqnq iefdahylkh kikkdkqalk dflrhtpynl ivrfknensl
      241 slqirrqlll qppsqwdelk eiaqqlnmst atiqrrlkqe gvsyqqlknd ircdiaierl
      301 sksndsiqni sddlhfhdps afhrafkkwt gvspgsyrks spnkkkrlgh le
//
LOCUS       WP_004654157             340 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            proteolyticus].
ACCESSION   WP_004654157
VERSION     WP_004654157.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter proteolyticus
  ORGANISM  Acinetobacter proteolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 340)
  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 340)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 340)
  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   4  (residues 1 to 340)
  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 340)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Acinetobacter proteolyticus"
                     /db_xref="taxon:1776741"
     Protein         1..340
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38253
     Region          22..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          252..332
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mnpslpgtyv slmadvvqkl nisaeklleg sgvgveqlse pfwyldfdif nnllnravel
       61 tnepalgvyl glqmtvschg svglaamvsq nlgealnvme qfiglrcpal kprlevengl
      121 aslyldqpmk nfkmgivgmt flmvgfaqms naitgsklki kaelnyvepa flaqvqellp
      181 ceisfnqdnn rlifsesyla lplimadpla arlareqckh dlnklvakrg ekhpltalvr
      241 ellfdevegf fkmkevadkl hltertlqrq lakegttfqm lmdqvrerya kkllnhheys
      301 issiseklgy sdvthftraf krwanqtpkq yrnlresiss
//
LOCUS       WP_004654661             378 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Pseudomonas savastanoi].
ACCESSION   WP_004654661
VERSION     WP_004654661.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas savastanoi
  ORGANISM  Pseudomonas savastanoi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 378)
  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 378)
  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   3  (residues 1 to 378)
  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   4  (residues 1 to 378)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 378)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 378)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Pseudomonas savastanoi"
                     /db_xref="taxon:29438"
     Protein         1..378
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39872
     Region          30..365
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(104..106,127..128,177,229,254)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mshtfyrkgf laiavatalg vssfaqadvk igvagpmtga nasfgqqymk gaqaaadain
       61 aaggvngeki vlvsgddace pkqavavanr lvdndkvigv vghfcsssti pasevysdag
      121 viaitpgstn ptvterglke mfrmcgrddq qgvvagdyiv dvlkgkkvav indkdtygkg
      181 ladatakqlv argvkpvlee gltrgekdfs alvtkirstg advvyfgglh peagplvrqm
      241 reqglkdvkf msddgivtde lvttaggaqy vdgvymtfga dprvlpdska vvdqfrksgy
      301 epegytlyay asiqalaagf ngaksnkgdk aaewlkahpv ktvmgekawd akgdlkvsdy
      361 vvyqwdatgk ykqlekqk
//
LOCUS       WP_004654883             343 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            proteolyticus].
ACCESSION   WP_004654883
VERSION     WP_004654883.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter proteolyticus
  ORGANISM  Acinetobacter proteolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 343)
  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 343)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 343)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 343)
  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   5  (residues 1 to 343)
  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   6  (residues 1 to 343)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Acinetobacter proteolyticus"
                     /db_xref="taxon:1776741"
     Protein         1..343
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39138
     Region          29..208
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          98..334
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mqglakplhr rmipetyvql lfeyleaqgh dpeqilgeaw pvpdpnafag vaiehwesll
       61 niaksylndp liglhvgqti sarhlgilga vlsacdnffs aiqrferyqr lifdvvpaqi
      121 qilsdcvels wdieeyqagg lvdetgrtvm vqfgrslirg kdtlqavhfi heqpaditpy
      181 eayfgcpvlf eqpvplirfd lemlklplks pdvalvaild khadqqlanl pqveeivelv
      241 rkqiayllhq gepdiaqlsq rlylsrrtlq rrlievgtnf rkelnlvrye laksylrdpr
      301 lhvidialll gysehspftr afkqwsgqsp qqyrddlqiq tii
//
LOCUS       WP_004657303             335 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            proteolyticus].
ACCESSION   WP_004657303
VERSION     WP_004657303.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter proteolyticus
  ORGANISM  Acinetobacter proteolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 335)
  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 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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 335)
  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   5  (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   6  (residues 1 to 335)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter proteolyticus"
                     /db_xref="taxon:1776741"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38744
     Region          51..193
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          82..330
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msqlknytgs vfgglghllk ayceaenisi peqlqqvqnl erfdyviwrd lledlnrlhp
       61 ksglgleiae yvqpkhlgii aylalscenl gealsryhdf hrliydgspl vvefnhpyas
      121 irweapephp tqltdeiaia lmvqflklfm sgdtihlhev hfvnaapkni siyeqyfhck
      181 vrfeqpktql llpvseafkp lktsdhtlqq lllqqaqall dklpnstqld qrlqhailtg
      241 lqknqyqidf iaeklglsvr qlqrhlqqqn ttfqervqqv rfmlateylk dphlslqeia
      301 lllcyseqsa fqrafkiwtg qtpqqwrnnn ityns
//
LOCUS       WP_004657836             391 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Acinetobacter proteolyticus].
ACCESSION   WP_004657836
VERSION     WP_004657836.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter proteolyticus
  ORGANISM  Acinetobacter proteolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Acinetobacter proteolyticus"
                     /db_xref="taxon:1776741"
     Protein         1..391
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42329
     Region          5..388
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 maisvlvinc gsssikyali serredriyg laenlgaada rikgvtlgge plelsipyad
       61 hakaletlla rlanynpqai ghrvvhggni tkaelltpel verieaatpl aplhnpahli
      121 gieatmrlfp qlpqvavfdt afhqtmpera yryalpqyly tehqvrrygf hgtshayvte
      181 raselaghkn eggwlsahlg ngsstcavwn ghsvdtsmgm tplegvvmgt rsgdvdpslh
      241 lflasnlgwd iqkidsmlnk esgllglsgl sndmrtlvea senghegatl aievfcyrla
      301 kslsalscgl prldglvftg gigensayvr ektlgylahf glqfsqeknn alprgtegri
      361 dngtgpqiwv iptdeegria ketrqvleht i
//
LOCUS       WP_004658508             359 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Moraxellaceae].
ACCESSION   WP_004658508
VERSION     WP_004658508.1
KEYWORDS    RefSeq.
SOURCE      Moraxellaceae
  ORGANISM  Moraxellaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales.
REFERENCE   1  (residues 1 to 359)
  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 359)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 359)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 359)
  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   5  (residues 1 to 359)
  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   6  (residues 1 to 359)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Moraxellaceae"
                     /db_xref="taxon:468"
     Protein         1..359
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40618
     Region          37..214
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          113..351
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mlhpslltgl astsesanip csytrligre ldlqardlpk llkfttltae qlmrddtmit
       61 asqqiqilqn slelsasdqf glrlgqrltp sthgsmgfli nsspnllavl qafqtflptr
      121 mslirletht naewttclif feqtlshavh rllsetvavi fsecaefivg rplteaviqf
      181 shpapdhhac yadylagtyq fdqpqlsirv ptelcliana saqhdsylla mqqcemilnr
      241 lktqqhstty qvqkamlsyp lgqlseedla aalfmnkrtl arrlvkents yrlirdrils
      301 ekassylhdp qisveaiasl lnyhdsanfr rafkrwfgvs psayrrkith rqeendlre
//
LOCUS       WP_004645468             113 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Acinetobacter].
ACCESSION   WP_004645468
VERSION     WP_004645468.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 113)
  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   3  (residues 1 to 113)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 113)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..113
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12257
     Region          2..113
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mqprmggiiq atipdietlf asympyvvgg glfipskqpv klgeevfvlt tlpdqtqkip
       61 ltgkviwvsq kqngikpqgf giqlsgekgv yfkneadrlv aglksegrks ytm
//
LOCUS       WP_004659686             287 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Pseudomonas].
ACCESSION   WP_004659686
VERSION     WP_004659686.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..287
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30839
     Region          1..278
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mnvdlhchst asdgalspta lvarahengv rvlsltdhdt legleearaa ahslgmqlvn
       61 gvelsctwgg atihilgygf dtqapaltea isrlhegrwl raeeisrkla ikgmpgaleg
      121 araiqqelgd sgnaparphf adfmvragfv kdraeafrkw lgagklgdvk qhwptleetv
      181 atlrasgawv slahpshydf trskrrklvg dfvqagghai evvngmqpad qvgtlailar
      241 efgllvtags dfhgpgnwge igtyrpvped lpplwcrfkh eqptaav
//
LOCUS       WP_004659979             335 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004659979
VERSION     WP_004659979.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 335)
  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 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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 335)
  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   5  (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   6  (residues 1 to 335)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38876
     Region          51..193
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          82..330
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msqlknytgs vygglghllk aycetkniei peqlqqvqnl erfdyviwrd lledlnrlnp
       61 ktglgleiae hvqpkhlgii aylalscenl gealaryhdf hrliydgspl vvefnppyas
      121 irweapepyp tqltdeiaia lmvqflklfm sgedinlhev hfvntapkni tvyeqyfrck
      181 vrfdqpktql llpvteafkp lrtgdhtlqq lllqqaqall dklpnstqld qrlqhailtg
      241 lqknqyqidf iaeklglsvr qlqrhlqqqn ttfqervqqv rfmlateylk dphlslqeia
      301 lllcyseqsa fqrafkiwtn qtpqqwrnnn ityns
//
LOCUS       WP_004660207             152 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Acinetobacter].
ACCESSION   WP_004660207
VERSION     WP_004660207.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..152
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=16527
     Region          4..132
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 misqraftli eliivvtvia illaiaypsy tayqirtqrv naqtemldva rnlsnyklan
       61 ynyagrtvsn ifgrstiplg kplydivltd angnpltasn anvrtwllva tpksgtnqfg
      121 ngviclndqg qrfwakgasa cilsptsnwd gr
//
LOCUS       WP_004661222             356 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Acinetobacter modestus].
ACCESSION   WP_004661222
VERSION     WP_004661222.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter modestus
  ORGANISM  Acinetobacter modestus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Acinetobacter modestus"
                     /db_xref="taxon:1776740"
     Protein         1..356
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39928
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvkniek nfgafhalkn isldfpegel vallgpsgcg kttllriiag lesadngqvl
       61 legedatnih vrerqvgfvf qhyalfrhmt vfeniafglr vrpratrpse aeikkrvtrl
      121 ldlvqlgfla drypaqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 tlhdelhits ifvthdqeea levadqiivm nkgdveqigs prevyekpat pfvfdflgqa
      241 nrfegehtsg iirigddriq lptsleapqg kviafarpne lhihtrpqpn tieatfirev
      301 wiagkviael qdrsgrtiei llsveeanlh qfrpnqtvwi saaqlhlfad qttqva
//
LOCUS       WP_004661314             333 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter modestus].
ACCESSION   WP_004661314
VERSION     WP_004661314.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter modestus
  ORGANISM  Acinetobacter modestus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 333)
  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   6  (residues 1 to 333)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Acinetobacter modestus"
                     /db_xref="taxon:1776740"
     Protein         1..333
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37912
     Region          25..200
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          125..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtskktsdag iflwmvyqtm qkmnldaaai fasvhlpdqp pdkfvrrdns tqsrfwqaaa
       61 eisqdsdigl hvgsnvpafr gqvieylfls sptfgdglkr tiryqalltd amsfkllfkn
      121 ettaiisgln hpirhyleca igillnffky msentflpie iglpyldgtt qeeyfktwgc
      181 pvklgqiegy iefnndllgq sspayepell kihehhaksq lellnkhkli eqiekilasg
      241 llesgefdqn ivakhlnrsa rslradlhll ntsyekviag yrerlarrll sqtqenidqi
      301 vyltgfseps afsrafkrwt getptayrqr kqk
//
LOCUS       WP_004662384             114 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Acinetobacter].
ACCESSION   WP_004662384
VERSION     WP_004662384.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 114)
  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   3  (residues 1 to 114)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 114)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..114
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12429
     Region          2..114
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mqpqmmggii qvnipdkatl qssympfvqg gglfvstkqa vkmgqevfvl atlpeqsqki
       61 pltgkviwis hkqthfkpqg faiqlagekg vyykneaekl lagskamdrp sftm
//
LOCUS       WP_004662570             349 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter modestus].
ACCESSION   WP_004662570
VERSION     WP_004662570.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter modestus
  ORGANISM  Acinetobacter modestus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 349)
  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 349)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 349)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 349)
  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   5  (residues 1 to 349)
  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   6  (residues 1 to 349)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Acinetobacter modestus"
                     /db_xref="taxon:1776740"
     Protein         1..349
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40306
     Region          44..179
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <140..341
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mqkqqipvip sryylrliei ligthqydne vlnafhnels ktellsiqqi eqfialglsl
       61 pntedlafel gknlklsshs lvgyalmtsp nlehalrlia qyfrlimpsf klsiqfptnq
      121 hkvelllepi lqmnkqclaf hieaiavgfy ysllelagqq lqryqiylsi pepvyaeryi
      181 hlvkanfhfn ytwisgirvv idqqqlalpl pladahslkv veqrcqeqiq kiyhqgeive
      241 wvsmmlrqan qiptltecak vlnistktlq rylqqqgvef qalkqkiste raidllensn
      301 ftithiayel gysnpanftr afnkvlgcsp qsyrskhqdq ryllqdnqt
//
LOCUS       WP_004664725             337 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004664725
VERSION     WP_004664725.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 337)
  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 337)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..337
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38513
     Region          22..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          249..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msrdtisihf vnaaltgvkr lgmdvetlls hvgieaellr qpkarispeq ytrfvkmlwm
       61 vtqdehvgfd vqprrlgtfa imcqliihsk tlgqalelss qfyklfgdew svslerdkhe
      121 arlvphipka ldpdhfites mlmiwhglas wlierrlple rvhfgyerpn hadeydalff
      181 apvmqfdapr teitfaadyl dlpirqddkt leeflkaapa qllvkfkntn sltsrirdvl
      241 ksqigeempt lndvasmlyl spqtlrrrla aegksyqgvk dalrrdaaih llltpnltle
      301 dvaqqvgfse tstfhrafkk wtgvtpglyr qlhghhs
//
LOCUS       WP_004665192             257 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter modestus].
ACCESSION   WP_004665192
VERSION     WP_004665192.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter modestus
  ORGANISM  Acinetobacter modestus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 257)
  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 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
REFERENCE   3  (residues 1 to 257)
  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   4  (residues 1 to 257)
  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 257)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Acinetobacter modestus"
                     /db_xref="taxon:1776740"
     Protein         1..257
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29909
     Region          15..255
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          183..255
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mkydetekfs flngievhef lyqkddvvsp hsslwgdfnf slngtlefdi egkyylspps
       61 yglwlpphtg hqslpvehei hyicirlhpk fgrflgdvcr cfsiepffra lviqileqqk
      121 sksspeyleh llqvlfdqlk qapahshylp qsnhpvlapi lekladpeqf nmslqqvlyn
      181 ftvserhvlr lsqqelqlsl sewrnrakii fainqirqgm tikqlaytlg yhhsssfief
      241 fkrytgqtpi qlknasi
//
LOCUS       WP_004665953             115 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Pseudomonas savastanoi].
ACCESSION   WP_004665953
VERSION     WP_004665953.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas savastanoi
  ORGANISM  Pseudomonas savastanoi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (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   2  (residues 1 to 115)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Pseudomonas savastanoi"
                     /db_xref="taxon:29438"
     Protein         1..115
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12137
     Region          41..112
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mrtrifsali falltsasva vnataapsss avspatmena apaavheqrn dkvnlntada
       61 qmlqkelagi rknkadaiva yrdangefts vdelievkgi gkailernre klaid
//
LOCUS       WP_004667126             795 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pseudomonas savastanoi].
ACCESSION   WP_004667126
VERSION     WP_004667126.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas savastanoi
  ORGANISM  Pseudomonas savastanoi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 795)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 795)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 795)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..795
                     /organism="Pseudomonas savastanoi"
                     /db_xref="taxon:29438"
     Protein         1..795
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=87918
     Region          21..795
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkrslvilai iiailaggag wyvnskqpvr dgeiamshlq apvtlryder gvphiraese
       61 adlyralgya haqdrlfqme mlrrlargel aeilgpnlve tdklfrtlri rehadayvar
      121 qdkntptwka leayidgvnq yqdtharpme fdalgipkrr fttedtvsig gylaysfaaa
      181 frteplltyv rdqlgpqylk vfdldwhpdg mlgskpalas adwkglaqla qlshkalega
      241 glpqfegsna wvisgsrtqs gkpilagdph irfsvpsvwy eaqlsapgfe lyghfpglnp
      301 faflghnmdf gwsltmfqnd dvdliaektn pdnpnqvwyh gqwvdmkrte qqiavkgqap
      361 vtltllesph gpivnnvmgk nagqtpiamw wsflvsanpv ldgfyeanra dtldkmrsaa
      421 ekiqspglni vwanakgdig wwaaaqlpir pqgvnpsfil dgstaqadkl gfypfsanph
      481 eenpargyiv sanfqplspt gmqipgyynp aergqelnrq lsdstikwdl aaskalqlgt
      541 qtdyapsilk plipvlrsvv sdpdeialve rlaswkgdyp vdsvgatlfn qflfdlteet
      601 fhdelgdtmf etllstrvld aalprlaada dspwwnnrns pheesrantv kvawratvsh
      661 lrslygtnpd ewvwgkahtl tqghplgsqk pldmifnvgp yaapgthevp nnlsssirpa
      721 pwpvgygpst rrlidfadpa hslginpvgq sgvpfdkhys dqakafvsge yvpqrfsekd
      781 vaehtegvlr lvpge
//
LOCUS       WP_004667370             403 aa            linear   BCT 20-JAN-2025
DEFINITION  TerD family protein [Pseudomonas savastanoi].
ACCESSION   WP_004667370
VERSION     WP_004667370.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas savastanoi
  ORGANISM  Pseudomonas savastanoi
            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 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Pseudomonas savastanoi"
                     /db_xref="taxon:29438"
     Protein         1..403
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=42439
     Region          3..403
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mtqlvpgana pvaagpltve vsyspladad idvsafllta agkvrgdqdm cfygqksvng
       61 gavqqteasa gravfsldps rldsviekva ltatiyenka sfgsvsrlal sitggieadi
      121 ptsgmketal ilgefylrqg awkfrcvaqg faggleplak nfgvevaapq dqpapapapa
      181 papapapapa pvpapapkst vslskitldk trasisleks sagfgeirvn lnwnrrndsk
      241 gggffsmkks naidldvgcl felqdglkga vqalgnsfgs lntepfiklm gddrtgsisd
      301 gewlhingah wskirrilvy afiyegapnw ketdgvvtih apgqppievr lneeggrqgm
      361 caiallendn gavkvtrrvd fhnghsnmdk aygwgmrwaa gsk
//
LOCUS       WP_004668398             459 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Acinetobacter sp. CIP-A165].
ACCESSION   WP_004668398
VERSION     WP_004668398.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CIP-A165
  ORGANISM  Acinetobacter sp. CIP-A165
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 459)
  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 459)
  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 459)
  AUTHORS   ter Beek,J., 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 459)
  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 459)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Acinetobacter sp. CIP-A165"
                     /db_xref="taxon:40373"
     Protein         1..459
                     /product="CmpA/NrtA family 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=50008
     Region          42..318
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mshlvkstcl mmcmtaavls lsgcgkkpet atnassntat eaektnlklg fikltdmvpl
       61 aiahekgyfq deglnvqlea qsnwkvlydr vaggeldgah mlaamplgsm tgitgnkeii
      121 tpftlsynga aitvsnsvwq kmkpnltmen gkpkhpisae alkvaanesk aagkpfnlgm
      181 tfpvgthnym mrywlaagdv npgvydandt sgnkgadvml svvpppqmva tmeagttmgy
      241 cvgepwnqqa vfrkigvpva tsdqmwkdgt dkvfgmtkdf aeknptttvk vvkalirasy
      301 wldqdnnanr aeavkiisrp nyvgadeavi ansmtgtfef eagdkrpvpn fntfykgqyg
      361 ipyysdavww ltqmrrwghv petkpdqwyl dmakkayqpe iyaqaakeli aegkmkaedf
      421 pdlstatyik apetsaldgv tfdanqpnaf lasfkiglk
//
LOCUS       WP_004668474             415 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Acinetobacter
            sp. CIP-A165].
ACCESSION   WP_004668474
VERSION     WP_004668474.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CIP-A165
  ORGANISM  Acinetobacter sp. CIP-A165
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 415)
  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 415)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Acinetobacter sp. CIP-A165"
                     /db_xref="taxon:40373"
     Protein         1..415
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=48431
     Region          13..387
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 msiaqtdlak klrqitlevq glnqkkpfgs gkaavlaaiq qlgyvqidtl svvsrahhht
       61 fwtripdyqp qlldqlvaer qifeywfhaa sylsmqdfry alpqmlsikn gesryfkadp
      121 qvmhnvydki riegpqkard feslsksnss wwnwkptkia leqlfmqgdl micarngiek
      181 vydlservlp stinttppta leyaeylvkt ylraygftti kqithlkkgq ilrqnvekil
      241 sqmlegkiiq kfevdeiqti yvrtdllekt yntnhsnlcl lspfdnsiih rervrtcfdf
      301 dfrlecytpq akrkygyfcl pilfgdvfig rvdckahrks aqfelihlhi enteidialw
      361 ltpflktlhr fvifnhcqsi yisrispiel sstihefikn gwdniqfene ilttk
//
LOCUS       WP_004669167             104 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [unclassified Acinetobacter].
ACCESSION   WP_004669167
VERSION     WP_004669167.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..104
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11646
     Region          1..102
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(6..7,25..26,34,37,39..40,42,45..46,48,56,61,68)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(25,56..57,59,86)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mnehelhrqi levialipng kvasygqiak laglpkharf vgyvlkhldk dskipwhrvi
       61 naqgkisvlr indkgeniqq slleqegvyl lngkvnlkvy gwti
//
LOCUS       WP_004669483             337 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004669483
VERSION     WP_004669483.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 337)
  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 337)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..337
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38499
     Region          22..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          249..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msrdtisihf vnaaltgvkr lgmdvetlls hvgieaellr qpkarispeq ytrfvkmlwm
       61 vtqdehvgfd vqprrlgtfa imcqliihsk tlgqalelss qfyklfgdew svslerdkhe
      121 arlvphipka ldpdhfites mlmiwhglas wlierrlple rvhfgyerpn hadeydalff
      181 apvmqfdapr teitfaadyl dlpirqddks leeflkaapa qllvkfkntn sltsrirdvl
      241 ksqigeempt lndvasmlyl spqtlrrrla aegksyqgvk dalrrdaaih llltpnltle
      301 dvaqqvgfse tstfhrafkk wtgvtpglyr qlhghhs
//
LOCUS       WP_004669602             232 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [unclassified Acinetobacter].
ACCESSION   WP_004669602
VERSION     WP_004669602.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 232)
  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 232)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 232)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..232
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=25704
     Region          3..210
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Site            order(97..98,101..102,104,132,135..136,139..140,142..143,
                     165,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          97..121
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          126..159
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          164..190
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mslsddeqfd qfksfakkyg saiisgilia liaffgweyw qkktlaeaqs qtakvqklmd
       61 eanvlagqpn afatisesad kivkedansv haiqtqflla klaydkddya aaekalkkve
      121 nsavkdaglv qivklrlada qlaqkkydea lktlanvtep tfkatvdelr gdifvakkdt
      181 esarkayqsa wdslierkke rqllqikles vgvlvddpei erpildtnvd es
//
LOCUS       WP_004669606             263 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Acinetobacter sp.
            CIP-A165].
ACCESSION   WP_004669606
VERSION     WP_004669606.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CIP-A165
  ORGANISM  Acinetobacter sp. CIP-A165
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   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 263)
  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 263)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Acinetobacter sp. CIP-A165"
                     /db_xref="taxon:40373"
     Protein         1..263
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28900
     Region          24..91
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          191..252
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 meinpnshqp tgsnspsstl gniqrpgeyl rqiriaqkke leeiaremnm pvktltalek
       61 ddytslpeat fikgyyraya kylnadasai ihrfdeiyvn dtglkashal nnspikimgk
      121 lsgsnsvrnr qwlkriailv ivgllgwlav tavqnwssss kddidvpkit nsnieilpma
      181 navttsgdql vlnfsrptsv hivdstakvl atgrqastlt ltgespfqir lddatavsls
      241 lnqeqislrp ytvngkaefr lsr
//
LOCUS       WP_004670917              83 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [unclassified
            Acinetobacter].
ACCESSION   WP_004670917
VERSION     WP_004670917.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..83
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8547
     Region          6..83
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mqtveikiea fgaierllpk alafefaagq lvqdvlthvv slypesatam ekcacaiged
       61 ivarqtalas sctlvllspv agg
//
LOCUS       WP_004670823             341 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Acinetobacter].
ACCESSION   WP_004670823
VERSION     WP_004670823.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 341)
  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 341)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38408
     Region          28..211
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          255..336
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkttstrqdq gipgvyglll ldvvsrwgys detlfapfhl tseqladpny riptpianel
       61 vkhalrltge stlgfhlgtq mrisihgfig yaimtahdit daialasrfi qlrlpflqly
      121 fstfgpkatl qlqcdiqvep lrteiilglt igimtmakal tgiedlsgev dldfpepdgf
      181 dkyrdkltst vrfnqphlis sfdkkylglk mvnadpiasq iainqcetel salgerrrla
      241 mrvrdiltns eqhylsienv adrlhmsdrt lkrqlaaegt sfstlvdevr yrhatsllsr
      301 tdysleqiad elgysdvanf srafkrwsgr spsnwrkdpy l
//
LOCUS       WP_004670290             339 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter sp. CIP-A165].
ACCESSION   WP_004670290
VERSION     WP_004670290.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CIP-A165
  ORGANISM  Acinetobacter sp. CIP-A165
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 339)
  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 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 339)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 339)
  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   5  (residues 1 to 339)
  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   6  (residues 1 to 339)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Acinetobacter sp. CIP-A165"
                     /db_xref="taxon:40373"
     Protein         1..339
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38479
     Region          23..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          91..331
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msqtatalts wvkaiqkale kagcdsqell kqagldiqvl ndpnarysle qtahlwrlsv
       61 eatqdscfgl kvasqvnhht fhvlgnslnt svtlkemfgr iiryfrlvtn ipeleffskg
      121 snhyflihvp eqvqpeaida fisvfirasr alqgsdfspl rielrrsepa dletyqsilk
      181 tpiifnaakd livfetasie qpldganpel tqeydeiimr ylarfdkeni larvklklie
      241 rlstgeihqq eiakslglsi rslqrklsee kttfsellds trqelamsyi kniaysitei
      301 ayilgftdvs sfsrafrrwt nlspvkyrdn nisnqssih
//
LOCUS       WP_004671391             114 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [unclassified
            Acinetobacter].
ACCESSION   WP_004671391
VERSION     WP_004671391.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 114)
  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   3  (residues 1 to 114)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 114)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..114
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12509
     Region          2..114
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mqhqmmggii qvnipdkatl qssympfvqg gglfvptkqa vkmgqevfil atlpeqsqki
       61 pltgkviwis hkqthfkpqg faiqlagekg vyykneaekl lagskamdrp sytm
//
LOCUS       WP_004672524             142 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [unclassified Acinetobacter].
ACCESSION   WP_004672524
VERSION     WP_004672524.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..142
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16014
     Region          1..136
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 msyfllflsa fgaatllplq seavlmtlli qglsnpfyll lvatignvlg scvnwwlglk
       61 iehfkdkkwf pvsqprleqa qqiyhkygfy slllswvpvi gdpitliagi mkerfgrfll
      121 ivtiakggry lfmyalyigl fs
//
LOCUS       WP_004673022             696 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Acinetobacter sp.
            CIP-A165].
ACCESSION   WP_004673022
VERSION     WP_004673022.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CIP-A165
  ORGANISM  Acinetobacter sp. CIP-A165
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 696)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Acinetobacter sp. CIP-A165"
                     /db_xref="taxon:40373"
     Protein         1..696
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=77455
     Region          13..696
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mknrfflknp ivmsgllfgs fapmlhaeta qesktmvlpt iqvigsqdga vskipgaavi
       61 vdqeqiqkfv ptstedilkr vsgvyvkpee esavvanigm rgissadykt liledgvpva
      121 pglfvgngry ynprvqrmds ievlkgssal rygpsniggv inyrtkqpkd galvdlsigs
      181 wdtykttvel ggsspnkdsn fgailswaks dgfmdksyem kdavikagta igdnqwlgvk
      241 fthyendani syrgqflgey hakkknnpap ddwflterns fdinhrwnin adtelqtlvy
      301 wsemnrdywr ygtnaaasqa agrwiytdsl ngnnraferv gaetrlvakh alfnipseae
      361 vglrlmnekm ddvtikatra tprtgsidrd rkdsaksial yaqnrlditd hlsvtpglri
      421 eryeqerldr kqnqsvktsn tevmpglgat fqlvpeaqly asvykafspa sngdaldglk
      481 dqkldaesst nwelgvrgqk difkyeltaf rmdfkhqvip ansnsnfqqt nggktyhqgl
      541 egavsvdldg gfdafanvtw vadaqfkgdr ydskdvmtak ddnripytpe wvanlgvgys
      601 yaglrtqlsa nymgsqftdt mntrpiaent anntfftgkl nsyttvdlts rytlndqvef
      661 ygavknledk rymaslrqgi yvgpersfea gvryrf
//
LOCUS       WP_004673137             159 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acinetobacter sp. CIP-A165].
ACCESSION   WP_004673137
VERSION     WP_004673137.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CIP-A165
  ORGANISM  Acinetobacter sp. CIP-A165
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Acinetobacter sp. CIP-A165"
                     /db_xref="taxon:40373"
     Protein         1..159
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=17511
     Region          1..>93
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkamnkqsaf tlielmvtva iiailaaiai psydiyirra dlstaqqemh kvaallekhr
       61 trnfsydgfv lkgtstnkgp yfdvpnatnt tllipldttt gkqkfilnln lnsqawslka
      121 esqsprnysl lftstgikck tkttanitnq scgtesedw
//
LOCUS       WP_004676884             356 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Acinetobacter parvus].
ACCESSION   WP_004676884
VERSION     WP_004676884.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter parvus
  ORGANISM  Acinetobacter parvus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Acinetobacter parvus"
                     /db_xref="taxon:134533"
     Protein         1..356
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39747
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvkniek hfgafhalkn isldfpegel vallgpsgcg kttllriiag lesadggqvl
       61 legedatnih vrerqvgfvf qhyalfrhmt vfdniafglr vrpratrpse aeikkrvtrl
      121 ldlvqlgfla drypaqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 tlhdelhits ifvthdqeea levadqiivm nkgdveqigs prevyekpat pfvfdflgqa
      241 nrfegehtgg iirlgddriq lptaidapqg kviafarpne lhihaqpqpn tieatflrev
      301 wiagkviael qdrsgrniei llsveeanlh qfkpnqtvwi saaqlhlfad qttqva
//
LOCUS       WP_004678880             625 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Acinetobacter parvus].
ACCESSION   WP_004678880
VERSION     WP_004678880.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter parvus
  ORGANISM  Acinetobacter parvus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 625)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Acinetobacter parvus"
                     /db_xref="taxon:134533"
     Protein         1..625
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68642
     Region          2..625
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mqstakkaal pamtlaalgv vfgdigtspl yalkesfhaa hglgiqpenv lgilsiifwc
       61 lmliisikyi aivmradnng eggimallal nlrkakisds kkiyliaigf vgaslffgdg
      121 iitpaisvls aveglsiatn vldpfivpia ivivttlflm qkhgtafvgk ffgpitllwf
      181 lslgilgvis vvqtpivlgm vsphwaiqfi fthpvqaffi mgavvltvtg gealyadmgh
      241 fgprpirfgw fsvvlpclvl nyagqgalll rnpaaienpf yllvpswaly pmiilatmaa
      301 viasqavisg vfslarqaiq lgylprlgik htsdseegqi yvpflnwlll iaivililif
      361 ktssnlasay glavtltmlc dtilvavfiy yawkwslpkv mlliipffil esvlvaaasl
      421 kmfsggwvpl ligavavmil mtwkrgrelt faklehdtls ldlfvksign nvhrvpgdav
      481 fltgtpnvvp hamlhnikhn kvlhernilv tvviedvpfv pqeerisvet lnehfyriki
      541 fygfkdepnv pkaliqayee lgfeydlmqi sffisrdriv htvgdgmspw reklfismqr
      601 ntspvsdfyq iptnrvvelg sqiei
//
LOCUS       WP_004678951             410 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Acinetobacter
            parvus].
ACCESSION   WP_004678951
VERSION     WP_004678951.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter parvus
  ORGANISM  Acinetobacter parvus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Acinetobacter parvus"
                     /db_xref="taxon:134533"
     Protein         1..410
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=46432
     Region          12..370
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mntsvylpnk intihvctnq idlgvltygs vhhyqpiqek qhvsltmtkk gmdgyssgsl
       61 hpifsqnlpe gfnrrfiaek laryakvndm yllalqgdqg igmlsyksel nlpeaeslsl
      121 geilsydske plfpqlleky ylrnslagmq pkvsvpnait tqtdrtvqqr dlivksfdse
      181 fplltvnefv cmeaarkcgl eppktylsen letyvverfd ktddgirlgy edfstlmkks
      241 ndpdakytgs yeallkatyl ytgssiever mykyivfncl igngdahlkn falqyssdmk
      301 nvfvsppfdi thtliyktid nkmalklngg kefpntsdli klaqndqiki rnpkeiiesl
      361 seniidhlks snevqlfngl rasmessvsn imtsnvstks yrhdkkrkfe
//
LOCUS       WP_004679417             875 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Acinetobacter parvus].
ACCESSION   WP_004679417
VERSION     WP_004679417.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter parvus
  ORGANISM  Acinetobacter parvus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 875)
  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 875)
  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 875)
  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   4  (residues 1 to 875)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..875
                     /organism="Acinetobacter parvus"
                     /db_xref="taxon:134533"
     Protein         1..875
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=98037
     Region          106..837
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mtqkldqmta ttlsstptnt itakinsfps afeqtdiqat llktalhahq lthtpdlaei
       61 psstkrikpl nnflgqdrar asveagislp ysgynifavg taglgkrtmi krllqqhakt
      121 matpddwvyv nnfknprqpi alrfpagqgs kfqnglqqaw qiilkqlerr fsaetyhnri
      181 erirqdtgdv qqqalveltk egeeldlkli srndkhvfip mqlkdneyhe ltqndlnalt
      241 skeraeinsn mrymekkler lglhlgdled dardqvssln reiatqvvtp riesilnknk
      301 evkgldlylk hyaediidnv elileqeedd ftpalfnrvp sryqanviia nkpnsgapvi
      361 fedfpthynl lghveqlthn gtittdftli rsgslhrang gflmleaeql leqpyawqgl
      421 kralksgqlk lsslehmltl tgsisiepas vpldikvvll aepeiyyeil evepelgsvf
      481 kiradftdtl qrndsneqay mqliadyvqa dkllpfdrsa laalltdssr qaedqsslsl
      541 hastlgdlir eahhhafkad dkivtdqhvn qalhhrqyrl gylrelywqd lsrgtqliet
      601 sghrlgqina lsvihyadve fglpsrltas vyqgggdild iersvelggs lhakgvllms
      661 sflkahfgre qilhfsaala feqsygqvdg dsatvaelsa lisaicqipi dqswaitgsm
      721 nqlgqvqpig gvnakiegff dacklqgftg kqgviiprqn mqhlmlrqdv ieavqagqfh
      781 vhaidtidqa leilmarpvg tldkkgrysk nsiyaavmeq leywqaiedg eaveteqpkk
      841 kkkrkkskkd emeakaadet vvevetlntl akkrk
//
LOCUS       WP_004681602             269 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Acinetobacter parvus].
ACCESSION   WP_004681602
VERSION     WP_004681602.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter parvus
  ORGANISM  Acinetobacter parvus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Acinetobacter parvus"
                     /db_xref="taxon:134533"
     Protein         1..269
                     /product="formate/nitrite transporter family protein"
                     /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=29217
     Region          2..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msyiapsefa vkvvdagesk lhmatrdvmi raymagaila iaavfavtig iqtgvpliga
       61 llfpvgfcml yllgydlltg vfvltplawi dkrpgvtipr ilkhwgwvfl gnfagaltva
      121 vlmaavytyg fatepneign kiahigenrt igykeygfgg wmtifirgml cnwmvslgvi
      181 gamvstsvsg kfiamwmpvm lffamgfehs vvnmflfpfa mmmggdfsim dyflwneipv
      241 algnlvggla ltglalytth vktapkrsf
//
LOCUS       WP_004682172             875 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: Lon protease family protein [Acinetobacter].
ACCESSION   WP_004682172
VERSION     WP_004682172.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 875)
  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 875)
  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 875)
  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   4  (residues 1 to 875)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..875
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..875
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=98138
     Region          109..837
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mtqkldqmta ttlsstptnt itakinsfps afeqtdiqat llktalhahq lthtpdlaei
       61 psstkrikpl nnflgqdrar asveagislp ysgynifavg taglgkrtmi krllqqhakt
      121 matpddwiyv nnfknprqpi alrfpagqgs kfqnalqqaw qiilkqlerr fsaetyhnri
      181 erirqdtgdv qqqalveltk egeeldlkli srndkhvfip mqlkdneyhe ltqndlnalt
      241 skeraeinsn mrymekkler lglhlgdled dardqvssln rdiatqvvmp rielilnknk
      301 evkgldiylk qyaediidnv elileqeedd ftpalfnrvp sryqanviia nkpnsgapvi
      361 fedfpthynl lghveqlthn gtittdftli rpgslhrang gflmleaeql leqpyawqgl
      421 kralksgqlk lsslehmltl tgsisiepas vpldikvvll aepeiyyeil evepelgsvf
      481 kiradftdtl qrndsneqay mqliadyvqa dkllpfdrsa laalltdssr qaedqsslsl
      541 hastlgdlir eahhhafkad dkivtdqhvn qalhhrqyrl gylrelywqd lsrgtqliet
      601 sghrlgqina lsvihyadve fglpsrltas vyqgggdild iersvelggs lhakgvllms
      661 sflkahfgre qilhfsaala feqsygqvdg dsatvaelsa lisaicqipi dqswaitgsm
      721 nqlgqvqpig gvnakiegff dacklqgftg kqgviiprqn mqhlmlrqdv ieavqtgqfh
      781 vhaidtidqa leilmarpvg tldkkgrysk nsiyaavmeq leywqaiedg eaveteqpkk
      841 kkkrkkskkd emeakaadet vvevetlntl akkrk
//
LOCUS       WP_004683487             625 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Acinetobacter].
ACCESSION   WP_004683487
VERSION     WP_004683487.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 625)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..625
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68659
     Region          2..625
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mqstakkaal pamtlaalgv vfgdigtspl yalkesfhaa hglgiqpenv lgilsiifwc
       61 lmliisikyi aivmradnng eggimallal nlrkakisds kkiyliaigf vgaslffgdg
      121 iitpaisvls aveglsiatn vldpfivpia ivivttlflm qkhgtafvgk ffgpitllwf
      181 lslgilgvis vvqtpivlgm vsphwaiqfi fthpvqaffi mgavvltvtg gealyadmgh
      241 fgprpirfgw fsvvlpclvl nyagqgalll rnpaaienpf yllvpswaly pmiilatmaa
      301 viasqavisg vfslarqaiq lgylprlgik htsdseegqi yvpflnwlll isivililif
      361 ktssnlasay glavtltmlc dtilvavfiy yawkwslpkv mlliipffil esvlvaaasl
      421 kmfsggwvpl ligavavmil mtwkrgrelt faklehdtls ldlfvksigd nvhrvpgdav
      481 fltgtpnvvp hamlhnikhn kvlhernilv tvviedvpfv pqeerisvet lnehfyriki
      541 fygfkdepnv pkaliqayee lgfeydlmqi sffisrdriv htvgdgmspw reklfismqr
      601 ntspvsdfyq iptnrvvelg sqiei
//
LOCUS       WP_004684242             371 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Brucella].
ACCESSION   WP_004684242
VERSION     WP_004684242.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
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   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   3  (residues 1 to 371)
  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   4  (residues 1 to 371)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 371)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 371)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..371
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39255
     Region          27..358
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(99..101,122..123,172,224,248)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mrktlfsgva laaviafggs awadvlvgig ipvtgpnavy gaqiqkgaea aikevndagg
       61 ingekiaiti gddvsdpkqg isvankfaad gvkfvighfn sgvtipasqv yaengileis
      121 pgatnpqyte qglwntfrtc grddqqgtva gqyifdhfkd akiavvhdkt pygqgladet
      181 kkklnelgtk etlyegvnvg ekdfsaliak lkqagvnvvy wgglhpeagl iirqmadqgl
      241 kaqfisgdgi vsnelasiag pavegtlntf gpdprnnpdn aelvkkfrda gfepeaytly
      301 syaavqslaq aakaagsndp qevakamkek gpfktvlgdl sydekgdpkl pgyvmykwek
      361 gadgkynyiq q
//
LOCUS       WP_004685161             374 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Brucella].
ACCESSION   WP_004685161
VERSION     WP_004685161.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 374)
  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 374)
  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
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 374)
  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   5  (residues 1 to 374)
  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   6  (residues 1 to 374)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 374)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 374)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..374
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39026
     Region          7..>48
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          72..353
                     /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 msihlgmvlk ilrdegpqsr aelarrcgls attlthltaq llkdgciaet dapvlpsgsp
       61 mpgrppvsvr lvpsahyvag vhigaeavqv aicdltaqlv tsaafdhaan dnplklthqt
      121 advlrnlvqa kgislgslvg igmgvpgpvd qvrrrnllsi ntgwrdvafa dameaelnip
      181 tvvehnvtam alaeahygig qgcpavlyvy lgtglgaglv vdgmpfrpgg hgavelghiq
      241 idpqgalcac gnrgcletfv servlrerga gsaepllaal arnpalhdev aghfttalan
      301 avnlltpdli vlgghfaeap eafyarlrcd lpprvlphmr dvlrierggf gnnadavgaa
      361 avaldhlfys gvsr
//
LOCUS       WP_004685815             196 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Brucella melitensis].
ACCESSION   WP_004685815
VERSION     WP_004685815.1
KEYWORDS    RefSeq.
SOURCE      Brucella melitensis
  ORGANISM  Brucella melitensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Brucella melitensis"
                     /db_xref="taxon:29459"
     Protein         1..196
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21610
     Region          1..165
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlrrlydwti slasrkaaew wlaiiafves svflvpadvl flpmalarpe rawryaliat
       61 vasvlggiag wylgyhayeq iakpvlemyg kldtferlrg ttsadaillm litsglahlp
      121 pikvvtilsg aaginiwlfi asaivargar ffllawllrr ygesirhfie krlgliagav
      181 aavlialfla vkflht
//
LOCUS       WP_004686379             651 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Brucella melitensis].
ACCESSION   WP_004686379
VERSION     WP_004686379.1
KEYWORDS    RefSeq.
SOURCE      Brucella melitensis
  ORGANISM  Brucella melitensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 651)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 651)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 651)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 651)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Brucella melitensis"
                     /db_xref="taxon:29459"
     Protein         1..651
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=70330
     Region          28..651
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msgelngndt saqaavsags vlegaafade geqhnesmkt lvlgalgvvy gdigtspiya
       61 frealhaaat ngilarsdil gvvslifwal tlvvtvkyvl fvlradnnge ggilslmalv
      121 rgalkgrpdl ilgvgicgaa lffgdavitp aisvlsameg leivapnltp fvvpatvvil
      181 vtlfsvqklg tgrvaivfgp imalwfvalg asglwhifdd ptvmaalnpy yavrfltvsp
      241 avafvtvgav flamtgaeal yadlghfgrk pivrawlwiv fpclllnyfg qaafilshge
      301 aaalpffqmi psfalwpmvl lataatvias qavitgaysv arqavqlnil srleiqhtse
      361 klhgqiyipr vnlllglavv ilvlgfekss nlaaaygiav tgnmlvttvl lyivmtriwn
      421 wrvsralpii lgflvidmlf fsaniikvhe ggwasigiat vlvlimwtwv rgtrhlfqkt
      481 rkaevpldli veqmakrppt ivpgtavflt gdpksaptal mhslkhykvl hennviltvv
      541 taskpwvasa drarvsqyne rfmlvtltfg ymqqpnipra lglcrrlgwk fdimttsffl
      601 srrslkasvh sgmplwqdkl fillartasd ateyfqiptg rvveigtqvn i
//
LOCUS       WP_004687819             368 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Brucella neotomae].
ACCESSION   WP_004687819
VERSION     WP_004687819.1
KEYWORDS    RefSeq.
SOURCE      Brucella neotomae (Brucella melitensis biovar Neotomae)
  ORGANISM  Brucella neotomae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 368)
  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 368)
  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   3  (residues 1 to 368)
  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   4  (residues 1 to 368)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 368)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Brucella neotomae"
                     /db_xref="taxon:29460"
     Protein         1..368
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37781
     Region          26..359
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(99..101,122..123,172,224,248)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mnlkllssva faatigfasa ayaditigvi apltgpvaaf gdqvkkgaet avevinkagg
       61 ikgekvvlkf addagepkqg vsaanqivgd gikfvvgpvt tgvavpvsdv lsengvlmvt
      121 ptatgpdlta rglenvfrtc grddqqaevm adyvlknmkd kkvavihdkg aygkgladaf
      181 kaainkggit evhydsvtpg dkdfsalvtk lksagaevvy fggyhaeggl lsrqlhdagm
      241 qavvlggegl snteywaigg tnaqgtlftn akdatknpaa kdaiqalkak nipaeaftmn
      301 ayaavevika gieragstdd saavakalhd gkpietaigt ltysetgdls spsfdifkwd
      361 dgkivgle
//
LOCUS       WP_004687998             182 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit [Brucella].
ACCESSION   WP_004687998
VERSION     WP_004687998.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 182)
  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 182)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 182)
  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   4  (residues 1 to 182)
  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   5  (residues 1 to 182)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..182
                     /product="TRAP transporter small permease subunit"
                     /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=19975
     Region          4..171
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 msvllalsra idaannfigk svswlvlvav lisainavtr klfnvssnaw leaqwylfsa
       61 vfliaagytl lhsehvkvdl lysrysrrtq llveifgtif fllpfciiti ylswpiveak
      121 iasgetsnnt gglvlwpvwl lipigfslla lqgiselikr iailqgripd tvaiedaeaq
      181 al
//
LOCUS       WP_004688447             682 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Brucella neotomae].
ACCESSION   WP_004688447
VERSION     WP_004688447.1
KEYWORDS    RefSeq.
SOURCE      Brucella neotomae (Brucella melitensis biovar Neotomae)
  ORGANISM  Brucella neotomae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 682)
  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 682)
  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 682)
  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 682)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Brucella neotomae"
                     /db_xref="taxon:29460"
     Protein         1..682
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=72856
     Region          16..681
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mteeqnakla pmeldevkar eleekfdsei rfrplapvaa rivgtlliil slfhyytags
       61 gllpemihrg ihlafvlglv flvfpfsrkg ydepakpsll rplgisvidw glaiiavvav
      121 ihvplipldd lafrvgnpts tdvvlgslli lilleatrrs vgwplpiisv lfmlyalygp
      181 smpgilvhpg atvsqlvdhl ylttqgiygi algvvatyvf hfvlfgvfat riglgqlfld
      241 caawvagrfa ggpakvsifg salfgmisgs svanavtvgs ltipamirlg ykrhfaaave
      301 sasstggqit ppimgaaafl mieflnlpyt tiilaaivpa fmhffgvlmq vhfeakrtgl
      361 rgmtkeempd lkealkrdwp tiiplvvlia vllsgytpyl aafwgitlci avgllnprkr
      421 mtigevfegl rdgakyalav gaaaatvgii vgvvtltgvg fkisyivtst aaqlatyfgt
      481 ilpvswfapq tltllftlvm tgmvcilmgc gipttanyii matiaapalg llgvepivah
      541 ffvfyygvla ditppvalaa yaaagmagad pfktgntafr lglgkvlvpf vfvfspslll
      601 vtsnfnwpdf viaffgcvig italgaalsg fflvrtkiwe nvllifaaml lvapeiyssi
      661 vglilllpvv vrhlvasrrp ay
//
LOCUS       WP_004688667             280 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Brucella neotomae].
ACCESSION   WP_004688667
VERSION     WP_004688667.1
KEYWORDS    RefSeq.
SOURCE      Brucella neotomae (Brucella melitensis biovar Neotomae)
  ORGANISM  Brucella neotomae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Brucella neotomae"
                     /db_xref="taxon:29460"
     Protein         1..280
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=29109
     Region          47..131
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
     Region          175..241
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mkrllattml aamvalpafa qggtliftge kqhqpvtskn gyfvaspgql ltsdfigqpv
       61 yngpsddadn igtvndiilg adgtpqaivi gvggflgvge kdvaigcnhf swvdksggtr
      121 wlmvdadkeq lekapvfdrn aaftangasr aaektvttkk tsrvipegmk pianeglsae
      181 kligamvyda detkigtigd vlmsadgqte afvvdvggfl ginskpvais ianldvatgk
      241 dgklsvftqf tkkdlqaqpa fseaaykedp egailhgaae
//
LOCUS       WP_004688711             371 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Brucella].
ACCESSION   WP_004688711
VERSION     WP_004688711.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
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   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   3  (residues 1 to 371)
  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   4  (residues 1 to 371)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 371)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 371)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..371
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39299
     Region          27..358
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(99..101,122..123,172,224,248)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mrktlfsgva laaviafggs awadvlvgig ipvtgpnavy gaqiqkgaea aikevndagg
       61 ingekiaiti gddvsdpkqg isvankfaad gvkfvighfn ssvtipasqv yaengileis
      121 pgatnpqyte qglwntfrtc grddqqgtva gqyifdhfkd akiavihdkt pygqgladet
      181 kkklnelgtk etlyegvnvg ekdfsaliak lkqagvnvvy wgglhpeagl iirqmadqgl
      241 kaqfisgdgi vsnelasiag pavegtlntf gpdprnnpdn aelvkkfrda gfepeaytly
      301 syaavqslaq aakaagsndp qevakamkek gpfktvlgdl sydekgdpkl pgyvmykwek
      361 gadgkynyiq q
//
LOCUS       WP_004689084             514 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Brucella suis].
ACCESSION   WP_004689084
VERSION     WP_004689084.1
KEYWORDS    RefSeq.
SOURCE      Brucella suis (Brucella melitensis biovar Suis)
  ORGANISM  Brucella suis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Brucella suis"
                     /db_xref="taxon:29461"
     Protein         1..514
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54925
     Region          13..514
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mknvvaaava pviilhpsdd vavarvpvra gdpigideit areligrghk valraipagr
       61 evlkygqvig vatrdiapge hvhlqnlaml psehahqfsi dieehgmvpd aerrhfmgyd
      121 rgaggvgtrn figvissvnc satvsryiad yfnrmggldg fdnvdgvval thgsgcalnt
      181 rsegyrlltr tiqgyakhpn fggvlliglg cetnqiapil ehyrieegsr lramtiqqhg
      241 gtrktidaai geikdmlpmv naakrspqpl snlkvalecg gsdgysgisa npalgyasdl
      301 ivrnggttvl setpeiygae hlltrravtp avaekllqri dwwrdytarn gdelnnnpsy
      361 gnklggltti lekslgavak ggsmpfkavy efaetiteqg fvfmdtpgyd pvavtgqvag
      421 gcnvicfttg rgsvsgfkps pcikiatkse myehmkedmd incggivtgn etieeagari
      481 fdhilavasg qktlseiydy gdnefvpwqv gavt
//
LOCUS       WP_004689754             682 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Brucella suis].
ACCESSION   WP_004689754
VERSION     WP_004689754.1
KEYWORDS    RefSeq.
SOURCE      Brucella suis (Brucella melitensis biovar Suis)
  ORGANISM  Brucella suis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 682)
  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 682)
  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 682)
  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 682)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Brucella suis"
                     /db_xref="taxon:29461"
     Protein         1..682
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=73007
     Region          16..681
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mteeqnakla pmeldevkar eleekfdsei rfrplapvaa rivgtlliil slfhyytagf
       61 gllpemihrg ihlafvlglv flvfpfsrkg ydepakpsll rplgifvidw glaiiavvav
      121 ihvplipldd lafrvgnpts tdvvlgslli lilleatrrs vgwplpiisv lfmlyalygp
      181 smpgilvhpg atvsqlvdhl ylttqgiygi algvvatyvf hfvlfgvfat riglgqlfld
      241 caawvagrfa ggpakvsifg salfgmisgs svanaatvgs ltipamirlg ykrhfaaave
      301 sasstggqit ppimgaaafl mieflnlpyt tiilaaivpa fmhffgvlmq vhfeakrtgl
      361 rgmtkeempd lkealkrdwp tiiplvvlia vllsgytpyl aafwgitlci avgllnprkr
      421 mtigevfegl rdgakyalav gaaaatvgii vgvvtltgvg fkisyivtst aaqlatyfgt
      481 ilpvswfapq tltllftlvm tgmvcilmgc gipttanyii matiaapalg llgvepivah
      541 ffvfyygvla ditppvalaa yaaagmagad pfktgntafr lglgkvlvpf vfvfspslll
      601 vtpnfnwpdf fiaffgcvig italgaalsg fflvrtkiwe nvllifaaml lvapeiyssi
      661 vglilllpvv vrhlvasrrp ay
//
LOCUS       WP_004690421             761 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: penicillin acylase family protein [Brucella].
ACCESSION   WP_004690421
VERSION     WP_004690421.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 761)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 761)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..761
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=84437
     Region          3..760
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mnvasarpav arqinlqgls dtveidydlw giphiyahsm ddlffgngya haadrlwqmd
       61 aarrralgrf aawagkeals sdmlmrrldl atvsradyaa lspetqrmce ryaqgvnawi
      121 dsgqlpaeyr llgerperwe gwhcvlvmrq rgilmgslwf klwraaafar igpdclhllr
      181 yedggterfv vpqeqsadrw sisleelrpa ieglmklfph datgggsnnw avdarhsktg
      241 mpivagdphr ayeipgmyaq ihltcdsfdv lglsvpgvpg fphfahneem awcvthafad
      301 ihdlyvedfs glphgayrte kgtekaqhrv eaiqvrgged vqidvwttrh gplilgsped
      361 gkgialkfvq lqpgdrsldc llpmltassi tefydmmepw glidhnlvsa dkkgnigvlv
      421 rakipardrl ngwlpmpgwt gahewrgmlp ferspreenp asgivvtann rtvpddwpdy
      481 ictdchpatr akrirsrles etpfspsdml silhddvsap aaeiaqklra itpkseparh
      541 llsmlagwqg dmapnklapt aymairqemt rilarvsdla gvadteisrl ppsvspfthl
      601 wwalpdqlrr nntsllggms wdellleave tvaqtfdpqp wgdahrpifr hplagafpeq
      661 aavlaptsry vggdgdcvla tgslpqsgat aaygpvakyi wdladwdass wvvfhgasgd
      721 pasphyrdqn erwargeqvp acysrenvra nsarhlimqp s
//
LOCUS       WP_004690787             277 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phytoene/squalene synthase family protein [Brucella].
ACCESSION   WP_004690787
VERSION     WP_004690787.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..277
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30578
     Region          1..275
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mnqnethcla llreadrdry lsvlyapqek rgalaalyaf naeiarirdl vheplpgevr
       61 lqwwrdling eargsaeahl vaaalietie kyelpriafd nycearvfdl yddpmpsrnd
      121 legycgetas aliqlagfil drdaaqahae taghagvaqa vagllrllpi hrrrgqvyvp
      181 admlkaigvt rdmllssedk sateravtim lalarehlai fdkakaglpq tlhpaflpma
      241 lvpaylnave rlgaqaaqkv adisairkqw lmfranf
//
LOCUS       WP_004691202             368 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Brucella].
ACCESSION   WP_004691202
VERSION     WP_004691202.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 368)
  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 368)
  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   3  (residues 1 to 368)
  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   4  (residues 1 to 368)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 368)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..368
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37809
     Region          26..359
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(99..101,122..123,172,224,248)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mnlkllssla faatigfasa ayaditigvi apltgpvaaf gdqvkkgaet avevinkagg
       61 ikgekvvlkf addagepkqg vsaanqivgd gikfvvgpvt tgvavpvsdv lsengvlmvt
      121 ptatgpdlta rglenvfrtc grddqqaevm adyvlknmkd kkvavihdkg aygkgladaf
      181 kaainkggit evhydsvtpg dkdfsalvtk lksagaevvy fggyhaeggl lsrqlhdagm
      241 qalvlggegl snteywaigg tnaqgtlftn akdatknpaa kdaiqalkak nipaeaftmn
      301 ayaavevika gieragstdd saavakalhd gkpietaigt ltysetgdls spsfdifkwd
      361 dgkivgle
//
LOCUS       WP_004691476             143 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Acinetobacter johnsonii].
ACCESSION   WP_004691476
VERSION     WP_004691476.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter johnsonii
  ORGANISM  Acinetobacter johnsonii
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Acinetobacter johnsonii"
                     /db_xref="taxon:40214"
     Protein         1..143
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14460
     Region          2..140
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mnaqkgftli elmivvaiig ilaaiaipay qdytirarvs ealttiaplk stvseniitn
       61 nlvtspltat acsgistvta tdnvasgtca lgvvsvttta kagavtiklt ptatvtdgiv
      121 snvkwvctad kekyapascr tga
//
LOCUS       WP_004691477              91 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Acinetobacter johnsonii].
ACCESSION   WP_004691477
VERSION     WP_004691477.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter johnsonii
  ORGANISM  Acinetobacter johnsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 91)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Acinetobacter johnsonii"
                     /db_xref="taxon:40214"
     Protein         1..91
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=10399
     Region          5..>91
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mlsqynsskl trsllllday ltpnqnelit ttldiehifp kkwqdtnyng wsradtdefl
       61 eklgnkvice kklniqagng yfgikkarya q
//
LOCUS       WP_004691621             651 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Brucella].
ACCESSION   WP_004691621
VERSION     WP_004691621.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 651)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 651)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 651)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 651)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..651
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=70356
     Region          28..651
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msgelngndt saqaavsags vlegaafade geqhnesmkt lvlgalgvvy gdigtspiya
       61 frealhaaat ngilarsdil gvvslifwal tlvvtvkyvl fvlradnnge ggilslmalv
      121 rgalkgrpdl ilgvgicgaa lffgdavitp aisvlsameg leivapnltp fvvpatvvil
      181 vtlfsvqklg tgrvaivfgp imalwfvalg asglwhifdd ptvmaalnpy yavrfltvsp
      241 avafvtvgav flamtgaeal yadlghfgrk pivrawlwiv fpclllnyfg qaafilshge
      301 aaalpffqmi psfalwpmvl lataatvias qavitgaysv arqavqlnil prleiqhtse
      361 klhgqiyipr vnlllglavv ilvlgfekss nlaaaygiav tgnmlvttvl lyivmtriwn
      421 wrvsralpii lgflvidmlf fsaniikvhe ggwasigiat vlvlimwtwv rgtrhlfqkt
      481 rkaevpldli veqmakrppt ivpgtavflt gdpksaptal mhslkhykvl hennviltvv
      541 taskpwvasa drarvsqyne rfmlvtltfg ymqqpnilra lglcrrlgwk fdimttsffl
      601 srrslkasvh sgmplwqdkl fillartasd ateyfqiptg rvveigtqvn i
//
LOCUS       WP_004691985             372 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [Brucella].
ACCESSION   WP_004691985
VERSION     WP_004691985.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 372)
  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 372)
  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 372)
  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 372)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..372
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40649
     Region          38..363
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mketlsrrsf ltkgaaigaa aatsgaalat paiaaelptl rwrltsgfpn nldtiyggav
       61 ymadavskmt dgkfqiqvfq ageivpapqa idavqantve mahtcgyyft gknptfaigt
      121 alpfgmntrl qnawlyhggg nelyneflsd ygivgivggn taaqmggwyr keiksaedlk
      181 glkmriagva gevmsrlgvv pqqlpggdiy pslergtida aewvgpydde klgfyqiapy
      241 yyypafwegg asvhffinkk qyeslpeayk valntaaeaa tqnmialydv kntaairslv
      301 skgvklqplp rdvldaaykv sfdlyaeyne knpawakiyp awkkfrdegf ewfrvaeyty
      361 dsyvyaaqaa gk
//
LOCUS       WP_004692319             264 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Acinetobacter johnsonii].
ACCESSION   WP_004692319
VERSION     WP_004692319.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter johnsonii
  ORGANISM  Acinetobacter johnsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acinetobacter johnsonii"
                     /db_xref="taxon:40214"
     Protein         1..264
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29336
     Region          1..260
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mtklavnlsm iftevpller falaqaagfk hveiqfpyel sieqiqtqlt lhdlslclin
       61 vpagdlmtgg nglagvpgke lefhhalqla vqyasalkvp svnilagkqp ldadllpcln
      121 tlsknlklac hifsehdiqp vfemingtdm prflvqniaq aqemleavqh palkmqydcy
      181 hmammgedvl qglqeniqdi ghiqfadcpg rhepdtaqim yanifewlqh ssydgfiaae
      241 yrpktvstqs fawkakyfaa hpqs
//
LOCUS       WP_004693238             342 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004693238
VERSION     WP_004693238.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 342)
  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 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 342)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 342)
  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   5  (residues 1 to 342)
  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   6  (residues 1 to 342)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..342
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38818
     Region          28..208
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          92..338
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mktvslrqdq gipgvyglll ldvvsrwgyn aetlfspfql tseqlaepef ripvhtanel
       61 vklasrltge ptlgyhlgtq mrisihgfig yaimtthdig ealvlanrfi qlrmpflqlf
      121 fstfgekatl qlrcdvdiep lrtdiaisii fgivsmskal tgienlagei dfdfpepegf
      181 dryraklpnh svrfdqphll lsfdkhylgf kmvnadplas qiainqceae lsamgerrrl
      241 smrvrdiltr seqhylsieh vadllhmsdr tlkrqlaaes tsfstivdev ryrhatslls
      301 rtdysleqia delgysdvan fsrafkrwsg rspsnwrkdp yl
//
LOCUS       WP_004693849             251 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Acinetobacter].
ACCESSION   WP_004693849
VERSION     WP_004693849.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..251
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28544
     Region          23..248
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 msnttekkry fepapqdidv enfkkviqsr rsvrkftdkp ipseildecl dlallapnss
       61 nlqpwtfyvv qnpskkkqlv kaclgqlaak taselivcva rtdrvdemak lnitefpfpe
      121 appaiqkyyr fipynyktgy fnalgnfkkv afkvartldk qlpvtafnqa daklwasktt
      181 alacenlvla lraygfdscm megfdeplvr kllnlndqqy pvmvigager aedgvffpqy
      241 rfdrelfiqk v
//
LOCUS       WP_004694781             702 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Acinetobacter johnsonii].
ACCESSION   WP_004694781
VERSION     WP_004694781.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter johnsonii
  ORGANISM  Acinetobacter johnsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Acinetobacter johnsonii"
                     /db_xref="taxon:40214"
     Protein         1..702
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=76835
     Region          12..702
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mslpqfkksv lalclfpsil yaadtaptvt lnpitvqaeg nwldeanaqk vlnhagartv
       61 iqrdelinrg atsvkealrt vpgiqapena gtagsdasls igvrgltsrf sprsqvlvdg
      121 vplsfapygq sqlslaptsl gniesidvvr gagsvrfgpq nvggiinfns rtipetfagt
      181 vdltteiaen ghvkfspnlf vggtldnglg lallysgvng egfrdkndds dindirlkaa
      241 yaideyakie anlhrydadv dmpggltpaq faenpyqslr nhdymkghrt dgsvkysykk
      301 ddnafellay htdtfrdagm ersgsklyqt aprnykvtai epryshayql gttenevsvg
      361 yrylhetsee avnrasyntv tvptneyawt kadgktdaha lfidnrtdvg awslipgvrf
      421 ekikttenmy klnkdasvln gvhaeksyda vlpifsvmyk andlwnifan ygksfaplqy
      481 sqmantnasg ayltmqglqp ekannyeigt hyldpylsle ftlfyidfsd elkrddatqt
      541 ysnlgatehk gaefgfkynl gaisdelsgi slyanttytk atasagenkg qdldfysqlv
      601 gnagidykvd qwtlntnfyg qsgqtasgth datgrygnip gyglvgvras ydfsntqlng
      661 lkvgfgvknl fdreyytrsa dqvggmyvga pqtyylqtsf df
//
LOCUS       WP_004695328             410 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: exonuclease SbcCD subunit D [Veillonella].
ACCESSION   WP_004695328
VERSION     WP_004695328.1
KEYWORDS    RefSeq.
SOURCE      Veillonella
  ORGANISM  Veillonella
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Veillonella"
                     /db_xref="taxon:29465"
     Protein         1..410
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46572
     Region          1..301
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          297..382
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrflhtadwh lgrifygqyl tedqahvleh qffnilkden idgillagdi fdravppiea
       61 ielwdsiitr lamdykvpff vvsgnhdgae rlevgrsmls qsgihiwgsp hhalmpfefe
      121 gtdgkvaicp mpfseprrig ealfadveat naestdteia divtqcyeqn cesalnlhny
      181 dqmyqawsdh lykqvpkgmr siaishafvm ggevggsert lsvggseqvn pqvfkdfhyt
      241 alghlhgpqr mgadyirysg splkysfdeh mqkksftiid mdtkgnvdis tipveakrdv
      301 vilegyfedl lndkalqakh rddyvqarll dtmpimdgma klrqvyhrcm tidlvgrvag
      361 pvadmgeaif kelnerdlfn qfaetvwkep ltekeqqyin svwdrilked
//
LOCUS       WP_004695134             336 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004695134
VERSION     WP_004695134.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 336)
  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   6  (residues 1 to 336)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..336
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38508
     Region          22..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          102..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msrdtisihf vnaaltgvkr lgmdvetlls hvgieaellr qpkarispeq ytrfvkmlwm
       61 vtqdehvgfd kqprrlgtfa imcqliihak tlgdalelss qfyklfgdew svtlerdkhe
      121 arlvpqipks mdpdhfites mlmiwhglas wlierrlple rvhfgyerpt hadeydalff
      181 apvmqfdmpr teitfaadyl dlpirqneet leeflkaapa qllvkfkntn sltsrirdvl
      241 ksqigeempt lndvasmlyl spqtlrrrla aegksyqgvk dalrrdaaih lllnpgltle
      301 dvaqqvgfse tstfhrafkk wtgvtpglyr qlhgyh
//
LOCUS       WP_004696461             401 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Veillonella].
ACCESSION   WP_004696461
VERSION     WP_004696461.1
KEYWORDS    RefSeq.
SOURCE      Veillonella
  ORGANISM  Veillonella
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Veillonella"
                     /db_xref="taxon:29465"
     Protein         1..401
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43760
     Region          1..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mnvlvvncgs sslkyqlldm ttetelakgl fekigdqdai fthkrpnadk lervepilnh
       61 kealrilldi lvdaefgvis smdeidavgh rvvhggekfa dsvlitpavm ealeecasla
      121 plhnppniqg ieaceaimps vpqvavfdta fhqtmpkeay myalpysyye dygirrygfh
      181 gtshkyvaqr caelmgkhmt dlriitchlg ngssvaaikg grsidttmgf tplsglimgt
      241 rtgdidpaiv pflmektgmt yeeidrvmnk esgvlgisgv sndfrvieea aangnkraql
      301 alnmfhykvr rvigafaavm ggvdaiifta gigengignr daicngleyl gtridsernn
      361 vrgkeqeisa egskvkifvi ptneeimiar dtqritaalk k
//
LOCUS       WP_004696311             195 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Acinetobacter].
ACCESSION   WP_004696311
VERSION     WP_004696311.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 195)
  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 195)
  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   3  (residues 1 to 195)
  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   4  (residues 1 to 195)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 195)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..195
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22194
     Region          1..191
                     /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"
ORIGIN      
        1 mpklkialid dnqeraqyir ssliehdfdv vacliidhin isrleqlsad villdmdhpq
       61 rdiiescvsq fnlptvlftk nshkdtiksa idagvtayiv dgidpsklen ileisieqfr
      121 khkklltdlq dtknkladrk dverakvllm qlhglsedda fqllrknams hrmtigemar
      181 rlldaqqllq sqlkd
//
LOCUS       WP_004697676             258 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Acinetobacter].
ACCESSION   WP_004697676
VERSION     WP_004697676.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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
REFERENCE   2  (residues 1 to 258)
  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 258)
  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 258)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..258
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28105
     Region          21..88
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          186..249
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mevnpnspqs ngssnalgni qrpgdylrqi ritqkrelsd vakelniplk tltaleqdey
       61 talpeatfik gyyrtyakfl kvdattiiqr fddiyandtg llpnhalnns pikimgklpg
      121 snrdrnrkwl krgliaivvi ailaalfgmi qnwsgstdea atpqtesdvq iinmngaaat
      181 tgdqlklefn rptsvhivds tgkvlatgrq astlelaget pfqiriddaa avslslnnes
      241 islspytvgg kadfrlsr
//
LOCUS       WP_004697681             232 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Acinetobacter johnsonii].
ACCESSION   WP_004697681
VERSION     WP_004697681.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter johnsonii
  ORGANISM  Acinetobacter johnsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 232)
  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 232)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 232)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Acinetobacter johnsonii"
                     /db_xref="taxon:40214"
     Protein         1..232
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=25602
     Region          4..209
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Site            order(96..97,100..101,103,131,134..135,138..139,141..142,
                     164,167..168,171..172,175)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          96..124
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          129..157
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          163..189
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msalsdeeql dslksftkky gsaiisgili aliaffgwqy wqkktlaqnq mntakvqqlm
       61 dearatqgda ftalsatadk ivkeapdsaq aiqtqllmak laydkadyas aekalkkven
      121 skvdddglvq ivklrlayaq laqkkfddai knlalvkdpa fkatadealg dvyvakndie
      181 nakkayqsaw dqlverkqer qilqiklesv gilvddpeie rplietaaee te
//
LOCUS       WP_004697783             340 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter johnsonii].
ACCESSION   WP_004697783
VERSION     WP_004697783.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter johnsonii
  ORGANISM  Acinetobacter johnsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 340)
  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 340)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 340)
  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   4  (residues 1 to 340)
  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 340)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Acinetobacter johnsonii"
                     /db_xref="taxon:40214"
     Protein         1..340
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39235
     Region          55..207
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          256..331
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqelqipngy fqlwnmylie qgidfhqlgf laqyryeleh vlqlpidtqs pfsffqtilq
       61 ltreqldcpq limemakfiq pkhfgvlgym atrsnsvaea lsyvmrfsrl vidgaevspm
      121 qmqqrgneiw ltwpflneky aslnemtmas ivhlakkifp dqlqflkiqm ahpaqmaqyh
      181 yqkfygcevs fnqacyayvm sadsltlksg fadpsltqll lkqaevaial kpryesvlqq
      241 ihsavadylk ahaeapkieq ianelhlstr tlqrqlqdwd slfkrvlese rmkrceyllq
      301 qglslteial qlgysgqsal araykqhsgq tllqlkrqlk
//
LOCUS       WP_004698711             401 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Veillonella].
ACCESSION   WP_004698711
VERSION     WP_004698711.1
KEYWORDS    RefSeq.
SOURCE      Veillonella
  ORGANISM  Veillonella
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Veillonella"
                     /db_xref="taxon:29465"
     Protein         1..401
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43830
     Region          1..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mnvlvvncgs sslkyqlldm ttetelakgl fekigdqdai fthkrpnadk leriepilnh
       61 kealrilldi lvdaefgvis smdeidavgh rvvhggekfa dsvlitpavm ealeecasla
      121 plhnppniqg ieaceaimpn vpqvavfdta fhqtmpkeay myalpysyye dygirrygfh
      181 gtshkyvaqr caelmgkhmt dlriitchlg ngssvaaikg grsidttmgf tplsglimgt
      241 rtgdidpaiv pflmektgmt yeeidrvmnk esgvlgisgv sndfrvieea aangnkraql
      301 alnmfhykvr rvigafaavm ggvdaiifta gigengignr daicngleyl gtridsernn
      361 vrgkeqeisv egskvkifvi ptneeimiar dtqritaalk k
//
LOCUS       WP_004699934             353 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Acinetobacter].
ACCESSION   WP_004699934
VERSION     WP_004699934.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..353
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39321
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvkniek hfgafhalkn isldfpegel vallgpsgcg kttllriiag lesaddgqvl
       61 legedatnvh vrerqvgfvf qhyalfrhmt vfdniafglr vrpratrpse aeikkrvtrl
      121 ldlvqlgfla drypaqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 nlhdelhits ifvthdqeea levadqiivm nkgnveqigs prevyekpat pfvfdflgqa
      241 nrfegehagg iirigndrik lpttvqapqg kviafarpde lhihsqpqan tieatfvrev
      301 wiagkvvael qdrngrliei alsseaakqh afkpnqtvwv sasqlhlfad qva
//
LOCUS       WP_004700162             872 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: Lon protease family protein [Acinetobacter].
ACCESSION   WP_004700162
VERSION     WP_004700162.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 872)
  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 872)
  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 872)
  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   4  (residues 1 to 872)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..872
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..872
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=97948
     Region          109..824
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mtqkldqvtt stlslaktnt tnvtinafps aleqpdikmt ldktalkpeq lthipdfeni
       61 pastkrikpl nnflgqdrak asveagislp ysgynifavg taglgkrtmi krllqqhakt
      121 mptpddwvyv ynfkharqpi alrfpagqgt kfqqalhqaw qiilkqlerr fsaetyhnri
      181 erireetgde qqqalveltk egeeldlkli srnekhgfvp vqvkddqvqe ltqteidaln
      241 tkqraeiaan vrymdkkler lglhlgdled dardkvsvln rdiatqvvmp ridlilnkys
      301 qvkgledylk qyaqdiienv elileqeedd fapamfnrvp aryqanvivs nkpnsgapvi
      361 fedfpthynl lghveqlthn gtittdftli rpgalhqang gflmleaeql leqpyawqgl
      421 kralksgqlk lsslehmltl tgsisiepaa vpldikvvlm aepeiyyeil evepelgsvf
      481 kiradftdtl qrndeneqay mqliadyvqt dkllpfdrsa laalltdssr qaedqsslsl
      541 hastlgdlir eahhhafkan eklvtdqhin lalqhrqyrl gylrelywqd lsrgtqliet
      601 sghrlgqina lsvihyadve fglpsrltas vyqgggdild iersvelggs lhakgvllms
      661 sflkahfgre qilhfsaala feqsygqvdg dsatvaelsa lisaisqipi dqswaitgsm
      721 nqlgqvqpig gvnakiegfy dacklqgltg kqgviiprqn mqhlmlrqdv idavqsgqfh
      781 ihaidtidqa leilmarpvg tldkkgrysk hsiyaavmeq leywqaiedg eeieeepkkk
      841 kknkkkikkh eeltandlpq etqeevatlk qk
//
LOCUS       WP_004702463             206 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Yersinia aldovae].
ACCESSION   WP_004702463
VERSION     WP_004702463.1
KEYWORDS    RefSeq.
SOURCE      Yersinia aldovae
  ORGANISM  Yersinia aldovae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 206)
  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 206)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 206)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Yersinia aldovae"
                     /db_xref="taxon:29483"
     Protein         1..206
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22049
     Region          1..204
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Site            order(92..93,96..97,99,124,127..128,133..134,136..137,159,
                     162..163,166..167,170)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          92..117
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          122..153
                     /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"
ORIGIN      
        1 mevyttendq vdavrrffse ngkalavgvv lgigalvgwr ywqshqntam teassayqqa
       61 snallansad gvaiaekfvq gnknnygvla glelahhfve qgefdkatqq lsqalgqtkd
      121 enllslinlr larvqlqlkk pdqalktlda vqgdgwtama qdvrgdalls kgdiagaraa
      181 yskgvesnas qalqallrmk lnnlss
//
LOCUS       WP_004702863             356 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter seifertii].
ACCESSION   WP_004702863
VERSION     WP_004702863.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter seifertii
  ORGANISM  Acinetobacter seifertii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 356)
  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 356)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 356)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 356)
  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   5  (residues 1 to 356)
  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   6  (residues 1 to 356)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Acinetobacter seifertii"
                     /db_xref="taxon:1530123"
     Protein         1..356
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40490
     Region          42..224
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <184..351
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mpkniyknan tviegnydnt slssntyllg ltslfdemgs qghsisevls gtnispdain
       61 qsslyisqvq kiqlfqniqr lsndpliglr agqkqrlsdf gvygyalyss rnfrqavelg
      121 irhiklagpi lkksfyirdd aavfegqdii algkllplvc efwfssmqtl iervlegpfq
      181 akklllpypa pdyaeqyekv fhcpvqfnag vmqwhfdlkw ldvpcpnanp itadmcksfc
      241 ermlgaaele epelvktirl illdgtglfp saqemaerlh mskrtlhrrl agfdltyqel
      301 ldetrrrlad eylrettltv deiaerigfs dtsnfrkayr hwtgispney rdklvl
//
LOCUS       WP_004703359             141 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Yersinia aldovae].
ACCESSION   WP_004703359
VERSION     WP_004703359.1
KEYWORDS    RefSeq.
SOURCE      Yersinia aldovae
  ORGANISM  Yersinia aldovae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 141)
  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   2  (residues 1 to 141)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Yersinia aldovae"
                     /db_xref="taxon:29483"
     Protein         1..141
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15050
     Region          73..140
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkfigklfvi ttllaslnih qavsaapvsa dsrsqekvls qplssatdni skksakvaeg
       61 ksenpktiaa hptenqtnqi nvnsasaeql aqflsgigrk kaeaivnyre qfgpfsdaeq
      121 lleipgigps flernsnklk m
//
LOCUS       WP_004705212             169 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: pilin [Acinetobacter].
ACCESSION   WP_004705212
VERSION     WP_004705212.1
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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..169
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=17307
     Region          2..144
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mnaqkgftli elmivvaiig ilaaiaipay qdytvraqvt eglnvaggvk tavndyfadv
       61 gdwpaniqaa vcgknatkvc aggtntdykg nyvtqvdvtn ggvditygnk antnalatkv
      121 lslipgsdta knvtwvcgna stpkgvtlat tatnnttida kylpgsckn
//
LOCUS       WP_004705236             158 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acinetobacter seifertii].
ACCESSION   WP_004705236
VERSION     WP_004705236.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter seifertii
  ORGANISM  Acinetobacter seifertii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Acinetobacter seifertii"
                     /db_xref="taxon:1530123"
     Protein         1..158
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=17096
     Region          1..>101
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkrnftyslg ftlielmivv vivaifaava ipsyqayvlr adasraqqqm qqiavqlarq
       61 ksrnfnykgf smgatssvnl pvgatgsaik ykitvrdgdd ttkpltdpaa lgqnwvirae
      121 asdpnnftyl fgsnglrckn katsnvtyit cgtgaepw
//
LOCUS       WP_004705285             496 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Yersinia aldovae].
ACCESSION   WP_004705285
VERSION     WP_004705285.1
KEYWORDS    RefSeq.
SOURCE      Yersinia aldovae
  ORGANISM  Yersinia aldovae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Yersinia aldovae"
                     /db_xref="taxon:29483"
     Protein         1..496
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=53976
     Region          1..496
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mqsiikihpl dnvavalqdl aadevietge fsvklaqpva rghkfaltai epsqmivkyg
       61 lpighaltli aagehihsqn aktnlsdlde yqyqpefsel ppqmadrevq iyrransnvg
      121 irnelwivpt vgcvngiarq iqqrflketq daegidgvyl fshpfgcsql gqdhentrtm
      181 lqnmvrhpna gavlviglgc ennqvdvfqt tlgpvdenrv hfmvcqqqdd eveaglehlh
      241 alyqvmrhda rvpgklselk fglecggsdg lsgitanpll grfsdyvian ggtsvltevp
      301 emfgaerilm srcrdeatfe ktvsmvndfk qyfiahnqpi yenpspgnka ggittleeks
      361 lgctqkagqs kvvdvlkyge rlqrpglnll sapgndavat salagagchm vlfstgrgtp
      421 yggfvptvkl atnselaakk phwidfdagk lihgtsmdsl ltefvdlivd iangkparne
      481 vndfrelaif ksgvtl
//
LOCUS       WP_004705711             352 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SPOR domain-containing protein [Acinetobacter].
ACCESSION   WP_004705711
VERSION     WP_004705711.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..352
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37847
     Region          <31..>249
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          270..344
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 msmnnkqrwm ggvvllgggv llaalllkgn eeikhvgaep qtstspklha kskpsaqegq
       61 mvqlqplavd vetekrllee qrrsrekava eqearaaefl amqqqaeada arkaaaeyaa
      121 inarraaaqe ssdnippeva gsdgktkgqq tdtkksvdta kaeadkkaae akkqaevdkk
      181 aaeakrqaev dkkaaeakkq aeadkkaaea khkaeaekka aeakhqaead kkaeakkhae
      241 aekktaeakh kadaekkaea ekarelleng dkkwmvqval aanqanadav vsklrakgyk
      301 vttsptskgi rimvgpakdr dtadaarkki tsdsslnmks awvidwvpld qr
//
LOCUS       WP_004706515             165 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Yersinia frederiksenii].
ACCESSION   WP_004706515
VERSION     WP_004706515.1
KEYWORDS    RefSeq.
SOURCE      Yersinia frederiksenii
  ORGANISM  Yersinia frederiksenii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Yersinia frederiksenii"
                     /db_xref="taxon:29484"
     Protein         1..165
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17567
     Region          1..152
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mkkaefyael krdlsaliag etnfiatlan asallyerld glnwagfyll dgkqlvlgpf
       61 qgkiacvrip vgkgvcgtav aenrvkrvgd vhafpghiac daasnaeivl pitvqgkvig
      121 vldidsivyd rfdeddelgl isvvaglceh lelcdsskyv iqtas
//
LOCUS       WP_004707586             134 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Yersinia frederiksenii].
ACCESSION   WP_004707586
VERSION     WP_004707586.1
KEYWORDS    RefSeq.
SOURCE      Yersinia frederiksenii
  ORGANISM  Yersinia frederiksenii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 134)
  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   2  (residues 1 to 134)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Yersinia frederiksenii"
                     /db_xref="taxon:29484"
     Protein         1..134
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14404
     Region          60..133
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkfigklfvi ttllagfniq playaastsp lqekapsqtt kattthhpvk ttqdkmvvta
       61 padrspesaq sqininsadv eqlaqflsgv grkkaeaivn yreqfgpftd aeqllevpgi
      121 gpsfleknss klkm
//
LOCUS       WP_004707878             206 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Yersinia frederiksenii].
ACCESSION   WP_004707878
VERSION     WP_004707878.1
KEYWORDS    RefSeq.
SOURCE      Yersinia frederiksenii
  ORGANISM  Yersinia frederiksenii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 206)
  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 206)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 206)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Yersinia frederiksenii"
                     /db_xref="taxon:29484"
     Protein         1..206
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22067
     Region          1..204
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 mevyttendq vdavrrffse ngkalavgvv lgigalvgwr ywqshqnsam teassayqqa
       61 sdalsansad gvalaekfvq gnnnnygvla glelahhfve qnefdkaaqq ltqalgqtkd
      121 enllslinlr larlqlqlkk pdealktlda vqgdgwtama qdvrgdalls kgdtagaraa
      181 yskgvesnas qalqallrmk lnnlsn
//
LOCUS       WP_004709840             496 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Yersinia frederiksenii].
ACCESSION   WP_004709840
VERSION     WP_004709840.1
KEYWORDS    RefSeq.
SOURCE      Yersinia frederiksenii
  ORGANISM  Yersinia frederiksenii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Yersinia frederiksenii"
                     /db_xref="taxon:29484"
     Protein         1..496
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54080
     Region          1..496
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mqsiikihpl dnvavalqdl aadevleige ssvklaqpvv rghkfaltai epgqmivkyg
       61 lpighaltli qpgehihsqn aktnlsdlde yqyqpefsdl ppqmadrevq iyrrangdvg
      121 irnelwiipt vgcvngiarq iqqrflketq daegidgvyl fshpfgcsql gqdhentrtm
      181 lqnmvrhpna gavlviglgc ennqvdvfqt tlgkvdedrv hfmvcqqqdd eveaglehlr
      241 alyqtmrndk rvpgklselk fglecggsdg lsgitanpll grfsdyvian ggtsvltevp
      301 emfgaerilm srcrdeatfe ktvsmvndfk qyfiahnqpi yenpspgnka ggittleeks
      361 lgctqkagqs qvvdvlkyge rlqrpglnll sapgndavat salagagchm vlfstgrgtp
      421 yggfvptvkl atnselaakk phwidfdagk lihgtsmdal ltefvelive iangkparne
      481 vndfrelaif ksgvtl
//
LOCUS       WP_004691597             458 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Acinetobacter johnsonii].
ACCESSION   WP_004691597
VERSION     WP_004691597.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter johnsonii
  ORGANISM  Acinetobacter johnsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Acinetobacter johnsonii"
                     /db_xref="taxon:40214"
     Protein         1..458
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=51024
     Region          10..446
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mnantapihn lqieqsvlaa lmtvagsyaq vesllteqdf hatrhklifs aivdldskns
       61 pydavlvnqw lemrnhgeas ggekylmqlm sdapssfynl qsyaeklkdf tvcrqaevea
      121 lkviqqarhl ttsrgelvqn aqaafanlnt esaseslfhi hdaasntfle isqkmeamia
      181 getmikgiqt giydldkklg dvepgcllvl aarpamgktt mmqlianhvs iiqkkpvlim
      241 sgempkeqia mrlccamapa digvlrnaph klpkeeftay tnavvmlknv pmqindtsrp
      301 sianiresir ktqhqygfvg avlvdylqim kttkpfared lkiayftgel kamakefncv
      361 ivllsqlnre lekrpnkrpv lsdlresgai eqdadqiifl yrdeiynkes qfrgiaeaiv
      421 gknrhgeagt aymhaqlkyc qftnldhdal nqiqgnli
//
LOCUS       WP_004710694             336 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Acinetobacter nosocomialis].
ACCESSION   WP_004710694
VERSION     WP_004710694.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter nosocomialis
  ORGANISM  Acinetobacter nosocomialis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Acinetobacter nosocomialis"
                     /db_xref="taxon:106654"
     Protein         1..336
                     /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=38776
     Region          2..269
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mrnlhidatk giliflvvlg hylerligwn eplnqailgs iyfvhmpafi fisgmffkee
       61 kilekliyfl slylpfqilf qlldafyngs lwtgtfhlaw fakpywvlwy lfgmgawtvl
      121 afflkkmayp llfsivlall vgcspinnys ysmgrifvfl pffmagaiyg ktifqyisql
      181 pyaklfavit lfiitavaai shysyywlfg slsylqlhvd vwqgmlirsv imllsamgvl
      241 slfiltqsfk qpwiglgqkt lpvyilhgfi iivlthqlsf kysveinili slvlailtcm
      301 vlqlqlferl iglisffiyr pfikllellk pkkgfn
//
LOCUS       WP_004711538             529 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Yersinia frederiksenii].
ACCESSION   WP_004711538
VERSION     WP_004711538.1
KEYWORDS    RefSeq.
SOURCE      Yersinia frederiksenii
  ORGANISM  Yersinia frederiksenii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Yersinia frederiksenii"
                     /db_xref="taxon:29484"
     Protein         1..529
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=56919
     Region          3..525
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mskilkides dnlivalknl qkgetvcwgd dhftlmtdvk akhkfsvedi aiggivsmyg
       61 tpvgkatkpi akgeavtvdn ikhyaapvql ndeqynwqap dissyidrtf kgylrsdgrv
      121 gtanywlvfp lvfcenrnvt kltdalndal gysdhsltrf amnlaggdap qvkekllphi
      181 egvrsitvss gcggaasdsm tmcevlaaya dhpnvigitv fslgcekaqv idfkdalkkc
      241 npqfskptly fkqqewenee qmmqsalket facmnevqpt prvdvplshl klgvkcgasd
      301 gfsgisgnpa mglvsdwvvt lggasalaef pelcgaegdm vkrcrhpedk skflslmagy
      361 ektanffnts iadnpspgni adglitdaik stgaakkggr apisavcdya epmpdtglsl
      421 vctpgndvva vtglvaagcn vvifstglgt ptgnpivpvl kistnteian rlkdiidfdc
      481 gpviegtpls dvsqalferv ietasrdyvv ksdrleqydf llwkrsldl
//
LOCUS       WP_004712849             257 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Yersinia rohdei].
ACCESSION   WP_004712849
VERSION     WP_004712849.1
KEYWORDS    RefSeq.
SOURCE      Yersinia rohdei
  ORGANISM  Yersinia rohdei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Yersinia rohdei"
                     /db_xref="taxon:29485"
     Protein         1..257
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=28830
     Region          1..169
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 myqvdynsyr siegfnlrvn slvihctaen fvdsmasltg dsvsvqylvp ditdesyiqa
       61 gfksmqifnl vdenarawha gesgwagrtg indtsigiei vnlatensgi fhfppypaeq
      121 itavkqlatn ilqrypditp vnvvahsdia ptrnsdpgpe fpwqdlydeg vgawfdddik
      181 ekytqqfvak gvptrdella rfstygydit fansesgykq lvralqlhfr pdnyngyidi
      241 etaailyalv ekyfhpl
//
LOCUS       WP_004713065             165 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Yersinia rohdei].
ACCESSION   WP_004713065
VERSION     WP_004713065.1
KEYWORDS    RefSeq.
SOURCE      Yersinia rohdei
  ORGANISM  Yersinia rohdei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Yersinia rohdei"
                     /db_xref="taxon:29485"
     Protein         1..165
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17673
     Region          1..152
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mkkaefyael krdlsaliag etnfiatlan tsallyerld glnwagfyll dgqqlvlgpf
       61 qgkiacvrip vgkgvcgtav senrvqrvgd vhefpghiac daasnaeivl pitvqgkvig
      121 vldidsivyd rfdeddelgl isvvaglceh lelcdstkyv tqtas
//
LOCUS       WP_004717022             681 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Yersinia ruckeri].
ACCESSION   WP_004717022
VERSION     WP_004717022.1
KEYWORDS    RefSeq.
SOURCE      Yersinia ruckeri
  ORGANISM  Yersinia ruckeri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 681)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..681
                     /organism="Yersinia ruckeri"
                     /db_xref="taxon:29486"
     Protein         1..681
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=76490
     Region          53..681
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mngcykshll lsffifissi plsinatedn kqtnmevigq pyseygiars syqqeqqkla
       61 riaggtnlmt pgeegrlgtl qdaldyqpgl viqnffggvd qprlnirgsg vqsaplsrgv
      121 tllqdglpln dadggfhisl lepresqfis virganavsp vsnalggeld fisytgadet
      181 griryeygsf grqgwqgalg grdgdldgri sisgdrfngy rqhsasrrna vranlgyege
      241 nfasrtwfsw tdlafdvags lsqeqlkanp rsvfplvlvr dphrnveqar ianrmswhgd
      301 nrqhqlglwa qhthdnfvtp vvyvlsggnt ygaqwlthlq qgqwhyrlga stdrsdmerd
      361 lhqnrrgkpd nykligaynm laqnhnlafg agwkpneqwr idtdlkgtra vrnalskdgr
      421 sgldqhwyfl spklgviwtp npqqrwfgsl nwsneapsfr eiisnkgllt plrpqqavtl
      481 emggsgtltr hikwdlalyr sliadelitt ydsegnsvgt fnygsntvhq giemgfkghi
      541 pmrdssieyr fawtyndfrf kggeyagkri ggippqlisa evlyqwqrws igpnlhwlpe
      601 itpvdhlnrt qiqardkyav wgikmdyrhp dgwsaylsmd nltdkryata svterevtsk
      661 qsktlfpgmg rsinggftyt f
//
LOCUS       WP_004717220             252 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Acinetobacter].
ACCESSION   WP_004717220
VERSION     WP_004717220.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..252
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28570
     Region          24..249
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 msqdtttkkr yyepapqdid ienfrkvies rrsvrkytek qipadvldac ldlallapns
       61 snlqpwtfyv vqsqakkkql vkaclsqlsa ktaaelivcv aridridema knnlthfpmp
      121 eapravkqyy kfiaynyktg ylnalgnfkk vafkvartld kqlpvtafnp adaklwaskt
      181 talacenlvl alraygfdsc mmegfdeplv rkilnlgdke fpvmvisage raedgvffpq
      241 yrfdrdlfiq kv
//
LOCUS       WP_004718000             206 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Yersinia ruckeri].
ACCESSION   WP_004718000
VERSION     WP_004718000.1
KEYWORDS    RefSeq.
SOURCE      Yersinia ruckeri
  ORGANISM  Yersinia ruckeri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 206)
  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 206)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 206)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Yersinia ruckeri"
                     /db_xref="taxon:29486"
     Protein         1..206
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=21927
     Region          1..204
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Site            order(92..93,96..97,99,126,129..130,133..134,136..137,159,
                     162..163,166..167,170)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          92..119
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          124..153
                     /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"
ORIGIN      
        1 mevyttendq vdavrrffse ngkalavgvv lgigalvgwr ywqshqvtal teasssfqka
       61 sealaannae gvaaaekfaq nnsnnygvla glelahhfva qgqfdkaaqq lslaqgntkd
      121 enllslihlr larvqlqlkk pedalktlda vngdgwtama qdirgdalls kgdvagaraa
      181 ytkgiesnas qalqsllrmk lnnlss
//
LOCUS       WP_004718084             336 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004718084
VERSION     WP_004718084.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 336)
  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   6  (residues 1 to 336)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..336
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38198
     Region          22..206
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <138..336
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msqltdasvv lrlgyqairr aglpteeils kagvalgqvd qnartplnaq fafwvaaeev
       61 sndpdiglhl gehlplyrgq viehlfisse nfgeglkral ayqrlisdaf hakliidddg
      121 rcyltngeqp wgenivnrhf secaisgilr ffkfitegrf epiyidfnfa ngasdgeyyr
      181 vygcpvslgq ketrlyfdps ileyplwqae pellqlheql aieklqelar ydlvgevrra
      241 igstlesget tletvaaqls itprrlrtql seantsfqqi lsdyrcrlak kllanttesv
      301 erivyltgfs epstfyrafk rwtnetpvey rkrkqr
//
LOCUS       WP_004718533             626 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Acinetobacter].
ACCESSION   WP_004718533
VERSION     WP_004718533.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 626)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 626)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 626)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 626)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..626
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=69559
     Region          2..626
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mqstakkaal paitlaalgv vfgdigtspl yalrqcflta hiaiteatvl gilslifwcm
       61 mltisfkyvt iimradnnge ggimsllaln lrsnriadnr kiylialgfi gaslffgdgi
      121 itpaisvlsa ieglsiatpm fnkwlmplai giltalflvq rhgtgtmgkf fgpitltwfa
      181 sigligihsi sqtpyvlsml sphwalnfif hqpfvafltm gaviltvtgg ealyadmghf
      241 grlpirlgwf iivlpcllln yagqgalllr npsaienpfy llvpewglyp mialataaav
      301 iasqavitgv fsmanqaiql rylprltvhh tsdveqgqiy lpfinwilyv silllivifq
      361 nsanlanayg vavtmtmlcd tilisilayg fwrwpkwkva lfaipflvid sifigstslk
      421 iisggwvpil igaivftilm twktgreivf nrlekdalpl dlfiksvsls detqfvpgqa
      481 vfltgnpniv phamlhnikh nkvlhernim vtvitrdvpy vpdqerirve vldkrfqrvf
      541 vyygfkdqpd ipnalelayk qlevefdmmh isffisrdrl ihtvgdgmap wreklfismq
      601 rntspvsdfy qippnrvvem gsqiei
//
LOCUS       WP_004720255             343 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004720255
VERSION     WP_004720255.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 343)
  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 343)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 343)
  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   4  (residues 1 to 343)
  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 343)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..343
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38830
     Region          28..213
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          257..338
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mktvsarqdq gipgvyglll ldivsrwgys aetlfapfnf tseqladpec riptplanel
       61 ikhalkltge stlgfhlgtq mrisihgfig yaimtahdit dalvlanrfi qlrmpflqly
      121 fstfgekatl qlqcdieiep lrteivmglt fgimtmakal tgidylhgdi dfdfpkpdgf
      181 dkyieklakq ynmrfeqphl iasfdksylg lkmvnadpia sqiainqcea elsalgerrr
      241 lamrvrdilt hseqhylsie nvadrlhmsd rtlkrqlaae gtsfstlvde vryrhatsll
      301 srtdytleqi adelgysdva nfsrafkrws grspsswrkd pyl
//
LOCUS       WP_004721005             299 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Yersinia ruckeri].
ACCESSION   WP_004721005
VERSION     WP_004721005.1
KEYWORDS    RefSeq.
SOURCE      Yersinia ruckeri
  ORGANISM  Yersinia ruckeri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 299)
  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 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   3  (residues 1 to 299)
  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   4  (residues 1 to 299)
  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 299)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Yersinia ruckeri"
                     /db_xref="taxon:29486"
     Protein         1..299
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33125
     Region          28..179
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          208..289
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 maaiddiqql maeqvarlap gngltpsavp rvnilfsdvh hprtpvmytp siviifqgkk
       61 vgylgskifq ydpknylllt vplpfecetf aspekplagl sihvdsqmlq dllvdigdde
      121 ldkprgntng vnaallteem lcaterlldv menplaarvl gpqivreilf yvlsgpcgap
      181 lqelvnrhgh fnqiaralrr ienqfaenln veqlaaevnm sisafhhnfk avtntsplqy
      241 lksyrlhrar vlmvhdglka staairvgye sasqfsrefk ryfghtpgde vaklrsnpv
//
LOCUS       WP_004722596             122 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Acinetobacter guillouiae].
ACCESSION   WP_004722596
VERSION     WP_004722596.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter guillouiae
  ORGANISM  Acinetobacter guillouiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 122)
  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 122)
  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   3  (residues 1 to 122)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Acinetobacter guillouiae"
                     /db_xref="taxon:106649"
     Protein         1..122
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14417
     Region          14..117
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mklnpklley aksmrhdatd aehlmwqllr aqrfmnlkfr rqhviepyiv dfycheldlv
       61 veldggqhnt dvvvaydner tqflealglk virywnddvl nrsevvledl wnicielkdt
      121 sp
//
LOCUS       WP_004723991             344 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter guillouiae].
ACCESSION   WP_004723991
VERSION     WP_004723991.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter guillouiae
  ORGANISM  Acinetobacter guillouiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 344)
  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 344)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 344)
  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   4  (residues 1 to 344)
  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 344)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Acinetobacter guillouiae"
                     /db_xref="taxon:106649"
     Protein         1..344
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39886
     Region          58..211
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          258..333
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqelqipngy fhlwqmylse rgidlatldf lqadekkhli gilsqpidtq ssyfffhqli
       61 ektkqaldcp qivfemaeyv rpehfgvlgy masrsttvae alqnimrfsr lvidgdevip
      121 mqmqlkgeyv hliwpfhhek yilineftna lmmhlarkiv ppnqfplhav hfahapqmai
      181 yhylkfygce vsfhqpqysf vlasaglnlk iqqadpslmq llvkqaeeai askpryetia
      241 qrlhlivaey lklkqhapki eeltqelhis trtlqrqlsd lqtsfkkive iermkrcefl
      301 leshmpfsei amqlgysdqs altraykafs gqtllekkqq lkss
//
LOCUS       WP_004724010             336 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Gammaproteobacteria].
ACCESSION   WP_004724010
VERSION     WP_004724010.1
KEYWORDS    RefSeq.
SOURCE      Gammaproteobacteria (g-proteobacteria)
  ORGANISM  Gammaproteobacteria
            Bacteria; Pseudomonadati; Pseudomonadota.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 336)
  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   6  (residues 1 to 336)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Gammaproteobacteria"
                     /db_xref="taxon:1236"
     Protein         1..336
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38402
     Region          22..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          102..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msrdtisihf vnaaltgvkr lgmdvdtlls hvgieaellr qpkarispeq ytrfvkmlwm
       61 vtqdehvgfd iqprrlgsfa imcqliihak tlgdalelss qfyklfgdew svaverdkhe
      121 arlvplipkt mdpdhfites mlmiwhglas wlierriple rvhfgyprpn hadeydalff
      181 apvmqfdmpr teitfaadyl dlpirqdeas leeflkaapa qllvkfkntn sltsrirevl
      241 ksqigeempt lndvasmlyl spqtlrrrla aegksyqgvk dalrrdaaih lllnpdltle
      301 dvaqqvgfse tstfhrafkk wtgvtpglyr qlhgyh
//
LOCUS       WP_004725901             264 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: hydroxypyruvate isomerase family protein
            [Acinetobacter].
ACCESSION   WP_004725901
VERSION     WP_004725901.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..264
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29486
     Region          1..257
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mtklavnlsl iftevplier falahlhgfh nveiqfpyel sieeiqaqle qydlslclin
       61 vpagdlmqgg nglagvpgqe lafhqalela ieyaealnvp nvnilagkqp qdadllpcln
      121 tlannlklac hllsnrdiqp vfemingtdm prflvqniaq gqemleavqh palkmqfdcy
      181 hmammgedvl aalqenidwi ghiqfadcpg rhepdtaqid ysaifswlkq saytgfiaae
      241 ykpqshsnqs fawkekyfsn nhsy
//
LOCUS       WP_004726497              98 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Vibrio furnissii].
ACCESSION   WP_004726497
VERSION     WP_004726497.1
KEYWORDS    RefSeq.
SOURCE      Vibrio furnissii
  ORGANISM  Vibrio furnissii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 98)
  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   2  (residues 1 to 98)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Vibrio furnissii"
                     /db_xref="taxon:29494"
     Protein         1..98
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10586
     Region          37..96
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkfntywlaf llaicwpvth amaadsaqvs deieitvnin tapaeelatl lkgiglkkaq
       61 aiveyreang afqskqeltq vkgigpsiva knddrill
//
LOCUS       WP_004726716             295 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Vibrio].
ACCESSION   WP_004726716
VERSION     WP_004726716.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 295)
  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 295)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 295)
  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   4  (residues 1 to 295)
  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 295)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..295
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32933
     Region          27..182
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          210..290
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtelaklmqq yvehhslhel egiaetaipg vwfyrsgagn qrrpfiyqsg iiilgqgqkn
       61 ihigpnpvqy gpndylvvgv pmpleceaiv eagkpllgls ididhsillk qvdlleqagf
      121 kpckqdkdnq cglksvnmge emlntckrlm halndgleaq ilgaslmeem vyraltsceg
      181 hvlfdlahhe ghyarvakal skvhreydqq ltvqqlaeea nmsissfhqa frgvtmespl
      241 qylkkvrlnk akeliqiegk rvndaarlvg ytspsqfsre ykrhfnetpr gakaa
//
LOCUS       WP_004726966             608 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Vibrio furnissii].
ACCESSION   WP_004726966
VERSION     WP_004726966.1
KEYWORDS    RefSeq.
SOURCE      Vibrio furnissii
  ORGANISM  Vibrio furnissii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 608)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 608)
  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 608)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Vibrio furnissii"
                     /db_xref="taxon:29494"
     Protein         1..608
                     /product="M4 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=65184
     Region          11..604
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mktlqrqvkg llavgtvmaf pvsaaqwvav edsgqfqqtl vaqkgsivtp angyqaikti
       61 qlpngkvkvr yqqlyhgvpv fntavvstes skgitkvqgm maqgieadva tvkptldekq
      121 aiakaadnfs aanasftgqd lpmenqsavl mvrlddqqqa qlvylvnffv asdtparpfy
      181 fidansgdvv kqwdglahae atgtgpggnq ktgmyqygtd ypgfavsktg stctmlssav
      241 ktvdlknkts gttaysydcn nssnyndyka vngaysplnd ahyfgkvvfd myndwlntsp
      301 ltfqltmrvh ygsnyenafw dgsamtfgdg ystfyplvdi nvsahevshg fteqnsglvy
      361 egmsgginea ysdiageaae yymrgsvdwv vgsdifkssg glryfdtpsk dgssidhasq
      421 yysgidvhhs sgvfnrafyl lsnkqgwdvr kgfevfavan qlywtpnstf degacgvvka
      481 aqdlgynvnd vtaafttvgv nsscsvdsgn elvkgqpvtg lsgsagsesf ytftvnsatt
      541 atvsissgsg dvdlyvkags kpttsswdcr pyrsgnneqc sisavagtty hvmlkgysay
      601 sgvtlrld
//
LOCUS       WP_004727327             249 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Vibrio furnissii].
ACCESSION   WP_004727327
VERSION     WP_004727327.1
KEYWORDS    RefSeq.
SOURCE      Vibrio furnissii
  ORGANISM  Vibrio furnissii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  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   3  (residues 1 to 249)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Vibrio furnissii"
                     /db_xref="taxon:29494"
     Protein         1..249
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27751
     Region          44..224
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mrsqsvatqh dpsgskvssr hktistlnst dalamvehgs eltlsittpv gtkficktpf
       61 igthsdtyll iempqvssed ltyffqegfw invraisprg egamihfrsq llhimhepit
      121 lamlsipntm qvtqlrkepr yevnlsgkvn qgerksecev rdlsksgcrf itaplgrsyq
      181 vgdqvsieif adkrgskifd plvgricnlq rsihyarygl eftdqgktna knllgqlkfn
      241 gtkltlnve
//
LOCUS       WP_004727858             356 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein [Vibrio].
ACCESSION   WP_004727858
VERSION     WP_004727858.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 356)
  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 356)
  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 356)
  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 356)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..356
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39487
     Region          3..351
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 maftqvalat slsiaatalt fnvqaaekil lktpvafgth lpalgtpiqw yadhitdtsg
       61 gtikmkiyep gklvnpaeil davstgkvns gyatagywqg tlpaaalfss vpfgpeagey
      121 mawlyfgngl klyqemydqg gynvkvlpca iispetsgwf kkpiekpedl kglnmrffgl
      181 gasvmeklgv gtvqmpggei fgalekgaid asefsqpaid erlgfykivk ynyfpgwhqq
      241 stvfellink dtwkkmdkaq qsavettcma tmtysiaege aiqysamqka qqngveiryw
      301 ndtmlnlfet twmevvdekk kadpffakvw ddlskfrhdy alweenaflp rkshtq
//
LOCUS       WP_004729217             626 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Acinetobacter].
ACCESSION   WP_004729217
VERSION     WP_004729217.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 626)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 626)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 626)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 626)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..626
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=69721
     Region          2..626
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mqstaqkaal pvitlaalgv vfgdigtspl yalrqcflta hlaiseasvl gilslifwcm
       61 mltisfkyvm vimradnnge ggimsllaln lrttrisdqk kiflialgfv gaslffgdgi
      121 itpaisvlsa ieglsiatpi fnqwlvplsi gilaglfmvq rhgtatmgkf fgpltmlwfl
      181 siggfglwsi iqtpfvlwmv npywayhfvv dqpyvafltm gaviltmtgg eaiyadmghf
      241 grlpirlawf iivlpcllln yagqgalllr spealanpfy mllpdwalfp miglataaav
      301 iasqavitgv fsmvnqaiql rylprlsvkh tsalergqiy lpfinwmlfi svlilillfe
      361 nsanlasayg vavtmtmlcg tilisilayg fwrwpvwkva lfavpflald lvfvastslk
      421 iasggwvpil igavlftilm twkdgralvl nrleqdalpi dlfiksismg egtkfvpgda
      481 ifltgtpniv phamlhnikh nkvlhernim ltvitrdipf vdrqeriele klsehfyrvf
      541 iyygfkdqpn ipealqqaye qwdfeydlmq isffisreri mhtvgegmap wreklfismq
      601 rntspvsdfy qippnrvvel gtqiqm
//
LOCUS       WP_004729392             204 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Vibrio].
ACCESSION   WP_004729392
VERSION     WP_004729392.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 204)
  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 204)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 204)
  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 11459477
            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="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22007
     Region          1..202
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 melydteeqq veaikdwwke ngkavifgav iglgglfgwr fyqdsvtsgq eaasasytka
       61 iqtlttkgvd geadvqsfid snskseyavl aamqlakaqv qagqldeala qlewaknatg
      121 daalkpvity rvarlqaeqg nfdaalsela tikeqswtgr vaelrgdisl rkgdkeaaya
      181 ayaeaqqadd asqtlqmkld dlak
//
LOCUS       WP_004729551             406 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Acinetobacter].
ACCESSION   WP_004729551
VERSION     WP_004729551.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..406
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44114
     Region          5..388
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msksvlvinc gsssikfall leeqnfrihg laenlgtena rikgvtvgne pvdihipfad
       61 hkkalevgle rlanyrpdai ghrvvhggsl tkaelindei iekireatpl aplhnpahli
      121 gieatkrlfp elpqvavfdt afhqtmpaha yryalpkfly tahgvrrygf hgtshayvse
      181 rgselagsfk qggwltahlg ngsstcavwn gksvdtsmgl tplegivmgt rsgdvdpslh
      241 sflaknlgwd iykidkmlns qsgllglsdl sndmrtliea seqgnedaal aievfcyrla
      301 kslaalscgl prlnglfftg gigensayir ektmtylphf gfnldknann elkrgtegri
      361 dsgtgpqiwv vptdeegria qevqsvvele verntakksk aevtpa
//
LOCUS       WP_004730212             243 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Vibrio splendidus].
ACCESSION   WP_004730212
VERSION     WP_004730212.1
KEYWORDS    RefSeq.
SOURCE      Vibrio splendidus
  ORGANISM  Vibrio splendidus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 243)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Vibrio splendidus"
                     /db_xref="taxon:29497"
     Protein         1..243
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=27532
     Region          6..236
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mtlsdhtiqe afendwytcf yqpkvqpsie kvtgvealfr ldipeegifs pgvfidrafa
       61 lgyeeeiffs vleqsltevk slsvhlnlav niskkvlanp dnvqkvrell wnasfkaeql
      121 tfelsendql deqlceqikr fkslgvrisi ddfgigysdm nkvislnvdk vkfdksivns
      181 iepassdlvk rtlayckesg ietvaegved adtrqmihql gfdryqgfly skplpitdlr
      241 lvm
//
LOCUS       WP_004731037             338 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Acinetobacter].
ACCESSION   WP_004731037
VERSION     WP_004731037.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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
REFERENCE   4  (residues 1 to 338)
  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 338)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..338
                     /product="CmpA/NrtA family 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=38281
     Region          2..249
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mstlekteln igyiplldcv ailwaekqgy faeqgltinl ireaswsslr drlaygflda
       61 ahslsamlpa aalgtdqlqv alqtplvlsv nqafislrqd lcyelgiqpe ddeqstskkl
      121 vqalqqnhpi nlayvykysi hhyclkewla ltdpqlakni qlmtspppsm vkgiskqvfd
      181 gfcvgepwni qaklegysfi vaasqnvipk vadkvlamtq ewaeqhpftv eavvkavqka
      241 qddlkqrpdl sevwdmlvdy qiiqfecsaq rhvydfykik niirnfvges aqpkvddfiw
      301 llqqmqkwen iemtaaekkq iaqqciyslq nqhadiig
//
LOCUS       WP_004731076             341 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio splendidus].
ACCESSION   WP_004731076
VERSION     WP_004731076.1
KEYWORDS    RefSeq.
SOURCE      Vibrio splendidus
  ORGANISM  Vibrio splendidus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 341)
  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   6  (residues 1 to 341)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Vibrio splendidus"
                     /db_xref="taxon:29497"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38717
     Region          32..212
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          95..338
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 meytavyepd mqafgildlq llsryfsssl tvdtllkgsn idefqlntpd thitlaqkla
       61 vfsnalessn veglglkvgq earfsdfgvl gyavfssetl ldallmgfky lrlagpvlkk
      121 tmsvehqtgy fraeqlield sllpfcceyw fsaiqslcee vlqqpfpslv irfpypkpty
      181 gdlyqeifrc rvefdceqle wqfdatslya plptanpitl qmclkscddm larvsaptsl
      241 kekisqmfie rpgcypsiea lstelgmssr tlrrhlkaad tsyqkildhv rfhlsrhyls
      301 sthmsieeis drvgfsdsan frhafrkwsg ssprqyrkdi g
//
LOCUS       WP_004731146             342 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004731146
VERSION     WP_004731146.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 342)
  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 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 342)
  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   4  (residues 1 to 342)
  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 342)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..342
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38645
     Region          32..209
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          256..337
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mktiaprqdq gipgvyglll ldvisrwgyn neslfqpfgl tseqladpdf riptpvanel
       61 vkyalkltge ptlgyhlgtq mrisihgfig yaimtannit dalvlanrfi qlrlpflqlf
      121 fstfgakatv qlqtdiqlep lrteisialm iglismakai tgvtdatgei dfdfkkpegf
      181 erfmakfpth qfrfeqphli lsfdksylmn klvhadpias qiainqcete lsalgerhri
      241 amrvrdilth aeqhylsies vadrlhmsdr tlkrqlaaeg tsfstlvdev ryrhatslls
      301 rtdftleqia delgysdvan fsrafkrwsg rspsnwrkdp yl
//
LOCUS       WP_004731459             294 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Vibrio].
ACCESSION   WP_004731459
VERSION     WP_004731459.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 294)
  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 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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..294
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32863
     Region          28..182
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          213..293
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mktlaqllqs yvehkgwddl egireteigg vwlyrssggn qrqpftyqsg iimlgqgkkn
       61 iyigdrpvty aagdylvvgv pmplecealp vngepllgls isidsqrlhs lvkkledqgf
      121 lesycnkhkq nssglesapm eeqmlesftr lvktlhcdie anilgdamvs eivyraltgs
      181 egrvlfdlah hdghyarvak alskvheeyd qtitvqslad eanmsvsafh nafrnvtfes
      241 plqylkkvrl nkakeliqle glrisdaarr vgysspsqfs refkrhfntt prav
//
LOCUS       WP_004731701             264 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Acinetobacter].
ACCESSION   WP_004731701
VERSION     WP_004731701.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..264
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30031
     Region          36..261
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mpnqnsqtss qttdssnpek kryyepapqd ididnfrkvi esrrsvrkft kkpipvevld
       61 acmdlallap nssnlqpwtf yvvqnpgkkk rlvkacmsql aaktaseliv ciartdride
      121 makrnvnefp fpeappaikk yykyipynyk tgylnafgnf kkvafkvart ldkqmpvsaf
      181 spadaklwat kttalacenl vlalraygfd scmmegfdep mvreilelnd eqypvmviga
      241 geraedgvff pqyrfdrelf iqkv
//
LOCUS       WP_004738035             335 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Acinetobacter baumannii].
ACCESSION   WP_004738035
VERSION     WP_004738035.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..335
                     /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=38956
     Region          2..269
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mrnlhidatk gvliflvvlg hylerligwn eplnqailgs iyfvhmpafi fisgiffkee
       61 kilekliyfl slylpfqllf qlldafyngs lwngtfqflw fakpywvlwy lfsmgiwtll
      121 afflkktayp vlcsiilall igfspinnys ysigrifvfl pffmtgaiyg ktifqyipql
      181 pyeklfavii lliitivaai shysyywlfg slsyiqlhvd lwqgvlirsv imllsamgvl
      241 slfvftqnfk qpwiglgqkt lpvyilhafv iivlthqlsf kysveinifi slvlavltcm
      301 vlqlqiferl irfislfvyk pfmklleiln pkkgl
//
LOCUS       WP_004737677             249 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio splendidus].
ACCESSION   WP_004737677
VERSION     WP_004737677.1
KEYWORDS    RefSeq.
SOURCE      Vibrio splendidus
  ORGANISM  Vibrio splendidus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 249)
  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 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   3  (residues 1 to 249)
  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   4  (residues 1 to 249)
  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 249)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Vibrio splendidus"
                     /db_xref="taxon:29497"
     Protein         1..249
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27823
     Region          5..247
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          175..242
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mhlnerlgei inlddhqvmv khyeshysse ihshdyshlv fihqgcqiis tdkdsllsmp
       61 gsliyipagv phradalkqs qvsllrlplg sipelseici ldispivtql fslwenggpe
      121 pklephyiqv lmdqctlcka vhnpliakeg mdrrllpvid alsnkpsikl sisnlskqtg
      181 asvrtlnrlf lasfkasfre irqkvvmera ekmmakgisa teiafeleys slsafstafk
      241 ehqkkapqn
//
LOCUS       WP_004738381             607 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Vibrio splendidus].
ACCESSION   WP_004738381
VERSION     WP_004738381.1
KEYWORDS    RefSeq.
SOURCE      Vibrio splendidus
  ORGANISM  Vibrio splendidus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 607)
  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 607)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Vibrio splendidus"
                     /db_xref="taxon:29497"
     Protein         1..607
                     /product="M4 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=66156
     Region          10..604
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mnqqrqlswk iaailgtsfg fnahaaemvt iendsllqqs liaqsksvap lelgfsevkr
       61 vvlpngktkv ryqqthfglp vfntsvvatl sknqpsqifg smaqgisddl ssiapklnke
      121 qaieaalssh rsftvgkksi enknaklvvr ldesqtaqmv ylvdffvasn yperpfffid
      181 amtgevlqkw nglnhakavg tgpggnsktn ryeygtdfpg fsidktgttc tlendavktv
      241 dlnnrtsgss aysyncsdda nytdhkyvng aysplndahy fgnvvfemyk ewmntsplsf
      301 qltmrvhyst dyenafwngs smtfgdgknt fyplvdinvs ahevshgfte qnsglvyrnm
      361 sggineafsd iageaaeyyl rgnvdwivgs difksegglr yfdqpskdgr sidhasdyyd
      421 glnvhlssgv ynrafyllan ksgwdvrkgf eiftvanqly wtanstfdag acgvakaaad
      481 mgytvadved afnsvgvnas cgptipgdnv ltkgtpianl sgnkysesfy tfsvdsassv
      541 tvaisggtgd adlyvkagsk pstsnydcrp yrtgnneqcs vnaqpgvtyh vllrgytnys
      601 gvtlrld
//
LOCUS       WP_004736087              99 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Vibrio].
ACCESSION   WP_004736087
VERSION     WP_004736087.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 99)
  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   2  (residues 1 to 99)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..99
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10610
     Region          38..98
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mrtiystlll sflmalsspa fsdsptkael ydgieitvni ntataeelsa llvgvgdkka
       61 qeivdyrdqn gafttaddlv svkgigeatv eknreriql
//
LOCUS       WP_004739275             217 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Acinetobacter
            baumannii].
ACCESSION   WP_004739275
VERSION     WP_004739275.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 217)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..217
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=25335
     Region          128..207
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mtvnegctkq virlskslve ehlvkllgyk lhrplvfdvh aplqgkikqw fqlamhlqem
       61 vsddyslcdd sgvwrnfesn lvimllnaqp hnysqelnlr qqgrpnyllk veqilinsln
      121 qplnlkelek vlgvsrerly rdfhlyfgqs piayfrnlrf evvhkrlqei rpwenvssia
      181 ldcgfqqlgr fsseykkkfg elpsetlfns ktsille
//
LOCUS       WP_004739390             277 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter baumannii].
ACCESSION   WP_004739390
VERSION     WP_004739390.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 277)
  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 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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..277
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31995
     Region          30..270
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          193..270
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 msnwvdiskd tntgietira hftghaydph whssyligvt esgiqqfhcr kkqinshagq
       61 vfmlepeeih dghapasdgf tyqmlylhpe wlkqrlqglf hnspdhyelv idaplksddq
      121 laiitsqafr hlhykemniv kdnsldvliq yiaqgkwlkk asqsscihvp qiahqirdil
      181 hdhlfedigl edisrmvgld ryhihrifks tfhlaphqyl iqlrltrard llarsispaq
      241 vasdlcfsdq shlsrwfkrc ygltpaayrk ictnlqd
//
LOCUS       WP_004739930              99 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Vibrio splendidus].
ACCESSION   WP_004739930
VERSION     WP_004739930.1
KEYWORDS    RefSeq.
SOURCE      Vibrio splendidus
  ORGANISM  Vibrio splendidus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 99)
  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   2  (residues 1 to 99)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Vibrio splendidus"
                     /db_xref="taxon:29497"
     Protein         1..99
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10584
     Region          38..98
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mrtlystlll siliflspta fadsptkael ydgieitvni ntataeelsa llvgvgdkka
       61 kdivdyrteh gafasaddlv svkgigeatv eknreriql
//
LOCUS       WP_004740180             176 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit [Vibrio].
ACCESSION   WP_004740180
VERSION     WP_004740180.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 176)
  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 176)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 176)
  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   4  (residues 1 to 176)
  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   5  (residues 1 to 176)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..176
                     /product="TRAP transporter small permease subunit"
                     /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=19780
     Region          4..169
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mrsliyieri fnrigdalgw lssmlfilli anvvydvvmr yafndvsiaf qemewhlfsa
       61 vfllgvpyai kagghvrvdv fyeqlsfkaq aiidllgtli fllpfcllva wfgidvakes
      121 yelgetsgdp gglpyrwiik amiplsfflm alsgvglilh slnkifnphl ihanhk
//
LOCUS       WP_004740327             204 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Vibrio].
ACCESSION   WP_004740327
VERSION     WP_004740327.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 204)
  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 204)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 204)
  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 11459477
            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="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=21975
     Region          1..202
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 melydseeqq veaikdwwke ngkavifgav iglgglfgwr yyqdsvvear eaasesytav
       61 isaldakgvd aqsdiqafid ankdaeysvl aamqlakvqv qagdlsaale qlewakaatk
      121 daalspllty rvarikaeqg efdaalsdla avtdeswkgr vaelrgdisl rkgdtdaays
      181 ayteaqqavd asqtlqikld dlak
//
LOCUS       WP_004741876             271 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Vibrio splendidus].
ACCESSION   WP_004741876
VERSION     WP_004741876.1
KEYWORDS    RefSeq.
SOURCE      Vibrio splendidus
  ORGANISM  Vibrio splendidus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Vibrio splendidus"
                     /db_xref="taxon:29497"
     Protein         1..271
                     /product="formate/nitrite transporter family protein"
                     /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=28824
     Region          5..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mstdfkpaef vqtmidvgea ktktgtrdll irstmagiil slavvvaitt ivqtgigivg
       61 alvfpvgfvi lsvmgydlvt gvfglaplak fdnrpgitwg rilrcwglvg lgnligsliv
      121 aflvavsltg nfslepnava qkfiavstgr slgfenmgmd gwitcfvrgi fcnlmvclgv
      181 ignmtartvs grvammwfpi ftffalvfeh tvvnmflfpl gmilgadfgi atwlnfnlip
      241 tilgnivggl fltcvplflt hartapslga k
//
LOCUS       WP_004742156             145 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: pilin [Acinetobacter].
ACCESSION   WP_004742156
VERSION     WP_004742156.1
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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..145
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14712
     Region          2..141
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mnaqkgftli elmivvaiig ilaaiaipay qdyiarsqms ealnlsdslk tnvtetygqi
       61 gtftgissga ngipasttvv gkyvsgvavq dgvitatmas snvskgiqgk tltltptdkg
      121 gsvtwactsn aeqkylpkac tggts
//
LOCUS       WP_004743119             193 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Vibrio tubiashii].
ACCESSION   WP_004743119
VERSION     WP_004743119.1
KEYWORDS    RefSeq.
SOURCE      Vibrio tubiashii
  ORGANISM  Vibrio tubiashii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 193)
  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 193)
  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   3  (residues 1 to 193)
  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   4  (residues 1 to 193)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 193)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Vibrio tubiashii"
                     /db_xref="taxon:29498"
     Protein         1..193
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22110
     Region          <78..193
                     /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"
ORIGIN      
        1 mhknlsknpl iicsdrveel arlstllaqe fdniiscqln qfeqmldrep nayvvvgwlq
       61 psaelrvvie ecrvrkhpll vvlkqldsnd isrlpermdy vlvpadtefc ltpwianacq
      121 irrsvvaled eieqlelrle erkiierakg llmkmhqvde daaykamrks amqssqtlaq
      181 vaknllqtle alk
//
LOCUS       WP_004743121             457 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein [Vibrio
            tubiashii].
ACCESSION   WP_004743121
VERSION     WP_004743121.1
KEYWORDS    RefSeq.
SOURCE      Vibrio tubiashii
  ORGANISM  Vibrio tubiashii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 457)
  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 457)
  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 457)
  AUTHORS   ter Beek,J., 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 457)
  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 457)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Vibrio tubiashii"
                     /db_xref="taxon:29498"
     Protein         1..457
                     /product="CmpA/NrtA family 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=50942
     Region          30..311
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mkwksaikrt lvgaaltttf yvpstlaelg epeledlkfg fikltdmapl avayekgyfe
       61 deglyvtlea qanwkvlldr vidgeldgah mlsgqplgat igigtqaevi tafsmdlngn
      121 aitvsnktwq qmkpniptea dgklvhpika dalkpvvesy ldkgkpfnmg mvfpvsthny
      181 elrywlaagg ihpgyyapks gdnsgqlnad vllsvtpppq mpatmeagti egycvgepwn
      241 qqavfkgiga pvvtdyeiwk nnpekvfgvs kswaekypnt hirvvkalir aahwldennn
      301 anrveavkll akseyvgadf eviansmtgt feyekgnvre vpdfnvffrh natypyysda
      361 iwyltqmrrw gqipeeksdd wymdvakevy rpdiyqqaaq aliedgvlns kdfpdfated
      421 gfrapqthfi dnivydgrsp naylekfsig lkgkdkv
//
LOCUS       WP_004743910             321 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Vibrio
            tubiashii].
ACCESSION   WP_004743910
VERSION     WP_004743910.1
KEYWORDS    RefSeq.
SOURCE      Vibrio tubiashii
  ORGANISM  Vibrio tubiashii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 321)
  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   2  (residues 1 to 321)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Vibrio tubiashii"
                     /db_xref="taxon:29498"
     Protein         1..321
                     /product="aminoglycoside 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=36524
     Region          62..262
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mqynyqplvs elgystlhsl dvlqtlwggy gelvrlyvdn tsvivkhvll pkpkhhpkgw
       61 ntdvshqrkl rsyqvelnwy qfaakrchak vpttlmvkqp eqelllvmed lkqvgftevv
      121 ttpsqhhlra clgwladfha qhighqgegl wevgtywhla tradelqals dvglkaraeq
      181 idsvlqnalf ttlvhgdakl anfcfspdgk naaavdfqyi gkgcamkdva lfmssavepq
      241 qcaemeawil deyfaalrla lqthqphlsa eeveaawrpl faiawadfqr fvkgwspehw
      301 kindyterlk dralemlkay p
//
LOCUS       WP_004743912             244 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Vibrio tubiashii].
ACCESSION   WP_004743912
VERSION     WP_004743912.1
KEYWORDS    RefSeq.
SOURCE      Vibrio tubiashii
  ORGANISM  Vibrio tubiashii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  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   3  (residues 1 to 244)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Vibrio tubiashii"
                     /db_xref="taxon:29498"
     Protein         1..244
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26738
     Region          52..221
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mntqaaaike qptrsasdrn vstlnstdal amiehggelt igittpvgtt frcktsfigt
       61 hsgnvilael pklseddlnf ffqegfwati raisprgega ivhfrgqlqh vlkapvpift
      121 lsvpqtmqvt qlrkeprfdv nlaarviaet hkldceirdl sksgcrfita plsrpfqigd
      181 eialnvqlss qkgaefaply gkvcnlqrsl hyarygvaft ddgkenakvl lghlkfdgtk
      241 ltlr
//
LOCUS       WP_004744161             411 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [Vibrio].
ACCESSION   WP_004744161
VERSION     WP_004744161.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 411)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 411)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..411
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=45748
     Region          18..406
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mlkaaltvkr tlstgekvlv gklvenskqs ffqfdeayls ghstslapfn lkpdtslqva
       61 pkephygihg vfgdslpdgw glylmdrvfr qnghnpkevt alerlaylgd rcmgalsyep
      121 eldlldeske sidiitlgra aieefegtes allehlmntg gsggarpkmn vtrlsngqys
      181 tlddalgtkl ivkltsekfd lkhseslvey cymqmarnvg ievpdfhlid aghgrfwleq
      241 erfdcteqgg rihmisacgl ldapfrepsl dyvdlvkatr imcsitesqk likrcmfnyl
      301 tvnqddhskn fsflasdadn wtlspfydiv yspnpykehm tafggngrtp ksamdqlaaq
      361 sglsskkaim vmaeeifett rsfsheakhl glspnlikei dkgmvekfka l
//
LOCUS       WP_004744639             575 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Vibrio tubiashii].
ACCESSION   WP_004744639
VERSION     WP_004744639.1
KEYWORDS    RefSeq.
SOURCE      Vibrio tubiashii
  ORGANISM  Vibrio tubiashii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 575)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Vibrio tubiashii"
                     /db_xref="taxon:29498"
     Protein         1..575
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=65564
     Region          <366..574
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mfysfnlcdd nsldlvlsgs qlysvendnk kretdldere rfvleflinn ssvdnpisln
       61 dldsayrsie cketerepwq ttirrlqskf krlttgygqs inekrlisnv cqkgyyvdlt
      121 rstmttpqnt dlklsdfkps lflmlgsflm tykmmllrks arvllyvgvi tslfyslhiy
      181 qltsiveqfr gnidhvaqel tslgchddet lsafnhslyl dsallispfd scfvdrdsve
      241 llstdyvnsl lnlpqfvysv rdndetyttm igrvslrave smysnnlwsl lvdglviqym
      301 neeevaigqs ggiriktkvl ssgttvsfya snlvveivsl ffvvsfalhw rkvarfirfc
      361 qdwtlldyel epvvdtkkkt tiyeeiltrv tqrsalqyie nlaenrlitf htillakvia
      421 nanrkgsagv yginicpssl lgdnyfilek hlsrlrpsev vleltensnl pydkeicani
      481 tklqqrgfki alddfgtgnn nvevvqkisp dylkidkefi rdidsneakq rllgmlseig
      541 amsacdiiqe gvetyaqqlt lqslgynlhq gylyv
//
LOCUS       WP_004745949             349 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter baumannii].
ACCESSION   WP_004745949
VERSION     WP_004745949.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 349)
  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 349)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 349)
  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   4  (residues 1 to 349)
  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 349)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..349
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39902
     Region          47..210
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          257..332
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqeftisngy fylwntylke kgidwqtlnl seiqtrqvqn ilsasidaqs sldlfielle
       61 itetrlhvtn lalemaacit panfgvlgym asrsdtlgqv veyiakfhrl vidgaqvvpi
      121 qieqdaskir lywplvddsn illseltlaa mvqlakqiap vhefllqhve fvhrargpvv
      181 hyqrffqckl sferpyyalt faseslnvrp qhadptlvql lvkqaeealv qrkihadlvq
      241 qihwivqeyf khkqqapkie diaielnvsv rslqrqlqal ntsfklilda ermkrceill
      301 sqnesltvia dqlgysdqsa larayknltg qtlltrkkql qliqknatk
//
LOCUS       WP_004746126             185 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Vibrio tubiashii].
ACCESSION   WP_004746126
VERSION     WP_004746126.1
KEYWORDS    RefSeq.
SOURCE      Vibrio tubiashii
  ORGANISM  Vibrio tubiashii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Vibrio tubiashii"
                     /db_xref="taxon:29498"
     Protein         1..185
                     /product="TRAP transporter small permease subunit"
                     /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=20669
     Region          17..179
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mskvlystpt vpmychierl ittaskalaw tnlalvavii iqvvlrkvfs ngqialeelq
       61 whlyatavmf gtayaqisnl hvrvdlfyhk fserkkalvd ligltllaip fvaivilhsy
      121 dfayeswrvn essaspsglp yrwliksvip lsftmlllsm larilrnlet lfggeqskga
      181 nhgse
//
LOCUS       WP_004746515             339 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter baumannii].
ACCESSION   WP_004746515
VERSION     WP_004746515.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 339)
  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 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 339)
  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   4  (residues 1 to 339)
  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 339)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..339
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38645
     Region          22..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          252..332
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mnpslpgtyv slmadvvqkl nvspeelleg sgvsveqlle pfwyldfnif nnllnravel
       61 tnepalgiyl glqmtvschg svglaamvsq nlgealnvme qfiglrcpal kprleienel
      121 aflyldqpmt nfkmgivgmt flmvgfaqms naitgqklei kaelnypepa fleqvqellp
      181 ceiqfnqpfn rlvfsenfla lplimadpla arlareqckh dlnklaakrg ekhpltalvr
      241 ellfdevegf fkmkdvaekl hltertlqrq lakegvtfqi lldqvrerha kkllnhheys
      301 isyiseklgy sevthftraf krwtnqtpkq yrnlreeqe
//
LOCUS       WP_004747349             242 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio tubiashii].
ACCESSION   WP_004747349
VERSION     WP_004747349.1
KEYWORDS    RefSeq.
SOURCE      Vibrio tubiashii
  ORGANISM  Vibrio tubiashii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 242)
  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 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   3  (residues 1 to 242)
  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   4  (residues 1 to 242)
  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 242)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Vibrio tubiashii"
                     /db_xref="taxon:29498"
     Protein         1..242
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27539
     Region          <70..239
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          159..237
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mdfrifkpcg klsdhiqaiw sinvtggqgg vvkkplycdg gsgltlllrg evclsntpis
       61 dpiivqkynh rtqiielshg allcgirfqp gmmlpslinn dtqimsvlma lheqmseqnq
      121 srnlttlyrw ceqqilplda dfakramlik latqgkigeq fpynqrqver rfrqwlgmsp
      181 kyfqrlrrvh sslsklrenp dvslvdfafe hgfsdqahmt refkaflltt pgelsrrlkt
      241 ts
//
LOCUS       WP_004747174             341 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter baumannii].
ACCESSION   WP_004747174
VERSION     WP_004747174.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 341)
  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   6  (residues 1 to 341)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39503
     Region          29..208
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          102..341
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mnglnkplyr rriseiyvql lfeyleklgh dpekvlgepw pkadsnhleg vdidhwesll
       61 iiakdylndp figlhvgqti taqhlgvlgs vflacenlga vlerferyqr lvydvypatv
      121 riyteyvels wdtkgeqvgp lsdetgrtvi vqfcrslirg kerlkeihfi herpenvqpy
      181 eeyfgcpvlf eqpvalmrfd keilslplkn sdaalvaile khadkllasl phsdeitdqv
      241 rkqiayllhq geptieqlae rlnysrrtlq rrlteagtnf rkelntvrye laksylkdlr
      301 lqiveialll gyaehspftr aykewsgktp qqareemnel r
//
LOCUS       WP_004747758             786 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Vibrio tubiashii].
ACCESSION   WP_004747758
VERSION     WP_004747758.1
KEYWORDS    RefSeq.
SOURCE      Vibrio tubiashii
  ORGANISM  Vibrio tubiashii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 786)
  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 786)
  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 786)
  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   4  (residues 1 to 786)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..786
                     /organism="Vibrio tubiashii"
                     /db_xref="taxon:29498"
     Protein         1..786
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88003
     Region          70..786
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mtiqrleanq lylsaelekl qskstkelap ideivgqera qkavefamsi kekgyniyai
       61 gqnglgkrtm ilrylnrhqh daaalfdwcy vanfedirtp kvlklpcgvg skfkqdiekl
      121 msklvnampl afdnelyysr adklknqlat kqeaelavit keakskgisl tittqgdyqf
      181 vamngeelht eesfeelsnk eqeyfgdtid elevqlrnmv rqlteweeay tekikklnde
      241 vtldvithfi kqlkkdysgy paiksyltel qqdivdnadi fleqsaeqge vatasldkkl
      301 prrykvnvlv srkneefpiv veenpnyhtl fgyietatfk gtvftdfsli rpgslhkang
      361 gvllmdaqkv leqpyvwdgl kralrarqls ftslekevtl tgtvsldpea ipldvkiilf
      421 gdyrtyqllq hydpefself rvtadfedem trnadselqy akfissvvnd ncmlhcdrka
      481 iariiehssr lagdqnkisl hsanianllr esnyvarqan snmirsshve ealsnqelrv
      541 srlkdsvmes fingttliht hgqavgqvna lsvlstseym fgapnritat tcygegevid
      601 iersvdlggs ihskgvmilt aylssvfgkt akvplsttit feqsyggvdg dsasmaefca
      661 vvsafskqpn rqdiaitgsm nqfgesqpig gvnekiegff dvceikgrtn eqgviiprsn
      721 mhnlmlrpdi vkavekgefh iwaidhvtea ielftgkaag tpsdegsypi dtvfgiaqak
      781 lnalrk
//
LOCUS       WP_004752349             712 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Leptospira kirschneri].
ACCESSION   WP_004752349
VERSION     WP_004752349.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kirschneri
  ORGANISM  Leptospira kirschneri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 712)
  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   3  (residues 1 to 712)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Leptospira kirschneri"
                     /db_xref="taxon:29507"
     Protein         1..712
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79967
     Region          1..700
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdlsevrdtf iseseellss mesnllilek dsknnegihs vfraihtikg tsgmfgyepi
       61 ekfthevesf ldkirsnkqs ltkegieflf lacdhirnll qgvgetlivd sqtsrnqvnl
      121 lslakklild dtsnpqkyev iqnqptssnh ldfhsnstfw qitlipnihl fesgldpstf
      181 ikylsqsgkv khifiypdsi pnwsefnpeh shlgfeisye spskgeeihs tfqflkegsy
      241 lkilapgcsl nlfmenyndf pfgkkaylna leiqkiltpe eiqklsytse nlniphttqt
      301 eqlstsienq kesdsiklqt ktlrvdsski dtlialvgel itqeanlsrk isdsenlqli
      361 esseslyrlv teirefalsl rmipisdlfe kykrvvrdls kelnkqvele iiggeteldr
      421 sviekisdpi vhilrnaldh gietseerir kgkpatgqlk iqashgtgsi lieinddgkg
      481 ldcdkileka iskglitrdq nlseseiysl ifqpgfstad qvtnlsgrgv gmdvvlrnie
      541 slrgtvqiqt lkdqgssfli rlpltlaiid gflvkaysly fivpmqmvre tveskvilng
      601 sssgtmnlrg ellpvlhlse flclesnsfk kenilileye dksfgiivnd lhgevqsvir
      661 pmaeifknik cfsgtsilgs geiafildvp glynsirdqe lnknkdltak tg
//
LOCUS       WP_004752605             114 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [unclassified
            Acinetobacter].
ACCESSION   WP_004752605
VERSION     WP_004752605.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 114)
  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   3  (residues 1 to 114)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 114)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..114
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12367
     Region          3..114
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mlqprmggii qanitdrvtl qasympfvng gglfissqqp vrlgqevfvl atlpdqsqki
       61 pltgkviwin ykesvakpqg faiqltndkg ayykaeaekl lagslslnhl syti
//
LOCUS       WP_004752735             204 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Leptospira kirschneri].
ACCESSION   WP_004752735
VERSION     WP_004752735.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kirschneri
  ORGANISM  Leptospira kirschneri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Leptospira kirschneri"
                     /db_xref="taxon:29507"
     Protein         1..204
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=22847
     Region          1..197
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mklvlgiaga sgsiyaerfi kalftiegtt flvcsnaslr vfreemrckv ssskelldfi
       61 vskykiqttr hkfeirsftd igadiasgsn fwkamvilpc smkmiasina gltenliera
      121 advtlkerrn livvpretpy nrihlknmle lhdaggiilp aspgfyqlpk tledlgdfis
      181 ekifkllgme lnlyppwtpk ntee
//
LOCUS       WP_004750725             356 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Leptospira].
ACCESSION   WP_004750725
VERSION     WP_004750725.1
KEYWORDS    RefSeq.
SOURCE      Leptospira
  ORGANISM  Leptospira
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Leptospira"
                     /db_xref="taxon:171"
     Protein         1..356
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=40096
     Region          1..352
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mgievknlvk rfgnftaidd lsldvpsgel vallgpsgsg kttllriiag ledadkgqvi
       61 fegrevgkkn akdrgvgfvf qhyalfrhmt ifeniafgle vrrraerpsk nvikdkvmsl
      121 lklvqlenfh nrypselsgg qrqrialara laieprflll depfgaldak vrkelrnwlr
      181 rlhdeihits vfvthdqeea levsdkvvil rsgkieqvgt pdevynhpkn sfvfhflgdv
      241 nlfhgrvqgg qtqlgeikvd apehseiena savgyvrpyd veilrepiea qtipaeiqyi
      301 hstgrnvkid lkrldtgtil esqlnssefq slnllpgetv hirfkkikvy vedyti
//
LOCUS       WP_004754200             391 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Leptospira kirschneri].
ACCESSION   WP_004754200
VERSION     WP_004754200.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kirschneri
  ORGANISM  Leptospira kirschneri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 391)
  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 391)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 391)
  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   4  (residues 1 to 391)
  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 391)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Leptospira kirschneri"
                     /db_xref="taxon:29507"
     Protein         1..391
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45468
     Region          120..372
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          294..372
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mdffpdlnfi dyliflkevl nryleylysa sivisfltgl sgfykatknr lnfvrgiflm
       61 sacfliighs kafslmtsdp ngmlnlekrv ffsyyygfav caslsstfyv mylfgvlqnp
      121 lrlslysfls fpiiflislm ienlisivyf gksvlftlqf sagifnlyya iknkmkkiyl
      181 nypvqnftlc taliihsigm wldapnlmil alsftgffii yffileynhp efwkvsfsse
      241 lmevksedsk tqtlqtnpkn lverldisri eekiqkfved reyldeeirl sdfsayigls
      301 lhqasyylnn ykdlsftdfl sfhrleeakr mieqrpdinl levalasgfn spssfrracl
      361 kftgkppkef rnyvlhqtip sitlelqnql g
//
LOCUS       WP_004754321             336 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter sp. ANC 3789].
ACCESSION   WP_004754321
VERSION     WP_004754321.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. ANC 3789
  ORGANISM  Acinetobacter sp. ANC 3789
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 336)
  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   6  (residues 1 to 336)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Acinetobacter sp. ANC 3789"
                     /db_xref="taxon:1217714"
     Protein         1..336
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38362
     Region          22..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <137..336
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mgqqtdasvv lrlgyqalrr aglsteqilt qagvamsqle tnqrtpvsaq nafwlaaeqv
       61 sqdpdiglhl gehlplyrgq viehlfmsse nfgeglqral ayqrlisdaf qaqlvcengr
      121 cyltngtqar pnrllnrhfs ecavsgvlrf fkfltegqfq pifidfnfqe gaapeeyfrv
      181 yecpvslgqk etrlyfdpai lkhplwqadp dllqlheqla neklqelary dlvdevrrai
      241 gatleqgett lesvaaqlqi tprrlrtlln daqtsfqqil sayrcrlakk llanthesie
      301 kivyltgfae pstfyrafkr wtnetpieyr krkqrd
//
LOCUS       WP_004754710             422 aa            linear   BCT 20-JAN-2025
DEFINITION  TerD family protein [Acinetobacter sp. ANC 3789].
ACCESSION   WP_004754710
VERSION     WP_004754710.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. ANC 3789
  ORGANISM  Acinetobacter sp. ANC 3789
            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 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Acinetobacter sp. ANC 3789"
                     /db_xref="taxon:1217714"
     Protein         1..422
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=46198
     Region          6..422
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mqliagantv lptpsvelvi rarvpqaidl ditayllaqt tqkvrgdtdm ifygqthtpn
       61 qsiqlfesas qpdhltriri ntaqldsaig kiaicatlte pahirdlqql sidllsdghv
      121 vatseintqs ktekalilae vynhngrwky rfvdqgfngg lkplaenfgv evaepsaapp
      181 qpqpspsvap pttsnnanif gqpvssttpt aqptpppssi nlskirldkp nssinltkyn
      241 gsfgkiqvnl nwnrsggdrg ksffrklsas qsvdldlgam iemqngaihi vqalgnrfgs
      301 yekspyaelq gddrtgssln genlwingeh wdqikriviy tyiyegaanw aatdaivnmq
      361 lpnqppievp vneggylstc aivelknvgg qiqanrqvqy fddqqkldeh ysfgfrwtvg
      421 rk
//
LOCUS       WP_004755251             308 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Acinetobacter sp. ANC
            3789].
ACCESSION   WP_004755251
VERSION     WP_004755251.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. ANC 3789
  ORGANISM  Acinetobacter sp. ANC 3789
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   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 308)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Acinetobacter sp. ANC 3789"
                     /db_xref="taxon:1217714"
     Protein         1..308
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34491
     Region          19..67
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msldatlwaw kapvntapqr lvllsladra gedhtcfpsy erlvqdtlln rktvvkvvse
       61 lielglirdt gerkgatkqv kvykllnvvg reestpklkq sqkrnsteig tlnspkngtl
      121 nspkfgtqnl ssnlpieskn knswlslkil kkelelatds etiehiktak wferelsafe
      181 nfnadkkhnp avmhylfadw llrnmskyqp qtekpqagks snkatglsek qiqafakkls
      241 llpeiatkya qgtetydqla irlaqklqnp seakklepyl hqvgfsgvln evaarlvpkk
      301 kkhavcak
//
LOCUS       WP_004755292             248 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 16S rRNA (cytidine(1402)-2'-O)-methyltransferase
            [Leptospira].
ACCESSION   WP_004755292
VERSION     WP_004755292.1
KEYWORDS    RefSeq.
SOURCE      Leptospira
  ORGANISM  Leptospira
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Zhao,M., Zhang,H., Liu,G., Wang,L., Wang,J., Gao,Z., Dong,Y.,
            Zhang,L. and Gong,Y.
  TITLE     Structural Insights into the Methylation of C1402 in 16S rRNA by
            Methyltransferase RsmI
  JOURNAL   PLoS One 11 (10), e0163816 (2016)
   PUBMED   27711192
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Kimura,S. and Suzuki,T.
  TITLE     Fine-tuning of the ribosomal decoding center by conserved
            methyl-modifications in the Escherichia coli 16S rRNA
  JOURNAL   Nucleic Acids Res 38 (4), 1341-1352 (2010)
   PUBMED   19965768
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Kozbial,P.Z. and Mushegian,A.R.
  TITLE     Natural history of S-adenosylmethionine-binding proteins
  JOURNAL   BMC Struct Biol 5, 19 (2005)
   PUBMED   16225687
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001055
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Leptospira"
                     /db_xref="taxon:171"
     gene            1..248
                     /gene="rsmI"
                     /GO_function="GO:0070677 - rRNA
                     (cytosine-2'-O-)-methyltransferase activity [Evidence
                     IEA]"
     Protein         1..248
                     /product="16S rRNA
                     (cytidine(1402)-2'-O)-methyltransferase"
                     /EC_number="2.1.1.198"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0070677 - rRNA
                     (cytosine-2'-O-)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0000451 - rRNA 2'-O-methylation [Evidence
                     IEA]"
                     /calculated_mol_wt=27926
     Region          9..228
                     /region_name="RsmI"
                     /note="16S rRNA C1402 (ribose-2'-O) methylase RsmI
                     [Translation, ribosomal structure and biogenesis];
                     COG0313"
                     /db_xref="CDD:440082"
ORIGIN      
        1 mriefqktlv lvsvslgnpg dltarakell ehsdiligee pqitskllks isvskqfflc
       61 nehttpeeir nlgeavinsg lsvlvsdagt pgiedpgrel vqevlkrggn vrsapgpiaf
      121 gavlsisgfk ispftfcgff srdsaerkke liyylkpght ivfyetpyry ksvlrdldwv
      181 fkktkddrei ffcldltlds efqfrgkled llkildtlpk gnpvivlsqr kekqdrfskt
      241 kklkrvsr
//
LOCUS       WP_004756189             335 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004756189
VERSION     WP_004756189.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 335)
  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 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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 335)
  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   5  (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   6  (residues 1 to 335)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38234
     Region          22..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <146..335
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mgqltdasvv lrfgyqairk aglpteeilt kagvalnqid tnartplsaq nafwiaaqev
       61 sndpdiglhl gehlplyrgq viehlfisse tfgeglkral ayqrlisdaf daklviqdgr
      121 cylsngeqyw sdnlvnrhfs ecamsgilrf fkfitegqfq piyidfnfne gadddeyfrv
      181 ygcpvslgqk etrlyfddav ldyplwqaep ellqlheqla ieklqelary dlvgevrrai
      241 gstlesgett letvaaqlni tprrlrtqls eantsfqqil sdyrcrlakr llastnesve
      301 rivyltgfse pstfyrafkr wtnetpveyr krkqr
//
LOCUS       WP_004757691             356 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Acinetobacter].
ACCESSION   WP_004757691
VERSION     WP_004757691.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..356
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39761
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvkniek hfgafhalkn isldfpegel vallgpsgcg kttllriiag lesadggqvl
       61 legedatnih vrerqvgfvf qhyalfrhmt vfdniafglr vrpratrpte aeikkrvtrl
      121 ldlvqlgfla drypaqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 tlhdelhits ifvthdqeea levadqiivm nkgdveqigs prevyekpat pfvfdflgqa
      241 nrfegehtgg iirlgddriq lptaidapqg kviafarpne lhihaqpqpn tieatflrev
      301 wiagkviael qdrsgrniei llsveeanlh qfkpnqtvwi saaqlhlfad qttqva
//
LOCUS       WP_004759356             391 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Leptospira kirschneri].
ACCESSION   WP_004759356
VERSION     WP_004759356.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kirschneri
  ORGANISM  Leptospira kirschneri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 391)
  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 391)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 391)
  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   4  (residues 1 to 391)
  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 391)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Leptospira kirschneri"
                     /db_xref="taxon:29507"
     Protein         1..391
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45496
     Region          120..372
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          294..372
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mdffpdlnfi dyliflkevl nryleylysa sivisfltgl sgfykatknr lnfvrgiflm
       61 sacfliighs kafslmtsdp ngmlnlekrv ffsyyygfav caslsstfyv mylfgvlqnp
      121 lrlslysfls fpiiflislm ienlisivyf gksvlftlqf sagifnlyya iknkmkkiyl
      181 nypiqnftlc talivhsigm wldapnlmil alsftgffii yffileynhp efwkvsfsse
      241 lmevksedsk tqtlqtnpkn lverldisri eekiqkfved reyldeeirl sdfsayigls
      301 lhqasyylnn ykdlsftdfl sfhrleeakr mieqrpdinl levalasgfn spssfrracl
      361 rftgkppkef rnyvlhqtip sitlelqnql g
//
LOCUS       WP_004759825             360 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter sp. CIP
            102129].
ACCESSION   WP_004759825
VERSION     WP_004759825.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CIP 102129
  ORGANISM  Acinetobacter sp. CIP 102129
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 360)
  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 360)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 360)
  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   4  (residues 1 to 360)
  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 360)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Acinetobacter sp. CIP 102129"
                     /db_xref="taxon:1144664"
     Protein         1..360
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41208
     Region          29..218
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <147..353
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          265..346
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mrdpfglfqe tisvsyahll leivhdyaid tetvlagtgl mltemkqada kmsahqwskl
       61 vvnalrltgn prlgieygfk lrptshgalg faflsctdve taltlcqqyf ctriqnftpe
      121 sfidedfvyv yldgvhpvkf gnqqqsdqlr hfliesllfg aiyflgvfse kivercevfv
      181 dwsdaqnykr idlsqikihf nqqrnglrfp kqylhcknpn adqvafqqal lycendklkl
      241 vkettrdlqk siksellyns sngyptlpli aqrlnmsert ikrhlqaqgt tflqilaevr
      301 fsqarkllqq pqytiqnvag lvgyeeatnf irafkkmfge tpsqyrksyl skatssditn
//
LOCUS       WP_004760535             137 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Acinetobacter sp. CIP 102129].
ACCESSION   WP_004760535
VERSION     WP_004760535.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CIP 102129
  ORGANISM  Acinetobacter sp. CIP 102129
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Acinetobacter sp. CIP 102129"
                     /db_xref="taxon:1144664"
     Protein         1..137
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14341
     Region          1..137
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mqkgftliel mivvaiigil aaialpayqd yvlksritaa fheissgkss yeifvnhqys
       61 tilspadisl nnetsicsis annpdntgta akaivctlkn tvglstgaei yisrssdgvy
      121 ncgttgiaak yrpngcs
//
LOCUS       WP_004760823             142 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Acinetobacter].
ACCESSION   WP_004760823
VERSION     WP_004760823.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 142)
  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   2  (residues 1 to 142)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..142
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15746
     Region          72..140
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mtlphpcsky navllillcv gclshlhaqq fdqsygqwka qqqardqqla kqpnnnyyls
       61 rptqqtsskp vsssvnqqgd kislnqanvq qlqtlngvge kkaqaiveyr qknggfktid
      121 elvnvkgigp klleknkarl ml
//
LOCUS       WP_004761434             396 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TerD family protein [unclassified Acinetobacter].
ACCESSION   WP_004761434
VERSION     WP_004761434.1
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 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..396
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=43865
     Region          1..396
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mqqltaganl vlaqpqcqik iktalpahid ldvsayllna qnkvrgdadm ifygqkhtln
       61 rsvelieana ktpylaqfnl ntqlldleln kialcatidg qsainalqni evelwqngql
      121 sataivnsae ktekalilae vyrykdqwkf rfvsqgfngg lkplaeyfgv eindqpntpp
      181 papvatppqs kinlskitld kgnsrinltk qtqgfgeiki nlnwnqrsiq pqsagffkkl
      241 lnqnqgidld lgclfemqdg tksviqalgn rfgdfngfpf iqlsaddrtg alqggewlri
      301 ngqywqeirr vvlfafiyeg vpnwaatdav vtifvpdqpp ieirltegqp lgmcgivelt
      361 nqagniqvqr hvryvpghke ldqafgfglr wvagsk
//
LOCUS       WP_004761598             356 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [unclassified Acinetobacter].
ACCESSION   WP_004761598
VERSION     WP_004761598.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..356
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39776
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvkniek hfgafhalkn isldfpegel vallgpsgcg kttllriiag lesadggqvl
       61 legedatnih vrerqvgfvf qhyalfrhmt vfdniafglr vrpratrpte aeikkrvtrl
      121 ldlvqlgfla drypaqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 tlhdelhits ifvthdqeea levadqiivm nkgdveqigs prevyekpat pfvfdflgqa
      241 nrfegehtgg iirlgddriq lptaidapqg kviafarpne lhihaqpqpn tieatflrev
      301 wiagrviael qdrsgrtiei llsveeanlh qfkpnqtvwi saaqlhlfad qttqva
//
LOCUS       WP_004762523             712 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Leptospira kirschneri].
ACCESSION   WP_004762523
VERSION     WP_004762523.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kirschneri
  ORGANISM  Leptospira kirschneri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 712)
  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   3  (residues 1 to 712)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Leptospira kirschneri"
                     /db_xref="taxon:29507"
     Protein         1..712
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79986
     Region          1..700
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdlsevrdtf iseseellss mesnllilek dsknnegihs vfraihtikg tsgmfgyepi
       61 ekfthevesf ldkirsnkqn ltkegieflf lacdhirnll qgvgetlivd sqtsrnqvnl
      121 lslakklild dtsnpqkyev iqnqptssnq ldfhsnstfw qitlipnihl fesgldpstf
      181 ikylsqsgkv khifiypdsi pnwsefnpeh shlgfeisye spskgeeihs tfqflkegsy
      241 lkilapgcsl nlfmenyndf pfgkkaylna leiqkiltpe eiqklsytse nlniphttqt
      301 eqlstsienq kesdsiklqt ktlrvdsski dtlialvgel itqeanlsrk isdsenlqli
      361 esseslyrlv teirefalsl rmipisdlfe kykrvvrdls kelnkqvele iiggeteldr
      421 sviekisdpi vhilrnaldh gietseerir kgkpatgqlk iqashgtgsi lieinddgkg
      481 ldcdkileka iskglitrdq nlseseiysl ifqpgfstad qvtnlsgrgv gmdvvlrnie
      541 slrgtvqiqt lkdqgssfli rlpltlaiid gflvkaysly fivpmqmvre tveskvilng
      601 sssgtmnlrg ellpvlhlse flclesnsfe kenilileye dksfgiivnd lhgevqsvir
      661 pmaeifknik cfsgtsilgs geiafildvp glynsirdqe lnknkdltak tg
//
LOCUS       WP_004762611             531 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase, partial [Leptospira kirschneri].
ACCESSION   WP_004762611
VERSION     WP_004762611.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kirschneri
  ORGANISM  Leptospira kirschneri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 531)
  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 531)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Leptospira kirschneri"
                     /db_xref="taxon:29507"
     Protein         <1..531
                     /product="M4 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]"
     Region          <26..481
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 ipttpptlpd tnygicfpdq tpcikqgsas trfsgvktit tytsgeenhy elkdysrgng
       61 iytyswefiq epddtfqfln ipivdanngw skfeyhddyn hdalldahwg iemtydyfks
      121 ihnwlsfdgn dskvvnnvhy velfaannaf wnpiteeify iycphnsvck tfgiprildp
      181 tyedftsldv vshefghgin gaiaglnydp epyalnegfs diwniavnny vnkvlgmqkn
      241 lwliadetvp gggmrsaenp ksttvlypgp ntyhgdlwdf ednephtnsl vlshwfytls
      301 kgkqgtndhh cgynvsgini ekaekiayks lhqlfptagy ssartaaiys akalygkfss
      361 evkstidawd avgvpaetts rggqgmvkpq hyitfvklsn lerssgndcg ykdnsylhpt
      421 vylgatynmv lssegspsnp pkahrwrvwi dfnrdgsydf semvvqdsin dtlggtlqks
      481 ikipttalig dtkmrvsmka vegnetyprf desfvegeve dysitinnfs l
//
LOCUS       WP_004766525             525 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Leptospira kirschneri].
ACCESSION   WP_004766525
VERSION     WP_004766525.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kirschneri
  ORGANISM  Leptospira kirschneri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 525)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Leptospira kirschneri"
                     /db_xref="taxon:29507"
     Protein         1..525
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=60251
     Region          282..516
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 miseysdlyv enkalssdty syslynlegk qlysepnynp lldldpklkk averfidygn
       61 snistfrrfk ndrniqlmvr sendriykvn feintkggyv laliestrnl ssteknriqr
      121 frslkhdlvr tlklektyfy linieiynhp flhkyetqiy eavfldlhte fltitnsqnv
      181 glristnqif fayqinkpdv dinwipssli symkntiqid nhefhlklsi gglhtseant
      241 splnilkglr anlrkvidsp fsrystqnqn dssnliatyl slrnsvhkke lllyyqpivn
      301 senkslhsle alsrwnhsak gmispdifip laeesgliss igtwviqnal ldlsqiqknn
      361 sfsfnpmisi nispfqlknp efadnlisyf sqlnlhpssv vleitesrye etaliieqma
      421 ilkrfgfqia iddfgignsn fsriekiecd yvkldkslii gvdtnqskrs vlkaisqvlf
      481 slgkkmvfeg ienaelesia idyganflqg fyygkptqit dlssf
//
LOCUS       WP_004767406             531 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Leptospira kirschneri].
ACCESSION   WP_004767406
VERSION     WP_004767406.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kirschneri
  ORGANISM  Leptospira kirschneri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 531)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Leptospira kirschneri"
                     /db_xref="taxon:29507"
     Protein         1..531
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=60953
     Region          282..516
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 miseysdlyv enkalssdty syslynlegk qlysepnynp lldldpklkk averfidygn
       61 snvstfrrfk ndrniqlmvr sendriykvn feintkggyv lahiestrnl ssteknriqr
      121 frslkhdlvr tlklektyfy linieiynhp flhkyetqiy eavfldlhte fltitnsqnv
      181 glristnqif fayqinkpdv dinwipssli symkntiqid nhefhlklsi gglhtseadt
      241 splnilkglr anlrkvidsp fsrystqnqn dssnliatyl slrnsvhkke lllyyqpivn
      301 senkslhsle alsrwnhsak gmispdifip laeesgliss igtwviqnal ldlsqiqksn
      361 sftfnpmisi nispfqlknp efadnlisyf sqlnlhpssv vleitesrye etaliieqma
      421 ilkrfgfqia iddfgignsn fsriekiecd yvkldkslii gvdtnqskrs vlkaisqvlf
      481 slgkkmvfeg ienaelesia idyganflqg fyygkptqit dlssfqfqit s
//
LOCUS       WP_004768539             367 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein, partial [Leptospira
            kirschneri].
ACCESSION   WP_004768539
VERSION     WP_004768539.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kirschneri
  ORGANISM  Leptospira kirschneri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 367)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Leptospira kirschneri"
                     /db_xref="taxon:29507"
     Protein         <1..367
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          267..341
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 vvigfllgfs klfssdgfnk sygsvlqsaa fflilnngil idqgtlrnds rmlfgsyygl
       61 vlysslavfv cfqyvlesld npwiyckrll givpitills yfipnlyfis fidilgfais
      121 iftfgwslkk vlksnksily fnlpflsffi sicfvfdflg tvfnkkdffl ltemipgsvi
      181 cytivlerff pslfnktatv tipetdivne ieletipipe akglikykyp psnflegidi
      241 ekvniklnqf idikgfkdee irlpdfaaal gltvhkasrf lneyknmsft dflnyhriie
      301 vinymekktd fnllnialec gfnsassfhr acvkftgksp rnlksyiqsn egsshtilrk
      361 pkirshs
//
LOCUS       WP_004768728             537 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase, partial [Leptospira kirschneri].
ACCESSION   WP_004768728
VERSION     WP_004768728.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kirschneri
  ORGANISM  Leptospira kirschneri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 537)
  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 537)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Leptospira kirschneri"
                     /db_xref="taxon:29507"
     Protein         <1..537
                     /product="M4 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]"
     Region          <31..487
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 yeagggdttp ptppdtnygi cfpdqtpcik qgsastrfsg vktittytsg eenhyelkdy
       61 srgkgiitys wefledpfmg iyflnvpivd anngwskfey hddynhdall dahwgigmty
      121 dyfksvhnrl sydgndskvv nnvhyfngfi gnnaywepmt eeiyyvycph nssicksfnl
      181 pvildptyed ftsldivshe fghgvngdla gfslgmepga ldegfsdiwn vgvnnyvnkv
      241 lgmqkniwlv gdetvpgggm rsvsnpkstt vlhpgpntyy gglwdfedne phtnslvlsh
      301 wfytlskgkq gindhwceyn vsginiekae kiaytalhyl fptsgyisar saavyaakvl
      361 ygkfssevks tidawdavgv padttsrgge gmykphyyit svklsnlern sgndcgykdn
      421 sylhptiikg ftynmvlsse gavsipskih kwrvwidfnr dgnfessemv vqdtvnssyg
      481 gtlqksiqip ttaligdtrm rvsmkaaqsg eayprsdesf aegevedysi tinnfsl
//
LOCUS       WP_004768745             391 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Leptospira kirschneri].
ACCESSION   WP_004768745
VERSION     WP_004768745.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kirschneri
  ORGANISM  Leptospira kirschneri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 391)
  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 391)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 391)
  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   4  (residues 1 to 391)
  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 391)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Leptospira kirschneri"
                     /db_xref="taxon:29507"
     Protein         1..391
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45468
     Region          120..372
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          294..372
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mdffpdlnfi dyliflkevl nryleylysa sivisfltgl sgfykatknr lnfvrgiflm
       61 sacfliighs kafslmtsdp ngmlnlekrv ffsyyygfav caslsstfyv mylfgvlqnp
      121 lrlslysfls fpiiflislm ienlisivyf gksvlftlqf sagifnlyya iknkmkkiyl
      181 nypiqnftlc talivhsigm wldapnlmil alsftgffii yffileynhp efwkvsfsse
      241 lmevksedsk tqtlqtnpkn lverldisri eekiqkfved reyldeeirl sdfsayigls
      301 lhqasyylnn ykdlsftdfl sfhrleeakr mieqrpdinl levalasgfn spssfrracl
      361 kftgkppkef rnyvlhqtip sitlelqnql g
//
LOCUS       WP_004768827             472 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Leptospira kirschneri].
ACCESSION   WP_004768827
VERSION     WP_004768827.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kirschneri
  ORGANISM  Leptospira kirschneri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 472)
  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 472)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Leptospira kirschneri"
                     /db_xref="taxon:29507"
     Protein         1..472
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=55421
     Region          27..77
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mnenqrvyrv ekdrnftivk nnfiddtrls lkataillia lrypdnwkms vktiarfksd
       61 kessissglk elvsygyady rkrrdvitge fesgwyffee sqkpevqikp iriknkgfek
      121 qkilfeeken lfldfplsen pllenplpen pglenqplsn tiyqrlskqv lfkqiqntsr
      181 eygapaqthv kepkenliev etnkkenpki dlpqltnpll ekplpenpsq enqplsntiy
      241 qglskqvlfk qiqntsreyg alaqthaiep tskkinprfq fpsiwltnfq nyylkehgse
      301 mgqsdpdlka lnslfeiskg dwkiieskiq iliqlrkqds kfwyeqslsp esiskfwsrl
      361 ferkekqyek nrmrnektnq tkyneskpms dkpieikdld pykcflvwgk tkllkqqlef
      421 yeqnpdplky egtkkilfek fvnevypvlv snsevkksti enkkvttkei va
//
LOCUS       WP_004769621             297 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Leptospira kirschneri].
ACCESSION   WP_004769621
VERSION     WP_004769621.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kirschneri
  ORGANISM  Leptospira kirschneri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 297)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Leptospira kirschneri"
                     /db_xref="taxon:29507"
     Protein         1..297
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=34553
     Region          69..290
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mkeifdlppn adlwssksas ttdtqtlfpf nekyemalei ltefenlsiv dssnlktsst
       61 qsydgeiltq lteilktgnf hteyqpilsl etgkiyayea larfrikgen icpefifnel
      121 hqdpdlffef ekelkrfqir nrprdkhlfl nldphvcknr sqaaewrkll skkkdivcei
      181 ientdstlie ntrfcldvlr renvpialdd vggdqnlfcf nfleyskfik fdkcwlrlfk
      241 tkpsykniaw gfldfakesn mlcilegiet sedflmaaem gfplaqgylf qsrnvlv
//
LOCUS       WP_004770155             512 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase, partial [Leptospira kirschneri].
ACCESSION   WP_004770155
VERSION     WP_004770155.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kirschneri
  ORGANISM  Leptospira kirschneri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 512)
  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 512)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Leptospira kirschneri"
                     /db_xref="taxon:29507"
     Protein         <1..512
                     /product="M4 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]"
     Region          <6..462
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 tpcikqgsas trfsgvktit tytsgeenhy elkdysrgkg iityswefle dpfmgiyfln
       61 vpivdanngw skfeyhddyn hdalldahwg igmtydyfks vhnrlsydgn dskvvnnvhy
      121 fngfignnay wepmteeiyy vycphnssic ksfnlpvild ptyedftsld ivshefghgv
      181 ngdlagfslg mepgaldegf sdiwnvgvnn yvnkvlgmqk niwlvgdetv pgggmrsvsn
      241 pksttvlgpg pntyhgdlwd fednephtns lvlshwfytl skgklgfndy ectynvsgig
      301 iekaeriayv allflsstsg ytsartaaii aaktlyglfs sevkstidaw davavpadtt
      361 srggqgmvrp hhyiasvkls nvkndsgndc gykdnsylhp tvlrgatynm vllsqgsasn
      421 ppkahkwrvw idfnrdgsfe ssemvvqdtv nssyggtlqk siqipanalt gyakmrvsmk
      481 aaqsgeayqr fdesfvegev edyivsiidf sl
//
LOCUS       WP_004770529             292 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter vivianii].
ACCESSION   WP_004770529
VERSION     WP_004770529.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter vivianii
  ORGANISM  Acinetobacter vivianii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 292)
  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 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 292)
  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   4  (residues 1 to 292)
  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 292)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Acinetobacter vivianii"
                     /db_xref="taxon:1776742"
     Protein         1..292
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33102
     Region          31..177
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          215..288
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mdesdqiser vrglahrvdg lvqiedfqte isgfslhrrt akqsihciyg lglgivlqgq
       61 kevlirdkvy rygagqtmlt tidlpaisrv tqasyhepfl gmmlaldlnl iietvqalde
      121 rielknfpaf siesmdhglv daltrlvgli eqptlveqla plikqeiiir llvgehgryl
      181 rnlvkakasd qnifsviqwl rnnflqenci etafeqanis aatlrnhfkq vtgmtplqyq
      241 kqlrlqeark lvlsqamnvq qiadlvgyes qsqftreysr lfgssprqdl qh
//
LOCUS       WP_004770572             334 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter vivianii].
ACCESSION   WP_004770572
VERSION     WP_004770572.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter vivianii
  ORGANISM  Acinetobacter vivianii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 334)
  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   5  (residues 1 to 334)
  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   6  (residues 1 to 334)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Acinetobacter vivianii"
                     /db_xref="taxon:1776742"
     Protein         1..334
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37988
     Region          23..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          96..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mpqtatalts wvkaikkale kagcdsksli eqagldiqal ndpnaryslq qtarlwqlat
       61 aatqdscfgl kvanqvnqht fhvlghslat sttlkemfir iiryfrlvtd ipelefygkd
      121 qnhyfiihvp devqyesida fisvfirscr alqgslfspl rielrrseps dletyrsiik
      181 aplifnapqd mivfdtatie lpleganpil sqeydeiimr ylarfdkeni qarikvkiie
      241 nlaageiqqq eiakslglst rslqrklsle ntsyseildk trqelassyi knnsysitei
      301 ayilgftdvs sftrafrrwt dcsplhyren lskt
//
LOCUS       WP_004770987             416 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Acinetobacter vivianii].
ACCESSION   WP_004770987
VERSION     WP_004770987.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter vivianii
  ORGANISM  Acinetobacter vivianii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Acinetobacter vivianii"
                     /db_xref="taxon:1776742"
     Protein         1..416
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=48086
     Region          3..289
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          289..387
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mtvrffhtsd whlgqffynh srhyeheqfl awlleqikqk qphalliagd ifdvinpssq
       61 aqkqlyqfla dahelaphmq tlmiagnhds gyrieqvepl lakynaktvg virwnedktl
      121 dlerlilpiy deqkqivawc ialpflrsae itgfnehttn sqnaiaylhq qlieeakrrk
      181 tddqalilms hahmqggets dserpiiign eealstslfd dsidyvalgh lhkpqkvqhp
      241 hirysgspip lsfseinykh qvvevtvdst qpenkldfev laiprsiqlh kikdeltavm
      301 qqlknlpsgp ienidhreyv dieyhtaipp qpnlrqqfed alpkdryrlv risrqylsne
      361 snaenkqris lepptpeklf qqiwekkgyh addevtkdfl slvneaqkkl eddqss
//
LOCUS       WP_004771330             120 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein, partial [Acinetobacter
            vivianii].
ACCESSION   WP_004771330
VERSION     WP_004771330.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter vivianii
  ORGANISM  Acinetobacter vivianii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   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 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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Acinetobacter vivianii"
                     /db_xref="taxon:1776742"
     Protein         1..>120
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          16..62
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msldasiwaw raevknssqr lvlltladra geshkcfpsl krmeadtkln rktiikvlde
       61 leadshikft gettgkgvkv yqllgvigre deeitstkng tspnngtgsk ngtgsengts
//
LOCUS       WP_004771838             341 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004771838
VERSION     WP_004771838.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 341)
  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 341)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38410
     Region          28..211
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          255..336
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mktsttrqdq gipgvyglll ldvvsrwgys detlfapfhl tseqladpny riptpianel
       61 vkhslrltge stlgfhlgtq mrisihgfig yaimtahdit daialasrfi qlrlpflqly
      121 fstfgpkatl qlqcdievep lrteiilglt igimtmaral tgiedlsgev dldfpepvgf
      181 dkyrdklsss irfnqphlis sfdkkylglk mvnadpiasq iainqcetel salgerrrla
      241 mrvrdiltns eqhylsiesv aerlhmsdrt lkrqlaaegt sfstlvdevr yrhatsllsr
      301 tdysleqiad elgysdvanf srafkrwsgr spsnwrkdpy l
//
LOCUS       WP_004772270             341 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter vivianii].
ACCESSION   WP_004772270
VERSION     WP_004772270.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter vivianii
  ORGANISM  Acinetobacter vivianii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 341)
  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 341)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Acinetobacter vivianii"
                     /db_xref="taxon:1776742"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38969
     Region          25..211
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          255..336
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkylwtyers ihsvrlmadf aaelgvshhq ilkgtgleqq qlldpntlvt gqqelqlirn
       61 lvekfgqrpl lgleigtryh fttfgslgla lissanirea lnfalayfpl sfafsqflvs
      121 eqaetqsvqi eivvdegipk tlwpfiierd vaalitvqrd lmqdhlcqkv vfsfplrgem
      181 qpytalfgvt pefggsknli vlnaekidqk lsmanelvlh aaeeqcrqtl dkrqsqkkyt
      241 hqvqqvlmns kgqipsmeev adrlylnsrt lrrylaqeqa sflqireevr kiladyylsl
      301 tqtsieqise wlgyaepasf ihaykrwygn tphatrlknk v
//
LOCUS       WP_004775619             232 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Acinetobacter].
ACCESSION   WP_004775619
VERSION     WP_004775619.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 232)
  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 232)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 232)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..232
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=25665
     Region          3..210
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 mslsddeqld slksfakkyg saiisgilia liaffgweyw qkktlaesqn qtakvqklmd
       61 eakaatgqpn afatlseaad kivkddadsa qaiqtqfima klayekqdya aaekalkkve
      121 nskvkdegll qvvklrlada qlaqnkfdda lktlsavtep afkatadelr gdifvakkdn
      181 esarkayqsa wdnllerkqe rqllqikles vgvlvddpef erpildtkvd es
//
LOCUS       WP_004776118             276 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004776118
VERSION     WP_004776118.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 276)
  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 276)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 276)
  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   4  (residues 1 to 276)
  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 276)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..276
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31609
     Region          51..273
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <175..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 msrrpreqvd ylhleelggl emlkasyyqq efsrhvhegf cigvieegaq rfyrtggnhv
       61 apqgdiilvn adevhtgssa vdtgwryrai yptpevfnel trdlttvhgt apwfreavlh
      121 deglaqqfri lfdlleqpnn tllkqtlfls tiawlvskys qvkphvtdls nakqrilnik
      181 elmasmpeqe fslaelaema nlsqwhflrq fkkhvglsph awlvqarlqk sqrllrqgln
      241 lsevsqqcgf sdqshfsrhf rqtfgitpgg yiaylk
//
LOCUS       WP_004776157             335 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter vivianii].
ACCESSION   WP_004776157
VERSION     WP_004776157.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter vivianii
  ORGANISM  Acinetobacter vivianii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 335)
  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 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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 335)
  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   5  (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   6  (residues 1 to 335)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter vivianii"
                     /db_xref="taxon:1776742"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38627
     Region          51..193
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          82..330
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msqlknytgs vfgglghllk ayceaenili peqlqqvqnl erfdyviwrd lledlnrlhp
       61 kaglgldiaa yvqpkhlgii aylalscenl gealaryhdf hrliydgspl lvelghpygs
      121 irweapephp tqltdeiaia lmvqflklfm sgdsihlhev hfinpapkni siyeqyfhck
      181 vrfdqpktql lipvseafkp lrtgdhtlqq lllqqaqall dklpnstqld qrlqhailtg
      241 lqknqyqldf iaeklglsvr qlqrhlqqqr ttfqervqqv rfmlateylk dphlslqeia
      301 lllcyseqsa fqrafkiwtg qtpqqwrnnn tiyns
//
LOCUS       WP_004776920             206 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Leptospira kirschneri].
ACCESSION   WP_004776920
VERSION     WP_004776920.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kirschneri
  ORGANISM  Leptospira kirschneri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Leptospira kirschneri"
                     /db_xref="taxon:29507"
     Protein         1..206
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22769
     Region          73..201
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mtskecsten ekvagkepdr vvrklfrqtl vgivilvlgv vflarvfpep vlvvsqkfie
       61 itgvfgvgvg imladslhvf ippdvflmla vagklnsvlv iasasigsli ggsvsyltgr
      121 illpkmeris ifvkrheqkl ehylhrygfw avvlaaltpl pyswvslaag amkmkyslff
      181 rgclfriprf iifyyliqfg wvgggm
//
LOCUS       WP_004777482             147 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Acinetobacter sp. CIP 102082].
ACCESSION   WP_004777482
VERSION     WP_004777482.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CIP 102082
  ORGANISM  Acinetobacter sp. CIP 102082
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Acinetobacter sp. CIP 102082"
                     /db_xref="taxon:1144663"
     Protein         1..147
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14802
     Region          1..146
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mksmqkgftl ielmivvaii gilaaiaipa yqdyvskska saaladiaag ktsyellfte
       61 kgaggftptk avpgdiglsa stgncsaitv vapdattgaa tdaikctinn pgrlgtgati
      121 sfdrttagly eckttvmntk ykpagca
//
LOCUS       WP_004777594             679 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase [Acinetobacter].
ACCESSION   WP_004777594
VERSION     WP_004777594.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 679)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..679
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..679
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=76510
     Region          58..>488
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mkhvtpeegq svniiaenie glrkllpdaf tengvnfetl rqllgdaqvl degeekygln
       61 whgkkkarqi altpstgtll pcpeesvnwd ttknlliegd nlevlkllqk syankikliy
      121 idppyntgee fiypdnyqes idtylkysgq idangmkfss ktevagrkht nwldmiyprl
      181 klaknllrwd gvlaisiddn elpqlcaicd eifgevnrkv iavkmseasg lkmgavkkng
      241 tipklkeylv likkngvrdi flepipkatw dteynifieg mnkthkefid qiqraehitd
      301 eminqldgls snweaksvae kikevgvsnd eketwlkena yricqattsa svlkianekr
      361 kscdaplffv psakreiayf vkatysness kprlqlifae dnlaihpgdi wtdikttgld
      421 gegyvsfkng kkplrlldrv isacvsdgdy vmdffagsgt sgeavmrnai krainlnfil
      481 vqlpepldpn nteqeesftf cksnnlkplv seltryrlta asqdlkslnn snlnaafgfk
      541 kfklsssnir lwnpdqtdle stllsheehl igkrteqdil yelllkrgvd ltapiekrev
      601 lgknlysigy galfacldes isrhqvedia qalinwykel apasethiff rdsafnddvs
      661 ktnmvaileq nginhvrsl
//
LOCUS       WP_004777621             712 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Leptospira kirschneri].
ACCESSION   WP_004777621
VERSION     WP_004777621.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kirschneri
  ORGANISM  Leptospira kirschneri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 712)
  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   3  (residues 1 to 712)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Leptospira kirschneri"
                     /db_xref="taxon:29507"
     Protein         1..712
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79968
     Region          1..700
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdlsevrdtf iseseellss mesnllilek dsknnegihs vfraihtikg tsgmfgyepi
       61 ekfthevesf ldkirsnkqs ltkegieflf lacdhirnll qgvgetlivd sqtsrnqvnl
      121 lslakklild dtsnpqkyev iqnqptssnh ldfhsnstfw qitlipnihl fesgldpstf
      181 ikylsqsgkv khifiypdsi pnwsefnpeh shlgfeisye spskgeeihs tfqflkegsy
      241 lkilapgcsl nlfmenyndf pfgkkaylna leiqkiltpe eiqklsytse nlniphttqt
      301 eqlstsienq kesdsiklqt ktlrvdsski dtlialvgel itqeanlsrk isdsenlqli
      361 esseslyrlv teirefalsl rmipisdlfe kykrvvrdls kelnkqvele iiggeteldr
      421 sviekisdpi vhilrnaldh gietseerir kgkpatgqlk iqashgtgsi lieinddgkg
      481 ldcdkileka iskglitrdq nlseseiysl ifqpgfstad qvtnlsgrgv gmdvvlrnie
      541 slrgtvqiqt lkdqgssfli rlpltlaiid gflvkaysly fivpmqmvre tveskvilng
      601 sssgtmnlrg ellpvlhlse flclesnsfe kenilileye dksfgiivnd lhgevqsvir
      661 pmaeifknik cfsgtsilgs geiafildvp glynsirdqe lnknkdltak tg
//
LOCUS       WP_004777896             296 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Leptospira kirschneri].
ACCESSION   WP_004777896
VERSION     WP_004777896.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kirschneri
  ORGANISM  Leptospira kirschneri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 296)
  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 296)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Leptospira kirschneri"
                     /db_xref="taxon:29507"
     Protein         1..296
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33451
     Region          21..77
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mgehypyikf fadiiesgvw anlssaaktl ylvllkfsdq hfkpvwpste illrltgfkt
       61 kksiiqgkrd liqagllqvt pgtghtssry yfcfnypgsk ippqgynfgn pgggetetqg
      121 vgkngpqgsg evapnhinit itnnqhqkpe krkkqvslde lekeygsttl tealtiargr
      181 gmetnlryvq gicknltkak ddfmpefnqn qerynerets wngflrwske rlakssietl
      241 ekikvepdgr tlcildpvte slrmiiakyf teeirppilv ifsakneenr itstkh
//
LOCUS       WP_004779069             356 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Leptospira
            kirschneri].
ACCESSION   WP_004779069
VERSION     WP_004779069.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kirschneri
  ORGANISM  Leptospira kirschneri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Leptospira kirschneri"
                     /db_xref="taxon:29507"
     Protein         1..356
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=40081
     Region          1..352
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mgievknlvk rfgnftaidd lsldvpsgel vallgpsgsg kttllriiag ledadkgqvi
       61 fegrevgkkn akdrgvgfvf qhyalfrhmt ifeniafgle vrrraerpsk nvikdkvmsl
      121 lklvqlenfh nrypselsgg qrqrialara laieprflll depfgaldak vrkelrnwlr
      181 rlhdeihits vfvthdqeea levsdkvvil rsgkieqvgt pdevynhpkn sfvfhflgdv
      241 nlfhgrvqgg qtqlgeikvd apehseiena savgyvrpyd veilrepiea qtipaeilyi
      301 hstgrnvkid lkrldtgtil esqlnssefq slnllpgetv hirfkkikvy vedyti
//
LOCUS       WP_004780611             429 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Acinetobacter
            variabilis].
ACCESSION   WP_004780611
VERSION     WP_004780611.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..429
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=49271
     Region          3..418
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mntvavlklt lhhgivgyla gfqsgknilv ftdsfrfdqq rptlslltsp lypqadkile
       61 ktyvthqrlh pllsnllpeg alreliaqsl kihidnefql laalghdlpg alittpldpe
      121 eipdeikfkl qisnpdqilk qeirtdnkfs lagvqmkfsm kakdgrftla qatettllgd
      181 wiiktpssrh afvplneysm mtlakmvgid vpeirlvdma llqdlpplnl pqeqyafaik
      241 rfdrqstant telihiedfa qifgayphqk ysttnyeqig kiiyqysdnk ifdiqqfasr
      301 llinillang dahlknwsmi yhdkrtprls paydilmtsv yiknerhfal nlaknkdwyl
      361 aemkhfeqwa ekvgvpwrvi ekqlheimdk arsvwpalll dlpmgsahke klrehwkklh
      421 pdfqiland
//
LOCUS       WP_004782043             372 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Leptospira kirschneri].
ACCESSION   WP_004782043
VERSION     WP_004782043.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kirschneri
  ORGANISM  Leptospira kirschneri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Leptospira kirschneri"
                     /db_xref="taxon:29507"
     Protein         1..372
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43574
     Region          61..230
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mvfkrkihpr vlykvlgaft ffviihllts filtnelrsi knfpfkgdki hspysetkhr
       61 wlkmafhlhs drdgfspfrs speeiqekyl ekkydlisit dylkisgtes knpkffpgye
      121 wgrdfnrkhi lalgaeslir dffplyasee niqwtidqiq ksgafivish pglegsisyk
      181 ilerlrgida vevfsnygdt fedwirlldq gipvlatsgd dlhyfpgeli ramklplyqr
      241 ifheltfsdq negeafvryi llntysierd eiirnlkkgn yvsvikiany medpkitelk
      301 ltkdliiaef pdkflkimfi gkngkilked klafrsfyqf rnedeyvimk vvfssgyiys
      361 npfyrtsnsd tk
//
LOCUS       WP_004782106             232 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Acinetobacter variabilis].
ACCESSION   WP_004782106
VERSION     WP_004782106.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 232)
  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 232)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 232)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..232
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=25754
     Region          5..209
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 msamtddeql eslksftkky gssiiigilv amiaffgwey wqkknlaesq mqtakvqqlm
       61 deaqaadgda faklsetadk ivkeapdsaq aiqtqlvmak laydkqdyaa aekalqkven
      121 skvddkglvq vvklrlayaq laqkkydaal ktldavtepa fkatadearg diyvakndie
      181 nakkvyqsaw dalierkeer qilqiklesv gvlvddpeie rpiietqvee ae
//
LOCUS       WP_004782380             250 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Acinetobacter
            variabilis].
ACCESSION   WP_004782380
VERSION     WP_004782380.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   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 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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..250
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=27668
     Region          16..67
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msvdatrwaw kapvknatqr lillsladra gehhtcypsn krlaqdtmln lktvqksvce
       61 lielgliadt gerkgstnqv rvlqligvds reynepkigi vkqtqkrnst kigndpkngt
      121 gnepkigvcn epkiglgnlp iepnnesnni kekfsfagel kklganeqli sdwlqvrkak
      181 kagntktaln gfmkqveksg lplntvleic virswqgfni dwlknidlse fqpkqttpap
      241 qnlktvkgaw
//
LOCUS       WP_004782794             405 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase family protein [Acinetobacter].
ACCESSION   WP_004782794
VERSION     WP_004782794.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 405)
  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 11465564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..405
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=43401
     Region          <135..183
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          274..403
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mfvrtmlavs lgcifagtvf aasnaeqpln pqvvtdvavq dpidplatea saaqaetris
       61 aqeqqdlkka sealdvlqdt edqtanigaa ptttkaptns aaakaswtld glnnaswyed
      121 igkgqfpvya rahvmlnnah aspgaidgts gkntlkaias fqqmngikpt gtltqetwda
      181 llakqgskpa fveytiteed lkgpyaesip sdyalqakmk glyytrvtem lgekfhmded
      241 flkklnpkat fkkagekliv anirnevped ihlivahkga kqlylfnsrn qmiasfpati
      301 gssstpsptg tykvtgvakn pwysyspsnf vqgnnkkpls lppgpngpvg niwiglskks
      361 fgihgtpnps aisktashgc irltnwdand lgrkvksgvt vrfle
//
LOCUS       WP_004783055             121 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: endonuclease domain-containing protein
            [Acinetobacter].
ACCESSION   WP_004783055
VERSION     WP_004783055.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 121)
  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 121)
  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   3  (residues 1 to 121)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..121
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14104
     Region          14..117
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mkidpqllef aksmrhtatn aehlmwqllr akrfmnlkfr rqhviapyiv dfycheiglv
       61 ieldggqhgt ddaieydaer tkflealdlm vvrywnrdvv gktdvvledl lqvcsqlkkd
      121 k
//
LOCUS       WP_004765633             526 aa            linear   BCT 20-JAN-2025
DEFINITION  type I restriction-modification system subunit M [Leptospira
            kirschneri].
ACCESSION   WP_004765633
VERSION     WP_004765633.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kirschneri
  ORGANISM  Leptospira kirschneri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 526)
  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   2  (residues 1 to 526)
  AUTHORS   Youell,J. and Firman,K.
  TITLE     Mechanistic insight into Type I restriction endonucleases
  JOURNAL   Front Biosci (Landmark Ed) 17 (6), 2122-2139 (2012)
   PUBMED   22652768
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Sistla,S. and Rao,D.N.
  TITLE     S-Adenosyl-L-methionine-dependent restriction enzymes
  JOURNAL   Crit Rev Biochem Mol Biol 39 (1), 1-19 (2004)
   PUBMED   15121719
REFERENCE   4  (residues 1 to 526)
  AUTHORS   Murray,N.E.
  TITLE     Type I restriction systems: sophisticated molecular machines (a
            legacy of Bertani and Weigle)
  JOURNAL   Microbiol Mol Biol Rev 64 (2), 412-434 (2000)
   PUBMED   10839821
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114514
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Leptospira kirschneri"
                     /db_xref="taxon:29507"
     Protein         1..526
                     /product="type I restriction-modification system subunit
                     M"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=59650
     Region          8..142
                     /region_name="HsdM_N"
                     /note="HsdM N-terminal domain; pfam12161"
                     /db_xref="CDD:463478"
     Region          162..422
                     /region_name="HsdM"
                     /note="Type I restriction-modification system, DNA
                     methylase subunit [Defense mechanisms]; COG0286"
                     /db_xref="CDD:440055"
ORIGIN      
        1 mlqnnpqlks lidklwnnfw sggisnplta ieqitylifm krlddletkr erdaeftgek
       61 yksrfsgkfk vpgsnelink kdlrwstfkh ftaeetllhi qtkvfpflke lngdaspfth
      121 hmqnavfimp kasllteaiq iiesifaeie kdanegghaf qdiqgdvyem llgeiatagk
      181 ngqfrtprhi ikliaelvap qlgqrvadpa cgtggfllga yqfmltdyir kkdpkkiikd
      241 edgfergals savdkkvkti ldnsfygydi dttmvrlglm nlmmhgidep hidykdtlsk
      301 kfnedkqydi vlanppftgn idkgdinesl tlpttksell fverifnmlr mggtagvivp
      361 qgvlfgsgka fvtlrkklie eselkavitl psgvfkpyag vstailiftk ggetehtwfy
      421 emladgysld dkrtkieqsd lmdivarfqs rdpkkdtkri eraffvpkqe ivgdkpeesk
      481 ydlslskyke evyeeieyes pklileklet ieeqiqaglk elksrl
//
LOCUS       WP_004784575             264 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Acinetobacter variabilis].
ACCESSION   WP_004784575
VERSION     WP_004784575.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..264
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29877
     Region          36..261
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mtnknsqtts qttdssnpek kryyepapqd idvdnfrkvi esrrsvrkft kkpipaevld
       61 acldlallap nssnlqpwtf yvvqnpskkk rlvkacmsql aaktaseliv cvartdrvde
      121 maklnisefp fpeappaikk yykyipynyk tgylnafgnf kkvafkvart ldkqmpvsaf
      181 spadaklwas kttalacenl vlalraygfd scmmegfdep mvrelldlnd qqypvmviga
      241 gerakdgvff pqyrfdqelf iqkv
//
LOCUS       WP_004784750             514 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Acinetobacter variabilis].
ACCESSION   WP_004784750
VERSION     WP_004784750.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..514
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=58305
     Region          4..437
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mplldwvnrn qaeetatstp yhllkfenay gdaehtkenl iiqgdnlqal kallplyggq
       61 vkcifidppy ntqsafehyd dklehaqwls mmyprlqllk ellaedgsiw itlddneahy
      121 mkvlcdevfs rknfvttiaw qkiyttknsa kffssmhdhv liysknidef ilndlpredk
      181 qnlayknpdn dergpwkatp iharnfyslg rysittpsgr vidgpptgty wriseenfik
      241 mdqdnriwwg qsgngipaqk rflsevrqgv tpntfwtfse aghngeakne lrsllpteed
      301 lfltpkpekl iqriiqlats kndlvldsfl gsgttsavah kmgrryigie mgehaktfvi
      361 prlekviage qggiskavnw qggggfsfyt lgnpvfddqg flnadvhfkd lasyvwwlet
      421 ktalnqtesf dnpylgthdg vayyllyngi lgdrrpnggn vltlsilnyl nechahegkr
      481 vvigeasrlg darlealeie fkqipyslyg nqaq
//
LOCUS       WP_004785016             198 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Leptospira meyeri].
ACCESSION   WP_004785016
VERSION     WP_004785016.1
KEYWORDS    RefSeq.
SOURCE      Leptospira meyeri
  ORGANISM  Leptospira meyeri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Leptospira meyeri"
                     /db_xref="taxon:29508"
     Protein         1..198
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21946
     Region          1..196
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mklvvglaga sgsiyaarfl ralyeleget yitaspaalr ifseeyetkv esceeilsfv
       61 etkwkpqtkh rfhvrnffdi gsdiasgsnt wdcmvvipcs mktvasmsag ltenlieraa
      121 dvtlkerrrl ivvpretpyn rihlknllal deagaiilpa spgfyqmpkt lddlgdfiag
      181 rifsllgvnq tlfpkwlg
//
LOCUS       WP_004789182             286 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Leptospira meyeri].
ACCESSION   WP_004789182
VERSION     WP_004789182.1
KEYWORDS    RefSeq.
SOURCE      Leptospira meyeri
  ORGANISM  Leptospira meyeri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 286)
  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 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   3  (residues 1 to 286)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 286)
  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   5  (residues 1 to 286)
  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   6  (residues 1 to 286)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Leptospira meyeri"
                     /db_xref="taxon:29508"
     Protein         1..286
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33579
     Region          21..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          135..286
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mdyydhikqa iefieknlre disaedvskn afqsrwhfqr ifryvtgysv ytyikkrrlt
       61 eagndlilgk dkiidialky hyttpesflr afrseygynp seyrnqlehk nfsklevdll
      121 rdgiridgsk ikthivtkne itfigktyrt tmqkcqneid ipkfwgefig ggfmepiknr
      181 lnqsligiyt nwdyaenfdv ligaqvtket kipsgfvthk lkpakymvft vpgntnvdil
      241 sgwkyiygtw mpntgyeref sddfdlfddr fqsntnpese iyipik
//
LOCUS       WP_004787072             150 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Acinetobacter].
ACCESSION   WP_004787072
VERSION     WP_004787072.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..150
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=16195
     Region          1..131
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mvnkshgftl ievliavaii gilaaiaips ylqyiikanr vdaqttlvdi askiqrykvs
       61 qgglsngssv ikltdlgypa lleipqnsnk plykvelssv tvegawelia epktstkqeg
      121 dgwlclnhkg eqfwskgvda cnfssnsswn
//
LOCUS       WP_004785199             336 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004785199
VERSION     WP_004785199.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 336)
  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 336)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..336
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38549
     Region          22..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          249..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msrdtisihf vnaalygvkr lgmdvdtlls hvgieaellh qpkarispeq ytrfikmlwm
       61 vtqdehvgfd kqprrlgtfa imcqliihak tlgdalelss qfyklfgddw svtlerdkhe
      121 arlvplipns mdpehfites mlmiwhglas wlierrlple rvhfsyprpa hadeydalff
      181 apvmqfdmpr teitfaadyl dlpirqneet leeflkaapa qllvkfkntn sltsrirdvl
      241 ksqigeempt lndvasmlyl spqtlrrrla aegksyqgvk dalrrdaaih lllnpdltle
      301 dvaqqvgfse tstfhrafkk wtgvtpglyr qlhgyh
//
LOCUS       WP_004789238             709 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor family protein
            [Acinetobacter].
ACCESSION   WP_004789238
VERSION     WP_004789238.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..709
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=78429
     Region          35..705
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 msllrldrlh ycilmsmgci ssplvwaedl tqdvtvlptl hveatrtdtt ylqtpasvfr
       61 idapqvdtss qvnltevvkg ipslqlrnre nyaqdlqlsm rgfgarstfg vrgirlyvdg
      121 ipatmpdgqg qtsnidlssl dhvevltgpf sslygnssgg tiltstkegq gkdsielsys
      181 ggshdksrag lvlqggakga nepsyvisss yfdtdgyreh sgaekvlnna klswnlddgs
      241 kinwvtnyvk ihaddpqglt rdqwnanpkq qvpflkqfnv rkdieqtqtg vtwskpindh
      301 nelyamaylg nrqvtqyqsi pkstqdanvn haggvidfer nyygadfrwt gkellpnttv
      361 svgvaldamd edrkgfenfn lvngqpsygv kgnlrrdedn tlwnidpylq aswqflptwr
      421 ldtgvrysnv hyksednyls ngddsgktdy nkvlpsaals wqiipelmay vsyakgfetp
      481 tftemayrpd gksgfnfdlt astsdtyetg lksqnylgdf tlavfqtktk ddivsagssn
      541 grstfrnadk tlregvefaw nkklwrdlta tasytyldat fdadipalgn iaqipsgnvi
      601 pgiaknqaya slawqpshgl yggvdvqymd kvyvndtnsd aapsysvtsa nvgyawvrgd
      661 wkvnsfarvd nlfdknyags vivndgngry fepadgrnws aglrvikqf
//
LOCUS       WP_004789780             160 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Acinetobacter].
ACCESSION   WP_004789780
VERSION     WP_004789780.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..160
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=17375
     Region          8..105
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mnkyyilrfn qgvtlielmv vivivaifas iaipsyqsys rratasaakg eilklaeqle
       61 rhksknftyr gftttsvtlp rggytieisd dttagnlltn aaangqtwvi katttdsrnf
      121 nfiaknsglr cqsltatavd ndcggtvtcn vcetnsenwq
//
LOCUS       WP_004789910             334 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004789910
VERSION     WP_004789910.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 334)
  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   5  (residues 1 to 334)
  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   6  (residues 1 to 334)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..334
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38865
     Region          <62..201
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          76..334
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mpqlknytgs vygglghllk ayceanqlai peqleqvqnl erfdyvvwrd lleiiykldp
       61 kpglgleiak yvqpkhlgii aylalscdnl gealiryhdf hrliydgspl vvelqgrygs
      121 irweatelhp tqltdeiaia lviqflrlfm shedvhlhev hflnaapkni rvyeqyfqcp
      181 vrfsqprtel lipiteihkp lssadhtlqq llvqqaqall eqlpnstqld qrlqhsiltg
      241 lqknqyqiey iaaqlglsvr qlqrhlqqqn ttfqervqqv rfmlateylk dphlslqeia
      301 lllcyseqsa fqrafkhwtn qtpqqwrdhf ldkk
//
LOCUS       WP_004790207             282 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Acinetobacter].
ACCESSION   WP_004790207
VERSION     WP_004790207.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..282
                     /product="formate/nitrite transporter family protein"
                     /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=31339
     Region          28..279
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mdheieekkv ektlswrekm aveeheklsp rlvyeiirrd gaeeldrpta alifsgiaag
       61 liisfsfvfk aiiasylpad avwtdlitni gytigfliai lghmqlften tittvvplfk
      121 pftfdklrav grlwgivilc nilgtalasl ffltthlftp didkaldela hhvgsfsatq
      181 nmlkgimsgl liaalvwmlp svsnkfllif fmtyliglgd fthvvvgste msylvwqgea
      241 sindylftfl vpttigniig gtgvftlliy gqvteelerk hk
//
LOCUS       WP_004791492             342 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004791492
VERSION     WP_004791492.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 342)
  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 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 342)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 342)
  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   5  (residues 1 to 342)
  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   6  (residues 1 to 342)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..342
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39276
     Region          28..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          98..336
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mvvqsslskg tisialvhea lsaayakgln tqiilnkagi ptelllspka rvpvttyaql
       61 wielanamnd effgmdshpm rrgsyklltk lvstaetlek alhdilkffn fvlddmrael
      121 irdqekaylv ihdqkqpkrm ftyatflmlv hglmcwlvdq riglnnirir clkpndiqdy
      181 lvrfgediqf naeinrvefd ahyldikikk dkkalydfle ktpqnllvrf knenalsvli
      241 rrhllklhpa qwpelkdvak qlniseatiq rrlkheggsy qqikneircd iaverlsktn
      301 dsiqdisedl sfqdpsafhr afkkwtgvsp gayreatfns id
//
LOCUS       WP_004791127             713 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Borreliella garinii].
ACCESSION   WP_004791127
VERSION     WP_004791127.1
KEYWORDS    RefSeq.
SOURCE      Borreliella garinii (Borrelia garinii)
  ORGANISM  Borreliella garinii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Borreliaceae; Borreliella.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 713)
  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   3  (residues 1 to 713)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Borreliella garinii"
                     /db_xref="taxon:29519"
     Protein         1..713
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=78965
     Region          1..713
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdssdvidkf knsfkeesie nisdieqall nleagsdqei insifrnlht ikgssgmfgf
       61 nftaslvhei etvldvikdg raafnqaaid atlmsvdfir eliegdeeis eidfdkrkqf
      121 lvdeikrvle tpnvkgafqe alendfskpd nssaleeclk vnsdnkfdde alrsefksyk
      181 ilfspakgil fhghkpinll nklidlgsgh vrakvdnipd lelispdnvy vdweirldte
      241 esresiadif ifldsqskid iqeldkclet dkgdnlglkn fnlssldrst kdsansafkk
      301 safigksfln gdknrsnvqd dtarskvnia sikvdskkld hlvnlvgelv tiqsklskea
      361 enrnsnilns isaefsllin elrdyttglr tvpieilfvk fqrivkdlst slgksilyha
      421 sggdtvldks iieklneplv hlirnsidhg iespeererl gkdpkgiikl sacqsgdsvi
      481 viieddgrgl dknkilkkai erniisdsaa ktlsnidvyn lifepgfsta ssvtdisgrg
      541 igmdvvkkqv eslrghvvle selgkytktk lvfpltlaii egwlvrvkde hfivplsnve
      601 sclesnnlis qmdgvetksn vmnyrgsmis firlreffqv sseksiseqv vvvntnsgkm
      661 givvdevlgq hqtvikalgk iysrvegvsg atilgdgsla lvvdidaitk lir
//
LOCUS       WP_004791977             670 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Borreliella garinii].
ACCESSION   WP_004791977
VERSION     WP_004791977.1
KEYWORDS    RefSeq.
SOURCE      Borreliella garinii (Borrelia garinii)
  ORGANISM  Borreliella garinii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Borreliaceae; Borreliella.
REFERENCE   1  (residues 1 to 670)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 670)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 670)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..670
                     /organism="Borreliella garinii"
                     /db_xref="taxon:29519"
     Protein         1..670
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=78402
     Region          <408..670
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mkevnnykni nsvvisknei dvrdliklks ifnliqivks ekalyseyvk qnnikfaiiy
       61 nhekpidfsi kvanelknin kihsiiisne kfdeeylkln hieiikdise leykkslihq
      121 kklfcdnqns tldfflnlse likeiviitn teneiiyine kgsknlnlpl ktsgnkikvt
      181 didirdwekl kkidlsyhtn sipefknili tnciltlknn kklyvdvfis tidqnnidkl
      241 itikeipnln eienykylei idsqdeiqna keiekllvnh mdiykkkkiy llnldlfltt
      301 eyeykedrek lnikilkimy skimslysey ifklknnnli viictsgden qiisiaqkik
      361 ktitlalkke diiifkfnig iievnlrenl elkipklmma tkisseykds npiiykeelp
      421 eavilknqnk ifqyilkaik ndfftlyyqk inplkknlkp kieiltrlfd hmgkpipneq
      481 ifnlidkynl taevdqlvvk kalreyksfv skngvhifsi nispyslksq nfriflkdtl
      541 lksqiplqni cleitetgil enfeiinkyf qelksfgikl alddfgsght slsyiktlpi
      601 dllkidgsfi kainsseidy viiksikkia dtknikiiae fvyneeilkk ineleidygq
      661 gflwhkpepi
//
LOCUS       WP_004792285             299 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004792285
VERSION     WP_004792285.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 299)
  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 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   3  (residues 1 to 299)
  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   4  (residues 1 to 299)
  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 299)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..299
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33955
     Region          34..181
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          210..289
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtlindlspv iektkalark vdgliqnedf qteisgfslh rrtnkqsihc iydlglgvil
       61 qgekqvlign eifsysrgqt mlttidlpav srvtqasyse pflgmmlkld igmiteiags
      121 menihvtsni psfsieemdi gliealdrlv dlvedpsmis qiaplikhei ivrlllgkhg
      181 dylrnlikis vseknifkvi swlrnnflnd vsvdeiadqa nmtpatfrnh freitrmtpl
      241 qyqkqlrlqe arklmlmqsi eirrvaesvg yesqsqftre yvrlfgitpq kdlkentak
//
LOCUS       WP_004792823             334 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004792823
VERSION     WP_004792823.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 334)
  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   5  (residues 1 to 334)
  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   6  (residues 1 to 334)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..334
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37985
     Region          23..197
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          119..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msksssdagi fllmtyqtmq kmgldaasif asvnlpnqpp dknirrdnst qqrfwtaaek
       61 isqdtdiglh vgrqmppfrg lvieylflss stfgeglqra lryqailtdv fdlkltvked
      121 eailsgfehp vrhylecgig iflnffkyit nnefrpsqit lsyqqgasas dyqeawncpv
      181 ilntnqgaii fpsallnkts paaepellki hetiaeqqls tlekhqlvye ierllsngll
      241 esgefdqkfi aeklnrnprt lradlqaint nyekilnqhr eklarrllah tqetidqivy
      301 ltgfsepsaf trafkrwsge tpsayrqrkq kqsn
//
LOCUS       WP_004794111             422 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: exonuclease SbcCD subunit D [Acinetobacter].
ACCESSION   WP_004794111
VERSION     WP_004794111.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..422
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=48415
     Region          9..294
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          294..393
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 msvsmsvhfl htsdwhlgqf fynhsrhyeh qqflswlltq iqekqphall iagdifdvin
       61 pgsqaqkqly qfladahria phmqtlmiag nhdsgyrieq vepllekyna ktvgvvrwne
      121 dktldldrll lpiynqnqdi vawclalpfl rsaeitgfne httnsknaia ylhqqliaea
      181 krrktpdqal ilmshahmqg getsdserpi iigneealst tlfedavdyv alghlhkpqk
      241 vgqphirysg spiplsfsei nykhqvvevk idptqeadsr lqfeaveipr ciqlhrirge
      301 lnevlqqlka lphgvienid hreyvdieyy sltppqpnlr qqfeaalppd ryrlvrisrq
      361 yvnkdstdsn itqkialepp tpeklfqniw ekqgynadda vlkdflslvq eaqkhlenda
      421 tp
//
LOCUS       WP_004794394             335 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004794394
VERSION     WP_004794394.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 335)
  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 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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (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   5  (residues 1 to 335)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37854
     Region          23..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          251..328
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpqtatalas wvkaiqkale kagvdsqpll eqagldiqal snpdaryslk qtanlwklav
       61 qktqdscfgl kvasqvnqnt fhvlghslit sttlkemflr iiryfrvvtd ipelefygqg
      121 nnhyfvihvp devqpesida fisvfirssr alqgsvfspl rielrrsepe dletfqsilk
      181 apivfnaakd mivfdtatie qpleganptl tqeydeiinr ylarfdkeni larvkvklie
      241 klstgdfqqq dvakslglsi rslqrklsae ntsyselldq trhelalsyi knsshnitei
      301 ayilgftdvs sftrafrrwt nlspvhyrek hlacs
//
LOCUS       WP_004794540             142 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Gammaproteobacteria].
ACCESSION   WP_004794540
VERSION     WP_004794540.1
KEYWORDS    RefSeq.
SOURCE      Gammaproteobacteria (g-proteobacteria)
  ORGANISM  Gammaproteobacteria
            Bacteria; Pseudomonadati; Pseudomonadota.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Gammaproteobacteria"
                     /db_xref="taxon:1236"
     Protein         1..142
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16155
     Region          1..141
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlsyfllfis afgaatllpl qseavlvtll lkgqysalll istatlgnvl gscvnwwlgl
       61 kieqfkhrkw fpvsekrleq aqrfyhkygf yslllswapi igdpitlvag lfkenfwrfl
      121 giviiakagr ylfiywvvmg fi
//
LOCUS       WP_004794712             232 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Acinetobacter].
ACCESSION   WP_004794712
VERSION     WP_004794712.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 232)
  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 232)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 232)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..232
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=25617
     Region          3..210
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 mslsdeeqfd slksfakkyg samisgilia liaffgwtyw qkknlatsqv etakvqqlmd
       61 eanasadnpn alssvtasad kivkddidsv qaiqtqfvla klayekqdya aaekalkkve
      121 nskvkdegli qvvklrlada qlaqnkydea lktlsgnvdp afkatveelr gdifvakkdv
      181 dsakkayqaa wnsllerkqe rqilqikles vgvlvedpqi erpiletqve es
//
LOCUS       WP_004794745             400 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Acinetobacter].
ACCESSION   WP_004794745
VERSION     WP_004794745.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..400
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42883
     Region          5..388
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 matsvlvinc gsssikyalv serredriyg laenlgaada rikgvtvgge plelsipyad
       61 hakaletlla rlanykpqai ghrvvhggsl tkaelltpei ieriraatpl aplhnpahli
      121 gidatvrlfp elpqvavfdt afhqtmppha yryaipkfly tdhnvrrygf hgtshayvsd
      181 kaselagnlk kggwltahlg ngsstcavwn gqsvdtsmgl tplegvvmgt rsgdvdpslh
      241 sflaknlgwd lakidkvlnn esgllglsql sndmrtviea aengnedacl aievfsyrla
      301 kslaalscgl ptldgliftg gigensayir ektlaylphf glqlnkdqnn nlkrgtegri
      361 dngtgpqiwv iptdeegria ketrqvveaa entasvasla
//
LOCUS       WP_004794884             146 aa            linear   BCT 20-JAN-2025
DEFINITION  division/cell wall cluster transcriptional repressor MraZ
            [Mycoplasmopsis canis].
ACCESSION   WP_004794884
VERSION     WP_004794884.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis canis (Mycoplasma canis)
  ORGANISM  Mycoplasmopsis canis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Chen,S., Jancrick,J., Yokota,H., Kim,R. and Kim,S.H.
  TITLE     Crystal structure of a protein associated with cell division from
            Mycoplasma pneumoniae (GI: 13508053): a novel fold with a conserved
            sequence motif
  JOURNAL   Proteins 55 (4), 785-791 (2004)
   PUBMED   15146477
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449500
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Mycoplasmopsis canis"
                     /db_xref="taxon:29555"
     Protein         1..146
                     /product="division/cell wall cluster transcriptional
                     repressor MraZ"
                     /GO_function="GO:0000976 - transcription cis-regulatory
                     region 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=16500
     Region          7..143
                     /region_name="MraZ"
                     /note="DNA-binding transcriptional regulator and inhibitor
                     of RsmH methyltransferase activity [Translation, ribosomal
                     structure and biogenesis]; COG2001"
                     /db_xref="CDD:441604"
ORIGIN      
        1 mvniiyglhs rnaddknrvi lppaireylg tnfmvsigfd gnadlrtkee fmkyikmled
       61 qssfdkrari itrsilgnsf evtldamnri slpkhvvekl aiqkevifig agtlvemwsk
      121 emydnfesey saddiaamaq eislgk
//
LOCUS       WP_004797145             437 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Mycoplasmopsis canis].
ACCESSION   WP_004797145
VERSION     WP_004797145.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis canis (Mycoplasma canis)
  ORGANISM  Mycoplasmopsis canis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Mycoplasmopsis canis"
                     /db_xref="taxon:29555"
     Protein         1..437
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=50387
     Region          13..>351
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mliereraga pakydliyid ppynteatkn dgnsiandke nvqatkfvyr dkysrngwln
       61 lmnerlklak ellkddgvif vsiddaeqay lkvlmdeifg eenfvaslpr itkmgggrfg
      121 knfiqnvhdy ihiysknkfi laefektesd wndykfsdnl geytikhpld ggsglksyqm
      181 einfkgaiyk prngknwsfs derinfmlnn nflvfkengm vyvknykkwe ikkikdnyei
      241 iekkdgisfn slkltnnefs naqgtnllns lkinfdypks inlinslirl innkntrild
      301 ffagsgttgh avlelnkedg gnrtftlvtn nenniglnvn yerlyrinhg igskgetfew
      361 anknepyksn lnvynikyyd islfnnidvk eivkelikll kdfgvnslse esekdytnll
      421 nsllslkpql kennesn
//
LOCUS       WP_004798253             264 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Acinetobacter sp. CIP
            102637].
ACCESSION   WP_004798253
VERSION     WP_004798253.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CIP 102637
  ORGANISM  Acinetobacter sp. CIP 102637
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acinetobacter sp. CIP 102637"
                     /db_xref="taxon:1144669"
     Protein         1..264
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29860
     Region          1..257
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mshlavnlsm ifkevplier falahthgfq hieiqfpyel eifdiqtqle qydlslclin
       61 vpagdlmqgg nglagipgre vefhhalela ihyataldvp rvnilagkqp ldadllpcln
      121 tlssnlklac hmlteqgiep vfemingtdm prflvqniaq aqemleainh palkmqydcy
      181 hmammgedvl tglqenlhqi ghiqfadcps rnepdtgnip ykqifdwlrq sdyrgyigae
      241 yrpktqsdqs fawkekyfsn dvnt
//
LOCUS       WP_004794584             264 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: hydroxypyruvate isomerase family protein
            [Acinetobacter].
ACCESSION   WP_004794584
VERSION     WP_004794584.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..264
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29536
     Region          1..257
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mgrlavnlsm iftevplier falahaqgfe yveiqfpyel tiadiqtqle rynlslclin
       61 vpagdlmqgg nglagipgqe iafhealela isyatalkvp rvnilagkqp ldadllpclk
      121 tlaanlklac nllsehdiep vfemingtdm prflvqniaq aqemleavnd ptlkmqydcy
      181 hmammgedvl eglqeninsi ghiqfadcpg rhepdtaeip yeqifswlkq ssyqnyiaae
      241 ykpentsnqs ftwkkkyfsd dvni
//
LOCUS       WP_004801008             150 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Amedibacillus dolichus].
ACCESSION   WP_004801008
VERSION     WP_004801008.1
KEYWORDS    RefSeq.
SOURCE      Amedibacillus dolichus
  ORGANISM  Amedibacillus dolichus
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Erysipelotrichaceae; Amedibacillus.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 150)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Amedibacillus dolichus"
                     /db_xref="taxon:31971"
     Protein         1..150
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16477
     Region          2..150
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mkqqqyetmi aqikallege hdmianmanl sailyhslpd inwagfylyk kdelilgpfq
       61 gkvacmhipl gkgvcgtcak tltlqliddv hsfpghiacd aasrseivlp iikentllgv
      121 ldidapmlkr fditdahyls nvvkllvqsl
//
LOCUS       WP_004799151             875 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Acinetobacter sp. CIP 102637].
ACCESSION   WP_004799151
VERSION     WP_004799151.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CIP 102637
  ORGANISM  Acinetobacter sp. CIP 102637
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 875)
  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 875)
  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 875)
  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   4  (residues 1 to 875)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..875
                     /organism="Acinetobacter sp. CIP 102637"
                     /db_xref="taxon:1144669"
     Protein         1..875
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=98143
     Region          106..832
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mtqkldqmta ttlsstptnt itakinsfps afeqtdiqat llktalhahq lthtpdlaei
       61 psstkrikpl nnflgqdrar asveagislp ysgynifavg taglgkrtmi krllqqhakt
      121 matpddwvyv nnfknprqpi alrfpagqgs kfqnalqqaw qiilkqlerr fsaetyhnri
      181 erirqdtgdv qqqalveltk egeeldlkli srndkhvfip mqlkdneyhe ltqndlntlt
      241 skeraeinsn mrymekkler lglhlgdled dardqvssln rdiatqvvmp rielilnknk
      301 evkgldiylk qyaediidnv elileqeedd ftpalfnrvp sryqanviia nkpnsgapvi
      361 fedfpthynl lghveqlthn gtittdftli rsgslhrang gflmleaeql leqpyawqgl
      421 kralksgqlk lsslehmltl tgsisiepas vpldikvvll aepeiyyeil evepelgsvf
      481 kiradftdtl qrndsneqay mqliadyvqa dkllpfdrsa laalltdssr qaedqsslsl
      541 hastlgdlir eahhhafkad dkivtdqhvn qalhhrqyrl gylrelywqd lsrgtqliet
      601 sghrlgqina lsvihyadve fglpsrltas vyqgggdild iersvelggs lhakgvllms
      661 sflkahfgre qilhfsaala feqsygqvdg dsatvaelsa lisaicqipi dqswaitgsm
      721 nqlgqvqpig gvnakiegff dacklqgftg kqgviiprqn mqhlmlrqdv ieavqtgqfh
      781 vhaidtidqa leilmarpvg tldkkgrysk nsiyaavmeq leywqaiedg eavetkqpkk
      841 kkkrkkskkd emeakaadet vvevetlntl akkrk
//
LOCUS       WP_004802486             286 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Eggerthia catenaformis].
ACCESSION   WP_004802486
VERSION     WP_004802486.1
KEYWORDS    RefSeq.
SOURCE      Eggerthia catenaformis
  ORGANISM  Eggerthia catenaformis
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Coprobacillaceae; Eggerthia.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Eggerthia catenaformis"
                     /db_xref="taxon:31973"
     Protein         1..286
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32496
     Region          5..257
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mnsdidlhih taasdgtdqp lelierikna hihifsitdh dtiqgvmqvk dqipkdltfi
       61 kgiefstitp irqahilgyd ydennalfqa iikegnilrk nkmlqrldyl kdihhiifnn
      121 yelnylysln svakphlasl ivkkgyasti seaiekying ipgeterida kaaieaikes
      181 ggiaiwahpl ggenvkrlse edfmkqfhyl lnagiqglev yysryddneq kylsdlalky
      241 hllisggsdy hgqtknielg tlnknhhfid tenlsllkll kkrnkn
//
LOCUS       WP_004795824             146 aa            linear   BCT 20-JAN-2025
DEFINITION  division/cell wall cluster transcriptional repressor MraZ
            [Mycoplasmopsis canis].
ACCESSION   WP_004795824
VERSION     WP_004795824.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis canis (Mycoplasma canis)
  ORGANISM  Mycoplasmopsis canis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Chen,S., Jancrick,J., Yokota,H., Kim,R. and Kim,S.H.
  TITLE     Crystal structure of a protein associated with cell division from
            Mycoplasma pneumoniae (GI: 13508053): a novel fold with a conserved
            sequence motif
  JOURNAL   Proteins 55 (4), 785-791 (2004)
   PUBMED   15146477
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449500
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Mycoplasmopsis canis"
                     /db_xref="taxon:29555"
     Protein         1..146
                     /product="division/cell wall cluster transcriptional
                     repressor MraZ"
                     /GO_function="GO:0000976 - transcription cis-regulatory
                     region 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=16473
     Region          7..143
                     /region_name="MraZ"
                     /note="DNA-binding transcriptional regulator and inhibitor
                     of RsmH methyltransferase activity [Translation, ribosomal
                     structure and biogenesis]; COG2001"
                     /db_xref="CDD:441604"
ORIGIN      
        1 mvniiyglhs rnaddknrvi lppaireylg tnfmvsigfd gnadlrtkee fmkyikmled
       61 qssfdkrari itrsilgnsf evtldamnri slpkhvvekl aiqkevifig agtlvemwsk
      121 emydsfesey saddiaamaq eislgk
//
LOCUS       WP_004802818             357 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SPOR domain-containing protein [Acinetobacter].
ACCESSION   WP_004802818
VERSION     WP_004802818.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..357
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39628
     Region          <77..>278
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          275..349
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 msmnnkqrwm ggvvllgggv llaalllkgn deieqdhtqa pvthpipkte tkpktaqpaq
       61 dsemvslqpl avdvetekrl leeqrrsrek avaeqearaa eflkmqqqae aaaarkaaee
      121 yaainarrta aqessdnipp elvedekaka qrladekrka dekkraeqqk adqqksdadk
      181 klaedkrkae adkkaaedkr kaeadkkaae dkrkaevdkk aaedkrkaea dkkaaedkrk
      241 aeaekkaade kkrkadedsk kkaeaekard lmengdkkwm vqvalaanqa nadavvsklr
      301 akgykvttsq tskgirimvg pakdrdtadn trkkittdes lnmksawvid wvpldqr
//
LOCUS       WP_004804233             581 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Eggerthia
            catenaformis].
ACCESSION   WP_004804233
VERSION     WP_004804233.1
KEYWORDS    RefSeq.
SOURCE      Eggerthia catenaformis
  ORGANISM  Eggerthia catenaformis
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Coprobacillaceae; Eggerthia.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Eggerthia catenaformis"
                     /db_xref="taxon:31973"
     Protein         1..581
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=65313
     Region          5..556
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mikirlirll sdskkyiiyq iaeqwlsllc qiviiysasv lisqaviktl tlsdtllygl
       61 lvlggillry gldilyakss fkassdvkrv lrnkiyskll rlgtsyreki kssevmqmag
      121 egveqlevyf grylsqffya llapltlfic llrvdfkasl illaavplip ivimivmkva
      181 kklldkyfti yyglgdtfle klhgmttlki ygadeqaale mdqeseqfrk itmkvlmmql
      241 nstavmdiva yggaavgmav almeyyhgav slkgtiliil laaefflpmr llgsffhigm
      301 ngikasdrif afldlpeanr gdlelddqel sidishmsfs ynkktevlkn ismnikpqtf
      361 vsivgvsgsg kstiakilig qnktyqgdik indisllnik eesllkhitm vsfasylfkg
      421 tirdnllmgn peatdsqmme alkqvnlydf icsqdsldtk lladasnlsg gqrqrlalar
      481 allhdseiyl fdeatsnidm eseemimhvi relakkktvi lishrlanvv nsdyiymlkd
      541 gviyeegthe qlmnhksayy alyseqkele syskkgenhg e
//
LOCUS       WP_004804238             391 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Acinetobacter higginsii].
ACCESSION   WP_004804238
VERSION     WP_004804238.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter higginsii
  ORGANISM  Acinetobacter higginsii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Acinetobacter higginsii"
                     /db_xref="taxon:70347"
     Protein         1..391
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42174
     Region          5..388
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 maisvlvinc gsssikyali serredriyg laenlgaada rikgvtlgge plelsipyad
       61 hakaletlla rlanynpqai ghrvvhggdi tkaelltpel verieaatpl aplhnpahli
      121 gieatmrlfp qlpqvavfdt afhqtmpera yryalpqfly tahqvrrygf hgtshayvte
      181 raselaghkn eggwlsahlg ngsstcavwn ghsvdtsmgm tplegvvmgt rsgdvdpslh
      241 lflasnlgwd iqkidsmlnk esgllglsgl sndmrtlvea senghdgatl aievfcyrla
      301 kslsamscgl prldglvftg gigensayvr ektlgylahf gfqfskeknd alargsegri
      361 ddgtgpqiwv iptdeegria ketrqvlept a
//
LOCUS       WP_004805032             499 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase family protein [Winkia].
ACCESSION   WP_004805032
VERSION     WP_004805032.1
KEYWORDS    RefSeq.
SOURCE      Winkia
  ORGANISM  Winkia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 499)
  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 19384773
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Winkia"
                     /db_xref="taxon:2692118"
     Protein         1..499
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=53032
     Region          106..208
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          383..497
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mmstqnpdye tsyvgiqptd agssspkkps skkkwiiiga ivaalllvaa aivgysiyfk
       61 dkavpgatva gksvtgmtas qvaekvqkes asaavrisgd atksaslsdl gykvdakkaa
      121 tealapsqgf lsrlaglfnp psvtptysst agkvsayaas llggaentpv nakvvlsedg
      181 safqlksgkp grginpdqla daaqkaaktl ssqdvhvkav qsepaitdqk akafldkank
      241 lvelpftity dsesyqpsae kkrawvdfge ngagkqtapk mnndrvlewv nklagqvskd
      301 pqnglknvds sgktlatvre pedgyaidna palakagtqa lnsnkeytgk ftskpkkaew
      361 etrtiargae klaypatege kwidinlsnh tisayqgaqm lrgpepmvdg mpgyetiqgt
      421 fqiqrkyrfd dmrgedyftp dvpfamyfsg gyaihgtpwr gsfgyagpsg shgcvnlpvs
      481 lagwyyewap vgtttvvhy
//
LOCUS       WP_004805374             203 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator [Winkia].
ACCESSION   WP_004805374
VERSION     WP_004805374.1
KEYWORDS    RefSeq.
SOURCE      Winkia
  ORGANISM  Winkia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 203)
  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 203)
  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   3  (residues 1 to 203)
  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   4  (residues 1 to 203)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 203)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 203)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Winkia"
                     /db_xref="taxon:2692118"
     Protein         1..203
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22403
     Region          15..200
                     /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"
ORIGIN      
        1 mtesklkses sksngrkvlv vedealirld ivetlvdagy evvgeaadge eavqkalele
       61 pdlcvmdvkm pkmdgitaae kimtelscav vmltafsqte lverardaga mayvvkpftp
      121 aellpaveia fsrhaelisl eeeiadmter fetrkavdra kgllmdrmgm tepesfrwiq
      181 ktsmdrrlsm revadavidq vge
//
LOCUS       WP_004805561             122 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Acinetobacter higginsii].
ACCESSION   WP_004805561
VERSION     WP_004805561.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter higginsii
  ORGANISM  Acinetobacter higginsii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 122)
  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 122)
  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   3  (residues 1 to 122)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Acinetobacter higginsii"
                     /db_xref="taxon:70347"
     Protein         1..122
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14317
     Region          15..118
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mepynknlkq asrnlrsnmt daeqllwqri rrkqilglqf yrqkpilnfi vdfycpavnl
       61 viecdggqhy tetgleadqn rdhalselgl itlrftnhqv lteidavveq vyyvvrqrle
      121 ff
//
LOCUS       WP_004806056             378 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: exonuclease SbcCD subunit D [Winkia].
ACCESSION   WP_004806056
VERSION     WP_004806056.1
KEYWORDS    RefSeq.
SOURCE      Winkia
  ORGANISM  Winkia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Winkia"
                     /db_xref="taxon:2692118"
     Protein         1..378
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41432
     Region          1..267
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          265..341
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkfihtsdwh lgrtlhgadm vpaqrlfids lvdlakehrv davlisgdvy dralpsagav
       61 elledalhrl tkftrviycp gnhdsakrlg fgaeffrdel vvvsrlsqvg kavpvadgvv
      121 yplpylepia ashffgtatt hqdvmsaamq lvsqdlqqrr qkdpslpavv mahafvlggi
      181 ssdserdisi ggveavsadl fekmsyvalg hlhryqhlqg pvpiyysgsp vpysfseagt
      241 akcallvacq dgnttvtrlp ipqvrpiati tgtleellsp afasyqdawv aaqvtdvsrp
      301 pnlhrqller fphlltvqfv gaqrrpslpt ttvvqqdpvq vtidfaqqvg rkeltqkgkq
      361 iveqiwyqvr kgdehaas
//
LOCUS       WP_004806650             384 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Winkia neuii].
ACCESSION   WP_004806650
VERSION     WP_004806650.1
KEYWORDS    RefSeq.
SOURCE      Winkia neuii
  ORGANISM  Winkia neuii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Winkia.
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   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   4  (residues 1 to 384)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Winkia neuii"
                     /db_xref="taxon:33007"
     Protein         1..384
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=41118
     Region          20..320
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mtsqktsept rhaaaggasi rlshmsktyp gadspavndf nldisageil alvgpsgcgk
       61 tttlkminrl iepstgkiii ngrdvtdmnp dklrrkigyv iqagglmphl svaqnvamvp
      121 kmlgwtkkri aarvdellra valepetyad ryprdlsggq qqrvgvaral aanppvllmd
      181 epfgavdpit rralqetlla tqarlgttvv ivthdldeal klgtriails eggrlrqvgt
      241 pehilmdpad efvsdfvgad aatrllkitp vedltpsrtv tahlgddrek vlaqaaaagg
      301 hgivilnedg splawlstkq yrastgrhpq dnslplvrgt dsaadvmelm ltsthngvlv
      361 vdrqgryrfa lrasdlldqi sqea
//
LOCUS       WP_004806916             341 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter higginsii].
ACCESSION   WP_004806916
VERSION     WP_004806916.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter higginsii
  ORGANISM  Acinetobacter higginsii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 341)
  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 341)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Acinetobacter higginsii"
                     /db_xref="taxon:70347"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39007
     Region          25..211
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          255..336
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mnylwsyqrs ihsvrlmadf aselgvshaq ilkgtgleqq qlldpnmlvt gqqefqlirn
       61 lvetfsqrpl lglevgqryh fttfgslglg lissanirea lnfalayfpl sfafsqfvvs
      121 elpetdniri dievdegipq mlrqfiierd iaalitvqhd lipenlcqkv vfgfqscgeq
      181 qpyhelfgva pefggsksfi ilnaekidqk lsmanelmlh saeqqcreil dkrqsqkkya
      241 dqvqhilmns kgkiltmeev adrlylnsrt lrrylaqeqt tfikireear kmmansylss
      301 tqtsieqise wlgyaepasf ihaykrwygk tphasrlknk v
//
LOCUS       WP_004807611             399 aa            linear   BCT 20-JAN-2025
DEFINITION  TerD family protein [Acinetobacter higginsii].
ACCESSION   WP_004807611
VERSION     WP_004807611.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter higginsii
  ORGANISM  Acinetobacter higginsii
            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 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Acinetobacter higginsii"
                     /db_xref="taxon:70347"
     Protein         1..399
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=44137
     Region          23..399
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mqqlitganl alsqsqcqvk ikttlaahig ldvtayvlna qakvrgdadm ifygqkqtpn
       61 rsvelveatt kapyiaqfnl ntqlfdadis klamcatidg qgainaiqdi qielwengql
      121 tatatvksae ktekalilae vyrhkeqwkf rfvnqgfngg lkplaehfgv eisdqaatpe
      181 pvpqpvptpv pqpkinlski tldkrnsqin lqkqahgfge ikinlnwnqr tqqaqsagff
      241 kkllnqnqsi dldlgclfem qdgsksviqa lgnrfgdfng fpfiqlsadd rtgaltegew
      301 lringqhwsq irrvvlfafi yegvpnwaet davvtiyvpd qppieirlte gqplgmcgiv
      361 elvnqggsiq vqrhvryvpg hreldqafgf glrwvagsk
//
LOCUS       WP_004807526             196 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Acinetobacter].
ACCESSION   WP_004807526
VERSION     WP_004807526.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 196)
  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 196)
  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   3  (residues 1 to 196)
  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   4  (residues 1 to 196)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 196)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..196
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22389
     Region          1..191
                     /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"
ORIGIN      
        1 mpklkialid ddqaraeyik tcliehdfdv vacftldhln ifklehlqad villdmdhph
       61 rdviescvsn fdlptvlftk ntdkdmikqa idagitayiv dgidpsrlht ildisieqyk
      121 khkklecdlk daktkladrk dvekakvllm qlhgltedta fqllrknams hrmtigemar
      181 rlldaqqlln nqlkde
//
LOCUS       WP_004807680             341 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004807680
VERSION     WP_004807680.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 341)
  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 341)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38368
     Region          28..211
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          255..336
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkttstrqdq gipgvyglll ldvvsrwgys detlfapfhl tseqladpny riptpianel
       61 vkhslrltge stlgfhlgtq mrisihgfig yaimtahdit daialasrfi qlrlpflqly
      121 fstfgpkatl qlqcdievep lrteiilglt igimtmakal tgiddlsgev dldfpepagf
      181 ekykdrltst vrfnqphlis sfdkkylglk mvnadpiasq iainqcetel salgerrrla
      241 mrvrdiltns eqhylsiesv aerlhmsdrt lkrqlaaegt sfstlvdevr yrhatsllsr
      301 tdysleqiad elgysdvanf srafkrwsgr spsnwrkdpy l
//
LOCUS       WP_004808908             412 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Cutibacterium
            avidum].
ACCESSION   WP_004808908
VERSION     WP_004808908.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium avidum
  ORGANISM  Cutibacterium avidum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (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   2  (residues 1 to 412)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Cutibacterium avidum"
                     /db_xref="taxon:33010"
     Protein         1..412
                     /product="aminoglycoside 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=44758
     Region          160..338
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mrrpawlgga gkdadgavll tgpeagellt aavehaggvl lewrldhvda npgqsttaty
       61 qarvqwqtgk rqelfgmsar angpamtdsr adiyvdgsre vavwrypddp dlpglsraay
      121 peqmatimsd lglvdggvsa dqinlrmigy rprrravlcv evpnrrfyvk vlrdgifqat
      181 larhdlltra svpsprvagv tddnllflte lpgrplskal fepgnpctae slvglldqlp
      241 pqvcelprrs pwsesvdhyc rmvaaampdq qdrldrmari isqglsglpq gnepthgdfh
      301 egqihvwngq vcgildvdti gpgrraddla clvahlstvq hmnssqadrm rqilagwvpv
      361 fdtrvdpvel rlrsaavais latgpyrsqe anwgaetlsl idaaealinq va
//
LOCUS       WP_004808973             315 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Cutibacterium avidum].
ACCESSION   WP_004808973
VERSION     WP_004808973.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium avidum
  ORGANISM  Cutibacterium avidum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 315)
  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 315)
  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   3  (residues 1 to 315)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Cutibacterium avidum"
                     /db_xref="taxon:33010"
     Protein         1..315
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35698
     Region          189..293
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mneldfewra nggvarihrf shlrgqadra vaagkavril pgvvsptsva ndprvrikav
       61 hmwhrdavli gkaalvmqgl kppgqhlhdl davkeveays rtrsieregi rvhrwrvprr
      121 yvterygmwv vepevsvlll aldgdwawvc ealrqglvsp escrasrssl swrfsrrqis
      181 saladinlrs wsipelefgr lmravgitgv kpnqavragn rryildkafe aekvaveidg
      241 raihgtidgy entmmrsanl drsgwkilht tptmirqhpq fvldwlashl hrrhrprttf
      301 pehilrqtia givpa
//
LOCUS       WP_004809402             192 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Acinetobacter].
ACCESSION   WP_004809402
VERSION     WP_004809402.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 192)
  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 192)
  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   3  (residues 1 to 192)
  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   4  (residues 1 to 192)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 192)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..192
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21611
     Region          1..191
                     /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"
ORIGIN      
        1 mpklkialid dnaeraefiq dsltahdfiv vacliihdls mthvknlqad villnmdhph
       61 rdiiescvsq yelptvlftq nsnkdtiksa idagvtayiv dgidpsklns imeisieqfr
      121 khkkllndlk etqdkladrr didkakslli qlhsmseeqa fallrknams hritlgemar
      181 rlldaqklls ge
//
LOCUS       WP_004809513             342 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004809513
VERSION     WP_004809513.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 342)
  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 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 342)
  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   4  (residues 1 to 342)
  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 342)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..342
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38722
     Region          32..209
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          256..337
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkmiaprqdq gipgvyglll ldvisrwgyn deslfkpfgl tseqladpef riptaiandm
       61 vkhalkltge ptlgyhlgtq mrisihgfig yaimtannit ealvlanrfi qlrlpflqlf
      121 fstfgvkatv qlqtdiqmep lrteisialm iglismakai tgisdatgei dfdfkkpegf
      181 erfmvkfpth qfrfeqphll lsfdksylmn klvhadpias qiainqcete lsalgerhri
      241 amrvrdiltn seqhylsiea vadrlhmsdr tlkrqlaaeg tsfstlvdev ryrhatslls
      301 rtdftleqia delgysdvan fsrafkrwsg rspsnwrkdp yl
//
LOCUS       WP_004809929             293 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Cutibacterium avidum].
ACCESSION   WP_004809929
VERSION     WP_004809929.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium avidum
  ORGANISM  Cutibacterium avidum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 293)
  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 293)
  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   3  (residues 1 to 293)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Cutibacterium avidum"
                     /db_xref="taxon:33010"
     Protein         1..293
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33778
     Region          179..285
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 melvdileas ggvakissvg rvarqarkaa regwvirplp rivmttdavr rpdawmravm
       61 lwrpnaiftg raalylagmr dvdvteidvi iphamprlpr rswlrfhrag resiiddrng
      121 frtthaytcf wlalrgdwea ataslragwv speelrdarr rlarkvspgt tkevlrqlld
      181 rpwsvaerel hallheyrvn gwranerlwi ngrvlfpdlw fkhekvivev dgytfhgkpr
      241 dyemtarrha llagagwrvi rvtpmmirea pelvldtirs alwrrhqgvl vpv
//
LOCUS       WP_004812474             395 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Anaerococcus hydrogenalis].
ACCESSION   WP_004812474
VERSION     WP_004812474.1
KEYWORDS    RefSeq.
SOURCE      Anaerococcus hydrogenalis
  ORGANISM  Anaerococcus hydrogenalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Anaerococcus.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Anaerococcus hydrogenalis"
                     /db_xref="taxon:33029"
     Protein         1..395
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43762
     Region          1..395
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkilvincgs sslkyqlfdm dneevlvkgl verigidgsr lkqekgedey iieedmkdht
       61 eavkhvfdai tdkengvisd lseidavghr fvhggekitk svvidenvre avkeyskfap
      121 lhnpanmmgl eacekllpnv knvavfdtaf hqsmpeenfl ygidykyyed qavrkygfhg
      181 tshdfitqkt aevlekdqkd lnmischlgn gssicaikeg ksfdttmglt pleglvmgtr
      241 sgdldptvvt flmneygydt kkmdnvlnke sgvlgvsgvs sdfrdlenaa ndgnkradia
      301 lkmfanrakr yiagymaevg nveaivftgg igensitmre simegfeqfg ikidpeknnv
      361 rggchlvstd dskvkvfvia tneelmiard tkklv
//
LOCUS       WP_004813016             140 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Acinetobacter].
ACCESSION   WP_004813016
VERSION     WP_004813016.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..140
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15640
     Region          3..134
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mtllilflsa fgaatllplq seavllgllv nssysaftli avasvgnilg scvnwylglr
       61 ieqykgrkwf pvseqqmqka qrsyqkygyw slllswvpmi gdpitliagl lkenfarfll
      121 ivsiakigry lfiymaysmi
//
LOCUS       WP_004813087             141 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Acinetobacter schindleri].
ACCESSION   WP_004813087
VERSION     WP_004813087.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter schindleri
  ORGANISM  Acinetobacter schindleri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 141)
  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   2  (residues 1 to 141)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Acinetobacter schindleri"
                     /db_xref="taxon:108981"
     Protein         1..141
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15789
     Region          70..139
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkiiknrsis relisiilti lsvlyssfaa aaqnesyadw kakqqqydar lkqqqnrpsq
       61 nhsnhylakp elaavssadr irlnsatveq lqqlhgighk kaeaiieyrn thgkfkrved
      121 iqlvkgigpa lfaknqarla l
//
LOCUS       WP_004813100             232 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Acinetobacter].
ACCESSION   WP_004813100
VERSION     WP_004813100.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 232)
  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 232)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 232)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..232
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=25691
     Region          7..209
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 msaiggdeql eslksftkky gssiitgilv aliaffgwey wqkknlaesq kqtakvqqlm
       61 ddarstqgda faklsdtadk ivkeapdsaq aiqtqlvmak laydkedyaa aeralkkven
      121 skvddaglvq vvklrlayaq laqkkydaal ktleavnepa fkatadearg diyvakndie
      181 nakkvyqsaw dtlverkeer qilqiklesv gvlvddpeie rpiidtqvee te
//
LOCUS       WP_004813650             336 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004813650
VERSION     WP_004813650.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 336)
  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 336)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..336
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39530
     Region          <62..202
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          249..328
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mhsiqddagt vygglghlll efylskqlpi pekllaiqdv erfefviwre llmqlqqklq
       61 tpalgleian fvqprhlgii aylalscetl seammryhdy hrlvydgspl evrvendyls
      121 iawvdvplnl atqltdevam almlkfvrsl matddihlhe vhfrqptnky lnlyeqyfrc
      181 kvrfdqpksv ifmhvselak plrqgdqtlq kllkqqaeal leklpntsqi dhriqqailt
      241 glqknmfqie hiarqlhwsv rqlqrhlqkq gktyqqrmqe irfmlaqqyl tdenlslhei
      301 slllgyseqs afqrafkqwt rqtpqqwrsd ylknkt
//
LOCUS       WP_004816992             233 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Acinetobacter].
ACCESSION   WP_004816992
VERSION     WP_004816992.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 233)
  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 233)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 233)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..233
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=25621
     Region          5..211
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 msamtddeql dsvksffkky gsamvtgvli aliaffgwey wqkktlaenq netakvqqlm
       61 dearaangda kvtaalvasa dkivkdnpds vhaiqaqivm akvaydkndy alaerelkkv
      121 enskikdagl lqvvkiklad aqlaqkkfde alktlsavnd pafqasadel kgdiyvaknd
      181 tenakksyqa awnavverkq erqilqikle svgvlvedpd lerpilatqv des
//
LOCUS       WP_004817015             153 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Acinetobacter].
ACCESSION   WP_004817015
VERSION     WP_004817015.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 153)
  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   2  (residues 1 to 153)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..153
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16882
     Region          92..152
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 msnqhfyfnr vvklikssfl lvllscslsl yaqqfdqayl nwkaqqqahd aqlkkvddqy
       61 ylsrpnsqks psnsshkgps ssaqssnssa lkvslnsana eqlqqltgvg akkaqaiiay
      121 rnqnggfksi ddlkkvkgig eklfeqnrar lsl
//
LOCUS       WP_004817180             364 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Anaerococcus hydrogenalis].
ACCESSION   WP_004817180
VERSION     WP_004817180.1
KEYWORDS    RefSeq.
SOURCE      Anaerococcus hydrogenalis
  ORGANISM  Anaerococcus hydrogenalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Anaerococcus.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Anaerococcus hydrogenalis"
                     /db_xref="taxon:33029"
     Protein         1..364
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42495
     Region          1..265
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          261..344
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkllhlsdlh igknigaysl ledqkycldq ileiikneni diviiagdif dtsipnsesm
       61 kvysdfvdki ifdlkkkiia isgnhdsgkr leisksffek nsyyifgssf dksltfkdef
      121 glvnfypipy islaraknei dpnienftdl yrillkdiny kdrnvlishc yanekafede
      181 eiegekplti ggndamdanl fenfdyvalg hlhrkhfvid ekirycgtfm kysfsevrqk
      241 ksvtvvdlkd nisikeieir plndfcqied yfenilkmen sndyiefilk ddqpidspma
      301 klkikfphav sirykntidl egyddieidl enlstmeifq kfykfkmden msekdkeifk
      361 kviq
//
LOCUS       WP_004818649             142 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acinetobacter guillouiae].
ACCESSION   WP_004818649
VERSION     WP_004818649.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter guillouiae
  ORGANISM  Acinetobacter guillouiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Acinetobacter guillouiae"
                     /db_xref="taxon:106649"
     Protein         1..142
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15339
     Region          1..125
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkqkgftlve llivvaiigi laaiaypsyq eyivrtnrvd aqsemlqiar nlsnykmakg
       61 tfkdakleng afeedypsvg eakykvklev skdnltwsln aapiagsqqa gngdvgldsq
      121 gqkcwskgtt ctpsattnwd gk
//
LOCUS       WP_004796601             244 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Mycoplasmopsis
            canis].
ACCESSION   WP_004796601
VERSION     WP_004796601.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis canis (Mycoplasma canis)
  ORGANISM  Mycoplasmopsis canis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
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
REFERENCE   2  (residues 1 to 244)
  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 244)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 244)
  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   5  (residues 1 to 244)
  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 10164212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Mycoplasmopsis canis"
                     /db_xref="taxon:29555"
     Protein         1..244
                     /product="winged 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=28571
     Region          30..95
                     /region_name="WHTH_GntR"
                     /note="Winged helix-turn-helix (WHTH) DNA-binding domain
                     of the GntR family of transcriptional regulators; cd07377"
                     /db_xref="CDD:153418"
     Site            order(30,32,55,57..58,66..70,72..73,76,86..87,89..92)
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:153418"
ORIGIN      
        1 msktykknid nfpqikkaik rnplneednt ktnsiilyli dlikskkvpv nkimpsehal
       61 merfncsrsv vvsayqklna lgavysiskr ghfvaenfhn likpvsfllk vdkqwgeemh
      121 dfvlpewfee rniifvdgtr mfkksfykkg eviaeadiwi stknldkfep vdlskplidi
      181 lserepikni vydihfekna nrlgyedmmv lmlfgyddds iciaakyyik pehfkfyhqe
      241 fsll
//
LOCUS       WP_004818688             170 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Anaerococcus hydrogenalis].
ACCESSION   WP_004818688
VERSION     WP_004818688.1
KEYWORDS    RefSeq.
SOURCE      Anaerococcus hydrogenalis
  ORGANISM  Anaerococcus hydrogenalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Anaerococcus.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Anaerococcus hydrogenalis"
                     /db_xref="taxon:33029"
     Protein         1..170
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19384
     Region          3..160
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mefdkvidkr vstrafldkk iekkdlekiv eagvkapvgk sqyenmaitv itnkefinei
       61 leeareivnd pkanpiysap yliiisakdg hvtrledtac iienmslkat dleigscyir
      121 gmferfdkka rfieklniek dfypvhglil gypkeelkgk nhsiktnyid
//
LOCUS       WP_004819290            1234 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein, partial [Acinetobacter guillouiae].
ACCESSION   WP_004819290
VERSION     WP_004819290.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter guillouiae
  ORGANISM  Acinetobacter guillouiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 1234)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 1234)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 1234)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..1234
                     /organism="Acinetobacter guillouiae"
                     /db_xref="taxon:106649"
     Protein         1..>1234
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
     Region          <204..388
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          339..>541
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          <1150..>1234
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 msrigsflnn rekmfeannv ggdlsstisa inniyselnn ansgnnreaf rsflllvqdv
       61 idlfpnsnnl niannlvrvv tlsdrlalnv ndyidtvtig sskynngfvk ktlvldifsd
      121 ataifselsk ftrasplgvv vnvfsmlfaa isngmnlape wndkqlihkd eilklfldgv
      181 sfvldssvel lqpiistven yipdglnpwa gdvvvliddk tggndikgiy nrkytifgnd
      241 gndilignkl ndyldggadn dflyggegnd vliggsgsde lyggagddvl vvseidtslt
      301 saenaakldq vgnkayggsg sdniyggngs delyagdkdn dpndagtink lyggggddyl
      361 yggagndyly gglgsdrlsg gdgndslyla sdsdpakial disknyaegg agndtihgsd
      421 gddsiftsdi nddaidkgti nyawgykged yirggdgkdf lyggddvdtl lggngddkly
      481 ggkngdtlyg gegndelyag rqkddpldte dnylyggkgd dilyggkgnd tlkggegfdt
      541 ykayyktlvn dedgkgilyy nnknllgaem ryksdslspp paldfiskgy dindkstggg
      601 rlsvissgkd wvryivlgdi nfkykeltte aldtrskddt dlgvrfyvtv ykdgsepppp
      661 eypkpkppla pppipptkyd plvldlnhdg kisttplgtd vyfdmdgnsf aektswvqat
      721 dgfvvldlne ngkidngkel fgtdtilpdg skasdgfkal eqydsnkdgl ingsdlifqk
      781 lkiwkdinqd gisqsnelft lsslgitsis lsnqlinsld ennvihtnkg sftqtvveng
      841 itqiksglae tllfevntse tvwqnpnetv esidtdisel pdfpgygsat slhdamqldl
      901 tgklkelvsa fsetpsdqqv llthqilyfw tnkklstate vknissiekf eivkviygke
      961 lewknwnpgn vndldgyfqk ilssayvqll sqtvkqdwid lvafqeerly esydpfppli
     1021 qppaggsgss sgsvyipnki yattwdslkp nkyvenvlnp tqvrevswtl vnttwhgdfs
     1081 laikglmnlf fmdyevgkie ieqfqfivqg ldpnspvlyk elieqftlsa qsildenird
     1141 lllesvfvld dsitgtngnd kikswagddn inslggddii yagmgddivn agdgedivyg
     1201 gddndrlsge ngndllngdl gndtlyggeg ndtl
//
LOCUS       WP_004820011             710 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Peptoniphilus indolicus].
ACCESSION   WP_004820011
VERSION     WP_004820011.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus indolicus
  ORGANISM  Peptoniphilus indolicus
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Peptoniphilus indolicus"
                     /db_xref="taxon:33030"
     Protein         1..710
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=80630
     Region          604..676
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 mdrklkkdfr erhkaslere mlkdetssip eesklkhsdd yrgkivhdke rfqdkvheki
       61 skvssyneqv qgtskrnary ratnkgsvns lnetgasdyd tevkngkiyd plgqdldndg
      121 iidrydndfr dsdyfestyy vddnlhkkde figsssknhk aqksmykrkn yseslytrkk
      181 ddvpkenkse gnkagkdavs ekenislskd qkkklkkdmv kvsalsglak gsetvrdyls
      241 hgsdenkgve agektadass klihgikrys dkkrakkgyd ltnkdykirk rksklefrda
      301 keelkktdey krasaykrfq kknqvkaais renksrlrdr ikegligtlk sskdmiirka
      361 kglmlifigi iilgtfvinf agtgmtgfmn stssvlttsy lskpnvlsei nqkfsamege
      421 lqrevdhvee nypgydeyil nnteyighnv hellsyitsr cgevknvsev esilkelfes
      481 mydleyreei eiryrtvtet ytdedgneyt esheepyeyk klivtlhkke mdsiirkvfa
      541 nypdnlkhye alflaqgnmg evfgnsdlis snggvgggke yeastevqkk ivnaayitps
      601 pgagwcamwv sqvyqnaglg yiggnandmy rnytftsdrs klkvgmlvav essssgstag
      661 ltyghvgiyi gdgkvidnig yirvttlddw iatfckhhpv gfgfppnvnr
//
LOCUS       WP_004821970             400 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Acinetobacter
            guillouiae].
ACCESSION   WP_004821970
VERSION     WP_004821970.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter guillouiae
  ORGANISM  Acinetobacter guillouiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (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   2  (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
REFERENCE   3  (residues 1 to 400)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Acinetobacter guillouiae"
                     /db_xref="taxon:106649"
     Protein         1..400
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46328
     Region          6..381
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mieslrrlal shqglispas fgtglsgtrh aiehlgyvqi dtisvverah hhilwsrvpd
       61 yqqshlnqlv kqqhifeywf haasylpmqd yryalphmts irngehryfn rgdqafmnei
      121 larakaegsi rlrnieqgnk qnsggwwnss larrsieqlf mqgdlmiser ngmekvyqlt
      181 eycipshldl svptleeyar ylfnttlrah gvfawkqllh lkvgqkirea mrdivneqld
      241 agvittlaql gssdkesqnl yiqtdaleql pnielkvkil spfdnlvihr erlntlfkfd
      301 yrlecyvtpp krvfgyfclp ilygdqivgr idckahrakn qfevislhle pqhlnhtiad
      361 pahffsalnt eihhfaqfnq cinineglhk ildesnkrfk
//
LOCUS       WP_004822405             342 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter guillouiae].
ACCESSION   WP_004822405
VERSION     WP_004822405.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter guillouiae
  ORGANISM  Acinetobacter guillouiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 342)
  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 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 342)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 342)
  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   5  (residues 1 to 342)
  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   6  (residues 1 to 342)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Acinetobacter guillouiae"
                     /db_xref="taxon:106649"
     Protein         1..342
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39590
     Region          33..210
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <231..339
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 meytvnnqqf seskgtisia lvhealssaq dkgydiqqil hdaeipleif qaaksriavs
       61 ayaklwtkia dhmndeffgm dshqmrrgcy kllskmvmqa dtlqtaieqi lqyfnfvldd
      121 fsskliiden yayivitdkl qtkrmfcyat yimlihslic wladqrilln qlqlkctppe
      181 ddsdyrvrfc enityqaden ylqfdanyln iqikrdqksw ygfikntpen lllrfknpla
      241 lssmirkqll siapaewlel gelsaqlnis eatiqrrlkn egssyqqlkn dirrdmaiel
      301 lgktthtlqd isellnfqda safhrafkkw tgvspgayre pk
//
LOCUS       WP_004823148             353 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Acinetobacter].
ACCESSION   WP_004823148
VERSION     WP_004823148.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..353
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39714
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvkniek nfgafhalkn isldfpegql vallgpsgcg kttllriiag lestdrgqvi
       61 legtdatnih vrerqvgfvf qhyalfrhmt vydnvafglr vrpkatrpne teikkrvtrl
      121 ldlvqlgfla drypaqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 tlhdelhits ifvthdqeea levadqivvm nkgdieqigs prevyekpat pfvfdflgqa
      241 nrfegenhqg iiqigedriq lptatqtang kviafarpne lkihtqpten tiqatflrel
      301 wiagkvmael qdrqgqliei alnpdeaklh qyrpnqtvwv sastlhlfen qva
//
LOCUS       WP_004824911             195 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Peptoniphilus lacrimalis].
ACCESSION   WP_004824911
VERSION     WP_004824911.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus lacrimalis
  ORGANISM  Peptoniphilus lacrimalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Peptoniphilus lacrimalis"
                     /db_xref="taxon:33031"
     Protein         1..195
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=22976
     Region          8..194
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mntlkeyiqe nliitnkeae elgytrhnls eltksgqler lrpglyqlkg kviddfvlis
       61 snsnriifsh qtalylhdls drtpnvfhis vpqgynashi knrykdlqvh yvkidlyeig
      121 kteikspqgn lipvydieri iceiiidrek idkqifteam kryfkspnkn lrrlikysrl
      181 fkiedeirky mevls
//
LOCUS       WP_004825011             262 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Acinetobacter].
ACCESSION   WP_004825011
VERSION     WP_004825011.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   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 262)
  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 262)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..262
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28601
     Region          24..91
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          190..251
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mevnpnsqqp tgsnvasngl gnvqrpgeyl rqirvsknld iqdvakelkm pvktlqaleq
       61 deykslpeat fikgyyrsya kflgvdatvi iqrfdeiyqn dtgllpnhal nnspikimgk
      121 lpgsnsdrnk kwlkraliai vaiaviwali agiqkftssk sndtdakpqe sevevlnlnn
      181 atatsgdqmv lnfshptsvh ivdstgkvla tgrqsatltl sgqspfqirl ddatavslsl
      241 nneqislspy tvngkaefrl sr
//
LOCUS       WP_004825388             123 aa            linear   BCT 20-JAN-2025
DEFINITION  zinc ribbon domain-containing protein [Peptoniphilus lacrimalis].
ACCESSION   WP_004825388
VERSION     WP_004825388.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus lacrimalis
  ORGANISM  Peptoniphilus lacrimalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
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 12181465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Peptoniphilus lacrimalis"
                     /db_xref="taxon:33031"
     Protein         1..123
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14329
     Region          24..120
                     /region_name="zinc_ribbon_15"
                     /note="zinc-ribbon family; pfam17032"
                     /db_xref="CDD:465334"
ORIGIN      
        1 mfficgitng kddlsydgdl fvhscgaygr yqvfmtyfkl slffipilkf nkkyfvrttc
       61 cdkiygldks lgqkiensid viineddlie ieyeqnsnfk icknckykth keflycpkcg
      121 qkl
//
LOCUS       WP_004826594             336 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004826594
VERSION     WP_004826594.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 336)
  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   6  (residues 1 to 336)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..336
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38198
     Region          22..206
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <138..336
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msqltdasvv lrlgyqairr aglpteeils kagvalgqvd qnartplnaq fafwvaaeev
       61 sndpdiglhl gehlplyrgq viehlfisse nfgeglkral ayqrlisdaf haklvvddng
      121 rcyltngeqp wgenivnrhf secaisgilr ffkfitegrf epiyidfnfs qgasdgeyyr
      181 vygcpvslgq ketrlyfdps ildyplwqae pellqlheql aieklqelar ydlvgevrra
      241 igstlesget tletvaaqls itprrlrtql seantsfqqi lsdyrcrlak kllantnesv
      301 erivyltgfs epstfyrafk rwtnetpvey rkrkqr
//
LOCUS       WP_004828103             279 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Anaerococcus
            lactolyticus].
ACCESSION   WP_004828103
VERSION     WP_004828103.1
KEYWORDS    RefSeq.
SOURCE      Anaerococcus lactolyticus
  ORGANISM  Anaerococcus lactolyticus
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Anaerococcus.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Anaerococcus lactolyticus"
                     /db_xref="taxon:33032"
     Protein         1..279
                     /product="formate/nitrite transporter family protein"
                     /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=30075
     Region          5..278
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mqtdlspdki lpraidvytn ktkikmgklm ilaffagvfv alaceastla assllgdrsk
       61 fpigklvqgl vftpglifvi laggelftgn tlmtiplldk kislgvmlrs wilvyfgnfi
      121 galfvaflls rsgqwffadg lvgvrtilia kgkidfsfgq alvlgllgnf lvclgvwmsl
      181 gaksygskvi saffpisvfv lsgfehsian myylpagila knfpdfaskt glgletlksl
      241 nisnmvfknl fpvtlgniig gtifigtlyf layrndnkd
//
LOCUS       WP_004828399             373 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Anaerococcus lactolyticus].
ACCESSION   WP_004828399
VERSION     WP_004828399.1
KEYWORDS    RefSeq.
SOURCE      Anaerococcus lactolyticus
  ORGANISM  Anaerococcus lactolyticus
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Anaerococcus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Anaerococcus lactolyticus"
                     /db_xref="taxon:33032"
     Protein         1..373
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42451
     Region          1..268
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          265..346
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkllhlsdlh igkslgnfsf ledqkyvldq ildiieerki davmiagdif dtavasadal
       61 dlynyfieki ifdikipvla isgnhdsakr ldvnkrfykt nkyylageyt kevvtleden
      121 gpihffllpf mslakarvif gedladftdl yrealkdyky edrnilithc yatefnqsle
      181 kdynegqkpl tiggsdcmda glfmgfdyva lghlhsahyv ldpkirysgt fmpysfdkkd
      241 nnksvtivdl gsesieieki pikllrdfev rtgffddlig epasdsyikf iledgatien
      301 amakfkkkfp navlinyasr svfamndedi nidienkstl elfedfvayk dkrqmtadek
      361 tvledvigvi neg
//
LOCUS       WP_004828983             102 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Acinetobacter].
ACCESSION   WP_004828983
VERSION     WP_004828983.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 102)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 102)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..102
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=10818
     Region          25..102
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mlnssvlskt aidhdskqss ptieikiecf gaierllpsd lslqtksgmt isdvlddlic
       61 rypkaeslld rcacaigedi iprqtllesd stvvllspva gg
//
LOCUS       WP_004830772             443 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Acinetobacter
            bereziniae].
ACCESSION   WP_004830772
VERSION     WP_004830772.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter bereziniae
  ORGANISM  Acinetobacter bereziniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 443)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 443)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Acinetobacter bereziniae"
                     /db_xref="taxon:106648"
     Protein         1..443
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=51073
     Region          40..431
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mkkftiqalf dthwldiael kildpekgsa spceleyqie yaisyldkrd ehacslslpv
       61 qliikheakt wfgflddiip sgaarrywin ylnlqkfsha eqdtilleke viapvgnlri
      121 kesippinpe stlhlrkfst advadrnadf leyaqqmgai sggatgagge apkllvryta
      181 dqkvwidtyq qsfdtpdqhy lvkfprnnrs eidcnilrae yyyyhelnel gfstidtanm
      241 rliegeryps lwlprfdtew cdqrwhrygl esvysilnks agshlnhfev idslcillkt
      301 idtkfnstqf vcewlerdll niifgnsdnh grntsflkkt gnvflspiyd fapmkadpeh
      361 virsttwgsp yeeggeyqwi qisqklapwc dpdisletlk slankllglk qrlidkgipk
      421 qiiempvlsf dyieaklkrw ell
//
LOCUS       WP_004832585             161 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Parvimonas micra].
ACCESSION   WP_004832585
VERSION     WP_004832585.1
KEYWORDS    RefSeq.
SOURCE      Parvimonas micra
  ORGANISM  Parvimonas micra
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Parvimonas.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 161)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Parvimonas micra"
                     /db_xref="taxon:33033"
     Protein         1..161
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18085
     Region          13..161
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfnpikyegn lgeqysylik dlyelcnnee ntianlsnaa allnffleki nwvgfyllde
       61 ktntlvlgpf qglpacvriq ngegvcgtsa slkktlnien vhnfkghiac dgksnseivi
      121 pifrndkifg vldidspifn rfskeeetyl eafvkqleth i
//
LOCUS       WP_004833482             278 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Acinetobacter
            baumannii].
ACCESSION   WP_004833482
VERSION     WP_004833482.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..278
                     /product="formate/nitrite transporter family protein"
                     /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=30735
     Region          28..278
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mdheleeekv dqtlswrekm aveeheklsp rlvyeiirrd gaeeldrpta alifsgiaag
       61 lvisfsfvfk aiiasyiptd aiwtdlitnf gytigfliai lghmqlften tittvvplfk
      121 pftldklrav grlwgivilc niigtalasl fflttdlftp nidkaldela hhvasfsatq
      181 nllkgvmsgl liaalvwmlp svsnkflvif fmtyliglgd fthvvvgste msylvwqgea
      241 slgeylfnfl ipttigniig gtgvftlliy gqvteele
//
LOCUS       WP_004807473              83 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Acinetobacter].
ACCESSION   WP_004807473
VERSION     WP_004807473.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..83
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8882
     Region          6..83
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mqtieikiea fgaierllpk plafefaadr mvkdvlahiv tlypeadham ekcacaiged
       61 iitrqtalen sctlvllspv agg
//
LOCUS       WP_004833784             372 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Anaerococcus prevotii].
ACCESSION   WP_004833784
VERSION     WP_004833784.1
KEYWORDS    RefSeq.
SOURCE      Anaerococcus prevotii
  ORGANISM  Anaerococcus prevotii
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Anaerococcus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Anaerococcus prevotii"
                     /db_xref="taxon:33034"
     Protein         1..372
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42959
     Region          1..267
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          264..346
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkllhlsdlh igksignysl iedqryalke ivriveerki dvvlvagdif dtsipsseal
       61 slysdfldel ifrldkkvla iagnhdsskr ldinknfyrs nnyflvsele repivledey
      121 gkinfylipf islakakaei dsdienftdl yrhilndisy edrnvlvshc yasnmgiyde
      181 eiyddgqkpl tiggsdamda nlfmefdyva lghlhrahfv idpkirysgt fmkysfdeal
      241 geksvtiidl tkdidiekip iknfrdfevr rgkfedilks easdnyikfi leddytiena
      301 maklkskfpl avsisyanka vfsredtldi dienkdavel ftdfykfkmd edmtndeiet
      361 lkriivcdqk dl
//
LOCUS       WP_004833815             240 aa            linear   BCT 20-JAN-2025
DEFINITION  YaaA family protein [Anaerococcus prevotii].
ACCESSION   WP_004833815
VERSION     WP_004833815.1
KEYWORDS    RefSeq.
SOURCE      Anaerococcus prevotii
  ORGANISM  Anaerococcus prevotii
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Anaerococcus.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Prahlad,J., Yuan,Y., Lin,J., Chang,C.W., Iwata-Reuyl,D., Liu,Y., de
            Crecy-Lagard,V. and Wilson,M.A.
  TITLE     The DUF328 family member YaaA is a DNA-binding protein with a novel
            fold
  JOURNAL   J Biol Chem 295 (41), 14236-14247 (2020)
   PUBMED   32796037
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Liu,Y., Bauer,S.C. and Imlay,J.A.
  TITLE     The YaaA protein of the Escherichia coli OxyR regulon lessens
            hydrogen peroxide toxicity by diminishing the amount of
            intracellular unincorporated iron
  JOURNAL   J Bacteriol 193 (9), 2186-2196 (2011)
   PUBMED   21378183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006857
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Anaerococcus prevotii"
                     /db_xref="taxon:33034"
     Protein         1..240
                     /product="YaaA family protein"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=28546
     Region          2..237
                     /region_name="YaaA"
                     /note="DNA-binding protein YaaA associated with the
                     oxidative stress response [Replication, recombination and
                     repair]; COG3022"
                     /db_xref="CDD:442258"
ORIGIN      
        1 mkiiispakr fkhfdniets silfpektqq lvnkirklsm neignlnktn dkltekayfd
       61 yqefdfndmp npalfsydgl vfkqfdmgdf kdrdflnnhv yiisalygpl kpftgirdyr
      121 lyfdndmidl ykfwaddiyk evfrdndlvi nlaskeyskt ikpylkendk fitidfkdek
      181 ngklrsvvaw tkqmrgkmlr eiiinkitdq eeiknieidg yifdpyiste dnmvfvrrdn
//
LOCUS       WP_004833931             278 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Anaerococcus].
ACCESSION   WP_004833931
VERSION     WP_004833931.1
KEYWORDS    RefSeq.
SOURCE      Anaerococcus
  ORGANISM  Anaerococcus
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Anaerococcus"
                     /db_xref="taxon:165779"
     Protein         1..278
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31766
     Region          4..254
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mkkiyadlhs htnhsdglle iedvlkrakd kgvevlaitd hdtsnhfgei kkkageigik
       61 tlkalemscy dyevdkkvhi valflpeetp nidnlcndfl krrdsnhrkl ikdlnkkgyd
      121 isyadckkfs pysivfksni iqalkekype kkeeitfski fgsmkdkkkn lemgyidvee
      181 gikailadda ipiiahpcqy enypeiekyv gfglkgieis hskmkeidyk itkdiankyd
      241 llesggtdfh dpdkhhfgef glskdefesl lekankti
//
LOCUS       WP_004833953             356 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SPOR domain-containing protein [Acinetobacter].
ACCESSION   WP_004833953
VERSION     WP_004833953.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..356
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38485
     Region          271..345
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 msmnnkqrwm ggvvllgggv llaalllkgn eeikqvdvqp qtstspklqa kpkqsaqegq
       61 mvqlqplavd vetekrllee qrrsrekava eqearaaefl amqqqaeada arkaaaeyaa
      121 inarraaaqe ssdnippeva gsenkakgqq tdtkksvdla kadadkkaae akrlaeadkk
      181 aaeakrqaea dkkaaeakrq aeadkkaaea krqaeadkka aevkrqaead kkaaeakrqa
      241 eadkkaaeak rkaeaekkae aekarellen gdkkwmvqva laanqanada vvsklrakgy
      301 kvttsptskg irimvgpakd rdtadttrkk itsdaslnmk sawvidwvpl dqrksd
//
LOCUS       WP_004834017             445 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Anaerococcus prevotii].
ACCESSION   WP_004834017
VERSION     WP_004834017.1
KEYWORDS    RefSeq.
SOURCE      Anaerococcus prevotii
  ORGANISM  Anaerococcus prevotii
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Anaerococcus.
REFERENCE   1  (residues 1 to 445)
  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 19384773
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Anaerococcus prevotii"
                     /db_xref="taxon:33034"
     Protein         1..445
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=50160
     Region          27..159
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          169..277
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          310..432
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mgslvftfit lpntyingkn vsfasresal eevgerfdle vsgrddrkln ldsdqidyna
       61 tipanasidq npfawplnmv glkkdqlkfd ykisydeekl deilkgsplf tnitepedag
      121 vvfkgdsfdl kdavmgnkld ytkvkddiir aistdhkdik leddfyespt vlsdspelka
      181 leedakkiea mnikfnfngf dlklkgedlv nmiyqegkkf qidydklmef madiadktdt
      241 ygrdrkfyat gigeivvnpg vygfvldqaa tgdevlklfn qrksgdvepi yeryaynree
      301 dgsdlgntyi evdisrqymw fykngelive splvtginqg gwqtnvgvgs ilskntnttl
      361 egvgfvgdry ktpvrfwmpi gwdgegfhda dwrysfggdi yqydgshgcl nlppsvaeiv
      421 fnnvevhtpv vvyesstnns pamiy
//
LOCUS       WP_004835572             337 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter baumannii].
ACCESSION   WP_004835572
VERSION     WP_004835572.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 337)
  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 337)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..337
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38410
     Region          25..208
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          252..333
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkyawafers vhsvrlmadf amesgisyqt ilqgtglsqq qlldpnmvvt ghqelqlihn
       61 lveqlgdrpt lglevgtryh fttfgplgma lmssasirea ldlaltyftl tfaftrfdvs
      121 dtpqgiriei deqdipssvr qfiierdaaa litvqrdlvq dnfcqylafs fqpkgdtepy
      181 rnlfgvmpef gaaksfvild pqkvdqkllm anelvlhtae eqcrqilekr qsqnkfttlv
      241 qqqlmsmrge mpsmdivadr lhlnirtlrr hlasegmtfi qireevrqvl aeqylalpka
      301 sveqiaewlg yaepasfiha ykrwhgktph amrlvqk
//
LOCUS       WP_004837143             169 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Anaerococcus tetradius].
ACCESSION   WP_004837143
VERSION     WP_004837143.1
KEYWORDS    RefSeq.
SOURCE      Anaerococcus tetradius
  ORGANISM  Anaerococcus tetradius
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Anaerococcus.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Anaerococcus tetradius"
                     /db_xref="taxon:33036"
     Protein         1..169
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18851
     Region          3..156
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mlfdevldkr ysarsykkdm ptdeeiekll daaykapian gaygecrlsv ikdkslmerf
       61 vkeyqekthk dknplyeapl fiifssskdt saayedagcv iehiclkate mglascyirg
      121 svnalgkeas yikdldldtg fypisglivg yadgdaqikn hhiktnyiv
//
LOCUS       WP_004837688              74 aa            linear   BCT 20-JAN-2025
DEFINITION  acyl carrier protein [Anaerococcus tetradius].
ACCESSION   WP_004837688
VERSION     WP_004837688.1
KEYWORDS    RefSeq.
SOURCE      Anaerococcus tetradius
  ORGANISM  Anaerococcus tetradius
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Anaerococcus.
REFERENCE   1  (residues 1 to 74)
  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 74)
  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 74)
  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   4  (residues 1 to 74)
  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 10011594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Anaerococcus tetradius"
                     /db_xref="taxon:33036"
     Protein         1..74
                     /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=8483
     Region          1..73
                     /region_name="acpP"
                     /note="acyl carrier protein; Provisional; PRK00982"
                     /db_xref="CDD:179197"
ORIGIN      
        1 mirerlkela iehldinpee idfdskisdl didsidlvdf imvledefsi efsdeeldei
       61 etladivsli eskn
//
LOCUS       WP_004838141             170 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Anaerococcus vaginalis].
ACCESSION   WP_004838141
VERSION     WP_004838141.1
KEYWORDS    RefSeq.
SOURCE      Anaerococcus vaginalis
  ORGANISM  Anaerococcus vaginalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Anaerococcus.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Anaerococcus vaginalis"
                     /db_xref="taxon:33037"
     Protein         1..170
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19347
     Region          3..163
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdfdkvidtr vstrkyidkk ieknnlekiv dagvkapvgn slyenmaitv isnkdliqei
       61 leeareivnd pkanpiysap yliiisakeg hitrledtac iienmalkat dleigscyir
      121 gmferfdkda rfikklnlee nfypvhglil gypkeklqgk nhkiktnyid
//
LOCUS       WP_004838315             344 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter baumannii].
ACCESSION   WP_004838315
VERSION     WP_004838315.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 344)
  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 344)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 344)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 344)
  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   5  (residues 1 to 344)
  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   6  (residues 1 to 344)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..344
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38783
     Region          21..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <249..336
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtpelpgtyi nllaeivkrr gvsceqfleg sgvtpeqlkk pywyvefntl nnllehaiql
       61 thepalagyl alemkascyg svgmaamvaa nlgealkife qfigsrcdaf kpelkqeqnd
      121 vywsihqplk sfqlssdati flllgfihia khltglsalg tvqlnmpepl gfskikdklg
      181 vsclfeqkhn iwifpkeylm qpvltadpml apllkvqckk didklklrsg wkaeisqvik
      241 kllinsqgei lkvkqvaqmm nmserslqry laientsfsa lvdltrkqya qellqnslms
      301 iesvalslgy adtshftraf krwmgvtpky yqtqlklknl dise
//
LOCUS       WP_004838318             364 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Anaerococcus vaginalis].
ACCESSION   WP_004838318
VERSION     WP_004838318.1
KEYWORDS    RefSeq.
SOURCE      Anaerococcus vaginalis
  ORGANISM  Anaerococcus vaginalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Anaerococcus.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Anaerococcus vaginalis"
                     /db_xref="taxon:33037"
     Protein         1..364
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42577
     Region          1..265
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          261..344
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkllhlsdlh igksigsysl ledqkfcleq ilkiiedekv divliagdif dtaipnneam
       61 kvysdfvdei ifnlkkkima isgnhdsgkr leisksffek nsyyiygnsf dekisfddey
      121 gkvnfypipy islaraknei dsnienftdl ykvllknidy kdrnvlishc yanekpyede
      181 kiegekplti ggndamdahl fkkfdyvalg hlhrkhfvld ekirycgtfm kysfseinqk
      241 ksltlidlke kisikeieik plndfekicd yfenilkmkn snayieftlk ddkpidspma
      301 klkmkfphav sikyeksini ekdedididf eelssleife efykfkmnek mtdlekeilk
      361 kviq
//
LOCUS       WP_004839391             344 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Anaerococcus
            vaginalis].
ACCESSION   WP_004839391
VERSION     WP_004839391.1
KEYWORDS    RefSeq.
SOURCE      Anaerococcus vaginalis
  ORGANISM  Anaerococcus vaginalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Anaerococcus.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Anaerococcus vaginalis"
                     /db_xref="taxon:33037"
     Protein         1..344
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39727
     Region          2..342
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mldveikkef tnfkldakft neegilgilg asgsgksltl kaiagiikpd ygrivlndri
       61 lfdkdkkini ptkdrkvayl fqdyalfpnm tvyeniktgl rekninseki inkkleelhi
      121 ghiknsmpem isggekqraa larilvnepe illldepysa idgylrwsie levrkiieey
      181 kiptlfvshd rdeiyrmcdd ivimtkgkse akkptkelfh npetmaaael sgcknfskve
      241 kigeniykae awnldldlek nhnekfigir ghdveisknk keknsfqmei ikeidqtfnt
      301 cllirkkegk gqitvfieke kwenlkneke lyftfdeeni iflk
//
LOCUS       WP_004823184             551 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease, partial
            [Peptoniphilus indolicus].
ACCESSION   WP_004823184
VERSION     WP_004823184.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus indolicus
  ORGANISM  Peptoniphilus indolicus
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Peptoniphilus indolicus"
                     /db_xref="taxon:33030"
     Protein         1..>551
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
     Region          2..550
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mfdkrlyiel kderkyivil vliktiemil nisviftigk fidtlikgee nyiklimtil
       61 iiaiiriatt klysnigyrv sievkktlre rlikkvysfk mefgekikis eiinlgvegi
      121 eqlnifysem lpqllfslig plilfiilcf inlkialiml vlvpviplai vmvqklankv
      181 vksywhsytn ladifidfly glttlkvfnv derqnvrlnd laedfraktm kllmvqlnni
      241 tvmdlvsycg aalgimlsln aykvgkisif gafyfillsq effnplrrlg slfhvamngi
      301 saakslfdvl eieteedykn tiedrglnik ienlnfsytd klvlnnlnie fennsitaiv
      361 gksgcgkstl akvlsgslks ykgkiyfngv sdinsdslve nialidnnpy ifngslrynl
      421 kmanedakde eliqvlekvg lknyflnkeg ldtllnsdgg nlsggqkqrl slaravlksp
      481 kllildesis nidieseqli ltllqemkks mniilithrl rnaenadyiy ymedgkikee
      541 gkfkeilkek l
//
LOCUS       WP_004842494             384 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Mediterraneibacter gnavus].
ACCESSION   WP_004842494
VERSION     WP_004842494.1
KEYWORDS    RefSeq.
SOURCE      Mediterraneibacter gnavus
  ORGANISM  Mediterraneibacter gnavus
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Mediterraneibacter.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Mediterraneibacter gnavus"
                     /db_xref="taxon:33038"
     Protein         1..384
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43645
     Region          1..276
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          273..362
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrfihlsdlh igrqlhqynl kedqehilge vveyarmlrp daiviagdvy dksvpsaeav
       61 gifdwfltal salkpeipil iisgnhdsaq ridyasgilg qkgiyiagkl pqnqeeflkk
      121 vtlqdeygev dfyllpflkp gyvrtvfdge mpesyskavq mllerelvdt tkrnvivthq
      181 fytgagqnte tcdseifsvg gidnvdvtpl lrfdyaalgh lhsaqkvgre svrypgtllk
      241 ysvsecnqtk slhlvtlkek gtpvevetyp lhplrdvkkf rgtlkellkt vpeeakedyv
      301 sitltdetdp yrpkeqlekv fshilevrmd nsrtrqklmk daevvrmasp leifgdffqe
      361 mqgralnaee qqvmnkiaee meee
//
LOCUS       WP_004842586             335 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Acinetobacter baumannii].
ACCESSION   WP_004842586
VERSION     WP_004842586.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..335
                     /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=38974
     Region          2..269
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mrnlhidatk gvliflvvlg hylerligwn eplnqailgs iyfvhmpafi fisgiffkee
       61 kilekliyfl slylpfqllf qlldafyngs lwngtfqflw fakpywvlwy lfsmgiwtll
      121 afflkktahp vlfsiilall igfspinnys ysigrifvfl pffmtgaiyg ktifqyipql
      181 pyeklfavii lliitivaai shysyywlfg slsyiqlhvd lwqgvlirsv imllsamgvl
      241 slfvftqnfk qpwiglgqkt lpvyilhafv iivlthqlsf kysveinifi slvlavltcm
      301 vlqlqiferl irfislfvyk pfmklleiln pkkgl
//
LOCUS       WP_004847446             629 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase
            [Mediterraneibacter].
ACCESSION   WP_004847446
VERSION     WP_004847446.1
KEYWORDS    RefSeq.
SOURCE      Mediterraneibacter
  ORGANISM  Mediterraneibacter
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Mediterraneibacter"
                     /db_xref="taxon:2316020"
     Protein         1..629
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=72273
     Region          61..507
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mekmrfesvd gfqenirrla difpscvkeq kdndgktirk vdintlqlll ginqkesetc
       61 efswvgkrea vkevykpirk tlrpvvqdsv ewdstgnlyi egdnldvlkl lqesyldsvk
      121 viyidppynt gndfiyaddf rirareyvna ggasqddknr myqnldysgr yhsdwcsmiy
      181 arllaarnll cddgvifisi ddneqanlkk icdevfgern fvncfiwncs taggirpkfa
      241 sktheyilcy aknktcldmf faplsgeaik myrekdergl yrdkdfvfkn kstnanqkye
      301 iicpdgervr pkdgyiyrfv rerfeqakee glvtfkrtkt gplvdqngdq ahwniyikky
      361 lgdamgapst lipkeavsiy nagtqcvqel fdgkrvfenv kpvnviqyfi nmaakdgdiv
      421 mdffsgsatt ahavmqtead knidlhyilv qipqecdkks eaykagykti ceigkerirr
      481 aaekikreng cenrdfgfrv lrldesnmed vyympeeytq emlcgletni kpdrtdldll
      541 facltewgll lskpysseki ggytvhyydg kelaacfnen isetvirkia gqhprravfc
      601 dasfsdsaak inmselfrti spetqikvi
//
LOCUS       WP_004848687             309 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Coprococcus eutactus].
ACCESSION   WP_004848687
VERSION     WP_004848687.1
KEYWORDS    RefSeq.
SOURCE      Coprococcus eutactus
  ORGANISM  Coprococcus eutactus
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Coprococcus.
REFERENCE   1  (residues 1 to 309)
  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 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   3  (residues 1 to 309)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 309)
  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   5  (residues 1 to 309)
  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   6  (residues 1 to 309)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Coprococcus eutactus"
                     /db_xref="taxon:33043"
     Protein         1..309
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35423
     Region          35..112
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          136..278
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mevenhlnwt eglinaidyi ethlidgevl dqntiarqay sspdnfrkvf hlitgytige
       61 yirnrrlsla geelissnrt vtdialeygy dtpesftkaf trfhgnspsy vrnnksglhn
      121 ftrivlrvta dggsmlnyri vkinnmciag ysrvftsldt aknnvlipkf treccsqswd
      181 klmeiksnne kpnnclfgyr sndfinidkf nneiscfnyt fgrmitkqei sglnisdysi
      241 tsipdgewic fdcsdttpag qqslwykiyt eflpfshyni vpdvtlecsn vslekeqnyl
      301 llqirpdkv
//
LOCUS       WP_004853194             206 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Klebsiella].
ACCESSION   WP_004853194
VERSION     WP_004853194.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 206)
  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 206)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 206)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..206
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22140
     Region          1..204
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 melynnendq vdalkrffae ngkalavgvi lgvgalvgwr ywtshqldta rgsslayena
       61 isalksdkpe alnaaqkfaa dskntygafa slelaqqfvd kndlqnaekq lqqgltaasd
      121 dnlksvinmr larvqlqlkq pdaalktlda vkgegwtaiv adlrgeills kgdkqgakaa
      181 weagaksdas palsemmrmk innlsi
//
LOCUS       WP_004853472             142 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Klebsiella].
ACCESSION   WP_004853472
VERSION     WP_004853472.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..142
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15337
     Region          5..140
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 msdslslisl fassflsatl lpgnsevvli amllagasqp wllvliaiig nslggvtnvi
       61 lgrlfplrkt srwqekasgw lrrygaaall lswapvigdl lcllagwmri swgpvlfflc
      121 lgkalryivi aaitlqgmtw wh
//
LOCUS       WP_004854377             546 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Bartonella doshiae].
ACCESSION   WP_004854377
VERSION     WP_004854377.1
KEYWORDS    RefSeq.
SOURCE      Bartonella doshiae
  ORGANISM  Bartonella doshiae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Bartonella doshiae"
                     /db_xref="taxon:33044"
     Protein         1..546
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=62968
     Region          9..497
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mrynkqklel twigkerrpk leprisledl eksyhashqv sdrdifdnkl ifgdnllalk
       61 aleqeytgkv kciyidppyn tgnafehyed glehsiwlsl mrdrlvllhh lladdgsiwi
      121 sidddeqayl kvmmdeifgr qnfvnniiwq kkyapqndtk wlsdnhdfvm vyaknktiwr
      181 pnllprsidm daryknpdnd prglwqsdnl sakrvtpkdi yeittpsgrk vmppagaswr
      241 vskqkfskll ednriwfgtd nsgvprikrf lsevkngmvs mtiwlyeevg hnqdakkevk
      301 vfnsdnvfat pkperlieri iqlasnpgdl vldsfagsgt tgavahkmgr kwimielgeh
      361 chthiiprlk qvidgtdqgg isknvnwqgg ggfryyrlap sllqkdpwgq wiisreynaa
      421 mlsevmckhm gfsyapdenh ywmqgystet dyiyvttnam thkqlhiise evgphrtlli
      481 ccsafdtkpe sfenltltki prailekcew grddyslnva nlepmavake spkdkdtmqa
      541 eldlfr
//
LOCUS       WP_004854870             264 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Acinetobacter gerneri].
ACCESSION   WP_004854870
VERSION     WP_004854870.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter gerneri
  ORGANISM  Acinetobacter gerneri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acinetobacter gerneri"
                     /db_xref="taxon:202952"
     Protein         1..264
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29557
     Region          1..257
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 msklavnism iftevplier falahahgfs hieiqfpyel siediqaqle lynlhiclin
       61 vpagdlmhgg nglagipgre vefhqaltqa ieyatalnvp svnilagkqp ldadllpcln
      121 tlsdnlklas hmlseykiqp vfemingtdm prflvqniaq aqemleavqh galkmqfdcy
      181 hmammgedvl aalkeniewi ghiqfadcpg rhepdtaqid faeifkwlqd ssyhgyiaae
      241 ykpqshsnqs fawkdkyftn nlsi
//
LOCUS       WP_004838626             195 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Anaerococcus vaginalis].
ACCESSION   WP_004838626
VERSION     WP_004838626.1
KEYWORDS    RefSeq.
SOURCE      Anaerococcus vaginalis
  ORGANISM  Anaerococcus vaginalis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Anaerococcus.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Anaerococcus vaginalis"
                     /db_xref="taxon:33037"
     Protein         1..195
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=22944
     Region          8..194
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mntlkeyiqe nlvitnkeae elgytrhnls eltkigqler lrpglyqikg kviddfilis
       61 snsnriifsh qtalylhdls drtpnvfhis vpqgynashi kkryedlqvh yvkkdlyeig
      121 kteikspqgn lipvydiert vcdiiidrek idkqifteai kryfkspnkn lrrlikygrl
      181 fkiedeirky mevls
//
LOCUS       WP_004854999             405 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Acinetobacter gerneri].
ACCESSION   WP_004854999
VERSION     WP_004854999.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter gerneri
  ORGANISM  Acinetobacter gerneri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 405)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Acinetobacter gerneri"
                     /db_xref="taxon:202952"
     Protein         1..405
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43776
     Region          5..387
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mstsvlvinc gsssikyalv serredrifg laenlgsada rikgittggq plelsiphad
       61 hekaletilg rlahhkpkai ghrvvhggtl tkaelltpei verireatpl aplhnpahlv
      121 gidatmrlfp elpqvavfdt afhqtmpaha yryalpkfly tehnvrrygf hgtshayvse
      181 rgselagsyk qggwltahlg ngsstcaiwn gqsvdtsmgl tplegvvmgt rsgdvdpsih
      241 sflasnlgwd iykidkmlns qsgllglsdl sndmrtliea seqgnddatl aievfcyrla
      301 kslaalscgl pridglfftg gigensayir ektlaylphf gfnlsleann elkrgtegri
      361 dsgvgpqiwv vptdeegria ketehvvdqe asahtkksed daala
//
LOCUS       WP_004855963             146 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Bartonella doshiae].
ACCESSION   WP_004855963
VERSION     WP_004855963.1
KEYWORDS    RefSeq.
SOURCE      Bartonella doshiae
  ORGANISM  Bartonella doshiae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Bartonella doshiae"
                     /db_xref="taxon:33044"
     Protein         1..146
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=15863
     Region          58..132
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mrkiafttli svlmasstya qslavpfese kisstgvvqv gkdmfaryvt platdfvass
       61 ligasvynie nenigevrdi ilrennmagi viavggflgi gesyvvvspe ttqmindygk
      121 wkiiinatkd slkeaptfky egrwar
//
LOCUS       WP_004859989             546 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Bartonella taylorii].
ACCESSION   WP_004859989
VERSION     WP_004859989.1
KEYWORDS    RefSeq.
SOURCE      Bartonella taylorii
  ORGANISM  Bartonella taylorii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Bartonella taylorii"
                     /db_xref="taxon:33046"
     Protein         1..546
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=62811
     Region          9..487
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mrynkqklel twigkerrpk leprilledp eksyhashqv sdqdifdnkl ifgdnllalk
       61 alereytgkv kcvyidppyn tgnvfehyed glehsiwlsl mrdrlellhh llaedgsiwi
      121 nlddseshya kvmcdeifgr knfvanviwq kkhtrsndsr wlsdnhdhil iftknkdswt
      181 rnllpradnn sksytnpdnd prgvwasgpc hvktpnlkdi yeiitpsgrk vmppagtswr
      241 fskkkmkeli tdnriyfgqd gnniprykrf rtevqdglvp itvwlkeevg hnqdakkevk
      301 qfnpenvfst pkperlveri ltistnpgdl vldsfagsgt tgavahkmgr kwimvelgeh
      361 chthiiprlk qvidgtdqgg iskninwqgg ggfryyrlap sllqqdpwgq wiisreynaa
      421 mlseamckhm gftyapdenh ywmqgystet dyiyvttnam theqlrvise evgsqrtlli
      481 ccsafdtkse sfenltltki pravlekcew grddyslnva nlepmavvke spkdkdtaqa
      541 eldlfg
//
LOCUS       WP_004861044             344 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter gerneri].
ACCESSION   WP_004861044
VERSION     WP_004861044.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter gerneri
  ORGANISM  Acinetobacter gerneri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 344)
  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 344)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 344)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 344)
  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   5  (residues 1 to 344)
  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   6  (residues 1 to 344)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Acinetobacter gerneri"
                     /db_xref="taxon:202952"
     Protein         1..344
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40038
     Region          28..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          127..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mklaveskgt isvallheal lqidqskldm qhilrsvgis peilnstkar iavsnyaalw
       61 ialadqlnde ffamdrhplr rgtfqllsrf vihaqnlqqa lqqilqffna vfddlkselc
      121 ienemayiim hdhdqpkrmf hyatylmlih glicwltgqr iplnqihvrc papiddqdyr
      181 vrfcekihyl snensvqfda sylsilikqd qstwyqfikn tpqnllvrfk nphassaivr
      241 killenghly wlelheiakq mhiseitlqr rlkseglnyq qlknelrcdi aieyltqsny
      301 siaeisqklh fndssafyra fkkwtgvnps ayrvdhende pvii
//
LOCUS       WP_004862908             202 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Bartonella vinsonii].
ACCESSION   WP_004862908
VERSION     WP_004862908.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..202
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22979
     Region          2..166
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 milnrlklwt islanrrtap hwlgfiafie ssvfpipidv lyipmllvhp krvyryafia
       61 ticsvlggia gwfighfayd tlakpilefy gqienfhalk nsatlqflii llitsgflhl
      121 ppikivtila gvigvhleif ivtcilarga rfyllawliq rfgqqamnfm vrhfkwivfm
      181 gcvtllvvyg vfiafvnkhl lf
//
LOCUS       WP_004864055             353 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Acinetobacter gerneri].
ACCESSION   WP_004864055
VERSION     WP_004864055.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter gerneri
  ORGANISM  Acinetobacter gerneri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Acinetobacter gerneri"
                     /db_xref="taxon:202952"
     Protein         1..353
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39573
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvkniek hfgafhalnn itldfpdgql vallgpsgcg kttllriiag lesadhgqil
       61 legndatnth vrerqvgfvf qhyalfrhmt vydnvafglr vrpratrpse aeikkrvtrl
      121 ldlvqlgfla drypaqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 tlhdelhits ifvthdqeea levadqiivm nkgnieqigs prevyekpat pfvfdflgqa
      241 nrfegvnhqg vvqigadrie lpsnrntpdg kviafvrpne lkihsepven aiqatflrev
      301 wiagkvvael qdregqliei nlspeqvklh qfrpnqtvwi saatlhlfan qva
//
LOCUS       WP_004864876             286 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Bartonella vinsonii].
ACCESSION   WP_004864876
VERSION     WP_004864876.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..286
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32642
     Region          1..278
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mkaslpycfd ilratdrdry isvlfapkkk rralaalyaf ngeiariret vhdpligemr
       61 lrwwydsivd dkiqnsqnnp ilsdlltait lfnlpkrafl rycdaqildl yhnpittlhd
      121 lefycgetas iilqlscqil dpdaaqdfkd iykyggiaqg lsgilrllsf mqsryhyylp
      181 tdvlkavgve redleshsvn dqqkcrivea mvavsrdhys kfyeasrtfp knvkpaflpl
      241 aiipaslqka eqlgakvfqe satlplihry wliaraaisg hfpkll
//
LOCUS       WP_004867468             233 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Acinetobacter gerneri].
ACCESSION   WP_004867468
VERSION     WP_004867468.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter gerneri
  ORGANISM  Acinetobacter gerneri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 233)
  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 233)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 233)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Acinetobacter gerneri"
                     /db_xref="taxon:202952"
     Protein         1..233
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=25352
     Region          4..211
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 mssltdteql dnaksfakky gssiitgili aliaffgwqy wqkrgagkeq khtaqvqqlm
       61 ddarsagtda nafnslsata nkitekspds vhaiqsqfvi aklaydkgdy aaaenalkkv
      121 anssikdegl lslvkirlad aelaqnknda alktlaevtd pafkatveea kgdayvaknd
      181 ienakkayqs awnavlerkq drqilqikle svgilvddpd ferpviqtqv des
//
LOCUS       WP_004867473             264 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Acinetobacter gerneri].
ACCESSION   WP_004867473
VERSION     WP_004867473.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter gerneri
  ORGANISM  Acinetobacter gerneri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   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 264)
  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 264)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acinetobacter gerneri"
                     /db_xref="taxon:202952"
     Protein         1..264
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28845
     Region          24..91
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          192..253
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mevnpnsqqs tgssvapnal gnvqrpgeyl rqirvsqnrd iesvakdlki qlktlnaleq
       61 ddykalpeat fikgyyrsya kylnvdanil iqrfdeiyqn dtgllpnhal nnspikimgk
      121 lpgsnsernr kwvkrglial avlvilflvv tgiqkwsakk saatdakpqq sdvqvmamnd
      181 ggasseagdq lvlnfnqpts vkivdgtgkv latgrqdstl tlhgsspfqi rlddakavsl
      241 slnneqisls pytvngkaef rlsr
//
LOCUS       WP_004867732             444 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Acidithiobacillus
            caldus].
ACCESSION   WP_004867732
VERSION     WP_004867732.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus caldus
  ORGANISM  Acidithiobacillus caldus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 444)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 444)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Acidithiobacillus caldus"
                     /db_xref="taxon:33059"
     Protein         1..444
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48570
     Region          4..408
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 msdarvlqvc igdpaievgt lwlssaggrn fsafqysaaw lrhprafals pdlplssekw
       61 ffhgdpqvah gsslppplad tipdawgrgl lrkarglsrd pdeftlltdv ddgsrlgalr
      121 lresesgpfl avaqdgagrv pplvdlnslv tdihrieaah pdrevlqrll gssaslggar
      181 pkctvrkpng dlalakftsr fdthpvekae vlalrlaqac giavpraelv ftqntavavl
      241 drfdrdgprr ipylsaqsfl glssavggty vdfaeqlrrf sgdvprdlre lfarvsftil
      301 vsnaddhlkn hgllyrgagg wrlspmfdvn paperdrrlk taildprdtr aslgllleaa
      361 effeleqdta rslvvdqaer iaglwrdvar rcgmttseir eyepafthee safarslgrt
      421 qasaagisep dprapapqkr qrke
//
LOCUS       WP_004869263             302 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Acidithiobacillus].
ACCESSION   WP_004869263
VERSION     WP_004869263.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus
  ORGANISM  Acidithiobacillus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Acidithiobacillus"
                     /db_xref="taxon:119977"
     Protein         1..302
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33763
     Region          24..268
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 metpqdtvre lgeaevvwpl gailgegplw sprqeavyfv dilgqkiaaf wpasgtgrfw
       61 eldepctwlv gyaddtcfla glrrqivtlr lgergvhlqr rfphpegepv snrfndakad
      121 pwgrvwagtm ddqeknptga lyrisgksma rvdapyivsn gpaftvdght lyhsdsalrr
      181 ifafdlsarg eirdkrlhiq fteldgypdg mtgdtdgglw vahfgagkvt rfdskgratd
      241 cvrlptpqvt svcfggaghr dlyittaard rrddpraghl yrltvpyrgl phhpyrrhpr
      301 hd
//
LOCUS       WP_004869956             337 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter gerneri].
ACCESSION   WP_004869956
VERSION     WP_004869956.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter gerneri
  ORGANISM  Acinetobacter gerneri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 337)
  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   6  (residues 1 to 337)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Acinetobacter gerneri"
                     /db_xref="taxon:202952"
     Protein         1..337
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39257
     Region          <62..202
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          92..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mislkdytgs vygglghllf afcqakglvi skklqqvqnl erfdystwre iltdidqqyq
       61 rpalgleiae yvepkhlgii ayiamscdsi gealnryydf hrliydgspl kvennqqyls
      121 irwedlpvel ttqvtneiai almvqflkrf lgfldiqlhe vhfshaapkd vmiyeryfkc
      181 kvrfsqarte lffpsselnk piqqgdqtlq lllkqqaqal leklpnttql derlqqailk
      241 glqtnhyqie aiadvlnmsv rrlqkhlqsq nstyqqrtqe vrlllakqyl ddphlslkei
      301 alllcyseqs afqrafklwt gmtpqqwrqd hshyikn
//
LOCUS       WP_004870839             298 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Klebsiella].
ACCESSION   WP_004870839
VERSION     WP_004870839.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..298
                     /product="formate/nitrite transporter family protein"
                     /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=32812
     Region          33..285
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mkpqthhdse dvevesdekq ngeeievdee rlpsqamath evirqegeke lerdamallw
       61 saiaaglsmg aslvakgifh vhlselpggf llenlgytfg fvivilarqq lftentvtav
      121 lpimhkptlg niglllrlwg vvlagnligt aiaawafdvm pvfdeptrea flkislkvmq
      181 npplemfana iisgwlvatm vwmfpaagsa kiiviilmtw lialadtthi vvgsveifyl
      241 vfngalpwqe fiwpfalptl agnicggtfi fallshaqir ndmshekkar aaeernkr
//
LOCUS       WP_004872265             199 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase
            [Acidithiobacillus].
ACCESSION   WP_004872265
VERSION     WP_004872265.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus
  ORGANISM  Acidithiobacillus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Acidithiobacillus"
                     /db_xref="taxon:119977"
     Protein         1..199
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21342
     Region          3..198
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 marrigvait gasgapyaqr llqrllaadc dvavvfsaaa rivwreelgq elptpmealt
       61 eslraglprt gtlrcyderd wfsplasgsh apealvicpc sggtlaavaq glsnnlaera
      121 advmlkegrk lilvprespi saihlenmlk larlgvtilp aspgfytrpq sidelldfvv
      181 arildqldlg rdfgpqwgl
//
LOCUS       WP_004873005             664 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Acidithiobacillus caldus].
ACCESSION   WP_004873005
VERSION     WP_004873005.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus caldus
  ORGANISM  Acidithiobacillus caldus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 664)
  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   3  (residues 1 to 664)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Acidithiobacillus caldus"
                     /db_xref="taxon:33059"
     Protein         1..664
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=71942
     Region          1..652
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msmdpdilrd yvsearelle qaqsdalale capdsdavla slfrafhtlk ggagfldada
       61 lvewthhled lldklrshvl pvtpttidvi lkgldviqcm ldelgrgvyp npgpsdlgqr
      121 icalasvedv htsppesase nvrpiaeqpt gvesaesgtl qawqklkpdg kvgvyvervs
      181 egkdkgavcv esaskagdda asdtisdeef eqvldalygh kapgvvppae rrvmdsqvas
      241 tavlpgalpq atapapvtsv aavkterpss tsetpestlr vesarldsvm nqvgelvllr
      301 nrflsamqtt igehedlari aremdltvnd mqstvmrlrm qpckrlfqql prvvrdvsrq
      361 lgkrvnlqfv gedveidkkv vdalsaplih lvrnsldhgi etpadrvmlg kneiatlris
      421 avhlgdkvri evsddgngid aqqvkqkave kgligqeeaa rltesdaidl ifrpgfstnd
      481 vvteysgrgv gmdvvkkttq slrgrldvht nlgtgttiam efpltlavlp vlylrlrrdv
      541 yaipissvss lidvdpqrly qvqgralyqa gpeqivpfvd lgeilhqrpi qlgteptdgi
      601 ltergllvvs evlgnedsvv kpidflsesh wyqgatlsgk gevvlildia nlkhsqaepk
      661 rgva
//
LOCUS       WP_004876603             415 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Acinetobacter
            venetianus].
ACCESSION   WP_004876603
VERSION     WP_004876603.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter venetianus
  ORGANISM  Acinetobacter venetianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 415)
  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 415)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Acinetobacter venetianus"
                     /db_xref="taxon:52133"
     Protein         1..415
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=48321
     Region          9..395
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mlinqnhilq qlrnitlaaq glhqksafgt gkaaviqtlt qlgyvqidtl smvarahhht
       61 fwtripdyqp qwldqlvaeg qifeywfhaa sylpiqdfry alpkmhsikn resryyqada
      121 qvmrhvydri riegaqkard feslskkqgs wwnwkptkma leqlfmqgdl misarngiek
      181 vydlservlp nhinttcpdp leyaeylvkt ylraygftti kqithlktep tlrknivlvl
      241 qhmleegviq klniaefpti yvvtglqdqi entphnnlsl lspfdnaiih rerikthfdf
      301 dfrlecyvpq akrkygyfcl pilfgdifig rvdckahrkn grfelihlhi entqidmssw
      361 lpsffdtlqr faqfnqcqsi eitqisppal ssvvrqflki gweeisfkgd altak
//
LOCUS       WP_004877320             464 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Yersinia
            mollaretii].
ACCESSION   WP_004877320
VERSION     WP_004877320.1
KEYWORDS    RefSeq.
SOURCE      Yersinia mollaretii
  ORGANISM  Yersinia mollaretii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 464)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 464)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Yersinia mollaretii"
                     /db_xref="taxon:33060"
     Protein         1..464
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=52617
     Region          26..379
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 makltiqifn dgfwhdaael vfadpergrq gsavlgydgd ysvdwmyrdd efscsinfpi
       61 elaytysskq wfaflddimp agasrrywin qlglqsmsas eqdyillkng tiapvgnmri
      121 kealpelhpd sqlmnirftl qdvierdssf leyaqqmgaa aggatgagge apklllccsn
      181 hdeiwidtfq ndidnpdthy lvkfprgkrt pidcdilrae yyfyqelasi gintintint
      241 intintinti ntekmklleg ehypslwlpr fdidfienkr vqyglesiys vmnaasgshl
      301 nhfdvirrls rklvsqyrvr elgqplnvea lviemvqrdl lnvafgnsdn hgrntalikr
      361 pegiwlspiy dfapmkadpe givrvtqwgs pyeeggnfnw qaiiaelsdl adpthvflaf
      421 qqtaqkligl kprlktrgvp dsilnmpgma fdyldeklkr waql
//
LOCUS       WP_004877396             232 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Acinetobacter].
ACCESSION   WP_004877396
VERSION     WP_004877396.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 232)
  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 232)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 232)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..232
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=25659
     Region          3..210
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Site            order(101..102,104,128,135..136,139..140,142..143,165,
                     168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          126..159
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          164..190
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mslsdeeqld qlksfakkyg saiisgilia liaffgweyw qkknlteaqs qtakvqklmd
       61 eakaassqpn afatlseaad kivkedpdsv qaiqtqfila kvaydkqdya aaekalkkve
      121 nskikdagll qivklrlada qlaqkkydda lktltavtep sfkatadelr gdiyvakkdn
      181 esarkayqsa wddlvkrkqe rqllqikles vgvlvddpei dspivdtkvd es
//
LOCUS       WP_004877504             393 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Acinetobacter venetianus].
ACCESSION   WP_004877504
VERSION     WP_004877504.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter venetianus
  ORGANISM  Acinetobacter venetianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Acinetobacter venetianus"
                     /db_xref="taxon:52133"
     Protein         1..393
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42318
     Region          5..388
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 maksvlvinc gsssikyali serredriyg laenlgsada rikgvtvgge plelsiphad
       61 hakaletlla rlanynpqai ghrvvhggnl tkaelltpei vkrieaatpl aplhnpahlv
      121 gieatmrlfp elpqvavfdt afhqtmpeya yryalpqnly tehhvrrygf hgtshayvte
      181 raselagakn qggwlsahlg ngsstcavwn gqsidtsmgm tplegvvmgt rsgdvdpslh
      241 lflasnlgwd iqkidnmlnk esgllglsgl sndmrtlvda sndghegatl aievfcyrla
      301 kslsalscgl prldglvftg gigensayvr ektlgylshf glqfskeknd alprgtegri
      361 dagqgpqiwv vptdeegria ketrqvveqt vsa
//
LOCUS       WP_004878274             105 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Acinetobacter].
ACCESSION   WP_004878274
VERSION     WP_004878274.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..105
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11753
     Region          2..105
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(7..8,26..27,35,38,40..41,43,46..47,49,57,62,69)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(26,57..58,60,87)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mkdsnelhrq ilevialipy gkvatygqia klagipkhar lvgyvlkhld qessipwhrv
       61 insqgkisvm rinekggniq qqlladegiy llnnkinlkv fswip
//
LOCUS       WP_004877950             335 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter venetianus].
ACCESSION   WP_004877950
VERSION     WP_004877950.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter venetianus
  ORGANISM  Acinetobacter venetianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 335)
  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 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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 335)
  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   5  (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   6  (residues 1 to 335)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter venetianus"
                     /db_xref="taxon:52133"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38820
     Region          51..193
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          82..328
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msqlknytgs vfgglghllk ayceakkiei peqlqqvqnl erfdyviwrd lledlnamhp
       61 ktglgleiae yvqpkhlgii aylalscenl gealaryhdf hrliydgspl ivefnppyvs
      121 irweapephp tqltdeiaia lmvqflklfm sgesihlhev hfvntapkni aiyeqyfhcr
      181 vrfeqpktql llpvseafkp lrtgdhtlqq lllkqaqall eqlpnstqld qrlqhsiltg
      241 lqknqyqidf iaeklglsvr qlqrhlqqqn ttfqervqqi rfmlateylk dphlslqeia
      301 lllcyseqsa fqrafkiwtg qtpqqwrkdn ttyns
//
LOCUS       WP_004878417             347 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter venetianus].
ACCESSION   WP_004878417
VERSION     WP_004878417.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter venetianus
  ORGANISM  Acinetobacter venetianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 347)
  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 347)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 347)
  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   4  (residues 1 to 347)
  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 347)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Acinetobacter venetianus"
                     /db_xref="taxon:52133"
     Protein         1..347
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39659
     Region          37..212
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          266..340
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpkqiihaes tqqfipatil aslihyaeqq ewdykkwfed sgldldqvqq sngfvrfsqm
       61 cdvirkaita ygqpdlglkm grseglismg ilgfamqsck tvadaleial efhrvsgsvl
      121 niefsihddi ctlevtessp tfdlkaffyd elfssviacl namlgdhddv iglelnyapt
      181 anledyqylf gcpvqlntts nkihfkssml nrnlknyspa nyataiqick qalkeidqln
      241 qvdfvhiveh lieqylperf emrqaadhlq mserhlrrkl lseglsfqqi rqnalerkak
      301 qlleknlsms eislqlgfse lrefrrafkr wtgqapsvyk qiceish
//
LOCUS       WP_004878514             356 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Acinetobacter venetianus].
ACCESSION   WP_004878514
VERSION     WP_004878514.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter venetianus
  ORGANISM  Acinetobacter venetianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Acinetobacter venetianus"
                     /db_xref="taxon:52133"
     Protein         1..356
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39945
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvkniek hfgafhalkn isldfpegel vallgpsgcg kttllriiag lesadggqvl
       61 legedatdih vrerqvgfvf qhyalfrhmt vfdniafglr vrpratrpse aeikkrvtrl
      121 ldlvqlgfla drypaqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 tlhdelhits ifvthdqeea levadqiivm nkgdveqigs prevyekpat pfvfdflgqa
      241 nrfegehsng iihidenriq lpntveapqg kviafarpne lhihtqphnn tieatflrev
      301 wiagkviael qdrsgrtiei llsveeanvh qfkpnqtvwi satqlhlfad qttqva
//
LOCUS       WP_004879327             759 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor family protein [Pseudomonas
            syringae group].
ACCESSION   WP_004879327
VERSION     WP_004879327.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 759)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..759
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=82696
     Region          33..759
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mnvkpmlnwq rlpaaclkia lilpifqvsh vkadavdtaq epgatattlg tvsvigqget
       61 rqvhrvteqd tkayaagsnp mkvlqrlpgv nfqssdplgr elgsqrislr gfdmhhlgyt
      121 ldgvtlgdms fgnfngltin raiipenias tevaegtgal gtasnsdlgg tlqftsanpd
      181 qtpglrlsqt lgsydttrtf lradtgqykg laayvaaeny danawkgdsp qrsnalnakv
      241 tydvdghhls fyhsrseyke stipslsksq idrlgynwtn yapdwqravn aangkfsggv
      301 tsvsdalyns snlrndeldi lsgtftlsda lildttvyhh hdsgagnsyy pfvytsgstt
      361 vpsnsirstf ygidrtgfqs alsyyvgehv vqagvwiqsn knsadrylfd ttgaapqsgi
      421 vevtglplaa tiqsqdyndl trqfyvrdtw tllddrlkle ygakhvvths tvkgsgtsas
      481 gslqakdnfl pqigatykln eqdeifasya qnmaafpsgt ssplytsqtt lnalngfkdl
      541 kpetsktvel gmrrstplya asaalygtrf dnrllaianc tgivicqngv anvgavssrg
      601 velslaltpd pnwrwsntmt ynrslyedny ssngtvvavk gkdvidaprw mlsssldwqw
      661 drwnagvqtn ymdkryytyt ndssvdaywv tnanmgydfg rfgdlkdttl slnlvnlfdr
      721 ryistintds saatdpagnl qilkvgsprs afvtlstrl
//
LOCUS       WP_004879696             291 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter venetianus].
ACCESSION   WP_004879696
VERSION     WP_004879696.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter venetianus
  ORGANISM  Acinetobacter venetianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 291)
  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 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   3  (residues 1 to 291)
  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   4  (residues 1 to 291)
  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 291)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Acinetobacter venetianus"
                     /db_xref="taxon:52133"
     Protein         1..291
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32752
     Region          24..175
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          202..283
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mmnqqqlisl flklvrkegf fataidgitl mrvdhntppi svlqeptlvf vlqgkkrgyi
       61 aketysfgqg eclivsvsmp fdcdtiasse qpmiavsmkl dadtvnella ktyfenyqft
      121 plttgmsviq ydetissvll rllntltseq dililgdqik rellyrviqh sgadalkglv
      181 vqgnlrpiyk iceyiqhhft ekltvemlae qanmstsafh kafkqvtqhs plqylkvvrl
      241 hkakqllqna dqsvaqaaya vgyqsssqfs refkkqfgfp pnqaevnidk e
//
LOCUS       WP_004880044             694 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Pseudomonas syringae group].
ACCESSION   WP_004880044
VERSION     WP_004880044.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 694)
  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   3  (residues 1 to 694)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..694
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=75108
     Region          3..684
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msinldqaqq tfivearell lameesllql esepgdqdai gavfraahti kgsaglfglt
       61 pivsfthive dvldrlregs vsvdaeliav llksgdhmle lievvasrge qlqaaalere
      121 aalrqalqay qapaqaaaqp vqtetvsdiq aerlwhislr fgvdvfrngm dplsflryln
      181 tlgqmvqvtt vtdsiptvee wdpeschlgf eidfrsaagy aainevfdfv redcaveita
      241 ldetaestgt dlvsqddtsp vihsgellgd qravprgpaq vsterassan eqknkdgryv
      301 rvnadkldel inlvgelvia saganllars cnnaplqeas stvsglveei ldgalhlrmi
      361 pigdtfnrfr rvvrdvsqel gkdidliisg aeteldktvv ekigdplmhl lrnamdhgie
      421 saearrasgk sakghlslna yhdsgsivie iaddgaglnr erilekaqer glvasgavlt
      481 dqeiynlife pgfstaeavt nlsgrgvgmd vvkrnitllr gtvdldsqpg qgtivrirlp
      541 ltlaiingfl vgidqstyvi pldmvqecie ldeqdrqssr dngyldlrge vlplvylrdh
      601 fnhegpvarr qnvvvvryae hkaglvvddl lgefqtvikp lgklfgglrg isgstilgsg
      661 avalildipa llnqivqlea rstqtpysls aaar
//
LOCUS       WP_004880065             339 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter venetianus].
ACCESSION   WP_004880065
VERSION     WP_004880065.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter venetianus
  ORGANISM  Acinetobacter venetianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 339)
  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 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 339)
  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   4  (residues 1 to 339)
  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 339)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Acinetobacter venetianus"
                     /db_xref="taxon:52133"
     Protein         1..339
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39294
     Region          29..220
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          264..339
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mslprhhkhh fisssyahll sevvaqwdis vetlfwgtgv eidklndlsy kislasfkkv
       61 iertieltqe egigfyagtq ikisshgllg ftvaisknay daiqtinqfv slqcsfvefd
      121 fkieqhlayy tiiydpslln ftdvsdtrsy efsciffltg fvhlvrffip dfkpsidlqc
      181 kyppyfsrfn kilnttfeei ryeqphtrli apaefldrpl smsdpltsek fkllcqkeld
      241 elvatqdily rvkrliddpt egllsidqva qklnltkrtl qrmlqekavs fqslyddvrk
      301 qkarklllnp litkeevakk lgysstssfn raykrwene
//
LOCUS       WP_004882795             330 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas
            syringae group].
ACCESSION   WP_004882795
VERSION     WP_004882795.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 330)
  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 330)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..330
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36931
     Region          22..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          243..325
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpepsslasw trslrkqlda lglnsddfck aagidtqrln dpeasfaasa taklwqlavq
       61 asgdpalglr vsrfvsptsf halgytlvas gslrevferi vryhsmaeds leldfraage
      121 ryefrftapt saqlpthell dafaaiyvrt crnrlgrnya plaihlqrpq penpqpwhel
      181 fraplffsas enrlefaced fdshldenpi vlteqvpsae plpsliweqr vrsaietllp
      241 dgepsaesia ealhltprsl qrhladegcr ydlllnqcrq nlalmhmsdp hsslsevayl
      301 lgfadtdsls rafkrwtgmt pgqyrsdlmr
//
LOCUS       WP_004880791             750 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Pseudomonas syringae group].
ACCESSION   WP_004880791
VERSION     WP_004880791.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 750)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 750)
  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   3  (residues 1 to 750)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..750
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..750
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79464
     Region          6..749
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msfgadeeil qdflveagei leqlseqlve lesrpddadl lnaifrgfht vkggagflql
       61 helvecchia envfdilrkg errvdselmd vvlealdtvn smfgqvrert dltpatpell
      121 aalsrlaepq sndavaepva evaevaapva eaaggdditd hefeqlldsl hgskpiaapa
      181 aapaaqasss deitdqefes lldqlhgkgk faadaapapa paakaggsap asdeitddef
      241 ealldqlhgk gsfdaavvap vaaeavaaka pvtakaaasd eitdhefenl ldelhgkgkf
      301 epeaivakap apaaaaapap aakpaaapap aakaepaqak aaapaparap aptgekpvat
      361 eaettvrvdt arldeimnmv gelvlvrnrl vrlglnsgde amskavsnld vvtadlqtav
      421 mktrmqpikk vfgrfprlvr dlarqlkkei ilelvgeetd ldknlveala dplvhlvrna
      481 vdhgietpee reatgksrgg kvilaaeqeg dhillsisdd gkgmdpnvlr siavkrgvmd
      541 kdaadrlsdt dcynlifapg fstkteisdv sgrgvgmdvv ktkisqlngs iniystkgqg
      601 skivikvplt laimptlmvm lgnqafafpl vnvneifhld lsttnvvdgq evvivrdkal
      661 plfylkrwlv ssaaheeqre ghvvilsvgt qrigfvvdql vgqeevvikp lgkmlqgtpg
      721 msgatitgdg rialildvps mlkryaarri
//
LOCUS       WP_004883387             335 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Acinetobacter].
ACCESSION   WP_004883387
VERSION     WP_004883387.1
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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..335
                     /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=38721
     Region          2..269
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mrnlhidatk giliflvvlg hylerligwn eplnqailgs iyfvhmpafi fisgmffkee
       61 kilekliyfl slylpfqilf qlfdafyngs lwtgtfhlvw fakpywalwy lfgmgawtvl
      121 afflkktayp vlfsivlall vgcspinnys ysigrifvfl pffmagviyg ktifqyipql
      181 pyaklfavii lfiitavaai shysyywlfg slsyfqlhvd lwqgilirsv imllsamgvl
      241 slfvltqnfk qpwsglgqkt lpvyilhgfv iivlthqlsf kysveinifi slvlailtcm
      301 vlqlqiferl irfislfvyk pfmtlleiln pkkgl
//
LOCUS       WP_004883404             336 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004883404
VERSION     WP_004883404.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 336)
  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   6  (residues 1 to 336)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..336
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38145
     Region          22..202
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <137..336
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mgqltdasvv lrfgyqairr aglpteeilt kagvalnqvd tnartplsaq yafwtaaqev
       61 skdpdiglhl gehlplyrgq viehlfisse tfgeglkral ayqrlisdaf daklvvedgr
      121 cyltngeqig adnlvnrhfs ecaisgvlrf fkfitegqfh pifidfnfse gasedeyfrv
      181 ygcpvslgqk etrlyfdpai ldfqlwqaep ellqlheqla ieklqelary dlvgevrrai
      241 gstlesgett letvaaqlni tprrlrtqls eantsfqqil sdyrcrlakk llantsesve
      301 rivyltgfse pstfyrafkr wtnetpveyr krkqhr
//
LOCUS       WP_004884306             287 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Pseudomonas].
ACCESSION   WP_004884306
VERSION     WP_004884306.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..287
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30976
     Region          1..278
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mnvdlhchst asdgalspta lvtrayengv rvlsltdhdt legleearet ahslgmqlvn
       61 gvelsctwgg atihilgyaf dtkapaltea iarlhegrwl raeeisrkla ikgmpgaleg
      121 araiqkelgd sgnaparphf adflvregfv kdraeafrkw lgagklgdvk qhwptledtv
      181 atlrasgawv slahpshydf trskrrklvg dfiqagghai evvngmqpad qvgtlailar
      241 efgllvtags dfhgpgawge igiyrpvped lpplwcrfkh dqptaav
//
LOCUS       WP_004884685             160 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Acinetobacter].
ACCESSION   WP_004884685
VERSION     WP_004884685.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..160
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=17368
     Region          3..117
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mskyynlkfn rgftlielmv tlltlailva iavpsyqsya rratasaaks eilklaerle
       61 qhksrnftyr gftttsvtlt rggytiqitd dttagnllts saangqtwvi ratttdsrnl
      121 nfiaknsglr cqsltatavd ndcggtttcn tceanseswq
//
LOCUS       WP_004885315             349 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004885315
VERSION     WP_004885315.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 349)
  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 349)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 349)
  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   4  (residues 1 to 349)
  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 349)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..349
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39877
     Region          47..210
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          257..332
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqeftisngy fylwntylke kgiawqslnl ndtqtrqiqn ilsasidaqs slhlftelle
       61 ltesqlqvsn lalemaacit panfgvlgym asrsdtlgqv vkyiakfhrl vidgeqvvpi
      121 qieqdaskir lywplvddsn ivlseltlaa mvqlakeiap lhdfllqhve fvhrprgplv
      181 lyqrffqckl sfdrpyyalt faseslnvrp qhadptlvql lvkqaeealv qrkihtdlvq
      241 qihwivqeyl khkqqapkie diaielnvsv rslqrqlqal ntsfklildt ermkrceill
      301 sqnesltaia dqlgysdqsa larahknltg qtlltrkkql qlthkntek
//
LOCUS       WP_004887838             343 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004887838
VERSION     WP_004887838.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 343)
  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 343)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 343)
  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   4  (residues 1 to 343)
  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 343)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..343
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38598
     Region          30..213
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          258..338
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mlefqdylra pssvqlllel gdqlniqrth llagtgltlt rlndtnsvvt pdeelgvinn
       61 likilsahta glglitgfnh qlttygilgy almssatgle amqlvqryla ltytfvkinf
      121 qqknkecmic ftepvgltqe lqrfvleram aatlrvisdi yegsfqldaf hlkygepesc
      181 llnipkeylg apiqfnqken ilkfnssqll htlphakpnt aamcerlcme lisqrhttlt
      241 ttmivrdflm napsgtllni keisnklnms ertlkrrlqd enisfralqn etlhrradsl
      301 laqnlnlgqv aeilgfsdls tfsqaykrwt gvapshykkq mik
//
LOCUS       WP_004889011             161 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Anoxybacillus flavithermus].
ACCESSION   WP_004889011
VERSION     WP_004889011.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacillus flavithermus
  ORGANISM  Anoxybacillus flavithermus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Anoxybacillus.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 161)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Anoxybacillus flavithermus"
                     /db_xref="taxon:33934"
     Protein         1..161
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17793
     Region          8..160
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfhtqtytgt reenytlvie qlkalisdkk nvvanlanas allnyflhdi nwvgfyiaeg
       61 nelvlgpfqg lpacvripfg kgvcgtaaae krtvrvadvh tfpghiacda asqseivvpm
      121 ikdghvigvl didspiknrf deideqylqr fvetlvryld i
//
LOCUS       WP_004889809             219 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Anoxybacillus].
ACCESSION   WP_004889809
VERSION     WP_004889809.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacillus
  ORGANISM  Anoxybacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 219)
  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   3  (residues 1 to 219)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Anoxybacillus"
                     /db_xref="taxon:150247"
     Protein         1..219
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25043
     Region          10..215
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mvkigvpltl elkysehmek ykckvaeied gkiyidypid mstnrtafll dgtqlkvsfv
       61 gedeavyafe aevlgrtkrn ipllilsypg dnqllriqrr qfvrvdaivd vaihplqnef
      121 vpfttvtsdi saggaaivlp hhetgikhgm tieiwlvlhm rsgdyhylhf parvvrifee
      181 nvvkaslefl evndvdrltl irysfekqle lrkkeqlda
//
LOCUS       WP_004892238             353 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Acinetobacter].
ACCESSION   WP_004892238
VERSION     WP_004892238.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..353
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39564
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvkniek hfgafhalnn isldfpdgql vallgpsgcg kttllriiag lesadggqvi
       61 legqdatnvh vrerevgfvf qhyalfrhmt vydnvafglr vrprstrpse teikkrvtrl
      121 ldlvqlgfla drypaqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 tlhdelhits ifvthdqeea levadqivvm nkgnveqigs prevyetpkt pfvfdflgqa
      241 nrfegqnngg iiqlgedriq fegaqkhpqg dvivfarpde lrisaqpqen aiqatfirel
      301 wiagkvvael ndrqgnliei sltpeearah qfrpnqtvwl splnlhlfan qva
//
LOCUS       WP_004893337             416 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Acinetobacter schindleri].
ACCESSION   WP_004893337
VERSION     WP_004893337.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter schindleri
  ORGANISM  Acinetobacter schindleri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Acinetobacter schindleri"
                     /db_xref="taxon:108981"
     Protein         1..416
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=47573
     Region          5..291
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          286..388
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mavhflhtsd whlgqffhnh drefehrhfl swlleqikqk qpnalliagd ifdvinpsss
       61 aqkqlyqflt sahalaphmq tlmiagnhds gyrieqvepf lakfnaraig visrkennql
      121 dldrlmvpiy speqkilawc lalpylrsae itglnehtss nqsaiaylhr qliaeakark
      181 qpdqalilms hahmqggets dserpivvgh eealstalfe dgidyvalgh lhkpqkvgqe
      241 hirysgspip lsfselnykh qvvevridpm qsdeqrfqye pliiprtvdl lriradlndl
      301 idqvkalpng eieqlfarhf leieytttap ppvdlrqqie qalppnryrl lrisriyqqv
      361 adssmhiski dlapptpesl fgnlwekmgy dpddsvkrdf lqllheaqqd idvqqp
//
LOCUS       WP_004894711             408 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Acinetobacter
            schindleri].
ACCESSION   WP_004894711
VERSION     WP_004894711.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter schindleri
  ORGANISM  Acinetobacter schindleri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 408)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 408)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Acinetobacter schindleri"
                     /db_xref="taxon:108981"
     Protein         1..408
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=46958
     Region          42..386
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 menfqlptei ksievftdnf kqgllthsgh yyyqpvqeqr fvsltmtlpd mqgyshgalh
       61 pifsqnlpeg hnrhfiaskl aryanvnemy llalqeangi gmlsykselq lpeveivsld
      121 eilnynsqvp lfpqllekyy lrnslagvqp kvsipnvttl tertvqqkdl ivksydadfd
      181 lltvnefvcm eaarycglqp pktylsanle tyiierfdka adgtklgyed fttllkrsnd
      241 pnekykgsye nllkatylyt rseaevvkmy kyivfnclig ngdahlknfa lqytpdmsdi
      301 fvsppfdith tliyknidnq lalkingskq fptkaellkl aespefrirn akeiieyfsd
      361 qiadylklsn eieyldglre sikqnlskvm sthsikpvyr hdkkkkyk
//
LOCUS       WP_004894872             192 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Acinetobacter].
ACCESSION   WP_004894872
VERSION     WP_004894872.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 192)
  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 192)
  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   3  (residues 1 to 192)
  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   4  (residues 1 to 192)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 192)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..192
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21578
     Region          1..191
                     /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"
ORIGIN      
        1 mpklkialid dnaeraefiq dsltahdfiv vaclivhdls mthvknlqad villnmdhph
       61 rdiiescvsq yelptvlftq nsnkdtiksa idagvtayiv dgidpsklns imeisieqfh
      121 khkkllndlk etqdkladrr didkakslli qlhsmseeqa fallrknams hritlgemar
      181 rlldaqklls ge
//
LOCUS       WP_004897025             320 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Lactobacillus johnsonii].
ACCESSION   WP_004897025
VERSION     WP_004897025.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus johnsonii
  ORGANISM  Lactobacillus johnsonii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (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   2  (residues 1 to 320)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 320)
  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   4  (residues 1 to 320)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Lactobacillus johnsonii"
                     /db_xref="taxon:33959"
     Protein         1..320
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=36613
     Region          2..250
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mmieyknisk kydgqeilkd vsfavkkgdi fvlvgpsgsg kttllkmfnr lieptkgqil
       61 lndkpikeyn lrklrektgy vlqtaslfpn ltvgenitiv leqegvdrke rrkkqeellk
      121 svdldpklyc drrpselsgg eqqrvgivra laadpevvlm depfsaldpv vrkqlqdlli
      181 nlheqfnktv mfvthdmqea irlgntigil hkgvleqvgk preilrhpat kfvqeffagn
      241 rinqkldlet llkselgvdp rfypkvdtlv ryhvdsvedl ikdcsnhpdt lfvaetrfge
      301 fliepkrvwn fflkwvaghd
//
LOCUS       WP_004897260             160 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Lactobacillus].
ACCESSION   WP_004897260
VERSION     WP_004897260.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus
  ORGANISM  Lactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Lactobacillus"
                     /db_xref="taxon:1578"
     Protein         1..160
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17977
     Region          1..152
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mnaifereav rkytneevee ekiqklidaf qaspcamhqt dvmelsvitk sellkkieds
       61 tdnscynapl ifmintkkds qfgerdasva aenvmveaad lglgsvyvmg gvfalnkfpe
      121 lqrelgmdeg yetsvlvpig ypadkeqved rrnrykvvrk
//
LOCUS       WP_004898856             424 aa            linear   BCT 20-JAN-2025
DEFINITION  TerD family protein [Acinetobacter brisouii].
ACCESSION   WP_004898856
VERSION     WP_004898856.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter brisouii
  ORGANISM  Acinetobacter brisouii
            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 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Acinetobacter brisouii"
                     /db_xref="taxon:396323"
     Protein         1..424
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=46454
     Region          5..424
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mqliagantv lptpsvelvi rarvpqaidl ditaylleqt tqkvrgdtdm ifygqthtpn
       61 qsiqlfesss qpdyltriri ntaqldsaig kiaicatlse pahirdlqql sidllsdghv
      121 vatseintqs ktekalilae vynhngrwky rfvdqgfngg lkplaenfgv evaepsaapp
      181 qpqpspsvap pitssnanif gqpvssttas pnsqpvppps sinlskirld kpnssinltk
      241 yngsfgkiqv nlnwnrsggd rgksffrkls asqsvdldlg amiemqngat hivqalgnrf
      301 gsyekspyie lqgddrtgss lngenlwing ehwdqikriv iytyiyegaa nwaatdaivn
      361 mqlpnqppie vpvneggyls tcaivelknv ggqiqanrqv qyfddqqkld ehygfgfrwt
      421 vgrk
//
LOCUS       WP_004899035             157 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Acinetobacter brisouii].
ACCESSION   WP_004899035
VERSION     WP_004899035.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter brisouii
  ORGANISM  Acinetobacter brisouii
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Acinetobacter brisouii"
                     /db_xref="taxon:396323"
     Protein         1..157
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=15985
     Region          2..150
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mnaqkgftli elmivvaiig ilaaiaipay qsyiaksqvt ravaelgalk tayedclnng
       61 qtatntcqig wtgsniqkll ipasvavkts aptnagtals ttgaiegqfd atnggasstl
      121 nnkkvqwnrt asgtwtcttd adskyapvgc pvggtvs
//
LOCUS       WP_004899653             290 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Leuconostoc citreum].
ACCESSION   WP_004899653
VERSION     WP_004899653.1
KEYWORDS    RefSeq.
SOURCE      Leuconostoc citreum
  ORGANISM  Leuconostoc citreum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Leuconostoc.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 290)
  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 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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Leuconostoc citreum"
                     /db_xref="taxon:33964"
     Protein         1..290
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33566
     Region          35..290
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <178..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 msympgnlts dafkheivqh eslhlpvqwl ihesdrlqqd vpkhwheele lsltvnghid
       61 qftvdgrpyh tktgdvlvin sgsvhsvpiq ksgteaftlf fnpdflraal pqaseivfat
      121 ypndvsaves telvdylyam hytvrhdpmn ylritrlayd ildelvmhfs nrefginphl
      181 iqtvderlyk ilfyikahiy ngltvaavae hfdistsyls ryfkiklqms playlqavrl
      241 nkayqylmnt nksmswisdt tgfgdvksfe rlfkkkygts pksyrqqfrk
//
LOCUS       WP_004901685             144 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acinetobacter brisouii].
ACCESSION   WP_004901685
VERSION     WP_004901685.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter brisouii
  ORGANISM  Acinetobacter brisouii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Acinetobacter brisouii"
                     /db_xref="taxon:396323"
     Protein         1..144
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15399
     Region          16..141
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mpistskimg llpnikmnni skvkgftlie lmivivilai iasfaipayg nyvkrahika
       61 aqsdlvalsl vlentyqrtl sypvstttnt attktaftsw npsedvfsyt atstassytl
      121 tatkgnctmt mtntssspss cdty
//
LOCUS       WP_004902741             626 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Acinetobacter brisouii].
ACCESSION   WP_004902741
VERSION     WP_004902741.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter brisouii
  ORGANISM  Acinetobacter brisouii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 626)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 626)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 626)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 626)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Acinetobacter brisouii"
                     /db_xref="taxon:396323"
     Protein         1..626
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68871
     Region          5..626
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mqtmtqkarl pamalaalgv vfgdigtspl yalkesfhea hglginpanv lgilsiifwc
       61 ltliisikyv aivmrvdnng eggimallal nlrkakiadn kkiyliaigf vgaslffgdg
      121 iitpaisvls aveglsiatd vfdpyimpia ivivvilflv qkhgtafvgk lfgpltliwf
      181 laigifgims iaktplvlgm fsphwavefi ftnpvmsffv mgavvltvtg gealyadmgh
      241 fgrtpirfaw fgvvlpclvl nyagqgalll rnpsaienpf fllvpswaly ptiilaaiaa
      301 viasqavisg vfslarqavq lgylprfgik htseseegqi yvpflnwlll taiiililif
      361 ktssnlasay glavtltmlc dtlligvfif yawkwsapkl lllitpflvl divlvaatsl
      421 kivsggwvpl liggiafgil mtwkrgrelm faklehdtlp idlfvksigs dtvhwvqgda
      481 vfltgtpnvv phamlhnikh nkvlhernil itvmvqdvpy vaqkerilve tltehfyriq
      541 vfygfkdepn vprdlkqaye elgfeydlmq isffisrdrv vhkvgdgmsp wreklfismq
      601 rntspvsdfy qiptnrvvel ggqiei
//
LOCUS       WP_004903303             616 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Acinetobacter brisouii].
ACCESSION   WP_004903303
VERSION     WP_004903303.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter brisouii
  ORGANISM  Acinetobacter brisouii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 616)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 616)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 616)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 616)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Acinetobacter brisouii"
                     /db_xref="taxon:396323"
     Protein         1..616
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68476
     Region          2..616
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msnkkissla laalgvvygd igtsplysfk eaflhglaln elnilsvlsa fiwsvllivt
       61 vkyisvvmqy nnngeggvls llalvlkkik pgskqarvvl llglfaaglf yadafitpai
      121 svlsaiegte litiqfkswi ipitisvlim lflfqrygtq kiggllfgpi miiwfltlgi
      181 lglkeifinp avlyafnpfy avqfffnqpk egifllsavf laltggealy admghfgara
      241 irvawyglvw psltlnylgq gallmhepta innpffllmp ssgliflvil atfatviasq
      301 atisgtfslt leasrlsllp rinflhtsdq ekgqvyipfi nwlmllgvlf lvvafkssga
      361 lasayglavs gtmlittill iymqllyras yfklcllglf liieigfvls nltkiatgaw
      421 lpiligcvvf silfiwqkgm hylkeerrnq slnldilpni lnqgihkvsg taiyltsdkd
      481 lipnallhnl khyqviheyn isltvetlns pyvaqedkvk vnevfdnfyq vtvyfgfrey
      541 pylvpliegl klhdwkfdlm sttffvsdti iinngnflnh vefnvfnilf rqageihqyf
      601 glppnrtvql gtqval
//
LOCUS       WP_004903574             103 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Acinetobacter brisouii].
ACCESSION   WP_004903574
VERSION     WP_004903574.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter brisouii
  ORGANISM  Acinetobacter brisouii
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Acinetobacter brisouii"
                     /db_xref="taxon:396323"
     Protein         1..103
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11428
     Region          1..101
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(5..6,24..25,33,36,38..39,41,44..45,47,55,60,70)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(24,55..56,58,85)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mqvelyrqil evvaripqgk vasygqvakm aglprharlv gkvlqsleeh sdipwhrvvn
       61 aqgkislsqt naqgenlqam rlidegivvm dgriklkvyq wgn
//
LOCUS       WP_004906634            1056 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Acinetobacter junii].
ACCESSION   WP_004906634
VERSION     WP_004906634.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter junii (Acinetobacter grimontii)
  ORGANISM  Acinetobacter junii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Acinetobacter junii"
                     /db_xref="taxon:40215"
     Protein         1..1056
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=122742
     Region          468..>838
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mstqfsalvs klkeifqinr pdldfgvyri lnarsteiae fldkrlktkv eqylgeakss
       61 ldenvlkele aelkaefgkr afneqgelid qeaiesalgq kyialtqada hemtdqsqvy
      121 shlltffsry yddgdfisqr rykgdtyaip ysgeevmlhw ankdqyytks gemfsnyrfk
      181 lndersvlfr lvsadtaren rkdndkdrrf iivtepktft ridedgeefe etivpfsiqn
      241 neltilfeya tlpkgskqet lniesynkiv saevlttdwl ndlaqpapte kepkrtvlhk
      301 hlstytqknt adyfihkdlg kflrheldfy iknevmhldd vvstdqfiqi erqlsiikcl
      361 rqigleiisf lasledfqkk lwlkkkfvvs aeycitldrv ddslyaeiae ntsqwqqwed
      421 lgfkgtdagw gtidylkqhq almvdtslfs iefkarllkt iddldaqtdg liihsdnfqa
      481 lrliekkynn tvqsiyidpp yntsaseily knsfkhsswa tlienriees tsllkkqgll
      541 cvtiddlely nlkmildqqf gaenflanvl irnnpsgrst lkgfsvnhey glfyskgele
      601 ngvgrlphde aqrsryslkd nkgffewenl rrngpdsrke drpkqyypik ynkveksial
      661 lpmewderkk twshsinsin eneiilwphh pkgelkvwry skehienepe rfqviekdgl
      721 fevyrkkyin segilprtww ekpgysardn gtralieffg qvaqfdfpka kdavkdcfkv
      781 lklnskdial dyfggsgtsa havidlnred kgtrkyilme qgeyfntvlk priqkvvysa
      841 dwkggkptnp esgishclkv vklesyedtl nnlelvrkga qqtllaeqqt stkpedqnay
      901 sdylmhymle leskdsllnv kdflkpfsyq mnittdsaga ferknidlve tfnyligmnv
      961 readyqldkg yvqitgqlrt geyttvlwrd cdkigyaeld qllaklkinp ndgeyqliyi
     1021 ngdhnvasky ttkegeekql kvrsieqtfl knmfee
//
LOCUS       WP_004908861             344 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Acinetobacter junii].
ACCESSION   WP_004908861
VERSION     WP_004908861.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter junii (Acinetobacter grimontii)
  ORGANISM  Acinetobacter junii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Acinetobacter junii"
                     /db_xref="taxon:40215"
     Protein         1..344
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38038
     Region          <75..>213
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          262..336
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 msmnnkqrwm ggvvllgggv llaalllkgn eeieqdkaqa tishpipktq snsntaqplq
       61 dgemvslqpl avdvetekrl leeqrlarek avaeqearaa eflkmqqeae aaaarkaaee
      121 yaalnarrss eqessdnipp elaeddkaka qrlaeekrkl dekkkaeqqk qdqlksdaek
      181 klaeekrkae aekkaaedkr kaeadkkaae dkrkaeaekk aaedkrkaea dkkaaddkkr
      241 kaeedakkka eaekardlme ngdkkwmvqv alaanqanad avvsklrakg ykvttsstsk
      301 girimvgpak drdvadatrk kissdeslnm ksawvidwvp ldqr
//
LOCUS       WP_004911236             160 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Providencia].
ACCESSION   WP_004911236
VERSION     WP_004911236.1
KEYWORDS    RefSeq.
SOURCE      Providencia
  ORGANISM  Providencia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Providencia"
                     /db_xref="taxon:586"
     Protein         1..160
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17394
     Region          1..152
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mdkkkyyhel sdnlsallag eydliatlan tsallydcle gvnwagfyls ngqelvlgpf
       61 qgkvacvrip fgkgvcgtaf snnqvqried vhafpghiac daasnaeivf plvvngqiig
      121 vldidspnis qfdhedekgl qhlvnqlcqh lamcsmpkyh
//
LOCUS       WP_004911694             349 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Providencia].
ACCESSION   WP_004911694
VERSION     WP_004911694.1
KEYWORDS    RefSeq.
SOURCE      Providencia
  ORGANISM  Providencia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 349)
  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 349)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Providencia"
                     /db_xref="taxon:586"
     Protein         1..349
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=38498
     Region          16..70
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msvklssyvw dgcasaglki tsvaimarla dfsnddgvcw psvptiarqi gagestvrta
       61 iknlekagwl ssekrrkgnr nasniyqlnv dklasaamaa lsqppvsdts nsdasksvas
      121 ksvpsesskn nrfdppesgg dpsvtskhdp lvtnsssqns cessdqskid flnrypeavi
      181 ystnfqkwgs andlkcaewl ferkcevfke lglkepkapn ltdwanevrl mvsvdghshk
      241 eicqfykrvi qddfwkknvq cprtlrnqwd dltlrlageq kvkvdaverd eaftriigsr
      301 skpqnrieei aselagksgv rrmtdfvgrk awagiwqqaa eqaakevta
//
LOCUS       WP_004912239             321 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter junii].
ACCESSION   WP_004912239
VERSION     WP_004912239.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter junii (Acinetobacter grimontii)
  ORGANISM  Acinetobacter junii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 321)
  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   6  (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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Acinetobacter junii"
                     /db_xref="taxon:40215"
     Protein         1..321
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36639
     Region          25..201
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <177..320
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mitnkasdag iflwmvyqtm qkmdldaani fasvhlpdqp pdksvrrdns tqrrfwdaae
       61 kisedsdigl hvggnippfr gqvieylfls sptfgeglkr tlryqalltn amsfqlevvd
      121 qntvglygle hpvrhyleca igillnffky itndafipfq vllpyenaad qkeykkvwnc
      181 dvlvgqrhga ilfeskilny pspahepell kmhehhaesq ldllnkhqli geiekilang
      241 llesgkfdqn vvaehlnksa rslradlqll nttyekviaq yrerlarrll sqtdesidqi
      301 vyltgfseps afsrafkrwt k
//
LOCUS       WP_004915417             160 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Leuconostoc].
ACCESSION   WP_004915417
VERSION     WP_004915417.1
KEYWORDS    RefSeq.
SOURCE      Leuconostoc
  ORGANISM  Leuconostoc
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Leuconostoc"
                     /db_xref="taxon:1243"
     Protein         1..160
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17393
     Region          3..158
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 msevqtksli aqildtwiqg ekseklilsn yanaaailhq nvddinwvgf ylydqqmkql
       61 vlgpflgkpa vtvispnsgv vgqsftaqst lvvpdvkafs ghivcdpisn aeivvpitka
      121 dgtklgvldi dsptlnrftk qdqsdledyi qtllayveqi
//
LOCUS       WP_004915828             332 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004915828
VERSION     WP_004915828.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 332)
  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 332)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 332)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 332)
  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   5  (residues 1 to 332)
  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   6  (residues 1 to 332)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..332
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38104
     Region          22..>155
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <236..332
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mllsklpgty vnllietiee wgisseevlv dthitfedlq ktywyvdsev fiqlleksvr
       61 ltgnaafpil mankmkvshy gnvgiaamss knleqalrvl eefiglycsv fklrleiege
      121 taflylthil vesestnkfi aflvasfani iskliktesd iliflkqkqs finnnfaykf
      181 eqvtdavcfd rellnihlkt adeivfklak kqcirdtekh iksrqtksim rsqiieliet
      241 sliqknigql nlsevakqln mssrtlqryl eiedttfkal iaevrkqyae amliqnelsi
      301 qeiseslgya dvshfsrafk nwtrvtpkaf rk
//
LOCUS       WP_004919988             233 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Acinetobacter].
ACCESSION   WP_004919988
VERSION     WP_004919988.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 233)
  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 233)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 233)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..233
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=25816
     Region          4..211
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Site            order(98..99,102..103,105,133,136..137,140..141,143..144,
                     166,169..170,173..174,177)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          98..122
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          127..159
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          165..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msalseeeql dnlksftkky gsaiisgili aliaffgwqy wqkktlaenq trtakvqqli
       61 dqaqaaeanp dalnnlyaaa dkivkdapds iqavqtefll akiaydkgdy ataekslkki
      121 enskindegl vqliklrlan aqlaqkkyde alktlslvtd pafkataeea rgdvyvaknd
      181 iasarkayqs awnvllerkq erqilqikle svgvlvddpe ierpildtqv des
//
LOCUS       WP_004919245             355 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Riemerella
            anatipestifer].
ACCESSION   WP_004919245
VERSION     WP_004919245.1
KEYWORDS    RefSeq.
SOURCE      Riemerella anatipestifer
  ORGANISM  Riemerella anatipestifer
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Riemerella.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 355)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Riemerella anatipestifer"
                     /db_xref="taxon:34085"
     Protein         1..355
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39101
     Region          2..354
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mpntviigsg scvpsniikg sdfldsiffd dnkelidkpv qevidkfvei teieerrysn
       61 leeynsdlgl kaslealeda gidkeeldyi iyasnfgevs nsgvsdfmps msarlknklg
      121 iknlscinyd mifgcpgwve amiladslik agrakyilvv ggdtlskvtd pydrnkmifa
      181 dgagavvvka deskdkgiia dstlcfngee lsylensssl npnvpqdkny irmrgrkiye
      241 falkyvpdai kstidkagls iqdidkilih qanakmdhai isrlhrlygm ktydeaiapm
      301 tiqkfgnssv atvptmynli kkgklgnhqf kqggyivfas vgagmninai lykmd
//
LOCUS       WP_004919995             369 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Providencia].
ACCESSION   WP_004919995
VERSION     WP_004919995.1
KEYWORDS    RefSeq.
SOURCE      Providencia
  ORGANISM  Providencia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
REFERENCE   1  (residues 1 to 369)
  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 369)
  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
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 369)
  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   5  (residues 1 to 369)
  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   6  (residues 1 to 369)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 369)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 369)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Providencia"
                     /db_xref="taxon:586"
     Protein         1..369
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40620
     Region          8..>56
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          76..363
                     /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 mtdkpevldl kptqrlllel irrygpisra elaklsnltp gaitqqcrel ifsglivege
       61 knigqrgqps lplklnpgga csigvsfssg fidlalvdfc gkkifstsev hlenqpliat
      121 ldqikkmvns tlkklklqha rilgvgyavp gfvksdgkkr qcvtwlkswr dadlqaefqa
      181 nlpwptwven nanaaaigel ysgqwnqyrd ltvlelgygi gagiiadhkl ltggfrnage
      241 vgmafptgth rpsykdllgt lsaagydeke llglikkkdi vietwyqrsl kqledtvlgc
      301 lqwldpqlii iggampkeit srfaeditdw lqyrldperp mvkvvhssig sesaslgaam
      361 lslyqiinq
//
LOCUS       WP_004921169             190 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Providencia].
ACCESSION   WP_004921169
VERSION     WP_004921169.1
KEYWORDS    RefSeq.
SOURCE      Providencia
  ORGANISM  Providencia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Providencia"
                     /db_xref="taxon:586"
     Protein         1..190
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20816
     Region          1..190
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mkkliigltg asgaiygvrl levlkpvknv ethlvmsaaa rqtlslethy svkevqqlad
       61 hhydsrdiaa aissgsfrtt gmvimpctmk tlsgivhsyt dtlvtraadv vlkegkklvl
      121 gvretplhlg hlkllvqaae mgavimppmp afyhqpksiq divdqtvnri ldqfdieldq
      181 dlftrwqggk
//
LOCUS       WP_004921388             419 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces griseoflavus].
ACCESSION   WP_004921388
VERSION     WP_004921388.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseoflavus
  ORGANISM  Streptomyces griseoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 419)
  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 419)
  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
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 419)
  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   5  (residues 1 to 419)
  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   6  (residues 1 to 419)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 419)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 419)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Streptomyces griseoflavus"
                     /db_xref="taxon:35619"
     Protein         1..419
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42879
     Region          16..56
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          79..386
                     /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 mpsgvhalvr rtheervlra lqengamsrg eiarvvglsr ttlseitghl lqrgaivvvd
       61 tdaskregsg rpaarlaldp asaqfmgvdf ghrrvhvvva dashevmasg aaryddttpw
      121 qertglalgl verltaeagv hfgalqgigi gvpgpypape gsapsratpv gtvlrpapeg
      181 vdiafaerfd apvivdnntr laalaeaitg adsvadlvyv rlsdgvgggl vvgghlvtgs
      241 sglagelghv tvepagrpcr cgkrgcletv asvpailaac wefglplenl rdladavsra
      301 hpvvdrvlre aaaalgrvvg aatmtlnpak vviggeitql apviveqvaa tlaadlfpta
      361 sagpaveaar lsdddgaiga laavfhnspl larypettdv tagpgtddpt eegavhvrp
//
LOCUS       WP_004923779             147 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: pilin [Acinetobacter].
ACCESSION   WP_004923779
VERSION     WP_004923779.1
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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..147
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14741
     Region          2..146
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mnaqkgftli elmiviaiig ilaaiaipay tdytvrarvs egltaassmk ttvsenilna
       61 galvagtpst agsscvgvqe isasnattnv atatcgassa gqiivtmdtt kakganitlt
      121 ptyasgavtw kctttsdkky vpsecrg
//
LOCUS       WP_004925811             197 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Streptomyces].
ACCESSION   WP_004925811
VERSION     WP_004925811.1
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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..197
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=21490
     Region          31..180
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mappmsasaf lralkaeglt vvevgdwrdh nrnhkgpwgp vhgvmihhtv tkgsartvdi
       61 crkgyaslpg plchgvitkd grvhlvgygr anhaglgddd vlraviaeqq rlpadnelnt
      121 dgnrhfygfe cenlgdgedp wpaaqleaie kaaaavcrhh gwnersvigh kewqpgkvdp
      181 rgytmtsmrk rigdrlg
//
LOCUS       WP_004926237             808 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Acinetobacter baylyi].
ACCESSION   WP_004926237
VERSION     WP_004926237.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baylyi
  ORGANISM  Acinetobacter baylyi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 808)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 808)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 808)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..808
                     /organism="Acinetobacter baylyi"
                     /db_xref="taxon:202950"
     Protein         1..808
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89969
     Region          59..103
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          144..808
                     /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 mgsfrhpffn pkplvlaihm atfsiatlpl vahaaatqvn ipaghlaqvl nryaleqgvn
       61 fifdstlfld iksqgiqgay eiddgfaell kntnyqikqt sngyrleekp vnskkeqivk
      121 ltplqskanq sgysglgtss gsilptitle aenhdtplkr intvgvlgnk svidtpysit
      181 tktaeeietr qtnslgkifv gdpsivtevn syssgwstpv sirglkldet ngykvngysv
      241 sawggefpve laqnvmalkg lsglmygfat pggvinyqtk qpteenllst kigyrsagil
      301 saqldtggri gedkqfgyrf nivkekgety ngsdadnlat alaldyrilp nlvwkgeiiy
      361 qdrhldneas mfswwgfqgn klpkpidgsd khivkgafyt ihtalaqtgl ywevndnwka
      421 eitqarirnr ntvnkafayi lnqqgdysin myqlggesir disqfmvtgl fdtgfvnhel
      481 ilgssfekkq ahdansnwda ntdvgniyqs qttyynnsms ftsafssniy qkqvflsdtl
      541 sfndhwqaii agryinynnq aniyqkevvt ptyaliykpi edwslyasys ealeegqkvt
      601 sstgkeyana eqyldptisk qyeigtkyqq drwhvsaaly rlermaiide mingqlnltq
      661 ngetiyqgfe lmggykftpd ltinaginln dpsiekvsev nasikgnrpa gaskiqavvq
      721 adwnipyidg lsvhgdvrhy gdtwyddent ikfddytlvn igggyqtris kkpvtfradi
      781 nnllnkkywm nsgagepvtf vlsakvdw
//
LOCUS       WP_004927040             122 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Providencia].
ACCESSION   WP_004927040
VERSION     WP_004927040.1
KEYWORDS    RefSeq.
SOURCE      Providencia
  ORGANISM  Providencia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
REFERENCE   1  (residues 1 to 122)
  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   2  (residues 1 to 122)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Providencia"
                     /db_xref="taxon:586"
     Protein         1..122
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13236
     Region          52..120
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mtwmkfikqs lgsaavilti lmcsqsalak kaeadkpvaa vvskkpkeek psenlketnq
       61 vninqasaee lakklhgigi qkakaiveyr ekygafntle nilevrgigp afleknrgkl
      121 al
//
LOCUS       WP_004929353             106 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Acinetobacter].
ACCESSION   WP_004929353
VERSION     WP_004929353.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..106
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11782
     Region          1..101
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(5..6,24..25,33,36,38..39,41,44..45,47,55,60,67)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(24,55..56,58,85)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mstelysqil evialvpfgk vatygqiarl aglpkharlv gytlknidqa sdipwhriin
       61 aqgkvstyhl nqigeniqln klrdegivvl ngkinlkkyq wlvsqs
//
LOCUS       WP_004929483             203 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LytR C-terminal domain-containing protein
            [Streptomyces].
ACCESSION   WP_004929483
VERSION     WP_004929483.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 203)
  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 10598501
            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="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=20890
     Region          84..174
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mggqyritgd ryprmrrprr rgrlvvmava svavlgvggw gtlqlidvft gggdsasaag
       61 tkaacadras rtaapkalpa pgtikvnvln attrsglaqk tadelkkrgf kigevtnatk
      121 eydkkvkgtg vllgpaaald tslpvlgaql agaerrtdpa rkggevdlii gdgfraltkk
      181 adadkalavl aepkpaptsk knc
//
LOCUS       WP_004929617             346 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004929617
VERSION     WP_004929617.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 346)
  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 346)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 346)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 346)
  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   5  (residues 1 to 346)
  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   6  (residues 1 to 346)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..346
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39607
     Region          32..214
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          104..343
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mniketdgln vnrdtisihf vnaaltgvkr lgmdvetlls hvgieaellr qpkarispeq
       61 ytrfikmlwm vtqdehvgfd iqprrlgtfa imcqliihak tlgqalelss qfyklfgdew
      121 svtlerdkhe arlvplipkt ldpdhfites mlmiwhglas wlierrlple rvhfsyprpa
      181 hadeydalff apvmqfdapr teitfaadyl dlplrqdeqt leeflkaapa qllikfkntn
      241 sltsrirevl ksqigeempt lndvasmlyl spqtlrrrla aegksyqgvk dalrrdaaih
      301 lllnpdltle dvaqqvgfse tstfhrafkk wtgvtpglyr qlhgyh
//
LOCUS       WP_004931760             214 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease family protein [Streptomyces].
ACCESSION   WP_004931760
VERSION     WP_004931760.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..214
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=23133
     Region          <116..209
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mskfyarrrl siaaaltgvi asvglfnapt asaalptpvs aatarsylat ldvrtenrtg
       61 ysrdlfphwi tqsgtcntre tvlkrdgsgv vtdsscaats gswyspydga twsaasdvdi
      121 dhlvplaeaw dsgasawtts rrqsfandlt rpqllavtdn vnqskgdqdp atwmpsrtay
      181 rctyvrawvq vkyyydlsvd saeksaltny lasc
//
LOCUS       WP_004932520             142 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Serratia].
ACCESSION   WP_004932520
VERSION     WP_004932520.1
KEYWORDS    RefSeq.
SOURCE      Serratia
  ORGANISM  Serratia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Serratia"
                     /db_xref="taxon:613"
     Protein         1..142
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14919
     Region          3..140
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 msstlavisl fgssflsatl lpgnseivlv alltqsrvsp ellvlaatlg ntlggltnvi
       61 igrllpalkp qrglatalgw lqrfgpaall lswvpvvgdl lcvlagwlrm pwgsvalflc
      121 igkalryivl amitvqgiaw wq
//
LOCUS       WP_004932522             411 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Streptomyces].
ACCESSION   WP_004932522
VERSION     WP_004932522.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 411)
  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 411)
  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   3  (residues 1 to 411)
  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   4  (residues 1 to 411)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 411)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 411)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 411)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..411
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42860
     Region          45..396
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(118..120,141..142,200,252,276)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mrqrsliait aalaagaltl tacgsrdedg ggssdagngg ttviigvdap ltgdlsalgl
       61 giknsvdlaa ktankekyve gvtfkieald dqgqasvgqq natklvankd vlgvvgplns
      121 svgesmqkvf dtaklvevsp antnpaltqg vnwqkektrp yksyfrtatt daiqgpfaaq
      181 yvyndakkkk vfviddkkty gaglaatfte efkklggkvv gtehinpdsk dfnavatkvk
      241 qsgadvvyyg geypqagpls kqikeagaki plvggdgiys adfiklsgaa gagdlatsvg
      301 apveelpsak efvanykdag ykeafeaygg ysydsawaii eavkkvvedn dgklpddars
      361 kvvdamqnvs fdgvtgkvsf defgdatnkq ltvysvkdgn watvksgtft g
//
LOCUS       WP_004935208             245 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Streptomyces].
ACCESSION   WP_004935208
VERSION     WP_004935208.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..245
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26793
     Region          28..240
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mttetplsga padgtddpal fatmstmram rrlrpdpvpg dlldrlvqaa vwgpsggnmq
       61 rfeyvvvtdp avmarlaplw krcvdaylat tgkyapagmd eaayarmvaa ieyqrdhfae
      121 tpaliipcyq fpaprieeeg lrryaealga eatehmgrvq erfaalaegs cvypgvqnll
      181 laaralglaa nitiwhlfle newkaalgip damntfaaip vgwprgrfgp vsrrpvaevv
      241 hrdrw
//
LOCUS       WP_004937144             495 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Serratia marcescens].
ACCESSION   WP_004937144
VERSION     WP_004937144.1
KEYWORDS    RefSeq.
SOURCE      Serratia marcescens
  ORGANISM  Serratia marcescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Serratia marcescens"
                     /db_xref="taxon:615"
     Protein         1..495
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=53861
     Region          1..495
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mqstikiheq dnvavalrdl aagecveleg aviqlaqpva rghkfalgpi akdediikyg
       61 qpighalaai gpgehihsqn aktnlsdlds yryqpqfptl ppqvadrevq lyrrvggevg
      121 irnelwivpt vgcvngiarq iqqrflqqtq aegidgvhlf shpfgcsqlg qdhantriml
      181 qnlarhpnag avlviglgce nnqvdafrat lgiederrlr fmvcqqqdde veaglallhe
      241 lyremrhdrr epgrlselkf glecggsdgl sgitanpllg rfsdyviang gttvltevpe
      301 mfgaerilms rcrdgetfdk tvdmindfkr yfiahqqpiy enpspgnkag gittleeksl
      361 gctqkaglsq vvdvlkyger lrvpglnlls apgndavats alagagchmv lfstgrgtpy
      421 ggfvptvkla tnselaakkp hwidfdagsl ihgvametll srfidlivei angrparnet
      481 ndfrelaifk sgvtl
//
LOCUS       WP_004936376             261 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Serratia].
ACCESSION   WP_004936376
VERSION     WP_004936376.1
KEYWORDS    RefSeq.
SOURCE      Serratia
  ORGANISM  Serratia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Serratia"
                     /db_xref="taxon:613"
     Protein         1..261
                     /product="formate/nitrite transporter family protein"
                     /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=27460
     Region          2..256
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mslhspkeia alavqagvnk sraplanlli lgflagafia tgflldihvi gtlpaewgsf
       61 gallgaavfp igliltilag gelltgnmmt lpmawfarei paiavlrnwf wvtlanlags
      121 vavayffghl lgltegaflh ktlaiaqakv dadflhafis gvgcnwlvcl avwlafaskd
      181 vpgkvigmwf pvmafvaigf qhvvanmfii paaifaggmg weqylpnfva vflgnalgga
      241 gfvglmyfla yrpglptseh a
//
LOCUS       WP_004938732             114 aa            linear   BCT 20-JAN-2025
DEFINITION  PilZ domain-containing protein [Acinetobacter soli].
ACCESSION   WP_004938732
VERSION     WP_004938732.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter soli
  ORGANISM  Acinetobacter soli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 114)
  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   3  (residues 1 to 114)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 114)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Acinetobacter soli"
                     /db_xref="taxon:487316"
     Protein         1..114
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12463
     Region          7..114
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mesrisggli hvhipdratl qasymhfvqd gglfipsres vtlgeeifvl atlpeqtlki
       61 pltgkviwis rkqagikpqg faiqlsgerg iyykteaeki lagsmssdrs nftm
//
LOCUS       WP_004939411             341 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Serratia marcescens].
ACCESSION   WP_004939411
VERSION     WP_004939411.1
KEYWORDS    RefSeq.
SOURCE      Serratia marcescens
  ORGANISM  Serratia marcescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 341)
  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 341)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Serratia marcescens"
                     /db_xref="taxon:615"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37811
     Region          20..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          247..329
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mssdqipvsg alavhlaaqg vdieqlgrla glpaglfger rdkiklttqq ffslwrilpq
       61 lnddpafglr lggeaapehy dialvaalhs atlgealqkv arykrlvcpe elmlvedgds
      121 mrlhtrwtms eghapallid amfaaitalc rrgtglplqp qaieltrrad aasplaryfg
      181 cpvtfnapld vlvfdralmr qpfvtynqam lavllpglea elaksqsahd lptqvmails
      241 rsmrgqrpsv nsvaaelyls prtlqrrlqq hgysyqqlld ktrhrtacrl laetdlepge
      301 iafvlgfeel nsfsrafiqw etltpsrwrt qraagqwenr t
//
LOCUS       WP_004941457             715 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Streptomyces
            mobaraensis].
ACCESSION   WP_004941457
VERSION     WP_004941457.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces mobaraensis
  ORGANISM  Streptomyces mobaraensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 715)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 715)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Streptomyces mobaraensis"
                     /db_xref="taxon:35621"
     Protein         1..715
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=75563
     Region          2..710
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mtsgaqpadt hcpycslqcg mrlrrivspe spgagpggtt vaveerpdfp vnrgalcgkg
       61 rsaaavlapg arltaplvrd rrtgrlreag wdealgraae gladaaarhg rdaagvfggg
      121 gltnekayll gkfarvvlrt anidyngrfc mssaaaaqra afgldrglpf pladiartgc
      181 lvlvggnpad tmppamryfr aqqaaggtlv vvdprrtrta etadlhlrpa pgtdlalalg
      241 llhlvvadgr vdeafvaart tgwerareaa mahwperver ltgvpvaamr ravelfcdap
      301 tgmvltargg eqhskgvdtv gawinlclat gragrphsgy gcltgqgngq ggrehgqkad
      361 qlpgyrsitd aaarahvaav wgvdpdtlpg pgrsayelld tlgtdggvra lllmgsnpvv
      421 saphashvte rlraldclvv cdvvrsetae ladvvlptaq waeetgtmtn legrvilrrr
      481 aldpppgvrt dldvlhglae rlgvgkgfpt eaeeafeelr easaggqady sgidyarira
      541 edgvfwpcpr agagrphhpg tprlfldrfa tpdgrarfad vshraaaeep dadyplrltt
      601 grvlahyqsg aqtrrtpeld raapgpfvev hpwlaarlgv adgtpltvts rrgsvtapav
      661 vtdrirpdtv fmpfhwpgpg rantltnpal dpvsrmpefk vcavrveaav tegar
//
LOCUS       WP_004944903             332 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter soli].
ACCESSION   WP_004944903
VERSION     WP_004944903.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter soli
  ORGANISM  Acinetobacter soli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 332)
  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 332)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 332)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 332)
  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   5  (residues 1 to 332)
  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   6  (residues 1 to 332)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Acinetobacter soli"
                     /db_xref="taxon:487316"
     Protein         1..332
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38661
     Region          25..193
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          96..332
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mltvknyags vygglgqllm cyceaeqlpv pdrlqaiqrl erfdyvvwre lldelyqlrp
       61 iaglglkias hvqpkhlgil ayialscesl gdalkryqdf yrlvydgspl kveqygayfs
      121 irweepephp tqltdeiama lmlqflqqfm cktrielyev hfinplpkda pvynryfqcp
      181 vrfsqpktql liplseaskv vgnadhtlqq llmqqahall drlphstqld qrlqqmilkg
      241 lqqnqyqiev iaqqlgisvr qlqrhlqqqh ssyqqrvqqv rymlateyls dphlslqdia
      301 lllcyseqsa fqrafkhwsg qtpqqwrqqs rr
//
LOCUS       WP_004945531             711 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Acinetobacter soli].
ACCESSION   WP_004945531
VERSION     WP_004945531.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter soli
  ORGANISM  Acinetobacter soli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Acinetobacter soli"
                     /db_xref="taxon:487316"
     Protein         1..711
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=78547
     Region          19..707
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mrflrfntls hciflatglg atgsvwaqdt adnpltlpvi qveatrtgtt ylqtpasifr
       61 vdapaqqqsa qvnltevvkg ipslqinnre nyaqdlqlsm rgfgarstfg vrgirlyvdg
      121 ipatmpdgqg qtsnidlssl dhvevltgpf sslygnssgg tiltttkegq gkdsielgys
      181 ggshdkgrsg iilqggakap nepsyvisss yfdtdgyrdh saarkvlnna kltwnlddgs
      241 kinwitnyvk inaddpqglt reqwkanpkq qvpflkqfdv rkeieqtqtg ltwtkplndq
      301 nelymmgylg nrqvtqyqsi pkstqdasen qaggvidfdr nyygadlrwt gkellphttl
      361 sagvaldfmd edrkgyenyi tvnnqpsygv kgklrrdedn tlwnidpylq aswqflptwr
      421 ldtglrysnv hyksddqyiv gvngddsgkt eyskvlpsaa lswqiqpell ayvsyakgfe
      481 tptftemayr pdglggfnfd lnastsdtye aglksqnrlg dftlaafqtk tkddivsags
      541 ingratfrna dktlregiel twnkalwrdl vatasygyld atfdadvpar gsvaaitsgn
      601 kipgiaknqg yvgitwkpqt gfyagldaqy ndkiyvddkn sdtapsytvm aayagyvwnm
      661 qawkvnvfgr vdnlldkdyv gsvivndgng ryfepadgrn wsagirvvkq f
//
LOCUS       WP_004945553             286 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Streptomyces mobaraensis].
ACCESSION   WP_004945553
VERSION     WP_004945553.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces mobaraensis
  ORGANISM  Streptomyces mobaraensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces mobaraensis"
                     /db_xref="taxon:35621"
     Protein         1..286
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29726
     Region          1..255
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mridlhthst asdgtdtpae lvrnavaagl dvvaltdhdg vgghaeaiaa lppgltlvtg
       61 aelscrlgga dgvgvhmlay lfdpaepefa aarelvrdgr epraramvar lrelgvpitw
      121 ervaelaqga vgrphvatam velgvidtvs daftpewign ggrayadkhe fdpfdavrlv
      181 kaaggvtvla hpmavkrgvc vpedaiaela aagldgievd hmdhdaptra rlrglaadls
      241 llptgssdyh grnktcelge fttdpeiyge itrratgafp vpgagg
//
LOCUS       WP_004947528             326 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Serratia plymuthica].
ACCESSION   WP_004947528
VERSION     WP_004947528.1
KEYWORDS    RefSeq.
SOURCE      Serratia plymuthica
  ORGANISM  Serratia plymuthica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Serratia plymuthica"
                     /db_xref="taxon:82996"
     Protein         1..326
                     /product="formate/nitrite transporter family protein"
                     /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=35792
     Region          38..289
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msdeqsrtta naddplkves keheqgksei evkeenlpsr aaavhelirm egekelerdw
       61 vallwsavaa glsmgaslva kgifharlpd epsrffieni gytfgfiivi marqqlften
      121 tvtavlpimh kptprnflil frlwgvvllg nligtglasl afihmpifdd ntrsafvsls
      181 eevmknspse mfangilagw iiatmvwmfp sagaakiwii vlmtylvaic dlthivvgsv
      241 eilylvfsga lpwqeffypf aiptlagnii ggtfifalis haqirndmsv kkqggeaggg
      301 krgrqgektv iaagatykih rilare
//
LOCUS       WP_004947841             882 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Acinetobacter soli].
ACCESSION   WP_004947841
VERSION     WP_004947841.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter soli
  ORGANISM  Acinetobacter soli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   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   4  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..882
                     /organism="Acinetobacter soli"
                     /db_xref="taxon:487316"
     Protein         1..882
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=98941
     Region          105..835
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mtqrldqmas tlssttttan tsktnnvpsa feqneiqstl ektalkaaql thipkledip
       61 sstrrikpln nflgqdrara sveagislpy sgynifavgt aglgkrtmik rllqqhaksm
      121 ptpddwvyvn nfknarqpla lrfpagtgpk fqsalhhawq tilkqlerrf taetyhnrie
      181 qirqetgkeq qdalveltke geeldlklis rneehcfvpv qykddqvhem tqndiealss
      241 keraeiasni rymdkklerl glhlgsledd ardrvsvlnr diakqvvipr meqilnkhkt
      301 vqgldeflkh yaddiiqnve mileqeeddf spalfnrvps ryqantivtn kpnsgapvif
      361 ddfpthynll ghveqltqng tittdftlir pgclhqangg flmleaeqll eqpyawqglk
      421 ralksgqlkl sslehmltlt gsisiepaav pldvkvilma epeiyyeile vepelgsvfk
      481 iradftdtlq rnevneqaym qliadyvqad kllpfdrsal aalltdssrq aedqsslslh
      541 astlgdlire ahhhafkagd kivsdkhinl alqhrqyrlg ylrelywqdl srgtqlietr
      601 ghrlgqinal svihyadvef glpsrltasv yqgggdildi ersvelggsl hakgvllmss
      661 flkahfgrsq ilhfsaalaf eqsygqvdgd satvaelsal isaisqlpid qswaitgsmn
      721 qlgqvqpigg vnakiegfyd acklqgltgk qgviiprqnm qhlmlrqdvi eavnngqfhv
      781 haietidqal eilmarpvgv ldkkgryskg siyaavmeql eywqaiedgd evedepkkkr
      841 kkkkktksed kkasedernt aqveesvavf pfakrkarrk ni
//
LOCUS       WP_004950316             232 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Acinetobacter].
ACCESSION   WP_004950316
VERSION     WP_004950316.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 232)
  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 232)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 232)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..232
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=25767
     Region          3..210
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Site            order(101..102,104,132,135..136,139..140,142..143,165,
                     168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          126..160
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          164..190
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mslsdeeqld slksfakkyg samisgilia liaffgweyw qkknlaesqn qtakvqklmd
       61 eakavagqpn afatvseaad kivkddadsv qaiqtqfila klayekqdya aaekalkkve
      121 nskvkdaglm qivkirlads qlaqkkydea lktlsnvsep afkatvdelr gdiyvakkdv
      181 esarkayqsa wnnvlerkqe rqllqikles vgvlvddpdf erpildtkvd es
//
LOCUS       WP_004951613             159 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acinetobacter junii].
ACCESSION   WP_004951613
VERSION     WP_004951613.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter junii (Acinetobacter grimontii)
  ORGANISM  Acinetobacter junii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Acinetobacter junii"
                     /db_xref="taxon:40215"
     Protein         1..159
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=17143
     Region          1..131
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mvkfnkgftl ieimivvaii gvlaafayps yqnhvrktkr vemqstlidl aakiqrykia
       61 nykvkdatti digiassypl qgqalydvtl spltsgalss eawtltatpk tgtsqvgtga
      121 itlnyqsikc wyegkdtpsl vettdadgnd vppdtctaw
//
LOCUS       WP_004952735             416 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Acinetobacter junii].
ACCESSION   WP_004952735
VERSION     WP_004952735.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter junii (Acinetobacter grimontii)
  ORGANISM  Acinetobacter junii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Acinetobacter junii"
                     /db_xref="taxon:40215"
     Protein         1..416
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=47823
     Region          3..289
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          289..387
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mtvrffhtsd whlgqffynh srhyeheqfl awlleqikik qphalliagd ifdvinpssq
       61 aqkqlyqfla dahdlapqmq tlmiagnhds gyrieqvdpl lekynaktvg virwnedksl
      121 dldrlilpiy deqkqivawc ialpflrsae itgfnenttn sqnaiaylhq hliaeakrrk
      181 tddqalilms hahmqggets dserpiiign eealsttlfd deidyvalgh lhkpqkvgqd
      241 hirysgspip lsfseinykh qvlevtidpi ktgnqvefea iaipraiqlh kikgelndvm
      301 qrlknlpqgl iecidhreyv dieyhtatpp qpnlrqqfed alpkdryrlv risrqylsne
      361 tnaeseskis lepptpeklf qqiwekkgys adddvtkdfl slvaeaqkkl eddqtv
//
LOCUS       WP_004952893             220 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Streptomyces
            mobaraensis].
ACCESSION   WP_004952893
VERSION     WP_004952893.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces mobaraensis
  ORGANISM  Streptomyces mobaraensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 220)
  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 220)
  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   3  (residues 1 to 220)
  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   4  (residues 1 to 220)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 220)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 220)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Streptomyces mobaraensis"
                     /db_xref="taxon:35621"
     Protein         1..220
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=24273
     Region          23..212
                     /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"
ORIGIN      
        1 msaaepqppv ddepqhtpph itrvviaede alirldlkem leeegysvvg eagdgetava
       61 larehrpdlv ildvkmpvld gisaaeriaa esiapvlmlt afsqrelver ardagamayl
      121 vkpfsksdvv paiemavsrf telkalekev adlaqrletr klvdraksvl qtqygltepa
      181 afrwiqktsm drrmsmqqva eaviedarek kaakeqqqsq
//
LOCUS       WP_004923998             283 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AfsR/SARP family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_004923998
VERSION     WP_004923998.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            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="AfsR/SARP family transcriptional regulator"
                     /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=31274
     Region          1..253
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 meikllgtlt anfgddfwtp saakhrqvla llalrarrtv pvwelvdelw gdrpprsaqa
       61 tlqtymmqlr rgiaavcgig gpvrakeila tahggyvlna tpdqvdalqh eslvsaglaa
      121 arkrdhrlts ellnqalglw rgdvlfdvpl gpvlrvevlr lqesrlsafe icvaadlalg
      181 rgievlarlt elaaryplhe rfhlqlmlsq yqagrmwqal etyrrlhtrl vtelglepse
      241 avreahqrml rgdspapatv vgdwdwgmra elggeplhsr gpa
//
LOCUS       WP_004953049             356 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Acinetobacter].
ACCESSION   WP_004953049
VERSION     WP_004953049.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..356
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39961
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvkniek hfgafhalkn isldfpegel vallgpsgcg kttllriiag lesadggqvl
       61 legedatdih vrerqvgfvf qhyalfrhmt vydniafglr vrpratrpse aeikkrvtrl
      121 ldlvqlgfla drypaqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 tlhdelhits ifvthdqeea levadqiivm nkgdveqigs prevyekpat pfvfdflgqa
      241 nrfegehheg iirigddriq lpnhlqapqg kviafarpne lhihaqpqpn tvqatflrev
      301 wiagrviael qdrsgrtiei llsveeanlh qfrpnqtvwi saaqlhlfad pttqva
//
LOCUS       WP_004953067             407 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Streptomyces mobaraensis].
ACCESSION   WP_004953067
VERSION     WP_004953067.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces mobaraensis
  ORGANISM  Streptomyces mobaraensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  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 407)
  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   3  (residues 1 to 407)
  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   4  (residues 1 to 407)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 407)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 407)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Streptomyces mobaraensis"
                     /db_xref="taxon:35621"
     Protein         1..407
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42830
     Region          40..392
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(114..116,137..138,197,249,273)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mlllttalta galtlsacgs rdddkggdng dkggrkttvv igldapltgd lsalgqgikn
       61 sahlavtnan ksnevpgvtf elsalddqaq ptsgqqnatk lagdkkvvgi vgplnssvaq
      121 smqqvaqsnt valispantt pdltqgkdwk qdrrkrqfst yfrtattdev qgafggkyah
      181 dqikaktayv iddqktygvg laaafstqft alggkiagte hvnpedrdfk aivskakssg
      241 adlvfyggey paaaplsqql kesgvkaplm ggdgmysady iklnkksagd yatsvgkpve
      301 qldsakkfie dykaagykdr yeayggstyd atwaiiqavk avvadnggkl pdgarakvve
      361 alnkvkfdgv tgtvsfdkyg dttntmitay qvegdtwkar hsaefkr
//
LOCUS       WP_004953564             354 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter junii].
ACCESSION   WP_004953564
VERSION     WP_004953564.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter junii (Acinetobacter grimontii)
  ORGANISM  Acinetobacter junii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 354)
  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 354)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 354)
  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   4  (residues 1 to 354)
  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 354)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Acinetobacter junii"
                     /db_xref="taxon:40215"
     Protein         1..354
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40587
     Region          28..218
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          265..346
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mrdpfglfqe nisvsyahvl leiteaygie nqtvlnntgl vlsamkhada kmsahqwskl
       61 vvnalqltgn hrlgieyglk lrptshgalg faflscadve taltlcqqyf ctriqnftpe
      121 wtvdqdfvyv ylddvhpvrf gdeqqsaqlr sflveclifg aihflslfsk elieqsevfl
      181 dweesndyqc ielskvkihf sqkrnglrfp kfflncknkn adqvsfqqal lycendkgrl
      241 vkenirdlqk sirsellyns sngyptlpmi aerlnmsert lkrhlqaqgt tflqiladvr
      301 fteakkmlqh kqysiqdias ivgyeeatnf irafkktfge tpsqyrkrsv akss
//
LOCUS       WP_004953720             306 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Acinetobacter junii].
ACCESSION   WP_004953720
VERSION     WP_004953720.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter junii (Acinetobacter grimontii)
  ORGANISM  Acinetobacter junii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   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 306)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Acinetobacter junii"
                     /db_xref="taxon:40215"
     Protein         1..306
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33689
     Region          16..67
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msldatiwaw kaevesstqr lillsladra gedhkcypsi mrmvkdtkmn rktiikvldd
       61 leqkalikft gsivgngvkv yqllgvvgre deitstkkgt sgkkgtstnl gtgsnigtst
      121 engiststkn gtetsteigt qnlsrnlsle sknkngwlcl kklrdelaqa dpdcnpeeii
      181 katwfnrelg afekfnaekn lcddlliyhf adsllrnksk ydksqktens kitrkksegl
      241 sekqiglfaq rlskhpefss kfaepgegye qlaariavkl sdpvqakawe sylkqvglet
      301 slgaaa
//
LOCUS       WP_004956071             518 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Acinetobacter junii].
ACCESSION   WP_004956071
VERSION     WP_004956071.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter junii (Acinetobacter grimontii)
  ORGANISM  Acinetobacter junii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Acinetobacter junii"
                     /db_xref="taxon:40215"
     Protein         1..518
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=59269
     Region          4..441
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mplldwvnrn qaeetatqvp yhllkfeksy gdqhqakenl iiqgdnlqal kallplyggq
       61 vkcifidppy ntqsafehyd dklehaqwls mmyprlqllk ellaedgsiw itlddneahy
      121 lkvlcdevft rsnfvanviw qkkysiandh ktiapvhdhl lvyrksekwl rnllprtven
      181 nkqyrlnddk glfrpdnytc gktieerpnl yyeviqpntg ekiypkktav wrysyeqhle
      241 hvkndmiywg kdgkgkvpaf krylhnlknd givpstfwsf dfaghtdlsr keirnildst
      301 slvndfitak pelliskilh iatnpndivl dsflgsgtta avahkmgrry igiemgehak
      361 thviprlekv ilgeqggiss tvnwqggggf sfytlgssvf ddngflnadv kfkdlasyvw
      421 wletkfaliq tenfdnpflg ihegtayyll yngilgdrrp nggnvlttsv lnyldechah
      481 dgkrivigea srlsptrlea lniefkqipy slygnkak
//
LOCUS       WP_004957916             450 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Serratia odorifera].
ACCESSION   WP_004957916
VERSION     WP_004957916.1
KEYWORDS    RefSeq.
SOURCE      Serratia odorifera
  ORGANISM  Serratia odorifera
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Serratia odorifera"
                     /db_xref="taxon:618"
     Protein         1..450
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=49421
     Region          5..422
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mtheeaesav iggllldeag pqtfdvlatl apeafstrqy remyqvikql amsggavtpf
       61 vvadklgdgy eaiavtvssq awaragvksy aemvrrnhfv rqaesiitdt legiktarsg
      121 ddaigaiqql qgsiqqlsfg dngrvalhin dllrgvtdri dsrltgaegs gniltgieel
      181 dkitngfept nlvllaarps vgktefalnl iekitdqggg vlmfsmemsa iqiaerqiag
      241 aggfstsklk kpqelededw arisdgigrm tdrpiwiida snltveqicq daermksehp
      301 elaavfvdyl glikvnerqr hdlavgevsr slkrlamrnk tpvvalsqls rgveqrpnkr
      361 pvnadlkdsg sieadadlim mlyrdelyne nspakgiaev nvtknrhgpl gtvyrqfryg
      421 hflpidqiea erlskqqpeq kerrygrgka
//
LOCUS       WP_004960275             317 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Serratia odorifera].
ACCESSION   WP_004960275
VERSION     WP_004960275.1
KEYWORDS    RefSeq.
SOURCE      Serratia odorifera
  ORGANISM  Serratia odorifera
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Serratia odorifera"
                     /db_xref="taxon:618"
     Protein         1..317
                     /product="formate/nitrite transporter family protein"
                     /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=35023
     Region          42..294
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msdkpnlgld dekrgdkgev kveskeqeqg kaeievdeek lpsraaavhe qirmegekel
       61 erdwlallws avaaglsmga slmakgifha rlpddpsrff ienigytfgf vivimarqql
      121 ftentvtavl pimhkptpkn flilfrlwsv vllgnligtg laaeafiqlp lfddatrqaf
      181 tdlakevmqn speemfangi lagwiiatmv wmfpssgaak iwvivlmtyl vaiadlthiv
      241 vgsveilylv fsgalpwqdf fypfaiptla gniiggsfif alishaqirn dmsnkakarr
      301 eaerakaqrd adpankp
//
LOCUS       WP_004961292             283 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Serratia odorifera].
ACCESSION   WP_004961292
VERSION     WP_004961292.1
KEYWORDS    RefSeq.
SOURCE      Serratia odorifera
  ORGANISM  Serratia odorifera
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 283)
  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 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   3  (residues 1 to 283)
  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   4  (residues 1 to 283)
  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 283)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Serratia odorifera"
                     /db_xref="taxon:618"
     Protein         1..283
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32528
     Region          29..278
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <179..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 magqnyleri alnerfisfn rmnsgsanyf hwhqclemlf vsrgygiaiv dnqqytlrpg
       61 rlfifppfkl hkvfveqnda nhyhrttlhl ehtviehflq pfpqrraqfq rlcysqsnaf
      121 icdladcqlq vetvldrfnq ryltgshqle dvaflalemm aflpekegea lkisqgspar
      181 imqwveenyq hkfslahlaa dlgrsksyls rlfsretgst iqeylltrrv kracellrss
      241 dlaigqiaaa vgfadapyfi scfkkmlgqt plqyrkgatg lgd
//
LOCUS       WP_004962203             114 aa            linear   BCT 20-JAN-2025
DEFINITION  PilZ domain-containing protein [Acinetobacter junii].
ACCESSION   WP_004962203
VERSION     WP_004962203.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter junii (Acinetobacter grimontii)
  ORGANISM  Acinetobacter junii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 114)
  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   3  (residues 1 to 114)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 114)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Acinetobacter junii"
                     /db_xref="taxon:40215"
     Protein         1..114
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12480
     Region          2..114
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mqpqmmggii qvnipdkatl qasympfvqg gglfvptkqa vkmgqevfil atlpdqsqki
       61 pltgkviwis hkqthfkpqg faiqlagdkg vyyrteaeri ltgaksldrp sytm
//
LOCUS       WP_004964787             408 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Serratia
            odorifera].
ACCESSION   WP_004964787
VERSION     WP_004964787.1
KEYWORDS    RefSeq.
SOURCE      Serratia odorifera
  ORGANISM  Serratia odorifera
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 408)
  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 408)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Serratia odorifera"
                     /db_xref="taxon:618"
     Protein         1..408
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46969
     Region          1..405
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mpipqislaa arslhlaaqg llvpskrkar pddviaairr mgllqidtis vvarspylvl
       61 fsrlgayspe wleqalagrq lfeywaheac flpiedfall rhrmldpqgm gwkysqawvd
      121 khqtaiddll ayvaeqgpvr sadfnaekkg sngwwdwkpe krhleilfta grlmvaerrn
      181 fhrvydlter llpdwhdatq alpaaaaree mltrscrylg ifkpewlady yrlkrvspqk
      241 lldrltrade impvqvsgld gtcyvhhsla qqlalaqqgk lkssvttlls pfdpvvwdrr
      301 raqqlfnfey rlecytpkek rqygyftlpv lqrgeligri dakmhrrkae fevisfhtep
      361 qvrmgrqrcq dvfqaierma kwhgatrvtl geipasvrse wgsgwdvg
//
LOCUS       WP_004971622             707 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Acinetobacter].
ACCESSION   WP_004971622
VERSION     WP_004971622.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 707)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..707
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=80153
     Region          462..696
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mgsikvrnpl lskklkrtet rlliiddnqi rfnqiceqlt anehrvqayl lddiknfekq
       61 lhltwdlvif graydlkvdq altlirasqq pnlpllllkp ddydatqyts yvrkgiydii
      121 nldyperfyf gliralsfsr lqqsqeqlmt elenaqsqaq alvedsskav aiiqegihaq
      181 anaeylqlfg lkseddligl plldllqpqd itdfkfrfkk vsqgqfehgr fdihsqnpll
      241 akqnplkief vgaaddaiqi tidientaqn tvpaqttadk aaakpstyql vnrtlakqps
      301 sanalvvfsl ancpesifqa dwqttknyft niqnflkeqt nvplfnvsng lvvglfqaes
      361 pailesklig lnsltkpqll tvdqhtypln lrigyvpftp diqnessfeq lisqgfanal
      421 pqqqeqhnsg ltldlsfges nlnviesaaa vpqsysesai iaairqsldr geihlkyqql
      481 ydkqdtnlyt yevtsgfifn sewksltgli dlaedpelsi kldrwilvea ckqlhnfitq
      541 ypeakliinl nkfvllqdrs fpefvsklit iigsrlshpl ilqfseedis qnlgdaqkqi
      601 sllrqhgaei slrdfghsiy sesilkqvdi hyltlhsalt eklaaddstq elqeqlsiys
      661 eikpvevllr dlndmnlfan awnvdarfiq gdyfqkkldh lidvqdq
//
LOCUS       WP_004972177             111 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Acinetobacter].
ACCESSION   WP_004972177
VERSION     WP_004972177.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..111
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12240
     Region          8..110
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(32,63..64,66,93)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(32..33,41,44,46..47,49,52..53,55,63,68,75)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mqttlsrkps delahmilnv vclipagqva tygqvarlag lpkharlvgy vlrhlsaeht
       61 vpwhrvinaq gkislsklna qgeniqtlkl qeegivviae kvnlkqyqwq n
//
LOCUS       WP_004974378             333 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004974378
VERSION     WP_004974378.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 333)
  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   6  (residues 1 to 333)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..333
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38994
     Region          46..202
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          92..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mqqfkeytgs vygglghllm cyyqakklpi peklhqiqnl erfdyalwrd llstleqqlp
       61 qpalgleiak yvqpkhlgii aylalscdhl gealqryhdf hrliydggpl qveaqndyls
      121 irwselpvhm ttqltdeiai almmeflkhf mqfediclhe vhfhhpapkn ialyeqyfhc
      181 kvrfsqpitq vllpvselak pfhqgdqtlq hlllqqaqal leklpnstqt dqrlqqailt
      241 glqknmyqie hiaqqlhisv rqlqrhlqqq gttyqkrmqe vrcllaeqyl qdphlslqei
      301 alllgyseqs afqrafkqwt qhtpqqwrmq ras
//
LOCUS       WP_004974505             153 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Acinetobacter towneri].
ACCESSION   WP_004974505
VERSION     WP_004974505.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter towneri
  ORGANISM  Acinetobacter towneri
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Acinetobacter towneri"
                     /db_xref="taxon:202956"
     Protein         1..153
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=15764
     Region          4..150
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mdcielmivv aiigilaava lpayqdytvr akvsevvlaa sqcrttvtet vqsavgatlp
       61 aagdwgcesa sqttkyvdsv atdnkgvitv taknidqlgs gknqltlipy kdantalang
      121 dvgvtvygwk cgdssagtti pqkylpgscr gqf
//
LOCUS       WP_004974525             153 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acinetobacter towneri].
ACCESSION   WP_004974525
VERSION     WP_004974525.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter towneri
  ORGANISM  Acinetobacter towneri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Acinetobacter towneri"
                     /db_xref="taxon:202956"
     Protein         1..153
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=16446
     Region          5..130
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkvgkqygft lielmivvai igilaaiayp syqeytrktk rvdaqaemvn iagqlqryki
       61 vnfkflksdg taielddigi seqlppsgta lynlalsnvt agtwtltatp igaqtgdghl
      121 vlnhrgekcw tkgsdknsgs pcmpsattnw dgh
//
LOCUS       WP_004950786             408 aa            linear   BCT 20-JAN-2025
DEFINITION  threonine synthase [Streptomyces mobaraensis].
ACCESSION   WP_004950786
VERSION     WP_004950786.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces mobaraensis
  ORGANISM  Streptomyces mobaraensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  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 408)
  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   3  (residues 1 to 408)
  AUTHORS   Parsot,C.
  TITLE     Evolution of biosynthetic pathways: a common ancestor for threonine
            synthase, threonine dehydratase and D-serine dehydratase
  JOURNAL   EMBO J 5 (11), 3013-3019 (1986)
   PUBMED   3098560
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10107605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces mobaraensis"
                     /db_xref="taxon:35621"
     Protein         1..408
                     /product="threonine synthase"
                     /EC_number="4.2.3.1"
                     /GO_function="GO:0004795 - threonine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009088 - threonine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42780
     Region          85..403
                     /region_name="Thr-synth_1"
                     /note="Threonine synthase is a pyridoxal phosphate (PLP)
                     dependent enzyme that catalyses the last reaction in the
                     synthesis of threonine from aspartate. It proceeds by
                     converting O-phospho-L-homoserine (OPH) into threonine and
                     inorganic phosphate. In plants; cd01563"
                     /db_xref="CDD:107206"
     Site            order(103,108..109,126,149,165,168..169,175,191..197,
                     199..201,213..214,245,359..361,362..363,400)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:107206"
     Site            order(132,158,259..263,398)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:107206"
     Site            132
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107206"
ORIGIN      
        1 mrfpadgpsg pfhphtpygp sasadaydpd apcgtirlrc gtcgrlhala epawrcadch
       61 glldlhgftp ampnavelgr rpptlwryae alplprppri slgegmtpli sapgrpdvll
      121 kadhlmptgs fkdrgavllv alaarlgvrk vmadssgntg tavaayaara glacevyvpa
      181 atsegkvaql raygaevrri egsredtaae aaraaeepgt fyashvhhpf fphgtktyvf
      241 elweqlggrl pgtlvlpagn gtlvlgarlg cqelldqrli drlpaitavq aagcaplara
      301 aalggevper vtaeptvaeg iaiarpargs qvlqavretg gtfvtvpedr ivaahrelar
      361 hglyveptsa vcwaalqegl vpehavegdr pfavvplcgn glkgkppe
//
LOCUS       WP_004976104             335 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004976104
VERSION     WP_004976104.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 335)
  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 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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 335)
  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   5  (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   6  (residues 1 to 335)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38291
     Region          22..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <137..335
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mgqltdasvv lrlgyqairr aglptedilt kagvalnqve anertplnaq yafwvaaeev
       61 skdpdiglhl gehlplyrgq viehlfisse nfgeglkral ayqrlisdaf daklvvedgr
      121 cyltngvqpw senivnrhfs ecamsgvlrf fkfitegrfq piyidfnfsd gaaddeyfrv
      181 fecpvslgqk etrlyfdpsi ldyplwqaep ellqlheqla leklqelary dlvgevrrai
      241 gstlesgett letvaaqlni tprrlrtqls eantsfqqil sdyrcrlakr llsntnesve
      301 rivyltgfse pstfyrafkr wtnetpveyr krkqr
//
LOCUS       WP_004978057             176 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Acinetobacter johnsonii].
ACCESSION   WP_004978057
VERSION     WP_004978057.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter johnsonii
  ORGANISM  Acinetobacter johnsonii
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Acinetobacter johnsonii"
                     /db_xref="taxon:40214"
     Protein         1..176
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=17354
     Region          2..150
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mnaqkgftli elmivvaiig ilaavaipay qdytvrakis elivagssak saisegfqtn
       61 gmdgvksaaa svakgttaap vskylksvaa sdagvitltt tsdaslpsda rgktiimspy
      121 araagtagan aalaagaags vewacasatn vqavarlstl tatgdlpaky apsecr
//
LOCUS       WP_004978173             625 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Acinetobacter johnsonii].
ACCESSION   WP_004978173
VERSION     WP_004978173.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter johnsonii
  ORGANISM  Acinetobacter johnsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 625)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Acinetobacter johnsonii"
                     /db_xref="taxon:40214"
     Protein         1..625
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68893
     Region          2..625
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mqstakkaal pamtlaalgv vfgdigtspl yalkesfhaa hglgitpanv lgilsiifwt
       61 mtmvitikys aivmradnng eggimallal nlrntnfshr kklllisigf igaslffgdg
      121 iitpaisvls aveglsiatd aldpyivpia isivtavfvm qkygtafvgk ffgpltllwf
      181 fslgllgiss iiqtplvlgm lsphwafqfi vtnplmaffi mgavvltvtg gealyadmgh
      241 fgpvpirlaw fivvlpclll nyagqgalll rdptaienpf yllvpewgly pmiflatmaa
      301 viasqavisg vfslarqaiq lgylprlnvk htsdseqgqi yvpllnwill asiivlilif
      361 qtssqlshay glavtmtmlc dtlliavfir ytwkwsmpkl vlliipflvl dlvlvsatsl
      421 kvlsggwvpl liggiafmll mtwkqgrelt faklqqdtlp ldlfvqsige qanwvegeav
      481 fltgtptvvp hamlhnmkhn kvlhqkniil tvkiqdvpyv eesnrfhvet mnqhfyrlel
      541 yygfkdemni pqaleavyqa idleynlmqi sffvsrerii stvgdgmapw reklfismqr
      601 ntspvsdfyq ippnrvvelg sqiei
//
LOCUS       WP_004979182             142 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Acinetobacter johnsonii].
ACCESSION   WP_004979182
VERSION     WP_004979182.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter johnsonii
  ORGANISM  Acinetobacter johnsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Acinetobacter johnsonii"
                     /db_xref="taxon:40214"
     Protein         1..142
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15971
     Region          1..142
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mmwalgllfl safgaatllp lqseavlvgl laqtqysvwl lvavaslgni lgscvnwwlg
       61 lkveqyknnk wfpvseqkml qaqgiyqkyg fwslllswvp vigdpitlia gllkenfvrf
      121 vvmvsiakig rylfvywmfs qf
//
LOCUS       WP_004978816             256 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Streptomyces viridosporus].
ACCESSION   WP_004978816
VERSION     WP_004978816.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces viridosporus
  ORGANISM  Streptomyces viridosporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces viridosporus"
                     /db_xref="taxon:67581"
     Protein         1..256
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25820
     Region          <112..>254
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mnrnratvsa vavtlltvgl avgpaaavpa aeakarvgad watqsivfta aagqtndlni
       61 fsmytsdgir rigfsdvvpl kpgdhcaysr pedttsvvce lpadssrpdr idvflgdgnd
      121 tiaaftpgig tvsggpgdde lhahtartvr gdagndmvmg pavlhggdgm dhlmgdssnq
      181 qmwggrgddm iegyggddtv hagpgddham ggdgrdivlg gpgndtldge ggddlvsggp
      241 gkdtveggpg rnivlp
//
LOCUS       WP_004980012             829 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Streptomyces
            viridosporus].
ACCESSION   WP_004980012
VERSION     WP_004980012.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces viridosporus
  ORGANISM  Streptomyces viridosporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 829)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 829)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 829)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..829
                     /organism="Streptomyces viridosporus"
                     /db_xref="taxon:67581"
     Protein         1..829
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=90273
     Region          43..780
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mvasvdrial pwgsrtpygr hgswperqdi clregvdpdt vqrwvqaasi lhsdgdamdi
       61 avvdgrmagv rgrtqdrvnr grlgpkdlfg wqanaspdrl trplvrrdgq lvecdwatam
      121 driatrsrel lhergpgsig fytsgqlfle eyytlavlar agigtnhldg ntrlctataa
      181 ealkesfgcd gqpgtyddid hadvialfgh nlaetqpvqw mrildrlegg dpprllcvdp
      241 rptrparaat vhlaprlgtn valfnallhe iirtdrvdhd yveahtvgfe elasrvedct
      301 pewaaricdv paarigeaae llgtadrlls tvlqgvyqsh qataaavqin nlhlirgmlg
      361 rpgagilqmn gqptaqntre cgangdlpgf rnwqnddhva dlarvwnvdp etiphyappt
      421 hamqmfryae qgsirmlwis gsnpavslpe lsrirsvlaq drlfvvvqdl fltetaqlad
      481 vvlpaatwge ktgtftnadr tvhlsdkavd ppgearpdld ifldyaarmd frdkdggpli
      541 twhdpesafe awkrcsagrp cdytglshdk lrggsgiqwp cnerapegtd rlytdgiswa
      601 hpdvcetygk dlvtgaaddv veyrslnpdg kamlkaasyl ppheapdaey pfqlttgrtl
      661 yhfhtrtktg rapqlneaap dvwveaapsd asalgldegd lvevatprga lrgrlrvtdi
      721 rpgllfvpfh ygywdtgggh apdggtpgra anettvtdwd paskqplykt aaaalrrver
      781 gdgrpapapt ttasapsrag tvpdtvggps alvtesvgap pdrrkeqpe
//
LOCUS       WP_004980013             338 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004980013
VERSION     WP_004980013.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  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   4  (residues 1 to 338)
  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 338)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37917
     Region          27..201
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          250..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 miplahtavl knylnvsqqf nfnpyyllsn aglnpaqlnd pkqripvdka ialleqsaei
       61 sgcevfgllm aeqrqiadfg elslllsyqh tlrdalqtiv myrnfinnal emyieeagnt
      121 viihlevvga steysrqaie lalgvthrfc amllsqkwrp lgvhfthsap qnlaihqrvf
      181 gcalefgsef ngivctvael dkanpqanta madhakryld idllqnenes siifdirksi
      241 ylllpmgrat idqvanlhgi nvrtlqrrle asqtsfsilt ndvrralvfr ylqnmnyslg
      301 qvsdilgysm pssftrwfig qfgvsplawr ndhkgath
//
LOCUS       WP_004980430             215 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Streptomyces viridosporus].
ACCESSION   WP_004980430
VERSION     WP_004980430.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces viridosporus
  ORGANISM  Streptomyces viridosporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Streptomyces viridosporus"
                     /db_xref="taxon:67581"
     Protein         1..215
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=23182
     Region          <109..194
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mlkttvrgll aaallilpla tpasaapvsl pladavaalp tadesregys rdqfrhwvds
       61 drdgcntrme vllaeslvap mvepgcrvta gewlsyydgv tvtvpsgldi dhvvplaeaw
      121 dsgasawtaq rreayandld aerslvavta rtnrskadqd paewlppntd ahctytvdwv
      181 stklrwgltv ddteratler laagcddtve yepap
//
LOCUS       WP_004981183             670 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter permease [Acinetobacter].
ACCESSION   WP_004981183
VERSION     WP_004981183.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 670)
  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 670)
  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 670)
  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 670)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..670
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..670
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=71969
     Region          15..663
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mtqneekvap eqldeqqqqa ilekfdresv trspsnksva wfiaaiaify slfhlfitfn
       61 plpeliqrsa hvaiglvlif llyparqsss rqsipwldwl laltalatfl ylwkeyqaim
      121 ttrggipntl divfailavv lvvegarrvm gwmlpilglv flsypffshy dwvpdrlltr
      181 sysisdifgq mylkteglys saigasvtfi flfilfgafl aksgmgklfn dlamalaghk
      241 qggpakvavi ssgfmgsing tavanvvgtg sftiplmkki gyhknfagav easasvggqi
      301 lppvmgasaf imaettgvsy gtialaatlp allyylgvma qvhfragkdn lkgvpkadlp
      361 rvkdvlkerg hllipivalv fflfqsipvs yaavytivlt vivasfrkst rmgfkeilea
      421 ladgakqsls vmaacavvgi iigvvsltsf gsvmtssims igagslfltl fftmiasmil
      481 gmglpsipay iitatmaapa lanfdiptlv ahmfvfyfgl fanitppval aafagagiag
      541 gdpmrtgfqa lklslagfiv pflfvynpam lmidtanvav narefafpaw ttivsivfts
      601 vvgilalgaa vegyfkvgln wfwriflgag alcmiipetv tdiigivmvv iaisinlmqa
      661 kkqnqsysls
//
LOCUS       WP_004981319             339 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter johnsonii].
ACCESSION   WP_004981319
VERSION     WP_004981319.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter johnsonii
  ORGANISM  Acinetobacter johnsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 339)
  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 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 339)
  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   4  (residues 1 to 339)
  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 339)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Acinetobacter johnsonii"
                     /db_xref="taxon:40214"
     Protein         1..339
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37959
     Region          21..202
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          249..331
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mgsyiraasl ggfedlvrsy ginpieilke igilpallrd pdsfihydhy lnllekaala
       61 cqddcfglkl galqnistig ligvymsrqt tilealsvaq kyvylhaegi vfhvsqhnal
      121 lcklnfvrls eyntdvpqks qlaiclvani lkdligpqwh aekicfkqka pqkgaqtfqa
      181 hfscpvefet dedalyfpas flsykpynfn edainqlivq qletqsstkt enntaliess
      241 vrmlmatgdc sienialcmg mhpkklqral kmqgttyrdi lenvrkkeal rmldagnvnl
      301 tdialqlgya elsifsrnfk swfgvpptel rdksrshiv
//
LOCUS       WP_004982674             277 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            viridosporus].
ACCESSION   WP_004982674
VERSION     WP_004982674.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces viridosporus
  ORGANISM  Streptomyces viridosporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 277)
  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 277)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Streptomyces viridosporus"
                     /db_xref="taxon:67581"
     Protein         1..277
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29032
     Region          19..89
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          200..255
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 msignspede rpfedvseea rpsvgralqq ariaagltvd dvstatrvri aivhaieadd
       61 faacggdvya rghirtlara vnldpaplia qyetehgngr paptpaaplf eaerirperr
      121 gpnwtaamva aivvvigfvg ftmvkggddg gkenvadgta stesasptpk aekpavpepe
      181 psdsaiaaap qdkvtvqvsa vdgrswisak dhngrllfdg llkqgesktf qdsskinlvl
      241 gdagaidlfv ngkkieddfq pgaverltyt kgdpqag
//
LOCUS       WP_004983711             285 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Streptomyces].
ACCESSION   WP_004983711
VERSION     WP_004983711.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..285
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29652
     Region          1..253
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mridlhthst asdgtdtpad lvrkagaagl dvialtdhdt trghaealaa lpagltlvtg
       61 aelscrldgv smhllaylfd peepallaer elvrddrvpr aqgmiaklna lgvpvtweqv
      121 ariagdgsvg rphvaaalve lgvvptvgda ftqewladgg rahvekhetd pfealrlvkg
      181 aggvavfahp aaskrgrtvp esaiaelaea gldgievdhm dhdpgtrarl rglaqelgll
      241 vtgssdyhgs rktcvlgeft tdpevygeit rratgafpvp gaggv
//
LOCUS       WP_004985142             202 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acinetobacter ursingii].
ACCESSION   WP_004985142
VERSION     WP_004985142.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter ursingii
  ORGANISM  Acinetobacter ursingii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Acinetobacter ursingii"
                     /db_xref="taxon:108980"
     Protein         1..202
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=22417
     Region          12..>117
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mrkmpiitiv lrsksyqygf slielmvvia ivaifaaiai psyqiyvrka dvasaqqemq
       61 riaeqlsrhk arnfsykgfd gsylykdkvg tlnpnfdatk qelkipidss rskytltimg
      121 sstdekgdtd psndvitqtl ltntgltnlg qswsikaesn tvtnpsnydl litstgircm
      181 nknkakvtyq tcgtkddgse qw
//
LOCUS       WP_004986056             347 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004986056
VERSION     WP_004986056.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 347)
  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 347)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 347)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 347)
  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   5  (residues 1 to 347)
  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   6  (residues 1 to 347)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..347
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40360
     Region          40..202
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          79..329
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mqrtfyhiks vssnlmrlle lfcdqhdltl pdrvkdyaln ervpfsewlf llnyieqqyp
       61 vpalglkiae lvkpehlgim ayiglssdnl tqalssflqf qrlsydfmdv svkchdneli
      121 iswefdpyfk agavadetmi aiffnlvnql iypnriainr iefvsaspkn pqlyesyfnc
      181 pvefshnktn myfplsnlnl tvpsadpvln qiliqqadil lqelpecnsf devvqraiiy
      241 avhqgkisie yvaqqlgyts rmfqyklkqq gytfkqrlnq vrkelaigyl adpslsildi
      301 slllsyqeqt sfnrsfknwt gmsplqyrrv ildeffeeqd npwnlmv
//
LOCUS       WP_004986081             279 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Acinetobacter].
ACCESSION   WP_004986081
VERSION     WP_004986081.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..279
                     /product="formate/nitrite transporter family protein"
                     /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=31225
     Region          30..279
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msaeekeqek etdntltwre kmaieehekl sprlvyeiir kngveelerp tkalifsgit
       61 agivisfsfv fksllnaylp dakwaflien mgytvgfvlv ilghmqlfte ntiatvvplf
      121 knfslkklka vfrlwgivfi snligtalaa ffllnphlfd adlmqsfdql ahhvasftis
      181 eniikgipag iliaslvwil psannkflli ffitylmalg gfthvivgsa emaywvfkgh
      241 atfseyifqf llpttlgnii ggtgvftlli ygqvneele
//
LOCUS       WP_004988974             194 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Streptomyces
            viridosporus].
ACCESSION   WP_004988974
VERSION     WP_004988974.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces viridosporus
  ORGANISM  Streptomyces viridosporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 194)
  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 194)
  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 194)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Streptomyces viridosporus"
                     /db_xref="taxon:67581"
     Protein         1..194
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21022
     Region          101..187
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(120,139..140,158,161,169..170,180,185)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mattrslssa psaplaapap erpryrlrav drddvatvad llppgatwlp apqhslpalp
       61 grppmvgylv lvpadqqppf pvaapepags agagpdddpl irvdtdrrta evdgrqldlt
      121 ylefellahl vahpgrvhtr ehlvgtvwgy ghvgdgrtvd vhiarlrrkl gpryrdtirt
      181 vrrvgykylp ptgr
//
LOCUS       WP_004989881             353 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Acinetobacter].
ACCESSION   WP_004989881
VERSION     WP_004989881.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..353
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39624
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvkniek hfgafhalkd isldfpegql vallgpsgcg kttllriiag lesadsgqvl
       61 legndatnvh vrerqvgfvf qhyalfrhmt vfdniafglr vrprttrpne aeikkrvtrl
      121 ldlvqlgfla drypaqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 tlhdelhits ifvthdqeea levadqiivm nkgnveqigs prevyekpst pfvfdflgqa
      241 nrfdaehhng tvhigenkii lpvtahapqg kviafarpde lhihaqphen sieaifvrei
      301 wiagkviael qdrqgrliei alspeearqh qfrpnqsvwv sasqlhlfad qva
//
LOCUS       WP_004991305             264 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: hydroxypyruvate isomerase family protein
            [Acinetobacter].
ACCESSION   WP_004991305
VERSION     WP_004991305.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..264
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29835
     Region          1..257
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 msqlavnlsl iftevplier falarqygfq hveiqfpyel sihqireqle qhhlslclin
       61 vptgdlmqgg nglagipgke iefhqaleqa iqyasaldvp rinilagkqp ldadllpcln
      121 tlasnlklac hlmtehgiep vfemingtdm prflvqniaq aqemleavqh palkmqydcy
      181 hlammgedvl eglkeninqi ghiqfadcpg rhepdtaeln faqifqwlqh sqyqgyiaae
      241 ykpqytsaqs fewknkyfsn dvnt
//
LOCUS       WP_004991732             169 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Acinetobacter ursingii].
ACCESSION   WP_004991732
VERSION     WP_004991732.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter ursingii
  ORGANISM  Acinetobacter ursingii
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Acinetobacter ursingii"
                     /db_xref="taxon:108980"
     Protein         1..169
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=17377
     Region          2..169
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mnaqkgftli elmivvaiig ilaavalpay qdytarakvs evvlaastcr tavseasqtg
       61 faatptannt fgcgeggssa splsqyvesi tttkdgvitv karqisqlgs nvnvdfipwt
      121 vatipasgtt gqavaadfnr aslnvikawq cksgrsngie akylpascr
//
LOCUS       WP_004991892             333 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter ursingii].
ACCESSION   WP_004991892
VERSION     WP_004991892.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter ursingii
  ORGANISM  Acinetobacter ursingii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 333)
  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   6  (residues 1 to 333)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Acinetobacter ursingii"
                     /db_xref="taxon:108980"
     Protein         1..333
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39060
     Region          <64..193
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          82..330
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 maliknyags iygglghllk lycesqhlvv psklleiqnl erfdyviwrd lleqiqqlqp
       61 qtglglriak yvqpkhlgil aylalscesl gealhryqdf hrlvydgspl kvefvspyfs
      121 ihweepelhp tqltdeiaia lmveflqqfm ckekielyev hfinsapkdl hmyeryfhcr
      181 vrfsqaktqi lipiseankv ignadhtlqq llmrqaqell qelphsnqld qrlqqailkg
      241 lqkneyqidq iaaqlglsvr qlqrhlqqqn mtfqqrtqqi rymlaleylk dphlslqeia
      301 lllcyseqsa fqrafkqwsg ltpqqwrqqy vhh
//
LOCUS       WP_004992456             336 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_004992456
VERSION     WP_004992456.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 336)
  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   6  (residues 1 to 336)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..336
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38474
     Region          22..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          94..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msrdtisihf vnaaltgvkr lgmdvetlls hvgieaellr qpkarispeq ytrfikmlwm
       61 vtqdehvgfd vqprrlgtfa imcqliihak tlgealdlss qfyklfgdew svtlerdkhe
      121 arlvpmipks ldpdhfites mlmiwhglas wlierrlple rvhfgyprpa hadeydalff
      181 apvmqfdmpr teitfaadyl dlpirqnekt leeflkaapa qllvkfkntn sltsrirdvl
      241 ksqigeempt lndvasmlyl spqtlrrrla aegksyqgvk dalrrdaaih lllnpdltle
      301 dvaqqvgfse tstfhrafkk wtgvtpglyr qlhgyh
//
LOCUS       WP_004992644             399 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Acinetobacter].
ACCESSION   WP_004992644
VERSION     WP_004992644.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..399
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43517
     Region          5..389
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mstsvlvinc gsssikyalv sdrrenriyg laenlgtaea rikgitvgge plelsiphad
       61 hekaletlla rlanykpqai ghrvvhggtl tkaelltpei ierivaatpl aplhnpahlv
      121 gidatmrlfp elpqvavfdt afhqtmpeha yryalpkffy tehyvrrygf hgtshayvsd
      181 raselagqfr qggwlsahlg ngsstcaiwn gesidtsmgl tplegivmgt rsgdvdpsih
      241 sfiannlgwd idkidkmlnk esgllglsdn lsndmrtlie asengnedar laievfsyrl
      301 akslaglscg lpkidglift ggigensayi rektmiylph fgfkldkdqn ntlqrgtegr
      361 idvgqgpqiw viptdeegri aketeqvvqq akkldvvig
//
LOCUS       WP_004992678             260 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Acinetobacter].
ACCESSION   WP_004992678
VERSION     WP_004992678.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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
REFERENCE   4  (residues 1 to 260)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..260
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28373
     Region          24..91
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          188..249
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 meinpnsqqp tgsssptsal gnvqrpgeyl rqirlaqkle lndvasdlnm plkaltaleq
       61 ddykslpepa fikgyyrsya kylktdatai iqrfdeiyan dtgllpnhal nnspikimgk
      121 lpgsksdrnr kwlkrslili lalivigviv tmlqnwsakk tntvtpqnsn vevlplnnga
      181 atsgdelvln fnrptsihiv dstgkvlatg rqasaltlng qspfqirldd atavslslnq
      241 epislspytv ngkadfrlsr
//
LOCUS       WP_004992966             390 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Streptomyces viridosporus].
ACCESSION   WP_004992966
VERSION     WP_004992966.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces viridosporus
  ORGANISM  Streptomyces viridosporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Streptomyces viridosporus"
                     /db_xref="taxon:67581"
     Protein         1..390
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41789
     Region          1..282
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          280..364
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkflhtsdwh vgkvlkghnr ldeqrtvlre ivrvardhrv davlvagdly essapsaqaq
       61 qllvqtllal rrtgaeviai agnhdhaatf dayrplmasa gitlagtarp aadggvveft
      121 arstgepvav allpflarrh avraaqlvte tpreaatgyg rlvrdllaal tagfrddtvn
      181 lvmahltaag gklgggersa qsvleywvpt safppdahyv alghlhrrqs lpapcpvhyc
      241 gspitldfge endstvvlvv eaevgtptrv taevpigsgr rlrtvrgtvd evtrraeefg
      301 ddylrvllce paraglrqdv qrllpnalev ridpgfaapv httgpsppad gadrspaelf
      361 hayciargia dervealftr lhdqatatha
//
LOCUS       WP_004993088             575 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Streptomyces
            viridosporus].
ACCESSION   WP_004993088
VERSION     WP_004993088.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces viridosporus
  ORGANISM  Streptomyces viridosporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 575)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Streptomyces viridosporus"
                     /db_xref="taxon:67581"
     Protein         1..575
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=60097
     Region          3..560
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mmvhpellra ariarrpllg atallgavav thlaqavlia lalariarge vsglpallaa
       61 vltavavrav lghrqcvlav ragarvrigl rdellerlaa lgplggtdnr agavratlvd
      121 gvegvdayvs rylpqllvtc vlplpllaav aavepyalla ltpalllalf aprwwdglla
      181 rrgqehwgsy ealsadylea lqgmpalraa gavartrarl eersaalhra tvaklrvslv
      241 dtgitdlavq ggtvaaalva casaasgrta atgtylvlml asecfrpvrd lsrawhaghl
      301 glsaadgitk lrtaqpavrd dgtepaphqp peirfddvhf typgaarpal rgitftadag
      361 httavvgpsg agkstllall lrrwdpdggn itldgtdhta ltlaslrrgi avvsqetylf
      421 hasvadnlrl arpdatdeel yaaagaagvh deitrlpdgy dtqvgergat lsggqrqrla
      481 larallagap vlvldeatsa vderresrig rellraargr tclvvahrla svrdadrivv
      541 ldggridgvg thtsllaqdg lyarlvaagr vqeaa
//
LOCUS       WP_004994314             173 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Acinetobacter ursingii].
ACCESSION   WP_004994314
VERSION     WP_004994314.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter ursingii
  ORGANISM  Acinetobacter ursingii
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Acinetobacter ursingii"
                     /db_xref="taxon:108980"
     Protein         1..173
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=17637
     Region          2..145
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mnaqkgftli elmivvaiig ilaaiaipay qdyttrakvt emlsvassak tsisegfqsg
       61 giigvnavva dinnkktqaa ntskyvakve atvdtgviti tsskdnslps taqgmtlklt
      121 pyqgtaglsk atvstgaplq wacssegttt akarvstvta gtmpakfvps eck
//
LOCUS       WP_004994630             500 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: replicative DNA helicase [Candidatus Phytoplasma].
ACCESSION   WP_004994630
VERSION     WP_004994630.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phytoplasma (plant yellows agents)
  ORGANISM  Candidatus Phytoplasma
            Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Acholeplasmatales;
            Acholeplasmataceae.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Candidatus Phytoplasma"
                     /db_xref="taxon:33926"
     Protein         1..500
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=58332
     Region          21..486
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mltneqkalk qiitylnqnk keqlefyfdl idpqwfcepq hrqifqalky ltlektslpp
       61 vdqspssaal isqlltylqt hfpqdhftnt slaflnddlf eennldcltn lkhtytqekl
      121 fqqllkiikp tfdhpdpyhr hlysqeifak lrkfmawiph qsdqtlftip qmatvhpeff
      181 ktdrqaqeti raeyyrlsen frglnqttng fkkgqvitig gytglgktsf vyhllldisq
      241 tkwqetthyp yilvfsyemt laenlsrfla nltqiplevi ftknweetgi spalytermr
      301 iakpflnnlk itfsydptkn idyvldlvyr rhleqqieiv vidhlqitka thhlendrla
      361 ideimtklkk lavelkivvi ilsqfsrdty hnysgkspai talkgsggie tnsdlvlmma
      421 efqpklsktr ekpfniyncd cqqlyatarg hesqkiiela ikknrsgakk dllyhfemtt
      481 qtfqeigyvs pyaedddedd
//
LOCUS       WP_004998042             196 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Acinetobacter].
ACCESSION   WP_004998042
VERSION     WP_004998042.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 196)
  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 196)
  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   3  (residues 1 to 196)
  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   4  (residues 1 to 196)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 196)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..196
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22501
     Region          1..191
                     /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"
ORIGIN      
        1 msklkialid ddferaefvq qnlrahdfdv vacltlehln dfqleqlqad villdmdhph
       61 rdliencvsh fdlptvlftk nthkdtikqa iaagvtayiv dgidparldt ileisieqyk
      121 khkqlesdlk etklkladrk diekakvllm qlhhlaedta fqllrknams hritmgdmar
      181 rlidaqqllh hplked
//
LOCUS       WP_004998260             344 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter ursingii].
ACCESSION   WP_004998260
VERSION     WP_004998260.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter ursingii
  ORGANISM  Acinetobacter ursingii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 344)
  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 344)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 344)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 344)
  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   5  (residues 1 to 344)
  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   6  (residues 1 to 344)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Acinetobacter ursingii"
                     /db_xref="taxon:108980"
     Protein         1..344
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39669
     Region          43..210
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <229..344
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mqriaqsnis psnkgtisia lvnealsvah srgfniekiv qpagisaell nfpkaripvs
       61 ayaqlwiela nhmddeffgm dshpmrrgsy qllakmvmha dtiekaltdi lkffsvlldd
      121 iqaefkveqn lacliihdqt htkrmfsyat flmlihgllc wladqrivid kislkcakpa
      181 ypqdyyvrfc eniefdaasn rvefnadylq ikikkdkksl yeflkqtpqn llvryknena
      241 lslmirrhli khhpalwpel kelsqqlnms eatiqrrlka enisyqqlkn dircdiaier
      301 lsktedciqd isdalnfhdp safyrafkkw tgvnpsayrt rslk
//
LOCUS       WP_004999155             194 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Nitrococcus mobilis].
ACCESSION   WP_004999155
VERSION     WP_004999155.1
KEYWORDS    RefSeq.
SOURCE      Nitrococcus mobilis
  ORGANISM  Nitrococcus mobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Nitrococcus.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Nitrococcus mobilis"
                     /db_xref="taxon:35797"
     Protein         1..194
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21716
     Region          4..162
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mrhlfsrlys atrygaghpr apwflaalsf aessffpvpp dvmlapmvlv qprravhfav
       61 lttlasvlgg llgyvigyya felvrpllys wgqwqsyltv hdwfdrwgfw vilvagfspi
      121 pykvftiaag amhvavipfi lasllgrggr fflvailvaw ggvklepwlr tyidwvgwvt
      181 vavlmlvvvc lrll
//
LOCUS       WP_004999525             279 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Acinetobacter
            ursingii].
ACCESSION   WP_004999525
VERSION     WP_004999525.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter ursingii
  ORGANISM  Acinetobacter ursingii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Acinetobacter ursingii"
                     /db_xref="taxon:108980"
     Protein         1..279
                     /product="formate/nitrite transporter family protein"
                     /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=31173
     Region          30..279
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msaeekeqek etdntltwre kmaieehekl sprlvyeiir kngveelerp tkalifsgit
       61 agivisfsfv fksllnaylp dakwaflien mgytvgfvlv ilghmqlfte ntiatvvplf
      121 knfslkklka vfrlwgivfi snligtalaa lfllnphlfd adliqsfdql ahhvasftis
      181 eniikgipag iliaslvwil psannkflli ffitylmalg gfthvivgsa emaywvfkgh
      241 atfseyifqf llpttlgnii ggtgvftlli ygqvneele
//
LOCUS       WP_004999907             146 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Nitrococcus mobilis].
ACCESSION   WP_004999907
VERSION     WP_004999907.1
KEYWORDS    RefSeq.
SOURCE      Nitrococcus mobilis
  ORGANISM  Nitrococcus mobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Nitrococcus.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Nitrococcus mobilis"
                     /db_xref="taxon:35797"
     Protein         1..146
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15378
     Region          1..146
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mrektsrrht ngftlielmi tvaivaiiaa iaypsytrhv ikshrstgqg klleimqaqe
       61 ryftinnsyt adltdlgyga asavpadggw ytvaaaacta stinqcvllt atpqnsqtad
      121 stcgnltlss rgqkgisgtg svgecw
//
LOCUS       WP_005000112              79 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Nitrococcus mobilis].
ACCESSION   WP_005000112
VERSION     WP_005000112.1
KEYWORDS    RefSeq.
SOURCE      Nitrococcus mobilis
  ORGANISM  Nitrococcus mobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Nitrococcus.
REFERENCE   1  (residues 1 to 79)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 79)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 79)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 79)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Nitrococcus mobilis"
                     /db_xref="taxon:35797"
     Protein         1..79
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8280
     Region          1..79
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mriefygvlq eaagrealel pidapsrvah ileelgeqip alqshlpria cavgdevipr
       61 semvtgdapl vllppvsgg
//
LOCUS       WP_005001216             397 aa            linear   BCT 20-JAN-2025
DEFINITION  TerD family protein [Nitrococcus mobilis].
ACCESSION   WP_005001216
VERSION     WP_005001216.1
KEYWORDS    RefSeq.
SOURCE      Nitrococcus mobilis
  ORGANISM  Nitrococcus mobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Nitrococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Nitrococcus mobilis"
                     /db_xref="taxon:35797"
     Protein         1..397
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=42563
     Region          23..397
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mnlqpgqnta lselsvcael swtpaatale ldpsafllts tgkvagdegf vfygqpksad
       61 gavvldaarr efllelkrls agiekvvial tidqgqkrgq rfgdlsevkl tvtgageplv
      121 fplaasgmse valiigefyk rngqwkfrav gqgfngglgp lathygvevk ddpeqaepst
      181 sppshsatpt psttassapv nlnkitlekk kpvsltkesg qygriivnln wtkgkggggf
      241 fsrnkgidld lgcfvelqsg akdvvqalgn tfgaydskpy ahlladdrtg easqgeflhi
      301 ngdqwsqlrr vlvyafiyeg apnwaaadav itikapdqpe lvvrldshss segmcavaml
      361 endggkikvs klidyyrghr fmdeaygwgf swragrk
//
LOCUS       WP_005002092             144 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Nitrococcus mobilis].
ACCESSION   WP_005002092
VERSION     WP_005002092.1
KEYWORDS    RefSeq.
SOURCE      Nitrococcus mobilis
  ORGANISM  Nitrococcus mobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Nitrococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Nitrococcus mobilis"
                     /db_xref="taxon:35797"
     Protein         1..144
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=15093
     Region          1..142
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mqkvqqgftl ielmivvaii gilaaiaipa yqdyvarsqm teafslasgq ktnvaeiwts
       61 egsfnsadng kfgiptntti ngkyvnkvdv lngkitatmq tagvssgisg ktlslspqth
      121 sgsiewkcss naaqkyipkn ctgt
//
LOCUS       WP_005001441             350 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SPOR domain-containing protein [Acinetobacter].
ACCESSION   WP_005001441
VERSION     WP_005001441.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..350
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38740
     Region          <73..>245
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          268..342
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 msmnnkqrwm ggvvllgggv llaalllkgk eeihqtqvqt qpkveqpakd nnrsnqagem
       61 vqlqplavdv etekrlleeq rrarekavae qearaadfla qqqqaeaaaa rkaaeeyaai
      121 narrnaaqes sdnippeitd qtkntaqkan dqkkseqqkl daekrlaeqk kqadaqklae
      181 qqkaeqlkkq keaeakrkae qervaaekka teekqrqlda ekaakkaaed krkaeaekka
      241 adekkhkaee dakkkaeadk ardllengdk nwmvqvalaa nqanadavvs klrakgykvt
      301 tsptskgiri mvgpsksret adaarkkivs dsslnmksaw vidwvpldqr
//
LOCUS       WP_005002273             233 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Acinetobacter].
ACCESSION   WP_005002273
VERSION     WP_005002273.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 233)
  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 233)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 233)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..233
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=25669
     Region          4..211
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 msalteeeql dnlksfgkky gsaiisgili aliaffgwqy wqkktlaenq vrtakvqqlm
       61 dqaqgaesnp dalsnlyasa dkitkdapds vqaiqtelml akvaydkady aaaekslkkv
      121 ensklnddgl lqlvklrlay aqlaqnkydd alktlalvad pafkataeea rgdiyvakkd
      181 iasakkayqs awddlakrkq erqilqikle svgvlvddpe ierpiidtqv dks
//
LOCUS       WP_005006449             276 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Nitrospina].
ACCESSION   WP_005006449
VERSION     WP_005006449.1
KEYWORDS    RefSeq.
SOURCE      Nitrospina
  ORGANISM  Nitrospina
            Bacteria; Pseudomonadati; Nitrospinota/Tectimicrobiota group;
            Nitrospinota; Nitrospinia; Nitrospinales; Nitrospinaceae.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Nitrospina"
                     /db_xref="taxon:35800"
     Protein         1..276
                     /product="formate/nitrite transporter family protein"
                     /function="5.7 : Nitrogen metabolism"
                     /function="7.2 : Anions"
                     /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=29512
     Region          6..259
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mfdtdidnls nqaekkiayl krspggyfll salagiylgf givlifsigg piaaggggay
       61 lklimgasfg ialslvifag selftgnnmv favgrlsrri girpilylfg lcfignlcgs
      121 vflawlvteg gslpassqel ivkvagmkmn lsakeaflrg ilcnwlvcla vwialrtkne
      181 sarlimifwc lfafiasaye hsianqtlls lamflphgae vslggfihnq iwvtlgnmvg
      241 ggllvgmvyw lansqpetqa esepaliqet lqeesa
//
LOCUS       WP_005006860             626 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Acinetobacter].
ACCESSION   WP_005006860
VERSION     WP_005006860.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 626)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 626)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 626)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 626)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..626
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=69471
     Region          2..626
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mqspaqkaal paitlaalgv vfgdigtspl yalrqcflta hlaiseasvl gilslifwcm
       61 mlsisfkyvt iimradnnge ggimsllaln lrttlisdkk kvylialgfi gaslffgdgi
      121 itpaisvlsa ieglsiatpi fnqwleplsi giltglfliq rhgtgtmgkf fgpitllwfm
      181 sigffgilsi lqtphvllmi npawafsfvv nqpyvafltm gaviltmtgg ealyadmghf
      241 grlpiklawf ivvmpcllls yagqgalllr npealanpfy mqipdwalyp miglataaav
      301 iasqavitgv fsmvnqaiql rylprltvrh tsdvergqiy lpfinwtlyi svlilillfe
      361 nsenlasayg vavtmtmlcg tilisvlays lwrwplwkva lfavpfllld fifvastslk
      421 ilsggwvpil igavlftilm twkdgralvf krlekdslpi dlfiksigfs netkfvpgda
      481 vfltgtpniv phamlhnikh nkvlhernim vtvmtrdipy vsdaercrve klddrfyrit
      541 ldygfkdqpn ipealekaya elgfeydlmq isffisrdri ihtlgegmsp wreklfismq
      601 rntspvsdfy qiptnrvvel gsqiei
//
LOCUS       WP_005007236             335 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005007236
VERSION     WP_005007236.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 335)
  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 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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 335)
  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   5  (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   6  (residues 1 to 335)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38255
     Region          22..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          98..335
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mgqltdasvv lrlgyqairr aglpteeilt kagvalgqve andrtplnaq yafwvaaeev
       61 skdsdiglhl gehlplyrgq viehlfisse nfgeglkral ayqrlisdaf haklvieddr
      121 cyltngvqpw aenlvnrhfs ecamsgvlrf fkfitegrfq piyidfnfsq gapddeyfrv
      181 yecpvslgqk etrlyfdpai ldyplwqaep ellqlheqla ieklqelary dlvgevrrai
      241 gstlesgett letvaaqlni tprrlrtqls eantsfqqil sdyrcrlakk llantaesve
      301 rivyltgfse pstfyrafkr wtnetpveyr krkqr
//
LOCUS       WP_005007485             232 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Acinetobacter bouvetii].
ACCESSION   WP_005007485
VERSION     WP_005007485.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter bouvetii
  ORGANISM  Acinetobacter bouvetii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 232)
  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 232)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 232)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Acinetobacter bouvetii"
                     /db_xref="taxon:202951"
     Protein         1..232
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=25524
     Region          4..209
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 mnalsddeql dnlksfskky gsaiisgili aliaffgwey wqkktlaesq tatakvqqlm
       61 dsaksaqgda fsqlstsads imkeapdspq aiqaqlvmak laydkadyas aekalkkven
      121 vkagddgliq ivklrlayaq laqkkydeal ktleavtdpa fkatadearg dvyvakndie
      181 nakkvyqsaw dalierkeer qilqiklesv gvlvddpeie rpiletqvee te
//
LOCUS       WP_005008484             838 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Acinetobacter bouvetii].
ACCESSION   WP_005008484
VERSION     WP_005008484.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter bouvetii
  ORGANISM  Acinetobacter bouvetii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 838)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 838)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 838)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..838
                     /organism="Acinetobacter bouvetii"
                     /db_xref="taxon:202951"
     Protein         1..838
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=91163
     Region          61..111
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          124..838
                     /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 mskfqvkttl aiairavllg apaltvglls tngyaaaaqs itvkkstldq alkqlaiqtg
       61 itisydaqaf skinsqglqg qyspeqalri llqpanleai klenggfsik plhtaasetq
      121 hpqlsttqas atsqdtnasa heitqlpaii vtaneesplt tegtnsyttk ataastglal
      181 slketpqlvs vvtrqqmedq nltqlmdvan qaagltikqg gnigsdnspi yargqtvdsy
      241 lldgikllns yssifqsqdt alfdrveivr ganglmtgag tasasinmvr kkpledfkas
      301 vsasagswdt yrtdldistp lnkegtirgr tvfayqtgds yidryseerk vaygvveadl
      361 ndntkaslgv syqqididgi arsglptyyt dgtpidwsrs dsaaanwsts drsttgyfad
      421 iehqlndrwk ikgvasrtit ssdeivgyvf sgsginkatg agsvlygtrw dykptqdlfn
      481 ltlngsfdlf nqthdvvvgt tyaksknkrp nstgwdtipi dnifawdgyt pakpdlktng
      541 wystdeksls aftaarlkls dplamiigar fddweriskt npetggtatn kkqeekeiip
      601 yigltydftp nwtaytsytt ifspqdkydl sgnfidplig nsteigikge ffdnqlniga
      661 aiyqtkednk ailitgapqi tlpngqkvsp yraesgtksr gieleatgki tdlwqlsasf
      721 trnlsqdskg dslnsdvpnn taklfttytl pqldealtig agirwqsdiy tyvtrtnsfk
      781 seqgsygivd lmarykinen ltanlnvnnl lnekyhlstl nsyygapanf qvgvkynw
//
LOCUS       WP_005008692             251 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Acinetobacter bouvetii].
ACCESSION   WP_005008692
VERSION     WP_005008692.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter bouvetii
  ORGANISM  Acinetobacter bouvetii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Acinetobacter bouvetii"
                     /db_xref="taxon:202951"
     Protein         1..251
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28499
     Region          23..248
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mtdtndkkry fepapqdidv enfkkviqsr rsvrkftkke ipaevlddcl dlallapnss
       61 nlqpwtfyvv qnpakkkqlv kaclgqlaak taselivcva rtdrndemak rnitefpfpe
      121 apaavqkyyk fipynyktgy lnalgnfkkv afkiarsldk qlpvtafnqa daklwasktt
      181 alacenlvla lraygfdscm megfdeplvr kllnlndqqy pvmvigager aedgvffpqy
      241 rfdrelfiqk v
//
LOCUS       WP_005009011             113 aa            linear   BCT 20-JAN-2025
DEFINITION  PilZ domain-containing protein [Acinetobacter bouvetii].
ACCESSION   WP_005009011
VERSION     WP_005009011.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter bouvetii
  ORGANISM  Acinetobacter bouvetii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 113)
  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   3  (residues 1 to 113)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 113)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Acinetobacter bouvetii"
                     /db_xref="taxon:202951"
     Protein         1..113
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12251
     Region          2..113
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mqprmggiiq anipdvetlf asympyvagg glfvpskqav kmgdevfvlt tlpeqsqkvp
       61 ltgkviwisq kqngikpqgf giqlagekgi yfkseaerml aglktegrrs ytm
//
LOCUS       WP_005009204             343 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter bouvetii].
ACCESSION   WP_005009204
VERSION     WP_005009204.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter bouvetii
  ORGANISM  Acinetobacter bouvetii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 343)
  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 343)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 343)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 343)
  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   5  (residues 1 to 343)
  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   6  (residues 1 to 343)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Acinetobacter bouvetii"
                     /db_xref="taxon:202951"
     Protein         1..343
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39884
     Region          29..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          101..342
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkrldgdyfk gtisirlvke alhnaerqgy eindlltqag iapellhtdk trvsviqyaq
       61 lwivladamn deffgmdhhp mrrgsytfls ksvlqaadlg kalshilqfl nlvlddfsst
      121 hfvqenyayi vikdsrqpkr mfsyatylml ihgmmcwlcg qrvilnriql kcaapqddsd
      181 yrmrfcddiq yhtdenyiqf dasylkiaik qdkkswhqfi qhtpynllvr fknpnalshq
      241 irkhfsqmpa sewaelpela qlfnmseatm qrrlkqegin fqqlkneirr dlainlleqt
      301 alslqdisgq lnfhdasafh rafkkwtgis pgayrqtknd npq
//
LOCUS       WP_005009924             195 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Acinetobacter].
ACCESSION   WP_005009924
VERSION     WP_005009924.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 195)
  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 195)
  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   3  (residues 1 to 195)
  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   4  (residues 1 to 195)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 195)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..195
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22271
     Region          1..191
                     /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"
ORIGIN      
        1 mpklkialid ddierasfik esliehgfev tacllidhln stdlqqlhad villdmdhph
       61 rdiiescvsq fdlptvlftk nshkdtikna ieagvtayiv dgidpekles ileisieqfk
      121 khkkllkdln etkckladrk diekakvllm qmhkieeeqa ftllrknams hrmtmgemar
      181 rlidaqallq sqfke
//
LOCUS       WP_005012469             283 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Acinetobacter bouvetii].
ACCESSION   WP_005012469
VERSION     WP_005012469.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter bouvetii
  ORGANISM  Acinetobacter bouvetii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Acinetobacter bouvetii"
                     /db_xref="taxon:202951"
     Protein         1..283
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30854
     Region          1..282
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mqgvdlhths nisdgtlspe qlvraageig ihtlaltdhd tmdglslaeg aakdlgiklv
       61 sgveissqws rpatkknygv hivalnmqhp epllalleqq kqiravrakq icdlliplig
      121 ediyadvvak vdnvpdrvtr thiaktlvek gyvsraqqaf dkyikegkka yvkfdglgle
      181 etiqvihasg gfavlahptr ydlsatniry lieifaqfgg davelppave plgtrqmvdr
      241 miaehglkvs vgsdfhgdnm pwirlgnipr vkegqagiwe sfv
//
LOCUS       WP_005012754             343 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter bouvetii].
ACCESSION   WP_005012754
VERSION     WP_005012754.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter bouvetii
  ORGANISM  Acinetobacter bouvetii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 343)
  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 343)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 343)
  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   4  (residues 1 to 343)
  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 343)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Acinetobacter bouvetii"
                     /db_xref="taxon:202951"
     Protein         1..343
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39331
     Region          51..207
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          256..331
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqelqipngy fqlwrmhmae lkmddahlhf lapyqqqlnh vlslpidsqs phsffsavme
       61 ltrqhldcpq lifemakfir aehfgvlgym asrsdsvaea lqhimrfsrl vidgaavipm
      121 qlqskgkeiy lywplhddky alvnelttac marlakqifp aslqllkiqf ahapqmaryh
      181 yekffgcsve fghakysfvi ssdsldlkse ladpslkrll lkqaeeaias kphfenivpq
      241 ihvhvaeylr lnaqapkies iaeelhlsvr tmqrqlngqn tsfkqvldae rmkrceqllq
      301 qntpiaqial qlgysdqsal araykastre tlmqrkkrlk pql
//
LOCUS       WP_005012844             381 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Bordetella holmesii].
ACCESSION   WP_005012844
VERSION     WP_005012844.1
KEYWORDS    RefSeq.
SOURCE      Bordetella holmesii
  ORGANISM  Bordetella holmesii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 381)
  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 381)
  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   3  (residues 1 to 381)
  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   4  (residues 1 to 381)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 381)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 381)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Bordetella holmesii"
                     /db_xref="taxon:35814"
     Protein         1..381
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40799
     Region          29..365
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(105..107,127..128,177,229,253)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mtlrtpikll aagiaaaclt svaqaadikf gfaapltgpq shygedmqng ltlaleeanq
       61 kgvkvdgkpv kfvlvsrddq adarvavqva qqlvdedvng ilghfnsgtt ipasrvyhda
      121 glpqismats peytkqgyet tfrmmtsdtq qggavgkfmv dklhakkval iddrtaygqg
      181 ladevekavk aaggqivrre yttdkandft siltnikgva pdaifyggld aqsgpmkrqm
      241 qtlglkaplv sgemtrsdtf iklagdaaeg tyaslagvpl dkmsagkdfa qryqtrfkka
      301 pgvyapyayd gawnmitaie hagsakpeky lpelaklnrk gatsehiayd angdlkeisv
      361 tlyqvkngkw emvetmvsqa q
//
LOCUS       WP_005012920             266 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter bouvetii].
ACCESSION   WP_005012920
VERSION     WP_005012920.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter bouvetii
  ORGANISM  Acinetobacter bouvetii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 266)
  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 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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Acinetobacter bouvetii"
                     /db_xref="taxon:202951"
     Protein         1..266
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30147
     Region          29..266
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          185..262
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mpqnlkrdpa alkqlptndd iartlwisfr ddpalsaypa hghawgefiy afngvmevhi
       61 dqvdyitppp ygiwlppnlq hsglnrtavs hgtlyvherl csrmpqqagi llssslvsai
      121 fehlrqrslp edspeyqrll qvmldqlqqa klvssylphs shpalmqild flhqhpddss
      181 plqvlaqqan mtertlarcc lkelgmslne wrqrlkvika msmltagkkv esialdlgya
      241 nasafinmfk rwmnltpdqf rklnqp
//
LOCUS       WP_005013406             396 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Bordetella holmesii].
ACCESSION   WP_005013406
VERSION     WP_005013406.1
KEYWORDS    RefSeq.
SOURCE      Bordetella holmesii
  ORGANISM  Bordetella holmesii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Bordetella holmesii"
                     /db_xref="taxon:35814"
     Protein         1..396
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42971
     Region          7..394
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mnsqntilvi nagsssikfy lygisearel spilggqleg igtqhsrlvv rdahgqtmtd
       61 rqiaprhaad vrdaqevvgt wlsghlsgsp lavghrvvhg gpdlhtpvlv ddaiidklks
      121 ytslaplhqp nnlapiqvir erlpalpqva cfdtafhrth savadryavp etmyqegvhr
      181 ygfhglsyey vaqrlqralp dlkggkivaa hlgsgvsaca mldgksmdst mgftaleglp
      241 mgtrpgrldp giglwlmerg mshdeiqhfl yhecglkgls gigndmrele asdapaarla
      301 ldyfawrvae gmvglgcamn gidafiftag igensasmra riarhwewlg vhiddernkg
      361 hgpristeds kigvyvvrtn eeliiaqhtl dlvsar
//
LOCUS       WP_005013940             272 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Bordetella holmesii].
ACCESSION   WP_005013940
VERSION     WP_005013940.1
KEYWORDS    RefSeq.
SOURCE      Bordetella holmesii
  ORGANISM  Bordetella holmesii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Bordetella holmesii"
                     /db_xref="taxon:35814"
     Protein         1..272
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28179
     Region          196..269
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mglftrkdsa sesspsrprp svsseaqaae lrgrarrrla gavalvlaav ivlpmmldse
       61 pvpvsddipv ripdrnspyq pnvsepvavp qtpaspappa dtapapaaap datvpppeav
      121 aqvpavpppv aattppprpl dalkpvekpa lvkpadkpkn esgsrsddga ralallegrt
      181 papaaakpva kpaakgnfvl qvasyttqtd arerrgklhq agvtnafveq atisgkqqyr
      241 lrvgpfpsre aaqaaqarlr tlgydngfia aq
//
LOCUS       WP_005014220              83 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Acinetobacter].
ACCESSION   WP_005014220
VERSION     WP_005014220.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..83
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8875
     Region          3..83
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 msqikiriea fgaverqlpq nfeiicksqs tvsqildqvg hnypealaim ercacaiged
       61 iisrqtsltt dstlvllspv agg
//
LOCUS       WP_005014707             113 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Acinetobacter].
ACCESSION   WP_005014707
VERSION     WP_005014707.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 113)
  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   3  (residues 1 to 113)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 113)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..113
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12120
     Region          2..112
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mqprmggiiq vnipdratlq asymgfvqgg glfipsqqpv kmgeevfvla tlpgqaqkvp
       61 ltgkviwisr kqngirpqgf giqlsgekgi yyrseaekll agsltsdrpg ytv
//
LOCUS       WP_005015335             819 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Bordetella holmesii].
ACCESSION   WP_005015335
VERSION     WP_005015335.1
KEYWORDS    RefSeq.
SOURCE      Bordetella holmesii
  ORGANISM  Bordetella holmesii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 819)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 819)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 819)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Bordetella holmesii"
                     /db_xref="taxon:35814"
     Protein         1..819
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88683
     Region          67..119
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          94..819
                     /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 masrqsstfl vtllrarpar lclavqlala apaavwaqaa satdivfaia pttldqalgq
       61 fgsaakltva asptltrgvm tqglsgrytp eqglaqllag tglqavanpn gegyqlrrap
      121 qdgagvstla pvavtgaydm aategsgsyt sgvvtigkgk qsvkdipqsv tvvtrqrmdd
      181 qnatslddvl anstgmtlyk spmggnyvfs rgfrvdtyqf dgvnrefyyp qansftsstv
      241 ildrveivrg angllqgags psasvnlvrk rplaenqlql ttsagswdny radidatgpl
      301 nesgtlrgra vasyndrdyf ydvaksrntv lygvlsydia psttitggvs hedlrstpff
      361 hglphytngd diglkrstsf aqhwnrwngk qtsafvelah rfnqdwsvkl tgnstqesnd
      421 skyaftegav npltgsgptm yagifdfsth nkalnldidg vfdalgrkhs vsfgasvnhl
      481 tskndfatar lgrgldiwnp dhdvpeptda wlrenayrgd atiikmkqtg vygvgrfsla
      541 dpltlvagar vswyentary rdsgdrytdp ykengvvtpy ggliyafnpq wsgyvsyaei
      601 fepqnaldat gklldpmvgk nyelgvkgel mggrvntsia vfridqknra qqdlagicsv
      661 gdvcyissgk vrsqgveaei sgevlpgwqv fagytfnslk flddtsvsnt nfgrtftpkh
      721 mlrlwsdyrl pgelsawtlg agvnyqsgsy tetrgvrvsq spyavwnarv sykinknwta
      781 alnvnnvfdk tyyqtigapg wgsfygdprn atltlrgtf
//
LOCUS       WP_005015667             710 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Bordetella holmesii].
ACCESSION   WP_005015667
VERSION     WP_005015667.1
KEYWORDS    RefSeq.
SOURCE      Bordetella holmesii
  ORGANISM  Bordetella holmesii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Bordetella holmesii"
                     /db_xref="taxon:35814"
     Protein         1..710
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73801
     Region          12..710
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mtavtqrpga gleyffdaqg iavigasddi tkiggrpvhm likygyagpv ypinpkggtv
       61 qglpayanvr dtptvpqlai lavpasataa alrdcatrgv kaaivlssgf veagpqgaal
      121 qaelvqigrd hdmrilgpnc lgavnvadrl igsfsialee nmpaaghvgi vsqsgnvgsh
      181 tmqsvarrgm gvsrfiatgn eadvdvadgi aalaqdpstr iilccmetcr hagklidalr
      241 mardlgkpvi vlkigstekg qaaaashtga ltgsdavida ifrrhgvlrv rsvealidig
      301 haasllmpnr lprtdavtlv aasggfgimm adamseagmv lpalaehtqq rireavptas
      361 tgnpvdasaq mssrpdillk mltallddpa egalvlfmsl slyntrlrgi ylqalaevra
      421 shpdrllmii sqgpadaveq italgipvfa sidsaatgla gllqlgrlqa gapapasmap
      481 aepvdttvfr nefeakrala ragidvpqei iahnaddaar aadaigypvv vkvvsediah
      541 kteaggvaln ltdavslrqa yaqvlsnaar hapqaridgv lvapmlrggt eliagisqdp
      601 vfgpivmvgm ggiyaevlkd vavqavpvse healemirsl kmfaildgar gqakadieta
      661 artvarlsaf ayrhrddiae idmnpilvrp qgqgvvvlda lmvprthpvp
//
LOCUS       WP_005016221             138 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Acinetobacter].
ACCESSION   WP_005016221
VERSION     WP_005016221.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 138)
  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   2  (residues 1 to 138)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            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="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15370
     Region          68..137
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mknsnkffrl keilslmlgl laclwlasag qvqaqqfdds ylkwknqqld hdrrllqqtg
       61 smtmssgpaa qistekvsln rgsadqlqqv lsgvgekkaq aiveyrnkng kfnsiedlqk
      121 vkgigpklfe knksrltl
//
LOCUS       WP_005017074             162 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Bordetella holmesii].
ACCESSION   WP_005017074
VERSION     WP_005017074.1
KEYWORDS    RefSeq.
SOURCE      Bordetella holmesii
  ORGANISM  Bordetella holmesii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 162)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Bordetella holmesii"
                     /db_xref="taxon:35814"
     Protein         1..162
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17301
     Region          8..162
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfqaaplsta skpqfyrelv aqaqallage cdrianaanl aalawqalpq inwcgfyffd
       61 gqelvlgpfq gkpacvrial srgvcgaaas qrqtqvvpdv hafpghiacd aasrseivvp
      121 lvldgqllgv wdvdspvpgr fddddrqgmq alcqvyldsl ar
//
LOCUS       WP_005018179             183 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Acinetobacter].
ACCESSION   WP_005018179
VERSION     WP_005018179.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..183
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=19966
     Region          29..151
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mrnmlkratk ssspslacwa gqcrlgdcrg ftlielmvvv tiiailaaia fpsyavysrr
       61 aaesqaqqem qkiaeqlerh kaknfsykgf dpnyiygeta ampivkvpig stgtatkyqi
      121 tirdlndpsk lltdaaaagr gwtikaevnn dpqnynllmt saglrcknka tvtyvscnss
      181 egw
//
LOCUS       WP_005019470             317 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Acinetobacter].
ACCESSION   WP_005019470
VERSION     WP_005019470.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (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   2  (residues 1 to 317)
  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 317)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..317
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35654
     Region          27..68
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
     Region          <249..309
                     /region_name="repM_Acin"
                     /note="replication initiation protein RepM; NF038290"
                     /db_xref="CDD:468455"
ORIGIN      
        1 msldatnwaw rvgltekkgg sriplkrlil lsladraged hccypsmqrl ekdtglerkt
       61 vlkiiaelle drlivdtger kgstrrvkvy rlngvngret mpktaplqek nlseivpete
      121 qsqkrnhsvn gmlnsanngt lnsavngtqn lpmnlseesk nkkdrlcfkk lreeifladd
      181 sinfdtlmns kwserekraf etynvgknms cdlmiyhfad wlinayrtky snpqqaasvk
      241 pagtgsqsnr lsekqihtfa qklsqhpefs grfsepgesy eklaariavk ladpvqakkw
      301 epylkqvgfn gslavga
//
LOCUS       WP_005020011             708 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor family protein
            [Acinetobacter].
ACCESSION   WP_005020011
VERSION     WP_005020011.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..708
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=79321
     Region          13..703
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mkssaslsaf pykklllsac ilqaswaqaq evvqlapitl eatrtdtswl etpasvyrie
       61 qpqnqnnldv nlsetlkgvp glqinnreny aqdlqismrg fgarstfgvr girlyidgip
      121 atmpdgqgqt snidlgsldh ievlsgpfss lygnssggti ltttregkgr dsvelgyagg
      181 shhknktslv lqggadkage psyiisssyf dtdgfrehsa arkvlnnakl swnledgsqv
      241 nwvvnhvdin addpggltrq qwkddprqqa sfirqfdtrk eiqqtqtgvt wskpindqhe
      301 lygmaylgqr hviqyqsipn taqanprhag gvidfdriyy gtdlrwtgke llpnttlsig
      361 maldamdedr qgyenfvlnn ntpqygvkgn lrrdekntlw nidpyiqasw qflpdwrvds
      421 glrysnvhye skdkyirgtn gddsgqtdyq kllpsialsw niipdstlyi syakgfetpt
      481 ftemayptlg tsginfdlkp assdsyelgf ktqnnwgdfs taifhtqtrn divsaesnng
      541 rntfqnakrt qregielywn knlwqelyaq asysylnakf dadipgsdsr atvykgniip
      601 giaknqayia lnwqpetgfq agldvryndk iyvddinsdt apsytvmaan igyvwknadw
      661 kintfarvdn lldkdyvgsv ivndgnkrff epadrrnwsa glkmirsf
//
LOCUS       WP_005023287             403 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Helicobacter pullorum].
ACCESSION   WP_005023287
VERSION     WP_005023287.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pullorum
  ORGANISM  Helicobacter pullorum
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Helicobacter pullorum"
                     /db_xref="taxon:35818"
     Protein         1..403
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43791
     Region          1..398
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mdilvincgs sslkyqlint dteevlasgi cdrigidggq fsykpkdgek stqnieikdh
       61 evaiklvlga ltnpfngavk sletikaigh rivhggehft hsaiiteevi ynieecadla
      121 plhnpahllg iracqhlmpn tpmvavfdta fhqtmppkaf iyglpyeyyt kykirrygfh
      181 gtshsyvskr taeflgiple nskiitchlg ngssicaven gksidtsmgl tpleglvmgt
      241 rsgdidpavi dyiaqkenls tkeimnilnk ksgvlgisgl ssdfrdllaa dekgdlkarf
      301 arevfayrva kyigsytaal tgvdaisfca gvgenakfir gkivshlqfl gitldekanl
      361 etigregiis tsdskvkvcv iptneelmia rdtkalvska ynl
//
LOCUS       WP_004994442             273 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AfsR/SARP family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_004994442
VERSION     WP_004994442.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..273
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=29944
     Region          1..253
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mkiqvlgplg aevnggsivp tagkprqils llalhpgrvm pvsvlmeeiw gteppqsalt
       61 tlqtyilqlr rrlgtamgpd apevakdvla trhggyllqi paesvdvhey ermvaegrsa
      121 feagdddssa slfrkalglw rgsvlvdvrv gpileievmr leesrlgtle rridadlrlg
      181 rhseliaeli eltarypqhe glhsqamval yrsgrqasal diyrklrirl ieelgvepsp
      241 qvqrlhqaml avdpqldvaa gprrsstfdl yaa
//
LOCUS       WP_005024688              97 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Bilophila].
ACCESSION   WP_005024688
VERSION     WP_005024688.1
KEYWORDS    RefSeq.
SOURCE      Bilophila
  ORGANISM  Bilophila
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae.
REFERENCE   1  (residues 1 to 97)
  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   2  (residues 1 to 97)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Bilophila"
                     /db_xref="taxon:35832"
     Protein         1..97
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9985
     Region          18..86
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mniktiasav laavvlcaap afadgkmnln tateqelsan pavgpelakg ivefrenvgd
       61 iksmdellev kgvtpevlek lkqavtveai egaecsc
//
LOCUS       WP_005023472             262 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: hydroxypyruvate isomerase family protein
            [Acinetobacter].
ACCESSION   WP_005023472
VERSION     WP_005023472.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 262)
  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 262)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..262
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29208
     Region          1..257
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 msklavnlsm iftevplier falahahgfq hveiqfpyel eieqiarqlh kyklglclin
       61 vpagdlmqgg nglagvpgqe iafhraleqa idyaialkvp sinilagkqp edadllpcln
      121 tlahnlklac hlateqgiqp vfeminatdm prflvqniaq aqemleavnh palkmqydcy
      181 hmammgedvl aslqeniasi ghiqfadcpg rhepdtaqis yseiftwlkq skysgfiaae
      241 ykprahsnas fhwknkyfpd qi
//
LOCUS       WP_005026373              99 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Bilophila wadsworthia].
ACCESSION   WP_005026373
VERSION     WP_005026373.1
KEYWORDS    RefSeq.
SOURCE      Bilophila wadsworthia
  ORGANISM  Bilophila wadsworthia
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Bilophila.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Bilophila wadsworthia"
                     /db_xref="taxon:35833"
     Protein         1..99
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11367
     Region          1..99
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(25,56..57,59,80)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(25..26,34,37,39..40,42,45..46,48,56,61,68)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mvhkdliyei lsvveeipkg cvatygqiar ligrdknsrl vgkvlsmaey ygdypchrvv
       61 nhagrlvpgw leqrllleae qvvmkddrhv dlkkcrwdy
//
LOCUS       WP_005025268             251 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Bilophila
            wadsworthia].
ACCESSION   WP_005025268
VERSION     WP_005025268.1
KEYWORDS    RefSeq.
SOURCE      Bilophila wadsworthia
  ORGANISM  Bilophila wadsworthia
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Bilophila.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Bilophila wadsworthia"
                     /db_xref="taxon:35833"
     Protein         1..251
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=27990
     Region          5..>224
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mldvqirkrl atgrksgdsf sldvslscat rrlvlfghsg sgktltlqsl aglvrpdggy
       61 ikigddvlya sekgidlpar erhlgyvfqd yalfphltvr rnvefaldkt krtlfgrpsp
      121 aarksvddll erfevghlae rypreisggq rqrvalaral itaprmllld epfaaldpll
      181 rvrmrreirv lldewnipvv lithdpadvd afadslavyr ngmirhvldd yparrasepd
      241 alsllaplve v
//
LOCUS       WP_005027608             174 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Acinetobacter].
ACCESSION   WP_005027608
VERSION     WP_005027608.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..174
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=19403
     Region          1..>60
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkknnngvsl lelvvciaiv ailasfaipa yqeyraqqea kslphllnmq iiqaknyalt
       61 yrnqivicss qnleqcedeq wnkgllifid tnndkelnsn ekilstvmld leygrldwrg
      121 alnkprlffk adtglprgsn gsffycasss aslnkrlvls pmghlrvesl astc
//
LOCUS       WP_005028498             511 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase [Acinetobacter].
ACCESSION   WP_005028498
VERSION     WP_005028498.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..511
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=58207
     Region          4..421
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mplldwvnrn qaeetasqvp fhllkfqktf gdtdtakenl iiqgdnlqil ksllplyggk
       61 vkcvfidppy ntqsafehyd dklehaqwlt mmyprlqllk elltedgsiw itlddneshy
      121 lkvmcdeifg rknfvanivw qkrysrenre aigdahdhll vyaknsmefk kvrnlvpmne
      181 tqakvyknpn ndpkgrwrgi pmtaqaghat peqfyeivsp sgkpfrppeg rcwgvsraty
      241 drlleegriy fgkngdsqpn iirylsevkg vvpwtwwnhe dhghtdeakk esqllygkde
      301 tfsspkperl iekilyiatn kgdmvldsfl gsattaavah kmerhyigie mgdhaqthvi
      361 prlekviege qggisksvew qggggfsfyk lgnavfddqg flnsdvkfmd lasyiwwlet
      421 ksafnsalsl enpflgvhdg vsyfllyngi lgdrrpnsgn vlthsilnfl ndchtsegkr
      481 viigeasrlg ktkldelnie fkqipyslyg n
//
LOCUS       WP_005028838             821 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Bilophila wadsworthia].
ACCESSION   WP_005028838
VERSION     WP_005028838.1
KEYWORDS    RefSeq.
SOURCE      Bilophila wadsworthia
  ORGANISM  Bilophila wadsworthia
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Bilophila.
REFERENCE   1  (residues 1 to 821)
  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 821)
  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 821)
  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   4  (residues 1 to 821)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Bilophila wadsworthia"
                     /db_xref="taxon:35833"
     Protein         1..821
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=90422
     Region          74..820
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mskikslpgq rlcsslppdr vpwetsdaip rnghrkvapq pralkalela lhihtagyni
       61 ylsgesnlgr tymlreflep rirkaqtppd llyvnnfddp drpmllsvpa gqgkklrsvl
      121 sqaladirke lpvrldneky vkkrselqdr fqavrsglik qmdktagkeg fnldmdeqgs
      181 ltlyplvegk rlsedeyehl dptlrqglkq kgdtllrams gmvrklnsae qsfrsdertl
      241 eqevigsvls avltpaveri lkncagpdge pdstlkkyfe alrqdildhp egflpretqp
      301 aqalsaalsg daqhpetdty lyevnvfvdn sgnkgaplii edhpttanll gcveresemg
      361 alvtdftlik agslhrangg flvlhledil qhpgawegll ralragsarl eeagdvpdga
      421 vrtkgiepqp vplnlkvvli gneelyeall tnddrfaklf kikahmtetv ertaadirsw
      481 lirvagiide thllpfsrta laglvdfssr vaedqrklsl kfplmrdvmi easamaamkq
      541 salveaehle ealearmyra nlveelymee ydrelikvrt sgsavgrvng lsvswygdfe
      601 fglphqisct vgvghggiid lereaelggp ihtkamlilk sylvdqfarn kplvmtgslc
      661 feqnyggieg dsasgaelaa llsalsgvpl klslaitgav sqsgqimavg gvsrkiegff
      721 gicsrrgltg eqgvivprdn vdhlmlspri reavdtgkfg iypvehitea lelltgipag
      781 kplknggftr dslydlvdrr lqefghsaeh ayskplrrrk k
//
LOCUS       WP_005029029             530 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Bilophila wadsworthia].
ACCESSION   WP_005029029
VERSION     WP_005029029.1
KEYWORDS    RefSeq.
SOURCE      Bilophila wadsworthia
  ORGANISM  Bilophila wadsworthia
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Bilophila.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Bilophila wadsworthia"
                     /db_xref="taxon:35833"
     Protein         1..530
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=56561
     Region          2..530
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mqkilridpk dnlivtlrdl aqgdiieneg qriqlvtdvp akhkftrepv pvggivtlyg
       61 vpvgkavapl qsgeritvdn vvhyaaevdl sdavpymwka pdvsrwanrt fdgvirpdgr
      121 vgtanywlii plvfcenrna lklrdalert lgyagdhlad farslvggtg capaprpfph
      181 idgiraithn ggcggtaqda wtlcrmlaay adhpnvaglt vfslgcekaq iglfqealre
      241 rnlgfdkpci llrqqdwsse vkmmeeavrk tlahfknadl verrpvplsk lklgvkcggs
      301 dgfsgisanp aigevsdrvv tlgggsalae fpelcgvean misrcirked karflelmrr
      361 yeaaanacga sisdnpspgn ihdglitdai ksagaakkgg kapisavldy aepmpdagls
      421 lvctpgndve avtglvaagv nvvlfstglg tptgnpivpv ikvatntava erlsdlidfd
      481 cgpiidgepi aaaadrllek vldtasgrys tkadrlgqhd flfwkrevsl
//
LOCUS       WP_005030068             391 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Bilophila
            wadsworthia].
ACCESSION   WP_005030068
VERSION     WP_005030068.1
KEYWORDS    RefSeq.
SOURCE      Bilophila wadsworthia
  ORGANISM  Bilophila wadsworthia
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Bilophila.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Bilophila wadsworthia"
                     /db_xref="taxon:35833"
     Protein         1..391
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42798
     Region          2..388
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mrlevylnar gerrfvglle erggdilfey dkrfldsgie lspfllplrp gvasdpkrtf
       61 dglfgvfnds lpdgwgllll drllrrsglp leritplsrl slvgsggmga leyepvtpdp
      121 dplperidld gvaeeawrtl nedplpvetl rtlmalngss cgarpkimvr vsgdrrlivp
      181 davaepgcdp wlikfparhd dpaigrmeya cslaakragi empdtalfpg rdgaayfgvr
      241 rfdredggkv hvhtacgllh ashryasldy enlfrlgksl trnpedvekl vrlmafnvrl
      301 gnqddhsknf sflldakgrw rlapaydltp srgvggeqtc mvngkgrdit dkdmiaaasv
      361 vdvpartvka ileqvgeava alpailaevs g
//
LOCUS       WP_005030619             188 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Bilophila wadsworthia].
ACCESSION   WP_005030619
VERSION     WP_005030619.1
KEYWORDS    RefSeq.
SOURCE      Bilophila wadsworthia
  ORGANISM  Bilophila wadsworthia
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Bilophila.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Bilophila wadsworthia"
                     /db_xref="taxon:35833"
     Protein         1..188
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20253
     Region          1..188
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mhrlvlgisg asgmplaqav lenlatvsdl evhliisaga ervlqaecgi psaalaryah
       61 avhessdmaa gpssgswhhd gmiicpcsms slasiasgag snlihraadv tlkerrplvi
      121 varetplnli hlknmqavte agavvmpftp afytrdtsle ammrhftgrl ldqfriehhl
      181 ckrwrddr
//
LOCUS       WP_005030667             638 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Bilophila wadsworthia].
ACCESSION   WP_005030667
VERSION     WP_005030667.1
KEYWORDS    RefSeq.
SOURCE      Bilophila wadsworthia
  ORGANISM  Bilophila wadsworthia
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Bilophila.
REFERENCE   1  (residues 1 to 638)
  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 638)
  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 638)
  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 638)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Bilophila wadsworthia"
                     /db_xref="taxon:35833"
     Protein         1..638
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=69254
     Region          1..628
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mnetplhepl iaeegkeker vftgtperiv niclasisal iiywtvyvsa dvmwkhglyi
       61 mtvfcmtlvi ypfekkpkvn hvslvdwlli igsiagsaya iweyldrfmr lgmltemdif
      121 fgclmlflgl evgrrvigws ltlvsivlil yslygfvipg hfghggfdle avvtqvyagm
      181 egyyglsakm miqyvapfil mgafleksga gdffirlafa ltrntvggpa kaavigsall
      241 gsisgsavan vsstgvltip mmkkvgyrph vagaieaaas tggqimppim gavaflmaef
      301 tqipyltivt vatgpiilyy itlmafihfe akkhnigqmk dhhipsartv csegwhffva
      361 imviivimaf gyspgmsalg giitlivihs iksrkvdfkm lyeamvlggr yslgigslvg
      421 cigiilslvg ltgvglklsw lfttlangsp lvaillvgli smilgmglas gpayivtaia
      481 vgpaladmgf plmtahfimm wfsidseitp pvglasivga gianadpmkt mftafkyaka
      541 lyilpilfyy rpalllqssl fdialtfvtv mfgliafaav wenylmrrtt llerilllgg
      601 alllfipghi wdfagiglfi ivyclqryyc pagfrqta
//
LOCUS       WP_005031540             443 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Acinetobacter
            bereziniae].
ACCESSION   WP_005031540
VERSION     WP_005031540.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter bereziniae
  ORGANISM  Acinetobacter bereziniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 443)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 443)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Acinetobacter bereziniae"
                     /db_xref="taxon:106648"
     Protein         1..443
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=51025
     Region          40..431
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mkkftiqalf dthwldiael kildpekgsa spceleyqie yaisyldkrd ehacslslpv
       61 qliikheakt wfgflddiip sgaarrywin ylnlqkfsha eqdsillekg viapvgnlri
      121 kesippinpe stlhlrkfst advadrnadf leyaqqmgai sggatgagge apkllvryta
      181 dqkvwidtyq qsfdtpdqhy lvkfprnnrs eidcnilrae yyyyhelnel gfstidtanm
      241 rliegeryps lwlprfdtew rdqrwhrygl esvysilnks agshlnhfev idslcillkt
      301 idtkfnstqf vcewlqrdll niifgnsdnh grntsflkkt gnvflspiyd fapmkadpeh
      361 virsttwgsp yeeggeyqwi qisqklapwc dpdisletlk slankllglk qrlidkgvpk
      421 qiiempvlsf dyieaklkrw ell
//
LOCUS       WP_005032175             139 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Holophaga foetida].
ACCESSION   WP_005032175
VERSION     WP_005032175.1
KEYWORDS    RefSeq.
SOURCE      Holophaga foetida
  ORGANISM  Holophaga foetida
            Bacteria; Pseudomonadati; Acidobacteriota; Holophagae;
            Holophagales; Holophagaceae; Holophaga.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Holophaga foetida"
                     /db_xref="taxon:35839"
     Protein         1..139
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14756
     Region          1..125
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mrrhrngkng fslievllvl ailgiistia ipsylgqrrr arvigdaqtn aqvlrmalet
       61 rkaengvygt tgtytwtngt psnstflpsf tpkgnskmnf slllgstglt ytltvqdptv
      121 ggatiltttq tgsttiaay
//
LOCUS       WP_005032814             353 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Acinetobacter bereziniae].
ACCESSION   WP_005032814
VERSION     WP_005032814.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter bereziniae
  ORGANISM  Acinetobacter bereziniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Acinetobacter bereziniae"
                     /db_xref="taxon:106648"
     Protein         1..353
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39657
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvkniek nfgafhalkn isldfpegql vallgpsgcg kttllriiag lesadrgqvi
       61 legtdatnsh vrerqvgfvf qhyalfrhmt vydniafglr vrpkstrpne teikkrvtrl
      121 ldlvqlgfla drypaqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 tlhdelhits ifvthdqeea levadqivvm nkgdieqigs prevyekpat pfvfdflgqa
      241 nrfegenhqg iiqigddriq lpstqntadg kviafarpne lkihaqpten aiqatflrel
      301 wiagkvmael qdrqgqliei alnpeeaklh qyrpnqtvwv sastlhlfen qva
//
LOCUS       WP_005033943             191 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Holophaga foetida].
ACCESSION   WP_005033943
VERSION     WP_005033943.1
KEYWORDS    RefSeq.
SOURCE      Holophaga foetida
  ORGANISM  Holophaga foetida
            Bacteria; Pseudomonadati; Acidobacteriota; Holophagae;
            Holophagales; Holophagaceae; Holophaga.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Holophaga foetida"
                     /db_xref="taxon:35839"
     Protein         1..191
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20835
     Region          3..191
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 msnkrftlai tgatgsafgv avlrrlaenp gveqvslllt ptgrrclede teltqedlla
       61 ispkvrhlye ndlgadissg shrqdgmvvl pcsagtlgri asgtsenlva raadvclker
      121 lplvlcvret plnrihlenl lrvndsgalv mplmpsfyhr petledlyea fatrvldrlg
      181 laeedgrrwk g
//
LOCUS       WP_005034097             348 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Holophaga foetida].
ACCESSION   WP_005034097
VERSION     WP_005034097.1
KEYWORDS    RefSeq.
SOURCE      Holophaga foetida
  ORGANISM  Holophaga foetida
            Bacteria; Pseudomonadati; Acidobacteriota; Holophagae;
            Holophagales; Holophagaceae; Holophaga.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 348)
  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 348)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Holophaga foetida"
                     /db_xref="taxon:35839"
     Protein         1..348
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38910
     Region          31..215
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <176..348
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          261..342
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpqptlqiel hrilvhyfed leavmgeggm gaayagllad lrletsdfqe psgrlsfeky
       61 italqwvdgt gripglglkl gsrkrygtyg lsgiavltqn tlgqvnqaav dgfefcwghf
      121 lrlqvriege wsvsryetsp pslalcapli eqatatgirl iseaipgqdw svcrarfayp
      181 aplyahlyrr flpfecefgq panelripaa waslpsalae esvqdfctar lqamfkeefg
      241 rsylerqirr ilwdsapdrl pdlpevarcl evsertlraa laregtsfra iqndivirra
      301 qqllsdprls vkevafalgf aqppsftraf lkatnetpeh yrsriaar
//
LOCUS       WP_005034359             360 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Holophaga foetida].
ACCESSION   WP_005034359
VERSION     WP_005034359.1
KEYWORDS    RefSeq.
SOURCE      Holophaga foetida
  ORGANISM  Holophaga foetida
            Bacteria; Pseudomonadati; Acidobacteriota; Holophagae;
            Holophagales; Holophagaceae; Holophaga.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 360)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Holophaga foetida"
                     /db_xref="taxon:35839"
     Protein         1..360
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38984
     Region          4..359
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mlrirtvvtg tgscipprri pnesfsghaf fqdygqpypa geiakiiskf kditdiaerr
       61 yaaedqvasd lafeagraai ldagidpetl dyiivaqnfg dvrpdslrtd qvptlaakvk
      121 aklgianpec vaydlpfgcp gwvqaviqah yylqsgdarr alvigaetls rvsdpfdrds
      181 miyadgagav vleaqehage vgilahatrs dtlehvgllw lgpsfnqete deelyikmkg
      241 rklyeyavsh vpgvvrrsle kagltlsdvd kvlihqangk mdeailkrig rlygvselpe
      301 gimpmtvswl gnssvatipt lldlvrkgkm eghslesgdv tviasvgagm ninsivyrmp
//
LOCUS       WP_005034957             237 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Acinetobacter bereziniae].
ACCESSION   WP_005034957
VERSION     WP_005034957.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter bereziniae
  ORGANISM  Acinetobacter bereziniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Acinetobacter bereziniae"
                     /db_xref="taxon:106648"
     Protein         1..237
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27484
     Region          1..>82
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 miqsefepvl mqvinvfcte fptelhsvyv ygsvakgtav igqsdldlcv vfvqpvddve
       61 rkisqiksdi maltsffskv dvdigvlqdv lnennrkswg awikffchpl ygdnlsrqfe
      121 nveidrsvil ainqgydqei qhyfemlatt rfdlqdsvnl kksllkriir llpltwleie
      181 qwpvnldntv lqalqkypeq kpmfeyllke lenpdvlscd cldqvqeiyl wvcrhik
//
LOCUS       WP_005034999             419 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Holophaga foetida].
ACCESSION   WP_005034999
VERSION     WP_005034999.1
KEYWORDS    RefSeq.
SOURCE      Holophaga foetida
  ORGANISM  Holophaga foetida
            Bacteria; Pseudomonadati; Acidobacteriota; Holophagae;
            Holophagales; Holophagaceae; Holophaga.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Holophaga foetida"
                     /db_xref="taxon:35839"
     Protein         1..419
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=45612
     Region          8..402
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mdtqhsekni lvincgsssl kyevfkmpqr eslgkglver igdcsgflaq tsprgeirie
       61 qpisdhavam glvakalvde esgilgslte iqgvghrvvh ggekfassva inddvmealq
      121 envelaplhn paniigieev trllphigqv gvfdtafhqt mppaaylygl prefydkyri
      181 rrygfhgtsh rfvagralhl mkrvaentnl itchlgngas vtaiesgrsi dtsmgftple
      241 gvmmgtrsgd vdpsilgfle drgysskdlq silnkksgll glsgvsndlr dvekaaqegn
      301 ahaeealevf ahkvrkyiga yaaelvkvdg liftggigqw gakmraricr rlehmgivmd
      361 ynlnghmggs egivshnysr ttilvvptne elqiamdayd ilfpgsrgdc qrrkndahl
//
LOCUS       WP_005035606             325 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Acinetobacter bereziniae].
ACCESSION   WP_005035606
VERSION     WP_005035606.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter bereziniae
  ORGANISM  Acinetobacter bereziniae
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Acinetobacter bereziniae"
                     /db_xref="taxon:106648"
     Protein         1..325
                     /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=37760
     Region          2..266
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mrdtyldsck atliflvvlg hflermigwd dpfnhallgt iyfihmpafi fisgmlfnek
       61 kwrknilffi slylpfqilf pafdaiwsgq fqinwnlfer pywilwyllg miawtmithf
      121 liktkfplli alifalcigl spwnnyqysi griftflpff vvgalygkei lvkiqqshfs
      181 qvvslsllga iailvyftql npfwlygsls ysqlkvsipv gigmrlacll isslgiyatf
      241 vwikslnqhf vhlgqntlav yllhgfvvml varywqldfn lfievsicii lsvltcwilq
      301 qsifdrglrr lslwlikpae klgfk
//
LOCUS       WP_005036276             720 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Acinetobacter
            calcoaceticus].
ACCESSION   WP_005036276
VERSION     WP_005036276.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 720)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..720
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..720
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=79635
     Region          31..716
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 msllrldrlh ycilmsmgci ssplvwaddl aqditvlptl hveatrtdtt ylqtpasvfr
       61 vdapqadtss qvnltevvkg ipslqirnre nyaqdlqlsm rgfgarstfg vrgirlyvdg
      121 ipatmpdgqg qtsnidlssl dhvevltgpf sslygnssgg tiltstkegq gkdsielsys
      181 ggshdksrag lvlqggakga nepsyvisss yfdtngyreh sgaekvlnna klswnlddgs
      241 kinwvtnyvk ihaddpqgls ytqwkanpkq vndaeniykv rkdieqtqtg mtwskpindk
      301 nelyvmaylg nrqvtqyqsi pmstqeannn qaggvidfer nyygtdlrwt gkellpnttv
      361 svgvaldamd edrkgfenfn lvngqpsygv kgnlrrdedn tlwnidpylq aswqflptwr
      421 lntgvrysnv hykskdnyls ngddsgktdy skvlpsvals wqilpelmay msyakgfetp
      481 tftemayrrd gesgfnfdlt astsdtyetg lksqnslgdf tlvvfqtktk ddivsagnsn
      541 grstfrnadk tlregveftw nkklwrdlta tasyayldat fdadipasgs iaqipsgnai
      601 pgiaknqaya slawqpthgl yggvdvqymd kvyvndtnsd aapsysvtsa nvgyawvvnd
      661 wkiisfarvd nlfdknyags vivndstqik vngqmvpakr yfepadgrnw saglrvikqf
//
LOCUS       WP_005036593              95 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Holophaga foetida].
ACCESSION   WP_005036593
VERSION     WP_005036593.1
KEYWORDS    RefSeq.
SOURCE      Holophaga foetida
  ORGANISM  Holophaga foetida
            Bacteria; Pseudomonadati; Acidobacteriota; Holophagae;
            Holophagales; Holophagaceae; Holophaga.
REFERENCE   1  (residues 1 to 95)
  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   2  (residues 1 to 95)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Holophaga foetida"
                     /db_xref="taxon:35839"
     Protein         1..95
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10217
     Region          22..86
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mprilrtavl alalplfagd rtpqapvnin tasvtelmql pkvgaktaer ivayrkqhgg
       61 fkrteelmnv kgigeksfak lrthlsvgtk pankp
//
LOCUS       WP_005037036             336 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005037036
VERSION     WP_005037036.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 336)
  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   6  (residues 1 to 336)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..336
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38184
     Region          22..202
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          75..336
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mgqltdasvv lrfgyqairr aglpteeilt kagvalnqvd tnartplsaq yafwtaaqev
       61 skdpdiglhl gehlplyrgq viehlfissd tfgeglkral ayqrlisdaf daklvieegr
      121 cyltngeqig adnlvnrhfs ecaisgilrf fkfitegqfh pifidfnfse gaaedeyfrv
      181 ygcpvslgqk etrlyfdpai ldfqlwqaep ellqlheqla ieklqelary dlvgevrrai
      241 gstlesgett letvaaqlni tprrlrtqls eantsfqqil sdyrcrlakk llantnesve
      301 rivyltgfse pstfyrafkr wtnetpveyr krkqhr
//
LOCUS       WP_005037398             185 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Holophaga foetida].
ACCESSION   WP_005037398
VERSION     WP_005037398.1
KEYWORDS    RefSeq.
SOURCE      Holophaga foetida
  ORGANISM  Holophaga foetida
            Bacteria; Pseudomonadati; Acidobacteriota; Holophagae;
            Holophagales; Holophagaceae; Holophaga.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Holophaga foetida"
                     /db_xref="taxon:35839"
     Protein         1..185
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20161
     Region          4..178
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mnevvktilk rrstraytps qiseeelhvl letarfapsg mnrqpwhftv vqnpetlhri
       61 neacrqvllg sgvkameera kgnnfsicyq aptlilvavd eqvhtgrldg avalenmfla
      121 aesmglgscw ihavsmlfng ganeelrkel hipagfvvig sgafghkaae aqaaprkent
      181 itvlk
//
LOCUS       WP_005038322             160 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acinetobacter calcoaceticus].
ACCESSION   WP_005038322
VERSION     WP_005038322.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..160
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=17418
     Region          8..105
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mnkyyilrfn qgvtlielmv vivivaifas iaipsyqsyn rratasaakg eilklaeqle
       61 rhksknftyr gftttsvtlp rggytieisd dttagnlltn gaangqtwvi katttdsknf
      121 nfiaknsdlr cqsltatavd ndcggtvtcn vcetnsenwq
//
LOCUS       WP_005039787             729 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Acinetobacter
            calcoaceticus].
ACCESSION   WP_005039787
VERSION     WP_005039787.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..729
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=79563
     Region          25..729
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 merssalslp nfkfkvstls yaiglactyl aipahaedta tsalptitik aqgnwleean
       61 aetvhkhpga rtiidrkrld etaatsirea lkqipgvqaq dssgtggsdv slnigvrgla
      121 srlsprstvl vdgvplsfap ygqpqlslap vsigniesvd vvrgagsvrf gpqnvggiin
      181 fatrsipqdf sgtvsltsey asgtdqvkls pnlfvggtld nglglallys gtkgngyrea
      241 nnkididdvm lksayqfndk dsvalnlhhy egrgempegl tqaqyaenpy qssgeknyfa
      301 grrtdvslry nhkdeknnfe vltyyidsfr tsnletvlas gdkrldsapr dykvyaiepr
      361 ysriyelgnt qnevtvgyry lkeessefag rtasyaagss apdfaprsss eggtkahavy
      421 vdnrmelgrw titpgvrfes iethnnftgy nkgqpntvyp kidsdeflps lsvmysanen
      481 wnifanagvs fgpqqysqla rlegttatat teglhpeksn nyeigtkylg nglnaeftvf
      541 yldfdkelsl vrdagnngiw tdlgatshkg vetgisydfg qlsdaleglk vygnytftka
      601 vaeagqfkdk dlpfysrhvg nvglgytmdk walnadmfaq skqhspdlpd snvyqteeta
      661 dgkygdipgy ttfavrtsyd lssqvkglki aggiknvfdk qyftrstdst ggkyvgqprt
      721 fylqisfdf
//
LOCUS       WP_005040313             349 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            calcoaceticus].
ACCESSION   WP_005040313
VERSION     WP_005040313.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 349)
  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 349)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 349)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 349)
  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   5  (residues 1 to 349)
  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   6  (residues 1 to 349)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..349
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40153
     Region          28..218
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          93..347
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkdpyglska sipisyahll leimvdkgfs aleilkkski pltlldqlda ritpmqwskl
       61 aweslilskd sglgyeyglk lrltahgpmg yalmsspnlr qaievstqff nmrlkdyria
      121 llddhefsii eikethpvvs nqpaqaetlr rffyeclmfg viqagqflre hdladielsv
      181 dwsepsyhka yqhllptihf nqptnqiryk kqlldlpikm adpiafkqal aqceaeqlrf
      241 seqikdiclt vkaelnlkpq lgyptfdeia drlnmssrtl rrhlnqvgss yvqlleeaqq
      301 keaenlllns dmeiqeialy lgyiqptnft rafkkwtgmt pihfrkkte
//
LOCUS       WP_005041626             382 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Acinetobacter
            calcoaceticus].
ACCESSION   WP_005041626
VERSION     WP_005041626.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 382)
  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 382)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..382
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44617
     Region          13..371
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mtsslkqltl fnqglgktsr fakgmdgtlq aiehlgyvqi dtisvverah hhilwsrvpd
       61 ydlshlnnlv rerqifeywy haasylpmkd yryalpamms vrkgesryfn rgdqhlmnei
      121 larvraegri rlrdidknnk kslgnwwntg pgrrafqqly mqgdlmicer ngmekvydlt
      181 erclpenidl sqptlyeyaq ylfnttlrah gaftwkqlvh lkgkdlketm rvvlkeqida
      241 gvvsaiklvd gqtlyvdvaa ieqnvntdfg lkilspfdns lihrdrltsl fefdyriecy
      301 vpaakrvfgy fclpilyqde lvgridckah rtvkelevis ihlektikdk elfffeleqe
      361 ikrfaefnqc tiinnkvikl ir
//
LOCUS       WP_005041981             340 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            calcoaceticus].
ACCESSION   WP_005041981
VERSION     WP_005041981.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 340)
  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 340)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 340)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 340)
  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   5  (residues 1 to 340)
  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   6  (residues 1 to 340)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..340
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38702
     Region          25..208
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          86..339
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkyawafers vhsvrlmadf avesgisyqt ileetgisqq qlldpnmvvt gqqelqvihn
       61 lveqlgdrpt lgldvgtryh fttfgplgma lmssasirea ldlaltyfsl tfaftrflvs
      121 dtdegiriei edegvppsvr qfilerdaaa litvqrdlvq dnfcqymafa fqpkaevqpy
      181 idlfgilpef gaaknfvlld phkvdqklqm andlilhtae eqcrqildrr qtqkkfinlv
      241 qqqlmkvrge mpsmdmvadr lhlnartlrr hlsqegmtfi qireevrqvl aeqyltlpka
      301 sieqiaewlg yaepasfiha ykrwhgktph avrlsgksst
//
LOCUS       WP_005042913             335 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            calcoaceticus].
ACCESSION   WP_005042913
VERSION     WP_005042913.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 335)
  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 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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (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   5  (residues 1 to 335)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37864
     Region          23..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          251..328
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpqtatalas wvkaiqkale kagvdsqpll kqagldvqal ndpdaryslk qtanlwklav
       61 qatedscfgl kvasqvnqnt fhvlghslit sttlkemflr iiryfrivtd ipelefygeg
      121 knhyfvihvp devqpesida fisvfirssr alqgsvfspl rielrrsepe dlenfksilk
      181 apivfnapkd mivfdtatie qpldggnpsl tqeydeiinr ylarfdkeni larvkvklie
      241 klstgdfqqq dvakslglsi rslqrklsae ntsyselldn trhelalsyi knsshnitei
      301 ayilgftdvs sftrafrrwt dlsplhyrek hlsls
//
LOCUS       WP_005044000             187 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acinetobacter calcoaceticus].
ACCESSION   WP_005044000
VERSION     WP_005044000.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..187
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=20616
     Region          3..>103
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mlkqraftli elmvavviia ilaaiaypsy tryfekkdla vakqeaqria telerfkakn
       61 fsykgfdaty lynagtvtpy dkttgslllp ldatsttaky tltlldstqh lplsilkdsd
      121 dketadsakv qglnwvitve rakdssgepk qannydllin sdgfrcmtkv knvvsgytnc
      181 gsssetw
//
LOCUS       WP_005044729             142 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Acinetobacter calcoaceticus].
ACCESSION   WP_005044729
VERSION     WP_005044729.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..142
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16087
     Region          1..141
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlsyfllfis afgaatllpl qseavlatll lkgqysalll isiatlgnvl gscvnwwlgl
       61 kieqfkhrkw flvsekrlqq aqsfyhkygf yslllswtpi vgdpitlvag lfkenfwrfl
      121 giviiakggr ylfiywvvmg fi
//
LOCUS       WP_005044123             334 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            calcoaceticus].
ACCESSION   WP_005044123
VERSION     WP_005044123.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 334)
  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   5  (residues 1 to 334)
  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   6  (residues 1 to 334)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..334
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38869
     Region          27..201
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          92..334
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mpqlknytgs vygglghllk ayceanqlav peqleqiqnl erfdyviwrd lleviyklap
       61 kpglgleiak yvqpkhlgii aylalscdnl gealiryhdf hrliydgspl vvelygqyas
      121 irweatelhp tqltdeiaia lviqflrlfm shqdvhlhev hflnnapkni rvyeqyfqcp
      181 vrfsqprtql lipiteinkp lssadhtlqq llvqqaqall eqlpnstqld qrlqhsiltg
      241 lqkdqyqiey isaqlglsvr qlqrhlqqqn ttfqervqqv rfmlateylk dphlslqeia
      301 lllcyseqsa fqrafkhwtn qtpqqwrdqf ldke
//
LOCUS       WP_005046158             277 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            calcoaceticus].
ACCESSION   WP_005046158
VERSION     WP_005046158.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 277)
  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 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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..277
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31982
     Region          30..270
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <166..270
                     /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 msnwvdiskd tntgietira hftghaydph whssyligvt esgiqqfhcr kkqinshagq
       61 vfmlepeeih dghapasdgf tyqmlylhpd wlkqriqglf hnspdhyelv idaplksdeq
      121 laiitsqafq hlhykemniv kdnsldllih hiaqgkwlkk ahqsssthtp riahqirdil
      181 hdhlfedigl ediarmigld ryhihrifka tfhlaphqyl iqlrltrard llarsispaq
      241 vasdlcfadq shlsrwfkrc ygltpaayrk ictnlqd
//
LOCUS       WP_005046183             339 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            calcoaceticus].
ACCESSION   WP_005046183
VERSION     WP_005046183.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 339)
  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 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 339)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 339)
  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   5  (residues 1 to 339)
  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   6  (residues 1 to 339)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..339
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38967
     Region          27..211
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          91..336
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msiqlywdfp rsisairill migqqhglts escienthis lndlsqpnfe vkaeqeflvi
       61 rnllklldpt lplsieaglr hhtttfgawg failssqtmk ealhfamryf qlssifcnle
      121 viqediytll ifdhsqlpdd lacflverdl itvisiqrdv lpiqfpvmsi nvalpapvya
      181 dkfpeltgyp iqfnqprsci ifesslldlp lpqadpfira ryeeecqqlw trrsslgsys
      241 qkvrnillqq psqmpridem aahlqvnlrt lqrhlaiegv tyeqliddir kdlaedllkt
      301 tnltveevai qlgysevsaf srafkrwkgi sprnfrwqk
//
LOCUS       WP_005046722             358 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            calcoaceticus].
ACCESSION   WP_005046722
VERSION     WP_005046722.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 358)
  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 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   3  (residues 1 to 358)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 358)
  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   5  (residues 1 to 358)
  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   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..358
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41329
     Region          34..220
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <195..350
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtagglhkki rdnsgskvli glvihflehv nffginreel llqgeliddk lsdsnqcval
       61 yhfermityt yntcknpvia ldffqkmdst aygvlghlvp lssnlkqaid tlkefqplig
      121 cigdislqlr sdtvywkwdc rsddpifnrc aneynlawwv slirlvrneq fsvlkavhfk
      181 hslakpelqn yyneffgcsv yfdqpetall llpkslnmal rtgnaglyes vrifasklle
      241 qqkaeknftq qvksqiylll hkdklsrenv aeqlgvnvrt lsrklqqdgn lsystlldqv
      301 rfelainyle vhhehsvlfi skalgfytsh sfiswfkskt nltpmqyrkn knteypqy
//
LOCUS       WP_005046870             349 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            calcoaceticus].
ACCESSION   WP_005046870
VERSION     WP_005046870.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 349)
  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 349)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 349)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 349)
  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   5  (residues 1 to 349)
  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   6  (residues 1 to 349)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..349
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40082
     Region          28..218
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          93..347
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkdpyglska sipisyahll leimvdkgfs aleilkkski pltlldqlda ritpmqwskl
       61 awesiilskd sglgyeygik lrltahgpmg yalmsspnlr qaievstqff nmrlkdyria
      121 lldehefsii eikethpvvs nqaaqaetlr rffyeclmig viqagqflre hdladielsv
      181 dwsepsyhka yqhllptihf nqptnqiryk kqlldlpikm adpiafkqal aqceaeqlrf
      241 seqikdiclt vkaelnlkpq lgyptfdeia nrlnmssrtl rrhlsqvgss yvqlleeaqq
      301 keaenlllns dmeiqeialy lgyiqptnft rafkkwtgmt piqfrkkei
//
LOCUS       WP_005047299             320 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Acinetobacter
            calcoaceticus].
ACCESSION   WP_005047299
VERSION     WP_005047299.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 320)
  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 320)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..320
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35508
     Region          22..74
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
     Region          <253..312
                     /region_name="repM_Acin"
                     /note="replication initiation protein RepM; NF038290"
                     /db_xref="CDD:468455"
ORIGIN      
        1 msldatnwaw kvhiptkkgg slpalklvvl lsmadrased htcypsakrl aadckidrkt
       61 vmkilaelsd dglitdtger kgqtkqvvvy rlngvvgred tvptmgpleg enldgkstnv
      121 gtvptveqfq qfhervptip vkgpnvgtrn llknlseesk nkktwlslkk lgeeirlatd
      181 qetyeqikna twfdrelraf elynaeknlc delmhyhfad wlinacgkyq areqtgfrns
      241 gssvrgapsa qeklsdkqvh tfaqklsqhp efasqfaaag esydqlaari avklsdpaqa
      301 kqwepylkqv gfkgslqgaa
//
LOCUS       WP_005048171             340 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            calcoaceticus].
ACCESSION   WP_005048171
VERSION     WP_005048171.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 340)
  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 340)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 340)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 340)
  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   5  (residues 1 to 340)
  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   6  (residues 1 to 340)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..340
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38774
     Region          25..208
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          86..339
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkyawafers vhsvrlmadf avesgisyqt ileetgisqq qlldpnmvvt gqqelqvihn
       61 lveqlgdrpt lgldvgtryh fttfgplgma lmssasirea ldlaltyfsl tfaftrflvs
      121 dtdegiriei edesvppsvr qfilerdaaa litvqrdlvq dnfcqymaft fqpkaevqpy
      181 idlfgilpef gaaknfvlld phkvdqklqm andlilhtae eqcrqildrr qtqkkfinlv
      241 qqqlmrvrge mpsmdmvadr lhlnartlrr hlaqegmtfi qireevrqvl aeqyltlpka
      301 sieqiaewlg yaepasfiha ykrwhgktph avrlsgksst
//
LOCUS       WP_005049956             345 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            calcoaceticus].
ACCESSION   WP_005049956
VERSION     WP_005049956.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 345)
  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 345)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     Protein         1..345
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38714
     Region          21..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          251..331
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mnpelpgtyi nlivetvkrw gvsceqlldg sgitvdqlkk pywyvefnhl nqlieraiel
       61 ckepalagyl alemtascyg svgmaaivsp nlgealkile qfigsrcevf kpelkqknny
      121 aywfihqpvk efqlspnani fllvgfvqia kkltglsnlg kvelqmpepi gfaqissqla
      181 vtclfnqkrn swifskdyla qpvltadpml aplvnaqckr dieklklhsg wkgqvkqvae
      241 kllmngqget vklgqvaqvm nisertlqry latentsfti lvdslkkqha qkllaqnnms
      301 iekvaltlgy aetshftraf krwmgvtpky fqthskmdel sshlg
//
LOCUS       WP_005054318             341 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter beijerinckii].
ACCESSION   WP_005054318
VERSION     WP_005054318.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter beijerinckii
  ORGANISM  Acinetobacter beijerinckii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 341)
  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 341)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Acinetobacter beijerinckii"
                     /db_xref="taxon:262668"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38445
     Region          32..211
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          255..336
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mktpstrqdq gipgvyglll ldvvsrwgyn detlfapfhl tseqladpny riptpianel
       61 vkhslrltge stlgfhlgtq mrisihgfig yaimtahdit daialasrfi qlrlpflqly
      121 fstfgpkatl qlqcdievep lrteiilglt igimtmakal tgiedlsgev dldfpepigf
      181 ekyrdkltsi vrfnqphlis sfdkkylglk mvnadpiasq iainqcetel salgerrrla
      241 mrvrdiltns eqhylsiesv adrlhmsdrt lkrqlaaegt sfstlvdevr yrhatsllsr
      301 tdysleqiad elgysdvanf srafkrwsgr spsnwrkdpy l
//
LOCUS       WP_005055301             105 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Acinetobacter beijerinckii].
ACCESSION   WP_005055301
VERSION     WP_005055301.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter beijerinckii
  ORGANISM  Acinetobacter beijerinckii
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Acinetobacter beijerinckii"
                     /db_xref="taxon:262668"
     Protein         1..105
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11785
     Region          2..104
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(7..8,26..27,35,38,40..41,43,46..47,49,57,62,69)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(26,57..58,60,87)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mqdtnelqrq ilevvalipy gkvasygqva klaglpkhar lvgyvlkhld sqskipwhrv
       61 insqgkisvh rlneqgenvq knllneegiy llnnkvnlkt fgwnt
//
LOCUS       WP_005057319             366 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter beijerinckii].
ACCESSION   WP_005057319
VERSION     WP_005057319.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter beijerinckii
  ORGANISM  Acinetobacter beijerinckii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 366)
  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 366)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 366)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 366)
  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   5  (residues 1 to 366)
  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   6  (residues 1 to 366)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Acinetobacter beijerinckii"
                     /db_xref="taxon:262668"
     Protein         1..366
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41862
     Region          51..232
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <237..358
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mryptglktl fcggqnglmp irtsdkndqq qfipptilas lihyaeqqqw dyaawfensg
       61 ldiaqirqtq gvvrftqlcd virqamtayq hpdlglklgs seglismgil gfamqscktv
      121 adaldialry hrisgsvlni nfslqtdmce vevteshpca dlkaffydel fssiitclna
      181 mlgdhddvis lelsyfpnqy qeqyktifgc piqfnspkni irfntsmlqr glknyspany
      241 ataiqiceqa lkeidqlnqv gyvhlldhli eqqlperfkm qqaaehlris erhlrrqlll
      301 eglsfqqirq nvlerkakql leqnlsmsei slqlgfselr efrrafkrwt gqapsvykhe
      361 iillna
//
LOCUS       WP_005059382             141 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Acinetobacter beijerinckii].
ACCESSION   WP_005059382
VERSION     WP_005059382.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter beijerinckii
  ORGANISM  Acinetobacter beijerinckii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Acinetobacter beijerinckii"
                     /db_xref="taxon:262668"
     Protein         1..141
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15963
     Region          1..141
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 msylllflsa fgaatllplq seavlmtllv qgrsnpfyli lvatignvlg scvnwwlglk
       61 iehfkdkkwf pvseqrllqa qqiyhkygfy slllswtpvi gdpitliagl mkenfwrfll
      121 ivtiakggry ltlyalylgl f
//
LOCUS       WP_005059353             386 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Mycobacteroides abscessus].
ACCESSION   WP_005059353
VERSION     WP_005059353.1
KEYWORDS    RefSeq.
SOURCE      Mycobacteroides abscessus (Mycobacterium abscessus)
  ORGANISM  Mycobacteroides abscessus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacteroides.
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   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   4  (residues 1 to 386)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Mycobacteroides abscessus"
                     /db_xref="taxon:36809"
     Protein         1..386
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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]"
                     /note="Members of the family are the ATP-binding subunit
                     of ABC transporters for substrates such as betaine,
                     L-proline or other amino acids, choline, carnitine, etc.
                     The substrate specificity is best determined from the
                     substrate-binding subunit, rather than this subunit, as it
                     interacts with the permease subunit and not with substrate
                     directly.; Members of the family are the ATP-binding
                     subunit of ABC transporters for substrates such as
                     betaine, L-proline or other amino acids, choline,
                     carnitine, etc. The substrate specificity is best
                     determined from the substrate-binding subunit, rather than
                     this subunit, as it interacts with the permease subunit
                     and not with substrate directly."
                     /calculated_mol_wt=42429
     Region          16..322
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 msdvtqnatt tggarilldg vtklydgkst pavdnvtmei pagetvmfvg psgcgktttm
       61 kminrliept sgrifigded vtdknpdelr rhigyviqga glfphftvgd niaivpklln
      121 wdkqriderv delldlvnld paqyrnrypr elsggqqqrv gvaralaadp pvllmdepfg
      181 avdpitrqrl qdellrlqee lsktivfvth dfdeavklgd riailregsq ivqydtpevi
      241 lanpandfvr gfvghgaalk qltmtrvrdv elheaavahv gddpaqaiea aesidrehvi
      301 vldsherplr wssldelrap nalqrvsqde dlekvslast ltdaledmlt sshgvvvvtg
      361 rrntyqgvir vetimdamae mraaaq
//
LOCUS       WP_005059884             192 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acinetobacter beijerinckii].
ACCESSION   WP_005059884
VERSION     WP_005059884.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter beijerinckii
  ORGANISM  Acinetobacter beijerinckii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Acinetobacter beijerinckii"
                     /db_xref="taxon:262668"
     Protein         1..192
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=21471
     Region          19..>118
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mdkinkistc ltcstyslsr trggstgftl ielmvvlviv aiftaiaips yqeyvrradv
       61 stvqqemqki aeqlerhkak nftyrgfdpn fiynvvgpmd yvtlprgavg saikytitiy
      121 dgdgstrllt datvpavira rswvmvaktn nvrnydllmt seglecknkt kvnikfnttn
      181 krwecgvgee sw
//
LOCUS       WP_005060055             626 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Acinetobacter].
ACCESSION   WP_005060055
VERSION     WP_005060055.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 626)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 626)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 626)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 626)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..626
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=69685
     Region          2..626
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mqstakkaal pvmtlaalgv vfgdigtspl yairecfrtg hmpineasvl gilslifwcm
       61 nlsisykyvs vimradnnge ggiisllaln lrstvfsdkn kiylialgfi gaslffgdgi
      121 itpaisvlsa ieglslitpa ldqwlvpial giltalfmvq rhgtatmgkf fgpitllwfi
      181 sigliglwsi iqtpyvlmmi npywalnfvf eqpaiafitm gavvltmtgg ealyadmghf
      241 grmpiklawf iivlpcllln yagqgalllr npqaienpfy ilvpewalfp miglataaav
      301 iasqavitgv fsvanqaiql rylprltvhh tsdveqgqiy lpfinwvlfi svvilillfe
      361 ssaelasayg vavtmtmlcg tilistlayg vwrwawwkva lftipflfld lvfvastslk
      421 ilaggwvpil igvvvytilm twkrgreivy nrmetnalpi elfiksigms kethfvpgea
      481 ifltgtpniv phamlhnikh nkvlhdrnvm ltvytqdipy vaaadrlkve kledhfyrif
      541 vyygfkdqpn ipnaleqayk eldfefdmmq msffisrdri vhtvgdgmsp wreklfismq
      601 rntspvsdfy qiptnrvvel gsqiei
//
LOCUS       WP_005060048             335 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter beijerinckii].
ACCESSION   WP_005060048
VERSION     WP_005060048.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter beijerinckii
  ORGANISM  Acinetobacter beijerinckii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 335)
  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 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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 335)
  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   5  (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   6  (residues 1 to 335)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter beijerinckii"
                     /db_xref="taxon:262668"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38820
     Region          25..201
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          82..330
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msqlknyigs vfgglghllk ayceaehiav peqlqlvqnq erfdyviwrd lledlnrlhp
       61 ktglgleiae yvqpkhlgii aylalscenl gealaryhdf hrliydgspl vvefnepyvs
      121 irweapephp tqltdeiaia lmvqflklfm sgetihlhev hfvniapkni svyeqyfhck
      181 vrfeqpktql llpvaeafkp lktgdhtlqq lllqqaqall dklpnstqld qrlqhailtg
      241 lqknqyqidf iaeklglsvr qlqrhlqqqn ttfqervqqv rfmlateylk dphlslqeia
      301 lllcyseqsa fqrafklwtn ltpqqwrknn tiyns
//
LOCUS       WP_005060063             639 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Acinetobacter beijerinckii].
ACCESSION   WP_005060063
VERSION     WP_005060063.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter beijerinckii
  ORGANISM  Acinetobacter beijerinckii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Acinetobacter beijerinckii"
                     /db_xref="taxon:262668"
     Protein         1..639
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=72754
     Region          66..>514
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mpnqdqlkmh spnlvdsnie kiaalfpncv teaqgensev kktidfdllk qelshvlveg
       61 eqeryrldwv gkkesiltan apiaktlrpc reesvnfdst enlfiegdnl ealkllqeny
      121 lgkvkmiyid ppyntgndfi yeddfaestd affersnqtd degnklvant dsngrfhsdw
      181 lsmmysrlkl arnllsddgi iffqigqeev snaekmlsev fgdsnklaii srvaktasda
      241 gkffapstdy licyaknesl srsfndevkv dlfkkvenvg prkgelyrdd valyqssltl
      301 ersrnaryfi ecpdgtkcip pegkrwrvve etflgmkdrn eivfketkss plfdeignks
      361 kwnlytksyl tdrqekgaap rnyidqfinr qgadlikkig ipfdfskpvg likylikiin
      421 qdkditildf fagssttaha vmqlnaedqg hrkfimvqlp eptdekseaf kagykniaei
      481 skericragq kiltenaeke gienldigfr vlkidstnmk dvyytpdayt qadildladh
      541 ikedstsedl lfqvmldwgl elslpieqki iqgkevfyva gnslvacfde infamvdeia
      601 qdkplrvvsa eraiqldhdk tnikerfkql spetevkfi
//
LOCUS       WP_005060315             341 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Mycobacteroides].
ACCESSION   WP_005060315
VERSION     WP_005060315.1
KEYWORDS    RefSeq.
SOURCE      Mycobacteroides
  ORGANISM  Mycobacteroides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Mycobacteroides"
                     /db_xref="taxon:670516"
     Protein         1..341
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=36775
     Region          6..330
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mtaentitvr gankhygdfa aldnidfdvp sgsltallgp sgsgkstllr siagldnpds
       61 gtitingrdv tgvppqrrdi gfvfqhyaaf khltvwenva fglkirkkpk aeikkkvddl
      121 levvglsgfh trypaqlsgg qrqrmalara lavdpqvlll depfgaldak vredlrawlr
      181 rlhdevhvtt vlvthdqaea ldvadriavl nkgrieqvgs pedlydrpan sfvmsflgpv
      241 aklngilvrp hdirvgrnad laraaaegtg ettgvtkatv drvvylgfev rveltsaatg
      301 eqftaqitrg daealglreg dpvyvrvtrv pdvgelaeva s
//
LOCUS       WP_005062168             354 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter beijerinckii].
ACCESSION   WP_005062168
VERSION     WP_005062168.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter beijerinckii
  ORGANISM  Acinetobacter beijerinckii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 354)
  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 354)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 354)
  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   4  (residues 1 to 354)
  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 354)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Acinetobacter beijerinckii"
                     /db_xref="taxon:262668"
     Protein         1..354
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40545
     Region          28..218
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          265..346
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mrdpfglfqe nisvsyahvl leiteaygie nqtvlhntgl vlaamkhada kmsahqwskl
       61 vvnalqltgn hrlgieyglk lrptshgalg faflscadve taltlcqqyf ctriqnftpe
      121 wtvdenfvyv ylndvhpvrl gdeqqsaqlr sflveclifg aihflslfsk eliaqsevfl
      181 dweesddyqc ielskvkihf sqkrnglrfp kfflncknkn adqvsfqqal lycendkgrl
      241 vkenirdlqk sirsellyns sngyptlpmi aehlnmsert lkrhlqaqgt tflqiladvr
      301 fteakkmlqq kqysiqdias ivgyeeatnf irafkktfge tpsqyrkrcl sivn
//
LOCUS       WP_005059418             264 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Acinetobacter
            beijerinckii].
ACCESSION   WP_005059418
VERSION     WP_005059418.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter beijerinckii
  ORGANISM  Acinetobacter beijerinckii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acinetobacter beijerinckii"
                     /db_xref="taxon:262668"
     Protein         1..264
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29637
     Region          1..257
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 msnlavnlsm iftevplier falahahgfq hveiqfpyel eiidiqnqle qynlslclin
       61 vpagdlmqgg nglagipgke vefhhalela iryatalnvp rvnilagkqp ldadllpcln
      121 tlssnlklac hllseqgiep vfemingtdm prflvqniaq aqemleainh palkmqydcy
      181 hmammgedvl aglqenlhqi ghiqfadcpn rhepdtgsia ykqifdwllq sdyrgfigae
      241 yrpqyqsdqs lawkkkyfsn dvnt
//
LOCUS       WP_005064258             352 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SPOR domain-containing protein [Acinetobacter].
ACCESSION   WP_005064258
VERSION     WP_005064258.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..352
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38136
     Region          <28..>273
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          270..344
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 msmnnkqrwm ggvvllgggv llaalllkgn eeikqveaqp sastspktqt kpkettegqm
       61 vqlqplavdv etekrlleeq rrarekavae qearaaefla mqqqaeadaa rkaaaeyaai
      121 narrtaaqes sdnippelvg eakaknqqtn tvnkttdtsk idadkkaaea krqaeadkka
      181 aeakrqaead kkateakrqa eadkkaaeak rqveadkkaa eakrqaeadk kaaeakrqae
      241 adkkasdakr kaeaekkaea ekarelleng dkkwmvqval aanqanadav vsklrakgyk
      301 vttsptskgi rimvgpakdr dtadaarkki tsdsslnmks awvidwvpld qr
//
LOCUS       WP_005064307             709 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor family protein
            [Acinetobacter].
ACCESSION   WP_005064307
VERSION     WP_005064307.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..709
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=78309
     Region          35..705
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 msllrldrlh ycilmsmgci ssplvwaedl tqdvtvlptl hveatrtdtt ylqtpasvfr
       61 idapqvdtss qvnltevvkg vpslqirnre nyaqdlqlsm rgfgarstfg vrgirlyvdg
      121 ipatmpdgqg qtsnidlssl dhvevltgpf sslygnssgg tiltstkegq gkdsielsys
      181 ggshdksrag lvlqggakga nepsyvisss yfdtdgyreh sgaekvlnna klswnlddgs
      241 kinwvtnyvk ihaddpqglt hdqwnanpkq qvpflkqfnv rkdieqtqtg vtwtkpindk
      301 nelyamaylg nrqvtqyqsi pkstqdasin haggvidfer dyygadfrwt gkellpnttv
      361 svgvaldamd edrkgfenfn lvngqpsygv kgnlrrdedn tlwnidpylq aswqflptwr
      421 ldtgvrysnv hykskdnyls ngddsgktdy skvlpsaals wqilpelmgy vsyakgfetp
      481 tftemayrpd gesgfnfdlt astsdtyetg lksqnqfgdf tlavfqtktk ddivsagnsn
      541 grstfrnadk tlregvefaw nkklwrdlta tasytyldat fdadipalgs iaqipsgnai
      601 pgiaenqaya slawqpshgl yggvdvqymd kiyvndtnsd aapsysvtsa nvgyawvmgd
      661 wkvnsfarvd nlfdknyags vivndgngry fepadgrnws aglrvikqf
//
LOCUS       WP_005065915             336 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Mycobacteroides abscessus].
ACCESSION   WP_005065915
VERSION     WP_005065915.1
KEYWORDS    RefSeq.
SOURCE      Mycobacteroides abscessus (Mycobacterium abscessus)
  ORGANISM  Mycobacteroides abscessus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacteroides.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 336)
  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 336)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Mycobacteroides abscessus"
                     /db_xref="taxon:36809"
     Protein         1..336
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36407
     Region          30..213
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          257..335
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpptgarpfw dyprspaatr nlvdaardrg fgpdaclegt giteadltap davitgvqel
       61 rvvrnllalt kdpaglgiev gtryqlasag ilgfallssp tmgealsvgl rfsqlsstfh
      121 hftlkvgetd stfdlddndv ptdvrqflle rdlmaiagiv pilfggampa garimlrtgp
      181 qtplrllael ltvefdsprn alvfptalla eplptadpht aalcvrqcee llelrrarsg
      241 vageirnqll rlpghvptmg qvaaslhige rtlhrrlare gtsyrallde vretlarell
      301 rngfsvrevs drlgysepaa fthaytrwrg mppsar
//
LOCUS       WP_005066247             264 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: hydroxypyruvate isomerase family protein
            [Acinetobacter].
ACCESSION   WP_005066247
VERSION     WP_005066247.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..264
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29504
     Region          1..257
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mgrlainlsm iftevplier falahaqgfe yveiqfpyel siadiqtqle rynlslclin
       61 vpagdlmqgg nglagipgqe tafhealela iryatalnvp rvnilagkqp ldadllpclk
      121 tlaanlklac nllsehdiep vfemingtdm prflvqniaq gqemleavnh palkmqydcy
      181 hmammgedvl eglqeninli ghiqfadcpg rhepdtaqip yeqifswlkq ssyqnyiaae
      241 ykpengsnqs ltwkkkyfsd dvni
//
LOCUS       WP_005066537             386 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Mycobacteroides abscessus].
ACCESSION   WP_005066537
VERSION     WP_005066537.1
KEYWORDS    RefSeq.
SOURCE      Mycobacteroides abscessus (Mycobacterium abscessus)
  ORGANISM  Mycobacteroides abscessus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacteroides.
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   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   4  (residues 1 to 386)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Mycobacteroides abscessus"
                     /db_xref="taxon:36809"
     Protein         1..386
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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]"
                     /note="Members of the family are the ATP-binding subunit
                     of ABC transporters for substrates such as betaine,
                     L-proline or other amino acids, choline, carnitine, etc.
                     The substrate specificity is best determined from the
                     substrate-binding subunit, rather than this subunit, as it
                     interacts with the permease subunit and not with substrate
                     directly.; Members of the family are the ATP-binding
                     subunit of ABC transporters for substrates such as
                     betaine, L-proline or other amino acids, choline,
                     carnitine, etc. The substrate specificity is best
                     determined from the substrate-binding subunit, rather than
                     this subunit, as it interacts with the permease subunit
                     and not with substrate directly."
                     /calculated_mol_wt=42428
     Region          16..322
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 msdatenati tggarilldg vtklydgkst pavdnvtmei pagetvmfvg psgcgktttm
       61 kminrliept sgrifigded vtdknpdelr rhigyviqga glfphftvgd niaivpklln
      121 wekqriderv delldlvnld paqyrnrypr elsggqqqrv gvaralaadp pvllmdepfg
      181 avdpitrqrl qdellrlqee lsktivfvth dfdeavklgd riailregsq ivqydtpevi
      241 lanpandfvr gfvghgaalk qltmtrvrdv elheaavahv gddpaqaiea aesidrehvi
      301 vldsherplr wssldelrap nalqrvsqde dlekvslast ltdaledmlt sshgvvvvtg
      361 rrntyqgvir vetimdamae mraaaq
//
LOCUS       WP_005067107             142 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: pilin [Acinetobacter].
ACCESSION   WP_005067107
VERSION     WP_005067107.1
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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..142
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14355
     Region          2..>108
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mnaqkgftli elmivvaiig ilaaiaipay qnyiaksqas eaftladglk ttintnlqag
       61 tcfaggaaav taadkvagky geaviggsap sctitytfks sgvsnkltsk kigmnvsetg
      121 iltknsdtdt paellpqsft as
//
LOCUS       WP_005069634             332 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005069634
VERSION     WP_005069634.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 332)
  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 332)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 332)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 332)
  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   5  (residues 1 to 332)
  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   6  (residues 1 to 332)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..332
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37833
     Region          23..197
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          78..332
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msknssdagi flwmtyqtmq qmgldaasif asvnlpnqpp dknirrdnst qqrfwtaaee
       61 isedpdiglh vgsqmpafrg lvieylflss stfgeglqra lryqdlltdv fnlslivekd
      121 iallvgfehp vrhylecgig iflnffkyit nnefrpsqit lpyqqgasan nyqeawkcpv
      181 ilnqkqgaii fpstllnkas paaepellki hetiaeqqls nlekhqlvya ierllsngll
      241 esgqfdqkfi aeqlnrnprt lradlqaint nyekilnqhr eklarrllan tketldqivy
      301 ltgfsepsaf trafkrwtge tpsayrqrkq kq
//
LOCUS       WP_005070121             843 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [Acinetobacter].
ACCESSION   WP_005070121
VERSION     WP_005070121.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 843)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 843)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 843)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..843
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..843
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=92456
     Region          62..110
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          127..843
                     /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 mkdyqakskl alairavlws tplvvtalts tsiyaaqtys isirqstldq aikqlaiqtg
       61 ttisydnasl sktkskalqg nyavedalsl llqnhpfeav kvnnggysir vkappapiep
      121 kvfqleaikt kasnnnefdt agsetgtahl atihvnadhg eklttegsgl ytakattasn
      181 glalslretp qlvsvitnqq mkdqnltqlt dvvsqaagls ikqggnigsd nspiyargke
      241 vdsylldgvk lmssyasifq sqdmalfdrv evvrganglm tgagsasasi nlvrkkplqd
      301 fkasvsadig swdsyrtdid vstplnesgs irgrtlfayq ksdsyidryn eerkvayavv
      361 eadltdqtka slgasyqqid ltgvargglp sfytdgtlin wsrsdsaaas wtgsdrstts
      421 yfadiehqfn drwklkgvvs rtitdsdeiv gytyssegid kvtgsgamly atrwdyrptq
      481 dlfnltlngs fdlfnqthdv vlgttytksk nkrptysgwn ngmtwdgtlk nifawdgstp
      541 nrpetkidgw ysgddrsqsv fgavrlkatd nlavilgtri edwervtgnh sdakntttyt
      601 tqeesgkvip yvgitydftd nwtayvsytn ifspqdkkav tgeyidplig nstelgikge
      661 ffdnqlnvga aiyqteednt aialtnvfap dgsqayrtes gtksrgfeie atgkltdlwq
      721 vsasfsrnls kdsqdnrlnt gvpnntaklf ttytlpylde altigggvrw qseiyeknav
      781 satgrftqes yalvdlmary kvnnnlmlnf nvnnlfneky hlattnsyyg aptnfrvgvk
      841 yew
//
LOCUS       WP_005070444             356 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005070444
VERSION     WP_005070444.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 356)
  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 356)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 356)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 356)
  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   5  (residues 1 to 356)
  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   6  (residues 1 to 356)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..356
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40567
     Region          42..224
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          105..354
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mpnnvykntn aviegnydnt slgantyllg ltslfdemgs qghsisdvls gtnispdamn
       61 qsslyisqvq kiqlfqniqk lshdpliglr agqkqrlsdf gvygyalyss rnfrqavelg
      121 irhiklagpi lkksfyirdd vavfegqdii algkllplvc efwfssmqtl iervlegpfq
      181 akklllpypa pdyaeeyekv fhcpvqfnag vmqwhfdlkw ldvpcpnanp itadmcksfc
      241 ermlgtaele epelvktirl illdgtglfp saqemaerlh mskrtlhrrl agfnltyqel
      301 ldetrrrltd eylrettltv deiaerigfs dtsnfrkayr hwtgispney riqyln
//
LOCUS       WP_005072413             368 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Mycobacteroides abscessus].
ACCESSION   WP_005072413
VERSION     WP_005072413.1
KEYWORDS    RefSeq.
SOURCE      Mycobacteroides abscessus (Mycobacterium abscessus)
  ORGANISM  Mycobacteroides abscessus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacteroides.
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   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   4  (residues 1 to 368)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Mycobacteroides abscessus"
                     /db_xref="taxon:36809"
     Protein         1..368
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=39557
     Region          1..301
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mitfenvtkq ypdgttavdd lnmhvdkgsf tvfvgpsgcg kttsmrminr mtdltsgllt
       61 vdgadvrtvd pvklrlgigy viqnaglmph qrvidnvatv pvlrgesrra arktalevle
      121 rvgldpklat rypaqlsggq qqrvgvaral aadppillmd epfsavdpnv rddlqaemqr
      181 lqaelnktiv fvthdideav klgdkvavfg pggvlqqyde pervlsnpas dfvagfigrd
      241 rgyrglqfre aggvplyeir qvrepqiadl iiapgdwvlv cnadgtpfgw mddagvdvyr
      301 sgkslydsvi aggslfgpdg tlrqaldaal sspcglgvai dadgrvrggv rgddvltald
      361 rqrrngqr
//
LOCUS       WP_005075092             323 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Mycobacteroides abscessus].
ACCESSION   WP_005075092
VERSION     WP_005075092.1
KEYWORDS    RefSeq.
SOURCE      Mycobacteroides abscessus (Mycobacterium abscessus)
  ORGANISM  Mycobacteroides abscessus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacteroides.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Mycobacteroides abscessus"
                     /db_xref="taxon:36809"
     Protein         1..323
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34021
     Region          1..314
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mlldgaslwf rsyfgvpdsi tspdgrpvna vrgfldtvsq litlhqphrl avcldldwrp
       61 awrvaaipsy kahrvvtddp ragrpsdtvg pqtvdieevp deltpqvdmi admldafgia
      121 sagaagfead dvlgtlaane rrdpvivvsg drdllqvvad vpvpvrvfym grgfakatll
      181 gptevaeqyg vpleragaay aelallrgdp sdglpgvpgv gektaaklla efgsldgilt
      241 aaddpksglt kavraklqaa tvyiaaaepv vrvavdapvi vdrdsdalpr tardprrvae
      301 lgaelgigsa vtrlrkaldg lpr
//
LOCUS       WP_005077023             337 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter pittii].
ACCESSION   WP_005077023
VERSION     WP_005077023.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter pittii
  ORGANISM  Acinetobacter pittii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 337)
  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 337)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Acinetobacter pittii"
                     /db_xref="taxon:48296"
     Protein         1..337
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38386
     Region          25..208
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          252..333
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkyawafers vhsvrlmadf avesgisyet ilkgtglsqq qlldpnmvvt ghqelqlihn
       61 lveqlgdrpt lglevgtryh fttfgplgma lmssasirea ldlaltyftl tfaftrfdvs
      121 dtpqgiriei deqdipssvr qfiierdaaa litvqrdlvq dnfcqylafs fqpkgdaepy
      181 qnlfgvmpef gaaksfvild pqkvdqkllm anelvlhtae eqcrqilekr qsqnkfttlv
      241 qqqlmnvrge mpsmeivaer lhlnvrtlrr hlalegmtfi qireevrqvl aeqylalpka
      301 sveqiaewlg yaeptsfiha ykrwhgktph amrlvqk
//
LOCUS       WP_005077079             356 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005077079
VERSION     WP_005077079.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 356)
  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 356)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 356)
  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   4  (residues 1 to 356)
  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 356)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..356
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40705
     Region          42..224
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          270..351
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpknlykdtn aiiegnydnt slgantyllg ltslfdemgl qghsisdvls gtnispdamn
       61 qsslyisqvq kiqlfqniqr fshdpliglr agqkqrlsdf gvygyalyss rnfrqavelg
      121 irhiklagpi lkksfyirdd vavfeghdii tlgkllplvc efwfssmqtl iervlegpfq
      181 akklllpypa pdyaeeyeki fhcpvqfnag vmqwhfdlkw ldvpcpnanp itadmcksfc
      241 ermlgaaele epelvktirl illdgtglfp saqemaerlh mskrtlhrrl agfnltyqel
      301 ldetrrrlad eylrettlti deiaerigfs dtsnfrkayr hwtgispney riqyln
//
LOCUS       WP_005078455             141 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Acinetobacter].
ACCESSION   WP_005078455
VERSION     WP_005078455.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..141
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15055
     Region          1..122
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkngftliel mivvaiiail aaiatpsylq ylrkghrtav qsemmniaqt leaekivhnr
       61 ypsnatitsi ygssvspqqg qalynlafss itdsswvlta tpiatssqag dgiiclndqg
      121 qkfwakgatd calsatsnwl q
//
LOCUS       WP_005079149             400 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Acinetobacter].
ACCESSION   WP_005079149
VERSION     WP_005079149.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..400
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42898
     Region          5..388
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 matsvlvinc gsssikyalv serredriyg laenlgaada rikgitvgge plelsipyad
       61 hakaletlla rlanykpqai ghrvvhggsl tkaelltpei ieriraatpl aplhnpahli
      121 gidatvrlfp elpqvavfdt afhqtmppha yryaipkfly tdhnvrrygf hgtshayvsd
      181 kaselagnlk kggwltahlg ngsstcavwn gqsvdtsmgl tplegvvmgt rsgdvdpslh
      241 sflaknlgwd lakidkvlnn esgllglsql sndmrtviea aengnedacl aievfsyrla
      301 kslaalscgl ptldgliftg gigensayir ektlaylphf glqldkdqnn nlkrgtegri
      361 dngtgpqiwv iptdeegria ketrqvveaa entasvasla
//
LOCUS       WP_005080706             216 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Mycobacteroides abscessus].
ACCESSION   WP_005080706
VERSION     WP_005080706.1
KEYWORDS    RefSeq.
SOURCE      Mycobacteroides abscessus (Mycobacterium abscessus)
  ORGANISM  Mycobacteroides abscessus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacteroides.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Mycobacteroides abscessus"
                     /db_xref="taxon:36809"
     Protein         1..216
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23805
     Region          8..211
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mtslnlsade vltttrsvrk rldfdkpver avveeclnia mqaptgsnhq gwhwviveda
       61 ekkkaiadiy regwnkyakg agatyaegdt raerkakvvd sagylaenfe rsplflipci
      121 egrldnlpvv gaasswgsll pavwsfmlaa rnrglgsawt tlhlmddgek rtadivgipf
      181 dkvtqgglfp iaytvgtdfr lakrqpladv lhwdtw
//
LOCUS       WP_005081592             416 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Acinetobacter haemolyticus].
ACCESSION   WP_005081592
VERSION     WP_005081592.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter haemolyticus
  ORGANISM  Acinetobacter haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Acinetobacter haemolyticus"
                     /db_xref="taxon:29430"
     Protein         1..416
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=47805
     Region          3..289
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          289..387
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mtvrffhtsd whlgqffynh srhyeheqfl awlleqikik qphalliagd ifdvinpssq
       61 aqkqlyqfla dahdlapqmq tlmiagnhds gyrieqvepl lekynaktvg virwnedksl
      121 dldrlilpiy deqkqivawc ialpflrsae itgfnehttn sqnaiaylhq hliaeakrrk
      181 tddqalilms hahmqggets dserpiiign eealsttlfd deinyvalgh lhkpqkvgyd
      241 hirysgspip lsfseinykh qvvevtidpn atenqvefea iaipraiqlh kikgelndvm
      301 qrlknlpqga igsidhreyi dieyhtatpp qpnlrqqfed alpkdryrlv risrqylsne
      361 tnaeseskin lepptpeklf qqiwekkgys vddevskdfl slvaeaqkkl eddqav
//
LOCUS       WP_005082674             237 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Mycobacteroides abscessus].
ACCESSION   WP_005082674
VERSION     WP_005082674.1
KEYWORDS    RefSeq.
SOURCE      Mycobacteroides abscessus (Mycobacterium abscessus)
  ORGANISM  Mycobacteroides abscessus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacteroides.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Mycobacteroides abscessus"
                     /db_xref="taxon:36809"
     Protein         1..237
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25722
     Region          3..209
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 melydvmrtt faareftrdp lpdnvldril dnarfapsgg nrqaghvivv kdpatreslv
       61 eatkpgarry faqvvagesp wnpvsptrvn petiaatvvp esvaaplrta gavlvvcvdl
      121 rlvaavdqdl ervgvvagas vyplvwnill aaraegyggt lttmavaeep kvrellgipd
      181 tyavaavlpi gkpvkqltrl rrnraaefvt rerfdgppwr tttgehhses pryprsh
//
LOCUS       WP_005084354             104 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Acinetobacter].
ACCESSION   WP_005084354
VERSION     WP_005084354.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..104
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11763
     Region          1..102
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(6..7,25..26,34,37,39..40,42,45..46,48,56,61,68)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(25,56..57,59,86)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mneqelhrqi levidlipyg kvasygqiak laglpkharl vgfvlkhldq eskvpwyrvi
       61 naqgrisvnr indkgenvqq clleaegvyf engkvdfkif gwti
//
LOCUS       WP_005085626             337 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Mycobacteroides abscessus].
ACCESSION   WP_005085626
VERSION     WP_005085626.1
KEYWORDS    RefSeq.
SOURCE      Mycobacteroides abscessus (Mycobacterium abscessus)
  ORGANISM  Mycobacteroides abscessus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacteroides.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 337)
  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   6  (residues 1 to 337)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Mycobacteroides abscessus"
                     /db_xref="taxon:36809"
     Protein         1..337
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36769
     Region          22..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <157..335
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mellsipprw gtlaselaqq qgmdaakmli daqisprfla geptmispaq lravtrevla
       61 rtgdlsfgsc qapvppealr vlmfslatse tagaafarwa afrdamplvp smtvarsgef
      121 atvvlvspsp klpdvtftew tlalvirvws wlimraihae rillpqarpa grsdrsnilk
      181 apvefgsnsa avildaklld vpilrseqei tsildhpeqi wfdvgryhre lpervsrivg
      241 ssigqgiptv sdiaaalnma psalqrslrn efgtsirrir daalrteaik sledgsesln
      301 dlsvrlgfse lsaftrafrr wtgaspaqyr ngtrsvk
//
LOCUS       WP_005086521             337 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Mycobacteroides
            abscessus].
ACCESSION   WP_005086521
VERSION     WP_005086521.1
KEYWORDS    RefSeq.
SOURCE      Mycobacteroides abscessus (Mycobacterium abscessus)
  ORGANISM  Mycobacteroides abscessus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacteroides.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 337)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Mycobacteroides abscessus"
                     /db_xref="taxon:36809"
     Protein         1..337
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36500
     Region          1..318
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 msvsifdiss ylpenrvsae yfaqyakddd laenvmfrsp ayrhhvande savdmaerav
       61 aglrerhgat vldevdillt htqlpdlpfv gcggevanrl qirpewildv hnggcvsfvl
      121 mlklvqqmmv sssarsaliv niqnaagqif vqeqvrstaq asipgdgata tlitrdggsp
      181 vlgietrnfg efagdmtyav tphrkyweag sgqgrvafte hkiskvlarg nrmvpevala
      241 vcdrigiast dldalvtnqp nriflrnwsd alqlpkekhp dtfdecgnlf gvgiphtldk
      301 aiaerqvrpg dtvmlagfah agdyaaaaav rwggrgq
//
LOCUS       WP_005088030             459 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Acinetobacter haemolyticus].
ACCESSION   WP_005088030
VERSION     WP_005088030.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter haemolyticus
  ORGANISM  Acinetobacter haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 459)
  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 459)
  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 459)
  AUTHORS   ter Beek,J., 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 459)
  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 459)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Acinetobacter haemolyticus"
                     /db_xref="taxon:29430"
     Protein         1..459
                     /product="CmpA/NrtA family 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=49952
     Region          41..318
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mshfvkstcl tmcmtavvls lsgcgkkpet akdavsntat gaektnlklg fikltdmvpl
       61 aiahekgyfq deglnvqlea qsnwkvlydr vaggeldgah mlaamplgam tgitgnkeii
      121 apftlsynga aitvsntvwq qmkpqlsmen gkpkhpisaa slkgaadqsk asgkpfnlgm
      181 tfpvgthnym mrywlaaggv npgvydandt sgnkgadvml svvpppqmva tmeagttmgy
      241 cvgepwnqqa vfrkigvpva tsdqmwkdga dkvfgmtkdf aeknptttvk vvkalirasy
      301 wldqdnnanr seavkiisrp nyvgadeavi ansmtgtfef eagdkrpvpn fntfykgqyg
      361 ipyysdavww ltqmrrwghi petkpdqwyl dmakkayqpe iyaqaakeli aegkmkaedf
      421 pdfstanyik apetsaldgv rfdanqpnaf lasfkiglk
//
LOCUS       WP_005089198             340 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter haemolyticus].
ACCESSION   WP_005089198
VERSION     WP_005089198.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter haemolyticus
  ORGANISM  Acinetobacter haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 340)
  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 340)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 340)
  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   4  (residues 1 to 340)
  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 340)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Acinetobacter haemolyticus"
                     /db_xref="taxon:29430"
     Protein         1..340
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39608
     Region          38..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          262..337
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msvkiiigyl rllnrvlqqe hidlskvavp elwqdfyscl enpdqqdfdv eryaqllqaa
       61 qpyfsrpitl vlaeranlqd lglmgylast sldlqqalql lqryyslifk qtnleqlnvq
      121 qfsdyiqivw sasypdyrem yelnlallfk iaqsivqdtl hppqmiqfgy tphtalfhfe
      181 kfygcpiqvq tgqyairfsn qilkaksiaa dqqlnqvlst qaqqslnhvt sfdiqqqqlr
      241 qkiqsfieqg llqqeevlss yvakhlhcse rtlqrqlkay hlnfqdildq yrleqsklyl
      301 qqgksfseia erlnyadqsa fgrafkrwtg vtpkqflktl
//
LOCUS       WP_005089206             359 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Acinetobacter haemolyticus].
ACCESSION   WP_005089206
VERSION     WP_005089206.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter haemolyticus
  ORGANISM  Acinetobacter haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Acinetobacter haemolyticus"
                     /db_xref="taxon:29430"
     Protein         1..359
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39730
     Region          277..351
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 msmnnkqrwm ggvvllgggv llaalllkgn deieqdkaqa rtaqqtaqte skpklaqpaq
       61 dsemvslqpl aidvetekrl leeqrharek avaeqearaa eflkmqqeae aaaarkaaee
      121 yaainarrma aqqssdnipp elieddaaka qrlaeekrkl eekrkaeaek kaaedkrkae
      181 tdqkaaeerr kaeaekkaae dkrkaeaekk aaedkrkaea ekkaaedkrk aeaekkaaee
      241 krkadaekka aedkrkaeee akkkaeaeka relmengdkn wmvqvalaan qanadavvsk
      301 lrakgykvtt sptskgirim vgpskdreta daarkkiaad eslnmksawv idwvpldqr
//
LOCUS       WP_005089267             730 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Acinetobacter
            haemolyticus].
ACCESSION   WP_005089267
VERSION     WP_005089267.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter haemolyticus
  ORGANISM  Acinetobacter haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 730)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Acinetobacter haemolyticus"
                     /db_xref="taxon:29430"
     Protein         1..730
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=81040
     Region          19..727
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mpsmkinfly gcvvlcmglg sssiwatesn seltvqlpti tveatrmntd ylhtpasvfr
       61 vdtseqqqsa qvnltelvkg vpslqlnnre nyaqdlqlsm rgfgarstfg vrgirlyvdg
      121 ipatmpdgqg qtsnidlasl shlevltgpf sslygnssgg tlltttkegq gkdsielnyt
      181 ggshdknrag iilqggaknq nepsyvisss yfdtdgyreh sdarkvlnna kltwnledgs
      241 kinwitnyvk inandpqgln ktqwqqnprq vndanntydv rkdieqtqtg vtwskpindq
      301 helylmgywg nrqvtqyqsi pkggvtlkdd kpiysgqksp kqaggvidfd rnyygadfrw
      361 tgkellpntt lsvgvaldam dedrkgfenf nakgiygvkg nlrrdedntl wnidpylqas
      421 weflptwrld tgvrysnvhy kskdhftsgp deygtingdd sgkhdyskll psialswqvi
      481 pellayvsya kgfetptfte mayrpdglgg fnfdleasss dtyefglksq nqlgdftlav
      541 fqtktkddiv sagsvdgrat frnadktlre gveltwnkal wrdlvinasy gyldatfdan
      601 vpekkddgki lasaipsgnl ipgiakqray aavawkpntg fyggldaqyn dkiyvndtnt
      661 eaapsytsvs aytgylwtln dwrvntyari dnmldknyig svivndgngr fyepadgrnw
      721 sagfsvtkqf
//
LOCUS       WP_005090684              83 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Acinetobacter].
ACCESSION   WP_005090684
VERSION     WP_005090684.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..83
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8862
     Region          6..83
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mqtievkiea fgaierllpk alsfefahhq svkdvlqqiv tlypessnam ekcacaiged
       61 ivtrqttlds sctlvllspv agg
//
LOCUS       WP_005090551              98 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Mycobacteroides abscessus].
ACCESSION   WP_005090551
VERSION     WP_005090551.1
KEYWORDS    RefSeq.
SOURCE      Mycobacteroides abscessus (Mycobacterium abscessus)
  ORGANISM  Mycobacteroides abscessus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacteroides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Mycobacteroides abscessus"
                     /db_xref="taxon:36809"
     Protein         1..98
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10391
     Region          5..96
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(27,55..56,58,80)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 maavteeqve lvrslvasip agrvatygdi adaaglasar ivgwimrtds adlpwhrvig
       61 asgrpaphir trqlellrae gvlavdgria lrdvrhgf
//
LOCUS       WP_005091333             416 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Acinetobacter haemolyticus].
ACCESSION   WP_005091333
VERSION     WP_005091333.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter haemolyticus
  ORGANISM  Acinetobacter haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Acinetobacter haemolyticus"
                     /db_xref="taxon:29430"
     Protein         1..416
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=47873
     Region          3..289
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          289..387
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mtvrffhtsd whlgqffynh srhyeheqfl awlleqikik qphalliagd ifdvinpgsq
       61 aqkqlyqfla dahdlapqmq tlmiagnhds gyrieqvepl lekynaktvg virwnedksl
      121 dldrlilpiy deqkqivawc ialpflrsae itgfnenttn sqnaiaylhq hliaeakrrk
      181 tddqalilms hahmqggets dserpiiign eealsttlfd deidyvalgh lhkpqkvghd
      241 hirysgspip lsfseinykh qvvevtidpi ktenqvefea iaiprtiqlh kikgelndvm
      301 qrlknlpqgv iecidhreyv dieyhtatpp qpnlrqqfed alpkdryrlv risrqylsnq
      361 tnaesvskis lepptpeklf qqiwekkgys addevtkdfl slvaeaqkkl eddqtv
//
LOCUS       WP_005092331             264 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Acinetobacter
            haemolyticus].
ACCESSION   WP_005092331
VERSION     WP_005092331.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter haemolyticus
  ORGANISM  Acinetobacter haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acinetobacter haemolyticus"
                     /db_xref="taxon:29430"
     Protein         1..264
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29533
     Region          1..257
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mshlavnlsm iftevplier falahahgfq hveiqfpyel eifdiqaqln qynlslclin
       61 apagdlmqgg nglagvpgle ttfhqalela isyatalnvp rinilagkqp ldadllpcln
      121 tlasnlklac hmltehhiep vfemingtdm prfliqniaq gqemleavnh palkmqydcy
      181 hmammgedvl aglqenihqi ghiqfadcps rhepdtgnip ykqifdwllq sdyqgiiaae
      241 yrpkehsdqs lawkqkyfsn dvnt
//
LOCUS       WP_005092912             386 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Mycobacteroides abscessus].
ACCESSION   WP_005092912
VERSION     WP_005092912.1
KEYWORDS    RefSeq.
SOURCE      Mycobacteroides abscessus (Mycobacterium abscessus)
  ORGANISM  Mycobacteroides abscessus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacteroides.
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   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   4  (residues 1 to 386)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Mycobacteroides abscessus"
                     /db_xref="taxon:36809"
     Protein         1..386
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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]"
                     /note="Members of the family are the ATP-binding subunit
                     of ABC transporters for substrates such as betaine,
                     L-proline or other amino acids, choline, carnitine, etc.
                     The substrate specificity is best determined from the
                     substrate-binding subunit, rather than this subunit, as it
                     interacts with the permease subunit and not with substrate
                     directly.; Members of the family are the ATP-binding
                     subunit of ABC transporters for substrates such as
                     betaine, L-proline or other amino acids, choline,
                     carnitine, etc. The substrate specificity is best
                     determined from the substrate-binding subunit, rather than
                     this subunit, as it interacts with the permease subunit
                     and not with substrate directly."
                     /calculated_mol_wt=42414
     Region          16..322
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 msdatenati tggarilldg vtklydgkst pavdnvtmei pagetvmfvg psgcgktttm
       61 kminrliept sgrifigded vtdknpdelr rhigyviqga glfphftvgd niaivpklln
      121 wdkqriderv delldlvnld paqyrnrypr elsggqqqrv gvaralaadp pvllmdepfg
      181 avdpitrqrl qdellrlqee lsktivfvth dfdeavklgd riailregsq ivqydtpevi
      241 lanpandfvr gfvghgaalk qltmtrvrdv elheaavahv gddpaqaiea aesidrehvi
      301 vldsherplr wssldelrap nalqrvsqde dlekvslast ltdaledmlt sshgvvvvtg
      361 rrntyqgvir vetimdamae mraaaq
//
LOCUS       WP_005094432              86 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: zinc ribbon domain-containing protein
            [Acinetobacter].
ACCESSION   WP_005094432
VERSION     WP_005094432.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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 12181465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..86
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=9518
     Region          19..>67
                     /region_name="zinc_ribbon_15"
                     /note="zinc-ribbon family; pfam17032"
                     /db_xref="CDD:465334"
ORIGIN      
        1 mffifgfgpk tktieksqfl cpvcrtrtgy elkqqrhyfs lffiplipls kpktafvtcs
       61 ncgtampstv ldhaqpepgs nsnlea
//
LOCUS       WP_005096939             333 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Acinetobacter].
ACCESSION   WP_005096939
VERSION     WP_005096939.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 333)
  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 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   3  (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   4  (residues 1 to 333)
  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 333)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..333
                     /product="CmpA/NrtA family 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=37350
     Region          2..241
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mstlekteln igyiplldcv ailwaekqgy faeqgltinl ireaswsslr drlaygflda
       61 ahclsamlpa aalgtdqlqv alqtplvlsm nqafislrqd lchelgidae ddeksssqkl
      121 vqalqqqqkm nlayvykhsi hhycikewla ltdvniahki qlmtsppasm vkgiseqvfd
      181 gfcvgepwni qaklegysli vaasqnvipk vadkvlamtq ewaelhpctv kalvnavqka
      241 qtdlkqradl sqvwdmlvdy qiiqfecsaq rhvcdyhkiq niirnlvgas akpqladfiw
      301 lieqiekwdg veiseiekkq iaaqcmyaem lfa
//
LOCUS       WP_005096998             342 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005096998
VERSION     WP_005096998.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 342)
  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 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 342)
  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   4  (residues 1 to 342)
  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 342)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..342
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38762
     Region          32..209
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          256..337
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mktiaprqdq gipgvyalll ldvisrwgyn deslfksfgl steqladpdf riptpvanel
       61 vkhalklsge ptlgyhlgtq mrisihgfig yaimtakdit dalvlanrfi qlrmpflqlf
      121 fstfgakatv qlqtdiqlep lrteisiali fgmismakai tgidyaagei dfdfkkpegf
      181 erfmakfphh qfrfeqphli lsfdksylmn klvhadpias qiainqcete lsalgerhri
      241 amrvrdilth seqhylsies vadrlhmsdr tlkrqlaaeg tsfstlvdev ryrhatslls
      301 rtdfsleqia delgysdvan fsrafkrwsg rspsnwrkdp yl
//
LOCUS       WP_005097572             353 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Acinetobacter].
ACCESSION   WP_005097572
VERSION     WP_005097572.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..353
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39512
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvqniek hfgafhalkn isldfpdgql vallgpsgcg kttllriiag lesadggqvi
       61 legqdatnvh vrerevgfvf qhyalfrhmt vfdniafglr vrprktrpse aeikkrvtrl
      121 ldlvqlgfla drypaqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 tlhdelhits ifvthdqeea levadqivvm nkgnveqigs prevyetpat pfvfdflgqa
      241 nrfegqnngg iiqlgqdrih fdgaknaaqg evilfarpde lrihaqpqdn aiqatfirel
      301 wiagkvvael ndrqgnliei lltpdearah qfrpnqtvwl savnlhlfen qva
//
LOCUS       WP_005097588             267 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [unclassified
            Acinetobacter].
ACCESSION   WP_005097588
VERSION     WP_005097588.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..267
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30256
     Region          39..264
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mstenssiia qspetidsan pdkkryyepa pqdidvdnfr kviesrrsvr kftkkpiped
       61 vldacldlal lapnssnlqp wtfyvvqnpa kkkrlvkacm sqlaaktase liicvartdr
      121 idemakrnvn efpypeapaa ikkyykyipy nyktgylnvf gnfkkvafkv artldkqmpv
      181 safspndakl watkttalac enlvlalray gfdscmmegf depmvrdilg lndqqypvmv
      241 igagerakdg vffpqyrfdr elfiqkv
//
LOCUS       WP_005089845             879 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Acinetobacter haemolyticus].
ACCESSION   WP_005089845
VERSION     WP_005089845.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter haemolyticus
  ORGANISM  Acinetobacter haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 879)
  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 879)
  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 879)
  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   4  (residues 1 to 879)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..879
                     /organism="Acinetobacter haemolyticus"
                     /db_xref="taxon:29430"
     Protein         1..879
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=98373
     Region          109..837
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mtqkldqmta ttlsltptnt itanitaips afeqadiqat ltktalkanq lthipdlaki
       61 psstkrikpl nnflgqdrar asveagislp ysgynifavg taglgkrtmi krllqqhakt
      121 mqtpddwvyv nnfknprqpi alrfpagqgs kfqnalqqtw qiilkqlerr fsaesyhnri
      181 erirqatgev qqqalaeltk egegldlklv srndkhvfip mllkddeyhe ltqqdlstls
      241 skersdissn irymekkler lglhlgdled dardqvssln rdiasqvvmp riesilnknk
      301 evkglelylk hyaediienv elileqeedd ftpalfnrvp aryqanviia nkpnsgapvi
      361 fedfpthynl lghveqlthn gtittdftli rpgslhrang gflmleaeql leqpyawqgl
      421 kralksghlk lsslehmltl tgsisiepas vpleikvvll aepeiyyeil evepelgsvf
      481 kiradftdtl qrndsneqay mqliadyvqa dkllpfdrsa laalltdssr qaedqsslsl
      541 hastlgdlir eahhhafkad dkivthdhvn qalhhrqyrl gylrelywqd lsrgtqliet
      601 sghrlgqina lsvihyadve fglpsrltas vyqgggdild iersvelggs lhakgvllms
      661 sflkahfgre qilhfsaala feqsygqvdg dsatvaelsa lisaicqipi dqswaitgsm
      721 nqlgqvqpig gvnakiegfy dacklqgltg kqgviiprqn mqhlmlrqdv ieaveagqfh
      781 vhaidtidqa leilmarpvg tldkkgrysk nsiyaavmeq leywqaiedg eaveddepkk
      841 kkkrkktkkd qtesksvnen etvevkslks hakvkarrk
//
LOCUS       WP_005098471             320 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase LdtC [Enterobacteriaceae].
ACCESSION   WP_005098471
VERSION     WP_005098471.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Magnet,S., Dubost,L., Marie,A., Arthur,M. and Gutmann,L.
  TITLE     Identification of the L,D-transpeptidases for peptidoglycan
            cross-linking in Escherichia coli
  JOURNAL   J Bacteriol 190 (13), 4782-4785 (2008)
   PUBMED   18456808
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Magnet,S., Bellais,S., Dubost,L., Fourgeaud,M., Mainardi,J.L.,
            Petit-Frere,S., Marie,A., Mengin-Lecreulx,D., Arthur,M. and
            Gutmann,L.
  TITLE     Identification of the L,D-transpeptidases responsible for
            attachment of the Braun lipoprotein to Escherichia coli
            peptidoglycan
  JOURNAL   J Bacteriol 189 (10), 3927-3931 (2007)
   PUBMED   17369299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: BlastRule
            Evidence Accession :: NBR008111
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     gene            1..320
                     /gene="ldtC"
     Protein         1..320
                     /product="L,D-transpeptidase LdtC"
                     /calculated_mol_wt=34519
     Region          30..308
                     /region_name="PRK10260"
                     /note="L,D-transpeptidase; Provisional"
                     /db_xref="CDD:182341"
ORIGIN      
        1 mmiktrfsrw ltfftfaaav alalpakant wplppassrl vgenkfhvve ndggsleaia
       61 kkynvgflal lqanpgvdpy vpragsvlti plqtllpdap regiviniae lrlyyyppgk
      121 nsvtvypigi gqlggdtltp tmvttvsdkr anptwtptan irarykaqgi elpavvpagp
      181 dnpmghhair laayggvyll hgtnadfgig mrvssgcirl rdddiktlfs qvtpgtkvni
      241 intpikvsae pngarlvevh qplsekiddd pqllpitlns amqsfkdaaq tdaevmqhvm
      301 dvrsgmpvdv rrhqvspqtl
//
LOCUS       WP_005099559             337 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Mycobacteroides
            abscessus].
ACCESSION   WP_005099559
VERSION     WP_005099559.1
KEYWORDS    RefSeq.
SOURCE      Mycobacteroides abscessus (Mycobacterium abscessus)
  ORGANISM  Mycobacteroides abscessus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacteroides.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 337)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Mycobacteroides abscessus"
                     /db_xref="taxon:36809"
     Protein         1..337
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36483
     Region          1..318
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 msvsifdiss ylpengvsae yfaqyakddd laenvmfrsp ayrhhvadde savdmaerav
       61 vglrerhgat vldevdillt htqlpdlpfv gcggevanrl qirpewildv hnggcvsfvl
      121 mlklvqqmmv sstarsaliv niqnaagqif vqeqvrstaq asipgdgata alitrdggsp
      181 vlgietrnfg efagdmtyav tphrkyweag sgqgrvafte hkiskvlarg nrmvpevala
      241 vcdrigiast dldalvtnqp nriflrnwrd alqlpkekhp dtfdecgnlf gvgiphtldq
      301 aiaerqvrpg dtvmlagfah agdyaaaaav rwggrgq
//
LOCUS       WP_005100301             721 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Acinetobacter lwoffii].
ACCESSION   WP_005100301
VERSION     WP_005100301.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter lwoffii
  ORGANISM  Acinetobacter lwoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Acinetobacter lwoffii"
                     /db_xref="taxon:28090"
     Protein         1..721
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=80681
     Region          19..721
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mhmtkiplkk splslmilsi vsghlyaeta vepdnvqqln tivisaeqna npqqqyqkel
       61 aqvsggtnfi gepqleqqrl attadvfrlq pgiyaqsagn egakisirgs ginrtsgaha
      121 sgthvliddi pftgpggtay ellepwwidh vgvyrgangf kqgglalggt inyrtktgad
      181 qdgselkyem gshgyqkyqf stgrkldqmd yylaltstqf dgiqdhaegd gkglafnlgy
      241 qispdietrf yaryreskhl tpgritqeql kndpeaansf nlavdakriq pgstwlantt
      301 twnlqddakl tgslayhhyp ldlressyrt nvdyeditar fqyekpyqfl glehqgrial
      361 rstthrpdsg vtetirrdtt idgtlypadt vtrrytyrgs dnvlqfdqet tlndqfkldl
      421 glaavythre sevtypvasp evsryewnfa prlgltyqpn esvqwfanls rsiepahpwa
      481 mawsspyyfd sgvasgrvra piyldtqtan sfelggrgqs vfgdwalsyy yskvknellt
      541 semiktyedg snrpsepiav esnatptihq gvelsldtpl heseygelrl qqaytlsdfq
      601 ykndplfgkn qlpgipkhly qaqlsyalnn glyiglntey vskmahdyan srfsddyqiw
      661 gidlgyapeh qswktwinfk nitdekyaav vipglndqga dvtrsspgeg fstyagvsfk
      721 f
//
LOCUS       WP_005101482             265 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Mycobacteroides abscessus].
ACCESSION   WP_005101482
VERSION     WP_005101482.1
KEYWORDS    RefSeq.
SOURCE      Mycobacteroides abscessus (Mycobacterium abscessus)
  ORGANISM  Mycobacteroides abscessus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacteroides.
REFERENCE   1  (residues 1 to 265)
  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 11691890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Mycobacteroides abscessus"
                     /db_xref="taxon:36809"
     Protein         1..265
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=28024
     Region          34..131
                     /region_name="LDT_IgD_like"
                     /note="IgD-like repeat domain of mycobacterial
                     L,D-transpeptidases; cl17506"
                     /db_xref="CDD:248060"
     Region          161..263
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mvvavsvvga alagravgve ttavslpldm svrsiaplpd rrvgiahpvv vtfnepvadr
       61 gaaeralgit stppmtgrye wldnnavqws pdrfwpphst vklmvggkpa eistgpalig
      121 iasvsrhtft vsyegvwrrp sdgatglpap hhlprlgeeg vfpasmgrpe yptplgtysv
      181 lgkersvlmd sssvgipvta pdgykidven avrfttrglf vhsapwavpa mgyenvshgc
      241 islppaaaew yfnnvnigdp vvvqe
//
LOCUS       WP_005101810             262 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: hydroxypyruvate isomerase family protein
            [Acinetobacter].
ACCESSION   WP_005101810
VERSION     WP_005101810.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 262)
  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 262)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..262
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29438
     Region          1..257
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 miklavnlsm iftevplier falaraqgfn hveiqfpyel tigqiqnqls thqlnlclin
       61 vpagdlmqgg hglagipgqe iefrhaveqa iqyatalnvp rvnilagkqp rdcdllpcln
      121 tlasnlkmac smllehqiep vfemingtdm prfliqnvaq aqemleavhh palkmqydcy
      181 hmammgedvl etlqeniasi ghiqfadcpg rhqpntgsiq yhdifqwlkh sqyqgyvaae
      241 ykpsghsnds fdwkaeffpe hd
//
LOCUS       WP_005101997             258 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Mycobacteroides abscessus].
ACCESSION   WP_005101997
VERSION     WP_005101997.1
KEYWORDS    RefSeq.
SOURCE      Mycobacteroides abscessus (Mycobacterium abscessus)
  ORGANISM  Mycobacteroides abscessus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacteroides.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Mycobacteroides abscessus"
                     /db_xref="taxon:36809"
     Protein         1..258
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=27385
     Region          118..251
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 msslksppen dkllsqllqt lfalaavavi vvlivngtlf gkdnrissel skitgqeqrd
       61 dgappsasti sgtgtpspdp stltvaapgs kdgyararfg qpwtddvdie gghngcstrd
      121 dilqrdltgi tlsgsckvms gtladpytgq visfvygkkt salvqidhlv slanvwvsga
      181 atwdlpelkk iandplnlla vngssneskg eksadqwlpe ntafdctyvk rqvmvknkyr
      241 ltvtaaekat mqqfygac
//
LOCUS       WP_005103262             140 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Acinetobacter].
ACCESSION   WP_005103262
VERSION     WP_005103262.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 140)
  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   2  (residues 1 to 140)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..140
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15242
     Region          69..138
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkkipyqigp twislllscw lgfisigtvh atatdymewk tqqqqhdarl kkkaastass
       61 esnhylakpa lsassaadki slnnatveql qqlngigqkk aeaiiehrqk ngkfksieei
      121 qlvkgigpal faknkaklal
//
LOCUS       WP_005103250             232 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Acinetobacter].
ACCESSION   WP_005103250
VERSION     WP_005103250.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 232)
  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 232)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 232)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..232
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=25657
     Region          7..209
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Site            order(100..101,103,131,134..135,138..139,141..142,164,
                     167..168,171..172,175)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          125..159
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          163..189
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msamsgdeqf eslksftkky gssmitgili aliaffgwey wqkknlaesq mhtakvqqlm
       61 ddaqaskgdg faklsetadk ivkeapdsaq aiqtqlvmak laydkedyaa aekalqkven
      121 skvddkglvq vvklrlayaq laqkkydaal ktleavtepa fkatadearg diyvakndie
      181 nakkvyqsaw dalierkeer qilqiklesv gvlvddpeie rpiietqaee aa
//
LOCUS       WP_005104571             721 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Acinetobacter].
ACCESSION   WP_005104571
VERSION     WP_005104571.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 721)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 721)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..721
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=81991
     Region          19..>154
                     /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          <151..233
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          477..710
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cl29561"
                     /db_xref="CDD:453023"
ORIGIN      
        1 mgsievrnpl lskklkrtet rlliiddnqi rynqirdllt sndyqvdavl lddlqsfekq
       61 lnfnwdliif graydlkyeq alslvrlsqq pnlpmillkp ddyqaeqyaq yirkgvydil
      121 nfdylerfyv glvralsfsr lsqsqqhlmt eletaqiqaq slvddsnrav atiqegihiq
      181 anadylklfg lqnedeiigl plldllqpsd lndfktrfkk isqgqfdlgr veiqslnphv
      241 sasnplklef lpstaeedav qisidtqskt vssdktpgkp svfqslkrel hkqsapvnal
      301 vtfsfsaydp ellqsdwatf sgyfkaakef lteqthiplf kleydvvvgl fqadskaile
      361 sklislnals kpqlitvgpk sfplnlrlgy vmleqglqde mhcntligqa fstslpqaea
      421 vpefkldipa slsspvavem psidfsvaet pvasptlaav spavtsipsa tpsilkalse
      481 clergeihlk yqqlydkedt rlyayevtsg fifenkwqdi ssllelhedd elsikldrwi
      541 lveaskqlhn fitqypdasl ivnlnravlf kdrtfpefis klitiirskv khplilqfse
      601 edillnqqda qkylrvlyeh galialrdfg qsmyspnllr eleldgvslh snltnmlnkd
      661 teieqlqeki tsyneikpln ilirelndmt lfanawnvda rfiqgnyfqk kldhlidvqd
      721 h
//
LOCUS       WP_005105382             626 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Acinetobacter].
ACCESSION   WP_005105382
VERSION     WP_005105382.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 626)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 626)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 626)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 626)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..626
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=69707
     Region          2..626
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mqstaqkaal pvitlaalgv vfgdigtspl yalrqcflta hlaiseasvl gilslifwcm
       61 mltisfkyvm vimradnnge ggimsllaln lrttrisdqk kiflialgfv gaslffgdgi
      121 itpaisvlsa ieglsiatpi fnqwlvplsi gilaglfmvq rhgtatmgkf fgpltmlwfl
      181 siggfglwsi iqtpfvlwmv npywayhfvv dqpyvafltm gaviltmtgg eaiyadmghf
      241 grlpirlawf iivlpcllln yagqgalllr spealanpfy mllpdwalfp miglataaav
      301 iasqavitgv fsmvnqaiql rylprlsvkh tsalergqiy lpfinwmlfi svlilillfe
      361 nsanlasayg vavtmtmlcg tilisilayg fwrwpvwkva lfavpflald lvfvastslk
      421 iasggwvpil igavlftilm twkdgralvl nrleqdalpi dlfiksismg egtkfvpgda
      481 ifltgtpniv phamlhnikh nkvlhernim ltvitrdipf vdrqdriele klsehfyrvf
      541 iyygfkdqpn ipealqqaye qwdfeydlmq isffisreri mhtvgegmap wreklfismq
      601 rntspvsdfy qippnrvvel gtqiqm
//
LOCUS       WP_005105389             336 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005105389
VERSION     WP_005105389.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 336)
  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   6  (residues 1 to 336)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..336
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38974
     Region          27..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          82..336
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mlvlknyvgs vygglghlll dyyqlkqlev pekllaiqnl erfdfalwrd llttldqqlq
       61 rpalgleiaq lveakhlgii gylalssetl geafmryhdy hrliydggll qlqwqgdyls
      121 igwvevpfhl ntqltdeiai almtefvkan vqnphgvqly evhfqhampk nialyeqyfg
      181 ckvrfsqarn qvlmhvsels rplkqgdqsl qkllmqqaka llekfphstl idqqlqqail
      241 iglqknlfqi ehiaeqmnfs vrqlqrhlqk qgktyqqcmq eircmmamqy lkdphlslqe
      301 tamllgyseq safqrafkqw tqltpqqwrq qnmsaa
//
LOCUS       WP_005106920             721 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Acinetobacter lwoffii].
ACCESSION   WP_005106920
VERSION     WP_005106920.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter lwoffii
  ORGANISM  Acinetobacter lwoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Acinetobacter lwoffii"
                     /db_xref="taxon:28090"
     Protein         1..721
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=80653
     Region          19..721
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mhmtkiplkk splslmilsi vsghlyaeta vepdnvqqln tivisaeqna npqqqyqkel
       61 aqvsggtnfi geqqleqqrl attadvfrlq pgiyaqsagn egakisirgs ginrtsgaha
      121 sgthvliddi pftgpggtay ellepwwidh vgvyrgangf kqgglalggt inyrtktgad
      181 qdgselkyem gshgyqkyqf stgrkldqmd yylaltstqf dgiqdhaegd gkglafnlgy
      241 qispdietrf yaryreskhl tpgritqeql kndpeaansf nlavdakriq pgstwlantt
      301 twnlqddakl tgslayhhyp ldlressyrt nvdyeditar fqyerpyqfl glehqgrial
      361 rttthrpdsg vtetlrfnte ignqtypadt vtrrytyrgs dnvlqfdqet tlndqfkldl
      421 glaavythre sevtypvasp evsryewnfa prlgltyqpn esvqwfanls rsiepahpwa
      481 mawsspyyfd sgvasgrvra piyldtqtan sfelggrgqs gfgdwalsyy yskvknellt
      541 seiiktyedg snrpsepiav esnatptihq gvelsldtpl hesqygelrl qqaytlsdfq
      601 ykndplfgkn qlpgipkhly qaqlsyalnn glyiglntey askmahdyan srfsddyqiw
      661 gidvgyapeh qswktwinfk nitdekyaav vipglndkga dvarsspgeg fstyagvsfk
      721 f
//
LOCUS       WP_005106904             338 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Acinetobacter lwoffii].
ACCESSION   WP_005106904
VERSION     WP_005106904.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter lwoffii
  ORGANISM  Acinetobacter lwoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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
REFERENCE   4  (residues 1 to 338)
  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 338)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Acinetobacter lwoffii"
                     /db_xref="taxon:28090"
     Protein         1..338
                     /product="CmpA/NrtA family 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=38297
     Region          2..249
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mstlekteln igyiplldcv ailwaekqgy faeqgltinl iheaswsslr drlaygflda
       61 ahclsamlpa aalgtdqlqv alqtplvlsv nqafislrqd lcyelgiqpe ddeqntskkl
      121 vqalqqnhsi nlayvykysi hhyclkewla ltdpqlakni qlmtspppsm vkgiskqvfd
      181 gfcvgepwni qaklegysfi vaasqnvipk vadkvlamtq ewaeqhpftv eavvkavqka
      241 qddlkqrpdl sevwdmlvdy qiiqfecsaq rhvydfykik niirnfvgks aqpkvddfiw
      301 llqqmqkwed iemtvaekkq iaeqciyslq sqhadiig
//
LOCUS       WP_005106978             434 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Acinetobacter
            lwoffii].
ACCESSION   WP_005106978
VERSION     WP_005106978.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter lwoffii
  ORGANISM  Acinetobacter lwoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 434)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Acinetobacter lwoffii"
                     /db_xref="taxon:28090"
     Protein         1..434
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=49911
     Region          24..390
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mdqyctlqiy qedewldcai veivgqqqtg wqaatrtsyl feyaifymnl sdghalayhl
       61 pvnvqntlqs twpaflmdll pqgygrkell rqlnfsentq eqadwallka gagnpignlr
      121 ikeayewlqg qfpvqqnhgf sldqvverqe nfieslasyg lfiagssgiq gewpkllltq
      181 ghddlfyldh tltdhqvkqh wlvkfsrgsd qnldkilmhe alymkiaqyl glrvhqelel
      241 hgktlfiprf drkvsdgkve riaqesiasl ggkagfgvrm thnqicsllm qcctepkqei
      301 feylkrdlan valgnkdnht rntaiqrfnn giirltplfd fapmwlhpdg iarttrwerd
      361 dhggmpiwhs vieqiaestm idpkeikavl ieqlplyqgl lehmqylqla peilensqyr
      421 idnicqqlee lnyg
//
LOCUS       WP_005107354             875 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Acinetobacter lwoffii].
ACCESSION   WP_005107354
VERSION     WP_005107354.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter lwoffii
  ORGANISM  Acinetobacter lwoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 875)
  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 875)
  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 875)
  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   4  (residues 1 to 875)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..875
                     /organism="Acinetobacter lwoffii"
                     /db_xref="taxon:28090"
     Protein         1..875
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=98296
     Region          106..832
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mtqrldqins siasntsttp qkirsdllis afeqseiknt ldhtrltstq lthipnleki
       61 pastkrikpl nnflgqdrar asveagialp ysgynifavg taglgkrtmv krllqqhakt
      121 metpndwvyv nnfqnqrqpi alelpsgqgp kfqamlnqsw qtilkqlerr ftaetyhnri
      181 emirqetgde qqqalieltk egaeldlkli srhdehcfvp vhliddklqe msqedlnals
      241 nkdraelasn mrymdkkler lglhlgdled dardrvqiln rdiakqvvlp rveqilakfk
      301 hveglehylk yyaediinnv eivleqeedd ftpalfsrvp aryqanviit hkpnsgapvi
      361 fedfpthynl lghveqltqn gtittdftli rpgtlhkang gflmleaeql leqpyawqgl
      421 kralksghlk lsslehmitl tgsisiepas iplnikvill aepeiyyeil elepelgsif
      481 kiradftdtl qrnddneqay mqliadyvqs dkllpfdrsa laalltdssr qaedqsslsl
      541 haltlgdlir eahhhafqag dkmvsekhin taldhrkyrl gylrelywqd ltrgtqliet
      601 rghrlgqina lsvihyadve fglpsrltas vyqgggdild iersvelggs lhakgvllms
      661 sflkahfgre qtlhfsaala feqsygqvdg dsatvaelsa llsaisqlpi dqswaitgsm
      721 nqlgqvqpvg gvnakiegff dacklqgltg kqgviiprqn mqhlmlrkdv tiaveegqfh
      781 ihaidtidqa leilmarpvg tldkkgrysk nsiyaavmaq ldywqaiedg aelvevpkkk
      841 kkkkkkkdkk qivepqteve advstveqpd aated
//
LOCUS       WP_005107698             421 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Acinetobacter lwoffii].
ACCESSION   WP_005107698
VERSION     WP_005107698.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter lwoffii
  ORGANISM  Acinetobacter lwoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Acinetobacter lwoffii"
                     /db_xref="taxon:28090"
     Protein         1..421
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=47979
     Region          5..295
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          290..385
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mavhflhtsd whlgqffhnh drefehaqfl twlleqikak qphalliagd ifdvinpass
       61 aqrqlyqfla dahdlaphmq tlmiagnhds gyrieqvepl lakfnakavg ivgrtaennl
      121 nlnlnldrll ipiydqdkni iawcltlpyl rsaeitglne htsnnqnais ylhqqliaea
      181 karkqphqal ilmshahmqg getsdserpi ivgneealst alfddvidyv alghlhkpqk
      241 vgqphirysg spiplsfsei nykhqivevr idpeqnpenr fqydalsipr tvelfrvrek
      301 lenlittiqa lpageieqls arhflevgyt tdapppvdlr qqieqalpan ryrllrisri
      361 yqqqvdlsss qskidlappt peslffniwk kmgyeqdhsv qrdfqellne aqhelaqkqq
      421 a
//
LOCUS       WP_005107814             140 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Acinetobacter lwoffii].
ACCESSION   WP_005107814
VERSION     WP_005107814.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter lwoffii
  ORGANISM  Acinetobacter lwoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Acinetobacter lwoffii"
                     /db_xref="taxon:28090"
     Protein         1..140
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15404
     Region          1..140
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mslfllflsa fgaatllplq seavllgllv qgeqsavlli avaslgnilg scvnwylglk
       61 iehyknkkwf pvsadkmlka qatyqkygyw slllswvpii gdpitliagl lkenlvrfll
      121 mvsiakigry lfvyaafamf
//
LOCUS       WP_005108535             142 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acinetobacter lwoffii].
ACCESSION   WP_005108535
VERSION     WP_005108535.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter lwoffii
  ORGANISM  Acinetobacter lwoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Acinetobacter lwoffii"
                     /db_xref="taxon:28090"
     Protein         1..142
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15295
     Region          4..124
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mlyrqgftli elmiviaiig ilaaiaypsy qnykirthrv naqaemmaia qnltkfkitn
       61 gnyasatiga vyggnvipke gtplykldls vttsswelta tpenntsqtg tgvivldssg
      121 nkcwektstp ctptatsnwd gr
//
LOCUS       WP_005109495             344 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter baumannii].
ACCESSION   WP_005109495
VERSION     WP_005109495.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 344)
  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 344)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 344)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 344)
  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   5  (residues 1 to 344)
  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   6  (residues 1 to 344)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..344
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38958
     Region          21..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <249..336
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtpelpgtyi nllaeivkrr gisceqfleg sgvtpeqlkk pywyvefntl nnllehaiql
       61 thepalagyl alemkascyg svgmaamvsa nleealkile qfigsrcdaf kpelkqeqdd
      121 vywsihqplk sfqlssdati flllgfvyia khltglsslg tvqlnmpepl gfskikdklg
      181 vsclfeqkhn iwifpkeylm qpvltadpml apllkaqckk didklklrsg wkaeisqvik
      241 kllinsqgei lkvkqvaqmm nmserslqry laientsfsa lvdltrkqya qdllqnssms
      301 ieavalrlgy adtphftraf krwmgvtpky yqtqlklknl eire
//
LOCUS       WP_005110763             293 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Acinetobacter
            baumannii].
ACCESSION   WP_005110763
VERSION     WP_005110763.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..293
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32949
     Region          13..255
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 meikvlvdvk tklgecptwd avrqrlfwvd ivdgrlfccd efggnirawe vhkkigsfal
       61 qenyngaiva ledglyqldf dtgnlkficn pepdlpqnrl ndgrvdrrgr fvfgsmnrle
      121 dgntaslyrl dadykiekle nnintsnsic wspdgaklyf adtwqgeiws ydydletgqi
      181 snktifckid tsdggsadgs tvdregylwn akvysgqlvr yrpdgqidri iempvkkits
      241 avfggknldv lfvtsmsqpp lprfpddnql rgsvfaiygl giqgladarf mge
//
LOCUS       WP_005111315             204 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Mycobacteroides abscessus].
ACCESSION   WP_005111315
VERSION     WP_005111315.1
KEYWORDS    RefSeq.
SOURCE      Mycobacteroides abscessus (Mycobacterium abscessus)
  ORGANISM  Mycobacteroides abscessus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacteroides.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Mycobacteroides abscessus"
                     /db_xref="taxon:36809"
     Protein         1..204
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=22318
     Region          1..187
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mriviamtga tgavlgvrll enlaarpdie thlvisrwgr atidyetdrt pveveklada
       61 vykpddmyap issgsfttda tivvpcsmkt vaairagysd gliaraadvt lkerrrlvlv
      121 pretplseih ldnmlalsrm gahivppmpa fyqmpntidd lvnhtvmril daagieneta
      181 prwrglparn erntnkngnp ygvq
//
LOCUS       WP_005112689             217 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Mycobacteroides abscessus].
ACCESSION   WP_005112689
VERSION     WP_005112689.1
KEYWORDS    RefSeq.
SOURCE      Mycobacteroides abscessus (Mycobacterium abscessus)
  ORGANISM  Mycobacteroides abscessus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacteroides.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Mycobacteroides abscessus"
                     /db_xref="taxon:36809"
     Protein         1..217
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=24079
     Region          16..197
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mqpdgrwerl rqiaanqfgl ftahqaralr vrryelsrma dagqlwrarh gvyaftdesa
       61 dkypyedwaa qwlalrpaad vgerrgdpdv vishqsaaei ldlgtivshd ilhlsgprri
      121 nvrsarvlah rqpvgecdad wqlveglpva taprviedla aahidgshlg iaiedalhrg
      181 ladvddihar ldrhantwna rngtelalrl ltsagrh
//
LOCUS       WP_005113704             254 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Mycobacteroides abscessus].
ACCESSION   WP_005113704
VERSION     WP_005113704.1
KEYWORDS    RefSeq.
SOURCE      Mycobacteroides abscessus (Mycobacterium abscessus)
  ORGANISM  Mycobacteroides abscessus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacteroides.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Mycobacteroides abscessus"
                     /db_xref="taxon:36809"
     Protein         1..254
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=26981
     Region          107..237
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mkvvrralvl gvvaiaaata vghpwsaesf tsalksmwat idstaapaat tpldpsetgn
       61 viaglldhah vvdrlpnvpg yergckrgqa csfgpawndp qnhsgcdtrs rilqaqladv
      121 ivkpnthnck vlsgtlhdpy tgqviaydag rdpsavqldh vfalgrswda gaslwdeakr
      181 valandpvnl favsgpanre ksdsglewlp pnrdfqctyi arylavavty dlnittndrd
      241 iavrqcpait ggav
//
LOCUS       WP_005118054             236 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Mycobacteroides abscessus].
ACCESSION   WP_005118054
VERSION     WP_005118054.1
KEYWORDS    RefSeq.
SOURCE      Mycobacteroides abscessus (Mycobacterium abscessus)
  ORGANISM  Mycobacteroides abscessus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacteroides.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Mycobacteroides abscessus"
                     /db_xref="taxon:36809"
     Protein         1..236
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=25948
     Region          89..>200
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 msnrtmliva iaaaiavvva yqvstryrll ranavagqrn iptlvrgqdp lagvivvpkr
       61 irssdyqrse fgdawsddtd apsgrngcdt rndilnrdlt dksfvytrrc psavgagllh
      121 dpytgvqvaf mrgpksgdav qidhivplay awdmgarewq patrwrfand panliavqgq
      181 ankdkgdqap gswmppnkaf wcqysmqfae vvrgyhlsvd ersanairka tqtcph
//
LOCUS       WP_005124324             385 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Acinetobacter
            baumannii].
ACCESSION   WP_005124324
VERSION     WP_005124324.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 385)
  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 385)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..385
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44761
     Region          7..373
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mtsslkkial lkqglgknsp faagrqgtle aiehlgyvqi dtisvverah hhilwsrvpn
       61 ydlshlnslv rerqifeywy haasylpmkd yryalpamms vrkgesryfn rgdqhlmnei
      121 larvraegki rlrdidkknk eslgnwwntg pgrrafeqly mqgdlmicer ngmekvydlt
      181 erclpenidl slptlyeyaq ylfnntlrah gaftwkqlvh lkkndlketm rvvlkeqida
      241 gvvsaiklad gqtlyvdvta ieqqldtdfg lkilspfdns lihrdrltsl fefdyriecy
      301 vpaakrvfgy fclpilyqne lvgridckah rtvkelevis lhlektvkdk ehfffeldqe
      361 lkrfaafnqc stvndkvvkl irskl
//
LOCUS       WP_005128604             292 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Acinetobacter].
ACCESSION   WP_005128604
VERSION     WP_005128604.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..292
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32836
     Region          13..255
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 meikvlvdvk tklgecptwd avrqrlfwvd ivdgrlfccd efggnirawe vhkkigsfal
       61 qenyngaiva ledglyqldf etgnlkficn pepdlpqnrl ndgrvdrqgr fvfgsmnrle
      121 dgntaslyrl dadykiekle nnintsnsic wspdgtklyf adtwqgeiws ydydletgqi
      181 snktifckid tsdggsadgs tvdregylwn akvysgqlvr yrpdgkidri iempvkkits
      241 avfggknldv lfvtsmsqpp lprfpddnql rgsvfaiygl giqgiadarf mg
//
LOCUS       WP_005128822             331 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Gammaproteobacteria].
ACCESSION   WP_005128822
VERSION     WP_005128822.1
KEYWORDS    RefSeq.
SOURCE      Gammaproteobacteria (g-proteobacteria)
  ORGANISM  Gammaproteobacteria
            Bacteria; Pseudomonadati; Pseudomonadota.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 331)
  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   6  (residues 1 to 331)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Gammaproteobacteria"
                     /db_xref="taxon:1236"
     Protein         1..331
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37664
     Region          23..198
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <188..331
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mfkkssdagi flwmtyqtmq nmgldaesif asvnlpnqpp dktirrdnst qyrfwnaaei
       61 iskdqniglh vgsqmpafrg lvieylflss stfgeglkra lkyqalltdv fdltltveqd
      121 kailsgfehs vrhyleaaig iflnffkyit nnsfapteih ltyskgasnd nykkvwkcpv
      181 vlgqstgaii fpstllqqvs paaepellkv heniaeqqla nlekhrliya ierllgngll
      241 esgnfdqkfi aeqlnrnprt lradlqaint syeqilnhyr erlarrllah tqesidqivy
      301 ltgfsepsaf trafkrwtge tpsayrqrkq k
//
LOCUS       WP_005129180             315 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Citrobacter].
ACCESSION   WP_005129180
VERSION     WP_005129180.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..315
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=34769
     Region          1..305
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 miefshvnkt ynqqqavsdl nlhlgegsfs vligtsgsgk sttlkminrl vehdsgqirf
       61 ageeirslpv lelrrrmgya iqsiglfphw tvaqniatvp qlqkwsrari ddrteelmal
      121 lgleadlrhr yphqlsggqq qrvgvarala adpqvllmde pfgaldpvtr salqqemtri
      181 hrllgrtivl vthdidealr laehlvlmda gkvvqqgtpl smltapvndf vrtffghsel
      241 gvrllslrtv gdftrrgeql ageplvdemt lrdalsvfva rgcdvlpvvn aqgvargtlh
      301 fhdllsetph setsv
//
LOCUS       WP_005129557             335 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005129557
VERSION     WP_005129557.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 335)
  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 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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (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   5  (residues 1 to 335)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37983
     Region          23..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          251..328
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msqtatalas wvkaiqkald kagcdsqtll kqagldiqal hnpdarysle htatlwrlav
       61 eatqdscfgl kvasqvnqnt fhvlghsltt sttlkemflk iiryfrivtd ipelefygqg
      121 nnhyfvihvp eevqpesida fisifirscr alqeslfspl rielrrsepe dldtfqnilk
      181 apiifnapkd mivfdtatie kpleganpsl sqeydeiiir ylarfdkeni larvklklie
      241 klssgdfqqq eiakslglsi rslqrklsae ntsyselldd trhelalsyi kntghsvtei
      301 ayilgftdvs sftrafrrwt dlspihyrek ylacs
//
LOCUS       WP_005130408             701 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Acinetobacter baumannii].
ACCESSION   WP_005130408
VERSION     WP_005130408.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..701
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=76954
     Region          12..701
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mllphfkksv ltlclfpsil yaadtyptvt lnpitvqaeg nwldeanaqk vlnhagartv
       61 iqrdelinrg vtsvkealrt vpgiqapena gtagsdasls igvrgltsrf sprsqvlvdg
      121 vplsfapygq sqlslaptsl gntesidvvr gagsvrfgpq nvggiinfns rtipetfagt
      181 vdltteiaen ghvkfnpnlf vggtldnglg lallysgvng egfrdkndds dindirlkaa
      241 yaideyakie anlhrydadv dmpggltpaq faenpyqslr nhdymkghrt dgsvkysykk
      301 ddkafellay htdtfrdagm ersgsklyqt aprnykvtai epryshayql gttenevsvg
      361 yrylhetsee avnrasyntv tgptneyawt kadgktdaha lfidnrtdvg awslipgvrf
      421 ekikttenmy klnkdasvln gvhaeksyda vlpsfsvmyk andlwnifan ygksfaplqy
      481 sqmantnasg ayltmqglqp ekannyeigt hyldpylsle ftlfyidfsd elkrddatqt
      541 ysnlgaehkg aefgfkynlg aisdelsgis lyanttytka tasagenkgq dldfysqwvg
      601 nagidykvdq wtlntnfygq sgqtasgthd atgrygnipg yglvgvrasy dfsntqlngl
      661 kvgfgvknlf dreyytrsad qvggmyvgap qtyylqtsfd f
//
LOCUS       WP_005130659             625 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Acinetobacter baumannii].
ACCESSION   WP_005130659
VERSION     WP_005130659.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 625)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..625
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68795
     Region          19..625
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mqntakkatl patalaalgv vfgdigtspl yalkesfhaa hglgiqpenv lgilsiifwc
       61 lmliisikyv aivmradnng eggimallal nlrkakiadn kkiymiaigf igaslffgdg
      121 iitpaisvls aveglsiatd vfdpfimpia iaiivtlflv qkhgtafvgk ffgpitlvwf
      181 lslgilgihs viqtpvvlgm fsphwaiqfi yhhpimtffv mgavvltvtg gealyadmgh
      241 fgpvpirlaw ffvvlpclvl nyagqgalll rdpaaienpf yllvpqwaly pmiimatmat
      301 viasqavisg vfslarqaiq lgylprlsik htseseegqi yvpflnwlll iaiiililif
      361 ktssnlasay glavtltmlc dtilvavfiy sawkwslpkv lfliipffil esvlvgatsl
      421 kilsggwvpl ligaiavtil mtwkrgrelt faklehdtls ldlfvksign svhwvpgdav
      481 fmtgtpnvvp hamlhnikhn kvlhqrnilv tvviedvpfv apeerittet laehffriki
      541 fygfkdemnv pkalmqayeq lgleydlmhi sffisrdriv hsvgdgmspw reklfismqr
      601 ntspvsdfyq iptnrvvelg sqiei
//
LOCUS       WP_005130864             349 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter baumannii].
ACCESSION   WP_005130864
VERSION     WP_005130864.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 349)
  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 349)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 349)
  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   4  (residues 1 to 349)
  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 349)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..349
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39899
     Region          47..210
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          257..332
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqeftisngy fylwntylke kgidwhtlnl seiqtrqvqn ilsasidaqs sldlfielle
       61 itetrlhvtn lalemaacit panfgvlgym asrsdtlgqv veyiakfhrl vidgaqvvpi
      121 qieqdaskir lywplvddsn illseltlaa mvqlakqiap lhefllqhve fvhrargavv
      181 hyqrffqckl sferpyyalt faseslnvrp qhadptlvql lvkqaeealv qrkihadlvq
      241 qihwivqeyf khkqqapkie diaielnvsv rslqrqlqvl ntsfklilda ermkrceill
      301 sqnesltaia dqlgysdqsa larayknltg qtlltrkkql qliqknatk
//
LOCUS       WP_005131359             342 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter baumannii].
ACCESSION   WP_005131359
VERSION     WP_005131359.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 342)
  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 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 342)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 342)
  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   5  (residues 1 to 342)
  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   6  (residues 1 to 342)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..342
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39287
     Region          28..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          98..334
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mvvqsslskg tisialvhea lsaayakgln tqiilnkagi paellmtpka rvpvatyaql
       61 wielanamdd effgmdshpm rrgsyklltk lvstaetlek alydilkffn fvlddirgel
      121 ireqekaylv ihdqeqpkrm ftyatflmlv hglmcwlvdq rislnsiavr cpkpndiqdy
      181 lvrfcedief naetnqiefd ahyldikikk dkkalydfle qtpqnllvrf knenalsvvi
      241 rrhllklhpa ewpelkdvaq qlniseatvq rrlkhegvsy qqikneircd iaierlsksn
      301 dsiqdisedl nfhdpsafhr afkkwtgvsp gayrdnlttf kq
//
LOCUS       WP_005132772             337 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter baumannii].
ACCESSION   WP_005132772
VERSION     WP_005132772.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 337)
  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 337)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..337
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38392
     Region          31..208
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          252..333
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkyawafers vhsvrlmadf amesgisyqi ilqgtglsqq qlldpnmvvt ghqelqlihn
       61 lveqlgdrpt lglevgtryh fttfgplgma lmssasirea ldlaltyftl tfaftrfdvs
      121 dtpqgiriei deqdipssvr qfiierdaaa litvqrdlvq dnfcqylafs fqpkgdaepy
      181 rnlfgvmpef gaaksfvild pqkvdqkllm anelvlhtae eqcrqilekr qsqnkfttlv
      241 qqqlmsmrge mpsmdivadr lhlnirtlrr hlasegmtfi qireevrqvl aeqylalpka
      301 sveqiaewlg yaepasfiha ykrwhgktph amrlvqk
//
LOCUS       WP_005127321             334 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase LdtE [Shigella flexneri].
ACCESSION   WP_005127321
VERSION     WP_005127321.1
KEYWORDS    RefSeq.
SOURCE      Shigella flexneri
  ORGANISM  Shigella flexneri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Shigella.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Monton Silva,A., Otten,C., Biboy,J., Breukink,E., VanNieuwenhze,M.,
            Vollmer,W. and den Blaauwen,T.
  TITLE     The Fluorescent D-Amino Acid NADA as a Tool to Study the
            Conditional Activity of Transpeptidases in Escherichia coli
  JOURNAL   Front Microbiol 9, 2101 (2018)
   PUBMED   30233559
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Cava,F., de Pedro,M.A., Lam,H., Davis,B.M. and Waldor,M.K.
  TITLE     Distinct pathways for modification of the bacterial cell wall by
            non-canonical D-amino acids
  JOURNAL   EMBO J 30 (16), 3442-3453 (2011)
   PUBMED   21792174
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Magnet,S., Dubost,L., Marie,A., Arthur,M. and Gutmann,L.
  TITLE     Identification of the L,D-transpeptidases for peptidoglycan
            cross-linking in Escherichia coli
  JOURNAL   J Bacteriol 190 (13), 4782-4785 (2008)
   PUBMED   18456808
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF047955.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Shigella flexneri"
                     /db_xref="taxon:623"
     gene            1..334
                     /gene="ldtE"
     Protein         1..334
                     /product="L,D-transpeptidase LdtE"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=35955
     Region          7..303
                     /region_name="PRK10260"
                     /note="L,D-transpeptidase; Provisional"
                     /db_xref="CDD:182341"
ORIGIN      
        1 mkraslltlt ligafsaiqa awavdyplpp tgsrlvgqnq tytvqegdkn lqaiarrfdt
       61 aamlileann tiapvpkpgt titipsqlll pdaprqgiiv nlaelrlyyy ppgenivqvy
      121 pigiglqgle tpvmetrvgq kipnptwtpt agirqrsler giklppvvpa gpnnplgrya
      181 lrlahgngey lihgtsapds vglrvssgci rmnapdikal fssvrtgtpv kvinepmkys
      241 vepngmryve vhrplsaeeq qnvqtmpytl pagftqfkdn kavdqklvdk alyrragypv
      301 svssgatpaa snapsvesaq ngepeqgnml ratq
//
LOCUS       WP_005135026             342 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005135026
VERSION     WP_005135026.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 342)
  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 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 342)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 342)
  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   5  (residues 1 to 342)
  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   6  (residues 1 to 342)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..342
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39164
     Region          28..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          98..336
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mvvqsslskg tisialvhea lsaayakgln tqiilnkagi paellmtpka rvpvatyaql
       61 wielanamdd effgmdshpm rrgsyklltk lvstaetlek alydilkffn fvlddirgel
      121 ireqekaylv ihdqkqpkrm ftyatflmlv hglmcwlvdq riglnriavr cpkpndiqdy
      181 lvrfcedief naktnqiefd ahyldikikk dkkalydfle qtpqnllvrf knenalsvvi
      241 rrhllklhpa ewpelkdvaq qlniseatvq rrlkhegvsy qqikneircd iaierlsksn
      301 dsiqdisedl nfhdpsafhr afkkwtgvsp gayreatlns ta
//
LOCUS       WP_005134772             709 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor family protein [Acinetobacter
            calcoaceticus/baumannii complex].
ACCESSION   WP_005134772
VERSION     WP_005134772.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus/baumannii complex
  ORGANISM  Acinetobacter calcoaceticus/baumannii complex
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Acinetobacter calcoaceticus/baumannii complex"
                     /db_xref="taxon:909768"
     Protein         1..709
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=78415
     Region          35..705
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 msllrldrlh ycilmsmgci ssplvwaedl nsdvaklptl hveatrtdtg ylqtpasvfr
       61 ietpqvdsss qvnltevvkg ipslqirnre nyaqdlqlsm rgfgarstfg vrgirlyvdg
      121 ipatmpdgqg qtsnidlssl dhvevltgpf sslygnssgg tiltstkegq gkdsielsys
      181 ggshdksrag lvlqggakga nepsyiisss yfdtdgyreh sgaekvlnna klswnlddgs
      241 kinwvtnyvk ihaddpqglt hdqwnanpkq qvpflkqfnv rkdieqtqtg vtwskpindk
      301 nelyamaylg nrqvtqyqsi pkstqdasin haggvidfer nyygadfrwt gkellpnttl
      361 svgvaldamd edrkgfenfn lvngqpsygv kgnlrrdedn tlwnidpylq aswqflptwr
      421 ldtgvrysnv hyksednyls ngddsgktdy dkvlpsvals wqilpelmay vsyakgfetp
      481 tftemayrpd gqsgfnfdlt astsdtyetg lksqnqlgdf tlavfqtktk ddivsagnsn
      541 grstfrnadk tlregvefaw nkklwrdlia tasysyleat fdadipalgn iaqissgnai
      601 pgiaknqaya slawqpshgl yggvdvqymd kvyvndtnsd aapsysvtsa nvgyawvmgd
      661 wkvnsfarvd nlfdkkyvgs vivndgnsry fepadgrnws aglrvikqf
//
LOCUS       WP_005138031             730 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Acinetobacter baumannii].
ACCESSION   WP_005138031
VERSION     WP_005138031.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 730)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..730
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=80864
     Region          35..726
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 msllrldrlh ycilmsmgci ssplvwaedl nsdvaklptl hveatrtdtg ylqtpasvfr
       61 ieapqvdsss qvnltevvkg ipslqirnre nyaqdlqlsm rgfgarstfg vrgirlyvdg
      121 ipatmpdgqg qtsnidlssl dhvevltgpf sslygnssgg tiltstkegq gkdsielsys
      181 ggshdksrag lvlqggakga nepsyiisss yfdtdgyreh sgaekvlnna klswnlddgs
      241 kinwvtnyvk ihaddpqglt rdlwqqnpkq idpdirdknf nvrkdieqtq tgvtwskpin
      301 dknelyamay lgnrqviqyq siprcafkkd tqicipksaq lnpnhaggvi dfernyygad
      361 frwtgkellp nttlsagval damdedrkgf enfnlvngqp sygvkgnlrr dedntlwnid
      421 pylqaswqfl ptwrldtgvr ysnvhykskd nylsngddsg ktdydkvlps aalswqilpe
      481 lmayvsyakg fetptftema yqtdisksgf nfglkpstsd tyetglksqn llgdftlavf
      541 qtktkndivs agnlggrstf rnadktlreg vefawnkklw rdltatasyt yldatfdanv
      601 pekldqddkv lasaiptgna ipgiaknqay aslawqpshg lyggvdvqym dkvyvndtns
      661 daapsysvts anvgyawvmg dwkvnsfarv dnlfdkkyvg svivndgnsr yfepadgrnw
      721 saglrvikqf
//
LOCUS       WP_005140040             335 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter baumannii].
ACCESSION   WP_005140040
VERSION     WP_005140040.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 335)
  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 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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (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   5  (residues 1 to 335)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37906
     Region          23..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          251..328
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpqtatalas wvkaiqkale kagvdsqpll eqagldiqal snpdaryslk qtanlwklav
       61 qktqdscfgl kvasqvnqnt fhvlghslit sttlkemflr iiryfrvvtd ipelefygqg
      121 nnhyfvihvp devqpesida fisvfirssr alqgsvfspl rielrrskpe dletfqsilk
      181 apivfnapkd mivfdtatie qpleganpsl tqeydeiinr ylarfdkeni larvkvklie
      241 klstgdfqqq dvakslglsi rslqrklsae ntsyselldq trhelalsyi knsshnitei
      301 ayilgftdvs sftrafrrwt dlspihyrek ylacs
//
LOCUS       WP_005145936             876 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: Lon protease family protein [unclassified
            Acinetobacter].
ACCESSION   WP_005145936
VERSION     WP_005145936.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 876)
  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 876)
  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 876)
  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   4  (residues 1 to 876)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..876
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..876
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=98182
     Region          106..837
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mtqkldqmta ttlsltptnt itanlnslps afeqtdiqpt ltktalraeq lthipdlaei
       61 psstkrikpl nnflgqdrar asveagislp ysgynifavg taglgkrtmi krllqqhakt
      121 mptpndwvyv nnfknprqpi alrfpagqgt kfqnalqqaw qiilkqlerr fsaesyhnri
      181 erirqdtgdv qqqalveltk egeeinlkli srndkhvfip iqlkeneyhe ltqnelnalp
      241 skerteinsn irymekkler lglhlgdled dardrvssln rdiatqvvmp riesilnknk
      301 evsglelflk hyaediidnv elileqeedd ftpalfnrvp sryqanviia nkpnsgapvi
      361 fedfpthynl lghveqlthn gtittdftli rpgslhqang gflmleaeql leqpyawqgl
      421 kralksgqlk lsslehmltl tgsisiepas vpldikvill aepeiyyeil elepelgsvf
      481 kiradftdtl qrndsneqay mqliadyvqa dkllpfdrsa laalltdssr qaedqsslsl
      541 hastlgdlir eahhhafkad dkividqhvn qalhhrqyrl gylrelywqd lsrgtqliet
      601 sghrlgqina lsvihyadve fglpsrltas vyqgggdild iersvelggs lhakgvllms
      661 sflkahfgre qilhfsaala feqsygqvdg dsatvaelsa lisaicqipi dqswaitgsm
      721 nqlgqvqpig gvnakiegfy dacklqgltg kqgviiprqn mqhlmlrqdv idavqagqfh
      781 vhaidtidqa leilmarpvg tldkkgrysk nsiyaavmeq leywqaiedg eaveddepkk
      841 kkkrkkakke taeakvseet aveakslksl kqkkkr
//
LOCUS       WP_005146608             264 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: hydroxypyruvate isomerase family protein
            [unclassified Acinetobacter].
ACCESSION   WP_005146608
VERSION     WP_005146608.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..264
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29604
     Region          1..257
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mshlavnlsm iftevplier falaqahgfq hveiqfpyel diidirtqle qynlslclin
       61 vpagdlmqgg nglagvpgre vefhqalela ityanalnvp rvnilagkqp ldadllpcln
      121 tlssnlklac hmlteqgiqp vlemingtdm prflvqniaq aqemleavnh palkmqydcy
      181 hmammgedvl aglqenidqi ghiqfadcpd rhepdtgnia ykqifdwllq sdyrgliaae
      241 yrpktqsyqs fawkkkyfsn dvnt
//
LOCUS       WP_005146940             159 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Acinetobacter sp. ANC 3929].
ACCESSION   WP_005146940
VERSION     WP_005146940.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. ANC 3929
  ORGANISM  Acinetobacter sp. ANC 3929
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Acinetobacter sp. ANC 3929"
                     /db_xref="taxon:1217707"
     Protein         1..159
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17497
     Region          10..159
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 maeelvlqqg hkaeqyqnii pqiqaivede tdvianlani caalkqqfdw fwigfylvkd
       61 selvlgpfqg piactriakg cgvcgtawqq qqviivpdvd qfpghiacss askseivlpi
      121 mkngqcvgvl dvdsdelnqf deidaeylkq litvietfi
//
LOCUS       WP_005149717             232 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [unclassified Acinetobacter].
ACCESSION   WP_005149717
VERSION     WP_005149717.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 232)
  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 232)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 232)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..232
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=25615
     Region          3..210
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 mslsddeqld slksfakkyg samisgilia liaffgweyw qkknlaeaqn qtakvqklmd
       61 eakaasgqpn afaslsetad kivkddadsa qaiqtqfima klaydkqdya aaekalkkve
      121 nskvkdagll qivkirladt qlaqskydea lktlssvtdp afkataeelr gdifvakkdn
      181 asarkayqsa wdnllerkqe rqllqikles vgvlvddpef erpildtkvd es
//
LOCUS       WP_005150007             337 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Acinetobacter].
ACCESSION   WP_005150007
VERSION     WP_005150007.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 337)
  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 337)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..337
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38522
     Region          22..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          249..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msrdtisihf vnaaltgvkr lgmdvetlls hvgieaellr qpkarispeq ytrfvkmlwm
       61 vtqdehvgfd vqprrlgtfa imsqliihsk tlgqalelss qfyklfgdew svslerdkhe
      121 arlvphipka ldpdhfites mlmiwhglas wlierrlple rvhfgyerpn hadeydalff
      181 apvmqfdapr teitfaadyl dlpirqdekt leeflkaapa qllvkfkntn sltsrirdvl
      241 ksqigeempt lndvaamlyl spqtlrrrla aegksyqgvk dalrrdaaih llltpnltle
      301 dvaqqvgfse tstfhrafkk wtgvtpglyr qlhghhn
//
LOCUS       WP_005151848             356 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [unclassified Acinetobacter].
ACCESSION   WP_005151848
VERSION     WP_005151848.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..356
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39816
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvkniek nfgafhalkn isldfpegel vallgpsgcg kttllriiag lesadggqvl
       61 legedatdih vrerqvgfvf qhyalfrhmt vfdniafglr vrpratrpse aeikkrvtrl
      121 ldlvqlgfla drypaqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 tlhdelhits ifvthdqeea levadqiivm nkgdveqigs prevyekpat pfvfdflgqa
      241 nrfegehtdg iirigddriq lptlldapqg kviafarpne lhihtqpqan tieatflrev
      301 wiagrvvael qdrsgrtiei llsveeanlh qfkpnqtvwi saaqlhlfad qstqva
//
LOCUS       WP_005152410             341 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Acinetobacter].
ACCESSION   WP_005152410
VERSION     WP_005152410.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 341)
  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 341)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38368
     Region          28..211
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          255..336
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkttstrqdq gipgvyglll ldvvsrwgys detlfapfhl tseqladpny riptpianel
       61 vkhalrltge stlgfhlgtq mrisihgfig yaimtahdit daialasrfi qlrlpflqly
      121 fstfgpkatl qlqcdievep lrteiilglt igimtmakal tgiddlkgev dldfaepagf
      181 ekykdrltst vrfnqphlis sfdkkylglk mvnadaiasq iainqcetel salgerrrla
      241 mrvrdiltns eqhylsienv aerlhmsdrt lkrqlaaegt sfstlvdevr yrhatsllsr
      301 tdysleqiad elgysdvanf srafkrwsgr spsnwrkdpy l
//
LOCUS       WP_005153416             339 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Acinetobacter].
ACCESSION   WP_005153416
VERSION     WP_005153416.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 339)
  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 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 339)
  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   4  (residues 1 to 339)
  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 339)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..339
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38927
     Region          19..197
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          110..339
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          255..335
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkrsilglmy liqgmrhvgi dvdarlanmg ihadaldpss iipdeiewdi lqyisqdisp
       61 eqglfigqhy alagygpflm llvtsdtlhk allngvqfqq lthlfgslql rieddliyll
      121 yrpidlsmhl gqlraqceis gtykflqdif kmmglevphi qielpfhrpk dltllaayqd
      181 yyghdvkfgc aqaafilent qilntkipsa diltyriyee kclqdiqhle ktaslkltvv
      241 eyvedylemq ngvipsmaet acaldipert lrhqlqqmqt sykeirerli kqkaikfien
      301 ssysieqvae mlgysesaaf nhafkrwfgl sprqyhrnh
//
LOCUS       WP_005153072             292 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Acinetobacter].
ACCESSION   WP_005153072
VERSION     WP_005153072.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 292)
  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 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 292)
  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   4  (residues 1 to 292)
  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 292)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..292
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32903
     Region          24..175
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          202..283
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mmndqtlinl flklipkegf fataidgitl mrvdhntppi avlqeptlvf vlqgqkhgyi
       61 gtetysfqqa eclivsvsmp fdcdtiasle apmlaismkl eadtvnella ktyfenyqfk
      121 plttgmcviq ydqtlssvli rllntltseq dvlilgdqik rellyrviqh sgadalnglv
      181 aqgnlrpiyk iceyiqhhft ekltiemlae qanmsistfh kafkqvtqhs plqylkvvrl
      241 hkakqllqna dqsvaqaaya vgyqsssqfs refkkrfgfp pkhaefntet es
//
LOCUS       WP_005156057             297 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Amycolatopsis azurea].
ACCESSION   WP_005156057
VERSION     WP_005156057.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis azurea
  ORGANISM  Amycolatopsis azurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 297)
  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 297)
  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   3  (residues 1 to 297)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Amycolatopsis azurea"
                     /db_xref="taxon:36819"
     Protein         1..297
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33304
     Region          191..296
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mprnqyattc efsgpfvgsr avsegdltra qlrsgpynrl fqdvyvpvgi prdhelrcka
       61 allvapegav ltgcsaatvr gfpfslendp vefvvpearg fhslsgthfr rtrllgqdfe
      121 pwrdgliatp srmtmdiltd trlrrsfprv vgfldmllha gfidgatlda ylrprhdngi
      181 vrarqalafs dgraesipes evrvwlrlgd ieaepqvevf dgtrflgrld laireaklai
      241 eydgawhleg eqprldarrr alieaegwef vviakeelyt dpramvrrvr aalnsrv
//
LOCUS       WP_005156363             213 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Amycolatopsis azurea].
ACCESSION   WP_005156363
VERSION     WP_005156363.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis azurea
  ORGANISM  Amycolatopsis azurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Amycolatopsis azurea"
                     /db_xref="taxon:36819"
     Protein         1..213
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23087
     Region          6..204
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdtsvtdhll sttravrrkl dldrpvepev leeclrlalq aptpgnqqaw rwlvvrdqgv
       61 kdqlselfrr vgkayletna aalgkaidep svarafasgq hlidvidrvp vyvipcltgr
      121 psgdnatdaa fyggifpavw nfqlalrsrg lgstlttyhl theaeaaeil gipadvtqvg
      181 llpvayttvp dfkpasrvpl sevayldgwg nal
//
LOCUS       WP_005156497             309 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Amycolatopsis azurea].
ACCESSION   WP_005156497
VERSION     WP_005156497.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis azurea
  ORGANISM  Amycolatopsis azurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Amycolatopsis azurea"
                     /db_xref="taxon:36819"
     Protein         1..309
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33919
     Region          14..278
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mneldaagit apalraayte crrinahhgr tfflatrllp artrpfahal ygfarmadev
       61 vdnpapgtdp avalddvavm vgqvfdggtp adpvltalad tvrrhdldre lfdaflrsmt
      121 mdlkvteyat yadlkeyihg saeviglqml pvfgtvvpvd eavpgaaalg eafqltnflr
      181 dvgedldrgr lylpteelaa fgvdrellaw srarglpdrr vrralavava rnravyrrae
      241 agipllrees rdcvrtalvl yegildeiaa lgydvlntra vvprrrraav alprllastw
      301 snsrlrlrs
//
LOCUS       WP_005156716             335 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter sp. NIPH 284].
ACCESSION   WP_005156716
VERSION     WP_005156716.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. NIPH 284
  ORGANISM  Acinetobacter sp. NIPH 284
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 335)
  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 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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 335)
  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   5  (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   6  (residues 1 to 335)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter sp. NIPH 284"
                     /db_xref="taxon:1217704"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38784
     Region          31..193
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          82..330
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msqlknytgs vygglghllk aycetkniei peqlqqvqnl erfdyviwrd lledlnrlnp
       61 kiglgleiae hvqpkhlgii aylalscenl gealaryhdf hrliydgspl vvefnppyas
      121 irweapepnp tqltdeiaia lmvqflklfm sgedlnlhev hfvntapkni mvyeqyfrck
      181 vrfdqpktql llpvteafkp lrtgdhtlqq lllqqaqall dklpnstqld qrlqhailtg
      241 lqknqyqidf iaeklglsvr qlqrhlqqqn ttfqervqqv rfmlateylk dphlslqeia
      301 lllcyseqsa fqrafkiwtg ltpqqwrknn tiyss
//
LOCUS       WP_005157551             272 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Amycolatopsis azurea].
ACCESSION   WP_005157551
VERSION     WP_005157551.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis azurea
  ORGANISM  Amycolatopsis azurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Magnet,S., Arbeloa,A., Mainardi,J.L., Hugonnet,J.E., Fourgeaud,M.,
            Dubost,L., Marie,A., Delfosse,V., Mayer,C., Rice,L.B. and Arthur,M.
  TITLE     Specificity of L,D-transpeptidases from gram-positive bacteria
            producing different peptidoglycan chemotypes
  JOURNAL   J Biol Chem 282 (18), 13151-13159 (2007)
   PUBMED   17311917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13395997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Amycolatopsis azurea"
                     /db_xref="taxon:36819"
     Protein         1..272
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=27894
     Region          <107..>158
                     /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          156..272
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(229..230,233,246..249,251)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mtrsqtscga arphaaaall alalvvlagc gstpaeggga aaavapqsss pealaalpea
       61 ntfgelksap adpahelpag gevlhpkada aiyrapgaep iarlpetqig sptwvpviar
      121 qgdwaqvllp trpngatgwl hatpetvesa qndyevrvdl agfrleilea gkqtgswtig
      181 tgkpqhptpt grafilasik esvntyspiv lplsshsdsh etfgggpgtv glhtwpdnsf
      241 vgkatsdgci rvtrealdrl velplgtvvh it
//
LOCUS       WP_005158222             416 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Acinetobacter sp. NIPH 284].
ACCESSION   WP_005158222
VERSION     WP_005158222.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. NIPH 284
  ORGANISM  Acinetobacter sp. NIPH 284
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Acinetobacter sp. NIPH 284"
                     /db_xref="taxon:1217704"
     Protein         1..416
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=48108
     Region          3..289
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          289..387
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mtvrffhtsd whlgqffynh srhyeheqfl awlleqikak qphalliagd ifdvinpssq
       61 aqkqlyqfla dahelapqmq tlmiagnhds gyrieqvepl lakynaktvg virwnqdksl
      121 dlerlilpiy deqkqivawc ialpflrsve itgfnehttn sqnaiaylhq qlieeakrrk
      181 tddqalilms hahmqggets dserpiiign eealstalfd dsidyvalgh lhkpqkvqhp
      241 hirysgspip lsfseinykh qvvevsidpt ksedsfnfea lpiprsiqlh kikdelsvvm
      301 qhlrnlpnep ienlehreyv dieyhtstpp qpnlrqqfed alpkdryrlv risrqylsne
      361 snaeskqnis lepptpeklf qqiwekkgyh addevtkdfm slvaeaqkql eddqtv
//
LOCUS       WP_005158427             252 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Amycolatopsis azurea].
ACCESSION   WP_005158427
VERSION     WP_005158427.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis azurea
  ORGANISM  Amycolatopsis azurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Amycolatopsis azurea"
                     /db_xref="taxon:36819"
     Protein         1..252
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=28500
     Region          1..249
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mlqfrllgpl eivlpdgril epssekmcki lgilllrnev ssvdvltrel wddnpprsal
       61 ttlqtyvyht rrmfdqacet geekpslvtr ppgyelkvpa eqvdtkvfer svakgrellg
      121 egdaeeagsi lrqglalwrg palanvdagd vlrghishle elriralelr ieadrargqr
      181 rdlipelrsl vvsyplnewf hsqlinelhh ggrraealqa yqdlrrilnd elglepmaei
      241 rrlhrdllas ta
//
LOCUS       WP_005158829             314 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Yersinia enterocolitica].
ACCESSION   WP_005158829
VERSION     WP_005158829.1
KEYWORDS    RefSeq.
SOURCE      Yersinia enterocolitica
  ORGANISM  Yersinia enterocolitica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (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   2  (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   3  (residues 1 to 314)
  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   4  (residues 1 to 314)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Yersinia enterocolitica"
                     /db_xref="taxon:630"
     Protein         1..314
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=35248
     Region          1..310
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mihfhqvsky fagkravdnl tlqiskgeft vligtsgsgk sttlkminrl iehdegeihf
       61 ageeirnykp edirrrmgya iqsiglfphw tvehnigtvp qllkwpqeri rlrviellel
      121 lhldpeqflh ryphqlsggq qqrvgvaral aadpevllmd epfgaldpvt rsalqfeitr
      181 ihqlsgrtiv lvthdideal aladrivlmd ggrviqqgtp lemltqpvnd fvrdffgrsd
      241 lgikllslgr aeqrirrget migqpilgtt slrealslfv srqtdkllvv deqgqplgvl
      301 yfadliadad rgev
//
LOCUS       WP_005159597             365 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter sp. NIPH 284].
ACCESSION   WP_005159597
VERSION     WP_005159597.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. NIPH 284
  ORGANISM  Acinetobacter sp. NIPH 284
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 365)
  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 365)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 365)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 365)
  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   5  (residues 1 to 365)
  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   6  (residues 1 to 365)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Acinetobacter sp. NIPH 284"
                     /db_xref="taxon:1217704"
     Protein         1..365
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42086
     Region          49..229
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          119..357
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mrllsiqpiy ssifhfcmsk stdldlnsak dtisialire alsvaasrgl dilhianqag
       61 vsvellsstk arvpvmqcar lwielaehmn deflgmdrhp mrrgsyslla klafsaetle
      121 qaiqeilkfl slvlddiqge liqqgakayl ilhdrehpkr mftystylml vhslmcwlsd
      181 qripfqkmtf kchqpveiqd yrvrfcediq fnadqnlief danylkhkik kdkqalndfl
      241 rqtpynlivr fknenslslq irrqlllqpp sewdelkeia qqlnmstati qrrlkqegvs
      301 yqqlkndirc diaierlskt ndsiqsisdd lsfhdpsafh rafkkwtgvs pgayraktlf
      361 skiea
//
LOCUS       WP_005160866             258 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Yersinia enterocolitica].
ACCESSION   WP_005160866
VERSION     WP_005160866.1
KEYWORDS    RefSeq.
SOURCE      Yersinia enterocolitica
  ORGANISM  Yersinia enterocolitica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Yersinia enterocolitica"
                     /db_xref="taxon:630"
     Protein         1..258
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=29180
     Region          1..167
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mymidynnfr aiksfnsrvr flvlhytaen fensinsltg nnvsvhylvp dldddsykka
       61 gfnnirifnl vdenarawha gvsswagran indtsigiei vnlatehsgv fdfppypenq
      121 iaavkqlaan ilqrypdisp thvvahsdia ptrksdpgpk fpwlelynng igawydsetk
      181 ekfvqqftqq glptkadlls yfktygydis iassddgyqh lvrafqlhlr sdnydghidi
      241 etvailyalv ekyfpaqn
//
LOCUS       WP_005161201             253 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [unclassified
            Acinetobacter].
ACCESSION   WP_005161201
VERSION     WP_005161201.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..253
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28809
     Region          25..250
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mseqnqtdkk ryyepatqdi dvanfrkvie srrsvrkftd kpipseilde cldlallapn
       61 ssnlqpwtfy vvqnpskkkq lvkaclgqla aktaselivc vartdrvdem akrnisefpf
      121 peapamvqky yrfipynykt gyfnalgnfk kvafkvartl dkqlpvtafn padaklwatk
      181 ttalacenlv lalraygfds cmmegfdepl vrkilklndq qypvmvigag eratdgvffp
      241 qyrfdrdlfi qkv
//
LOCUS       WP_005162152             340 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Acinetobacter].
ACCESSION   WP_005162152
VERSION     WP_005162152.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 340)
  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 340)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 340)
  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   4  (residues 1 to 340)
  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 340)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..340
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39516
     Region          40..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          262..337
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msvkiiigyl rlfnrvlqqe qidlskvvap elwqafhtcl qnpdehdfdv eryalllqsa
       61 qayfprpitl vlaehanlqd lglmgylast sldlqqalql lqryyslvfk qtnleqlnvq
      121 qfsdyiqivw gasysdyrem yelnlalifk isqsivqdal ippqmiqfgy aphtalyhfe
      181 kfygcpiqiq agqyaicfsn qilkaksiaa dqqlnhvlst qaqqslnsia sfeiqqqqfr
      241 qkiqthieqr llqqeellls yvakrlhcse rtlqrqlkty qlnfqnildq yrleqsklyl
      301 qqgkslseia erlnyadqsa fgrafkrwtg itpkqflksl
//
LOCUS       WP_005165157             212 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Yersinia
            enterocolitica].
ACCESSION   WP_005165157
VERSION     WP_005165157.1
KEYWORDS    RefSeq.
SOURCE      Yersinia enterocolitica
  ORGANISM  Yersinia enterocolitica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
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   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   3  (residues 1 to 212)
  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   4  (residues 1 to 212)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 212)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 212)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Yersinia enterocolitica"
                     /db_xref="taxon:630"
     Protein         1..212
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=23652
     Region          17..200
                     /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"
ORIGIN      
        1 mrpsdsrisa talllsrgir cvvlhpdded getltnhlrr mgfkvqafwp ipeqlpadtd
       61 lifyalqsdk pepdvswlap gkhaliavia yenptfidqa lkmgagttit tpirvsglls
      121 amvfalhhaq qqrqmsdrie rlekkvlgir qvseakailm rmhsigeeqa yeilrhqamd
      181 kritveeisc aliqandifs wttpgvansr kn
//
LOCUS       WP_005165501             399 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Amycolatopsis azurea].
ACCESSION   WP_005165501
VERSION     WP_005165501.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis azurea
  ORGANISM  Amycolatopsis azurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 399)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Amycolatopsis azurea"
                     /db_xref="taxon:36819"
     Protein         1..399
                     /product="amidohydrolase family protein"
                     /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=41716
     Region          4..395
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mtlqllltad rilprpgtpv sdgavlvegd rilaaglrad vvaqaspdae rldfpgatll
       61 pglfnahvhl afdatremlp nflaseddal ragakdrlgq llrsgvttvr dlgdrdalga
      121 rvraeleaeg aaaprlltag apltvlnghc hffggvvgdd dsvramidan aaagadvikv
      181 masggqiteg gadmwesqfd iralrliveh aaahglpvaa hahgadaiet aveagvatie
      241 hctwmtgpqr qdrrehvakr maaegiaacs tssrnwrtla ermgeelakt vygrlswlee
      301 lgvpllagtd aglpgsvfdd pvgalelyew lgfgrrrile iatedsaagl glgdvtgrla
      361 pglsadvlvv dgdpladlsa lrnlrlilar gvvvsgksr
//
LOCUS       WP_005166814             319 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Amycolatopsis azurea].
ACCESSION   WP_005166814
VERSION     WP_005166814.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis azurea
  ORGANISM  Amycolatopsis azurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 319)
  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 319)
  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   3  (residues 1 to 319)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Amycolatopsis azurea"
                     /db_xref="taxon:36819"
     Protein         1..319
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35967
     Region          194..296
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mtrpfdsshl pdvfrgsvar kaglitasql rgssvrrlfq dvytradvev thelrcrgaa
       61 llappeavlt grsaatvqgv elakphdpve mvvpekqrfg pivgikvrrt eikpeeskpw
      121 ngiriarrtr valdlllrls prksgwvrrl rigvpdldqf mraeklsdll lnrefygrrn
      181 rgirlarhal rlsdpraesp pesevrivla aggitatpqv evfsrtghfi arldlgdkeh
      241 kvaieydgrw hntpeqrahd rrrrrrveae gwrfvivtae dlandfkgiv davwrarrga
      301 ispltaprpg qegvrmarv
//
LOCUS       WP_005168158             314 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Yersinia enterocolitica].
ACCESSION   WP_005168158
VERSION     WP_005168158.1
KEYWORDS    RefSeq.
SOURCE      Yersinia enterocolitica
  ORGANISM  Yersinia enterocolitica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (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   2  (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   3  (residues 1 to 314)
  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   4  (residues 1 to 314)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Yersinia enterocolitica"
                     /db_xref="taxon:630"
     Protein         1..314
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=35153
     Region          1..307
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mihfhqvsky fagkravdnl tlqiakgeft vligtsgsgk sttlkminrl iehdegeihf
       61 ageeirnykp edirrrmgya iqsiglfphw tvernigtvp qllkwpqeri rlrviellel
      121 lhldpeqflh ryphqlsggq qqrvgvaral aadpevllmd epfgaldpvt rsalqfeitr
      181 ihqlsgrtiv lvthdideal aladrivlmd ggrviqqgtp lemltqpang fvrdffgrsd
      241 lgikllslgr aeqrirrget mtgqpilgtt slrealslfv srqtdkllva deqgqplgvl
      301 yfadliadvd rgev
//
LOCUS       WP_005168633             262 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: hydroxypyruvate isomerase family protein
            [Acinetobacter].
ACCESSION   WP_005168633
VERSION     WP_005168633.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 262)
  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 262)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..262
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29603
     Region          1..257
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 miklavnlsm iftevplier falaraqgfn hveiqfpyel tigqiqnqls ihqlnlclin
       61 vpagdlmqgg hglagipgre iefrhaveqa iqyatalnvp rvnilagkqp ldcdllpcln
      121 tlasnlkmac smllehqiep vfemvngtdm prfliqnvaq aqemleavnh palkmqydcy
      181 hmammgedvl eslkenihli ghiqfadcpg rhqpntasiq yhdifqwlkh sqyqayvaae
      241 ykpmqhsnds fvwkaeffpe hd
//
LOCUS       WP_005168824             153 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acinetobacter pseudolwoffii].
ACCESSION   WP_005168824
VERSION     WP_005168824.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter pseudolwoffii
  ORGANISM  Acinetobacter pseudolwoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Acinetobacter pseudolwoffii"
                     /db_xref="taxon:2053287"
     Protein         1..153
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=16454
     Region          1..134
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mvkkysygft lielmivvav igilaaiayp syqdsvrkan ridaqssmmd iatklqkyki
       61 arfsfekadg tfvtladigv tnqipstgta lytialsnqg lgtwtltatp tgmqstdgyl
      121 vlnhrgqrcw tkgsdknggt vcvpsatsnw dgr
//
LOCUS       WP_005169217             272 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Gordonia aichiensis].
ACCESSION   WP_005169217
VERSION     WP_005169217.1
KEYWORDS    RefSeq.
SOURCE      Gordonia aichiensis
  ORGANISM  Gordonia aichiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Gordonia aichiensis"
                     /db_xref="taxon:36820"
     Protein         1..272
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29840
     Region          28..116
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          <95..269
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          185..265
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mpargehhtg gpdtrgvlyp arlptfdria apddlapiva wfwipqwnla pgrtsrqnil
       61 pfpacnlvve pdgvtivgpt mrcshrdltg tgwavgallr pagaaaldis prelrddarq
      121 yhatelfesi saamsvespa iaeaasrfss wlrerttrap dsallanemv dliaadrsii
      181 rvddlarrls msvrsvqrla dryiglspla virryrlqea aerlraepei tiaevaadla
      241 ytdqahfsad frhtlglppg eyrrsvekav ds
//
LOCUS       WP_005169604             401 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Gordonia aichiensis].
ACCESSION   WP_005169604
VERSION     WP_005169604.1
KEYWORDS    RefSeq.
SOURCE      Gordonia aichiensis
  ORGANISM  Gordonia aichiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 401)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Gordonia aichiensis"
                     /db_xref="taxon:36820"
     Protein         1..401
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=42912
     Region          173..398
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 merasddegs galpdvvvst ladpqrraca vyghrktvaa algvvaevve algpgvlsdq
       61 raplewvlwi pqdverilav ldrglaasas vidatrvfvd faygvsgdvs atsedrgtda
      121 gavvrsadaa lslaletqrr maiaqtdtya rleesldlav rlttssgmdf qqfyqpivrm
      181 adgvtvgfes llrwitadgv llpgdflava ehtstivpig rngvtqavra lrdsiepryg
      241 pdafvsinls rqqlvddtiv dhvvaeidry gvgpgqiwie vqenevigfd tdaqraverl
      301 hdsgctisid dlgsgfsalr yvrdlpvdvl kvdralisam pdspsdravv raicemaqtm
      361 diatvaegve lsidfsgvee lgfqyaqgiy fgapapfapr d
//
LOCUS       WP_005171525             344 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Gordonia aichiensis].
ACCESSION   WP_005171525
VERSION     WP_005171525.1
KEYWORDS    RefSeq.
SOURCE      Gordonia aichiensis
  ORGANISM  Gordonia aichiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 344)
  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 344)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 344)
  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   4  (residues 1 to 344)
  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 344)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Gordonia aichiensis"
                     /db_xref="taxon:36820"
     Protein         1..344
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38120
     Region          98..332
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          253..332
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mtdpddlpgs ldqqrvhdwh hrlgttnqlg snrsrrlhrq grsgadnymp tftldadgdp
       61 adfdeylfwr plslvvtyvl lrtpatmsrt sariaerhsp yvlfgttdal vhghviaggr
      121 ehsyarsnpl aalsmsqpfa vtndsvaefs svwvpaemvd addlagsdpv iadsplsrat
      181 avflrnfahd vavrgadvdv dtemaaidll rstlnphrar tisaldspti lrervsevid
      241 rnyrdpafda dtlaamlhls rrqlyrrlsd fdespaemia qrrldkahel lsctgtfglk
      301 avarasgfss vatlrnrfaa rygmtpvefr hqtgfrhqad sddn
//
LOCUS       WP_005171741             436 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Acinetobacter pseudolwoffii].
ACCESSION   WP_005171741
VERSION     WP_005171741.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter pseudolwoffii
  ORGANISM  Acinetobacter pseudolwoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Acinetobacter pseudolwoffii"
                     /db_xref="taxon:2053287"
     Protein         1..436
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=49077
     Region          10..421
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mieiynnsie qcvlaalmtv qnsletvmnd ldencfyasr hqeiykaitd lanenkpydv
       61 vfveqklnek sslvgitpae ylmtlmsdap ssfynlesyv aelnklkahr evekmgrsiq
      121 evardltvpd vhnaaeniln kattneklek ssftfeealk ragdqliqka eakankqytg
      181 vkfnlphldn vvgtiqsghf cviggrpgsg kstlaqmvai qtamqfkeav lvvsaemdve
      241 tftnrcisal tqipydnihn aelfdgmmkd fayaqdrfse lpihiedkqk ptiaeihsya
      301 rkakrnykkl gciiidylql vrdptkkdry qevssisrdl kamakefdcp vialaqlnre
      361 sekgkrpkas dlkesgqieq dadqillvhp imnsddemps giteiiiakn rhgkkglvrv
      421 mdrldicrfa svrlee
//
LOCUS       WP_005174191             496 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Yersinia enterocolitica].
ACCESSION   WP_005174191
VERSION     WP_005174191.1
KEYWORDS    RefSeq.
SOURCE      Yersinia enterocolitica
  ORGANISM  Yersinia enterocolitica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Yersinia enterocolitica"
                     /db_xref="taxon:630"
     Protein         1..496
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=53995
     Region          1..496
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mqsiikihpl dnvavalqdl aaddvleige fsvklaqpva rghkfaltai apgqmivkyg
       61 lpighaltli qpgehihsqn aktnlsdlde yqyqpefsel ppqmadrevq iyrrangdva
      121 vrnelwiipt vgcvngiarq iqqrflketq daegidgvyl fshpfgcsql gqdhentrtm
      181 lqnmvrhpna gavlviglgc ennqvdvfqt tlgpvdedrv hfmvcqqqdd eveaglehlh
      241 alyqvmrhdq rvagklselk fglecggsdg lsgitanpll grfsdyvian ggtsvltevp
      301 emfgaerilm srcrdeatfe ktvsmvndfk qyfiahnqpi yenpspgnka ggittleeks
      361 lgctqkagqs kvvdvlkyge rlqhpglnll sapgndavat salagagchm vlfstgrgtp
      421 yggfvptvkl atnselaakk phwidfdagk lihgtsmddl ltefvdlivd iangkparne
      481 vndfrelaif ksgvtl
//
LOCUS       WP_005174073             297 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Yersinia enterocolitica].
ACCESSION   WP_005174073
VERSION     WP_005174073.1
KEYWORDS    RefSeq.
SOURCE      Yersinia enterocolitica
  ORGANISM  Yersinia enterocolitica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 297)
  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 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   3  (residues 1 to 297)
  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   4  (residues 1 to 297)
  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 297)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Yersinia enterocolitica"
                     /db_xref="taxon:630"
     Protein         1..297
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32791
     Region          29..180
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          208..289
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mvevtdiqaq magmiaglaq gngltpstvp kvkilystvh qprtpvmytp svviifqghk
       61 vgylgskvfq ydptnylilt vplpfecetf aspevplagi sihidsqmlq dliidigdde
      121 ldkpfgntsg vnssalteem lcaterlldv msnprdarvl gpqivreiiy yvlcgqcgga
      181 lqalvnrhgh fnqitktlrr ienqfadnln veqlaadvnm svsafhhnfk avtntsplqy
      241 lksyrlhrar mmilhdglka staankvgye sasqfsrefk ryfgltpsee vaklrtn
//
LOCUS       WP_005174261              82 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Gordonia aichiensis].
ACCESSION   WP_005174261
VERSION     WP_005174261.1
KEYWORDS    RefSeq.
SOURCE      Gordonia aichiensis
  ORGANISM  Gordonia aichiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 82)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 82)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 82)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 82)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Gordonia aichiensis"
                     /db_xref="taxon:36820"
     Protein         1..82
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8353
     Region          10..82
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mtltvrffaa araaagtdts vvdvpndatl gdlehtlaas hpelvqvlar csylrdaval
       61 cdraaplgdc ttidvlppfa gg
//
LOCUS       WP_005174534             206 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Gordonia aichiensis].
ACCESSION   WP_005174534
VERSION     WP_005174534.1
KEYWORDS    RefSeq.
SOURCE      Gordonia aichiensis
  ORGANISM  Gordonia aichiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Gordonia aichiensis"
                     /db_xref="taxon:36820"
     Protein         1..206
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22235
     Region          17..201
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mtdllpldpd elltttrsvr krldlqrpvp ievvrealev atqaptgsna qgwhwivitd
       61 adlkrqvady yarsfaaysa qrtvstetar rvaasaqyla dvmgdvpvlv lgaiktggdl
      121 pegnqagvwg sllpgawslm lalrarglgs awttlhltye qevaellgip dgvhqgvllp
      181 vaytqgtdfs paqrkplddi lhvngw
//
LOCUS       WP_005176154             187 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Gordonia aichiensis].
ACCESSION   WP_005176154
VERSION     WP_005176154.1
KEYWORDS    RefSeq.
SOURCE      Gordonia aichiensis
  ORGANISM  Gordonia aichiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Gordonia aichiensis"
                     /db_xref="taxon:36820"
     Protein         1..187
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19622
     Region          <74..175
                     /region_name="COG4322"
                     /note="Uncharacterized protein, contains DUF2272 domain
                     [Function unknown]"
                     /db_xref="CDD:443463"
ORIGIN      
        1 mvvviaagcv aglravsghd dalsrvaaka gvgsfrpgfp aletaglspt rarivdvvra
       61 eyernapgtv ysggvdeswc adfvstvmrk agvsfdnpns gswripgvat ltdylhssgr
      121 wraasrvpep gdivlydkpn hfrqhtnivv ardgdtvttv ggaesqgitl dhfdvrtvqg
      181 vqgygvp
//
LOCUS       WP_005178043             366 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Gordonia
            aichiensis].
ACCESSION   WP_005178043
VERSION     WP_005178043.1
KEYWORDS    RefSeq.
SOURCE      Gordonia aichiensis
  ORGANISM  Gordonia aichiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Gordonia aichiensis"
                     /db_xref="taxon:36820"
     Protein         1..366
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38344
     Region          21..353
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msgpdtrglr asirsatpfl eidldvpagt tcailgpngs gksttlaala glqrtegsti
       61 gyagrslqna ttfvpphrrs vvllaqqprl fphlsvarnv afgpesaglp rrevaerter
      121 wlaavgvtef gdrmpkqlsg gqaqrvaiar alaaepdvll ldepfaaldv dvaqqmrtlm
      181 rslisersgc tvlvthdlvd avaladdvav iehgrvvgrg ptrevlrrpg tafaaalagl
      241 nmfvgsfepp atvigvdggr vtgvsadvrr pdaaavatfs pravalylda pqgsprtvlg
      301 gmvaevmpqg dhaivrcdvs gqvisaevtw ravedlalha grdvhlvika nevrvyeatp
      361 sldapd
//
LOCUS       WP_005179119             270 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Gordonia aichiensis].
ACCESSION   WP_005179119
VERSION     WP_005179119.1
KEYWORDS    RefSeq.
SOURCE      Gordonia aichiensis
  ORGANISM  Gordonia aichiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 270)
  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 270)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Gordonia aichiensis"
                     /db_xref="taxon:36820"
     Protein         1..270
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28691
     Region          5..263
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mdtrrltvnc silftelpll rrpqaardag fdavefwwpf gaavpsdsdv aafiaavqda
       61 gvrlthlnfa agdlsagerg llshpdtsge frdsvevavg igqrlgtvgf nalygnrvdg
      121 ldsarqdaia tenlafaara aatigadili eplsaipdyp lrsaddaiav ahrvlgdhgi
      181 dnvllladly hlavngedld ralaqhadri ghvqladapg rgepgtgtid lgrhlhtldd
      241 agytgwlsle yrrtlpdpfg wlagfaiepr
//
LOCUS       WP_005180475             189 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: pilin [Acinetobacter].
ACCESSION   WP_005180475
VERSION     WP_005180475.1
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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..189
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=19472
     Region          1..147
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mktvqkgftl ielmivvaii gilaavalpa yqdytvrakv seailagsac rtavteaiqn
       61 givptkgnwg ceqgtpesaa dagdakrask mvamvdvnsd alpgqititl eklpelkaas
      121 etviqmtplv dtntalkatc tgegdtrkcd fssaasagis ewscgpqasd agtptkylpa
      181 tcrtvqsfs
//
LOCUS       WP_005179435             117 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: endonuclease domain-containing protein
            [Acinetobacter].
ACCESSION   WP_005179435
VERSION     WP_005179435.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 117)
  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 117)
  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   3  (residues 1 to 117)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..117
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=13374
     Region          15..115
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mkpynknlkq asrdlrnnmt eaekllwsrl rnkqilglsf yrqkpilnyi vdfycpavnl
       61 viecdgsqhf tdegleadri rdealaqlgl kvlrfdnsqv mariddvvna iisicns
//
LOCUS       WP_005182061             335 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005182061
VERSION     WP_005182061.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 335)
  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 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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 335)
  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   5  (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   6  (residues 1 to 335)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38345
     Region          22..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <137..335
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mgqltdasvv lrlgyqairr aglpteeilt kagvalnqve andrtplgaq yafwvaaeev
       61 srdpdiglhl gehlplyrgq viehlfisse nfgeglkral ayqrlisdaf daklvieddr
      121 cyltngqqpw adnivnrhfs ecamsgilrf fkfitegkfq plyidfnfqq gaaddeyfrv
      181 yecpvslgqn etrlyfdpsi leyplwqaep ellqlheqla leklqelary dlvgevrrai
      241 gstlesgett letvaaqlni tprrlrtqls eantsfqqil sdyrcrlakk llantnesve
      301 rivyltgfse pstfyrafkr wtnetpveyr krkqr
//
LOCUS       WP_005183877             400 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase family protein [Acinetobacter].
ACCESSION   WP_005183877
VERSION     WP_005183877.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 400)
  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 11465564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..400
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=42573
     Region          <131..179
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          269..396
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mfvrsllams lscilanvay aaptteqpln pkkisaavqd pidplavdra tsnvaaqpas
       61 svaataasep qvntgaasvv sqqlentpda kttttapavp aswtmdaina aewpeglpkg
      121 qnpayarahv mlnnshaspg aidgsngknt lkaiasfqqm ngltptgqlt ketwdalvak
      181 qtkpayveyt itdadlkgpy adaipsdyal qakmkglyyt rvtemlgekf hmderflkql
      241 npnanfkkag ekiivanvrn dlpedihliv ahkgarqlyl fnsrnqmias fpatigstdt
      301 psptgtykvv gvaknpyysy spsnfvqgkn lkpltlppgp napvgniwig lskksfgihg
      361 tpnpsliskt ashgcirltn wdandlgakv rsgvtvkfle
//
LOCUS       WP_005182211             147 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Yersinia].
ACCESSION   WP_005182211
VERSION     WP_005182211.1
KEYWORDS    RefSeq.
SOURCE      Yersinia
  ORGANISM  Yersinia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae.
REFERENCE   1  (residues 1 to 147)
  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   2  (residues 1 to 147)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Yersinia"
                     /db_xref="taxon:629"
     Protein         1..147
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15290
     Region          82..141
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkfigklfvi talfaglsiq qiafaapgsp tsntqdktln srshtpinsq vkagsppakv
       61 aeknqgqvst aaataagtpt gsasqinins ataeqlaqfl sgigrkkaea ivsyreqfgp
      121 ftdteqllev pgigpsfler nntklkm
//
LOCUS       WP_005185004             159 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Acinetobacter dispersus].
ACCESSION   WP_005185004
VERSION     WP_005185004.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter dispersus
  ORGANISM  Acinetobacter dispersus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Acinetobacter dispersus"
                     /db_xref="taxon:70348"
     Protein         1..159
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17438
     Region          10..159
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 maeelvlqqg hkaeqyqsii pqiqaivede sdvianlani caalkqqfgw lwigfylvkd
       61 delvlgpfqg piactriakg rgvcgaawqq qqvivvpdvd qfpghiacss asrseivlpi
      121 mkagecvgvl didsdelnqf dqidaeylqe lmliiekli
//
LOCUS       WP_005185056             391 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Acinetobacter].
ACCESSION   WP_005185056
VERSION     WP_005185056.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            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="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42330
     Region          5..388
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 maisvlvinc gsssikyali serredriyg laenlgaada rikgitlgge plelsipyad
       61 hakaletlla rlanynpqai ghrvvhggdi tkaelltpel verieaatpl aplhnpahli
      121 gieatlrlfp qlpqvavfdt afhqtmpera yryalpqyly tehqvrrygf hgtshayvte
      181 raselaghkn eggwlsahlg ngsstcavwn ghsvdtsmgm tplegvvmgt rsgdvdpslh
      241 lflasnlgwd iqkidsmlnk esgllglsgl sndmrtlvea senghegatl aievfcyrla
      301 kslsalscgl prldglvftg gigensayvr ektlgylahf gfqfskeknn alprgtegri
      361 dngagpqiwv iptdeegria ketrqvleht i
//
LOCUS       WP_005185686             335 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter dispersus].
ACCESSION   WP_005185686
VERSION     WP_005185686.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter dispersus
  ORGANISM  Acinetobacter dispersus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 335)
  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 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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 335)
  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   5  (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   6  (residues 1 to 335)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter dispersus"
                     /db_xref="taxon:70348"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38704
     Region          51..193
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          82..330
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msqlknytgs vfgglghllk ayceaeniyi peqlqqvqnl erfdyviwrd lledlnrlhp
       61 ksglgleiaa yvqpkhlgii aylalscenl gealaryhdf hrliydgspl vvefnppyas
      121 irweapephp tqltdeiaia lmvqflklfm sgdtihlhev hfvnaapkni siyeqyfhck
      181 vrfeqpktql llpvseafkp lrtgdhtlqq lllqqaqall dklpnstqld qrlqhailtg
      241 lqknqyqidf iaeklglsvr qlqrhlqqqn ttfqervqqv rfmlateylk dphlslqeia
      301 lllcyseqsa fqrafkiwtg qtpqqwrnnn ityns
//
LOCUS       WP_005185471             184 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acinetobacter dispersus].
ACCESSION   WP_005185471
VERSION     WP_005185471.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter dispersus
  ORGANISM  Acinetobacter dispersus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Acinetobacter dispersus"
                     /db_xref="taxon:70348"
     Protein         1..184
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=20255
     Region          1..122
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkknhgftlv elmivmvima ifaaiaipgy kqfmqrkdfe aakqealrvs selerfkgkn
       61 fsykgfdasf vypdynsttg elflpvgsts tnakyiltlv dsgaskkplt ilssggketa
      121 dsqavrglgw amkvervqna ggepkdpanf dllllsgglk cmtitknrfd qyecnptwad
      181 vetw
//
LOCUS       WP_005185693             626 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Acinetobacter dispersus].
ACCESSION   WP_005185693
VERSION     WP_005185693.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter dispersus
  ORGANISM  Acinetobacter dispersus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 626)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 626)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 626)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 626)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Acinetobacter dispersus"
                     /db_xref="taxon:70348"
     Protein         1..626
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=69491
     Region          2..626
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mqstakkaal pamtlaalgv vfgdigtspl yairqcfvtg hvdisegsil gilslifwcm
       61 nltisfkyvs mimradnnge ggimsllaln lrssvfsnkn kiflialgfi gaslffgdgi
      121 itpaisvlsa ieglslvtpa ldrwlvpial giltalfmvq rhgtatmgkf fgpitllwfa
      181 sigliglwsi iqtpyvlmmi npywafhfvf dqptvafitm gaviltmtgg ealyadmghf
      241 grvpiklawf lvvlpcllln yagqgalllr dakaienpfy llvpdwalfp miglataaav
      301 iasqavitgv fsmanqaiql rylprltvhh tsdveqgqiy lpfinwvlfi svvilillfe
      361 ssaelasayg vavtmtmlcg tilistlayg vwrwplwkva ifavpfliid lifvgstslk
      421 ilsggwvpil igvvvytilm twkrgreivy nrmetnalpi elfiksigms kethfvpgea
      481 ifltgtpniv phamlhnikh nkvlhernvm vtvytqdipy vaeadrlkve kldehfyriy
      541 myygfkdqpn vpnaleqayk klgfefdmmq msffisrdri vhtvgdgmsp wreklfismq
      601 rntspvsdfy qiptnrvvel gsqiei
//
LOCUS       WP_005188328             341 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter dispersus].
ACCESSION   WP_005188328
VERSION     WP_005188328.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter dispersus
  ORGANISM  Acinetobacter dispersus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 341)
  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 341)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Acinetobacter dispersus"
                     /db_xref="taxon:70348"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38941
     Region          30..211
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          257..332
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mnylwsyqrs ihsvrlmadf aaelgvshvq ilkgtgleqq qlldpnmlvt gqqefqlirn
       61 lvetfsqrps lglevgqryh fttfgslglg lissanirea lnfalayfpl sfafsqfvvs
      121 elpetdniri dievdegipq ilrqfiierd iaalisvqhd lipenlcqkv vfgfqscgeq
      181 qpyhelfgva pefggsksfi ilnaekidqk lsmanelmlh saeqqcreil dkrqsqkkya
      241 dqvqhilmns kgkipameev adrlylnsrt lrrylaqeqt tfikireear kmmansylss
      301 tqtsieqise wlgyaepasf ihaykrwygk tpyasriknk v
//
LOCUS       WP_005189070             196 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Acinetobacter].
ACCESSION   WP_005189070
VERSION     WP_005189070.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 196)
  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 196)
  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   3  (residues 1 to 196)
  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   4  (residues 1 to 196)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 196)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..196
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22359
     Region          1..191
                     /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"
ORIGIN      
        1 mpklkialid ddqaraeyik tcliehdfdv vacftldhln ifklehlqad villdmdhph
       61 rdviescvsn fdlptvlftk ntdkdtikqa idagitayiv dgidpsrlht ildisieqyk
      121 khkklecdlk daktkladrk dvekakvllm qlhgltedta fqllrknams hrmtigemar
      181 rlldaqqlln nqlkde
//
LOCUS       WP_005190499             830 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Acinetobacter dispersus].
ACCESSION   WP_005190499
VERSION     WP_005190499.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter dispersus
  ORGANISM  Acinetobacter dispersus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 830)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 830)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 830)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..830
                     /organism="Acinetobacter dispersus"
                     /db_xref="taxon:70348"
     Protein         1..830
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=92664
     Region          62..112
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          132..830
                     /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 mkdyqakttl alavrailwg mplsvvsiat tsayaanvyq isissttldq alkqlaiqtg
       61 ttisydsttl skiksaslkg nysvetalet llkphafeai kvpnagysiq akatvaavep
      121 kvvkleaiht radqtrngnt qqannstqlp tisikaasqn mtnvgkqaqn ikdvpqsvtv
      181 msrqrideqg lktlddvlvq ttgvtreqlw lnnnysargl kienirydgg stssledrsn
      241 sadmaqydav evlrgadglf gageaggvin ltskrpkaet eingsisags wnnyrgefda
      301 tgsltqdqsv kgrlvtvfqd rdffykptqs rremvygals fdllpettlf tgvsyqkdkv
      361 dafnaslprw edgadlhfsr stttgapwgw ierkntsffa nlqhqinddw ktqlnvrhni
      421 gndainsaem egavsyethq sqwwryqddt rfkettmdln lqgsfnlfeq khdlilgidh
      481 snnqkdyrqn wtyyangdaf nrvappewey paaiwdtntt hknnksalyg slklrpvddl
      541 aliiggrytf kdeltinnhn snientyted kkfvpyygit ydilpsttay asfaeiyknq
      601 rnyltaadgp glepltgrni efgikhqina nllasiayfd ikkekekvyn tytsipnsns
      661 lccyigtgsm eskgvdveln gnispdwnls vgytynknek kdntenpynt ytpknllkiw
      721 ttyqldqivd gleigggvia qsknyatgsv kefnpvtqkf dgarknielv qpnyaiwsar
      781 vaydinpqwn ialnlnnifd ktyystignp gygnfygepr nvlltlkasy
//
LOCUS       WP_005190890             245 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Gordonia amarae].
ACCESSION   WP_005190890
VERSION     WP_005190890.1
KEYWORDS    RefSeq.
SOURCE      Gordonia amarae
  ORGANISM  Gordonia amarae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 245)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Gordonia amarae"
                     /db_xref="taxon:36821"
     Protein         1..245
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=26212
     Region          3..>219
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 msttftydsa ylagtagdle pglpvsagqq yvdglpgafa dsspdrwgrn lidkrrraaq
       61 reasqrlpaa taidylvgvs ditrqgdlrf adrrdpksfl apghdvpklv slpellnaad
      121 nvsrsdalav gdldavksll dagsgslgga rpkasvradd grlliakfph pgdewdvmaw
      181 ekttldlaea agitaprrrl trvgtrnvll verfdrsgsf rvgyirvrsn csqmpsrtds
      241 lssgs
//
LOCUS       WP_005191907             206 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Yersinia intermedia].
ACCESSION   WP_005191907
VERSION     WP_005191907.1
KEYWORDS    RefSeq.
SOURCE      Yersinia intermedia
  ORGANISM  Yersinia intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 206)
  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 206)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 206)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Yersinia intermedia"
                     /db_xref="taxon:631"
     Protein         1..206
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22053
     Region          1..204
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 mevyttendq vdavrrffse ngkalavgvv lgigalvgwr ywqshqntvl teassayqqa
       61 snalsansad gvafaekfvq gnnnnygvla glelahhfve qnvfdkaaqq ltqalgqtkd
      121 enllslinlr larlqlqlkk pddalktlda vqgdgwtama qdvrgdalls kgdtagaraa
      181 yskgvesnas qalqallrmk lnnlss
//
LOCUS       WP_005192014             255 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Gordonia amarae].
ACCESSION   WP_005192014
VERSION     WP_005192014.1
KEYWORDS    RefSeq.
SOURCE      Gordonia amarae
  ORGANISM  Gordonia amarae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 255)
  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   2  (residues 1 to 255)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Gordonia amarae"
                     /db_xref="taxon:36821"
     Protein         1..255
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=27073
     Region          162..224
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mssttdprwv dpsaaarlad rkwrwknsiw vfapalclgf vscagfiyaa nkvhnrkwtv
       61 yavistvvtl avclcafife tddhkvadwa inlvlvswil hliagislrn nylrllaqrq
      121 aqdelapfgi pplapaptyp ppptpaapap vqglvgmndf yaptpaqldi nsasaaelsa
      181 ttglgpaqad aviaartrvg gfrsfeeiaa saglaphhla rlrevsfgps qpdpgsaphn
      241 ppppppvpgg rildi
//
LOCUS       WP_005193190             232 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Acinetobacter].
ACCESSION   WP_005193190
VERSION     WP_005193190.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 232)
  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 232)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 232)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..232
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=25613
     Region          3..210
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 mslsdeeqld slksfakkyg samisgilia liaffgweyw qkknlaeaqn qtakvqklmd
       61 eakaasgqpn afaslsetad kivkddadsa qaiqtqfima klaydkqdya aaekalkkve
      121 nakvkdagll qivkirladt qlaqskydea lktlstvtdp afkataeelr gdifvakkdn
      181 asarkayqsa wdnllerkqe rqllqikles vgvlvddpdf erpildtkvd es
//
LOCUS       WP_005193820             159 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acinetobacter sp. NIPH 298].
ACCESSION   WP_005193820
VERSION     WP_005193820.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. NIPH 298
  ORGANISM  Acinetobacter sp. NIPH 298
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Acinetobacter sp. NIPH 298"
                     /db_xref="taxon:1217692"
     Protein         1..159
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=17420
     Region          1..110
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkamnkqsaf tlievmvtva iiailaaiai pgydiyirra dlstaqqemh kvaallekhr
       61 trnfsydgfv lkgtstnkgp yfdvpnatnt tllipldttt gkqkftliln lnsqawslka
      121 esqsprnysl lltstgikck tkttanitnq scgtesedw
//
LOCUS       WP_005193614             391 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Acinetobacter sp. NIPH 298].
ACCESSION   WP_005193614
VERSION     WP_005193614.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. NIPH 298
  ORGANISM  Acinetobacter sp. NIPH 298
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Acinetobacter sp. NIPH 298"
                     /db_xref="taxon:1217692"
     Protein         1..391
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42368
     Region          5..388
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 maisvlvinc gsssikyali serredriyg laenlgaada rikgitlgge alelsipyad
       61 hakaletlla rlsnynpqai ghrvvhggnm thaeqltqqt idrirdaipl aplhnpanli
      121 gieatmalfp qlpqvavfdt afhqtmpera yryalpqfly dqhqvrrygf hgtshayvte
      181 raselagqkn qggwlsahlg ngsstcavwn gqsldtsmgm tplegvvmgt rsgdvdpslp
      241 lflsnnlgwd iqkidsmlnk dsgllglsgl sndmrtlvea senghegail aievfcyrla
      301 kslsalscal prldgliftg gigenstdvr ektlaylshf glqfsqeknn slargsegri
      361 dqgtgpqiwv iptdeegria ketrqvleqt v
//
LOCUS       WP_005193307             430 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Gordonia amarae].
ACCESSION   WP_005193307
VERSION     WP_005193307.1
KEYWORDS    RefSeq.
SOURCE      Gordonia amarae
  ORGANISM  Gordonia amarae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 430)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Gordonia amarae"
                     /db_xref="taxon:36821"
     Protein         1..430
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=46130
     Region          190..416
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mrapvrywlm ltdvtysgsg ggggdgdtcs rstlnkvava vtcdpyqrva fthgparals
       61 aaqastraia hdlgsaakft qtgettwryv vdlpddpdeh dallqhlvrl stcgdddpdg
      121 lyldccagfa vgphlpaatt dhdlaeyasa alslclrstd rirfaenesr aevrdgltla
      181 hrlrlssaad fplvyqpivr lsdrqvmgfe allrwrpdqd vltpdhfmee aeasslildi
      241 glmtipviie tfantlaplc asdepfvtin lssrqltdpa lagyigrtld nfsvdpgrlw
      301 ielredaaiq ndsstskvid qlhqlgcris iddlgsgysa lsyirdlpvd vlkidrdlin
      361 qvtcdpvsaa vvdaicqmck avgihivaeg iesedilpvl hgfgigygqg ylfghptaaa
      421 alagrtatag
//
LOCUS       WP_005192738             408 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Gordonia
            amarae].
ACCESSION   WP_005192738
VERSION     WP_005192738.1
KEYWORDS    RefSeq.
SOURCE      Gordonia amarae
  ORGANISM  Gordonia amarae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 408)
  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 408)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Gordonia amarae"
                     /db_xref="taxon:36821"
     Protein         1..408
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44873
     Region          1..407
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mtkdrlsaaq arrialaaqg fvdkrptaap tmahlkrvlg rtgliqmdsv nvavrahylp
       61 lfsrlgpydr qllaraawqp pgkprflaey waheaalipv ddwplmrwrm defaggrwky
      121 trevmarnaa maddvvavid dlgpsmprdi eaalgivrgq gkagswwerg evkhicealf
      181 aagqlsavrd gnfsrfydrt erfigpdvaa iridradaqr vlvaraaasl gvatpadiad
      241 yyrmsradtq raiddaveeg mvrevtvggw dgpaylaada rtpravsvst ilspfdplvf
      301 frpralrlfg fhyrieiytp ahkrvhgyyv hpyllgddia arvdlkadrs agvlrvpaah
      361 lepgrdrdlv aehlatdltt marwlgldgv aiggagdlaa rlsraigt
//
LOCUS       WP_005177303             304 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Gordonia aichiensis].
ACCESSION   WP_005177303
VERSION     WP_005177303.1
KEYWORDS    RefSeq.
SOURCE      Gordonia aichiensis
  ORGANISM  Gordonia aichiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Gordonia aichiensis"
                     /db_xref="taxon:36820"
     Protein         1..304
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33174
     Region          17..290
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 msrrirvdlh aphtrydeva dasaalvins ysssfglasr llaesvrvhv rniyalvrva
       61 deivdaprpg qgpderrial drlesdtdda ldsgsstnlv vhafarsars tgidrsltap
      121 ffssmrmdlt rsahdeasla eyiygsaevv glmclrafva depraheryd elspgarhlg
      181 aafqkvnflr dfatdsgdlg rryligldpa hpaeeawtrw ldeidadlav aadtiprlpr
      241 nsrvavcvah dlfaelnarl rdppasmaar qrvrvstpvk triaaaailr rgqprarasa
      301 avva
//
LOCUS       WP_005193828             143 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acinetobacter sp. NIPH 298].
ACCESSION   WP_005193828
VERSION     WP_005193828.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. NIPH 298
  ORGANISM  Acinetobacter sp. NIPH 298
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Acinetobacter sp. NIPH 298"
                     /db_xref="taxon:1217692"
     Protein         1..143
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15583
     Region          4..125
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 myykkkgftl ielmivvaiv ailaaiayps yqdyvkrtkr adaqaemmdi ahrlsqykvv
       61 nrnyssatin giygtnvipk sgvalydldl ivtastwtlt alpivtsaqk ddgililnse
      121 gqkcwvkgas icalsatsnw dgr
//
LOCUS       WP_005193830             176 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acinetobacter sp. NIPH 298].
ACCESSION   WP_005193830
VERSION     WP_005193830.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. NIPH 298
  ORGANISM  Acinetobacter sp. NIPH 298
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Acinetobacter sp. NIPH 298"
                     /db_xref="taxon:1217692"
     Protein         1..176
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=19554
     Region          3..>103
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 minrgftlie lmivvmlvai iaaiaipsye hftrraiaaq aqqemhklae qlerhksrnf
       61 tyrgfnpryl yptppsprid sfdetkqelt lplesanpky tltivdgsvg nplltssdai
      121 gqrwaikais ndvrnssfll tstgvkceti tpvnietdpa kgvgcdykhd deseed
//
LOCUS       WP_005195352             359 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Acinetobacter sp. NIPH 298].
ACCESSION   WP_005195352
VERSION     WP_005195352.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. NIPH 298
  ORGANISM  Acinetobacter sp. NIPH 298
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Acinetobacter sp. NIPH 298"
                     /db_xref="taxon:1217692"
     Protein         1..359
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39601
     Region          <75..>255
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          277..351
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 msmnnkqrwm ggvvllgggv llaalllkgn eeieqdktqt qiehpsaqte skpklaqpaq
       61 dsemvslqpm avdietekrl leeqrqarek avaeqealaa dflkmqqeae aaaarkaaee
      121 yaainarrna aqessdnipp elieddkvka qrlaeekrkl eekrkadadk kaaddkrkad
      181 adkkaaedkr kaeadkkaae dkrkaeadkk aaedkrkaea dkkaaedkrk aeadkkaaed
      241 krkaeadkka adekrkaeed akkkadaeka rellengdkn wmvqvalaan qanadavvsk
      301 lrakgykvtt sptskgirim vgpskdreta daarkkiaad eslnmksawv idwvpleqr
//
LOCUS       WP_005195697             126 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Acinetobacter sp. NIPH
            298].
ACCESSION   WP_005195697
VERSION     WP_005195697.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. NIPH 298
  ORGANISM  Acinetobacter sp. NIPH 298
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 126)
  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 126)
  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   3  (residues 1 to 126)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Acinetobacter sp. NIPH 298"
                     /db_xref="taxon:1217692"
     Protein         1..126
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14498
     Region          15..111
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mkpynknlkq asrnlrssmt daeqllwqri rrkqilglqf yrqkpilnfi vdfycpavnl
       61 viecdggqhy teegleadqn rdqtlselgl lvlrfsnhqi ltethavveq vywsvqqsle
      121 spscgt
//
LOCUS       WP_005196377             387 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Gordonia rubripertincta].
ACCESSION   WP_005196377
VERSION     WP_005196377.1
KEYWORDS    RefSeq.
SOURCE      Gordonia rubripertincta
  ORGANISM  Gordonia rubripertincta
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
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
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 387)
  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   5  (residues 1 to 387)
  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   6  (residues 1 to 387)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 387)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 387)
  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 20324439
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Gordonia rubripertincta"
                     /db_xref="taxon:36822"
     Protein         1..387
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40683
     Region          <31..>83
                     /region_name="COG3355"
                     /note="Predicted transcriptional regulator
                     [Transcription]"
                     /db_xref="CDD:442583"
     Region          84..372
                     /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 mhvstprlel snkpaalvlr aarlagplfr ddaaertgls istvnrqvsa llkaglirer
       61 adlapsgaig rprlpfevnl aefltlgihi gykvtsitth dllhrvvgai qiptpeadtp
      121 eetlaaigvs arrfaerwng krvlwvgval ggrvaeggiv dhprlgwega pvgrviaeav
      181 glpvsvashv eamaaaelvl npddeqssfl yfyaremlgi afsvggtvht ptagppvigh
      241 fptgattlld phrtgrlepa vsdtgiveaa qalelsvtdv eglhglartg dataralfee
      301 raevlgrtvg liadifnpdh iilggqaftd ypttlptvar avretsivak rdvrvshsga
      361 tvqqqaagav sldaiysdpl qaitlta
//
LOCUS       WP_005196871             289 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter sp. NIPH 298].
ACCESSION   WP_005196871
VERSION     WP_005196871.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. NIPH 298
  ORGANISM  Acinetobacter sp. NIPH 298
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 289)
  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 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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Acinetobacter sp. NIPH 298"
                     /db_xref="taxon:1217692"
     Protein         1..289
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32655
     Region          24..175
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          202..284
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mmndqtltal flkivhkegf fttaidgitl mrvdhdtppi avlqeptlvf vlqgqkrgyi
       61 gtetysfqqg eclivsvsmp fdcdtiaspe fpmiaigmkl eadtvnella ktyfenyqfk
      121 plttgmsviq ydqnissvlf rllntltseq dililgdqik rellyrviqh sgadalkglv
      181 aqgnlrpiyk iceyiqhhft ekltvemlae qanmstsafh kafkqvtqhp plqylkvvrl
      241 hkakqllqne nqsvaqaaya vgyqsssqfs refkkqfgfs pnqtelnke
//
LOCUS       WP_005197353             178 aa            linear   BCT 20-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Gordonia
            rubripertincta].
ACCESSION   WP_005197353
VERSION     WP_005197353.1
KEYWORDS    RefSeq.
SOURCE      Gordonia rubripertincta
  ORGANISM  Gordonia rubripertincta
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 178)
  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 178)
  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 11443472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Gordonia rubripertincta"
                     /db_xref="taxon:36822"
     Protein         1..178
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18851
     Region          <57..176
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          127..175
                     /region_name="LysM"
                     /note="LysM domain; pfam01476"
                     /db_xref="CDD:396179"
ORIGIN      
        1 mrtatlidpv rstdpargdv lerprpmrrg dgrrpvdgrp vpesavrvrr vastqcaspv
       61 gmrgrapvvp vsrpaqpaps avirrrrrta tailagvgla lavwviavvg qnyaatvtps
      121 svgtevvhvr sgdslstias rvapemprea vvdeiiqlnd lpssglrvgq pllapryh
//
LOCUS       WP_005197791             736 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Acinetobacter sp. NIPH
            298].
ACCESSION   WP_005197791
VERSION     WP_005197791.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. NIPH 298
  ORGANISM  Acinetobacter sp. NIPH 298
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Acinetobacter sp. NIPH 298"
                     /db_xref="taxon:1217692"
     Protein         1..736
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=80260
     Region          41..736
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mkftsystac lvkfppssls laiatllsgi chsavanevp qaetqtlati siqaqgnwle
       61 eanaekvlqh agarsiidqn rldeiattsi rdalkqipgv qvqdsngtgg sdvslnigvr
      121 gltsrlsprs tvlmdgipla vapygqpqls lapvsmgnie svdvvrgags vrfgpqnvgg
      181 iinfttraip qefsgsvglt tefatgtdql kytpnlflgg tldnglglal lysgtkgdgy
      241 reannnidid dvmlktayqw tdqdqiainl hhyegrgemp egltaekfve npyqsnqsrn
      301 yfagrrsdis vkyshkdeln nfellgyyvd sfrtsdlesi gnkgtstlss sprdykyfgi
      361 eprysrayqw asmdnevtvg yrylqeesse fsgrsqydta tgspgksian ttseggtkah
      421 aiyidnrfgi gdwvitpglr fesidthnnf taysngiptn tinpkiksee flpslsvlyk
      481 anenwnifan agvsfgpqqy nqlvttktvd gkntafstld glhpekskny eigtkylgng
      541 lsaeltifyl dfdkelfler pdtigtgiwt dlgatshkgi etgisydfgq ladaleglka
      601 ygnytftkat seagkfegkd lpyysrhlgn lglafqvdqw sinadmfaqs kqhapgsgdv
      661 yqtqetadgr igdipgystf avragydfsh qlkglkvagg vknvfdkqyf trssdstggk
      721 yvgqprtffl qtsfdf
//
LOCUS       WP_005198564             292 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Gordonia
            rubripertincta].
ACCESSION   WP_005198564
VERSION     WP_005198564.1
KEYWORDS    RefSeq.
SOURCE      Gordonia rubripertincta
  ORGANISM  Gordonia rubripertincta
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Gordonia rubripertincta"
                     /db_xref="taxon:36822"
     Protein         1..292
                     /product="formate/nitrite transporter family protein"
                     /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=31411
     Region          2..265
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msyvnpsefa vkmvdageak vflstrdtii raymagaila laaafavtvt vrtgepllga
       61 llfpvgfcll ylmgfdlltg vftlvplali dkrrgvtvks mlrnwswvfl gnflgaftva
      121 vmmavivtyg fsvdpdeigq qlghigesrt vgyaehgaag mltlfirgvl cnwmvstgvv
      181 gammstslpg kvlamwmpvm vffymgfehs ivnmflfpsg lmlggdfsig dylvwneipt
      241 vignlvgglt lvgltiyith artaadrrpv shdettevdv aapveietvk tv
//
LOCUS       WP_005201123             341 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Gordonia
            rubripertincta].
ACCESSION   WP_005201123
VERSION     WP_005201123.1
KEYWORDS    RefSeq.
SOURCE      Gordonia rubripertincta
  ORGANISM  Gordonia rubripertincta
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 341)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Gordonia rubripertincta"
                     /db_xref="taxon:36822"
     Protein         1..341
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36276
     Region          5..337
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mtpnpvslvd latylpekvv paayyaqyae ddtladnvmf rapafrhhaa egetsadmmi
       61 satrdlferh gddflddvdv vlthsqlpev pvrgcggela hrlgirpstv ldvhnggcaa
      121 fifmieiaga llraggghka llglaqnsag qvftqeqvrg kaqaaipgdg aavavltvdd
      181 vdaspilglr chsfgqysgd mtgvsdpprk yweagsgqmh igftdskiak vlargnrmvp
      241 evaievadei gispadldwf vtnqpsrifl rnwrealelp dshhpdtfde cgnlfavaip
      301 vtldaaisdg rigegdvvmm aafahagdfs gaaamrwagr p
//
LOCUS       WP_005201434             335 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005201434
VERSION     WP_005201434.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 335)
  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 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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 335)
  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   5  (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   6  (residues 1 to 335)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38721
     Region          51..193
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          82..330
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msqlknytgs vfgglghllk ayceaenihi peqlqqvqnl erfdyviwrd lledlnrlhp
       61 ksglgleiaa yvqpkhlgii aylalscenl gealaryhdf hrliydgspl vvefnhpyas
      121 irweapephp tqltdeiaia lmvqflklfm sgdtihlhev hfvntapkni siyeqyfhck
      181 vrfeqpktql llpvseafkp lktgdhtlqq lllqqaqall dklpnstqld qrlqhailtg
      241 lqknqyqidf iaeklglsvr qlqrhlqqqd ttfqervqqv rfmlateylk dphlslqeia
      301 lllcyseqsa fqrafkiwtg qtpqqwrnnn tiyns
//
LOCUS       WP_005201444             626 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Acinetobacter].
ACCESSION   WP_005201444
VERSION     WP_005201444.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 626)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 626)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 626)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 626)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..626
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=69522
     Region          2..626
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mqstakkaal pamtlaalgv vfgdigtspl yairqcfvtg hvdisegsil gilslifwcm
       61 nltisfkyvs mimradnnge ggimsllaln lrssvfsnkn kiflialgfi gaslffgdgi
      121 itpaisvlsa ieglslvtpa ldrwlvpial giltalfmvq rhgtatmgkf fgpitllwfa
      181 sigliglwsi iqtpyvlmmv npywafhfvf dqptvafitm gaviltmtgg ealyadmghf
      241 grvpiklawf lvvlpcllln yagqgalllr dakaienpfy llvpdwalfp miglataaav
      301 iasqavitgv fsmanqaiql rylprltvhh tsdveqgqiy lpfinwvlfi svvilillfe
      361 ssaelasayg vavtmtmlcg tilistlayg vwrwplwkva lfavpfliid lifvgstslk
      421 ilsggwvpil igvvvytilm twkrgreivy nrmetnalpi elfiksigms kethfvpgea
      481 ifltgtpniv phamlhnikh nkvlhernvm vtvytqdipy vadedrlkve kldehfyriy
      541 myygfkdqpn vpnaleqayk elgfefdmmq msffisrdri vhtvgdgmsp wreklfismq
      601 rntspvsdfy qiptnrvvel gsqiei
//
LOCUS       WP_005201460             650 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase [Acinetobacter].
ACCESSION   WP_005201460
VERSION     WP_005201460.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 650)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..650
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..650
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=74905
     Region          31..>415
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mttenntldl peenpqegvf kfepikgypm lnwkgkrpft stryypaqlk eqhgeavngw
       61 lnkifwgdnl qvmshllref rgkvdliyid ppfdskadyk kkvslragsv endqtafeek
      121 qytdiwandd ylqfiferic llrellsnkg vlfvhcdwrk nfhirailee vfgsqnyrne
      181 iiwvrstnpk gsqyvsskfd vftdtihfvt ktdeynfnid dikvpltpee ieekyyrtde
      241 rgryydgpie rsismgarpn svyeykgytp siagwrltke klidldskgn lgwtsnnkpf
      301 rklrpeddkg kpignfwndi sllnsqsaer vgyptqkpek lleriiract npndlifdcf
      361 mgsgttqava mklgrkfiga dinlgaiqtt tkrlikvaee lgntqpelgd eqvlysgfev
      421 ynvnhydvfr npvqakelli qaldiqpipn svydgekdgr mvklmpvnhi atrqdvneli
      481 hgvdykafek rkeekpnqpv ekitifcmgh epdlaafvqq sigykldiev vdilrdrsdl
      541 qfkrdsealf kveggnlvvd kfypmnllqk lsqtkesvsd wremvesimi dwnydgavfq
      601 ptltdipaqn elvqgqyaip edagtiriki tdllsesler dlteeelang
//
LOCUS       WP_005201789             344 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-oxoacyl-ACP synthase III family protein [Gordonia].
ACCESSION   WP_005201789
VERSION     WP_005201789.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 344)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..344
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36455
     Region          9..340
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mnnptapavv ladvagylpe nrvpasyfsq faenddladn imfsapafrh haaegetsad
       61 mmlsaartlt erhgddyldd vtvvlthsql pevpvrgcgg eladrlglrp ttvldvhngg
      121 ctafihmidl aaallaaagg gkallglaqn sasqiftqeq vrgkaqaaip gdgaaaavvs
      181 lddpagspvl glvthsygey sadmtsvaep drryweagtg eihigfteak itkvlargnr
      241 mvpaaaieva dsidirpsel dwfitnqpnr iflrnwreal elpaerhpdt fdecgnlfgv
      301 glpitldtav sdgriqpgdv vmmsafahag dfagaaairw sdrh
//
LOCUS       WP_005202311             719 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor family protein
            [Acinetobacter].
ACCESSION   WP_005202311
VERSION     WP_005202311.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 719)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..719
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..719
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=78673
     Region          31..719
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mtcsisapld fskfkpstls caitaliscv atttfaddsq snttqtlati siqaegnwle
       61 qanakkvlnh pgartvvdqq sleargttsv kealrtvpgv qvsensgtsg sdaslsigvr
      121 gltsrfsprs qlmidgvpla vapygqpqls lapttlgnme sidvvrgags vrfgpqnvgg
      181 iinfntrsip enfaasvgmt tevaengnlk vnpnlfvgtt ldnglglall ysgvngdgyr
      241 dqndysnind lrlkasyald dyssieanlh ryeakvdmpg gltpaqyaqn pyqslrnhdy
      301 megnrndisl kynykkdnna fevlayhlds yrdagversg sslyqiaprd ykvtaiepry
      361 shafqlgdtl nevsvgyryl ketssesver adynsdtgps dfygwtkadg dteahavyvd
      421 nrtdlgawsf tpgirferik tnenmyklnr dysvlngvna sksydavlps favmykandq
      481 wnifanygks faplqysqma ntnargaylt mdglnpekad nyeigthyld dylsleftlf
      541 yidfadqlkr ddatqtysnl gatkhkgael gfkynlgain ddlanvsmya nttytkatas
      601 agqdsgneld fysnwvgnag vdykrdqwtf ntnlyaqsrq tasgnnndgt grygnipgyg
      661 ivgvraaydf adtslsglkv glgvknlfnh dyytrsadqv ggiyagpsrt yylqtsfdf
//
LOCUS       WP_005202661             625 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Acinetobacter].
ACCESSION   WP_005202661
VERSION     WP_005202661.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 625)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..625
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68853
     Region          19..625
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mqnttkkaal patalaalgv vfgdigtspl yalkesfhaa hglgiqpenv lgilsiifwc
       61 lmliisikyi aivmradnng eggimallal nlrkaklset kkiyliaigf igaslffgdg
      121 iitpaisvls aveglsiatn vldpfivpia ivivttlflm qkhgtafvgk ffgpitlvwf
      181 lslgilgias viqtpvvlgm vsphwaiqfi fthpvqsffi mgavvltvtg gealyadmgh
      241 fgprpirfgw fsvvlpclvl nyagqgalll rhpaaienpf yllvpswaly pmiilatmaa
      301 viasqavisg vfslarqaiq lgylprlgik htsdseegqi yvpflnwlll iailililif
      361 qtssnlasay glavtltmlc dtilvavfiy yawkwslpkv flliipffil esvlvaaasl
      421 kifsggwvpl ligavamiil mtwkrgrelt faklehdtls ldlfirsigd nvhrvpgdav
      481 fltgtpnvvp hamlhnikhn kvlhernila tvviedvpyv pqeerihvet ldnhfyriki
      541 fygfkdepnv pralaqayeq lefeydlmqi sffisrerim hsvgdgmapw rehlfismqr
      601 ntspvsdfyq iptnrvvelg sqiei
//
LOCUS       WP_005202804             331 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005202804
VERSION     WP_005202804.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 331)
  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   6  (residues 1 to 331)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..331
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37702
     Region          40..200
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <163..331
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mteipsipsv lleliakylq qnnisnlqld elskqyahqa rmplhkwwnl leqiyqqhpt
       61 pvlghfigel aephhihilg ylalsspnli gflncfrnfq pllqnsasfs ivqkedrfcm
      121 cwtpvvhkns qlsnevllsg vlstirkilq qpeicplkie fsatapidit pyaevygcpv
      181 sfdsdvlrlw lpleilhlpi psrdphlkkl lnqqaeallk sipnpdtflk dlqllivnml
      241 kigepsaeni akqmnlslrs fyrklsgynl qysdlvksir lelaktyltk salslteial
      301 llgyaeqsaf srafkqwehl tpseyrkshl s
//
LOCUS       WP_005203355              83 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Acinetobacter].
ACCESSION   WP_005203355
VERSION     WP_005203355.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..83
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8822
     Region          6..83
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mqtieikiea fgaierllpk alafefakdq mvkdvlshii nlypdansam ekcacaiged
       61 ivtrqtaldt sctlvllspv agg
//
LOCUS       WP_005203507              82 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Gordonia sputi].
ACCESSION   WP_005203507
VERSION     WP_005203507.1
KEYWORDS    RefSeq.
SOURCE      Gordonia sputi
  ORGANISM  Gordonia sputi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 82)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 82)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 82)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 82)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Gordonia sputi"
                     /db_xref="taxon:36823"
     Protein         1..82
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8250
     Region          10..82
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mtltvrffaa araaagvdlt eidvpadatl gdleralgag hpaltpvlar csylrdaial
       61 cdrtaplgdc atidvlppfa gg
//
LOCUS       WP_005204774             333 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005204774
VERSION     WP_005204774.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 333)
  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   6  (residues 1 to 333)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..333
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38036
     Region          25..201
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          102..332
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtskktsdag iflwmvyqtm qkmnldaaai farvhlpdqp pdkfvrrdna tqqrfwqaae
       61 qishdpdigl hvghnvppfr gqvieylfls satfgeglkr tiryqalltd amsfnlemin
      121 ehrvmisgln hpvrhyleca igillnffky isdetftple iglpylngad qeeyqeiwgc
      181 pvkfgqdngy icfdsaqltt psaahepell kvhehhaasq lellnkhqli neiekilasg
      241 llesgefdqn iisrhlgrst rslradlqll ntgyekviah yrerlarrll sqtkesidqi
      301 vyltgfseps afsrafkrwt getptayrqr kqt
//
LOCUS       WP_005205170             830 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [Acinetobacter].
ACCESSION   WP_005205170
VERSION     WP_005205170.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 830)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 830)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 830)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..830
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..830
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=92848
     Region          62..112
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          132..830
                     /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 mkdyqakttl alavrailwg mplsvisiat tsayaanvyq isissttldq alkqlaiqtg
       61 ttisydsttl skiksaslkg nysvetalet llkphafeai kvanagysiq akatvaavep
      121 kvvkleaiht radqtrnsna qqesnstqlp tisikaasqn mtnvgkqaqn ikdvpqsvtv
      181 msrqrldeqg lktlddvmvq ttgvtreqlw lnnnysargl kienirydgg stssledrsn
      241 sadmaqydav evlrgadglf gageaggvin ltskrpkaet eingsisags wnnyrgefda
      301 tgsltedqsv kgrlvtvfqd rdffykptqs rremvygals fdllpettlf tgvsyqkdkv
      361 dafnaslprw edgadlhlpr sttmgapwgw ierkntsffa nlqhqinddw ktqlnvrhni
      421 gndainsaem egavsydthq sqwwryqddt rfkettmdln lqgsfnlfeq khdvilgidh
      481 snnqkdyrln wtsyangdaf nrvappewdy paiswennst nknnksalyg slklrpvddl
      541 alilggrytf kdeltinnhn inientyted kkfvpyygit ydispsttty asfaeiyknq
      601 rnyltaadgp glepltgrni efgikhqina nllasiayfd ikkekekvyn aytsipnsns
      661 lccyigtgsm eskgidveln gnispdwnls vgytynknek kdntdtpyns ytpknllkiw
      721 ttyqldqivn gleigagvia qsknynkgwv refnpvtqkf dgtlknielv qpnyaiwsar
      781 vaydinpqwn ialnlnnifd ktyystigyp gygnfygepr nflltlkasy
//
LOCUS       WP_005205836             201 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Gordonia].
ACCESSION   WP_005205836
VERSION     WP_005205836.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 201)
  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 13014342
            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="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=21253
     Region          81..200
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(149..150,153,173..176,178)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 misvtkkhsr artarslvlg yawpalaaia vlavtiatvv gltlhssata dsapptdnar
       61 svaapiiprp scpeksdgka ivvglasqhm vlcldgrqis dvpvttgsvd rgagtplgtw
      121 rieshdvdrt lsgpgytvfv hywlhlfgdi gfhdspwqkf pygdttaykt rgsegcihvp
      181 gneikhlydw agdgtpvtit a
//
LOCUS       WP_005206364             259 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005206364
VERSION     WP_005206364.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 259)
  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 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   3  (residues 1 to 259)
  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   4  (residues 1 to 259)
  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 259)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..259
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28958
     Region          32..247
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          173..248
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mdslkndnag wsgqaaialg iaaflgqsgn nhphhhyahq itmslnadqp vqviadgqly
       61 qaptlfipak lkhqlitgdy lslyidtcha lttrfnlefh astqvgevsi dlqqllqhsf
      121 hsqiplnhgl adflkntqls nsapyrnpqk leyilallyq gvlqsnipdr qslaqvagls
      181 esrfshwfre qvglplrsyr kwlrlmcglt qmqngraltd tahqadfadq ahftrtciel
      241 lgvrpselsq mqgqiffie
//
LOCUS       WP_005205857             712 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase [Gordonia].
ACCESSION   WP_005205857
VERSION     WP_005205857.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..712
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=78640
     Region          9..>459
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 marhtgrlel twtdkdrall stgdgkydyt ftdhddprvr evrllrevdr ieaptpadrp
       61 ndlpeptvdn llitgdamha ldalaktpew aakyrgkvkl vyidppfntg qaftqyedni
      121 ehsiwltmlr drlrqikpll skdgsvwvhl dhvevhrcrs vmdeilgsdn faaevawqka
      181 dstrndaktl svdhdtllvy raspewspnr lprtaesdar fsspdrdprp wfddnptapg
      241 akthqgmvya iehpmtgelv ypargrcwwt qqsqileimn eyapyelrdl gdvhkraelc
      301 gvkpddvrqn vmavalsvpl aearvcarer ydqgawpqil lrsggegglg rkayvpnkgl
      361 vastwwtndl vghnreakae vkaifpnlna fatpkperll erviqigsdp gdivldcfag
      421 sgttaavahk mgrrwvtsel iadtveaftk arlirvlkgd dpggvttssv rvaangvslp
      481 ldvdpkaaqq fqttlgrvlg nppaegddle appltlnpak vlagavrdaq krgelslgad
      541 diatlltllr qvgndgalse vditksvkte lnrrtrtrda vtvkwhgggg fthlevapsm
      601 yevddedgdv ylspeavngv wsrsvaaqlk ftftpdhpvf cgvrgrqrlv vvdgvadeiv
      661 vrtvveqlgv keravvvakv vlpeaqtllt elspgsrlrk aprdlfpkrt vk
//
LOCUS       WP_005206697             159 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LytR C-terminal domain-containing protein [Gordonia].
ACCESSION   WP_005206697
VERSION     WP_005206697.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 159)
  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 10598501
            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="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=16258
     Region          74..157
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mnadrepnrl plragamlll avavvfvglg whsaatsgqs peeglrdaqa svattstpas
       61 ssatsastse rlcvinagsv sglasevtdd lkakgftmss psnydggsft entilyrdss
      121 qkaeaqkvat algsspsveq rpssftmcrd giavvvvtr
//
LOCUS       WP_005207024             264 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: hydroxypyruvate isomerase family protein
            [Acinetobacter].
ACCESSION   WP_005207024
VERSION     WP_005207024.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..264
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29657
     Region          1..257
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mshlavnlsm iftevplier falahahgfq hveiqfpyel dvidirtqle qhnlslclin
       61 vpagdlmqgg nglagvpgre iefhqalela iryataldvp rvnilagkqp ldadllpcln
      121 tlasnlklac hmlteqgiep vfemingtdm prflvqniaq aqemleainh palkmqydcy
      181 hmammgedvl tglqenidqi ghiqfadcpd rhepdtgnip ykqifdwllq sdyrgliaae
      241 yrpktqsdqs fawknkyfsn dvnt
//
LOCUS       WP_005207073             141 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Acinetobacter].
ACCESSION   WP_005207073
VERSION     WP_005207073.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..141
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15934
     Region          1..136
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 msylllflsa fgaatllplq seavlmtlli qglsnpfyli lvatignvlg scvnwwlglk
       61 iehfkdkkwf pvseqrllqa qqiyhkygfy slllswtpvi gdpitliagl mkenfwrfll
      121 ivtiakggry ltlyalyigl f
//
LOCUS       WP_005208274             738 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Acinetobacter dispersus].
ACCESSION   WP_005208274
VERSION     WP_005208274.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter dispersus
  ORGANISM  Acinetobacter dispersus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Acinetobacter dispersus"
                     /db_xref="taxon:70348"
     Protein         1..738
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=80599
     Region          23..738
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mksvscsaal likfqpssls laiaisligs shvafaeevq pnepqtlati siqaqgnwle
       61 nanaekvqqh agartiidhk rldeiattsi rdalkqipgv qvqdsngtgg sdvslnlgvr
      121 glasrlsprs tvlmdgvpls fapygqpqls lapvsmgnie svdvvrgags vrfgpqnvgg
      181 iinfttraip qafsgsvglt tefatgtdql kytpnlfigg tldnglglal lysgskgdgy
      241 reannkidid dvmlktsyqw tdqdaiavnl hhyegrgemp egltaaqfad npyqsnqsrn
      301 yfagrrsdvs vkyshkdeqn nfellgyyvd sfrtsdlesi gnkgtntlsn sprdykyfgi
      361 eprysraysw agmdnevtvg yrylqeesse fsgrtipynt ltgtpgdrip nttsdggtka
      421 haiyidnrfg lanwvitpgv rfesidthnd ftayqdgvvt ntvypkikse eflpslsvly
      481 kanenwnifa nagvsfgpqq ynqlvttqmv nkttntaftt ldglhpeksk nyeigtkylg
      541 nglnaeltvf yldfdkelml erpdaigtgi wtnlgatshk gvetgfsydf gqladalegl
      601 kiygnytftk atseagkfeg kdlpyysrhi gnlglayqid hwsinadmfa qskqhapgsg
      661 dvyiteetad grtgdipgys tfavrtgydf snqlkglkia ggvknvfdtq yytrssdatg
      721 gkyvgqprtf flqtsydf
//
LOCUS       WP_005209374             372 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Gordonia].
ACCESSION   WP_005209374
VERSION     WP_005209374.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 372)
  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 372)
  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
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 372)
  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   5  (residues 1 to 372)
  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   6  (residues 1 to 372)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 372)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 372)
  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 15726307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..372
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38032
     Region          7..>74
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          81..331
                     /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 mlrgvvpatl qigstpaaav lhairvgapi trdrladvtg lspatinrqv talagqglvt
       61 erpdlvspgs igrpknpltl drdtlcaagm higarrtllt ivdlggrply shavltprgd
      121 adaalaelcg qlreladrfs grrllwggaa vggsvdaasg tvdhpilgwh raqlgpalad
      181 aldvpvsvce hveamaaael llgqtiidaa sglffyaret tgmamtlngr vhipargags
      241 iahvrvdapv lcpgsgatls dvigseptlr aakrlgispd aspivderar ilgevvatfr
      301 dalnpdsvvv agdafaahph glapvqaafd aasktdwpme ltpslfgvtv pegaaivval
      361 sviyadpvas la
//
LOCUS       WP_005210425             159 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Acinetobacter dispersus].
ACCESSION   WP_005210425
VERSION     WP_005210425.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter dispersus
  ORGANISM  Acinetobacter dispersus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Acinetobacter dispersus"
                     /db_xref="taxon:70348"
     Protein         1..159
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17421
     Region          10..159
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 maeelvlqqg hkaeqyqsii pqiqaivede sdvianlani caalkqqfgw fwigfylvkd
       61 nelvlgpfqg piactriakg rgvcgaawqq qqvivvpdvd qfpghiacss asrseivlpi
      121 mkvgecvgvl dvdsdelsqf devdaeylqq litlietfi
//
LOCUS       WP_005211191             297 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Clostridium celatum].
ACCESSION   WP_005211191
VERSION     WP_005211191.1
KEYWORDS    RefSeq.
SOURCE      Clostridium celatum
  ORGANISM  Clostridium celatum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Clostridium celatum"
                     /db_xref="taxon:36834"
     Protein         1..297
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33617
     Region          1..269
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 msyidlhmhs nysddgefsp kelvrlclek gikyfsisdh nstkgineai rycedkeiti
       61 ipaieldcti dgvnlhllgy gidyesdvfe dieaniisqe qiaskermrl irelgidfdn
      121 elidrlskng vvngeiiaea amifdknqen pllkpyyeng srsdnpyvnf ywdfcsqgka
      181 aysevkfisl keaikvikdn ggvtvlahpg nnvkenkell ekiisfgveg ievyssyhnk
      241 nqinfyydfa lknnllmtcg sdfhgktkps isigsvssgd neekiikelk srimfkk
//
LOCUS       WP_005211288             830 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Acinetobacter dispersus].
ACCESSION   WP_005211288
VERSION     WP_005211288.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter dispersus
  ORGANISM  Acinetobacter dispersus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 830)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 830)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 830)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..830
                     /organism="Acinetobacter dispersus"
                     /db_xref="taxon:70348"
     Protein         1..830
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=92745
     Region          62..112
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          132..830
                     /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 mkdyqakttl alavrailwg mplsvisiat tsayaanvyq isissttldq alkqlaiqtg
       61 ttisydstsl skiksaslkg nysvetalet llkphafeai kvantgysiq akatvaavep
      121 kvvkleaiht radqtrnsna qqesnstqlp tisikaasqn mtnvgkqaqn ikdvpqsvtv
      181 msrqrldeqg lktlddvmvq ttgvtreqlw lnnnysargl kienirydgg stssledrsn
      241 sadmaqydav evlrgadglf gageaggvin ltskrpkaet eingsisags wnnyrgefda
      301 tgsltedqsv kgrlvtvfqd rdffykptqs rremvygals fdllpettlf tgvsyqkdkv
      361 dafnaslprw edgadlhlpr sttmgapwgw ierkntsffa nlqhqinddw ktqlnvrhni
      421 gndainsaem egavsydthq sqwwryqddt rfkettmdln lqgsfnlfeq khdlilgidh
      481 snnqkdyrln wtyyadgdaf nrvappewdy palswatntt nknnksalyg slklrpvddl
      541 alilggrytf kdeltinnhn snientyted kkfvpyygit ydilpsttay asfaeiyknq
      601 rnyltaadgp glepltgrni efgikhqint nllasiayfd ikkekekvyn tytsipnsns
      661 lccyigtgsm eskgvdveln gnispdwnls vgytynknek kdntenpyns ytpknllkiw
      721 ttyqldqivd gleigggvia qsknyaagsv refnpvtkkf dgawksielv qpnyaiwsar
      781 vaydinpqwn ialnlnnifd ktyystigyp gygnfygepr nflltlkasy
//
LOCUS       WP_005211522             356 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Acinetobacter dispersus].
ACCESSION   WP_005211522
VERSION     WP_005211522.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter dispersus
  ORGANISM  Acinetobacter dispersus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Acinetobacter dispersus"
                     /db_xref="taxon:70348"
     Protein         1..356
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39804
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvkniek hfgafhalkn isldfpegel vallgpsgcg kttllriiag lesadggqvl
       61 legedatdih vrerqvgfvf qhyalfrhmt vfdniafglr vrpratrpse aeikkrvtrl
      121 ldlvqlgfla drypaqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 tlhdelhits ifvthdqeea levadqiivm nkgdveqigs prevyekpat pfvfdflgqa
      241 nrfegehtgg iirigddriq lptlldapqg kviafarpne lhihtqpqan tieatflrev
      301 wiagrvvael qdrsgrtiei llsveeanlh qfkpnqtvwi saaqlhlfad httqva
//
LOCUS       WP_005211763             200 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Clostridium celatum].
ACCESSION   WP_005211763
VERSION     WP_005211763.1
KEYWORDS    RefSeq.
SOURCE      Clostridium celatum
  ORGANISM  Clostridium celatum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Clostridium celatum"
                     /db_xref="taxon:36834"
     Protein         1..200
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22902
     Region          1..>188
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mlvdlhihty ysdgtmspqe vvedakskgl giiaitdhdv ldsynefkae aekngiiair
       61 gveidsifeg hlvhllaykf ndnerfinlv neakrtllkt seelikkman dyenisiedy
      121 dsyeydrrkg gwkgihylle rniteglfdg mkfygqyecg hekfdfpsvk evcevtheag
      181 gyvvlahpst iikiklrkkf
//
LOCUS       WP_005207343              70 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Gordonia sputi].
ACCESSION   WP_005207343
VERSION     WP_005207343.1
KEYWORDS    RefSeq.
SOURCE      Gordonia sputi
  ORGANISM  Gordonia sputi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 70)
  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 70)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 70)
  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 10558483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..70
                     /organism="Gordonia sputi"
                     /db_xref="taxon:36823"
     Protein         1..70
                     /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=7396
     Region          16..67
                     /region_name="HTH_IclR"
                     /note="IclR helix-turn-helix domain; pfam09339"
                     /db_xref="CDD:430539"
ORIGIN      
        1 maneqspdrp saelgsvarv vaildavgsv erdlgvsdis rrvaiskssa hrialelveh
       61 gllerdgtry
//
LOCUS       WP_005211934             341 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter dispersus].
ACCESSION   WP_005211934
VERSION     WP_005211934.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter dispersus
  ORGANISM  Acinetobacter dispersus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 341)
  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 341)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Acinetobacter dispersus"
                     /db_xref="taxon:70348"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38340
     Region          28..211
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          255..336
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkttstrqdq gipgvyglll ldvvsrwgys detlfapfhl tseqladpny riptpianel
       61 vkhslrltge stlgfhlgtq mrisihgfig yaimtahdit daialasrfi qlrlpflqly
      121 fstfgpkatl qlqcdievep lrseiilglt igimtmakal tgiddlsgev dldfpepagf
      181 ekykdrlsst vrfnqphlis sfdkkylglk mvnadpiasq iainqcetel salgerrrla
      241 mrvrdiltns eqhylsiesv aerlhmsdrt lkrqlaaegt sfstlvdevr yrhatsllsr
      301 tdysleqiad elgysdvanf srafkrwsgr spsnwrkdpy l
//
LOCUS       WP_005212076             338 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter dispersus].
ACCESSION   WP_005212076
VERSION     WP_005212076.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter dispersus
  ORGANISM  Acinetobacter dispersus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 338)
  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   5  (residues 1 to 338)
  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   6  (residues 1 to 338)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Acinetobacter dispersus"
                     /db_xref="taxon:70348"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38290
     Region          22..200
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          102..335
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mvplahtavl knyldvsqql dlnpyqllsd agiypaqlqd stqripvdka vtlleqsaql
       61 sgcesfglhm aeqrqladfg elslllsyqq tlrdglytiv qyrnlinnal emyieevght
      121 viirvevitt ateysrqaie lalgithrfc aallqkwhpl sihfthdaph dtamhqrmfg
      181 cslefgsefn givcntteld ktnphanttm lahakrflet dllhresess iifdirksih
      241 lllpmgrati dqvahthgin vrtlqrrlea ahtnfsvlin dvrrnlvfry lknlnyslgq
      301 vsdilgysmp ssftrwfsse fgmspttwrn nnrsamks
//
LOCUS       WP_005212338             625 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Acinetobacter dispersus].
ACCESSION   WP_005212338
VERSION     WP_005212338.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter dispersus
  ORGANISM  Acinetobacter dispersus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 625)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Acinetobacter dispersus"
                     /db_xref="taxon:70348"
     Protein         1..625
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68869
     Region          19..625
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mqsttkktal patalaalgv vfgdigtspl yalkesfhaa hglgiqpenv lgilsiifwc
       61 lmliisikyi aivmradnng eggimallal nlrkakisdt kkiyliaigf igaslffgdg
      121 iitpaisvls aveglsiatn vldpfilpia ivivttlflm qkhgtafvgk ffgpitllwf
      181 lslgvlgits viqtpivlgm isphwaiqfi fthpiqsffi mgavvltvtg gealyadmgh
      241 fgprpirfgw fsvvlpclvl nyagqgalll rnpaaienpf yllvpswaly pmiilatmaa
      301 viasqavisg vfslarqaiq lgylprlsik htsdseegqi yvpflnwlll iailililif
      361 qtssnlasay glavtltmlc dtilvavfiy yawkwslpkv flliipffil esvlvaaasl
      421 kmfsggwvpl ligaaamiil mtwkrgrelt faklehdtls ldlflrsign nvhrvpgdav
      481 fltgtpnvvp hamlhnikhn kvlhernilv tvviedvpfv aqeerisvea ldqyfyriki
      541 fygfkdepnv pralaqayqq lefeydlmqi sffisrerim hsvgdgmapw rehlfismqr
      601 ntspvsdfyq iptnrvvelg sqiei
//
LOCUS       WP_005212484             292 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter dispersus].
ACCESSION   WP_005212484
VERSION     WP_005212484.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter dispersus
  ORGANISM  Acinetobacter dispersus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 292)
  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 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 292)
  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   4  (residues 1 to 292)
  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 292)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Acinetobacter dispersus"
                     /db_xref="taxon:70348"
     Protein         1..292
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32917
     Region          25..175
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          202..283
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mmndqtlinl flklvhkegf fatsidgitl mrvdrntppi avlqeptlvf vlqgqkrgyi
       61 gtetysfkqs eclivsvsmp fdcdtiaspe apmiaismkl eadrvnella ktyfenyqfk
      121 plttgmsviq ynqtisnvli rllntltseq dvlilgdqik rellyrviqh sgadaltglv
      181 aqgnlrpiyk iceyiqhhft ekltvemlae qanmstsafh kafkqvtqys plqylkvvrl
      241 hkakqllqna dqsvaqaaya vgyqsssqfs refkkqfgfp pkhaesntet es
//
LOCUS       WP_005212605             200 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Clostridium celatum].
ACCESSION   WP_005212605
VERSION     WP_005212605.1
KEYWORDS    RefSeq.
SOURCE      Clostridium celatum
  ORGANISM  Clostridium celatum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 200)
  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 200)
  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   3  (residues 1 to 200)
  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   4  (residues 1 to 200)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 200)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Clostridium celatum"
                     /db_xref="taxon:36834"
     Protein         1..200
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22586
     Region          14..199
                     /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"
ORIGIN      
        1 mylswykgai fidsvlivss skkgitffte mlsqnsyeei vtvtnggear rllverdfdl
       61 ciinaplvde fgdefasniv sngigqailv vktdiynevs ekveklgvit iakpmnraif
      121 wsalkiatat fnkisilkne nnkllqkied irmidrakci liqylnmtea eahryiekqa
      181 mdmrttkrsi adgilktyen
//
LOCUS       WP_005212665             114 aa            linear   BCT 20-JAN-2025
DEFINITION  PilZ domain-containing protein [Acinetobacter dispersus].
ACCESSION   WP_005212665
VERSION     WP_005212665.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter dispersus
  ORGANISM  Acinetobacter dispersus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 114)
  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   3  (residues 1 to 114)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 114)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Acinetobacter dispersus"
                     /db_xref="taxon:70348"
     Protein         1..114
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12424
     Region          2..114
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mqpqmmggii qvniadkatl qssfmpfvvg gglfvptkqa vkmgqevfvl atlpeqsqki
       61 pltgkviwis hkqthfkpqg faiqlvgekg vyykneaekl lagmkgldrp sytm
//
LOCUS       WP_005212979             334 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter dispersus].
ACCESSION   WP_005212979
VERSION     WP_005212979.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter dispersus
  ORGANISM  Acinetobacter dispersus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 334)
  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   5  (residues 1 to 334)
  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   6  (residues 1 to 334)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Acinetobacter dispersus"
                     /db_xref="taxon:70348"
     Protein         1..334
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37837
     Region          28..210
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          128..334
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mplnkqfert vpgtyialmv dvvsrwdisa dellsnsgft qeqlvqplwr adakivmail
       61 rraleltqip alefgfylgm qmtitchglm gmaamlakdv kqalniaqef islqssihti
      121 kldvvgthav iifeqteayy ldeviqiall vgfaqmgkni sgqeltgfad vqfskpdyfd
      181 kllplipgev rfnrpttrle fkkeildlpl lhsdaiaerl areecksqlr kllkqnsfnn
      241 ilqdliydea mgisplteil kkvqmseral qrklenegtn fralvdkvrc ekaiqllknp
      301 nlsleniaah lgytnsknfs rafkrwtgts prry
//
LOCUS       WP_005213108             331 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter dispersus].
ACCESSION   WP_005213108
VERSION     WP_005213108.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter dispersus
  ORGANISM  Acinetobacter dispersus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 331)
  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   6  (residues 1 to 331)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Acinetobacter dispersus"
                     /db_xref="taxon:70348"
     Protein         1..331
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37777
     Region          41..200
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <163..331
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mteipsipsv llelidkylq qhnisnnqln eltqqyanqs rmplhkwwsl lehiyqqhpt
       61 pvlghyigel sephhihilg ylalsspnli sflncfknfq pllqnsasfs ivqkedrfcm
      121 cwtpvvhkns qlsnevllsg vlstirkilq rpeicplkie fsatapvdia pyaavyacpv
      181 sfnsdvlrlw lpleilhlpi psrdphlkkl ldqqaeallk sipnpdtflk dlqllivsml
      241 kigepsaeni akqmnlslrs fyrkltsynl qysdlvksir velaksylvk selslteial
      301 llgyaeqsaf srafkqwehl tpseyrkshl s
//
LOCUS       WP_005213589             400 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Acinetobacter dispersus].
ACCESSION   WP_005213589
VERSION     WP_005213589.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter dispersus
  ORGANISM  Acinetobacter dispersus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 400)
  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 11465564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Acinetobacter dispersus"
                     /db_xref="taxon:70348"
     Protein         1..400
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=42619
     Region          <131..179
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          269..396
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mfvrsllams lscilanvay aaptteqpln pkkisaavqd pidplavdra tsnvatqpas
       61 svaataasep qvntgaasvv sqqlentpda kttttapavp aswtmdaina aewpeglpkg
      121 qnpayarahv mlnnshaspg aidgsngknt lkaiasfqqm ngltptgqlt ketwdalvak
      181 qtkpayveyt itdadlkgpy adsipsdyal qakmkglyyt rvtemlgekf hmderflkql
      241 npnanfkkag ekiivanvrn dlpedihliv ahkgarqlyl fnsrnqmias fpatigstdt
      301 psptgtykvv gvaknpyysy spsnfvqgkn lkpltlppgp napvgniwig lskksfgihg
      361 tpnpsliskt ashgcirltn wdandlgakv rsgvtvkfle
//
LOCUS       WP_005213772             285 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Clostridium celatum].
ACCESSION   WP_005213772
VERSION     WP_005213772.1
KEYWORDS    RefSeq.
SOURCE      Clostridium celatum
  ORGANISM  Clostridium celatum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 285)
  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 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   3  (residues 1 to 285)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 285)
  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   5  (residues 1 to 285)
  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   6  (residues 1 to 285)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Clostridium celatum"
                     /db_xref="taxon:36834"
     Protein         1..285
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32678
     Region          21..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..283
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mewiesirka isyieenite dlsieeiadr vnispfyfqk gfgmlcgysl seyikrrrla
       61 lagseilstn gkiidiaiky gydspdsftk aftrfhgvtp savrkegamv ksfvalrikf
      121 sleggyimdy kivekdefkv igaskkfkyd safmevplfw nehisqgkln eicgmygini
      181 deemggnefe yliaedyste kegmegyivk tipkftwaif pcygpsptai qetnkkifse
      241 wlpnereysi aagyniemyt dpsqykkgtl denyysevwi pvkkn
//
LOCUS       WP_005213923             276 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Clostridium celatum].
ACCESSION   WP_005213923
VERSION     WP_005213923.1
KEYWORDS    RefSeq.
SOURCE      Clostridium celatum
  ORGANISM  Clostridium celatum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Clostridium celatum"
                     /db_xref="taxon:36834"
     Protein         1..276
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31145
     Region          1..250
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mvicdlhths tasdgkfsps evvkkaydrg vkylaltdhd tlsgiqeake taekldihfi
       61 pgvelsttyk getihilgyf rgddyknvel nnfledlktk riaraheivr rlkkfndiei
      121 dvnevlkngk dtiarphiak aimdagynyt keyifdnfig dhcpayipan klateegial
      181 lrkynalvil ahpvllkklh vldvlhldfd giegiyglnt kedterflki vdqkniltsc
      241 gsdshgyeed dkkhgflgsq sieenrlnkf idalnn
//
LOCUS       WP_005215270             356 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Acinetobacter].
ACCESSION   WP_005215270
VERSION     WP_005215270.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..356
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39911
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvkniek hfgafhalkn isldfpegel vallgpsgcg kttllriiag lesadngqvl
       61 legedatnih vrerqvgfvf qhyalfrhmt vfdniafglr vrpratrpse aeikkrvtrl
      121 ldlvqlgfla drypaqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 tlhdelhits ifvthdqeea levadqiivm nkgdveqigs prevyekpat pfvfdflgqa
      241 nrfegehtsg iirigddriq lptsleapqg kviafarpne lhihtrpqan tieatfirev
      301 wiagkviael qdrsgrtiei llsveeanlh qfrpnqtvwi saaqlhlfad qttqva
//
LOCUS       WP_005215467             269 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Clostridium celatum].
ACCESSION   WP_005215467
VERSION     WP_005215467.1
KEYWORDS    RefSeq.
SOURCE      Clostridium celatum
  ORGANISM  Clostridium celatum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Clostridium celatum"
                     /db_xref="taxon:36834"
     Protein         1..269
                     /product="formate/nitrite transporter family protein"
                     /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=29200
     Region          2..261
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mykreidnlt hsaevkiglf nqsipkylts aflgsffvsl gimliysigg vmhhagvety
       61 kvlmgacfgv altlvfmcgg dlftsnamim tvgslekkvt wldalkiwvt vwvgnliggv
      121 vgaflyvqag lasgkseyig efivsnvatk mntpgmelfv rgllcnvlvc latwcayklk
      181 eetakilmiw wclftfitag fehsvanmgf ltmglllphg advsimgfih nigwvslgnf
      241 vggivfvglp yyfismdktk ksisdksaa
//
LOCUS       WP_005215911             168 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Clostridium celatum].
ACCESSION   WP_005215911
VERSION     WP_005215911.1
KEYWORDS    RefSeq.
SOURCE      Clostridium celatum
  ORGANISM  Clostridium celatum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 168)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Clostridium celatum"
                     /db_xref="taxon:36834"
     Protein         1..168
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=19313
     Region          49..167
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(117..118,121,141..144,146)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkllsaiksi fskrkyrfsk nstlenetyi iestkfintn nfysktnyfi widtanfktn
       61 ifkgsnknwv lihsylcslg kpteptikgt fyagpkgysf geargfrcly ytqikdnyli
      121 hsipynldgs irdprlgmrl tdgcvrlate nskwiydnvp sgttifin
//
LOCUS       WP_005215913             170 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Clostridium celatum].
ACCESSION   WP_005215913
VERSION     WP_005215913.1
KEYWORDS    RefSeq.
SOURCE      Clostridium celatum
  ORGANISM  Clostridium celatum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 170)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Clostridium celatum"
                     /db_xref="taxon:36834"
     Protein         1..170
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=19592
     Region          51..170
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(119..120,123,143..146,148)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 milknkikni yyilkskkes isvkyrapsn ynekvskfin nknlssstky liyvdtenfq
       61 vnifvgsknn wildknyics igkpstptpk gffkigakgy sfgenhgyic yyysqfkgny
      121 lfhsilynld ntirdgrlgf kisngcirls kinakwiydn ipygttvyiv
//
LOCUS       WP_005215999              83 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Acinetobacter modestus].
ACCESSION   WP_005215999
VERSION     WP_005215999.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter modestus
  ORGANISM  Acinetobacter modestus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Acinetobacter modestus"
                     /db_xref="taxon:1776740"
     Protein         1..83
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8921
     Region          6..83
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mqtidikiea fgaierllpk elafefaenq tveevlshiv mlypeatkam dkcacaiged
       61 ivlrqtvlnt sctlvllspv agg
//
LOCUS       WP_005217049             875 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Acinetobacter modestus].
ACCESSION   WP_005217049
VERSION     WP_005217049.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter modestus
  ORGANISM  Acinetobacter modestus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 875)
  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 875)
  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 875)
  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   4  (residues 1 to 875)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..875
                     /organism="Acinetobacter modestus"
                     /db_xref="taxon:1776740"
     Protein         1..875
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=98130
     Region          109..837
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mtqkldqmta ttlsstptnt ttakinslps afeqtdiqtt lkktaltpeq lthilnlaei
       61 psstkrikpl nnflgqdrar asveagislp ysgynifavg taglgkrtmi krllqqhaks
      121 mptpndwvyv nnfknprqpi alrfpagqgt kfqnalqqtw qiilkqlerr fsaesyhnri
      181 erirqetgdv qqqalieltk egqeldlkli srddkhvfip mqlieneyqe ltkndldals
      241 skeraeitsn mrymekkler lglhlgdled dardqvsiln reiatqvvtp rmesilnknk
      301 evkgldlylk hyaediidnv elileqeedd ftpalfnrvp sryqanviia nkpnsgapvi
      361 fedfpthynl lghveqlthn gtittdftli rpgslhqang gflmleaeql leqpyawqgl
      421 kralksgqlk lsslehmltl tgsisiepas vpldikvvll aepeiyyeil evepelgsvf
      481 kiradftdtl qrnnsneqay mqliadyvqa dkllpfdrsa laalltdssr qaedqsslsl
      541 hastlgdlir eahhhafkad dkivtdqhvn qalhhrqyrl gylrelywqd lsrgtqliet
      601 sghrlgqina lsvihyadve fglpsrltas vyqgggdild iersvelggs lhakgvllms
      661 sflkahfgre qilhfsaala feqsygqvdg dsatvaelsa lisaisqipi dqswaitgsm
      721 nqlgqvqpig gvnakiegfy dacklqgltg kqgviiprqn mqhlmlrqdv ieavqagqfh
      781 vhaietidqa leilmarpvg tldkkgrysk nsiyaavmeq leywqaiedg eaveddepkk
      841 kkkrkktkka etetkssees tveakslksl rkknr
//
LOCUS       WP_005217816             416 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Acinetobacter modestus].
ACCESSION   WP_005217816
VERSION     WP_005217816.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter modestus
  ORGANISM  Acinetobacter modestus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Acinetobacter modestus"
                     /db_xref="taxon:1776740"
     Protein         1..416
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=48187
     Region          3..289
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          289..387
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mtvrffhtsd whlgqffynh srhyeheqfl awlleqikak qphalliagd ifdvinpssq
       61 aqkqlyqfla dahelapqmq tlmiagnhds gyrieqvepl lekynaktvg virwnqdksl
      121 dlerlilpiy dqqkqivawc ialpflrsae itgfnehttn sqnaiaylhq qlieeakrrk
      181 tddqalimms hahmqggets dserpiiign eealstalfd dsidyvalgh lhkpqkvqhp
      241 hirysgspip lsfseinykh qvvevsidpk knedafsfea lpiprsiqlh kikdelsvvm
      301 qrlrnlpnep ienlehreyv dieyhtttpp qpnlrqqfed alpkdryrlv risrqylsne
      361 staeskqtis lepptpeklf qqiwekkgyh addevtqdfm slvaeaqkql eddqti
//
LOCUS       WP_005219805             893 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase [Helicobacter].
ACCESSION   WP_005219805
VERSION     WP_005219805.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter
  ORGANISM  Helicobacter
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae.
REFERENCE   1  (residues 1 to 893)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..893
                     /organism="Helicobacter"
                     /db_xref="taxon:209"
     Protein         1..893
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=104089
     Region          418..803
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mdykkafysk leecylgaki kayekahtaq ntqsstsnaq sgfsnllsik eqyfshikay
       61 ldsaipnddf nshdiynkly tffdsylndt gtpffhdtpl ykniyakvyt nskdtslfyk
      121 tkdlyyvksd tlytsltlsd enelaqiyfd tseyrqnadn tkrklifkld kieqtstdtq
      181 dsiptiyikv lsqkdlfpdl navfkensne lsedfikslk ahkipldear ikklftsykk
      241 qnevdffihk naraflqeqf dlwfyhylyk dsefqewsvk sishlqrirn ialeiiglig
      301 dfedelkavw lkpkfvkvvn yvfsldlilk hlalsdkaqn ttlldsickd kgfekqikew
      361 qdlglidesf qaqnisekil sddkykflpl dtkhfskeik ykilsvfddi esilngelik
      421 adnfqalnsl mpkyqnkvdl iyidppynts nndfvymdkf nhaswlsmia nrlelarefl
      481 qdsgsifisi ddneqarlki lcdsifsedn fisngiyekv kirknsaqyf seshehilif
      541 arnrdiwkrk llprkdlkgy knpdndprgv wipipihanh yydadykitk pngvilekpk
      601 nqswrlseen fkkhikenri wwgngngypm ikrflsevqe glvprtifyy detggnpagd
      661 kalkdtfdnl kvfenpkpeg liqqiaeigs nensiildff agsgtsvata qklgrkwlgi
      721 emgehfykvi lprlkkviag fqsgiskecd yqgggafryy elesyeealk eceyvladfq
      781 cerktskiad nnteaiypak dyqkaqkiid yrksrklikk lnkgetitld msgyrkefdl
      841 fhtlanlqgl kikrlfldsk giescefdng eilnrdsidl akypklknli wwe
//
LOCUS       WP_005221074             139 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Marichromatium purpuratum].
ACCESSION   WP_005221074
VERSION     WP_005221074.1
KEYWORDS    RefSeq.
SOURCE      Marichromatium purpuratum
  ORGANISM  Marichromatium purpuratum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Marichromatium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Marichromatium purpuratum"
                     /db_xref="taxon:37487"
     Protein         1..139
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14452
     Region          1..135
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkrqqsgftl ielmivvaii gvlaaiampa yqdyvaksqv aaglaeitpg ktemelmvne
       61 grtadynavt dlglkaatss cnvtanvdnt gagtivctlt gnpkiigkki twtrstdgew
      121 tcafdgdkkf atkgcpass
//
LOCUS       WP_005221239             110 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Acinetobacter sp. CIP 101934].
ACCESSION   WP_005221239
VERSION     WP_005221239.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CIP 101934
  ORGANISM  Acinetobacter sp. CIP 101934
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Acinetobacter sp. CIP 101934"
                     /db_xref="taxon:1144661"
     Protein         1..110
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12009
     Region          4..108
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(28,59..60,62,89)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(28..29,37,40,42..43,45,48..49,51,59,64,71)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mpakpsdela rmilnviali pqgkvasygq laqlaglprh arlvgrvlre mdevsdlpwh
       61 rvvssqgkis vqkldeqgmn iqasklleeg vavikgkinl klyqwdgsiq
//
LOCUS       WP_005221887             315 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Acinetobacter sp. CIP
            101934].
ACCESSION   WP_005221887
VERSION     WP_005221887.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CIP 101934
  ORGANISM  Acinetobacter sp. CIP 101934
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (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   2  (residues 1 to 315)
  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 315)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Acinetobacter sp. CIP 101934"
                     /db_xref="taxon:1144661"
     Protein         1..315
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35823
     Region          27..74
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msldattwaw kvrqkqkpgg stkplkrlvl lsladraged hcaypsvarl vedtemdrkt
       61 vlkiideliq dgliedtger kgrtkqvkvy rlvgvngret vptmesfnae neglkgtnig
      121 tvptteqfqr svervptfrg kspnvgtrnl sknlsieskn kkswfcfnkl reemfltdds
      181 idfeiivdsk wierekrafe synaekpmsd elmiyhfadw vinafknkys skpnsekpag
      241 tkyqsqhlse kqifvfaekl shhpeftskf sepgetyekl aariavklkd paqakkwegy
      301 lkqvgfngdl sdiaa
//
LOCUS       WP_005222771             353 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Acinetobacter].
ACCESSION   WP_005222771
VERSION     WP_005222771.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..353
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39520
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvkniek hfgafhalnn isldfpdgql vallgpsgcg kttllriiag lesadggqvi
       61 legqdatnvh vrerevgfvf qhyalfrhmt vydnvafglr vrprstrpse teikkrvtrl
      121 ldlvqlgfla drypaqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 tlhdelhits ifvthdqeea levadqivvm nkgnveqigs prevyetpkt pfvfdflgqa
      241 nrfegqnngg iiqlgedriq faaaqqhpqg dvivfarpde lrisaqpqen aiqatfirel
      301 wiagkvvael ndrqgnliei sltpeearah qfrpnqtvwl splnlhlfan qva
//
LOCUS       WP_005222283             342 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter sp. CIP
            101934].
ACCESSION   WP_005222283
VERSION     WP_005222283.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CIP 101934
  ORGANISM  Acinetobacter sp. CIP 101934
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 342)
  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 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 342)
  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   4  (residues 1 to 342)
  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 342)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Acinetobacter sp. CIP 101934"
                     /db_xref="taxon:1144661"
     Protein         1..342
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38777
     Region          32..209
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          256..337
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkmivprqdq gipgvyglll ldvisrwgyn deslfkpfgl tseqladpef riptaiandm
       61 vkhalkltge ptlsyhlgtq mrisihgfig yaimtannit ealvlanrfi qlrlpflqlf
      121 fstfgvkatv qlqtdiqmep lrteisialm iglismakai tgisdatgei dfdfkkpegf
      181 erfmvkfpth qfrfeqphll lsfdknylmn klvhadpias qiainqceae lsalgerhri
      241 amrvrdiltn seqhylsiea vadrlhmsdr tlkrqlaaeg tsfstlvdev ryrhatslls
      301 rtdftleqia delgysdvan fsrafkrwsg rspsnwrkdp yl
//
LOCUS       WP_005222914             359 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Marichromatium
            purpuratum].
ACCESSION   WP_005222914
VERSION     WP_005222914.1
KEYWORDS    RefSeq.
SOURCE      Marichromatium purpuratum
  ORGANISM  Marichromatium purpuratum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Marichromatium.
REFERENCE   1  (residues 1 to 359)
  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 359)
  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 359)
  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 359)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Marichromatium purpuratum"
                     /db_xref="taxon:37487"
     Protein         1..359
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39028
     Region          1..355
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mqrrdfikgv gvgslalgaa atgaahakae yrwkmvttwp knfpglgtga nklaeligem
       61 sggriavrvy gagelvpafe vfdavsrgta emghgsayyw kgkseaaqff stvpfgmtaq
      121 emnawiyygg glelwqelyg qfglvpapag nsgvqmagwf nkeinsvddl kglkmripgl
      181 ggevlaragg tpvnlpggel ftalqngtid atewvgpynd lafglykaar yyyypgwhep
      241 gtimeamvnr ealeslpkdl qaivmnackv inqdmlaeyt arnpvalstl vdehgvelrr
      301 lpddviarlr gladevvaei aerdafsakv yssyrkflaq arewsaiseq tylrardqv
//
LOCUS       WP_005223170             343 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SPOR domain-containing protein [Acinetobacter].
ACCESSION   WP_005223170
VERSION     WP_005223170.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..343
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38230
     Region          <61..>264
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          265..328
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mnnkqrwmgg vvllgggvll aalllkgkae idhhsvnvpe qpaqvesrdv ggpssltvdv
       61 etekrlleqq rrdrekavae qearaaefla mqqqaeadaa rkaaeeyaal nahrmgqqss
      121 dnippelved eqakqkrlae dkaaaqkrle qqnltqqqhs sdavkkeaer kaaeekrkae
      181 erkaaekkea erkaaeekrk aeekrkaeqq kaeeqrkaae kkeaeqktae ekrkaeekrk
      241 aeeakkkaea ekarkllege ddkqwmvqva laaneanada iaaklrakgy kvtksptskg
      301 irimvgpskd reaadairkk iasdaslnmk sawvndwvpl dkr
//
LOCUS       WP_005223705             123 aa            linear   BCT 20-JAN-2025
DEFINITION  PilZ domain-containing protein [Marichromatium purpuratum].
ACCESSION   WP_005223705
VERSION     WP_005223705.1
KEYWORDS    RefSeq.
SOURCE      Marichromatium purpuratum
  ORGANISM  Marichromatium purpuratum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Marichromatium.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 123)
  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   3  (residues 1 to 123)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 123)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Marichromatium purpuratum"
                     /db_xref="taxon:37487"
     Protein         1..123
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13503
     Region          1..123
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mssptnslga lggqqrilnf airdksalya sympyikngg lfipttkryq lddeiflllq
       61 lmeetdripv agrvvwitpp gaegnrsvgv gvqfsdqdkg aarrkiedyl agmlnserpt
      121 htm
//
LOCUS       WP_005224178             709 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Marichromatium purpuratum].
ACCESSION   WP_005224178
VERSION     WP_005224178.1
KEYWORDS    RefSeq.
SOURCE      Marichromatium purpuratum
  ORGANISM  Marichromatium purpuratum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Marichromatium.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 709)
  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   3  (residues 1 to 709)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Marichromatium purpuratum"
                     /db_xref="taxon:37487"
     Protein         1..709
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76612
     Region          3..707
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mtidmtrfyq vffdeagehl aemetlllel digapdpevl naifraahsi kggagtfgfq
       61 dvarvthile tlldrlrkhe laptvemida tlqagdllka qlaahqrgee fedpqiaevc
      121 erleqlsqgg tiepppepia gfadprpcwr lvfaaellgg sgdereagla aalaelgele
      181 rhvpadapad rltwrlctea ereaiveifd flcdpeevei ipeatveede gfgffedapg
      241 sergadqeld gfglfggspg meqvaetagr arderqqgfg ffdsapgvpe aaetaaaaaa
      301 pvaggepprq apagarrqpq gessirvsve kvdqlinlvg elvithamla esasaldpva
      361 qerifdglan lernsrdlqq avmsirmmpi sfvfnrfprv vrdtasaldk kvtlkliged
      421 teldkglier ladplnhlvr nsidhgieta qqrleqgkpe tgeivlaash rggnvvvevs
      481 ddgagldrdr llakavergv alpdnpsdke vwqlifapgf stakavtdis grgvgmdvvr
      541 rnieamngrv eidsepgrgt ritirlpltl aildgmsvrv cnetfilplt viresirpqa
      601 gqcktlagkg nvvhvgeeyl plvalhqifg lspqqvaaee tilviiesne graalqvdel
      661 laqhqvviks letnyrkveg isgatimgdg rvamildvda lvrlsrkts
//
LOCUS       WP_005224451             404 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Marichromatium purpuratum].
ACCESSION   WP_005224451
VERSION     WP_005224451.1
KEYWORDS    RefSeq.
SOURCE      Marichromatium purpuratum
  ORGANISM  Marichromatium purpuratum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Marichromatium.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Marichromatium purpuratum"
                     /db_xref="taxon:37487"
     Protein         1..404
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43862
     Region          1..400
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkvlvlnsgs ssikyqlfrs edwtaiasgm varigetege mrlewldadg vmqrdqndla
       61 vpshqegidf ivetlqshgv lgdvselsai ghrvvhggph fkhpvivdad vlaelhevip
      121 laplhnpghl agievsrkhf psvpsvvvfd tafhqtmppt ayryaipeyl ytehrirryg
      181 fhgtshhyva kraaelldkp leqcnlitmh lgngasasai rngrcvdtsm gltpleglmm
      241 gtrcgdmdpa vpiylskhlg lnaeaidhml nrqsgllgic gvndmrevvr laergnerae
      301 lalgmmthrl kkyigayyae lgavdaivft ggigensaev ragacaglea lgieldaaan
      361 agradeaglc istaesrvql wviptneele iaqqtlatve rkrr
//
LOCUS       WP_005224765             609 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Marichromatium purpuratum].
ACCESSION   WP_005224765
VERSION     WP_005224765.1
KEYWORDS    RefSeq.
SOURCE      Marichromatium purpuratum
  ORGANISM  Marichromatium purpuratum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Marichromatium.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Marichromatium purpuratum"
                     /db_xref="taxon:37487"
     Protein         1..609
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=69003
     Region          57..>479
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mkkltredga spdlvadnie rlrelfpevf adglidfdal ketlgdyvdd reerysftwn
       61 gksrakqiaq tpsmgtlrpc peesvnwdtt knifiegdnl evlkllqksy hrkvkmiyid
      121 ppyntgkefi ypdkwqdnld tylrytgqvd degfkvsana etsgryhtnw lnmmyprlkl
      181 arnllrddgl lfvsiddhea hnlrhildev fgvenfmaai awekrytrsn nakafyslkd
      241 tllvyrrsdv lehlretrte kadsgysnpd kdprgdwtts sfvnpatkek rpnlvypita
      301 pdgrvvehpt hawknseeey rrlvsenrlw wgqdgdakyp rkkiflseae gmvpvniwdh
      361 keagttdegg levkalfdgk avfdnpkptr lirkmlglst ntnscdivld ffagsgstgd
      421 avmqqnmddg gnrrfilvql pehidderfg svasisiarl raasakvave nrgfrafkls
      481 ssnikpwdae fdsidqdlve svdnikpnrs eddvlyelll kygldlaipt dtrdiegrkv
      541 tvigagaliv cladnitlev vsgitalkde fqpevmrvvf kdagfaddvv ktnavqilrq
      601 agiddvksl
//
LOCUS       WP_005225311             279 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Enterococcus casseliflavus].
ACCESSION   WP_005225311
VERSION     WP_005225311.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus casseliflavus
  ORGANISM  Enterococcus casseliflavus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 279)
  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 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   3  (residues 1 to 279)
  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   4  (residues 1 to 279)
  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 279)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Enterococcus casseliflavus"
                     /db_xref="taxon:37734"
     Protein         1..279
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32691
     Region          20..274
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <177..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 myferteene ettkhtttnr sfaiyqrclq qkrgdqlplh whdelqivwv eegsfvytid
       61 deqillskne aiiinsrvlh gavlasenvr yccfdfssdf iadpvfkeai eqlvhdrtrs
      121 yrrltltaqh qafvqtvrlp llieqrftly elflaalsql maarpaspkk etiylmlafv
      181 heryqepltv paiakaaain trtctalfrq yttltpinyl idyrlsqakn llietdepis
      241 ticyhvgfnh lsyfskrfqr kfgltplqyr ktyreddrn
//
LOCUS       WP_005226017             317 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_005226017
VERSION     WP_005226017.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
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
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            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="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=35881
     Region          5..313
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mtpiiefknv skkfdqklvi dqldlsinkg eifvlvgpsg sgktttlkmi nalseptdgd
       61 iyfkekrike yniqkmrwqm gyvlqqialf ptmdvkqnie vipemlgwsk kdrseavdrl
      121 ltqvkldpeq yrhrmpkels ggeqqrigil ralaanpeii lmdepfsald pisrnslqel
      181 vldlhqelgt tiifvthnmk eavklgtria vmnqgkivqc dtpevivsqp ktafvksffe
      241 etgedeaklv tagdlirmnf fsndinqadp kiaastplne lytlfashet lvieenhqli
      301 gslrrkdvfa flsrdrt
//
LOCUS       WP_005226611             335 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005226611
VERSION     WP_005226611.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 335)
  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 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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 335)
  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   5  (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   6  (residues 1 to 335)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38101
     Region          22..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          98..335
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mgqltdasvv lrfgyqairk aglpteeilt kagvalnqvd tnartplsaq nafwiaaqdv
       61 skdpdiglhl gehlplyrgq viehlfisse tfgeglkral ayqrlisdaf dakliiedgr
      121 cyltngeqfw pdnlvnrhfs ecamsgilrf fkfitegqfe piyidfnfse gaaddeyfrv
      181 ygcpvslgqk etrlyfdaav ldyplwqaep ellqlheqla ieklqelary dlvgevrrai
      241 gstlesgett letvaaqlni tprrlrtqls eantsfqqil sdyrcrlakk llantsesve
      301 rivyltgfse pstfyrafkr wtnetpveyr krkqr
//
LOCUS       WP_005226633             683 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Enterococcus].
ACCESSION   WP_005226633
VERSION     WP_005226633.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 683)
  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   3  (residues 1 to 683)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            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="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=75910
     Region          1..674
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          174..252
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 mddnsvyrtl ffeetddhla qlndhvlqle ndpkdsalln difrsahtlk gmaatmgydv
       61 mtqlthkmen ifelfktgtl qvtqqsisli fkcldrlsel vedlreerdl qpaqiadlla
      121 eldqtehsgg isteteasqk ptavgaltpq lqqidpsdly vieqaagdgy qavqiavrld
      181 aqsmlkgara flimeklgqa gdvlytepda qtleegtfes dfsllyltqq tladveqnia
      241 snseieafvv apfdpsaavl eeaeellqpv ptpepetsal qrattetkek sptpahhasa
      301 qnqsirvdln rldsfldlvs elvvyrnqle dvsereniea vkdpleqvsr ltselqdlvl
      361 rirmqqvnvv fsrfprmvrd lsnelqkeme lvifgeetel dktvvselse plvhllrnsv
      421 dhgieapdvr eklgkprkgt irlaayqegn rviitleddg kgldpqvika saekkglate
      481 glsdealqql ifhpgfstaq evtnisgrgv gmdavqskit qlggtiemks qpnkgtqfvi
      541 klpltlsiiq almvrvgaet faiplnlver vvmvkeeeii qtvsdevyrf qeeliplvrt
      601 dqllaiegdp sekkfaiivn ndqqfhgila deligqqeiv ikkidpllqk lnryqgatim
      661 gngsialild ihaicqekkd drl
//
LOCUS       WP_005227361             255 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Enterococcus].
ACCESSION   WP_005227361
VERSION     WP_005227361.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 255)
  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 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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (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   5  (residues 1 to 255)
  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 11454538
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30403
     Region          8..255
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          176..253
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mnvtysgfqm hnavsdhiyr psglkhylfv ltlspmvftf eddhqetsek gscilfpptv
       61 yqdyrgkedf fnsfvefqtd qvieetyaip cnqlfqpkni qqinkliqki nhesllpqrh
      121 teeliaaymt nllvllernf eesipqpqne hyqlfqamrl kmlvnceqqw dfyqfsrels
      181 igksqfykly qqffhttpke dllqarfqkf fylrsnetlt ireaafqsgf qninhfnrlf
      241 akrygcaptk yqqeq
//
LOCUS       WP_005227012             357 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter courvalinii].
ACCESSION   WP_005227012
VERSION     WP_005227012.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter courvalinii
  ORGANISM  Acinetobacter courvalinii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 357)
  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 357)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 357)
  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   4  (residues 1 to 357)
  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 357)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Acinetobacter courvalinii"
                     /db_xref="taxon:280147"
     Protein         1..357
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40109
     Region          40..222
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          241..>293
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          269..349
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mrksaaghnv iegryddpdt gsgipllgls sllnemqqqg ypipvvlegt giavealtsa
       61 tsnvsqyqkl klfqniqrls kdpligirag qkqrlsdfgv ygyalyasrn lqqaaelgmr
      121 hiklagpvlk ktfyiqnnta ifegheiial gkllplvcef wfssiqtlie cvleapfqaq
      181 klllpypapa yaeeyqkafr cpvefdadvm qwhfalewld qpcpnanpit admcqsfcar
      241 mlgtadeqqe pelvrtirll lldsvggfpt aqaiadqlhl skrtlyrrla dlemsyqeil
      301 dstrrrlade ylatslsvde iaerlgfsdt snfrkayrkw vgispneyra hknriie
//
LOCUS       WP_005227505             195 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Enterococcus casseliflavus].
ACCESSION   WP_005227505
VERSION     WP_005227505.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus casseliflavus
  ORGANISM  Enterococcus casseliflavus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 195)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Enterococcus casseliflavus"
                     /db_xref="taxon:37734"
     Protein         1..195
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=22781
     Region          <15..176
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 msekieqell sifpqlyfda qpifqmkads qkvigyelll rsternrfpl sffqqvikyk
       61 klhtrllqwy rneifsllhp neetkislni hpqqlsypet flmladlapy hdrilieite
      121 ddtepsiacd pksflmnkin qikkmrfsva lddvgtgihs ltniapmldk idvikfspis
      181 lrvlsqkeif flidf
//
LOCUS       WP_005228385             257 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005228385
VERSION     WP_005228385.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 257)
  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 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
REFERENCE   3  (residues 1 to 257)
  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   4  (residues 1 to 257)
  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 257)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..257
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29679
     Region          1..255
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          181..255
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mkqnvaeqfp llrdievhef lyqkddivsp hssiwgdfnf slngtlefdi egqyylspps
       61 yglwlpprte hqslpvehei hyicirlhpr lgdflgdvcr cfsiepffra lvihileqqk
      121 laaapeyleh llqvlydqlk qapayshylp qsthpvlapi leqlsdpalf qlslqkvlgn
      181 favserhvlr lsqqelqlsl sewrnrakii fainqirqgm tikqlafalg yhhsssfief
      241 fkrytgqtpi qlknasl
//
LOCUS       WP_005228761             141 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Acinetobacter courvalinii].
ACCESSION   WP_005228761
VERSION     WP_005228761.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter courvalinii
  ORGANISM  Acinetobacter courvalinii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Acinetobacter courvalinii"
                     /db_xref="taxon:280147"
     Protein         1..141
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15975
     Region          1..136
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 msyfllflsa fgaatllplq seavlmtllv qglsnpfyli lvatignvlg scvnwwlglk
       61 iehfkdkkwf pvseqrlkqa qqiyhkygfy slllswtpvi gdpitliagl mkenfwrffv
      121 ivtiakggry ltlyalyvgi f
//
LOCUS       WP_005229974             341 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005229974
VERSION     WP_005229974.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 341)
  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 341)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38396
     Region          28..211
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          255..336
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mktsttrqdq gipgvyglll ldvvsrwgys detlfapfhl tseqladpny riptpianel
       61 vkhslrltge stlgfhlgtq mrisihgfig yaimtahdit daialasrfi qlrlpflqly
      121 fstfgpkatl qlqcdievep lrteiilglt igimtmaral tgiedlsgev dldfpepagf
      181 ekyrdklsss irfnqphlis sfdkkylglk mvnadpiasq iainqcetel salgerrrla
      241 mrvrdiltns eqhylsiesv aerlhmsdrt lkrqlaaegt sfstlvdevr yrhatsllsr
      301 tdysleqiad elgysdvanf srafkrwsgr spsnwrkdpy l
//
LOCUS       WP_005230719             465 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase family protein [Enterococcus].
ACCESSION   WP_005230719
VERSION     WP_005230719.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 465)
  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 13100268
            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="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=51293
     Region          <11..>69
                     /region_name="PknB_PASTA_kin"
                     /note="Stk1 family PASTA domain-containing Ser/Thr kinase;
                     NF033483"
                     /db_xref="CDD:468045"
     Region          <131..>217
                     /region_name="YoaR"
                     /note="Vancomycin resistance protein YoaR (function
                     unknown), contains peptidoglycan-binding and VanW domains
                     [Defense mechanisms]; COG2720"
                     /db_xref="CDD:442033"
     Region          236..329
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          348..465
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(416..417,420,438..441,443)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mtrsnkhtda knntkkivli vvaallvvia ggytyrstyy anrflpktei dgidisnktv
       61 aeanallhdr ysqedftikd gdsewktvnl aqfglqtdft delqslkdeq nqwswgmayv
      121 saaeektlgn lsvdqdtlts etntiqkele slnedrtksa datlekgedg fsikpevdgd
      181 aidvdkavad lqeaivsgeq elnlvdyvtk psvtaddpdl tkemdslnki akvtgnytin
      241 gntfqipret imdwlsykdg nttidedkvr syvtsigeqy ntstnsstfk stkqgevtvp
      301 agtlswtiqt daetealiea lkagedftrt piaqgstdag splfgntyie vdlknqhmwy
      361 ykdgqlvlet aiisgkpatp tptgvfyvwn keedatltge dyaspvdywm pidwtgvgih
      421 dsdwqteygg dlwktrgshg cintppgvmk elyskaevgt pvivi
//
LOCUS       WP_005230439             338 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter courvalinii].
ACCESSION   WP_005230439
VERSION     WP_005230439.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter courvalinii
  ORGANISM  Acinetobacter courvalinii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 338)
  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   5  (residues 1 to 338)
  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   6  (residues 1 to 338)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Acinetobacter courvalinii"
                     /db_xref="taxon:280147"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38136
     Region          22..200
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          83..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mvplahtavl knyldvsqql elnpyqllsd agiypaqlqd stqripvdka valleqsaql
       61 sgcesfglhm aeqrqladfg elslllsyqh tlrdglstiv qyrnlinnal emyieevght
      121 viiridvita steysrqaie lalgithrfc aallqkwqpl sihfthdaph dtamhqrmfg
      181 cslefgsefn givcnateld ktnphanttm lahakrflet dllhresess iifdirksih
      241 lllpmgrati dqvahthgvn vrtlqrrlea ahtnfsvlin dvrrnlvfry lknlnyslgq
      301 vsdilgysmp ssftrwfsse fgmspttwrn nnktviks
//
LOCUS       WP_005230825             641 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: VirB4 family type IV secretion system protein
            [Enterococcus].
ACCESSION   WP_005230825
VERSION     WP_005230825.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 641)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 641)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..641
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=72972
     Region          39..639
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mlnekeiqtl vkegfdlsfi ekiqpqggit fpedrmvagd gtyaclhiyq lakrpapfwl
       61 ttimnnqnsi tkfdlapidk evilsdidka mreldsqaee nrtrtqrnea vnefrslery
      121 aneinqgdev skmvdiriyv tadtqeelek evgdlrrslk amgyksvsyi gkqaqewlaf
      181 fqsyseqqne pgskegitvp ssaigggypf nhqflndtgg gylgktdtgg sfiynpymit
      241 alrksfssml lgksgmgkst llklieelly gkrtiirgfe knrdwykliq sqngkiydls
      301 gkegmlnpme platitdtsg kvidelnsyl qhratffnkv rflnpamrsv dildfgkimd
      361 dfyisygllp enytqnqkdi hiigldpsky ptvgefkqfv dhfvesgykd rvtdvkmvem
      421 enfqtvitsm ceqygsifng rstfrnidee dvlffdieti ghfddevykc mlytamnivw
      481 nqalkngrkq kialengdit pdevrffaff ldecqeilsp dtvfvvkqvv kflkemrkfs
      541 agaffatqsp qellpetssd dyiskikqvf elcnakfflq ldasvsetmk kamgnlltdg
      601 qyedlalleq gevivnlggn nnykiktdpd qeqlkrfagg h
//
LOCUS       WP_005230829             114 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Acinetobacter].
ACCESSION   WP_005230829
VERSION     WP_005230829.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 114)
  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   3  (residues 1 to 114)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 114)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..114
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12407
     Region          2..114
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mqpqmmggii qvnipdkatl qssympfvqg gglfvptkqa vkmgqevfvl atlpeqaqki
       61 pltgkviwis hkqthfkpqg faiqlagekg vyykneaekl lagskgldrp sytm
//
LOCUS       WP_005231007             344 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter courvalinii].
ACCESSION   WP_005231007
VERSION     WP_005231007.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter courvalinii
  ORGANISM  Acinetobacter courvalinii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 344)
  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 344)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 344)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 344)
  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   5  (residues 1 to 344)
  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   6  (residues 1 to 344)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Acinetobacter courvalinii"
                     /db_xref="taxon:280147"
     Protein         1..344
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39571
     Region          44..210
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <140..340
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mqkqqipvip aryylrliei ligthqydnh vlsalqqqla qtellsiqqi eqfiemglsl
       61 pntqdlafvl gknlklsshs lvgyalmtsp nlehalrlia qyfrlimpsf klsiqfpahq
      121 qkvellfepi lqmnkqclaf hieaiavafy ysllelagqq lqryqiylsi peptyqeryl
      181 slvkasfqfn yswlsgirvv idqqqlalpl pladahslkv veqrcqeqiq kiyhqgeive
      241 wvsmmlrqan qvptltecar vlnistktlq rylqqqgvef qelkqqiste raidllenss
      301 ltitaiayel gysnpanftr afnkvmgcsp qayrlkhqdq irsl
//
LOCUS       WP_005231103             139 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Enterococcus casseliflavus].
ACCESSION   WP_005231103
VERSION     WP_005231103.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus casseliflavus
  ORGANISM  Enterococcus casseliflavus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Enterococcus casseliflavus"
                     /db_xref="taxon:37734"
     Protein         1..139
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15884
     Region          27..126
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 msiivafhfy fniqiedkef gyliytisdi qklctpifle wkikkaflfg syarneatet
       61 sdldilidge gsllqnifdv irlksklssa lkkeidlttl rainaetnqk rnpllkenie
      121 adcvmiydfk tsdsfkvkg
//
LOCUS       WP_005231403             237 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Acinetobacter courvalinii].
ACCESSION   WP_005231403
VERSION     WP_005231403.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter courvalinii
  ORGANISM  Acinetobacter courvalinii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Acinetobacter courvalinii"
                     /db_xref="taxon:280147"
     Protein         1..237
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27886
     Region          1..>82
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 miqkayqpil kdlisvfare ftieldslyi ygsiakgkav vgqsdidicv vfkheitnld
       61 qkiaeikvkl itrypfipki dvdvgylkdv ldeknkkrwg awlkffctni ygrdlthffq
      121 eitidreviq ainqgyneei htyfelleik dkpqaellnl kkslikrmir llpltmrhie
      181 ewplalndti dqtvqvypqq kdrlyfllqe ldeptltnvi slnrlretyv wieahll
//
LOCUS       WP_005231903             105 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Acinetobacter].
ACCESSION   WP_005231903
VERSION     WP_005231903.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..105
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11824
     Region          2..105
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(7..8,26..27,35,38,40..41,43,46..47,49,57,62,69)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(26,57..58,60,87)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mqdtnelhrq ilevialipy gkvasygqva klaglpkhar lvgyvlkhld kqseipwyrv
       61 insqgkisvt rinqrgenvq qmlleqegiy llngkvslkt fgwqp
//
LOCUS       WP_005233625             181 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Acinetobacter].
ACCESSION   WP_005233625
VERSION     WP_005233625.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..181
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=19916
     Region          1..>74
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mknmhnkkwt lripqqgftl ielmvvvviv ailatiaips yqayarraia sqaqqevqkl
       61 aeqlerhkgk nfsylgfeps ylykdnngnl igyntsnaql nlplnssgta vkyivsvrdg
      121 tdatklltnt talgqrwaik aesqdpnnft flmtstgiqc knmtkanvsy tgcgtggmnt
      181 w
//
LOCUS       WP_005233419             394 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Enterococcus].
ACCESSION   WP_005233419
VERSION     WP_005233419.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            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="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43560
     Region          2..392
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msktiainag ssslkwqlyq mpeetvvakg iveriglkds iftikygedq kfeqiidind
       61 hevavkmlld qlielnilga ydeitgvghr vvhggedfpd svvitdevme riqalaefap
      121 lhnpanlmgi tafkkilpei isvavfdtsf hatmpkhnyl yslpleyyne fkvrkygfhg
      181 tshryvsera aemlgkpiee lkiitchlgn gasitavdgg ksvdtsmgft plagvtmgtr
      241 sgdidpavlp ylmekldlni demvdvlnkk sgllgltgis sdmrdleany dkeevkvayd
      301 vftdrirkyi ggyvttmngv daivftagig endahvrsev ikgmtwfgce ldadqnakrg
      361 eelvistees kvkvlliptd eelmiardve rlrg
//
LOCUS       WP_005234554             124 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Acinetobacter variabilis].
ACCESSION   WP_005234554
VERSION     WP_005234554.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 124)
  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 124)
  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   3  (residues 1 to 124)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..124
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14270
     Region          15..115
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mkpynknlkq asrdlrnnlt daekllwsrl rnkqilglqf yrqkpilnyi vdfycpaanl
       61 viecdgsqhf taegleadri rdealaqlgf kvfrfdngql veqldsvvev iyqyclnqla
      121 tesp
//
LOCUS       WP_005235633             715 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Acinetobacter variabilis].
ACCESSION   WP_005235633
VERSION     WP_005235633.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..715
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=78582
     Region          15..712
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mhlhttrlpm kstlscliac isqgiyaeep vtevqrlapi vveatrtdra iletpastyy
       61 lnqeqqnsln vnlsetlkgv pglqlnnren yaqdlqismr gfgarstfgv rgvrlyvdgi
      121 patmpdgqgq tsnidlnsld hievlsgpfs slygnssggt iltqsregqg pdsvtlgysg
      181 gsqnkgqtnl vlqggsenas epsyiisssy fdtdgfrdhs gahkvlnnak ltwdlddgsk
      241 inwinnyvki aaddpggltr dqwrenpkqv aanvllynar keieqvqtgl twnkpineln
      301 eiyamvyagq rsvtqyqstp kcayvkdtdv cipntiqlgk khaggvidfd rnfygadirw
      361 mgkevihnlk liagvaidgm tedrkgyqnf vgntlgvkge lrrnedntlw nadpyiqasy
      421 nfapdwtlda glrysnvhfk sedrylsngd nsgkttyekl lpsvalswki lpdlmtyasy
      481 aqgfetptft emaypadgsn dvlslkaaes etyelglksa nrfgdmtlaa fqtqtkndiv
      541 sagsdggrst frnadktlrk glelswnkdl wrdltaqasy syidatfdad ipaigtvaav
      601 ssgnyipgia knqafvslgw kpengfnagl dvrysdrifv ndinsevaps ytvaganvgy
      661 nwnvkdlsik tfarvdnlfd kdysgsvivn esngrfyepa egrnwsagls vtkqf
//
LOCUS       WP_005235002             883 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Acinetobacter variabilis].
ACCESSION   WP_005235002
VERSION     WP_005235002.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 883)
  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 883)
  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 883)
  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   4  (residues 1 to 883)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..883
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..883
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=99288
     Region          109..838
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mtqrldqihs sissnttisq qnissdllis afeqseitpt lektclkpaq ltriadpdki
       61 pastkrikpl nnflgqdrar asveagialp ysgynifavg taglgkrtmv krllqqhakt
      121 mqtpndwvyv nnfqnprqpi alefpagqgp kfqtmlhqsw qsilkqlerr fttenyhnri
      181 emirqetgde qqlalieltr egeeldlkli srndehcfvp ihlkddkvqe msqedlnals
      241 nkdraeiasn mrymdkkler lglhlgdled dardrvqvln rdiakqvvmp rveqmltkfk
      301 hvegleqylk qyaediinnv eivleqeedd ftpaqfsrvp arfqanvivt hkpnsgapvi
      361 fedfpthynl lghveqltqn gtittdftli rpgslhnang gflmleaeql leqpyawqgl
      421 kralksghlk lsslehmltl tgsisiepas iplnikvvll aepeiyyeil elepelgsif
      481 kiradftdtl qrndeneqay mqliadyvqs dkllpfdrsa lsalltdssr qaedqsslsl
      541 haltlgdlir eahhhafeag dkmvsekhin taldhrkyrl gylrelfwqd ltrgtqliet
      601 rghrlgqina lsvihyadve fglpsrltas vyqgggdild iersvelggs lhakgvllma
      661 sflkahfgre qtlhfsaala feqsygqvdg dsatvaelsa lisaisqlpi dqswaitgsm
      721 nqlgqvqpig gvnakiegff dacklqgltg kqgviiprqn mqhlmlrkdv iaaveegqfh
      781 ihaidniaqa leilmarpvg tmdkkgrysk nsifaavmeq leywqaiedg aefeeeprkk
      841 kkkkkkkkdk apikevltdp dtlaealvae skeleksedq aed
//
LOCUS       WP_005235727             721 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Acinetobacter variabilis].
ACCESSION   WP_005235727
VERSION     WP_005235727.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter variabilis
  ORGANISM  Acinetobacter variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Acinetobacter variabilis"
                     /db_xref="taxon:70346"
     Protein         1..721
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=80426
     Region          19..721
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mnmtkiplkk nplslmilsa fsghlyaett laqdsvqqld tivvtteqnt nsqkqteael
       61 asvsggtnfi sdqqlqhqrl gttadvfrlq pgiyaqspgn egakisirgs ginrtsgaha
      121 sgtyvmiddi pftgpggtay ellepwwidh vgvyrgangl kqgglslggt vnyksktgae
      181 qngselkyea gshgyqkyqf stgrqldkld yylavtgsqf dgiqdhaegd gkglafnlgy
      241 qispdietrf yaryreskhl tpgritqeql knnpgaandf nlavdakriq pgstwlantt
      301 twnlrddakl tgslayhhyp ldlressyrt nvdyedisar iqyekpyelf glehqgkvaf
      361 rstthrpnsg vtetirrdtt idgtlypadt vtrrytyrgs dnvlqfdqet qlndqfkldl
      421 glaaaythre sevtypvasp evsryewnfa prigltyqpn etlqwfanls rsiepahpwa
      481 mawsspyyfd ggvasgrvre piyldtqtan tlelggrgqs awgdwalsyy yskvknellt
      541 seliktyedg serpsepiav esnatptlhq gvelsldtlf yasqqgelrl rqaytlsdfq
      601 ykndplfgkn qlpgipkhly qaqlsyalnn glymglntey askmahdyan srfsddyqiw
      661 gidlgyapeh qswktwinfk nitdekyaav vipglndqga dvarsspgeg fstyagvsfk
      721 f
//
LOCUS       WP_005238302             276 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Acinetobacter].
ACCESSION   WP_005238302
VERSION     WP_005238302.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 276)
  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 276)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 276)
  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   4  (residues 1 to 276)
  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 276)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..276
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31662
     Region          51..273
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <175..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 msrrpreqvd ylhleelggl emlkasyyqq efsrhvhegf cigvieegaq rfyrtggnhv
       61 apqgdiilvn adevhtgssa vetgwryrai yptpevfyel trdlttvhgt apwfreavlh
      121 deglaqqfrl lfdlleqqnn tllkqtlfls tiawlvskys qvkpqivdls nakqrilnik
      181 elmasmpeqe fslaelaama nlsqwhflrq fkkhvglsph awliqarlqk sqrllrqgln
      241 lsevsqqcgf sdqshfsrhf rqtfgitpgg yiaylk
//
LOCUS       WP_005238416             164 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [unclassified Acinetobacter].
ACCESSION   WP_005238416
VERSION     WP_005238416.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..164
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=17772
     Region          1..118
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mlsrrltpsq gftlielliv vviiaifaai aipsyqvyar raqasqaqqe iqrlatelek
       61 hksrnfnyvd fstianaspk sdvvtlptga tgagiqytit vrdgddptkt lfangvngks
      121 wvitaqaana knwsfvlnsn gmrckrqdtt iafdcsgsgv eqtw
//
LOCUS       WP_005239800             159 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [unclassified
            Acinetobacter].
ACCESSION   WP_005239800
VERSION     WP_005239800.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..159
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17580
     Region          10..159
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 maeelvlqhg hkaeqyqsil pqiqaiiede tdvianlani caalkqqfgw fwigfylvke
       61 helvlgpfqg piactriakg rgvcgtawqq qqvvivpdvd qfpghiacss askseivlpi
      121 mkngtcvgvl didsdelnqf deidaeylkq lmpliekfi
//
LOCUS       WP_005241237             196 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [unclassified Acinetobacter].
ACCESSION   WP_005241237
VERSION     WP_005241237.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 196)
  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 196)
  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   3  (residues 1 to 196)
  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   4  (residues 1 to 196)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 196)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..196
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22310
     Region          1..191
                     /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"
ORIGIN      
        1 mpqlkialid ddqaraeylk acliehgfdv vacftldhfn ifklehlqad villdmdhph
       61 rdviescvss fdlptvlftk ntdketikqt idagitayiv dgiepsrlht ileisieqyk
      121 khkklkcdlk daqtkladrk diekakvllm hlhglpegta fqllrknams hrmtigemar
      181 rlldaqqlln nqlkde
//
LOCUS       WP_005242099             360 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Acinetobacter].
ACCESSION   WP_005242099
VERSION     WP_005242099.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 360)
  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 360)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 360)
  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   4  (residues 1 to 360)
  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 360)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..360
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41042
     Region          29..218
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          265..346
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mrdpfglfqe tisvsyahll leivqdyavd tetvlsgtgl rlaemkqada kmsahqwskl
       61 vvnalkltdn prlgieygfk lrptshgalg faflsctdve talslcqqyf ctriqnftpe
      121 whiendfvyv hlddvhpvkl ggaeqsdqlr sfliecllfg aihflslfse kiaencevfv
      181 dwadsqnyks vdlsqikiqf nqqrnglrfp khylqcknsn adqvafqqal lycendklkl
      241 lkestrdlqk sirsellyka gnayptlpii aqrlnmsert ikrhlqaqgt tflqilaevr
      301 fsqakkllqq pqysvqdvaa lvgyeeatnf irafkkmfge tpsqyrksyl sktdssnitf
//
LOCUS       WP_005242846             363 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Acinetobacter].
ACCESSION   WP_005242846
VERSION     WP_005242846.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 363)
  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 363)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 363)
  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   4  (residues 1 to 363)
  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 363)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..363
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41586
     Region          51..232
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          284..358
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mryptglktl fcggqnglmp irssdkndqq qfipptilas lihyaeqqqw dyaawfensg
       61 ldtaqiqqtq gvvrfsqlcd vvrqamttyq qpnlglklgs seglismgil gfamqscktv
      121 adaldialry hrisgsvlni dfsihadlce levtepypcn elkaffydel fssiitclna
      181 mlgdhddvis lelsylpsey qqqyselfgc piqfnrdkni mrfsssllqr slknyspany
      241 ataiqiceqs lkeidqlnqv gyvhlldhli eqhlperfem qhaaehlris erhlrrqlla
      301 eglsfqqirq nvlerkakql leqnlsmsei slqlgfselr efrrafkrwt gqapsiykqe
      361 ahf
//
LOCUS       WP_005243355             340 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005243355
VERSION     WP_005243355.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 340)
  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 340)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 340)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 340)
  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   5  (residues 1 to 340)
  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   6  (residues 1 to 340)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..340
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38784
     Region          25..209
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          89..340
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mqhhwdfprh inavrvllav gqshgltvtq clknsditle dlskihhein vqqefqvlrn
       61 lidllgseip igveaglrhh tttfgawgfa ilssptieaa lhlalrylql ssffcklets
      121 kvgehtvitf nhdslpqdlv yflaerdytt imslqkdilp lslpvmeinv alptpvyadr
      181 fveltgyain fdqprsciii etrllnlplp qadhftrtyy ekecqnlwir rstigkfsqk
      241 irnilllkps qmpnieeiat qleitvrmlq rhlasegity erlvsnired laedllttte
      301 ltieeiaaql gyseasafsr afkrwknvsp kyfranssql
//
LOCUS       WP_005243688             253 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Rhodococcus opacus].
ACCESSION   WP_005243688
VERSION     WP_005243688.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus opacus
  ORGANISM  Rhodococcus opacus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Rhodococcus opacus"
                     /db_xref="taxon:37919"
     Protein         1..253
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=27409
     Region          106..246
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mprsavpntg siittirtkw pwilagllvv vlvtmltpdp ddtlaagtgp vapsevtdaq
       61 qiqtafaqls tlevkgrapk tgydrelfga swtdnvsvdl grngcdtrnd ilrrdlvdit
      121 srdrtrncvv qsgmlrdlyt gtiiaftrgt ktsdavqidh vvalsdawqk gaqlldtqtr
      181 adlandprnl qavdgptnqr ksdadastwl pplaayrcty varqvevkva yrlwvtpper
      241 damaavltgc gar
//
LOCUS       WP_005244177             354 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SPOR domain-containing protein [Acinetobacter].
ACCESSION   WP_005244177
VERSION     WP_005244177.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..354
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39277
     Region          <74..>250
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          272..346
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 msmnnkqrwm ggvvllgggv llaalllkgn qeieqdqtha pvthpipkte skpktaqpaq
       61 dsemvslqpl avdvetekrl leeqrrsrek avaeqearaa eflkmqqqae aaaarkaaee
      121 yaainarraa aqessdnipp elvedekaka qrlaedkrka dekkrieqqk ndqqksdtdk
      181 klaedkrkae aekkaaeekr kaeadkkaae dkrkaeaekk aaeekrkaea dkkaaedkrk
      241 aeadkkaaed krkaeaekka eaekardlme ngdkkwmvqv alaanqanad avvsklrakg
      301 ykvttsptsk girimvgpak drdiadatrk kitsdeslnm ksawvidwvp ldqr
//
LOCUS       WP_005244190             340 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005244190
VERSION     WP_005244190.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 340)
  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 340)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 340)
  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   4  (residues 1 to 340)
  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 340)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..340
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39500
     Region          84..340
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          262..339
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 msvkiiigyl rlfnrvlqqe qvdlskvvap elwqafqacl enpdekdfdv eryalllqaa
       61 qphftrpitl vlaehanlqd lglmgylast sidlqqalql lqryyslvfk qtnleqldvq
      121 qypeyiqiiw sasysdyrem yelnlalifk iaqsivqdal vppqiiqfgy aphtalyhfe
      181 kfygcpiqiq qgqyairfsn qilkaksiaa dqqlnhvlst qaqqslnsvs sfevqqqqfr
      241 qkihafieqg vlqqeellqr yvakrlhcse rtlqrqlkaf elnfqdvldq yrleqsklyl
      301 qqgksfseia erlnyadqsa fgrafkrwtg vtpkqflksl
//
LOCUS       WP_005246032             140 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Acinetobacter sp. CIP 51.11].
ACCESSION   WP_005246032
VERSION     WP_005246032.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CIP 51.11
  ORGANISM  Acinetobacter sp. CIP 51.11
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Acinetobacter sp. CIP 51.11"
                     /db_xref="taxon:1144670"
     Protein         1..140
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15573
     Region          1..140
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mslfllflsa fgaatllplq seavllgllv qnkqhavlli avaslgnilg scvnwylglk
       61 iehyknkkwf pvsadkmlka qktyqkygyw slllswvpii gdpitliagl lkenfarfll
      121 mvsiakigry lfvyaafamf
//
LOCUS       WP_005244206             345 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Rhodococcus opacus].
ACCESSION   WP_005244206
VERSION     WP_005244206.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus opacus
  ORGANISM  Rhodococcus opacus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 345)
  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   6  (residues 1 to 345)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Rhodococcus opacus"
                     /db_xref="taxon:37919"
     Protein         1..345
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37568
     Region          22..218
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          98..343
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtartipadf vrrslelsar sgvdlspals aagittasle dplarltptq vtaftqavwq
       61 itgdelfglg papvprgtfr lvclalihta dlsaalerma dilralpslp alhigpgvng
      121 gtrmtidirp aaaerstedv qssleatrvt tdfllillhr faawlvgkrv rllavelpyp
      181 aplpqlaeny dhifgvpvtf dsdipavefd navmrapiiq teetledylr esptllmser
      241 dydstasaqv rrvlelgmkg rtstaediae mlsisvphlr rllrqdgtsl nqlreevlrd
      301 aavaglrrge tvedlsarlg fsepsafrra fkrwtgstps syrga
//
LOCUS       WP_005246282             338 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Acinetobacter sp. CIP 51.11].
ACCESSION   WP_005246282
VERSION     WP_005246282.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CIP 51.11
  ORGANISM  Acinetobacter sp. CIP 51.11
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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
REFERENCE   4  (residues 1 to 338)
  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 338)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Acinetobacter sp. CIP 51.11"
                     /db_xref="taxon:1144670"
     Protein         1..338
                     /product="CmpA/NrtA family 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=38300
     Region          2..249
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mstlekteln igyiplldcv ailwaekqgy faeqgltinl iheaswsslr drlaygflda
       61 ahclsamlpa aalgtdqlqv alqtplvlsv nqafislrqd lcyelciqpe ddeqntskkl
      121 vqalqqnhsi nlayvykysi hhyclkewla ltdpqlakni qlmtspppsm vkgiaeqvfd
      181 gfcvgepwni qaklegysfi vaasqnvipk vadkvlamtq ewaeqhpftv eavvkavqka
      241 qddlkqrpdl sevwdmlvdy qiiqfecsaq rhvydfykik niirnfvgks aqpkvddfiw
      301 llqqmqkwed iemtaaekkq iaeqciyslq sqhadiig
//
LOCUS       WP_005246313             721 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Acinetobacter sp. CIP
            51.11].
ACCESSION   WP_005246313
VERSION     WP_005246313.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CIP 51.11
  ORGANISM  Acinetobacter sp. CIP 51.11
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Acinetobacter sp. CIP 51.11"
                     /db_xref="taxon:1144670"
     Protein         1..721
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=80566
     Region          19..721
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mhmtkiplkk splslmilsi vsghlyaeta vepdnvqqln tivisaeqna npqqqyqkel
       61 aqvsggtnfi geqqleqqrl attadvfrlq pgiyaqsagn egakisirgs ginrtsgaha
      121 sgthvliddi pftgpggtay ellepwwidh vgvyrgangf kqgglalggt inyrtktgad
      181 qdgselkyem gshgyqkyqf stgrkldqmd yylaltgtqf dgiqdhaegd gkglafnlgy
      241 qispdietrf yaryreskhl tpgritqeql kndpeaansf nlavdakriq pgstwlantt
      301 twnlqddakl tgslayhhyp ldlressyrt nvdyeditar fqyekpyqfl glehqgrial
      361 rstthrpdsg vtetirrdtt idgtlypadt vtrrytyrgs dnvlqfdqet tlndqfkldl
      421 glaavythre sevtypvasp evsryewnfa prlgltyqpn esvqwfanls rsiepahpwa
      481 mawsspyyfd sgvasgrvra piyldtqtan sfelggrgqs gfgdwalsyy yskvknellt
      541 semiktyedg snrpsepiav esnatptihq gvelsldtpl hesqygelrl qqaytlsdfq
      601 ykndplfgkn qlpgipkhly qaqlsyalnn glyiglntey askmahdyan srfsddyqiw
      661 gidvgyapeh qswktwinfk nitdekyaav vipglndkga dvarsspgeg fstyagvsfk
      721 f
//
LOCUS       WP_005246994             124 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Acinetobacter sp. CIP
            51.11].
ACCESSION   WP_005246994
VERSION     WP_005246994.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CIP 51.11
  ORGANISM  Acinetobacter sp. CIP 51.11
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 124)
  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 124)
  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   3  (residues 1 to 124)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Acinetobacter sp. CIP 51.11"
                     /db_xref="taxon:1144670"
     Protein         1..124
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14547
     Region          16..119
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mnkkfdpqll qfaksmrhtt tdaenlmwql lrakrfmnlk frrqhviapy ildfycheig
       61 lvieldgsqh gtddaieydv ertkfleavg ltvvrywnhd vlgrtdvile hlwqvctelk
      121 qtsp
//
LOCUS       WP_005247551             264 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Acinetobacter sp. CIP 51.11].
ACCESSION   WP_005247551
VERSION     WP_005247551.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CIP 51.11
  ORGANISM  Acinetobacter sp. CIP 51.11
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acinetobacter sp. CIP 51.11"
                     /db_xref="taxon:1144670"
     Protein         1..264
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30060
     Region          36..261
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mpnqnsqtss qttdssnpek kryyepapqd ididnfrkvi esrrsvrkft kkpipvevld
       61 acldlsllap nssnlqpwtf yvvqnpgkkk rlvkacmsql aaktaseliv ciartdride
      121 makrnvnefp fpeappaikk yykyipynyk tgymnafgnf kkvafkvart ldkqmpvsaf
      181 spadaklwat kttalacenl vlalraygfd scmmegfdep mvreilklnd eqypvmviga
      241 geraedgvff pqyrfdrelf iqki
//
LOCUS       WP_005247915             722 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Acinetobacter sp. CIP
            51.11].
ACCESSION   WP_005247915
VERSION     WP_005247915.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CIP 51.11
  ORGANISM  Acinetobacter sp. CIP 51.11
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Acinetobacter sp. CIP 51.11"
                     /db_xref="taxon:1144670"
     Protein         1..722
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=80134
     Region          15..719
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 myqspkfpfv rstlscliac agqniyaend tqevqrldti viqatrtdre rlttpasvyy
       61 lnqeqdnsln vnlsetlkgv pglqlnnren yaqdlqismr gfgarssfgv rgvrlyvdgi
      121 patmpdgqgq tsnidlnslg hievlgggfs slygnssggt iltttregqg adsielghsa
      181 gsqnkgqtkl vlqggsenas epsyvisssy fdtngyrdhs sahkvlnnak ltwdledgsk
      241 inwvnnyvki eaddpggltr pqweanpkqv vgnvtkynar keieqlqtgl twnkpindqh
      301 elygmaywgq ravtqyqsip kcayeentdi ckpntvqlar nhpggvidfd rqfygadlrw
      361 tdrdvlpntk liaglavdam tedrkgylny vgntfgvkge lrrdedntlw nadpylqisy
      421 nfmpdwtlda glrysnvhfk skdkflangn nsgktdyqkl lpsaalswqi fpelmtyasy
      481 aqgfetptft emaypasgsf dkalnlkaae setyelglks anilgdftva vfqtktkndi
      541 vsagndngrs tfrnadktlr egielswnkn lwrdltaqas ysyidatfda dipeilnqng
      601 siavsrvesg nyipgiaknq aflslgwkpe kglhagldvr ysdkiyvndl nsdaaprytv
      661 aganvgyhwk mqdwavntfa rvdnlfdkdy sgsvivnesn nrffepaegr nwsaglsvtk
      721 ef
//
LOCUS       WP_005248313             211 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Acinetobacter].
ACCESSION   WP_005248313
VERSION     WP_005248313.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..211
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=23563
     Region          1..>76
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkspfsqnks qlgftlielm vvvvivalla aialpsyqiy vqrshlaqaq qemqklaeql
       61 erhkaknfsy kgfeasylyr dkdgvlnsnf dtakqqislp ihstnpsyrl siigfytvse
      121 fekdeegnvt stikdpeikt dllnkkidfd kssqsdmfai gsswaikaes ldqknyglll
      181 nslgakcmnk kdytkvsyts cgnegdgaes w
//
LOCUS       WP_005249068             227 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Rhodococcus].
ACCESSION   WP_005249068
VERSION     WP_005249068.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (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   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..227
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=24660
     Region          <26..88
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          <68..223
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 myterrsvfp gavvwqktaa ggeaailpdg cmdliwmngd vvvagpdsrp yltrsregdr
       61 yvglrcspgi lpdllgvpae eltnlrvpla elltdratre flgriaddae pgraleefar
      121 srrllgpppd sripaiarll eqqtsvreva drigvgerql hrlcrrqfgy gpkmlarilr
      181 lqsalglads sipaaqaagm agfadqahli reaheltgrt fgqlvtv
//
LOCUS       WP_005249165             690 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Rhodococcus opacus].
ACCESSION   WP_005249165
VERSION     WP_005249165.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus opacus
  ORGANISM  Rhodococcus opacus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 690)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Rhodococcus opacus"
                     /db_xref="taxon:37919"
     Protein         1..690
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70488
     Region          7..684
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 msaivdrdlt alfdprsvav lgasndetky gnwisvqalr mtgsrsvhlv nrrgerilgh
       61 pslrslseld ervdlvvitv paqgfeeavd dalaagatai vgvtagfael gaagkavqdr
      121 vvervraaga vllgpnclgv ldsstaltla snplpagrva llsqsgnmal elsqflearg
      181 hgfsrfaslg nqadlgaadl irscvehddt dliavycedf gdgrafvdaa aqasragkpv
      241 llltvggsea svrgaqshtg sltsdsavid aacraagvyr vssprqladv aatllgygpa
      301 evrrvgvvad ggghagvasd vveaagltvp eftadvssal rallppsagv tnpvdlagag
      361 eqditsfvsv ldtilqspai dsvlltgyfg gygsygenla raevdtaram aetarthgkp
      421 vvvhtmhpds aaarvladsg vpvfraveda agafgviaet aapqhpagge sepaepvtsd
      481 aywdarelfr gagvefpdaq lvrtcaeava aadsvgypvv lkamgllhks dsggvalgle
      541 taqqltdaft rmdgslaapa ycvesmadls egvelivgvq tdprfgpvam vglggiftev
      601 ladvafalap vdaetargll dtlrasallr gvrgrppinl daaadaiaav tavatahpei
      661 aeleinplfv tpkqalglda rivlntsntn
//
LOCUS       WP_005254638             625 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Acinetobacter sp. CIP 102136].
ACCESSION   WP_005254638
VERSION     WP_005254638.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CIP 102136
  ORGANISM  Acinetobacter sp. CIP 102136
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 625)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Acinetobacter sp. CIP 102136"
                     /db_xref="taxon:1144665"
     Protein         1..625
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68724
     Region          6..625
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mqnnvskpav paltlaalgv vfgdigtspl yalkesfhat rglpinelni lgilslifwt
       61 itlivslkyv lvimradnng eggimallal nlrqkglsrg krlaiiilgf igaslffgdg
      121 iitpaisvls aveglsvaap sfdrfiipis igilialfav qkhgtammgk ffgpitllwf
      181 lsigaigims iiqspfvlal fsphwaflfv innplisffv mgavvltvtg gealyadmgh
      241 fgilpiklgw flivlpclml nyagqgalll rdpsaitnpf ylllpsally pmiilataaa
      301 viasqalisg vfsmakqaiq lgylprltvl htsaseigqi yipllnwllf isitililif
      361 esssklagay glavtvtmfc dtllvaflay sywkwktwkv llfiipfafi dlvllssnll
      421 kvliggwvpv viavivftlm mtwkkgreil qdklqketlp lnvflehleq tgqkvsgnav
      481 fltgtpqvvp hallhnlkhn kvlhernflv tiktseipyv deakrivtev lengffriti
      541 hygfkeepnv phslkqafsv ldleydlmnt sffvsrerli pslsskmstw reklfvamqk
      601 ntspvsdfyk ipsnrvvelg sqiei
//
LOCUS       WP_005255111             142 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Acinetobacter vivianii].
ACCESSION   WP_005255111
VERSION     WP_005255111.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter vivianii
  ORGANISM  Acinetobacter vivianii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 142)
  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   2  (residues 1 to 142)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Acinetobacter vivianii"
                     /db_xref="taxon:1776742"
     Protein         1..142
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16114
     Region          78..140
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mifrqasskh rlfllmilcv gcishlnaqq fdqsyqqwka qqqardqqla nqannnyyls
       61 rpasqqnikq vssslniqgd kislnqanlq qlqtlngvge kkaqtimeyr qknggfksid
      121 elmnikgigp klfeknkarl ml
//
LOCUS       WP_005255255             159 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Acinetobacter vivianii].
ACCESSION   WP_005255255
VERSION     WP_005255255.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter vivianii
  ORGANISM  Acinetobacter vivianii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Acinetobacter vivianii"
                     /db_xref="taxon:1776742"
     Protein         1..159
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17496
     Region          10..159
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 maeelvlqqg hkveqyqsil pqiqaivede sdvianlgni caalkqqfgw fwigfylvkg
       61 nelvlgpfqg piactriakg rgvcgsawqq qqvivvpdvd qfpghiacss dskseivlpi
      121 mkngecvgvl didsdelnqf deidaeylkq lmsviekfi
//
LOCUS       WP_005255842             237 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Rhodococcus opacus].
ACCESSION   WP_005255842
VERSION     WP_005255842.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus opacus
  ORGANISM  Rhodococcus opacus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Rhodococcus opacus"
                     /db_xref="taxon:37919"
     Protein         1..237
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=25226
     Region          93..233
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mrhrprtafl algaatvigl tgcsaiadad pgtgslggap aapapvfdaa palakldtla
       61 vkgrapktgy treqfgpsws ddnsvegghn gcdtrndilr rdlvdltykt strdcvvatg
      121 tlhdtytgtt iafvrgqdts tavqidhvva lsdawqkgaq qlspeqrrdl andprnlqav
      181 dgptnskksd sdaaswlppn kayrctyvsr qidvkalyrl wvtqaekdam sqvlhsc
//
LOCUS       WP_005256017             278 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Rhodococcus opacus].
ACCESSION   WP_005256017
VERSION     WP_005256017.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus opacus
  ORGANISM  Rhodococcus opacus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Rhodococcus opacus"
                     /db_xref="taxon:37919"
     Protein         1..278
                     /product="formate/nitrite transporter family protein"
                     /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=29567
     Region          2..263
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msyvkppdlv tamidagask vlmstrdtvi raymggaila lgavfavtvg vqtgqpliga
       61 llfpvgfcil yllgydlltg vfvlapmawf dkrpgvtgfg vlrnwglvfl gnflgaftva
      121 vmmaivftyg faadpnqige aighigesrt lgyaeygasg mltlfvrgvl cnwmvstgva
      181 gamiatdvhg kviamwmpvm lffamafehs vvnmflfpsg lllggdftll dyliwneipt
      241 vlgnmigglv ftglalylah rhtsgtpvad reaeletl
//
LOCUS       WP_005256409             416 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Acinetobacter vivianii].
ACCESSION   WP_005256409
VERSION     WP_005256409.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter vivianii
  ORGANISM  Acinetobacter vivianii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Acinetobacter vivianii"
                     /db_xref="taxon:1776742"
     Protein         1..416
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=48035
     Region          3..289
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          289..387
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mtvrffhtsd whlgqffynh srhyeheqfl awlleqikqk qphalliagd ifdvinpssq
       61 aqkqlyqfla dahefaphmq tlmiagnhds gyrieqvepl lakynaktvg virwnedktl
      121 dlerlilpiy deqkqivawc ialpflrsae itgfnehttn sqnaiaylhq qlieeakrrk
      181 sddqalilms hahmqggets dserpiiign eealstslfd dsidyvalgh lhkpqkvqhp
      241 hirysgspip lsfseinykh qvvevtvdst qpenkldfea laiprsiqlh kikdeltavm
      301 qqlknlpsgp ienidhreyv dieyhtaipp qpnlrqqfed alpkdryrlv risrqyllne
      361 snaenkqsis lepptpeklf qqiwekkgyh addevtkdfl slvneaqkkl eddqss
//
LOCUS       WP_005257692             336 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Rhodococcus opacus].
ACCESSION   WP_005257692
VERSION     WP_005257692.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus opacus
  ORGANISM  Rhodococcus opacus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 336)
  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   6  (residues 1 to 336)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Rhodococcus opacus"
                     /db_xref="taxon:37919"
     Protein         1..336
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36990
     Region          21..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          87..332
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkplaryasl ngylelcrsl gvdpvplmrs vgldpsglal qdrwipaaai ahlleqsvea
       61 sghedfgarl aerrqfsnlg plslvvreep dvrsalrvlt rythtyneal qtrmsesngl
      121 atlrveldvg eatetrqsve lavgvlhrll rgflgggwkp lavcfphpap adtathrrlf
      181 gpvvnfdhef agividagdl aepnkmsdpl lrrytqqlle sweasddvti vsrvreliel
      241 llptgrcsve qvarslgvdr rtvhrrlaes getfstvlda trvelaermv anprlsltei
      301 advlafsaps nfsrwfsgrf gcspsrwraq ragdsg
//
LOCUS       WP_005257781             292 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter vivianii].
ACCESSION   WP_005257781
VERSION     WP_005257781.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter vivianii
  ORGANISM  Acinetobacter vivianii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 292)
  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 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 292)
  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   4  (residues 1 to 292)
  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 292)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Acinetobacter vivianii"
                     /db_xref="taxon:1776742"
     Protein         1..292
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32761
     Region          24..169
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          202..283
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mmndqklinl flklvqkegf fataidgivl mrvdhntppi avlqeptlvf vlqgqkrgyi
       61 gtetysfqqg eclivsvsmp fdcdtiasae apmiaismkl eadtvnella ktyfenyqfk
      121 plttgmsviq ydqtissvln rllqtltseq dvlvlgdqik rellyrviqh agadalkglv
      181 aqgnlrpiyk iceyiqhhft ekltvemlae qanmstsafh kafkqvtqhs plqylkivrl
      241 hkakqllqna dqsvaqaaya vgyqsssqfs refkkqfgfp pkhaesntet es
//
LOCUS       WP_005258670             334 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter vivianii].
ACCESSION   WP_005258670
VERSION     WP_005258670.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter vivianii
  ORGANISM  Acinetobacter vivianii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 334)
  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   5  (residues 1 to 334)
  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   6  (residues 1 to 334)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Acinetobacter vivianii"
                     /db_xref="taxon:1776742"
     Protein         1..334
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37977
     Region          23..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          96..334
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mqqtatalts wvkaiqkale kagcdsksli eqagldiqal ndpnaryslq qtarlwqlat
       61 aatqdscfgl kvanqvnqht fhvlghslat sttlkemfir iiryfrlvtd ipelefygkd
      121 qnhyfiihvp devqyesida fisvfirscr alqgslfspl qielrrseps dletyrsiik
      181 aplifnapqd mivfdtatie lpleganpil sqeydeiimr ylarfdkeni qarikvkiie
      241 nlaageiqqq eiakslglst rslqrklsle ntsyseildk trqelassyi knnsysitei
      301 ayilgftdvs sftrafrrwt dcsplhyren lsks
//
LOCUS       WP_005258080             411 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [Rhodococcus].
ACCESSION   WP_005258080
VERSION     WP_005258080.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 411)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 411)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            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="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44198
     Region          7..405
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mvenlssvdr advykgerla gslvreggdv vfrydtaylq dpgapqvawt iptsstevra
       61 sggsvppffa gllpegirlr gavaatktse ddhltilmav gadtigdvrv lpagvpppet
      121 apmfdpdave rqdlralfeh msgheavkld ptslpgvqak vsaqmystpi atekgpailk
      181 lsppqgypql venehffmgl aaqcglpvad hqlvrdgkgn agllvarfdr rvdpsgrvir
      241 tpqedacqvm gmfpaakyrl ktesvitala gvcergggsa rvatlellrl vaysyaigng
      301 dlhgknfsvq laesglwsvt paydllctqp ylgwrdpmal dfygkankln rrhfvesggr
      361 lgvperavtr mldgvrkgig rgieeietig ftakenallr tlmerrsdel g
//
LOCUS       WP_005260374             209 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Rhodococcus].
ACCESSION   WP_005260374
VERSION     WP_005260374.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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   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   3  (residues 1 to 209)
  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   4  (residues 1 to 209)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 209)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 209)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..209
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22767
     Region          15..207
                     /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"
ORIGIN      
        1 mvamnapqqq gvpsqprrvv vaedealirl dlvemlreeg ydvvgeagdg qaavdlavel
       61 kpdlvimdvk mprrdgidaa seiaakriap vviltafsqr elverardag amaylvkpfs
      121 tadlvpavel aasrfkevta lereisdlse rletrkiver akgvlmekqs ltepeafkwi
      181 qraamdrrst mkavaqvvle tlggeapts
//
LOCUS       WP_005258723             625 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Acinetobacter].
ACCESSION   WP_005258723
VERSION     WP_005258723.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 625)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..625
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68642
     Region          19..625
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mqstvkkaal patalaalgv vfgdigtspl yalkesfhaa hglaiqpenv lgilsiifwc
       61 lmliisikyi aivmradnng eggimallal nlrkakitdh kkiyliaigf igaslffgdg
      121 iitpaisvls aveglsiatn aldpfiipia lvivitlflm qkhgtafvgk ffgpitlvwf
      181 lslgllgias viqtplvlgm isphwaiqfi fthpvqsffi mgavvltvtg gealyadmgh
      241 fgpqpirlgw fsvvlpclvl nyagqgalll rnpaaienpf yllvpswaly pmiilatmaa
      301 viasqavisg vfslarqaiq lgylprlsik htsdleagqi yvpflnwlll vaivvlilif
      361 qtssnlasay glavtltmlc dtilvavfiy yawkwslpkv llliipffll esvlvaatsl
      421 kmfsggwvpl liggiaitil mtwkrgrelt faklehdtls lelfvksign svlrvpgdav
      481 fltgtpnvvp hsmlhnlkhn kvlhernilv tvvvedipfv sheerisvet ldehfyriki
      541 fygfkdepnv pqalvqayeq lefeydvmqi sffisrdriv hsvgdgmspw rerlfismqr
      601 ntspvsdfyq iptnrvvelg sqiei
//
LOCUS       WP_005261821             263 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Acinetobacter].
ACCESSION   WP_005261821
VERSION     WP_005261821.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   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 263)
  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 263)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..263
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28766
     Region          23..90
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          191..252
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mevnpnspsn hssvapnalg niqrpgeylr qirinqqrnl edvakelnip lktltaleqd
       61 eykslpeatf ikgyyrtyak flgvdassii qrfdeiytnd tgllpnhaln nspikimgkl
      121 pgskrdrnrk wlkrifitlv lllilgalfa miqnwsssns qnssevsgvg asnveilnld
      181 tgaalsgdql kldfnrptsv hivdsagnvl atgrqasslq lngeapfqir lddasavsls
      241 lnnenislsp ytvngkaefr lsp
//
LOCUS       WP_005262131             721 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Acinetobacter sp. CIP 101966].
ACCESSION   WP_005262131
VERSION     WP_005262131.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CIP 101966
  ORGANISM  Acinetobacter sp. CIP 101966
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 721)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 721)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Acinetobacter sp. CIP 101966"
                     /db_xref="taxon:1144662"
     Protein         1..721
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=82089
     Region          19..>154
                     /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          <151..233
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          477..710
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cl29561"
                     /db_xref="CDD:453023"
ORIGIN      
        1 mgsievrnpl lskklkrtet rlliiddnqi rynqirdllt shdyqvdavl lddlqsfekq
       61 lnfkwdllif graydlkyeq algivrlsqq pdlpmillkp dnyqaeqyaq yirkgvydil
      121 nfdylerfyv glvralsfsr lsqsqqhlmt eletaqiqaq slvddsnrav atiqegihiq
      181 anadylklfg lqnedeiigl plldllqpsd lndfktrfkk isqgqfdlgr veiqslnphv
      241 sasnplklef lpstaeedav qisidtqsqt vssnktpgkp svfhslkrel nkqpapvnal
      301 vtfslsaydp ellqsdwttf sgyfeavkef lmeqthislf kleydvvvgm lqadskaile
      361 sklislnals kpqlitvgqk tfplnlrlgy vmleqglqde mhcntligqa fstslpqaea
      421 vaefkldipa slsspvavem psidfsvaet pvasptlaav spavtsipsa tpsilkalse
      481 clergeihlk yqqlydkedt rlytyevtsg fifenkwqdi ssllelhedd elsikldrwi
      541 lveaskqlhn fitqypdasl ivnlnravlf kdrtfpefis klitiirskv khplilqfse
      601 edillnqqda qkylrvlyeh galialrdfg qsmysqnllr eleldgvslh ssltnmlnkd
      661 teieqlqeki tsyneikpln ilirelndmt lfanawnvda rfiqgnyfqk kldhlidvqe
      721 h
//
LOCUS       WP_005262405             690 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Rhodococcus opacus].
ACCESSION   WP_005262405
VERSION     WP_005262405.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus opacus
  ORGANISM  Rhodococcus opacus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 690)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Rhodococcus opacus"
                     /db_xref="taxon:37919"
     Protein         1..690
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70425
     Region          7..685
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 msaivdrdlt alfdprsvav lgasndetky gnwisvqalr mtgsrsvhlv nrrgerilgh
       61 pslrslseld ervdlvvitv paqgfeeavd dalaagatai vgvtagfael gaagkavqdr
      121 vvervraaga vllgpnclgv ldsstaltla snplpagrva llsqsgnmal elsqflearg
      181 hgfsrfaslg nqadlgaadl irscvvhddt dliavycedf gdgrafvdaa aqasragkpv
      241 llltvggsea sirgaqshtg sltsdsavid aacraagvyr vssprqladv aatllgygpa
      301 evrrvgviad ggghagvasd vveaaglavp eftadvssal rallppsagv tnpvdlagag
      361 eqditsfvsv ldtilqspai dsvlltgyfg gygsygesla raevdtaram aetarthgkp
      421 vvvhtmhpds aaarvladsg vpvfraveda agalgviaet aapqhpagge sepaepvtsd
      481 aywdarelfr gagvefpdaq lvrtcaevva aadsvgypvv lkamgllhks dsggvalgle
      541 taqqltdaft rmdgslaapa ycvesmadls egvelivgvq tdprfgpvam vglggiftev
      601 ladvafalap vdaetargll dtlrasallr gvrgrppinl daaadaiaav tavatahpei
      661 aeleinplfv tpkealglda rivldtsntn
//
LOCUS       WP_005262965             434 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Acinetobacter sp.
            CIP 101966].
ACCESSION   WP_005262965
VERSION     WP_005262965.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CIP 101966
  ORGANISM  Acinetobacter sp. CIP 101966
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 434)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Acinetobacter sp. CIP 101966"
                     /db_xref="taxon:1144662"
     Protein         1..434
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=49798
     Region          24..415
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mdqyctlqiy qedewldcai veivgqqqtg wqaatrtsyl feyaisymdl sdghalayhl
       61 pvnvqntlqs twpaflmdll pqgygrkell rqlnfsentq eqadwallka gagnpignlr
      121 ikeayewlqg qfpvqqnhgf sldqvverqe nfieslasyg lfiagssgiq gewpkllltq
      181 ghddlfyldh tltdhqvkqh wlvkfsrgsd qnldkilmhe alymkiaqyl glrvhqelel
      241 hgktlfiprf drkvsdgkve riaqesiasl ggkagfgvrm nhnqicsllm qcctepkqei
      301 feylkrdlan valgnkdnht rntaiqrfnk giiqltplfd fapmwlhpdg iarttrwkrd
      361 dhggmpiwhs vieqiaestm idpkeikavl ieqlplyqgl lehmqhlqla peilensqyr
      421 idnicqqlee lnhg
//
LOCUS       WP_005263692             262 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: hydroxypyruvate isomerase family protein
            [Acinetobacter].
ACCESSION   WP_005263692
VERSION     WP_005263692.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 262)
  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 262)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..262
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29447
     Region          1..257
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 miklavnlsm iftevplier falaraqgfn hveiqfpyel tigqiqnqls thqlnlclin
       61 vpagdlmqgg hglagipgqe iefrhaveqa iqyattlnvp rvnilagkqp ldcdllpcln
      121 tlasnlkmac smllehqiep vfemingidm prfliqnvaq aqemleavhh palkmqydcy
      181 hmamigedvl etlqeniasi ghiqfadcpg rhqpntgsir yhdifqwlkh sqyqgyvaae
      241 ykpsghsnds fdwkaeffpe hd
//
LOCUS       WP_005264664             284 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Rhodococcus opacus].
ACCESSION   WP_005264664
VERSION     WP_005264664.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus opacus
  ORGANISM  Rhodococcus opacus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Rhodococcus opacus"
                     /db_xref="taxon:37919"
     Protein         1..284
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29692
     Region          1..257
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mlidlhthst asdgtdspad lvraagaagl divaitdhdt tagwaeavaa lpaglalvrg
       61 memscegrge dgrpvavhll adlfdpahaa farererlrn erivrirama elmmedglpi
      121 dadevlaeag paagrphlar almragvvgs vgeafvdlla prgryfvdks dtplddavql
      181 vaeaggvsvl ahgrartrgr llsldhvrdl agaglhglea hhpdhssdda rvlqeladec
      241 glvvtgssdy hgtnkairlg efstdtdefd tlvskasgvq vvsa
//
LOCUS       WP_005264951             234 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Rhodococcus opacus].
ACCESSION   WP_005264951
VERSION     WP_005264951.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus opacus
  ORGANISM  Rhodococcus opacus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Rhodococcus opacus"
                     /db_xref="taxon:37919"
     Protein         1..234
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=25005
     Region          90..229
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mrllyvaawl vailtvcgcg vslldlsgpg papgsppray ieellgrvat vesrphpggy
       61 qrgcsgkelc vfgpawtddq daaaghdgcd trnnvlaldl rsvafrdgtr gcvvlsgvla
      121 dpysgevlqf dradakavqi dhvyplaaaw dmgastwspe rrlrfandvt fnllavngad
      181 nqdkgdrtpq dwlppnpayh cfyagkylsv aveyglpvtl adrdalaeva ercp
//
LOCUS       WP_005265792             264 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Acinetobacter].
ACCESSION   WP_005265792
VERSION     WP_005265792.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..264
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29992
     Region          36..261
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mpnqnsqtss qttdssnpek kryyepapqd idvdnfrkvi esrrsvrkft kksipvevld
       61 acldlallap nssnlqpwtf yvvqnsgkkk rlvkacmsql aaktaseliv ciartdride
      121 makrnvnefp fpeappaikk yykyipynyk tgylnafgnf kkvafkvart ldkqmpvsaf
      181 spadaklwat kttalacenl vlalraygfd scmmegfdep mvreilklnd eqypvmviga
      241 geraedgvff pqyrfdrelf iqki
//
LOCUS       WP_005266176             264 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Crystallibacter
            crystallopoietes].
ACCESSION   WP_005266176
VERSION     WP_005266176.1
KEYWORDS    RefSeq.
SOURCE      Crystallibacter crystallopoietes
  ORGANISM  Crystallibacter crystallopoietes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Crystallibacter.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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   3  (residues 1 to 264)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Crystallibacter crystallopoietes"
                     /db_xref="taxon:37928"
     Protein         1..264
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29307
     Region          162..263
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mlaagyskas lhrsiaegrv irvrsglltl pdsdplvrha vsnnglvsca savkelglwg
       61 lkdpqqphlw vphgrpvagf rqkdstvetv rhrgrlvgnk rpgayapvld vvlhalrcrp
      121 plealviaes avikrklrrq dllnhlpgpr ngpfrallgk idptsesple tiarelfhnv
      181 glraepqvhi egvgrvdllv errviveldg fdfhwsrsmf rkdrrrnnaa mlsglqtlry
      241 lyedlvfepd tvvaqvlsla rqaa
//
LOCUS       WP_005266192             217 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Crystallibacter crystallopoietes].
ACCESSION   WP_005266192
VERSION     WP_005266192.1
KEYWORDS    RefSeq.
SOURCE      Crystallibacter crystallopoietes
  ORGANISM  Crystallibacter crystallopoietes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Crystallibacter.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Crystallibacter crystallopoietes"
                     /db_xref="taxon:37928"
     Protein         1..217
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=24201
     Region          69..202
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mwgkfvaavf tavlllsgfa vpaeaasvyk aslrtaarsl pvavekntgy drdryfgdwk
       61 dtnrdcqntr aevliqeskv rttyttsrrc tvrsgkwvts wdnrthtsas avqidhlvpv
      121 heawgsgars wsqarrvafy ndlgdgrmls aqtsklnsak qakgpedwmp pknrckyvad
      181 wvamkirwgl kadsrersal iryadscast titvtrv
//
LOCUS       WP_005262817             714 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Rhodococcus opacus].
ACCESSION   WP_005262817
VERSION     WP_005262817.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus opacus
  ORGANISM  Rhodococcus opacus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 714)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 714)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..714
                     /organism="Rhodococcus opacus"
                     /db_xref="taxon:37919"
     Protein         1..714
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=74440
     Region          8..713
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mdrtlidmtg phslsallap rnvvivgase rsawsagsfs nfarlgfegq vhlvnrkggt
       61 vhgqpahrsc aeigeqvdla lllvaaeavp nalrdiaaag irfavvlaag fdeigangra
      121 mqqqitelal elgvtcvgpn clgfinlvdk vpawsgrmae lttgamavvs qsgatahtia
      181 afaaqqnigv shvvstgnes mvdtttmati liedervrsv amfiesirda rtfrslarra
      241 aelgkpival kigsselaae iaqshtgalv gddrlvdaal rqfgvirvrs leqlvmtagl
      301 lsrtgplatg dlgvvsmsgg acdlvadrad asgvrlpila datkarlael lpefctlrnp
      361 ldstgaasak pelfrdsifa iaddpsvaiv aaihvhptee rgeaikarlr idapalagsa
      421 tpvilldqti atidpgtvrn leelgiplam tgldhvveaa ghaiwwsqwl rpdhlptasa
      481 pdlsylagag gvwseaesla llvehgvpav pyahvrdeea aveaagrlgs plvvklvspd
      541 ivhksdiggv llgldspeav rrayrqvqaa vlavpgaqse galissmrsg gvemivgvvr
      601 dqqwgltlav glggvlvhvi ddsvlrtlpv setdvrqmls elrgkalldg vrgskpvdld
      661 alvaailnva slaerlgdsl esieinpfrv egstvealda sivwaprgsd eahp
//
LOCUS       WP_005266356             338 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Acinetobacter].
ACCESSION   WP_005266356
VERSION     WP_005266356.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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
REFERENCE   4  (residues 1 to 338)
  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 338)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..338
                     /product="CmpA/NrtA family 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=38347
     Region          2..242
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mstlekteln igyiplldcv ailwaekqgy faeqgltinl ireaswsslr drlaygflda
       61 ahclsamlpa aalgtdqlqv alqtplvlsv nqafislrqd wcyelgiqpe ddeqstskkl
      121 vqalqqnhpi nlayvykysi hhyclkewla ltdpqlakni qlmtspppsm vkgiaeqvfd
      181 gfcvgepwni qaklegysfi vaasqnvipk vadkvlamtq ewaeqhpftv eavvkavqka
      241 qddlkqrsdl sevwdmlvdy qiiqfecsaq rhvydfykik niirnfvgks aqpkvddfiw
      301 llqqmqkwed iemtvaekkq iaeqciyslq sqhadiig
//
LOCUS       WP_005269060             703 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Crystallibacter crystallopoietes].
ACCESSION   WP_005269060
VERSION     WP_005269060.1
KEYWORDS    RefSeq.
SOURCE      Crystallibacter crystallopoietes
  ORGANISM  Crystallibacter crystallopoietes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Crystallibacter.
REFERENCE   1  (residues 1 to 703)
  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 703)
  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 703)
  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 703)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Crystallibacter crystallopoietes"
                     /db_xref="taxon:37928"
     Protein         1..703
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=74574
     Region          64..693
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mterldgnga vtaralppeg rkrghrhada paskedfgvl hgpkgtfdpd kdtideeali
       61 aefeaekpar hlsgkpkliv qvmgvalslf alywvfnpma tqfylpaflm lglsltflvy
      121 rgwgrtarak etgradnphi vdwvlavvai vpfmyiisdw dgffrraiip tyldlimgti
      181 aivlvleacr rtvgilvpav vmfffayayf gpyfpdpfqt safgwirlvg hnvmgtqgif
      241 gvptdvaaty iilftiygav lsasgatkff idlsfsafgq srsgpgrtvt lagfllgtvs
      301 gsgvattvtl ggiswpllrk agypkehgga vlaaagigai mspptlgaaa fiiaallnvs
      361 ylevliwati ptllyylgii laiemdarrf ktkavdfeak pvgklllrfg yhfsslvaiv
      421 vfmalgmtpf ravvyatala fvlsffdres wmtpkriwda latgatgals vipvmaaagl
      481 ivgvmtltgl glklaniivd faggslflta lfsaisvill glavpvtasf iiswviigpa
      541 lqdvgvpafa aamfifyysv lsevspptal spfaasaitg gkpiptmwlt wrytlsaflv
      601 pfifvlsgpg igllmqggil tvllalavsa vavsalavtt ggwilgpanw lergliglgs
      661 lpllvmepmy lgigaaviai glplhvirik rhshtaasae aag
//
LOCUS       WP_005269473             111 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Crystallibacter
            crystallopoietes].
ACCESSION   WP_005269473
VERSION     WP_005269473.1
KEYWORDS    RefSeq.
SOURCE      Crystallibacter crystallopoietes
  ORGANISM  Crystallibacter crystallopoietes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Crystallibacter.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Crystallibacter crystallopoietes"
                     /db_xref="taxon:37928"
     Protein         1..111
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12144
     Region          20..111
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mrllpalsdg krgellavld flmqrrrlva hlaainhiqs vavfgsvarr eekldsdvdf
       61 lvnpddeasl fhlaqfaedm egllgrpadv vsrrgldpel drailteava l
//
LOCUS       WP_005270799              83 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Acinetobacter colistiniresistens].
ACCESSION   WP_005270799
VERSION     WP_005270799.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter colistiniresistens
  ORGANISM  Acinetobacter colistiniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Acinetobacter colistiniresistens"
                     /db_xref="taxon:280145"
     Protein         1..83
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8881
     Region          6..83
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mqtieikiea fgaierllpk plafefaadr mvkdvlahiv tlypeanham ekcacaiged
       61 iitrqtalei sctlvllspv agg
//
LOCUS       WP_005269939             337 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            colistiniresistens].
ACCESSION   WP_005269939
VERSION     WP_005269939.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter colistiniresistens
  ORGANISM  Acinetobacter colistiniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 337)
  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   6  (residues 1 to 337)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Acinetobacter colistiniresistens"
                     /db_xref="taxon:280145"
     Protein         1..337
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38419
     Region          25..209
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          89..334
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mqhhwdfprh inavrvlvav gqshgltvaq clknsditle dlskihhein vqqefqvlrn
       61 lidllgseip igveaglrhh tttfgawgfa ilssptieaa lhlalrylql ssffcklets
      121 kvgehtvitf nhddlpqdlv yflaerdytt imslqkdilp lslpvmeinv alptpvyadr
      181 fveltgyain fdqprsciii etsllnlplp qadhftrtyy ekecqnlwir rstigkfsqk
      241 irnilllkps qmpkieeiai qleitvrmlq rhlategity erlmsnired laedllttte
      301 ltieeiatql gyseasafsr afkrwknvsp khfrtgs
//
LOCUS       WP_005270831             338 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            colistiniresistens].
ACCESSION   WP_005270831
VERSION     WP_005270831.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter colistiniresistens
  ORGANISM  Acinetobacter colistiniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 338)
  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   5  (residues 1 to 338)
  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   6  (residues 1 to 338)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Acinetobacter colistiniresistens"
                     /db_xref="taxon:280145"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38332
     Region          22..200
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          83..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mvplahtaal knylvvsqql dlnpyqllsd agiypaqlqd stqripvdka vtlleqsall
       61 sgcecfglhm aeqrqladfg elslllsyqh tlrdglytiv qyrnlinnal emyieevght
      121 viirvevitt eteysrqaie lalgithrfc aaflqkwhpl sihfthdaph dtamhqrmfg
      181 cslefgsefn givcnateld ktnphanttm lahakrflet dllhresess iifdirksih
      241 lllpmgrati dqvahthgin vrtlqrrlea ahtnfsvlin dvrrnlvfry lknlnyslgq
      301 vsdilgysmp ssftrwfsse fgmspttwrn nnktvmks
//
LOCUS       WP_005271288             314 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Crystallibacter crystallopoietes].
ACCESSION   WP_005271288
VERSION     WP_005271288.1
KEYWORDS    RefSeq.
SOURCE      Crystallibacter crystallopoietes
  ORGANISM  Crystallibacter crystallopoietes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Crystallibacter.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Crystallibacter crystallopoietes"
                     /db_xref="taxon:37928"
     Protein         1..314
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33111
     Region          1..>232
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mtdrlmlldt aslyfrafhg vpdslkapdg tpvnavrgll diiarlvtdf qptqlvacwd
       61 ddwrpgwrvd llpsykahrv aeavpggidv eetppglvaq lplirevldv lgiavvgape
      121 headdvigsl aaqadlpvdv vtgdrdlfql vddsrnvrvi ytargmskle tvtdatvvgk
      181 ygvlpvqyad yavlrgdasd glpgvsgige ktaakllqef vdldgiiaaa gdhttamgap
      241 mrakisaaad ylaaaprvvn vvrdlsfggf daslrpldag rlsrmdglkt ehnlggsvqr
      301 vlkalgndpq aags
//
LOCUS       WP_005271529             383 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Acinetobacter
            colistiniresistens].
ACCESSION   WP_005271529
VERSION     WP_005271529.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter colistiniresistens
  ORGANISM  Acinetobacter colistiniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 383)
  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 383)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Acinetobacter colistiniresistens"
                     /db_xref="taxon:280145"
     Protein         1..383
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44667
     Region          7..377
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 misllkrlal shqgleknns faeglsgtqq aiehlgyvqi dtisvverah hhvlwsrvpn
       61 yqlvhlnqlv qdqlifehwa haasylpmrd yryamplmhs irngesryfs rgdqklmhei
      121 laqvkaegri rlrnmqkekr egsagwwnag psrkaieqlf mqgdlmicer ngmekvydlt
      181 ercipqgldv stptlleyaq ylldttirah gvftwkqllh lktnkdlrdi mrklldeqid
      241 agvinlikle sgqtvyvasa vlehepkiea evkilspfdn lvihrerlsc lfdfdyriec
      301 yvpaakrqyg yfclpllyad dfvgridckv hrreqrlevi slhledtkmq nrddfllale
      361 relqrfaqfn qcttidlnki kmr
//
LOCUS       WP_005271960             300 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            colistiniresistens].
ACCESSION   WP_005271960
VERSION     WP_005271960.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter colistiniresistens
  ORGANISM  Acinetobacter colistiniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (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
REFERENCE   5  (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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Acinetobacter colistiniresistens"
                     /db_xref="taxon:280145"
     Protein         1..300
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33994
     Region          39..185
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          219..295
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 myskigdamd asdqtkelvk iladkvgrlv qdedfqteis gfslhrrtvk qsihciyglg
       61 lgivlqgqke vlirdkvygy gagqtmltti dlpaisrvtq asyrepflgm mlpldldlii
      121 etvqaldnki klknlpafsi edldtplina ltrlvdliee pqmieqlapi ikqeivlrll
      181 vgqhgvylrn lvkatisnqh ifsvihwlrn nflqenclqv afeqanmsaa tfrnqfknit
      241 gmtplqyqkq lrlqearkmv lsqslniqqi adrvgyesqs qfireysrlf gstpsrdgqr
//
LOCUS       WP_005273818             122 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Acinetobacter
            colistiniresistens].
ACCESSION   WP_005273818
VERSION     WP_005273818.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter colistiniresistens
  ORGANISM  Acinetobacter colistiniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 122)
  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 122)
  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   3  (residues 1 to 122)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Acinetobacter colistiniresistens"
                     /db_xref="taxon:280145"
     Protein         1..122
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14342
     Region          15..118
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mkpynknlkq asrnlrsnmt daeqllwqri rrkqilglqf yrqkpilnfi vdfyspavnl
       61 viecdggqhy tklgleadqn rdhtlselgl itlrftnhqi ltemdavveq iyyvvrqrle
      121 tf
//
LOCUS       WP_005274738             349 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            colistiniresistens].
ACCESSION   WP_005274738
VERSION     WP_005274738.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter colistiniresistens
  ORGANISM  Acinetobacter colistiniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 349)
  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 349)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 349)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 349)
  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   5  (residues 1 to 349)
  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   6  (residues 1 to 349)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Acinetobacter colistiniresistens"
                     /db_xref="taxon:280145"
     Protein         1..349
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40369
     Region          41..212
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          89..344
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mnknlnfdln sakdtisnal irealsvaas rglnivnian ragisaellt sskarvpvtq
       61 caqlwvelae smndeflgmd rhpmrrgsyr llaklafnae tleqalqeil kflslvlddi
      121 hgelvqrgsk aylilhdreh pkrmftysty lmlvhslmcw lsdqrigfht msfrchppve
      181 lqdyrvrfce diqfnadqnq iefdahylkh kikkdkqaln dflrhtpynl ivrfknensl
      241 slqirrqlll qppsqwdelk eiaqqlnmst atiqrrlkqe gvsyqqlknd ircdiaierl
      301 sksndsiqni sddlhfhdps afhrafkkwt gvspgtyrsk slkrtiddi
//
LOCUS       WP_005274841             104 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Crystallibacter
            crystallopoietes].
ACCESSION   WP_005274841
VERSION     WP_005274841.1
KEYWORDS    RefSeq.
SOURCE      Crystallibacter crystallopoietes
  ORGANISM  Crystallibacter crystallopoietes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Crystallibacter.
REFERENCE   1  (residues 1 to 104)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Crystallibacter crystallopoietes"
                     /db_xref="taxon:37928"
     Protein         1..104
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=10445
     Region          21..103
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 meaaedpsee esvnkadpll ifnaagvngl ggsvsqrasa dgwsvalvdn wqgaamansv
       61 ifynpgqaan aqaigqllgi sdlretapga vadfvtvvlg pgfq
//
LOCUS       WP_005275412             345 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            colistiniresistens].
ACCESSION   WP_005275412
VERSION     WP_005275412.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter colistiniresistens
  ORGANISM  Acinetobacter colistiniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 345)
  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 345)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Acinetobacter colistiniresistens"
                     /db_xref="taxon:280145"
     Protein         1..345
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38487
     Region          31..213
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          258..338
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mfefqdylra pssvqlliel akqhnvqgsl llvgtglsls rlndancvvs aeqeiavitn
       61 liqhlamdtt alglvigfqh klttygilgy almssatgld afklakrylp ltytfvkisf
      121 rlekqhaiis ftepaslsae lqqfvvaram aatsrvisdi yessfqfdaf hlknhqpqqs
      181 laefpqhfla apilfeqksn elifnaaqln qplshanant aamcerlcte litqrhttlt
      241 ttmivrdfls napsgklltl pdiasklhis ertlkrrlqe enssfrliqn etlqqranef
      301 lckdlslaqv aedlgfsdls tfsqaykrwt gitpsqfkke kkpts
//
LOCUS       WP_005275882             154 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acinetobacter colistiniresistens].
ACCESSION   WP_005275882
VERSION     WP_005275882.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter colistiniresistens
  ORGANISM  Acinetobacter colistiniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Acinetobacter colistiniresistens"
                     /db_xref="taxon:280145"
     Protein         1..154
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=16453
     Region          1..131
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mvkkdrgftl ielmivvtii gilaavayps yqeyvrrtkr tdaqadmiel agrlqrykia
       61 nftflksdgs tpigiadvgh sgilpqsgga tlytlalsnv tagtwtliat ptgaqtgdgh
      121 ivlnyrgerc wvrgsdknsg tactpsattn wdgr
//
LOCUS       WP_005277046             141 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Acinetobacter
            colistiniresistens].
ACCESSION   WP_005277046
VERSION     WP_005277046.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter colistiniresistens
  ORGANISM  Acinetobacter colistiniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 141)
  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   2  (residues 1 to 141)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Acinetobacter colistiniresistens"
                     /db_xref="taxon:280145"
     Protein         1..141
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16069
     Region          71..139
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mrlpqsrskh kffllmilcl gcishlkaqq fdqsyqhwka qqqardqqla rqadnnyyls
       61 rptqqlpkqv sssvniqgdk islnqanlqq lqmlngvgek kaqaiveyrq knggfktvde
      121 lmnikgigpk lleknksklm l
//
LOCUS       WP_005277067             264 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Acinetobacter
            colistiniresistens].
ACCESSION   WP_005277067
VERSION     WP_005277067.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter colistiniresistens
  ORGANISM  Acinetobacter colistiniresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acinetobacter colistiniresistens"
                     /db_xref="taxon:280145"
     Protein         1..264
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29665
     Region          1..257
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mshlavnlsm iftevplier falahahgfq hveiqfpyel dvidirtqle qhnlslclin
       61 vpagdlmqgg nglagvpgre iefhqaleqa iryataldvp rvnilagkqp ldadllpcln
      121 tlasnlklac hllteqgiep vfemingtdm prflvqniaq aqemleainh palkmqydcy
      181 hmammgedvl aglqenidqi ghiqfadcpd rhepdtgnip ykqifdwlqq sdyrgliaae
      241 yrpkiqsdqs fawkkkyfsn dvnt
//
LOCUS       WP_005281908             142 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Edwardsiella].
ACCESSION   WP_005281908
VERSION     WP_005281908.1
KEYWORDS    RefSeq.
SOURCE      Edwardsiella
  ORGANISM  Edwardsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Hafniaceae.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Edwardsiella"
                     /db_xref="taxon:635"
     Protein         1..142
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14944
     Region          5..140
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 msefwaiagm fvssftsatl lpgnsevvls glliaaqapv fgllvaaivg nvlggatnvv
       61 igralpqvtp qrglavalgw lqrygaaall lswlpvigdl lcvlagwlrl pwgavllylt
      121 lgkavryall awltlygmsw wh
//
LOCUS       WP_005282618             276 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter courvalinii].
ACCESSION   WP_005282618
VERSION     WP_005282618.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter courvalinii
  ORGANISM  Acinetobacter courvalinii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 276)
  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 276)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 276)
  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   4  (residues 1 to 276)
  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 276)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Acinetobacter courvalinii"
                     /db_xref="taxon:280147"
     Protein         1..276
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31639
     Region          51..271
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <175..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 msrrpreqvd ylhleelggl emlkasyyqq efsrhvhegf cigvieegaq rfyrtggnhv
       61 apqgdiilvn adevhtgssa vdtgwryrai yptpevfnel trdlttvhgt apwfreavlh
      121 deglaqqfrl lfdlleqpnn sllkqtlfls tiawlvskys qvkphvtdls nakqrilnik
      181 elmatmpeqe fslaelaema nlsqwhflrq fkkhvglsph awlvqarlqk sqrllrqgln
      241 lsevsqqcgf sdqshfsrhf rqtfgitpgg yitylk
//
LOCUS       WP_005283396             141 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Acinetobacter courvalinii].
ACCESSION   WP_005283396
VERSION     WP_005283396.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter courvalinii
  ORGANISM  Acinetobacter courvalinii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 141)
  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   2  (residues 1 to 141)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Acinetobacter courvalinii"
                     /db_xref="taxon:280147"
     Protein         1..141
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16041
     Region          71..139
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 milqqvcrkh kfflfiilcl gcvsplkaqq fdqayqqwkt qqqlrdqqla nqannnyyls
       61 rptqqapqwl sssvntpgdk islnqaslqq lqmlngvgek kaqaimeyrq knggfksvde
      121 lmnikgigpk lleknkarlm l
//
LOCUS       WP_005283488             113 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Edwardsiella tarda].
ACCESSION   WP_005283488
VERSION     WP_005283488.1
KEYWORDS    RefSeq.
SOURCE      Edwardsiella tarda
  ORGANISM  Edwardsiella tarda
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Hafniaceae; Edwardsiella.
REFERENCE   1  (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   2  (residues 1 to 113)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Edwardsiella tarda"
                     /db_xref="taxon:636"
     Protein         1..113
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11798
     Region          44..111
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mslftlllss plwlsllffp lrpqaapvis sttttmpasg argstapqge rlninqasap
       61 alaagmtgvg ldkaqaivdf rqqhgafssl eqllqvkgig ralleknrar lal
//
LOCUS       WP_005285512             196 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Acinetobacter].
ACCESSION   WP_005285512
VERSION     WP_005285512.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 196)
  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 196)
  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   3  (residues 1 to 196)
  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   4  (residues 1 to 196)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 196)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..196
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22345
     Region          1..191
                     /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"
ORIGIN      
        1 mpklkialid ddqaraeylk acliehdfdv vacftldhfn lfklehlqad villdmehph
       61 rdviescvsn fdlptvlftk nadkdtikqt idagitayiv dgidpsrlht ildisieqyk
      121 khkklegdlk daktkladrk diekakvllm qlhgltedta fqllrknams hrmtigemar
      181 rlldaqqlln nqlkde
//
LOCUS       WP_005285560              83 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Acinetobacter courvalinii].
ACCESSION   WP_005285560
VERSION     WP_005285560.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter courvalinii
  ORGANISM  Acinetobacter courvalinii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Acinetobacter courvalinii"
                     /db_xref="taxon:280147"
     Protein         1..83
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8910
     Region          6..83
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mqtieikiea fgaierllpk alafvfaenq svkdvltriv klypeadqam ekcacaiged
       61 mvtrqtaldr sctlvllspv agg
//
LOCUS       WP_005286414             312 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Edwardsiella tarda].
ACCESSION   WP_005286414
VERSION     WP_005286414.1
KEYWORDS    RefSeq.
SOURCE      Edwardsiella tarda
  ORGANISM  Edwardsiella tarda
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Hafniaceae; Edwardsiella.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 312)
  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 312)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Edwardsiella tarda"
                     /db_xref="taxon:636"
     Protein         1..312
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35186
     Region          20..67
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msmmlmamam kiktgnplrk lvllkladna ndqgecwpsi pylaatcems ersvqnhikw
       61 lheqgflwve prkskngghq sniyhltler rlrspleede kgdlppeenq ekngaaqgtg
      121 sagangasls evpaqqirqg lsfdslgvaq plhpepiikn lslepippfp pnnsefvepd
      181 kdktdrgkpd wtepdrhyre ldnpeadhle renltrrsae rmdygaylaa ynelvgdrlp
      241 havtvneerk rklrslvksl atpnlegfra yvsafldhak pfyfgfgdag wiadfdyllr
      301 qktltrvreg tl
//
LOCUS       WP_005286907             489 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein, partial [Edwardsiella
            tarda].
ACCESSION   WP_005286907
VERSION     WP_005286907.1
KEYWORDS    RefSeq.
SOURCE      Edwardsiella tarda
  ORGANISM  Edwardsiella tarda
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Hafniaceae; Edwardsiella.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Edwardsiella tarda"
                     /db_xref="taxon:636"
     Protein         1..>489
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
     Region          6..>484
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mkiagyalnp vavalllagl stahaeervi vsgnllgdar aeavktypgs rsvisnqqlt
       61 qdanrsidda lqhvpnvkiq detgtgilaq iavrglqdsr sgyvqmlldg iplalapygq
      121 tglslfpvtf qtidridvvr ggaavqygpn nvggviniis kpiplrwtnt vsqrttlagh
      181 grnlydtyls sggmlndrvg lqiegnlikg safrqhsrqt vqnyrikglw ninddsslnl
      241 tyqyydadaq lpgalssady qqdrtqstrl qdgyqgrtqr lsavyntlld rvgpfdsgef
      301 nwtlfghlsh rsfdvglsqq pglvwapdrp adikqssprd fkvwgteprl tlyhggsain
      361 qkitlgarli denidylvqr hyltsarpdq vtrdwkfrnq gvagylsdav mlfddsltlt
      421 pgirfeqvne hyrdnhsgqv vknrdqqwlp gitlgyqatp swflyanaqk slrapqvtqi
      481 vkggqrgae
//
LOCUS       WP_005289543             206 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Edwardsiella].
ACCESSION   WP_005289543
VERSION     WP_005289543.1
KEYWORDS    RefSeq.
SOURCE      Edwardsiella
  ORGANISM  Edwardsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Hafniaceae.
REFERENCE   1  (residues 1 to 206)
  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 206)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 206)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Edwardsiella"
                     /db_xref="taxon:635"
     Protein         1..206
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22105
     Region          1..204
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 mevysteneq vdairhflqe ygktlvvgvv igvgalfgwr ywanhqqagm aqasqtyqqa
       61 sealsggkqd gvalseafik enannygvla alqlaqhevd kaefskaqsq lawaagqakd
      121 enlkalsdlr larvqlqdnq ldaalktldg vtakgwqala qdvrgdvllk kgdakgarea
      181 yskglaegas qslqallrmk lnnlss
//
LOCUS       WP_005291811             142 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [unclassified
            Acinetobacter].
ACCESSION   WP_005291811
VERSION     WP_005291811.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 142)
  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   2  (residues 1 to 142)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..142
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16077
     Region          72..140
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mtlpqlsskh rffllmilcl gcvshlnaqq fdqsyqqwkt qqqardqqla kqsnnnyyls
       61 rptqqqnsqh lsssvniqgg kislnqanlq qlqtlsgvge kkaqaimeyr qkngafksvd
      121 elmnikgigp klleknrarl ml
//
LOCUS       WP_005292945             333 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter sp. NIPH
            2100].
ACCESSION   WP_005292945
VERSION     WP_005292945.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. NIPH 2100
  ORGANISM  Acinetobacter sp. NIPH 2100
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 333)
  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   6  (residues 1 to 333)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Acinetobacter sp. NIPH 2100"
                     /db_xref="taxon:1217708"
     Protein         1..333
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37992
     Region          25..195
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <131..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtsrktsdag iflwmvyqtm qmmdidaaai farvhlpdqp pdkfvrrdns tqqrfwkaav
       61 eiskdldigl higanvpafr gqvieylfls sptfgeglkr tmryqalltd amsfnldmin
      121 edtvmisgln hpvrhyleca igillnffky isdetfiple iglpyhegah pneyqkiwgc
      181 pvrlgqengy iyfdatqltt aspahepell kvhehhaasq lellnkhqli neiekilasg
      241 llesgdfdqn ivaqylgrsa rslradlqll nttyekviah yrerlarrll shtqesidqi
      301 vyltgfseps afsrafkrwt getptayrqr kqa
//
LOCUS       WP_005293674              83 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [unclassified
            Acinetobacter].
ACCESSION   WP_005293674
VERSION     WP_005293674.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..83
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8826
     Region          6..83
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mqtieikiea fgaierllpk alafefaedq mvkdvlshit slypdastam ekcacaiged
       61 ivtrqtaldr sctlvllspv agg
//
LOCUS       WP_005293991             693 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Edwardsiella tarda].
ACCESSION   WP_005293991
VERSION     WP_005293991.1
KEYWORDS    RefSeq.
SOURCE      Edwardsiella tarda
  ORGANISM  Edwardsiella tarda
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Hafniaceae; Edwardsiella.
REFERENCE   1  (residues 1 to 693)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..693
                     /organism="Edwardsiella tarda"
                     /db_xref="taxon:636"
     Protein         1..693
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=77207
     Region          6..693
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mkiagyalnp vavalllagl stahaeervi vsgnllgdar aeavktypgs rsvisnqqlt
       61 qdanrsidda lqhvpnvkiq detgtgilaq iavrglqdsr sgyvqmlldg iplalapygq
      121 tglslfpvtf qtidridvvr ggaavqygpn nvggviniis kpiplrwtnt vsqrttlagh
      181 grnlydtyls sggmlndrvg lqiegnlikg safrqhsrqt vqnyrikglw ninddsslnl
      241 tyqyydadaq lpgalssady qqdrtqstrl qdgyqgrtqr lsavyntlld rvgpfdsgef
      301 nwtlfghlsh rsfdvglsqq pglvwapdrp adikqssprd fkvwgteprl tlyhggsain
      361 qkitlgarli denidylvqr hyltsarpdq vtrdwkfrnq gvagylsdav mlfddsltlt
      421 pgirfeqvne hyrdnhsgqv vknrdqqwlp gitlgyqatp swflyanaqk slrapqvtqi
      481 vkggqrgael awnyesgvry tpwttlslqa dyyridytds kiiydnasat fvnlgraryq
      541 gieleafysp afldglklha gyayldsqql vganagrqmp yasrhqlvld gryqwrdttf
      601 alsayyysaa fsdkensree sakgdagrlp aytvwnaqvt qqlyhdrdsq lsgyltvnnl
      661 lnkdyyyrgi dtspwgrqpa pgrsvtlgvd ytf
//
LOCUS       WP_005295085             338 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter sp. NIPH
            2100].
ACCESSION   WP_005295085
VERSION     WP_005295085.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. NIPH 2100
  ORGANISM  Acinetobacter sp. NIPH 2100
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  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   4  (residues 1 to 338)
  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 338)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Acinetobacter sp. NIPH 2100"
                     /db_xref="taxon:1217708"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38562
     Region          27..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          252..332
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mnpslpgtyv slmadvvqkl nvpteklleg sgihieqlsq pfwyldfdif ndllnravel
       61 thepalgvyl glqmtvschg svglaamvsq nlgealnvme qfiglrcpal kprlevedgl
      121 aslyldqpmt nfkmgivgmt flmvgfaqms naitgkkldi kaelnyfeps fiqqvqellp
      181 cevsfnqekn rltfsenyla lplimadpla arlareqckh dlnklvakrg ekypltalvr
      241 ellfdevdgf fkmrevadkl yltertlqrq lakegitfqi lmdqvrerya krllnhheys
      301 isyiseklgy sdvthftraf krwtsqtpkq yrslresf
//
LOCUS       WP_005295384             378 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Acinetobacter
            sp. NIPH 2100].
ACCESSION   WP_005295384
VERSION     WP_005295384.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. NIPH 2100
  ORGANISM  Acinetobacter sp. NIPH 2100
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 378)
  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 378)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Acinetobacter sp. NIPH 2100"
                     /db_xref="taxon:1217708"
     Protein         1..378
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44098
     Region          8..374
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mlsllkglal shqgleknnt fgegrsgtln aiehlgyvqi dtisvverah hhvlwsrvpn
       61 yqldhlnqlv kaqkvfehwa haasylpmrd yryamplmha irngerryfk sdphlmkeil
      121 arvkaegkiq lrnmqkekre gpagwwnsgp nrkaleqlfm qgdlmicern gmekifdlte
      181 rclpegidls tptlheyahy llnmnirahg vftwkqllhl kgkelrevmr tvldenidag
      241 lvkvikleng qmiyaatavl ehepaiqaql kilspfdnlv ihrerlsslf dfdyriecyv
      301 paakrqygyf clpllyadrf vgridckvhr rekrlevirl hledpnmqdr eafikalele
      361 lqrfavfnqc tevdqyri
//
LOCUS       WP_005296984             391 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Acinetobacter sp. NIPH 2100].
ACCESSION   WP_005296984
VERSION     WP_005296984.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. NIPH 2100
  ORGANISM  Acinetobacter sp. NIPH 2100
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Acinetobacter sp. NIPH 2100"
                     /db_xref="taxon:1217708"
     Protein         1..391
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42285
     Region          5..388
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 maisvlvinc gsssikyali sehredriyg laenlgaada rikgvtlgge plelsipyad
       61 hakaletlla rlanynpqai ghrvvhggni tkaelltpel verieaatpl aplhnpahli
      121 gieatmrlfp qlpqvavfdt afhqtmpera yryalpqyly tehqvrrygf hgtshayvte
      181 raselaghkn hggwlsahlg ngsstcavwn ghsvdtsmgm tplegvvmgt rsgdvdpslh
      241 lflasnlgwd iqkidsmlnk esgllglsgl sndmrtlvea senghegatl aievfcyrla
      301 kslsalscgl phldglvftg gigensayvr ektlgylahf glkfskeknn alprgtegri
      361 dngsgpqiwv iptdeegria ketrqvleht i
//
LOCUS       WP_005297456             335 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter sp. NIPH
            2100].
ACCESSION   WP_005297456
VERSION     WP_005297456.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. NIPH 2100
  ORGANISM  Acinetobacter sp. NIPH 2100
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 335)
  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 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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 335)
  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   5  (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   6  (residues 1 to 335)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter sp. NIPH 2100"
                     /db_xref="taxon:1217708"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38581
     Region          51..193
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          82..330
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msqlknytgs vfgglghllk ayceaeniai peqlqqvqnl erfdyviwrd lledlnrlhp
       61 kaglglqiaa yvqpkhlgii aylalscenl gealaryhdf hrliydgspl vvelshpygs
      121 irweapephp tqltdeiaia lmvqflklfm sgdsihlhev hfvnpapkni siyeqyfhck
      181 vrfeqpktql lipvseafkp lrtgdhtlqq lllqqahall dklpnstqld qrlqhailtg
      241 lqknqyqidf iaeklglsvr qlqrhlqqqn ttfqervqqv rfmlateylk dphlslqeia
      301 lllcyseqsa fqrafkiwtg qtpqqwrnnn ityns
//
LOCUS       WP_005297470             614 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Acinetobacter sp. NIPH 2100].
ACCESSION   WP_005297470
VERSION     WP_005297470.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. NIPH 2100
  ORGANISM  Acinetobacter sp. NIPH 2100
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 614)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..614
                     /organism="Acinetobacter sp. NIPH 2100"
                     /db_xref="taxon:1217708"
     Protein         1..614
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=70082
     Region          7..538
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mtktkleltw igkdkrprle prilledfsl syhatnkvse ndifdnklif gdnllalkal
       61 ereyagkvkc iyidppyntg qafdhyddgl ehsiwlslmk erfeilknll tvdgvffcql
      121 nddelayckv lldevfgrsn flnqvsvkmk qtsgasggge dkrlkknvey iliytkdkds
      181 dlgfkkfndv ydeedlfevi gqmrdegksw kytrvikdfg erkflktild gsgepidifi
      241 henveiepis qiikkekite qecyvkyfdk ifrdtnaqss irtrvmdain gehdfvsiey
      301 vpksgkskgr kttlyykgnn cdliawlrdv avkkgnklvk lekagtywdg fplnnltkeg
      361 gvvfpngkkp ealiqkvlel stepndlvld sfggsgttga vahkmgrrwi mvelgehcht
      421 hiiprlqkvi ngkdtggitk alnwkggggf ryyklapslm kkdqwdnwvi npeynqemlv
      481 eamcklegyt ytpseteywn hgrgsetdfi yvttqtltdp qlqaiseevg egrtlliias
      541 awrsknidrf inltlkkipn siikacewgh ddyslnvqnl pisepdteek tiakkikntk
      601 kqsqamgdlf gdqt
//
LOCUS       WP_005297899             211 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Aeromonas].
ACCESSION   WP_005297899
VERSION     WP_005297899.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 211)
  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 10614777
            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="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=23905
     Region          46..210
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mkqtdwikrw galwlsvpll lgalcfssss haswdqdlyr qlglagkldk qvfrkalnsy
       61 qsvrhkrkpi ltiidyskps tqrrlfvidv krhkllyhtw vshgrnsger darqfsnqfn
      121 smksslgvyr taetyqgkhg yslrldglsp gqnsnarkra ivvhgadyas prhllkydkl
      181 grswgcpalp keqsraiidi ikggsviyah g
//
LOCUS       WP_005298818             731 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Aeromonas dhakensis].
ACCESSION   WP_005298818
VERSION     WP_005298818.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 731)
  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   3  (residues 1 to 731)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..731
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=77474
     Region          6..730
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mafevdedil qdflveasei leqlseqlvd lekrpddknl lnaifrgfht vkggagflsl
       61 telvdvchga envfdilrng krtvtaelmd vilqaldain vmfaqvqnre ppspasaeil
      121 hdlhelckpe geeqlltasa gssapveaaa pvaeevavia epepaavpep eqeasvvsgg
      181 gsideisade ferlldelhg vggaptaaas paapssgdit ddefealldq lhgqgqhgga
      241 pevnplksvq kevdeliddd eferlldelh grgqspqssm sapaapqtpa paapvtpapa
      301 aakpapapaa akpaaapaaa kpapapapsk qaapapadsa vqsdttvrvd tktldvimnm
      361 vgelvlvrnr lvslgiasnd edmskavanl dvvtadlqga vmktrmqpik kvfgrfprvv
      421 rdlartlkke ielvmvgeet dldknlveal adplvhlvrn scdhgvempd vrekagkprq
      481 gtitlsasqq gdhillcied dgagmdpekl ksiaisrgvl dadtaarmsd ndaynlifap
      541 gfstkseisd isgrgvgmdv vktsivslng svhidstwgk gtrleikvpl tlailptlmv
      601 evgeqtfalp lgcvneifhl dlkkanmvdg qltiivreka iplfylhnwl vrgknrksrq
      661 dtghvvivqi gtqqigfvvd nligqeevvi kpldsllqgt pgmagatits dggialildv
      721 psllkayarr h
//
LOCUS       WP_005300403             282 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Acinetobacter sp. NIPH
            542].
ACCESSION   WP_005300403
VERSION     WP_005300403.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. NIPH 542
  ORGANISM  Acinetobacter sp. NIPH 542
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Acinetobacter sp. NIPH 542"
                     /db_xref="taxon:1217688"
     Protein         1..282
                     /product="formate/nitrite transporter family protein"
                     /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=31311
     Region          28..279
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mdheieekkv ektlswrekm aveeheklsp rlvyeiirrd gaeeldrpta alifsgiaag
       61 lvisfsfvfk aiiasylpad avwtdlitni gytigfliai lghmqlften tittvvplfk
      121 pftfdklrav grlwgivilc niigtalasl ffltthlftp didkaldela hhvgsfsatq
      181 nmlkgimsgl liaalvwmlp svtnkfllif fmtyliglgd fthvvvgste msylvwqgea
      241 sindylftfl vpttigniig gtgvftlliy gqvteeleqk hq
//
LOCUS       WP_005300791             152 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Aeromonas].
ACCESSION   WP_005300791
VERSION     WP_005300791.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            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="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16600
     Region          4..152
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 miekqafyrt lnqqaqalle gepdlianla nlsallnqel tdinwvgfyl lqgetlvlgp
       61 fqgkpacvri pvgrgvcgta vaegktqlid dvhqfeghia cdgasnaeiv iplrrrgeii
      121 gvldidspif nrfdeqdrig leetvqiles ml
//
LOCUS       WP_005300832             659 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: Lon protease family protein [Aeromonas].
ACCESSION   WP_005300832
VERSION     WP_005300832.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 659)
  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 659)
  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 659)
  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   4  (residues 1 to 659)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..659
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73208
     Region          7..639
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 maeltseqlk pafaieqfpa lselepipfa alqpraisgi krlasfdgdc pvmllngfpg
       61 vdyedvcqtl iaasngkdgd lfdlcytenl nnpfkpiwlr lqpgtgiefc emvgellklm
      121 shhldaerlv trimrkqnnd pkiddflsdl aahvaqglef qhpvlinlli hheeqeapvv
      181 ygrdlnwdtl fgsinyqteq gsvyanqhll epgllrqang gylilqldel ldqphlwfkl
      241 knamqkgeld wnayqegktl tpfftpeatp iklklilvgd rldvaefqml drdmserifl
      301 radlvsevni eeelpdylqy lawlrerwnl ldftpaalaa lcrhasrlcd hqewlslsev
      361 qlsaimrmad slareleadv vtdehirgal eeqdyrlnyl veqsdqgvid gqillqtdge
      421 evgqinglsv iqvsghpydf gepvrltatv hlgdgdvadi erkaelaghi hakammiihg
      481 ylsnkfgaen psplsanlvf eqsyheidgd sasltglcal lsalarqpiy qhfavtgavd
      541 qfgnvqavgg vnekiegffr vckihgltgk qgillpgtna qqlnlsdevi aaveagqfhi
      601 hpvdhveeai elltgcvage pdmpdtlfgr iqqrldelng teavkggvlr rlfgrlfgv
//
LOCUS       WP_005301816             546 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Aeromonas dhakensis].
ACCESSION   WP_005301816
VERSION     WP_005301816.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 546)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..546
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=61687
     Region          9..526
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mlnklgsnql mvmalicapl lllqglwlaf astpltllli latsllgfgl lirlvmrlqq
       61 adrerqeqvw cralqlrdpt cletptaqaa lqqllahfne aeldahrqis elhnqatqde
      121 ltqlqnrhaf rrdmtellqr dqdtqtatlv lvratelgkl naqrgfqsgd ayikdianli
      181 nkvvsrfpgh qvyrisgadf avlvrpeani pppllgrdlk iafdhyqqqh elesaaysgl
      241 trlssgqkie ailaradlal araqtetvng waiqqddnvv elqgqhhwkl vltelleqer
      301 idftyqpiqp mhrsmlayne iytrfsgadg tvlptdtlfa maqrldmvmr leqmlvihvm
      361 rqyrafgsnq srwginlssn llqnsafliw ldrqllndpn tsanlvfeld eehlernltg
      421 akrvfellrr ngsrsaicnf gkgigsfnlf relkpdyikl dpalitgleq dltnqqfvrm
      481 ivdvshrmgc qviaegveql gqkqllqgmy vdglqgylia rpqplrpdis qlglftedas
      541 tstese
//
LOCUS       WP_005302205             400 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [unclassified
            Acinetobacter].
ACCESSION   WP_005302205
VERSION     WP_005302205.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acinetobacter
  ORGANISM  unclassified Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="unclassified Acinetobacter"
                     /db_xref="taxon:196816"
     Protein         1..400
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42912
     Region          5..388
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 maisvlvinc gsssikyalv serredriyg laenlgaada rikgvtvgge plelsipyad
       61 hakaletlla rlanykpqai ghrvvhggsl tkaelltpei ieriraatpl aplhnpahli
      121 gidatvrlfp elpqvavfdt afhqtmppha yryaipkfly tdhnvrrygf hgtshayvsd
      181 kaselsgnlk kggwltahlg ngsstcavwn gqsvdtsmgl tplegvvmgt rsgdvdpslh
      241 sflaknlgwd lakidkvlnn esgllglsql sndmrtviea aengnedacl aievfsyrla
      301 kslaalscgl ptldgliftg gigensayir ektlaylphf glqldkdqnn nlkrgtegri
      361 dngtgpqiwv iptdeegria ketrqvveaa entasvasla
//
LOCUS       WP_005302244             263 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Acinetobacter].
ACCESSION   WP_005302244
VERSION     WP_005302244.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   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 263)
  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 263)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..263
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28743
     Region          24..91
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          191..252
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 meinpnsqqp tgsslptsal gniqrpgeyl rqirvaqnke lgqvssdlnm pvktltaleq
       61 ddykslpeat fikgyyrsya kylntdatai iqrfdeiyan dtgllpnhal nnspikimgk
      121 lpgsnsdrnk kwlkrallai vviavvsliv mgiqkwtskk edadlpkvnq ssvevlpmkg
      181 natstvgdql vlnfnrptsv hivdatgkvl atgrqsstln lngespfqir lddatavsls
      241 lnqeqislsp ytvngkaefr lsr
//
LOCUS       WP_005302425             142 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Acinetobacter].
ACCESSION   WP_005302425
VERSION     WP_005302425.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..142
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16111
     Region          1..141
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlsyfllfis afgaatllpl qseavlvtll lkgqysalll igtatlgnvl gscvnwwlgl
       61 kieqfkhrkw fpvsekrleq aqrfyhkygf yslllswapi igdpitlvag lfkenfwrfl
      121 givviakagr ylfiywvvmg fi
//
LOCUS       WP_005303244             269 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Aeromonas dhakensis].
ACCESSION   WP_005303244
VERSION     WP_005303244.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (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   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..269
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30002
     Region          5..118
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          175..248
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mmqcrkfqpa pdlapwlaqg wewrlgqpqp mpeifpgtga eilfnlgdpl titilssada
       61 prtvtvatgv avllcprhar lrfaahgqth llglrlrssa cfdlfgvple qlsdrvlsld
      121 elgivcpdpq wlmqagalga wlrrqvasrp prdlalvrai erlyygtpai elqlqlgmsa
      181 rtfqrrlrsh lgvdaryflr tarfqralrq llsgapslda lleqgycdqp hfikschfft
      241 grspgqlltp ehqrlnhysp qinrlagsl
//
LOCUS       WP_005303274             118 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Aeromonas].
ACCESSION   WP_005303274
VERSION     WP_005303274.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..118
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12644
     Region          7..108
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(31,60..61,63,89)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(31..32,40,43,45..46,48,51..52,54,60,65,72)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mrtestpapl nkvarieail alipagrvvs ygqvadlagl pgrarlvgkv lretdkvlpw
       61 hrvlgaagti slpkgsagfd rqagllqeeg vpviggrvrm kewqwqpdla ellfllpf
//
LOCUS       WP_005304061             385 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Acinetobacter
            sp. NIPH 542].
ACCESSION   WP_005304061
VERSION     WP_005304061.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. NIPH 542
  ORGANISM  Acinetobacter sp. NIPH 542
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 385)
  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 385)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Acinetobacter sp. NIPH 542"
                     /db_xref="taxon:1217688"
     Protein         1..385
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44897
     Region          13..373
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mtsslkqltl fnqglgktsr ftkgvdgtlq aiehlgyvqi dtisvverah hhilwsrvpd
       61 ydlnhlnslv rerqifeywy haasylpikd yryalpamms vrkgesryfn rgdqhlmnei
      121 larvgaegki rlrdidknnk kslgnwwntg pgrrtfeqly mqgdlmicer ngmekvydlt
      181 erclpenidl rmptlyeyaq ylfnntlrah gaftwkqlvh lkkndlkeam rvvlkeqvda
      241 gvvsavklad gqtlyvdvaa ieqklttdfg lkilspfdns lihrdrltsl fefdyriecy
      301 vpaakrvygy fclpilyqde lvgrldckah rsikelevis lhlektikdk ehfffeldqe
      361 lkrfavfnqc ltvndkvikl irtki
//
LOCUS       WP_005305494             663 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Photobacterium damselae].
ACCESSION   WP_005305494
VERSION     WP_005305494.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Photobacterium damselae"
                     /db_xref="taxon:38293"
     Protein         1..663
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=73881
     Region          1..663
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mkysitlltl lpclsygsev ttldevlvvd hnsavlhptr maqekiirnq pgggslitdk
       61 piisarpeda lsqqagvvvq sfsggndqtr lsvrgsgiqs fpptrglaif qngfpindad
      121 gsfnlglvnf sntqfisvlr ganalrsats slggeielfs nqgrqnnqvs yqlgsfgrqn
      181 tfatvggens dgdinlsanl ddydgyrtqs sshrkglsln styflsdhls nslyvdlakl
      241 rfnipgplsk dqleddptqa npmyakakpf rhlenirigd rlsfaqgqqr ydlqlwysht
      301 fddfktpmsr yishintygs slsadiklnd qhhltsylsf dqsdidrsfy aknnasmgvy
      361 nltannlrfn vrdhyqidrn fsviagtdfa lshrngeskh qnldqlyrtf apkigalyqw
      421 naantlftnv sysaevptfw diqdtkgqnv ilkpleqqka ttyeigargs lldswyydla
      481 iyhaivdnei vltyddsgtq mgafnyqgts whqgvelaln ktqhfgstel dynltwtfnr
      541 ytfqsglyqg khlptipdhi itaqikakhg kfgagadmny vptstpvdyv nsgrqeldpy
      601 livnvgvdyq pitdltlwak vdnildenya amsvardkvg sskqptqfpg lgrsvnigfq
      661 yky
//
LOCUS       WP_005306343             275 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Aeromonas dhakensis].
ACCESSION   WP_005306343
VERSION     WP_005306343.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (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   5  (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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..275
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29806
     Region          25..275
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <170..275
                     /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 mdplsillah aapqaslffa gnlcqhshss dypagghlhl lrrgelllre eggeplllte
       61 ptlilyargq ahrleprela gcdlvcasvs fgpagdsplq lalpdtlvlp lqtipaiapv
      121 ltllfeeafa erygqppils rllevllill lrhlveqglc rqgmlaglsd prlaraiaam
      181 hqrgdepwtv atlareagms rarfaahfqa ltgqtpldyl trwrmvlasq qllagesitq
      241 valgagysgg tafgrafere fgmspgrwlk arqre
//
LOCUS       WP_005306915             352 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005306915
VERSION     WP_005306915.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 352)
  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 352)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 352)
  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   4  (residues 1 to 352)
  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 352)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..352
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40604
     Region          29..216
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          265..346
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqdpfglfhe tisisyarll leicekydis aaillentgl slldikqyda kmsahqwskl
       61 vanalrltgn nrlgieygsa lrptahgslg faflscvdve talnlcqhff ctriqsfipn
      121 wtfdeklvyi ylddvhpvkl gdeqqsqqlr afliesllfg gihllelliq enleeceifl
      181 dwcessdyee ilnknikyhf nskrnaiafp lkylkqsnpq gdlvafqqai qycekdkgli
      241 vkdathhlqn sikmellhnf nknypslpei akrlnmsert ikrhlqtqgt sflqllneir
      301 fkeakkllak eqyniqdian ligyeestnf vrafkkysgi tphqyrkklk se
//
LOCUS       WP_005308961             111 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: endonuclease domain-containing protein [Aeromonas].
ACCESSION   WP_005308961
VERSION     WP_005308961.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 111)
  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 111)
  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   3  (residues 1 to 111)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..111
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=13002
     Region          10..102
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mrthpfakrm rreatlaeqk lwlqlrdrrl agvkfrrqmp igpyivdfis leqrliievd
       61 gsqhnepagr qydgartayl nqqgfrvirv wnndvlsrme avlellllsl r
//
LOCUS       WP_005309156             254 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005309156
VERSION     WP_005309156.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 254)
  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 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   3  (residues 1 to 254)
  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   4  (residues 1 to 254)
  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 254)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..254
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29837
     Region          1..254
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          180..254
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mknedqqfsl lnsievhefl yqkedivrph aslwgdfnfs lngilemqve eqiylsppsy
       61 glwippqtvh qsthidheih yicirlhpsl csilgdvckc fsiqpffrtl vlqileqqkq
      121 tekaeylehl lqvlfdqlkq apayshylpq trhpvllpil eklsdpllfd hslqqllqnf
      181 svsdrhllrl sqqelqlsls ewrnrakivy aihqirqgts ikrlaydlgy qhsssfieff
      241 krytgqtpiq mrnn
//
LOCUS       WP_005309492             589 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: M4 family metallopeptidase [Aeromonas].
ACCESSION   WP_005309492
VERSION     WP_005309492.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 589)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 589)
  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 589)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..589
                     /product="M4 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=62623
     Region          1..588
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mnkvylavvl acwgsaalaa eqvdvhqvag iqgapsgaag vsalagdgef rqvravklpn
       61 gqqrvryeqt whgipvwgqv lvaeqslggq isqvsgqilr qidadlaspt aalspadaas
      121 karagakgsn ervklfvmqd dagqaklvyl vswlaaseep srpfvmidaq tgnelkrweg
      181 inhkdatgpg gniktgkyfy gsdfgplqvd dncrmtsanv dtlnmnhatt ggtihqftcp
      241 entvkeinga ysplndahyf gnvvfdmyrn wyntapltfk lkmrvhysrn yenafwdgsq
      301 mtfgdgattf yplvsldvaa hevshgfteq nsglvysgqs ggineafsdm ageaaenymk
      361 gsndwlvgaq ifkgngslry fedptrdgrs ighasdyydg idvhhssgvy nrafyllant
      421 sgwntrkafe vfvlanrlyw ganttfdqga cgvtkaatdl gysvtdvaaa fttvgvnatc
      481 ggttpptgsv lqngvpvtgl saakggklnf tidvpagksq lviassggtg dadlyvkfgs
      541 vptsssydcr pyksgnaetc tlnspkagtw nvqlsafsaf sgvtlkasy
//
LOCUS       WP_005309646             349 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter sp. NIPH 542].
ACCESSION   WP_005309646
VERSION     WP_005309646.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. NIPH 542
  ORGANISM  Acinetobacter sp. NIPH 542
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 349)
  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 349)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 349)
  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   4  (residues 1 to 349)
  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 349)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Acinetobacter sp. NIPH 542"
                     /db_xref="taxon:1217688"
     Protein         1..349
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39954
     Region          <65..206
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          257..332
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqdftisngy fylwntylke rgmdwqalnl tdvqarqvqn ilassidaqs slnfflelle
       61 ltesqlqvsn lalematcit panfgvlgym asrsgsfaev leyimkfhrl vidgeqvvpm
      121 qieqdaskir lywplvddsn iilceltlaa mvqlakqiap lhdfllqqve fvhrargplv
      181 hyqrffqckl sfekpyyalt faseglsirp qhadptlmql lvkqaeeala qrkihtdlaq
      241 qihwivheyf kqkqqapkie diaielnisv rslqrqlqsl ntsfklilda ermrrceill
      301 nqnasltlia eqlgysdqsa larahknltg qtllarkrql qltnknaik
//
LOCUS       WP_005309767             719 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Acinetobacter sp. NIPH
            542].
ACCESSION   WP_005309767
VERSION     WP_005309767.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. NIPH 542
  ORGANISM  Acinetobacter sp. NIPH 542
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 719)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..719
                     /organism="Acinetobacter sp. NIPH 542"
                     /db_xref="taxon:1217688"
     Protein         1..719
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=79369
     Region          31..715
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 msllrldrlh ycilmsmgci sspfvwadds aqniavlptl hveatrtdtt ylqtpasvfr
       61 idapqvdtss qvnltevvkg ipslqlrnre nyaqdlqlsm rgfgarstfg vrgirlyvdg
      121 ipatmpdgqg qtsnidlssl dhvevltgpf sslygnssgg tiltstkegq gkdsielsys
      181 ggshdksrag lvlqggakga nepsyvisss yfdtdgyreh sgaekvlnna klswnlddgs
      241 kinwitnyvk ihaddpmgle rkdwqenpkq iapyvknmgf narkdieqtq tgvtwskpin
      301 dqnelyamay lgnrqvtqyq aipngatsqk lpthagavid fernyygadf rwtgkellpn
      361 ttfsagiald nmdedrqgyn nfvmvngkes ygvkgnlrrd edntlwnidp ylqaswqflp
      421 twrldtgvry snvhykskdn ylsngddsgk tdynkvlpsa alswqilpel mayvsyakgf
      481 etptftemay qtdtlksgfn fdlkpstsdt yetglktqnl lgdftlavfq tktkndivsa
      541 gslggrstfr nadktlrega efawnkklwr dltatasyty ldatfdasvp eklgqdgkvl
      601 asaitsgnai pgiaknqaya slawqpshgl yggvdvqymd kvyvndtnsd aapsysvtsa
      661 nvgyawvmgd wkvnsfarvd nlfdknyags vivndgngry fepadgrnws aglrvikqf
//
LOCUS       WP_005309898             341 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter sp. NIPH 542].
ACCESSION   WP_005309898
VERSION     WP_005309898.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. NIPH 542
  ORGANISM  Acinetobacter sp. NIPH 542
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 341)
  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   6  (residues 1 to 341)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Acinetobacter sp. NIPH 542"
                     /db_xref="taxon:1217688"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38182
     Region          21..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <238..336
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mnpelpgtyi nllvetvkrw gvsgeqlldg sgitleelkk pywyvelnml nelveraiel
       61 ckepalaghl alsmtascyg svgmaaivsp nlgealkile qfigsrckvf kpelkqddnd
      121 acwsihqpvn afqlspnani fllvgfvqia kkltglshlg kvelqmpepv gfsqighqlv
      181 vtclfnqkcn rwifpkeyla qpvltadpml apllnaqckr dieklklksg wkgqvkqvae
      241 klllngeiqa lkvgqvahim nmsertlqry laldqtsftf lvdslkkeqa qkllaqnnms
      301 iekvalmlgy aetshftraf krwmgvtpky fqtqqkmddl s
//
LOCUS       WP_005309916             421 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces
            pristinaespiralis].
ACCESSION   WP_005309916
VERSION     WP_005309916.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pristinaespiralis
  ORGANISM  Streptomyces pristinaespiralis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 421)
  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 421)
  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
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 421)
  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   5  (residues 1 to 421)
  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   6  (residues 1 to 421)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 421)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 421)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Streptomyces pristinaespiralis"
                     /db_xref="taxon:38300"
     Protein         1..421
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43359
     Region          18..>69
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          81..388
                     /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 mqmptgvhal vrrtheervm ralrengams rgeiarvvgl srttlseitg sllqrgaivv
       61 vdtdasrreg sgrpaerlal dpasaqfmgv dfghrrvhvv iadasheima sdsvryddta
      121 dwrtrtelal glvdrlgtgt gvhygalqgi gigvpgpypa pegaawprat pgatvlrpap
      181 egvdvafaer fdapvivdnn trlaalaeai sgadsvadlv yvrlsdgvgg glvvggqlvt
      241 gsaglagelg hvtvepagrp crcgkrgcle tvasvpgils acwefglrle nlqdlaaava
      301 aahpvadrvl reaaaalgrv vgaatmtlnp akvviggeit rlapviveqv aatlaaelfp
      361 tapagpvvea arlsdddgai galaavfhss pllarypgtt dvkgrsdarr sttegaahvr
      421 p
//
LOCUS       WP_005310347             262 aa            linear   BCT 20-JAN-2025
DEFINITION  formate dehydrogenase accessory sulfurtransferase FdhD [Aeromonas
            salmonicida].
ACCESSION   WP_005310347
VERSION     WP_005310347.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas salmonicida
  ORGANISM  Aeromonas salmonicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Aeromonas salmonicida"
                     /db_xref="taxon:645"
     Protein         1..262
                     /product="formate dehydrogenase accessory
                     sulfurtransferase FdhD"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0097163 - sulfur carrier activity
                     [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28484
     Region          14..247
                     /region_name="FdhD"
                     /note="Formate dehydrogenase assembly factor FdhD, a
                     sulfurtransferase [Energy production and conversion];
                     COG1526"
                     /db_xref="CDD:441135"
ORIGIN      
        1 mvqpaihhal psldhlveev avsiningin havmmatpdd lddfaigflf cesiirhnhd
       61 vhdirvspae hgfvldvtia nrclaqlqqr rrrltgatgc gicgveaveq afpplpalpl
      121 tppldvalla elrpqiarwq lkgqhsgalh aalaldehgl ilhcredigr hnaldkligl
      181 llrqpqacdt lvvtsrcgse lvqkaalfga rhlvclasps qlavrlalky nlnvvhipkf
      241 dapvsyssyr padpigeche sy
//
LOCUS       WP_005312752             305 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Acinetobacter].
ACCESSION   WP_005312752
VERSION     WP_005312752.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   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 305)
  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 10617438
            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="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33930
     Region          16..67
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msldatiwaw raevqnssqr lvlltladra genhkcfpsl krmekdtkln rktiikvlde
       61 lesgklikft getagngvki yqligvlgre eetltntkng tstnnrtgsn lgtgskngts
      121 tnigmptste ngtatstnig tqnlpmnlpi esinkkhwlc skklsleiaq anpainpnev
      181 isstwfnref rafeifnaek tmcddlmiyh fanwlleaka kmdrlnrsaq pnhkpeskap
      241 ltekqikfla gklsrlpdfg kyavgneshe qlavrletml kdpknlekws eyltevgfkq
      301 kgaaa
//
LOCUS       WP_005315627             152 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Aeromonas].
ACCESSION   WP_005315627
VERSION     WP_005315627.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            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="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16371
     Region          4..152
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 miekqafyrg lnqqaqalle gepdlianla nlsallalel tdinwvgfyl lqgdtlvlgp
       61 fqgkpacvri pvgrgvcgta vaegktqlid dvhqfeghia cdgasnaeiv ipvrrggeii
      121 gvldidspif nrfdekdrig leetvqiles ml
//
LOCUS       WP_005315874             304 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            pristinaespiralis].
ACCESSION   WP_005315874
VERSION     WP_005315874.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pristinaespiralis
  ORGANISM  Streptomyces pristinaespiralis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptomyces pristinaespiralis"
                     /db_xref="taxon:38300"
     Protein         1..304
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33673
     Region          2..60
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          80..256
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 maalfgsrvr rlrtaagltq aqlgakthvv stritqvera sgarptlela raldaalgad
       61 gllvdlwphv yresfpdwsr tfmaysaqaa airqytghvv pgllqteeya ravlsvglsh
      121 rneehleerl tarlerqkrl dppdppella ildetvlrkr iggddvmrrq larlleaaaq
      181 phitvlvlpf degahdvlgg sltvltlpdg sevaytegad hgqlfedpad vrrfavaydr
      241 lraaalpprr slhmirsame edyrdpnlps rsarrrlaqe qlqqsggrrl rrggrrnprr
      301 gsgt
//
LOCUS       WP_005316275             217 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            pristinaespiralis].
ACCESSION   WP_005316275
VERSION     WP_005316275.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pristinaespiralis
  ORGANISM  Streptomyces pristinaespiralis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 217)
  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 217)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Streptomyces pristinaespiralis"
                     /db_xref="taxon:38300"
     Protein         1..217
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=23066
     Region          44..94
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mavaqlnapl casppvpavg irhinlphne rfvvvgnhla qhdrlsltai glsvhiqslr
       61 tgtrisvkkl aerfpegedr isdalneler ygylrrtrvr lpsgqlittt esfsnppamr
      121 vrapgqpapv pqreapppsv eppvpdpvag pepvplrqqt gprprptell ppplpaappg
      181 asrpdpfqtc dacdlafrap epglcsacap vavlvas
//
LOCUS       WP_005316427             945 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Streptomyces pristinaespiralis].
ACCESSION   WP_005316427
VERSION     WP_005316427.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pristinaespiralis
  ORGANISM  Streptomyces pristinaespiralis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 945)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 945)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 945)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..945
                     /organism="Streptomyces pristinaespiralis"
                     /db_xref="taxon:38300"
     Protein         1..945
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=102709
     Region          36..941
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mpanttassp kkkkgrrarl lvlvlvlalv agvgygayws istvrasfpq ttgsvqlagl
       61 ggkvevkrdg hgipqiyadt dedlfraqgf vqaqdrfwem dvrrhmtagr lsemfgsgqv
      121 etdaflrtlg wrhvaqeeyd tklsaetkky lqaysegvna ylkgrsaeei sveyaalsft
      181 ndykpepwsp vdsvawlkam awdlrgnmks eidrslltsr lsekqikdly psypfernkp
      241 iveeggisqv tgkfdpaakp sdledgstgg dtgdgtgtgd gtgtgtgtgt gdgtgtgsag
      301 gaadassgps sqlaalsdsi davpallgps gngigsnswv vgggytttgk pllandphla
      361 pqlpslwyqm glhcretsek crydvagytf sgmpgviigh nqdiawgftn lgadvtdlyl
      421 ekltgdsylv gdeekqlttr kevikvagga sktitvrstg hgplvsdrsd elekvgekap
      481 vsnaapdras gygvalqwta lqpgrtmdav felnrakdfq sfrkaaqnfe vpsqnliyad
      541 tkgnigyqap gripvraqgd gstpapgwdp aykwtdyipf delpyeynpd rgyivtanqa
      601 vidaekypyl itkdygygar sqrindlies kiqdggkist edmrtmqtdn sseiaklltp
      661 yllkidvsdp yvreaqklle gwdytqepds gaaayfnavw rnvlklafgn klpkelrveg
      721 eclsvrpads tapdddleer vrecgqrdpd saqpdggdrw fevvrrllkd edntwwqspr
      781 trteqatdtr dellgramad arweltarlg kdasswswgr lhqltltnqt lgtngpgflq
      841 tilnrgpwnl gggeaavnat gwnaaggyev vwvpsmrmvv nvgewdesrw inltgasgha
      901 ynahytdqtd mwangelldw aysaqavsag tadtltlvpp ghsvp
//
LOCUS       WP_005316631             256 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Streptomyces pristinaespiralis].
ACCESSION   WP_005316631
VERSION     WP_005316631.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pristinaespiralis
  ORGANISM  Streptomyces pristinaespiralis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptomyces pristinaespiralis"
                     /db_xref="taxon:38300"
     Protein         1..256
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=27052
     Region          116..253
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mnrhgvvgrg aavllaalll tgcdglgide ggaegdggps rgapaaggts planprgtep
       61 glaalvteqe raaareligk vdtkgrgprt gydrdeygya wmdtadgvpl arngcdtrnd
      121 llardgkela frdgsdcvvv amtihdpytg rtiewrkqda aevqidhvvp lsyswqmgaa
      181 rwdeakrrrl andplnllpv egransaksd sgpaswlpps kpvrcsyavr faqvavkyel
      241 pvtgadkrim laqcgg
//
LOCUS       WP_005317513             573 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Acinetobacter higginsii].
ACCESSION   WP_005317513
VERSION     WP_005317513.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter higginsii
  ORGANISM  Acinetobacter higginsii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Acinetobacter higginsii"
                     /db_xref="taxon:70347"
     Protein         1..573
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=65401
     Region          3..>459
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mptlnwigke avekhhkevp yrllepvagl scnedeqggn llvqgdnlha lkallpryag
       61 kvdciyidpp yntgnegwiy ndnvnspeir kwlgeivgke getldrhdrw lcmmyprlsm
      121 lksflkeegv ilisiddnev anlrlimdei wgvnnficql vwekgrknda kyvsvgheyi
      181 liyarnknkl keknikwrek kpgadeilie lnrlrtlykn dyasiekdls kfyknlakdh
      241 pskkhsrysk vdnkgiwrdd nmswpkpdgp kynvihpvtg lpcaippngw rystlekmqe
      301 qiglgkvvfr edhseppirk tyliqtsede fddesavqva gsyfyrsalq aknelrdifk
      361 keifdypkds dvlarwidyv tpkdglvlds fagsgttaha vlklnanfgs nrkfilvemd
      421 kniatkvtfe rikrvtkgyi nrngediegl gssfqfckls qeplfnasgh irndvsfsql
      481 aefvwfcetg tgytgkadsp llgiyegrai yllyngilkd lteqggnilt kqvfdvlpkf
      541 egvkviyaaa nrlggkakre nivfkqtpya lev
//
LOCUS       WP_005317534             335 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005317534
VERSION     WP_005317534.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 335)
  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 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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 335)
  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   5  (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   6  (residues 1 to 335)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38676
     Region          51..193
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          82..330
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msqlknytgs vfgglghllk ayceaenihi peqlqqvqnl erfdyviwrd lledlnrlhp
       61 nsglgleiaa yvqpkhlgii aylalscenl gealaryhdf hrliydgspl vvefnhpyas
      121 irweapephp tqltdeiaia lmvqflklfm sgdtihlhev hfvnaapkni siyeqyfhck
      181 vrfeqpktql llpvseafkp lktgdhtlqq lllqqaqall dklpnstqld qrlqhailtg
      241 lqknqyqidf iaeklglsvr qlqrhlqqqn ttfqervqqv rfmlateylk dphlslqeia
      301 lllcyseqsa fqrafkiwtg qtpqqwrnnn ityns
//
LOCUS       WP_005317124             392 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces
            pristinaespiralis].
ACCESSION   WP_005317124
VERSION     WP_005317124.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pristinaespiralis
  ORGANISM  Streptomyces pristinaespiralis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 392)
  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 392)
  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
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 392)
  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   5  (residues 1 to 392)
  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   6  (residues 1 to 392)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 392)
  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 20283677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Streptomyces pristinaespiralis"
                     /db_xref="taxon:38300"
     Protein         1..392
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39734
     Region          20..65
                     /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(34,36..38,47)
                     /site_type="other"
                     /note="non-specific DNA interactions [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            47..53
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            order(48..49,53)
                     /site_type="other"
                     /note="sequence specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238044"
     Site            48..49
                     /site_type="other"
                     /note="putative cAMP binding site [chemical binding]"
                     /db_xref="CDD:238044"
     Region          84..362
                     /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 mnrsmagvga nlpalrshna alvldllrta geggisrlel aegtgltpqa vskivarlre
       61 egtvaeagqr astggkprtv lrlvpsagya lgvhldrdel tvvlldlagt rvagrrvpld
      121 lgagteavva ktvaevgvll adadpagpag pvlgdaglrv lgvgvampgp ldhfngvtqr
      181 vtgypqwegf plrdvlagrl glpvvldkdt naaalgialr gpgdsfaylh lgtglgaglv
      241 lggvlyrgar tdagefghqv iqldgpectc grrgcievlc leavargdie gaarllgvga
      301 tnlvelldie rvllggrvid daadefvggv ravlaartdv pvaaaaegge qivadgaaql
      361 vlaplfgrse avspaaasqe epqanrpape ir
//
LOCUS       WP_005318196             253 aa            linear   BCT 20-JAN-2025
DEFINITION  phosphonate ABC transporter ATP-binding protein [Aeromonas
            salmonicida].
ACCESSION   WP_005318196
VERSION     WP_005318196.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas salmonicida
  ORGANISM  Aeromonas salmonicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
REFERENCE   2  (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   3  (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   4  (residues 1 to 253)
  AUTHORS   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 253)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Aeromonas salmonicida"
                     /db_xref="taxon:645"
     Protein         1..253
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=26884
     Region          14..248
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 miavalngag lrlgesrilh plrlqieage cvaiigpsga gktsllrlig telrgelals
       61 lwgedpwals trarqrlrsr igmvwqqppl pasqpvvtav lagrlgqwsl vrallsllrp
      121 cdpdgarael arlgladkwq qrcgelsggq lqrvgiarvl yqqpdlmlad epvsaldpvl
      181 aqssldalla qarthgstli aslhavelal erfpriiglr egrvqfdcpa tavtpamlga
      241 lyagdqealp cvg
//
LOCUS       WP_005318260             280 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            pristinaespiralis].
ACCESSION   WP_005318260
VERSION     WP_005318260.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pristinaespiralis
  ORGANISM  Streptomyces pristinaespiralis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 280)
  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 280)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Streptomyces pristinaespiralis"
                     /db_xref="taxon:38300"
     Protein         1..280
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30677
     Region          20..70
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          93..267
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 msdvrhinal dpgaspldyy gyelrrhret agltqkqlga ivnytgslvg qvetarklpt
       61 aefservdaa lgtggllsrl lglvlrsqlp awfqqvaele arateictfh thlvhgllqt
      121 rgyaravlga mevanlddrt tvrlarqsif gkqaspvlwa ifgeaalrqe iggpevmrtq
      181 lrhllsytdd prvniqvlpf kagvhaglqg sfdlfhftsd psilytegyg tghptanpdt
      241 vkdcslrydh lqaaalsikd saqlirdime erygehdgva
//
LOCUS       WP_005318862             386 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Streptomyces pristinaespiralis].
ACCESSION   WP_005318862
VERSION     WP_005318862.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pristinaespiralis
  ORGANISM  Streptomyces pristinaespiralis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 386)
  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 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   3  (residues 1 to 386)
  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   4  (residues 1 to 386)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 386)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 386)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 386)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces pristinaespiralis"
                     /db_xref="taxon:38300"
     Protein         1..386
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40213
     Region          35..370
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(108..110,131..132,183,234,258)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mlnktivkla iplavgalal tgcgsdsgsg dgavkiafqg plsgdnvalg enmqngvkla
       61 idqanakgdl dfkieyvagd dqglpdkata taqkiiddpg vvavvgpafs gptntssply
      121 aesglvtvsp satnplltdk engftsflrg vpndnmqgag matyyakklq akkvylvddk
      181 tdygvglatv aekglkdagi evvkksvpqk tpdysatakd vvnskadali yagyyqdaap
      241 fakklkdagy kgaaisgdgt ndmkfvelag dasenwfltc pctdatveag tkkfaedyqk
      301 efgrapgtys aeaydianmi iaevkkagad verealrdal akasykgltk tfsfgengef
      361 kgtdvylyqv kggkigyqgn inelag
//
LOCUS       WP_005320287             388 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Streptomyces pristinaespiralis].
ACCESSION   WP_005320287
VERSION     WP_005320287.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pristinaespiralis
  ORGANISM  Streptomyces pristinaespiralis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Streptomyces pristinaespiralis"
                     /db_xref="taxon:38300"
     Protein         1..388
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41868
     Region          1..270
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          266..357
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrllhtsdwh lgrsfhrvsm ldaqaafldh lvatvrerev davlvagdvy dravpplaav
       61 alfddalhrl adagvptvmi sgnhdsarrl gvgaglidra gihlrtdpag cgtpvllade
      121 hgpvacyglp ylepslvrae fgtekaahes vlaaamerir adlatreegt rsvvlahafv
      181 mggeesdser ditvggvcav pagvfrgvdy valghlhgcq titerirysg splaysfset
      241 dhrktmwlvd ldasgavtae riecpvprpl arlrgsieel lespeldrhe esfveatltd
      301 avrpadpmar ltrrfphvls lvfepdraps dasasyaqrl rgrsdqqiae dfvahvrggn
      361 gpddgertvl rtafedvrvd agvrevag
//
LOCUS       WP_005320544             366 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Streptomyces pristinaespiralis].
ACCESSION   WP_005320544
VERSION     WP_005320544.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pristinaespiralis
  ORGANISM  Streptomyces pristinaespiralis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Streptomyces pristinaespiralis"
                     /db_xref="taxon:38300"
     Protein         1..366
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34715
     Region          <20..202
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          183..>359
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mmnairrrrp gcrvllscca nvfaaaaivg lgateagaqv ptcfgvpatt tgttgtsgrd
       61 vivgtagpdv inglggddli cglggddrlr ggpgndsidg gdgndgvvgd sfdatgvtga
      121 tgtdrllgga gddslvgdns agfqgtasga ardslyggpg ddslvgdtng esasggasdr
      181 leggegndgl igdsvaffna sgagddvlle gpgelgdatg dsvsivgnas gaggddivdl
      241 gadggtiaig dhaasqgtai gsgndritgg sagefeivgd sglgdpsgat aghdqisgrg
      301 gddvlfgdnv gpdgsvttvg gsdridagsg ndtlrggpan dflngssgtd dcdgeagvdf
      361 etncev
//
LOCUS       WP_005321177             828 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Streptomyces
            pristinaespiralis].
ACCESSION   WP_005321177
VERSION     WP_005321177.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pristinaespiralis
  ORGANISM  Streptomyces pristinaespiralis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 828)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 828)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 828)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..828
                     /organism="Streptomyces pristinaespiralis"
                     /db_xref="taxon:38300"
     Protein         1..828
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=90060
     Region          43..779
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 meesvdriae pwggrtpypr hgawptrvdt hlargvaehe vqrwvqsasi lhsdgdamdi
       61 avkdgrmvgv rgravdrvnr grlgpkdlfa wqanaspdrl trplirqdgr lvetdwptam
      121 drvvarsrel ldergpgsig fytsgqlfle eyytlavlar agirtnhldg ntrlctstaa
      181 ealkesfgcd gqpgsyddid hadvialfgh nlaetqpvqw mrvldrlega dpprlvcvdp
      241 rptqvarhat vhlaprvgtn vallnallhe tirhdrvdha yieahtvgfe elaarvkdct
      301 aewaaavcdv parliveaae vlggadrlls tvlqgvyqsh qataaavqin nlhlirgmlg
      361 rpgagvlqmn gqptaqntre cgangdlpgf rnwendehva dlaevwnvep atiphyappt
      421 hamqifryae qgsvrmlwis gtnpavslpe larirsilsg erlfvvvqdl fltetaqlad
      481 vvlpaatwge ktgtftnadr tvhlsdkave ppgearpdld ifldyaarmd frdkdggpli
      541 pwhdpesafe awkrcsagrp cdytglsygl lrggsgiqwp ctkddpsgtp rlytdgiswa
      601 hpdrceaygk dlvtgastsv veyrslnpdg kamlkaaefl plheapsqdy pfqlttgrtv
      661 yhfhtrtktg rapqlnaaap dvwveisead aaardlaegd lvevgsprgs lrgrlrvtgl
      721 rrgtlfvpfh ygywdtpags gpnatvpgra anettitdwd aaskqplfkt aaatltlvek
      781 gggqhspapt ttasrpgrda gvpatqggpd alarqttddr pareggrr
//
LOCUS       WP_005321617             331 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            pristinaespiralis].
ACCESSION   WP_005321617
VERSION     WP_005321617.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces pristinaespiralis
  ORGANISM  Streptomyces pristinaespiralis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces pristinaespiralis"
                     /db_xref="taxon:38300"
     Protein         1..331
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=35859
     Region          1..253
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mkfrilgpve vhdertgvri lptgakqral lgalvvksgq ivsvhrlide lwgeqppana
       61 tnalqahvar lrrllpvpep gsgephhewi vtrslgyvlr lgragtdadr fhrlaaqgra
      121 aaatdpeqaa ellrqalalw rgpalegsvl gdicaaeaaq leenrltale alydaclraa
      181 rhgeitgele elttdhpmre rfydllmlal yrcgrqaeal svydrarrrl vhelgvepgp
      241 alrgrmeail qhdprlaapg pagqlarvhp lppppapapt apgpaggpda tvlnltgeia
      301 rlrsriehls leqealmrrf dqlvanpasg h
//
LOCUS       WP_005323031             725 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor family protein
            [Acinetobacter].
ACCESSION   WP_005323031
VERSION     WP_005323031.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 725)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..725
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..725
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=79476
     Region          37..725
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mlgnqlmkcs fshpvsfskf kpstlscait aliscvattt faddsqsntt qtlatisiqa
       61 egnwleqana kkvlnhpgar tvvdqqslea rgttsvkeal rtvpgvqvse nsgtsgsdas
      121 lsigvrglts rfsprsqlmi dgvplavapy gqpqlslapt tlgnmesidv vrgagsvrfg
      181 pqnvggiinf ntrsipenfa asvgmtteva engnlkvnpn lfvgttldng lglallysgv
      241 ngdgyrdqnd ysnindlrlk asyalddyss ieanlhryea kvdmpggltp aqyaqnpyqs
      301 lrnhdymegn rndislkyny kkdnnafevl tyhldsyrda gversgssly qiaprdykvt
      361 aiepryshaf qlgdtlnevs vgyrylkets sesvdranyn rdtgpsdfyg wtkadgdtea
      421 havyvdnrtd lgawsftpgi rferiktnen myklnrdysv lngvnasksy davlpsfavm
      481 ykandqwnif anygksfapl qysqmantna rgayltmdgl npekadnyei gthylddyls
      541 leftlfyidf adqlkrddat qtysnlgatk hkgaelgfky nlgainddla nvsmyantty
      601 tkatasagqd sgneldfysn wvgnagvdyk rdqwtfntnv yaqsrqtasg nnndgtgryg
      661 nipgygivgv raaydfadts lsglkvglgv knlfnqdyyt rsadqvggiy agpsrtyylq
      721 tsfdf
//
LOCUS       WP_005323033             737 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor family protein
            [Acinetobacter].
ACCESSION   WP_005323033
VERSION     WP_005323033.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 737)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..737
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=80176
     Region          23..737
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mkiascsaas likfqpssls laiaislsgi shvafadegq paetqtlati siqaqgnwld
       61 nanaekvqqh agarsiidrk rldeiattsi rdalkqipgv qvqdsngtgg sdvslnigvr
      121 gltsrlsprs tvlmdgvpls fapygqpqls lapvsmgnie svdvvrgags vrfgpqnvgg
      181 iinfttraip kefsgsvglt tefatgtdql kytpnlfigg tldnglgmal lysgskgday
      241 reannkidid dvmlktayqw tdqdaiafnl hhyegrgemp egltaaqfad nayqsnqsrn
      301 yfagrrsdvs vkyshkdeln nfevlgyyvd sfrtsdlesv anngtsrisn sprdykyfgi
      361 eprysraysw agmdnevtvg yrylqeesse fsgrtasynt ltgtpseria nttseggtka
      421 haiyidnrfg lanwvitpgv rfesidthnd ftayqngvat ntvypkiksd eflpslsvly
      481 kanenwnifa nagvsfgpqq ynqlvttksv ggvntaattl dglhpekskn yeigtkylsn
      541 glsaeltvfy ldfdkelmle rpdnigtgiw tdlgatshkg vetgisydfg qladaleglk
      601 vygnytftka tseagkfegk dlpfysrhvg nlglayhvdq wsvnadmfaq skqhapgsgd
      661 vyqteetadg rtgdipgyst favrtgydfs nqlkglkiag giknvfdkqy ytrssdstgg
      721 kyvgqprtff lqtsydf
//
LOCUS       WP_005324099             230 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Corynebacterium].
ACCESSION   WP_005324099
VERSION     WP_005324099.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 230)
  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   2  (residues 1 to 230)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..230
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=23613
     Region          <85..>112
                     /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"
     Region          172..229
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 maapkiserl reftqptgee ellavdyprp rlrispwqac avavilvigv vvwlginars
       61 eessgmpepa alseapseep seiivsvige vaepglktle pgarvadald aaqplpgaet
      121 malnhaqrls dgqqlhilps gaapapapge papagensss pggsasgsgv slnsataeel
      181 telkgigevt aqaivayree hggfkdveel levsgigpak laqlkdqvql
//
LOCUS       WP_005325691             291 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phytoene/squalene synthase family protein
            [Corynebacterium].
ACCESSION   WP_005325691
VERSION     WP_005325691.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..291
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31528
     Region          6..278
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mltrydqaas raaaqvmgqy stsfslatrl lrgrvradir hlyavvriad elvdgaaaqa
       61 htdpaaalda yektilaapq qrlhtdpvvh ayaitarrcg fhrehlvaff ssmradlthr
      121 eyspselqdy iygsaeaigl lclqiflaee nvspadraam ergaralgsa fqkinflrdl
      181 redsstlgrt yfqqapsgri deatksalia eirrelataa ltidllpasa rvgvsaaadi
      241 faeltnrlaa tpatalattr vsvpnhtkaw laaravrrrg hssqisptge n
//
LOCUS       WP_005326367             377 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator
            [Corynebacterium].
ACCESSION   WP_005326367
VERSION     WP_005326367.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
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
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 377)
  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   5  (residues 1 to 377)
  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   6  (residues 1 to 377)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 377)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..377
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40023
     Region          19..68
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          87..353
                     /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 mikpgpvftr prtpaakclh lvrlnpiitr selveatgls qptitratts llnagliqer
       61 tdltqsrgrg rptvpleaad ndwalggiav gtkqtyigly dtkgrtlsee elttpvanls
      121 eddflehima ginrmmtsln hrlvslgvtt sgtvddnglv taenlnwhgv diaerlrfqf
      181 gvpvvvssai pailgsetqa aeigtservl vlfaddsigs alsvedevsp iipvpathse
      241 llghgtsehl latqhileav rhegveaasl adaaqvansh pavrailder arqlgaitae
      301 lvkdnspatv viaggaftdd pkapkqfaat vrasagkelq lrmipghkei vravartvat
      361 dqllrqpldl grslqha
//
LOCUS       WP_005327162             248 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Aeromonas media].
ACCESSION   WP_005327162
VERSION     WP_005327162.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas media
  ORGANISM  Aeromonas media
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 248)
  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 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   3  (residues 1 to 248)
  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   4  (residues 1 to 248)
  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 248)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Aeromonas media"
                     /db_xref="taxon:651"
     Protein         1..248
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27304
     Region          1..248
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <142..248
                     /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 mtrpgaassl sapcpfslrr yqsdisshsh dfaqlvipld gpleievqgq grrlapgfac
       61 viapglrhdy aadpalsflv qeshwlpeal gerpfiplde pqrhylaflh qmvrqgrhva
      121 gmeqvwlall aqsqgmgptl aprmtrvqch ieahlaeplg nerlaavacl gqsqfkhafr
      181 qqfgmsashy irsrrmalar tllaqtalpi gevasrcgyq dqgafaerfl aetgltpsrw
      241 rqqngpqp
//
LOCUS       WP_005328006             261 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Corynebacterium
            tuberculostearicum].
ACCESSION   WP_005328006
VERSION     WP_005328006.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium tuberculostearicum
  ORGANISM  Corynebacterium tuberculostearicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Corynebacterium tuberculostearicum"
                     /db_xref="taxon:38304"
     Protein         1..261
                     /product="formate/nitrite transporter family protein"
                     /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=27054
     Region          18..233
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mslndaakaa avkkvtllde sfsrfavrst lagvylcigt afagvvgqav ngvapgmgav
       61 afslffgvgl failllgael atgnmmymvy aasnkhvswg kalylllitt ifnlvgaiif
      121 aaimamsakf adldpshllv tvsegkltks pqgmlveaia anfvvnmgiv gavfakdaas
      181 kffviipiig afvalglehv ianfclfsit lfasdpvpaa ltagnvalnw ilvwignlig
      241 gglliggvya wlnrgpeayr d
//
LOCUS       WP_005328298             132 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Acinetobacter sp. CIP 102143].
ACCESSION   WP_005328298
VERSION     WP_005328298.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CIP 102143
  ORGANISM  Acinetobacter sp. CIP 102143
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Acinetobacter sp. CIP 102143"
                     /db_xref="taxon:1144666"
     Protein         1..132
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=13415
     Region          1..130
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mivvaiigil aavaipayqd yttrakvsev itagaackts vaeyyqstgs lpvnteqagc
       61 ssnatpmvks lavdkgvitv tasdslaakf ststkntyvl rptatsaaap ltwsctgsti
      121 egkylpaecr gt
//
LOCUS       WP_005331830             353 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Dorea
            formicigenerans].
ACCESSION   WP_005331830
VERSION     WP_005331830.1
KEYWORDS    RefSeq.
SOURCE      Dorea formicigenerans
  ORGANISM  Dorea formicigenerans
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Dorea.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Dorea formicigenerans"
                     /db_xref="taxon:39486"
     Protein         1..353
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=40284
     Region          1..341
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mgikvdikrk lgefsldihf qteskrigil gasgcgksmt lksiagietp dfgmiqiddk
       61 vlfdsankvd lkpqkrnvgy lfqnyalfpt mtvakniaag lkgskeekqk kvqemiekfe
      121 ltgladrlpg qlsggqqqrv alarimayep dvilldepfs aldvflkdrl qqeliemlkd
      181 yegtvimvsh srdeiyrfse ellimdqgkp viygetkeif akpvykeaak ltgcknfsri
      241 krvdahtaei ldwgitlhtn qeideqatwf gyrahdfvpv wgkrkenclk inveseaalp
      301 fernyylype geenqnkqti cwflqrkkle kigekgmpdy lelteegmmf lrg
//
LOCUS       WP_005333651             426 aa            linear   BCT 20-JAN-2025
DEFINITION  galactokinase [Dorea formicigenerans].
ACCESSION   WP_005333651
VERSION     WP_005333651.1
KEYWORDS    RefSeq.
SOURCE      Dorea formicigenerans
  ORGANISM  Dorea formicigenerans
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Dorea.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   McAuley,M., Kristiansson,H., Huang,M., Pey,A.L. and Timson,D.J.
  TITLE     Galactokinase promiscuity: a question of flexibility?
  JOURNAL   Biochem Soc Trans 44 (1), 116-122 (2016)
   PUBMED   26862196
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Holden,H.M., Thoden,J.B., Timson,D.J. and Reece,R.J.
  TITLE     Galactokinase: structure, function and role in type II galactosemia
  JOURNAL   Cell Mol Life Sci 61 (19-20), 2471-2484 (2004)
   PUBMED   15526155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Dorea formicigenerans"
                     /db_xref="taxon:39486"
     Protein         1..426
                     /product="galactokinase"
                     /EC_number="2.7.1.6"
                     /GO_function="GO:0004335 - galactokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0005534 - galactose binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0046835 - carbohydrate phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=45455
     Region          34..405
                     /region_name="GalK"
                     /note="Galactokinase [Carbohydrate transport and
                     metabolism]; COG0153"
                     /db_xref="CDD:439923"
ORIGIN      
        1 mkkwndvyqm vkngdldasl lktgcenlka arerathvme gfkesfgate dtmvalcsap
       61 grteicgnht dhqhgrvlaa avnldflacv alngtsvvhf qsegwpmtsv nladlevkee
      121 ekettaslir gvlaklhkag ypvagfdmyv tstvlpgsgl sssaacevli gttgnhlfcq
      181 dkfdaveiak igqaaeneyf gkpcglmdqt assvgdavai dfkdpanpiv rsinadltgl
      241 glalciidcg adhaaltney asipeemskv aahfgkkvlr evkeedllad laqvrkeagd
      301 ravlralhfy addrraaeea dalerkdkea flnlvkesgr sswellqnit paaaithqdm
      361 avalavaeka lngkgacrvh gggfagtiqa fvpvedvcef kktmetmlse gcchvlsirp
      421 agglil
//
LOCUS       WP_005335069             408 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Aeromonas
            veronii].
ACCESSION   WP_005335069
VERSION     WP_005335069.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas veronii (Aeromonas ichthiosmia)
  ORGANISM  Aeromonas veronii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 408)
  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 408)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Aeromonas veronii"
                     /db_xref="taxon:654"
     Protein         1..408
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46969
     Region          1..401
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 msithlslqd arhlqlaaqg llaprrskat padllatirr mallqidtis vvarspylvl
       61 fsrlgqyepr wleqlladge ifeywaheac fvpredyrll rhrmldpaam gwkfsanwla
      121 thqqeigqli erirqhgpvr aadferttgk gngwwdwkpe krhlevlfts gqlmvrerrn
      181 fqrvydlaer vipewsdqrd lpsveqaqrd mvrascralg lvktgwvady yrlrrgkyda
      241 llhqladege llpirvegwq hgafvhasla delaraqagt lkathttils pfdplvwdrk
      301 raselfnfdy riecytpapk rqygyfvlpl lhrgklvgrm dakahrqqgi feikslylea
      361 gvrvtrtlaq dlakalqkla dwhqtpqlry gaipanllal whesasak
//
LOCUS       WP_005334890             118 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Aeromonas].
ACCESSION   WP_005334890
VERSION     WP_005334890.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..118
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12600
     Region          7..108
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(31,60..61,63,89)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(31..32,40,43,45..46,48,51..52,54,60,65,74)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 msiepspspl nkaarieaii alipagrvvs ygqvadlagl pgrarlvgkv lretdkvlpw
       61 hrvlgaagti slpkgspgfa eqtgrlqqeg vvviggrvrm kewqwqpdla ellfllpf
//
LOCUS       WP_005335308             211 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Aeromonas veronii].
ACCESSION   WP_005335308
VERSION     WP_005335308.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas veronii (Aeromonas ichthiosmia)
  ORGANISM  Aeromonas veronii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 211)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Aeromonas veronii"
                     /db_xref="taxon:654"
     Protein         1..211
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=23723
     Region          46..210
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mrqargnidw qggwlllpll lisliwssta daswdqslyr qlglagkldk qtfrqalnsy
       61 qtvrhkrkpi ltiidyskps tqrrlfvidm krhkllyhtw vshgrnsgel aakrfsnqln
      121 srqsslgvyr taetylgkhg yslrldglsp gknsnarkra ivvhgaayas pthlrkydkl
      181 grswgcpalp keqaraiidt ikggsviyah g
//
LOCUS       WP_005335506             197 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Aeromonas veronii].
ACCESSION   WP_005335506
VERSION     WP_005335506.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas veronii (Aeromonas ichthiosmia)
  ORGANISM  Aeromonas veronii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Aeromonas veronii"
                     /db_xref="taxon:654"
     Protein         1..197
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22399
     Region          3..169
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mklfsrlyvl vmqwarhkha pwylsitafi esvfwpipvd vmlapmalak phkawhyatl
       61 atvfsvlgal fgyalgyalg yalwdpvvlp lvesvgylgk idiarswfeq wgiwvifias
      121 ftpipykvft vtagllqmal lpfiitslig rgmrfflvag lmrwggekme rklmhyvdvl
      181 gwlciglavv ayfwfsr
//
LOCUS       WP_005336880             172 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Dorea sp. AGR2135].
ACCESSION   WP_005336880
VERSION     WP_005336880.1
KEYWORDS    RefSeq.
SOURCE      Dorea sp. AGR2135
  ORGANISM  Dorea sp. AGR2135
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Dorea.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Dorea sp. AGR2135"
                     /db_xref="taxon:1280669"
     Protein         1..172
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19027
     Region          4..165
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mnevlnniyt rrsirkfkeq dvpkdlvdei vkagtyapsg knlqtyrfyv mqnadsikrl
       61 qdvvakgmen paytlygaka ivlvacekea vngvsdcsca ienmllaahs lglgacwinq
      121 lkycgdkeev adyleglgid kdmqvvgmvg mgypdeerea akrqddlvty ln
//
LOCUS       WP_005338652             271 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Dorea].
ACCESSION   WP_005338652
VERSION     WP_005338652.1
KEYWORDS    RefSeq.
SOURCE      Dorea
  ORGANISM  Dorea
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Dorea"
                     /db_xref="taxon:189330"
     Protein         1..271
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30596
     Region          1..179
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mkldmhchvk egsidskvsl deyitllker gfdgmlitdh dtykgyrhwk yqmkgkvhdd
       61 fvvlkgieyd tcdgghilci mpegvkmrll elrglpvavl idfvhkhggi lgpahpcggk
      121 ylsftntkry ykspelfkrf dfieafnace saesnaralk laqkykkpgi ggsdahrpnc
      181 vgmgytilpe rvtcetelia lirsksavie tggslygktt kdkmgkadki ltysfwfynk
      241 agtimrkrkr mlngkienpv dpidpielky m
//
LOCUS       WP_005338998             270 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Dorea formicigenerans].
ACCESSION   WP_005338998
VERSION     WP_005338998.1
KEYWORDS    RefSeq.
SOURCE      Dorea formicigenerans
  ORGANISM  Dorea formicigenerans
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Dorea.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Dorea formicigenerans"
                     /db_xref="taxon:39486"
     Protein         1..270
                     /product="formate/nitrite transporter family protein"
                     /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=27817
     Region          3..269
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mnspkeiann yiaigkgkvn tpvakmfvlg ilagifiafg gvastavavs iplasvgkfl
       61 gacifpgglt mvllagself tgncllvipl ckkeitlggm lknwvvvylg nmvggigvaa
      121 icvfshqagl fnnglaasmi staagkvsls fgdaflrgia cnflvciavw isfaakqvss
      181 kiiglffpim mfvlcgfehs vanmyyiaag ifakgnaayl eaataagadv sgltwgamft
      241 knllpvtlgn iiggavlvgl aywfvylkdd
//
LOCUS       WP_005340253             240 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Aeromonas veronii].
ACCESSION   WP_005340253
VERSION     WP_005340253.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas veronii (Aeromonas ichthiosmia)
  ORGANISM  Aeromonas veronii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 240)
  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 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   3  (residues 1 to 240)
  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   4  (residues 1 to 240)
  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 240)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Aeromonas veronii"
                     /db_xref="taxon:654"
     Protein         1..240
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26503
     Region          1..240
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <120..238
                     /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 msrfslrhyh hhvcshshdf aqlvipldgp leievqgwgr rlapgsacii apgerhdyaa
       61 dpalsflvqe sdwlpgdlaa cpfieldepq rhylaflhrm vaegrqvagm eqvwlsllae
      121 gqgmqsaamp rlaarilkvq rhidanlaap ltnqqlaaia clgqsqfkla frqqlgvsvs
      181 hyirsrrmal artllagtql pvgeiasrcg yqnqgafser flaetgltps lwrqqngrlp
//
LOCUS       WP_005340452             134 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Aeromonas veronii].
ACCESSION   WP_005340452
VERSION     WP_005340452.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas veronii (Aeromonas ichthiosmia)
  ORGANISM  Aeromonas veronii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Aeromonas veronii"
                     /db_xref="taxon:654"
     Protein         1..134
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14056
     Region          6..133
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 migyfrgfsl ielmivisiv ailgtiaypa yqqyvltshr veakamllna anrqetyfmd
       61 fnqyassaaa lgissaseng lyqlsiavsg ntytlsasag aataqakdtd ctvfsinqlg
      121 vksasgaasn scwe
//
LOCUS       WP_005343066             355 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Aeromonas
            veronii].
ACCESSION   WP_005343066
VERSION     WP_005343066.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas veronii (Aeromonas ichthiosmia)
  ORGANISM  Aeromonas veronii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Aeromonas veronii"
                     /db_xref="taxon:654"
     Protein         1..355
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38986
     Region          1..351
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvqqlnk hfnqyaalad inldfhdgel vallgpsgcg kttllriiag leqadsgsvi
       61 irgedasdlh vrernvgfvf qhyalfrhmt vfenvafglr vkprserpae aairarvkel
      121 ldlvqlshva eryptqlsgg qrqrvalara lavqpkvlll depfgaldaq vrkelrrwlr
      181 elhdelhvts lfvthdqeea levadrvvlm nagrveqigt paevydqpas sfvhsflgsv
      241 nqfrgrvaeq gfgvgeqllg gpsashlahg saaiayvrph eldilpadap ggiratitrl
      301 lpmgprirve lrgdgetkga hyeaelskea aklfapgqgv rlvarqaqfy pdyqi
//
LOCUS       WP_005346223             399 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Anaerobutyricum hallii].
ACCESSION   WP_005346223
VERSION     WP_005346223.1
KEYWORDS    RefSeq.
SOURCE      Anaerobutyricum hallii
  ORGANISM  Anaerobutyricum hallii
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Anaerobutyricum.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Anaerobutyricum hallii"
                     /db_xref="taxon:39488"
     Protein         1..399
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44743
     Region          1..293
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          289..380
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mklihtadwh lgknieghsr leeqrlflkd finiceeeqa diiiiagdiy dnynpsamae
       61 qlfydtlkql srngdcmtvv iagnhdnper lvasgplard hgivmagtpn svitpgmygk
      121 neitesdagy ihaiihgeea dillvpfpse krlnevylde teeetkkaas ysekmsslfg
      181 slathfheds ihliashlfv mnsvedgser siqlggsymv ggeifpenad yialghvhkp
      241 qkvpgcpkar ysgsplpfnv retsfdkqvi avtltagspc tirelplpvy kpievwhcen
      301 iddaveqcea nadrecwvyl evktdhyihe edikkmkaik adilsitpvl pedesedfsa
      361 sdlkeqpfde lvknfyrkkf hvdigeetfs llmsiieen
//
LOCUS       WP_005347980             408 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Aeromonas
            veronii].
ACCESSION   WP_005347980
VERSION     WP_005347980.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas veronii (Aeromonas ichthiosmia)
  ORGANISM  Aeromonas veronii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 408)
  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 408)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Aeromonas veronii"
                     /db_xref="taxon:654"
     Protein         1..408
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47346
     Region          1..401
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 msithlslqd arhlqlaaqg llaprrskat padllatirr mallqidtis vvarspylvl
       61 fsrlgqyepr wleqlladge ifeywaheac fvpredyrll rhrmldpaam gwkfsanwla
      121 thqqeidqli erirdhgpvr aidferttgk gsgwwdwkpe krhlevlftt gqlmvrerrn
      181 fqrvydlaer vipewsdqlh lpsvaeaqrd mvrascralg lvktgwvady yrlrrgkydv
      241 llhlladege llpvrvegwq hdafvhvsla delmqvkegr lkathttals pfdplvwdrk
      301 raselfnfdy riecytpapk rqygyfvlpl lhrgklvgrm dakahrqqgi feikslylev
      361 gvrvtrtlaq dlvkalhkla dwhqtpqlry gaipanllal whesvide
//
LOCUS       WP_005344913             441 aa            linear   BCT 20-JAN-2025
DEFINITION  zinc ribbon domain-containing protein [Anaerobutyricum hallii].
ACCESSION   WP_005344913
VERSION     WP_005344913.1
KEYWORDS    RefSeq.
SOURCE      Anaerobutyricum hallii
  ORGANISM  Anaerobutyricum hallii
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Anaerobutyricum.
REFERENCE   1  (residues 1 to 441)
  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 12359304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Anaerobutyricum hallii"
                     /db_xref="taxon:39488"
     Protein         1..441
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51167
     Region          201..227
                     /region_name="zf-ribbon_3"
                     /note="zinc-ribbon domain; pfam13248"
                     /db_xref="CDD:404185"
     Region          406..429
                     /region_name="zinc_ribbon_2"
                     /note="zinc-ribbon domain; cl11198"
                     /db_xref="CDD:448157"
ORIGIN      
        1 mkltwseasv fafvwacalg yivasrilew nferflpsnw yfvvkkrlaq peakslrtek
       61 vpkkisnvle elltlmqtgn lqkstvrmdr tfqekvmhev kllegrglsr qlhftnvkls
      121 eenakkrdfr hwsdsgrewr eviveaavsd kylhrdsgkv ihesiyphgs illrqsrhir
      181 hnevgekdrq keqrfyskys eifcpscgaq iqlkgdetnc pycggfiqsn fydwqiedfm
      241 iyqtpdpnmd nlkytsvtil lsflptfpcv ylitnmyiai gvamtltiil slsllwirar
      301 kidelenlek eivrydegwl isninealyk tlltpellsy svnniklkgv entsdkttis
      361 veamlkqtfl qnnkhivtks ekhnwklcrs rypnrikskg qavvmekecp scganyipdn
      421 ngccsycgys lqvdnakwkl l
//
LOCUS       WP_005348846             382 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Anaerobutyricum hallii].
ACCESSION   WP_005348846
VERSION     WP_005348846.1
KEYWORDS    RefSeq.
SOURCE      Anaerobutyricum hallii
  ORGANISM  Anaerobutyricum hallii
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Anaerobutyricum.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Anaerobutyricum hallii"
                     /db_xref="taxon:39488"
     Protein         1..382
                     /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=44029
     Region          8..280
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mseavkkstk riykwdnlkc flivmvvigh fvnqyapisn tmkslslfiy sfhmplfifl
       61 sgllqkrwsq rckfqwdkpl yyimigyalk vciygikilf hqkavfqwfe dtgipwymfa
      121 maafmviayl ikelplwfvl pisilaacla gydenigsfl ylsriivffp fyytgycldi
      181 kklqevlnkt wikclsaifl tdmilytlak iednysyirl ftgrnaysli nvescgavhr
      241 lmfyviaflm giaiislipn ckvpvvgkvg artlqiyfwh rlilyvltfs gitgnliknv
      301 psgwvwiyla maiilpfvls aevfsapltl lkngeniila gieklsinfy kwkestltvl
      361 pvlefitivl iliyygedvg il
//
LOCUS       WP_005348990             145 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Aeromonas].
ACCESSION   WP_005348990
VERSION     WP_005348990.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..145
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16033
     Region          5..145
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 msemmemglg wlflsaftsa tllpgssevl lgamaakgew smaslllwat lgntlgsmtt
       61 wwlgwlatfk kkpedfqgrg eqkalgwlkq hghwclllaw tpvvgdglcl lagwlrlsfw
      121 rsliliglgk lfryalvfll ashif
//
LOCUS       WP_005350298             256 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Aeromonas diversa].
ACCESSION   WP_005350298
VERSION     WP_005350298.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas diversa
  ORGANISM  Aeromonas diversa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 256)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Aeromonas diversa"
                     /db_xref="taxon:502790"
     Protein         1..256
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=29220
     Region          18..243
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mkevtggtag esgcrlclee arlefdfsma fqpivncrqk tlfgyealvr glnnepahti
       61 isritdqnry lfdqlcrtka ialaarlqlq qilsinflpn avyrpercir ttlqaanehh
      121 fpverimfei tedervsdnq hirdiieyyh trgfitaldd fgagysglnr ladfqpdiik
      181 ldmhllrgvd ddprrqaivr hsvamcreld itvlaegvet reelaclqtm gvdlmqgyff
      241 arpgfetlpp vdftrf
//
LOCUS       WP_005345569             424 aa            linear   BCT 20-JAN-2025
DEFINITION  galactokinase [Anaerobutyricum hallii].
ACCESSION   WP_005345569
VERSION     WP_005345569.1
KEYWORDS    RefSeq.
SOURCE      Anaerobutyricum hallii
  ORGANISM  Anaerobutyricum hallii
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Anaerobutyricum.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   McAuley,M., Kristiansson,H., Huang,M., Pey,A.L. and Timson,D.J.
  TITLE     Galactokinase promiscuity: a question of flexibility?
  JOURNAL   Biochem Soc Trans 44 (1), 116-122 (2016)
   PUBMED   26862196
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Holden,H.M., Thoden,J.B., Timson,D.J. and Reece,R.J.
  TITLE     Galactokinase: structure, function and role in type II galactosemia
  JOURNAL   Cell Mol Life Sci 61 (19-20), 2471-2484 (2004)
   PUBMED   15526155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Anaerobutyricum hallii"
                     /db_xref="taxon:39488"
     Protein         1..424
                     /product="galactokinase"
                     /EC_number="2.7.1.6"
                     /GO_function="GO:0004335 - galactokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0005534 - galactose binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0046835 - carbohydrate phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=46788
     Region          35..415
                     /region_name="GalK"
                     /note="Galactokinase [Carbohydrate transport and
                     metabolism]; COG0153"
                     /db_xref="CDD:439923"
ORIGIN      
        1 mkttelkkgf qdgkyeellr diyidesvld yqkeryikai esfeelfgek eveiysapgr
       61 seiggnhtdh qlgrvlaasi nldaiaivak kengvvlkse gypminvsla dllpkkeeeg
      121 tseglirgva aklkeegyei ggfeayvtsd vlngagmsss aafevltgni lsglynegkv
      181 spvliaqagq yaenvffgkp cglmdqmass vgnlifidfa dvknpvikkv nvnfedfdhs
      241 lciidtkgsh adltdeyaai peemkkvaay fgkevlhqid knefyihipe irkvagdrav
      301 lramhwfeet drvidqvnal ekedfegfks likasgdssf kylqnvysvk nlsrqemavg
      361 lafsdvilkg rgvsrvhggg fagtiqafvp ndivdiykkn medifgqdac hvlkirkygg
      421 mkvl
//
LOCUS       WP_005351924             152 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Aeromonas].
ACCESSION   WP_005351924
VERSION     WP_005351924.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            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="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16589
     Region          4..152
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 miekqpfyrt lnqqakalle getdlianla nlsallnqel eeinwvgfyl lqgetlvlgp
       61 fqgkpacvri pvgrgvcgta vaegrtqlid dvhqfdghia cdgasnseiv ipvrrggeii
      121 gvldidspif nrfdqedrig leetvqiles ml
//
LOCUS       WP_005352857             149 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Aeromonas diversa].
ACCESSION   WP_005352857
VERSION     WP_005352857.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas diversa
  ORGANISM  Aeromonas diversa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Aeromonas diversa"
                     /db_xref="taxon:502790"
     Protein         1..149
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15775
     Region          11..148
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mpdlalwlga hgltalfvsa fvsatllpgg sevllgamva qqqwslssll gwatlgntlg
       61 smttfalgww arrhkapedf tgrgeqtals wlqlhghwal llawapivgd glcllagwlr
      121 maplracili glgklarygt vallagqfi
//
LOCUS       WP_005353667             742 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Aeromonas veronii].
ACCESSION   WP_005353667
VERSION     WP_005353667.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas veronii (Aeromonas ichthiosmia)
  ORGANISM  Aeromonas veronii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 742)
  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   3  (residues 1 to 742)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Aeromonas veronii"
                     /db_xref="taxon:654"
     Protein         1..742
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=78518
     Region          6..741
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mafevdedil qdflveasei leqlseqlvd lekrpddknl lnaifrgfht vkggagflsl
       61 gelvdvchga envfdilrng krtvtaelmd vilqaldain vmfaqvqnre apspasddll
      121 hdlhelckpe geeqlrtats aaaavesepa apvvveevap evvepaaiss eptpvngggs
      181 ideisadefe rlldelhgvg gaptkmaaaa piaggsgdit ddefealldq lhgqgqhmga
      241 pevnplksvq kevdeliddd eferlldelh grgqgpqstl apaapaapaa paapaapaap
      301 aapaapaavt ppkpttpvak papaapakpa eaakapapaa kaapapaens avqsdttvrv
      361 dtktldvimn mvgelvlvrn rlvslgiasn deemskavan ldvvtadlqg avmktrmqpi
      421 kkvfgrfprv vrdlartlkk eielvmvgee tdldknlvea ladplvhlvr nscdhgvemp
      481 dvrekagkpr qgtitlsasq qgdhillcie ddgagmdpek lksiaisrgv ldadtaarms
      541 dndaynlifa pgfstkaeis disgrgvgmd vvktsivsln gsvhidstwg kgtrleikvp
      601 ltlailptlm vevgeqtfal plgcvneifh ldlkkanmvd gqltiivrek aiplfylhkw
      661 lirgankrsr qdtghvvivq igtqqigfvv dsligqeevv ikpldnllqg tpgmagatit
      721 sdggialild vpsllkayar rh
//
LOCUS       WP_005353799             640 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Aeromonas diversa].
ACCESSION   WP_005353799
VERSION     WP_005353799.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas diversa
  ORGANISM  Aeromonas diversa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 640)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 640)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 640)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Aeromonas diversa"
                     /db_xref="taxon:502790"
     Protein         1..640
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=71128
     Region          79..633
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mtlyrqllat mvllfgllfl vsywvqfnst rsylaqqqet tvintatslg laltpyletg
       61 dkvgaesvin avfdggyyrq vrldllasns vierenttqi kgvpdwfial dlfpevsyes
      121 tltsgwlqlg qlkivghpgq ayyelwggms elasgfligf litvlllmra lhyllrplqq
      181 iceeaveieq hhfghtiplp rtyelrqvvq aintlaskla yqfkeqadea emlrervykd
      241 avsglgnray fvgqinawia eggtggvllv avdilddiyr degyaardnm vksiaaclqe
      301 llqgrddcav arisateyav lypttdkeql rslaelineq iadlvvnpid esraisvvga
      361 vmrehdedls alltkadnal sqarnarrga ivmeghgqge lmgrlawrdl vqeaitshll
      421 rfkaqpacrf ddqseihael fasihkegqd yfagqfmpai eqfqmgavfd ravleslati
      481 meakpslsis vnimagslcs ndfsawlkef laahpvlkgr lffeipegai mkhrdevanf
      541 vmvvreqgyg wgvdhfgrhf qslgyletlq pvyvkvdhgy tsqvleagad tsflsavcrt
      601 ahnagimtia trveneeqvk alsrlhidgy qgfvhpaqni
//
LOCUS       WP_005354246             211 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Aeromonas].
ACCESSION   WP_005354246
VERSION     WP_005354246.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 211)
  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 10614777
            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="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=23803
     Region          46..210
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mrqargnidw qrgwlllpll lisliwssta daswdqslyr qlglagkldk qtfrqalnsy
       61 qtvrhkrkpi ltiidyskps tqrrlfvidm krhkllyhtw vshgrnsgel aakhfsnqln
      121 srqsslgvyr taetylgkhg yslrldglsp gknsnarkra ivvhgaayas pthlrkydkl
      181 grswgcpalp keqaraiidt ikggsviyah g
//
LOCUS       WP_005358092             591 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Aeromonas veronii].
ACCESSION   WP_005358092
VERSION     WP_005358092.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas veronii (Aeromonas ichthiosmia)
  ORGANISM  Aeromonas veronii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 591)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 591)
  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 591)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Aeromonas veronii"
                     /db_xref="taxon:654"
     Protein         1..591
                     /product="M4 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=63677
     Region          1..590
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mnkiylaval acwgsaalaa qeveinvtan giramtglsa asgtlqledg efrqvrvvkl
       61 pngqqrirye qvwngipvmg qvvvadksln gqlqqasgrm lrqidqdvas paatlspqda
      121 askakagskg sneqvklyvm qdenglarlv yqvsfiaegd kpsrpfvild aqsgeelkrw
      181 eginhkdatg pggniktgky fygadfgpli vddncrmtsp nvdtinlnha tsggaihqft
      241 cpenrvkein gaysplndah yfgnvvfdmy rnwyntaplt fklkmrvhys knyenafwdg
      301 sqmtfgdgat tfhplvsldv aahevshgft eqnsgliysg qsggineafs dmageaaefy
      361 mkgsndwlvg aqifkgngsl ryfedptrdg rsighaadyr egmdvhhssg vynrafylla
      421 tssgwntrka fevfllanrl ywgantnyqq gacgvsrata dlgynqadva rafqtvgvda
      481 scgttpppsd nvlqngvpvs nlaaskggkl nytlnvpagt rslqisssgg tgdadlyvrf
      541 gsaptsssyd crpykggnne scsftnpkag twhvqlsgfs afsgvtlkas y
//
LOCUS       WP_005360536             152 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Aeromonas].
ACCESSION   WP_005360536
VERSION     WP_005360536.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            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="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16530
     Region          4..152
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 miekqpfyrt lnqqakalle getdlianla nlsallnqel aeinwvgfyl lqgetlvlgp
       61 fqgkpacvri pvgrgvcgta vaegrtqlid dvhqfdghia cdgasnseiv ipvrrggeii
      121 gvldidspif nrfdqqdrig leetvqiles ml
//
LOCUS       WP_005361912             721 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Aeromonas veronii].
ACCESSION   WP_005361912
VERSION     WP_005361912.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas veronii (Aeromonas ichthiosmia)
  ORGANISM  Aeromonas veronii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 721)
  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   3  (residues 1 to 721)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Aeromonas veronii"
                     /db_xref="taxon:654"
     Protein         1..721
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79456
     Region          1..694
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdinkarmlf feeayeqcdn leqalldrvg hplgadtynq mfrtahtikg sasmlglell
       61 vrfthsmeni larlrsgeld lddaliqlll rcndqlrdll qsaehnpelk qvetqqilal
      121 msqmqgfqsl psmtipaptv madakpgitt serwhlsvrf ypalfrdgfd vlallkylgn
      181 qgeihyimpv wrpwpplqll dstdcflgye iviesgcgae klrsafdfva tqsiivllpv
      241 hgdlslyrda aptlcawlge evgtqyarwk qagsltaadi qallqpalme ptppattsla
      301 tdtpepvnas rkslirsdsh yiridaakld qlinrvgelv iaasattlqa hqagnvemie
      361 svavvnglve girddaltlr mvpiheifnr fprvvhelsl qtgksvtlni qnadtdidks
      421 mvekltdpll hlvrnaidhg iekpsvrqdk gkpeqgritl nayhdagavv vevsddgdgi
      481 srekvlakaq qaglvsdikv msdsdvyqll fapgfstnse vnelsgrgvg ldvvrrnlda
      541 lrgdvtvesn pgqgttfrlr lpltlaiidg frvevadtsf viplemmtec lelpdseeel
      601 tvqqlylrge wlpyvhlral fglppaqgse fvvvvhhger raglvvdhli gelqtvikpl
      661 gelfrplrgi sgstilgngh palildipql laqvtmweqq rilhtlsegd lsapcrhaeg
      721 i
//
LOCUS       WP_005364110             177 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Photobacterium angustum].
ACCESSION   WP_005364110
VERSION     WP_005364110.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium angustum
  ORGANISM  Photobacterium angustum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Photobacterium angustum"
                     /db_xref="taxon:661"
     Protein         1..177
                     /product="TRAP transporter small permease subunit"
                     /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=19866
     Region          4..172
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mkslitlerf fnrigdvlgw fasilfllll vnvvydvvmr yvfndvsial qemewhlfsa
       61 vfllgvpyai rsaghvrvdv fyerlsrksq aiidilgtlf fllpfcllva wygidftkes
      121 yalgetsgdp gglayrwiik amiplsfglm aisglglvvh slntlfnpqh aalkqdq
//
LOCUS       WP_005364531             489 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Photobacterium angustum].
ACCESSION   WP_005364531
VERSION     WP_005364531.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium angustum
  ORGANISM  Photobacterium angustum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 489)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Photobacterium angustum"
                     /db_xref="taxon:661"
     Protein         1..489
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=56259
     Region          244..482
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 maaskknnkk syiifvlsli ftfivsllys yiaghsvnes vayeiytavh epeekvirsh
       61 ynqipkaqrq amleqivvdn kdlkgifyik dgkyiysdrd vsikkdivad lsnkvdeykn
      121 kavyyyidkk diygspafiy mfkfgsgfyq mifyqeaitp pssifssyvv snidntilsg
      181 nnkdtftiae dtlhglslsv itgislshff diyliaflpv lmiillipsv iekvqvrqdn
      241 ilidinagir nkefipfyqg vysieqnrfv gvellcrwny kkqkilspas finiledsgq
      301 intvtlelln qlaidqelld tinsemyfsv nvtvnmlldd nfvesviqfl tqnprlknri
      361 tfelterdkr fdyiadvkea mcllhshsvk walddfgtgy snfltmhklp idiikvdrmf
      421 isskndiisf diltkiidll dtwklpiime gveteeelnk vkslsidliq gyyfskplsv
      481 ddfikyars
//
LOCUS       WP_005364930             176 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Photobacterium angustum].
ACCESSION   WP_005364930
VERSION     WP_005364930.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium angustum
  ORGANISM  Photobacterium angustum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (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   2  (residues 1 to 176)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Photobacterium angustum"
                     /db_xref="taxon:661"
     Protein         1..176
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19004
     Region          <28..>172
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          105..175
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mfkkllltla filpfasqaa ttdttklikk cetkykadkq kkmdcitkvk ksakkevdka
       61 kktssskvtd tkkdlkttss klnskkdtak ksvtgskkaa ttksktavkk qlkavnvnta
      121 saselaaslp gigeakakai vdyrkkngkf ktskdlekvt glgeksvgsm kkylkf
//
LOCUS       WP_005366546             353 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Photobacterium
            angustum].
ACCESSION   WP_005366546
VERSION     WP_005366546.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium angustum
  ORGANISM  Photobacterium angustum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 353)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Photobacterium angustum"
                     /db_xref="taxon:661"
     Protein         1..353
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=39999
     Region          260..335
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mevksqlssl kntvssgwks vipfanfnie enhtfdmthf eglwlkqyls titpeyhals
       61 tqitkiaqsv npltfnfysl alwtspdryt qlhtlchysa llnssirfhl denkgdninl
      121 wllsnepiak hsteslslla lhfalllnvi kqtwgtqtlk gdaylpsltn lrieqqlfdn
      181 liassalnik chysfplirl sfskkslslp ltdsdpvinq nslwqlkhql vnyqqnnvih
      241 qvyralrslp dleaasgnhi aslmdisfrt lnrrlaclst syrgvlenyk lemalslldn
      301 selgladiaq qlgfsdlstf srafkrwtgl cpsqltsknq tiaprvvshw eli
//
LOCUS       WP_005361215             492 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Eubacterium ventriosum].
ACCESSION   WP_005361215
VERSION     WP_005361215.1
KEYWORDS    RefSeq.
SOURCE      Eubacterium ventriosum
  ORGANISM  Eubacterium ventriosum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Eubacteriaceae; Eubacterium.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Magnet,S., Arbeloa,A., Mainardi,J.L., Hugonnet,J.E., Fourgeaud,M.,
            Dubost,L., Marie,A., Delfosse,V., Mayer,C., Rice,L.B. and Arthur,M.
  TITLE     Specificity of L,D-transpeptidases from gram-positive bacteria
            producing different peptidoglycan chemotypes
  JOURNAL   J Biol Chem 282 (18), 13151-13159 (2007)
   PUBMED   17311917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19085844
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Eubacterium ventriosum"
                     /db_xref="taxon:39496"
     Protein         1..492
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=54085
     Region          38..156
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(99..100,103,129..132,134)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
     Region          205..271
                     /region_name="DUF5011"
                     /note="Domain of unknown function (DUF5011); pfam16403"
                     /db_xref="CDD:435320"
     Region          373..443
                     /region_name="DUF5011"
                     /note="Domain of unknown function (DUF5011); pfam16403"
                     /db_xref="CDD:435320"
ORIGIN      
        1 mkkitsklva vlmivvmafg isgtatvkte akeskgyvik vnlgtncttv ykngkaikam
       61 icspsnetpt gtfytpvkyr whemigncya qyctrittgi lfhsvwyykn gdkstmsvka
      121 ynvmgqkash gcvrllckds kwiydhcalg tkvvifrgtk kddpikrpsf tpitngkftd
      181 wdptdpdpkn pyksnkpvit akvktieygt kvklsdlitv kdragnvltk knakittvgk
      241 iktsklgkyk ikfkvkdslg nsktktltfk vvdtkkpvis gavknpdval nssvnvlanv
      301 taktaagkni tskikvtvky nkkkvkikng vvkfankgky yitykvkgtn kktakktiky
      361 vvkdhkvslt mknttvkvkq nstfnplnyv asvkdykgna lniknsvtvt gkvdtkkpgt
      421 yiltykaqys nqaytartat lkvvveavaq qpttkpvttq pttkvpettt kvpetttkap
      481 etttvpettt sk
//
LOCUS       WP_005366884             607 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Photobacterium angustum].
ACCESSION   WP_005366884
VERSION     WP_005366884.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium angustum
  ORGANISM  Photobacterium angustum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 607)
  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 607)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Photobacterium angustum"
                     /db_xref="taxon:661"
     Protein         1..607
                     /product="M4 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=67227
     Region          10..603
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mnlqrqtsck iavllgtsvg fsvhaaemve vndnkvlfqs lkaqstsitp letgfaeikk
       61 vvlpngktkv ryqqtylgvp vfntsvvatl snnkpsgvyg lmakginrdl psitprlnee
      121 eailaaitsh qsvannnhni enknaklivk lddnqtakiv ylvdffiase hperpfyivd
      181 ainggilehw dglnhtkasg mgpggnikts eyiygldfdg lpinkegtic tlenaavktv
      241 nlnnetegni ayqyncidnd nfndfryvng afsplndahy fgnvvfnmyq dwmntsplnf
      301 qltmrvhygs eyenafwngt smtfgdgkdr fyplvdinvs ahevshgfte qnsglvykdm
      361 sggineafsd iageaaeyyl rgkvdwivgs difksegglr yfdqpskdgr sidhasqyyd
      421 gmnvhfssgv fnrafyllan kpnwgvrkgf eiftlanqly wtanstfeeg acgvvkaaed
      481 fgytvkdvvn afksvgvdas cgspipndnv likwkpikdl sgsensktyy vfnvdkastv
      541 mvslaggkgd adlyvranrk pttstfdcrs nrsgneemch lyaqpgvtyy vllhgytryt
      601 kltlrld
//
LOCUS       WP_005369265             203 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Photobacterium angustum].
ACCESSION   WP_005369265
VERSION     WP_005369265.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium angustum
  ORGANISM  Photobacterium angustum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 203)
  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 203)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 203)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Photobacterium angustum"
                     /db_xref="taxon:661"
     Protein         1..203
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22194
     Region          1..201
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 mndyateeqq veaikswwqe ngkavvlgav iglgglwgwr yyqsevhaak haasdsytqv
       61 vsaldenskd avaeaktfid ankgsqyavl talqlakvqv dnkdldgavt qlqwvlnntk
      121 deailplatt rlariyaeqq kfdealaelk kvtvpswksk vaelrgdill qkgditgare
      181 ayveaqqegs spalqmkldd laq
//
LOCUS       WP_005369457             129 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Photobacterium angustum].
ACCESSION   WP_005369457
VERSION     WP_005369457.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium angustum
  ORGANISM  Photobacterium angustum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Photobacterium angustum"
                     /db_xref="taxon:661"
     Protein         1..129
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=13825
     Region          1..129
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mmtkqkgvtl iemliaiaii gvltaiayps yqsyvlkghr tqtmgdmikv qlnleehftq
       61 nsnynspvis gsncticdtd snryafsiss atgsytitat aksdkgqnqd ecgnltlnqn
      121 gtgtpascw
//
LOCUS       WP_005369926             190 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Methylomicrobium album].
ACCESSION   WP_005369926
VERSION     WP_005369926.1
KEYWORDS    RefSeq.
SOURCE      Methylomicrobium album
  ORGANISM  Methylomicrobium album
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Methylococcales; Methylococcaceae; Methylomicrobium.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Methylomicrobium album"
                     /db_xref="taxon:39775"
     Protein         1..190
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20544
     Region          3..190
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mpkkrliiam tgatgavygv rmlehlkpqp ewethlvvsd agvvnlkhem gmkradlsrl
       61 advthgigdi aatiasggfk tegmiiapcs mktlaavahg fgdnlisrsa dvvlkerrrl
      121 vimpretpln lmhirnmatv temggiifpp mpafysksds laemvnetvg rvldmfgvnv
      181 dglytpwdgl
//
LOCUS       WP_005369949             141 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Methylomicrobium].
ACCESSION   WP_005369949
VERSION     WP_005369949.1
KEYWORDS    RefSeq.
SOURCE      Methylomicrobium
  ORGANISM  Methylomicrobium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Methylococcales; Methylococcaceae.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Methylomicrobium"
                     /db_xref="taxon:39773"
     Protein         1..141
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14705
     Region          9..140
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mreawfeigg lfvsafvsat iapggseavl ayllaegrhp alalvgaatl gntlgamttw
       61 glgmlaakry paasllpeks qkaldvvmkr giwalffswl pvigdalcfa ggwlklpllt
      121 gtlvillgkl grygaiawvf g
//
LOCUS       WP_005370328             751 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Photobacterium angustum].
ACCESSION   WP_005370328
VERSION     WP_005370328.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium angustum
  ORGANISM  Photobacterium angustum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 751)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 751)
  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   3  (residues 1 to 751)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..751
                     /organism="Photobacterium angustum"
                     /db_xref="taxon:661"
     Protein         1..751
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=80801
     Region          6..750
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          245..>367
                     /region_name="Agg_substance"
                     /note="LPXTG-anchored aggregation substance; NF033875"
                     /db_xref="CDD:411439"
ORIGIN      
        1 msfdldedil qdflieagei lellseqlve lerspddsel lnaifrgfht vkggagflsl
       61 telvdachga envfdllrtg krsvtselmd vilealdcin vmfeqvkehq pldraeqrll
      121 dalhyysqpa tdysqpatad eiapiskpve appvdviaev tsepaitsnn envttgdsvd
      181 dmtqdefdrl ldelhgagqs pskpttpept ahnnveaqln fdsgditdde ferlldelhg
      241 sgkgpgnsdt saagvttpss pvtpsstvpe dtgagdsddl mtddeferll delhgagksp
      301 sleeqasaaq standlteve aavssaqstp mvtppapvsa thqppaersa kpvavkeksk
      361 pqadatvrvd tstldtimnm vgelvlvrnr lvslglntnd eemskavsnl dvvtadlqga
      421 vmktrmqpik kvfgrfprvv rdlarslkke ivlemrgeet dldknlveal adplvhlvrn
      481 svdhgiempd vreqvgkprt gtvllsasqe gdhilltied dgggmdaekl rsiavergvm
      541 dadaasritd neaynlifap gfstkkeisd isgrgvgmdv vktginqlng sihidsvlgk
      601 gtridikvpl tlailptlmv gvgeqpfalp lasvneifhl dlnktntvdg qltiivrdka
      661 iplfylqdwl snmtgrtnkd rghghvvivq ighqrigfvv dtligqeevv ikpldsllqg
      721 tpgmagatit sdghialild vpsllkhyag h
//
LOCUS       WP_005370452             138 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Photobacterium angustum].
ACCESSION   WP_005370452
VERSION     WP_005370452.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium angustum
  ORGANISM  Photobacterium angustum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 138)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Photobacterium angustum"
                     /db_xref="taxon:661"
     Protein         1..138
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=15492
     Region          <21..98
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mqrfltlgvr gllmilervi sslsslkeln fdiikidklf vnsadtdavt ssilnniasl
       61 gkelqcklva egvetetqln tlksllidyt qgfyfsapts rcgfiefkte hneqilktmv
      121 kntkrcvrlk yhgptlyi
//
LOCUS       WP_005370895             401 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Methylomicrobium album].
ACCESSION   WP_005370895
VERSION     WP_005370895.1
KEYWORDS    RefSeq.
SOURCE      Methylomicrobium album
  ORGANISM  Methylomicrobium album
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Methylococcales; Methylococcaceae; Methylomicrobium.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Methylomicrobium album"
                     /db_xref="taxon:39775"
     Protein         1..401
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43828
     Region          9..392
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mrsdefmlli invgsatvkt rlfdsslrei armnadygng ggirlngwds rgkdierhip
       61 enamarqals avfdewreql pdlqaplgai ghrvvhgggd ftcatrmtse vsarlaelda
      121 yaplhnplnr lgvsmaeaaf pgipqyavfd tafhrqmpeh asrypippal sgnvefrrfg
      181 fhgiscqysv traatllskd raninciilh lgggasatav lggrgvdtsm gfspteglmm
      241 ttrsgdidpm ipvtllregw tadrldrlln resgllgvcg agdmrevlrl aengdqrarl
      301 avdiycyrir kyigalcavl gdvdaliftg gigehaplir qkiaegldrl gfaidveanl
      361 rvsehdrdig spikkprilv ihaeeereia aqilnrleyr s
//
LOCUS       WP_005374183             707 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter permease [Vibrio].
ACCESSION   WP_005374183
VERSION     WP_005374183.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 707)
  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 707)
  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 707)
  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 707)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..707
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=75800
     Region          1..698
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 msdsiekelq kfelptrtdf pwvtttitvf gvvlsalhiw fntlstlpel wisathfagf
       61 avicalwypa hislkqskla lgidvliamg avacllyipy aedalyergv kfvtsdwvfa
      121 imailiviel irrtmgwfip vlivvclsyv vlwgkwatgi fhfpglsmet llyrsfysse
      181 gmfgsisris wtfvfmfilf gaflvrsgvg dyiinvaraa agkiiggpgf iavigsglmg
      241 svsgssvant vstgvisipl mqkagfpsrf aagveaaast ggqlmppvmg agafimasyt
      301 qipyvdiiav sfipaliyfl svaffvriea krsgvqkitt sdesllkvli sgwhnlipla
      361 vlvtllvqgf tptyaaglsi isvvvaswfs kdhkmgpkai iealsqgakn mattavllvg
      421 iglvinvist tgigntfslm idgwangdlf imivlialas lvlgmglpvt aayivlgtls
      481 apalykliae nqllelmvsg qlpeqakaif mlaapeklel lnapmaleta kemvalvpad
      541 fmetlleqsl gmeavglall aahliifwls qdsnvtppvc ltafaaatia ktppmrtglm
      601 awkiakglyl vplliaytgl vswdvtsvit vgffaiigty aligaiegyl egplniltrl
      661 llvvvgtllv whdipmlvrv ascavfvavf iysgrkfklq qsqlsvl
//
LOCUS       WP_005375118             786 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: Lon protease family protein [Vibrio].
ACCESSION   WP_005375118
VERSION     WP_005375118.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 786)
  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 786)
  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 786)
  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   4  (residues 1 to 786)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..786
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..786
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88096
     Region          70..786
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mailrleakq lysvadlenm pckstkelpp ideivgqera qkavefamsi kekgyniyai
       61 gqnglgkrtm ilrylnrhqh daaalfdwcy vanfedtrtp kvlklpcgig nklrvdieal
      121 mgkllnalpl afdnemyfsr aerlknqlaa kqqneldris reakekgisl tlttqgdyqf
      181 vamngdelht eesfdvlskk eqeqfsdaid elevrlrsmv relteweety sdkikklnde
      241 vtldvithfi kklkvdyaqy seiktyltel qkdivenadi fldqsgeqge iatasldkkl
      301 prrykvnvlv srkssefpiv veenpnyhsl fgsietatfk gtvftdfsli ragslhkang
      361 gvllmdaqkv leqpyvwdgl kralrarqls ftslekevtl tgavsldpep ipldikiilf
      421 gdyrtyqllq hydpefself rvtadfedem krtpeselhy arfissvvhd nnmlhcdrka
      481 iariieyssr lsgdqsklsl hsanianllr esnyvarqan snmirighve ealnnqemrv
      541 srlrdnvmet fingttlirt egeavgqvna lsvlstsdym fgapnritat tcygdgdvid
      601 iersvdlggs ihskgvmils aylssvfgkt arvpltttit feqsyggvdg dsasmaelca
      661 vvsafskqpn rqdiaitgsm nqfgqaqpig gvnekiegfy dvcvikgrhd gqgviiprsn
      721 vhnlmlrsdi vkavekgefn iwaidhvtea ielftgkvag eptdegsypi dtifglaqak
      781 lnslrk
//
LOCUS       WP_005375168             196 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Vibrio].
ACCESSION   WP_005375168
VERSION     WP_005375168.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            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="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19687
     Region          <4..175
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 msasdndtyl gdagvnnqfa dfdggddlfi gfggndsfvg gggndyvigg dgddrltgga
       61 gddilragtg ndylgggtgn dlllgllgdn klnggvgedi lvagsgdnvl vggsngdkfv
      121 ftdkfgghge akvvdftige dslhiisdsv tdfgdlsfsy davgnavftd gadltvklig
      181 vtetdintyg adlfvi
//
LOCUS       WP_005375313             241 aa            linear   BCT 20-JAN-2025
DEFINITION  YaaA family protein [Veillonella atypica].
ACCESSION   WP_005375313
VERSION     WP_005375313.1
KEYWORDS    RefSeq.
SOURCE      Veillonella atypica
  ORGANISM  Veillonella atypica
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Veillonella.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Prahlad,J., Yuan,Y., Lin,J., Chang,C.W., Iwata-Reuyl,D., Liu,Y., de
            Crecy-Lagard,V. and Wilson,M.A.
  TITLE     The DUF328 family member YaaA is a DNA-binding protein with a novel
            fold
  JOURNAL   J Biol Chem 295 (41), 14236-14247 (2020)
   PUBMED   32796037
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Liu,Y., Bauer,S.C. and Imlay,J.A.
  TITLE     The YaaA protein of the Escherichia coli OxyR regulon lessens
            hydrogen peroxide toxicity by diminishing the amount of
            intracellular unincorporated iron
  JOURNAL   J Bacteriol 193 (9), 2186-2196 (2011)
   PUBMED   21378183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006857
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Veillonella atypica"
                     /db_xref="taxon:39777"
     Protein         1..241
                     /product="YaaA family protein"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=27327
     Region          2..211
                     /region_name="YaaA"
                     /note="DNA-binding protein YaaA associated with the
                     oxidative stress response [Replication, recombination and
                     repair]; COG3022"
                     /db_xref="CDD:442258"
ORIGIN      
        1 mkivlspskt ktishtaavi rdgqfqplit qkivkhvqsl dvaalgkalk lkddkaqsif
       61 dfyeefeshp vgfacesydg iafkyldwag lsdeakafge thlaimsaly gvveptmgvr
      121 dyrldmvdkv glnlyeiwre avdayfhked wilnlaskey akmvnhpkvv tvefwelrgd
      181 tykqmstssk msrgmmahac ltnqvkhvrd lprkingfmc vtdiesitip sesmtvryer
      241 k
//
LOCUS       WP_005376399             272 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Vibrio].
ACCESSION   WP_005376399
VERSION     WP_005376399.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 272)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..272
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=31101
     Region          25..255
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 melknqsdye ryikqdnlge yyvvlnqftf hsvyqpifdr rqriigmeal lrirgidgsl
       61 irpdvflann aldpyfrlcv eflsramhir nfaryfagtp iklflnvmpq tlltltkdmg
      121 fkdngllykr lselgmspsd vvfevveesc gntdllikav qlmkangfif aiddfgaqhs
      181 diarvqqlcp diikidrsyl ldycagetfs ihsavdladh mgakviiegv eedvqlqamy
      241 qlnldyyqgf ylgkpcaihh wtdslniett vh
//
LOCUS       WP_005376943             103 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: endonuclease domain-containing protein [Vibrio].
ACCESSION   WP_005376943
VERSION     WP_005376943.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 103)
  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 103)
  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   3  (residues 1 to 103)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..103
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=11982
     Region          1..102
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 msqleklllq hiralklevp vseyrfhetr rwrfdfaype lqlaievegg twsngrhnra
       61 kgyeadceky ntaalrgwtv lrftgdmikk glaiqmieea lrd
//
LOCUS       WP_005377317             401 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Veillonella].
ACCESSION   WP_005377317
VERSION     WP_005377317.1
KEYWORDS    RefSeq.
SOURCE      Veillonella
  ORGANISM  Veillonella
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Veillonella"
                     /db_xref="taxon:29465"
     Protein         1..401
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43913
     Region          1..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mnvlvvncgs sslkyqlldm tnetelakgl fekigdqdai fthkrpnadk lervepilnh
       61 kealrilldi lvdpefgvik smdeidavgh rvvhggekfa dsvlitpavm ealeecssla
      121 plhnppniqg ieacqaimpn vpqvavfdta fhqtmpkeay myalpysyye eygirrygfh
      181 gtshkyvaqr caelmgkhms dlriitchlg ngssvsaikg grsidttmgf tplsglimgt
      241 rtgdidpaiv pflmdktgms yeevdrvmnk esgvlgisgv sndfrvieea asngnkraql
      301 alnmfhykvr rvigafaavm ggvdaiifta gigengignr daicngleyl gtridpernn
      361 irgkeqeisa egskvkifvi ptneeimiar dtqritsalk k
//
LOCUS       WP_005378892             274 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Veillonella].
ACCESSION   WP_005378892
VERSION     WP_005378892.1
KEYWORDS    RefSeq.
SOURCE      Veillonella
  ORGANISM  Veillonella
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Veillonella"
                     /db_xref="taxon:29465"
     Protein         1..274
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31326
     Region          1..243
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mrvdfhmhst fsdgvetpeq llqhaieadl kmialtdhde iagidvmlqn nssiqiitgc
       61 efsghykgkd ihilgygfnh hdeglrkfie ffkekresri keiisrciah gydisfselq
      121 nlypntksyg rphvarllid hgyakdvqdv fdgilnsksp cyipkvklev peildiihna
      181 nglavlahpk lvrndeyvae llnysfdgve vyhskhdydd eikyltmake rnlfvtggsd
      241 yhgipnrypy hlgeyvvdsn lvnqfierir cisa
//
LOCUS       WP_005379938             153 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Vibrio].
ACCESSION   WP_005379938
VERSION     WP_005379938.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..153
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16733
     Region          5..153
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mleafntsfe slalwfsdsa lwvlfmtgfl satllpggse aglvatlsln qysvssivmv
       61 atigntlggl tnywlglwip nkaqeekhgh talkwlskyg ywglffswlp vigdplclaa
      121 gwlrmkflpc viliflgkaa rysllaaiyl glf
//
LOCUS       WP_005380492             189 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Veillonella atypica].
ACCESSION   WP_005380492
VERSION     WP_005380492.1
KEYWORDS    RefSeq.
SOURCE      Veillonella atypica
  ORGANISM  Veillonella atypica
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Veillonella.
REFERENCE   1  (residues 1 to 189)
  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 189)
  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   3  (residues 1 to 189)
  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   4  (residues 1 to 189)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 189)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 189)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Veillonella atypica"
                     /db_xref="taxon:39777"
     Protein         1..189
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21425
     Region          1..187
                     /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"
ORIGIN      
        1 mrilivddes lirmdlrdii eseqhevvge asngveaitm ckelkpdavl mdvkmpeldg
       61 ieaarqigfn hlapvvllts ysqqdlvtka resgvygyli kpvreeqlip tlemacgrfl
      121 ddlesrqqma dlektleerk iiqkatgilm dlykitedes ynrirqlsmk kresivnick
      181 liiqqassn
//
LOCUS       WP_005381979             241 aa            linear   BCT 20-JAN-2025
DEFINITION  YaaA family protein [Veillonella atypica].
ACCESSION   WP_005381979
VERSION     WP_005381979.1
KEYWORDS    RefSeq.
SOURCE      Veillonella atypica
  ORGANISM  Veillonella atypica
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Veillonella.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Prahlad,J., Yuan,Y., Lin,J., Chang,C.W., Iwata-Reuyl,D., Liu,Y., de
            Crecy-Lagard,V. and Wilson,M.A.
  TITLE     The DUF328 family member YaaA is a DNA-binding protein with a novel
            fold
  JOURNAL   J Biol Chem 295 (41), 14236-14247 (2020)
   PUBMED   32796037
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Liu,Y., Bauer,S.C. and Imlay,J.A.
  TITLE     The YaaA protein of the Escherichia coli OxyR regulon lessens
            hydrogen peroxide toxicity by diminishing the amount of
            intracellular unincorporated iron
  JOURNAL   J Bacteriol 193 (9), 2186-2196 (2011)
   PUBMED   21378183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006857
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Veillonella atypica"
                     /db_xref="taxon:39777"
     Protein         1..241
                     /product="YaaA family protein"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=27294
     Region          2..211
                     /region_name="YaaA"
                     /note="DNA-binding protein YaaA associated with the
                     oxidative stress response [Replication, recombination and
                     repair]; COG3022"
                     /db_xref="CDD:442258"
ORIGIN      
        1 mkivlspskt ktishtaavi rdgqfqplit qkivkhvqsl dvaalgkalk lkgdkaqsvf
       61 dfyeefevhp vgfacesydg iafkyldwtg lsdeakafge thlaimsaly gvveptmgvr
      121 dyrldmvdkv glnlyeiwre avdayfhked wilnlaskey akmvnhpkvv tvefwelrgd
      181 tykqmstssk msrgmmahac ltnqvkhvrd lpreingfic vtdiesitip sesmtiryer
      241 k
//
LOCUS       WP_005382623             213 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Vibrio].
ACCESSION   WP_005382623
VERSION     WP_005382623.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 213)
  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 10614777
            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="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=23776
     Region          50..211
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mkklillftc allsvspfaf akqsdneprd hlrpkqvehv fkqakldgiv dfklfsdayi
       61 ayhktpdrkk svltiidysk pstekrfyvv dldkkkliyn tyvshgvnsg kktatqfsnv
      121 vnsrktslgt fltdttyygs ngyslrldgl ssglndkare ryivvhgady anpsfikkng
      181 ylgrswgcpa lpeklsreii dtikggsviy asa
//
LOCUS       WP_005382915             265 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Vibrio].
ACCESSION   WP_005382915
VERSION     WP_005382915.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 265)
  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 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   3  (residues 1 to 265)
  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   4  (residues 1 to 265)
  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 265)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..265
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30160
     Region          26..265
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <164..262
                     /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 mehiqyyatd hdnlslieak yqkfafqrhy hldfhlglit hgaqkfqyqg nshqvghgqi
       61 vimppdelhd gqsklesgye vnvfaiephl lsdladlkqn gqiihfneli isdpqifsql
      121 snlhgllrre nlsqltkdcl pfegfnqlfd rygslerqkv vplgnqslgt lkdylmanld
      181 qavrldslse lcqlsptqfq rhfkaqtgmt pyawfarlrl eqgmkllqag qcgtdvahqi
      241 gfydqahfsk afkqtygvsp sqvar
//
LOCUS       WP_005385679             411 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: exonuclease SbcCD subunit D [Veillonella].
ACCESSION   WP_005385679
VERSION     WP_005385679.1
KEYWORDS    RefSeq.
SOURCE      Veillonella
  ORGANISM  Veillonella
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Veillonella"
                     /db_xref="taxon:29465"
     Protein         1..411
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46694
     Region          1..302
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          298..383
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrflhtadwh lgrifygqyl tedqahvlen qfftilkdek idgillagdi fdravppiea
       61 ielwdsiitr lamdykvplf vvsgnhdgae rlevgrsmls rsgihiwgsp hhalqpfefe
      121 gadgkvaicp mpfseprrig dalglgasvs kpvdidmted slfsyvetee qepaslnlhn
      181 ydqmyqawsd ylykqvpkgm csiaishafv mggevggser tlsvggseqv spqvfkdfhy
      241 talghlhgpq rmgadyirys gsplkysfde htqkksftii dmdkkgnvdi stipveakrd
      301 vvilegyfed llnnkelqak hkddyvqarl ldtmpimdgm aklrqvyhrc mtidlvgrva
      361 tpmadmdeav fkelnerelf nqfaetvwke pltereqqyi nsvwdrilke d
//
LOCUS       WP_005386027             401 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Veillonella dispar].
ACCESSION   WP_005386027
VERSION     WP_005386027.1
KEYWORDS    RefSeq.
SOURCE      Veillonella dispar
  ORGANISM  Veillonella dispar
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Veillonella.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Veillonella dispar"
                     /db_xref="taxon:39778"
     Protein         1..401
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43846
     Region          1..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mnvlvvncgs sslkyqlldm ttetelakgl fekigdqdai fthkrpnadk lervepilnh
       61 kealrilldi lvdaeygvik smdeidavgh rvvhggekfa dsvlitpavm ealeeccala
      121 plhnppniqg ieacqaimpn vpqvavfdta fhqtmpkeay myalpyeyye dygirrygfh
      181 gtshkyvaqr caelmgkhms dpriitchlg ngssvsaikg grsidttmgf tplsglimgt
      241 rtgdidpaiv pflmnktgmn ydevdtvmnk ksgvlgisgv sndfrvieea aangnkraql
      301 alnmfhykvr rvigafaavm ggvdaivfta gigengignr daicngleyl gtridsernn
      361 irgkeqeisa egsrvkifvi ptneeimiar dtqritaslk k
//
LOCUS       WP_005387529             248 aa            linear   BCT 20-JAN-2025
DEFINITION  YaaA family protein [Veillonella dispar].
ACCESSION   WP_005387529
VERSION     WP_005387529.1
KEYWORDS    RefSeq.
SOURCE      Veillonella dispar
  ORGANISM  Veillonella dispar
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Veillonella.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Prahlad,J., Yuan,Y., Lin,J., Chang,C.W., Iwata-Reuyl,D., Liu,Y., de
            Crecy-Lagard,V. and Wilson,M.A.
  TITLE     The DUF328 family member YaaA is a DNA-binding protein with a novel
            fold
  JOURNAL   J Biol Chem 295 (41), 14236-14247 (2020)
   PUBMED   32796037
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Liu,Y., Bauer,S.C. and Imlay,J.A.
  TITLE     The YaaA protein of the Escherichia coli OxyR regulon lessens
            hydrogen peroxide toxicity by diminishing the amount of
            intracellular unincorporated iron
  JOURNAL   J Bacteriol 193 (9), 2186-2196 (2011)
   PUBMED   21378183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006857
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Veillonella dispar"
                     /db_xref="taxon:39778"
     Protein         1..248
                     /product="YaaA family protein"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=28074
     Region          2..218
                     /region_name="YaaA"
                     /note="DNA-binding protein YaaA associated with the
                     oxidative stress response [Replication, recombination and
                     repair]; COG3022"
                     /db_xref="CDD:442258"
ORIGIN      
        1 mkivlspskt ktiidaaknd gavnhavrdg qfqphitqei vkhvqsldvm algkalklkd
       61 dkaqalfdfy qdfeshpvgl acesydgiaf kyldwanlsd eakafgeshl vvmsalygvv
      121 eptmgvrdyr ldmvdkvgin lydtwretvd ayfhkedwil nlaskeyakm vnhpkvvtve
      181 fwelrgdtfk qmstsskmsr gmmahaclte qvkhvrdlpr eingftcvtd iesitipses
      241 mtvryerk
//
LOCUS       WP_005387971             282 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein [Vibrio].
ACCESSION   WP_005387971
VERSION     WP_005387971.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            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="formate/nitrite transporter family protein"
                     /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=30012
     Region          5..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mstdfkpaef vqtminvgea ktntstrdll lrgtmagvil slavvvaita ivqtgiglvg
       61 alvfpvgfvi lsvmgydlvt gvfglaplak fanrpgitwg rifrcwglvg lgnligsliv
      121 aylvaisltg nfslelnava kkfvavstar slgfenmgmd gwitcfvrgi fcnlmvclgv
      181 ignmtarsvs grvammwfpi fiffalvfeh tvvnmflfpl gmilgadfgi atwlnfnlip
      241 tilgnivggl vmtciplylt haktapsina eeevkaqpam ak
//
LOCUS       WP_005389219             215 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Corynebacterium
            glucuronolyticum].
ACCESSION   WP_005389219
VERSION     WP_005389219.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium glucuronolyticum
  ORGANISM  Corynebacterium glucuronolyticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 215)
  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   2  (residues 1 to 215)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Corynebacterium glucuronolyticum"
                     /db_xref="taxon:39791"
     Protein         1..215
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21752
     Region          155..214
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mstnrrkiad rigelsqptg tethlnvafp rvsidpkqav aavavivvgl cffflhggae
       61 eadeftpipa vetsappsev vvsvvgavdr pglitlpega rvadalaqag pqpeanlvav
      121 nqaqklvdgt qitvpvqgvv gavgaaepgg gaggvslnsa taaqlqeldg vgektaaaii
      181 ayreqnggfs sleqlqdvkg igpatfdklk nkvtl
//
LOCUS       WP_005392148             270 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Vibrio].
ACCESSION   WP_005392148
VERSION     WP_005392148.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 270)
  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 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   3  (residues 1 to 270)
  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   4  (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   5  (residues 1 to 270)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..270
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30381
     Region          16..268
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <174..268
                     /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 msdsdnpkal pyqeimlpkp aelitlpsym dchdhsytqi viglkgqaef evrgrgnlvg
       61 pgqgcvvtac sdhafggvin qsdilvlnmp kptnddpeml qkinnlerdh vyfqldgqiq
      121 kliqmlvqem rnhpddllls racndtvial mqrhisafet srkesrfdle aidryieqhl
      181 shkisvaqla grvflgesqf hclfkeqmgi tphqyvlgkr idmarelieq ghlslgqiae
      241 ftgfssqstf thtftrlqgi spsrykkqvg
//
LOCUS       WP_005392412             196 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Vibrio].
ACCESSION   WP_005392412
VERSION     WP_005392412.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            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="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19689
     Region          <3..175
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mstsdndtyl gdagvnnqfa dfdggddlfi gfggndsfvg gggndyvigg dgddrltgga
       61 gddilragtg ndylgggtgn dlllgllgdn klnggvgedi lvagsgdnvl vggsngdkfv
      121 ftdkfgghge akvvdftige dslhiisdsv tdfgdlsfsy davgnavftd gadltvklig
      181 vtetdintyg adlfai
//
LOCUS       WP_005394880             786 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: Lon protease family protein [Vibrio].
ACCESSION   WP_005394880
VERSION     WP_005394880.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 786)
  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 786)
  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 786)
  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   4  (residues 1 to 786)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..786
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..786
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88052
     Region          70..786
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mailrleakq lysvadlenm pckstkelpp ideivgqera qkavefamsi kekgyniyai
       61 gqnglgkrtm ilrylnrhqh daaalfdwcy vanfedtrtp kvlklpcgig nklrvdieal
      121 mgkllnalpl afdnemyfsr aerlknqlaa kqqneldris reakekgisl tlttqgdyqf
      181 vamngdelht eesfdalskk eqeqfsdaid elevrlrsmv relteweety sdkikklnde
      241 vtldvithfi kklkvdyaey seiktyltel qkdivenadi fldqsgeqge iatasldkkl
      301 prrykvnvlv srnssdfpiv veenpnyhsl fgsietatfk gtvftdfsli ragslhkang
      361 gvllmdaqkv leqpyvwdgl kralrarqls ftslekevtl tgavsldpep ipldikiilf
      421 gdyrtyqllq hydpefself rvtadfedem krtpeselhy arfissvvnd nnmlhcdrks
      481 mgriieyssr lsgdqtklsl hsanianllr esnyvarqan snmirighve ealknqemrv
      541 srlrdnvmet fvngttlirt egkaigqvna lsvlstsdym fgapnritat tcygdgdvid
      601 iersvdlggs ihskgvmils aylssvfgkt arvpltttit feqsyggvdg dsasmaelca
      661 vvsafskqpn rqdiaitgsm nqfgeaqpig gvnekiegfy dvcvikgrhe gqgviipqsn
      721 vhnlmlrsdi vkavekgefn iwaidhvtea ielftgkvag eptdegsypi dtifglaqak
      781 lnslrk
//
LOCUS       WP_005397144             213 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Vibrio].
ACCESSION   WP_005397144
VERSION     WP_005397144.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 213)
  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 10614777
            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="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=23845
     Region          48..211
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mkklillfiw tflsaspfaf akqadnevks hipqnqieqv fkqakldgvv dfklfrdayi
       61 aykktpdrkk svltiidysk pstekrfyvv dldkkkliyn tyvshgvnsg kktatqfsnv
      121 vnsrktslgt fltdttyygs ngyslrldgl ssglndkare ryivvhgady anpsfikkng
      181 ylgrswgcpa lpkklsreii dtikggsviy asa
//
LOCUS       WP_005397994             272 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Vibrio].
ACCESSION   WP_005397994
VERSION     WP_005397994.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 272)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..272
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=30966
     Region          25..255
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 melknqsdye ryikqdnlge yyvvlnqftf hsvyqpifdk hqriigmeal lrirgidgsl
       61 irpdvflann gldpyfrlcv eflsramhir nfarcfagtp iklflnvmpq tlltltkdmg
      121 fkdngllykr lsdlgmspsd vvfevveesc gdtdllikav qlmrangfif aiddfgaqhs
      181 diarvqqlcp diikidrsyl ldycagetfs ihsavelaah mgakviiegv eedvqlqamy
      241 qldldyyqgf ylgkpcaihh wtdslniett vh
//
LOCUS       WP_005399701             353 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Acinetobacter].
ACCESSION   WP_005399701
VERSION     WP_005399701.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..353
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39410
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvkniek hfgafhalnn isldfpdgql vallgpsgcg kttllriiag lesadggqvi
       61 legedatnvh vrerevgfvf qhyalfrhmt vfdniafglr vrpratrpse aeikkrvirl
      121 ldlvqlgfla drypaqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 tlhdelhits ifvthdqeea levadqiivm nkgnveqigs prevyekpat pfvfdflgqa
      241 nrfegqnnag tiqigedriq ldslrnapsg dviafarpde lrihaqpqdn aiqatfvrel
      301 wiagkvvael hdrqgkliei sltseeaklh qfrpnqtvwl spsnlhlfak paa
//
LOCUS       WP_005400758             132 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Acinetobacter johnsonii].
ACCESSION   WP_005400758
VERSION     WP_005400758.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter johnsonii
  ORGANISM  Acinetobacter johnsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 132)
  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   2  (residues 1 to 132)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Acinetobacter johnsonii"
                     /db_xref="taxon:40214"
     Protein         1..132
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14651
     Region          63..130
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mikikvslli iallllslla wvpssyaqsf dqnylnwkae qqawddriqa pkrvkravsp
       61 vqaqpmlstn kislnqasvd qlqqlqgvgl kkaqaivayr qkqgpfktid elqqvrgigp
      121 aifaknktrl gl
//
LOCUS       WP_005400700             341 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter johnsonii].
ACCESSION   WP_005400700
VERSION     WP_005400700.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter johnsonii
  ORGANISM  Acinetobacter johnsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 341)
  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   6  (residues 1 to 341)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Acinetobacter johnsonii"
                     /db_xref="taxon:40214"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39783
     Region          30..210
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          99..338
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtasehanaq kdsisialvh ealfeaekqg yavadilkna ginsellsat karvsvnqya
       61 qlwtelanvm ndeffgmdrh amrrgsfqfl sksllhttql dqaiqhilqf mnlvlddfss
      121 hlmvqehyay iviyerqqpk rmfsyatyim lihalmcwli gqrvilnqiq lkcdaprddi
      181 dykvrfceni lyqmaenyiq fdanylkmpi kqdskswyqf iqqtphillt ryknphstss
      241 qirrylmqep piqwlelsei ahhfnmseat iqrrlksegf syqqlkndir rdmaiellsn
      301 sqvslqdisi elnfhdpsaf hrafkkwtgv spgayrqnkd a
//
LOCUS       WP_005400806             405 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Acinetobacter johnsonii].
ACCESSION   WP_005400806
VERSION     WP_005400806.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter johnsonii
  ORGANISM  Acinetobacter johnsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 405)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Acinetobacter johnsonii"
                     /db_xref="taxon:40214"
     Protein         1..405
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43683
     Region          5..387
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mstsvlvinc gsssikyalv serredrifg laenlgsada rikgitaggq plelsiphad
       61 hekaletile rlshynpqai ghrvvhggtl tkaellteei veriraatpl aplhnpahlv
      121 gidatmrlfp elpqvavfdt afhqtmpaha yryavpkfly tehnvrrygf hgtshayvse
      181 rgselagsfk qggwltahlg ngsstcaiwn gqsvdtsmgl tplegvvmgt rsgdvdpslh
      241 sflannlgwd iykidkmlns qsgllglsdl sndmrtliea seqgnedatl aievfcyrla
      301 kslaalscgl prldglfftg gigensayir ektvaflphf gfnlskeand slkrgtegri
      361 dtgtgpqiwv iptdeegria ketasvadev iqtaakksed nvaia
//
LOCUS       WP_005401570             626 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Acinetobacter].
ACCESSION   WP_005401570
VERSION     WP_005401570.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 626)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 626)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 626)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 626)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..626
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=69219
     Region          2..626
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mqstakkaal paitlaalgv vfgdigtspl yalrqcflta hlaiseasvl gilslifwcm
       61 mltvsfkyvt iimradnnge ggimsllaln lrttlisdnk kiylialgfi gaslffgdgi
      121 itpaisvlsa ieglsiatpi fnqwleplsi giitglflvq rhgtgtmgkf fgpltllwfl
      181 aigalglwsi fqtphvllmv npywalsfvf nqpyvafltm gaviltmtgg ealyadmghf
      241 grlpirlawf iivlpcllln yagqgalllr dadalanpfy mlipewalfp miglataaav
      301 iasqavitgv fsmvnqaiql rylprlavrh tsevergqiy lpfinwalyi svlilillfe
      361 nsenlasayg vavtmtmlcg tilisilayg lwrwpmwkva lfavpfllld tvfvastslk
      421 ilsggwvpil igavlytilm twkdgralvl krlekdslpi dlfiksismg setkfvpgda
      481 vfltgtpniv phamlhnikh nkvlhernim vtvitrdipf vpsqerssve kldvrfyrit
      541 lyygfkdqpn ipqalemaya elgfeydlmq isffisreri istvgdgmap wreklfismq
      601 rntspvsdfy qiptnrvvel gsqiqi
//
LOCUS       WP_005401704             232 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Acinetobacter].
ACCESSION   WP_005401704
VERSION     WP_005401704.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 232)
  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 232)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 232)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..232
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=25603
     Region          4..209
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Site            order(96..97,100..101,103,131,134..135,138..139,141..142,
                     164,167..168,171..172,175)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          96..124
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          129..157
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          163..189
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msalsdeeql dslksftkky gsaiisgili aliaffgwqy wqkktlaenq mntakvqqlm
       61 dearatqgda ftalsatadk ivkeapdsaq aiqtqllmak laydkadyas aekalkkven
      121 skvdddglvq ivklrlayaq laqkkfddai knlalvkdpa fkatadealg dvyvakndie
      181 nakkayqsaw dqlverkqer qilqiklesv gilvddpeie rplietaaee te
//
LOCUS       WP_005401812             694 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor family protein
            [Acinetobacter].
ACCESSION   WP_005401812
VERSION     WP_005401812.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..694
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=77240
     Region          25..694
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mekrcflknp ivmsgllfss fipnlyaape qeqksmvlpm iqvigsqeda vskipgaavi
       61 vdqeqikqvi ptstedilkr vsgvyvkpee esavvanigm rgissadykt liledgvpva
      121 pglfvgngry ynprvqrmds ievmkgssal rygplniggv inyqtkqpkd galvdvsvgs
      181 wdtykttvel ggsspnkdsk vgailswaks dgfmdkgyem kdavikagta igdnqwlgvk
      241 fthyendani syrgqflgey qnekesnpap ddwflterns fdvnhrwnin ddmelqtlfy
      301 wsemnrdywr ydvdgaaska agqwiykdtl ngnnraferi gaetrlvtkh tlfnisseae
      361 vglrlmnekm ddvtikatra tprtgtvnkd vkdsaksval yaqnrlditd qlsvtpgvri
      421 ehyeqqredk kknesvktsn tevmpglgvt fqldpavqly gsvykafspa lngdslsglq
      481 dqkldaetav swefglrgqq dalsyemtaf rmdfdnqiip ansnsdfqst nggktynqgl
      541 egavnleldn gfdvfanltw vidaqfkgdr ynkngtlksr dgdrvpytpe wianlglgyt
      601 yaglrtqlsa nytgsqftde lntkpivent sgfftgking yttvdlttry tlndqvefyg
      661 avknladkry iaslrqgiyv gpersleagv ryrf
//
LOCUS       WP_005402480             353 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter junii].
ACCESSION   WP_005402480
VERSION     WP_005402480.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter junii (Acinetobacter grimontii)
  ORGANISM  Acinetobacter junii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 353)
  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 353)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 353)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 353)
  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   5  (residues 1 to 353)
  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   6  (residues 1 to 353)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Acinetobacter junii"
                     /db_xref="taxon:40215"
     Protein         1..353
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40463
     Region          41..212
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          100..345
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msklpnqdin sakdtisnal irealsvaas rglnivnian kagisaellt stkarvpvnq
       61 saqlwvelak smndeflgmd thpmrrgsyk vlaklafgad tleqaiqdil kflalilddi
      121 hgelvqegsk aflilhdrdq pkrmftystf lmlvhslmcw lsdqrisfhr msfrchqpve
      181 iqdyrvrfce niefnaeqnk iefdahylkh kikkdkqaln eflkhapynl ivrfknensl
      241 slqirrqlil qppsewaelk diaqqmnmst atiqrrlkqe gvsyqqlknn ircdiaierl
      301 sktndsiqsi sddlnfhdps afhrafkkws gvspgsyrkt spskkllvnq fed
//
LOCUS       WP_005402599             291 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter junii].
ACCESSION   WP_005402599
VERSION     WP_005402599.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter junii (Acinetobacter grimontii)
  ORGANISM  Acinetobacter junii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 291)
  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 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   3  (residues 1 to 291)
  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   4  (residues 1 to 291)
  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 291)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Acinetobacter junii"
                     /db_xref="taxon:40215"
     Protein         1..291
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32717
     Region          24..175
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          202..284
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mmnnqilssl flklvakegf fataidgitl mrvdhntppl avlqeptlvf vlqgskrgyi
       61 gtetyafqqg eclivsvsmp fdcdtfaspe lpmiaasmkl eantvnella kiyfendkfk
      121 alttgmsviq ydetisnvli rllktlsseq dslilgeqik rellyrviqh sgadaltglv
      181 vqgnlrqiyk iceyiqhhft ekltvemfae qanmsisafh kafkqvtlhs plqylkvtrl
      241 hkakqmlqne nqsvaqaaya vgyqsssqfs refkkqfgfs pnqtevnihk e
//
LOCUS       WP_005404618             172 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Acinetobacter radioresistens].
ACCESSION   WP_005404618
VERSION     WP_005404618.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..172
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=17257
     Region          2..168
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mnaqkgftli elmivvaiig ilaaialpay qdytirarvs ealsvaggak ttvaenitan
       61 ggvlpaasan gnkgacagvs lfdaksktda knvgnvekld ctpatgaivv tmndkgkgvt
      121 ltltptadta avkgatpdkd vaavnnpgia wkctttegsf kyvpaecrnt as
//
LOCUS       WP_005404639             335 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005404639
VERSION     WP_005404639.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 335)
  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 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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 335)
  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   5  (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   6  (residues 1 to 335)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38734
     Region          51..193
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          82..330
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msqlknytgs vygglghllk aycetkniei peqlqqvqnl erfdyviwrd lledlnrlnp
       61 ktglgleiae hvqpkhlgii aylalscenl gealaryhdf hrliydgspl vvefnppyas
      121 irweapepnp tqltdeiaia lmvqfhklfl sgedlnlhev hfvntapkni mvyeqyfrck
      181 vrfdqpktql llpvteafkp lrtgdhtlqq lllqqaqall dklpnstqld qrlqhailtg
      241 lqknqyqidf iakklgvsvr qlqrhlqqqn atfqervqev rfmlateylk dphlslqeia
      301 lllcyseqsa fqrafklwtg ltpqqwrknn tiyss
//
LOCUS       WP_005404642             625 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Acinetobacter].
ACCESSION   WP_005404642
VERSION     WP_005404642.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 625)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..625
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=69051
     Region          2..625
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mqssakkaal paitlaalgv vfgdigtspl yalkesfhaa hglgistanv lgilsiifwt
       61 mtlvitikyi aivmradnng eggimallal nlrntrfsdr kkllliaigf igaslffgdg
      121 iitpaisvls aveglsiatd aldpyivpia itivttlfim qkygtafvgk ffgpltllwf
      181 fslgllgiss iiqtpvvlgm fsphwafqfi vshplmtffi mgavvltvtg gealyadmgh
      241 fgpvpirlaw ffvvlpclvl nyagqgalll rnpsaienpf yllvpewaly pmiflatmaa
      301 viasqavisg vfslarqaiq lgylprltvk htsdseqgqi yvpllnwvll asiivlilif
      361 qtssrlanay glavtltmlc dtlliaafir yswkwkmpkl mlliipflil dlvlvsatsl
      421 kvfsggwvpl liggvaflll itwkqgrelt fvklqqdtlp lelfvesigd qanwvegeav
      481 fltgtptvvp hamlhnmkhn kvlhqkniil tvkiqdvpym pdeqrfhvev lnqhfyrvel
      541 yygfkdemni phaleavyea leleynlmqi sffvsrerii stvgdgmapw reklfismqr
      601 ntspvsdfyq iptnrvvelg sqiei
//
LOCUS       WP_005404782             341 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005404782
VERSION     WP_005404782.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 341)
  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 341)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39560
     Region          44..209
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          259..337
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msvfkisngy fhlwktclqs kslnwrqldl saeqqqqleh ilslpidtqs dmqffldlie
       61 vsrqqwslpn lvldmaycis panfgvlgym asnsatlaqa iqyvmrfhrl vidseqalpl
      121 hiteyknkir lywplvdeqm tvlceltlaa mvhlarqiip eqqlflqave fvhfpkvsll
      181 nyqkffqctl kfqqpyyait fareslnsrp yqadstliql lvrqaeeala skataqdltq
      241 qihwivgeyl kqqqraplle wiadelhlsv rslqralkkq ntsfkeivdl qtmkrcelll
      301 vqneslnria eqlgysdqsa lvraykrvrg stllafrraq q
//
LOCUS       WP_005405262             625 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Acinetobacter radioresistens].
ACCESSION   WP_005405262
VERSION     WP_005405262.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 625)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..625
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=69050
     Region          2..625
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mqssakkaal paitlaalgv vfgdigtspl yalkesfhaa hglgistanv lgilsiifwt
       61 mtlvitikyi aivmradnng eggimallal nlrntrfsdr kkllliaigf igaslffgdg
      121 iitpaisvls aveglsiatd aldpyivpia itivttlfim qkygtafvgk ffgpltllwf
      181 fslgllgiss iiqtpvvlgm fsphwafqfi vshplmtffi mgavvltvtg gealyadmgh
      241 fgpvpirlaw ffvvlpclvl nyagqgalll rnpnaienpf yllvpewaly pmiflatmaa
      301 viasqavisg vfslarqaiq lgylprltvk htsdseqgqi yvpllnwvll asiivlilif
      361 qtssrlanay glavtltmlc dtlliaafir yswkwkmpkl mlliipflil dlvlvsatsl
      421 kvfsggwvpl liggvaflll itwkqgrelt faklqqdtlp lelfvesigd qanwvegeav
      481 fltgtptvvp hamlhnmkhn kvlhqkniil tvkiqdvpym pdeqrfhvev lnqhfyrvel
      541 yygfkdemni phaleavyea leleynlmqi sffvsrerii stvgdgmapw reklfismqr
      601 ntspvsdfyq iptnrvvelg sqiei
//
LOCUS       WP_005405842             267 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Acinetobacter
            radioresistens].
ACCESSION   WP_005405842
VERSION     WP_005405842.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   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 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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..267
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29071
     Region          26..93
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          195..256
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mevnpnsqqp tgsssnvapn algnvqrpge ylrhiriakn leletvaadl kiplktlkal
       61 eqddyktlpe aafikgyyrs yakylgtdat aiiqrfdeiy andtgllpnh alnnspikim
      121 gklpgsnsdr nrkwikraiv aavilllvwl vvaaiqnwts gkkdeterpa vaqsevqivd
      181 ldnslnaaas gdqlvlnftr ptsvhivdat gkvlatgrqd stltlsgesp yqirlddata
      241 vslslnseqi slspytvngk aefrlsr
//
LOCUS       WP_005405568             341 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            radioresistens].
ACCESSION   WP_005405568
VERSION     WP_005405568.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 341)
  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   6  (residues 1 to 341)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39959
     Region          29..206
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          92..341
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mdrtdleesk gtisvslvhe almvaysrgl dtrlilqkae iapeilhsak aripisayar
       61 lwtaladhmn deffgmdrhp mrrgsyqlls kmllqaetle kavqdmlkfl nfilddlqve
      121 lqleqdkayl vlhdqgpvkr mfsyatylml vhglicwlsg qrvildkiel rcmqplddqd
      181 yrvrfcekiy ygasqnrief srhyleikik kdknawydfl khtpqnllvr yknpdslsfs
      241 irkylselip aewpeltdia arfnlsettm hrrlkyegvs yqqlkndirr diaieyltht
      301 dlslqdiseq ldfhdasafh rafkkwtgvs pgtyrqnrsk l
//
LOCUS       WP_005406885             353 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Acinetobacter].
ACCESSION   WP_005406885
VERSION     WP_005406885.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..353
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39631
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvkniek hfgafhalkn isldfpegql vallgpsgcg kttllriiag lesadggqvl
       61 legsdatdvh vrerqvgfvf qhyalfrhms vfdniafglr vrprstrpse aeikkrvtrl
      121 ldlvqlgfla drypaqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 tlhdelhits ifvthdqeea levadqivvm nkgnieqigs prevyekpat pfvfdflgqa
      241 nrfegqyqqg iiqigqdriq lphsveiaqg kvvafarpde lrihaqpqdn tiqaiflrei
      301 wiagnvvael qdrngnliei tlspeevkqh qfraqqnvwi sasalhlfed qva
//
LOCUS       WP_005406969             336 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter
            radioresistens].
ACCESSION   WP_005406969
VERSION     WP_005406969.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 336)
  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 336)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..336
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38346
     Region          22..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          249..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msrdtisihf vnaaltgvkr lgmdvetlls hvgieaellr qpkarispeq ytrfikmlwm
       61 vtqdehvgfd vqprrlgtfa imcqliihak tlgdalelss qfyklfgdew svtlerdkhe
      121 arlvplipks mdpdhfites mlmiwhglas wligrriple rvhfsyarpa hadeydalff
      181 apvmqfdapr tevtfaadyl dlpirqndes leeflktapa qllvkfknvn sltsrirdvl
      241 ksqigeempt lndvasmlyl spqtlrrrla aegksyqgvk dalrrdaaih lllnpeltle
      301 dvaqqvgfse tstfhrafkk wtgvtpglyr qlhgyh
//
LOCUS       WP_005407289             195 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Acinetobacter
            radioresistens].
ACCESSION   WP_005407289
VERSION     WP_005407289.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 195)
  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 195)
  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   3  (residues 1 to 195)
  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   4  (residues 1 to 195)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 195)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..195
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22366
     Region          1..191
                     /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"
ORIGIN      
        1 msklkivlid ddleraeyir vsllehhfdv vaclvidhsn msylqqlhad villdiqnph
       61 rdiiencvsh fdlptvlftk nshkdtiksa idagvtayiv dgidpakldn ilqisieqfk
      121 khrkllnalk etegkladrk diekakvllm qmhhlseeda frllrknams hrmtmgkmar
      181 rlldaqqllq trlkd
//
LOCUS       WP_005407037             341 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005407037
VERSION     WP_005407037.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 341)
  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 341)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39535
     Region          44..209
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          259..337
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msvfkisngy fhlwktclqs knlnwcqldl saeqqqqleh ilslpidtqs dmqffldlie
       61 vsrqqwslpn lvldmaycis panfgvlgym asnsatlaqa iqyvmrfhrl vidseqvlpl
      121 hiteyknkir lywplvdeqm tvlceltlaa mvhlarqiip eqqlflqave fvhfpkvsll
      181 nyqkffqctl kfqqpyyait fareslnsrp yqadstliql lvrqaeeala skataqdltq
      241 qihwivgeyl kqqqraplle wiadelhlsv rslqralkkq dtsfkeivdl qtmkrcelll
      301 vqneslnria eqlgysdqsa laraykrvrg stllafrraq q
//
LOCUS       WP_005407699             282 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Stenotrophomonas maltophilia].
ACCESSION   WP_005407699
VERSION     WP_005407699.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas maltophilia
  ORGANISM  Stenotrophomonas maltophilia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas; Stenotrophomonas
            maltophilia group.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Stenotrophomonas maltophilia"
                     /db_xref="taxon:40324"
     Protein         1..282
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28959
     Region          169..236
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mltralivvl ailnlgvacw wllrdapqkp apppqpagva elrwvpggvd aaaaaeataa
       61 aptaplmere paektavavt palaapakpe iakpqaaeat pvaaaakpat ppaptpapek
      121 pvtppvaaep prcialgpfa draaatnaqg kastllsqvr lreqpaasgs aryrvmlpaa
      181 anreeaqatv krivaaglsd yyiisqgeea navalgqyrn regaerrmaa vqaagfqprl
      241 vasgdagqww legqlaagaq paqaqqrsga aqsrslectr lr
//
LOCUS       WP_005408414             361 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Stenotrophomonas maltophilia].
ACCESSION   WP_005408414
VERSION     WP_005408414.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas maltophilia
  ORGANISM  Stenotrophomonas maltophilia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas; Stenotrophomonas
            maltophilia group.
REFERENCE   1  (residues 1 to 361)
  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 11482063
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Stenotrophomonas maltophilia"
                     /db_xref="taxon:40324"
     Protein         1..361
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=37988
     Region          41..339
                     /region_name="PRK06132"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:235709"
ORIGIN      
        1 mlphrpttlm lalalalpll ahaaaptaaa kptaaaassa evrgptdlkp geylwhpeis
       61 ptgpivlvvs ldeqrayvyr ngiaigltti ssgkaghetp tgvftilqkd kdhrsnlyns
      121 apmpymqrlt wdgialhggs lpghpashgc vrlpqafaqk lfsetqrgdt vvvadakssp
      181 mtlaypsvla pvnargqalp eaeggapaqa wwddsaapag qvgilvslhd qrlyvlrdgv
      241 migesplkad alpafqgttl fvmgqgysdt pspldvnqrl hqwtaypllg qdraqatpdl
      301 latpslpmal ppdfarqlyq vlvpgttllv tslpavrpsp aesgmqpvle seppgstlkg
      361 n
//
LOCUS       WP_005409528             609 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Stenotrophomonas maltophilia].
ACCESSION   WP_005409528
VERSION     WP_005409528.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas maltophilia
  ORGANISM  Stenotrophomonas maltophilia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas; Stenotrophomonas
            maltophilia group.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 609)
  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   3  (residues 1 to 609)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Stenotrophomonas maltophilia"
                     /db_xref="taxon:40324"
     Protein         1..609
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=64944
     Region          6..608
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msavsddita dfiieaqeil drlgeqlvsl eqapqdteql navfrgyhtl kggagflgvt
       61 amvelchaae ealgiaragq avlqahhfda aqqsldylqs mldavssgte pgyappdlia
      121 qfdmnggtaa pvaaaapaaa gsdlitddef ealldqlhgg naptavapar kaddglised
      181 efealldqlh ggaapgakpa atvaaapaaa prpapapapa akpaakpmae aehtvrvdtk
      241 rldaivnlig elvlsrnrlk tlrarlrdee ldravstldi atarlqsavm rtrmqpvgkv
      301 fsrfpkvard varslkkevd lelvgaetel drnlvealad plvhlvrnai dhgvempdlr
      361 eaqgkprmgh vrlsaqqegd yvsievqddg agidpeklra karekglidp eaaarlssee
      421 clhlvflpgf stkqqvtdis grgvgmdvvq srirelsgqi qiqselgrgs rflirvpltl
      481 ailptllvqa gedvyalpla rvmevlhapr tslgwfdgra vldrrshtlp lvdlrqwldv
      541 tpaastllti vvlqagearf glvvdqvrgr eevvikplpk alrglrgyag atligdgrma
      601 lildvdgir
//
LOCUS       WP_005409520             663 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Stenotrophomonas].
ACCESSION   WP_005409520
VERSION     WP_005409520.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 663)
  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   3  (residues 1 to 663)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..663
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=70120
     Region          3..658
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msmdlqrfha tffeesregl dameagllal esgqqdaeii nsvfraahsi kggagtfgfd
       61 aiaglthvle tlldelragk raleghavda mlssvdvlra llreaehgqa adpaavaavk
      121 arleavlsgq aapsapaaaa akvddtpeaw qigftpapsl fmsgndplri irelehlgsl
      181 qvaarmerlp gfaqldplea hlawdlglvg kvprskiedt fawvlddcel dirpaappsl
      241 atqapvaasp stpaavvpaa paapaaggaa tqeaetsirv svdkvdalin lvgelvitqa
      301 mlkqvshald pvhaeslfag ldqlerntrd lqeavigvrm lpvdavfrrf prlvrdlssr
      361 lgkqvrlrtv gegteldkgl iekiadplvh lvrnsidhgl empdvrrgag kdetgtitla
      421 ashqgghivi evsddgrgld rakilakate rglavpdnpt dsqvwdlifq pgfstadavt
      481 dlsgrgvgmd vvrrniqalg gevqiesslg tgtrtlirlp ltlaildgmt vavagetlil
      541 playvlealq pqaedirsma gegrvlrvrg eylpilslse yygygnrapg seslvvvveg
      601 dgqkialevd elvgqqqvvv kniennyrri ggvsgatilg dgrvalivdi gglvrslrmp
      661 qaa
//
LOCUS       WP_005409675             336 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Stenotrophomonas
            maltophilia].
ACCESSION   WP_005409675
VERSION     WP_005409675.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas maltophilia
  ORGANISM  Stenotrophomonas maltophilia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas; Stenotrophomonas
            maltophilia group.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 336)
  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   6  (residues 1 to 336)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Stenotrophomonas maltophilia"
                     /db_xref="taxon:40324"
     Protein         1..336
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37230
     Region          21..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <136..326
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 maskttfpie qglrpllkdm giridhvlrr aglpedllsr ptgvlttteh frlwqgleae
       61 aadpqlplri agmiqadsfv pplfaalcsa nmtqavqrla tykrlmapmr metstgaqge
      121 llvmphwiga esgvpfilva tevaflmrli rlgtrehiqa mkvtlptlpd pahanayaey
      181 fgvairrdat acitlspsda drpfltanda iwemfepdlr rrlgeldata ttaqrvrsvl
      241 lellpggqss veavasrlam strtlqrrld degdsfrsiv nrtredlakh yltqtklsis
      301 eisfllgfdd pnsfyrafhg wtgrtpdsmr skalpn
//
LOCUS       WP_005409907             222 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Stenotrophomonas maltophilia].
ACCESSION   WP_005409907
VERSION     WP_005409907.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas maltophilia
  ORGANISM  Stenotrophomonas maltophilia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas; Stenotrophomonas
            maltophilia group.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Stenotrophomonas maltophilia"
                     /db_xref="taxon:40324"
     Protein         1..222
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=24505
     Region          17..>220
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mwldlqvrrr lqaagqdfvl dvslqctqrq vvlfgpsgag ksltlkavag llrpgqghvr
       61 lqgqtlfdaa tavdlppqrr rlgyvfqdya lfphlsvrqn vafglqkgwl nprvgqrfda
      121 veqwlhafri dtvgdllpsq vsggqrqrta laralvtqpq allldepfsa ldhdlrqhlr
      181 qeletvldkt giplllishd pqdvamfgqq varvvdgriv gg
//
LOCUS       WP_005410196             703 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Stenotrophomonas
            maltophilia].
ACCESSION   WP_005410196
VERSION     WP_005410196.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas maltophilia
  ORGANISM  Stenotrophomonas maltophilia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas; Stenotrophomonas
            maltophilia group.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Stenotrophomonas maltophilia"
                     /db_xref="taxon:40324"
     Protein         1..703
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=76815
     Region          19..702
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mslssyrptp sllflavslg lsstaaaapq attldavqvt aaadasaqar ealkrvpgas
       61 nlidvakads rlstsadvla yqpgisaqsp gnegtkisir gsginrgpga hasgiavsid
      121 glpltgpggt pyelleplwl srvevlrgan gfergalalg gaidyvsrsg rdsagvqlhy
      181 eagsrgyqkr giswggvsgd vdyflaytdt gfdgyqrhar gdgkgamanv gwqitpelqt
      241 rffvryretn hetpgrltrd qirndpraan aanlaidarr pqpgstwvgn vttlqideds
      301 slqaglvyhk ypmdlnesly rqqldyanln atldyrrrhr lfgldsettv glrvthdlda
      361 dvreslrfas ngyaagtrtr dfrhhgtdst lhvgntltfn drlrmqtgla lintrrdvqv
      421 twpssggrlr dhdwdyaprl gftwqhsaqt qwfgnlsrsv eaphpwsmiw gsnqyfgpgn
      481 gpssgrqrap vpmqnqtatt lelgargdaa lgrweltgyy ahvnhellsv elqpvpnlfi
      541 aennasptvh rgmeagldst lwqaapgrls lrqaytfsdf ryrhdarfgs nrlpglprha
      601 yqaelrfdha sglyaalnte yasriavdya nsywadshvi fgsrigydap ggrwqawaem
      661 rnlgnrhyaa tvtpgyddag kdvarstpgd grgvyagvrw rfd
//
LOCUS       WP_005410277             747 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor family protein
            [Stenotrophomonas].
ACCESSION   WP_005410277
VERSION     WP_005410277.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 747)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..747
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=81445
     Region          24..747
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mpshaplrrn llallvcasl pslavaetap atdaqsattl dsisvigrge arqvqrvtae
       61 dmkvlppgan plkllaakpg vhfesadatg ayewstsisl rgfnqnrlgy tldgiplgnm
      121 aygnsnglhi sravisenlg gaevstgiga lgtpstsnlg gvfqfysidp steygvvlaq
      181 sfgsdnarrs yarldtgdhq gfaaylsgvy segdkwkgkg sqelkqfngk atynfgtdsr
      241 italsnasrr veadyqdlsl emidrlgwdw dnyapdwdra vaaargkysg gvnspwdayy
      301 sghglrnddv ssiagdfgln esmrlkvnvy nhsnrgqghw fspsnpsnpg tsreipisir
      361 tteyaidrtg vtsaftwnva gheleaglwy ednghsvqrn fyyidgpitd dfflrnpdqr
      421 vwhqryttit rqfyvqdrfr lfddrltidi gaksphtrtr vrtplgsyan nssltskkgl
      481 lpqagfnfkl negneifgsf aknvaayalg vgspfnvpqa afdasaknlk peqsrtielg
      541 wrgygqgyea svavydvkfd nrllaiaqcv gilgcpalfs nvgsvtsrga eatlqlkpmq
      601 dltwsnalsw ndstydndyv nngvvptrgk ktvdtpewmf astlawtpgp wdlrlaanhv
      661 gkryvtytnd vsvpsywlvn asvaydfgkl gpaqnltval nltnltdkry lssintngty
      721 aadptrslat mqvgaprqvm atatvhf
//
LOCUS       WP_005410636             320 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase family protein [Stenotrophomonas].
ACCESSION   WP_005410636
VERSION     WP_005410636.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 320)
  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 11465564
            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="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=33785
     Region          <50..100
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          188..317
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mplpvyrstl lalsllaspa faqapppglp apiaekagpd taarsalhaq vlldranfsp
       61 gqidgevgsn qrravsgfqa ahgltvtgel ddatwqalqa dtvtplasyt ltsedvagpf
      121 qavpkgpaaq aklkslgfnn veeslgerfh aspellklln pgvdlskagn riqvpniaps
      181 plpkaakvvv dksdsslqll daqgkviaqv pvssgsqhdp lpigewkilg vyrdppfhyn
      241 pklfwdarkg ekkatlppgp nnpvgrvwid lskphyglhg tpepghvgkt eshgcvrmtn
      301 wdalrvadav dtsvpvvmqe
//
LOCUS       WP_005412144             160 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Stenotrophomonas maltophilia].
ACCESSION   WP_005412144
VERSION     WP_005412144.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas maltophilia
  ORGANISM  Stenotrophomonas maltophilia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas; Stenotrophomonas
            maltophilia group.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Stenotrophomonas maltophilia"
                     /db_xref="taxon:40324"
     Protein         1..160
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17021
     Region          8..159
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfanasltgs kpeqyaqlle qarglvyaes drianaanls alvyhalpdl nwvgfylydg
       61 kelvvgpfqg lpacvripld kgvcgaaasq rvtqrvedvd afpghiacds asrselvvpl
      121 lrgdeligvf didspkvgrf daddqtglea iarvfvealg
//
LOCUS       WP_005413943             747 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Stenotrophomonas
            maltophilia].
ACCESSION   WP_005413943
VERSION     WP_005413943.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas maltophilia
  ORGANISM  Stenotrophomonas maltophilia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas; Stenotrophomonas
            maltophilia group.
REFERENCE   1  (residues 1 to 747)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Stenotrophomonas maltophilia"
                     /db_xref="taxon:40324"
     Protein         1..747
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=81478
     Region          24..747
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mpshaplrrn llallvcasl pslavaetap atdaqsattl dsisvigrge arqvqrvtae
       61 dmkvlppgan plkllaakpg vhfesadatg ayewstsisl rgfnqnrlgy tldgiplgnm
      121 aygnsnglhi sravisenlg gaevstgiga lgtpstsnlg gvfqfysidp steygvvlaq
      181 sfgsdnarrs yarldtgdhq gfaaylsgvy segdkwkgkg sqelkqfngk atynfgtdsr
      241 italfnasrr veadyqdlsl emidrlgwdw dnyapdwdra vaaargkysg gvnspwdayy
      301 sghglrnddv ssiagdfgln esmrlkvnvy nhsnrgqghw fspsnpsnpg tsreipisir
      361 tteyaidrtg vtsaftwnva gheleaglwy ednghsvqrn fyyidgpitd dfflrnpdqr
      421 vwhqryttit rqfyvqdrfr lfddrltidi gaksphtrtr vrtplgsyan nssltskkgl
      481 lpqagfnfkl negneifgsf aknvaayalg vgspfnvpqa afdasaknlk peqsrtielg
      541 wrgygqgyea svavydvkfd nrllaiaqcv gilgcpalfs nvgsvtsrga eatlqlkpmq
      601 dltwsnalsw ndstydndyv nngvvptrgk ktvdtpewmf astlawtpgp wdlrlaanhv
      661 gkryvtytnd vsvpsywlvn asvaydfgtl gpaqnltval nltnltdkry lssintngty
      721 aadptrslat mqvgaprqvm atatvhf
//
LOCUS       WP_005414172             320 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Stenotrophomonas maltophilia].
ACCESSION   WP_005414172
VERSION     WP_005414172.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas maltophilia
  ORGANISM  Stenotrophomonas maltophilia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas; Stenotrophomonas
            maltophilia group.
REFERENCE   1  (residues 1 to 320)
  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 11465564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Stenotrophomonas maltophilia"
                     /db_xref="taxon:40324"
     Protein         1..320
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=33688
     Region          <50..100
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          188..317
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mplpvyrstl lalsllaspa faqapppglp apiaekagpd taarsalhaq vlldranfsp
       61 gqidgevgsn qrravsgfqa argltvtgel ddatwkalqa etvgplagyt ltaedvagpf
      121 eaipkgpaaq aklkslgygs veealgerfh aspellrvln pgidlakagn riqvpniapa
      181 alpkatkivv dksdstlqll daqgkviaqv pvssgsqhdp lpigewkilg vyrdppfhyn
      241 pklfwdarkg ekkatlppgp nnpvgrvwid lskphyglhg tpepghvgkt eshgcvrmtn
      301 wdalrvadav dtsvpvvmqe
//
LOCUS       WP_005413241             663 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Stenotrophomonas maltophilia].
ACCESSION   WP_005413241
VERSION     WP_005413241.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas maltophilia
  ORGANISM  Stenotrophomonas maltophilia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas; Stenotrophomonas
            maltophilia group.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 663)
  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   3  (residues 1 to 663)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Stenotrophomonas maltophilia"
                     /db_xref="taxon:40324"
     Protein         1..663
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=70178
     Region          3..658
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msmdlqrfha tffeesregl dameagllal esgqqdaeii nsvfraahsi kggagtfgfd
       61 aiaglthvle tlldelragk raleghavda mlssvdvlra llreaehgqa adpaavaavk
      121 arleavlsgq aapsapaaae akvddtpeaw qigftpapsl fmsgndplri irelehlgsl
      181 qvaarmerlp gfaqldplea hlawdlglvg kvprskiedt fawvlddcel dirpaappsl
      241 atqapvaasp stpaavvpaa paapaaggaa tqeaetsirv svdkvdalin lvgelvitqa
      301 mlkqvshald pvhaeslfag ldqlerntrd lqeavigvrm lpvdavfrrf prlvrdlssr
      361 lgkqvrlrtv gegteldkgl iekiadplvh lvrnsidhgl empdvrrgag kdetgtitla
      421 ashqgghivi evsddgrgld rakilakate rglavpdnpt dsqvwdlifq pgfstadavt
      481 dlsgrgvgmd vvrrniqalg gevqiesslg tgtrtlirlp ltlaildgmt vavagetlil
      541 playvlealq pqaedirsma gegrvlrvrg eylpilslse yygygnrapg seslvvvveg
      601 dgqkialevd elvgqqqvvv kniennyrri ggvsgatilg dgrvalivdi gglvrslrmp
      661 qaa
//
LOCUS       WP_005414276             639 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Stenotrophomonas maltophilia].
ACCESSION   WP_005414276
VERSION     WP_005414276.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas maltophilia
  ORGANISM  Stenotrophomonas maltophilia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas; Stenotrophomonas
            maltophilia group.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 639)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 639)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 639)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 639)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 639)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Stenotrophomonas maltophilia"
                     /db_xref="taxon:40324"
     Protein         1..639
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=69628
     Region          19..639
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msssqtphaa ahgghghaps agglalviga igvvfgdigt splytlkeaf sphyglnsdh
       61 dtvlgvlsla fwalnlvvtl kyvtiimrad ndgeggimal maltqrtlrh gsrsayvvgi
      121 lgifgaslff gdgvitpams vlsaveglev aapglhvfiv pvtlvvllav faaqrfgtek
      181 igkafgpima iwfvslaaig iynivdapev lkafnpwwgi rffmehgwhg ifilgavvla
      241 vtggealyad mghfglrpir hawyffvlpc lvlnylgqga lvlnhpealk npffeavpsw
      301 alypmiilat maaviasqsv itgafsvsrq amqlgyiprm rikhtshdti gqiyipginw
      361 giavmvfglv lafrsssnla vaygisvsat mlidtlllav varslwpksr gwllplcvvf
      421 fiidlgfvia ngakllqgaw fpvvlgiflf tmmrtwrrgr ellrdeirkd girldtflpg
      481 lmlappvrvp gtavfltadp tvaphalmhn lkhnkvlher nvflhvetlp ipyamegqrl
      541 kiesvgdefy rvyvrfgfme tpdvplalmr scdhggiyfd pmdttffasr etivatanrg
      601 mpiwrdklfa lmhrnaapat gffripgnrl velgaqvei
//
LOCUS       WP_005415580             361 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Stenotrophomonas maltophilia].
ACCESSION   WP_005415580
VERSION     WP_005415580.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas maltophilia
  ORGANISM  Stenotrophomonas maltophilia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas; Stenotrophomonas
            maltophilia group.
REFERENCE   1  (residues 1 to 361)
  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 11482063
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Stenotrophomonas maltophilia"
                     /db_xref="taxon:40324"
     Protein         1..361
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=37912
     Region          41..339
                     /region_name="PRK06132"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:235709"
ORIGIN      
        1 mlphrpttlm lalalalpll ahaaapapaa kpaaatagta evrgptdlkp geylwhpeis
       61 ptgpivlvvs ldeqrayvyr ngiaigltti ssgkaghetp tgvftilqkd kdhksnlyns
      121 apmpymqrlt wdgialhggs lpghpashgc vrlpqafaqk lfsetqrgdt vvvadakssp
      181 mtlaypsvla pvnargqalp eteggapaqa wwndsaapag qvgilvslhd qrlyvlrdgv
      241 migesplkad alpafqgttl fvmgqgfsdt pspldanqrl hrwtaypllg qdraqatpdl
      301 latpslpmal padfarqlyl vlvpgttllv tslpavrpsp aesgmqpvle seppgstlkg
      361 n
//
LOCUS       WP_005415966             135 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Stenotrophomonas].
ACCESSION   WP_005415966
VERSION     WP_005415966.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..135
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14553
     Region          6..135
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mlhtpmprra agftlielmi vvivigilaa iaipsyqeyv rrshravvka dlaeyaqrae
       61 ryhtsnnsyt gyalptkvsp rdggtarynl dykgdgtsft itatpqgtqa kdscgklsvd
      121 qanrktadgg vascw
//
LOCUS       WP_005416827             222 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Stenotrophomonas maltophilia].
ACCESSION   WP_005416827
VERSION     WP_005416827.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas maltophilia
  ORGANISM  Stenotrophomonas maltophilia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas; Stenotrophomonas
            maltophilia group.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Stenotrophomonas maltophilia"
                     /db_xref="taxon:40324"
     Protein         1..222
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=24664
     Region          21..>220
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mwldlqvqrr lqaagqefvl dvslqctqrq vvlfgpsgag ksltlkavag llrpgqghvr
       61 vqgqtlfdaa tgvdlppqrr rlgyvfqdya lfphlsvrqn vafglekgwl nprnrqrfda
      121 veqwlhafri dtvgdllpsq vsggqrqrta laralvtqpq allldepfsa ldhdlrqhlr
      181 qeletvldrt giplllishd pqdvamfgqq varvvdgriv gd
//
LOCUS       WP_005416978             326 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Stenotrophomonas maltophilia group].
ACCESSION   WP_005416978
VERSION     WP_005416978.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas maltophilia group
  ORGANISM  Stenotrophomonas maltophilia group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 326)
  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 326)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Stenotrophomonas maltophilia group"
                     /db_xref="taxon:995085"
     Protein         1..326
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35687
     Region          67..321
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          235..317
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mvdggvedsd dsglrsidla tlsgvlrvcd velllldgng praafasrvh eealfcsitc
       61 gfhcrgrfml ppdwamlgyl hatdetmswc hgvpltpgma ltimpegise ftlspgthmt
      121 lmlvpvarvq rkltelslrs tppagqalsl fnlasdatpl arhyqqlhlq lgqgaglqpd
      181 etenllhehv qallgagaad rpgctrarrt hyliaqraen fmrlnlrrni ymneicdaag
      241 vserglryaf edlfgtspnr ylsmlrlcaa crslsmadss rrsvkaials cglwdlsrfa
      301 dnyrkvfgel prdtlmrapa qigqpa
//
LOCUS       WP_005417160             116 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Aliivibrio fischeri].
ACCESSION   WP_005417160
VERSION     WP_005417160.1
KEYWORDS    RefSeq.
SOURCE      Aliivibrio fischeri (Vibrio fischeri)
  ORGANISM  Aliivibrio fischeri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Aliivibrio.
REFERENCE   1  (residues 1 to 116)
  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 116)
  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   3  (residues 1 to 116)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Aliivibrio fischeri"
                     /db_xref="taxon:668"
     Protein         1..116
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=13805
     Region          17..116
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mpnifnqkky ctlrqnlrnd mpsaekklwf ylrkkqlgvk frrqhgigky vvdffcserk
       61 lvieldgdsh fsieaqkyde irnlfiknlg irvvrftnqd vldncenvll cikkyi
//
LOCUS       WP_005417323             702 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Stenotrophomonas
            maltophilia].
ACCESSION   WP_005417323
VERSION     WP_005417323.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas maltophilia
  ORGANISM  Stenotrophomonas maltophilia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas; Stenotrophomonas
            maltophilia group.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Stenotrophomonas maltophilia"
                     /db_xref="taxon:40324"
     Protein         1..702
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=76752
     Region          19..701
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mslssyrpip sllsltvslg isstaaaapq attldavqvt aadasaqare alkrvpgasn
       61 vidvakadsr lssnadvlay qpgisaqspg negtkvsirg sginrgpgah asgiavsidg
      121 lpltgpggtp yelleplwls rvevlrgang fergalalgg aidyvsrsgr dsagvqlhye
      181 agsrgyqkrg lswggvngdv dyflaytdte fdgyqrhahg dgkgamanig wqitpdlqtr
      241 ffvryretnh etpgrltrdq irndphaana anlaidarrp qpgstwvgnv ttlqidedss
      301 lqaglvyhty pmdlneslyr qqldyanlna tlnyrrrhrl fgldsettvg lrvthdldad
      361 vreslrfasn gytagtrtrd frhhgtdstl hvsntlafnd rlrmqaglal intrrdvqvt
      421 wpssggrlhe qdwdyaprlg ftwqhsaqtq wfgnlsrsve aphpwsmiwg snqyfgpgng
      481 pstgrqrapv pmqnqtattl elgargdaal grweltgyya hvnhellsve lqplpnlfia
      541 ennasptvhr gieagldstl wqaapgrlsl rqaytfsdfr yrhdarfggn rlpglprhay
      601 qaelrfdhas glyaalntey asriavdyan sywadshvif gsrigydapg grwqawaemr
      661 nignrhyaat vtpgyddagk dvarstpgeg rglyagvrwr fe
//
LOCUS       WP_005417781             143 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Aliivibrio fischeri].
ACCESSION   WP_005417781
VERSION     WP_005417781.1
KEYWORDS    RefSeq.
SOURCE      Aliivibrio fischeri (Vibrio fischeri)
  ORGANISM  Aliivibrio fischeri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Aliivibrio.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Aliivibrio fischeri"
                     /db_xref="taxon:668"
     Protein         1..143
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15645
     Region          4..143
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mfdwfnadsa lwvlfssgfl satllpgase asliatlqln sfstwlvvfv atlgntlggi
       61 tnywlglllp dktssqkhgh kaiqwikkyg ywtllfswlp iigdplclaa gwlrlrfwpc
      121 ivligigkaa ryallslavn gil
//
LOCUS       WP_005417945             203 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Aliivibrio fischeri].
ACCESSION   WP_005417945
VERSION     WP_005417945.1
KEYWORDS    RefSeq.
SOURCE      Aliivibrio fischeri (Vibrio fischeri)
  ORGANISM  Aliivibrio fischeri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Aliivibrio.
REFERENCE   1  (residues 1 to 203)
  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 203)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 203)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Aliivibrio fischeri"
                     /db_xref="taxon:668"
     Protein         1..203
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=21568
     Region          1..201
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 meayeteeqq veaikswwke ngkavviggv vgigailgwk yyqssqitak etasaayera
       61 ltalqasgad avestqafid anksneyasl aalqlakvqv eagqlenale qlnwvasnsk
      121 desltamaqv rsariqaeqg nfdaalatla nvkpvswaar vaelkgdial rqgdiatars
      181 aytealqagm nqavqmkldd lae
//
LOCUS       WP_005418214             269 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Aliivibrio fischeri].
ACCESSION   WP_005418214
VERSION     WP_005418214.1
KEYWORDS    RefSeq.
SOURCE      Aliivibrio fischeri (Vibrio fischeri)
  ORGANISM  Aliivibrio fischeri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Aliivibrio.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Aliivibrio fischeri"
                     /db_xref="taxon:668"
     Protein         1..269
                     /product="formate/nitrite transporter family protein"
                     /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=28595
     Region          2..265
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msynkpsefv qtmidvgeak iktssrdlil rgtmagiils lavvvaitti vqtgvgivga
       61 lvfpvgfcil slmgydlvtg vfglaplakf enrkgvswgr vfrcwglvgl gnligsliva
      121 alialsltmn fsvepnavgq kfmavatart vgfenlgmdg witcfvrgil cnlmvclgvi
      181 gnmtarsvag kiaamwlpif iffalvfeha vvnmflfplg mmlgadfgit twlsynlipt
      241 ilgnivggll ftciplylth vktapslda
//
LOCUS       WP_005420048             275 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Stenotrophomonas maltophilia group].
ACCESSION   WP_005420048
VERSION     WP_005420048.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas maltophilia group
  ORGANISM  Stenotrophomonas maltophilia group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Stenotrophomonas maltophilia group"
                     /db_xref="taxon:995085"
     Protein         1..275
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29802
     Region          31..101
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          127..270
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 msatgkalwy iethadrpla ladiaaaagl spfhlsrlfq artgtsvvry lrgrrltaaa
       61 qqlasgagdi lqvalgagyt thaaftrafs eqfgqtperv reqgtdglal vqairmdeap
      121 sacieaprll etpafqvagi gvrhtrdsgg aipgqwaqln rewpmpapis fgvccnsddk
      181 ggfdyiaalp astvpsvpah wqrvdiparr ylvawhsghi sairstwfwl ldhylpasnl
      241 sladapdler ydarfdehtg qggveiwlpv ddrph
//
LOCUS       WP_005420890             140 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Aliivibrio fischeri].
ACCESSION   WP_005420890
VERSION     WP_005420890.1
KEYWORDS    RefSeq.
SOURCE      Aliivibrio fischeri (Vibrio fischeri)
  ORGANISM  Aliivibrio fischeri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Aliivibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Aliivibrio fischeri"
                     /db_xref="taxon:668"
     Protein         1..140
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14366
     Region          1..120
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkkrqgqkgf tlielmivva vigvlsaiai pkyqefakkg avasgiatls alktniedhm
       61 atngsfptts aaigiinssi gtvdldssvs ggikleftdg aangsfvalk ressgewgcs
      121 yygttvteld ipgceytaap
//
LOCUS       WP_005422089             159 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Clostridia].
ACCESSION   WP_005422089
VERSION     WP_005422089.1
KEYWORDS    RefSeq.
SOURCE      Clostridia
  ORGANISM  Clostridia
            Bacteria; Bacillati; Bacillota.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Clostridia"
                     /db_xref="taxon:186801"
     Protein         1..159
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=18235
     Region          49..147
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
ORIGIN      
        1 manedkkdfn amlhdnkdmp kfqiitdqks iekyggskmy fappidydkv mkkipygkvi
       61 tvgkireyfa elsgadftep itagifvsiv awasyqrsed etpywrtlka ngelnakypn
      121 gieaqkekle aeghtiiqkg rknvryyvkd yenslfdlk
//
LOCUS       WP_005422119             349 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Blautia
            obeum].
ACCESSION   WP_005422119
VERSION     WP_005422119.1
KEYWORDS    RefSeq.
SOURCE      Blautia obeum
  ORGANISM  Blautia obeum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Blautia.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Blautia obeum"
                     /db_xref="taxon:40520"
     Protein         1..349
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39976
     Region          1..347
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 maiqvniekn fkgfslksvf esntsatgil gasgsgksmt lrciagietp drgkivingr
       61 tvfdsekkin lkpqerrigy lfqnyalfpt mtvkdnilcg yrgeegqree kardfmkryq
      121 leglenryps qlsggqqqrv alarmmigep eailldepfs aldgylkdvl qkdiqeflkq
      181 yqgdmlmvth srdeafrfcn elmllkdgkt lifgdtrklf eqpqlleaar ltgcknssri
      241 ermgeyqvfa ldwgislrte qkveldmthi airghwirps ekagenclvf eaaeyvettf
      301 ehqylvkspg medgavlwwm rpkksftdeh dknlpkylyl ppehlmllk
//
LOCUS       WP_005422128             373 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Aliivibrio
            fischeri].
ACCESSION   WP_005422128
VERSION     WP_005422128.1
KEYWORDS    RefSeq.
SOURCE      Aliivibrio fischeri (Vibrio fischeri)
  ORGANISM  Aliivibrio fischeri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Aliivibrio.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 373)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 373)
  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 373)
  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 373)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Aliivibrio fischeri"
                     /db_xref="taxon:668"
     Protein         1..373
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42825
     Region          20..97
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(30,49..50,68,71,79..80,90,95)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 msnkikfhnf tllinekkii tksnkeikln svernilsll iqnptviftk eeihnhswck
       61 eikchssvvp qaisllrkkl smhglepiet vkgkgykaah lvqdqsmgmy salvlflsii
      121 silileypvs nlgnekltsf kfkkinnniv ttsasnkfdt sklklednvk yfinnqnnfi
      181 sisacklknn ictnvynaiy fkkestpikm adlisnvkfd ddmdlllvkk dkltslsaei
      241 qlrslnnkky ngelfinfdl ektnnnayfs kkttyikesg ysggfgyasv nkitpiknkn
      301 hhkylikkid ddnllslrfq fgmvknskmt yaynllsgpr ekqsysysyp isknisyyfn
      361 demnisyiay kht
//
LOCUS       WP_005422504             776 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Aliivibrio fischeri].
ACCESSION   WP_005422504
VERSION     WP_005422504.1
KEYWORDS    RefSeq.
SOURCE      Aliivibrio fischeri (Vibrio fischeri)
  ORGANISM  Aliivibrio fischeri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Aliivibrio.
REFERENCE   1  (residues 1 to 776)
  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 776)
  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 776)
  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   4  (residues 1 to 776)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Aliivibrio fischeri"
                     /db_xref="taxon:668"
     Protein         1..776
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=87373
     Region          70..776
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mstsplsykl ayrsaeldde lckstknitp ideivgqdra qqavefamsi pdrgyniyav
       61 gqnglgkrtm vlrylkrhkp vgngmydwcy vtnfddtrrp kvlklpmgtg aefkkeieki
      121 tlklvkaipl afdnelyytr tgtlknqltd qqesllatlt keakgkgvsl avttqgeyqf
      181 ialngeelht eetfealdrq eqrslessid eleiklrslv rqltewedky sakieklned
      241 visqvltvnf eaiktkykes kviiqhlkdm ekdiienfdi fiqegneete layaslekkl
      301 prryqinllv nqdneqfpli veespsyhnl fgyienatyk gtvftdfsli rpgslhkang
      361 gvllmdavkv lerpyvwdgl kralraqnln lsslekevtl sgtvslepep iplnvkiilf
      421 gdhqtyqllq hydsefself kvtadfeddm prtavsefhy aqfissivqd gkllqcdkra
      481 ieriieyssr qsgdqnrlsl hsedisnllk etnyiaraan snmirlkhve qalsnkehrv
      541 nrvqdgvmqs fkngttliqt egsvigqina lsvlstsnhq fgmpnritat tsfgkgevfd
      601 ierkvelggs ihskgvfils aylaslfgkn kaiplktyit feqsyggvdg dsasmaefcs
      661 iisaysdiaa rqdlaitgsm nqfgeaqpig gvnekiegfy evckikglnk nqgviipesn
      721 vqnlmlsaei vqaiekeefs iwpvkhvsea valftgmele nneqtgiydl ikqkla
//
LOCUS       WP_005425502             228 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Blautia].
ACCESSION   WP_005425502
VERSION     WP_005425502.1
KEYWORDS    RefSeq.
SOURCE      Blautia
  ORGANISM  Blautia
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 228)
  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   2  (residues 1 to 228)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Blautia"
                     /db_xref="taxon:572511"
     Protein         1..228
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=23863
     Region          <76..>122
                     /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"
     Region          101..227
                     /region_name="comE"
                     /note="comEA protein; TIGR01259"
                     /db_xref="CDD:213597"
ORIGIN      
        1 mkvnfyslil sifflaglsg msgcqknkte imldgqdtvs esetqddtqa gndatedlae
       61 akisaeaels empvetepem ifvdvcgavm npgvyeldgs srvfqaieaa ggflpeaaas
      121 avnqaqpvsd gqqiyvptqe eaeegalpaa iqpadpgset tdangvvnin tadasalksl
      181 sgigdakaqa iltyreehgf fssieeimqv pgikestfsa ikdkiavk
//
LOCUS       WP_005426648             153 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Vibrio].
ACCESSION   WP_005426648
VERSION     WP_005426648.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..153
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16754
     Region          5..153
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mleafnaafe nlalwfsdsa lwvlfmtgfl satllpggse agliatlsln qysvssiiiv
       61 atigntlggl tnywlglwip nktqdekhah talkwlskyg ywglffswlp vigdplclaa
      121 gwlrmkflpc lvliflgkaa rysllaaiyl glf
//
LOCUS       WP_005426649             658 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Blautia obeum].
ACCESSION   WP_005426649
VERSION     WP_005426649.1
KEYWORDS    RefSeq.
SOURCE      Blautia obeum
  ORGANISM  Blautia obeum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Blautia.
REFERENCE   1  (residues 1 to 658)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Blautia obeum"
                     /db_xref="taxon:40520"
     Protein         1..658
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=74957
     Region          49..489
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mpikyvpfip epvegqavlg nfnrilrykg addvsmtiqr gmplyemekk etvgensdgn
       61 mvirgecvsa caylkeqsiq vdlvyidppf asgadyakkv yirrnpkvae viaraeqeld
      121 vdelrafeek mygdiwdkek ylswmyenlm aiksvmsesa siyvhldyhi ghyvkillde
      181 ifgednfrne iiwkratahs daefygnnfd ciyfytksqt eyvfntvyqp ydesyiarfs
      241 rtdpdgrkwd sgnltakglq gggydyeykg yrslwrmple tmermdregr ihitknggir
      301 skvyldelpg mpaqsmwldv npinsqanek vdyatqkpea lieriisass nendivadff
      361 agsgvtaavs hklnrkfits diglnsiqtt rdrlvsdgse fdvleikdgv qlyrnpvqtm
      421 dkikslipgl knedsldsfw egaisdsklg tipvyvpnlm dsasklldkv tmnriihqai
      481 peldndikka ivyyiditde veimnfiked dsttveielr dlksilddvv igdyaefhae
      541 eiaggyavai dkfmsdrvls kiaefnqkaf lnssakkpyk pieiseegle lieflsldct
      601 atggewhsds eikidkngyv ivegnktkef wdgyirstkk plrlkirnic gdetvwev
//
LOCUS       WP_005427050             282 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein [Vibrio].
ACCESSION   WP_005427050
VERSION     WP_005427050.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            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="formate/nitrite transporter family protein"
                     /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=30090
     Region          5..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mstdykpaef vqtminvgea ktntstrdll lrgtmagiil slavvvaitt mvqtgigivg
       61 alvfpvgfvi lsvmgydlvt gvfglaplak fanrpgitwg rifrcwglvg lgnligsliv
      121 aylvaisltg nfslelnava kkfvavstar slgfenmgmd gwitcfvrgi fcnlmvclgv
      181 ignmtarsvs grvammwfpi fiffalvfeh tvvnmflfpl gmilgadfgi atwlnfnlip
      241 tilgnivggl vmtciplylt haktapsina eeevkaqpam ak
//
LOCUS       WP_005428400             177 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Blautia obeum].
ACCESSION   WP_005428400
VERSION     WP_005428400.1
KEYWORDS    RefSeq.
SOURCE      Blautia obeum
  ORGANISM  Blautia obeum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Blautia.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Blautia obeum"
                     /db_xref="taxon:40520"
     Protein         1..177
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19742
     Region          3..174
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mefqkvletr rtvrkysagv treqmeellr aaqeapswkn sqtgryycvl seemvdkirv
       61 eclpdagnag ksehaaliit tfvhdragfq kdgsadnelg ngwgcydlgl qnenlilkat
      121 dlglstlimg lreadrlrei lhipetetiv sviavgkaae epirphrkpi eeiakff
//
LOCUS       WP_005430541             212 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Sutterella wadsworthensis].
ACCESSION   WP_005430541
VERSION     WP_005430541.1
KEYWORDS    RefSeq.
SOURCE      Sutterella wadsworthensis
  ORGANISM  Sutterella wadsworthensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sutterellaceae; Sutterella.
REFERENCE   1  (residues 1 to 212)
  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 212)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 212)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Sutterella wadsworthensis"
                     /db_xref="taxon:40545"
     Protein         1..212
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22835
     Region          1..208
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 maydleeqes idqmkawwdr wgtpvtsvvc vcclafagwn gwnwwqrnqa akasqiyaal
       61 qnavathdlk nvqslsagli seysstlyap laafasaqsa sdagdladak aklnwvieks
      121 grpeydtvar vrlagvlfde gkldeaaavl aaakpaeaqk vlvldrqgdi waakgdlqka
      181 rdawtqaqaa lnsqdplnrv lelklaalps as
//
LOCUS       WP_005429882             189 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Sutterella wadsworthensis].
ACCESSION   WP_005429882
VERSION     WP_005429882.1
KEYWORDS    RefSeq.
SOURCE      Sutterella wadsworthensis
  ORGANISM  Sutterella wadsworthensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sutterellaceae; Sutterella.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Sutterella wadsworthensis"
                     /db_xref="taxon:40545"
     Protein         1..189
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20274
     Region          18..189
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mttktielpa prklkmtlte alkarktirs fttepisdad lstllwctag itrpdgkrtv
       61 pscldlrtvs vcvlradgaw rwnaskntle lltpedlraa stmgqhafvd tapvtlvfvv
      121 eatprtqmar phwayldagt mveaaylagt alglggvarg svagpelgkr mklpatyepv
      181 fcftcghpa
//
LOCUS       WP_005435697             146 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Sutterella].
ACCESSION   WP_005435697
VERSION     WP_005435697.1
KEYWORDS    RefSeq.
SOURCE      Sutterella
  ORGANISM  Sutterella
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sutterellaceae.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Sutterella"
                     /db_xref="taxon:40544"
     Protein         1..146
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15316
     Region          5..143
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mqdflfewls gagaeaavfa safisstlmp ggseallaga lsqtpddtpr lcrlvllata
       61 gntlgamttw ligrlipere ktdralvwlr rwgapallls wlpvvgdalp laagwlrmpa
      121 ascavwvavg kllryvvvaa gtlslv
//
LOCUS       WP_005435791             434 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Sutterella wadsworthensis].
ACCESSION   WP_005435791
VERSION     WP_005435791.1
KEYWORDS    RefSeq.
SOURCE      Sutterella wadsworthensis
  ORGANISM  Sutterella wadsworthensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sutterellaceae; Sutterella.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Sutterella wadsworthensis"
                     /db_xref="taxon:40545"
     Protein         1..434
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=48088
     Region          5..292
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          288..384
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mpklrifhsa dwhigkelgt idrtddfrvf irdflelvek rrpdvillag difdtsmpan
       61 saqrlyydmi ralsgtsvma tvitagnhds qrfleapral letmncfvag espesqafvl
      121 rddageplla vaavpflreg dvrggsiddt datraarfes gvrkhydtvn gfldealdga
      181 rvpriamghl fvtgsrlrpd ddpttpnesa yvgslrnvta dafgtdwdyv alghihnsqt
      241 vkaqipmrys gspvslsysh ipyrhhivel tfdetggmtf eelpvrqpre fvrvsgtfee
      301 lradiaeaga thekpfveat ltsdecvpdl ageltawgea hgvivtavrn qqaarkyeed
      361 elnapslddl tpesvfksfl eerfetrega ddayrklmpl ldeaveevri etrpaiesad
      421 tpnqekntae evpa
//
LOCUS       WP_005435972             709 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Sutterella wadsworthensis].
ACCESSION   WP_005435972
VERSION     WP_005435972.1
KEYWORDS    RefSeq.
SOURCE      Sutterella wadsworthensis
  ORGANISM  Sutterella wadsworthensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sutterellaceae; Sutterella.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Sutterella wadsworthensis"
                     /db_xref="taxon:40545"
     Protein         1..709
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76487
     Region          4..707
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mnildkimkp rsiavvgast kqhtigsdim krlreygyag pvypvnpkgg vieglpayat
       61 vldipgevdl aviivnarfv lqtidqchek gikglcvisa gfketgtega rleaellerv
      121 rrygmrcvgp nclgvvnthp avrmdacfae alpergnigf vsqsgalggg ilnilrdlnl
      181 gfaqfisign qadvnaetal eywegdkdvr qillymesiq npvnfrrias rlskkkpvla
      241 lkagrsaaga saasshtgsl agadlaadal lrqsgviref slknlfatak vfancpipkg
      301 drvaivtnsg gpgimgtdai cekgmkmael tdetkaklrs flpaaasvrn pvdmiasapi
      361 ehyrqtletv ladpnvdmvi tiylpflglk dtdvaraime ikaahpekpv vgvfmtksef
      421 ftafsaadvn vpffmyveea veglarlneq rlwierpegv lpdfkvdger arniirtala
      481 dgrdqlttre sidvldaygv rvcragfaad edaavavadr igypvvmkmt skttshktdv
      541 ggvrvnigsa ealraeyrdl vakldergll dglegviiqe mvngsremvc giatdpqygp
      601 mlmfglggvf vevmkdvafr iapvtdtdar dmvrsvkayk llqgargttp adiakveetl
      661 lrlsqlvtdl pfideldinp lmisektgep iavdgrikvr rceaesala
//
LOCUS       WP_005435788             270 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Vibrio].
ACCESSION   WP_005435788
VERSION     WP_005435788.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 270)
  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 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   3  (residues 1 to 270)
  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   4  (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   5  (residues 1 to 270)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..270
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30128
     Region          16..268
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <174..268
                     /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 msdsdnpkap pykeimlpkp aelitlpsym dchdhaytqi viglkgqaef evrgqgnlvg
       61 pgqgcivtas sdhafggvih qsdilvlnmp kpanddpeml qkinnlersh lyfqldgqiq
      121 kliqmlvqem rnhpddllls racndtvial mqrhisafet skkesrfdld aidryieqhl
      181 shkisvaqla gsvflgesqf hslfkdqmgi tphqyvlgkr idmardlieq ghltlgqiae
      241 ftgfssqstf thtftrlqgl spsqykkqvg
//
LOCUS       WP_005437541             344 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Saccharomonospora
            azurea].
ACCESSION   WP_005437541
VERSION     WP_005437541.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora azurea
  ORGANISM  Saccharomonospora azurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Saccharomonospora azurea"
                     /db_xref="taxon:40988"
     Protein         1..344
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37428
     Region          32..315
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mlthrfpagg ppsvsaltrr elaaaqvvep plraayarcr elnaqhgrty flatrllpap
       61 rrpavhalyg faryaddlvd gdvgvreaea glaaldaalr paladghsde pvlaaladtv
      121 arygiepdlf trflrsmrmd ltttdyptra alseyvhgsa eviglqllpv lgtvcdpaea
      181 aphaaalgna fqltnflrdv gedldrgrvy lpadelaahg vdrdlllwcr rvghadpkvr
      241 raladqvert rgvyrrawpg ipllrpesrp cvaaaftlys rildviaeag ydvfasravv
      301 gtsrrvalat gtmmrtwagr phrvpplrhr lvvaeaadtt kgwr
//
LOCUS       WP_005437658             329 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Saccharomonospora azurea].
ACCESSION   WP_005437658
VERSION     WP_005437658.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora azurea
  ORGANISM  Saccharomonospora azurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 329)
  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 329)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 329)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 329)
  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   5  (residues 1 to 329)
  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   6  (residues 1 to 329)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Saccharomonospora azurea"
                     /db_xref="taxon:40988"
     Protein         1..329
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35129
     Region          24..>165
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          97..315
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mvgwdfrrsv asvallaafa aergvpaeav lsgtgldtat vrdphaqvea rqelavvrnl
       61 lahcgggpte lgsavgrryh atvygiwgfa vtssrtvgda irlalryvql tyvfcvpelr
      121 lvgdlvalhc radtvpadvr sfllardmaa ittlmedllg vradphprrd titlprdlld
      181 rpmpqandht aamceeqcra llaerstrgg vartvrdrll avdglahgma avaadlgmtt
      241 rtlrrrlaae gtgfralvde vrqtlaeell atrslsveqv aerlgygdaa afvraftrwt
      301 gvtpgryars grvrrgcpas aaggfsgga
//
LOCUS       WP_005438935             313 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Saccharomonospora azurea].
ACCESSION   WP_005438935
VERSION     WP_005438935.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora azurea
  ORGANISM  Saccharomonospora azurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Saccharomonospora azurea"
                     /db_xref="taxon:40988"
     Protein         1..313
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32968
     Region          1..307
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mtaplvllda aslyfrsffa lpesmtapdg tpvnavrgfa dtvarvltdr rparlvacld
       61 adwrpdfrve alpsykahrv aetsddgpda evvpdtltpq vpiilellea vgiavaeaeg
      121 yeaddvigtl aareserpve vvtgdrdlfq lvrhepspvs viyvgkgwak aevlgpeeva
      181 aryvlpvena gaayadmsml rgdpsdglpg vqgigektaa klitrfgsle glliaargah
      241 rdvppktrlr laeaadylaa aplvvrvatd apvtgsaddh vpaapadpdr vaelaerynl
      301 ggsvnrllaa lpg
//
LOCUS       WP_005439832             204 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Saccharomonospora
            azurea].
ACCESSION   WP_005439832
VERSION     WP_005439832.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora azurea
  ORGANISM  Saccharomonospora azurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
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   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   3  (residues 1 to 204)
  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   4  (residues 1 to 204)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 204)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 204)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Saccharomonospora azurea"
                     /db_xref="taxon:40988"
     Protein         1..204
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22189
     Region          15..200
                     /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"
ORIGIN      
        1 mteaateand aapapqrrvl vaedealirl dlvemlreeg yevvgeagdg eeaiklagel
       61 kpdlvildvk mpkldgieaa akitgdriap vviltafsqr dlverareag tmaylvkpfa
      121 krdlvpaiel avsrfaelqa leaevagltd rletrktidr akgllmthqg lsepdafrwi
      181 qrtamdrrtt mkavaeavie nvgk
//
LOCUS       WP_005439926             208 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Saccharomonospora azurea].
ACCESSION   WP_005439926
VERSION     WP_005439926.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora azurea
  ORGANISM  Saccharomonospora azurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Saccharomonospora azurea"
                     /db_xref="taxon:40988"
     Protein         1..208
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=22436
     Region          <110..204
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mrrlaaavag atvlasallt appaaayppt ppdestaran laqltvapdg smdgydrekf
       61 phwspqdgnc ntretvlvrd gsdvvvdnac eptsgswysv ydgvwvgdds dvhidhvvpl
      121 aeawrtgard wsesrreafa ndlgsqqlia vsgssntskg dkapedwkpe ntgywcmyar
      181 swinvkhtyd ltvsdaevta leemldac
//
LOCUS       WP_005440307             204 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Vibrio].
ACCESSION   WP_005440307
VERSION     WP_005440307.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 204)
  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 204)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 204)
  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 11459477
            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="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22099
     Region          1..202
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 melydteeqq veaikdwwke ngkaviigav vglgglfgwr yyqdsviqas eaasqsyttv
       61 mnalqtkgad aqadiqafid snevkeysvl aalqlakvqv dakdlsaale qlkwaqsntk
      121 daalsplisy riarieaemg nfdaanaeld kvtdaawtgr iaeqrgdial rqgdkeaaya
      181 ayteaqqaad asptlqmkld dlak
//
LOCUS       WP_005440732             292 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Vibrio harveyi
            group].
ACCESSION   WP_005440732
VERSION     WP_005440732.1
KEYWORDS    RefSeq.
SOURCE      Vibrio harveyi group
  ORGANISM  Vibrio harveyi group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 292)
  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 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 292)
  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   4  (residues 1 to 292)
  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 292)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Vibrio harveyi group"
                     /db_xref="taxon:717610"
     Protein         1..292
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33730
     Region          <92..288
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          207..286
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mqiptvgfdh kksnqaeiei fdleslhgqe ykshspqkph ritffmmvyi ekgsgvhmvd
       61 fkqypfesgs ilfvrreqvq afdlsnkpsg kviiftqafl dqvhanmrlp nytpthlnqa
      121 rspllsldea tcqsakllig evikeiesqh sdplivmylf ssfalmlhrl rpeerhdklt
      181 keqsyklarf fdllqanyeh irdanwyagq mgstyktlnv icklatnlta kqmidafvti
      241 eikrrlvvsn vttqqlafdf gfedasnfvr yfknqtdmtp sqfqkqyaep ql
//
LOCUS       WP_005440873             387 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Saccharomonospora azurea].
ACCESSION   WP_005440873
VERSION     WP_005440873.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora azurea
  ORGANISM  Saccharomonospora azurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Saccharomonospora azurea"
                     /db_xref="taxon:40988"
     Protein         1..387
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41968
     Region          1..270
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          266..352
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrllhtsdwh vgrtfhgtdl ladqdtvlah laelverlsv dvvvvagdvy dravpsaeav
       61 rvattalrrl reagaelvit pgnhdsaarl gafadfaeag glhlrttida idrpvlleda
      121 hgpvafygip ylepdparla lgvpearght gvlteamrrv redlatrgpg vrsvvlahaf
      181 vtggvgsese rtiavggveq vpgcvfdgmd yvalghlhgp qrladylrys gsplaysfse
      241 ttrksvwvvd lddrglagvd rvelpvprpl atlrgrldel ledpehddlh ecylsvtltd
      301 pvrpveamrr lrarfphavh ldwepeggag aalryseavr grtdleiaen fltdcrgaep
      361 tererallve aleaagradv dpeevlr
//
LOCUS       WP_005441416             367 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Saccharomonospora azurea].
ACCESSION   WP_005441416
VERSION     WP_005441416.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora azurea
  ORGANISM  Saccharomonospora azurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Saccharomonospora azurea"
                     /db_xref="taxon:40988"
     Protein         1..367
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37757
     Region          1..355
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mtlraeltvs raafalslel evpdggvlav lgpngagkst vlsclaglvr aerarvrlge
       61 rvldgdgvhv pphrrgvgll aqtallfphl svldnvafap rsqgaprara rdvarrwlae
      121 veaedladrt ptelsggqaq rvalaralag dpelllldep laaldvdaap avrgllrrvl
      181 rdggrrlttv lvthdpldal tlsdhvavla qgrivergpt revlasprta ftarlvgmnl
      241 vagvavrsga taavrtasgl rffgvpvhdl ddgdaavavf epgavavhpr naevggsprn
      301 vvdavvtave phgpvvrlrt gegisadltp asvadlgldp gtpvrlavka aavslhaavg
      361 tqgvsrg
//
LOCUS       WP_005441752             256 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Saccharomonospora azurea].
ACCESSION   WP_005441752
VERSION     WP_005441752.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora azurea
  ORGANISM  Saccharomonospora azurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Magnet,S., Arbeloa,A., Mainardi,J.L., Hugonnet,J.E., Fourgeaud,M.,
            Dubost,L., Marie,A., Delfosse,V., Mayer,C., Rice,L.B. and Arthur,M.
  TITLE     Specificity of L,D-transpeptidases from gram-positive bacteria
            producing different peptidoglycan chemotypes
  JOURNAL   J Biol Chem 282 (18), 13151-13159 (2007)
   PUBMED   17311917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13395997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Saccharomonospora azurea"
                     /db_xref="taxon:40988"
     Protein         1..256
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=26630
     Region          <90..>127
                     /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          142..256
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(213..214,217,230..233,235)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mvafaaaatl tlltaacgsd aentaeaagg eqqqeqsaan lpeatthgkl pnaptdpdpr
       61 aatdgevlhp treltvhdav dgkaiarlpv qqissptwvp viqregdwaq illptrpnga
      121 sgwidtsgda vesaendfvv nvdldafsle iledgkqige wtvgigssds ptptgrayii
      181 asiaetvndy spivlplsyh sdshetyggg pgtvgihtwp ddsfvgkans dgcirvtqea
      241 ldaltklplg tivniv
//
LOCUS       WP_005442451             333 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio owensii].
ACCESSION   WP_005442451
VERSION     WP_005442451.1
KEYWORDS    RefSeq.
SOURCE      Vibrio owensii
  ORGANISM  Vibrio owensii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 333)
  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   6  (residues 1 to 333)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Vibrio owensii"
                     /db_xref="taxon:696485"
     Protein         1..333
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38032
     Region          31..197
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <249..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mrtvrfiram gilnmnnlal skynlssdel gipasvfhnp mgliplravs ewyrrveers
       61 ndpdvilnls rdielqklgp vgrwlfsgnd lastirrvny gtsnlqsgaf fageqsgkii
      121 kwtyhnpfie tsvkvhdsir caifmikilr eflgedyqpl rvmisgsrkn salykeyfgc
      181 evewsqpkte iwingddrla srqvnhredn rlamsfsdld dllnmpdped elkviyevvn
      241 ysshyglptl ervstllgls eqqfqrrlhk lglnfstvsg yvlsnvaael lskqnsiddi
      301 alrlgytnva sfnrmfkkhr gltpkqyaar lek
//
LOCUS       WP_005445191             662 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Saccharomonospora azurea].
ACCESSION   WP_005445191
VERSION     WP_005445191.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora azurea
  ORGANISM  Saccharomonospora azurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 662)
  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 662)
  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 662)
  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 662)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..662
                     /organism="Saccharomonospora azurea"
                     /db_xref="taxon:40988"
     Protein         1..662
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=68387
     Region          20..635
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 maqdtegtrd apaaspshpt dtqeaqaray dresryrtrl gpwkwvvtvl gtaltlfqly
       61 talfgtftsv iqgavhvgma lslvyllypa kkewagrpgv plydvvlcal allangyivv
      121 dyerlttqav vfgftpfdvv vataaialil eatrrcvglp ivviavaala ygyfgpsmpi
      181 fahpgftfds lvaesvysst svfgtpvqvs stfiflflff gvvlvktnig qffndlafgl
      241 tgrytggtak aavvasglqg mvsgssvant vasgsftipm mkragfrphv agaaeatast
      301 ggqlvppmmg aavfimgeyt gipynelily aivpavlyyl gvfsgvhfea lrtgvlgspk
      361 eqlprlrgll grayllaplv vivglllagr spanaalfgi aaallvslvr adtrlsprrf
      421 aqlfeagara alpviaacas agiiagtvtr tglggklagg ivdlaggsfv lililtmvac
      481 lvlgmglptt anyvvtatva apilvalgvp vvaahffvff fgivaditpp vclaayagag
      541 laganpmrtg ltafklaapa flvpyvfvle pqlllqdptf gvftvtlvta vvgivavaag
      601 lvgfapdagp vlriglvlgg laaihpdpwv slvgfvviaa vvvarrwgrt grggrgpeaa
      661 vg
//
LOCUS       WP_005446338             326 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Vibrio harveyi].
ACCESSION   WP_005446338
VERSION     WP_005446338.1
KEYWORDS    RefSeq.
SOURCE      Vibrio harveyi
  ORGANISM  Vibrio harveyi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Vibrio harveyi"
                     /db_xref="taxon:669"
     Protein         1..326
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35827
     Region          71..143
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
     Region          146..>229
                     /region_name="kgd"
                     /note="multifunctional oxoglutarate
                     decarboxylase/oxoglutarate dehydrogenase thiamine
                     pyrophosphate-binding subunit/dihydrolipoyllysine-residue
                     succinyltransferase subunit; cl39092"
                     /db_xref="CDD:476867"
ORIGIN      
        1 memkkalhss rivqsglslg llvacaqfst pvlaseflcq asqasnkelp vleqscpigk
       61 glwgkkvpqg gndffwiqcg llpkpmslak akpiygkitt dvwmkpeqkg yrcligpyte
      121 fakasqdlqr vktlpiykea firvvgkggt vpakqtkpmt kpvakpvtpv vpaatrantd
      181 afktkdapak vapkspepva akpakmtkpa qptikndnve vrlktvlkgk tfvvpylien
      241 nnqfymehgk pwnrlsysss mkvcqqlgmh latasefkil rdsgvmeknk wplqlpywgk
      301 dkkglfadre pnqltgtsll nvicvk
//
LOCUS       WP_005446580              99 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Vibrio].
ACCESSION   WP_005446580
VERSION     WP_005446580.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 99)
  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   2  (residues 1 to 99)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..99
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10806
     Region          38..97
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkwmltlcll llapmswaee sksantkaak yegieitvnv ntasaqeiat mlkgigekka
       61 kdiveyrneh gpfktvadlt kvkgigdatv kkneerill
//
LOCUS       WP_005446614             516 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Saccharomonospora azurea].
ACCESSION   WP_005446614
VERSION     WP_005446614.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora azurea
  ORGANISM  Saccharomonospora azurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 516)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Saccharomonospora azurea"
                     /db_xref="taxon:40988"
     Protein         1..516
                     /product="amidohydrolase family protein"
                     /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=55047
     Region          39..477
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mngfdrrsfl awlssgvvaa atlgrggsva vaatenagpd sagalllrda tvfdgtgapa
       61 rpgtsivisg drivaigrwn rgeslpdipg lrvvdcsgry vipglwdlht hssdvtptvp
      121 alqlvhgvtg vremrgseat havrrrierg elagprmvva sntldgpdsp vpgatlidtd
      181 ddardaadra sgegadllkv ysflhsdehd aiathaarvg lpfaghspsl lpvqevvrrg
      241 qrsvehnygm hlstsrraee hfehlaalpd dpadpqwwgr raallerevf qtydrgraad
      301 laglfvehga whvptfaves ayarhpsrfl ddeetqelaa rwlpatirqe weamarawpe
      361 wtperaelel ayldarlelv gdlaadgapl gtgtdsgaay vfpglathde lellvragls
      421 parallaatr daarcagqtd agtltagaka dllvldadpl adithtrrih avvargrhhg
      481 paerqrlfdd ieraaqedvp agstrstlgc capttg
//
LOCUS       WP_005446876             202 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Saccharomonospora
            azurea].
ACCESSION   WP_005446876
VERSION     WP_005446876.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora azurea
  ORGANISM  Saccharomonospora azurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Saccharomonospora azurea"
                     /db_xref="taxon:40988"
     Protein         1..202
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21223
     Region          <3..171
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mttleplwdd esvrmndggc drqgrfycgs maydetpgrg slyrldpdgt trtvltgvtv
       61 sngiawnadg dtvyyidspt rrvdafdvdp gtgrfsarrt vvhvaaehgv pdglaldvdg
      121 glwvalwggg avhrytpegv ldevidvgps qvtacafggp dltdlyitts rqgiaqdaqp
      181 tagalfhcrp giaglptaaf ag
//
LOCUS       WP_005446948             282 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein [Vibrio].
ACCESSION   WP_005446948
VERSION     WP_005446948.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            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="formate/nitrite transporter family protein"
                     /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=30028
     Region          5..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mstdfkpaef vqtminvgea ktntstrdll lrgtmagiil slavvvaitt ivqtgvgvvg
       61 alvfpvgfvi lsvmgydlvt gvfglaplak fanrpgitwg rifrcwglvg lgnligsliv
      121 aylvaisltg nfslelnava kkfvavstar slgfenmgmd gwitcfvrgi fcnlmvclgv
      181 ignmtarsvs grvammwfpi fiffalvfeh tvvnmflfpl gmilgadfgi atwlnfnlip
      241 tilgnivggl vmtciplylt haktapsina eeevkaqpam ak
//
LOCUS       WP_005449498             404 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein
            [Saccharomonospora azurea].
ACCESSION   WP_005449498
VERSION     WP_005449498.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora azurea
  ORGANISM  Saccharomonospora azurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 404)
  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 404)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Saccharomonospora azurea"
                     /db_xref="taxon:40988"
     Protein         1..404
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44767
     Region          1..403
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mktvrldvar rtvlaaqgfa dprpgvapdr rhlrrvlsrl hvlqldsvnv avrahyaplf
       61 arlgpydrel vdaaawthsa rrprllvecw aheaslvpve dwpllhsgak prgwwrhygr
      121 iadaepalvd dvlavvkelg plgagaiera lsgptartpg swwersdvkk vcewlfgige
      181 lttgarrgfe rlydlservl ppdvlartvd artaarglve raaraygiat epdlrdyyrl
      241 apevtrqava elveagvler vrvdtwrapa yrhadattpr rvegrallcp fdplvwersr
      301 terlfgfryr ieiyvpeaer vhgyyvfpfl ldgalvarvd lkadraagvl rvpgafaesg
      361 vergrvaael aaelgvmaaw lgldgvsvge rgdlaadlrr avgd
//
LOCUS       WP_005449589             774 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Saccharomonospora azurea].
ACCESSION   WP_005449589
VERSION     WP_005449589.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora azurea
  ORGANISM  Saccharomonospora azurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 774)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 774)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Saccharomonospora azurea"
                     /db_xref="taxon:40988"
     Protein         1..774
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=84436
     Region          23..774
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 maismlpaap glaaaddgrs rsrlhvdgld spvrivvdkw dvphiyaknt adlffaqgyn
       61 aarerlfqmd lwrrkglgql sevfgeayve qdraarlmly rgdmeqewes ygsegklaas
      121 rfaegvnayv drlaekpeel paefrkfsye parwtaedvv rirahglsqn lysevdrari
      181 acvggvdadq frirltpehe amvpegfdpc slpadvldty slavgglsgd gepssaaalq
      241 egsnawalsp hrtttgrpil andphralns pstryvahln apgldvigag epfapgialg
      301 hngtsawglt vsamdqedly yyeldpenpn ryrydggwee mttvteeiav agggsevvel
      361 qytrhgpvik vdeeanraya lraawlepgm spyygslkhl ratsfaefrk smdswrapgl
      421 sqvyanvdge tglavgglap krtgydgllp vpgdgryewd gfvppssmpr vhnpengiia
      481 taneyngtda glgyewaspv rrdriveald araksspads gavqndvhsl yarrlvellq
      541 plssddpvia ealamlqdwd atlskdsdaa vlfevwfmwh lgpnflfsvl ppetagaifl
      601 pdqdvlvdam enpdeyfgad gaaqrdalll stlkaafadv eqrlgtdrse wtwggllttp
      661 fphplseltd ddtaaewnag pvptggawht vnlagydpve yenlsgpslr illdvgnwda
      721 skminapgqs gdpdspgyka mvekwgdgey vpllysaaai krnqaeeivl lpkr
//
LOCUS       WP_005450079             464 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase, partial [Saccharomonospora azurea].
ACCESSION   WP_005450079
VERSION     WP_005450079.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora azurea
  ORGANISM  Saccharomonospora azurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Saccharomonospora azurea"
                     /db_xref="taxon:40988"
     Protein         <1..464
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
     Region          4..464
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 ppcrdlpaga lvrkyghvig vatrdirege hvhthnlamp ehaatlspgd dgvrqtevpa
       61 dlrrtfdgiv rpdgsvatrn yvgvlttvnc satvarrivr rteddiaelg pegvdgvval
      121 thgsgcglas egegwellrr tlvgyarhpn igalvvvglg cevnavsslm aelglaehvp
      181 vasftiqdag gtvdaidrge klvrdlaaql agtrrtevgv ehlvlglkcg gsdawsglta
      241 npalgvagdl llaaggasvl getpeiygaq gllagravrt evadalldrv awwerytreh
      301 gttldgnpsp gnkeggitti lekslgavak sghspltavr dyaepvqrpg ltfmdtpgyd
      361 pvsvtgmiag ganvvcfttg rgsvfgsrpv ptvklatnad varrlagdmd vdcspiveeg
      421 tpvaelgrri ydhvldvasg rrtlseqlgl ggeelvpwqk gavl
//
LOCUS       WP_005451191             329 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Saccharomonospora azurea].
ACCESSION   WP_005451191
VERSION     WP_005451191.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora azurea
  ORGANISM  Saccharomonospora azurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 329)
  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 329)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 329)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 329)
  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   5  (residues 1 to 329)
  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   6  (residues 1 to 329)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Saccharomonospora azurea"
                     /db_xref="taxon:40988"
     Protein         1..329
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35146
     Region          24..>165
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          97..315
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mvgwdfrrsv asvallaafa aergvpaeav lsgtgldtat vrdphgqvea rqelavvrnl
       61 lahcgggqte lgsavgrryh atvygiwgfa vtssrtvgda irlalryvql tyvfcvpelr
      121 lvgdlvalhc radtvpadvr sfllardmaa ittlmedllg vradphprrd titlprdlld
      181 rpmpqandht aamceeqcra llaerstrgg vartvrdrll avdglahgma avaadlgmtt
      241 rtlrrrlaae gtgfralvde vrqtlaeell atrslsveqv aerlgygdaa afvraftrwt
      301 gvtpgryars grvrrgcpas aaggfsgga
//
LOCUS       WP_005451239             265 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Vibrio].
ACCESSION   WP_005451239
VERSION     WP_005451239.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 265)
  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 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   3  (residues 1 to 265)
  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   4  (residues 1 to 265)
  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 265)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..265
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30190
     Region          26..262
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <164..262
                     /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 mehiqyyatd hdnlslieak yqkfafqrhy hldfhlglit hgaqkfqyqg nshqvghgqi
       61 vimppdelhd gqsklesgye vnvfaiephl lsdladlkqn gqiihfneli isdpqifsql
      121 snlhgllrre nlsqltkdcl pfegfnqlfd rygslerqkv vplgnqslgt lkdylmanld
      181 qavrldslse lcqlsptqfq rhfkaqtgmt pyawfarlrl eqgmkllqag qcgtdvahqi
      241 gfydqahfsk afkqtygvsp sqvtr
//
LOCUS       WP_005451618             702 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Vibrio harveyi].
ACCESSION   WP_005451618
VERSION     WP_005451618.1
KEYWORDS    RefSeq.
SOURCE      Vibrio harveyi
  ORGANISM  Vibrio harveyi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 702)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 702)
  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 702)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Vibrio harveyi"
                     /db_xref="taxon:669"
     Protein         1..702
                     /product="M4 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=76059
     Region          58..624
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 metatphsyr vittavllsa myfssfsfaa kperlennhg ylvslekrnq sstqnvgkal
       61 glqkenrvek iqsnqgkngn lhtryqqtyk gipvwgkqiv vhrdqngkik ringtlvkdi
      121 addisnvsps lkageakskv qkqfvidgyq iedqkqalti yvdndnvahl ayevrffads
      181 esahkptrpt flvdahtgkv lhqyeglaha sangpggnlk igeyqygvdy ealnvqqsgs
      241 tcimdingvv ktvnlngrts gsthtftcpt ntvkeingay splndahyfg kvvydmyldw
      301 lgiapltfql emrvhyrkry enafwngssm tfgdgdtyfy plvsldvsah evshgfteqn
      361 snliyseqsg gineafsdia geaaefysrg sndwkvgydi rksangalry mdnppldgrs
      421 ighasdyvsg mdvhyssgvf nkafyllate ygwgtqksfv tfayanqnyw tpdatydsaa
      481 agvlaaaqal gysgtditna faqvgvstng gvveppvttc ditvlvkgvs stvdsastgq
      541 wrcftidvpt gstelnvvts gsdgdadlyv klgsapsetd ydcrsyssns nesctlasps
      601 aatwhigvya yatynnlsvt atyvedeapp ppppetditt sstnngktwt arisgsgllg
      661 gswslggvcn sdtecalsgi pkktssvnft lsdgrvftil kp
//
LOCUS       WP_005451438             391 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Saccharomonospora azurea].
ACCESSION   WP_005451438
VERSION     WP_005451438.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora azurea
  ORGANISM  Saccharomonospora azurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 391)
  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 391)
  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
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 391)
  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   5  (residues 1 to 391)
  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   6  (residues 1 to 391)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 391)
  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 20170230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Saccharomonospora azurea"
                     /db_xref="taxon:40988"
     Protein         1..391
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40097
     Region          <22..>62
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          81..369
                     /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 mshersaptg qealrrirtg avlaalrehg pvsrtelael tgyrpssltm ivrdlmasgh
       61 ivqagtggss ggrrphllef npsaeslval slegeqanad vvdlsgellg gysrrvdpar
      121 plddlvavtt daldahpdpr psrvvfslpg vatekgsvtl spvlralged slatalsers
      181 gipvqvendv nlialgerer gaaadvddlv lihvgygiga avvsggslcr gaagfageig
      241 flptsvppdp htgdrgrfeq rwsvpgisaa lsevnghrtl epvaelaara depavarlrr
      301 nvieawafaa vvcacvtnpa rivfagaapq lgeaglaelg evvrasapsa pevvyaalga
      361 qalnvgavsp sllshaaapt qspqssprkg s
//
LOCUS       WP_005451687             272 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Vibrio harveyi].
ACCESSION   WP_005451687
VERSION     WP_005451687.1
KEYWORDS    RefSeq.
SOURCE      Vibrio harveyi
  ORGANISM  Vibrio harveyi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 272)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Vibrio harveyi"
                     /db_xref="taxon:669"
     Protein         1..272
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=31126
     Region          25..255
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 melkkqsdye qyirqdslge yyvvlnqytf hsvyqpifdk hqnmigmeal lrirgadgan
       61 irpdlffadt sidtyfrlcm eflsraihir nfarhfagsp iklflnvmpq tlltltkdmg
      121 fkdngllykr lhelgmepsd vvfevveesc gdtelliqav qlmrangflf aiddfgshhs
      181 dmsrvkqlcp diikidrsyl ldycsgdtla ianavelaee mnakvviegv eenmqlsamq
      241 alnldyyqgf ylakpnsinh wtkhaqnsev lh
//
LOCUS       WP_005451807             208 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Saccharomonospora azurea].
ACCESSION   WP_005451807
VERSION     WP_005451807.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora azurea
  ORGANISM  Saccharomonospora azurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Saccharomonospora azurea"
                     /db_xref="taxon:40988"
     Protein         1..208
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=22571
     Region          <111..198
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mvlsgcaavd kvagseggat gtatntetgg adgaddartq laelkvapdg gmdgysrdrf
       61 phwsnqgegc ntretvlkrd gdgvkvddkc rptsgswtsp ydgetwtdpa dvdidhvvpl
      121 aeawrsgada wtdeererfa ndldgvnlla vtdnvnqskg dkgpedwqpp lesywctyai
      181 lwidvkhtwe ltveedekat ledmldrc
//
LOCUS       WP_005452823             193 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Vibrio].
ACCESSION   WP_005452823
VERSION     WP_005452823.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            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="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19553
     Region          <8..172
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 msinhthngd sgdnhktdfd ggndifvgfg gndsfvaggg ndyvvggagd drliggagdd
       61 ilkagegndy lgggtgndkl lgllgdnkln ggvgddtlls gsgdnvligg tgadkfiftd
      121 kfgghgeakv vdftigedsl hivsdsvtsy edltftydan gsavftdgad ltvkligvtq
      181 ediesygsdl fii
//
LOCUS       WP_005452854             239 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Saccharomonospora
            cyanea].
ACCESSION   WP_005452854
VERSION     WP_005452854.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora cyanea
  ORGANISM  Saccharomonospora cyanea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (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   2  (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   3  (residues 1 to 239)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Saccharomonospora cyanea"
                     /db_xref="taxon:40989"
     Protein         1..239
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26193
     Region          27..74
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msieainwal ntapipthrr dasslaivlv glanhadpdg rnafpslnrl mrytrlsers
       61 vryalralee lglirrsadq eivaayrkra drrpnnydlv irqpvdnppg egqnlppgdq
      121 hegqtqqarg aksrttrgrd cprtvlnrdk nrpagkraap gtvgpvcgqc dgrdsdpvsa
      181 rvvwldvdrt rsvrcprchp aksvdtddpt ssedftsgge ktadprhesp vgkpqggrr
//
LOCUS       WP_005453298             334 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Saccharomonospora cyanea].
ACCESSION   WP_005453298
VERSION     WP_005453298.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora cyanea
  ORGANISM  Saccharomonospora cyanea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 334)
  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 334)
  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   3  (residues 1 to 334)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Saccharomonospora cyanea"
                     /db_xref="taxon:40989"
     Protein         1..334
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37460
     Region          204..305
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mdvkvrsvsd aagmsatisi ndvfrgsvar ahgyvtaael ggprfrrlfq dvyvpahvpv
       61 thelrcrgaa livpkeavlt grsaatvlgv elanpydpve fvvpevhrfg pikgihvrrt
      121 dvkpqesrpw ngiriarpwr aaldlvlrls prvqswvrrl riavpdldaf vrsgrvtlkq
      181 lrrtwkgrrn rgirlaraal smvdpraesl pesdlrvvlk tggfepvpqy sitrggreva
      241 rldlalkdtk taieydgrwh rsskqirrdk arrkrlvteg wnfvivtaek lagdykrild
      301 evrqaqsrre israsksrrc rvfsarnass ssgg
//
LOCUS       WP_005453303             288 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Vibrio].
ACCESSION   WP_005453303
VERSION     WP_005453303.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 288)
  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 288)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 288)
  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   4  (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   5  (residues 1 to 288)
  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 12820790
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33876
     Region          37..285
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <168..285
                     /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 mahiekvpqr pgfswryrri depkkeydfh fhddvyelvi hrhfsgtlhi ghhelevthn
       61 qmlliapgvp hsihstlven ncethviwfk rewianlmfy ctelrkldpl lkaankgvvf
      121 sertaqqvve llqelmkvpa meqlarfihv lsllahdeaa ktlmthsyls mseheqqere
      181 rvakvsayle qhfarkitla dlandlslse savtrlfkkh fkepfsqrlm klrinhaadl
      241 lqstelpigi vfervgyrnq alfnrhfkty kgltprdyrq hyqqriqp
//
LOCUS       WP_005453323             707 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Vibrio harveyi].
ACCESSION   WP_005453323
VERSION     WP_005453323.1
KEYWORDS    RefSeq.
SOURCE      Vibrio harveyi
  ORGANISM  Vibrio harveyi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 707)
  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 707)
  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 707)
  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 707)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Vibrio harveyi"
                     /db_xref="taxon:669"
     Protein         1..707
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=75844
     Region          1..698
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 msdsiekelq kfelptrtdf pwvtttitvf gvvlsalhiw fntlstlpel wisathfagf
       61 avicalwypa hislkqskia lgidvliamg avacllyipy aedalyergv kfvtsdwvfa
      121 imailiviel irrtmgwfip vlivvclsyv vlwgkwatgi fhfpglsmet llyrsfysse
      181 gmfgsisris wtfvfmfilf gaflvrsgvg dyiinvaraa agkiiggpgf iavigsglmg
      241 svsgssvant vstgvisipl mqkagfpsrf aagveaaast ggqlmppvmg agafimasyt
      301 qipyvdiitv sfipaliyfl svaffvriea krsgvqkitt sdesllkvli sgwhnlipla
      361 vlvtllvqgf tptyaaglsi isvvvaswfs kdhkmgpkai iealsqgakn mattavllvg
      421 iglvinvist tgigntfslm idgwangdlf imivlialas lvlgmglpvt aayivlgtls
      481 apalykliae nqllelmvsg qlpeqakaif mlaapeklel lnapmaleta kemvalvpad
      541 fmetlleqsl gmeavglall aahliifwls qdsnvtppvc ltafaaatia ktppmrtglm
      601 awkiakglyl vplliaytgl vswdvtsvit vgffaiigty aligaiegyl egplniltrl
      661 llvvvgtllv whdipmlvrv ascavfiavf iysgrkfklq qsqlsvl
//
LOCUS       WP_005453818              96 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Saccharomonospora cyanea].
ACCESSION   WP_005453818
VERSION     WP_005453818.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora cyanea
  ORGANISM  Saccharomonospora cyanea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Saccharomonospora cyanea"
                     /db_xref="taxon:40989"
     Protein         1..96
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10535
     Region          1..96
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(5..6,24..25,33,35,37..38,40,43..44,52,57,62)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(24,52..53,55,77)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mneelherir evvasvpegt vatygdvaal agattprlvg rvlaedghdl pwhrilrang
       61 tpaphlareq larlraegvl adgqrvdlrr frwrps
//
LOCUS       WP_005456685             278 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Saccharomonospora
            cyanea].
ACCESSION   WP_005456685
VERSION     WP_005456685.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora cyanea
  ORGANISM  Saccharomonospora cyanea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 278)
  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 278)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Saccharomonospora cyanea"
                     /db_xref="taxon:40989"
     Protein         1..278
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29525
     Region          12..277
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mekeatsvth slrfevncsi lftelpller paavkaagfg gvefwwpfpe avpsdadvdr
       61 fvtavsdagv qlvglnffag dmpggdrglv swpgrsgefr dnvdvvvgig erlgtkgfna
      121 lygnrvdgdp eaqddlaven lafaaeavar iggtvlvepv sgaqryplkt aadaltvidr
      181 vrddtgatnv glladlyhla vngddvdkvi adhthrvahv qladapgrnq pgtgelpldr
      241 qltdleangy sgwvgleykp tgasadgfdw lprerrga
//
LOCUS       WP_005457069             831 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Saccharomonospora
            cyanea].
ACCESSION   WP_005457069
VERSION     WP_005457069.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora cyanea
  ORGANISM  Saccharomonospora cyanea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 831)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 831)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 831)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..831
                     /organism="Saccharomonospora cyanea"
                     /db_xref="taxon:40989"
     Protein         1..831
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=90972
     Region          36..775
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 madriadiwg trtphakdtp wpvrvdlhld eglapsdvda wvqsacvlcs ngcacdiavk
       61 dgrmvgirgr agdvvnhgrl gpkglygswq wnrtdrltrp lvrsdgrlqe tdwdtamsli
      121 vrrsrellde tgplshgfyt sgqlfleeyy tlgvigkagl gtphmdgntr lctataaaal
      181 ketfgsdgqp gsysdiescd alflfghnma etqtvlwarv ldrlhgadpp vvvavdprrt
      241 pvteacaqsg gvhlaplpgt nqalmnglir eiitrgwidh dyvaahtlgy delaatvepy
      301 tpehvaricr idphdvrraa evfgtsdrvl stvlqgfyqs hqataaacqv nnlhllrgll
      361 grpgcgilqm ngqptaqntr eagadgdlpg frnwdnpehi qqlaelwnvd pltiphwapp
      421 thamqiwrya eqgsirflwi satnpavslp elprireila kedlfvvvqd gfltetaeya
      481 dvvlpaalwg ekqgtftnvn rtvhlsekav eppgearsdl difldyarrm dlrdrdgdpl
      541 ikwsdpesaf eawkecsrgr lcdytglsyd rlrggsgipw pcndeypdgc drlyadavfp
      601 thadvcesyg rdlltggtts rseyhalrpe gqallrsaey vsppeqaggd ypfvcttgrt
      661 vyhfhtrtkt grsrrlrraa pepwvelser daaelgvaeg dvvsvesrrg rvelpvrvgr
      721 grdgvvflpf hygywdsgad ghtraanelt ltdwdpvskq plyklsavrv tkladgagpa
      781 paptttasap hdpagvtats gnddvaedva vteppppapt pdrtpnvphh s
//
LOCUS       WP_005457302             369 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Saccharomonospora cyanea].
ACCESSION   WP_005457302
VERSION     WP_005457302.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora cyanea
  ORGANISM  Saccharomonospora cyanea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Saccharomonospora cyanea"
                     /db_xref="taxon:40989"
     Protein         1..369
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=38919
     Region          1..359
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mrvltvnpgs sslklavvdg gvvaaeehva ewdgvtrdel egfaaahppv havsvrvvhg
       61 gdrttptvld egslaelrcq vplapvhqpr sltlarhald lpagvpvvgc fdtafhaglp
      121 ahvatyplpr rwrdryglrr ygfhglslah atrrtaelld rpvrrlrlvc chlgagvsvt
      181 avvggrsldt smgftplega amatrcgsid pgiplyllre hglsvsdvea alnrnsglag
      241 lsgtsgdvre vlrsrargdp earlaldvyl hrlrremaaq avsaaepdav vltggvaehq
      301 pglraelfdg allgarvdpa rnratgdrli saessrtavv lvtcreenel arlceetlsv
      361 gptgapaps
//
LOCUS       WP_005457777             744 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Vibrio parahaemolyticus].
ACCESSION   WP_005457777
VERSION     WP_005457777.1
KEYWORDS    RefSeq.
SOURCE      Vibrio parahaemolyticus
  ORGANISM  Vibrio parahaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 744)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 744)
  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   3  (residues 1 to 744)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Vibrio parahaemolyticus"
                     /db_xref="taxon:670"
     Protein         1..744
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79012
     Region          6..743
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          92..>356
                     /region_name="DamX"
                     /note="Cell division protein DamX, binds to the septal
                     ring, contains C-terminal SPOR domain [Cell cycle control,
                     cell division, chromosome partitioning]; COG3266"
                     /db_xref="CDD:442497"
ORIGIN      
        1 msydldedil qdflieagei lellseqlve lennpedkdl lnaifrgfht vkggagflsl
       61 aelvdtchga envfdvlrng qrsvtpslmd tmlkaldtvn tqfqavqdre aleaadpall
      121 delhrlckpe sedevatvve epivtpepvi pepanevpaa paaditeags igsvdeitqd
      181 efeklldelh gkgaapgast saptaaapvq asapvldngd itddeferll delhgvgqsp
      241 saataapvet pkapepaapa vsaasgdsdl mtdeefekll delhgagkgp tleeldmatk
      301 pasalapeap kpapvaqpap vstpasapkp aakpvavkee pkasapavkk pqaeatvrvd
      361 tstldtimnm vgelvlvrnr llslglnsdn eemskavanl dvvtadlqga vmktrmqpik
      421 kvfgrfprvv rdlarnlnkd ivlemrgeet dldknlveal adplihlvrn svdhgiempe
      481 drvkagksrt gkvilsasqe gdhielaivd dgggmdpnkl rgiavkrgmm dedaaarlsd
      541 kecfnlifap gfsskekisd isgrgvgmdv vktaintlng sididselgk gtkitikvpl
      601 tlailptlmv gvgghpfalp lasvneifhl dlsrtnvvdg qltiivrdks iplfylqnwl
      661 asksprveqr ighghvvivq igsqrvgfvv dtligqeevv ikpldnllqg tpgmagatit
      721 sdghialild vpdllkqyaa asri
//
LOCUS       WP_005458767             241 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Saccharomonospora cyanea].
ACCESSION   WP_005458767
VERSION     WP_005458767.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora cyanea
  ORGANISM  Saccharomonospora cyanea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Saccharomonospora cyanea"
                     /db_xref="taxon:40989"
     Protein         1..241
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27119
     Region          11..229
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mtsapfdvle tdrlltttrs vrrrldferp vprevieeal evavqaptan nqqnwrwvvi
       61 tetsvkeqla elfdiswrfh qkevwtasgr rrnsrqaqrn ndsaaqlard iarvpvlvvp
      121 cvlgrppdig aidtewlrsr addaatardd vrigamrasi fygsifpavw sfqlalrsrg
      181 lgstitcmhl pferrvgell gipagvtqvc mvpvaytvgt dfapakrypa ksrtswerwq
      241 a
//
LOCUS       WP_005459892             253 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Saccharomonospora cyanea].
ACCESSION   WP_005459892
VERSION     WP_005459892.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora cyanea
  ORGANISM  Saccharomonospora cyanea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Magnet,S., Arbeloa,A., Mainardi,J.L., Hugonnet,J.E., Fourgeaud,M.,
            Dubost,L., Marie,A., Delfosse,V., Mayer,C., Rice,L.B. and Arthur,M.
  TITLE     Specificity of L,D-transpeptidases from gram-positive bacteria
            producing different peptidoglycan chemotypes
  JOURNAL   J Biol Chem 282 (18), 13151-13159 (2007)
   PUBMED   17311917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13395997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Saccharomonospora cyanea"
                     /db_xref="taxon:40989"
     Protein         1..253
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=26290
     Region          <87..>124
                     /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          139..253
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(210..211,214,227..230,232)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mlalaaaatl alltsacggg dadnaaeaas geqqaaslpe attygeipna pkdpepnapt
       61 egevlhptre ltvhdavdgn piarlpvkqi ssptwvpvik regdwaqill ptrpngatgw
      121 intsggaves aendylvnvd lksfsleilk dgeqigkwtv gigepdsptp pgrayiiasi
      181 eetvndyspi vlplsyhsns hetygggpgt vgihtwpdds fvgkansdgc irvtkdalda
      241 lvklplgtiv niv
//
LOCUS       WP_005459562             103 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Saccharomonospora cyanea].
ACCESSION   WP_005459562
VERSION     WP_005459562.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora cyanea
  ORGANISM  Saccharomonospora cyanea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 103)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Saccharomonospora cyanea"
                     /db_xref="taxon:40989"
     Protein         1..103
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=10645
     Region          22..103
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mstagtdgvi etsqgadqht ltvrvryfas araaagvdse lvrlspsasv adavehlrta
       61 hperlprvld aasflldgia vrdldrplpd gaeldvlppf agg
//
LOCUS       WP_005458575             265 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Vibrio].
ACCESSION   WP_005458575
VERSION     WP_005458575.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 265)
  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 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   3  (residues 1 to 265)
  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   4  (residues 1 to 265)
  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 265)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..265
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30347
     Region          26..262
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <173..262
                     /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 meqiqyyatd hdqlslieak yqkfafqrhy hldfhlglit hgeqkfhyqg shhqvghgqi
       61 vimppdelhd gqsklasgyq vnvfsiephl lsdladlkqn gqiirfneli isdpqifsql
      121 snlhallrre nlsqltkdcl pfegfnqlfd rygslarqkv iplgkqslnt lkdylmanld
      181 qsvrleslse lcqlsptqfq rhfkaqtgmt pyawfarlrl eqgmkllqag qcgtevahqi
      241 gfydqahfsk afkqtygvsp sqvtr
//
LOCUS       WP_005461813              96 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Saccharomonospora glauca].
ACCESSION   WP_005461813
VERSION     WP_005461813.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora glauca
  ORGANISM  Saccharomonospora glauca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Saccharomonospora glauca"
                     /db_xref="taxon:40990"
     Protein         1..96
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10534
     Region          1..95
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(5..6,24..25,33,37..38,40,43..44,52,57,62)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(24,52..53,55,77)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mneelherir evvasvpegt vatygdvaal agastprlvg rvlaedghdl pwhrilradg
       61 tpaphlareq larlraegvl adgrridlrk frwkpl
//
LOCUS       WP_005462564             153 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Vibrio].
ACCESSION   WP_005462564
VERSION     WP_005462564.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..153
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16743
     Region          5..153
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mldafnsafe hlalwfsdsa lwvlfltgfl satllpggse agliatlsln qyavssillv
       61 atigntlggl tnywlglwip nktqeekhgh talkwlakyg ywglffswlp iigdplclaa
      121 gwlrmkflpc viliflgkaa rysllaaiyl glf
//
LOCUS       WP_005463706             341 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Saccharomonospora
            glauca].
ACCESSION   WP_005463706
VERSION     WP_005463706.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora glauca
  ORGANISM  Saccharomonospora glauca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Saccharomonospora glauca"
                     /db_xref="taxon:40990"
     Protein         1..341
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37403
     Region          32..315
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mtvatvlahh dgaprgvvhr elaaahvtep plraayahcr elnarhgrty flatrllpap
       61 rrpavhalyg farhaddivd gdlppdeaaa rlssldtalr talterrsde pvlaaltdtv
      121 trydidpdlf trflrsmrmd lttssyptra aleeyvhgsa eviglqllpv lgtvsapeea
      181 aphaaalgsa fqltnflrdv aedldrgrvy lpadelaayg vdrdlltwcr tvgyaeprvr
      241 raiadqvert rrvyrrawpg iallrpesrp cvataftlys rildviaetg ydvfagravv
      301 starrvalat gtvvrtrvgp prrsaplrrh vrlaptakeg n
//
LOCUS       WP_005463763             454 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein [Vibrio
            parahaemolyticus].
ACCESSION   WP_005463763
VERSION     WP_005463763.1
KEYWORDS    RefSeq.
SOURCE      Vibrio parahaemolyticus
  ORGANISM  Vibrio parahaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 454)
  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 454)
  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 454)
  AUTHORS   ter Beek,J., 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 454)
  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 454)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Vibrio parahaemolyticus"
                     /db_xref="taxon:670"
     Protein         1..454
                     /product="CmpA/NrtA family 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=50530
     Region          27..308
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mkwssmlkvs aislsvittv sakaelgepe iedlkfgfik ltdmaplava yeqgffedeg
       61 lyvtleaqan wkvlldrvid geldgahmla gqplgatigi gtkaevitaf smdlngnait
      121 vsndtweqmk phipkqpdgk pvhpikadsl kpvvdsyrdk gksfnmgmvf pvsthnyelr
      181 ywlaaggihp gfyapdsgdn sgqldadvll svtpppqmpa tmeagtikgy cvgepwnqqa
      241 vfkgigtpvv tdyeiwknnp ekvfgvskaw aeknpnthir vvkaliraah wldensnanr
      301 qeavkmlaks eyvgadadvi ansmtgtfey ekgdkrdvpd fnvffrhnat ypyysdaiwy
      361 ltqmrrwgqi sseksddwym dvakevyrpd iyqqaaqali edgvlskkdf pdfsaedgfr
      421 ppqthfidni vydgrepnky lekfsiglkg kdkv
//
LOCUS       WP_005464816             827 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Saccharomonospora
            glauca].
ACCESSION   WP_005464816
VERSION     WP_005464816.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora glauca
  ORGANISM  Saccharomonospora glauca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 827)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 827)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 827)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..827
                     /organism="Saccharomonospora glauca"
                     /db_xref="taxon:40990"
     Protein         1..827
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=90874
     Region          36..775
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 madriadlwg trtpyakdts wpvrvdrhld eglapsdvdt wvrsacvlcs ngcacdiavk
       61 dgrmvgirgr agdvvnhgrl gpkglygsrq whrtdrltrp lvrrdgrlre tdwdtamdlv
      121 vrrsrellae tgplshgfyt sgqlfleeyy tlsvigkagl gtphmdgntr lctataaaal
      181 kesfgsdgqp gsysdidsce alflfghnma etqtvlwarv ldrlhgadpp vvvavdprrt
      241 pvteacarsg gvhlaplpgt nqalmngllr evitrgwvdh dyvtahtlgy delavtvqpy
      301 tpehvaricr vdpddlrraa eifgtsgrvl stvlqgfyqs hqataaacqv nnlhllrgll
      361 gkpgcgvlqm ngqptaqntr etgadgdlpg frnwdnpehv rqlaelwnvd patiphwapp
      421 thamqiwrya eqgsirflwi satnpavslp qlprvreila kddlfvvvqd gfrtetteya
      481 dvvlpaalwg ekqgtftnad rtvhlsdkav eppgearsdl eifcdyarrm dlrdrdgapl
      541 itwndpesaf eawkecsrgr pcdytglsye klrggsgvpw pcndeypngr drlyadavfp
      601 thadvcesyg rdlltggits reeyharnpd gravlraaey vpppeepdge yplvcttgrt
      661 vyhfhtrtkt grsrqlrraa pkpwiemsrn daaalglteg dpvrvesrrg rvelpvrvgg
      721 grdgvvflpf hygywdsdtd draraanelt ltawdpvskq plyklgavrv tkladgkgpa
      781 papttaasap hdpagvpatt gdddvwedva atrpppapps pdvphhs
//
LOCUS       WP_005465016             423 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Saccharomonospora glauca].
ACCESSION   WP_005465016
VERSION     WP_005465016.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora glauca
  ORGANISM  Saccharomonospora glauca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 423)
  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 423)
  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
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 423)
  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   5  (residues 1 to 423)
  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   6  (residues 1 to 423)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 423)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 423)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Saccharomonospora glauca"
                     /db_xref="taxon:40990"
     Protein         1..423
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44122
     Region          18..67
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          87..385
                     /region_name="ASKHA_ATPase_ROK_BsXylR-like"
                     /note="ATPase-like domain of Bacillus subtilis xylose
                     repressor (XylR) and similar proteins; cd24076"
                     /db_xref="CDD:466926"
ORIGIN      
        1 mtdsgpagqh tvrrhncalv ldaiasspgv sraevaartg ltkatvstlv drlvtaslvr
       61 eegrqhrsgp grrgtslsls pdgpcglgve igvdylatcv vgltgevhae hvrrfdnrdr
      121 ppsrvlaraa reldraladt arrrltvggv gvavpglvet ssgrvidapn lgwqdvdlat
      181 dlrehlptlp gdlmignean laavaeleal rhrdedtpds fvyvsaeigi gagivldgal
      241 fdgshglgge lghfpvqprg prcscgargc lerlagqdai leragaadvd tlvtrldaae
      301 rpaitavrsa grmlgsalsa vvnlldvtti vlggtyarlh pwlvdpltae ltdrlmgspw
      361 rsvevrrsvl gaeaavrgaa tsalrtvltd pdtyiarrvq aedrttnsvg sridggsgss
      421 pas
//
LOCUS       WP_005466138             387 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Saccharomonospora glauca].
ACCESSION   WP_005466138
VERSION     WP_005466138.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora glauca
  ORGANISM  Saccharomonospora glauca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Saccharomonospora glauca"
                     /db_xref="taxon:40990"
     Protein         1..387
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42197
     Region          1..270
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          266..353
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrllhtsdwh vgrtfhgadl ladqdavlah laelverlsv dvvlvagdvy dravpsaeav
       61 rvatvalrrl rragaelvit sgnhdsaarl gafadfaeag glhlrttiea idrpvllrde
      121 ygpvalygip ylepdparla lglkdarght avlgeamrrv rkdlserspe trsvvlahaf
      181 vtggvssese rtiavggveq vpgsvfdgvd yvalghlhgp qrlaehlrys gsplaysfse
      241 tapksvwivd ldehglaavd rvelpvprrl atlrgrldel ledpaheevr eyylsvtltd
      301 pvrpvdamrr lrgrfpyavh ldwepeggas galryslavr grtdieiven fladcrgsep
      361 sererellva aleaagrana dhrevvr
//
LOCUS       WP_005466438             369 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Saccharomonospora glauca].
ACCESSION   WP_005466438
VERSION     WP_005466438.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora glauca
  ORGANISM  Saccharomonospora glauca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Saccharomonospora glauca"
                     /db_xref="taxon:40990"
     Protein         1..369
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38169
     Region          1..353
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mtlhaelvlr raefalsvsl dvpdggvlav lgpngagkst vlaclaglvr aqrayvtlge
       61 rvldddavhv pahrrgvgll eqrallfphl svldnvafsp rargvpkaea rdvarrwlae
      121 vdasdladrt paalsggqaq rvaiaralag epdlllldep laaldvdaap avrgvlrrvl
      181 rdggrklttv lvthdpldal tlsdhvavla dghivergpt revlasprta faarlagvnl
      241 vagvaertga gaavrtesgl lfhgmpardl adgdaavavf dpgavavhpr daavvgsprn
      301 vvdavvtale phgpvvrvrt reglsadltp asvadlalep gtpvrlavka aavsvhaapr
      361 tpnegrrrq
//
LOCUS       WP_005466932             227 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Saccharomonospora glauca].
ACCESSION   WP_005466932
VERSION     WP_005466932.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora glauca
  ORGANISM  Saccharomonospora glauca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Saccharomonospora glauca"
                     /db_xref="taxon:40990"
     Protein         1..227
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=24781
     Region          <130..223
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mtssntlrvi sitagvlllg gcsavrsgae aggeaastap kqstisqsas adeekarkql
       61 aelvvapdgs mdgydrdrfp hwsnqgnscn trevvlqrdg tdvkvdekcr pisgswtspy
      121 dgetwtdpad ldidhvvpla eawrsgaalw tdeereqfan dldgvnllav tdnvnqakgd
      181 kapedwkppl esywctyaih widvkhtwel tveedevaal eemldrc
//
LOCUS       WP_005467619             752 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Porphyromonas catoniae].
ACCESSION   WP_005467619
VERSION     WP_005467619.1
KEYWORDS    RefSeq.
SOURCE      Porphyromonas catoniae
  ORGANISM  Porphyromonas catoniae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Porphyromonadaceae; Porphyromonas.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Porphyromonas catoniae"
                     /db_xref="taxon:41976"
     Protein         1..752
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=84375
     Region          41..752
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 myhtagrlal alsisllgle amaqtsatds isesrdsvrh isevvvyarq mlgskfearn
       61 rtgsayylsp kelakfgytd isrilravpg vniyeedgyg lrpnislrgt kaerserisl
      121 medgilaapa pyaapaayyf pnaarmyaie vlkgssqvqy gpfttggavn mvstpipktf
      181 haglrssygs ygtfnsyvhv gndhkhigyl ieylryqskg fkkdepnert gfyrndvvgk
      241 lrlhsdegae trqalelklg fanehsdesy vglseqdfas rpyyryrgaq mdhlrtrhvq
      301 talthlidft ggmkvttsvy yhyfwrnwyk lndvrvgdqk gekrtieevl adpetnaryl
      361 diltgatdrl gealmlranq rsyhsrgiqt kveyrlpfls sylqleagar yhadledrfq
      421 hddsysiegg kmslfraglp gsqsnritta hafasyllgk wtragwtita glrledvely
      481 krdyttqdpr rtghlriegs nhatallpsl ginyrilrpl sifagvhqgf appsvmtyyk
      541 qkpeksinle aglrlttedl kveaigyynd ysnmlgsdla aaggqgtldq ftvgaarvqg
      601 feflaswqpl pkswevrlpv qvsytltdtq iknefyssaw gevfagdelp yifrhavnaq
      661 lgleykwlea nlsirynsdm rttpgqvria kahlipshti idaslkarin ryltlslnav
      721 nlankvylvs rhpsglrpgh pfgiyggvri nl
//
LOCUS       WP_005469152             385 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Vibrio sp. 16].
ACCESSION   WP_005469152
VERSION     WP_005469152.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. 16
  ORGANISM  Vibrio sp. 16
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 385)
  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 385)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Vibrio sp. 16"
                     /db_xref="taxon:391586"
     Protein         1..385
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44044
     Region          1..374
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mqsltlaqaq klallsqglp tagvkgssya ktlntfeqlg yiqidtisvv qrahhhtlws
       61 rnpsyhpkhl dqlvadrhvf eywshaaayl pmsnyryslp rkvaiksgqq rhwyckdrdl
      121 mknvlariea egplmakdfe skahktdgwh tkptkqalen lymqgdlmia errgfhkvyd
      181 ltqrvlpqni dtsmptpqeh grflvlsylk ahgfgtiqem vyqlkdvkts vtqaigelve
      241 mgeiepimvn hqpyyacvks lnllgkrlnr kqarilspfd nlliqrkras aifnfdylie
      301 cyvpqakrqf gyfslpilwd gklvaradck vdkksatlnv lhlslepgli ntddfmpale
      361 kelqafarfn qceqfhivkq sinvg
//
LOCUS       WP_005469597             331 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Vibrio sp. 16].
ACCESSION   WP_005469597
VERSION     WP_005469597.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. 16
  ORGANISM  Vibrio sp. 16
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 331)
  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   2  (residues 1 to 331)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Vibrio sp. 16"
                     /db_xref="taxon:391586"
     Protein         1..331
                     /product="aminoglycoside 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=37928
     Region          42..259
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mgafksmmek gryqaivkql gfntlhrvdv lqslwggyge lvrlwidsts vvvkhitlpk
       61 pehhprgwnt elshkrklhs yqvemnfyqr vasqcegyat vpqtllveqg dnelllvmed
      121 lsqigfsqvi qeaskthlra alrwfahfha qhmssradgl wptgtywhld trpdefaals
      181 dlrlkhaaek idrtlkfapy stlvhgdgkl anfcfdpsge raaavdfqyv gngcamkdia
      241 lfmssavppe eceameawil deyftqlria lsqyrpelds kdveqklrpm fmvawadfqr
      301 fvkgwspnhw kinaytenlt lralkfieqs s
//
LOCUS       WP_005471359             376 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: exonuclease SbcCD subunit D [Vibrio].
ACCESSION   WP_005471359
VERSION     WP_005471359.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..376
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42344
     Region          1..269
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          266..352
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkflhtsdwh lgrqfhnvsl lddqvvvlnq ivdyikqnpv dalvvagdiy drsvpptaai
       61 evmnrfvnqv cgelnlpiil ipgnhdgaqr lgfgsgrmks aglhilsdfe qmltpvvies
      121 eigpvafygm pysdpeqvrh hfkqsvsthd eahqlltqqi cqqfqpshkn vlishcfvdg
      181 aiesdserpl siggsdrvsh ehftsfdyva lghlhqpqkk geeyirysgs lmkysfseqh
      241 qrkgmtlvel desgfkqsth idltaphemr ilegemeell sagqtdpkfd dyllvrlldk
      301 hailnpmdkl ravypnvlhl ekpgmlvgve qqmakaklar semdmfrdfy leaqdsalsd
      361 eqesalsgii kqltkq
//
LOCUS       WP_005471584             338 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Enterococcus].
ACCESSION   WP_005471584
VERSION     WP_005471584.1
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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..338
                     /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=39262
     Region          6..274
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mshsprtayf dnakfllmil vvfshllqpf igdhkfyhdl yyfiftfhmp afvflagyfa
       61 kpltkgskvr dlvkkfllpy vffqlfytvy ywvigldasl niqllnpqwa lwfllsmffw
      121 qlslvffqkm tarkaillsv llsifagylp finqvltlqr tfvflpffii gfyfpknemq
      181 flqgtrikki slvflpiiyl fialfhgmnk ymvfgskpye dylsyplfgg plrgvffvig
      241 llgiigflrl vprqqlfftk wgkntllvyl lqgifikglr alaitelnls llgfmalivv
      301 svlltillas rpvrqfyarf eegisfvllg lgifmian
//
LOCUS       WP_005471535             320 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_005471535
VERSION     WP_005471535.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (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   2  (residues 1 to 320)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 320)
  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   4  (residues 1 to 320)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            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="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=36278
     Region          5..312
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mepiiefkqv vkefegqvvl keldlsihqg eifvlvgpsg sgkttslkmi nglieptegn
       61 vyfkqkrvkd yqlqklrwki gyvlqqialf ptmsvkenie iipemlgwdk nrrnqrvdel
      121 ltevglepet fkkrmpaels ggqsqrigil ralaaepdii lmdepfsald pisrtnlqdl
      181 vldlhnklgn tivfvthnmn ealklgdrig vmnegrlvqc dtpekirtep ktdfvraffd
      241 etqgaqqeqr lqaiidsgyy qqsttqegms ldvkvplsqv yevlanhehl vvteqgqaig
      301 evsrtdifhf lsqeeqdekl
//
LOCUS       WP_005472145             182 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit [Vibrio].
ACCESSION   WP_005472145
VERSION     WP_005472145.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 182)
  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 182)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 182)
  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   4  (residues 1 to 182)
  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   5  (residues 1 to 182)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..182
                     /product="TRAP transporter small permease subunit"
                     /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=20539
     Region          4..169
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mrsliyiera fnrfgdflgw lssilfilll anvvydvvmr yvfndvsiaf qemewhlfsa
       61 vfllgvpyai kagghvrvdl fyerlsnkaq aiidvlgtlf flfpfcllva yygidfakes
      121 yalgetsgdp gglpyrwiik amiplsfffm avsgvglllh sinkivnphl lyqasqnqks
      181 es
//
LOCUS       WP_005473816             282 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Vibrio sp. 16].
ACCESSION   WP_005473816
VERSION     WP_005473816.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. 16
  ORGANISM  Vibrio sp. 16
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Vibrio sp. 16"
                     /db_xref="taxon:391586"
     Protein         1..282
                     /product="formate/nitrite transporter family protein"
                     /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=30108
     Region          5..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mstdfkpaef vqtminigea ktktsardll lrgtmagiil slavvvaitt ivqtgvgvvg
       61 alvfpvgfvi lsvmgydlvt gvfglaplak fegrpgitwn rifrcwglvg lgnligsliv
      121 aylvaisltg nfslelnava kkfiavstar slgfenmgmd gwitcfvrgi fcnlmvclgv
      181 ignmtartva grvammwfpi fiffalvfeh tvvnmflfpl gmilgadfgi atwlnfnlip
      241 tilgnivggl imtciplylt haktapslsd eenvnakpvl ak
//
LOCUS       WP_005475477             153 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Vibrio sp. 16].
ACCESSION   WP_005475477
VERSION     WP_005475477.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. 16
  ORGANISM  Vibrio sp. 16
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Vibrio sp. 16"
                     /db_xref="taxon:391586"
     Protein         1..153
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17215
     Region          9..153
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mleafnasfq sialwfsdsa lwvlfitgfl satllpggse agllaalsln qfstfsiilv
       61 atlgntlggl tnywigwwlp nrtqnekhgh kalqwlskyg ywslffswlp iigdplclaa
      121 gwlrmrfwpc fwlvligkaf rysllaaiyf gff
//
LOCUS       WP_005475654             133 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Vibrio].
ACCESSION   WP_005475654
VERSION     WP_005475654.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..133
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=13083
     Region          1..>92
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkqtnnrkak gftlielmiv vavigvlaai aipqyqkyve kgalgsalat atalktnyed
       61 ylavsgaapa svsdigavsf algtvsldas gaievgitsg ggsgssvkla rsvdgswdct
      121 isasagvkin gcg
//
LOCUS       WP_005476145             403 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Streptomyces].
ACCESSION   WP_005476145
VERSION     WP_005476145.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 403)
  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 403)
  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
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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   5  (residues 1 to 403)
  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   6  (residues 1 to 403)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 403)
  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 18624027
            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="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41470
     Region          1..>61
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          81..392
                     /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 mavtagtpgt psvlrtmndr aaldlllehg plsrtrigkl tglskptasq llarleasgl
       61 vlatstsegr pgpsaqlyev npaaayaagl dvtpervraa vadvtgrtvg syefpttgrr
      121 laqpvvqqvt aaldgavkaa glarddvhrl vigtpgafdp nngrlryash ppgwhsptll
      181 ddlaaalpmp vgyendvnlv avaeqrlgaa rghgdfvllw negglgaalv lggrlhrgwt
      241 ggagevgflp vpgtplvrqv skagsggyqe lagsqaipkl ardlgvqdip sgpyaevaaa
      301 lvaraaeadd gphrrllety athlatglas lvsvldpelv vlsgasltsg geplralvqa
      361 eleelaapqp rlvvggvreh pvlrgalesa lsatrdevfd tsr
//
LOCUS       WP_005477176             186 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease family protein [Streptomyces].
ACCESSION   WP_005477176
VERSION     WP_005477176.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..186
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=20678
     Region          <57..171
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mhdrrhqvlt irdedrtgye rtkfrhrida drdgchtrse vlieeavtap eqgvncalsg
       61 giwyspydsi tfdqaraldi dhlvplaesw dsgasswtag erqayandld dpraliavsa
      121 ssnrskadqd pttwqppaeg yrctyatdwt aiktrwalav dpaeqatltd vldscpeavi
      181 evtrar
//
LOCUS       WP_005478132             786 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Vibrio parahaemolyticus].
ACCESSION   WP_005478132
VERSION     WP_005478132.1
KEYWORDS    RefSeq.
SOURCE      Vibrio parahaemolyticus
  ORGANISM  Vibrio parahaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 786)
  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 786)
  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 786)
  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   4  (residues 1 to 786)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..786
                     /organism="Vibrio parahaemolyticus"
                     /db_xref="taxon:670"
     Protein         1..786
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=87971
     Region          70..786
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mailrlepqq lysvadlenm pckstkelpp ideivgqera qkavefamsi kekgyniyai
       61 gqnglgkrtm ilrylnrhqh dadalfdwcy vanfedtrtp kvlklpcgig nklrvdieal
      121 mgkllnalpl afdnemyfsr adrlknqlan kqqneldris reakehgisl titsqgdyqf
      181 vamngdelht eesfdalskk eqeqfsdsid alevslrsmv reltewedty sdkikklnde
      241 vtldvithfi kklkvdysey seiktyltel qkdivenadi fldqsgeqge iaaasldkkl
      301 prrykvnvlv srnnsdfpiv veenpnyhsl fgsietatfk gtvftdfsli ragslhkang
      361 gvllmdaqkv leqpyvwdgl kralrarqls ftslekevtl tgavsldpep ipldikiilf
      421 gdyrtyqllq hydpefself rvtadfedem krtpeselhy arfissvvhd nnmlhcdrka
      481 iariieyssr lsgdqsklsl hsanianllr esnyvarqan snmirighve eamknqemrv
      541 srlrdsvmet flngttlilt egsaigqvna lsvlstsdym fgapnritat tcygdgdvid
      601 iersvdlggs ihskgvmils aylssvfgkt arvpltttit feqsyggvdg dsasmaefca
      661 vvsafskqpn rqdiaitgsm nqfgeaqpig gvnekiegfy dvcvikgrhs gqgviiprsn
      721 vhnlmlradi vkavekgefh iwaidhvtea ielftgkvag eptdegsypi dtifglaqak
      781 lnslrk
//
LOCUS       WP_005478569             920 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase [Streptomyces].
ACCESSION   WP_005478569
VERSION     WP_005478569.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 920)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..920
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..920
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=102114
     Region          144..551
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 maaprrgnvk iaanrtkavq airhedtrvn nptadaidlv teeveqsktl lyprdpsldp
       61 qlvwkgkdeq drqdleipap pifrqeriep rylvkqlmde tkkrrenagg egteeelslf
      121 gtdffddgip deldkvdwyn hqmnwtnrmi lgdslqvmas laerenlrgk vqmvyidppy
      181 gikfnsnwqv saqsrdvkdg altsatreve qlkafrdtwd lginsylayl rdrlitardl
      241 lstsgsvfvq igdenvhlvr clldevfgge nfvsqitflk tssststfgg tadyiiwyak
      301 srqdmkfrql frekatggag gsgytrvrlp ngtvrpltkt evadnstlpe garifagdnl
      361 tsqsmgrtkg egaaswfrve iggrsfdpgp karwktnepg mrkliaasrv tpttgknlsy
      421 vrylddfpam plsdvwtdtl gqnqfggdkv yvvqtalpav trcmimctdp gdlvldptcg
      481 sgttayvaeq ygrrwitids srvaitlarh rimgalypsy lladspegka keaelsqqpl
      541 drspskhdir rgfvyecvph itlksiannp dikdgltrdq idkaikkhae fetlydrpye
      601 nkkavrvaga ftveslsphr svsfdqevpa sekaaemmps gasyeetile hvkkagvqng
      661 yrnerlefes vepvsgrilt avgirkdaee gtparvgial gpeygtvdsl fiknaareal
      721 rfgkidllli lgfafdanat eatneineer gefsviqerh vgtmtvlnvr mnpdlamgde
      781 lantgvgnlf tvfgepdiev tetsdgqlva eikgldifnp ttgdvraegp ddimmwsidt
      841 dydaeafivr hvyfsgengk stglnpyerl gkalkgqide ealatlfttk srpfpkpesg
      901 rlavkvvnyy gdevlkaiev
//
LOCUS       WP_005478947             278 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AfsR/SARP family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_005478947
VERSION     WP_005478947.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            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="AfsR/SARP family transcriptional regulator"
                     /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=29807
     Region          1..252
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 meirvlgplv ahldhtsvvp saakprqvla llalhagqvv tvstlldelw gdapprtapa
       61 tlqtyirqlr rrlgtvlgpt avrgpkdilc tryggyaldv agpddatqfq rlsvagqtal
      121 regaareasa llhqalalwr gpaladvqig ralevetvrl eetrlgalda rieadmrlgr
      181 haallgelta laaqhplhet vhaqlmlaly rsgrpshalg iyqrlrqcli relalepstr
      241 lqrlhqailr adpvlespdp avsagdglra vpltpasv
//
LOCUS       WP_005479139             262 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Vibrio].
ACCESSION   WP_005479139
VERSION     WP_005479139.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 262)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            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="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=29587
     Region          28..254
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mmsisqllgc iskqvdgqyi aqyeeltlrs vfqpiykkdl siiglealvr istadgsmir
       61 pdlffqspsi sehvqlnver lsrlihiknf gqsryrnkkl flnvlpraae mlakdlsysh
      121 llkqvicead lcreqivmel velsagdesf lykatkelsd ggfklaiddy ginastierv
      181 kcvrpdiikm drslllkyed gdfsalieal alakelsskt viegietehq lnlmkklgfd
      241 myqgyllamp qtlemyeeak ta
//
LOCUS       WP_005480015             239 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Streptomyces].
ACCESSION   WP_005480015
VERSION     WP_005480015.1
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 11459553
            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="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=25876
     Region          90..228
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mgtrrasksg sgtggasaag ggdtgrrvgr raliigtava avgtavvakd elkrawwrvp
       61 gvrkprkege vdytgakwvs asdanwrmad rpddfgidmv iihvtqgsfa savkvfqdpe
      121 hgaaahyivr kdghvtqmir eldvayhagn rdynersvgi ehegfvekpe dfttemyeas
      181 arltarvcar ydipvdrehi lghvevpgtd htdpgegwdw drymklvraa aaaqsstsa
//
LOCUS       WP_005480097             694 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: M4 family metallopeptidase [Streptomyces].
ACCESSION   WP_005480097
VERSION     WP_005480097.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 694)
  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 694)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..694
                     /product="M4 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=71906
     Region          69..671
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mqkesvlrrq shrrtshtsn tfghsarrra aagalvavta llaaavqsga asaapekaps
       61 aagkanpgal svkltpaqra elireanatk aataeklnlg akeklvvrdv vkdrdgtvht
      121 ryertygglp vlggdlvvkt skagatqgiv katkakiavs sltptvtkar aekqalgaak
      181 aekakspevn raprkvvwaa ggkpvlayet vvggfqhdgt pqelhvvtda tsgaklyewe
      241 avetgtgntv ysgsvtlgtt qsgstfnltd gargghktyn lnrgtsgtgt lfsgpddvwg
      301 ngspsnlesa gadahygaal twdyyknvhg rngirgdgvg aysrvhygnn yvnafwqdtc
      361 fcmtygdgsg nanpltsidv aahemthglt sntaglnysg esgglneats difgstvefy
      421 aanssdvgdy ligeeining ngtplrymdk pskdgsskda wysgigsidv hyssgpanhf
      481 fyllsegsga ktingvnyds ptsdglpvtg igrakaeqiw fkalttkfts ttnyaaartg
      541 tlavagelyg ttsaeytavq nawaginvgs rpgggggggt sfesttdvsi pdngaavtsp
      601 vtvsgrtgna psnlavavdi vhtyigdlqv qlvapdgtay tlkaygtggs tdninttytv
      661 nassevangv wqlrvqdnaa rdtgyinswk ltfp
//
LOCUS       WP_005480250             193 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator [Vibrio].
ACCESSION   WP_005480250
VERSION     WP_005480250.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 193)
  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 193)
  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   3  (residues 1 to 193)
  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   4  (residues 1 to 193)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 193)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            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="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21798
     Region          10..193
                     /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"
ORIGIN      
        1 mtqstsktpi ivccdslqeq arlsgllskd ydniigsqla qlealmqrep sasvvvgwqq
       61 ptaelrlivd fcrrksapll ivlkqlssnd inrlssqmdy vlmphdtefa lqpwidhatl
      121 vrerfermns eiesltnkie erklvekakg llmkvhnvde ehaykamrns amqssqtltq
      181 vaknlitalq lmd
//
LOCUS       WP_005480795             157 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Vibrio].
ACCESSION   WP_005480795
VERSION     WP_005480795.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..157
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17074
     Region          4..151
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mnieqyqrlt kqavaliese pdfianlanl ssllfmeled lnwagfyltk gdelvlgpfq
       61 gkpacvripm grgvcgtaak tnttqrvydv hefeghiacd aasnseivip fsikgkvagv
      121 ldidspsigr fnetdeeglt hfmsevekll nshanda
//
LOCUS       WP_005481254             701 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Vibrio parahaemolyticus].
ACCESSION   WP_005481254
VERSION     WP_005481254.1
KEYWORDS    RefSeq.
SOURCE      Vibrio parahaemolyticus
  ORGANISM  Vibrio parahaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 701)
  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 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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Vibrio parahaemolyticus"
                     /db_xref="taxon:670"
     Protein         1..701
                     /product="M4 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=75795
     Region          16..624
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mdlgskyqrk lvvgfvlvsp llvspslsaa qlerlepnhg rvvslekqnl aatqnvakal
       61 glkpgnnvqk lkanqdkngd vhvryqqtyk gipiwgkqiv lhrdkqgkik rfggtlvhdi
      121 gqdisnttpq lslerirskv qkpyldvgyh iedqqqglri yiddkdvahl ayeiqffads
      181 eqalnptrpt ylvdaksgev llqyeglaha eadgpggnqk igfyeygkey dpllvqqsgs
      241 tcimdtpniv qtinldgrts gsvhtfncpt ntvkeingay splndahyfg kvvydmykdw
      301 lntapltfql qmrvhyrkry enafwngssm tfgdgasyfy plvsldvsah evshgfteqn
      361 snliysgqsg gineafsdma geaaefysrg sndwkvgfdi rksptgalry mdnppldgrs
      421 idhasqyvsg mdvhyssgvf nkafyllavd ydwgtentfk afahanqnyw tpsatfdsaa
      481 agvlaaaqdl slpasdvtaa faqvgvstdg gvveppssac davslsngts sniesastgq
      541 whcftidvpa ngsdltitta gsngdadlyv klgsapslsn ydcrsissns nevcsfatps
      601 egtwhigvya ysgisnvsvt asyteqeapp psggvttqsi nngktwtaiv tgsglhdgvw
      661 nnnpsdscgn dsecsksgid kktgsvsftl sdgqtfvilk p
//
LOCUS       WP_005482500             641 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: molybdopterin oxidoreductase family protein
            [Streptomyces].
ACCESSION   WP_005482500
VERSION     WP_005482500.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 641)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 641)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 641)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..641
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=70981
     Region          13..634
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mrkrdrtpkt ytrlthplvr dcrdepfrra sweealdraa rglarnrdaf glfscaratn
       61 emnyvaqkfa rvvmgtnnvd scnrtchaps vaglsaafgs gggtssyeei ehtdvivmwg
      121 snarfahpif fqhvlkgihn garmyavdpr rtstaewaes wmglnvgtdi pmahaigrei
      181 ihaglaneaf ieratsgfee yralvepwtl slaekvtgvp aaavrelaha yaraeraqlc
      241 wtlgitehhn gtdnvralin lslltghvgr yasglqplrg qnnvqgggdm gaipnrlpgf
      301 qdildpesrl kfesawdtvi qphhglnlte mfeameegsl kavycigenp aqseadseqa
      361 vrrlgqldfl vvqdifltrt aqladvvlpa tagwaetdgt ttnserrvqr vrravtppge
      421 aredidiicd lasrlghewk yadaeavwne lrsvspdhyg mtyerlareq giqwpcpdpd
      481 rlepsylhgr lwdpdparrg plapfgivrh dppvdltder fpirlttgrr ldsyntgvqs
      541 ggyasplrrg eyielcpeda erygvavgee vqvssrrgsv vapvwidlal rpglafmtmh
      601 fpdevdtnql tieancpiag taefkasair ieklpvativ r
//
LOCUS       WP_005483136             362 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein [Vibrio].
ACCESSION   WP_005483136
VERSION     WP_005483136.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 362)
  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 362)
  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 362)
  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 362)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..362
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40888
     Region          9..358
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 msliqkslkr vlkmtavvaa mtfvatsasa aekvyrlkla etwgpnfpif gdttknmakm
       61 aeemsngrlq iridsankhk apfgvfdmvk sgqydmghsa syywkgkvpn tlyftsmpfg
      121 mlpteqyawf yygggmelme kvysphnlms fpggntdvqm ggwfqkeiks vddlqglkmr
      181 ipgfageila elgakptnia pgelytsler rtidalewvg psldlrmgfh kiapyyytgw
      241 hepatelqfl vnkrtwerlp ddlkailqva mktaaydmyt qskhesgknw asiqseypnv
      301 evkdfppevm dalraandkl lkqhaeedal akeiqesqan yikqvrpwsn ishraylnsq
      361 aq
//
LOCUS       WP_005483200             253 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Streptomyces].
ACCESSION   WP_005483200
VERSION     WP_005483200.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 253)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..253
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=25861
     Region          87..238
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(192..193,200,211..214,216)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 msdeltvrlr elaetaevpp pgsgaevrat agrrrrrrrt saavaggcaa aglaavltln
       61 aashgtqqrp ptaasdvpsa saapeavvdl srhvltfagr elpisagker tptptglmtv
      121 tgkhatvvat getvrlgsdy dlklswaltl spvedagprt geargtveat dgtepsgsad
      181 erttlspswg egvwiaaiah netapgsldt tdgwiglrta darwlyermp eggvveirgv
      241 gatpspsasp psg
//
LOCUS       WP_005483601             173 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Vibrio
            parahaemolyticus].
ACCESSION   WP_005483601
VERSION     WP_005483601.1
KEYWORDS    RefSeq.
SOURCE      Vibrio parahaemolyticus
  ORGANISM  Vibrio parahaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
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   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 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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Vibrio parahaemolyticus"
                     /db_xref="taxon:670"
     Protein         1..173
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19349
     Region          21..80
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msrnqfsitk qiieanlkks hgltvaeqsv lvtlssyfgk rgnsntyscf psqdriaeqv
       61 gctrptvnna lqklerlrfi rssyrgtnts klytwlgipt leeeeteels ptnergdtvs
      121 sesqtgndsd tensdalass tvnavqlqre qhqatsdwwn dfeeelevse spf
//
LOCUS       WP_005483819             330 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-oxoacyl-ACP synthase III family protein
            [Streptomyces].
ACCESSION   WP_005483819
VERSION     WP_005483819.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 330)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            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="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34003
     Region          5..312
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mttsigilgt gsylpkeeig neeiarrvpg itaewigrrt litgrryaap deatsdlarh
       61 aataalddag vtadridhli vatstgdapl pptsslvqsa lgahraacfd iniacagfvy
      121 aldiaralva qrpgtlalvi gadlysrfld ytdrgtavll gdaagaavvg avpepygild
      181 velagrgdah eliwiegggs rvpasaqtva ngghhlrmig rgvadfvman vppmitplle
      241 rtgttlddia hfvphqangv llaelvercg ltgarthtpl vkygnmgaas vpvaldeasr
      301 ahllgdgevl llagfgagma aglcllrwsa
//
LOCUS       WP_005483955             231 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase family protein [Streptomyces].
ACCESSION   WP_005483955
VERSION     WP_005483955.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 231)
  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 12830887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..231
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=24810
     Region          <49..87
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          118..225
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mgdigrrgav altitglltp ltlamgtapa qaasctatkg pyqkqvekfl grpvdgkqst
       61 adceairafq tkhgispnlg yagsvtwgvm dlmnkqkavg knpnaagkcp tnkgriacvn
      121 ltlqlswiqd ggklvygpvp vrtgrdgyet rtglkkiywr nidhvssiyh vpmpyaqffd
      181 ggqafhsvgv smwnppgshg ctnmtktdak kywsllkkgd dvyvygrkpg t
//
LOCUS       WP_005485951             936 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: penicillin acylase family protein [Streptomyces].
ACCESSION   WP_005485951
VERSION     WP_005485951.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 936)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 936)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 936)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..936
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..936
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=102574
     Region          42..936
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mptdnpassg qqsgksgrkk grkvrllliv lvlaiiggvg ygafwsvstv rasfpqtkgs
       61 ialeglsgpv dvkrdghgip qiyassdedl fmaqgyvqaq drfyemdvrr hmtagrlsem
      121 fgesqvdnde flrtlgwhri aeeeykktls aetrkylday akgvnaylag kdgdeisley
      181 aalgfandyr peewtpvdsv awlkamawdl rgnmqdeidr almtsrlgpk qiadlypqyp
      241 ydrngtivre gqydeltktw sdgsgptqna dgstqgtgqs vdgstqgtgg tgtgtgtagt
      301 stdsgalqtq ldglygvled lpeavgvngn gigsnswvvs gdhtitgkpl landphlsaa
      361 lpsvwyqmgl hckavsakcq ydvsgytfsg mpgvvighna diawgmtnsg vdvtdlylek
      421 ltgdgyqygs kvlpfdtree tievaggtsk kivvrttkdn apllsdrsse lvqvgkkatv
      481 gqdapdrgdg ygialrwtal dpsttmdavf amnkakgwdd fraaaalfdv psqnliyadt
      541 eghigyqlpg riptrgkgdg sipapgwdar yrwtgyidqd elpyeydper gyivtanqav
      601 vdkkypytlt adwgygtraq ritsliaski kgggkistdd mrqmqmdnss eiakllvpll
      661 lkidvndphv reaqkllegw dytqdadsaa aayfnsvwrn ilklafgdkl pkelrvegqc
      721 lsvepvdatg padedrrvre cgrrdadqaq pdggdrwfev vrkiiddqdn dwwstpktrt
      781 ekaadtrdel fkramrdarw eltaklgkdi dtwswgrlhr lflknqtlga dgpgflkyml
      841 nrgpwklggg eatvnatgwn aaggyevvwv psmrmvvnlg dldkskwinl tgasghayna
      901 hytdqtdkwa kgelltwsfs dkavergtsd tlllkp
//
LOCUS       WP_005486270             282 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Vibrio
            parahaemolyticus].
ACCESSION   WP_005486270
VERSION     WP_005486270.1
KEYWORDS    RefSeq.
SOURCE      Vibrio parahaemolyticus
  ORGANISM  Vibrio parahaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Vibrio parahaemolyticus"
                     /db_xref="taxon:670"
     Protein         1..282
                     /product="formate/nitrite transporter family protein"
                     /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=30043
     Region          5..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mstdfkpaef vqtminvgea ktntstrdll lrgtmagiil slavvvaita mvqtgiglvg
       61 alvfpvgfvi lsvmgydlvt gvfglaplak fanrpgitwg rifrcwglvg lgnligsliv
      121 aylvaisltg nfslelnava kkfvavstar slgfenmgmd gwitcfvrsi fcnlmvclgv
      181 ignmtarsvs grvammwfpi fiffalvfeh tvvnmflfpl gmilgadfgi atwlnfnlip
      241 tilgniiggl vmtclplylt haktapslsv eedviaepai ak
//
LOCUS       WP_005488655             377 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: exonuclease SbcCD subunit D [Vibrio].
ACCESSION   WP_005488655
VERSION     WP_005488655.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..377
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42818
     Region          1..270
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          267..353
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkfihtsdwh lgrqfhnvsl ledqqavleq liqyiennpv davivagdvy drsvpptiai
       61 ellnrvvkri cgelntpmil isgnhdgaer lgfgseqmkr sglhiisnfe dmltpvviet
      121 kaaghvafyg mpyndpeqvr yvykepvsth deahkllaek iteqfqsehr nilishcfvd
      181 gaieseserp lsiggsdrvs hehflnfdyv alghlhqpqk kgeeyirysg slmkysfgeq
      241 nqkkgftlve igkdgfigae hieltaphem rivegeleqi lewgktdpkn edyllvrlmd
      301 khailnpmek lrtvypnvlh lekpgmligv eqemaqakla rseidmfkdf faeaqdsels
      361 neqeqaisdi ikqlsqq
//
LOCUS       WP_005490076             660 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Halanaerobium saccharolyticum].
ACCESSION   WP_005490076
VERSION     WP_005490076.1
KEYWORDS    RefSeq.
SOURCE      Halanaerobium saccharolyticum
  ORGANISM  Halanaerobium saccharolyticum
            Bacteria; Bacillati; Bacillota; Clostridia; Halanaerobiales;
            Halanaerobiaceae; Halanaerobium.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 660)
  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   3  (residues 1 to 660)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Halanaerobium saccharolyticum"
                     /db_xref="taxon:43595"
     Protein         1..660
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=73756
     Region          1..660
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          169..242
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 mqeneylkif faeakeyiev lnngiltlen npedketida ifraahslkg maaamgfekl
       61 telthklens ldkiregeik vktefidllf qaldniqylv kaveenngke pegfdldali
      121 aelnaytean dfkesqtaav dtsenvrdfl teaekeelle rkkdkekvyh lkaevvdeef
      181 ksvrafmllk kldeigqlfk sepprntien seadidqlni ialswlekee fkteieaqss
      241 iklisldelq sseikidsek esksntvqkn kvssfnssst vrvdiskldt lmnmvgelli
      301 nksrlesldi kktkfkeimp qldrvtmdlh hivmqirmvp vgvmfsrfpr mmrdlankmn
      361 keidfvmsgq eteldrsiid eladplthll rnaidhgiek paarkaagkd gkgkvellay
      421 qkgseiiiev kddgagikaa aiakkavdkg iieqeeveql ekrdildfvf hpgfstaqei
      481 tdvsgrgvgm divrstvkkl dgqvsidsep gegstfkitl pltlaisqal mvkiigdtfa
      541 iplsavsetl tietenikki rgkdvivlre ttipivsaaa ifgdddqksf knsekdlsvv
      601 ilksgerkvg lvveellnqq eivikslgky lqetryisga tiigdgdval ivdvrdvvsr
//
LOCUS       WP_005490275              98 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Halanaerobium
            saccharolyticum].
ACCESSION   WP_005490275
VERSION     WP_005490275.1
KEYWORDS    RefSeq.
SOURCE      Halanaerobium saccharolyticum
  ORGANISM  Halanaerobium saccharolyticum
            Bacteria; Bacillati; Bacillota; Clostridia; Halanaerobiales;
            Halanaerobiaceae; Halanaerobium.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Halanaerobium saccharolyticum"
                     /db_xref="taxon:43595"
     Protein         1..98
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11067
     Region          1..95
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mtaqeiiefl qikrsilnrf gvknialfgs yvsgqannns didllvefke gektfdnymd
       61 lkfylednln kdvdlvikda lkeelkedil gsakyala
//
LOCUS       WP_005490192             383 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Halanaerobium
            saccharolyticum].
ACCESSION   WP_005490192
VERSION     WP_005490192.1
KEYWORDS    RefSeq.
SOURCE      Halanaerobium saccharolyticum
  ORGANISM  Halanaerobium saccharolyticum
            Bacteria; Bacillati; Bacillota; Clostridia; Halanaerobiales;
            Halanaerobiaceae; Halanaerobium.
REFERENCE   1  (residues 1 to 383)
  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 383)
  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
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 383)
  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   5  (residues 1 to 383)
  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   6  (residues 1 to 383)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 383)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 383)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Halanaerobium saccharolyticum"
                     /db_xref="taxon:43595"
     Protein         1..383
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44402
     Region          16..>77
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Site            order(21,24,73)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
     Region          69..346
                     /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 mdkkdrlkll ykkllenesl tkteladkld lsltaisdyi nelvesgwii prkkadssgg
       61 rraviyqinp eskyiialdl kdshfyifis dlksnliksk ihyldnydfk nyvseiikva
      121 kallvdleig iekilalgis isgitdfenk ivkrsnqlnw tdkalaqaie kqleipvfve
      181 tdvrvyayne leaedknnit vvlyigegig lsliirnkil qgytnrvgdn rffgkelenl
      241 nyiirndqyi keindlpyys knfeqqtink lnekykefis qnqknrqeln dftdyiasmm
      301 lstinllnpk kvlltgnvfd yndliynqvk akisegemyh lpqikrndhs qnplekalls
      361 flmhkflgid dfdftkekln dfs
//
LOCUS       WP_005490328             332 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Halanaerobium
            saccharolyticum].
ACCESSION   WP_005490328
VERSION     WP_005490328.1
KEYWORDS    RefSeq.
SOURCE      Halanaerobium saccharolyticum
  ORGANISM  Halanaerobium saccharolyticum
            Bacteria; Bacillati; Bacillota; Clostridia; Halanaerobiales;
            Halanaerobiaceae; Halanaerobium.
REFERENCE   1  (residues 1 to 332)
  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 332)
  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 332)
  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 332)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Halanaerobium saccharolyticum"
                     /db_xref="taxon:43595"
     Protein         1..332
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=36978
     Region          1..332
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mkkcqissil vmillvslil sgsifaadye mkighsqsvk tprhkacvyf kliveretdg
       61 rvevkiypsn qlgteaemle svkmgaiqat lggqfeaasp klliytmpfl fedisavhdi
      121 irgpigdkia saaeandiki latgvagglr nfsnneraie tpadmqglkm rtppidsiik
      181 tieaiggnpv svpyaelyma lktgvadgqe npftnmvdkk lyevqkylti vnyqfhpspl
      241 ytsldwynsl dselqvtlek cadkmmiynd elnregteds lavlqkemev nyltdeqrqm
      301 fidasqsvyd yyieqgffsq aeideireaa sn
//
LOCUS       WP_005496812             804 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Shewanella benthica].
ACCESSION   WP_005496812
VERSION     WP_005496812.1
KEYWORDS    RefSeq.
SOURCE      Shewanella benthica
  ORGANISM  Shewanella benthica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 804)
  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 804)
  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 804)
  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   4  (residues 1 to 804)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..804
                     /organism="Shewanella benthica"
                     /db_xref="taxon:43661"
     Protein         1..804
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89551
     Region          91..800
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mpisplspls sdqlyrssel sgleadckst khltpldeiv gqeraqqave famsmpdkgy
       61 niyalgrngl gkhtmvmryl nryepngrgh tlhdwcyvin fdesrvpkvl klssgsgief
      121 kkdvekfiik ltkalplafd nemyyssaek lksqlsnrqe salkgltkea kdasisltit
      181 aegsyellam kgeeahtdet fkalskkqqd vletsivele sklrviirqf tvweeeysdk
      241 qqkqdeqvaq dvlthlmtkl kekysgipav ksylgamhkd ildnldlfle dneeqlalsy
      301 asldkkmprr yqvnvlvnqd ddkmpiivee spnyhsifgy ienatfkgti fsdfslirsg
      361 slhkanggvl midaakvleq pyvwdglkra lrsrklsfss lerevtlsgt isldpeaipl
      421 dvkiilfgdy qtyqllqhyd pefselfrvt adfedvmprt eksealyakf issivhgnkm
      481 lhcdrnaikr iiefssrqad dqnklslhsa dianllresn ycaravnanm irashveqal
      541 hnhemrvcrv kdnvmesfit gttlistqdh avgqvnalsv iatsdhqfga pnritattaf
      601 gegkvfdier kvdlggslhs kgvmilsayl asllgktaki pltthitfeq syggvdgdsa
      661 tmaelcaivs sfsnqairqd iaitgsmnqf geaqpiggvn ekiegffdvc tikgrtntqg
      721 viipktnvqn lmlrsdivea vkkgkfniwa idhvsqaiel ltgiesginl drqskqldeh
      781 padsvlglaq arlnelrets tasa
//
LOCUS       WP_005498791             262 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Vibrio parahaemolyticus].
ACCESSION   WP_005498791
VERSION     WP_005498791.1
KEYWORDS    RefSeq.
SOURCE      Vibrio parahaemolyticus
  ORGANISM  Vibrio parahaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 262)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Vibrio parahaemolyticus"
                     /db_xref="taxon:670"
     Protein         1..262
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=29669
     Region          28..254
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mmsisqllgc iskqvdgqyi aqyeeltlrs vfqpiykkdl siiglealvr istadgsmir
       61 pdlffqspsi sehvqlnver lsrlihiknf gqsryrnkkl flnvlpraae mlakdlsysh
      121 llkrvicead lrreqivmel velsagdesf lykatkelsd ggfklaiddy ginastierv
      181 kcvrpdiikm drslllkyed gdfsalieal alakelsskt viegietehq lnlmkklgfd
      241 myqgyllamp qtlemyeeak ta
//
LOCUS       WP_005480098             553 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: M4 family metallopeptidase [Streptomyces].
ACCESSION   WP_005480098
VERSION     WP_005480098.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 553)
  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 553)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..553
                     /product="M4 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=57434
     Region          47..>539
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mtpfyarhqr ttlaiatava agallttalt tgataqpapv adkakpagaq valtpaarta
       61 likkadaatt etadeiglga keelvvrdvl kdadgtvhtr yertfgglpv lggdlvvhes
      121 kagaiksvtr atkatvkvad ltadvtkata ekqalkaaka egstkteadk aprkviwaas
      181 gkpalayetv vggfqhdgtp qqlhvvtdae tgkklyewea vqtgsgksky ngsvtlgttl
      241 sgstynltda grgghktynk arstsssagt lftdaddvwg tgsisssstd qnaavdahyg
      301 aqvtwdfykn vlgrngiknn gvaaysrvhy gnayvnafwd dscfcmtygd gtsntkplts
      361 ldvaghemsh gltantarln ysgesgglne atsdifgtav efyaanasdp gdyligekid
      421 ingngtplry mdqpskdgds anywssslgs ldvhyssgpa nhfffllseg sgaktingvs
      481 ynsptsngat itgigrakav qiwykalsty mtsttnykga rtatlnaass lygassaeya
      541 avnaawaavn vna
//
LOCUS       WP_005498946             282 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Vibrio
            parahaemolyticus].
ACCESSION   WP_005498946
VERSION     WP_005498946.1
KEYWORDS    RefSeq.
SOURCE      Vibrio parahaemolyticus
  ORGANISM  Vibrio parahaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Vibrio parahaemolyticus"
                     /db_xref="taxon:670"
     Protein         1..282
                     /product="formate/nitrite transporter family protein"
                     /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=30041
     Region          5..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mstdfkpaef vqtminvgea ktntstrdll lrgtmagiil slavvvaita mvqtgiglvg
       61 alvfpvgfvi lsvmgydlvt gvfglaplak fanrpgitwg rifrcwglvg lgnligsliv
      121 aylvaisltg nfslelnava kkfvavstar slgfenmgmd gwitcfvrgi fcnlmvclgv
      181 ignmtarsvs grvammwfpi fiffalvfeh tvvnmflfpl gmilgadfgi vtwlnfnlip
      241 tilgniiggl vmtclplylt haktapslsv eedviaepai ak
//
LOCUS       WP_005499779             786 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Vibrio parahaemolyticus].
ACCESSION   WP_005499779
VERSION     WP_005499779.1
KEYWORDS    RefSeq.
SOURCE      Vibrio parahaemolyticus
  ORGANISM  Vibrio parahaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 786)
  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 786)
  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 786)
  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   4  (residues 1 to 786)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..786
                     /organism="Vibrio parahaemolyticus"
                     /db_xref="taxon:670"
     Protein         1..786
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88017
     Region          70..786
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mailrlepqq lysvadlenm pckstkelpp ideivgqera qkavefamsi kekgyniyai
       61 gqnglgkrtm ilrylnrhqh dadalfdwcy vanfedtrtp kvlklpcgig nklrvdieal
      121 mgkllnalpl afdnemyfsr adrlknqlan kqqneldris reakehgisl titsqgdyqf
      181 vamngdelht eesfdalskk eqeqfsdsid alevslrsmv reltewedty sdkikklnde
      241 vtldvithfi kklkvdysey seiktyltel qkdivenadi fldqsgeqge iaaasldkkl
      301 prrykvnvlv srnnsdfpiv veenpnyhsl fgsietatfk gtvftdfsli ragslhkang
      361 gvllmdaqkv leqpyvwdgl kralrsrqls ftslekevtl tgavsldpep ipldikiilf
      421 gdyrtyqllq hydpefself rvtadfedem krtpeselhy arfissvvhd nnmlhcdrka
      481 iariieyssr lsgdqsklsl hsanianllr esnyvarqan snmirighve eamknqemrv
      541 srlrdsvmet flngttlilt egsaigqvna lsvlstsdym fgapnritat tcygdgdvid
      601 iersvdlggs ihskgvmils aylssvfgkt arvpltttit feqsyggvdg dsasmaefca
      661 vvsafskqpn rqdiaitgsm nqfgeaqpig gvnekiegfy dvcvikgrhs gqgviiprsn
      721 vhnlmlradi vkavekgefh iwaidhvtea ielftskvag eptdegsypi dtifglaqak
      781 lnslrk
//
LOCUS       WP_005499482             724 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Shewanella benthica].
ACCESSION   WP_005499482
VERSION     WP_005499482.1
KEYWORDS    RefSeq.
SOURCE      Shewanella benthica
  ORGANISM  Shewanella benthica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 724)
  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   3  (residues 1 to 724)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Shewanella benthica"
                     /db_xref="taxon:43661"
     Protein         1..724
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76523
     Region          6..721
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msfdvdeeil qdflieagei lellseqlvt lenhpedsel lnaifrgfht vkggagflsl
       61 spmvdichea entfdllrtg klevsaelmd vilqavdain vmfaqtqagq qqetadatll
      121 anlkllssas slpvaaaaap naasielfdq tplvgdsgie lfdcapqpis tiageggide
      181 inddefeall dalhgggnsp tatqpvavsa papsqsddit ddefesllde lhgsgkfdkq
      241 assaslvdtp pavdadgisd defeklldel hgagagpgvg saavanksvp avksvapatp
      301 vaakaaakaa akavvpakka vaksastnip qaettvrvdt arldqimnmv gelvlvrnrl
      361 lslgvsrdde emskalanld lvtadlqgav mktrmqpikk vfgrfprvvr dlartlkkei
      421 tltmigedtd ldknlveala dplvhlvrns vdhgiempae reasgkprtg titlsasqeg
      481 dhillkiedd gagmdpnklk eiaiargvld degaarmsdq eaynlifapg fstkveisdi
      541 sgrgvgmdvv ktriaqlngt vhidsikgkg tvleikvplt laimptlmve vasqvfalpl
      601 ssvseifnld ltktnivdgq ltvivrqkav plfylehwls rtpsnlkhgd kthghvvivq
      661 lgtqqigfvv dsligqeevv ikplgtmlhg tpgmagatit sdggialild vpgllkhyar
      721 kqtk
//
LOCUS       WP_005501853             143 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Grimontia hollisae].
ACCESSION   WP_005501853
VERSION     WP_005501853.1
KEYWORDS    RefSeq.
SOURCE      Grimontia hollisae
  ORGANISM  Grimontia hollisae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Grimontia.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Grimontia hollisae"
                     /db_xref="taxon:673"
     Protein         1..143
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15989
     Region          3..142
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdwingesal wvlfstgfls atllpggsea nlvyllkqre fgvgilvlva tlgntlggmt
       61 nywigrvipa rtleqkhgqk ainwlqrygy wtlllswlpv igdplclaag wlrlkqrwcw
      121 iliatgkalr ylilslitrg ily
//
LOCUS       WP_005502008             105 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Shewanella benthica].
ACCESSION   WP_005502008
VERSION     WP_005502008.1
KEYWORDS    RefSeq.
SOURCE      Shewanella benthica
  ORGANISM  Shewanella benthica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (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   2  (residues 1 to 105)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Shewanella benthica"
                     /db_xref="taxon:43661"
     Protein         1..105
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11248
     Region          45..100
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkstlvsatl maaifslsvy agdvssqskt ihqkenshqv qqlnvnints siaqlvllkg
       61 igeskakaiv eyresngkfe vigdlsnvkg igpklveknr mflsl
//
LOCUS       WP_005503591             188 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Grimontia hollisae].
ACCESSION   WP_005503591
VERSION     WP_005503591.1
KEYWORDS    RefSeq.
SOURCE      Grimontia hollisae
  ORGANISM  Grimontia hollisae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Grimontia.
REFERENCE   1  (residues 1 to 188)
  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 188)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 188)
  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   4  (residues 1 to 188)
  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   5  (residues 1 to 188)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Grimontia hollisae"
                     /db_xref="taxon:673"
     Protein         1..188
                     /product="TRAP transporter small permease subunit"
                     /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=21143
     Region          7..176
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 metaspflia lvrginrfsd wtgrfvswfv laivlitfvv vvmryvfntg svfmqesvly
       61 fhnyvimlga ayallkgahv rvdifyrpms drkkawvdlm gflllllptc afifyiawdy
      121 vaaswaimeg sqeaggvdar yifktsillm palviiqgla ealkallmlt gyqalakqle
      181 dhdeehal
//
LOCUS       WP_005503473             108 aa            linear   BCT 20-JAN-2025
DEFINITION  PilZ domain-containing protein [Shewanella benthica].
ACCESSION   WP_005503473
VERSION     WP_005503473.1
KEYWORDS    RefSeq.
SOURCE      Shewanella benthica
  ORGANISM  Shewanella benthica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (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   3  (residues 1 to 108)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Shewanella benthica"
                     /db_xref="taxon:43661"
     Protein         1..108
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11791
     Region          2..108
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 midlvvnfdt lhqlyraymp fiqpaglfia tseshylgqe ltiayqlpga vnrhefqgmv
       61 vwinplgasg grpagigiki lsdaelhkqh ieillarels sgdltctm
//
LOCUS       WP_005504300             378 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Rothia].
ACCESSION   WP_005504300
VERSION     WP_005504300.1
KEYWORDS    RefSeq.
SOURCE      Rothia
  ORGANISM  Rothia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 378)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Rothia"
                     /db_xref="taxon:32207"
     Protein         1..378
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=40815
     Region          1..376
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mlilvvnags sslkyqvrdt slpeaeqmlt sglvenigtd vpnhevafdi mseklepvlh
       61 grelqavghr vvqgaekfth ptllteevvq qiddlsplap lhnpahvqgm raamhkwpsl
      121 pqvaifdtaf hstmpeeawr yaipydladk ysirrygfhg tsheyvshva admlgiarde
      181 fngivahlgn gasvtavkgg ksvdtsmgyt plaglimgtr sgdidpsalt tilsregidg
      241 erldtilnke sgllalagsn dmrkvveaaq sgderaqlal dmtsyrlmky iggynlvvgg
      301 aqaliftagi gensgdfrkl vldrlgalgi kyneeenakr speprviste dsaikvlvip
      361 tneekaiaea teelvksl
//
LOCUS       WP_005507237             316 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Rothia mucilaginosa].
ACCESSION   WP_005507237
VERSION     WP_005507237.1
KEYWORDS    RefSeq.
SOURCE      Rothia mucilaginosa
  ORGANISM  Rothia mucilaginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Rothia.
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   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   4  (residues 1 to 316)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Rothia mucilaginosa"
                     /db_xref="taxon:43675"
     Protein         1..316
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=33960
     Region          39..294
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mtaqnpsaqp penspqnlss pqipwaknaa tgstqaggir fenitksyps rtgepttvlq
       61 nlnlhipagq itvfvgpsgc gkttslrmin rmvepnsgti tidgvnvhek npyelrrgig
      121 yvmqqgglmp hrtvaqniat vprllgasrk eaqaralell dvvgldssya krypsqlsgg
      181 qvqrvgvara laadapvllm depfsavdpv vrtdlqkell rlqrqlakti vfvthdidea
      241 lllgdtiavf aeggrlaqfg tpeeilyspa ddfvrsfvsr svaglldeqt vrqvrarrla
      301 asreaqngaa egekse
//
LOCUS       WP_005508003             465 aa            linear   BCT 20-JAN-2025
DEFINITION  galactokinase [Rothia mucilaginosa].
ACCESSION   WP_005508003
VERSION     WP_005508003.1
KEYWORDS    RefSeq.
SOURCE      Rothia mucilaginosa
  ORGANISM  Rothia mucilaginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Rothia.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   McAuley,M., Kristiansson,H., Huang,M., Pey,A.L. and Timson,D.J.
  TITLE     Galactokinase promiscuity: a question of flexibility?
  JOURNAL   Biochem Soc Trans 44 (1), 116-122 (2016)
   PUBMED   26862196
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Holden,H.M., Thoden,J.B., Timson,D.J. and Reece,R.J.
  TITLE     Galactokinase: structure, function and role in type II galactosemia
  JOURNAL   Cell Mol Life Sci 61 (19-20), 2471-2484 (2004)
   PUBMED   15526155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Rothia mucilaginosa"
                     /db_xref="taxon:43675"
     Protein         1..465
                     /product="galactokinase"
                     /EC_number="2.7.1.6"
                     /GO_function="GO:0004335 - galactokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0005534 - galactose binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0046835 - carbohydrate phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=49412
     Region          19..450
                     /region_name="GalK"
                     /note="Galactokinase [Carbohydrate transport and
                     metabolism]; COG0153"
                     /db_xref="CDD:439923"
ORIGIN      
        1 msmtataqwa alpdhsaeia rvreefitay gyepdgvwsa pgrlnllgey idflggsclp
       61 mplpyrtyva galrrdgvlr aaslqmpgde rtvvirdiqp ghlkgwftyv agvawamnqe
      121 ggrdimlpde fgadllinsr vpvggglsss aalecstala llelscpvre ecpeadatpa
      181 dsdalrarla qvcitaenkm agahtggldq taslrsypeq alvvdfrdfs iepvavdiaq
      241 hglsflvidt ntpheltdgg faarraasea cadalglrfl rdalpedlsc agmdaraaka
      301 wradlvdssv nraldaleda grpcsfprgw vrhafhdmtl vgrasyllqh adelgfaafe
      361 eagriftesf vsmrdelrvs rpeiddavqv cldrgalgar ivgggfggav maliptsqle
      421 aaadavatay avrgyaaprf lpmvagfaas hdwaagatpt dipvl
//
LOCUS       WP_005508172             196 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LytR C-terminal domain-containing protein [Rothia].
ACCESSION   WP_005508172
VERSION     WP_005508172.1
KEYWORDS    RefSeq.
SOURCE      Rothia
  ORGANISM  Rothia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 196)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Rothia"
                     /db_xref="taxon:32207"
     Protein         1..196
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=19609
     Region          102..188
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 msyprdefde vdentarrgt yravnadpak spkgaiplva agvvglligg amyvyaprta
       61 spqysastak sssapasasa ssapakasas asatktglae sisvavynaa apagsasraa
      121 alltgytine tanytgvapa tsvvyyaegy qsqaqsiask lgitqvrqat anvemgnhev
      181 ivilssdyta sataae
//
LOCUS       WP_005508370              88 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Rothia mucilaginosa].
ACCESSION   WP_005508370
VERSION     WP_005508370.1
KEYWORDS    RefSeq.
SOURCE      Rothia mucilaginosa
  ORGANISM  Rothia mucilaginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Rothia.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 88)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 88)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Rothia mucilaginosa"
                     /db_xref="taxon:43675"
     Protein         1..88
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8916
     Region          1..88
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mqvhffaaar saagttqlsv plvelpsatl galiehlgqs legttpsglt laqvmeqcsf
       61 lvngarsdaq aplqdadrvd vlppfagg
//
LOCUS       WP_005510374             326 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Corynebacterium
            amycolatum].
ACCESSION   WP_005510374
VERSION     WP_005510374.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..326
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36287
     Region          12..313
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mptpqslsti alpqsyelcr dimtshgrty slatrllapr qqravwslya warivddyvd
       61 cpadadrspt hieatvtrls elfhsavvsg slddvhrdrd ravisaaakt frdydidpql
      121 sadfvhsmlm dvpdtschia hfetweqlds ymwgsaavig lemmpilgtr tgvsreeatp
      181 yaeclgkafq vtnflrdiae dfrrgriylp lneweafgvg teeigycaam gqttpavrqa
      241 layfiarnra lyaeatsgvg mlevpgrqai raaeilysdi lgeiermnyn vfaqraqvgr
      301 arkakialpl lfravagrlr qelsea
//
LOCUS       WP_005514264             211 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Prescottella equi].
ACCESSION   WP_005514264
VERSION     WP_005514264.1
KEYWORDS    RefSeq.
SOURCE      Prescottella equi (Rhodococcus equi)
  ORGANISM  Prescottella equi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Prescottella.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Prescottella equi"
                     /db_xref="taxon:43767"
     Protein         1..211
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23614
     Region          3..198
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdletalttt rtvrkrldfs rpvprevide clrlalqapn gsnrqlwhwv ivddpavraq
       61 vadlyregla damgrtnmrn pdpaqsgrir psveylgehl hevpalaipv lkddargmev
      121 fmqasrwgsv ipavwsfmla lrarglgsaw ttvhllrerr madllgipdg ytqvglfpva
      181 ytlgtdfkpa srrpvdevrs wnrfeapqsa s
//
LOCUS       WP_005514441             298 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Prescottella].
ACCESSION   WP_005514441
VERSION     WP_005514441.1
KEYWORDS    RefSeq.
SOURCE      Prescottella
  ORGANISM  Prescottella
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Prescottella"
                     /db_xref="taxon:2979332"
     Protein         1..298
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31320
     Region          1..257
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mridlhthst asdgtdspae lvrkaaasgv dvlaitdhdt tagwkeaaaa lpsglrlvrg
       61 memscegrge dgrpvavhll aylfdpesqe favererlrd ervtrlrama vrmaaaglpi
      121 dpeailadag pavgrphlar alvragvvdt vgdaftdlls trspyyveks dtpleravem
      181 vadaggvsvi ahararargr lldlehirel aehglgglev dhpdhgaadt allrslaael
      241 dlvatgssdy hgknktialg qhttapeale eivaratgvp vltgdavtdv patdgarr
//
LOCUS       WP_005515144             338 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Prescottella].
ACCESSION   WP_005515144
VERSION     WP_005515144.1
KEYWORDS    RefSeq.
SOURCE      Prescottella
  ORGANISM  Prescottella
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  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   4  (residues 1 to 338)
  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 338)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Prescottella"
                     /db_xref="taxon:2979332"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37355
     Region          22..213
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          258..338
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mslatvpadf lkralrlaet agadlastle asgidvasld dprsrltpeq vtaftqaawq
       61 ltddelfgig aspvprgtfr liclslihrp dlgsalerma dvtralpvpp itlvrserst
      121 rlevrvdvrd dayspefvde afrlvtdfel illhrfaawl vgrrvrlrav lipypepear
      181 fakhydaifg vpvtfgaava tlefdnailr apiiqdedtl aeylrespnl llserdydst
      241 asaqvrrvle mgargrtcta deiaemlsis vphlrrllrq egtslnalre evlrdaavaa
      301 lrrgepvdel sarlgfseas afrrafkrwt gatpgayr
//
LOCUS       WP_005516614             281 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio mimicus].
ACCESSION   WP_005516614
VERSION     WP_005516614.1
KEYWORDS    RefSeq.
SOURCE      Vibrio mimicus
  ORGANISM  Vibrio mimicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 281)
  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 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   3  (residues 1 to 281)
  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   4  (residues 1 to 281)
  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 281)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Vibrio mimicus"
                     /db_xref="taxon:674"
     Protein         1..281
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30653
     Region          28..273
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <167..265
                     /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 mdalssliqh aapkaslffs gnlcqssese ehanggqlhl lrrgelalhq tgsaiqiise
       61 ptlivyprgr hhrlqplhfs gcdlvcarlt frdsplfral pdaliipltk ldglaptinl
      121 lfdeafsqry ahnavvasll dlllllllrh lvehnlcesg llaamtdpkl akaieaihan
      181 pdtpwtivdl aklagmsraq faarfhqvig qpplsyvtes rlllaqqlll agqpvkfial
      241 evgysggvaf sraferqfgl tptrwlqqqk nigteaigpt e
//
LOCUS       WP_005517302             281 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio mimicus].
ACCESSION   WP_005517302
VERSION     WP_005517302.1
KEYWORDS    RefSeq.
SOURCE      Vibrio mimicus
  ORGANISM  Vibrio mimicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 281)
  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 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   3  (residues 1 to 281)
  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   4  (residues 1 to 281)
  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 281)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Vibrio mimicus"
                     /db_xref="taxon:674"
     Protein         1..281
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30678
     Region          28..273
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <167..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 mdalssliqh aapkaslffs gnlcqssese ehanggqlhl lrrgelalhq tgsavqtise
       61 ptlivyprgr hhrlqplhfs gcdlvcarlt frdsplfral pdaliiplak ldglaptinl
      121 lfdeafsqry ahnavvasll dlllllllrh lvehnlcesg llaamtdpkl akaieaihan
      181 pdtpwtivdl aklagmsraq faarfhqvig qpplsyvtes rlllaqqlll agqpvkfial
      241 evgysggvaf sraferqfgl tptrwlqqhk nigteaiept e
//
LOCUS       WP_005518024             203 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Prescottella].
ACCESSION   WP_005518024
VERSION     WP_005518024.1
KEYWORDS    RefSeq.
SOURCE      Prescottella
  ORGANISM  Prescottella
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Prescottella"
                     /db_xref="taxon:2979332"
     Protein         1..203
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=22184
     Region          28..201
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 magwtdprre ptpdtgedlr rlalrqagyf ttgqalrlgc ttediggrla egswlrierd
       61 lfrlasfprs dleefakwca wfegaavvsh qsaaelhglg hlhpsfvhls tqatapaptr
      121 rlalhrrelr aqdyevvgtf gittplctal dlatggiaqd lfdevvcdgv aigridpekl
      181 raecigrpqq vaeriehalg acq
//
LOCUS       WP_005519520             339 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Corynebacterium
            matruchotii].
ACCESSION   WP_005519520
VERSION     WP_005519520.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium matruchotii
  ORGANISM  Corynebacterium matruchotii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 339)
  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 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 339)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 339)
  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   5  (residues 1 to 339)
  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   6  (residues 1 to 339)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Corynebacterium matruchotii"
                     /db_xref="taxon:43768"
     Protein         1..339
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37993
     Region          18..194
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <142..324
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkrhileqny prllasvgid aeqvlrkagv aedtfthhpp tmttsnyfaf ltaigklcpp
       61 gsavqlasat gieqfsppvf asycarngrv cierlkqykr iigplefhtt gttkqmiiel
      121 vcegyelpsf lvecefvflv nllrtatgeh itptsvqlhq ldvdravvdf lgclpqvgps
      181 nviafatrdm elpfishnds mwsyfepelq rrlaeldadd syttrvqsal memlpggetg
      241 iddvahrlgm skrtlqrklg aekttfqaql khtrqllaqh yltttsmkvd eiayllgyie
      301 lnsflrafyt wlgmspreyr arhavdgqtl rpptpptpp
//
LOCUS       WP_005521224             272 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Vibrio mimicus].
ACCESSION   WP_005521224
VERSION     WP_005521224.1
KEYWORDS    RefSeq.
SOURCE      Vibrio mimicus
  ORGANISM  Vibrio mimicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Vibrio mimicus"
                     /db_xref="taxon:674"
     Protein         1..272
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30309
     Region          35..116
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          <94..263
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          186..264
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 msmpnanlef kiaslhsvqp wfvlgakrfn slltpesplt shfysfdasd nhdssiaipd
       61 gcidllfdcd adapkayicg splealkadf mkghyylgvr frpgvvpdll nldveevisn
      121 rldlsellyg adrileqvck agdflskara vndfvsqfdc rpcshltmev iarvtqargn
      181 iqiqdlvndt gysartlqrt frndtgltpk afsraircqs avykishnnq lplsdlafdl
      241 gfsdqahfqr efkklvsvtp mdyqsltkse kp
//
LOCUS       WP_005522088             216 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Corynebacterium
            matruchotii].
ACCESSION   WP_005522088
VERSION     WP_005522088.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium matruchotii
  ORGANISM  Corynebacterium matruchotii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 216)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Corynebacterium matruchotii"
                     /db_xref="taxon:43768"
     Protein         1..216
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=21016
     Region          126..215
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mpdiqpqrel plrgvamili svalllamwg iysmtggksa kvhnaastds aaasavsiqp
       61 aapagpvtsa pgvpapssga papasapapa gavasgaaap gapsgatagt agaagastsa
      121 gdksavtvhv lnnstiqgla akakeqltrq gyrvgqvgny srsvvpqntv yytdneqqar
      181 elaekvggva qqrpadlpae tagpgslvvv latsfn
//
LOCUS       WP_005523559             103 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Vibrio mimicus].
ACCESSION   WP_005523559
VERSION     WP_005523559.1
KEYWORDS    RefSeq.
SOURCE      Vibrio mimicus
  ORGANISM  Vibrio mimicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 103)
  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   2  (residues 1 to 103)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Vibrio mimicus"
                     /db_xref="taxon:674"
     Protein         1..103
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10916
     Region          42..101
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mqfkttlmtv llslclpamp mlvsaeetnp taqteegivi tvnintasae elatllkgig
       61 lkkaqaivdy reangpfnsi ddltkvkgig eatvrnnatr ill
//
LOCUS       WP_005524470             339 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Corynebacterium
            matruchotii].
ACCESSION   WP_005524470
VERSION     WP_005524470.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium matruchotii
  ORGANISM  Corynebacterium matruchotii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 339)
  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 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 339)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 339)
  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   5  (residues 1 to 339)
  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   6  (residues 1 to 339)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Corynebacterium matruchotii"
                     /db_xref="taxon:43768"
     Protein         1..339
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37982
     Region          18..194
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <142..324
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkrhileqny prllasvgid aeqvlrkagv aedtfthhpp tmttsdyfaf ltaigklcpp
       61 gsavqlasat gieqfsppvf asycarngrv cierlkqykr iigplefhtt gttkqmsiel
      121 vcegyelpsf lvecefvflv nllrtatgeh itptsiqlhq ldvdravvdf lgclpqvgps
      181 nviafatrdm elpfishnds mwsyfepelq rrlaeldadd syttrvqsal memlpggetg
      241 iddvahrlgm skrtlqrklg aekttfqaql khtrqllaqh yltttsmkvd eiayllgyie
      301 lnsflrafyt wlgmspreyr arhavdgqtl rpptpptpp
//
LOCUS       WP_005527096              86 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Corynebacterium matruchotii].
ACCESSION   WP_005527096
VERSION     WP_005527096.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium matruchotii
  ORGANISM  Corynebacterium matruchotii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 86)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 86)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 86)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Corynebacterium matruchotii"
                     /db_xref="taxon:43768"
     Protein         1..86
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8806
     Region          1..86
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mdihyfaaar aarglaheri tttaatlael vdelgrlpga gttdsglsla qvlsrcsflv
       61 dgrhanmdta isaaervdvl ppfagg
//
LOCUS       WP_005528247             306 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Vibrio campbellii].
ACCESSION   WP_005528247
VERSION     WP_005528247.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..306
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34209
     Region          12..268
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mentalkcls nhgktwrfas fllskqqveq aarlyyfcrc iddiadgtad kqlafeslee
       61 vqrqlslgks depfvddflq lssqldipvm haftlvrgvq sdidsvliqs eceliqyayr
      121 vagvvglmmc pilkadnkgm pyaidlgial qltniardvl edaemgrryl pyqwcpiape
      181 diasderdsv rstvsaaivr lltladqyys sarqgyqflp ppsrraiiva esvyrqigvk
      241 lrkrglqywk grtvvtpfsk vavamsalst saleateghd tclhqplvvl seykkfrsef
      301 dgntqs
//
LOCUS       WP_005529269             149 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Vibrio campbellii].
ACCESSION   WP_005529269
VERSION     WP_005529269.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (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   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..149
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16813
     Region          76..143
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mldvppiitq lfsvwknetq dpkladqyid vlidqcsrca ptthpfvaqg smdrrlliii
       61 ealsdkptik msisqlsqkt gasvrtlnrl flshfkasfk eirnkvvmer aeqmmkkgis
      121 atvvafeley sslssfstay nkhqkqnmd
//
LOCUS       WP_005530477             236 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Vibrio campbellii].
ACCESSION   WP_005530477
VERSION     WP_005530477.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..236
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25084
     Region          <13..>132
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mshtnldlnw ifgtseddnm tgtkgsdtsd vfigfggddk fvgfggddyv fggwgddtll
       61 ggrgndllvg gsgndylsgg lgndslfggc gddiifdysg nnfinagwgn dtvvvgdgns
      121 viaggcgsdt fvmtnrlaig vpdqpvssnd ievkaeildf nichdklvfd mgldtnddgi
      181 rdtfldsadd ltlsyndfgw avfssdefnv evtlkgidag ymnyiehyni difdfa
//
LOCUS       WP_005530517             363 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Corynebacterium striatum].
ACCESSION   WP_005530517
VERSION     WP_005530517.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 363)
  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 363)
  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
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 363)
  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   5  (residues 1 to 363)
  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   6  (residues 1 to 363)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 363)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 363)
  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 18263812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..363
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38602
     Region          19..68
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          83..345
                     /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 mlkpgpvftr prtpaakclh lvrlnpiitr selveatgls qptitrataa llqkglvqer
       61 ndltrsrgrg rptvplevae nnwilagiav gtsqthigfy dtmgrtired dvstpvaqls
      121 eedfiehima gvnrlmtgld rklvsvgvtt sgtvdnegri tasnlgwenv diaerlrfqf
      181 gvpvvvssai pailgsetqa aelgntdpvl vlfaddsiga alsandevsq iiplpatsql
      241 adpeesltta avlrklgrtg tlaeavaaaa nnpaerkild drarqlgeia allvneyqpa
      301 tvvvagsafl ddpaapklfa aavrekagrs tqlrvipslk eivraitrai aldpllrvpl
      361 elf
//
LOCUS       WP_005502078            1136 aa            linear   BCT 20-JAN-2025
DEFINITION  chromosome segregation protein SMC [Shewanella benthica].
ACCESSION   WP_005502078
VERSION     WP_005502078.1
KEYWORDS    RefSeq.
SOURCE      Shewanella benthica
  ORGANISM  Shewanella benthica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 1136)
  AUTHORS   Cobbe,N. and Heck,M.M.
  TITLE     The evolution of SMC proteins: phylogenetic analysis and structural
            implications
  JOURNAL   Mol Biol Evol 21 (2), 332-347 (2004)
   PUBMED   14660695
REFERENCE   2  (residues 1 to 1136)
  AUTHORS   Jessberger,R.
  TITLE     The many functions of SMC proteins in chromosome dynamics
  JOURNAL   Nat Rev Mol Cell Biol 3 (10), 767-778 (2002)
   PUBMED   12360193
REFERENCE   3  (residues 1 to 1136)
  AUTHORS   Harvey,S.H., Krien,M.J. and O'Connell,M.J.
  TITLE     Structural maintenance of chromosomes (SMC) proteins, a family of
            conserved ATPases
  JOURNAL   Genome Biol 3 (2), REVIEWS3003 (2002)
   PUBMED   11864377
REFERENCE   4  (residues 1 to 1136)
  AUTHORS   Strunnikov,A.V. and Jessberger,R.
  TITLE     Structural maintenance of chromosomes (SMC) proteins: conserved
            molecular properties for multiple biological functions
  JOURNAL   Eur J Biochem 263 (1), 6-13 (1999)
   PUBMED   10429180
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11493846
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1136
                     /organism="Shewanella benthica"
                     /db_xref="taxon:43661"
     Protein         1..1136
                     /product="chromosome segregation protein SMC"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003682 - chromatin binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0030261 - chromosome condensation
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=127105
     Region          2..1126
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
ORIGIN      
        1 mrlkqiklag fksfvdstti pflsplsaii gpngcgksni idavrwvlge ssakhlrgds
       61 madvifngst arrpvsvasv elnfenldgr ltgeyssyqe ivvkrqvsrd gdsnyflngq
      121 kcrrkditdl fmgtglgprs yaiieqgtis klieskpqel rvfieeaagi srykerrret
      181 eirirhtren lerlgdirne lghqldklae qataakqyre lkqserqlds ellvsrylel
      241 tdqteiltld vnrlelakae veaekehtel eltrlnvqlv eldgeeqkrv esfylsgtqi
      301 akleqdlkhr qqqdshveqr isgiaqklkq hkdtlsaaea sqqalredla lkqpqfelay
      361 ssltrvtsdl sehelkvses raklaehkek vssyrlahev srgklshqgv mleqtraqlt
      421 sieqeaagll eqeaakieqd nqsrltqwqs damergeind ehddklselv qaqinlkakq
      481 ealgqslaee rgrlalvtkl lpddvsqega kalwqlievq pgwekaveli fdgllkmpag
      541 vdkgefgfeg rkhqqwpgvs snanlspwls qvqwadsleq areqvvgise hqrivtadgy
      601 llgrgfvikk gtdsgslvql kceqealeas idgsksllse lnrqghdlda qikplkiels
      661 sgietlqqln vaiaslsvqi eadkqrnqer nrrrehldse larlksllnk lqegevsila
      721 rlneaqsslk qgeqvqtslv qgleelvdsr rickdqyqql qrddrelsqv cqtlttklal
      781 neqsidqqgv rieeltlaks alehqlveqs vasedgrlss lkeqlgqala qqqtkqaela
      841 slraqqtqlq essdsagitk kqqlgkienl tqsistlklr reglkgqads qlmqfkeqdi
      901 eleqvksald lnisaqtrqr eleriraqii hlgainlaai eeyeqrserk nyldsqdadl
      961 tsalssleea irkidketks rfkdtfdkvn kdlgllfpkv fgggsaelal thddlletgv
     1021 timarppgkk nstihllsgg ekaltalslv faifrlnpap fcmldevdap lddanvdrfc
     1081 rlvkemsqsv qfifishnki tmeladqlig vtmhepgvsr ivavdideav aladag
//
LOCUS       WP_005530830             262 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Vibrio campbellii].
ACCESSION   WP_005530830
VERSION     WP_005530830.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 262)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            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="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=29820
     Region          28..255
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mmsitqllgc iskqldgqyi ahykqltlrs vfqpiyqkdl siiglealvr isnqdgqmir
       61 pdqffqsnti pvkdqinver lsrlihisnf cqskfsnkkl flnvlpkase mlakdmsysn
      121 llkqaiiead lrreqivmel veldasdenc lykatkelsd ngymlaiddy gvdastverv
      181 kcvrpniiki drslllryes gdfaclmeal slakdirskt viegietehq lnlmkklgfd
      241 myqgyllamp qtleayqevk ta
//
LOCUS       WP_005530862             293 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Corynebacterium striatum].
ACCESSION   WP_005530862
VERSION     WP_005530862.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 293)
  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 293)
  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   3  (residues 1 to 293)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..293
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33099
     Region          <18..54
                     /region_name="TroA-like"
                     /note="Helical backbone metal receptor (TroA-like domain).
                     These proteins have been shown to function in the ABC
                     transport of ferric siderophores and metal ions such as
                     Mn2+, Fe3+, Cu2+ and/or Zn2+. Their ligand binding site is
                     formed in the interface between...; cl00262"
                     /db_xref="CDD:469696"
     Region          161..254
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mdkglvsglt ksqlathikh grvtkiargl nvwgrptple vlwavqqryp qavatgrtaa
       61 qlylkrevtl plelaapkrl pastyysarr svreqtrevl gcavqnplla laqidwgcgi
      121 elcealyagh rgrekleadr aeisslsara qellrsavlf tdssaeiava ralqqaglki
      181 ecnvfigvyr wdivipsrki aieinglkfh selgvwirdh wknneavlrg wrtlrytghc
      241 vahhldyive qvaqppnwsr rfysfvhlwh kallpkqeya lppepewvhe isp
//
LOCUS       WP_005531384             523 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein/permease
            [Corynebacterium].
ACCESSION   WP_005531384
VERSION     WP_005531384.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..523
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=54096
     Region          3..523
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 maapldprlm rlvppvrgli lrtgsfqald tvlviargvl igtvaartit sdahlrelwp
       61 lllavlavvl lhaaaawass raqahavgkt vdalrmrtlr alatrdprvv qeesgqwrhv
      121 ltrgmedfrp ylsqflpalv avciatpaal vtiayfdwvs avfalvtlpl ipafmvliga
      181 ltaqhtqrrl avtaglggql adlvrgaptl ralhatkqpt rsvgslgerh skatmgvlrl
      241 aflssfalef latlsvalva vniglrlvtg siellpalvv liivpevfnp vravgssfha
      301 aadgleaaqm llgvidsaaa kpevtggyrt lagsevsvsh vsisgrdgmr pqdltfkarp
      361 galtvlsgan gsgkstvlla llgalpdaav tgtvrlppgs aylaaspalv tgtvaenlal
      421 tdatdsalaa aqdavplgvg hahdvatggt gisagqrerv givrtlavda pcylldepta
      481 hlspelvtnv iaalqaraha gavvlvashd prliakadev iel
//
LOCUS       WP_005531851             507 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Vibrio campbellii].
ACCESSION   WP_005531851
VERSION     WP_005531851.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 507)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..507
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=57558
     Region          247..483
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mmlvavlsfc vtmlalipfs hkhhkkltee atltiesefy dyvahlthll dddfflkscd
       61 dlihdlrasi fglgmakdia ifdpsgkvsc msserhpsfs iyspvltrlg dsaghttlaf
      121 tqrvltnnqa lflfftkqhg rgisvvfpke llevlisdif rfgnidyrie imektvissv
      181 kshqlrfekv sssvlpftvy saisypfyfq fllskfwvgl lgmacalfih lyfssrkfak
      241 nslefslsra ikernltvhy qpivdqrdgs viggeslvrw ddpvqgfisp sifiplaekv
      301 gliehitylv ldkvismins nkiafddryi svnvcrslil radfirqves rlkynyfise
      361 hlvfeiteea iftgselvil rqhldrltal giriavddfg tgysgldfis qysfdiikid
      421 rvfvnnlgng qtiqplleai ytltktlgma vivegvedln qlkilrnlgf yniqgfyfsq
      481 plpkldfldy lnvkpttafk eckstai
//
LOCUS       WP_005531976             178 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Corynebacterium striatum].
ACCESSION   WP_005531976
VERSION     WP_005531976.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..178
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=19708
     Region          <81..152
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mkhyylaglc avsalwalnf wapgpplgvs ttpervrilg ydrelfggwl pstkdtvraa
       61 qttpmgladp ysglhnppav eidhvfplsa awdmgawgwd nkrkakfand plnlvatdka
      121 lnqaksdslp sewlppanrc dysrrlaava rkydlplpaa dvrtmrrqcr fdfrlpng
//
LOCUS       WP_005532379             157 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Vibrio campbellii].
ACCESSION   WP_005532379
VERSION     WP_005532379.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..157
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17154
     Region          4..151
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mnieqyqrlt kqavaliese kdyianlsni sallfmelen lnwagfyltk gdelvlgpfq
       61 gkpacvripm grgvcgtaaq tnsvqrvydv hefeghiacd aasnseivip ftingevagv
      121 ldidspnigr fneideeglt yfmaevekll nshanda
//
LOCUS       WP_005533719             145 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Vibrio campbellii].
ACCESSION   WP_005533719
VERSION     WP_005533719.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..145
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15431
     Region          8..>99
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mirisgcngy nkrfrgmtli elliavvivg iiaaiaypsy snhaitahrt valsdisriq
       61 lelettyngg ydwsgiisgg scticdsdad rfsfsiassa taaytitata ksdrgqdgds
      121 cfpssqdkki tltstniesp secwn
//
LOCUS       WP_005534069             153 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Vibrio campbellii].
ACCESSION   WP_005534069
VERSION     WP_005534069.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            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="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16755
     Region          5..153
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mleafnaafe nlalwfsdsa lwvlfmtgfl satllpggse agliatlsln qysvssiiiv
       61 atigntlggl tnywlglwip nktqdekhah talkwlseyg ywglffswlp vigdplclaa
      121 gwlrmkflpc lvliflgkaa rysllaaiyl glf
//
LOCUS       WP_005535749             673 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Vibrio campbellii].
ACCESSION   WP_005535749
VERSION     WP_005535749.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 673)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 673)
  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 673)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..673
                     /product="M4 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=74272
     Region          1..608
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mrnvtllslv pfafasqaaq ivehsqtdis ealniagkss ympastelsy qninrveigq
       61 qtlvrkqqlh ygvpvyghsv vadlsakgfa qsidgnvvvg idndldstlp misanqaiei
      121 atgteqgfas nespendara elmvwldeqn tahliykvda vkivnlrpsr pitlvdaksg
      181 eimdqwegla fleaegpggn qksgryyfgp ntkfggfqvd qycqmnsdnv etinmnnqqw
      241 ggqvhrfncn vnnyreinga yapmndahyf gqrvfdmyre wlgarpiqqk ltmrvhygsn
      301 ygnafwdgrq mtfgdgnssm yplatwdvia hevshgfteq nsgleyrgms ggmnesfsdv
      361 aaaalsqyvh gsfnwkmgeh vmkyspamry finpshdgas ighvnqyyrg idvhhssgif
      421 nkafyhlats sgwsikkafm ayatanqlyw tpnstfqqga egvckaaqkl gyessavtsa
      481 fsqvgvqvmn cesgqpnpnp npgpdtgmne lslnmpvaiq snaageqqfv lrrtssddvw
      541 vqtyngfgnv elyvaidrpa tpsdydcsst nmgneeacgf ggiqgsdiyv tvtntqsasd
      601 aylavsetyg tpqpnpepqd qcaslqewsp ynyypagssv kywgnrfvat qdnwgadpfq
      661 nywfwtfegs cnd
//
LOCUS       WP_005536063             270 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio campbellii].
ACCESSION   WP_005536063
VERSION     WP_005536063.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 270)
  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 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   3  (residues 1 to 270)
  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   4  (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   5  (residues 1 to 270)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..270
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_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          16..268
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <174..268
                     /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 msnpdnpkap lhkeimlpkp aelitlpsym echdhaytqi viglkgqaef evrgqgnlvg
       61 pgqgcivtas sdhafggvih qsdilvlnmp kpanddseml qkinnlersh lyfqldgqiq
      121 kliqmlvqem rnhpddllls racndtvial mqrhisafet srkesrfdld aidryieqhl
      181 shkisvaqla gsvflgesqf hslfkdqmgi tphqyvlgkr idmardlieq ghltlgqiae
      241 ftgfssqstf thtftrlqgl spsqykkqvg
//
LOCUS       WP_005538877             278 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Aggregatibacter
            actinomycetemcomitans].
ACCESSION   WP_005538877
VERSION     WP_005538877.1
KEYWORDS    RefSeq.
SOURCE      Aggregatibacter actinomycetemcomitans
  ORGANISM  Aggregatibacter actinomycetemcomitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Aggregatibacter.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Aggregatibacter actinomycetemcomitans"
                     /db_xref="taxon:714"
     Protein         1..278
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30629
     Region          1..266
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mtkydlhchs tasdgvlspt evvlrahekg vnvlaltdhd tvagvlearq qaeksgirli
       61 ngveistvwe nrsihivglg fdishekmta llteqarlrd iraqeigekl ekigvenaya
      121 earklagege vtrahyarhl vqigkvsndg qafkrylgqg ksayvkpqwa dipttidiih
      181 qaggaavlah plrytmtmkw vrklaenfks wggdameisg cgqrpdqfql lvklaeehql
      241 agsmgsdfhf pcawvelgkl kplpehipfv ldikndla
//
LOCUS       WP_005539045             271 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Johnsonella ignava].
ACCESSION   WP_005539045
VERSION     WP_005539045.1
KEYWORDS    RefSeq.
SOURCE      Johnsonella ignava
  ORGANISM  Johnsonella ignava
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Johnsonella.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Johnsonella ignava"
                     /db_xref="taxon:43995"
     Protein         1..271
                     /product="formate/nitrite transporter family protein"
                     /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=28912
     Region          1..271
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mlstkevmek yvslgenkvn tpflktllla viagffiala gvganaaiat ienpsiakli
       61 savvfpagls mvscagcelf tgdslivisl ldkkikfssm lkcwiivyig nligsvlial
      121 lasaskqlsl ydsklavmti siavkktsls fsqglflgig cnflvciavl ialsanstad
      181 kiagvffpil lfvvsgfehs vanmyyipag iiakmnpeyl rlavekgiev drlnissfll
      241 knllpvtign liggtlvgll ywyiylrkvk k
//
LOCUS       WP_005540307             578 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Aggregatibacter
            actinomycetemcomitans].
ACCESSION   WP_005540307
VERSION     WP_005540307.1
KEYWORDS    RefSeq.
SOURCE      Aggregatibacter actinomycetemcomitans
  ORGANISM  Aggregatibacter actinomycetemcomitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Aggregatibacter.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Aggregatibacter actinomycetemcomitans"
                     /db_xref="taxon:714"
     Protein         1..578
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=65537
     Region          7..504
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mtkqkleltw igkhkrpkle arilledaek syhvkvrsen dvfdnrlifg dnllalkale
       61 qefagkvkcv fidppyntgs afthyddgle hsiwlglmrd rleiikrlls ddgslwitid
      121 dneahylkvl cdevfgrrnf vvnaiwvkks apqndakwis dthdhvfvya knkeiwkink
      181 lsrtekqnsi yknsddfdgv nesgewygrg pwyadnitvk tvsqtgiyev vtpggrkvlp
      241 pdgrawaysk erfwelikdn riwfgkdgkn kptvkrflse vgdkgvvpks vwdytevgen
      301 rnarqevmkf nsidpfstpk perfierilt iatnpgdlvl dsfagsgttg avahkmgrrw
      361 imvelgehch thiiprlqkv idgedqggis kavnwqgggg fryfrlaptl ivndkwgnqi
      421 inpdynpeml aealaklegf tympsenlww qhgyssesdf iyvttqtlta eqlqalsdev
      481 ganrsllicc sawrgitaek aaerfpnlsl kkipkmilar cewghddysl nvanlpmaet
      541 epektprsse nkpaaktkak kaksavenqg glfdgeda
//
LOCUS       WP_005541391             571 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Johnsonella ignava].
ACCESSION   WP_005541391
VERSION     WP_005541391.1
KEYWORDS    RefSeq.
SOURCE      Johnsonella ignava
  ORGANISM  Johnsonella ignava
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Johnsonella.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 571)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Johnsonella ignava"
                     /db_xref="taxon:43995"
     Protein         1..571
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=64000
     Region          23..554
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mlingallkl aknlkkhiis vsllscfiga vtvfqafyls kvinaiferp dkimyyficf
       61 lfavflqmvl rypanmlsis seasikldir ntlldriygl glakltders gklctllldr
      121 iealapyysi ylpnlitvlf vsmgciiyig sinlnvclta ligilgmlit paftykylwg
      181 sgtevwkeyd kfgsdfldni qgmktlknlk ackirrqeml riskeihkkt mnhmkittie
      241 nflfelsani gsvlsvvyav ylsasghina gsvvfvlfmi rncfipvysl mlawhvgyng
      301 itasseieni lkeeipvwke nfdfadtntl strrlsfsyn nhdvilnnid ldlkpgktya
      361 fvgksgegks tlvsllagly pytsgeiwfk nlpltldtvs rwrenisavw qnpyvfngtl
      421 kdnllfakpd atdteinaai keanledila klpygidtel gengsilsgg ekqrlaaarc
      481 flknteilif deatssldek nqgfiqesie llkkgktaii iahrlstvkn adiiymidgg
      541 riiasgthee lynncqtyhn lvksqedgne k
//
LOCUS       WP_005541934              87 aa            linear   BCT 20-JAN-2025
DEFINITION  zinc ribbon domain-containing protein [Johnsonella ignava].
ACCESSION   WP_005541934
VERSION     WP_005541934.1
KEYWORDS    RefSeq.
SOURCE      Johnsonella ignava
  ORGANISM  Johnsonella ignava
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Johnsonella.
REFERENCE   1  (residues 1 to 87)
  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 10577258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Johnsonella ignava"
                     /db_xref="taxon:43995"
     Protein         1..87
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=9964
     Region          5..86
                     /region_name="Zn_ribbon_2"
                     /note="Putative zinc ribbon domain; pfam12674"
                     /db_xref="CDD:463667"
ORIGIN      
        1 mdtkycqcca mpigegtdly gtnsdgsvne dyckycfekg dftfkgtmee mieicvphvv
       61 eankdmdeds arkmmmeffp tlkrwke
//
LOCUS       WP_005544852             191 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Aggregatibacter actinomycetemcomitans].
ACCESSION   WP_005544852
VERSION     WP_005544852.1
KEYWORDS    RefSeq.
SOURCE      Aggregatibacter actinomycetemcomitans
  ORGANISM  Aggregatibacter actinomycetemcomitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Aggregatibacter.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Aggregatibacter actinomycetemcomitans"
                     /db_xref="taxon:714"
     Protein         1..191
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21577
     Region          3..164
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mklfgamydk tmqwskhrfa pfwlsfvsfi eaiffpippd vmlipmsmsk pqsavkfamf
       61 tatasvlggm igyalgyyaf nlvehyitqw gyqaswqtti hwferwgmlv vfvagfspip
      121 ykvfticagv mqmafipfvi tafisrtarf llvaklaawg gekfaaklrk siefigwsvv
      181 alavvaylil r
//
LOCUS       WP_005545912             438 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Paenibacillus alvei].
ACCESSION   WP_005545912
VERSION     WP_005545912.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus alvei
  ORGANISM  Paenibacillus alvei
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Paenibacillus alvei"
                     /db_xref="taxon:44250"
     Protein         1..438
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=50161
     Region          10..433
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 misdmtilhd lqaeqavigs ifldpaaind vmflsdrdfa naqhrlifqv mlnlskreip
       61 idiitvteef kkfnrvqdmg svsylshlan saptaaniqy ygqivrskai rrraveygnk
      121 linmagedfe tdedflaave eevlelrpis fsrmrsmkes kkdyfehlkt kaaklqtglf
      181 nqfdewaqlw rgwlyvlagr pgvgktakal mlgygiaknn pgagtvmiws qemdenevkd
      241 rlvsmiagvn yprlirkggd dgftpeewkk idaayseiek lplyiqdsag vtideiratv
      301 kqfkkrhgkv aavivdylqi meipqkknet raqaigkvtr taktlarrnk mvfillsqld
      361 rsvdneepkl rhlkesgsie qdadvveflw ynhndqpern kkiidsifak grnvgtnrfr
      421 ldfqwwyqkf veipkktp
//
LOCUS       WP_005547361             453 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Paenibacillus alvei].
ACCESSION   WP_005547361
VERSION     WP_005547361.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus alvei
  ORGANISM  Paenibacillus alvei
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Paenibacillus alvei"
                     /db_xref="taxon:44250"
     Protein         1..453
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=49949
     Region          255..315
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 msnmrakmtf rfddsnqgkd klerqgmetn qkserltdwe elsdgtivns iepdrtgqae
       61 heeyseaitv enrhiekaes dilpvkpihe pveneherve rwiretdhqp gyeipkngys
      121 lsssiedpas gslsdqgell wngvhtrsrk ppvwrviasv agalatgalf gflalslfkg
      181 evsmpnpnna ipvfandkqg kggessahgt atneqskvka gdttskpssa asgggsaata
      241 tglyvtdvni pekvfymlqy gvfaqeegaq kaaselrelg maamaeksdq hrvyaaiats
      301 kedamglssl lknkqmelyv rtlnrpaiak lafqgdsasv eqflgqsdvv ndwlmtqsiv
      361 ylekanteaf sqeiteqlrk dhqkwtqqms avqkgipdqs ktswtelvqs mntaisavne
      421 ynkqpssshl wsiqqavmhy rnaeaawlet mkv
//
LOCUS       WP_005547407             288 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Paenibacillus].
ACCESSION   WP_005547407
VERSION     WP_005547407.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 288)
  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 288)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 288)
  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   4  (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   5  (residues 1 to 288)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..288
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33861
     Region          37..282
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <166..278
                     /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 mntiadirpy iraahmynyr gtreeqlrrg ysyafhlfld ghghmtiddh ryavsngtli
       61 fvrpgqwhsf ehapnetmna cniycdlwea pppnqptfay ewdefdpkwl taqkpctele
      121 slptctslrp ypyfielvkh vlaaynrrgc ytkqaasasf yswliqwyda srlpnpsdyr
      181 iarilermde hpeqrhsvdy wcsecgleks qfyrlfkqet gispktyllq armkkaavll
      241 mesrqsitei almlgydsih yfsnqfscvy gisptlyrtn nsyhkmdr
//
LOCUS       WP_005547917             399 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Paenibacillus alvei].
ACCESSION   WP_005547917
VERSION     WP_005547917.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus alvei
  ORGANISM  Paenibacillus alvei
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Paenibacillus alvei"
                     /db_xref="taxon:44250"
     Protein         1..399
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43747
     Region          1..283
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          280..370
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrilhtadwh fgrtlegrsr lneqaafvde fvqladeeqa dliliagdiy dsvnppaaae
       61 qlfyeaaarl srsgqrpvvi isgnhdhpdr lsasaplvhe lgvtligqpt leavtihcar
      121 tgedaviagl pypsearlge lltssneehe lrsaysakvg qllqrqamhf rpsavnlims
      181 hlyvlgglet dserpiqvgg aytvdpsvfa clgapaapqy salghlhrpq avkgpgviry
      241 sgsplgysfs eagqaksvtl ldlapgmeam pqerflssgk pliewnvrgg yeevlrwiee
      301 grdagawldv rihltealtm eqiqklrrih egivnirpiy peieriaaee grrselpvhe
      361 lfrrfyerqt ggakpddalv dcfleliged glekegega
//
LOCUS       WP_005548119             161 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Aggregatibacter actinomycetemcomitans].
ACCESSION   WP_005548119
VERSION     WP_005548119.1
KEYWORDS    RefSeq.
SOURCE      Aggregatibacter actinomycetemcomitans
  ORGANISM  Aggregatibacter actinomycetemcomitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Aggregatibacter.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Aggregatibacter actinomycetemcomitans"
                     /db_xref="taxon:714"
     Protein         1..161
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=18258
     Region          8..161
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mldlfswdww qslfgehrlw imfasaflss tvlpgnseii fltiaapllw sgyhhfsiev
       61 qsllwvavig ntlgslttyv lgrwlpafnk ppqnaelawt lektqrygsl vlffswlpii
      121 gdvfcavagw lrlnwlaclv fialgkivry vfllflgvaf l
//
LOCUS       WP_005548233             315 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Paenibacillus alvei].
ACCESSION   WP_005548233
VERSION     WP_005548233.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus alvei
  ORGANISM  Paenibacillus alvei
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Paenibacillus alvei"
                     /db_xref="taxon:44250"
     Protein         1..315
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34044
     Region          31..282
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mnkrsddiqa eetmlyapqg aggsseehgg adlhthtias dgmttpaynv klaylaglha
       61 vaitdhdtvl gvpeavaage qygvqvvpgv eistvedgid ihvlgyfldi sntkllerla
      121 elravrdrrn emlvakltel gipltmeevv selgrplspg etvgrphiad alvrrgivqn
      181 mkeafdeylg aggkayvnpp rirsqeavaw ihdaggaavm ahpgiyhrdd lvvrlldaap
      241 wdgievwhsd hsaedakryk emacargllq tagsdfhgar kgdvfhgalg grrvktdvvr
      301 elqeraqrvr aerss
//
LOCUS       WP_005548420             109 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Aggregatibacter
            actinomycetemcomitans].
ACCESSION   WP_005548420
VERSION     WP_005548420.1
KEYWORDS    RefSeq.
SOURCE      Aggregatibacter actinomycetemcomitans
  ORGANISM  Aggregatibacter actinomycetemcomitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Aggregatibacter.
REFERENCE   1  (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   2  (residues 1 to 109)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Aggregatibacter actinomycetemcomitans"
                     /db_xref="taxon:714"
     Protein         1..109
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11210
     Region          39..107
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkamkhllas lfvlgsvfag savaaekaae pavqteqpaa taavgekvni ntasaaeiqk
       61 alvgigakka eavvqyrekh gnfsaveqll evqgigkatl eknrdrial
//
LOCUS       WP_005549088             235 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Paenibacillus alvei].
ACCESSION   WP_005549088
VERSION     WP_005549088.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus alvei
  ORGANISM  Paenibacillus alvei
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 235)
  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 18524722
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Paenibacillus alvei"
                     /db_xref="taxon:44250"
     Protein         1..235
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=26195
     Region          49..155
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
     Region          166..232
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 msvyrlkitc lrllsiflli hlgidmldhn laraqpirtv qsdpnafsiv ifphlhrlvv
       61 mkngistksy hiavgnpttp tpagefriif kgenwgpsfg prwlglnvsw ghygihgtnk
      121 phsigrhvsh gcirmrnkdv melyemipig tkvvimghvl gdlkhdprnl aegdaggdvq
      181 liqsrlqsag yftgrcdgkf rsnttsalkr yqrdhqltqd gvvtfaiyih lglie
//
LOCUS       WP_005552848             191 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Aggregatibacter actinomycetemcomitans].
ACCESSION   WP_005552848
VERSION     WP_005552848.1
KEYWORDS    RefSeq.
SOURCE      Aggregatibacter actinomycetemcomitans
  ORGANISM  Aggregatibacter actinomycetemcomitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Aggregatibacter.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Aggregatibacter actinomycetemcomitans"
                     /db_xref="taxon:714"
     Protein         1..191
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21545
     Region          3..164
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mklfgamydk tmqwskhrfa pfwlsfvsfi eaiffpippd vmlipmsmsk pqsavkfamf
       61 tatasvlggm igyglgyyaf nlvehyitqw gyqaswqtti hwferwgvlv vfvagfspip
      121 ykvfticagv mqmafipfvi tafisrtarf llvaklaawg gekfaaklrk siefigwsvv
      181 alaviaylil r
//
LOCUS       WP_005553124             578 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Aggregatibacter
            actinomycetemcomitans].
ACCESSION   WP_005553124
VERSION     WP_005553124.1
KEYWORDS    RefSeq.
SOURCE      Aggregatibacter actinomycetemcomitans
  ORGANISM  Aggregatibacter actinomycetemcomitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Aggregatibacter.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Aggregatibacter actinomycetemcomitans"
                     /db_xref="taxon:714"
     Protein         1..578
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=65525
     Region          7..504
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mtkqkleltw igkhkrpkle arilledaek syhakvrsen dvfdnrlifg dnllalkale
       61 qefagkvkcv fidppyntgs afthyddgle hsiwlglmrd rleiikrlls ddgslwitid
      121 dneahylkvl cdevfgrrnf vvnaiwvkks apqndakwis dthdhvfvya knkeiwkink
      181 lsrtekqnsi yknsddfdgv nesgewygrg pwyadnitvk tvsqtgiyev vtpggrkvlp
      241 pdgrawaysk erfwelikdn riwfgkdgkn kptvkrflse vgdkgvvpks vwdytevgen
      301 rnarqevmkf nsidpfstpk perfierilt iatnpgdlvl dsfagsgttg avahkmgrrw
      361 imvelgehch thiiprlqkv idgedqggis kavnwqgggg fryfrlaptl ivndkwgnqi
      421 inpdynpeml aealaklegf tympsenlww qhgyssesdf iyvttqtlta eqlqalsdev
      481 ganrsllicc sawrgitaek aaerflnlsl kkipkmilar cewghddysl nvanlpmaet
      541 epektprsse nkpaaktkak kaksavenqg glfdgeda
//
LOCUS       WP_005556103             278 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Aggregatibacter
            actinomycetemcomitans].
ACCESSION   WP_005556103
VERSION     WP_005556103.1
KEYWORDS    RefSeq.
SOURCE      Aggregatibacter actinomycetemcomitans
  ORGANISM  Aggregatibacter actinomycetemcomitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Aggregatibacter.
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   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   4  (residues 1 to 278)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Aggregatibacter actinomycetemcomitans"
                     /db_xref="taxon:714"
     Protein         1..278
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=31282
     Region          9..276
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mkinrtpfie frgvskyydg qhavqtlnlt iyqgeffvlv ggsgsgkstt lrminaltep
       61 tdgdvyfqgk rikdynihtl rhrigyvlqq ialfptmtva qnialmpdil gwhknerksr
      121 vntllelvnl ppaqyqdryp relsggeqqr igilraiaan phlllmdepf saldplvrta
      181 lqdqislihk kfgttivfvt hdmqealkla crigvmqngk lvqvgtpnei qqqpansyvk
      241 slfasseqal tvekvimqye qlskaeqasv rkwlarns
//
LOCUS       WP_005557355             109 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Aggregatibacter
            actinomycetemcomitans].
ACCESSION   WP_005557355
VERSION     WP_005557355.1
KEYWORDS    RefSeq.
SOURCE      Aggregatibacter actinomycetemcomitans
  ORGANISM  Aggregatibacter actinomycetemcomitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Aggregatibacter.
REFERENCE   1  (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   2  (residues 1 to 109)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Aggregatibacter actinomycetemcomitans"
                     /db_xref="taxon:714"
     Protein         1..109
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11346
     Region          39..107
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkamkhllas lfvlgsvfag saaaaekaae pavqmeqptt tatvgekvni ntatateiqk
       61 alvgigakka eavvqyrekh gnfsaveqll evqgigkatl eknrdrial
//
LOCUS       WP_005540395             428 aa            linear   BCT 20-JAN-2025
DEFINITION  galactokinase [Johnsonella ignava].
ACCESSION   WP_005540395
VERSION     WP_005540395.1
KEYWORDS    RefSeq.
SOURCE      Johnsonella ignava
  ORGANISM  Johnsonella ignava
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Johnsonella.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   McAuley,M., Kristiansson,H., Huang,M., Pey,A.L. and Timson,D.J.
  TITLE     Galactokinase promiscuity: a question of flexibility?
  JOURNAL   Biochem Soc Trans 44 (1), 116-122 (2016)
   PUBMED   26862196
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Holden,H.M., Thoden,J.B., Timson,D.J. and Reece,R.J.
  TITLE     Galactokinase: structure, function and role in type II galactosemia
  JOURNAL   Cell Mol Life Sci 61 (19-20), 2471-2484 (2004)
   PUBMED   15526155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Johnsonella ignava"
                     /db_xref="taxon:43995"
     Protein         1..428
                     /product="galactokinase"
                     /EC_number="2.7.1.6"
                     /GO_function="GO:0004335 - galactokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0005534 - galactose binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0046835 - carbohydrate phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=47389
     Region          34..393
                     /region_name="GalK"
                     /note="Galactokinase [Carbohydrate transport and
                     metabolism]; COG0153"
                     /db_xref="CDD:439923"
ORIGIN      
        1 mdisknmkmi rstdcrvlfr klygtkkaea aalryeniid vfvkryksqd fqlfsspgrv
       61 eiggnhtdhn fgkvlggsit fdiaaaaaan qtpivniyse rfgeitisls alesnktykg
      121 srelakgvlr almemgykvg gfdayldssi iksagvsssa afenilcqiv stlfnqgsie
      181 prtyayagqf aeniywkkas glldqltcgi ggilainfvn pedplirkid fsfeacgyni
      241 ilvqtgnehe dfkeeysaip hdmkkiagyf gykglgqvfe ekilfnlqsl rayagdravm
      301 ralhfyaeng rveneiealr sgnfdkfldn vkesgdsswk ylqncysikn peeqgicigl
      361 aiselfikrh krgacrvhgg gfggvimaii peeitsqyvf hmenllgkgc ayvtsirpyg
      421 saclnell
//
LOCUS       WP_005557783             161 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Aggregatibacter actinomycetemcomitans].
ACCESSION   WP_005557783
VERSION     WP_005557783.1
KEYWORDS    RefSeq.
SOURCE      Aggregatibacter actinomycetemcomitans
  ORGANISM  Aggregatibacter actinomycetemcomitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Aggregatibacter.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Aggregatibacter actinomycetemcomitans"
                     /db_xref="taxon:714"
     Protein         1..161
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=18238
     Region          8..161
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mldlfswdww qslfgehrlw imfasaflss tvlpgnseii fltiaapllw sgshyfsidi
       61 qsllwvavig ntlgslttyv lgrwlpafnk ppqnaelawv lektqrygsl mlffswlpii
      121 gdvfcavagw lrlnwlaclv fialgkivry vfllflgvaf l
//
LOCUS       WP_005559700             193 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Aggregatibacter
            actinomycetemcomitans].
ACCESSION   WP_005559700
VERSION     WP_005559700.1
KEYWORDS    RefSeq.
SOURCE      Aggregatibacter actinomycetemcomitans
  ORGANISM  Aggregatibacter actinomycetemcomitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Aggregatibacter.
REFERENCE   1  (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   2  (residues 1 to 193)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Aggregatibacter actinomycetemcomitans"
                     /db_xref="taxon:714"
     Protein         1..193
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=20819
     Region          123..191
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkslksllav avvmtvsttv faeesvftev edgaksawqt vksdaktvgg kvkegavkvk
       61 datkekfvea keatketftk akdatkekfa egkkavkdtf qyekpapved ksttkeksav
      121 enkakitrsk kvdintadaa tlenlsgige akakaiveyr ekngkfknln dlsnvpgigd
      181 atlekvkshv rfn
//
LOCUS       WP_005560300            1051 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LysM peptidoglycan-binding domain-containing protein
            [unclassified Rhodococcus (in: high G+C Gram-positive bacteria)].
ACCESSION   WP_005560300
VERSION     WP_005560300.1
KEYWORDS    RefSeq.
SOURCE      unclassified Rhodococcus (in: high G+C Gram-positive bacteria)
  ORGANISM  unclassified Rhodococcus (in: high G+C Gram-positive bacteria)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 1051)
  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 1051)
  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 11447266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="unclassified Rhodococcus (in: high G+C
                     Gram-positive bacteria)"
                     /db_xref="taxon:192944"
     Protein         1..1051
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=111382
     Region          63..221
                     /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          229..273
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
ORIGIN      
        1 msanaarsrl aglgyllilv mlvagipaal walrgnpldi pwsdfeglla spddgsllia
       61 llplvgwaaw atftvpille laatlrgvka pklrllrsqq rtatflvsga lllltagtat
      121 aapvltqpad vgstspyaph sqqedpsasp qtqvdpratr vavqpagptv ttvrgdtlwg
      181 laqqhlgegr ryaeildlnr tavpepgfla egltlqlpas qpevvrgayt vkqgdtlwdi
      241 aerelgdplr fmeittpdgt pagelitvgq qlimptaasa aadatpapal vpptdavpap
      301 apapegvpap apapeavpap apasapvdva pnwqldpvep qmpadlvtnd appetdtedg
      361 ssgvvfiglg isavaaaglt ghlalrrrkq qhrrrrgeri alpaetaiqa eqaltaaadp
      421 lttthvdial rhlahhcrst sialpgllav fvgdndielg lveqislpap wtqiddttws
      481 vdprafprsv pkaeispypa ltavgtsndg relllnleqi ghlaisgtpt atagvlrala
      541 velavspiad slhlnlvgyc adlaeaidng rithsedadt vlttlanhve ldseiladnd
      601 fesiaqarta yttseltape ivliadpvte aqagllagia rhapriafaa vttesahtna
      661 twtlevddng savlarpgaa sagitvttld eesyasvldl ltttsreprv ahkgdnpdir
      721 weaarldndi stdefitssd patfsvvgne dldhavdrpe psdsdevtae relpeadhiw
      781 irllgepavt ppspgpaegr ekslteiaal littdggvla adidskiwph dveaartgta
      841 eqekeakarl rrrrnealsr lrkwlgdtet gepaliksgd rtgrtpqrlh davttdwdyw
      901 qelvnahpad vdsarlsaal alvtgqpfss ddptaygwad htkqdmisav tdvaeefatr
      961 yirgqqvpqd laaahaaaet glkvdivheg cwraaiiath fsgdtettqr lidrmiteld
     1021 aleeepehet kmllsqldst ygshyrigav s
//
LOCUS       WP_005560523             394 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Rhodococcus opacus].
ACCESSION   WP_005560523
VERSION     WP_005560523.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus opacus
  ORGANISM  Rhodococcus opacus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Rhodococcus opacus"
                     /db_xref="taxon:37919"
     Protein         1..394
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42327
     Region          1..272
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          272..359
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrilhtsdwh igrtfhgvdl ltdqarvlda iaalvaehgm dvvvvpgdvy drsipsadav
       61 tvcnrgfeai rdagavivat sgnhdsaarl gagaafsrag glhlmttvag igspvvleda
      121 hgpvafygip ylepeitraq ldvptarsha eildaamdrv rtdldrrndt tpltrsvvla
      181 hafvvgaeat gsersisvgg vetvsasafg gvdyvalghl hspqtlaeni rysgsplpys
      241 fgerthskav ylvdldadgl rtvervdlpv vrglrqltgt vqelleddty rdaedcyvsa
      301 vltdperpvd amrslqtrfp favhlewqrp eggddlryrd kvhgrsdlqi trsfltdvrs
      361 epstgeirlv eaalgfadra gedtaevval eqta
//
LOCUS       WP_005560906             333 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Rhodococcus (in: high G+C Gram-positive bacteria)].
ACCESSION   WP_005560906
VERSION     WP_005560906.1
KEYWORDS    RefSeq.
SOURCE      unclassified Rhodococcus (in: high G+C Gram-positive bacteria)
  ORGANISM  unclassified Rhodococcus (in: high G+C Gram-positive bacteria)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 333)
  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 333)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="unclassified Rhodococcus (in: high G+C
                     Gram-positive bacteria)"
                     /db_xref="taxon:192944"
     Protein         1..333
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37197
     Region          <71..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <162..331
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          255..331
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 milndegvpp llfvqllerq aldpdalarl rnimsregtd eatliqhdvq apirwfrevy
       61 peldvdqatl lgfafaeqaq ltsfgplsfp lvsagsvaei velltylpli stalspqfhp
      121 sehgltvgft ahtsdpaldc lvvtycgsal lrlldmlagd mptvtlhlsw papplltnhe
      181 dvlagrlffd apmsflhvpa dtlnevcrfs dpltyrlaig dlqrtldqrg rttsfsekvr
      241 rlleedpgqg sshwvahels iststlkrrl seegttfrel rqsflreram lrlldrsmsv
      301 sevatelgys dltnfshafk rwtgrspnef rhp
//
LOCUS       WP_005563413             367 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-oxoacyl-ACP synthase III family protein
            [Rhodococcus].
ACCESSION   WP_005563413
VERSION     WP_005563413.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 367)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..367
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38853
     Region          21..355
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mvkrwlvmet engdlrmpfa trlagagrhl pathltttdl msttrhsthi dlerltgire
       61 rrvsvgdeds ytlaisaald clerssrdag sidvvvscsi tkfhggltqw leptmssava
      121 qaigaqgamt fdlsnacagm ltgvtvmnnw irqgiveral vvsgeyisql gqnaaqhirn
      181 imskelaslt lgdagaalll erapagsagi glagfttvad ysrlclaypk ggdpgarmft
      241 nsrgiqraai adtplllhev ldaagislhd idhvithqts arairkgmae vtatlgdspr
      301 hdavitvdry gntastthtv alveeleagr iragetvali alasgleigv vlltldeelv
      361 aryghsh
//
LOCUS       WP_005565063             338 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Rhodococcus].
ACCESSION   WP_005565063
VERSION     WP_005565063.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 338)
  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   5  (residues 1 to 338)
  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   6  (residues 1 to 338)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36897
     Region          21..202
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          101..332
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mavltrgsai srvdelitel ggdadallrs hgidplavgd fdryvryeda aavlghaare
       61 fdcldfglrl ggmqsiaslg plsvilrnae tvgeaitnvc rflgnlapad tarlttsags
      121 aiysystilh ndfdrrqtve ksqtlamnai nvmsgdrvip ikvtfqherl aplesyfdvf
      181 acpvefgqsq naihlspahl trviedrdea alalaqeyla rvhsgvalae hvrdvtrrll
      241 lvgeaglsrv aravslhert lqrelaaegt tfekildevr ratawelaat glqasqlasa
      301 lgyaeqssft racrrwyges prdllkrrrg srpedpil
//
LOCUS       WP_005568748             278 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Aggregatibacter
            actinomycetemcomitans].
ACCESSION   WP_005568748
VERSION     WP_005568748.1
KEYWORDS    RefSeq.
SOURCE      Aggregatibacter actinomycetemcomitans
  ORGANISM  Aggregatibacter actinomycetemcomitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Aggregatibacter.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Aggregatibacter actinomycetemcomitans"
                     /db_xref="taxon:714"
     Protein         1..278
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30457
     Region          1..266
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mtkydlhchs tasdgvlspt evvlrahekg vnvlaltdhd tvagvsearq qaeksgirli
       61 ngveistlwe nrsihivglg fdisheklta llaeqaclrd iraqeigakl ekigvenaya
      121 earklagege vtrahyarhl vqigkvsndg qafkrylgqg ksayvkpqwa dipttidiih
      181 qaggaavlah plrytmtmkw vrklaenfks wggdameisg cgqrpdqfql lvklaeehql
      241 agsmgsdfhf pcawvelgkl kplpehipfv lnikndla
//
LOCUS       WP_005570367             278 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Aggregatibacter
            actinomycetemcomitans].
ACCESSION   WP_005570367
VERSION     WP_005570367.1
KEYWORDS    RefSeq.
SOURCE      Aggregatibacter actinomycetemcomitans
  ORGANISM  Aggregatibacter actinomycetemcomitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Aggregatibacter.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Aggregatibacter actinomycetemcomitans"
                     /db_xref="taxon:714"
     Protein         1..278
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30510
     Region          1..266
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mtkydlhchs tasdgvlspt evvlrahekg vnvlaltdhd tvagvsearq qaeksgirli
       61 ngveistlwe nrsihivglg fdisheklta llaeqarlrd iraqeigakl ekigvenaya
      121 earklagege vtrahyarhl vqigkvsndg qafkrylgqg ksayvkpqwa dipttidiih
      181 qaggaavlah plrytmtmkw vrklaenfks wggdameisg cgqrpdqfql lvklaeehql
      241 agsmgsdfhf pcawvelgkl kplpehipfv lnikndla
//
LOCUS       WP_005572470             773 aa            linear   BCT 20-JAN-2025
DEFINITION  AAA family ATPase [Rhodococcus opacus].
ACCESSION   WP_005572470
VERSION     WP_005572470.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus opacus
  ORGANISM  Rhodococcus opacus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 773)
  AUTHORS   Liu,Y., Sung,S., Kim,Y., Li,F., Gwon,G., Jo,A., Kim,A.K., Kim,T.,
            Song,O.K., Lee,S.E. and Cho,Y.
  TITLE     ATP-dependent DNA binding, unwinding, and resection by the
            Mre11/Rad50 complex
  JOURNAL   EMBO J 35 (7), 743-758 (2016)
   PUBMED   26717941
REFERENCE   2  (residues 1 to 773)
  AUTHORS   Chen,Z., Luong,T.T. and Lee,C.Y.
  TITLE     The sbcDC locus mediates repression of type 5 capsule production as
            part of the SOS response in Staphylococcus aureus
  JOURNAL   J Bacteriol 189 (20), 7343-7350 (2007)
   PUBMED   17704228
REFERENCE   3  (residues 1 to 773)
  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   4  (residues 1 to 773)
  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
REFERENCE   5  (residues 1 to 773)
  AUTHORS   Hopfner,K.P., Karcher,A., Craig,L., Woo,T.T., Carney,J.P. and
            Tainer,J.A.
  TITLE     Structural biochemistry and interaction architecture of the DNA
            double-strand break repair Mre11 nuclease and Rad50-ATPase
  JOURNAL   Cell 105 (4), 473-485 (2001)
   PUBMED   11371344
REFERENCE   6  (residues 1 to 773)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..773
                     /organism="Rhodococcus opacus"
                     /db_xref="taxon:37919"
     Protein         1..773
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=80786
     Region          3..>656
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          7..182
                     /region_name="AAA_23"
                     /note="AAA domain; pfam13476"
                     /db_xref="CDD:463890"
     Region          <648..762
                     /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            685..694
                     /site_type="other"
                     /note="ABC transporter signature motif"
                     /db_xref="CDD:213222"
     Site            713..718
                     /site_type="other"
                     /note="Walker B"
                     /db_xref="CDD:213222"
     Site            721..724
                     /site_type="other"
                     /note="D-loop"
                     /db_xref="CDD:213222"
     Site            743..749
                     /site_type="other"
                     /note="H-loop/switch region"
                     /db_xref="CDD:213222"
ORIGIN      
        1 mlrlksleit nirsvehvtl nvdpdgttal ygpsgvgksg ildalpwclw gdtgsagsaa
       61 alrregstep aqatatvlig sdeivalrri trsdsgvesa saklwingvk qsnvtpaslt
      121 riitdltglt aktfrgafym aqgqltdlmt gtpakvqetf eeltglddlt kriqglreqc
      181 keaavraeal pgdpaevtrt addakeagre sdrlqqesnr aaaaaasart iwdtanqrak
      241 elqsaeraar dsreavvgae alaadaaqtv naarlrlhdl geasegdpev qgaatrtaca
      301 aleqalselt rrgtelkaaa gqessartaa eqaraahdsv dpdalatavt dgqaevdagr
      361 aahqevlraa hvadaavaqr deaiatlsra mdaaacptcr qdvgdvaali deqnaildqa
      421 rkdaaaahqk attldralld aetrlrkahd alanvaslar vaehaeeaas aatrhadqaa
      481 atlaelvaah qnepaptgre qihsaalavh eqlteqlsta rgvtaawitl tdtiaraaaa
      541 sgrvdqaraa vvdapsptdv aaaesreatt rvdldtaqag aadaaaqaqa aratamqldg
      601 iaddaatrwn lkreaaeqae vtriardigi alrrdllaey catisaaatd iltrlggehv
      661 gfmidetfvp qvvlpdgttr atrqlsggek araavcafig fsrqlagggk pgmlfadeit
      721 asqdeafrrd mltmlralem pmivvshtad vldiasrvir lqrpplgstq laa
//
LOCUS       WP_005571860             371 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Rhodococcus].
ACCESSION   WP_005571860
VERSION     WP_005571860.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (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   2  (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   3  (residues 1 to 371)
  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   4  (residues 1 to 371)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..371
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=39514
     Region          1..304
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mitfdkvtka ypdgttavne ldlecpsgki talvgpsgcg kttslrminr lieptsgtis
       61 ldgestadmd pallrrrigy viqhaglfph rtivdnvatm pkllgktkke artramelle
      121 tvglaanfad rypwqlsggq qqrvgvaral aadpafmlmd epfsavdpvv rsqlqdeflr
      181 lqkdigktii ivthdideal klgdqvvvlr tggilaqsat plelltepad efvadfvgrd
      241 rgyrslgfsn ldgrvetvae pvarlgdsss dartrttddw llvvdpankp igwvqpakvv
      301 drirpddvnl sgtvadahgt mralldaals apskrgvvvd gdgvlvgtvt ahaavaaies
      361 adlvaaeama r
//
LOCUS       WP_005574642             340 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-oxoacyl-ACP synthase III family protein
            [Rhodococcus].
ACCESSION   WP_005574642
VERSION     WP_005574642.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 340)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..340
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36245
     Region          4..333
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mdtvslidia gylpenrvga dyfaqfaasd rlaenimfra pkfrhhiasd enavdmaera
       61 iaplverngs elvanvdili thtqlpdvpi lgtggelarr mgitpdwvvd lhnggcasfv
      121 ymiklarqim qtgdastali vsvqnsagqi ftqsdvrala qsavpgdgag acllvkseaa
      181 pvlglecrty pefagdmtaa vdpprrywea gtgqlhigft esriakvfar gnrlvpeval
      241 avckqigitp daidtlvtnq pnrlflrnwr dalelpaerh pdtfdecgnl fgaaipvtld
      301 ienragripn gslvmmsafa hagdfagaga irwgaapagv
//
LOCUS       WP_005574834             284 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Rhodococcus opacus].
ACCESSION   WP_005574834
VERSION     WP_005574834.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus opacus
  ORGANISM  Rhodococcus opacus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 284)
  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 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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Rhodococcus opacus"
                     /db_xref="taxon:37919"
     Protein         1..284
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30628
     Region          <73..266
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          188..267
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 msvadsdtav ssgafrrpaa plralvtgyd gyrlagfepg ihlglpspcl tvivtidepl
       61 diaaqatpeq apgrydtlas giatapvtir hdgnqhgvql alsplgaral lrvptaalgs
      121 wvvgleellg pdarelterl slepgwderf ailddvltrr aapaeidphl trawhllvag
      181 egtrvgdvah evgwsrrhlv nkfvaeygvt pkdvvrlsrf hrshrmlkga agatladvsa
      241 vcgyydqahm ardwrdlagv apsrwreidp fsfvqdpyhd dgae
//
LOCUS       WP_005574994             253 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease family protein [Rhodococcus].
ACCESSION   WP_005574994
VERSION     WP_005574994.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..253
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=27365
     Region          106..246
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mprsavpntg siittirtkw pwilagllvv vlvtmlspdp ddtlaagtgp vapsevtdaq
       61 qiqmafaqls tlevkgrapk tgydrelfga swtdnvsvdl grngcdtrnd ilrrdlvdit
      121 srdrtrncvv qsgtlrdlyt gtiiaftrgt ktsdavqidh vvalsdawqk gaqlldaqtr
      181 adlandprnl qavdgptnqr ksdadastwl pplaayrcty varqvevkva yrlwvtpper
      241 damaavltgc gar
//
LOCUS       WP_005576665             582 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Aggregatibacter
            actinomycetemcomitans].
ACCESSION   WP_005576665
VERSION     WP_005576665.1
KEYWORDS    RefSeq.
SOURCE      Aggregatibacter actinomycetemcomitans
  ORGANISM  Aggregatibacter actinomycetemcomitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Aggregatibacter.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 582)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 582)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Aggregatibacter actinomycetemcomitans"
                     /db_xref="taxon:714"
     Protein         1..582
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=64667
     Region          3..560
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mmidkrlint vadskkwiai nvlwnwvali ggiisavvfa iclqwaferl ltlqsavift
       61 vvliaclalr awagkmavka sykastqvkh klrtliyqkl ssmplnqvnq qstssviqva
      121 segveqleiy fgrylpqlfy sllapltlfv flvffnvpts lillvcvpli pmsiiavnki
      181 akrllakyws iyvglgssfl dnlqglitlk iyqdddykar qmdieaenfr titmkvltmq
      241 lnsvslmdll ayggaalgil tallqfqdgn ltifgvvlfi llaseffipl rllgsffhva
      301 mngkaaseki ftlldtplee nksavdfpvk nevtvqinel hfayseekpa ingltlsiqp
      361 kqltvfvgks gcgkstlvsl lmgfyqaqqg eilfngidik qinrhslyrh vslvshssyi
      421 fkgslrenml mtlsnasdea iyqcleqvnl anfvrenggl empllsrgsn lsggqiqrla
      481 larallhnad vyvfdeatsn idveseeiil qfiqqlkhsk tivmishrla navnadqiyv
      541 lqsgrlaesg dhaslmaeng iyaemfnqqk nlenirtgan ha
//
LOCUS       WP_005577013             191 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Aggregatibacter actinomycetemcomitans].
ACCESSION   WP_005577013
VERSION     WP_005577013.1
KEYWORDS    RefSeq.
SOURCE      Aggregatibacter actinomycetemcomitans
  ORGANISM  Aggregatibacter actinomycetemcomitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Aggregatibacter.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Aggregatibacter actinomycetemcomitans"
                     /db_xref="taxon:714"
     Protein         1..191
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21474
     Region          3..164
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mklfgamydk tmqwskhgfa pfwlsfvsfi eaiffpippd vmlipmsmsk pqsavkfamf
       61 tatasvlggm igytlgyyaf nlvehyitqw gyqaswqtti hwferwgvlv vfvagfspip
      121 ykvfticagv mqmafipfvi tafvsraarf llvaklaawg gekfaaklrk siefigwsvv
      181 vlaviaylil r
//
LOCUS       WP_005578525             867 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Aggregatibacter
            actinomycetemcomitans].
ACCESSION   WP_005578525
VERSION     WP_005578525.1
KEYWORDS    RefSeq.
SOURCE      Aggregatibacter actinomycetemcomitans
  ORGANISM  Aggregatibacter actinomycetemcomitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Aggregatibacter.
REFERENCE   1  (residues 1 to 867)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..867
                     /organism="Aggregatibacter actinomycetemcomitans"
                     /db_xref="taxon:714"
     Protein         1..867
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=99744
     Region          294..>670
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mlhwankdqy ytksgenfsn ytfdlngkkv hfrlveadva kdnrkdnekd rvfvlaepti
       61 qrhidengee ietdilpiee kgdeliirfe ykampkgkkq adyldqavek lksfafqnea
      121 ylelfslmpt ekekertllk kylqdytakn tadyfihknl gkflnqeldf yiknevmnld
      181 niqaetafse ieqhlqqiki lknvaqeiia flaqledfqk klwlkkkfva gthylitldh
      241 lsdelieavl anaaqleqwq tlfnvkasgl taeklrenyp hlvvdtslfe psfqadilkt
      301 ienldeqtng llihsdnfqa lnllqaryke qvkciyidpp ynansslily kntfkhsswl
      361 slmssrmelg knllmlnasq svaideveqe llgqlldftf sgwkkvaipi vhnprgqqgk
      421 nisyvheyff lmypndteky isdvkraeid srnlrdsgte sdrtdakncf ypfytkdgsi
      481 igigdipddd fhplqanvpl edgivaiypl nengdekkwr yarqsvenil dklevkpgrn
      541 snqiifnkdt gvmrslwvdp kydaseygtk vlqdvlgseq akgfsypksi htvkeiisaq
      601 lgnkapnfvv dyfagsgtta havinlnred ngnrkyilve qgeyfdtvlk prvqkvifse
      661 kwkegkpeag englngvsqi vkvlklesye dtlnnlelrk ptyafdfdeq vqndyllhym
      721 ldvesrgsll stehfakpfd yelniatssa gayqpqkidl vetfnyligl rvntvddrre
      781 rgmvsvegtl psgektliiw rdvermdyea lnryldsrdi npqdsefdvv yingdhnipt
      841 vfadsddvvk tlkvrsiege flermfs
//
LOCUS       WP_005581077             278 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Aggregatibacter
            actinomycetemcomitans].
ACCESSION   WP_005581077
VERSION     WP_005581077.1
KEYWORDS    RefSeq.
SOURCE      Aggregatibacter actinomycetemcomitans
  ORGANISM  Aggregatibacter actinomycetemcomitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Aggregatibacter.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Aggregatibacter actinomycetemcomitans"
                     /db_xref="taxon:714"
     Protein         1..278
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30658
     Region          1..266
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mtkydlhchs tasdgvlspt evvlrthekg vnvlaltdhd tvagvlearq qaeksgirli
       61 ngveistvwe nrsihivglg fdishekmta lltkqarlrd iraqeigekl ekigvenaya
      121 earklagege vtrahyarhl vqigkvsndg qafkrylgqg ksayvkpqwa dipttidiih
      181 qaggaavlah plrytmtmkw vrklaenfks wggdameisg cgqrpdqfql lvklaeehql
      241 agsmgsdfhf pcawvelgkl kplpehipfv ldikndla
//
LOCUS       WP_005545896             501 aa            linear   BCT 20-JAN-2025
DEFINITION  AAA family ATPase [Paenibacillus alvei].
ACCESSION   WP_005545896
VERSION     WP_005545896.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus alvei
  ORGANISM  Paenibacillus alvei
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Liu,Y., Sung,S., Kim,Y., Li,F., Gwon,G., Jo,A., Kim,A.K., Kim,T.,
            Song,O.K., Lee,S.E. and Cho,Y.
  TITLE     ATP-dependent DNA binding, unwinding, and resection by the
            Mre11/Rad50 complex
  JOURNAL   EMBO J 35 (7), 743-758 (2016)
   PUBMED   26717941
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Chen,Z., Luong,T.T. and Lee,C.Y.
  TITLE     The sbcDC locus mediates repression of type 5 capsule production as
            part of the SOS response in Staphylococcus aureus
  JOURNAL   J Bacteriol 189 (20), 7343-7350 (2007)
   PUBMED   17704228
REFERENCE   3  (residues 1 to 501)
  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   4  (residues 1 to 501)
  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
REFERENCE   5  (residues 1 to 501)
  AUTHORS   Hopfner,K.P., Karcher,A., Craig,L., Woo,T.T., Carney,J.P. and
            Tainer,J.A.
  TITLE     Structural biochemistry and interaction architecture of the DNA
            double-strand break repair Mre11 nuclease and Rad50-ATPase
  JOURNAL   Cell 105 (4), 473-485 (2001)
   PUBMED   11371344
REFERENCE   6  (residues 1 to 501)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Paenibacillus alvei"
                     /db_xref="taxon:44250"
     Protein         1..501
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57127
     Region          4..>122
                     /region_name="SbcC"
                     /note="DNA repair exonuclease SbcCD ATPase subunit
                     [Replication, recombination and repair]; COG0419"
                     /db_xref="CDD:440188"
     Region          <152..>381
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
ORIGIN      
        1 mhiklkqlrl fcfknhrkln vdfseitril gqngegksti geavtwllyg vdtfgsktdp
       61 spttyefdqv vvhllltvdd kqvllskelp kgkaakyyin evpkkakeye lfveqlfdkh
      121 lflslftpty fftqhweeqr aqllryvlpp snkeviaqlp epqaeklaal vkkkllddlq
      181 aqhaenrrkq dkaliaaksr tktleeqiqs mpdidgndgv eiaeklseit gkisvhanev
      241 aaaresngrl erlktqirat ydtanqvrnd ytslkeapik dtcdacgqml tgealehtkq
      301 hrqrhldelk ykyktmseqy srmkeefeel rvveisdisd mlqqrveiea qlkaiesldr
      361 laiaieeakq nerdihesyt esvfildaik afrskeaemm aekvgglfer ltlklfienk
      421 gdgeqkpnfe iemdgkpyrk lstaekilag lelisvlseq sgvtaptfid naesiikyqa
      481 psgqliecrv admpltvqev q
//
LOCUS       WP_005582676             221 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Schnuerera ultunensis].
ACCESSION   WP_005582676
VERSION     WP_005582676.1
KEYWORDS    RefSeq.
SOURCE      Schnuerera ultunensis
  ORGANISM  Schnuerera ultunensis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Tepidimicrobiaceae; Schnuerera.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 221)
  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   3  (residues 1 to 221)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Schnuerera ultunensis"
                     /db_xref="taxon:45497"
     Protein         1..221
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25941
     Region          20..219
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mvkkiselni gdrielirin skgkknyisq ildimdeevf ivsgpiykse ivlihkdeiv
       61 kvsyiidnkg rysfnarvlr reyervykle lqkisntkrf qlrgfyrfai dipaikqfpi
      121 krgnkkeivt ekcrtkdvsg gglmlysnyk heigdivlck fniddhqina kgkivrieni
      181 dtfdydyglg irfidisend rdriiqfifl kqrllrekgl i
//
LOCUS       WP_005582756             619 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Schnuerera ultunensis].
ACCESSION   WP_005582756
VERSION     WP_005582756.1
KEYWORDS    RefSeq.
SOURCE      Schnuerera ultunensis
  ORGANISM  Schnuerera ultunensis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Tepidimicrobiaceae; Schnuerera.
REFERENCE   1  (residues 1 to 619)
  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 619)
  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 619)
  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 619)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Schnuerera ultunensis"
                     /db_xref="taxon:45497"
     Protein         1..619
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=65965
     Region          12..611
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mekeqirsky slitivsilm aifhiytalf gvltalwqrs ihlcfgmlit fllkskdssn
       61 kvkkslnill ammalatvvf fivdfdgivq rfsqpntsdm iigtilillt lefarrnvgn
      121 ilpgiaivfl lyamfgsylp gilwhrgydl qriitqvsls tegifgvslg vsanfififv
      181 lfgsilsvtd igkfyidlai kgvgktpggp akaavvsssl fgsisgsava nvagtgciti
      241 plmkstgysk efsgaveava stggqimppm mgaaafimae ilgipyykva igaaipaviy
      301 fgsvfamvhf rarrigltgi dtsslpsike mlktkgillt plillivllv gvqmsamkas
      361 vytvlvtlai avvfcgmrtk elidafedaa ktsvivisst acagiivami nltgiglkfs
      421 nimislaggn ifvilvllml asllmgmglp ttpsylilav lgapalirlg veplaahmfv
      481 fyfgcismit ppvalavyaa tsiaesdfwk tsfeavklgi tafivpymfv ynpsllaigk
      541 pitilttait aiigavilga gisgwllvra dikerillii sglflidprf itnllgllgl
      601 vlvlifhrkr kslenstss
//
LOCUS       WP_005585933             254 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Schnuerera ultunensis].
ACCESSION   WP_005585933
VERSION     WP_005585933.1
KEYWORDS    RefSeq.
SOURCE      Schnuerera ultunensis
  ORGANISM  Schnuerera ultunensis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Tepidimicrobiaceae; Schnuerera.
REFERENCE   1  (residues 1 to 254)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Schnuerera ultunensis"
                     /db_xref="taxon:45497"
     Protein         1..254
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=28732
     Region          36..78
                     /region_name="PG_binding_1"
                     /note="Putative peptidoglycan binding domain; pfam01471"
                     /db_xref="CDD:460223"
     Region          100..224
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mttirkffgl giiimiilgl ftgksyaema dngsilkeyl ssgyndnile qrntllrfqa
       61 ennlsvdgii gditnealae enkkiidiip eeimkkewfi vinktkkilt vynngeiykk
      121 ypvalgkdst ptpdhkftii nklknpywgg mggkfkpirg gasdnplgkr wlglstekyr
      181 gygihgnsap fsigryisag cirminedve elfeyipikt dvwigtekal eewgikqyie
      241 yekkeeicsv lqli
//
LOCUS       WP_005586958             165 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Schnuerera ultunensis].
ACCESSION   WP_005586958
VERSION     WP_005586958.1
KEYWORDS    RefSeq.
SOURCE      Schnuerera ultunensis
  ORGANISM  Schnuerera ultunensis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Tepidimicrobiaceae; Schnuerera.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Schnuerera ultunensis"
                     /db_xref="taxon:45497"
     Protein         1..165
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18469
     Region          8..162
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfkldpikkm teeerlkymn mllksqlsse kdslanlsna tgiimacidr lnwagfyilr
       61 gdelvlgpfq glpacnriei gkgvcgtave traiqlvpdv hqfpghiacd aasnselvip
      121 iikeekaygv ldldspekgr ftklekeyfi kfidilneyi dwsni
//
LOCUS       WP_005588376             185 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Schnuerera ultunensis].
ACCESSION   WP_005588376
VERSION     WP_005588376.1
KEYWORDS    RefSeq.
SOURCE      Schnuerera ultunensis
  ORGANISM  Schnuerera ultunensis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Tepidimicrobiaceae; Schnuerera.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Schnuerera ultunensis"
                     /db_xref="taxon:45497"
     Protein         1..185
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=19991
     Region          1..185
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mkivvgisgg sgsiyavsll kalqqldiet hlvvttmggy vtehecgigl eelkgmatyf
       61 hdnknfaapi asgsfkvdgm vvipcsmktl ssvangfsds lltracdvti kekrkmvlvp
      121 retplspihl enmlklskig vtifppspgf ynhpesiedi vlnmtgrild mlgidnnlvn
      181 rwkgq
//
LOCUS       WP_005589763             265 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Streptococcus].
ACCESSION   WP_005589763
VERSION     WP_005589763.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus
  ORGANISM  Streptococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptococcus"
                     /db_xref="taxon:1301"
     Protein         1..265
                     /product="formate/nitrite transporter family protein"
                     /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=28825
     Region          9..241
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mvestfipki eaacrkkegl fdtskgkyav rsifagaflt fstgagaiaa dltnkivpgt
       61 grflfpfifa wglayivfln aelvtsnmmf ltagtflkki dwkkaliilf yctffnliga
      121 liagwlfans aayaglskes fiagvvqmkl arsnelille gilanvfvni ailsfvlvkd
      181 staklflvis aiymfvfltn ehlaanfasf aivkfssaas qvanfgigni lrhwavtfvg
      241 nligggllig lpyawfnkke ehyvd
//
LOCUS       WP_005590430             201 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Streptococcus cristatus].
ACCESSION   WP_005590430
VERSION     WP_005590430.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus cristatus
  ORGANISM  Streptococcus cristatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Streptococcus cristatus"
                     /db_xref="taxon:45634"
     Protein         1..201
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22672
     Region          3..198
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mkflelnkkr hatkhfndkp idpkdvrtai eiatlapsah nsqpwkfvvv rernealagi
       61 tfgsnqdqik eapvtialft dtdlakrark iarvagvknf sdeqlqfymq nlpaefaryn
      121 dqqksdylal naglvamnlv laltdqgigs niilgfdksk vnevleider frpellitvg
      181 ytddklepsy rlpvdeiiek r
//
LOCUS       WP_005590452             277 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptococcus cristatus].
ACCESSION   WP_005590452
VERSION     WP_005590452.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus cristatus
  ORGANISM  Streptococcus cristatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 277)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 277)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Streptococcus cristatus"
                     /db_xref="taxon:45634"
     Protein         1..277
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30921
     Region          19..102
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          125..276
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mmhqfnrtme yleskldaev dlqqfqqlsg ysyalfsrlf siladttlae ylrnrrlsea
       61 vtdlressek vidialkygy esadafsaaf kkfhgatpse vrngkpyrvf prlqlslkit
      121 ggknmdikiq kksaftvagv lleaidnsqc psaweqlyan hsfeslesmg sgqsfglcsd
      181 vkegeiinym aaydvtdiak aealglsike ipaaeyaivp vkgaipasih hawkyvlevf
      241 fpetgyrhsg apdfevyteg dmsspdyqme lwipvvk
//
LOCUS       WP_005594486             282 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Vibrio scophthalmi].
ACCESSION   WP_005594486
VERSION     WP_005594486.1
KEYWORDS    RefSeq.
SOURCE      Vibrio scophthalmi
  ORGANISM  Vibrio scophthalmi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Vibrio scophthalmi"
                     /db_xref="taxon:45658"
     Protein         1..282
                     /product="formate/nitrite transporter family protein"
                     /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=30020
     Region          2..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msylkpaefi qtmidtgeak vrtstrdlil rgmmagiils lavvvaitti tqtgigivga
       61 lvfpvgfcil slmgydlvtg vfglaplakf enrpgvtwnr vfrcwglvgl gnligsllva
      121 glialsltmn fsvepnavgq kfiaiatart vgfenlgadg witcfvrgil cnlmvclgvi
      181 gnmtarsvag kiaamwlpif iffalvfeha vvnmflfplg mmlgadfgia twlnynlipt
      241 ilgnivgglv mtciplylth kktapaldad veieaqpaln tk
//
LOCUS       WP_005594553             265 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio scophthalmi].
ACCESSION   WP_005594553
VERSION     WP_005594553.1
KEYWORDS    RefSeq.
SOURCE      Vibrio scophthalmi
  ORGANISM  Vibrio scophthalmi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 265)
  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 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   3  (residues 1 to 265)
  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   4  (residues 1 to 265)
  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 265)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Vibrio scophthalmi"
                     /db_xref="taxon:45658"
     Protein         1..265
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30530
     Region          20..262
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <155..262
                     /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 mdrvkysntv sesinlidar yrqfvfqrhy hldfhiglit qgeqrfhhqg qnhhvgqghv
       61 vimapdelhd gnsvlergyq tkvfaidpnw ltqlaeytqp eqilsfrqsi ianpdifqql
      121 yqlhlllgds dqcqlakdcl plegleqlft qfgygqpeka splgrqsivt lkefilahld
      181 epirleqlan mchltptqfq rhfkqkmgit pyawlsrlrl eqamkllqqg hnatyvahhv
      241 gfydqahfsk afksnfgvpp tqise
//
LOCUS       WP_005595531             447 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein, partial [Vibrio scophthalmi].
ACCESSION   WP_005595531
VERSION     WP_005595531.1
KEYWORDS    RefSeq.
SOURCE      Vibrio scophthalmi
  ORGANISM  Vibrio scophthalmi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 447)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Vibrio scophthalmi"
                     /db_xref="taxon:45658"
     Protein         1..>447
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <193..446
                     /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 msvnrfrfvl fvvfvlsavi yiaksvwsmq lenkdyffml itfvlfsvwf wffasyhylr
       61 hsigllemav ishdvresvg ikteiktlpi leltnsintm lfrirekyen qscensieni
      121 trlpninwvg knsnhvsvea fvifeiesin geieslkyie yevfirefis alksvlgddv
      181 liiyveqgky avgldscfri ehfvdliksi gtfpfevsgn qiyvnfwfgs saktdismrm
      241 vdllddakls lyeskrtmir hvhfessmry nsqlkvsnyn rlksailnne fmpyfqpiid
      301 letnsvvgae slarwidper gvlgpiefis lsedtglidl iglsilresl iwfknnaqyv
      361 kdanefslhv nvsikqlmnr nfskdvkdmi fslgysyknv hfeftesiym esemvmnnln
      421 elsdlgikfs iddfgtgyss fsylrdi
//
LOCUS       WP_005595884             104 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Vibrio scophthalmi].
ACCESSION   WP_005595884
VERSION     WP_005595884.1
KEYWORDS    RefSeq.
SOURCE      Vibrio scophthalmi
  ORGANISM  Vibrio scophthalmi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (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   2  (residues 1 to 104)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Vibrio scophthalmi"
                     /db_xref="taxon:45658"
     Protein         1..104
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11044
     Region          43..102
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mnikalvlsv vltfslpfta vlaeqqpdsp penpkydgie ivvnvnqasa qeiadllkgi
       61 gltkaqaivd yrdqqgpfkr iedlakvsgv geatvaknvg riel
//
LOCUS       WP_005597835             160 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Actinobacillus pleuropneumoniae].
ACCESSION   WP_005597835
VERSION     WP_005597835.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus pleuropneumoniae
  ORGANISM  Actinobacillus pleuropneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Actinobacillus pleuropneumoniae"
                     /db_xref="taxon:715"
     Protein         1..160
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17713
     Region          19..156
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mtdyitslls lffseenqlf tmflsaflsa tvlpgnseii fttlatqisl tnsdlfsaqm
       61 lwllsvatlg nslgssvtya mgllipkpld lkhktaqwal rlcekygafa lllsslpiig
      121 dllcgiagwl rfnlwqslif iclgkfiryl illfalspwf
//
LOCUS       WP_005598110             207 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Actinobacillus pleuropneumoniae].
ACCESSION   WP_005598110
VERSION     WP_005598110.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus pleuropneumoniae
  ORGANISM  Actinobacillus pleuropneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
REFERENCE   1  (residues 1 to 207)
  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 207)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 207)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Actinobacillus pleuropneumoniae"
                     /db_xref="taxon:715"
     Protein         1..207
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23031
     Region          6..207
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 msneylnkte eqqfeeaknw fkengtpilv aviiacaatl gwnfwqnhqv qaaqqtsaty
       61 qnvmesylqd peknqpliek fisenkdssy avfsqlesak qavekadfaa aktvlqsalt
      121 stsdaslqti irfrlatldy qlknyddala tlgqitdqvw eqrklvltgd ilvakgdkas
      181 akgvyekaka tatnqdkvli dvrlnnl
//
LOCUS       WP_005598801             373 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Vibrio scophthalmi].
ACCESSION   WP_005598801
VERSION     WP_005598801.1
KEYWORDS    RefSeq.
SOURCE      Vibrio scophthalmi
  ORGANISM  Vibrio scophthalmi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 373)
  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 373)
  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 373)
  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 373)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Vibrio scophthalmi"
                     /db_xref="taxon:45658"
     Protein         1..373
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=41534
     Region          14..369
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mralhsffdg klklgiatla asvalvgcge ekqadtakqa epekvyklkl aetwgpnfpi
       61 fgdatknmak maeemsngrl vitidssnkh kaplgvfdmv ksgqydlghs asyywkgkvp
      121 ntlyftsmpf gmlpteqyaw fyygggmelm eevysahnll sfpggntdtq mggwfqkein
      181 svddlqglkm ripgfageil aeigakptni apgelytsle rrtidalewv gpsldlrmgf
      241 hkiapyyytg whepgtelqf lvnqrtwdsl padlqsilqt amktaaydmy tqskhesgkn
      301 wasiqseypn vqvkdfpvev iaalreandr llsdhaakdd lakkiqasqa ayieqvrpws
      361 nishraylns qaq
//
LOCUS       WP_005598803             177 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Vibrio scophthalmi].
ACCESSION   WP_005598803
VERSION     WP_005598803.1
KEYWORDS    RefSeq.
SOURCE      Vibrio scophthalmi
  ORGANISM  Vibrio scophthalmi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Vibrio scophthalmi"
                     /db_xref="taxon:45658"
     Protein         1..177
                     /product="TRAP transporter small permease subunit"
                     /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=20139
     Region          4..169
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mrrliyierl fnrfgdwlgw lssilfilll invvydvvmr yafndvsiaf qemewhlfsa
       61 vfligvpyai kagghvrvdl fyerlsnkaq aiidllgtvf fllpfcllva wygidfakes
      121 yvlgetsgdp gglsyrwiik gmiplsflfm avsgiglmlh slnrivnphl mhaqank
//
LOCUS       WP_005600254             727 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Vibrio scophthalmi].
ACCESSION   WP_005600254
VERSION     WP_005600254.1
KEYWORDS    RefSeq.
SOURCE      Vibrio scophthalmi
  ORGANISM  Vibrio scophthalmi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 727)
  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   3  (residues 1 to 727)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Vibrio scophthalmi"
                     /db_xref="taxon:45658"
     Protein         1..727
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=77296
     Region          6..726
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msydldedil qdflveagei lellseqlve lennpddkdl lnaifrgfht vkggagflal
       61 telvdtchga envfdilrng qrkvtadlmd tmlraldavn vqfqavqdge plppseqsll
      121 delhrlskpa sveeaivaap vaepvievpa piveepvaat aapsasside itqdefekll
      181 delhgsgtap gsapapapka pepamaasgd itddefekll delhglgkgp gkednvvasa
      241 ppapaapapt vssgdedlmt daefekllde lhgqgkgpsp eeleaatkpv aqveapqaaa
      301 peaiapppvm papvasapea vpakkeapvp akktqaeatv rvdtstldii mnmvgelvlv
      361 rnrllslgln sadeemskav snldvvtadl qgavmktrmq pikkvfgrfp rvvrdlarsl
      421 nkditlemrg edtdldknlv ealadplihl vrnsvdhgie mpedrvkagk srtgkvilsa
      481 aqegdhiqla ivddgggmnp dvlrgiavkr gmmdedaasr ltdkecfnli fmpgfsskek
      541 isdisgrgvg mdvvktaint lngsididse mgkgtqitik vpltlailpt lmvgvaghpf
      601 alplasvnei fhldlsrtnv vdgqltiivr dksiplfylq nwlapragfv eqrkghghvv
      661 ivqlgsqrvg fvvdtligqe evvikpldnl lqgtpgmaga titsdghial ildvpdllkr
      721 yasasri
//
LOCUS       WP_005601670             207 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Actinobacillus pleuropneumoniae].
ACCESSION   WP_005601670
VERSION     WP_005601670.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus pleuropneumoniae
  ORGANISM  Actinobacillus pleuropneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
REFERENCE   1  (residues 1 to 207)
  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 207)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 207)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Actinobacillus pleuropneumoniae"
                     /db_xref="taxon:715"
     Protein         1..207
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23017
     Region          6..207
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 msneylnkte eqqfeeaknw fkengtpilv aviiacaatl gwnfwqnhqv qaaqqtsaty
       61 qnvmesylqd peknqplvek fisenkdssy avfsqlesak qavekadfat aktvlqsala
      121 stsdaslqti irfrlatldy qlknyddala tlgqitdqvw eqrklvltgd ilvakgdkas
      181 akgvyekaka tatnqdkvli dvrlnnl
//
LOCUS       WP_005604104             645 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Actinobacillus
            pleuropneumoniae].
ACCESSION   WP_005604104
VERSION     WP_005604104.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus pleuropneumoniae
  ORGANISM  Actinobacillus pleuropneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
REFERENCE   1  (residues 1 to 645)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..645
                     /organism="Actinobacillus pleuropneumoniae"
                     /db_xref="taxon:715"
     Protein         1..645
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=73501
     Region          62..585
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mqklkmhsad ltaqniekia alfpncvter evngkleqai dfdllkqels stivegnqer
       61 yqlnwvgkan atvlanapin ktlrpcrees vnfdttqnlf iegdnlealk llqetylgkv
      121 kmiyidppyn tdkdfiykdn famanedyql esgqvdeegn rlvvnsesng rfhsdwlsmi
      181 ysrlklarnl ltddgvifis iddnevanlk ricdeifggn nfiaqlptim nlkgnndefg
      241 fagtheytlv ytnnkidlvl nqfeineedl dawmedeigf ykqganlkst genaprekrp
      301 nlyfpifidd enkiyitend ippneykgrl itiypitdgn emswrwsknk flneiydviv
      361 vrndngvaly kkqrpslgdl pskkpktify kpeyssgngt sqikeifknk lfqnpkpiel
      421 imdflrigtn vnscildffa gsattahavm qlnaedggnr kfimvqipeq tdekseahka
      481 gyhtiaeisk erirragqki kqekpdaadl digfrvlkid ssnmadiyyn pqqikqgdlf
      541 sqvehikadr teedllfqvl ldwgvdltlp iekrvlngkn vyfvdgnalv acfdkaideg
      601 iiqeiakhqp lrsvfrddgf vsdtakinad qlfkqlaphs elrvi
//
LOCUS       WP_005603703             683 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Eshraghiella crossota].
ACCESSION   WP_005603703
VERSION     WP_005603703.1
KEYWORDS    RefSeq.
SOURCE      Eshraghiella crossota
  ORGANISM  Eshraghiella crossota
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Eshraghiella.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 683)
  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   3  (residues 1 to 683)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Eshraghiella crossota"
                     /db_xref="taxon:45851"
     Protein         1..683
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=74828
     Region          1..683
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          178..254
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 mdvsqyleif veetkehlqs lndnilvlen epenkdtine ifrsahslkg magtmgykrm
       61 qtlthdmenv fseirndklk vtsdlvdilf qcldaleayl dniintqdeg tddnaaiikl
      121 lndylnggsg vaeqaapqaa qaapqtadgv vtdfskvnfa dfeqhaimea gtknlnvygv
      181 hvkidpscil kaaraflvfk sveelgeiik sipsaqdied ekfdldfdif vitgesldkv
      241 latvrnvsei kdaegsiikl dekkeekpee tektesakpa tvpkagkpan sqpakgkpvv
      301 nrsvrvdidk ldvlmnlvse liiaknglvs aaatsnteen qsvneqieyl ervttnlhes
      361 vmnvrmvpie tvvnrfprmi rdlskkldkk melymtgeet eldrtvidei gdplmhllrn
      421 sadhglesae vrrergkdei gtiflnafqd gnnvvievgd dgngidiekv kskaiergti
      481 tpeqaevmsd kevidllflp sfstsekitd vsgrgvgldv vkskieslgg vvecksvlge
      541 gstftirlpl tlaiiqalmv klgneqyaia lgsiqtiedi plsdikyvqg kevinlrgni
      601 ipiirlgell dvpdrtepde slivvvikkg dkqaglvvds lvgqmeivik slgkyinink
      661 misgatilgd gevaliidan aii
//
LOCUS       WP_005604247             190 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Actinobacillus
            pleuropneumoniae].
ACCESSION   WP_005604247
VERSION     WP_005604247.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus pleuropneumoniae
  ORGANISM  Actinobacillus pleuropneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Actinobacillus pleuropneumoniae"
                     /db_xref="taxon:715"
     Protein         1..190
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20937
     Region          2..187
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mkqriiigis gasgfqygyk alellksldv ethlvltkga emtrsletki ereqlldlas
       61 qvhsihnvga siasgsfktl gmlvapcsir tlsaialgfs dnlltraadv vlkerrklvl
      121 mvretplnla hidnmrrvte mggiifppvp afyqhpttid elvthsvara ldlfdfnlpm
      181 prwgetnnke
//
LOCUS       WP_005605243             114 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Actinobacillus pleuropneumoniae].
ACCESSION   WP_005605243
VERSION     WP_005605243.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus pleuropneumoniae
  ORGANISM  Actinobacillus pleuropneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
REFERENCE   1  (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   2  (residues 1 to 114)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Actinobacillus pleuropneumoniae"
                     /db_xref="taxon:715"
     Protein         1..114
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12345
     Region          42..112
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkkfarfsis fiiallsads iakpnnppvs eptpvvqqmt ttnktadkqn qvnintadaa
       61 eiksklvgig ekkaqaivdy rtkngafiti eqltevsgig kttleknrer itle
//
LOCUS       WP_005607603             959 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Actinobacillus
            pleuropneumoniae].
ACCESSION   WP_005607603
VERSION     WP_005607603.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus pleuropneumoniae
  ORGANISM  Actinobacillus pleuropneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
REFERENCE   1  (residues 1 to 959)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..959
                     /organism="Actinobacillus pleuropneumoniae"
                     /db_xref="taxon:715"
     Protein         1..959
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=111193
     Region          398..839
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mqeifqinqp dldfgiyril nsrqneiqqf ltrtlpnnin gafngnfeqa nsvynhlytf
       61 fsryydqgdf isqrrykgdt yaipyageev mlhwankdqy ytksgenfsn yaftlengkk
      121 vqfrlveadt akdnrkdndq trvfaliepk iktetdengd eiqtdirpie engdlltirf
      181 eyksvnkkek qadyimqave kiqnfaisde fqdifkpmpt eknktrtlle kyltdytakn
      241 tadyfihknl gkflnqeldf yiknevmnld niqdstdfsh ieqnlqtikt lktvakeiia
      301 flaqledfqk klwlkkkfva gchylitldh lteeqvqqal dnpkqtaqwq alfnvetsdq
      361 naleicknyp hlvvdtslfe pkfqaevlgs lidldkqtng llihsdnfqa lnllqeryke
      421 qvkciyidpp yntnatpiiy kngykhsswn slllnrmemg lklasssaiq ftaidhaelf
      481 nlgkiqddlf teqnriaiip iqhnpkgrnq avffsencey mfcyakditk asfnqvaidr
      541 evldtftekd digrfrwenf vrartswskk nkpnnwysiy vnedlseltl ekkdgyievl
      601 pvtnqgeftw knipssfeel nvngyfkaek engkvvvyhk yreqqvfknf wsqkkyqsef
      661 ngtnllkail genpfsfpks iyavldsiki vsgkndiild yfagsgttah avinlnredn
      721 gnrkyilveq geyfdtvlkp rvqkvifake wkdgkpqsdn gafggvsqiv kvlklesyed
      781 tlnnlalrkp aqdlvdmgls etvqndysln ymldvesrds llntkhfakp fdyqlniatt
      841 sagasdkkti dlvetfnyli glrvseindk renglvtvqg tnasgektlv iwrdcekydy
      901 drlndylnrh kinpqesefd vvyingdhnv ptvfagndes vkmlkvrsie aeflqrmfe
//
LOCUS       WP_005608855             266 aa            linear   BCT 20-JAN-2025
DEFINITION  3-deoxy-manno-octulosonate cytidylyltransferase [Tritonibacter
            mobilis].
ACCESSION   WP_005608855
VERSION     WP_005608855.1
KEYWORDS    RefSeq.
SOURCE      Tritonibacter mobilis
  ORGANISM  Tritonibacter mobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Tritonibacter.
REFERENCE   1  (residues 1 to 266)
  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 266)
  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 10787365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Tritonibacter mobilis"
                     /db_xref="taxon:379347"
     Protein         1..266
                     /product="3-deoxy-manno-octulosonate cytidylyltransferase"
                     /EC_number="2.7.7.38"
                     /GO_function="GO:0008690 - 3-deoxy-manno-octulosonate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0033468 -
                     CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28800
     Region          1..259
                     /region_name="KdsB"
                     /note="CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell
                     wall/membrane/envelope biogenesis]; COG1212"
                     /db_xref="CDD:440825"
ORIGIN      
        1 msvlivipar yastrypgkp laeltgatgk trtlierswr aacdvdgvdr vvvatdddri
       61 kaaaegfgae vvmtstecan gtercaeaha alggnfevvv nlqgdapltp pwfiedlvng
      121 lkaapdmgla tpvlrcdgat lnsllqdrre grvggttavf aadhsalyfs kevipyqsgt
      181 yedaddtpvf hhvgvyayrp dalaaypdwp vgpletlegl eqlrflengr kilcvvvear
      241 grefwelnnp qdmpkiesmm lkmgle
//
LOCUS       WP_005609232             123 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Actinobacillus
            pleuropneumoniae].
ACCESSION   WP_005609232
VERSION     WP_005609232.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus pleuropneumoniae
  ORGANISM  Actinobacillus pleuropneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
REFERENCE   1  (residues 1 to 123)
  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 123)
  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   3  (residues 1 to 123)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Actinobacillus pleuropneumoniae"
                     /db_xref="taxon:715"
     Protein         1..123
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14752
     Region          19..115
                     /region_name="Endonuclease_DUF559"
                     /note="Putative endonuclease; cd01038"
                     /db_xref="CDD:411708"
     Site            order(23,52,69,78)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:411708"
ORIGIN      
        1 mqpyskslkp lsqklrsdqt daerklwqri nrdqlldfrf nrqkpllnyi vdfycpkakl
       61 iieldgsqhy epdyqekdrl rdeelnslgf tvmrfsndev yfeiesvveq iylflenvra
      121 nlp
//
LOCUS       WP_005610289             167 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Tritonibacter mobilis].
ACCESSION   WP_005610289
VERSION     WP_005610289.1
KEYWORDS    RefSeq.
SOURCE      Tritonibacter mobilis
  ORGANISM  Tritonibacter mobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Tritonibacter.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Tritonibacter mobilis"
                     /db_xref="taxon:379347"
     Protein         1..167
                     /product="TRAP transporter small permease subunit"
                     /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=18767
     Region          3..166
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mvlirlidgl neivgkavsy vavifagmii ydvvmrygfn aptlwafdlt kmffgfyfvl
       61 lggyalrhqa hvkvdlvten lpsrprqive vlgylifffp fcwvfvtksw efalrsyaqg
      121 ettygavqip vypvkiamav aacllaiqgv sevlklifkq seqrhvg
//
LOCUS       WP_005612412             160 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Actinobacillus pleuropneumoniae].
ACCESSION   WP_005612412
VERSION     WP_005612412.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus pleuropneumoniae
  ORGANISM  Actinobacillus pleuropneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Actinobacillus pleuropneumoniae"
                     /db_xref="taxon:715"
     Protein         1..160
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17675
     Region          19..156
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mtdyitslls lffseenqlf tmflsaflsa tvlpgnseii fttlatqisl tnsdlfsaqm
       61 lwllsvatlg nslgssvtya mgllipkpld lknksarwal alcekygvfa lllsslpiig
      121 dllcgiagwl rfnlwqslif iclgkfiryl illfvlspwf
//
LOCUS       WP_005611442             401 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [[Ruminococcus] lactaris].
ACCESSION   WP_005611442
VERSION     WP_005611442.1
KEYWORDS    RefSeq.
SOURCE      [Ruminococcus] lactaris
  ORGANISM  [Ruminococcus] lactaris
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Mediterraneibacter.
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
REFERENCE   3  (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   4  (residues 1 to 401)
  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   5  (residues 1 to 401)
  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   6  (residues 1 to 401)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 401)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 401)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="[Ruminococcus] lactaris"
                     /db_xref="taxon:46228"
     Protein         1..401
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44748
     Region          43..84
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          107..394
                     /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 mllfqevhdk tllykknkkv ynslikylik edkktenkdk rnitrkkiin yvlnnhvtsk
       61 aeiakelnls lptvlanvnd llekmvleet geyastggrk aksiginksy chamgilita
      121 nhiemvlvnl gdeiikkdri rlkftaelsy ctevaqkvkt flegelakdt llgigvaipg
      181 iidqkeqivl kshalgieny slrfleqale ipvyfendan aamlaekkqk ypnaiylsln
      241 htlggafcid gklfrgqnqk agefghmilv pggrkcycgk sgcadaycaa svltqgnrqs
      301 ldafmekies gdekilqtwn eyldhlavli snlrmaydmd iilggdvggv lsdymiplge
      361 kvmayngfeh dvsylkncsy kkeasavgaa kyfftkhmve l
//
LOCUS       WP_005612858             711 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Tritonibacter mobilis].
ACCESSION   WP_005612858
VERSION     WP_005612858.1
KEYWORDS    RefSeq.
SOURCE      Tritonibacter mobilis
  ORGANISM  Tritonibacter mobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Tritonibacter.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 711)
  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   3  (residues 1 to 711)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Tritonibacter mobilis"
                     /db_xref="taxon:379347"
     Protein         1..711
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76127
     Region          19..693
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msgsiqdtff eeceelleam degltaiegg dhdpevvnav fravhsikgg agafgldelv
       61 afahkfetvf devrsnklel dtkliqlllr csdhladlvt vsrdggsvde ehndvliagl
      121 eeyldeeeed ltfepmglgg psvplplave eeksyeirfr plkemfgtgn epfflfqals
      181 elgtlevvld etelpgfdam amddsylawn ltltttepks aveavfefve glcelsiasd
      241 kdaeeeaaal aalnaafgvp gdsaepetpa pfdapapaea tpmatpqate kvetvkpesn
      301 kseqrgpkpt lrvdlervdr linavgelii nhsmlaqqia nldvadlrdv etelegfknl
      361 ardiqegvms iraqpvkplf qrmarivrea ssatektakl itegentevd ktvierlsdp
      421 lthilrnavd hgiekpedre aagknrtgei rlsashrsgs vcieikdnga ginrprvkqi
      481 aiekglipen adltdaeidn llflpgfsta kevsnlsgrg vgmdvvknav talggrinvs
      541 stpgkgstft iilpltlavm dgmvvsvadq tmvvpitsii etmrgsddmi nslgadgtll
      601 sirgnfvpic dvagalglrk pegdkppgvy llvetetgqr salavddihd qrqvviksld
      661 gvcgnipgva aatilgdgki amildsesii aasptsatfd sdrrmsnaia s
//
LOCUS       WP_005613951             242 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein, partial [Actinobacillus pleuropneumoniae].
ACCESSION   WP_005613951
VERSION     WP_005613951.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus pleuropneumoniae
  ORGANISM  Actinobacillus pleuropneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Actinobacillus pleuropneumoniae"
                     /db_xref="taxon:715"
     Protein         <1..>242
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
     Region          <191..>242
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 dvnyaevkfr rvdndlmlfg yhdtdsvtvk sfyshvdyqf dklefadrsi trdelikagl
       61 hlygtdgndd ikdhadwdsi leggkgndil rggygadtyi fskghgqdiv yedtnndnra
      121 rdidtlkftd vnyaevkfrr vdndlmlfgy hdtdsvtiks fynhvdyqfd klefadrsit
      181 rdelgkqgma lfgtdgddni ndwgrnsvid agagndtvng gngddtligg kgndilrggy
      241 ga
//
LOCUS       WP_005614556             265 aa            linear   BCT 20-JAN-2025
DEFINITION  phosphonate ABC transporter ATP-binding protein [Pseudomonas
            avellanae].
ACCESSION   WP_005614556
VERSION     WP_005614556.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas avellanae
  ORGANISM  Pseudomonas avellanae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
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   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Pseudomonas avellanae"
                     /db_xref="taxon:46257"
     Protein         1..265
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=28707
     Region          3..247
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mtlrlsaidl rhsngtlalr gldlsierge rvaiigpsga gkttllnlla salppsagql
       61 kvlgvnpwrl ssrqrqqlrs rialihqapp lparqrvvta vsagklgqwg lgksllnllh
      121 pldvpgarav ltrldladkl fercqqlsgg qlqrvgiara lyqapellla depvsamdpr
      181 ladhtlallc qhaiehnvtl vaslhavela lahfpriigv rdgrihfdlp ageverqhld
      241 tlyaneqlsp qqvcevaetv wtprc
//
LOCUS       WP_005614775             699 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Pseudomonas avellanae].
ACCESSION   WP_005614775
VERSION     WP_005614775.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas avellanae
  ORGANISM  Pseudomonas avellanae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 699)
  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   3  (residues 1 to 699)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Pseudomonas avellanae"
                     /db_xref="taxon:46257"
     Protein         1..699
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=75308
     Region          3..689
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msinldqaqq tfivearell qameesllql esepgdqgai gaifraahti kgsaglfglt
       61 pivsfthive dvldrlregs vavdagliav llksgdhmle lievvasrge alqpaalere
      121 aalrqalqiy qapgsvpaed tacapdaveg eqaevlwhis lrfgvdvfrn gmdplsflry
      181 lntlgqmihv ttvtdsipav eswdpeschl gfeidfrsaa ghdainevfd fvredcvvli
      241 tpveqtpess eptgtdlvsq naqspvvagg ellgdqravp rvpgqttave rpasgsehka
      301 kdgsyvrvna dkldelinlv gelviasaga sllarssnnd plqeasstvs glveqildga
      361 lhlrmipigd tfnrfrrvvr dvsqelgkdi dliingaete ldktvvekig dplmhllrns
      421 mdhgiesaea rraagkpakg hlnlnafhds gsivieiadd gaglnreril ekaqqrglva
      481 agasltdqei ynlifepgfs taeavtnlsg rgvgmdvvkr nitllrgtvd ldsqpgqgti
      541 vrirlpltla iingflvgid qftyvipldm vqecieldeh drqssrdkgy ldlrgevlpl
      601 vylrdhfnhe gpparrqnvv vryaehkagl vvddllgefq tvikplgklf galrgisgst
      661 ilgsgavali ldipallnqi vqmetrltqp plslspasr
//
LOCUS       WP_005615073             809 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas avellanae].
ACCESSION   WP_005615073
VERSION     WP_005615073.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas avellanae
  ORGANISM  Pseudomonas avellanae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 809)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 809)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 809)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..809
                     /organism="Pseudomonas avellanae"
                     /db_xref="taxon:46257"
     Protein         1..809
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88443
     Region          70..120
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          97..809
                     /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 msvhkpatqq pasltrivrr tllgmalsap ltsiivaapa waqtaatrqf dipsgsvdsa
       61 laqfsatagv nisfdpsqaq gqrsrglhga ytvdsglrql lagsklqavl lsngsyslip
      121 vvdatlqldp tsitgkaves aagpmegfva trssagtktn tpiieipqsi svitrqqmqa
      181 qgaqtvtdal ryvpgvkvea ygldpkgfdw lylrgfngqa ssdylnglrq qnnsyaffrs
      241 epysldridv vrgpasslfg qgdaggivnr vskkpeanhv nevqltggnh drlqgqfdig
      301 gvlsddqhll yrvvglarev dtqvdyadgh alkddrlyia psltwapded tsltllsdfm
      361 rdsnggslfa ystpnghttn tlmgdhsfnh ldqeqfslgy efrhrlddtw efrqnarygq
      421 vdlifqnllp tavdtntgnv triadrfdqh mdtfnldnql qadfttgpls htllmgvdyt
      481 wqdadisrwr tqapglnlna pqyglaiarp naanslssid ydqtieqvgg yiqdqikfdd
      541 hwivtaggry dyvrnaldnh vgassnqkdn aftgrlglty ltefglapyv syaesftpnt
      601 gtdrngsafd psmahqwevg vkyqptdail mtlaaydltk tnvltteivg gvntgftvas
      661 geqqsrgiea eikarldqhw dliasytyth aeitksnrgd egkrpanvpr hmastwlnyt
      721 fndtplkgls lgggarytgv lygdngntyh idnytlfdag asypinkhvt vsvnaqnlld
      781 teyvatcdds yecypgmrrt lltsvkysw
//
LOCUS       WP_005616016             195 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Tritonibacter].
ACCESSION   WP_005616016
VERSION     WP_005616016.1
KEYWORDS    RefSeq.
SOURCE      Tritonibacter
  ORGANISM  Tritonibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 195)
  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 195)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 195)
  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   4  (residues 1 to 195)
  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   5  (residues 1 to 195)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Tritonibacter"
                     /db_xref="taxon:2083206"
     Protein         1..195
                     /product="TRAP transporter small permease subunit"
                     /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=22195
     Region          4..192
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 migamlgyvr vvdavnyrig rlmmwglfam mgillwssis ktfflpslwt lemaqfamvt
       61 yyilggpysi qigsnvrmdl fyhnwstrrk awfdaftvla litylgilfy gglgstaysl
      121 gywgdnpfaf fwglitgaee vghmerasta wrpfiwpiks imvfgfflml lqaiselfkd
      181 iarlkghdip serps
//
LOCUS       WP_005616048             631 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Pseudomonas avellanae].
ACCESSION   WP_005616048
VERSION     WP_005616048.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas avellanae
  ORGANISM  Pseudomonas avellanae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 631)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 631)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 631)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 631)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 631)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 631)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Pseudomonas avellanae"
                     /db_xref="taxon:46257"
     Protein         1..631
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68307
     Region          1..631
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msqtnshaqa ggtakpigll iaavgvvygd igtsplytlk evfqggygve vthdailgvl
       61 slifwsliwv vsfkymafvl radnqgeggi malmalarra sakhpklqmm mvvfglfgaa
      121 lfygdsmitp avsvlsameg lelafdgldh wivpmalvvl vglfliqrhg tarigvlfgp
      181 vmvvwflvlg algvygimqs pevlkavnpa wglnffiihp gigvailgav vlaltgaeal
      241 yadmghfgrk sisrawfilv lpalllnyfg qgalvlgnpe avrnpfylla pswallplig
      301 lstmatiias qavisgafsm tlqaiqlgyi prmhiqhtss daqgqiyiga vnwalmvgvi
      361 mlvigfessg alasaygvav tgtmlcttil vstvmlmlwk wppllavpll iclllvdglf
      421 faanvpkifq ggafpvlaga vlfilmttwk rgkqllaeri degglplpif igsirvqpph
      481 rvqgtavflt arsdavphal lhnmlhnqvl heqvvlltvv yedtprvpsa qrfevesyge
      541 gfyrvilhfg fidepdvpaa lalchlaeld fspmrttyfl sretvipskm dgmarwreal
      601 fafmlknang nlrffklpfn rvielgtqve m
//
LOCUS       WP_005616832             154 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Tritonibacter mobilis].
ACCESSION   WP_005616832
VERSION     WP_005616832.1
KEYWORDS    RefSeq.
SOURCE      Tritonibacter mobilis
  ORGANISM  Tritonibacter mobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Tritonibacter.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 154)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Tritonibacter mobilis"
                     /db_xref="taxon:379347"
     Protein         1..154
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16422
     Region          2..153
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mrvnyedlsk tvaalteget devalmatva celhhaddrf dwtgfyrvte pevlkigpyq
       61 gghgclvipf argvcgaaar lnetqlvddv eafpghiacs sstrseivlp vrnkagevig
      121 vldidsnqpa afdqedqaal eslldavfgn lstt
//
LOCUS       WP_005617171             801 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas avellanae].
ACCESSION   WP_005617171
VERSION     WP_005617171.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas avellanae
  ORGANISM  Pseudomonas avellanae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 801)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 801)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 801)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..801
                     /organism="Pseudomonas avellanae"
                     /db_xref="taxon:46257"
     Protein         1..801
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87368
     Region          60..107
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          110..801
                     /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 mptpssrlrt grvktcglrl gglvlalafq gevlaeefdf dipaqalnsa lkelgrqgdl
       61 qilynpddvn gklgsavhgr ltpeqavadl lkkadvahsf eantlilgia asaqpmnlgp
      121 vaikgdhfgi ttegsgsyaa tgviinktsq slrdtpqsvt vmtrqlmndk nltgldevma
      181 qtpgitfsqr nfgshvfssr gfaledesyt idgvagqgys vtgwmtpdme iydrvevlrg
      241 aaglligagn pggavnlvrk rptaipqlsi ttragswdqy rvdldasskl ndsgsvrgrf
      301 vtsyedrgsf idglqktapl lygiletdls edttltlglr hqsadihgfs ifglprysng
      361 kavdlprats laqgwnrhqt rtdevfsele thfdenwsgt lsathsdgaf eqkvayaqga
      421 idpatqsgsr lvktlfrsda lqsdgfdshl dgrfdafglt hqvtvggnws eqkrdsryat
      481 vnanqpldif ntdhnaiaep arpawrstdy sdkrygvysn lrlsltesls lvmggrvswy
      541 dyqsqsagvt traqennqvt pflgviydln rdwswyasyt diflpqsgyr nasgafldpa
      601 igashetgik gelfdkrlnv sfalfyvkqk dvaveddaha gqclsndayg tcylngdirr
      661 skgidmeisg eplpglqtla gytfnltrgs dgqsisaetp rhmlrlsssy tlpgtwrrlt
      721 vgggvsaqsg ysehettqpi dnpgraiwda raswkidehw svalngnnll drkyykatgd
      781 idrgnyygdp rnyvltlrgd f
//
LOCUS       WP_005617488             210 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Pseudomonas syringae group].
ACCESSION   WP_005617488
VERSION     WP_005617488.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 210)
  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 210)
  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   3  (residues 1 to 210)
  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   4  (residues 1 to 210)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 210)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 210)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..210
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=23229
     Region          22..206
                     /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"
ORIGIN      
        1 mtlraakkrl rndsaggikd lrdisvlvih pddedgrnli aqlqrigcqv rvqwpiperl
       61 hseadvivla vspeslstnt pwllhsatpp iipviayenp iivealvqln acsvipspvr
      121 sfglltalai tlsqarktre rekhvkrleg rmavmrtvqq akiilmetkg lseidaynal
      181 rdqamakrep vekiaealvk ahelfqqacs
//
LOCUS       WP_005618635             317 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Pseudomonas
            avellanae].
ACCESSION   WP_005618635
VERSION     WP_005618635.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas avellanae
  ORGANISM  Pseudomonas avellanae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 317)
  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   2  (residues 1 to 317)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Pseudomonas avellanae"
                     /db_xref="taxon:46257"
     Protein         1..317
                     /product="aminoglycoside 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=35221
     Region          46..225
                     /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"
     Region          131..297
                     /region_name="CotS"
                     /note="Thiamine kinase or a related kinase [Coenzyme
                     transport and metabolism]; COG0510"
                     /db_xref="CDD:440276"
ORIGIN      
        1 msyaqslntr llgalasygf daaphvepvt qgvaspsrls tewagfrvig angncyvkvl
       61 qadmaqlidv eqaaqaseca grsgaaprll gadqthgvli fedlgpqwrt arlddllapg
      121 rldalwalkr qvhagpapdf trspmtdier lralckrdgv alpaehqwid rcvdmvwqal
      181 qkrqlrsvpv hgdgvasnvm vsgdgqlrlv dfdyggcmdp wydvaitlne lysfesewra
      241 gisawagqcl eidyavcrly alindwywtl wgfwsgstsa rqlefskvgq wtllrcrqcv
      301 qdprlegwmr qiqegra
//
LOCUS       WP_005618502             428 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Pseudomonas
            avellanae].
ACCESSION   WP_005618502
VERSION     WP_005618502.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas avellanae
  ORGANISM  Pseudomonas avellanae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 428)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 428)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Pseudomonas avellanae"
                     /db_xref="taxon:46257"
     Protein         1..428
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47492
     Region          16..413
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mleqvnvfye gwgerwqwgt lvsttaltgr plivfeysne arqrglelss ytlpleggql
       61 rrdfpdhqlh lpgpvydalp dgwglllmdr mfrrcgltta rigslerlay igshamgalt
      121 fepvapkgqe skvhipleql aaevqevlhg dgdeflqtll lvggspqgar pkalvyrdpe
      181 tggfttavtp rfeawlvkfp akeehaevca iemvyaeclr mcgietpdtq yfrlpdglaa
      241 faskrfdrrd glripmqsls aftganyrsp gvldyvnflr atkmctndvr emavaferav
      301 fnvafnnrdd hpknfayims qdgqwklspa ydvtfcegpg gyhqmdvmge alsisrtqml
      361 rlaeeaevpe dvagrmidgi cdvasrfati aesicpgait pdslrmvqgc idqnvarldr
      421 gyvgggrr
//
LOCUS       WP_005618806             345 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas avellanae].
ACCESSION   WP_005618806
VERSION     WP_005618806.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas avellanae
  ORGANISM  Pseudomonas avellanae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 345)
  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   6  (residues 1 to 345)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Pseudomonas avellanae"
                     /db_xref="taxon:46257"
     Protein         1..345
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38941
     Region          32..212
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          100..336
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtlksdwyea dsrfipghyq patlidlals rgidshrllk gtglfyediv agktrlspqq
       61 cfalianaqr qmdaddtsfl fgqrlfpghy gaashalrha qnlhqaleil lrqqallspl
      121 ltprleldeh faylywldsc gageqqrfll easmtalvam sqlvgnarlp wecsfcheep
      181 ryveqywvhl gentafgrpl dmmrlprhcl tqawpgaspi avqvaqqeaa gqlaalgmqa
      241 slldrlhqhl rdnvreaasl eqvaqafams patlkrklhk hgtsfqaqhd larkhvalyl
      301 yqikgmsnea vadylnfndp anfrrsfkrw tgstptliqr lfnfd
//
LOCUS       WP_005603522             364 aa            linear   BCT 20-JAN-2025
DEFINITION  threonine synthase [Actinobacillus pleuropneumoniae].
ACCESSION   WP_005603522
VERSION     WP_005603522.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus pleuropneumoniae
  ORGANISM  Actinobacillus pleuropneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
REFERENCE   1  (residues 1 to 364)
  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 364)
  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   3  (residues 1 to 364)
  AUTHORS   Parsot,C.
  TITLE     Evolution of biosynthetic pathways: a common ancestor for threonine
            synthase, threonine dehydratase and D-serine dehydratase
  JOURNAL   EMBO J 5 (11), 3013-3019 (1986)
   PUBMED   3098560
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10107605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Actinobacillus pleuropneumoniae"
                     /db_xref="taxon:715"
     Protein         1..364
                     /product="threonine synthase"
                     /EC_number="4.2.3.1"
                     /GO_function="GO:0004795 - threonine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009088 - threonine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40458
     Region          48..361
                     /region_name="Thr-synth_1"
                     /note="Threonine synthase is a pyridoxal phosphate (PLP)
                     dependent enzyme that catalyses the last reaction in the
                     synthesis of threonine from aspartate. It proceeds by
                     converting O-phospho-L-homoserine (OPH) into threonine and
                     inorganic phosphate. In plants; cd01563"
                     /db_xref="CDD:107206"
     Site            order(68,73..74,89,112,128,131..132,138,154..160,162..164,
                     176..177,208,321..323,324..325,358)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:107206"
     Site            order(95,121,221..225,356)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:107206"
     Site            95
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107206"
ORIGIN      
        1 mkficnqcqq iapvstrqak cqcgglwtld yqppkfdlne idqhewnlfr yrkfialqde
       61 swrdislgeg mtpivrfden vllkmdyfmp tlsfkdrgaa vlishcksig vdsvvqdssg
      121 nagnsvaayc akagiqceif vpegtspkki nmieshgaka nvikgsrdhc advcrakven
      181 egvyyanhvy npffyegtkt yiyetfeqlg ripkhivvpv gndtlfigvi kglehllesg
      241 videmptiia lqseycdpll qavkkgqkfa eqveikptia egiaigqpmr aseilayaek
      301 yairfvhape dkiiaarnal akkgiyceht taanyaaylh ycelygaved clitmcgtgl
      361 ksdh
//
LOCUS       WP_005620828             194 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Actinobacillus
            pleuropneumoniae].
ACCESSION   WP_005620828
VERSION     WP_005620828.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus pleuropneumoniae
  ORGANISM  Actinobacillus pleuropneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Actinobacillus pleuropneumoniae"
                     /db_xref="taxon:715"
     Protein         1..194
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21395
     Region          2..187
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mkqriiigis gasgfqygyk alellksldv ethlvltkga emtrsletdi ereqlldlas
       61 qvhsihnvga niasgsfktl gmlvapcsir tlsaialgfs nnlltraadv vlkerrklvl
      121 mvretplnla hidnmrrvte mggiifppvp afyqhpttid elvthsvara ldlfdfdlpm
      181 prwgeannke kecl
//
LOCUS       WP_005621489             191 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Actinobacillus ureae].
ACCESSION   WP_005621489
VERSION     WP_005621489.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus ureae
  ORGANISM  Actinobacillus ureae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
REFERENCE   1  (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   2  (residues 1 to 191)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Actinobacillus ureae"
                     /db_xref="taxon:723"
     Protein         1..191
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19650
     Region          121..190
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkslktllal giamtvsavs faevanplts vnnnaksavs nqvtqaknsv ankvptaket
       61 lataktqvta tdkvtnakea lntskvskan alddvkasak ekvravktqa aektavpakt
      121 savkvpaatk vnvnmadakt lqtisgigev kaqaiidyrn kvgkiknaae lsnisgigea
      181 tiqkvvpyls f
//
LOCUS       WP_005622057             356 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Actinobacillus ureae].
ACCESSION   WP_005622057
VERSION     WP_005622057.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus ureae
  ORGANISM  Actinobacillus ureae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Actinobacillus ureae"
                     /db_xref="taxon:723"
     Protein         1..356
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=40170
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 maisvkqink hfeqfqalnn idfsiqngel nallgpsgcg kttllriiag letatsgqil
       61 fddcdvtqls akerdigfvf qhyalfrhmt iadniafglr mkpkqerlse aeiqakvknl
      121 leliqlehig grypdqlsgg qrqrvalara iatepkvlll depfgaldak vrkdlrrwlr
      181 dfhheinlts ifvthdqnea levadkiilm nkgqieqigt peqvykqprs afvanflgdv
      241 nilhgyilag mlhidtfkkp ieqyyaaddv vvyvrpheia iskthkensl kgiisrvhta
      301 gptvflevlh knhepieisv syaqfgqeqf avgdevyfqp lllnffvqnd liefmi
//
LOCUS       WP_005622749             586 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Actinobacillus ureae].
ACCESSION   WP_005622749
VERSION     WP_005622749.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus ureae
  ORGANISM  Actinobacillus ureae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Actinobacillus ureae"
                     /db_xref="taxon:723"
     Protein         1..586
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=67929
     Region          31..467
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mpeifsegki dfdkfqqlfs dkistepdry hlnwagksqa yqqlqiptqk tltpcveesv
       61 dfeqtqnili egenldvlka lqksyfnsik miyidppynt gndfvyndnf aqsqtdyqaq
      121 tgeigedgfl kkafrknake nghfhsnwln mmlprlhlar nllkddgvif isiddneqaq
      181 lkllcgevfg eenfvanviw khteqnknde kyfsrqfnyl lvykksnaln kfrfprteqd
      241 nvnysnpdnd pkgkwrsgdv rspnfrktlc fnittpsgki isppdngwrw neesikekia
      301 tgeiifiade tkivrkiyls eqegrvpenl wqgelsgttr isnaeikdif enaifdtpkp
      361 trflkrimel fhfdkdylvl dffagsstta havmqlnaed ngnrrficvq lpeetdekse
      421 aykagfknia eiskerirra gsqilqknee nrpldvgfkv fkltdshfkq wqsptaenla
      481 qqlemfidnv kenaepqaml yeillrlglk ltcnvryenn ifwiedeksq hyaillehid
      541 enllnsvinv qpqkvvaldr lfagnyalkk naelqmkdan iaffvi
//
LOCUS       WP_005624806             166 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Actinobacillus ureae].
ACCESSION   WP_005624806
VERSION     WP_005624806.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus ureae
  ORGANISM  Actinobacillus ureae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Actinobacillus ureae"
                     /db_xref="taxon:723"
     Protein         1..166
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17504
     Region          <2..>39
                     /region_name="Peptidase_M10_C"
                     /note="Peptidase M10 serralysin C terminal; cl23859"
                     /db_xref="CDD:451582"
     Region          <9..122
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mlcgtelkdl idggagndtl ygfgghdnlf ggeghdilvg glgagdylsg gvgsdtyifs
       61 gdfghdvvad kgaksdfdli rftdlnseev tfslkgsnlf itdttdegnf ievvnylndg
      121 ansieqfdfk dgsatvdvvy ntdgscdicv sytpvqvqqe qvsfya
//
LOCUS       WP_005625565             581 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Haemophilus
            haemolyticus].
ACCESSION   WP_005625565
VERSION     WP_005625565.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus haemolyticus
  ORGANISM  Haemophilus haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Haemophilus haemolyticus"
                     /db_xref="taxon:726"
     Protein         1..581
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=64203
     Region          3..560
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mmidkrlint vadskkwigv tvlwnwvalv ggiisavvfs yilqaayfke ltmsgavglg
       61 viliaalalr afagkksvqa syfastkvkh elrsliyrkl asmplnqvnq qstssiiqva
      121 segveqleiy fgrylpqlfy sllapltlfa fliffsfkta iillicvpli pmsiiavnki
      181 akkllakyws iyvglgssfl dnlqglitlk iyqddaykak amdeeaehfr kitmkvltmq
      241 lnsvslmdll ayggaaigil tallqfqdaq lsvlgvilfi llsseffipl rllgsffhva
      301 mngkaasdki ftlldtpven qqsavdfeak nnvqveikdl hfaysaekpa iqgltltiqp
      361 nqlsvfvgks gcgkstlvsl lmgfnkaqqg eilfngqnas eidrtsfyqk vslvshssyv
      421 fkgslrenmt makidatdeq iyacleqvnl aqfvrenggl dmpllsrgan lsggqiqrla
      481 larallhnae lyifdeatsn idveseeiil qfiqqfkqqk tivmishrla navnadcinv
      541 ldqgklieqg thetlmakqg ayaemfqqqk dleqirevan a
//
LOCUS       WP_005627581             406 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Mycolicibacterium hassiacum].
ACCESSION   WP_005627581
VERSION     WP_005627581.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium hassiacum (Mycobacterium hassiacum)
  ORGANISM  Mycolicibacterium hassiacum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 406)
  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 406)
  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   3  (residues 1 to 406)
  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   4  (residues 1 to 406)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 406)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 406)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Mycolicibacterium hassiacum"
                     /db_xref="taxon:46351"
     Protein         1..406
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42054
     Region          81..405
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(152..154,175..176,225,276,300)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mrgrvargav avgsagllvl giagcqqqeg sgsengtaas dlkiveqvqi dqdgkevppp
       61 eagdaadpag dgnaecppva iamagalngp daalginikn giqlaidkhn aanpgcqvql
      121 ktfdtegdpq kasqvapriv ddasiiglig pafsgetnat gdvfnqaglv avtasatnvt
      181 lsekgwrtff rglgndgvqg pavanyiknt lghqkvcvvd dstdygvgla qavretlgpv
      241 adqscnssvk kgdkdfsvav nqvksadads vffsgyyaea apfvqqlrda gfegvffsad
      301 gtkdpefvkq agsasrdall scpcgpatgd faeeyttkfg qepgtysseg ydlatillkg
      361 idsgavtrpq lleyvrdydg qgiarryqws ptgeltssli wiykvq
//
LOCUS       WP_005627728             364 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Mycolicibacterium hassiacum].
ACCESSION   WP_005627728
VERSION     WP_005627728.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium hassiacum (Mycobacterium hassiacum)
  ORGANISM  Mycolicibacterium hassiacum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Mycolicibacterium hassiacum"
                     /db_xref="taxon:46351"
     Protein         1..364
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37624
     Region          20..350
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mtravtglyl ravveergvd vefevapgev lavigpngag kstalhvvag lirpdagqvr
       61 lgarvltdta agthvpthdr rvglllqdpl lfphlsvaan vafsprssra aatrwlaeve
      121 aaelaerrpr qlsggqaqrv alaralaaep qvllldepma gldvaaaaai rtllrrvlar
      181 dgrcavlvth dlvdvltlad rvlvlesgrv aecgpaaavl agprsgfaar fagvnlvrgv
      241 ataagvlttd wgqqwhgtad gepavgrpav avfppaavav yrerphgspr ntvavtiagl
      301 dahgstvrlr gadqpdgapg laaditaeaa aelrpapger vfftvkaqev rllpgpdsge
      361 rqvs
//
LOCUS       WP_005627992             319 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Mycolicibacterium hassiacum].
ACCESSION   WP_005627992
VERSION     WP_005627992.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium hassiacum (Mycobacterium hassiacum)
  ORGANISM  Mycolicibacterium hassiacum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Mycolicibacterium hassiacum"
                     /db_xref="taxon:46351"
     Protein         1..319
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34139
     Region          1..309
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 maaplllldg asmwfrsyfg vptsitapdg rpvnavrgfl davatvitre rpsrlvvcrd
       61 ddwrpqwrvd lipsykahrv leetpgddpd veevpddltp qvdmifeild afgiptagap
      121 eheaddvlgt lvarerrdpv vvvsgdrdll qlvrdepvsv rvlylgagla katkwgpaev
      181 aekygvpidr agpayaelal lrgdpsdglp gvpgigekta aallarhgsl agilaaardp
      241 dssmskahrr kllaaadyia raeavvkvav dadldwstpt delpltardp atvaelaery
      301 gvvspvgrlq kaldslpdr
//
LOCUS       WP_005628453             207 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Haemophilus haemolyticus].
ACCESSION   WP_005628453
VERSION     WP_005628453.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus haemolyticus
  ORGANISM  Haemophilus haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 207)
  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   2  (residues 1 to 207)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Haemophilus haemolyticus"
                     /db_xref="taxon:726"
     Protein         1..207
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21860
     Region          139..206
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkslksllsv taltlaisgs alanenplat lkdvakdnvk ttvsenvksv kdsasaakgn
       61 vlekvsstke kategvssvk ekmaatkekv dsvkdkakal kdssseyshk alkhkaadkv
      121 ketkekaaek mnsakdnvks vvdsakinin kadantlqql sgigekkaqa iidyrnkvgk
      181 ikdiaelski dglgsttiek iapfltf
//
LOCUS       WP_005629400             157 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Haemophilus haemolyticus].
ACCESSION   WP_005629400
VERSION     WP_005629400.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus haemolyticus
  ORGANISM  Haemophilus haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Haemophilus haemolyticus"
                     /db_xref="taxon:726"
     Protein         1..157
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17332
     Region          11..151
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdifsffsad fwqthalclm ffsaflsatv lpgnsevifv alavpklmlg slfnadilal
       61 iliatagnsl gslttygigr wmpkfdpknh rtlwvtnqik rygaitllls wlpvvgdlfc
      121 aiagwlrlnf vvssvfiflg klvryvallf fsapfll
//
LOCUS       WP_005629726             317 aa            linear   BCT 20-JAN-2025
DEFINITION  DNA polymerase domain-containing protein [Mycolicibacterium
            hassiacum].
ACCESSION   WP_005629726
VERSION     WP_005629726.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium hassiacum (Mycobacterium hassiacum)
  ORGANISM  Mycolicibacterium hassiacum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Zhu,H., Nandakumar,J., Aniukwu,J., Wang,L.K., Glickman,M.S.,
            Lima,C.D. and Shuman,S.
  TITLE     Atomic structure and nonhomologous end-joining function of the
            polymerase component of bacterial DNA ligase D
  JOURNAL   Proc Natl Acad Sci U S A 103 (6), 1711-1716 (2006)
   PUBMED   16446439
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Zhu,H. and Shuman,S.
  TITLE     A primer-dependent polymerase function of pseudomonas aeruginosa
            ATP-dependent DNA ligase (LigD)
  JOURNAL   J Biol Chem 280 (1), 418-427 (2005)
   PUBMED   15520014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Mycolicibacterium hassiacum"
                     /db_xref="taxon:46351"
     Protein         1..317
                     /product="DNA polymerase domain-containing protein"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=34686
     Region          9..287
                     /region_name="LigD"
                     /note="Eukaryotic-type DNA primase [Replication,
                     recombination and repair]; COG3285"
                     /db_xref="CDD:442515"
ORIGIN      
        1 mttrerrygv eltnldepls plagatkrdl vdyldeiady llpaladrpl tvlrvlrgqr
       61 pfmqkntpky tpewvptvti waessqrqvr yplcndrrtl lwlanqrave yhpalgladn
      121 iyrpthlvld ldppdddfak vvavaqlvrq tlddhglvga vktsgakglh vfvpvadtga
      181 ddvaaatral aaraaaldpa iattayiktd ragkvfvdst raggatvvaa ysprlrpglp
      241 vsfpldwadl dtvtpgdftv ytavdaaaer psweqlmapp qrlpeelief ghtipvarva
      301 amhegrrrar arrqagd
//
LOCUS       WP_005630086              84 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Mycolicibacterium hassiacum].
ACCESSION   WP_005630086
VERSION     WP_005630086.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium hassiacum (Mycobacterium hassiacum)
  ORGANISM  Mycolicibacterium hassiacum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 84)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 84)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 84)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 84)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Mycolicibacterium hassiacum"
                     /db_xref="taxon:46351"
     Protein         1..84
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8612
     Region          4..84
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mtvqltiryf aaaraaagtd eqiiavepgt tiaalvdrlg adkpelakvl qrcsflldgv
       61 atrdrdtlld gagsvdvlpp fagg
//
LOCUS       WP_005630993             115 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Haemophilus haemolyticus].
ACCESSION   WP_005630993
VERSION     WP_005630993.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus haemolyticus
  ORGANISM  Haemophilus haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (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   2  (residues 1 to 115)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Haemophilus haemolyticus"
                     /db_xref="taxon:726"
     Protein         1..115
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12157
     Region          46..114
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mklmktlfts milcgalgas safaeekate qavqpvvatq teaqvastav sdklnintat
       61 aseiqkaltg igakkaeaiv qyrekhgnft saeqllevqg igkatlernr dritf
//
LOCUS       WP_005632259             581 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Haemophilus
            haemolyticus].
ACCESSION   WP_005632259
VERSION     WP_005632259.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus haemolyticus
  ORGANISM  Haemophilus haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Haemophilus haemolyticus"
                     /db_xref="taxon:726"
     Protein         1..581
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=64236
     Region          3..560
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mmidkrlint vadskkwigv tvlwnwvalv ggiisavvfs yilqaayfke ltmssavglg
       61 viliaalalr afagkksvqa syfastkvkh elrsliyrkl asmplnqvnq qstssiiqva
      121 segveqleiy fgrylpqlfy sllapltlfa fliffsfkta iillicvpli pmsiiavnki
      181 akkllakyws iyvglgssfl dnlqglitlk iyqddaykak amdeeaehfr kitmkvltmq
      241 lnsvslmdll ayggaaigil tallqfqdaq lsvlgvilfi llsseffipl rllgsffhva
      301 mngkaasdki ftlldtpvet qqsavnfeak nnvqveikdl hfaysaekpa iqgltltiqp
      361 nqlsvfvgks gcgkstlvsl lmgfnkaqqg eilfngqnas eidrtsfyqk vslvshssyv
      421 fkgslrenmt makidatdeq iyacleqvnl aqfvrenggl dmqllsrgan lsggqiqrla
      481 larallhnae lyifdeatsn idveseeiil qfiqqfkqqk tivmishrla navnadcinv
      541 ldqgklieqg theslmakqg ayaemfqqqk dleqirevan a
//
LOCUS       WP_005632657             157 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Haemophilus haemolyticus].
ACCESSION   WP_005632657
VERSION     WP_005632657.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus haemolyticus
  ORGANISM  Haemophilus haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Haemophilus haemolyticus"
                     /db_xref="taxon:726"
     Protein         1..157
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17171
     Region          11..151
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdifsflsad fwqthalclm fvsaflsatv lpgnsevvfv alavpklvlg slfsadilal
       61 iliatagnsl gslttygigr wmpkfdpkny rtlwainqlr rygaiallls wlpvvgdlfc
      121 aiagwlrlnf vasslfiflg klvryvallf fsapfll
//
LOCUS       WP_005633112             192 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Haemophilus haemolyticus].
ACCESSION   WP_005633112
VERSION     WP_005633112.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus haemolyticus
  ORGANISM  Haemophilus haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Haemophilus haemolyticus"
                     /db_xref="taxon:726"
     Protein         1..192
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21534
     Region          3..164
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mkifgtmydk tmqwsthrfa tfwlsfvsfi eaiffpippd vmlipmsmsk pksavkfafy
       61 taiasviggv igyaigyyat dwvenivqqw gygahwakai nwfeqwgvlv vfvagfspip
      121 ykvftlcsgv mqmaffpfai tafisrlarf llvaklaawg gekfaaklrk sieiigwsvv
      181 alaviayfil kn
//
LOCUS       WP_005633541             495 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Parabacteroides merdae].
ACCESSION   WP_005633541
VERSION     WP_005633541.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides merdae
  ORGANISM  Parabacteroides merdae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Parabacteroides merdae"
                     /db_xref="taxon:46503"
     Protein         1..495
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54055
     Region          3..495
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mrtyiqinpa dnvvvavknl qtgvslding rtivvlqdip aghkvalqdf kegdhvikyg
       61 apigharevi ttgswvnekn iktnleglre yefnpqpipe qpsgkslsfk gyrrkngevg
      121 irneiwvipt vgcvngithr ladrlrqetq gtgvdaivaf phnygcsqlg ddhentrkil
      181 rdmvlhpnag avlvvglgce nnqvgafrem lgnydterir fmetqkvdde letgmellrk
      241 lyaiasqdkr tdiplselhv glkcggsdgf sgitanpllg vfsdflvaqg gttvltevpe
      301 mfgaetilmn rseskavfek tvhlindfks yfienkqpiy enpspgnkag gistleeksl
      361 gctqkagtsa vrdvmlyger lktkglnlls apgndlvast alassgchlv lfttgrgtpf
      421 gtfvptvkvs tnsnlnarkp nwidfnagsl legesmeelr erfirfiigi asgnptnnek
      481 ndyreiaifk sgvtl
//
LOCUS       WP_005633698             404 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Parabacteroides merdae].
ACCESSION   WP_005633698
VERSION     WP_005633698.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides merdae
  ORGANISM  Parabacteroides merdae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 404)
  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 404)
  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
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 404)
  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   5  (residues 1 to 404)
  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   6  (residues 1 to 404)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 404)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 404)
  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 19786117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Parabacteroides merdae"
                     /db_xref="taxon:46503"
     Protein         1..404
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44548
     Region          20..>65
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
     Region          81..393
                     /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 mntkfllssd nnnrnellkk kiihyyiang datiadlgre mdlsiptvtk lvaelqddgy
       61 ildfgkqetn ggrkpniygl npasgyfvgv dmlkdklnia aidfkgdkvq leenipyqle
      121 ntpasleqfc kiiddfivsl pvernkilai gvnitgrvnp asgysysify feekplaqil
      181 eerlqtkvfi endsramtyg eymkgvvqge knilfvnmaw glglgiiidg nlyygksgfs
      241 gefghfcmfe nevlchcgkk gcleteasgs afhriliery regsntilag kldsgeeisl
      301 gdlleavrke dvlcidilek mgvnlgkgia glmnifnpel vilggtlsla geyislpiks
      361 airkyslnlv nqdteikisk lgeragafga cllsrskllg mihy
//
LOCUS       WP_005634095             204 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Haemophilus haemolyticus].
ACCESSION   WP_005634095
VERSION     WP_005634095.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus haemolyticus
  ORGANISM  Haemophilus haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 204)
  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 204)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 204)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Haemophilus haemolyticus"
                     /db_xref="taxon:726"
     Protein         1..204
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22520
     Region          1..204
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 maysieeeqe inqlkdwwke ngktiivafi lgvggmfgwr ywqahqaeqi aqasaqydal
       61 iysaqqdeqa kkanieqfvq ansktayavf alldeakkvt ekqdfaaaea nlnqaltqsq
      121 devltsival rlsavqfqlg qldnalttln qvkgesfnar kailtgdiqv akgdkvaakn
      181 sfeqaqqsgs qleqqmakmk lnnl
//
LOCUS       WP_005635269             343 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Haemophilus
            haemolyticus].
ACCESSION   WP_005635269
VERSION     WP_005635269.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus haemolyticus
  ORGANISM  Haemophilus haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 343)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Haemophilus haemolyticus"
                     /db_xref="taxon:726"
     Protein         1..343
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=39659
     Region          <55..330
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mnfcrillkp lkknealsgy steglhyltg nknfnpelpf srqefitvkp qkqqgmsisg
       61 fqpklqliik dehfdsvnqq gnyilkpspe eypflaeneh atmrimkelg fdvpenglvs
      121 fageenqkef afvikrfdrd eqqkpmhqeq ldgamnirdk ygkigadneq yvsyeqiakf
      181 ilqhtenhla qqreifrrii yayllgnndl hlrnfsfiyp knshpklapi ydfvsvspyp
      241 eifnstllal pllareegna tlakgfntqy geyigddfve fgeniglnkn viiqklipei
      301 tqekekveqi ysqsfmpqvh idcvlknyrk rlallnvlne pel
//
LOCUS       WP_005636585             255 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Tritonibacter mobilis].
ACCESSION   WP_005636585
VERSION     WP_005636585.1
KEYWORDS    RefSeq.
SOURCE      Tritonibacter mobilis
  ORGANISM  Tritonibacter mobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Tritonibacter.
REFERENCE   1  (residues 1 to 255)
  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 255)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Tritonibacter mobilis"
                     /db_xref="taxon:379347"
     Protein         1..255
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27877
     Region          1..255
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mpkfaanlsm lfaelpyldr fsaaaaagfe avevlfpyef aaketqrall anglelllin
       61 apppnytggd pgyaavpeqa drfqrdirrv lryadmlkag rihvmagpak gdaaretfvq
      121 nlraaadsap qqqftiepln ngdfpgyfld dynlavdild evgrdnvtlq fdayhaqlih
      181 gdalkvweaf gdrathvqfa aapsrcepgn gpldfdalfa aiddsgyqgw vsaeytpstp
      241 rtedslrwmr alqaa
//
LOCUS       WP_005638987             270 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Parabacteroides
            merdae].
ACCESSION   WP_005638987
VERSION     WP_005638987.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides merdae
  ORGANISM  Parabacteroides merdae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (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   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Parabacteroides merdae"
                     /db_xref="taxon:46503"
     Protein         1..270
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30979
     Region          3..112
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          <62..255
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 myteyqpcgl lsayidkywv fkgktelgty fkilpdgccd fifsigdtaq cvgtnqpvmq
       61 pyrcffvgpm ttfselvtnt psvhmlgvrf hpcgltafck pplseftnqr iscndltllf
      121 tdsfaeslce aqtlqqqicl ierflihrlk dnyeidpqip favqqinrsk grlpilqlmd
      181 eicicqrhfe rkfkaytgyt pkeyswimkf rntidllknc ipdnlltiav eagyydlshf
      241 nkeirqlsgn tpasflsipi pedvlltyle
//
LOCUS       WP_005639694             294 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: hydroxypyruvate isomerase family protein
            [Parabacteroides].
ACCESSION   WP_005639694
VERSION     WP_005639694.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 294)
  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 294)
  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 11466508
            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="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32779
     Region          47..294
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mknisrrtai ktvlagsaam avsgmeaaap akkkkvekpe plkgnirhsv skwcfgsypl
       61 defceickni giesielldp kdwpivqkhg ltvamaqgag lgidrgfndp klhdelvasy
      121 eqvipmvaea gltnlicfag rrngvtdlqg wencekglkr lmpiaekynv vltmellnsv
      181 ghkdylcdht vwgaelcrri gspnfkllyd iyhmqimegn viehirkyhq yfshihtggv
      241 pgraeidetq elyypaimka ivetgykgfv gqefvpkqed kiaslekcir icdv
//
LOCUS       WP_005639837             165 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Tritonibacter mobilis].
ACCESSION   WP_005639837
VERSION     WP_005639837.1
KEYWORDS    RefSeq.
SOURCE      Tritonibacter mobilis
  ORGANISM  Tritonibacter mobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Tritonibacter.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Tritonibacter mobilis"
                     /db_xref="taxon:379347"
     Protein         1..165
                     /product="TRAP transporter small permease subunit"
                     /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=18237
     Region          1..159
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mlrvadaldg inrglahvir wlallmvlaq faivvgryvf gvnsiaaqes vlymhstlfm
       61 laagytllvd khvrvdvfya glsprgqrri difghvflll psmmallyws wpsvrnswsi
      121 legpiavggi eavfllksli pafcvlimlq svallirllc erpaq
//
LOCUS       WP_005639972              97 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein
            [Parabacteroides].
ACCESSION   WP_005639972
VERSION     WP_005639972.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..97
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11088
     Region          3..97
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mrskeeymel lrsyflnkak aygvvkmalf gsvvrgeqte tsdvdvayeg kadillrcrm
       61 kqeledlfgc rvdiirlreq lsgtaflqni skellyv
//
LOCUS       WP_005640876             157 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Haemophilus].
ACCESSION   WP_005640876
VERSION     WP_005640876.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus
  ORGANISM  Haemophilus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Haemophilus"
                     /db_xref="taxon:724"
     Protein         1..157
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17256
     Region          11..151
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdifsffsad fwqthalclm fvsaflsatv lpgnsevvfv alavpklalg slfstdilal
       61 vffatlgngl gslttygigr wmpkfdpknh ctlwvmnqik rygaitllls wlpvvgdlfc
      121 aiagwlrlnf vvssvfifig klvryvallf fsapfll
//
LOCUS       WP_005641906             686 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate--CoA ligase family protein [Parabacteroides].
ACCESSION   WP_005641906
VERSION     WP_005641906.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..686
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=74885
     Region          6..686
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 minrelinpq sivvvggsnn vhkpggrlvr nlldgkykge lyvvnakedd vqglksyhsv
       61 hdipetelai isipgpacpe avdvlakqkn vkafivisag fgeethegai leeqmlksin
      121 eagasligpn ciglmnmhyh gvftqpipef hadgvdfiss sggtalfiie saltkglrfs
      181 svwsvgnskq igveevieym drnfdpvlds kikmlyieqi knpdkllyha sslirkgchi
      241 aaikagstdv gkraasshtg aiansdsave alfrkagivr cfsreelttv asiftlkevk
      301 gkncaiitha ggpavmlada lekgrlnvpk ldgplaaelk sklypgaavg npidiigtgt
      361 pehlataidf cencfedidl mmvifgspgl vklydtyevl hkkmeeckkp ifpvlpsivt
      421 agpevksfvk kghvnfsdev tlgtalsrvl ntpkpmstdi qlygvdvpev rriidrlpgs
      481 gylnpeevrt llkaaqiplv eeftstdrde lvafakrvkf pvvakvvgpi hksdmggval
      541 nirseehlif eyermmrlpd vtavmvqpml kgqelflgak yedrfghvvl cglggifvev
      601 lkdvsyglsp lsydetysmi rslrgypiik gtrgqrgvde qqyadiivrl stllrfasei
      661 kemdinplva terglfavda ririek
//
LOCUS       WP_005641206             391 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Parabacteroides].
ACCESSION   WP_005641206
VERSION     WP_005641206.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 391)
  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 391)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 391)
  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   4  (residues 1 to 391)
  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 391)
  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 11454538
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44173
     Region          130..390
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          313..390
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mdihtlyiia yatsttsclg scaillflny gnietnpvyl karrilafat flvaigllis
       61 lttrkwqpvg wdiasfpvtl iassqtllft fslillfneq yatrqrillh atpsllftla
      121 yagacliwkd hpvyaysewk slvtnppsli rtlyllayii qsgiyaklfl herhtylsll
      181 ggvktedrwl klgqvtsaff lasgiglctl slalnphlph eitvtflftv fyfafgifya
      241 nfsstyrdvr trireqnsaf sppagadmee licylqpddd nnrlfkdiea yfqkeqpyld
      301 pdfrisdlpr tiganphkls tavgratglt vqdyvlrlri ghsadllllp enaertiedi
      361 afssgfqsts tynrnflklm kttpsrfrsr t
//
LOCUS       WP_005631673              69 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TOBE domain-containing protein [Haemophilus].
ACCESSION   WP_005631673
VERSION     WP_005631673.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus
  ORGANISM  Haemophilus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae.
REFERENCE   1  (residues 1 to 69)
  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 10015732
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Haemophilus"
                     /db_xref="taxon:724"
     Protein         1..69
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=6991
     Region          1..69
                     /region_name="Mop"
                     /note="molybdenum-pterin binding domain; TIGR00638"
                     /db_xref="CDD:273189"
ORIGIN      
        1 mkisarnqlk gkvvsiengs vnaivhidig ggnvlsstvs laavkelnle vgkeayaiik
       61 atsvmvgve
//
LOCUS       WP_005644989             301 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Parabacteroides].
ACCESSION   WP_005644989
VERSION     WP_005644989.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..301
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32569
     Region          25..267
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mttscspkve mipaelayqa eattgegsiw hperhtlfwv diegqtlyey hpdtkecssw
       61 kfdrmvstvv petdstviia lqdeivrvnl hdghttsiap ipdengkvrc ndgkcdpagh
      121 lwvgtmgfga pkgagtlytv spagtvttkl kkvtisngiv wssnkkfmyy ndtptgkiar
      181 yrydadngdi lfdgiavtlp ggtgvpdgma idsddhlwva qwggygvycy npytgellak
      241 vevpapnvas cafggkkmdt lyittaragl seeqlreypl sgsvfcckpg vkgirancfg
      301 e
//
LOCUS       WP_005646772             115 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Haemophilus haemolyticus].
ACCESSION   WP_005646772
VERSION     WP_005646772.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus haemolyticus
  ORGANISM  Haemophilus haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (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   2  (residues 1 to 115)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Haemophilus haemolyticus"
                     /db_xref="taxon:726"
     Protein         1..115
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12219
     Region          46..114
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mklmktlfts vvlcgalvas safaeektae qavqpvvatq teaqvapatv sdklnintat
       61 vseiqkvltg igakkaeaiv qyrekhgnft saeqllevqg igkatlernr dritf
//
LOCUS       WP_005648795             248 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Parabacteroides].
ACCESSION   WP_005648795
VERSION     WP_005648795.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 248)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..248
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=27139
     Region          51..215
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mllriclylf llflpanytt trsssplipa dpaaamssvc rqlyadmqld smvdytafeq
       61 aitgaqaier rnkdiitlid ftkpsteerl yvldirhkrl lfsslvshgk nsggnyatsf
      121 snkvnsykss lgffvtenty qgkngyslvl nglekgindr akeraivvhg anycspsvav
      181 stgrlgrsfg cpalppslak piintikdgt llyiyandke ylsqstilst grsispnsii
      241 alnslire
//
LOCUS       WP_005650516             232 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Haemophilus
            influenzae].
ACCESSION   WP_005650516
VERSION     WP_005650516.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus influenzae
  ORGANISM  Haemophilus influenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
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   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 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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Haemophilus influenzae"
                     /db_xref="taxon:727"
     Protein         1..232
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26269
     Region          16..67
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msmrlmvqam nckvgnpark lvllkladna nddgicfpsy qyiadkcemt rrsaishiec
       61 likmglvskk erknkdgsis nlyflhleqg senfalggen islgsekfap itshslepvn
      121 epkkttqkse semllerfgi tgqlakdfia hrktkrgais etqlsrlqkq adkagisice
      181 vveiciernw qgfnaswdwr deklrtsqaq kmsfeeknal pwnrpedwen vl
//
LOCUS       WP_005650743             192 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Haemophilus influenzae].
ACCESSION   WP_005650743
VERSION     WP_005650743.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus influenzae
  ORGANISM  Haemophilus influenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Haemophilus influenzae"
                     /db_xref="taxon:727"
     Protein         1..192
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21513
     Region          3..164
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mkifgtmydk tmewskhrfa afwlsfvsfi eaiffpippd vmlipmsmsk pkgavkfafy
       61 taiasviggi igyaigfyat dwvenivqqw gyaahwakav swfeqwgvlv vfvagfspip
      121 ykvftlcsgv mqmaffpfvi tafisrlarf llvaklaawg gekfaaklrk sieiigwavv
      181 vlaviayfil kn
//
LOCUS       WP_005650824             343 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Haemophilus
            influenzae].
ACCESSION   WP_005650824
VERSION     WP_005650824.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus influenzae
  ORGANISM  Haemophilus influenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 343)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Haemophilus influenzae"
                     /db_xref="taxon:727"
     Protein         1..343
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=39725
     Region          <55..330
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mnfcrillkp lkknevhsgy stkglhyltg nknfnpelpf srqefitvkp qkqqgmsisg
       61 fqpklqliik dehfdsvnqq gnyilkpspe eypflaeneh atmrimkelg fdvpenglvs
      121 fageqnhkef afvikrfdrd eqqteihqeq ldgamnirdk ygkigadneq yvsyeqiakf
      181 ilqhtenhla qqreifrrii yayllgnndl hlrnfsfiyp knshpklapi ydfvsvspyp
      241 eifnstllal pllareegna tlakgfntqy geyigddfve fgeniglnkn viiqklipei
      301 iqekekveqi ysqsfmpqph idcvlktyrk rlallnvlhe pel
//
LOCUS       WP_005652025             157 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Haemophilus influenzae].
ACCESSION   WP_005652025
VERSION     WP_005652025.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus influenzae
  ORGANISM  Haemophilus influenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Haemophilus influenzae"
                     /db_xref="taxon:727"
     Protein         1..157
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17351
     Region          16..151
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdifsffsad fwqanslcfm fisaflsatv lpgnsevifv alavpklmlg slfnadilal
       61 iliatagnsl gslttygigr wmpkfdpkny rtlwainqlr rygaiallls wlpvigdlfc
      121 aiagwlrlnf vasslfiflg kmvryvallf fstpfll
//
LOCUS       WP_005654317             192 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Haemophilus].
ACCESSION   WP_005654317
VERSION     WP_005654317.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus
  ORGANISM  Haemophilus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Haemophilus"
                     /db_xref="taxon:724"
     Protein         1..192
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21600
     Region          3..164
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mkifgtmydk tmewskhrfa vfwlsfvsfi eaiffpippd vmlipmsmsk pksavkfafy
       61 taiasviggv igyaigfyat dwvenivqqw gyavhwakav swfkqwgvlv vfvagfspip
      121 ykvftlcsgv mqmaffpfvi tafisrlarf llvaklaawg gekfaaklrk sieiigwsvv
      181 vlaviayfil kn
//
LOCUS       WP_005658520             288 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Dethiosulfovibrio
            peptidovorans].
ACCESSION   WP_005658520
VERSION     WP_005658520.1
KEYWORDS    RefSeq.
SOURCE      Dethiosulfovibrio peptidovorans
  ORGANISM  Dethiosulfovibrio peptidovorans
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Dethiosulfovibrionaceae; Dethiosulfovibrio.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   3  (residues 1 to 288)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Dethiosulfovibrio peptidovorans"
                     /db_xref="taxon:47055"
     Protein         1..288
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32610
     Region          25..77
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mernividnr kfwfarvdis vlldegiday akatyavlca yagsgrecfp saetlakkvk
       61 csrdrlfksl rilvefgvle kvtqsnksfq tvnkyiltgg adsrqavrqt dtespserlp
      121 qsvsrtpgvr qadprcpsdv hrtrdieles kndkdivgks aentaglpld pvpgeevvpq
      181 pgetpppcpy raiadlwdev mvpmgkrgvr ilsetrqntl rsrwrakgdp gappwpwadl
      241 ktwreyflyv sqskflvdgr fcdfdwvikk snwikiregk yhqegdcr
//
LOCUS       WP_005658989             581 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Haemophilus
            influenzae].
ACCESSION   WP_005658989
VERSION     WP_005658989.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus influenzae
  ORGANISM  Haemophilus influenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Haemophilus influenzae"
                     /db_xref="taxon:727"
     Protein         1..581
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=64371
     Region          3..560
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mmidkrlint vadskkwigv tvlwnwvalv ggiisavvfs yilqaayfhe lsplsavilg
       61 illiaalalr afagkksvqa sylastkvkh elrsliyrkl asmplnqvnq qstssiiqva
      121 segveqleiy fgrylpqlfy sllapltlfa fliffsfkta iillicvpli pmsiiavnki
      181 akkllakyws iyvglgssfl dnlqglitlk iyqddtykak amdkeaehfr kitmkvltmq
      241 lnsvslmdll ayggaaigil tallqfqdaq lsvlgvilfi llsseffipl rllgsffhva
      301 mngkaasdki ftlldtpvet qqsavdfeak nnlqveikdl hfsyseekpa itgldvsilp
      361 nqlsvfvgks gcgkstlvsl lmgfnkaqqg eilfngqnal nidrtsfyqk vslvshssyv
      421 fkgslrenmt makidatdeq iyacleqvnl ahfvrenggl dmqllsrgtn lsggqiqrla
      481 larallhnae lyifdeatsn idveseeiil qfiqqfkqqk tivmishrla navnadcinv
      541 ldqgklieqg theslmakqg ayaemfqqqk dleqirevan a
//
LOCUS       WP_005659063             288 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Dethiosulfovibrio
            peptidovorans].
ACCESSION   WP_005659063
VERSION     WP_005659063.1
KEYWORDS    RefSeq.
SOURCE      Dethiosulfovibrio peptidovorans
  ORGANISM  Dethiosulfovibrio peptidovorans
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Dethiosulfovibrionaceae; Dethiosulfovibrio.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   3  (residues 1 to 288)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Dethiosulfovibrio peptidovorans"
                     /db_xref="taxon:47055"
     Protein         1..288
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32708
     Region          25..77
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mernividnr kfwfarvdis vlldegiday akatyavlca yagsdrecfp saetlakkvk
       61 csrdrlfksl rilvefgvle kvtqsnksfq tvnkyiltgg adsrqavrqt dtespserlp
      121 qsvsrtpgvr qadprcpsdv hrtrdielep kndkdivgks aentaglpld pvpgeevvpq
      181 pgetpppcpy raiadlwdev mvpmgkrgvr ilsetrqntl rsrwrtkgdp gappwpwadl
      241 ktwreyflyv sqskflvdgr fcdfdwvikk snwikiregk yhqegdcr
//
LOCUS       WP_005659552             642 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Dethiosulfovibrio peptidovorans].
ACCESSION   WP_005659552
VERSION     WP_005659552.1
KEYWORDS    RefSeq.
SOURCE      Dethiosulfovibrio peptidovorans
  ORGANISM  Dethiosulfovibrio peptidovorans
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Dethiosulfovibrionaceae; Dethiosulfovibrio.
REFERENCE   1  (residues 1 to 642)
  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 642)
  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 642)
  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 642)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Dethiosulfovibrio peptidovorans"
                     /db_xref="taxon:47055"
     Protein         1..642
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=67711
     Region          1..636
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mseeilknpl pveepdskkr tltgwqytlv aglalaassf hlytaafglf aamyqrsvhw
       61 lfmgvilfli ypasknrpkd ridpldwvla illsigclni llnwqeiair qgapiasdvy
      121 lgvimvvlvi egtrramgwp lpimaiisll yaffgpyfpg ilahggipig elapfqylrt
      181 dgifgvplgv sasfiflfvl fgaflstsga gqffidlava ltgrsqggpg kaavvssalm
      241 gtvsgsscan tvttgaftip lmkqsgysse fagaivaaas tggqvmppvm gaaafimaqf
      301 lgisyweivv aaaipatlyf vsimamvhfr agkigmkrls gedlpkagkv lkegwhllip
      361 iitliaflat gyspvkavfw sivfligcsw lgkkehrmtp grilqamidg aigavdvaaa
      421 cacsgivigv igitgvglaf ssfvlslshg ilpfalmltm vgsiilgmgv pttaqyiits
      481 tlaapalaem gvpmmaahlf clyfgvladv tppvalatya asgiaksnpm ktgftaliva
      541 vagflvpymf vynhyllfqg nifqiaigcg saflciigla sgvqgyflth iniveraall
      601 atpfliiapy mtanliavgl mvavfmfqkl klsraaqlss ng
//
LOCUS       WP_005659906             204 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Haemophilus influenzae].
ACCESSION   WP_005659906
VERSION     WP_005659906.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus influenzae
  ORGANISM  Haemophilus influenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 204)
  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 204)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 204)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Haemophilus influenzae"
                     /db_xref="taxon:727"
     Protein         1..204
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22545
     Region          1..204
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 maysieeeqe inqlkewwke ngktiivafi lgvggmfgwr ywqahqaeqi aqasaqydal
       61 insvqqdeqa kkanieqfvq ansktayavf alldeakkat ekqdfsaaea nlnqaltqsq
      121 devltsiial rlsavqfqlg qldnalstln qvkgesfnar kailtgdiqv akgdkvaakn
      181 sfeqaqqmgs qleqqmakmk lnnl
//
LOCUS       WP_005660577             195 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Dethiosulfovibrio peptidovorans].
ACCESSION   WP_005660577
VERSION     WP_005660577.1
KEYWORDS    RefSeq.
SOURCE      Dethiosulfovibrio peptidovorans
  ORGANISM  Dethiosulfovibrio peptidovorans
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Dethiosulfovibrionaceae; Dethiosulfovibrio.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Dethiosulfovibrio peptidovorans"
                     /db_xref="taxon:47055"
     Protein         1..195
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=21377
     Region          3..129
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(8..11,43..45,48,72,111,125)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mvwkahfdgg srgnpgiaga gaalyddenr lvwrgaeplg ertnneaeym aailvlkevl
       61 rrglseielc gdsklvinql sgawkikepr lgvlaeefka lakglsvrfr wvprkdnsea
      121 drmanlamdg lapsddvsse keettsqavv eivvfsdgde ryfvdlprlr csceefcskg
      181 dcvhlkicrd agfap
//
LOCUS       WP_005661086             622 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Dethiosulfovibrio peptidovorans].
ACCESSION   WP_005661086
VERSION     WP_005661086.1
KEYWORDS    RefSeq.
SOURCE      Dethiosulfovibrio peptidovorans
  ORGANISM  Dethiosulfovibrio peptidovorans
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Dethiosulfovibrionaceae; Dethiosulfovibrio.
REFERENCE   1  (residues 1 to 622)
  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 622)
  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 622)
  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 622)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..622
                     /organism="Dethiosulfovibrio peptidovorans"
                     /db_xref="taxon:47055"
     Protein         1..622
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=66284
     Region          1..619
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mrklqgttak lfylyvlamg ffhlytalfg tyeaylqrai hltwvlpmaf ilypiggkke
       61 gqeltdnsip wydwilaaas lapgiyiman ytdityrmaq vdpvttaqli lgslltvlll
      121 eatrrvvglp laliaaffta ymyygnympg imkglsfsfh evieqiylid egifsiplgv
      181 satfvmifli fggfleksgv gayfmefaqa ftgtspggpa kiavvssalf gsisgaavan
      241 vygtgtftip lmkrigyppf fagaveavas tggqimppim gagafimasf lgeqfrtimi
      301 aavlpallyy savllmvhlg alknnlkgls pedlpdkkvv ikklymmspi avliyllltg
      361 ytpmlaavig igaawlvsmp nketrmgpka ildavytgak nipvvciaca aaglvvgsvs
      421 ltgigfkfvg lvfslangap fialilialv slvlgmglpt tsayilgaal gvpalaklgf
      481 dplaahmfvf yfaivsnitp pvalaayaas siadaspnkt gfqamklgil afiipfafcy
      541 dqglllsagl tnnvisvlgg igalfsmgys mlaytnhrih qwqravflvv gvaclwpmft
      601 vkiagviati vfgwlwraki in
//
LOCUS       WP_005661162             175 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Dethiosulfovibrio].
ACCESSION   WP_005661162
VERSION     WP_005661162.1
KEYWORDS    RefSeq.
SOURCE      Dethiosulfovibrio
  ORGANISM  Dethiosulfovibrio
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Dethiosulfovibrionaceae.
REFERENCE   1  (residues 1 to 175)
  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 175)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 175)
  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   4  (residues 1 to 175)
  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   5  (residues 1 to 175)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Dethiosulfovibrio"
                     /db_xref="taxon:47054"
     Protein         1..175
                     /product="TRAP transporter small permease subunit"
                     /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=19658
     Region          10..168
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mmitlykkti nglsaamgwl cgigtlvmgl ilfyevvrry ffnsptiwtq evsvyifmwc
       61 mfggasyalq kgkhvnidll tvklspkaqs klkvltsffg alfcseiavq gwdmiesavk
      121 yqkhsptplh vplwipqsal flgftllalq fvvliieeia firtgerdsv qevnh
//
LOCUS       WP_005662119             652 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Dethiosulfovibrio peptidovorans].
ACCESSION   WP_005662119
VERSION     WP_005662119.1
KEYWORDS    RefSeq.
SOURCE      Dethiosulfovibrio peptidovorans
  ORGANISM  Dethiosulfovibrio peptidovorans
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Dethiosulfovibrionaceae; Dethiosulfovibrio.
REFERENCE   1  (residues 1 to 652)
  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 652)
  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 652)
  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 652)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..652
                     /organism="Dethiosulfovibrio peptidovorans"
                     /db_xref="taxon:47055"
     Protein         1..652
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=68867
     Region          19..646
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 msdilegkia eenqtidldd lrkkfdtear yrelgdwqgm litilavsms afhfytsgfg
       61 lllalqqrav hlafvmslvf llyparqssp kdkiplmdfa laavaaysal ylminfnelv
      121 nraglptqmd ivmgficill lleatrrvss pilpciaiff liycfygraf pelfqhrgfs
      181 ikriinhmyl gtegvfgipl gvsatfvfmf ilfgsvleqt glgkfiidla malaghstgg
      241 pakvavlssg lmgsisgssv anvcttgmft iplmksvgyq shfagaveav astggqimpp
      301 vmgaaafima qflgipyihv alaaivpall yyfavmiqvh leanrlglkg lpkeqlpkla
      361 pllkekglll lpiigiiyfl iagytplkaa fngilisiav syfnretwlt pkklaaafen
      421 gargaigvac acatvgiivg tatltglglr iasavvaiag gkllptlllt mvacillgag
      481 lpttanfivt stmcapalfq lgvapiaaym fvlyfgiaad lsppvalaay agagiagadp
      541 fktgataikl alagflvpyi yaynpilvlv nftlgrfams vgtavlgvfl lgmstvgfyk
      601 csmnpvfriv alsgalclli pgiysdlagl svlvvlhvlq aakakrlnas aa
//
LOCUS       WP_005662325             334 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Dethiosulfovibrio
            peptidovorans].
ACCESSION   WP_005662325
VERSION     WP_005662325.1
KEYWORDS    RefSeq.
SOURCE      Dethiosulfovibrio peptidovorans
  ORGANISM  Dethiosulfovibrio peptidovorans
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Dethiosulfovibrionaceae; Dethiosulfovibrio.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 334)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Dethiosulfovibrio peptidovorans"
                     /db_xref="taxon:47055"
     Protein         1..334
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35688
     Region          7..333
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mallqgrsvr lvatgmavpe rvmdndelar ivdtsnewiv ertgirerri askdenasdl
       61 aiaacrqaid rsgvdvdsid mvvvatnspd tlfpsvaarv qgaigaskag afdvqsgctg
      121 svyslsvass giasglwnrv lvcgvevlsr lidwedrttc vlfgdgagav mleagekedp
      181 gvmvcdmksd gtkwdyitlp gglsslpasr dtlaekkhfv smkgndvfkf tqrvlpgylk
      241 dvcsdagmsp sdidrwifhq anrrimegvl krlgvsedra innlerygnt saasvflaln
      301 eayeggsitc nsgqkvlits fgagmtygaf iyea
//
LOCUS       WP_005662537             157 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Haemophilus influenzae].
ACCESSION   WP_005662537
VERSION     WP_005662537.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus influenzae
  ORGANISM  Haemophilus influenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Haemophilus influenzae"
                     /db_xref="taxon:727"
     Protein         1..157
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17351
     Region          16..151
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdifsffsad fwqanslcfm fisaflsatv lpgnsevifv alavpklmlg slfnadmlal
       61 iliatagnsl gslttygigr wmpkfdpkny rtlwainqlr rygaiallls wlpvvgdlfc
      121 aiagwlrlnf vtsslfiflg kmvryvallf lstpfll
//
LOCUS       WP_005662699             632 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Massilia timonae].
ACCESSION   WP_005662699
VERSION     WP_005662699.1
KEYWORDS    RefSeq.
SOURCE      Massilia timonae (Telluria timonae)
  ORGANISM  Massilia timonae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Telluria group; Massilia.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 632)
  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   3  (residues 1 to 632)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Massilia timonae"
                     /db_xref="taxon:47229"
     Protein         1..632
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=65680
     Region          1..632
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mddmlkdfvv eamdlavnve ehllrlerdp dnketlnavf rsfhtikgga gfmglpalva
       61 achltenlfd alrtgaapvt plaveaalqa sgfvadqlgd lnngtppegl aqmpgdleri
      121 lmdaiegkds apaaaapapa aapapvvava aevaqatpva paaagedgld wtgmynavvp
      181 aanaidasaa taavpaaapa aaavavaapv aapaaaapak nwdgverrtd tkpaaaapak
      241 desiridavk ldallevage svqaanqaav llerlqqfkf egqaavliat ltetlerasr
      301 ysaelqratl atrmqpvgrl fqkfprlvre lakdlgkdve ltiegaetev drvvvdslyd
      361 plvhmlrnal dhgvespeer vaagkpakaf illkawqean svmivlqddg kgmdpvklrk
      421 kavdkglige ngaqsdeday qlvflpgfst kevassvsgr gvgmdvvkta veknrgairi
      481 esslgkgtrf airlpielsi vptmlvstsg aqlalpmavv ervvelpddf acvggapvlk
      541 dqgrplpvrs lalalgyeaa sekvgivina pqpyilamea vdgtadlvik pmtaltvegi
      601 tgtarsaege lvlvvglsfl mdgcrssvrl aa
//
LOCUS       WP_005662923             221 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein [Massilia].
ACCESSION   WP_005662923
VERSION     WP_005662923.1
KEYWORDS    RefSeq.
SOURCE      Massilia
  ORGANISM  Massilia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Telluria group.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Massilia"
                     /db_xref="taxon:149698"
     Protein         1..221
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=22255
     Region          25..101
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mgyadrdkyg iykdstsagp gpslmgadtl igdsvvnaae edlgdikeim ldmqtgqvay
       61 avlafggflg vgeklfavpw qalhldtvnk rfvlnvekdr lksapgfdkd awpdmsdlsw
      121 asgihsfygt dpnrsgaptm gpgvpmggmv ggagtgssty aggamgssvg aghagssslg
      181 gagagmgdsr anqgpgssid prsgnlgddd dlsrirgsni g
//
LOCUS       WP_005663301             167 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Massilia].
ACCESSION   WP_005663301
VERSION     WP_005663301.1
KEYWORDS    RefSeq.
SOURCE      Massilia
  ORGANISM  Massilia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Telluria group.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Massilia"
                     /db_xref="taxon:149698"
     Protein         1..167
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=18435
     Region          13..154
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 miesavqwll dflaaptvgl tsifivsfvs atllplgsep avfavikanp dmfwpailvg
       61 tlgntlggaf dyflgyrakv afakerqsrw fgwlkrygak tmllswlpgi gdplctlagw
      121 lhlpfwpsvm ymaigkfary ltmtlallyi pdsfwtnlgd mltritg
//
LOCUS       WP_005663967             625 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Massilia timonae].
ACCESSION   WP_005663967
VERSION     WP_005663967.1
KEYWORDS    RefSeq.
SOURCE      Massilia timonae (Telluria timonae)
  ORGANISM  Massilia timonae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Telluria group; Massilia.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 625)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Massilia timonae"
                     /db_xref="taxon:47229"
     Protein         1..625
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=67946
     Region          2..625
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mtsdskkssl aaltlaavgi vygdigtspl ytlravfddt hglplntpni lgvislifwa
       61 ltvivslkyv slvlrahnrg eggimalmal atnsvprhsr wsfpllaigv igatmfygds
      121 vitpaisvlg aieglevaap gmshyvvpla vvvlvvlysv qrhgtagigr ffgpvmlvwf
      181 lalaamgivn ivqspeilna lnpwhaahfm ldnkllafia lgavvlaitg aealyadmgh
      241 fgakpirmaw fliaypaltl nylgqgglli adpgavenpf yhqlgtwsvi plvilstmaa
      301 viasqatisg tysmtkqaia lgllprmril htseseigqi yipavnwlql avvliavvgf
      361 gssdelagay giavtatmmm ttvltffvtr yrwrmplwvc lgatgfflii dvllfsattt
      421 kvfhggwfpl lmggvlltlm ltwkrgralv fenlqkhaip leafmeslfv apptrvpgta
      481 iflrgesdgv phamlhnlsh nkvlhervvf ltvhmreepw vpfeeqidiv dlghncyqln
      541 ihygfkdead ipdildrcga lglsfemmet sffiarqtvi sgpgggmapw rehlyvamsr
      601 narsaadyyq irsnrvielg tqiei
//
LOCUS       WP_005665897             249 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Massilia timonae].
ACCESSION   WP_005665897
VERSION     WP_005665897.1
KEYWORDS    RefSeq.
SOURCE      Massilia timonae (Telluria timonae)
  ORGANISM  Massilia timonae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Telluria group; Massilia.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  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   3  (residues 1 to 249)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Massilia timonae"
                     /db_xref="taxon:47229"
     Protein         1..249
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27251
     Region          34..244
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mieaeledwh dyevgsrrei vallrqigek nqlirmlikg eadvcvtsil avdedsgtvv
       61 ldrsveraqn erivaagrvk cettldkiri lfgadglgpt twrgepalra dipptlirlq
      121 rreyyrmptp vsnpvralvp vpmdagggmg vfplhdisvg gvalldnklq lsasvgrvie
      181 gcrielpeig piatsleirn sldltllnhk tsrrlgcqfv disrgglaav qryitklere
      241 rnaklagla
//
LOCUS       WP_005666250             228 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Massilia timonae].
ACCESSION   WP_005666250
VERSION     WP_005666250.1
KEYWORDS    RefSeq.
SOURCE      Massilia timonae (Telluria timonae)
  ORGANISM  Massilia timonae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Telluria group; Massilia.
REFERENCE   1  (residues 1 to 228)
  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 228)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 228)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Massilia timonae"
                     /db_xref="taxon:47229"
     Protein         1..228
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=24902
     Region          1..206
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 maydhqeqeq ldsfkafwsq ygniiiwvli lalgsyagwn ywkthqrnks veasalydel
       61 qtsllandna kvqrvagdir akyessayap maalaaakta feandlktak aqlqwaaehg
      121 ndeyksianl rlagvlldek afdealkvln gkflpqftse vndrkgdvlv aqnklneara
      181 ayvaaiaamd pnapgrqlvq ikleaiggtv padkkseqek aaeqkaaa
//
LOCUS       WP_005666452             157 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Haemophilus influenzae].
ACCESSION   WP_005666452
VERSION     WP_005666452.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus influenzae
  ORGANISM  Haemophilus influenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Haemophilus influenzae"
                     /db_xref="taxon:727"
     Protein         1..157
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17329
     Region          16..151
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdifsffstd fwqanslclm fisaflsatv lpgnsevifv alavpklmlg slfnadilal
       61 iliatagnsl gslttygigr wmpkfdpkny rtlwainqlr rygaiallls wlpvvgdlfc
      121 aiagwlrlnf vtsslfiflg kmvryvallf lstpfll
//
LOCUS       WP_005667623             581 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Haemophilus
            influenzae].
ACCESSION   WP_005667623
VERSION     WP_005667623.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus influenzae
  ORGANISM  Haemophilus influenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Haemophilus influenzae"
                     /db_xref="taxon:727"
     Protein         1..581
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=64457
     Region          3..560
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mmidkrlint vadskkwigv tvlwnwvalv ggiisavvfs yilqaayfhe lsplsavilg
       61 illiaalalr afagkksvqa syfastkvkh elrsliyrkl asmplnqvnq qstssiiqva
      121 segveqleiy fgrylpqlfy sllapltlfa fliffsfkta iillicvpli pmsiiavnki
      181 akkllakyws iyvglgssfl dnlqglitlk iyqddaykak amdkeaehfr kitmkvltmq
      241 lnsvslmdll ayggaaigil tallqfqdaq lsvlgvilfi llsseffipl rllgsffhva
      301 mngkaasdki ftlldtpvet qqsavnfeak nnlqveikdl hfsyseekpa itglnlsilp
      361 nqlsvfvgks gcgkstlvsl lmgfnkaqqg eilfngqnal nidrtsfyqk vslvshssyv
      421 fkgslrenmt makidatdeq iyacleqvnl ahfvrenggl dmqllsrgan lsggqiqrla
      481 larallhnae lyifdeatsn idveseeiil qfiqqfkqqk tivmishrla navnadcinv
      541 ldqgklieqg thkelmekqg ayaemfqqqk dleqirevan a
//
LOCUS       WP_005667626             343 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Haemophilus
            influenzae].
ACCESSION   WP_005667626
VERSION     WP_005667626.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus influenzae
  ORGANISM  Haemophilus influenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 343)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Haemophilus influenzae"
                     /db_xref="taxon:727"
     Protein         1..343
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=39739
     Region          <55..330
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mnfcrillkp lkknealsgy saeglhyltg nkhfnpelpf srqefitvkp qkqqgmsisg
       61 fqpklqliik dehfdsinqq gnyilkpspe eypflaeneh atmhimkelg fdvpenglvs
      121 fageqnhkef afvikrfdrd eqqkpmhqeq ldgamnirdk ygkigadneq yvsyeqiakf
      181 ilqhtenhla qqreifrrii yayllgnndl hlrnfsfiyp knshpkiapi ydfvsvspyp
      241 eifnstllal pllareegna tlakgfytqy geyigddfve fgeniglnkn viiqklipei
      301 iqekekveqi ysqsfmpqph idcvlktyrk rlallnllhe pel
//
LOCUS       WP_005669452             389 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Massilia timonae].
ACCESSION   WP_005669452
VERSION     WP_005669452.1
KEYWORDS    RefSeq.
SOURCE      Massilia timonae (Telluria timonae)
  ORGANISM  Massilia timonae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Telluria group; Massilia.
REFERENCE   1  (residues 1 to 389)
  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 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   3  (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   4  (residues 1 to 389)
  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 389)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Massilia timonae"
                     /db_xref="taxon:47229"
     Protein         1..389
                     /product="CmpA/NrtA family 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=42520
     Region          14..264
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mglatggvwa agsdkpekte irigfipltd casvvmasvl gfdkkygvkf vlskeaswag
       61 vrdklangdl daahvlygll ygvqmgiggq rkdmavlmgl nnngqaitls kqlankgavd
      121 gqslaklmra ekrdftfaqt fptgthamwl yywlaangvn pmkeakvitv pppqmvanmr
      181 vgnmdgfcvg epwghraimd gigitaittq diwrdhpekv lgstlefakk hpntcramma
      241 aiieasrwid asmanknkma eviaaksyvn tskdaidqri lgryqnglgk twddqnymkf
      301 yndgavnfpy lsdgmwfmtq hrrwgllkqd pdylavasav nqialykdaa tlakapvpss
      361 pmrssklmdg svwdgkdpka yaasfkvrv
//
LOCUS       WP_005670894             500 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Massilia].
ACCESSION   WP_005670894
VERSION     WP_005670894.1
KEYWORDS    RefSeq.
SOURCE      Massilia
  ORGANISM  Massilia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Telluria group.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Massilia"
                     /db_xref="taxon:149698"
     Protein         1..500
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51436
     Region          <30..212
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          <276..456
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mannmnrakd aqdagarale rvgaqhakrd gisfdfdags apydyairvg tgavntlsgs
       61 etrdylwglg gddaldggag ednlfgdaga dllvggdggd rmmggmgndr lyggaeadgl
      121 mggagndlld egeghgdlng gagddiligg lgadafmisp dsgndvirdf tagpgmfdhl
      181 ainglswadl sfadtpdgvk iswdggsvlm ngvtkadlsq ddfmfaespe lppssrpada
      241 ptperptmse egpvingsdr snpafdriad amlrrdtpvq fgftgdetyr vkvgtevadt
      301 fdgaetwdhf fgrdgndqlf gnggddilqg dagddslegg agsdrldggm gndqldggda
      361 edevmggdgn dvidagaghd mieggmgndt irggtgadaf mvmpdsgndv vldfeargaa
      421 qgafdhiafi dimpdqvsvq datagalisw dtngdgaadg svllqgvyma dlrqsdfmfn
      481 eepafiagvs tvgsnyvfpl
//
LOCUS       WP_005661031             378 aa            linear   BCT 20-JAN-2025
DEFINITION  threonine synthase [Dethiosulfovibrio peptidovorans].
ACCESSION   WP_005661031
VERSION     WP_005661031.1
KEYWORDS    RefSeq.
SOURCE      Dethiosulfovibrio peptidovorans
  ORGANISM  Dethiosulfovibrio peptidovorans
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Dethiosulfovibrionaceae; Dethiosulfovibrio.
REFERENCE   1  (residues 1 to 378)
  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 378)
  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   3  (residues 1 to 378)
  AUTHORS   Parsot,C.
  TITLE     Evolution of biosynthetic pathways: a common ancestor for threonine
            synthase, threonine dehydratase and D-serine dehydratase
  JOURNAL   EMBO J 5 (11), 3013-3019 (1986)
   PUBMED   3098560
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10107605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Dethiosulfovibrio peptidovorans"
                     /db_xref="taxon:47055"
     Protein         1..378
                     /product="threonine synthase"
                     /EC_number="4.2.3.1"
                     /GO_function="GO:0004795 - threonine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009088 - threonine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40427
     Region          49..365
                     /region_name="Thr-synth_1"
                     /note="Threonine synthase is a pyridoxal phosphate (PLP)
                     dependent enzyme that catalyses the last reaction in the
                     synthesis of threonine from aspartate. It proceeds by
                     converting O-phospho-L-homoserine (OPH) into threonine and
                     inorganic phosphate. In plants; cd01563"
                     /db_xref="CDD:107206"
     Site            order(68,73..74,92,115,131,134..135,141,157..163,165..167,
                     179..180,209,323..325,326..327,362)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:107206"
     Site            order(98,124,223..227,360)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:107206"
     Site            98
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107206"
ORIGIN      
        1 mlkclrcgas cgddepiwrc pdcgghldhi tekllsispe eikrgplsmw rysktmpvrs
       61 pekavtmgeg ltplipveld gvkplvkmdf lcptgsykdr gisvlvsrlr elgitslied
      121 ssgnagaama ayctagglnc svyvpdytsa gkcvqieayg aelirvpgtr edttdaamaa
      181 aretyygshn wspwfvegvk tfayeiweql gwtapdhlvl plgqgslvlg ayralselrd
      241 mglidhipki hgvqsancap larayesgld vpenitkaet vaegissatp lrgaevleav
      301 krsrgsivav dekpivegif alasrgiyve ptsavvvpgi sklmesgais kgettvvfls
      361 gsglkatdki lelrrkik
//
LOCUS       WP_005672803             129 aa            linear   BCT 20-JAN-2025
DEFINITION  PilZ domain-containing protein [Lautropia mirabilis].
ACCESSION   WP_005672803
VERSION     WP_005672803.1
KEYWORDS    RefSeq.
SOURCE      Lautropia mirabilis
  ORGANISM  Lautropia mirabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Lautropia.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 129)
  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   3  (residues 1 to 129)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Lautropia mirabilis"
                     /db_xref="taxon:47671"
     Protein         1..129
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13436
     Region          16..129
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mstqhqglag gmagnkpatr pgviplsike ksallaaymp flengglfvp tdksaqlgde
       61 lyiiltlmdd atktaipgrv awvtpagatn rrqgigiqfs ktdasvvare kietllgpal
      121 ksppssyti
//
LOCUS       WP_005672147             416 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Lautropia mirabilis].
ACCESSION   WP_005672147
VERSION     WP_005672147.1
KEYWORDS    RefSeq.
SOURCE      Lautropia mirabilis
  ORGANISM  Lautropia mirabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Lautropia.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Lautropia mirabilis"
                     /db_xref="taxon:47671"
     Protein         1..416
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=45630
     Region          18..411
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mstrtesnis esgldeglvl vlncgsssik falydaaehp lpkrpmwsgk avdiggpnvt
       61 yedsdtpcgp lrteddgrrp yvaaidyira rvrkrvgqrr ligvahrvvh ggpkyshpvr
      121 mdaevladlk syiplaplhq pyaleaiaal mdgvpdlpqv acfdtsfhyt mpkvekqlgl
      181 phevwdkglr rygfhglsye ymalslpely gdiskgkviv ahlgsgaslc amedlksqst
      241 tmgfsvldgl mmgtrpgtld pgailflmes eklslkdmtr mlyhksgllg vsglspeprv
      301 llareneege vgerirdamr lyvrrvirqi gsliammngi dmlvftagvg ensaeirrri
      361 legmtyfgik vdqeankana pvistpdsav kvviqptnee wiaarhavql llgkeq
//
LOCUS       WP_005673693             536 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Lautropia mirabilis].
ACCESSION   WP_005673693
VERSION     WP_005673693.1
KEYWORDS    RefSeq.
SOURCE      Lautropia mirabilis
  ORGANISM  Lautropia mirabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Lautropia.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Lautropia mirabilis"
                     /db_xref="taxon:47671"
     Protein         1..536
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=60143
     Region          3..>422
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mptlnwigke avvkhhkevp frllepvpel scgdadsgnl ivqgdnlhal kallpryagq
       61 vkciyidppy ntgnegwvyn dnvnspeirk wlgevvgkeg etldrhdrwl smmyprlvll
      121 kqflredgai fisiddneva tlrllmdeif earnfvgtvi wqkkyavsnd hktiapmhdf
      181 vlvyqrspsw qrnllprgke kdnqyrnede kgkfrisdyt caktaeerpn lyypvtnpnt
      241 geeiwpkrtr vwaysqeehq rhvaegliyw gkdgkgkvpa ykrykhslrn dgvvpqtlwp
      301 hefaghtdgs rkelrevlhd ipsvsdfatp kpslliqrvl qiatdkdsli ldsfagsgtt
      361 ghavlkqnae dggkrrfilv emdtgiannv trerikrvad gytnakgqav eglsggfqfc
      421 rlsaeplfna dgqirsdvkf aqlaefvwfa etgtgftgta nspllgvheg raiyllyngi
      481 lkdkslgggn vltgpvfdvl pkfagpkviy aaanrmggra aregitfkqt pyalev
//
LOCUS       WP_005676273             586 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LysM peptidoglycan-binding domain-containing protein
            [Bacteroides].
ACCESSION   WP_005676273
VERSION     WP_005676273.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 586)
  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 586)
  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 15193204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..586
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=66721
     Region          <32..76
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          <67..129
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          159..200
                     /region_name="LysM"
                     /note="Lysin motif; smart00257"
                     /db_xref="CDD:197609"
ORIGIN      
        1 mkpinrlflf llfisasyai syaqenqsff lhtiekgqsl ysiskmynvt tsdiirlnpg
       61 cdekiyagqt ikipkgkdtq kgetfhtiqa getlyklttm ynvsakaice anpglsaenf
      121 rigqvilipl ekeptntvqt svtqpaiqgp vvarckemhk vkrketifsv sreygiseqe
      181 linanpelkk gmkkgqllci pypsatpvqp tpkedlyavp psnselfrks ketpknisti
      241 kaalllpfqe dkrmveyyeg flmavdslkr tgtsldlyvy dcgkevstln tilakkemke
      301 mnvifgpmhq sqikplsdfa ekngirlvip fsqkgeevfn npavyqintp qsylysevye
      361 hftrqfpnsh vifiesanpd kekadfisgl kqelkskgis mrtvdesatk etlkaalrnd
      421 kenifiptsg knvllikilp qltllvrdnp gpnihlfgyp ewqtntkdhl esffeldvyf
      481 yssfytntlf paavqftnay hkwyskdlas kypnyamlgf dtgffflkgl srygselenn
      541 lskmnltpiq tgfkfervnn wggfinkkvf firftknfel vkldfe
//
LOCUS       WP_005680128             375 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Bacteroidales].
ACCESSION   WP_005680128
VERSION     WP_005680128.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidales
  ORGANISM  Bacteroidales
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia.
REFERENCE   1  (residues 1 to 375)
  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 375)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 375)
  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   4  (residues 1 to 375)
  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 375)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bacteroidales"
                     /db_xref="taxon:171549"
     Protein         1..375
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43097
     Region          121..374
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          291..371
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mkslfilqlv ccvitamlal qlamaslqvr wkvwryeisr wilvasmlff svhyllqmih
       61 glraqgadvg aafnilfytp vafaitlsii niestgnkvr ryclrgmmay iliaivfvig
      121 mfksqslhig nmlyvmlglf vasmayfili irketkarkq klmenfgidl ipyvrysqas
      181 iillyfaagl lpvailfntl lyiigplill sviffvhtfi amgyyitpke vipeendaea
      241 kvteaedmkd gknthgtnil tanrkmeiel alkkwceegf ykdyevniys latklgykkn
      301 elteyfnqse ytnfrtwlsd irfneavrmm kanpeysida istecgfssh twiyrifkqk
      361 tgmspsqwrk qfasi
//
LOCUS       WP_005680723             189 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Bacteroides].
ACCESSION   WP_005680723
VERSION     WP_005680723.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..189
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20902
     Region          6..179
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mktneileni karrsvrayt gqqvseedlq avleaatyap sgmhletwhf taiqnadklt
       61 elnerikgaf aksdeprlke rgqsktyccy yhaptlvivs neptqwwagm dcacaienmf
      121 laahslgigs cwinqlgttc ddpevrafit slgvpenhkv ygcvalgyad skipmkekkv
      181 kdgtitivk
//
LOCUS       WP_005680733             279 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Bacteroides caccae].
ACCESSION   WP_005680733
VERSION     WP_005680733.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides caccae
  ORGANISM  Bacteroides caccae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Bacteroides caccae"
                     /db_xref="taxon:47678"
     Protein         1..279
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31709
     Region          200..279
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mkmdfpqvdl ptevlawtnv tedilniykq scrlqaciva ictegsmkas inlldyeirp
       61 ndlitllpgt iiqfrertek vclcfvgfsa hctgrvnlmk nignaypkll eqpvvplsed
      121 vagylkdyfa llsrascnen fdmdpelvel slqtiltsir liyhnypgen sssnrkkeic
      181 reliqsiteh yknerraqfy adqlgislqh lsttvrqvtg ksvldtiayi vimdakaklk
      241 gtnmtiqeia yslnfpsasf fgkyfrryvg mtplefrnr
//
LOCUS       WP_005681931             686 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Bacteroides caccae].
ACCESSION   WP_005681931
VERSION     WP_005681931.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides caccae
  ORGANISM  Bacteroides caccae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Bacteroides caccae"
                     /db_xref="taxon:47678"
     Protein         1..686
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73931
     Region          4..686
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mittqllrpe sivvvgasnn vhkpggailk nlinggyqge lravnpkeke vqgvpafadv
       61 kdlpdtdlav lavpaalcpd ivetlagtkq trafiilsag fgeethegal leeriletvn
      121 kygasligpn ciglmntwhh svfsqpipnl nlkgvdliss sgatavfile savtkglqfn
      181 svwsvgnakq igvedvlqfm denfdpekds hlkllyiesi qnpdrllfha sslirkgcki
      241 aaikagsses gsraasshtg aiassdsave alfrkagivr cfsreelttv gcvftlpelk
      301 gknfaiitha ggpgvmltda lskgglnvpk legelaeelk tqlfpgaavg npidilatgt
      361 pehlrlcidy ceekfenida mmaifgtpgl vtmfemydvl hekmqtckkp ifpilpsint
      421 agaevaafla kghvnfadev tlgtalsriv napkpavpei elfgvdvpri rriidsiped
      481 gyiephyvqa llhaagiplv defvsdnkee ivafarrcgf pvvakvvgpv hksdvggvvl
      541 nikseqhlal efdrmmqipd arsimvqpml kgtelfigak yeekfghvvl cglggifvev
      601 lkdvssglap lsyeeaysmi hslraykiiq gtrgqkgvne dkfaeiivrl stllrfatei
      661 kemdinplla tekavvavda rikiek
//
LOCUS       WP_005683640             292 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Mycoplasmopsis alligatoris].
ACCESSION   WP_005683640
VERSION     WP_005683640.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis alligatoris (Mycoplasma alligatoris)
  ORGANISM  Mycoplasmopsis alligatoris
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Mycoplasmopsis alligatoris"
                     /db_xref="taxon:47687"
     Protein         1..292
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33816
     Region          1..287
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mkdkfllidg nlmlfqsfya tynpnnsyvm qsqsgittng iyqffrtlyn llnsvkpkyi
       61 fiafdakekt nrhliypeyk agrrkapeii feqfhytkel lsklnipsse ingaeaddli
      121 atlskiqdve kiifskdqdl lqlvnddisi lyrdtfsnqy skitkdnfee kylikpnqip
      181 dykaingdns dnlpgvkgig kigaikllke fgtwqniynn ldkhsttvqk klvesqemsk
      241 lcydlaklny dveeldlnle nyflninyqq akdlflelgl envlarlesi kw
//
LOCUS       WP_005684685             564 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Lacticaseibacillus
            rhamnosus].
ACCESSION   WP_005684685
VERSION     WP_005684685.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus rhamnosus (Lactobacillus rhamnosus)
  ORGANISM  Lacticaseibacillus rhamnosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Lacticaseibacillus rhamnosus"
                     /db_xref="taxon:47715"
     Protein         1..564
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=61999
     Region          4..544
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mfgllkygrd qrwaggieal fdwlptllpi lialnlgtgh qvaalvttlv lmavwvgyvv
       61 gyerhhrhaw amsakrelrd ryfaalyqrn davattaadh aviqrdlggl nnldmfystl
      121 fptilqagmt flvliglsfw yrswlallpf gcvfliglam mflgkrmsaq nkahlsgflk
      181 mggrfmddlr gmttlvmyga adryaqkfad dseffrqatm nllktqlqtl fvingfvylt
      241 vfaggfitav qlvagqlpva gafatwftla mmmvnarqlg yfvhvvksng pslaailati
      301 akakevpdtv kitdnrplsq itldqvsvgy aadaplvtgi natlvpgkly glagengtgk
      361 stliqailgr lkplsgaima dqtavsalsn vqqaavfgyv saneylfsgt iqenlllgnr
      421 fgdqwqarla slglmqfvps lekgyatqvg engrllspgq rqqlafarml ladktvylld
      481 eitssidean aavilqavkk lsrhkivlfi shdlkamtqa devwfthdhq ltvanhqtly
      541 qkqpayrqlv dnpemmenev nsnd
//
LOCUS       WP_005685868             132 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Lacticaseibacillus rhamnosus].
ACCESSION   WP_005685868
VERSION     WP_005685868.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus rhamnosus (Lactobacillus rhamnosus)
  ORGANISM  Lacticaseibacillus rhamnosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 132)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 132)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Lacticaseibacillus rhamnosus"
                     /db_xref="taxon:47715"
     Protein         1..132
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=14149
     Region          2..126
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(7..10,40..42,45,71,108,122)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mlklytdgat kgnpgpagig ilvsglpqqi qhhaalpams nheaefaaai agfklliess
       61 lttgtvayys dsklviqaie kryakhypal taellslide fplvlpnwip drqnrgahhl
      121 aqqglhqaed es
//
LOCUS       WP_005686818             204 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Haemophilus influenzae].
ACCESSION   WP_005686818
VERSION     WP_005686818.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus influenzae
  ORGANISM  Haemophilus influenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 204)
  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 204)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 204)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Haemophilus influenzae"
                     /db_xref="taxon:727"
     Protein         1..204
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22517
     Region          1..204
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 maysieeeqe inqlkdwwke ngktiivafi lgvggmfgwr ywqahqaeqi aqasaqydtl
       61 insvkqdeqa kkanieqfvq ansktayavf alldeakkat ekqdfsaaea nlnqaltqsq
      121 devltsival rlsavqfqlg qldnalttln qvkgesfnar kailtgdiqv akgdkvaakn
      181 sfeqaqqsgs qleqqmakmk lnnl
//
LOCUS       WP_005690165             343 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Haemophilus
            influenzae].
ACCESSION   WP_005690165
VERSION     WP_005690165.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus influenzae
  ORGANISM  Haemophilus influenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 343)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Haemophilus influenzae"
                     /db_xref="taxon:727"
     Protein         1..343
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=39724
     Region          <55..330
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mnfcrillkp lkknealsgy saeglhyltg nkhfnpelpf srqefitvkp qkqqgmsisg
       61 fqpklqliie ddhfnsinqq gnyilkpspe eypflaeneh atmrimkelg fdvpenglvs
      121 fageqnhkef afvikrfdrd kqqktmhqeq ldgamnirdk ygkigadneq yvsyeqiakf
      181 ilqhtenhla qqreifrrii yayllgnndl hlrnfsfiyp knshpklapi ydfvsvspyp
      241 eifnstllal pllvreegna tlakgfntqy geyigddfve fgeniglnkn viiqklipei
      301 tqekekveqi ysqsfmpqph idcvlktyrk rlaflnllne pel
//
LOCUS       WP_005691472             246 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein
            [Lacticaseibacillus rhamnosus].
ACCESSION   WP_005691472
VERSION     WP_005691472.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus rhamnosus (Lactobacillus rhamnosus)
  ORGANISM  Lacticaseibacillus rhamnosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 246)
  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 246)
  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 246)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 246)
  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   5  (residues 1 to 246)
  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 10164212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Lacticaseibacillus rhamnosus"
                     /db_xref="taxon:47715"
     Protein         1..246
                     /product="winged 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=27850
     Region          5..69
                     /region_name="WHTH_GntR"
                     /note="Winged helix-turn-helix (WHTH) DNA-binding domain
                     of the GntR family of transcriptional regulators; cd07377"
                     /db_xref="CDD:153418"
     Site            order(5,7,30,32..33,41..45,47..48,51,61..62,64..67)
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:153418"
ORIGIN      
        1 mhrspkyvqv ynqilkmikq gqlapgaklp seevlttefe vsrvtlrtal sllkedgfir
       61 sihgqghfve asesqkksgi ealgnpmlks lvlpiesret yfhenqasef tdrlfdrqna
      121 pydtlniwyq nkgenigntl aivlpttiqm fgvdlsdsaa iinfleetiy qkasssnvli
      181 tlsdrqqktf rrtfgdtspl ilmtedifgf ngerllqnkh yipanlyran vmryqndlqn
      241 qigave
//
LOCUS       WP_005692425             343 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Haemophilus
            influenzae].
ACCESSION   WP_005692425
VERSION     WP_005692425.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus influenzae
  ORGANISM  Haemophilus influenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 343)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Haemophilus influenzae"
                     /db_xref="taxon:727"
     Protein         1..343
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=39729
     Region          <55..330
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mnfcrillkp lkknevhsgy stkglhyltg nkhfnpelpf srqefitvkp qkqqgmsisg
       61 fqpklqliik ddhfdsvdqq ghyilkpspe eypflaeneh atmrimkelg fdvpenglvs
      121 fageqnqkef afvikrfdrd eqqkpmhqeq ldgamnirdk ygkigtdneq yvsyeqiakf
      181 ilqhtenhla qqqeifrrii yayllgnndl hlrnfsfiyp knshpklapi ydfvsvspyp
      241 eifnstllal pllareegna tlakgfntqy geyigddfve fgeniglnkn viiqklipei
      301 tqekekveqi ysqsfmpqph idcvlktyrk rlallnvlne pel
//
LOCUS       WP_005692429             581 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Haemophilus
            influenzae].
ACCESSION   WP_005692429
VERSION     WP_005692429.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus influenzae
  ORGANISM  Haemophilus influenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Haemophilus influenzae"
                     /db_xref="taxon:727"
     Protein         1..581
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=64398
     Region          3..560
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mmidkrlint vadskkwigv tvlwnwvalv ggiisavvfs yilqaayfhe lsplsavilg
       61 illiaalalr afagkksvqa syfastkvkh elrsliyrkl asmplnqvnq qstssiiqva
      121 segveqleiy fgrylpqlfy sllapltlfv fliffsfkta villicvpli pmsiiavnki
      181 akkllakyws iyvglgssfl dnlqglitlk iyqddaykak amdkeaehfr kitmkvltmq
      241 lnsvslmdll ayggaaigil tallqfqnaq lsvlgvilfi llsseffipl rllgsffhva
      301 mngkaasdki ftlldtpvet qqsavdfeak nnvqveikdl hfsyseekpa itgldlsilp
      361 nqltvfvgks gcgkstlvsl lmgfnqaqqg eilfngqnal nidrtsfyqk vslvshssyv
      421 fkgslrenmt makidatdeq iyacleqvnl ahfvrenggl dmqllsrgan lsggqiqrla
      481 larallhnae lyifdeatsn idveseeiil qfiqqfkqqk tivmishrla navnadcinv
      541 ldqgklieqg theilmakqg ayaemfqqqk dleqirevan a
//
LOCUS       WP_005692542             564 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Lacticaseibacillus
            rhamnosus].
ACCESSION   WP_005692542
VERSION     WP_005692542.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus rhamnosus (Lactobacillus rhamnosus)
  ORGANISM  Lacticaseibacillus rhamnosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Lacticaseibacillus rhamnosus"
                     /db_xref="taxon:47715"
     Protein         1..564
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=62225
     Region          4..544
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mfgllkygrd qrwagvieal fdwlptllpi lialnlgtgh qvtalvttlv lmavwlgyvv
       61 gyerhhrhaw amsakrelrd ryftalyrrn davattaadh aviqrdlggl nnldmfystl
      121 fptilqagmt flvliglsfw yrswlallpf gcvfliglam mflgkrmsaq nkahlsgflk
      181 mggrfmddlr gmttlvmyda adryaqkfad dseffrqatm nllktqlqtl fvingfvylt
      241 vfaggfitav qlvagqlpva gafatwftla mmmvnarqlg yfvhvvksng pslaailati
      301 akakaapdtv kitdnrplsq itldqvsigy aadaplvtgi natlvpgkly glagengtgk
      361 stliqailgr lkplsgaima dqtavsalsn vqqaavfgyv taneylfsgt iqenlllgnr
      421 fgdqwqarla slglmqfvps lekgyatqvg engrllspgq rqqlafarml ladktvylld
      481 eitssidean aaiilqavkk lsrhkivlfi shdlkamtqa devwfihdhq ltvanhqrly
      541 qkqpayrqlv dnpemmenev nsnd
//
LOCUS       WP_005693683             157 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Haemophilus influenzae].
ACCESSION   WP_005693683
VERSION     WP_005693683.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus influenzae
  ORGANISM  Haemophilus influenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Haemophilus influenzae"
                     /db_xref="taxon:727"
     Protein         1..157
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17361
     Region          16..151
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdifsffsad fwqanslcfm fisaflsatv lpgnsevifv alavpklmlg slfnvdilal
       61 iliatagnsl gslttygigr wmpkfdpkny rtlwainqlr rygaiallls wlpvvgdlfc
      121 aiagwlrlnf vtsslfiflg kmvryvallf lstpfll
//
LOCUS       WP_005693849             114 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Haemophilus influenzae].
ACCESSION   WP_005693849
VERSION     WP_005693849.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus influenzae
  ORGANISM  Haemophilus influenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Haemophilus influenzae"
                     /db_xref="taxon:727"
     Protein         1..114
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13048
     Region          10..101
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mtsfaqldik seelaivkti lqqlvpdytv wafgsrvkgk akkysdldla iiseepldfl
       61 ardrlkeafs esdlpwrvdl ldwattsedf reiirkvyvv iqekektvek ptal
//
LOCUS       WP_005694589             192 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Haemophilus influenzae].
ACCESSION   WP_005694589
VERSION     WP_005694589.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus influenzae
  ORGANISM  Haemophilus influenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Haemophilus influenzae"
                     /db_xref="taxon:727"
     Protein         1..192
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21557
     Region          3..164
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mkifgtmydk tmewskhrfa vfwlsfvsfi eaiffpippd vmlipmsmsk pksavkfafy
       61 taiasviggi igyaigfyat dwvenivqqw gyaahwakav swfeqwgvlv vfvagfspip
      121 ykvftlcagv mqmaffpfvi tafvsrlarf llvaklaawg gekfaaklrk sieiigwsvv
      181 vlaviayfil kn
//
LOCUS       WP_005680986             346 aa            linear   BCT 20-JAN-2025
DEFINITION  galactokinase [Bacteroides caccae].
ACCESSION   WP_005680986
VERSION     WP_005680986.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides caccae
  ORGANISM  Bacteroides caccae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   McAuley,M., Kristiansson,H., Huang,M., Pey,A.L. and Timson,D.J.
  TITLE     Galactokinase promiscuity: a question of flexibility?
  JOURNAL   Biochem Soc Trans 44 (1), 116-122 (2016)
   PUBMED   26862196
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Holden,H.M., Thoden,J.B., Timson,D.J. and Reece,R.J.
  TITLE     Galactokinase: structure, function and role in type II galactosemia
  JOURNAL   Cell Mol Life Sci 61 (19-20), 2471-2484 (2004)
   PUBMED   15526155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Bacteroides caccae"
                     /db_xref="taxon:47678"
     Protein         1..346
                     /product="galactokinase"
                     /EC_number="2.7.1.6"
                     /GO_function="GO:0004335 - galactokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0005534 - galactose binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0046835 - carbohydrate phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=39059
     Region          3..345
                     /region_name="GalK"
                     /note="Galactokinase [Carbohydrate transport and
                     metabolism]; COG0153"
                     /db_xref="CDD:439923"
ORIGIN      
        1 mdlwftpsen sqvhleslsf egfvefdiat ktqikqgqwg dyvrgakyal skrfnlkygi
       61 ngvlqgslpv gglsssaavl iayvmafaka ngislkpfev vliaseaere yiglnnglld
      121 qacialgqkn sllfldcdsn hyriinrnls mpdfeigiff sgltrslvns dynlrvyeck
      181 ttawnilaya dqplktfdkt flrdipkesf ektrdimpar fsrrsehfys eyrrvrqgvt
      241 awetgnlqlf dklsfdsces sihnyecgsp eliaiynimh klsgvyggrf sgagfkgavi
      301 alvdpaykes ieaevtkqyl aqfpeyemtf ktywvkpddg arfien
//
LOCUS       WP_005695955             234 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Haemophilus].
ACCESSION   WP_005695955
VERSION     WP_005695955.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus
  ORGANISM  Haemophilus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae.
REFERENCE   1  (residues 1 to 234)
  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   2  (residues 1 to 234)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Haemophilus"
                     /db_xref="taxon:724"
     Protein         1..234
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=24553
     Region          <40..>197
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          164..233
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkslrslltl tslalavsgs alatntsvlp tkedvvtnsk smvestkadv knaandklks
       61 msdsasstks naldkvntak ekatsakdam kdkatsakda vkekasalke katennqpsi
      121 kdkatekfns vkdnakekas eaktkaadkv kevkekaast kdaakekvas sakvninkad
      181 aetlqklsgi gekkaqaiid yrnkvgkiks aaelsnidgi geatiekitp flsf
//
LOCUS       WP_005695592             204 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Haemophilus parainfluenzae].
ACCESSION   WP_005695592
VERSION     WP_005695592.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus parainfluenzae
  ORGANISM  Haemophilus parainfluenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 204)
  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 204)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 204)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Haemophilus parainfluenzae"
                     /db_xref="taxon:729"
     Protein         1..204
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22313
     Region          1..204
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 maytieeeqe lnqlkewwkd ngktiiaafi lgvggmlgwr ywqsyqanqi mqasaeydal
       61 vyttnkdaaa qqakmaefvk ahdktsyavf slldeakgfv akqdyasaen slkqaiaqsq
      121 ddiltslaal rlsavqfqqg qfdaalasln qvksqgfsar kdllagdiqi akgdvngaka
      181 sfenaqksgn plekqmaqmk lnnl
//
LOCUS       WP_005697031             581 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein/permease
            [Haemophilus].
ACCESSION   WP_005697031
VERSION     WP_005697031.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus
  ORGANISM  Haemophilus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Haemophilus"
                     /db_xref="taxon:724"
     Protein         1..581
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=64237
     Region          3..560
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mmidkrlint vadskkwigi tvlwnwvali ggiisavvfs yilqaayfne lgplsavilg
       61 ivliaalalr afagkksvqa syfastkvkh elrsliyrkl asmtlnqvnq qstsniiqva
      121 segveqleiy fgrylpqlfy sllapltlfa fliffsfkta lillicvpli pmsiiavnki
      181 akkllakyws iyvglgssfl dnlqglitlk iyqddaykak amdeeaehfr kitmkvltmq
      241 lnsvslmdll ayggaaigil tallqfqadq ltvlgvilfi llsseffipl rllgsffhva
      301 mngkaasdki ftlldtpvet qtqavdfaak naiqvdiqdl hfayseekpa itgldlsilp
      361 nqltvfvgks gcgkstlvsl lmgfnkaqqg killngqeiq eidrhsfyek vslvshnsyv
      421 fkgslrenmt makvdatdeq iyacleqvnl aqfvrdnggl dmpllsrgan lsggqiqrla
      481 larallhnaa lyifdeatsn idveseeiil qfiqqfkqqk tivmishrla navnadcinv
      541 leqgklieqg theelmakqg ayagmfqqqk dleqirevan a
//
LOCUS       WP_005697934             573 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase [Haemophilus].
ACCESSION   WP_005697934
VERSION     WP_005697934.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus
  ORGANISM  Haemophilus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Haemophilus"
                     /db_xref="taxon:724"
     Protein         1..573
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=65429
     Region          7..499
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mkkqkleltw igkhkrpkle arilledsek syhakvrses aafdnrlifg dnllalkale
       61 qeftgkvkcv fidppyntgs afahyddgle hsiwlglmrd rleiikrlls ddgslwitid
      121 dneahylkvl cdevfgrgnf vanviwqkvy sermdakgfs tshdhlliyq ksekfkplpl
      181 akeqksaqfn ffdenvgkyy rrrslrkegs eslrqdrpsm wypikapdgs eifpvkpdgv
      241 egrwrwkken vseksnqlef vnkdgkweiy vkqyqeenpt rppatlwptd evghnheakl
      301 evrafnsedv fdtpkperli ervlqiattp gdlvldsfag sgttgavahk mgrrwimvel
      361 gehchthiip rlqkvidged qggiskavnw qggggfryfr laptlivndk wgnqiinpdy
      421 npemlaeala klegftymps eslwwqhgys sendfiyvtt qslsveqlqv lsdevgvsrs
      481 lliccsawrg itadqaaerf pnlslkkipk milkrcewgh ddyslnvanl pmaeeepepr
      541 ssenqpaakt ksvkrksave nqgglfdgmd sne
//
LOCUS       WP_005698380             204 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Haemophilus].
ACCESSION   WP_005698380
VERSION     WP_005698380.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus
  ORGANISM  Haemophilus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae.
REFERENCE   1  (residues 1 to 204)
  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 204)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 204)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Haemophilus"
                     /db_xref="taxon:724"
     Protein         1..204
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22264
     Region          1..204
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 maytieeeqe lnqlkewwkd ngkaiiaafi lgvggmlgwr ywqsyqanqi mqasaeydal
       61 vyttnkdaaa qqakvaefvk ahdktsyavf slldeakgfv akqdyasaen slkqaiaqsq
      121 ddiltslaal rlsavqfqqg qfdaalasln qvksqgfsar kdllagdiqv akgdvngaka
      181 sfenaqkngn plekqmaqmk lnnl
//
LOCUS       WP_005700471             278 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Aggregatibacter aphrophilus].
ACCESSION   WP_005700471
VERSION     WP_005700471.1
KEYWORDS    RefSeq.
SOURCE      Aggregatibacter aphrophilus
  ORGANISM  Aggregatibacter aphrophilus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Aggregatibacter.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Aggregatibacter aphrophilus"
                     /db_xref="taxon:732"
     Protein         1..278
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30379
     Region          1..266
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mtkydlhchs tasdgvlspk evvlrayekg vnvlaltdhd tvagvseark qadllgiqli
       61 ngvelstlwe nrsihivglg fdishekmta llaeqarlrd iraqeigakl akagvvnayl
      121 etkqlagdge vtrahyarhl vqigkvssdn qafkrylgqg ksayvkpqwi dipnaieiih
      181 aaggiavlah plrytmttkw vrkltesfka wggdameiss cgqsrdqfql lvkiaednql
      241 agsvgsdfhf pstwlelgkl aplpphipfv ldlknnlv
//
LOCUS       WP_005700796             274 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Aggregatibacter aphrophilus].
ACCESSION   WP_005700796
VERSION     WP_005700796.1
KEYWORDS    RefSeq.
SOURCE      Aggregatibacter aphrophilus
  ORGANISM  Aggregatibacter aphrophilus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Aggregatibacter.
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   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   4  (residues 1 to 274)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Aggregatibacter aphrophilus"
                     /db_xref="taxon:732"
     Protein         1..274
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=30689
     Region          9..>243
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mqnnlvpfie frgagkqydg kyavrdldlt iyqgeffvlv ggsgsgkstt lrminaliep
       61 tdgnvylhgk rikdydirql rhqigyvlqq ialfptmtva enielmpdvl gwpkaerkar
      121 vnelldlvel dpahyrnryp helsggeqqr igilraiaak pqvllmdepf saldplvrtv
      181 lqdqiamihq kfgttivfvt hdmqeaakla crigvmhngk lvqigtpeai kkqpandyvq
      241 slfstadapd aqriinqflr ldkqgqeavk ravl
//
LOCUS       WP_005704188             193 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Aggregatibacter aphrophilus].
ACCESSION   WP_005704188
VERSION     WP_005704188.1
KEYWORDS    RefSeq.
SOURCE      Aggregatibacter aphrophilus
  ORGANISM  Aggregatibacter aphrophilus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Aggregatibacter.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Aggregatibacter aphrophilus"
                     /db_xref="taxon:732"
     Protein         1..193
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21253
     Region          4..193
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mkdkkqlvig itgasgavya irllellkah plvethliis qaakqtisae tnyslsqvre
       61 fadhdydvrd igaavssgsf risgmvvlpc siktlsgian cyaddlitra advclkeykp
      121 lilcvretpl hlghlrlmtq aaeigarivp lmpafyhrpq tvddiinqgv nrlldqldis
      181 leqdlferwq gnk
//
LOCUS       WP_005704724             198 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Aggregatibacter aphrophilus].
ACCESSION   WP_005704724
VERSION     WP_005704724.1
KEYWORDS    RefSeq.
SOURCE      Aggregatibacter aphrophilus
  ORGANISM  Aggregatibacter aphrophilus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Aggregatibacter.
REFERENCE   1  (residues 1 to 198)
  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   2  (residues 1 to 198)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Aggregatibacter aphrophilus"
                     /db_xref="taxon:732"
     Protein         1..198
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21350
     Region          147..>197
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkplksllal avamtvsttv laeesvlsdv knnakaawqt vkteakdvgg qvkegaikvk
       61 dgavevkdkv ankmksakea tketfteakd ttkekfaeak datkekftea kdvtkekfse
      121 gkkavkrqfk neqpaqveek stvkegakst atrskkvdin sadaatlqsl sgigevkaka
      181 iieyrekngk iknleels
//
LOCUS       WP_005706157             207 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Haemophilus parahaemolyticus].
ACCESSION   WP_005706157
VERSION     WP_005706157.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus parahaemolyticus
  ORGANISM  Haemophilus parahaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 207)
  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 207)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 207)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Haemophilus parahaemolyticus"
                     /db_xref="taxon:735"
     Protein         1..207
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23222
     Region          6..207
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 msseylnkte eqqfeeaknw fkenstpill aifvfatasf gwnfwkshqa esaiqasisy
       61 qatmeayeqd pvknqplvak fleeakgtny aifmqleeak navvkgdfaa aksqlqaaln
      121 evkdpslqsi irfrlaavdf qlkefdsala nleqikdqaw darkqlfvad llaakgdkea
      181 aksayeqika ktsgqereli elkinnl
//
LOCUS       WP_005706276             272 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Haemophilus parahaemolyticus].
ACCESSION   WP_005706276
VERSION     WP_005706276.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus parahaemolyticus
  ORGANISM  Haemophilus parahaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Haemophilus parahaemolyticus"
                     /db_xref="taxon:735"
     Protein         1..272
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30157
     Region          1..269
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mkydlhshst asdglltpte lvnraveqgv emlaltdhdt vagiteakla aqnqpirfis
       61 gvevsivwqe ksihlaalnv dethpelval ldnqaalreq raveigekla kagildayeg
      121 akklasgevt rahygrflle qeyvrnieha fkkylgqgkl ayvkpkwcem qeaieivhqa
      181 ggvisiahpl rykmtgrwvr rliedfkqag gdgievagcg qtpdqrqlit rwakefdlya
      241 sggsdfhypt gwvelgrglt lpqeckpiwg lf
//
LOCUS       WP_005706489             180 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Haemophilus parahaemolyticus].
ACCESSION   WP_005706489
VERSION     WP_005706489.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus parahaemolyticus
  ORGANISM  Haemophilus parahaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (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   2  (residues 1 to 180)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Haemophilus parahaemolyticus"
                     /db_xref="taxon:735"
     Protein         1..180
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18800
     Region          110..179
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkplkallal avamtatssf aetanplatf kqeaktainn elssakktvt qtessaatdm
       61 skmknavvek aksevkavkn daktaretln svkteatekv daaksatkna vakaekvaki
      121 ninkadaatl qklsgigeak akaiveyrnk vgkiknaael skisgigdat iekispyltf
//
LOCUS       WP_005707401             122 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Haemophilus parahaemolyticus].
ACCESSION   WP_005707401
VERSION     WP_005707401.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus parahaemolyticus
  ORGANISM  Haemophilus parahaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 122)
  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   2  (residues 1 to 122)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Haemophilus parahaemolyticus"
                     /db_xref="taxon:735"
     Protein         1..122
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12652
     Region          55..120
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkkintfais livglfstav fanevttqpt tlstqppvvt apatstapvn iqqvtadpns
       61 vnintasaae iqdklvgigg kkaqaivdyr tkngaflsie qlkevsgiga atleknrsri
      121 vl
//
LOCUS       WP_005708350             228 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein, partial [Haemophilus
            paraphrohaemolyticus].
ACCESSION   WP_005708350
VERSION     WP_005708350.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus paraphrohaemolyticus
  ORGANISM  Haemophilus paraphrohaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (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   2  (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   3  (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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Haemophilus paraphrohaemolyticus"
                     /db_xref="taxon:736"
     Protein         1..>228
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          16..67
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msmlltaqam klkvgnptrk lvllkladna ndkgecfpsy qhiadhcevs rrsvishida
       61 likmglvekk srknqdgsss nlyilhlekg senisppser isppsengsl ppsenispit
      121 nhsinqsinq nnivrtvqnf evhfeqfwqa gmtkvnkqks lksfksayes yhaeypttle
      181 dftqmliddi rkrlalhqyg fdklhpttyl nnsrwldeyp tvatspqn
//
LOCUS       WP_005709215             180 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Haemophilus
            paraphrohaemolyticus].
ACCESSION   WP_005709215
VERSION     WP_005709215.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus paraphrohaemolyticus
  ORGANISM  Haemophilus paraphrohaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (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   2  (residues 1 to 180)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Haemophilus paraphrohaemolyticus"
                     /db_xref="taxon:736"
     Protein         1..180
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18785
     Region          <15..143
                     /region_name="valS"
                     /note="valyl-tRNA synthetase; Provisional; PRK14900"
                     /db_xref="CDD:237855"
     Region          112..179
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkplkallal avamtatssf aettnplatf kqeaktainn elssakkavt qtetsaatdm
       61 skmknavvek aksevkavkn daktaretln svkteatekv daaksaaknt vakaekaaki
      121 ninkadaatl qklsgigeak akaiveyrnk vgkiknaael skisgignat iekispyltf
//
LOCUS       WP_005708840             165 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Haemophilus paraphrohaemolyticus].
ACCESSION   WP_005708840
VERSION     WP_005708840.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus paraphrohaemolyticus
  ORGANISM  Haemophilus paraphrohaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Haemophilus paraphrohaemolyticus"
                     /db_xref="taxon:736"
     Protein         1..165
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=18157
     Region          <60..158
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mitdyltslf sllfsseyqf vvmfvsslis ssllpgnsei vfttiasqli iserslysfs
       61 lfgliavati gntlgslitf amgkllpepk aqenkyadwa idklnrygtl mlllswlpiv
      121 gdllcglagw lrlpilqsti ciligkfary ivllvgvypi vkyim
//
LOCUS       WP_005711086             432 aa            linear   BCT 20-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein
            [Lacticaseibacillus rhamnosus].
ACCESSION   WP_005711086
VERSION     WP_005711086.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus rhamnosus (Lactobacillus rhamnosus)
  ORGANISM  Lacticaseibacillus rhamnosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 432)
  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 432)
  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 13086029
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Lacticaseibacillus rhamnosus"
                     /db_xref="taxon:47715"
     Protein         1..432
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=46930
     Region          32..219
                     /region_name="GH25_muramidase"
                     /note="Endo-N-acetylmuramidases (muramidases) are
                     lysozymes (also referred to as peptidoglycan hydrolases)
                     that degrade bacterial cell walls by catalyzing the
                     hydrolysis of 1,4-beta-linkages between N-acetylmuramic
                     acid and N-acetyl-D-glucosamine residues; cl10448"
                     /db_xref="CDD:447900"
     Site            order(36,58,90,92,124,126,152,174,202,213)
                     /site_type="active"
                     /db_xref="CDD:119373"
     Region          <202..431
                     /region_name="PRK06347"
                     /note="1,4-beta-N-acetylmuramoylhydrolase"
                     /db_xref="CDD:180536"
     Region          387..431
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
ORIGIN      
        1 mkfktklitl vvaflaaisf alpsqvnaak gdqgvdwsry qgdngvfgys tdkfgisqig
       61 gysgygtyeq ttyktqvasl iaagkrahty iwwqnidntn lakqvldhfl pevqtpkgsi
      121 valdyeagst ntatllwald yvrdagytpm lygyksflms hidlsqiasr yqlwlaeypd
      181 ynvttvpnyg yfpsfdnvgi fqftstyrag gldgnvdltg itdsgyngst ttgsgktyvk
      241 patstpatka gqkannttls qikvgdsvkv nfgttrwang vampswvqgk tytvqqvsgs
      301 nvllggimsw inrsnvellt ttgvpsvssg ssytvqsgds wwsiaykygm smytlasnng
      361 ksiysvihpg dvirvsgasy ssvvshtyyt vrsgdsfwsi aykygismyt laanngksiy
      421 sliypgesly ik
//
LOCUS       WP_005710041             160 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Lacticaseibacillus rhamnosus].
ACCESSION   WP_005710041
VERSION     WP_005710041.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus rhamnosus (Lactobacillus rhamnosus)
  ORGANISM  Lacticaseibacillus rhamnosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Lacticaseibacillus rhamnosus"
                     /db_xref="taxon:47715"
     Protein         1..160
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17046
     Region          8..153
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mttldpiiid qldglltget npitvlanas allndsmsel nwagfylyng ktgqldlgpf
       61 qgkvacmhiq pgkgvvgtsy qqnsvirvan vhefaghiac dsasnaeivv pinvngetva
      121 imdidspkln rfsendeqil tqfgqtlanh ldtaalntvy
//
LOCUS       WP_005711259             158 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Glaesserella parasuis].
ACCESSION   WP_005711259
VERSION     WP_005711259.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..158
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17836
     Region          19..156
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 msdyltallg ifldkenqyl imfassflss tllpsnseii fstfatqafa nnhslyglfi
       61 satlgnslgs lttyflaklf pppnyheqqn qrirfalkfs qqygvwvllf swlpivgdlf
      121 cgvagwlrfd fwkslcfivl gkairyalll wsvylvvg
//
LOCUS       WP_005712439              99 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Glaesserella parasuis].
ACCESSION   WP_005712439
VERSION     WP_005712439.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..99
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11132
     Region          7..96
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 midlteqqlh lvqrilathl pnvpvwvfgs rikgtakrfs dldlalitdt pltihqqaql
       61 elafsdsdlp fkvdlidwas csdsfkqiil qkyevlpcl
//
LOCUS       WP_005713296             308 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Lacticaseibacillus
            rhamnosus].
ACCESSION   WP_005713296
VERSION     WP_005713296.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus rhamnosus (Lactobacillus rhamnosus)
  ORGANISM  Lacticaseibacillus rhamnosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
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   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 308)
  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 308)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Lacticaseibacillus rhamnosus"
                     /db_xref="taxon:47715"
     Protein         1..308
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32870
     Region          1..69
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          228..285
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mdeigqklrd ariekgytid dlqqitkiqk ryliaieegh fdalpgdfyv rafikqyadt
       61 vgldgdellt qfqqdipepq pqeyaaqsve nktratraee aspvnrlrry lpqiaiaafv
      121 ivaiiviyvv mlfsqsgpkq tipadsesva vsskrssska skasssskss kssassssks
      181 sekaskeskk ksdkldisva aangatqavt lknlptsgnk ltlgangata wisvivngst
      241 twqgsltsgn tqevtlpdnt stfqvrsgna tattielngk kvdisngtsv vrtitftsst
      301 seseasqe
//
LOCUS       WP_005714102             456 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Lacticaseibacillus rhamnosus].
ACCESSION   WP_005714102
VERSION     WP_005714102.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus rhamnosus (Lactobacillus rhamnosus)
  ORGANISM  Lacticaseibacillus rhamnosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 456)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Lacticaseibacillus rhamnosus"
                     /db_xref="taxon:47715"
     Protein         1..456
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=50044
     Region          <2..>56
                     /region_name="PknB_PASTA_kin"
                     /note="Stk1 family PASTA domain-containing Ser/Thr kinase;
                     NF033483"
                     /db_xref="CDD:468045"
     Region          76..189
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          <240..312
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          334..456
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(407..408,411,429..432,434)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mnkkkwwlla lgavvillgg fyifrsmhyr dhflpntevl gvdvsdqtvs aankkliqqf
       61 serkytfved dkkvlkvkgs algisqdfkq gltqvlnkqn pwqwttsifa gqkahadedp
      121 sinktaltkf aqttadklnq grqgpenakl vadgtkykiq kevngtqida dklattvtnv
      181 ldnhqqtvnl aaaykkptvt asssslqtte rdmnklagtn vslqiqtktv tvpqatvmsw
      241 iindngkatv ssqavtnyvs alsqqystik ktrqfnsqqq gtvsvpagty gwsinvsatt
      301 amivasvkag qdlnkeivhn gsgystdgdi gntyvevske kqhewyikdg kvvmdsdivt
      361 gkpgqdtpsg vfyvwskqrn atlrgknddg sdyaspvsyw mpidytgvgl hdspwqpkyg
      421 gdwykehgsh gcvnnppdfm aklyaavdeg tpvivy
//
LOCUS       WP_005714015             113 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Glaesserella parasuis].
ACCESSION   WP_005714015
VERSION     WP_005714015.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (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   2  (residues 1 to 113)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..113
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12306
     Region          41..110
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkklsrytfs llfglfsatt faeekvttst eptpvvmqqv aatqkvntnv vnintatase
       61 iqdklvgiga kkaqaiveyr ekngkflnve qltevsgigk atleknrdri vie
//
LOCUS       WP_005714105             232 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Lacticaseibacillus rhamnosus].
ACCESSION   WP_005714105
VERSION     WP_005714105.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus rhamnosus (Lactobacillus rhamnosus)
  ORGANISM  Lacticaseibacillus rhamnosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 232)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Lacticaseibacillus rhamnosus"
                     /db_xref="taxon:47715"
     Protein         1..232
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=26240
     Region          111..232
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(177..178,181,205..208,210)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkritelmhh laammyylhs hhlkpkyrnr lffiavfitv cliavftgqh akesastass
       61 yasvtklakt nhtpsytaae itrvtpkkid wkapfesrpy pdvtkhpnls lhvnlkkqrv
      121 fikdgsktly tmyastgidd ttphgdftiq dergyeffnp neqmgahyyt sfylhgtylf
      181 hsvptdvngn yiqseaaklg kkpgshgcvr lsisdakwiy ehiptgtpvs ih
//
LOCUS       WP_005714296             206 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Glaesserella parasuis].
ACCESSION   WP_005714296
VERSION     WP_005714296.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 206)
  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 206)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 206)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..206
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22887
     Region          1..206
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 msdylnktee qqfeeakswf kengtpivva iflvaaatfg wnywqkhqie vaqttsasyq
       61 qvmesylqnp eknaplvqkf iaenkdssya vfaqleeakq aadkgdfatt ktlltqslgs
      121 ttdatlqnvi rfrlatvdyq lkefdaalat lsqikdtawd frkqlltgdl laakgdkaaa
      181 ksayeqakek agdanqilid vrlnnl
//
LOCUS       WP_005715551             161 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Aggregatibacter segnis].
ACCESSION   WP_005715551
VERSION     WP_005715551.1
KEYWORDS    RefSeq.
SOURCE      Aggregatibacter segnis
  ORGANISM  Aggregatibacter segnis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Aggregatibacter.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Aggregatibacter segnis"
                     /db_xref="taxon:739"
     Protein         1..161
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=18158
     Region          4..156
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mfdlfswdgw falfgehrlw imfasaflsa tvlpgnseii fvtlitpllw agspyfsmei
       61 qsllwiavtg ntlgslttya lgrwlptfnt ppqnakltwv lektqrygsv mlffswlpvv
      121 gdvfcavagw lrlnwvacli fmtlgkivry vfllflgvtv l
//
LOCUS       WP_005722836             162 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Lactobacillus crispatus].
ACCESSION   WP_005722836
VERSION     WP_005722836.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..162
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17669
     Region          2..153
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mvnsiftnrr avrnfssesi sddeikslia afqttpcgmh qtdvmslvvv kdealrdkie
       61 tktdnacyha pvlfiintkk dsmfgerdas cgaenimlea tdlglgsvyv mggaarlndd
      121 selqkelgid pafqtsvivp vgkigekpea tdrsnryqvt iy
//
LOCUS       WP_005723286             399 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Lactobacillus crispatus].
ACCESSION   WP_005723286
VERSION     WP_005723286.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..399
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43905
     Region          2..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkkilainsg sssfkfklft fpdekviseg madrvglngs tftikvkgek hqekvdipds
       61 etavtillen lkkydliddp keiigighri vaggeefkds tlidekslqk iydlkqyapl
      121 hntaeadvin afmkvlpgvp evavfdtsfh qtldpvhyly slpykyyeky garkygahgt
      181 svryvsqkaa eimkrdlkdl klivchlgsg asvtavkdgk sfdtsmgfsp magitmssrs
      241 gdvdpsllaf vmkkenldad qmlkvlnnes gllgisgisp dmrdlrgdmt klegekkkra
      301 dlarnifinr iiryvgaytl emrgldgiaf tagvgehdfg vrehvmdsle llglkpdsaa
      361 nkenatiitk pdstivgmvi ptneelmier dvvrvaglk
//
LOCUS       WP_005725669             303 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Lactobacillus crispatus].
ACCESSION   WP_005725669
VERSION     WP_005725669.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 303)
  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 303)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10097223
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..303
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33173
     Region          7..283
                     /region_name="TBP_aldolase_IIB"
                     /note="Tagatose-1,6-bisphosphate (TBP) aldolase and
                     related Type B Class II aldolases. TBP aldolase is a
                     tetrameric class II aldolase that catalyzes the reversible
                     condensation of dihydroxyacetone phosphate with
                     glyceraldehyde 3-phsophate to produce tagatose 1; cd00947"
                     /db_xref="CDD:238477"
     Site            order(28..30,33,53,56..58,63,67,70..71,230..231,233..234,
                     237,241,244)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238477"
     Site            order(86..87,174..176,178,205..206,208,227,229..230)
                     /site_type="active"
                     /db_xref="CDD:238477"
     Site            order(87,175,205)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238477"
     Site            order(174,176,178,206,208)
                     /site_type="other"
                     /note="Na+ binding site [ion binding]"
                     /db_xref="CDD:238477"
ORIGIN      
        1 mayfdngnqi fkdarknhya vgayntnnle wtraelraae etrtplliqv stgaakymgg
       61 ykfvkdmvad qmdsmnisvp vilnldhgdf esakecialg yssvmfdgha lptdenlakt
      121 keiiklaher gisveaeigk igenqgggel asvedakkfv aagvdklacg ignihgvypa
      181 dwkglnfdrl keiaeavpdt plvlhggsgi pedqvkkaik lgiakinint efqlafqeat
      241 rkyiedekdl dkkakgydpr klllpgaeai takmkemisw mgtktiddel kdasfdrssl
      301 nee
//
LOCUS       WP_005726312             151 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Lactobacillus crispatus].
ACCESSION   WP_005726312
VERSION     WP_005726312.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 151)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..151
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16640
     Region          2..151
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mtatteekyk llveqarali egeddwiant anlsallfns lndvnfagiy ryengelilg
       61 pfqgmpacvh iqmgkgvcgt taqneetqiv knvhefaghi acdsasnsei vvpifkqekl
      121 wgvfdfdstk lanfdetdkk ylteiaevif a
//
LOCUS       WP_005726509             391 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Lactobacillus crispatus].
ACCESSION   WP_005726509
VERSION     WP_005726509.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..391
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42776
     Region          2..391
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkkvlainsg sssfkyklfs fpdekviasg madrvgmdna vfkiklngke yikntsipdq
       61 eaavsllien lkkfhvlksl delagvghrv vnggkvfres alidekklqq ifdlgelapl
      121 hnvpeamgik afmkiipdvp qvavfdtsyh tsldqvnyly pipykyyeky girkygahgi
      181 svsyvaprta rlmgrnlytl klivchlgsg asvtavkngk sldtsmgfsp ltgvamgtrs
      241 gdfdpsaley imqktsmtve eavdmlnhks gmlgvsgvss dmrdllaskk kharlarkif
      301 vnrvvryvga yaaemdgidg ivftagigeh dpgvragvms alhylglepd ykanrtdgek
      361 fiskpdskvk alivptneel miarevirla k
//
LOCUS       WP_005728047             305 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: class II fructose-bisphosphate aldolase
            [Lactobacillus].
ACCESSION   WP_005728047
VERSION     WP_005728047.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus
  ORGANISM  Lactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 305)
  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 305)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10097223
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Lactobacillus"
                     /db_xref="taxon:1578"
     Protein         1..305
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33314
     Region          7..285
                     /region_name="TBP_aldolase_IIB"
                     /note="Tagatose-1,6-bisphosphate (TBP) aldolase and
                     related Type B Class II aldolases. TBP aldolase is a
                     tetrameric class II aldolase that catalyzes the reversible
                     condensation of dihydroxyacetone phosphate with
                     glyceraldehyde 3-phsophate to produce tagatose 1; cd00947"
                     /db_xref="CDD:238477"
     Site            order(28..30,33,53,56..58,63,67,70..71,232..233,235..236,
                     239,243,246)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238477"
     Site            order(86..87,176..178,180,207..208,210,229,231..232)
                     /site_type="active"
                     /db_xref="CDD:238477"
     Site            order(87,177,207)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238477"
     Site            order(176,178,180,208,210)
                     /site_type="other"
                     /note="Na+ binding site [ion binding]"
                     /db_xref="CDD:238477"
ORIGIN      
        1 mayfdngnqi fkdarknhya vgayntnnle wtraelraae etrtplliqv stgaakymgg
       61 ykfvkdmvad qmdsmnisvp vilnldhgdf esakecialg yssvmfdghk ldteenlakt
      121 keiiklaher gisveaeigk igenqgadgg elasvedakr fvaagvdkla cgignihgvy
      181 pegwkglnfd rlkeiaeavp neplvlhggs gipedqvkka iqlgiakvni ntefqlafqk
      241 atreyieagk dldkgnkgyd prklllpgte aitdamkemi gwlgtktidd elkdasfdrs
      301 slnee
//
LOCUS       WP_005728173             134 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Lactobacillus crispatus].
ACCESSION   WP_005728173
VERSION     WP_005728173.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 134)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..134
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=14496
     Region          2..131
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mtatteekyk llveqarali egeddwiant anlsallfns lndvnfagvy ryendelilg
       61 pfqgmpacvh iqmgkgvcgt aaqakttqiv kdvhefaghi acdsasnsei vvpifnqgkl
      121 wgvfdfdstk llsv
//
LOCUS       WP_005728184             400 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Lactobacillus crispatus].
ACCESSION   WP_005728184
VERSION     WP_005728184.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 400)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..400
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=44826
     Region          125..246
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          275..400
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(351..352,355,373..376,378)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mqsrtemrkr nnrnnlylii igiivviaii cgfvihnqrv aaersqreya sthfnpnvti
       61 ygvqvgkltv nkatakinkq adnvvflrnk kiiaekddkv qtisqaevkn iftkqhtdlp
      121 skqkyvfksa kideakkslq kiqnavvtyk ingqefklka ddlihevtyk ggkykftdvk
      181 klhakmeaid qevktlkksy kftvptgnkv ngktitvkne sygwgiyvkk avaavenafi
      241 ngqdvvggsk yiygegysty ahgygksnhg igknyvvvsi knqelwvvrk gkvavhltdv
      301 vtgtenksna tpkgvwyimy kespsvlrgy nddgskyask vqywmpftls gcglhdaswr
      361 sdwsksaylt ggshgcvnir paeirsvwnn vltndavivy
//
LOCUS       WP_005729167             650 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Lactobacillus crispatus].
ACCESSION   WP_005729167
VERSION     WP_005729167.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 650)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..650
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..650
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=75036
     Region          42..97
                     /region_name="TypeIII_RM_meth"
                     /note="Type III restriction/modification enzyme
                     methylation subunit; pfam12564"
                     /db_xref="CDD:432638"
     Region          175..569
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mtveskamdh irkvleqfgn kyfasngalk rttviedldn ydkdlmtall sddllhktyt
       61 skiagveife inkfvdmlky keywadsftk fdnkigltvg gkyiddsedv vldfpykdtv
      121 lkagmtkedv ehsgdadesf lnetlakpei dellepkilv natkydksgt hransikndd
      181 slilkgnnli alyslksrft ekvklvyldp pyntksdsfk yndkfsnsaw ltfmknrlei
      241 ardflttdgs ifvqiddnem pylkvlmdei fgkdnfigni iwkkktgssd ttsiaivtey
      301 ilvyaknnae vtfsknpdsy dkkryrytde yvdrrgpfyy dtldrgglqy sdslnygvta
      361 pdgsvlyphg rheyvndgwi wkwskdkvkw glengfcqfi ktgdkyklky kvylnvnnkd
      421 eiikrnapwk niiegimntn atseinklfg nkafdtpkpe allkfiinlg tfeedrvmdf
      481 fmgssttqav amkmdrhfig vdqmdyvdti svprlqmvin geqggiskdv nwkgggsfiy
      541 aklmpknqnf vkeiqeaeni etlfkifyrm kqeadidfrv dldkfersis epgtpiflqe
      601 ckrelirild knqlyynyad iddadvrskl sdndyqfnks fyslnesgee
//
LOCUS       WP_005729493             145 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Lactobacillus crispatus].
ACCESSION   WP_005729493
VERSION     WP_005729493.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..145
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15604
     Region          6..136
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mgslsddlkn livafqtapc gmnqtdvmnl vvvkdeglrn kikektdnac ynapvlfvin
       61 tkkdsmfger dascaaenim laatdlglgs vyvmggavrl ndagelqkel gidpafqtsv
      121 ivpvgkiaek peetdrsnry qvtiy
//
LOCUS       WP_005729841             768 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Lactobacillus
            crispatus].
ACCESSION   WP_005729841
VERSION     WP_005729841.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 768)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 768)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..768
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..768
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=86689
     Region          128..746
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mslaslfkkk reeqdlpdde qytdedqqdy dsddegfeqa peedgyidls qnpagtgksp
       61 deeddqdped eyydnrdapt tvlgqpslln vigpsywstd dlmqdefimr enmksktygi
      121 aayvppsgyp rmldtqvfqe llaqgnidlt ldivprtrrd tmhdlsnmln viranaeyqn
      181 ekgqsfqlre niakyndidn lldeiqfden rlydvaismi vwgtsdrdvn knfgvasdll
      241 anegisvtpy akrqksgflt tlplgarisy lddtyrnvdr kslavmdiar nasgrfnggi
      301 pfgnnqatps qnteflnifg tethrpvnyn mgivsesggg ksaankikia revailgfeh
      361 rsidpdgeyv llakklgqln ltitanakfv inpcalslfe tpleeetmtd stghqlspae
      421 meeqirlndd dhrqvvthkd gtkyvhqvni sqttsniegf vnviltsngd erkmnvgekn
      481 lldnaidsvi ddlqitedpn slyldkagmv ndvyqdhlpk peptlsdiyq klvlqnteed
      541 gqpsakvsrl ldalklylrd gkrpifdgqt ffgrgrspll ndykyvnfni sqlegsikrv
      601 ayyvltqylw erwmknpaka mtkkvldade ilqfiddpem saffevivrr drkrngsitw
      661 itqdierfqg npkakalvtn sefmfvlatk pehrqlmket vdltdgaldi ltgnpdpgeg
      721 ilreegesiw irtnpsqkem dfvesnravg qarknrnaie ainkaieg
//
LOCUS       WP_005732250             824 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: penicillin acylase family protein [Pseudomonas
            syringae group genomosp. 2].
ACCESSION   WP_005732250
VERSION     WP_005732250.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group genomosp. 2
  ORGANISM  Pseudomonas syringae group genomosp. 2
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 824)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 824)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 824)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..824
                     /organism="Pseudomonas syringae group genomosp. 2"
                     /db_xref="taxon:251698"
     Protein         1..824
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=89871
     Region          40..824
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 maspalrhfl prfgaaaaaa sflslagcql gggdpetvlp asgtfplkgl aqnvsvrrnn
       61 mgmpliesst yhdalftlgy ihagdrigqm lgmrllaqgr lsemagadal evdrlmrsvn
      121 lkqnasdlyn aasprlkrff dvyargvnay lfryrdklpa dvansgykpe ywkpedsali
      181 fsllnfslsv nlqeelsalv laqkvgadkl awllptypde elpfaeadkl kglnlnnqvn
      241 dlsdlnkial qlsdlnmlgv aassnwavap qrsrsgksll asdmqlpagl nsawsfvqir
      301 apkyqvsgvs iaglplvlsg fngklawsms nvkgdnqdlf lekikregnr isymadgkwm
      361 paashqetfl vkggspiret vyetrhgall nasatppgng lslalqvpnf kddksldaff
      421 dlsrapnvek afdtsreira itlnmifada snigwqvtgr fpnrregqgl lpspgwdgky
      481 dwdgfadsml hpydqdprqg wlaaanqrti pkgygmqlsn swgyperaer iaelansgkq
      541 dlrstvamqy dqtttfaakl ktmfqapgms kplkqaidal qeadrnkare aftrlmafdg
      601 klsatsadaa lyelflqesa kqifldelgp etspawqalv anasssyspq adhllgrdds
      661 pywddvktpq kedkpailar slaaavtsgd sllgsdhkaw qwgklhrdnw tstsplakql
      721 gggefnrgas paggdhstln vsgfewgkgf dthvapglrm ivdfslvepm tglistgqsg
      781 npaspyyans iepwqkgqym siplqqqnye kgygkqrltl tpgk
//
LOCUS       WP_005733634             795 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: penicillin acylase family protein [Pseudomonas].
ACCESSION   WP_005733634
VERSION     WP_005733634.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 795)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 795)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 795)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..795
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..795
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=88039
     Region          2..795
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkrslfilai ifallaggag wyvnsklpvr dgeiamsrlq apvtlryder gvphiraese
       61 adlyralgya haqdrlfqme mlrrlargel aeilgpnlve tdklfrtlri rehadayvar
      121 qdkntptwka leayidgvnq yqdtharpme fdalgipkrr fttedtvsig gylaysfaaa
      181 frteplltyv rdqlgpqylk vfdldwhpdg mlgskpalas adwkglaqla qlshkalega
      241 glpqfegsna wvisgsrtqs gkpilagdph irfsvpsvwy eaqlsapgfe lyghfpglnp
      301 faflghnmdf gwsltmfqnd dvdliaektn pdnpnqvwyh gqwvdmkrte qqitvkgqap
      361 vtltllesph gpivnnvmgk nagqtpiamw wsflvsanpv ldgfyeanra dtldkmrsaa
      421 ekiqspglni vwanakgdig wwaaaqlpir pqgvnpsfil dgstaqadkl gfypfsanph
      481 eenpargyiv sanfqplspt gmqipgyynp aergqelnrq lsdstikwdl aaskalqlgt
      541 qtdyapsilk plipvlrsvv sdpdeialve rlaswkgdyp vdsvgatlfn qflfdlteet
      601 fhdelgdtmf etllstrvld aalprlaada dspwwnnrns pheesrantv kvawrasvsh
      661 lrslygtnpd ewvwgkahtl tqghpmgsqk pldmifnvgp yaapgthevp nnlsssirpa
      721 pwpvgygpst rrlidfadpa hslginpvgq sgvpfdkhys dqakafvsge yvpqrfsekd
      781 vaehtegvlr lvpge
//
LOCUS       WP_005733333             631 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Pseudomonas].
ACCESSION   WP_005733333
VERSION     WP_005733333.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 631)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 631)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 631)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 631)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 631)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 631)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..631
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68200
     Region          1..631
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msqtnshgea agtakpigll iaavgvvygd igtsplytlk evfqggygve vthdailgvl
       61 slifwsliwv vsfkymafvl radnqgeggi malmalarra sakhpklqmm mvvfglfgaa
      121 lfygdsmitp avsvlsameg lelafdgldh wivpmalivl vglfliqrhg tarigvlfgp
      181 vmvtwflvlg algvygimqs pevlkavnpa wgvnffiihp gigvailgav vlaltgaeal
      241 yadmghfgrk pisrawfilv lpalllnyfg qgalvlgnpe tvrnpfylla pgwallplig
      301 lstmatiias qavisgafsm tlqaiqlgyi prmhiqhtss daqgqiyiga vnwalmagvi
      361 llvigfessg alasaygvav tgtmlcttil vstvmlmlwk wppllavpll iclllvdglf
      421 faanvpkifq ggafpvlaga vlfilmttwk rgkqllaeri degglplpif igsirvqpph
      481 rvqgtavflt arsdavphal lhnmlhnqvl heqvvlltvv yedsprvpaa qrvevesyge
      541 gfyrvilhfg fidepdvpaa lalcdlpeld fspmrttyfl sretvipskm dgmarwreal
      601 fafmlknang nlrffklpfn rvielgtqve m
//
LOCUS       WP_005733673             811 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: Lon protease family protein [Pseudomonas].
ACCESSION   WP_005733673
VERSION     WP_005733673.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 811)
  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 811)
  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 811)
  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   4  (residues 1 to 811)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..811
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..811
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89472
     Region          77..789
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mpdsvaanlr laphaltrpf saeqfsfatt nelepfrgvl gqeravealq fgvamprpgy
       61 nvfvmgepgt grfsfvkryl kaegkrmktp sdwvyvnnfd eprepkalel ppgtahefta
      121 digglidnll vtfpavfehp syqqkkssid rafnqrydra ldvierlsle kdialyrdss
      181 niaftpmadg kaldeaefsq lpeadrerfh edisaleerl neelaslpqw kresnnqlrq
      241 lneetitltl qpllaplsek yaenaavcay lqamqvyllk tlveqlvdda ktdaqarkll
      301 eeqyspslvv gntrdggapv vfeqhptydn lfgrieystd qgalyttyrq lrpgalhran
      361 ggflileaek mlgepfvwda lkrtlqsrkl kmesplgelg rvatvsltpq vipwnvkiii
      421 igsrslyytl qdldpdfqem frvlvdfdee ipmvdetleq faqllktrts eegmapltad
      481 avarlatysa rlaehqgrls arigdlfqlv seadfirqla sddktdaghi eralkakatr
      541 tgrvsarild dmmagvilid tdgaavgkcn gltvlevgds afgvparisa tvypggsgiv
      601 dierevnlgq pihskgvmil tgylgsryaq efplaisasi aleqsygyvd gdsaslgeac
      661 tlisalsrtp lkqcfaitgs inqfgevqav ggvnekiegf frlcearglt geqgaiipha
      721 nvttlmlder vvqavrdgqf hiyavrqade alsllvgepa gapdengefp egsvnarvve
      781 rlrdiaemls dedlkeelek epaqlqpelk v
//
LOCUS       WP_005727263             134 aa            linear   BCT 20-JAN-2025
DEFINITION  3-hydroxyacyl-ACP dehydratase FabZ family protein [Lactobacillus
            crispatus].
ACCESSION   WP_005727263
VERSION     WP_005727263.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
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 10101294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..134
                     /product="3-hydroxyacyl-ACP dehydratase FabZ family
                     protein"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=15132
     Region          17..128
                     /region_name="FabZ"
                     /note="FabZ is a 17kD beta-hydroxyacyl-acyl carrier
                     protein (ACP) dehydratase that primarily catalyzes the
                     dehydration of beta-hydroxyacyl-ACP to trans-2-acyl-ACP,
                     the third step in the elongation phase of the bacterial/
                     plastid, type II, fatty-acid...; cd01288"
                     /db_xref="CDD:238615"
ORIGIN      
        1 mpmntaeiqs kldcqaplml ldrvttlnkd qqviaqksvs anesyfqghf penpimpgvl
       61 lieamveatq fmwdrsdlil trvkrgrfre mvkpgmqlti kvnaikkyac qakvliddkd
      121 vcvadlefkv teen
//
LOCUS       WP_005733825             265 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phosphonate ABC transporter ATP-binding protein
            [Pseudomonas syringae group genomosp. 2].
ACCESSION   WP_005733825
VERSION     WP_005733825.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group genomosp. 2
  ORGANISM  Pseudomonas syringae group genomosp. 2
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
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   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Pseudomonas syringae group genomosp. 2"
                     /db_xref="taxon:251698"
     Protein         1..265
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=28660
     Region          3..247
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mtlrlsgiel rhsdgtlalr gldlniarge rvaiigpsga gkttllnlla salppsagql
       61 evlgadpwql sskrrqrlrs rialihqapp lparqrvita vsagklgqwg lgksllnllh
      121 pldvsgtrev larldladkl fercqqlsgg qlqrvgiara lyqapellla depvsamdpr
      181 ladhtlallc qhaiehhvtl vaslhavela lahfpriigv rdgqihfdla anevdrqhld
      241 tlyaneqlsp qpapdvsetp wtprc
//
LOCUS       WP_005735093             271 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Pseudomonas].
ACCESSION   WP_005735093
VERSION     WP_005735093.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..271
                     /product="formate/nitrite transporter family protein"
                     /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=28178
     Region          5..251
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mslntpqqia eiavesgvkk ahlglsslmi lgflagafia lgflldihvs tmiphewasl
       61 gnllgavvfp vglilvvlag gelltgnmms lpmalfagri glgqlvrnwv lvtlanliga
      121 lfvaycfghv vgltegpfma ktvaianakv gasfeqafis gigcnwlvcl avwlsyaskd
      181 vigkvvgmwf pvmafvaigf qhivanmfvi paaifagals waqfgdnfvp vflgnavgga
      241 vfvglayhla ffnaaarpae lsrasgaqap e
//
LOCUS       WP_005736172             631 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Pseudomonas syringae
            group].
ACCESSION   WP_005736172
VERSION     WP_005736172.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 631)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 631)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 631)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 631)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 631)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 631)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..631
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68299
     Region          1..631
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msqtnshaqa ggtakpigll iaavgvvygd igtsplytlk evfqggygve vthdailgvl
       61 slifwsliwv vsfkymafvl radnqgeggi malmalarra sakhpklqmm mvvfglfgaa
      121 lfygdsmitp avsvlsameg lelafdgldh wivpmalvvl vglfliqrhg tarigvlfgp
      181 vmvvwflvlg algvygimqs pevlkavnpa wglnffiihp gigvailgav vlaltgaeal
      241 yadmghfgrk pisrawfilv lpalllnyfg qgalvlgnpe avrnpfylla pswallplig
      301 lstmatiias qavisgafsm tlqaiqlgyi prmhiqhtss daqgqiyiga vnwalmvgvi
      361 mlvigfessg alasaygvav tgtmlcttil vstvmlmlwk wppllavpll iclllvdglf
      421 faanvpkifq ggafpvlaga vlfilmttwk rgkqllaeri degglplpif igsirvqpph
      481 rvqgtavflt arsdavphal lhnmlhnqvl heqvvlltvv yedtprvpsa qrfevesyge
      541 gfyrvilhfg fidepdvpaa lalchlaeld fspmrttyfl sretvipski dgmarwreal
      601 fafmlknang nlrffklpfn rvielgtqve m
//
LOCUS       WP_005737554             398 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [Pseudomonas syringae group].
ACCESSION   WP_005737554
VERSION     WP_005737554.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 398)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..398
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43872
     Region          20..391
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mmttlqvatp qgesgrivss agdylfryhh dastqaavsl lmplrmdeyr hrelhpifqm
       61 nlpegyvleq lrnrlakias vdpmlllals gssspigrvk vsspevdall qrqqfpgerl
      121 deilawdgte difaglvdry ilragisgvq pkvlvpehqd sapqrftskt sdlivksgrg
      181 efpglainef icmsvakeag itvpefylsd nfklfvmrrf drddqcnpig fedmaalmgl
      241 paekkysksy saiakairlf capdqvqdsl aqlfaivtls civgngdahl knfgllysdp
      301 iqrdarlapa ydivnttayi pedvlaldlv gnkslfasrq glldfaqacd varpqevisg
      361 qlqaleqvla rslelseqvp eviaairrca epfmrtfg
//
LOCUS       WP_005738441             290 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Pseudomonas syringae group].
ACCESSION   WP_005738441
VERSION     WP_005738441.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..290
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31194
     Region          13..261
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mnwlpvsehr fklaegafwd aeeqalywvd iagflacrli ageyrqwrmp epvsafipte
       61 qgdalvtlas gvyrldltse ktslslfcva dptpgnrane arcdtsgrlw lgsmqnnida
      121 eggdvplvrr sgglfrvdad asvtrlldgq givntllwnt dssvlysadt ldeviyqypv
      181 ladgtlgprq iwaaeqsrgs pdgsamdaqg yvwnarwggs clirfapdgs vdrvvdlpvs
      241 hptscvfagt dlqtlyvtsa apgdahgqfd gavlmahvgi sgkacqrfag
//
LOCUS       WP_005739411             199 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein, partial [Pseudomonas amygdali].
ACCESSION   WP_005739411
VERSION     WP_005739411.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas amygdali
  ORGANISM  Pseudomonas amygdali
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 199)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Pseudomonas amygdali"
                     /db_xref="taxon:47877"
     Protein         <1..199
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <7..177
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 kltaplltqa lqrasswpap irlsfnlsah dcatwesvst iveiiensgf dasrldleit
       61 etavmqdiaq vqqaiaqfrq lgcgislddf gtgfsslsql halaltklki drsfvtgvhd
      121 npasykivks lvalsldmsl gcviegvetq delnaltslg ctmvqgyfys ppisfaetla
      181 wletpddera fgytascrv
//
LOCUS       WP_005744672             160 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Pseudomonas syringae
            group].
ACCESSION   WP_005744672
VERSION     WP_005744672.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..160
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17055
     Region          27..159
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 midlqntgag lngygllaaq lealladerd fianaaqfsa flytqiddln wagfylnrne
       61 elvlgpfqgq iacvripfgr gvcgaaaqsr qtqrvqdvhe fpghiacdsa snselvvplv
      121 kdglligvld ldspsvgrfn evdqagierl aaiflastdc
//
LOCUS       WP_005745583             146 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Pseudomonas syringae group
            genomosp. 2].
ACCESSION   WP_005745583
VERSION     WP_005745583.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group genomosp. 2
  ORGANISM  Pseudomonas syringae group genomosp. 2
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Pseudomonas syringae group genomosp. 2"
                     /db_xref="taxon:251698"
     Protein         1..146
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16371
     Region          2..144
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mfeltsylgl favafgaatl lplqseavla gmllsehyvt tlllltattg nvlgsvmnwy
       61 lgrsverfrh krwfpiserh ldkaqiiyrr hgrwalllsw vpiigdpitm iagvlreplw
      121 sfllvvtfak alryltltai tlgwav
//
LOCUS       WP_005745604             275 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Pseudomonas syringae group genomosp. 2].
ACCESSION   WP_005745604
VERSION     WP_005745604.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group genomosp. 2
  ORGANISM  Pseudomonas syringae group genomosp. 2
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (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   2  (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   3  (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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Pseudomonas syringae group genomosp. 2"
                     /db_xref="taxon:251698"
     Protein         1..275
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29902
     Region          23..69
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msvqamswal sqqivteahg rhvllclany adqdgraafp sisslsrdtg lsprtvqyri
       61 rdlenlgvik rgnqaipsay isqkdrlpvc ydidlkrgah hapgaredit gctpehngvh
      121 attergaqha pnppinhplt ihnhkegdna sdkdeqkgks irknpkfdpv sakpdnasek
      181 awadfcdmrk tkrapltlra cemiaaklan hadpdavldk stasswsdvy pesilpgtsa
      241 kngkpsrhtr ldqvdhtdgl eldgngnyri agdgq
//
LOCUS       WP_005752891             435 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Pasteurella
            multocida].
ACCESSION   WP_005752891
VERSION     WP_005752891.1
KEYWORDS    RefSeq.
SOURCE      Pasteurella multocida
  ORGANISM  Pasteurella multocida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Pasteurella.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Pasteurella multocida"
                     /db_xref="taxon:747"
     Protein         1..435
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=50395
     Region          5..423
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mekltlqiyl eqawcdlafl yfdsetyqlc nfeyltdyvv qhygktgeha vslnypvnvf
       61 iddttslwsw lsdiapagas rrywlealdi kqeseekqqf lllkhaaisp ignlrikdav
      121 peqvevrlfd ldkakdrqsd fleyvnqsga mvggatgagg eapklllkrr enqvwidnqq
      181 qgqdqdvsyl vkyprgnysp idcdilraey hyyqelaqlg fdtidttrmr leegkrypsl
      241 wlprfdivqr egkthrlafe svysllqkqg gvldhettlr qlieristar lqfaqtdfvi
      301 ewvkrdllni afgnsdnhgr nmaflrdeqr iwlapiydfa pmradpegii rtttwqtkge
      361 ypqefageyh feriaevlad lveptllmqe lrrlagslvd lksrlvqrnl pqsildfpai
      421 gfdylpeklk kwgli
//
LOCUS       WP_005754115             195 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Pasteurella multocida].
ACCESSION   WP_005754115
VERSION     WP_005754115.1
KEYWORDS    RefSeq.
SOURCE      Pasteurella multocida
  ORGANISM  Pasteurella multocida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Pasteurella.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Pasteurella multocida"
                     /db_xref="taxon:747"
     Protein         1..195
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21357
     Region          5..193
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mkndkkrlii gisgasgaiy airllevlkp ldhiethlii snaakqtiaa etdysiqavk
       61 aladvnydvr digaaissgs yrtlgmiilp csiktlsgia hsytddlitr aadvclkerk
      121 plvlcvretp lhlghlrlmt qaaeigaqit plmpafyhhp ktvqdivdqs vnrlcdqfei
      181 qlaqdlfqrw ggeaq
//
LOCUS       WP_005754648             147 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Pasteurella multocida].
ACCESSION   WP_005754648
VERSION     WP_005754648.1
KEYWORDS    RefSeq.
SOURCE      Pasteurella multocida
  ORGANISM  Pasteurella multocida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Pasteurella.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 147)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Pasteurella multocida"
                     /db_xref="taxon:747"
     Protein         1..147
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16039
     Region          1..144
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mnyalllkql eqilepetyi isrmantsaf lyqhmpelnw vgfylvkdgv lkvgpfqgkv
       61 acsdigfgkg vcgytwqtgt ttvvddvhqf aghivcdsas qsevvvpifq ggemiaeldv
      121 dsprlarfsa edvaflenca alicike
//
LOCUS       WP_005759338             248 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Pseudomonas syringae group].
ACCESSION   WP_005759338
VERSION     WP_005759338.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  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   3  (residues 1 to 248)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..248
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28460
     Region          36..241
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mngssaddap qppkvlntpl eiaanlrlll eshdpliitf heraqrfqsy llevdrdsnv
       61 maldemiprd gerflsnges frvegfhdgv riawesssqm eivdtdgqrl yrgpmpeevi
      121 yhqrrnafra alklaqlvdi eiggdrlksp ltgklldisa tgcklrfegd vsermqlgqv
      181 yerfiaklpf gamtapvelr ylhfeerfht tfagvrfhnm sglvqrqver fvyqlqrear
      241 rfdkdddf
//
LOCUS       WP_005760986             221 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Pasteurella bettyae].
ACCESSION   WP_005760986
VERSION     WP_005760986.1
KEYWORDS    RefSeq.
SOURCE      Pasteurella bettyae
  ORGANISM  Pasteurella bettyae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Pasteurella.
REFERENCE   1  (residues 1 to 221)
  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   2  (residues 1 to 221)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Pasteurella bettyae"
                     /db_xref="taxon:752"
     Protein         1..221
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=23243
     Region          151..220
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkalksilal slglalstsv laaesssnvf sdakdvaktt keqvvsvkks aadklassks
       61 stadstmdkv nsakekanla knsvtdkass vkekagsmke anaekvsvik ekassmkesa
      121 tekmknmkdn atehkhssve kvsnqkeklt sstkvspssk inintadaet lqsltgigev
      181 kaqaiidyrk kvgkiknase lsningigev tvekiapyls f
//
LOCUS       WP_005761639             582 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Pasteurella bettyae].
ACCESSION   WP_005761639
VERSION     WP_005761639.1
KEYWORDS    RefSeq.
SOURCE      Pasteurella bettyae
  ORGANISM  Pasteurella bettyae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Pasteurella.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 582)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 582)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Pasteurella bettyae"
                     /db_xref="taxon:752"
     Protein         1..582
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=65193
     Region          3..560
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mmidkrlint vpdskkwiki tvlwnwltlv ggiisavvfa yvlqqafkqe lslisavvff
       61 iilvgalylr sfaskksvna syfastqvkh hlrtliyqkl ssmplnqvnq qstssviqia
      121 segveqieiy fgrylpqlfy sllapltlfi flvffnapta lvllvcvpli pmsiiavnki
      181 akkllakywg iyvglgssfl dnlqglitlk tyqddeykaq qmnveaehfr kitmkvltmq
      241 lnsvslmdll ayggaaigii malleyqegd isifgvilfi llsseffipl rllgsffhva
      301 mngkaasdki falldtavee ntdaetfkkq eqvkvqindl hfaynaekta ingltltiep
      361 kqltvfvgks gcgkstlvsl lmgfykpqqg eilfnqqnsa kidrtslyqh iclvshssyv
      421 fkgslrenml manlqatdeq iyhaleqvnl anfvhenggl dmpllsrgtn lsggqiqrla
      481 larallhdad lyifdeatsn idiaseeiil qfiqrlkqqk tivmishrla navhadhiyv
      541 lqagqlaeqg thtelmynng lytemftqqq dlenvrkeak ha
//
LOCUS       WP_005760075             213 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Pseudomonas syringae group].
ACCESSION   WP_005760075
VERSION     WP_005760075.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 213)
  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 213)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 213)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..213
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22661
     Region          4..208
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 msgtedeela vmkdwwqrng kplltgglla lvvvlgwqfw hryqagqsqg asmlyqqlle
       61 taltpsgqad tarvaeisgk lksefggtty aqfgslfvak vavdagkldd aaaelktvad
      121 kpandtlgei arqrlarvla aqnktddalk lldgdadkaf lasreelkgd llvqlgrtde
      181 ayaayqkaks alsedaavgg lqmklddlak gda
//
LOCUS       WP_005761802             274 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Pasteurella bettyae].
ACCESSION   WP_005761802
VERSION     WP_005761802.1
KEYWORDS    RefSeq.
SOURCE      Pasteurella bettyae
  ORGANISM  Pasteurella bettyae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Pasteurella.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Pasteurella bettyae"
                     /db_xref="taxon:752"
     Protein         1..274
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31589
     Region          1..251
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mifadlhvht nhsdgvceik dvlenalqhd ikvlsitdhd ttnhydeifa ygkhlglnii
       61 kgvemsyydf dvykkvhvvg lwlndltpni dklcghtlac rdayhkelin elsekgydic
      121 yqdakkfsky nivfkmnifq alrekypqem tkerykqlfa sktshetdik mgyipvrdgi
      181 eailqdggip ilahpcvynn ydeigkyvdy glkgleinhs kmkeidfklt qefakkyhll
      241 ksggsdfhdp nllkfgdfgl tkeqfeqlaf yarg
//
LOCUS       WP_005763196             204 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Pasteurella dagmatis].
ACCESSION   WP_005763196
VERSION     WP_005763196.1
KEYWORDS    RefSeq.
SOURCE      Pasteurella dagmatis
  ORGANISM  Pasteurella dagmatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Pasteurella.
REFERENCE   1  (residues 1 to 204)
  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 204)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 204)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Pasteurella dagmatis"
                     /db_xref="taxon:754"
     Protein         1..204
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23165
     Region          1..204
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Region          91..117
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(93..94,97..98,100,124,130..131,134..135,137..138,
                     160,163..164,167..168,171)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          122..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 maytieeeqe lnqlkawwse nhktviasvi lafaailgwn ywksyqitkt qqtsaayeyl
       61 iyrnttdlte rnkdieqfvq esgknvystl allnkakvev eqqfyalaek tlkqavtdap
      121 ddilasiasl rlasvqyqqh dyngaldsln kvksdvwdsk kyllmgdisl akgdivsakt
      181 nyekaqekas pleaqwlkvr lnnl
//
LOCUS       WP_005763901             587 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Pasteurella
            dagmatis].
ACCESSION   WP_005763901
VERSION     WP_005763901.1
KEYWORDS    RefSeq.
SOURCE      Pasteurella dagmatis
  ORGANISM  Pasteurella dagmatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Pasteurella.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 587)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Pasteurella dagmatis"
                     /db_xref="taxon:754"
     Protein         1..587
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=65435
     Region          3..560
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mmidkrlint vsdskkwvak tvlwnwvalv asivsavifa lcleqafeqt ltlgtlfsya
       61 inlvvalair afagkmsvka syqastnvkh elrtlifqkl aamplnqvnq qstssiiqva
      121 segveqleiy fgrylpqlfy sllapltlfi flvwfnapta lillvcvpli pmsiiavnki
      181 akrllhkyws iyvglgssfl dnlqglitlk iyqdddykak qmdieaekfr titmkvltmq
      241 lnsvslmdll ayggaaigil tallqfqsdn lgifgvilfi llaseffipl rllgsffhva
      301 mngkaasdki ftlldtpvet nesavdfrae nqvqvdiqnl hfaynaekqa ingldltiqp
      361 kqltvfvgks gcgkstlvsl lmgfhkaqqg kilfngqeiq dldrhsfyrh vslvshnsyv
      421 fkgtlrenml manlnatdeq iydvleqvnl anfvrenggl dmallsrgsn lsggqiqrla
      481 larallhnan fyifdeatsn idveseeiil sfiqrlkaek tivmishrla navkadqiyv
      541 lqqgvlaeqg nheslmaang iyaemfnqqr nlenirentr nggqqya
//
LOCUS       WP_005764689             146 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Pseudomonas].
ACCESSION   WP_005764689
VERSION     WP_005764689.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            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="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16205
     Region          2..144
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mfeltsylgl lavafgaatl lplqseavlv gmllseryat illlliattg nvlgsvvnwy
       61 lgrsierfrh krwfpvserh ldkaqtiyar hgrwalllsw vpiigdpitm iagvmreplw
      121 sfllvvtlak alryltlaai tlgwav
//
LOCUS       WP_005765699             191 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Pseudomonas].
ACCESSION   WP_005765699
VERSION     WP_005765699.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 191)
  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 191)
  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   3  (residues 1 to 191)
  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   4  (residues 1 to 191)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 191)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            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="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21428
     Region          1..191
                     /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"
ORIGIN      
        1 mlrillindt arkvgrlrsa lteagfevid esgliidlpa rveavrpdvi lidtespgrd
       61 vmeqvvlvsr dqprpivmft dehdpgvmrq aiksgvsayi vegiqaqrlq pildvamarf
      121 esdqalraql hardqqlaer krielakgll mkmkdcneee aytlmrrqam srqqkliqva
      181 eqiiamsell g
//
LOCUS       WP_005765613             330 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas
            syringae group].
ACCESSION   WP_005765613
VERSION     WP_005765613.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 330)
  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 330)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..330
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36568
     Region          22..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          243..325
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpepsslasw tralrkqlda lgvdshalcr sagihmesld dpgaqfpada iarlwqlavh
       61 asldpalglr vsrfvsptaf halgytlvas gslrevferi vryramaeds leldfravge
      121 ryefrfgtpk scqlpahell dafaaiyvrt crsrlgrgya plsvhlqrpa pdnpqpwedl
      181 frspvmfsaq enllefggdd fdshlddgpm qvneqkangd plpsliweqr vrsaietllp
      241 dgeptaesia aalhlstrsl hrhladegcc ydlllnqcrq nlallhmndp qsslseiayl
      301 lgftdtesls rafkrwtglt pgqyrsalgr
//
LOCUS       WP_005766004             206 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Bartonella bacilliformis].
ACCESSION   WP_005766004
VERSION     WP_005766004.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bacilliformis
  ORGANISM  Bartonella bacilliformis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Bartonella bacilliformis"
                     /db_xref="taxon:774"
     Protein         1..206
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=23723
     Region          7..170
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mnikqnikrl knwtislgtr rtasywlgfi vfiessffpv pgdvlyipms llrpkkayhy
       61 afiatvcsil ggilgwyiga yaydsiarpv lefydkydyf qalqthitqe mlvvciflsg
      121 lfhippikmt tlfagamdip lwlfattsli argarfyffa wliqrfgsqv lsfiskqwkw
      181 vlftgliafg liyglfstvl kyylnf
//
LOCUS       WP_005766350             317 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: aminoglycoside phosphotransferase family protein
            [Pseudomonas].
ACCESSION   WP_005766350
VERSION     WP_005766350.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 317)
  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   2  (residues 1 to 317)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            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="aminoglycoside 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=35366
     Region          46..225
                     /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"
     Region          131..274
                     /region_name="CotS"
                     /note="Thiamine kinase or a related kinase [Coenzyme
                     transport and metabolism]; COG0510"
                     /db_xref="CDD:440276"
ORIGIN      
        1 msyaqslntr llgalasygf dsephvepvt qgvaspsrls tewagfrvsf gesrcyakvl
       61 yadmtpvidf vsaaqasqca glsgaaprll sgdeqsgvli fedlgpqwrt arlddllvpg
      121 rldalwalkr qvhagpapdf trspmadier lralckrdgv alpaeqqwid rcvdmvwqal
      181 qkrqlrsvpv hgdgvasnvm vsgdgrlrlv dfdyggcmdp wydvaitlne lysfesewra
      241 gisawagqcl evdyavcrly alindwywtl wgfwsgsisa rqlefskvgq wtllrcrqcv
      301 qdprlegwmr qiqegra
//
LOCUS       WP_005767069             795 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pseudomonas syringae].
ACCESSION   WP_005767069
VERSION     WP_005767069.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 795)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 795)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 795)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..795
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..795
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=87972
     Region          21..795
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkrslvilai iiaiiaggag wyvnskqpvr dgeiamsrlq apvtlryder gvphiraene
       61 adlyralgya haqdrlfqme mlrrlargel aeilgpnlle tdklfrtlri rehadayvah
      121 qdkttatwka leayidginq yqdtharpme fdvlgiprrr ftaedtlsig gylaysfaaa
      181 frteplltyv rdqlgpqylk vfdldwhpdg mldakpalas adwkglaela qlshkaleda
      241 glpqfegsna waisgsrtqs gkpilagdph irfsvpsvwy eaqlsapgfe lyghfpalnp
      301 faflghnmdf gwsltmfqnd dvdliaektn pdnpnqvwyh gqwvdmkrte qqiavkgqap
      361 vtltliesph gpivnnvmgk nagqtpiamw wsflvsanpv ldgfydanra dtldkmrsaa
      421 ekiqspglni vwanakgdig wwaaaqlpir pegvnpgfil dgstaqadkl gfypfsanph
      481 eenpargyiv sanfqplspt dmqipgyynp aergqelnrq lsdssikwdl aaskalqlst
      541 qtdyapsilr plipvlrsai sdpdelalve rlaswkgdyp vdsvgatlfn qflfdlteet
      601 fhdelgdalf etllstrald salprlaada dspwwnnrns pheesrantv kvawrasvsh
      661 lrslygtnpd ewlwgkahtl tqghplgsqk pldsifnvgp yaapgthevp nnlsssirpa
      721 pwpvgygpst rrlidfadpa hslginpvgq sgvpfdkhys dqakafvnge yvpqrfseed
      781 vaahtegvlr lvpge
//
LOCUS       WP_005767530             147 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Bartonella bacilliformis].
ACCESSION   WP_005767530
VERSION     WP_005767530.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bacilliformis
  ORGANISM  Bartonella bacilliformis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Bartonella bacilliformis"
                     /db_xref="taxon:774"
     Protein         1..147
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=16209
     Region          59..133
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mkkmtsialv sifmlshays qfftllsese ivlasnvaqv gsdraphyev tpltadfvvs
       61 sligadiytm egenigkvkd illrqndieg iiivfggflg igeryvvvps vaikmthddg
      121 kwklithmtk dalqdapefk yeglwvr
//
LOCUS       WP_005767709             287 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Pseudomonas].
ACCESSION   WP_005767709
VERSION     WP_005767709.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..287
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30802
     Region          1..278
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mnvdlhchst asdgalspta lvaraheygv rvlsltdhdt legleearta ahslgmqlvn
       61 gvelsctwgg atihvlgygf dtqapaltea iarlhegrwl raeeisrkla ikgmpgaleg
      121 araiqqalgd sgnaparphf adfmvragfv kdraeafrkw lgagklgdvk qhwptledtv
      181 atlrasgawv slahpshydf trskrrklvg dfvqagghai evvngmqpad qvgtlailar
      241 efgllvsags dfhgpgnwge igtyrpvped lpplwcrfkh eqptaav
//
LOCUS       WP_005769231             214 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Coxiella burnetii].
ACCESSION   WP_005769231
VERSION     WP_005769231.1
KEYWORDS    RefSeq.
SOURCE      Coxiella burnetii
  ORGANISM  Coxiella burnetii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Coxiella.
REFERENCE   1  (residues 1 to 214)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Coxiella burnetii"
                     /db_xref="taxon:777"
     Protein         1..214
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=22903
     Region          108..211
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mksllitait taflwggvav addtlddpay tyaltlgdqd npedtadfve sspntaflde
       61 npygliadaq nvvqdysrlp nqirapgerv fifsprilrw aaydadgylv asgkanggaa
      121 fcanlgrpcq tpvgsfrisr kgdascvssr fplptggapm pycmffsggn aihgspyisn
      181 rntshgciri ypgaaawlsh yfmragtkvi vlpy
//
LOCUS       WP_005770007             700 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Pseudomonas syringae group].
ACCESSION   WP_005770007
VERSION     WP_005770007.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 700)
  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   3  (residues 1 to 700)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..700
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=75332
     Region          3..690
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msinldqaqq tfivearell qameesllql endpgdqdai gaifraahti kgsaglfglt
       61 pivsfthive dvldrlregs vavdagliav llksgdhmle lievvasrge alqpaalere
      121 aalrqalhiy qapgsapaed tacapgavdg eqaevvwhis lrfgvdvfrn gmdplsflry
      181 lntlgqmiqv ttvtdgippv eswdpeschl gfeidfrsaa ghdainevfd fvredcvvli
      241 tpveqtpess eptgtdlvsq naqspvvang ellgdqravp rvpgqttave rpasggehks
      301 kdgsyvrvna dkldelinlv gelviasaga kllarscnnd plqeasstvs glveqildga
      361 lhlrmipigd tfnrfrrvvr dvsqelgkdi dliingaete ldktvvekig dplmhllrns
      421 mdhgiesaea rraagkpakg hlnlnafhds gsivieiadd gaglnreril dkaqqrglva
      481 agasltdqei ynlifepgfs taeavtnlsg rgvgmdvvkr nitllrgtvd ldsqpgqgti
      541 vrirlpltla iingflvgid qstyvipldm vqecieldeh drqssrdkgy ldlrgevlpl
      601 vylrdhfnhe gpparrqnvv vvryaehkag lvvddllgef qtvikplgkl fgalrgisgs
      661 tilgsgaval ildipallnq ivqlearlaq pphslspasr
//
LOCUS       WP_005770804             206 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Coxiella burnetii].
ACCESSION   WP_005770804
VERSION     WP_005770804.1
KEYWORDS    RefSeq.
SOURCE      Coxiella burnetii
  ORGANISM  Coxiella burnetii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Coxiella.
REFERENCE   1  (residues 1 to 206)
  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 206)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 206)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Coxiella burnetii"
                     /db_xref="taxon:777"
     Protein         1..206
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23596
     Region          1..206
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 mtellsdqeq iemikkwwrd ygraialaiv iglligfgwr ywhrhqlekt erasalymql
       61 qilasqnawd ktkpltdrli kdygktpyaa masflnakra veqnhlplal dqlqwvmkna
      121 ivsdlkqlar lrasrillae nrpkaalnll qtvddqayqp lvdeikgdiy aamgnresak
      181 qfyetaqqsm kamgindpyl tmkisq
//
LOCUS       WP_005771954             136 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Coxiella burnetii].
ACCESSION   WP_005771954
VERSION     WP_005771954.1
KEYWORDS    RefSeq.
SOURCE      Coxiella burnetii
  ORGANISM  Coxiella burnetii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Coxiella.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Coxiella burnetii"
                     /db_xref="taxon:777"
     Protein         1..136
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15086
     Region          6..135
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mefiqnsvmr vnlsgfslle lliamamaai ltviaypayr yylvaanrrs aevgllrias
       61 rleefhslne tyqgatlshl kienesrdyl fqlsqlttes ylikaipqak qaadhcgtls
      121 idqsghqkas esgcwn
//
LOCUS       WP_005773099             267 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Bartonella elizabethae].
ACCESSION   WP_005773099
VERSION     WP_005773099.1
KEYWORDS    RefSeq.
SOURCE      Bartonella elizabethae
  ORGANISM  Bartonella elizabethae
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Bartonella elizabethae"
                     /db_xref="taxon:807"
     Protein         1..267
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=30397
     Region          1..182
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 myridynsyr svksfsrrvr flvmhytaid fkasvmaltg ekvsahylvp dpseqtyrea
       61 gfkdmrifnl vdenerawha gvsawagysh lndssigiei vnlatshsks sedtvemnhh
      121 neefsfppyn piqidavkel alnilqrypg itptdvvghs diaigrksdp gaafpwkely
      181 eagigawydd epknryqeqf sksfpskeea leklkcygyd isaasteigy knlirafqlh
      241 frqekydgil dvetaailya lvdkyfs
//
LOCUS       WP_005776577             155 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Bacteroides].
ACCESSION   WP_005776577
VERSION     WP_005776577.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 155)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..155
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17261
     Region          9..155
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 maeeltfisg skeeqylsll pqvkaliege edlvanlanv aavlkeafdf fwvgfylvkq
       61 drlvlgpfqg pvactrirkg kgvcgtawee aktqlvpdve afpghiacss lsrseivvpl
      121 ikegrvwgvl didsdllnff detdrkylee mcryl
//
LOCUS       WP_005777012             189 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Bacteroides].
ACCESSION   WP_005777012
VERSION     WP_005777012.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..189
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21025
     Region          6..173
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mktnevleti karrsvrvyd kkqvpsedln aileaatyap sgmhyetwhf tavrnaakle
       61 elnnrikeaf aksddkrlqe rghsetyccy yhapslvivs ndptqwwagm dcacaienmf
      121 laarslgigs cwinqlgttc ddpevraylt slgvpenhkv ygcvalgyqa egvslkektv
      181 kegtitive
//
LOCUS       WP_005778962             340 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Bacteroides].
ACCESSION   WP_005778962
VERSION     WP_005778962.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 340)
  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 13014342
            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="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=38931
     Region          227..338
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkqtahiylf sllflfcacn renktnplqp etvavadsle qtppeekpka isaeqieivk
       61 dllydkytle dtypykdttr sfqwdkiker lalleniqqe psrwgilqny knrngeaplv
      121 rhykrnaykr iadtlgiery qsvplylltd tlvperyged gslvhfladg ekfvkvspiy
      181 igeewyvpkk yvkvlpdttr ftkaimidrr nqniatleqt gearwavrsm npattgrhrp
      241 pyaqetplgi fvlqekkarm iflkdgstat ggfapyasrf sdggyihgvp vneprkalie
      301 yspslgttpr shmcvrnats hskfifdwap vnetiifvle
//
LOCUS       WP_005779314             824 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pseudomonas amygdali].
ACCESSION   WP_005779314
VERSION     WP_005779314.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas amygdali
  ORGANISM  Pseudomonas amygdali
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 824)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 824)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 824)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..824
                     /organism="Pseudomonas amygdali"
                     /db_xref="taxon:47877"
     Protein         1..824
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=89767
     Region          40..824
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 maspalrhfl prfgaaaaaa sflslagcql gggdpetvlp asgtfplkgl aqnvsvrrnn
       61 mgmpliesst yhdalftlgy ihagdrigqm lgmrllaqgr lsemagadal evdrlmrsvn
      121 lkqnasdlyn aasprlkrff dvyargvnay lfryrdklpa dvassgykpe ywkpedsali
      181 fsllnfslsv nlqeelsalv laqkvgadkl awllptypde elpfaeadkl kglnlnnqvn
      241 glsdlnkial qlsdlnmlgv aassnwaiap qrsrsgksll asdmqlpagl nsawsfvqir
      301 apkyqvsgvs iaglplvlsg fngklawsms nvkgdnqdlf lekikregnr vsymadgkwl
      361 patahqetfl vkggsplret vyetrhgall nasatppgng lslalqvpnf kddksldaff
      421 dlsrapnvek afdtsreira itlnmifada snigwqvtgr fpnrregqgl lpspgwdgky
      481 dwdgfadsml hpydqdprqg wlaaanqrti pkgygmqlsn swgyperaer iaelansgkq
      541 dlrstvamqy dqtttfaakl ktmfqapgms kplkqaidal peadrnkare aftrlmafdg
      601 klsatsadaa lyelflqesa kqifldelgp etspawqalv anasssyspq adhllgrdds
      661 pywddvktpq kedkpailar slaaavtsgd sllgsdhkaw qwgklhrdnw tstsplakql
      721 gggefnrgas paggdhstln vsgfewgkgf dthvapglrm ivdfslvepm tglistgqsg
      781 npaspyysns iepwqkgqym siplqqqnye kgygkqrltl tpgk
//
LOCUS       WP_005780715             111 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Bacteroides].
ACCESSION   WP_005780715
VERSION     WP_005780715.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..111
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12317
     Region          12..106
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(15..16,34..35,43,46,48..49,51,54..55,57,65,70,77)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(34,65..66,68,89)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mkdykenksn lsetfcnevy svvreipags vvtygdiaal lgmpqysrmv gralkqvpag
       61 lslpchrvvn aigrlvpgwd eqrqllsdeg vsfrkngcvd lklhrwkrvs i
//
LOCUS       WP_005781433             343 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Bacteroides].
ACCESSION   WP_005781433
VERSION     WP_005781433.1
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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..343
                     /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=39580
     Region          4..281
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mgddknkrid fvdltkgvci ilvvmahigg afekldyhsm iasfrmplyf fisgiffksy
       61 eglfgffirk inklivpflf fylsafllky ivwkiapgvf qlpvswtell vvfhdhalik
      121 fnppiwflla lfncnilfyl vhslrdrklg lmfaltllig iagfymgkhq ielplyidia
      181 mtalpfyvag fwirrynffl fphrfdklip lcilaalvvm yftatfvgmr tnnyagnifq
      241 fwasafagif mimlfckkfk klpvisylgr ysvitlgiha pllhfeypvv srfihnewgq
      301 aivlllltlt iciaatpifl klipqavaqk dfiktkqsqq qes
//
LOCUS       WP_005782682             424 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [Bacteroides].
ACCESSION   WP_005782682
VERSION     WP_005782682.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 424)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 424)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..424
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48369
     Region          6..410
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mansnaetev fvyadwemyd sprligilyy ssvrgkdtys feydatwlke gieidpelpl
       61 fsgrlysass nnfgvfqdsa pdrwgmklik rreallakag krslkrivai dfllgiydrh
      121 rmgglrykid kdgefvcedk slaappwtsl relehaveqy eknadkldee tlkwinqlfa
      181 pgsslggarp kadvtdenqy pwiakfpskn dttdiglwem ivhdlaikag itvpqaqvkq
      241 fkskyhtyls krfdrtetgk rihyssamtl lnrsdgddas egssyldive liksisfrpi
      301 edleelfrrv mfsvcvsntd dhlrnhgfly tengwmlspa fdinpnedgi glklninedd
      361 nsldmdlvml tadyylisek raeeiknevv navklwrsva kkyhasesei alkslafnii
      421 nnht
//
LOCUS       WP_005783683             158 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Bacteroides].
ACCESSION   WP_005783683
VERSION     WP_005783683.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..158
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17327
     Region          1..146
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdafietvsq ilidwgypgl fisallagsi vpfsseivll glvklgldpt lclisaslgn
       61 taggmtcyym grlgridwie kyfkvkkeki dkmqrflqgk galmaffafl paigevisia
      121 lgymrsnvwl ttasmfagkl iryiillkam qealnlvm
//
LOCUS       WP_005783568             817 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [Pseudomonas].
ACCESSION   WP_005783568
VERSION     WP_005783568.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 817)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 817)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 817)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..817
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88809
     Region          64..108
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          91..817
                     /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 mshhpiqpla ralrrglfag vlatmpvlps lvqaaestea lrtydiaagn ldqalnrfas
       61 asgillsvda altegkhsag lkgrygigsg lqrllagsgl aavqsqggws lqaisgdgal
      121 qlgatqisgr qeqenawgpv ggivakrsas gsktdsalve ipqtinvita aeikargaqs
      181 vtqallytpg msaggfadrv klfdeptsrg faptplyldg lhlpygggst ggalqiepys
      241 lerievlkgp asvlygqnqp ggivnmvskr psetpihqvv leagtyehks aaidlsgpld
      301 eegqllyrlt glandaqdei nyvenkrqfi apsltwrpnd dtsltlfaqy qkdkgvpeaq
      361 glpasgtlwd npngkikrdv figepgvnqy nreqyvlgye lshrlndvwt lkqnaryaev
      421 ddrytaplhg yrfvanpntg vqdqrylqrf gvdwsqtnkv fgvdsiaqae fdtgalshtf
      481 iagldyyhsn sqfhglydrn ppvidlfkpv ygqrlnfgqp yrwdrtitqt glylqdqikl
      541 dkwvlvlggr ydwanvvnke piqdtrfask dqaftgragl vylfdngisp fvsysesflp
      601 lagtdanrkp fepstgkqye vgvkyqppgq ksfiqasvyq ldqdnvlttn pvdttfstqs
      661 gamrsrgvel eakavlsdaw evvasasrnd ikytkdndgr qgrhpagisp ltasmwvnyt
      721 vlgdtplagl gaglgvryar qslgdyyega fnvpsysvyd aslsydlgas plklkgvkla
      781 mnvqnltnkt yvsqctsdld cyygegrtvv ssltydw
//
LOCUS       WP_005783710             326 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Pseudomonas].
ACCESSION   WP_005783710
VERSION     WP_005783710.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   ter Beek,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 11438136
            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="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=36542
     Region          1..321
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msievrnvsk nfnafkalds inldiqsgel vallgpsgcg kttllriiag letpdagsiv
       61 fhgedvsghd vrdrnvgfvf qhyalfrhmt vfdnvafglr mkpknqrpne sqiaakvhel
      121 lnmvqldwls drypeqlsgg qrqrialara lavepkvlll depfgaldak vrkelrrwla
      181 rlhedinlts vfvthdqeea mevadrivvm nkgvieqigs pgdvyenpas dfvyhflgds
      241 nrlhlgedkh llfrphevsl srheledhha aevrdirplg attrvtlkve gqselieaev
      301 vkdhdsltgl argetlffkp kvwqka
//
LOCUS       WP_005783721             334 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_005783721
VERSION     WP_005783721.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  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   4  (residues 1 to 334)
  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 334)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..334
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37223
     Region          22..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          248..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mteptslasw tralrkqlda lglnsaalca eagldpqqmd dpnaryplsa ttrlwqlavq
       61 asgdpaiglr vsrfvspttf halgyalvas gslrevferi vryhqvvsda lsleltrhgd
      121 ayhfrllqpq gspapapeai dafvaiyvrt crnrlgrdya plavylrrpe padptpwhtv
      181 lrspvffaad edrlefaahd fdshlddanp elaehnetvl krtlahlqpl twerkvravi
      241 eaqlpdgeps aervaqalhl slrslqrhla degcrfdall necrqnlall hlrdpqcsla
      301 eishllgfad tssfnrafkr wtgmtpgqfr eglr
//
LOCUS       WP_005784525              96 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [Pseudomonas].
ACCESSION   WP_005784525
VERSION     WP_005784525.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..96
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10119
     Region          1..96
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mkpstaldlq raavrevigh fqisnprvfg svltgtdqeg sdldllvdap pgttlfdlgg
       61 lqveledllg vnvdlltpgd lplkfrakvl aearpv
//
LOCUS       WP_005784657             133 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Pseudomonas].
ACCESSION   WP_005784657
VERSION     WP_005784657.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            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="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14008
     Region          1..131
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mgmdsqgftl melliavaiv allagiaypg yigqvkkvyr aqivallseq aqhleraytr
       61 dgtfidaggv iagndhyris ailnpqdfdl latpavdsvm addacaafsl sstgmrsnpg
      121 aapemsrkvc wgq
//
LOCUS       WP_005785081             804 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas synxantha].
ACCESSION   WP_005785081
VERSION     WP_005785081.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas synxantha
  ORGANISM  Pseudomonas synxantha
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 804)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 804)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 804)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..804
                     /organism="Pseudomonas synxantha"
                     /db_xref="taxon:47883"
     Protein         1..804
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87098
     Region          63..113
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          90..804
                     /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 mksaaggwvk qwlgasvlav sglallplsv araqeqqsaq fnfalaakpl pqalsefsrv
       61 tgisviytde apfglnapav sgqmsatqal qrllsntgft frqidartla leplpsdgav
      121 nlgattisav nptqdstsyq ppptssvmrs hgllletpqt vnvvpaqvlr dqqprnldda
      181 lgnisgitqs ntlgstqdav mlrgfgdnrn gsimkdgmpv vqgramnata erievlkgps
      241 sllygiqdpg gvvnivskkp elvqstslta rgstfgsgkn gsggnldttg plgdsglayr
      301 livdhededy wrnygthret lvapslawyg dttqvvlaye hreflapfdr gtaidpktnh
      361 plnipatrrl depfnnmegr sdlyrltvdh dlnddwkahf gyswnretyd asqvrvvkvn
      421 tngtltrsmd gtqgalttdr fataslegkv dvagmqhdlv fglddeyrki yradlirqap
      481 rgtfdynnpv ygnevagskv sapdsnqtdl lrsdslffqd aihlndqwil vggaryqmyd
      541 qyagkgvpft antdgngqkw vpraglvyry tdqlsfygsy tesfkpnsti aplanktvls
      601 gslqpeeska welgtkfdlp gritasaalf tidkrnvlvq vgegltseys vagkvrsrgl
      661 eldasgqltd kwsligsyay tdaevtedpk lkgnrlqnva kstgslsavy dfgsilggdq
      721 lrvgagaryv geragdaans fdlpsytvad vfasydtrle gqkvkfqlnv knlfdrtyyt
      781 ssvntqfvsm gdarqvsvss tltf
//
LOCUS       WP_005789461             452 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Bacteroides fragilis].
ACCESSION   WP_005789461
VERSION     WP_005789461.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..452
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=49964
     Region          9..434
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 meinvqlrde dsekivlgti iternaleev rellskdsfy npfhlqiyea ilqvassgsr
       61 pdvvavknkl iangvkfdlm eymriasnct fdlyqyaarl hdlairrkfw digqylvsns
      121 yseaedildv snsvsnelas lfksssttis tindglesvy gmindnllgn rqltgiptgf
      181 ekidsksggl qksdliiiag etsqgktsfa vsimrnaasl gakiamysme mkkeqitari
      241 lsmesgvpan qimysrltds qiqaidvgvg kmsgkgiyfd drstsnidti issirymklk
      301 fgidgaiidy lqilnvnmkg ankeqqmgdv arrlknlake ldiwiitlsq lnrdtmnpvp
      361 tlgrlrdsgq iaeaadvvil iyrpevnkks ypndfsnvdt kgtamidiak grnigllrfi
      421 cgfnaattcf ynldyvpllg gkqsgaeddn pf
//
LOCUS       WP_005790358             191 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Pseudomonas].
ACCESSION   WP_005790358
VERSION     WP_005790358.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 191)
  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 191)
  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   3  (residues 1 to 191)
  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   4  (residues 1 to 191)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 191)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            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="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21433
     Region          1..191
                     /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"
ORIGIN      
        1 mlrillindt prkvgrlkaa lteagfevid esgltidlpa rvetvrpdvi lidtespgrd
       61 vmeqvvlvsr dqprpivmft dehdpnvmrq aiksgvsayi vegiqaqrlq pildvamarf
      121 esdqalraql qardlqlaer krielakgll mkmkscneee aytlmrrqam srqqkliqva
      181 eqiiamsell g
//
LOCUS       WP_005790927             343 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Bacteroides fragilis].
ACCESSION   WP_005790927
VERSION     WP_005790927.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..343
                     /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=39524
     Region          4..281
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mgddknkrid fvdltkgvci ilvvmahigg afekldyhsm iasfrmplyf fisgiffksy
       61 eglfgffirk inkliipflf fylsafflky ivwkiapgvf qlpvswtell vvfhdhalik
      121 fnppiwflla lfncnilfyl vhslrnrrlg lmfaltllig tagfymgkhq ielplymdva
      181 msalpfyvag fwirrynffl fphrfdklip lcilaalavm yftatfvgmr tnnyagnifq
      241 fwasafagif mimlfckkfk klpvisymgr ysvitlgiha pllhfeypvv srfihnewgq
      301 aialllltlt vciiatpifl klipqavaqk dfiktkqstq qgs
//
LOCUS       WP_005792214             295 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Pseudomonas].
ACCESSION   WP_005792214
VERSION     WP_005792214.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            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="formate/nitrite transporter family protein"
                     /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=32075
     Region          24..276
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 matqadgktp nlsqeeqqdv dknqppraav lheiirtqgd qelersvaal wwsalaaglt
       61 mglslmamgl lnsrlpdaeg fkviasfgyc agflavilar qqlftentlt avlpvmskpt
      121 lgnaarllrl wtvvlvgnlc gtllvayvml hlpifdtktd lafleigrki mendsgqmfa
      181 kgivsgwmia tmvwmipsme sakmwiiili tylmalgdft hivvgsaevs ylvfagelpw
      241 kdfwlvfagp tlagniiggs fifalishaq irsesslpgk aaadprhpqp trkdq
//
LOCUS       WP_005792685             692 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Acidovorax delafieldii].
ACCESSION   WP_005792685
VERSION     WP_005792685.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax delafieldii
  ORGANISM  Acidovorax delafieldii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Acidovorax delafieldii"
                     /db_xref="taxon:47920"
     Protein         1..692
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72007
     Region          8..689
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mtlhndntta laqallhpas valygasddv skmggrpvqf lkrsgfagri ypinpkraei
       61 qglrawpslq slpevpdqvf vltptdtvip avrecaavgv kvvtvlasgf sesgtegvqr
      121 eeelrqiare tgirilgpss lgvvnprtgl vltanaafae pdippgkvfv ashsgsmiga
      181 lvsrgkargv gfaglvsvgs evdlnvgeic satlddpaie gyllflesmr hgpelrafar
      241 aahragkpvi ayklgrsaaa aematthtga iageddiada ffkdlgiarv gvldalletf
      301 plakriples apkrvgvvtt tgggaamavd qlgirgvvve pasaatlhrl qqaglpctpg
      361 rvldmtlagt kyetmkgtld illtapefdl vlavvgssar fqpqlavkpi vecagqpkpl
      421 aamlvpdape alaaltaagv pcfrtpeacg daiaavlarr qpgqepaplp rqadtttlne
      481 aqaygildqi gvphasaavr rfdavatqpl pfafpvvakv csadiphkte vggvvlnirn
      541 eqelanaiat lrknladkap qasceevlvq pmqkglgevl vgyrvdpeag pivmlaaggi
      601 waevakdrsi rlapvtveaa qemitevnal kpltglrgka kgdldalara vsalsqlalk
      661 pelriveaev npllilpegq gvtavdalif qa
//
LOCUS       WP_005795562             324 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Acidovorax
            delafieldii].
ACCESSION   WP_005795562
VERSION     WP_005795562.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax delafieldii
  ORGANISM  Acidovorax delafieldii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (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   2  (residues 1 to 324)
  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 324)
  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 324)
  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 12807598
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Acidovorax delafieldii"
                     /db_xref="taxon:47920"
     Protein         1..324
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32660
     Region          17..86
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          <162..323
                     /region_name="PRK10856"
                     /note="cytoskeleton protein RodZ"
                     /db_xref="CDD:236776"
     Region          251..317
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mnetvaqesv aedgensrlt agallreart asgvhiaala valkvpvgkl ealesddfst
       61 lpdivfvral assvcrslkl dpqpvlallp qgesprlsds nvglnapvkv ftgksssaaf
      121 gvpgpkpvaw avgvlligaa lmvllprgrg vdwsawfgat qtgspvqgaa vpapvtlpas
      181 vagastpevr pvasdaspmp pavsaapavp valatesqkv apaaatdtgv plapasaagp
      241 gdeqapagll sfrarseswi qvreatggvv lqrklasnet vsvsgalpla vvvgradate
      301 vfvrgkpyel agvsrenvar fevk
//
LOCUS       WP_005795869             374 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Acidovorax
            delafieldii].
ACCESSION   WP_005795869
VERSION     WP_005795869.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax delafieldii
  ORGANISM  Acidovorax delafieldii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Acidovorax delafieldii"
                     /db_xref="taxon:47920"
     Protein         1..374
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=41474
     Region          1..368
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msieirnvsk qfgdfqalrd vsldiasgel iallgpsgcg kttllriiag letadvgsih
       61 fsgedttdvh vrernvgfvf qhyalfrhmt vfenvafglr vkprserpse aqikqkvmdl
      121 lklvqldwla erypsqlsgg qrqrialara lavepkvlll depfgaldak vrkelrrwlr
      181 rlhdelhvts ifvthdqeea levadrvvvi nqgkieqsgs pqqvwdnpas pfvygflgdv
      241 nlfhgraheg lvhmegield spehaqaqna kafayvrphd ldveryspga gldaqgrprg
      301 ivaqlsraiv vgpiarleli plddhkpadn aspdhlieaq ipaqqfkemg fkegetlvvt
      361 prrarvfldq aagi
//
LOCUS       WP_005795664             383 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Acidovorax delafieldii].
ACCESSION   WP_005795664
VERSION     WP_005795664.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax delafieldii
  ORGANISM  Acidovorax delafieldii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 383)
  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 383)
  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   3  (residues 1 to 383)
  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   4  (residues 1 to 383)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 383)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 383)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 383)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Acidovorax delafieldii"
                     /db_xref="taxon:47920"
     Protein         1..383
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40187
     Region          35..374
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(111..113,134..135,184,236,261)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mlsdsrlrfs lqltaaaala aacgatlaqd vqtvkighag pisggiahig kdtengvrma
       61 vedlntqnlv iggkkikfvl aaeddagdpr qatavaqklc dqkvagvvgh lqsgtsipas
      121 svynkcdlph itasasnpdl tkpgyktsfr liandnalga alalfaadhl klktvaiidd
      181 rtaygqgvas vfkatalqkg lkvvgeeftn dkatdfmail taiknkkpdg ifyggldaqa
      241 gpmlrqmeql glgevkffgg dalctpklpe laskspavkn vtcatggasv dkmqggsewk
      301 krydaqfpgq fqiyspyayd aamvlvdamk ransvdpvvy gpflsktqyk gvtanisfts
      361 kgelvtpavt lytykdgsrv aln
//
LOCUS       WP_005795973             700 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Acidovorax delafieldii].
ACCESSION   WP_005795973
VERSION     WP_005795973.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax delafieldii
  ORGANISM  Acidovorax delafieldii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 700)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Acidovorax delafieldii"
                     /db_xref="taxon:47920"
     Protein         1..700
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72294
     Region          5..691
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mtdlltsalq prsvaiigas dnihriggrp iyymqrhgfk gaiypvnpsr eeiqgcksya
       61 slsalpevpd lalvvvggdk avaaveecad lgvksavvia sgfgetgpeg velqrhmvar
      121 arakgmrlyg pntqglanfg tgaiagfstm fievppmdgp igivsqsggm samtygllrg
      181 rglgvrhvha tgneadvsvg elalavahdp dvrllllyle sianpamlaa aaaharerdl
      241 piiaikagrs aqgqkaassh tgslanedrt vdaffrqhgi wrvrdpheqa raaqaylkgw
      301 rpegrrlvvi snsgascvmg adaaedeglp laelsaqtqa avasklpgfa tasnpidvta
      361 allsdsglfg kvlpevaqdp aadlffinip vagagydvqt fardaaafea atgkpvavaa
      421 wqesvaepfs aqgiatfpne gealgvlaqv tnhtalmrkq rtawpalpqv qlpegvrgfl
      481 neadslalla rhgiptvplr lchsaqeard afdavgapav vkacsaevph ksehglvalg
      541 vatreqaadl yerfdakmqa mgvardgviv aatrkgrhef mvgarvdpvf gpvvvvgdgg
      601 knvealkdca vllppfstad vvqalgtlri apllagvrgd ppldvqalae iavavgrvia
      661 gargamasvd lnpvmvgaag egavvvdalv ecagvpssgs
//
LOCUS       WP_005796518             340 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Bacteroides fragilis].
ACCESSION   WP_005796518
VERSION     WP_005796518.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 340)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..340
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=38965
     Region          205..338
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkqtayiyll tlscllcacn renrtnlpqp qvtgvadsle tvppeekpka isaeqikikk
       61 dllydkytle dtypykdttr nfqwdkiker lalleniqqt psqwgilqny knrngeaplv
      121 rhykrnaykr iadtlgiery qsvplylltd tlvperyged gslvrfladg enfvkvspiy
      181 igeewyvpkr yvkvlpdtth fiktimidrr dqnimtleqt geaqwtvrsm npattgrhrp
      241 pyaqetplgi fvlqekktrm iflkdgstat ggfapyasrf sdggyihgvp vneprkalie
      301 yspslgttpr shmcvrnats hskfifdwap vnetiifvle
//
LOCUS       WP_005799015             346 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acidovorax delafieldii].
ACCESSION   WP_005799015
VERSION     WP_005799015.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax delafieldii
  ORGANISM  Acidovorax delafieldii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 346)
  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 346)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 346)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 346)
  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   5  (residues 1 to 346)
  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   6  (residues 1 to 346)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Acidovorax delafieldii"
                     /db_xref="taxon:47920"
     Protein         1..346
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38861
     Region          29..215
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <192..345
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mrcfpvdwes rlygpqkisa ivavlnrdgv aaeqalegtg lcdemlcsts trisyrqifa
       61 viknairlgk npalailagk emhataygmy gfgmlsspty edevqfilky geiigavaki
      121 sncaceenna tytldvvltp daqdpiyrfa lefscaahlt ifrdlygsnf kfsslclacp
      181 kpgyaelyee yfdcpvnfsq gvnqwridai wvdsprkmpd avahlmavey cqkflselsh
      241 vggvasqvrr allektpanf ptidlmaeel gmqertlrrr leaegttyre llagarklla
      301 idylranklk tmdiatrlgy sdvanfrnaf yrwtghtprh yrkqnn
//
LOCUS       WP_005797684             206 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Acidovorax delafieldii].
ACCESSION   WP_005797684
VERSION     WP_005797684.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax delafieldii
  ORGANISM  Acidovorax delafieldii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 206)
  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 206)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 206)
  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   4  (residues 1 to 206)
  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   5  (residues 1 to 206)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Acidovorax delafieldii"
                     /db_xref="taxon:47920"
     Protein         1..206
                     /product="TRAP transporter small permease subunit"
                     /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=22939
     Region          3..171
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mqallkfsrg vdwlntqvgk yviwlilgst lvsgvnavvr kvfnvssnay levqwylfaa
       61 sfllaagytl lqgehvkvdv issrlskraq iwidvfgfvc fltpfcfavl wfgipffwqg
      121 yvsaemssna gglmrwpvyl mlplgfglll lqcwselikr iaflqglied ptakklekta
      181 eeelaesirr lreaatgngt gtpkad
//
LOCUS       WP_005799213             447 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Acidovorax
            delafieldii].
ACCESSION   WP_005799213
VERSION     WP_005799213.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax delafieldii
  ORGANISM  Acidovorax delafieldii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 447)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 447)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Acidovorax delafieldii"
                     /db_xref="taxon:47920"
     Protein         1..447
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=49078
     Region          39..346
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mnssctlqlf ansawcdvgs vsllgpeaqg wrsktytgys vewaiehgga rdahafacrf
       61 pvglqafehp hwpvflidml pqgfgreell rrlglsvtag esvdwrllla gagnsvgnlr
      121 vkeaaswlaa nagplrgftd devaergddf aeflashglf vagssgvqge wpkilltrae
      181 dgllyldhtl adararehyi vkfgrgsnea lasilrheap ymalarmlgl rvhadlvllk
      241 ralfiprfdr qvtgggvlrl gqesigtltg npgfdavpsh devcrqllrq cthpltevle
      301 yikrdvanla lgnkdnharn tavqrdfsgg irltplydfa pmylhpdgia rrirwegnds
      361 sapdwnrvid kvceiaqtlr eekrlpsaqk kalrevcrpa lveglrpmae plkkiaahgt
      421 dfglepavha hlklgieaqa qrltaln
//
LOCUS       WP_005800135             189 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Bacteroides fragilis].
ACCESSION   WP_005800135
VERSION     WP_005800135.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..189
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20971
     Region          6..171
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mktnevleti karrsvrayn rkqipaddln aileagayap ngmhyetwhf tavrntvkle
       61 elnerikgaf sksddkhlre rghsetyccy yhaptlvivs nepkqwwagm dcacaienmf
      121 laatslgias cwinqlgttc ddpevraylt slgvpenhkv ygcvalgyka egallkektv
      181 kagtitive
//
LOCUS       WP_005800373             743 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Bacteroides fragilis].
ACCESSION   WP_005800373
VERSION     WP_005800373.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..743
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=84082
     Region          33..743
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mtnrkplfii lfslgysgiy sqeqqvkkds vyqlqeivvs sqqilgskfk arnrtgsayy
       61 ispeeirrlg ytdinrmlka vpgvnmyeed gfglrpnisl rgtkaerser isimedgvla
      121 apapysapaa yyfpnvarme aievlkgssq vqygpfttgg ainlvsipip nsfsgkanis
      181 ygskntfksh tsvgsswkhf gymveylryq sdgfkkyedh aakgfkrndi iakirvktdh
      241 vkgvnhalel kfgyadensd etyvglsadd fkktpflrya gsqmdklktd hrqwvatyll
      301 tfsnklkitt nayynyfhrn wyklndvrag itskekrsia dvlvdpetni ryfdiltgkt
      361 dreeeallvr annrtyrsrg iqtraeyrfn lnefffdlef glryhadeed rfqwddsysm
      421 knkkmvlfme gihgtnanrv tsanalagyl laklrydawt vtaglryedv dllkkdytke
      481 dlarsgkvri etpnharvli pgvglhyqlm paasvffgih kgfappsael yqkpessvnm
      541 elgtrvaign fraeligfyn nysnmlgsdl aasggagtle qfnvgearvk gaeflvqyqp
      601 lpkncnvrlp lqvsytytdt eirnsfeshs wgnvvrgdei pyifkhalnm qlgieckwfy
      661 anigarynsd mrtspgqgti aerekvpanl ifdaslnvfv nkyltvrlna inltnrvylt
      721 srhpaglrag hpfgiyagan vqf
//
LOCUS       WP_005800600             713 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein, partial [Acidovorax delafieldii].
ACCESSION   WP_005800600
VERSION     WP_005800600.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax delafieldii
  ORGANISM  Acidovorax delafieldii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 713)
  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 713)
  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 713)
  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   4  (residues 1 to 713)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Acidovorax delafieldii"
                     /db_xref="taxon:47920"
     Protein         <1..>713
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
     Region          1..713
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 pdlcylhnfd tperpralrl ppgqgrqlrv amlemartlq adipkrlagp dckaeaeaiq
       61 kawqaqeasa fatldafaea rhfrlsreag hmvftltgdk ghplteneal alprerraei
      121 daaeqalrae iarfletmrp lerardeala nlrrqtikpl lehavqdirq alkkqikdaa
      181 klgqwldqvq revlahlalf eagdpdddae derkqqladl larcqvnlav dnaersgapv
      241 ivednpqlrs lfgaidiqtd tdpphadfsg iragsllkah ggfivlhlrd lvedeglwpr
      301 lrrflrssrl qiddgspaah gtaapialqp eevdadvkiv ligsveeyya lqeadpdtar
      361 rfrvkvdfae rfaasaatrh atavfvahcc kkrclphfap aavallleqt hreaddqnrq
      421 salfgnteal viesaalcqa rggalvdapd vnaalhartl rhnypeeqlh esitegerli
      481 tlhgtvagqv namtqidlgd yrfgfpvrit artfaghegl lnierevdms gpihdkgvli
      541 lhsyltalfs hvtplalnas ivfeqeysgv egdsascael yallsslsgl plrqgigvtg
      601 alnqhgevlp vgginekieg wflaceaagl dgsqgvlipg rnrrhlmlnr rvqqaveqgr
      661 fhiyavdhvr dgialltges sgmeagpglr adaasasvlh raeatlrafr rac
//
LOCUS       WP_005802961             410 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Bacteroides fragilis].
ACCESSION   WP_005802961
VERSION     WP_005802961.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..410
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46072
     Region          2..288
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          283..388
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mirilhtadw hlgqtffgyd rtqehehfld wlagvltknk idvlivagdv fdvsnpsaas
       61 qrmfyrfihr vttenprlql vvvagnhdsa arlesplpll qemrteikgi vrkqngkidy
      121 ehllvelkna agevealcla vpflrqgdyp vvetegnpya egvkelyarl lkyalkkrtd
      181 gqalvavghl latgseiaek dhseriiigg lesvspesfp eqivytalgh ihkaqrvsgr
      241 eniryagspl pmsfaekhyh hgvvkvtlde gwaveiekle ytplvrllsi pateaaapde
      301 vldelrglel pedepmpyle vkvklsepep mlrqqveeil egkpvrlari vsfyrqeaeg
      361 sveeevltag lqemnplqiv katfensyqa empeelvnlf qeacrtinle
//
LOCUS       WP_005803299             335 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_005803299
VERSION     WP_005803299.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 335)
  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 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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (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   5  (residues 1 to 335)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37930
     Region          23..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          251..328
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpqtatalas wvkaiqkale kagvdsqpll ekagldiqal snpdaryslk qtanlwklav
       61 hktqdscfgl kvasqvnqnt fhvlghslit sttlkemflr iiryfrvvtd ipelefygqg
      121 nshyfvihvp devqpesida fisvfirssr alqgsvfspl rielrrsepe dletfqsilk
      181 apivfnapkd mivfdtatie qpleganptl tqeydeiinr ylarfdkeni larvkvklie
      241 klstgdfqqq dvakslglsi rslqrklsae ntsyselldq trhelalsyi knsnhnitei
      301 ayilgftdvs sftrafrrwt dlspihyrek ylacs
//
LOCUS       WP_005804668             298 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter sp. SH024].
ACCESSION   WP_005804668
VERSION     WP_005804668.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. SH024
  ORGANISM  Acinetobacter sp. SH024
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 298)
  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 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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Acinetobacter sp. SH024"
                     /db_xref="taxon:575565"
     Protein         1..298
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33432
     Region          28..184
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          214..294
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpqnhltehl vdaflhlapa eglyptfisn itlmrvdhst ppiavlqeps ivlviqglkr
       61 gyigkeifqf qqgqclfisi aipfncdtvv ennelmlaia ikfepqmmad litkmdkqqq
      121 vvtedahsed lklscglrvi dmnatisdva lrllnllrsk qdtfilgeqv krelvyrvvq
      181 asggnlvesl samasrngvi yticeiiqrd yyhnltvqel akqagmsisl fhqtfkkvtn
      241 ysplqyikit rlhkarelit nnkmgvaeaa yevgyvsasq fsrefkrlfg vppkssii
//
LOCUS       WP_005806520             398 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [unclassified
            Candidatus Neoarthromitus].
ACCESSION   WP_005806520
VERSION     WP_005806520.1
KEYWORDS    RefSeq.
SOURCE      unclassified Candidatus Neoarthromitus
  ORGANISM  unclassified Candidatus Neoarthromitus
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Candidatus Neoarthromitus.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="unclassified Candidatus Neoarthromitus"
                     /db_xref="taxon:2638829"
     Protein         1..398
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43660
     Region          1..398
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkilvincgs sslkyqlidm ntenaiakgl verigipgsn leqkvdgsne kykvevdlkn
       61 hkeaialvlk tlcddrfgli kdlseinaig hrvvhggeky sksvivdeev iknieecikl
      121 aplhnpanli gikacrelmk dtpmvvvfdt afhqtisdka fmyglpyely ekysirkygf
      181 hgtshfyvan ecaramgksi edlkiitchl gngasvsavn agksvdtsmg ftplqglmmg
      241 trcgdidpav vtflidelnm sgkevnelmn kksgflgvsg kssdsrdied laqqgdkrak
      301 ltldmycyri ksyigsyiaa mngvdaivft agigensait rygvckdmes lgiiidenkn
      361 nvrgklteis adnskvkiyl iptneelvia rdtqdllk
//
LOCUS       WP_005807724             111 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Bacteroides].
ACCESSION   WP_005807724
VERSION     WP_005807724.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..111
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12333
     Region          12..109
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(15..16,34..35,43,46,48..49,51,54..55,57,65,70,77)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(34,65..66,68,89)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mkdykenksn lsetfcnevy svvreipagr vvtygdiaal lgmpqysrmv gralkqvpag
       61 lslpchrvvn aigrlvpgwd eqrqllsdeg vsfrkngcvd lklhrwksds i
//
LOCUS       WP_005808028             283 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Bacteroides].
ACCESSION   WP_005808028
VERSION     WP_005808028.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..283
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32401
     Region          199..278
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 meksnlltlt ldqpfvagtd dfapfynrlh klncaiilyc rsghatlaid lkkyeitpnt
       61 qvvllpgsvi tleeksedlq isffashiem freacirfep sffrflkekp cytlppefta
      121 pingllhatg aifadtdhrf rnqiarnhlq sflldvydkv hrlfthkeie ggnrpnelfh
      181 kfvtlvhehc csqrdvvfya drlcistkyl tsicrslmgg sakkviddft aleikvllqs
      241 tdlsiqeiad rlsfpdqsyl gryfkrhegv spmeyrarla gik
//
LOCUS       WP_005809266              96 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein
            [Desulfitobacterium].
ACCESSION   WP_005809266
VERSION     WP_005809266.1
KEYWORDS    RefSeq.
SOURCE      Desulfitobacterium
  ORGANISM  Desulfitobacterium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfitobacteriaceae.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Desulfitobacterium"
                     /db_xref="taxon:36853"
     Protein         1..96
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11200
     Region          3..93
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mldknalear lreykpilek rysvkkigvf gsyarneqne dsdidlivef trpvgfqfve
       61 lklyleeiln rkvdlvtpna lkpqikenil revsyq
//
LOCUS       WP_005814548             289 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Desulfitobacterium
            hafniense].
ACCESSION   WP_005814548
VERSION     WP_005814548.1
KEYWORDS    RefSeq.
SOURCE      Desulfitobacterium hafniense
  ORGANISM  Desulfitobacterium hafniense
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfitobacteriaceae; Desulfitobacterium.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 289)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 289)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Desulfitobacterium hafniense"
                     /db_xref="taxon:49338"
     Protein         1..289
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32925
     Region          21..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..287
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mdwvkqlnea ihyieenltt eisyetiski agcsvynfqr mfsyiadkpl seyirsrrlt
       61 maafdllnst driidialky gyespdsfsr afksfhgvlp ssvrnetvql kscpklsfqi
      121 tikgayhmny qiehwpafkv mgishkvkta aafevipglw ekawqdgtmr rfmenfpdyr
      181 pagflgiaag gqwgdsegmn yiiavtnhvd vsecqpipvl egmeefafpa aawaifeang
      241 elpdatqkvy kqfytewlpn sgyaladlpv iecymqenrq evwialvkk
//
LOCUS       WP_005815118             285 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Desulfitobacterium
            hafniense].
ACCESSION   WP_005815118
VERSION     WP_005815118.1
KEYWORDS    RefSeq.
SOURCE      Desulfitobacterium hafniense
  ORGANISM  Desulfitobacterium hafniense
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfitobacteriaceae; Desulfitobacterium.
REFERENCE   1  (residues 1 to 285)
  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 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   3  (residues 1 to 285)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 285)
  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   5  (residues 1 to 285)
  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   6  (residues 1 to 285)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Desulfitobacterium hafniense"
                     /db_xref="taxon:49338"
     Protein         1..285
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32223
     Region          21..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..283
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mgwiegisda inyiednite eltmeniskq afvssfyfqk gfamlcgftv geyirqrrlt
       61 lagselvstd rkiidialky gydspdsftk aflrfhgvtp tavrkdgaml ksfaplkikf
      121 sleggfimdy riiekeaftv mgaakvfkyd tagteipkfw tehyqtgkdk ivcgmygvcv
      181 desmgsdefe yliadnytts seipdgfvtk vipkhswavf ackgamptsl qntnqkifse
      241 wlpnckdyei aagyniemyt nvadypkgnq denyyseiwi pvqkk
//
LOCUS       WP_005817398             180 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Desulfitobacterium].
ACCESSION   WP_005817398
VERSION     WP_005817398.1
KEYWORDS    RefSeq.
SOURCE      Desulfitobacterium
  ORGANISM  Desulfitobacterium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfitobacteriaceae.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Desulfitobacterium"
                     /db_xref="taxon:36853"
     Protein         1..180
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19089
     Region          3..170
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdtikaielr ksvrsylpkp veaeiitqlv ragnsapkvg ifhtsvienp gilgeineea
       61 lvqyqnsgdk llmgraaleg yqplygapvf flfsapfanp lkeattscaa tcitiaatal
      121 glgscyihsa lqgirgnskl mekigipfgl tpicgvvvgh saedslsphr sitenvnycr
//
LOCUS       WP_005816179             393 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Desulfitobacterium
            hafniense].
ACCESSION   WP_005816179
VERSION     WP_005816179.1
KEYWORDS    RefSeq.
SOURCE      Desulfitobacterium hafniense
  ORGANISM  Desulfitobacterium hafniense
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfitobacteriaceae; Desulfitobacterium.
REFERENCE   1  (residues 1 to 393)
  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 393)
  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
REFERENCE   3  (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   4  (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   5  (residues 1 to 393)
  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   6  (residues 1 to 393)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Desulfitobacterium hafniense"
                     /db_xref="taxon:49338"
     Protein         1..393
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43072
     Region          20..61
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          81..384
                     /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 mrtgmliykd vlsslspeak kilglilhkg amtksqlakv aglklttlnr mmlplekedl
       61 ilptetgest ggrkpviydv nprryyvigi disrlysqvv ltnlkmelle kdrfdmdrns
      121 spqatlnril dwvekvlekr eqgyvigvgi gtvgpldrks giilnpenfe argweniplk
      181 aiveertglp viidnganga vlaetrygsg kgmksviyln cgvgirtgvi ssgtlvrtin
      241 daddtfahmv idvngkpcrc gnqgcverys siyaimeafn perpvsyqel creaeesdtp
      301 arqvlqnaav rmgtglanfi qllnpglvvl sgplilhsql fyeicveaak rrrpwdkggh
      361 lvfsrggafe enaisigaaa lvvehylepe alg
//
LOCUS       WP_005817472             343 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Bacteroides fragilis].
ACCESSION   WP_005817472
VERSION     WP_005817472.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..343
                     /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=39584
     Region          4..281
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mgddknkrid fvdltkgvci ilvvmahigg afekldyhsm iasfrmplyf fisgiffksy
       61 eglfsffirk inkliipflf fylsafflky ivwkiapgvf qlpvswtell vvfhdhalik
      121 fnppiwflla lfncnilfyl vhslrnrrlg lmfaltllig ttgfymgkhq ielplymdva
      181 msalpfyvag fwirrynffl fphrfdklip lcilaalavm yftatfvgmr tnnyagnifq
      241 fwasafagif mimlfckkfk klpvisymgr ysvitlgiha pllhfeypvv srfihnewgq
      301 aialllltlt vciiatpifl klipqavaqk dfiktkqstq qgs
//
LOCUS       WP_005817543              84 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: zinc ribbon domain-containing protein
            [Desulfitobacterium].
ACCESSION   WP_005817543
VERSION     WP_005817543.1
KEYWORDS    RefSeq.
SOURCE      Desulfitobacterium
  ORGANISM  Desulfitobacterium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfitobacteriaceae.
REFERENCE   1  (residues 1 to 84)
  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 10577258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Desulfitobacterium"
                     /db_xref="taxon:36853"
     Protein         1..84
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=9246
     Region          3..77
                     /region_name="Zn_ribbon_2"
                     /note="Putative zinc ribbon domain; pfam12674"
                     /db_xref="CDD:463667"
ORIGIN      
        1 mktciacgmp mtkaadyalg deskdyclyc arpdgsmqsy pekvegmtdf lirtqgldqe
       61 aarqtairtl sklpawqdre itsc
//
LOCUS       WP_005818355             336 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [Bacteroides].
ACCESSION   WP_005818355
VERSION     WP_005818355.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 336)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 336)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..336
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=38094
     Region          <57..317
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mieltccpst lqkgfstysp valkelfnsq kvnhilpyng mdnneteqke fqdnnkhmsi
       61 sgaqqkyslv vdngqmrlsl eqeqatlllk tklseyanke ispanehltm qiasqvynip
      121 taanglcffq ndepayitrr fdiapngrkf rkedfaslag iskgnkgpny kydvlsyeem
      181 adiikqyvsa ssvevlkffr lvifnflfsn gdahaknfsl letpsgdfil apaydllntr
      241 lhifddhvfa lqrglfkent lngndgavtg kefiefgiri gippkrvhke lisfcqkaeq
      301 vrdlveksfl pnqlkkqyll hyqmrkdsyl svgipt
//
LOCUS       WP_005820020             189 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Bacteroides fragilis].
ACCESSION   WP_005820020
VERSION     WP_005820020.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..189
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20955
     Region          6..173
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mktnevleti karrsvrvyd kkqvpsedln aileaatyap sgmhyetwhf tavrnaakle
       61 elnnrikgaf aksddkrlqe rghsetyccy yhapslvivs ndptqwwagm dcayaienmf
      121 laarslgigs cwinqlgttc ddpevraylt slgvpenhkv ygcvalgyqa egvslkektv
      181 kagtitive
//
LOCUS       WP_005820434             347 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Actinobacillus
            minor].
ACCESSION   WP_005820434
VERSION     WP_005820434.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus minor
  ORGANISM  Actinobacillus minor
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Actinobacillus minor"
                     /db_xref="taxon:51047"
     Protein         1..347
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=39487
     Region          <53..329
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 msvcritlqa ltnseektgy stkgllaltg nekfnpmlpf srqeftsstp qkqkgmsisg
       61 yqpklqliiq dnqftsidqq glyilkpspa dypnlaeneh atiqlmkklg fcvpenglia
      121 fnaseltaek efafvikrfd rteegkpihk eqldgamnvr ekygkigndn eqyisyeqav
      181 kfilthtenn lsqrkelfrr ivyayllgnn dlhlrnfsli hskegtitla pvydfvsvap
      241 yselfnssil alpllakeeg gkelahgfdt qygeyigqdf iefgenigls krliiekllp
      301 eikaeaemve qvyqtsflpe khkeqilkay lrrlnllfil neekllk
//
LOCUS       WP_005820563             295 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Bacteroides].
ACCESSION   WP_005820563
VERSION     WP_005820563.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 295)
  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 295)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 295)
  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   4  (residues 1 to 295)
  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 295)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..295
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34897
     Region          45..295
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          216..295
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 meknkplela ldllkhsnmv cnneyrfvtp dfgivisfan meshlfrlgq pyrlkegrii
       61 rglrgkarii inlieytvyp qtivtfipgs ivelleftpd ydfqmiavdk dflpllrrdq
      121 lfeshvrqnl vtrvtdtewk lsdayftliw etvqektfrr evvqhllaal lhnikyirte
      181 eandashrfs hqeeifwrfi tlvnesskne rtvgfyadkl cltprylntl irqvshqtvm
      241 ewinqsvile akvllkhsdl lvyqisdelh fpnpsffckf fkrmtgmtpq eyqkr
//
LOCUS       WP_005805121             174 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: transcription termination/antitermination protein
            NusG [unclassified Candidatus Neoarthromitus].
ACCESSION   WP_005805121
VERSION     WP_005805121.1
KEYWORDS    RefSeq.
SOURCE      unclassified Candidatus Neoarthromitus
  ORGANISM  unclassified Candidatus Neoarthromitus
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Candidatus Neoarthromitus.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Kang,J.Y., Mooney,R.A., Nedialkov,Y., Saba,J., Mishanina,T.V.,
            Artsimovitch,I., Landick,R. and Darst,S.A.
  TITLE     Structural Basis for Transcript Elongation Control by NusG Family
            Universal Regulators
  JOURNAL   Cell 173 (7), 1650-1662 (2018)
   PUBMED   29887376
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Liu,B. and Steitz,T.A.
  TITLE     Structural insights into NusG regulating transcription elongation
  JOURNAL   Nucleic Acids Res 45 (2), 968-974 (2017)
   PUBMED   27899640
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Steiner,T., Kaiser,J.T., Marinkovic,S., Huber,R. and Wahl,M.C.
  TITLE     Crystal structures of transcription factor NusG in light of its
            nucleic acid- and protein-binding activities
  JOURNAL   EMBO J 21 (17), 4641-4653 (2002)
   PUBMED   12198166
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415705
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="unclassified Candidatus Neoarthromitus"
                     /db_xref="taxon:2638829"
     gene            1..174
                     /gene="nusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
     Protein         1..174
                     /product="transcription termination/antitermination
                     protein NusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
                     /calculated_mol_wt=19863
     Region          7..174
                     /region_name="NusG"
                     /note="Transcription termination/antitermination protein
                     NusG [Transcription]; COG0250"
                     /db_xref="CDD:440020"
ORIGIN      
        1 mstvlsnwyv lhtysgyenk vknsleklie snslhdyile ivvpthetie ksgnkikkvs
       61 kkvypgyvfv kmimsdemwy rvrnirgvtg fvgptgkeav pldqeeirfi esyvaenqdd
      121 lykvgnsvki ksgilkgkyv virevdnknk rikasidvig nniveidfcq ldrl
//
LOCUS       WP_005823302             184 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Bacteroides].
ACCESSION   WP_005823302
VERSION     WP_005823302.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 184)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..184
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=20424
     Region          44..174
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(130..131,134,147..150,152)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkkkiiryli ishltfilsi ggmavafyyy htaqmaqikn anilliskde mklrlidykg
       61 qelftadiac gknygnkekq gdlktpegtf kiidiqdask wkhdfgdgkg eiegaygnhf
      121 irletpghkg igihgthdpl sigtrategc iriknseler lvslirvptt viitpavkdi
      181 kpsk
//
LOCUS       WP_005821901             340 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-oxoacyl-ACP synthase III family protein
            [Bacteroides].
ACCESSION   WP_005821901
VERSION     WP_005821901.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 340)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            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="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37562
     Region          8..338
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mqaylnhlsi ylpqeirtna disrehpews vekisakvgi etrhlaasee tacdmackag
       61 kqlfddykid kgtidyvilc tqspdyrlps sacilqdqlg lpkscgafdy nlgcsgyiyg
      121 lglakgliis eqanrvlllt aetyskylsp kdkgnktifg daatasliss eltnrgvnys
      181 ieklsygtdg sgaasliirn ggsrhpqcva edvydeegnf iynpnylymd gksifnftaf
      241 evpqlvrenl kknklqitdi dlvifhqane ymlntvrkrc rieaekffvd iqdvgntvsn
      301 sipiaikkae engrlknvkk mllsgfgvgl smgtvvltkq
//
LOCUS       WP_005822417             686 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate--CoA ligase family protein [Bacteroides].
ACCESSION   WP_005822417
VERSION     WP_005822417.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..686
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73847
     Region          4..686
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mittqllhpq sivvvgasnn thkpggailk nlinggyqge lravnpkete vqgvpsfada
       61 kelpdtdlai laipaalcpe vvetlagekq trafiilsag fgeetregsl leeriletvn
      121 kygasligpn cigllntwhh svftqpipnl npqgadliss sgatavfile savakglqfn
      181 svwsvgnakq igvedvlqym detfdpqkds kikliyiesi knpdrllfha sslirkgcki
      241 aaikagsses gsraasshtg aiassdsave alfrkagivr cysrgelttv gciftlpelk
      301 grnfaivtha ggpgvmltda lskgglnvpk legpladelk sklfpgasvg npidilatgt
      361 pehlgiaidy ceekfenida ilaifgtpgl vtmfetyevl hqkmltckkp lfpvlpsvrt
      421 ageevaffle kghvnfadev mlgtalsrii napkpavpei elfgvdvpri rriidsipqn
      481 gyiephcvqa llhsagipvv eefvsgnkde vlafarrcgf pvvakvvgpv hksdvggvvl
      541 nikseqhlal efdrmmqise araimvqpml kgtelfigak yeekfghvvl cglggifvev
      601 lkdvssglap lsyeeaysmi hslraykiiq gtrgqkgvne dkfaeiivrl stllrfatei
      661 kemdmnplla tdkeviavda ririek
//
LOCUS       WP_005815415             236 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Desulfitobacterium hafniense].
ACCESSION   WP_005815415
VERSION     WP_005815415.1
KEYWORDS    RefSeq.
SOURCE      Desulfitobacterium hafniense
  ORGANISM  Desulfitobacterium hafniense
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfitobacteriaceae; Desulfitobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Desulfitobacterium hafniense"
                     /db_xref="taxon:49338"
     Protein         1..236
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=26527
     Region          2..164
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mpqiewvgtp nfrygrnglq plaivnhita gyypgcldwm qrsgsqasah ylvlrngril
       61 qlvkdentaw hagivnkpdw nlydgtnpny ytigiehegm pgdelteaqy qstlwlhkql
      121 itkypaitvd srhiighyri dsinrpncpg akfpwaelfa dlkgehdvdh lviyadgdvg
      181 aalllsfklk cpmvhkafae niqakhkhwv gvqgtngnrn yyyagsdrie taklgl
//
LOCUS       WP_005822825             159 aa            linear   BCT 20-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein
            [Actinobacillus minor].
ACCESSION   WP_005822825
VERSION     WP_005822825.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus minor
  ORGANISM  Actinobacillus minor
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
REFERENCE   1  (residues 1 to 159)
  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 159)
  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 11443421
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Actinobacillus minor"
                     /db_xref="taxon:51047"
     Protein         1..159
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16701
     Region          6..158
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          115..158
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
ORIGIN      
        1 mkksffllpl vvaftlagcn sttssevets davntantsg twqpadiqpt ampssmnqpv
       61 sqptygastt psyntsanss ysnstesvgn cqvirdtsgt pvytqmtkgc ytdstytvga
      121 kdtlylisfl sgtspsqias lnnmstttkl kvgqslrvr
//
LOCUS       WP_005823890             208 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Actinobacillus minor].
ACCESSION   WP_005823890
VERSION     WP_005823890.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus minor
  ORGANISM  Actinobacillus minor
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
REFERENCE   1  (residues 1 to 208)
  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 208)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 208)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Actinobacillus minor"
                     /db_xref="taxon:51047"
     Protein         1..208
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23008
     Region          6..208
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 msseylnkte eqqfeeaknw fkanstpill aificaaatf gwnfwkkhqv esaiqastsy
       61 qntmeaylqd paknqplvak fleeakgtny avfaqleevk qavtqadyak aqtllqntls
      121 atndatlqvv irfrlaeigy qlkqydeala vlaqiqgsaw esrkqllsad ilaakgdkaa
      181 aksayeqlka tatsesekal idlkinnl
//
LOCUS       WP_005825253             207 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Actinobacillus minor].
ACCESSION   WP_005825253
VERSION     WP_005825253.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus minor
  ORGANISM  Actinobacillus minor
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
REFERENCE   1  (residues 1 to 207)
  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   2  (residues 1 to 207)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Actinobacillus minor"
                     /db_xref="taxon:51047"
     Protein         1..207
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=20786
     Region          137..206
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkalktllal gvamtvsats fadttnplts lkdtaksaat nqvnavkesa vssvtnaktt
       61 assavsntks satsaltnak snvtekvtsa kttattardt lnsakttate katsakttvt
      121 ekatsakaaa tekatsvatk vkasskvnvn tadaatlqsl sgigeakaka iveyrnkvgk
      181 iksaselsni sgigdatiek itpyltf
//
LOCUS       WP_005825353             596 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LysM peptidoglycan-binding domain-containing protein
            [Bacteroides].
ACCESSION   WP_005825353
VERSION     WP_005825353.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 596)
  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 596)
  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 17581782
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..596
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=67816
     Region          <23..76
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          84..128
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
     Region          165..208
                     /region_name="LysM"
                     /note="Lysin motif; smart00257"
                     /db_xref="CDD:197609"
     Region          <487..546
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
ORIGIN      
        1 mktinriics lllasacsig aiaqenqsyf lhtiekgqsl ysiasmygvs qsdiiklnpg
       61 sdekifigrt lriprsaani qketyhtiet getlyrltvk ynvsakaicd anpglsaenf
      121 rigqvirips ttepqtmvpv etqsstvvan nnilgpvesr crdmhkvkrk etvfsisrey
      181 giseaeliaa npelkgenki kkgtflcipy pkaqteqniq sqaiptdsel frenrkkter
      241 fstikaavil pfldgvskse ssrmveyyeg llmavdslkr tgtsidlyty nsgpesasln
      301 silgksemkd mdiifgplyq qhikplaefa kkqdtrlvip ftskdntvfq npavyqintp
      361 qsylysevyd hfvrqfpnan vifieasqgt kdkaefikgl kdelrnrsip mkslkedvtv
      421 eslktvlrtd renifiptsg snltlikilp qltllvreqp esrvhlfgyp ewqtytkdhl
      481 eaffeldtyf yssfytnnll paainftksy rrwygkemde rypkfgmlgf dtgyfflkgl
      541 arygssfekn mqgldlipiq tgfkfqrvnn wggfinkkvf fvhftknfel vkldfd
//
LOCUS       WP_005826471             105 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Bacteroidaceae].
ACCESSION   WP_005826471
VERSION     WP_005826471.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidaceae
  ORGANISM  Bacteroidaceae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Bacteroidaceae"
                     /db_xref="taxon:815"
     Protein         1..105
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11768
     Region          1..100
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(6..7,25..26,34,37,39..40,42,45..46,48,56,61)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(25,56..57,59,80)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mdkdtfqqev ynvvaaippg rvvtygqiay lvgrpqcsrm vghamhdvpd gmclpchrvv
       61 nsqgrlapcw aeqralleae gvtfrkngcv dmkkcqwefm keqiq
//
LOCUS       WP_005826785             416 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Brevibacillus].
ACCESSION   WP_005826785
VERSION     WP_005826785.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus
  ORGANISM  Brevibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 416)
  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 416)
  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   3  (residues 1 to 416)
  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   4  (residues 1 to 416)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 416)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 416)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 416)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Brevibacillus"
                     /db_xref="taxon:55080"
     Protein         1..416
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44085
     Region          63..404
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(137..139,160..161,210,262,286)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkklshisil savlatsval tgcagtsnss ggtntsgggq qsaqnqtsts gsgggatdgg
       61 vikiatqtpl sgnqsslgda iktgaeyaln lrkeefkklg fdiqlfpqdd qadpkigvsn
      121 aemlisnpdv ygvvghlnsg vaipssvkye egklvmvspa ntavklteeg kktvhricar
      181 ddaqgpkaam yakntlgvkt afiihdktay gqglsdqvkl qfekdgvqll gyegitqgek
      241 dysavlnqvt aknpdiiffg glypeggilv kqarekgykg yfmggdglds sdmikiagda
      301 vegvvftsva gdvtqteegk kwaeeykktt nkpletysvy gfdsmnviln gvmeaikang
      361 gkkptreqvl eavhktkdfq gqftkvtfde kgdnvnadvf iykydkdkst fvgkae
//
LOCUS       WP_005826917             404 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Brevibacillus].
ACCESSION   WP_005826917
VERSION     WP_005826917.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus
  ORGANISM  Brevibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 404)
  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 404)
  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   3  (residues 1 to 404)
  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   4  (residues 1 to 404)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 404)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 404)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Brevibacillus"
                     /db_xref="taxon:55080"
     Protein         1..404
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42306
     Region          50..392
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(124..126,147..148,197,249,273)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkkqkslsil aatvalgtll agcgggqssa pqsnsgggst sgggageklv iavvgpmsgq
       61 ysdygstaka gaeyalkekq eafkalgfdv qlsaqddqad pkqgvavaqm lisnpdvvgv
      121 vghattgasi taaaqydqek lvmvspsatg sdlteqgkki vhricarddq qgskaaiyak
      181 nqlgvksafi mhdkaaygqg laeevkkqfe adgvqivgfe gvtagekdys avinqivskn
      241 pemiyfggyy sdagiivkqa rekgfkgifm ggdgydsadl vkiagaenan nvvftstvgd
      301 vgateegkkw iedfekstgn kvgiftsfgy dsmgvmlngl eeaikanggk kptreqvlea
      361 vhktkdykgk fvnvtfndkg dnefasvyvy kyedgkkvyi geak
//
LOCUS       WP_005827433             503 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [Bacteroides].
ACCESSION   WP_005827433
VERSION     WP_005827433.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..503
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54804
     Region          3..503
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 meakylkinp adnvavaita lpagekltvd gkeitlnedv paghkfalkd faegenviky
       61 gypigharka qkqgdwmnen niktnlsgll eytynpvnvd lntttlnlnt gapnltfrgy
      121 krkngdvgvr neiwiiptvg cvngiinqla eglrretggk gvdaimayph nygcsqlgdd
      181 hentkkilrd mvlhpnagav lvvglgcenn qpdvfreflg dydqervkfm vtqkvgdeye
      241 egmellrely akaiqdqred iplselrvgl kcggsdgfsg itanpllgmf sdflvaqggt
      301 svltevpemf gaetilmnrc rtkelfedtv klindfkeyf lshgepvgen pspgnkaggi
      361 stledkalgc tqkcgtsyve gvlpygerlk vkglnllsap gndlvaatal ascgchmvlf
      421 ttgrgtpfgt yvptmkistn stlaknkpgw idfnagvive nepmektcer fieyiikvas
      481 gefvnnekkg ykeiaifktg vtl
//
LOCUS       WP_005829980             152 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SPOR domain-containing protein [Bacteroides].
ACCESSION   WP_005829980
VERSION     WP_005829980.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..152
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16753
     Region          66..134
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mkklglllva cfafatisva qnnivksler nvpgqgkvti hqdariaali gseyvpagsd
       61 eqkvikssgy riqvyagnnt rqakneayav atrikehfpe ltvytsfnpp rwlcragdfr
      121 sieeadammr qlratgvfke vsivkeqini pl
//
LOCUS       WP_005827528             196 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Bacillota].
ACCESSION   WP_005827528
VERSION     WP_005827528.1
KEYWORDS    RefSeq.
SOURCE      Bacillota (firmicutes)
  ORGANISM  Bacillota
            Bacteria; Bacillati.
REFERENCE   1  (residues 1 to 196)
  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 196)
  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   3  (residues 1 to 196)
  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   4  (residues 1 to 196)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 196)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Bacillota"
                     /db_xref="taxon:1239"
     Protein         1..196
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21812
     Region          1..192
                     /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"
ORIGIN      
        1 mtqpkimvvd depiirmdlr emlenegyqv vaeakngeea velahrhkpd liimdvkmpg
       61 lngikasgii rsfsdcsill ltaysqkelv idarkagvta ylvkpvsedd lipaveials
      121 qkekvvslkk disdlkqkie drkcvekakg klmsalslee eaaykwmqqv smqrrmplvk
      181 laeeilagee tlfsqg
//
LOCUS       WP_005830979             159 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Bacteroides].
ACCESSION   WP_005830979
VERSION     WP_005830979.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..159
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17470
     Region          1..153
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdafvdtlvq llidwgyvgl fisallagsi ipfsseivmv alvkvglspa lcvlsatlgn
       61 tlggmtcyym grlgridwie kyfkvkreki ermqhflqgk galmaffafl pfvgeaiaia
      121 lgfmrsnlml tttsmfagkl vryiamlwal qgaismmny
//
LOCUS       WP_005831436             281 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Bacteroidaceae].
ACCESSION   WP_005831436
VERSION     WP_005831436.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidaceae
  ORGANISM  Bacteroidaceae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Bacteroidaceae"
                     /db_xref="taxon:815"
     Protein         1..281
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32352
     Region          5..108
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          <75..250
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mekiqviqpt kllapyikqy wflriddvkq gfqrsipagc valvfhkgnk iissfhkgtq
       61 pqsyisgqis tysdiefsfl dmviilfqpi gcrmffpypm eeftnqnigi dlldntclve
      121 leekineasd nyqivrliee yllnrlceni scnanrmmat ihninegegn isvlsqtacl
      181 gykqfkrifa eyvglnpkdf iqitrfrktf hilqstpqis iskvaydcgy ydkshlikef
      241 kmftgytptq lldicdtyte nlsvfnsvfi ndnkklnnia l
//
LOCUS       WP_005831908             244 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Brevibacillus agri].
ACCESSION   WP_005831908
VERSION     WP_005831908.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus agri
  ORGANISM  Brevibacillus agri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 244)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Brevibacillus agri"
                     /db_xref="taxon:51101"
     Protein         1..244
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=26792
     Region          11..232
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mtdsiqpqah ysvfqplvel angkcfgyea llscssgasp erlfqtarqs grlyeldtta
       61 mrgavfayfa evsqaqhapy lflnvfpstl lhpgfcalle emlaahpacc qrivleinea
      121 teedkmwdir llgqkirdlr aygylialdd vgsgaaslrk iveyepdivk ldryfgnqla
      181 lspnkqklvs lfvdfcrgqs hlvlegleep ddlataktlg vplgqgfllg rpralceavy
      241 lggv
//
LOCUS       WP_005832122             394 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Brevibacillus].
ACCESSION   WP_005832122
VERSION     WP_005832122.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus
  ORGANISM  Brevibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
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
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 394)
  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   5  (residues 1 to 394)
  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   6  (residues 1 to 394)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 394)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 394)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Brevibacillus"
                     /db_xref="taxon:55080"
     Protein         1..394
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42962
     Region          15..59
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          80..382
                     /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 mkkivkqdqd vikqhnklmi ldiiknkrpi sraeitkitr msatsigrfv selceegvir
       61 eteltssgvg rkaimldiep galytigvdi ekkrisfgim dfsetivahh rvehkalagt
      121 paetaalicq eirgmiarqg ipfekvigig igvpgvinye rgvvqlsstl gwkdvafael
      181 iekelgiktv idndlkvkil seylygsakg snktaligig tgigsaliin gevfrggsns
      241 agelghttld pngnlcecgk rgclqtyide nalilearrv kevtdvrevf aaarngerwa
      301 keivsrtaly igitinnivc mynpdtvils gdlvenyrei velveehsdq viwepfkgkf
      361 rvipselrge aivmgagala mqhfaplsgs wsge
//
LOCUS       WP_005832214             273 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Brevibacillus].
ACCESSION   WP_005832214
VERSION     WP_005832214.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus
  ORGANISM  Brevibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Brevibacillus"
                     /db_xref="taxon:55080"
     Protein         1..273
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30295
     Region          1..243
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mmdlhmhtta sdgklapadl lvwakqrgvt hlaitdhdtv dgyllareda arlglallpg
       61 iewntdgped elhilgygfd madprllhvm drrqreriew iaemiercnr lgvaitmeec
      121 aarakggvmv rthvaeaiae rgysptpqaa fetylrkgca ayvprpsfsa reaielthev
      181 ggiavlahpg iysfevklea llaygldgie vyypkhsaaq tafwerqaka nhlicsggsd
      241 fhghqsrnpy pvgsvpipae vkewwkccmf hqh
//
LOCUS       WP_005838654             276 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Phocaeicola].
ACCESSION   WP_005838654
VERSION     WP_005838654.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola
  ORGANISM  Phocaeicola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 276)
  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 276)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 276)
  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   4  (residues 1 to 276)
  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 276)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Phocaeicola"
                     /db_xref="taxon:909656"
     Protein         1..276
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32217
     Region          23..276
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          196..275
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 meilhttnee pfvsgtghfa gwenrlmkle dtailfcreg hahimidlqe yelapntqvv
       61 llpdtivkft nispdftisy iafsrilfqe vtarldlsff rflkenpcvt lpeertrsin
      121 glasgiedly hdrdncfrqq ilknyiqsfl ldiydkthrl flmkrpegis rqeelfkrfi
      181 qlvhkhcttq revsfyankl fitprylstv iqnvtnttak siidkhvile ikvllkstnl
      241 svqeisnqlc fpdqsffgry fkkhtglspl qyrnqn
//
LOCUS       WP_005836462             403 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: exonuclease SbcCD subunit D [Bacteroides].
ACCESSION   WP_005836462
VERSION     WP_005836462.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            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="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=45432
     Region          1..281
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          279..376
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkilhtsdwh lghtlynydr taeqqsflrq ltrivteeqp damvvsgdiy hysspaaatq
       61 kmytdamlni hqacpgmaiv vtagnhdsss kleidsslwq hfglnvvgni ertaeevnld
      121 khiieinnek ktigyviavp hvypqnfpll dtetprdqrq arffqallde vkkrntaqlp
      181 vvlmahlsie gsdrsghdes iggieyvpls amgegydyla lghihcpqdi kgshhharyc
      241 gtplpvsfde typhsvsiie lekgaepqis treienpipl vtlphdptpf edalklleey
      301 peekpaylrl nvltkgylpp dcnekasnaa kgkackycyi kttrerqadt deskpisiqe
      361 mqemspleia rlyyretege emdpelcqlm etvmqkvksk nns
//
LOCUS       WP_005839105             189 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Mitsuokella multacida].
ACCESSION   WP_005839105
VERSION     WP_005839105.1
KEYWORDS    RefSeq.
SOURCE      Mitsuokella multacida
  ORGANISM  Mitsuokella multacida
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Mitsuokella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF004685.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK06029
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Mitsuokella multacida"
                     /db_xref="taxon:52226"
     Protein         1..189
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20497
     Region          1..183
                     /region_name="VdcB"
                     /note="non-oxidative hydroxyarylic acid decarboxylases
                     subunit B; NF041206"
                     /db_xref="CDD:469110"
ORIGIN      
        1 mivgisgasg vimgwyllra lhempeveth liitegaavt fpyetelsla evcaladvvh
       61 dnhdmaasis sgsyetdgmi iipcsmktva givsgytddl llraadvclk egrkvvivpr
      121 empmsrihlr nikeaadygc cvvppvltfy ngadtvekqi qhiigkvlmq fhlhsrdfvp
      181 wqgsdaagr
//
LOCUS       WP_005839500             195 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Mitsuokella multacida].
ACCESSION   WP_005839500
VERSION     WP_005839500.1
KEYWORDS    RefSeq.
SOURCE      Mitsuokella multacida
  ORGANISM  Mitsuokella multacida
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Mitsuokella.
REFERENCE   1  (residues 1 to 195)
  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 195)
  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   3  (residues 1 to 195)
  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   4  (residues 1 to 195)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 195)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Mitsuokella multacida"
                     /db_xref="taxon:52226"
     Protein         1..195
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21749
     Region          6..193
                     /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"
ORIGIN      
        1 mahetlrivi adnesiirmd lremleeagh eivgeaidgr kaveltrqhr pdlvimdikm
       61 pqmdgitaar kiseeklapv llltafsqpe ivekakdsgv lgylvkpvqe tnlfpaieia
      121 msrwremqgl eqelaglrds lamrktldra kgilmaahhl sepeayrriq qyammkrltv
      181 kevaeaivka aggkv
//
LOCUS       WP_005839505             234 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Phocaeicola vulgatus].
ACCESSION   WP_005839505
VERSION     WP_005839505.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 234)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..234
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=27998
     Region          153..232
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mdsqeytihp hdvfvfmpgl lvsvietsph fttnyftlsn tffydvikti rsfspqffsy
       61 mksrflyplp eqemqyfmny ytllksrikl pksfsreaii allriifldl yndfenyinh
      121 rnntsttrke dlthrfytlm mdnyrehkev ifyadklhvs skylsevvke tsgkspkdwi
      181 idyslleike llknsslniq eitirtkfln qsalgrffkr htnmspseyr esty
//
LOCUS       WP_005840806             152 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SPOR domain-containing protein [Phocaeicola].
ACCESSION   WP_005840806
VERSION     WP_005840806.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola
  ORGANISM  Phocaeicola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Phocaeicola"
                     /db_xref="taxon:909656"
     Protein         1..152
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16936
     Region          65..133
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mryifillfl slglsalaqq niveslqrnr agegtvtirq dpkitgligs iytgnvtgge
       61 qkmlkargyr vqvyagnnsr varneannva akvkeefpdm pvyayfqppr wlcrvgdfrs
      121 ieeadaamrr lkatgvfkev sivreqinip ld
//
LOCUS       WP_005843961             158 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Prevotella dentalis].
ACCESSION   WP_005843961
VERSION     WP_005843961.1
KEYWORDS    RefSeq.
SOURCE      Prevotella dentalis
  ORGANISM  Prevotella dentalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 158)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Prevotella dentalis"
                     /db_xref="taxon:52227"
     Protein         1..158
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16920
     Region          2..155
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mtdkagayal llkqlaelvr getnetsvla nvaaaihqas drffwtgfym qqesgqplrl
       61 gpfqgppacy aipvgrgvcg tafaerrtlv vpdvelfpgh iacsslsrse ivvpvfrpgg
      121 epvgvldids rtpcafdetd trcleeamrl maaeiyag
//
LOCUS       WP_005846483             151 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Prevotellaceae].
ACCESSION   WP_005846483
VERSION     WP_005846483.1
KEYWORDS    RefSeq.
SOURCE      Prevotellaceae
  ORGANISM  Prevotellaceae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Prevotellaceae"
                     /db_xref="taxon:171552"
     Protein         1..151
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16300
     Region          2..151
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdaitdllin ygywgmllaa ffagsflpfs seavmlglla agldatmlvv ygtignvlgs
       61 llnygvgrmg klewigrylh vsqqsldras rfmaghgawm gffaflpilg saititlglm
      121 ranlfislvs mtlgkifryy vllygaslfm g
//
LOCUS       WP_005846355             286 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Prevotella dentalis].
ACCESSION   WP_005846355
VERSION     WP_005846355.1
KEYWORDS    RefSeq.
SOURCE      Prevotella dentalis
  ORGANISM  Prevotella dentalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 286)
  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 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   3  (residues 1 to 286)
  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   4  (residues 1 to 286)
  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 286)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Prevotella dentalis"
                     /db_xref="taxon:52227"
     Protein         1..286
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33651
     Region          49..283
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <173..281
                     /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 mnhydisqlq ittlntgyae hhsdwnwqnv rspfarlyyv tegeawvkme nrrihlqpdh
       61 iymippftvh snictgrfch yyihiyeapv dfsfleqlsy pheaagtshd relfcrlmel
      121 npsmqlpesn pqsydnsttl lrniaknkqr qfcdivesrg ilfillarfl kgarpkqdik
      181 derissvvgh irrhitepmd iptlarrafm sedhfirmfr kelgetpnsy virlkmerae
      241 lllvttrqpi kniaallgyd evpyfnrifk kkvgktpkey rmgkte
//
LOCUS       WP_005847158             250 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-deoxy-manno-octulosonate cytidylyltransferase
            [Phocaeicola].
ACCESSION   WP_005847158
VERSION     WP_005847158.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola
  ORGANISM  Phocaeicola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 250)
  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 250)
  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 10118537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Phocaeicola"
                     /db_xref="taxon:909656"
     Protein         1..250
                     /product="3-deoxy-manno-octulosonate cytidylyltransferase"
                     /EC_number="2.7.7.38"
                     /GO_function="GO:0008690 - 3-deoxy-manno-octulosonate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0033468 -
                     CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28711
     Region          2..238
                     /region_name="CMP-KDO-Synthetase"
                     /note="CMP-KDO synthetase catalyzes the activation of KDO
                     which is an essential component of the lipopolysaccharide;
                     cd02517"
                     /db_xref="CDD:133010"
     Site            order(8..10,49,76,96,98)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133010"
     Site            order(122,139,145..147,153..154,156..162,170,195..196,
                     199..201,208..211)
                     /site_type="active"
                     /note="oligomer interface [active]"
                     /db_xref="CDD:133010"
ORIGIN      
        1 mkviavipar ykstrfegkp lvnlcgkpmi wwvhhqlcqv kglseiyvat dderirkvcs
       61 dygikyvmts dshpthldrl aefaeniesd fyiningdep lmmpeyverl lptsdlnpvd
      121 fyfanamtki kktvevadis rikvvtdnlg yamymartpi pypkassdfd ymkfvgiqcf
      181 srsallfckd nkrgkiesie dideyrflen gkkikfveip aetlsvdtqa dvkivtevle
      241 rriknkeivl
//
LOCUS       WP_005846760             498 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Prevotella dentalis].
ACCESSION   WP_005846760
VERSION     WP_005846760.1
KEYWORDS    RefSeq.
SOURCE      Prevotella dentalis
  ORGANISM  Prevotella dentalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Prevotella dentalis"
                     /db_xref="taxon:52227"
     Protein         1..498
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54836
     Region          5..498
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mnestfikin padnvvvclr pvrqgetldv dgrrvevlqd tpaghkvlla dvkagtdiik
       61 ygypighare dlrrgqwvne tnlktnlsgt ldyeyrpvne elriphedlc fkgyrrssge
      121 vgvrneiwiv ptvgcvngia erlvrrltae trlegidavh awhhnygcsq lsgdhentrk
      181 vlrdiclhpn aggvlvlslg cennqpdqfm ellgnydrdr vkllvtqkvd gdeteaamql
      241 lrelyararq drredvplse lrvglkcggs dgfsgitanp lvgefsdylv aqggttilte
      301 vpemfgaeti lmnrcktpel frqtvelvnd fkeyflshge pvgenpspgn kaggistled
      361 kalgctqkcg raqvsgvlgy gdrlqhhgln llsapgndlv astalaaagc qlvlfttgrg
      421 tpfgtfvptm kistnndlya rkpnwidfna gqllrgmpma elnrrfiqkv iavasgektr
      481 neeneyseia ifkngvtl
//
LOCUS       WP_005847719             308 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Prevotella dentalis].
ACCESSION   WP_005847719
VERSION     WP_005847719.1
KEYWORDS    RefSeq.
SOURCE      Prevotella dentalis
  ORGANISM  Prevotella dentalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 308)
  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 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   3  (residues 1 to 308)
  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   4  (residues 1 to 308)
  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 308)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Prevotella dentalis"
                     /db_xref="taxon:52227"
     Protein         1..308
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34420
     Region          46..306
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          226..305
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mkekelrrls llqmrsllle aadtadadln qeihayvnrh vavakhmits vtrhltdhps
       61 lleemrvvlv rqghahpvin llpvdlqagd lfflgrnsta hvrglsddva gegvvmsdev
      121 fglalgnaip paldghlrsf rlslsaaeqa cfsqfvslly dtlqqddcsp qvflgmasaf
      181 wwyvdslyqr hapgdqaaqs reqqlfarfi alvnayarre htldfyasrl clsprymstl
      241 vrqvsgrgak awideallta ikvdlrhtsk plkqiadelc fpgmsffgkf fkrmtgqtpm
      301 ayrrsaeg
//
LOCUS       WP_005848342             605 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Phocaeicola vulgatus].
ACCESSION   WP_005848342
VERSION     WP_005848342.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 605)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..605
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=70353
     Region          25..314
                     /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          213..241
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          247..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(248,251..252,255..256,258,287,290..291,294..295,
                     297..298,321,324..325,334..335,338)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          285..315
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          320..350
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          <490..599
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtgmkmfklw mvvmllgllp vvseaqedin nainvqleyl kkypkdkdal rkvsflylnk
       61 adydqaifyg rqlfemgyne rdyngaviys hiclgqahmm kgnvkeaysh lgqarliges
      121 nkndsalcsv ynglglyasn vqkdyyrslt yffkgveaar cchydrlysi llsniagiyy
      181 lkndstglky alecyelghe rkdpyliysg stntaymyyl ksdyntalky iqeaeftmvq
      241 ndfydqsnvy nlygyilhkl nkddealgff rkaldlkeqg nissvmnsyl gyaeilmehh
      301 qydravrmlk agielsyqqa naiyrsdllk alsrcyeedg mlvealkyhk lyqletdsly
      361 naekeravge irakydmerq eneikqnrle llekenkmql liagficifi aasllyylyy
      421 rknklyltiv kqnqdairre qqlqnkideq faeigrqsal lqeyltdstk tslpqpekya
      481 sssltdekkq dlflrletll weekvftdnl ltkekvaeml gtnrtylsqi ineqtkqtft
      541 qfvngfrtke avrllsdpdn qtplkaisae lgfnsmttfy sqfqaatgmt paqyrnkvqe
      601 lhknr
//
LOCUS       WP_005849730             173 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Sulfitobacter].
ACCESSION   WP_005849730
VERSION     WP_005849730.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter
  ORGANISM  Sulfitobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 173)
  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 173)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 173)
  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   4  (residues 1 to 173)
  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   5  (residues 1 to 173)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Sulfitobacter"
                     /db_xref="taxon:60136"
     Protein         1..173
                     /product="TRAP transporter small permease subunit"
                     /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=19906
     Region          3..171
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mnamrryirv vdgfnyglgr immygifvlm gillwssynk tfaspqiwtl emaqfvmvgy
       61 yilggpyalq mganvrmdlf yaeltprkka wtdcitvffl liylvillwg giestmysfk
      121 yggersptaw rpymwpvkvt mcigitlmll qavselfkdi lflksaeetr dal
//
LOCUS       WP_005850265             314 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Sulfitobacter].
ACCESSION   WP_005850265
VERSION     WP_005850265.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter
  ORGANISM  Sulfitobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Sulfitobacter"
                     /db_xref="taxon:60136"
     Protein         1..314
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31490
     Region          5..213
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mlflaglmgl itvgaaafid igvededsat dedapagdvi sgtprddlii gsggsdqiag
       61 yggddlvgar ngddtvfgds gddtlrggag nddlhgndgd dllagaedad gltghndddi
      121 lqggaghdtl ngsaggdtlf gdsgddavmg glgddlligg rgqdalfggw gndtidgtvd
      181 pdrqdarvtd idegdylngg sgddvilags ndtvtpgagr ddvilgdwvs pdgivdirsf
      241 dieddslllv wddsdaaaia pkvavepdpe dlhshlismd gaivamvqsd qllmpgdlsl
      301 iplssalaag ltrg
//
LOCUS       WP_005850485             251 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: hydroxypyruvate isomerase family protein
            [Sulfitobacter].
ACCESSION   WP_005850485
VERSION     WP_005850485.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter
  ORGANISM  Sulfitobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 251)
  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 251)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Sulfitobacter"
                     /db_xref="taxon:60136"
     Protein         1..251
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27125
     Region          4..248
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mkpaanltll wselpyldrf avaakagfta vevlfpydla aketlracva nglqlilina
       61 pppnytggaq gfaavpelaa rfrvdiqrsf ryatalkvry lhvmagngqg alarqtfidn
      121 liwaadiapk gltltvepln pvampgyfmn dyalaadvlr avnrpnvglq ydsyhaqmih
      181 gdavavfeqy kdlivhvqlg dapdrsapga gtvdfpalfa alrragyrgw vsgeyipgpr
      241 tedslgwmtl s
//
LOCUS       WP_005850641             283 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Sulfitobacter].
ACCESSION   WP_005850641
VERSION     WP_005850641.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter
  ORGANISM  Sulfitobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Sulfitobacter"
                     /db_xref="taxon:60136"
     Protein         1..283
                     /product="formate/nitrite transporter family protein"
                     /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=31058
     Region          28..281
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mapliqrrvs rkkpqdaqae eksvseatal spkliyevir regeeelsrs krsliwsgia
       61 agvmislsvl geavfrtylp dtahrflien lgyslgflav imgrmqlfte ntittvlpim
      121 raktwhslmc mfrlwgivla anvvgafaaa mlflwtpais pevlpaildl shhatsmgay
      181 qgfwraipag vivalivwmm pqadetsffl ilvftwliaa gdfahivags vemavmildg
      241 qlglmaavfe fflpvlagni vggtiiftlv awgqvrdeve eek
//
LOCUS       WP_005850976             401 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Sulfitobacter].
ACCESSION   WP_005850976
VERSION     WP_005850976.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter
  ORGANISM  Sulfitobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
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   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 401)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Sulfitobacter"
                     /db_xref="taxon:60136"
     Protein         1..401
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45582
     Region          1..398
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mtlplignrd arriflhrhl lsdapqgpas gndllqliqg lgfvqldsin tvarahdlil
       61 fsrrqryrpq alktlyerdg alfehwthda avipmgyyph welrrqrdaq mlrqryknwh
      121 qhdfegrfqt vldqiraqgp vsssdvgqde prsnggwwdw hpsktaleyl wragalcvvg
      181 rdgfqkrydl tervidaalc dpsqapdeaq tidwccngal drlgfatpge laafwahisp
      241 aeakawvqre qaagrveqvq iagadgtvhr sfarpglasd pardmaptar lrvlspfdpa
      301 lrdrkraerl fgfryriemf vpapkrvygy yvfpilqgds iiarvdmkah rdrdtlvvra
      361 lwpepgsrwg kgkqaafeae lariirlagv sqiafedgwl r
//
LOCUS       WP_005850986             456 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Sulfitobacter].
ACCESSION   WP_005850986
VERSION     WP_005850986.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter
  ORGANISM  Sulfitobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 456)
  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 456)
  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 456)
  AUTHORS   ter Beek,J., 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 456)
  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 456)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Sulfitobacter"
                     /db_xref="taxon:60136"
     Protein         1..456
                     /product="CmpA/NrtA family 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=49931
     Region          25..303
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mkntfallla stsllataas aemlalekee ltfgfikltd maplavayel gyfedeglfv
       61 rleaqanwkv lldgvidgql dgahmlagqp laatigygtk ahiitpfsmd lngnaitvsn
      121 diwdemkpnv ptmddgrpqh pisasalapv vegykdrgep fnmgmvfpvs thnyeirywl
      181 aagglkpgyy saqdisgqid advllsvtpp pqmpatmeag tisgyavgep wnqqavfkgi
      241 gvpvitdydm wknnpekvfg itaefaednp nttlaltkal iraamwldan dnanreeave
      301 mlsrseyvga dadviansmt gffefekgdv rpapdfnvff rynatypfys daiwyltqmr
      361 rwgqidetkp dewyfetaad vyrpdiylqa arllvdegma deaafpwdsd gfksptpaad
      421 iidgisydgr apnayidslp iglksgqtvv dskveg
//
LOCUS       WP_005851321             401 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Phocaeicola].
ACCESSION   WP_005851321
VERSION     WP_005851321.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola
  ORGANISM  Phocaeicola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
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
REFERENCE   3  (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   4  (residues 1 to 401)
  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   5  (residues 1 to 401)
  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   6  (residues 1 to 401)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 401)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 401)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Phocaeicola"
                     /db_xref="taxon:909656"
     Protein         1..401
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44452
     Region          19..61
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          81..394
                     /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 mgenllkeie kgskmavmkk kiithyiyng sstitdlare mdlsvptvtk fidemceegy
       61 indygklets ggrhpslygl nadsgyfvgv evrqfsinlg linfkgdvvq lkmnvpfkak
      121 ntpesldelc klikhflqkv svekdkilni nvnlsgrvnp dlgysysifn fderpltdvi
      181 sekvggyrvs idndtramiy geymqgvvkg ekniifinvs wglgmgiiid gkiykgksgf
      241 sgefghnfgy eneiichcgk kgcietevsg aalhrilleh inngensiis ntkknledlt
      301 lddiidavnk edllcielve eigvklgrhv aglinifnpe lviiggalsr tgdyltqpit
      361 tairkytlnl mnrdsvives klkeragiig acmlsrsklf e
//
LOCUS       WP_005852280             222 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Sulfitobacter].
ACCESSION   WP_005852280
VERSION     WP_005852280.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter
  ORGANISM  Sulfitobacter
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Sulfitobacter"
                     /db_xref="taxon:60136"
     Protein         1..222
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=24115
     Region          1..160
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 madapdryls pnhgprrngl rpslivlhyt amdsaeaaca rlcdpaaevs ahylitgkge
       61 tvplvpedqr awhagagewq gqddinsrsi gieldnrgnh pfsepqmvtl etllrgimer
      121 wsippegvig hsdmapgrki dpgprfdwpr larqnlagkg sryaeknrgs dptpaafiaa
      181 ahaagytatd didlllhstr lryapwrkgp lcaadmslgh dl
//
LOCUS       WP_005852362             244 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Sulfitobacter].
ACCESSION   WP_005852362
VERSION     WP_005852362.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter
  ORGANISM  Sulfitobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Sulfitobacter"
                     /db_xref="taxon:60136"
     Protein         1..244
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24729
     Region          17..219
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mspllvmlfa afgpmlavfd pfgddtedep edeeipigtp dmgtttgagm ddaltpdpad
       61 peadaptdvp taedpaveti ddtaqppede aqsqtgtagd dtlqgtdgrd ilfggqgndt
      121 lsggvnaqdg sddgvadeli gedgddslrl gandtgiggt gadsftaiyg atggitvtdy
      181 dvgtdalive tddenasvtd qtvadgeltv tlstgltitl pgienplaed eilfvltnpl
      241 qdea
//
LOCUS       WP_005853084             645 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter permease [Sulfitobacter].
ACCESSION   WP_005853084
VERSION     WP_005853084.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter
  ORGANISM  Sulfitobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 645)
  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 645)
  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 645)
  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 645)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..645
                     /organism="Sulfitobacter"
                     /db_xref="taxon:60136"
     Protein         1..645
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=68407
     Region          1..638
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 msatqhppaa etavepsset trlgglfsft siafvllctf glgmglayvf gvpiggrrli
       61 egqyywvfig tflaaafial pavkshthvp iydivaaaag fgicmwfsmy aweivqagwt
      121 nfyagvvlwl lmleiarrsg gipfllvvlv lglyplvady fpgllmgipy tfermieahv
      181 frteglmgit tkivaeivlg flvfagvlia tgagqffidl anagfgkyrg gpakvsivas
      241 affgslsgsi fsniagtgsi tiptmkkvgy pphyagaiea castggvvmp pvmgaiafvm
      301 aitigvdyat vmvaailpsa lfyfglilqv dayaarkglv gmkpenlpsa revmkrgwpf
      361 llvmiflvwg llymrweyya pwyasalmia lsflqretmm tparifetlr qvgtlvtqta
      421 aiilpiafvv saltitgvtg smtsglvalg gdnvylvial gvlacfimgm aglaivayif
      481 lavtlapaii eigglntvav hffivyyaml svitppvgaa aflaatiaga kpmltsftam
      541 rlgvviyfvp lfflfqpalv lqgdltpliy vlpsiiigit llsgglegyl lgvgmvrpwl
      601 rlplgiagfa fsfpgltttl iagvasaalv aviwrdnrng vvavp
//
LOCUS       WP_005854828              98 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein
            [Parabacteroides].
ACCESSION   WP_005854828
VERSION     WP_005854828.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..98
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10925
     Region          1..98
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mnkqsvisll rkakqplsqs cgvkqlglfg stvresntes sdvdilidfe ddketysnfl
       61 laceileklf drlkvdivtl kglspfigqq ilkeveyv
//
LOCUS       WP_005854784             523 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Sagittula stellata].
ACCESSION   WP_005854784
VERSION     WP_005854784.1
KEYWORDS    RefSeq.
SOURCE      Sagittula stellata
  ORGANISM  Sagittula stellata
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sagittula.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Sagittula stellata"
                     /db_xref="taxon:52603"
     Protein         1..523
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=53278
     Region          6..519
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mrngqvasla qalvwpvqaw llaalladlm agtgalpvwg vaggfvalgv lragleriaq
       61 aqlsalaear igaaraeivs aeaaaaapsa lggpgalaal maeklealrp ylmryrparl
      121 ratvvpllil aiavsqswav alifvmagpl ipvfmalvgw aakeasarqm veigdlsdll
      181 vdrlsaladl rligaggpvv sgfaassegl rartmavlri aflsstvlel faalgvamva
      241 vwtgfhllgv igwgtwggvl spaagiwlll lapeffqplr dlaaawhdka aaeaveaela
      301 dwraearpal mrggdagapm gpvalrgvva rgialpdiev apgesvaitg psgagkttll
      361 rvlaglerps agevrvggrp lpevidgwra glgwmpqaph fldrslrynv gfgaevpddv
      421 varaqlaevl aalprgaltv lgergaglsg gearrvtlar almagrgall adeptadldp
      481 ataeavagal lgfaqaggsl ivathdagla arldrvvtlg aat
//
LOCUS       WP_005855077             364 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Sagittula stellata].
ACCESSION   WP_005855077
VERSION     WP_005855077.1
KEYWORDS    RefSeq.
SOURCE      Sagittula stellata
  ORGANISM  Sagittula stellata
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sagittula.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Sagittula stellata"
                     /db_xref="taxon:52603"
     Protein         1..364
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37597
     Region          48..299
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mpttrddnlf gtdmadfial legndtyhgl egndtidgea gddvlwggld ddwlkggigy
       61 dlllggegnd tieggldndt mdgeagndlm lggegddwmk gedgndtmdg esgndtvegg
      121 lgddwmkgeq grdlmlggeg ndtieggldd dtmdgeagnd lmlggegddw mkgedgndtm
      181 dgesgndtve gglgddwmkg eqgrdlmlgg egndtieggl dddtmdgeag ndlmlggegd
      241 dwmkgedgnd tmdgesgndl ieggagadwl kgeggndtlf ggagddllvg gdgadvfvfa
      301 qesgfdivad fqdgidkvnl tdlwggvisi fdtaegalvs vegydvalfm diaasalgfd
      361 dlvf
//
LOCUS       WP_005855335             367 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: transcription termination/antitermination protein
            NusG [Parabacteroides].
ACCESSION   WP_005855335
VERSION     WP_005855335.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Kang,J.Y., Mooney,R.A., Nedialkov,Y., Saba,J., Mishanina,T.V.,
            Artsimovitch,I., Landick,R. and Darst,S.A.
  TITLE     Structural Basis for Transcript Elongation Control by NusG Family
            Universal Regulators
  JOURNAL   Cell 173 (7), 1650-1662 (2018)
   PUBMED   29887376
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Liu,B. and Steitz,T.A.
  TITLE     Structural insights into NusG regulating transcription elongation
  JOURNAL   Nucleic Acids Res 45 (2), 968-974 (2017)
   PUBMED   27899640
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Steiner,T., Kaiser,J.T., Marinkovic,S., Huber,R. and Wahl,M.C.
  TITLE     Crystal structures of transcription factor NusG in light of its
            nucleic acid- and protein-binding activities
  JOURNAL   EMBO J 21 (17), 4641-4653 (2002)
   PUBMED   12198166
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415705
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     gene            1..367
                     /gene="nusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
     Protein         1..367
                     /product="transcription termination/antitermination
                     protein NusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
                     /calculated_mol_wt=41879
     Region          53..195
                     /region_name="NusG"
                     /note="Transcription termination/antitermination protein
                     NusG [Transcription]; COG0250"
                     /db_xref="CDD:440020"
ORIGIN      
        1 mdiltgkcsd rfmahvlkrr dqeavrwyvl tlptagggrd rispskglda elsrrerrge
       61 alfeyfspsy vearkvggkm vntkrpllyn yvfvhasede ifrlkrtlpl ynflprvssg
      121 grsyfpylsd remdtlrwva asysnelpvy vpdsgrllkg drvritsgpf tdmeaevvvq
      181 pggghkdvmv rildcmwvpl fevrrgeyel ielntggkhv ythldndrls eglhdalgry
      241 hargvvtded arlarevlrg yaslrgetdv ircklyslll paylllgesd efdrlhatmr
      301 smlpvikagq sralllvtly gctdsslyqr mahegvdpwl depspkksks vlirrlrdyd
      361 gwlkhne
//
LOCUS       WP_005855753              97 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein
            [Parabacteroides].
ACCESSION   WP_005855753
VERSION     WP_005855753.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..97
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11170
     Region          3..97
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mksrqeilal lrdfkvrkgk kygilkmgif gsvardqqte ssdvdiyyeg eaqglfslsh
       61 lkneleellg spvdiirlrd rmnqllrkri eregiyv
//
LOCUS       WP_005855773             702 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Sagittula stellata].
ACCESSION   WP_005855773
VERSION     WP_005855773.1
KEYWORDS    RefSeq.
SOURCE      Sagittula stellata
  ORGANISM  Sagittula stellata
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sagittula.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 702)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 702)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Sagittula stellata"
                     /db_xref="taxon:52603"
     Protein         1..702
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76517
     Region          457..>640
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 msatgrfvqs dhfganalql vnvdahghlg ptdgfqsaaq tlglnhfryp gggtenvidi
       61 trlengqire evrrfldwvr dsgtadepgk vtivlptktd lpaqqvedfv ylllreygpl
      121 iealeigney sigrydpnyd rsthpeenpn gdfvssmtea eygvaanrvi nasldamdry
      181 sagttgtahd pkillqigdi qgaastykgs gsfdmaneai vsflnarara avdggvahyy
      241 ynqsheddqs fthewyehrs ldwrienfsn wlghdvelyv tewnvlasny nqlgaasagi
      301 lleqfefmvq agvqdafvwp lqhrtgsnia gnrqvddidl tiggtafqmm aeslkpqtsq
      361 tgsvtafesi asdstgsndn vevnlfssay qdvifmtlrd lnratvnldi spflnadstv
      421 evthvtidrs tsdglsdmad edglnrigrr iidqeeadql atlaffdptd anhirdlgdg
      481 ryqtylptys sivpltanpt glddyyfate tdvdalvttl sgdylstgiv rvglmpydfv
      541 rvvidktash dggsgndhqv ggtgrdsmlg rlgndtmfgg egndtlkggh gddrlyggdg
      601 ndyivdgygn dliygqegdd efvlvagqdr vfggdgndsv svawakhdvs fqhldggltl
      661 vtpdgrvdmr evetveladd tvatddihvf vmdappnfdd ml
//
LOCUS       WP_005856023              89 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: zinc ribbon domain-containing protein
            [Bacteroidales].
ACCESSION   WP_005856023
VERSION     WP_005856023.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidales
  ORGANISM  Bacteroidales
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia.
REFERENCE   1  (residues 1 to 89)
  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 10577258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Bacteroidales"
                     /db_xref="taxon:171549"
     Protein         1..89
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10463
     Region          3..86
                     /region_name="Zn_ribbon_2"
                     /note="Putative zinc ribbon domain; pfam12674"
                     /db_xref="CDD:463667"
ORIGIN      
        1 mkfcqscgmp ltddykgtna dgsrnedycn ycymdgrfmq dmtmeqmidh caqftdeink
       61 qsgqnmtveq akemmrqfyp nlkrwknkp
//
LOCUS       WP_005856247             227 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Sagittula stellata].
ACCESSION   WP_005856247
VERSION     WP_005856247.1
KEYWORDS    RefSeq.
SOURCE      Sagittula stellata
  ORGANISM  Sagittula stellata
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sagittula.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Sagittula stellata"
                     /db_xref="taxon:52603"
     Protein         1..227
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=25314
     Region          1..152
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mteepvwhps pnvgdrrdca apdmivlhyt amktaeaard rlcdpaaqvs ahyvvaedgr
       61 twqlvrethr awhagagawg pvrdvnshsi gieiantgaa pfperqmvvv enllrrvmar
      121 wriapervvg hsdtapgrki dpgprfdwrr lalqgvavwp ddtgdpgqfl hdarrfgydv
      181 davgedvvln afrmrfrpga kgplededrr lmhdlanrwp vaqvalv
//
LOCUS       WP_005856409             496 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase, partial [Sagittula stellata].
ACCESSION   WP_005856409
VERSION     WP_005856409.1
KEYWORDS    RefSeq.
SOURCE      Sagittula stellata
  ORGANISM  Sagittula stellata
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sagittula.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Sagittula stellata"
                     /db_xref="taxon:52603"
     Protein         1..>496
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
     Region          1..496
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mttvrlsead nvvtavtale agqhgatqli prghklatra iakgapviky aqvigyaaed
       61 iaegahvhth nldfrnvdte yeyatnirpa peattqdtfm gyrrasgrvg trnfiavlts
      121 vncsataarq iaahftperl tdypnvdgva afvhgtgcgm agqgsegfea lqrvmwgyak
      181 npnvggvlma glgcemnqid wlveaygltp gplfqsmniq dvgglrktve lgirkieaml
      241 pivnearree cpaselmval qcggsdawsg itanpavgha cdllvaqggt gvlaetpeiy
      301 gaehlltara vdrevgeklv glirwwedyt arnkgsmdnn pspgnkkggl ttilekslga
      361 aakggttplt gvykyaepvt akgftfmdsp gydpasvtgq iasgcnlvcf ttgrgsafga
      421 kpspsmkvat ntemfdrlte dmdinagsil sdgksveevg reiyemwlrm asgektksel
      481 qglgdfefvp wqigav
//
LOCUS       WP_005856406             269 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Sagittula stellata].
ACCESSION   WP_005856406
VERSION     WP_005856406.1
KEYWORDS    RefSeq.
SOURCE      Sagittula stellata
  ORGANISM  Sagittula stellata
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sagittula.
REFERENCE   1  (residues 1 to 269)
  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 269)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 269)
  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   4  (residues 1 to 269)
  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   5  (residues 1 to 269)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Sagittula stellata"
                     /db_xref="taxon:52603"
     Protein         1..269
                     /product="TRAP transporter small permease subunit"
                     /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=29913
     Region          91..252
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mngesvwlgs mrgpirlamf ifiglslaiy awfliaqytt adpigmhemi rpggrplvqa
       61 llisialall fsslylsdfk gvievertgp fdifslvlgr lsmiatafiv vtmgfevvar
      121 yifnggtlwa nelslwiaaf vflmaglyam qqrshiriyv iydmmprwmq kasdcvsvfl
      181 iwvfvgcliw ggyndatrrl mnlegygsaw dppipgtvkt avlviglava lqalsnliad
      241 wnkapehhsa ddideheien irktlegdk
//
LOCUS       WP_005856425             347 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Parabacteroides].
ACCESSION   WP_005856425
VERSION     WP_005856425.1
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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..347
                     /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=40984
     Region          5..281
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mndlrisyid qlkgiaillv vlghvigynn cedsflwrfi ysfhmplfmf isgyvaqmtf
       61 rierfgwnet isflikklrt lllpmvtwgv vipffflrtm idqsfidcvl nfvktwgggl
      121 wffatlfils ilffvyrwvd kqinaksifv dlvillflfi lvillymlly kdaiysegir
      181 svfnyfmfyf lgsivckqtn lrslilnnkk fftfsfvmff llipsfvydm ssmfnqlmki
      241 vlslfaifsl ffivhhiswn rqvdnmfqyf greslsiyvt hngpfafllv itdyitlssv
      301 dnipcflflf ifslfisyas iwiknivsis pilelflygk sykrksi
//
LOCUS       WP_005856717             198 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Sagittula stellata].
ACCESSION   WP_005856717
VERSION     WP_005856717.1
KEYWORDS    RefSeq.
SOURCE      Sagittula stellata
  ORGANISM  Sagittula stellata
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sagittula.
REFERENCE   1  (residues 1 to 198)
  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 198)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 198)
  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   4  (residues 1 to 198)
  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   5  (residues 1 to 198)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Sagittula stellata"
                     /db_xref="taxon:52603"
     Protein         1..198
                     /product="TRAP transporter small permease subunit"
                     /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=21945
     Region          5..197
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mprvligfvr aveamnraig rvamylifal igvllwssvs kvaflpslwt letaqfvmva
       61 yyilggpysi qlgsnvrmdl fygnwsvtqk awvdaftvlf lmfylgvlly galgslaysm
      121 gyfgmqpley faeffgalft ggidgaagki gflersstaw rpmlwpiklv lafgiflmil
      181 qtlaelikdi grirgvei
//
LOCUS       WP_005856762             158 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Parabacteroides].
ACCESSION   WP_005856762
VERSION     WP_005856762.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 158)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..158
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17366
     Region          8..155
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 maeelrikng dkqemyetll pqiaslvgne tdlianmani aaalkqtfgf fwvgfyrvid
       61 nqlvlapfqg piactrikyg kgvcgtawke artiivpdvd afpghiacss asrseivvpv
      121 iwadkviavl didsdqpdsf detdqiflek ivellphq
//
LOCUS       WP_005856801             129 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Parabacteroides].
ACCESSION   WP_005856801
VERSION     WP_005856801.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (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   2  (residues 1 to 129)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..129
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15227
     Region          38..118
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 meekqkpsli errlyarilq imedkkpyld pqfnlcqlan lactnrtrls stlnnqtgmn
       61 fsrwlanyrv khliqefskc ltqepkelyk kagftsrtsf yrqfkevtgn tpieyfanly
      121 ydnvnhstk
//
LOCUS       WP_005857101             454 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Sagittula stellata].
ACCESSION   WP_005857101
VERSION     WP_005857101.1
KEYWORDS    RefSeq.
SOURCE      Sagittula stellata
  ORGANISM  Sagittula stellata
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sagittula.
REFERENCE   1  (residues 1 to 454)
  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 454)
  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 454)
  AUTHORS   ter Beek,J., 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 454)
  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 454)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Sagittula stellata"
                     /db_xref="taxon:52603"
     Protein         1..454
                     /product="CmpA/NrtA family 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=49542
     Region          25..301
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mktflaalaa stalvspala eldlekdelt fgfikltdma plavayeqgy fldeglfvtl
       61 eaqanwkvll dgviggqldg ahmlagqpla atigygteah iitpfsmdln gngitvsnav
      121 weemkpnipt nadglpqhpi sasalapvve kyksegkpfn mgmvfpvsth nyelrywlaa
      181 gglhpgyysp enitgqigad vllsvtpppq mpatleagti ygycvgepwn qaavfkgigv
      241 pvitdyelwk nnpekvfgit aefaeenpnt tlavvkalir aamwldendn anrmeaveil
      301 sqpeyvgada eviansmtgt feyekgdkre vpdfnvffry natypyysda vwyltqmrrw
      361 gqiaeaqpds wydevaksvy kpeiyleaar llvdeglane adfpwdtdgy keptpaedii
      421 dgiaydgkap nayleslpig lkgeqtvvgt evkg
//
LOCUS       WP_005857181             277 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Parabacteroides].
ACCESSION   WP_005857181
VERSION     WP_005857181.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
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   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 12122938
            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="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32665
     Region          196..273
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mnpfeierge sfiigdsdlr elldrpyksg ygmilfcykg tanisvdlsr wdirrntviv
       61 lipdtiltln assedfkvqy isfskvlfde avfrldppff rfikdspcyt hpadqeetin
      121 viirlfwliy mdrnnvyrdm ivknqlqcff lnmydktrys fssrqqngcn rgeelfhkfi
      181 ncihahyldq kevsfyanel cisprylsti trqvagesak tiidrhiile tkvllrttem
      241 tvqeitnhln fpsqsylgry fkkhtgespi eyrmkrk
//
LOCUS       WP_005857354             368 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: transcription termination/antitermination protein
            NusG [Parabacteroides].
ACCESSION   WP_005857354
VERSION     WP_005857354.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Kang,J.Y., Mooney,R.A., Nedialkov,Y., Saba,J., Mishanina,T.V.,
            Artsimovitch,I., Landick,R. and Darst,S.A.
  TITLE     Structural Basis for Transcript Elongation Control by NusG Family
            Universal Regulators
  JOURNAL   Cell 173 (7), 1650-1662 (2018)
   PUBMED   29887376
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Liu,B. and Steitz,T.A.
  TITLE     Structural insights into NusG regulating transcription elongation
  JOURNAL   Nucleic Acids Res 45 (2), 968-974 (2017)
   PUBMED   27899640
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Steiner,T., Kaiser,J.T., Marinkovic,S., Huber,R. and Wahl,M.C.
  TITLE     Crystal structures of transcription factor NusG in light of its
            nucleic acid- and protein-binding activities
  JOURNAL   EMBO J 21 (17), 4641-4653 (2002)
   PUBMED   12198166
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415705
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     gene            1..368
                     /gene="nusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
     Protein         1..368
                     /product="transcription termination/antitermination
                     protein NusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
                     /calculated_mol_wt=41777
     Region          53..195
                     /region_name="NusG"
                     /note="Transcription termination/antitermination protein
                     NusG [Transcription]; COG0250"
                     /db_xref="CDD:440020"
ORIGIN      
        1 mdiltskcsd rfmahvlkrr dqeavrwyvl tlptagggrd kispskgldv elsrrerrge
       61 alfeyfspsy vearkvggkm vntkrpllyn yvfihasene ifslkrtlpl ynflprvssg
      121 gqsyfpylsd remetlrwva asysnelpvy vpdsghllkg drvritsgpf admeaevvvq
      181 pggghkdvmv rildcmwvpl fevrageyel ielntggkhv ythldndrls eglhgalgry
      241 hssgsvveed aclarevlrg yaslrgetdv ircklyslll paykllgeed efdrlrstmr
      301 smlpvikapq sralllvtly gctdsslyqr mahelvdpwm eeaspkksks vlirrlrdyd
      361 rwlghgis
//
LOCUS       WP_005858066             586 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Sagittula stellata].
ACCESSION   WP_005858066
VERSION     WP_005858066.1
KEYWORDS    RefSeq.
SOURCE      Sagittula stellata
  ORGANISM  Sagittula stellata
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sagittula.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 586)
  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 586)
  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 586)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Sagittula stellata"
                     /db_xref="taxon:52603"
     Protein         1..586
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=61423
     Region          24..92
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          303..370
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
     Region          476..541
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 migrkthsnn gvtdpsvqgf ddyalrlgdv mrgeratlgk slldvqrelr ikasyisaie
       61 ncdpsafdtp gfiagyvrsy arylgmdpde afagfckesg fsvahgmsqe asvirkahde
      121 eapkprarnp laepkmpfap asdslfsqie praigsslvl ialiggigyg gwtvlqeiqr
      181 vqvtpvdqtp vvlseldpld aakagkaqpd sagteqmagv ftppsteafd rlyrpqaldv
      241 pvlvardepi stldpdsggl ysgrgpslpr vddsslaaaa laqglidqas tgavpvtags
      301 gvtvvavrpa wvqikdeagt vlysrvmnag daypvprdag tpkiqigesg aiyfnieget
      361 ygpagsrgav tedvslaaad lvdrfnpaqp gadddllavl veldmkraae pvnvassrsp
      421 sapvasrvas vprlygapat repaqqtqrl aeapaarqda vpnsprvlad tppgitvvat
      481 qetwvevtsp sgkklfaqtl qagqtyevpq tdqpptifsg naggvffavn gqtfgpygtt
      541 gqfgrnlals adsiqqqlqv adlsanqtla rvvaelrlqs adgpgr
//
LOCUS       WP_005858112             361 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Sagittula stellata].
ACCESSION   WP_005858112
VERSION     WP_005858112.1
KEYWORDS    RefSeq.
SOURCE      Sagittula stellata
  ORGANISM  Sagittula stellata
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sagittula.
REFERENCE   1  (residues 1 to 361)
  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 361)
  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 361)
  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 361)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Sagittula stellata"
                     /db_xref="taxon:52603"
     Protein         1..361
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=38600
     Region          1..354
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mdrrsflras tvgagaaaas tlaapayaqg qrtltmvtsw prgfavldda aqylvkfvge
       61 lsggdltidl kapgelvgaf evfdavssgq admyhaadyy figqhpgfay ftavpfggta
      121 qemvnwyyhg ggqdlhdelg sifnlkglma gnsgsqsggw frneiksadd fnglkfrmpg
      181 lggqvlgklg asvqnipgge lyqalssgal dglewvgpla deragfqeva kiyytagfhe
      241 pgsalsanvn ldvwndltdk qkailnygsm atthyqlaet lanngaalar lqaqgvktlq
      301 fsddvwdafg kasaevmden mndelfakir isfeeslats aswinksdgf yvqqrvrvlg
      361 q
//
LOCUS       WP_005859065             404 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Sagittula stellata].
ACCESSION   WP_005859065
VERSION     WP_005859065.1
KEYWORDS    RefSeq.
SOURCE      Sagittula stellata
  ORGANISM  Sagittula stellata
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sagittula.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Sagittula stellata"
                     /db_xref="taxon:52603"
     Protein         1..404
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39946
     Region          73..321
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mfflvgllgm mavgsiviag tadveedlad ngmgpddtsn eedagsdgsm itdladttgt
       61 scggeviawp gpsadpadih dedpevggpd aselqslfdl mglsglfsks qadtssvlpa
      121 pnvtaagdga geggaglnaa gtddsdtlsg tdatdllngg ggndvidgka gsddlrggdd
      181 adtllggegd dtlhgdggdd vlqgdggadv lyghdgndsl agnggddvlq gglgedvldg
      241 gtgndalhgr egadllrggr gidtlfggwg ddvlvgvtrd aegtdldagd flnggdgadt
      301 iivgsgdlvh ggegadslil gdwmtrqase lvdfdavedq lvivfddgpg tpepeleirv
      361 sadnsevtei vlngqvlttl ptndaptldg lvlvgesmad alvg
//
LOCUS       WP_005859175             355 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-oxoacyl-ACP synthase III family protein
            [Parabacteroides].
ACCESSION   WP_005859175
VERSION     WP_005859175.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 355)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..355
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39121
     Region          7..340
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 marweiknvg mkgvamavpk nvvttselgl lsqeeaevfd ntvgikrrhi apdtmcasdm
       61 cqaaaekllt elgwekdsid vllfesvtgd yrtpptscvl qdrlglsenc fcmdipmgcc
      121 gcmyaitvag nlltvgnvkr allligdtal rmgsvkdksr vplfgdcgta ialeydetan
      181 divvdfhtyg kgyealmtph ggfrhpatpa sfeyedfgng ivrapihtli ngmnvfsfai
      241 srppksvetf fadyninret didyflihqa nkmivdrivk klklpkekvp ynleefgnlg
      301 gasipslmvt riadqlrtke ttllmssfgl glswgtmwmk tkpmvisemv imkki
//
LOCUS       WP_005859940             187 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Sagittula stellata].
ACCESSION   WP_005859940
VERSION     WP_005859940.1
KEYWORDS    RefSeq.
SOURCE      Sagittula stellata
  ORGANISM  Sagittula stellata
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sagittula.
REFERENCE   1  (residues 1 to 187)
  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 187)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 187)
  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   4  (residues 1 to 187)
  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   5  (residues 1 to 187)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Sagittula stellata"
                     /db_xref="taxon:52603"
     Protein         1..187
                     /product="TRAP transporter small permease subunit"
                     /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=19588
     Region          33..164
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 msddssadtq dqfvpafaea pfgaalggva aamsavgtas igalmlliva dvigrnlldm
       61 pitgvseiaa rtvvaivflq vpaailqrrl tradflvrri graspaavsv leilfcitga
      121 vvfalivwas wpkfgsawtt aeffgvqgvw tiptwpfrgi tvlgaatatl aalyrvtref
      181 etmkaaq
//
LOCUS       WP_005860598             242 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Parabacteroides].
ACCESSION   WP_005860598
VERSION     WP_005860598.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 242)
  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   2  (residues 1 to 242)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..242
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=27864
     Region          102..172
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkwhdllyfs kgerqaltll lsliamawia iigtdfyrsq fqtvplvntg ikqdssqiys
       61 nktpsnsirk ekeshsnetk ipsegkskri rreskphfps ypkaekwpqg tvvelnsadt
      121 talkmvpgig svfakriiky rdllggfysv eqlgevygid edryeamksw fsvdpsvish
      181 lfvnqlsakk lashpyvsyk qariiekmir kkgklqgwed lslleefpeh eqqrlryyls
      241 fh
//
LOCUS       WP_005861131             306 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Parabacteroides].
ACCESSION   WP_005861131
VERSION     WP_005861131.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 306)
  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 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   3  (residues 1 to 306)
  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   4  (residues 1 to 306)
  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 306)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..306
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35741
     Region          63..291
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          211..290
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 msgnikkive pnsgidysle kdfkiftlsk elpittypsy irlgiviycv kgnakidiys
       61 nkhiitpkel iiilpgqlva ltdvsvdfqi ryftitesfy sdilsgisrf sphfffymrq
      121 hyyfkmedve tlsfvdffel lirkavdpen qyrresvill lrilfldiyn hykvnsldst
      181 atidvhkkel thkffqlvms nykvnrsvtf yanslcitpk yltmvvkevs gksakdwite
      241 ymilelkgll tnstlniqei vektqfsnqs slgrffrrht glsplqyrkk yltteqrtnf
      301 sknnti
//
LOCUS       WP_005861935             344 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Sagittula stellata].
ACCESSION   WP_005861935
VERSION     WP_005861935.1
KEYWORDS    RefSeq.
SOURCE      Sagittula stellata
  ORGANISM  Sagittula stellata
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sagittula.
REFERENCE   1  (residues 1 to 344)
  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 344)
  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 344)
  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 344)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Sagittula stellata"
                     /db_xref="taxon:52603"
     Protein         1..344
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=36870
     Region          4..337
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mktvatltaa laistasfvq aetldvastf pknmpflgeg aevlaknidi athgevklrv
       61 hgagdlvpal evlnqvssga ipagwdfigy wggtipvaal agampfgpgp dlftgwmweg
      121 ggmeivqkay tplnvkllpc hvtapepggw fnkeintved lqglrmrisg mggqvlnklg
      181 astqlipgge lyvalergri datefslpvv dkslgfaeia kyyyfpgwhq paswnslivn
      241 mdvwdgfgee vqeqimtack atvtwslaaa pepqgeiiee frsmgvetkr fpdevlaalr
      301 eastevleea aaadpivaea yqsiqdymak aqvwndlqqi paan
//
LOCUS       WP_005861951             336 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Sagittula stellata].
ACCESSION   WP_005861951
VERSION     WP_005861951.1
KEYWORDS    RefSeq.
SOURCE      Sagittula stellata
  ORGANISM  Sagittula stellata
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sagittula.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 336)
  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   6  (residues 1 to 336)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Sagittula stellata"
                     /db_xref="taxon:52603"
     Protein         1..336
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37289
     Region          22..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          105..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msdqtmaagf asafldyava egapraglla tarlceddla dqdtriptaa yqaliaagie
       61 alndtslllr hvletrletm sivgqivhas tsfphslgql nryarlmadv pipggrdrfe
      121 iaregdtvwl idhhpgdgsw nateasfarf isefrrsape hpfelalevt yappphanry
      181 pdlfrvpvtf rasrnalrin pvwldeafdg gkdyvfgvft rhadglmqal aendtlraav
      241 earvladlhe gtlsmdriar dlgmsrqtly rrlkdegvtf aevhddlrrr mamdylstrk
      301 vsvgetayll gfseasafvr afrrwtgmsp tawldn
//
LOCUS       WP_005862185             534 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Parabacteroides].
ACCESSION   WP_005862185
VERSION     WP_005862185.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 534)
  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 534)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 534)
  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   4  (residues 1 to 534)
  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 534)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..534
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=61721
     Region          <345..527
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          448..527
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mktsilyifl lsvlyacdsh sllppkqqld qqiaqlndys llsgplndql ceeiethaqe
       61 igndslllat rqiiytrycr lqdtaharml ldrmkpyair ikdkhllmnh lrmaflhaqi
      121 rqpaecerwi nearkyayin pqnwyitaas aclecglypq aliyadsalv nlkykvissp
      181 hlvkaialsr tgktaeaeew tqrcitdirh fqakhqihti sylqyqlfme yavslrkhgk
      241 nkealsvlee ldrvsfnnva tpllrnkdni eeykvrvarm lsechyatgn qseaiqqanr
      301 adslqshyaq eqmnirrkmi seslqnells trlksqkaea eqarliqyil tgviillmai
      361 ltggylwwrn hrrrlrqlfd llishhaawl lihdplplis rpqiklpdhs eantevttka
      421 dnllyqrils vmkeqkpfln pnldlvtlsr lvgtnrtqls ttlnrqtgmn fsrwlaeyrv
      481 hhllslvalr pdsditalas esgftsrtsf frqfrqvtgl tpnqyrnvrk etgk
//
LOCUS       WP_005863408             203 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Sagittula stellata].
ACCESSION   WP_005863408
VERSION     WP_005863408.1
KEYWORDS    RefSeq.
SOURCE      Sagittula stellata
  ORGANISM  Sagittula stellata
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sagittula.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Sagittula stellata"
                     /db_xref="taxon:52603"
     Protein         1..203
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22107
     Region          13..174
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mfnrcdseke camrriydwt maqaggqhal lalafvsfie asifpippdv lmipmilaap
       61 srawlialva tgssvlgglf gygigffffe tlgqpileff gkadkmaefn atfngagfwa
      121 vliagvtpfp fkvitimsgw tamplatflt talvarairf fvvagllyaf gapirdfier
      181 ylglvftlfv allvggflvl ryi
//
LOCUS       WP_005864960              98 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein
            [Parabacteroides].
ACCESSION   WP_005864960
VERSION     WP_005864960.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..98
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11355
     Region          3..98
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mksteeylsi lrsekeslfr kyqisnlglf gsvarheqre dsdidiyyes shmslftlcr
       61 lkselekllg csvdlfckre sfagtrmeks inkdliyv
//
LOCUS       WP_005865602             288 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Bartonella alsatica].
ACCESSION   WP_005865602
VERSION     WP_005865602.1
KEYWORDS    RefSeq.
SOURCE      Bartonella alsatica
  ORGANISM  Bartonella alsatica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Bartonella alsatica"
                     /db_xref="taxon:52764"
     Protein         1..288
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33118
     Region          10..278
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mvdflpyyfd ilratdrdry msvlfapkkk rralaalytf nvevsriret vhdpligeir
       61 lrwwydciah gemkksknnp iledlftait lfnlpktafl rycnaqildl yhnpietlhd
      121 lkfycgetas iilqlscqil dpdvaqdftd vykhggiaqg lsgvlrllsf mqsryqyylp
      181 adilkavgvd rrdlesyrvn neqkchiiea mvalsrdhyi kfyeysgalp rmlrpaflpl
      241 aiipaslqka lqlgatvfqe natlplirry wlitkaaisg dfpkillg
//
LOCUS       WP_005866078             339 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Parabacteroides].
ACCESSION   WP_005866078
VERSION     WP_005866078.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 339)
  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 13014342
            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="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=38785
     Region          205..337
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mmtrtvfill isslctlsyc tprtepaqte vltpvdsisk dsavimetlp phieiekell
       61 ydkhtledty pykdttrefq wekmkerlsl lesiqkepsq wailqnyknr ngeaplvkvf
      121 krdaykrvsd tlgveryqsv plylltdtvi peiygrdgsl vrikamdeds kfariqtvyd
      181 geeewyapkk yikqigdtvv fdkaifvdrh nqniatlehv gskwlvrsmn pattgqhrpp
      241 yaqetplgmy vlqekksrmi ylvdgsketg gfapyanrft ngayihgvpv naprksliey
      301 spslgttprs hmcvrnatsh aqfvydwapv nktivfvle
//
LOCUS       WP_005866080             246 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Parabacteroides].
ACCESSION   WP_005866080
VERSION     WP_005866080.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 246)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..246
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=27127
     Region          51..215
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mrriflylff ivlsvgsist ggvlralspe tgstsvavmg rqlyeemrld qwvcfdafmq
       61 glrgsekidr knkdiltlid fskpstaerm vvldirqkri lytslvshgk nsggnyatsf
      121 snengshkss lgfyltenty qgrngyslil nglekgindl akqraivihg asysdpsvaa
      181 ssgrlgrsfg cpalpvsvsk piintikngt llfiyandkn yltqssilst qqendifhek
      241 syqkvl
//
LOCUS       WP_005867359              97 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein
            [Parabacteroides].
ACCESSION   WP_005867359
VERSION     WP_005867359.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..97
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10989
     Region          6..97
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mrsaaeykei larfkkefga qfgikelgif gsvargehre dsdldvfvsl ekvepfiifd
       61 lkelleslck ckvdlvrlrd slrpalknni lkdgiyv
//
LOCUS       WP_005868085             314 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-oxoacyl-ACP synthase III family protein
            [Parabacteroides].
ACCESSION   WP_005868085
VERSION     WP_005868085.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 314)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..314
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34410
     Region          3..313
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mfinatgfyv peervdnqhf lelsgltsew ieqrtgihtr skakegenin tmsleavkda
       61 lpklpydite vdlivsasys pydtvataah tvqheytiad akalylssac ssflnalevv
      121 egyfamgkas kalvlsadkn sayynetdpk aghlwgdaaa affiskerig egdaeivevy
      181 tqglghlska meavhlrprd ggilmpegrd vfiqactymp knvlhllekn gytldnltyf
      241 ighqanmrim aniakqlnlp dekflhniee lgntgsvssa lvyaqndknf kkddliaitv
      301 fgggystgac likh
//
LOCUS       WP_005868371             485 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: replicative DNA helicase [Parabacteroides].
ACCESSION   WP_005868371
VERSION     WP_005868371.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..485
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=53835
     Region          24..458
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mankktltpt slpasltlpe erkaekallf gllasrkslp eiafrirpem fthpdialai
       61 eaylslhgkg egtdilsvek eirrlspera gqlpdlfela rqdgymevgg efvrqhcqyi
      121 reafvarrli lrchelahka aaddrdtqkl iselgtvade lgeqlslthe ipdmptatae
      181 amarvreire rvarggtagi htglggldrl mgglrtgslh vfaarpgmgk tafalfmavn
      241 aakqgvpvcv yslemsreql ifrmlgqiad vepskitkgt ateeemrale easrqlkelp
      301 icinqrsdiq ideircdisl rrrqgkcsla iidylqlvnr ddkgqtpnea isnitrkaki
      361 tamdeeipiv llcqlnrnce trgtysfrhq lsdlrdsgsi eqdadtvafi srlsvvnihe
      421 dpdthlptrg rgtillaknr qgelghvrfm hnegvtsfwd dtqpacvrka raaepkpkgk
      481 glfec
//
LOCUS       WP_005870350             116 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Campylobacter gracilis].
ACCESSION   WP_005870350
VERSION     WP_005870350.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter gracilis
  ORGANISM  Campylobacter gracilis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Campylobacter gracilis"
                     /db_xref="taxon:824"
     Protein         1..116
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12571
     Region          13..116
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 msaktapkkt inskdeilkf lssqkkrlfa vgvtelgffg syakgsadef sdidiaietd
       61 gakmvkklgn plsalvfldd fkkklsskfn vnvdlcdtts lsreekakll qgaiyv
//
LOCUS       WP_005870982             549 aa            linear   BCT 20-JAN-2025
DEFINITION  sensor histidine kinase [Campylobacter gracilis].
ACCESSION   WP_005870982
VERSION     WP_005870982.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter gracilis
  ORGANISM  Campylobacter gracilis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 549)
  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 549)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20493667
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Campylobacter gracilis"
                     /db_xref="taxon:824"
     Protein         1..549
                     /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=61373
     Region          36..261
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          <313..543
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mralrehnfk iyfiiifasl fvvllgvkny edakaqival adknkiaase nmvgnfsfwl
       61 derlhslvra akfmqnadai rddeklggfi rlfkensaef dalqflredg eifvdgkelg
      121 ddeampkslr tglvwfeetk stlaptvnfm qrhktlgept lnlcvpvmds gsfagvfcgv
      181 vklqnilknm ekfklapdsy afivthggei ltpmkdaalk kqiedkfkel flrgeditsl
      241 nigsnfisva eiptlnwfig agtdnekela allnsvlkna lillfafaal alvanflhnf
      301 myskiknlqd dyeallkhka rmseagelis ginhqfiqpv nslnlmissl lmlqkdgkld
      361 aatlehmlqk gqaatvllsd tieifrnfyk ssdspqkfsv qrcikdllkl mhtelskanv
      421 avslrefkde eatqrmgivq qillilihna kdavveryke qiakrqvfld ikfengtcki
      481 avtdygsgvs kaardkiltq pkttkkqgsg iglyfgkkla neklsgdirl lsagdpttfe
      541 lsfeinlke
//
LOCUS       WP_005871367             438 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Schaalia georgiae].
ACCESSION   WP_005871367
VERSION     WP_005871367.1
KEYWORDS    RefSeq.
SOURCE      Schaalia georgiae
  ORGANISM  Schaalia georgiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 438)
  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 438)
  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
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 438)
  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   5  (residues 1 to 438)
  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   6  (residues 1 to 438)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 438)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 438)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Schaalia georgiae"
                     /db_xref="taxon:52768"
     Protein         1..438
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45278
     Region          17..>107
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          <43..>86
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          110..407
                     /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 mpdhaaapas sgnghtcfea vrgerivqgm katnlkasnl slvlrrilas pgeitraais
       61 sstgitrati srlvddligr gfveeldpvg dsgrgrpanr ltptagrvta lgietnvsal
      121 dimlvdltgh vlahervrgd fagsdpirtm rrasraarrv vdaglppgal flgsgvgipg
      181 lvspttlala pnlkwrdipl dellapisyl dpvvvanead laafavahsv pgvpagppsf
      241 iyvsgevgvg sgivvdhrpl rgvrgwsgei ghicadpngp mcqcgargcl esylgvyala
      301 sragldrgag aagilreaav serarsalde agaalgrcla avinatdipv vvlggmvadl
      361 apalveparr elearvlqaa wappvirvwg asksltarga alrvlqrlvd dplswleeep
      421 gaewprarag gpdqsalr
//
LOCUS       WP_005871911             287 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Campylobacter].
ACCESSION   WP_005871911
VERSION     WP_005871911.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter
  ORGANISM  Campylobacter
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Campylobacter"
                     /db_xref="taxon:194"
     Protein         1..287
                     /product="formate/nitrite transporter family protein"
                     /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=30666
     Region          1..285
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mlnpaetaqa vsssmqhkah tplisiifla imagaaiamg difwahstvg maekqsigls
       61 nfiggitfsc glmmvvfygg hlftssvltg vpaadgklpl gktigywaiv wcfnfvggal
      121 iaymyyysgl plkydgyilq hfipaaagki napfhelfir gifcnvfvcm siwtatsesn
      181 lsgkffaimw migafvacsm ehcvanmfil tegiiakghy laaaggdvna lasslhgvta
      241 aqidsinwgn fivknmipvt lgnicgglff vglvgfmvnk ydmkkkd
//
LOCUS       WP_005872647             276 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Schaalia georgiae].
ACCESSION   WP_005872647
VERSION     WP_005872647.1
KEYWORDS    RefSeq.
SOURCE      Schaalia georgiae
  ORGANISM  Schaalia georgiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
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   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   4  (residues 1 to 276)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Schaalia georgiae"
                     /db_xref="taxon:52768"
     Protein         1..276
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=29609
     Region          1..267
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mirfdavskt ypggttaved fslqipehtt tvflgtsgcg kttlmrmvna mvaptsgrvl
       61 vrgqdvaeqd pvalrrsigy vlqegglfph rtiadniatv pllegvprrq araralelmd
      121 lvgldrdmag rypaqlsggq rqrvgvaral aneadillmd epfgaldplv radlqaelir
      181 ireqlgttil fvthdideaf llgdqiavlr tggraaqvgt aqellshpad dfvadfvgas
      241 raarpvridh rrgdlvvdea gtpvgtlcep drgarp
//
LOCUS       WP_005875436             685 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Porphyromonas gingivalis].
ACCESSION   WP_005875436
VERSION     WP_005875436.1
KEYWORDS    RefSeq.
SOURCE      Porphyromonas gingivalis
  ORGANISM  Porphyromonas gingivalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Porphyromonadaceae; Porphyromonas.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 685)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Porphyromonas gingivalis"
                     /db_xref="taxon:837"
     Protein         1..685
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72478
     Region          5..685
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mitpqliepc tiavigasqd vtkpggkvlq nilngsfqgr vlgvnpkvsn vqgvecvpdv
       61 kdlpqvdlai laiparfcpp tievlvkekg tkgiivfsag fsemgaegka lerqmaelan
      121 eagatligpn cvgvmnplhq svfttpvpvl tpkgcdfisg sgatavfime salskglsfs
      181 svysvgnaaq tgvedvlehl detfdaatss htlllyieti skpkrflkha rslvqkgcri
      241 aaiksgtssd ggraaashtg amlnsdvavd alfrkagvvr cysreelatv gavlqhpvlt
      301 gknmavitha ggpavmltda lsnggmsvpp ipeektrtll selfdgssva npidilatgt
      361 aeqlskvidt cekdldtidg mvvifgspgl fdvsdaydvi reqqkkckkp iyavlpsvin
      421 akegmerfia qggilfeeev alaraickvy qtpkpemtee selpkaaeir rllagksgml
      481 gtgdmlqlld ltgitrpqer lvtteteald aarsigfpla mkvmglahks daggvilnvs
      541 teegvkesfg klmqikgaeg vqvsqmesgv evfigvkkeg efghlitcgl ggifvevmkd
      601 ircalaplgk nealemirsl ksypiirgir gkqgindevi adtlckisrl laavpeieem
      661 dinplmgrge rlsavdvvvr lsdak
//
LOCUS       WP_005875678             215 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Oxalobacter paraformigenes].
ACCESSION   WP_005875678
VERSION     WP_005875678.1
KEYWORDS    RefSeq.
SOURCE      Oxalobacter paraformigenes
  ORGANISM  Oxalobacter paraformigenes
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Oxalobacter.
REFERENCE   1  (residues 1 to 215)
  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 215)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 215)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Oxalobacter paraformigenes"
                     /db_xref="taxon:556268"
     Protein         1..215
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=24114
     Region          1..204
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 maydleeqeq lesikawwkk hgnwitwvli ivlgcyavya ywgyyqrkqt aqasqlyyem
       61 qsavlsgdse ralrvakdtq ekfggtayap mvtlvaarma yeekdadtak sqlkwivdng
      121 kqdgykaiar irlagillde kaydegmkll svsfpepfas laedrkgdfl vaqnklaear
      181 iayqtaleka lpddpgkqli qlkleeigvp seskg
//
LOCUS       WP_005877145             321 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus durans].
ACCESSION   WP_005877145
VERSION     WP_005877145.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus durans
  ORGANISM  Enterococcus durans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
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
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Enterococcus durans"
                     /db_xref="taxon:53345"
     Protein         1..321
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=36212
     Region          5..312
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mtkliefkkv qkkygdkyai keldlaieeg eifvlvgpsg sgkttslkmi nglsqptsge
       61 vsfkgkalkd ydlqkmrwnm gyvlqqialf pnmtvkqnie vipemlgwek tkreqtadrl
      121 lekvgldpts yrnrmpqels ggeqqrigii ralaanpevl lmdepfsald plsraslqdl
      181 vlslhqdlgt tivfvthnmd eaiklgtria vmkdgeliqc etpeqlltnp knefvrsffd
      241 dslsqkeqtv keillaknyt kgisekdrpv vqfntplnev fallvdhesv niqenerisg
      301 eitrgdmfaf lsrkeednek v
//
LOCUS       WP_005877296             373 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Enterococcus durans].
ACCESSION   WP_005877296
VERSION     WP_005877296.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus durans
  ORGANISM  Enterococcus durans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Enterococcus durans"
                     /db_xref="taxon:53345"
     Protein         1..373
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43311
     Region          1..264
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          260..350
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrflhtadwh igkklqgydl iedqkyvlaq ileiakeekv daiviagdly drsvpavdai
       61 evfnelmvew nlhekfpifa isgnhdsnir lsagtpwfsh snyflqtrfe esfqpiefkn
      121 sqifllpyfe piaariyfed etiktiqqai ekvvdrmqea fdpnkkhili shfcvmgstk
      181 sdsetkievg gldavpgell epfdyvglgh lhnksalhqk narysgsplk fslseinqqk
      241 gvwivdleee lsltfreltp lfeieeitat fkelldptfy qkinrenyvq iyledrtiip
      301 nmmnqlrkiy prilgversn grevqvkrns kkvvtkdpqk lvqgffkemt neeltekqnq
      361 wltetlqelt ete
//
LOCUS       WP_005878517             224 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Oxalobacter paraformigenes].
ACCESSION   WP_005878517
VERSION     WP_005878517.1
KEYWORDS    RefSeq.
SOURCE      Oxalobacter paraformigenes
  ORGANISM  Oxalobacter paraformigenes
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Oxalobacter.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Oxalobacter paraformigenes"
                     /db_xref="taxon:556268"
     Protein         1..224
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24944
     Region          103..168
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mlkfvfwfll avnvivfast vdysgiskip aesrayepve dgririlsss rnaspvppve
       61 ekkkglseta cielenfnpq dadlfakkma lpankisrth tvkasgymvy ippfknikta
      121 ekriaelqak gitnyflipe gtrfrhaisl glfkteksar nlmeelekrs ihdaritarg
      181 kttesvsfkl nnlsgnqidh lntlltafpq vtrkecgvat eivq
//
LOCUS       WP_005878730             163 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Oxalobacter paraformigenes].
ACCESSION   WP_005878730
VERSION     WP_005878730.1
KEYWORDS    RefSeq.
SOURCE      Oxalobacter paraformigenes
  ORGANISM  Oxalobacter paraformigenes
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Oxalobacter.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Oxalobacter paraformigenes"
                     /db_xref="taxon:556268"
     Protein         1..163
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17953
     Region          13..153
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 miesavhwll sylaipevgl tsvflisfis atllplgsep avfavvaadk slfwqvmava
       61 aagntlggil nywigfgakk afakeretrw fgwlekygak tmllgwmpgi gdplctlagw
      121 lklpfwpcva ymaigklary vlmtwlllhi pdsswrelar flg
//
LOCUS       WP_005884370             173 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Fusobacterium mortiferum].
ACCESSION   WP_005884370
VERSION     WP_005884370.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium mortiferum
  ORGANISM  Fusobacterium mortiferum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (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   2  (residues 1 to 173)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Fusobacterium mortiferum"
                     /db_xref="taxon:850"
     Protein         1..173
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=20294
     Region          45..102
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkkilgilfi iflnfsityg npfennesfd iimsdnvlde nskyldinta skeemsnfgv
       61 ttrlarlive yreqtggfkn lnelkrikgi gqatfdklrk klmiktqiek kplyineand
      121 tlleyygfdk keikdirkyl nkngrinsnl dlmkvlsekn yrkyksiiky dkf
//
LOCUS       WP_005884397             217 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Fusobacterium].
ACCESSION   WP_005884397
VERSION     WP_005884397.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 217)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..217
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24111
     Region          38..201
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mlkkivtglv lcgsllfgad lsceenikti ykdlgienkl eystflkaiq gynriedkka
       61 gyitiidfsk psneerffvi dlenkkvdfs tyvthgknsg lgtavkfsnn pnsyqsslgf
      121 yltkntyegs ngyslrllgl epginsnamd rnivvhgady atkefmdkyg flgrslgcpa
      181 ipeeiskevi dyikggtvly ingndetyya kskyvql
//
LOCUS       WP_005885185             153 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Brevibacterium
            mcbrellneri].
ACCESSION   WP_005885185
VERSION     WP_005885185.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium mcbrellneri
  ORGANISM  Brevibacterium mcbrellneri
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (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   2  (residues 1 to 153)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Brevibacterium mcbrellneri"
                     /db_xref="taxon:53363"
     Protein         1..153
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17117
     Region          47..126
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mtlhpghqrh lqmelagsqa grlrvevttl maamqadlah pwrlvelaei ahlspsrrrq
       61 lfveilgmpp iawptlqrvr amartisatd tttrqataev gwmnqahaak qfrkltgrsp
      121 teyrakvwsq nepvgicrwc ghpikqpssr arg
//
LOCUS       WP_005886100             150 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Fusobacterium
            mortiferum].
ACCESSION   WP_005886100
VERSION     WP_005886100.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium mortiferum
  ORGANISM  Fusobacterium mortiferum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (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   2  (residues 1 to 150)
  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 150)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Fusobacterium mortiferum"
                     /db_xref="taxon:850"
     Protein         1..150
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17674
     Region          18..72
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 merpeyygil pskvryderl kpmekimfse ltalvrkkgy cyasnmyfat lygvhkstvs
       61 awisnlakcg hittkcimkd krveerriyi aeesdisyfp klekeksniv ddkildeifk
      121 ekierrektp eeledvrkkl lrdlfgcege
//
LOCUS       WP_005886558             191 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Pseudomonas syringae group].
ACCESSION   WP_005886558
VERSION     WP_005886558.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 191)
  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 191)
  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   3  (residues 1 to 191)
  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   4  (residues 1 to 191)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 191)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..191
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21388
     Region          1..191
                     /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"
ORIGIN      
        1 mlrillindt akkvgrlrsa lteagfevid esgliidlpa rveavrpdvi lidtespgrd
       61 vmeqvvlvsr dqprpivmft dehdpgvmrq aiksgvsayi vegiqaqrlq pilevamarf
      121 esdqalraql hardqqlaer krielakgml mkmkacneee aytlmrrqam srqqkliqva
      181 eqiiamsell g
//
LOCUS       WP_005886605             191 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Fusobacterium mortiferum].
ACCESSION   WP_005886605
VERSION     WP_005886605.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium mortiferum
  ORGANISM  Fusobacterium mortiferum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Fusobacterium mortiferum"
                     /db_xref="taxon:850"
     Protein         1..191
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21512
     Region          2..157
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mimetlkkir shrsftkkki smeeleemve stryasstrn aqklryvlin deelckkifp
       61 lvkfagaipw nptieeapta yilmcsenpl vnfterslyf dmgiasqnim lvanemgyag
      121 ciigsynkpe vdklvglpeg yvshtlltlg epkdtvtite aidgnttysr ddnnhhfvpk
      181 lslkdisllk k
//
LOCUS       WP_005886683             357 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Fusobacterium
            mortiferum].
ACCESSION   WP_005886683
VERSION     WP_005886683.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium mortiferum
  ORGANISM  Fusobacterium mortiferum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 357)
  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 357)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Fusobacterium mortiferum"
                     /db_xref="taxon:850"
     Protein         1..357
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=41564
     Region          18..72
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 meklnyfaim pakvrydenl kpmekliyse itvltnfkgy cyatnsyfak lygvhknsic
       61 awisnlvkyg ylkveyvlke idgekkqerr iyivdikein qakkevveki lerkvkeskk
      121 eeereviekd veveekvgtk keiedtnfce gvsqktvmvt entegpsqkn vrgyqsnlgd
      181 plnekteenn tsriikenny yiytyrgeen lpvvreilkk yselglppye yppeknlvmk
      241 aygelgakgv fkaleimsks nfvmekmcvd tilkvenlkk alngnfkadv eeksvelvgk
      301 kresikksgd ekkfeeseeg kqwkeeqkrk isellekdve eedtpelfsv eelfgkr
//
LOCUS       WP_005887008             400 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Fusobacterium].
ACCESSION   WP_005887008
VERSION     WP_005887008.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..400
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43319
     Region          1..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkvlvincgs sslkyqlmnp etrevfakgl cerigidgsr meyevpakdy evkiekpmpt
       61 hkealelvin aitdkehgvi asvdeveaig hrmvhggetf assvllteea maaveannel
      121 aplhnpanlm gvrtcmalmp gkpnvgvfdt afhqtmpaka fmyalpyedy selkvrkygf
      181 hgtshlyvse tmreimgnpe hskiivchlg ngasvsavld gksidtsmgl tplqglmmgt
      241 rcgdidpaav lfiknkrgls dkemdnrlnk qsgilgifgk ssdcrdmeng vaegderakl
      301 aeemfiyrik syvgayaaam ggvdaicfag gigenaagir agvieglefl gakldkavns
      361 vrqkgnvkls tedskvliyk iptneelvia rdtyrivtgk
//
LOCUS       WP_005887969             524 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Fusobacterium sp. HMSC064B12].
ACCESSION   WP_005887969
VERSION     WP_005887969.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium sp. HMSC064B12
  ORGANISM  Fusobacterium sp. HMSC064B12
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Fusobacterium sp. HMSC064B12"
                     /db_xref="taxon:1739279"
     Protein         1..524
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=60721
     Region          1..473
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 miyidppynt gkdfvykdnf tdnienykei tgqinkegik lttntetngr yhsdwlnmmy
       61 prlklarnll tddgvifisi ddneqanlkk icdeifgeen fvavaprktg agsaatnsds
      121 elrklndflf iylksrkakf rknikgsrky pyedkngkye lvklqasgsd atrrarpkmy
      181 ysiylkedgs lttdmnekni vkeiipnkvn eedgrwiwgk erfeemkekf tyydgetiyr
      241 klyydetedq nvyqvekawf dsftnaqgtk efdelfkkkk ifshpkpidl ikllinlsnk
      301 ensflildff sgsattahsv mqlnaedggn rkyimvqlpe lcdesseayk agykniceig
      361 kerirragek iksdeslple nrekldigfk ifkldssnik ewdtntkdlq qtlldsmeni
      421 ksdrtsldil yeillkygld lnipieenkd fysigggsll vslnqeinnk vinsiceeyk
      481 klleldkdfk ttvilrdnsf kndvdktnai kkleqvgine irsi
//
LOCUS       WP_005888086             243 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Fusobacterium sp. HMSC064B12].
ACCESSION   WP_005888086
VERSION     WP_005888086.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium sp. HMSC064B12
  ORGANISM  Fusobacterium sp. HMSC064B12
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 243)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Fusobacterium sp. HMSC064B12"
                     /db_xref="taxon:1739279"
     Protein         1..243
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=27598
     Region          55..224
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mkllkyvfsl iiyfifslsl faeinfsndf klsikkkfsd mdiklmytel clndkvsfsc
       61 fnnamhglek iedleifdns nnnllvmvdy tkpsteerlf iidlrkkqll isslvthgrg
      121 tgdlyatkfs nknnsystss gfyltgniyn gkhgeslely glekgkndna kkrtivmhsa
      181 yyankafaek ygrlgrskgc lalptdlnak iinlisggvv lyvhtnfden keydfsklls
      241 ksf
//
LOCUS       WP_005890123             921 aa            linear   BCT 20-JAN-2025
DEFINITION  AAA family ATPase [Fusobacterium sp. HMSC064B12].
ACCESSION   WP_005890123
VERSION     WP_005890123.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium sp. HMSC064B12
  ORGANISM  Fusobacterium sp. HMSC064B12
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 921)
  AUTHORS   Liu,Y., Sung,S., Kim,Y., Li,F., Gwon,G., Jo,A., Kim,A.K., Kim,T.,
            Song,O.K., Lee,S.E. and Cho,Y.
  TITLE     ATP-dependent DNA binding, unwinding, and resection by the
            Mre11/Rad50 complex
  JOURNAL   EMBO J 35 (7), 743-758 (2016)
   PUBMED   26717941
REFERENCE   2  (residues 1 to 921)
  AUTHORS   Chen,Z., Luong,T.T. and Lee,C.Y.
  TITLE     The sbcDC locus mediates repression of type 5 capsule production as
            part of the SOS response in Staphylococcus aureus
  JOURNAL   J Bacteriol 189 (20), 7343-7350 (2007)
   PUBMED   17704228
REFERENCE   3  (residues 1 to 921)
  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   4  (residues 1 to 921)
  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
REFERENCE   5  (residues 1 to 921)
  AUTHORS   Hopfner,K.P., Karcher,A., Craig,L., Woo,T.T., Carney,J.P. and
            Tainer,J.A.
  TITLE     Structural biochemistry and interaction architecture of the DNA
            double-strand break repair Mre11 nuclease and Rad50-ATPase
  JOURNAL   Cell 105 (4), 473-485 (2001)
   PUBMED   11371344
REFERENCE   6  (residues 1 to 921)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..921
                     /organism="Fusobacterium sp. HMSC064B12"
                     /db_xref="taxon:1739279"
     Protein         1..921
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=108543
     Region          1..919
                     /region_name="PRK03918"
                     /note="DNA double-strand break repair ATPase Rad50"
                     /db_xref="CDD:235175"
ORIGIN      
        1 miikkvqlen yrshsnttie ftkginlilg kngrgktsil eaistvmfnt kdrsgketgk
       61 syikfgekss kvdidfiand greynlktef fktkpkkqtl kdmigseydg diqekleelc
      121 gikkgfeety eniviakqne finifkakpk dreeifnkif ntqiykemyd sflkeaidky
      181 ksekenldsk inslkenmed keqitnflke ekeveknlqd rfkninvvsk nleneikdye
      241 tteielnnli knikdeenki kkylnilken iieakqakks kiivketeks yfeyleienr
      301 lkdlrenldn lldeqklniq yqnnieklel snknlkvdis nleeniskns ekkenlesei
      361 snlkikeedl dlklkkyttl ldelekleki kkeksddklk ttaeinifqk nlslkkdlfk
      421 ainieiiekk lsdfqeleke lklleeqkii feteiktlkk sskelsnkic pflnekcqnl
      481 edkeaedyfs skisiktedl enlkknieek tqilvekvvf edrkkqyfel eksikdlels
      541 skneeinlke ieldiknldm nikklienqe fqnsqmlrek kkelevelrn lnldekrenl
      601 knllenlete kekilknqns iesnlkkide fskkikvdtn kniesiksei ktfenklddl
      661 knpyneylkn nvlaedlenl llkvdknike lyslrtdknl lkekvsilee kiknikidel
      721 kekydiikee lneinkklgs sqekienykk ilekissqee kekklliefk klenkfnkan
      781 lirnevgqmg raiskymlsg isniasvnfn kitgrterie wsneekdkya vylvgqerki
      841 afeqlsggeq vsvaiairgt mteyftnskf mildeptnnl dterkkllae ymgeilnnle
      901 qsiivthddt fremaekiie l
//
LOCUS       WP_005891744             322 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein, partial
            [Aeromonas molluscorum].
ACCESSION   WP_005891744
VERSION     WP_005891744.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas molluscorum
  ORGANISM  Aeromonas molluscorum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Aeromonas molluscorum"
                     /db_xref="taxon:271417"
     Protein         1..>322
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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]"
     Region          1..311
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvqqlnk hfnqyaalsd inldfkdgel vallgpsgcg kttllriiag leqadtgril
       61 irgedagslh vrernvgfvf qhyalfrhmt vfenvafglr vkpraerpge pvirarvrel
      121 ldlvqlshva drhptqlsgg qrqrvalara lavqpkvlll depfgaldaq vrkelrrwlr
      181 elhnelhvts lfvthdqeea levadrvvlm nagkveqigt pvevydkpas afvhsflgsv
      241 nlfhgrvaaq gfgvgdrlla ggradlsqgs aaiayvrphe lelhpleahg gveatisrll
      301 pmgprirvel rgsaetngal fe
//
LOCUS       WP_005894279             811 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: Lon protease family protein [Pseudomonas syringae
            group].
ACCESSION   WP_005894279
VERSION     WP_005894279.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 811)
  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 811)
  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 811)
  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   4  (residues 1 to 811)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..811
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..811
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89514
     Region          65..789
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mpdsvaanlr laphaltrpf saeqfsfatt helepfrgvl gqeravealq fgvamprpgy
       61 nvfvmgepgt grfsfvkryl kaegkrmqtp sdwvyvnnfd eprepkalel ppgsahafia
      121 dinglidnll vtfpavfehp syqqkkssid rafnqrydra ldvierlsle kdialyrdst
      181 niaftpmadg kaldeaefsq lpeadrerfh edisaleerl neelaslpqw kresnnqlrq
      241 lneetitltl qpllaplsek yaenaavcay lqamqvyllk tvveqlvdda ktdaqarkll
      301 eeqyspslvv gnnhnggapv vfeqhptydn lfgrieystd qgalyttyrq lrpgalhran
      361 ggflileaek mlgepfvwda lkrtlqsrkl kmesplgelg rvatvsltpq vipwnvkiii
      421 igsrslyytl qdldpdfqem frvlvdfdee ipmvdetleq faqllktrts eegmapltad
      481 avarlatysa rlaehqgrls arigdlfqlv seadfirqla nddktdaghi eralkakatr
      541 tgrvsarild dmmagvilid tdgaavgkcn gltvlevgds afgvparisa tvypggsgiv
      601 dierevnlgq pihskgvmil tgylgsryaq efplaisasi aleqsygyvd gdsaslgeac
      661 tlisalsrtp lkqcfaitgs inqfgevqav ggvnekiegf frlcearglt geqgaiipha
      721 nvttlmlder vvqavrdgqf hiyavrqade alsllvgepa gtpdengefp egsvnarvve
      781 rlrdiaemls dedlkeelek epaqlqpelk a
//
LOCUS       WP_005894416             585 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Fusobacterium
            polymorphum].
ACCESSION   WP_005894416
VERSION     WP_005894416.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium polymorphum
  ORGANISM  Fusobacterium polymorphum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Fusobacterium polymorphum"
                     /db_xref="taxon:76857"
     Protein         1..585
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=66811
     Region          2..555
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 midkrlynfs gnikkyisit tflsciklia niffysifaf llvslinkdf sfsyshiiis
       61 iliivfvrqf stikvahilg nlvvdvkrnl rklifektlk lglaysqlfk tqelihlsvd
      121 nveqlevyfg gfltqfyywi vssfilffsi ayfnlkiafi llgfslaipl slyiilnkvk
      181 kiqkkyfaky mnvgtlflds lqglttlkly gtdekreeei akmseefrie tmrvlkmqll
      241 siavinwiiy agtilaiits iklflngslg lfpmlfifml apeffipmrt ltslfhvamt
      301 gvsaaeniis fvdspernnn gnkdfknene ikvsklnfsy pdgtqslkdi dmtfkkgnlt
      361 avvghsgcgk stlvsvlsge lkskeneifv ddidiqniki edkiknilki thdshifsgt
      421 vrenltmane nlsdeamiev lkkvklwdif sknkgldtsl esqgknlsgg qaqrvalara
      481 llydasvyif deatsnidie seeiilniiy slskektviy ishrlpaikn adciyvmdkg
      541 kviesgkhdk lyakkelyyn mykhqeelet yltkrgekye ksvnf
//
LOCUS       WP_005896146             795 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: penicillin acylase family protein [Pseudomonas
            syringae group].
ACCESSION   WP_005896146
VERSION     WP_005896146.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 795)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 795)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 795)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..795
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..795
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=88229
     Region          21..795
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkrslvilai iiailaggag wyinskqpvr dgeiamsrlq apvtlryder gvphihaene
       61 adlyralgya haqdrlfqme mlrrlargel aeilgpnlve tdklfrslri rehadayvah
      121 qdkntptwqa leayidginq yqdsharpme fdvlgipkrr fttedtmsig gylaysfaaa
      181 frteplltyv rdqlgpqylk vfdldwhpdg vlnskpalas adwkslgela qishkaleda
      241 glpqfegsna wvisgnrtqs gkpllagdph irfsvpsiwy eaqlsapgfe lyghfpalnp
      301 faflghnmdf gwsltmfqnd dvdliaektn pdnpnqvwyh gqwvdmtrte qqiavkgqpp
      361 vtlsllesph gpivnnvmgk nagqtpiamw wsflvsanpv mdgfyeanra dtlekmrsaa
      421 ekiqspglni vwanakgdig wwaaaqlpir pegvnpafil dgstaqadkl gfypfsanpq
      481 eenpargyiv sanfqplsps gmqipgyynp pergqelnrq lsdttikwdl taskalqlst
      541 qtdyapsilk plipvlrsvi sdpeelalve rlaswkgdyp vdsvgatlfn qflfdlteet
      601 fhdelgdalf etllstrald salprlaada dspwwnnrns pheesrantv kvawrasvsh
      661 lrslygtnpd ewvwgkahtl tqghplgsqp pldrifnvgp yaapgthevp nnlsssirpa
      721 pwpvgygpst rrlidfadpa hslginpvgq sgvpfdkhys dqakafvkge ympqrfsedd
      781 vaehtegvlr lvpge
//
LOCUS       WP_005896495             256 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Fusobacterium
            polymorphum].
ACCESSION   WP_005896495
VERSION     WP_005896495.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium polymorphum
  ORGANISM  Fusobacterium polymorphum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Fusobacterium polymorphum"
                     /db_xref="taxon:76857"
     Protein         1..256
                     /product="formate/nitrite transporter family protein"
                     /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=27505
     Region          6..256
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 madghktpse lvdymitvgi dkatkplfkl mllgifggaf ialggagnii sastlaktdp
       61 glakfvgacv fpvglimvvi lgselftsnc llsvaytnkk inftqlirnl vtvylfnyvg
      121 sfivayitvr ggsfnadsld ylqniathkv hadayvlfik gilcnvlvcg avllsytskd
      181 tigklvgawl pimlfvligy dhsianmfyl taakladssl evslilynlf yvtlgnilgg
      241 maiglplyfc yykkqa
//
LOCUS       WP_005897556             248 aa            linear   BCT 20-JAN-2025
DEFINITION  YaaA family protein [Fusobacterium polymorphum].
ACCESSION   WP_005897556
VERSION     WP_005897556.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium polymorphum
  ORGANISM  Fusobacterium polymorphum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Prahlad,J., Yuan,Y., Lin,J., Chang,C.W., Iwata-Reuyl,D., Liu,Y., de
            Crecy-Lagard,V. and Wilson,M.A.
  TITLE     The DUF328 family member YaaA is a DNA-binding protein with a novel
            fold
  JOURNAL   J Biol Chem 295 (41), 14236-14247 (2020)
   PUBMED   32796037
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Liu,Y., Bauer,S.C. and Imlay,J.A.
  TITLE     The YaaA protein of the Escherichia coli OxyR regulon lessens
            hydrogen peroxide toxicity by diminishing the amount of
            intracellular unincorporated iron
  JOURNAL   J Bacteriol 193 (9), 2186-2196 (2011)
   PUBMED   21378183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006857
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Fusobacterium polymorphum"
                     /db_xref="taxon:76857"
     Protein         1..248
                     /product="YaaA family protein"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=28967
     Region          2..245
                     /region_name="YaaA"
                     /note="DNA-binding protein YaaA associated with the
                     oxidative stress response [Replication, recombination and
                     repair]; COG3022"
                     /db_xref="CDD:442258"
ORIGIN      
        1 mkiifspske mreenifenk kiefteskfk dktniligil kekslseien imklkgklln
       61 ktykdiqdyd klkfipaism yygvsfkeln ledyseksle ylknnllils alygvflafd
      121 llkkyrldmt msiidkglyn fwkkdindyi snilskdevl lnlasgefsk lidnkkismi
      181 nidfkeekdg ayksvstysk kargqflnyf iknqianled ikkikldgys lnkdlsdekn
      241 liftrkns
//
LOCUS       WP_005898977             256 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Fusobacterium].
ACCESSION   WP_005898977
VERSION     WP_005898977.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..256
                     /product="formate/nitrite transporter family protein"
                     /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=27493
     Region          6..256
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 madghktpse lvdymitvgi dkatkplfkl mllgifggaf ialggagnii sastlaktdp
       61 glakfvgacv fpvglimvvi lgselftsnc llsvaytnkk inftqlirnl vtvylfnyvg
      121 sfivayitvr ggsfnadsld ylqniathkv hadayalfik gilcnvlvcg avllsytskd
      181 tigklvgawl pimlfvligy dhsianmfyl taaklsdssl evslilynlf yvtlgnilgg
      241 maiglplyfc yykkqa
//
LOCUS       WP_005899618             297 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Fusobacterium].
ACCESSION   WP_005899618
VERSION     WP_005899618.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..297
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=33987
     Region          47..209
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkkilafisl lflmvacsst ekvvssssrg ssvsrnqttv knigkfqvds nsyvatgkne
       61 riqfivvhyt atdnlgsike ltssrvsshf lvldeddnki ynlvpleqra whagasafrg
      121 rtnindtsvg ieivsdgiar eyrpdpnpyh pydhyvdykp iqiektaqii kyvaekynvp
      181 arnivahsdi apsrkkdpga kfpwkelydk ynigawydet dkqefmdeek fkatsireik
      241 delrkygyei nrldewdkes kdvvyafqlh fnpknatgem dletfailka lnkkypd
//
LOCUS       WP_005899670             585 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Fusobacterium sp.].
ACCESSION   WP_005899670
VERSION     WP_005899670.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium sp.
  ORGANISM  Fusobacterium sp.
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Fusobacterium sp."
                     /db_xref="taxon:68766"
     Protein         1..585
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=66848
     Region          2..555
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 midkrlynfs gnikkyisit tflscvklva niffysifaf llvslinkdf sfsysyiiis
       61 iliivfvrqf stikvahmlg nlvvdvkrnl rklifektlk lglaysqlfk tqelihlsvd
      121 nveqlevyfg gfltqffyci vssfilffsi ayfnlkiafi llgfslaipl slyiilnkvk
      181 kiqkkyfaky mnvgtlflds lqglttlkly gtdekreeei akmseefrve tmrvlkmqll
      241 siavinwiiy agtilaiits iklflngslg lfpmlfifml apeffipmrt ltslfhvamt
      301 gvsaaeniis fvdspernnn gnkefknene ikvsklnfsy pdgtqslkdi dmtfkkgnlt
      361 avvghsgcgk stlvsvlsge lkskeneifv ddidiqniri edkiknilki thdshifsga
      421 vrdnltmane nlsdetmiev lkkvklwdif sknkglntyl esqgknlsgg qaqrvalara
      481 llydasvyif deatsnidie seeiilniiy slskektviy ishrlpaikn adciyvmdkg
      541 kviesgkhne lytkkelyyn mykhqeelet yltkrgekye ksvnf
//
LOCUS       WP_005900278             243 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Fusobacterium].
ACCESSION   WP_005900278
VERSION     WP_005900278.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 243)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..243
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=27727
     Region          55..224
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mklfksifil ifyfifslsl faeikflndf nlnikkkfsd sdiklmytel clndkvsfsc
       61 fnnamhglek iedleffnns ndnllvivdy tkpsteerlf vidlrkkqll isslvthgrg
      121 tgglyatnfs nknnsystss gfyltgniyn gkhgeslvly glekdkndna qkrtivmhqa
      181 yyanksfakk ygrlgrskgc lalptdlnsk iinlisdgvv lyvhtnfden keydfsklls
      241 ksf
//
LOCUS       WP_005902785             581 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Fusobacterium
            nucleatum].
ACCESSION   WP_005902785
VERSION     WP_005902785.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium nucleatum
  ORGANISM  Fusobacterium nucleatum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Fusobacterium nucleatum"
                     /db_xref="taxon:851"
     Protein         1..581
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=66299
     Region          2..555
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 midkrlynfs gnikkyisit tflscvklia niffyfifaf llvslinkdf sfsysyiiis
       61 iliivfvrqf stikvahmlg nlvvdvkrnl rklifektlk lglaysqlfk tqelihlsvd
      121 nveqlevyfg gfltqfyyci vssfilffsi ayfnlkiafi llgfslaipl slyiilnkvk
      181 kvqkkyfaky mnvgtlflds lqglttlkiy gtdekreeei akmseefrie tmkvlkmqll
      241 siavinwiiy agtilaivts vklflngslg lfpmlfifml apeffipmrt ltslfhvamt
      301 gvsaaeniis fvdspernnn gnkefknene ikvsklnfsy pdgtqslkdi dmsfkkgnlt
      361 avvghsgcgk stlvsvlsge lkskeneifv ddidiqniki edkiknilki thdshiffgt
      421 vrenlamane nlsdetmiev lkkvklwdif sknkgldtsl esqgknlsgg qaqrvalara
      481 llydasvyif deatsnidie seeiilniiy slskektviy ishrlpaikn adciyvmdkg
      541 kviesgkhde lyakkelyyn mykhqeelet yltkrgenne k
//
LOCUS       WP_005903318             381 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Fusobacterium
            nucleatum].
ACCESSION   WP_005903318
VERSION     WP_005903318.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium nucleatum
  ORGANISM  Fusobacterium nucleatum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 381)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Fusobacterium nucleatum"
                     /db_xref="taxon:851"
     Protein         1..381
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43375
     Region          5..374
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mnkikslqvf ynekkvgtla lmknnivafe ydnewlnngf sispyslplk kqvfipkiep
       61 fdglygvfsd slpdgwgrll vdrmlnsqni npreinpisr laivgetgmg alsynpvynl
      121 ledkdyqedy dslalsckki lntkysddld nlfrlggssg garpkiltki nnedwiikfp
      181 sslddenigk leylyslcak kckinmpetk lfpskissgy fgvkrfdrkk sstdairkih
      241 misvsgllet shripnldyn dlmqltlnlt ksfedveklf rlmcfnvfsh nrddhsknfs
      301 fiyneeskkw elspaydlty sysingehat tvngngvnpd lkdilkvaen igldkkkaen
      361 iaseikkivk kdleiflsnn q
//
LOCUS       WP_005903722             243 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Fusobacterium nucleatum].
ACCESSION   WP_005903722
VERSION     WP_005903722.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium nucleatum
  ORGANISM  Fusobacterium nucleatum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 243)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Fusobacterium nucleatum"
                     /db_xref="taxon:851"
     Protein         1..243
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=27592
     Region          55..224
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mkllksvftl ilyfifslsl faevkfsndf nldikkkfsd leiktmyrdl slndkvsfsc
       61 fnnaihglek iedleifdss ndnllvmvdy tkpsteerlf iidlrkkqll isslvahgrg
      121 tgdlyatnfs nknnsystss gfyltgniyn gkngeslely glekgkndna rkrtivihsa
      181 yyanksfaek ygrlgrskgc lvlptdlntk iinlifggvv lyvhtnfden keydfsklls
      241 ksf
//
LOCUS       WP_005904104             176 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Fusobacterium nucleatum].
ACCESSION   WP_005904104
VERSION     WP_005904104.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium nucleatum
  ORGANISM  Fusobacterium nucleatum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (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   2  (residues 1 to 176)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Fusobacterium nucleatum"
                     /db_xref="taxon:851"
     Protein         1..176
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=20454
     Region          42..99
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
     Region          114..169
                     /region_name="HHH_3"
                     /note="Helix-hairpin-helix motif; pfam12836"
                     /db_xref="CDD:463723"
ORIGIN      
        1 mkkimlllgi fslfslnmys apdfsnndyk iimssqnmkd ekeelmdink vseqemlark
       61 vsksyvskii eyreitggfd kledmkrikg ignatyqkls kvfkvasapn kkmlninsad
      121 dmtlkyygls kkeikriqky ldkndritdn iefkkivnkk tyerlkdlin ydggkr
//
LOCUS       WP_005905186             398 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Fusobacterium].
ACCESSION   WP_005905186
VERSION     WP_005905186.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..398
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43629
     Region          1..398
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkilvincgs sslkyqlinp eteevfakgl cerigidgsk meyevvakdf ekkletpmps
       61 hkealelvis hltdkeigvi ssvdevdaig hrvvhggeef aqsvlvndev lkaieanndl
      121 aplhnpanlm girtcmelmp gkknvavfdt afhqtmkpea fiyplpyedy kelkvrkygf
      181 hgtshlyvsg vmreimgnpe hskiivchlg ngasitavkd gksvdtsmgl tplqglmmgt
      241 rcgdidpaav lfvknkrglt daqmdermnk ksgilglfgk ssdcrdmena vkegderail
      301 aesvsmhrlr syigayaaim ggvdaicftg gigenssmtr ekaleglefl gieldkeins
      361 vrkkgnvkls kntskvliyk iptneelvia rdtfrlak
//
LOCUS       WP_005905536             735 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Aeromonas molluscorum].
ACCESSION   WP_005905536
VERSION     WP_005905536.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas molluscorum
  ORGANISM  Aeromonas molluscorum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 735)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 735)
  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   3  (residues 1 to 735)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..735
                     /organism="Aeromonas molluscorum"
                     /db_xref="taxon:271417"
     Protein         1..735
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=80814
     Region          1..716
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          <261..>325
                     /region_name="nfrB"
                     /note="phage adsorption protein NrfB; PRK11234"
                     /db_xref="CDD:236884"
ORIGIN      
        1 mdldqalqty lvearellee messllrles tpeddeiiga vfraahtikg saglfglapi
       61 igfthivedi ldqvrnhrla isaeliklll escdhinllv nivveqgdnp gpaelaqdgm
      121 lrerlqiyqq gdteslvrlp csqtspverq dpgpqamtel whislrfgre vfkngmepts
      181 flrylatlge ivaietitaa lpgwqaldpe ncylgyeidf dstaskesis evfefvrddc
      241 qililpphsk laeylaliea lpeenemlgq llvktgaltq aeleaalhlq hlhaqaphar
      301 lgeilisqga vdevvvdaal kkqnqgkeqk nkeqrfvrvh adklddlinl vgelvvassg
      361 anllaqrlrd sqlleatsvi amlveeirdg alhlrmvpig etfnrfqrvv rdvsqeldkd
      421 itlrisgadt eldksvveki gdplmhlvrn amdhgiesae rrqqagkpsq gtltlnafhd
      481 sgsivleiqd dgagldkeki lkkalerdii apgqqlseqd iyqlifepgf staeavtnls
      541 grgvgmdvvk rniqalrgsv elhsetgkgt lvrirlpltl aiidgflvrv gsahyvipld
      601 mviecvelte dalqdtlgrd yinlrgevlp fvrlqhyfdi qsqpgrreni vvvshggqks
      661 glvvdellge lqtvikplgk lfnhlrgisg ssilgggdia lildipalvq saiqrelhql
      721 ghqvmghtls pssin
//
LOCUS       WP_005908853             398 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Fusobacterium].
ACCESSION   WP_005908853
VERSION     WP_005908853.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..398
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43647
     Region          1..398
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkilvincgs sslkyqlinp eteevfakgl cerigidgsk meyevvakdf ekkmetpmps
       61 hkealelvis hltdkeigvi ssvdevdaig hrvvhggeef aqsvlvndev lkaieanndl
      121 aplhnpanlm girtcmelmp gkknvavfdt afhqtmkpea fiyplpyedy kelkvrkygf
      181 hgtshlyvsg vmreimgnpe hskiivchlg ngasitavkd gksvdtsmgl tplqglmmgt
      241 rcgdidpaav lfvknkrglt daqmdermnk ksgilglfgk ssdcrdmena vkegderail
      301 aesvsmhrlr syigayaaim ggvdaicftg gigenssmtr ekaleglefl gieldkeins
      361 vrkkgnvkls kntskvliyk iptneelvia rdtfrlak
//
LOCUS       WP_005909991             192 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Fusobacterium].
ACCESSION   WP_005909991
VERSION     WP_005909991.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..192
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21761
     Region          2..151
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 miienikhtr shrrftekni kedeilemle garfsastkn aqilrysyti ddekcqklfs
       61 avslggllkn edkatleerp rgfilistkk dvktpdskly fdvgiasqni iliadelgyg
      121 acivisynkk vfeeilelpe eydskvviil geskdvvkli dskdekdtky fvengvhyvp
      181 klklgdlilg kk
//
LOCUS       WP_005910033             176 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Fusobacterium animalis].
ACCESSION   WP_005910033
VERSION     WP_005910033.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium animalis
  ORGANISM  Fusobacterium animalis
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (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   2  (residues 1 to 176)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Fusobacterium animalis"
                     /db_xref="taxon:76859"
     Protein         1..176
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=20487
     Region          42..104
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkklmlllgv fslfslslys apdlsnndyk iimssqnmkd ekeelmdinr vseqdmlark
       61 vsksyvskim eyreitggfd kledmkrikg igdatyqkls kffkvgsepn kkmlninsan
      121 eitlkyygfs kkeikkiqky ldkndritdn iefqkivnkk tyerlkdlin ydggkr
//
LOCUS       WP_005912533             243 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Fusobacterium].
ACCESSION   WP_005912533
VERSION     WP_005912533.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 243)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..243
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=27626
     Region          55..224
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mkllkyvfsl iiyfifslsl faeinfsndf klsikkkfsd mdiklmytel clndkvsfsc
       61 fnnamhglek iedleifdns nnnllvmvdy tkpsteerlf iidlrkkqll isslvthgrg
      121 tgdlyatkfs nknnsystss gfyltgniyn gkhgeslely glekgkndna kkrtivmhsa
      181 yyankafaek ygrlgrskgc lvlptdlnak iinlisggvv lyvhtnfden keydfsklls
      241 ksf
//
LOCUS       WP_005914021             352 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Xanthomonas].
ACCESSION   WP_005914021
VERSION     WP_005914021.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..352
                     /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=38448
     Region          16..295
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mrahhltdan tapaltrdwq idaakalaia lvvlghasgm ppayklfays fhvplffvls
       61 gwvgerfghr altaasvvkl artllvpyla ffmvayalwl ltaaidghag hpqtrpwwhp
      121 ltgllwangs rlyvlpalwf lpalfvttla yialrarlsa aavatislpl alawagwfps
      181 lqqrlplald vlpvalffia fggwlsrfad alrslraqvw alallplaal wwwlagwngq
      241 vdvnnlqfgq saaifllvsl lgtamtfcva yfirrlrwvq wigtntllil cthtlvflvt
      301 tsvvartgli arsaigtpaw alglsafaia asvpmravlv piapwmlglk rk
//
LOCUS       WP_005914191             658 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Xanthomonas].
ACCESSION   WP_005914191
VERSION     WP_005914191.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 658)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 658)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 658)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..658
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=70597
     Region          109..643
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 maardpvsst trddtatrnr plraetppad hwrrwadeva spadtavpvs aaiipapata
       61 aaaspaaava tpravaasss arvaaapapt asptsaapaa phdgednvaa dapyrvlive
      121 ddrsqalfaq svlhgagmha qvemtaasvp qaiqdyhpdl ilmdlhmpel dgirlttlir
      181 qqpgqqllpi vfltgdpdpe rqfevldsga ddfltkpirp rhliaavsnr irrarqqalq
      241 qageqvsvrs npetglptrg hvmdlladal erkqsgglff ieiasalglr erygyaayer
      301 lmtqaghrla saaqpyplar lndnsfllla vdmpeasleq qaleirqrls anafpvreee
      361 svhvrcaigv aplglgfddt gsaleavert alqarlrsdg vqtylapsqa eqqeqlrlve
      421 gqlelayqpi vavaggdtaq yqvllrlrqa dgtllsagqv ipaaeaagri adldqqvmdh
      481 algllhlyqh aspplrlfvs qsprtlarda fadwllkalv ergvagqsli vdlrlddali
      541 havtvqqfca klmpagvqfc lsqfepgdea nallaqlpls fvrmanrfad ahgnaavrde
      601 lrgvidiahq rglliigqri edpqaaaamw msgvdfiqgn lvqtvgkeld fdftsavl
//
LOCUS       WP_005914479             212 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Xanthomonas].
ACCESSION   WP_005914479
VERSION     WP_005914479.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 212)
  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 212)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 212)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..212
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22828
     Region          1..200
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Region          93..119
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(95..96,99..100,102,126,129..130,133..134,136..137,
                     155,158..159,162..163,166)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          124..151
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          154..181
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 maiddlldeh eqgervrswl rkngaglvgg vllglalilg wqwwqtrtnt alveangryd
       61 avvksiqakd ldkaakdiva lddgkggiya elaalrlaka qvdagknaea iktlrdvpae
      121 gelkqivqqr larlltesgk pdeaikllad aqdhasleir adalvvqgkp dearalytka
      181 lttvdvaspq rrlletklmd vggkvpdpae qi
//
LOCUS       WP_005913333             110 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Xanthomonas axonopodis].
ACCESSION   WP_005913333
VERSION     WP_005913333.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas axonopodis
  ORGANISM  Xanthomonas axonopodis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (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   2  (residues 1 to 110)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Xanthomonas axonopodis"
                     /db_xref="taxon:53413"
     Protein         1..110
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11583
     Region          26..86
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mksftvvlks lllalllssn ayaldkvdin tasaeeldkv lmnvgrskae aivehrqang
       61 pfksaeelal vkgiglktve rnrdlievga tmapakkaak gaavkpvgrr
//
LOCUS       WP_005914743             160 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Xanthomonas].
ACCESSION   WP_005914743
VERSION     WP_005914743.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..160
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16910
     Region          8..160
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfatssltgs kpeqyaqlta qaqalvhgep drianaanla alifhslpsl nwagfyfydg
       61 relvvgpfqg lpacvripld kgvcgaaast rqsqriadvd afpghiacds asrselvipl
      121 vkgdaligvl dldspeldrf daddqrglea iaqlfvdale
//
LOCUS       WP_005900016             248 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YaaA family protein [Fusobacterium].
ACCESSION   WP_005900016
VERSION     WP_005900016.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Prahlad,J., Yuan,Y., Lin,J., Chang,C.W., Iwata-Reuyl,D., Liu,Y., de
            Crecy-Lagard,V. and Wilson,M.A.
  TITLE     The DUF328 family member YaaA is a DNA-binding protein with a novel
            fold
  JOURNAL   J Biol Chem 295 (41), 14236-14247 (2020)
   PUBMED   32796037
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Liu,Y., Bauer,S.C. and Imlay,J.A.
  TITLE     The YaaA protein of the Escherichia coli OxyR regulon lessens
            hydrogen peroxide toxicity by diminishing the amount of
            intracellular unincorporated iron
  JOURNAL   J Bacteriol 193 (9), 2186-2196 (2011)
   PUBMED   21378183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006857
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..248
                     /product="YaaA family protein"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=28899
     Region          2..245
                     /region_name="YaaA"
                     /note="DNA-binding protein YaaA associated with the
                     oxidative stress response [Replication, recombination and
                     repair]; COG3022"
                     /db_xref="CDD:442258"
ORIGIN      
        1 mkiifspske mreenifenk kiefteskfk dktniligil kekslseien imklkgklln
       61 ktykdiqdyd klkfipaism yygvsfkeln ledyseksle ylknnllils alygillafd
      121 lvkkyrldmt msiidkglyn fwkkdindyi snilskdevl lnlasgefsk lidnkkismi
      181 nidfkeekdg ayksvstysk kargqflnyl iknqianled ikkikldgys lnkdlsdekn
      241 liftrkns
//
LOCUS       WP_005914936             668 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Xanthomonas].
ACCESSION   WP_005914936
VERSION     WP_005914936.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 668)
  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   3  (residues 1 to 668)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..668
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=71073
     Region          3..661
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msmdlqrfha tffeesregl dameagllsl eegnrdpeii nsvfraahsi kggaatfgfe
       61 avaglthvle tlldelrsnk rqlesnavda mlgsvdvlra llreaehgtp adpaavkavh
      121 trlnavlage aptaaavakp keeepeawhi gftpapslfm sgndplriir elehlgplqi
      181 aarlermpgf enidpleayl awdlgligki prskiedtfa wvvddceldi rpmavpgppp
      241 slavdapaaa pvvavaaapt avaepaaaat pakaaaaeae ssirvsvdkv dalinlvgel
      301 vitqamlkqv stgldpahae qlfagldlle rntrdlqeav igvrmlpvda vfrrfprlvr
      361 dlssrlgkqv rlrtigeste ldkgliekia dplvhlvrns idhglempda rrasgkdetg
      421 titlaashqg ghivievsdd grglnrakil ekatergiav pdnptdaqvw dlifapgfst
      481 adavtdlsgr gvgmdvvrrn iqglggevql esnagsgtrv lirlpltlai ldgmtvsvag
      541 etlilplsyv lealqpaped vramagdgrv lrvrgeylpi lsltnyygfg gqqsskeslv
      601 vvvegdgqki alevdellgq qqvvvknien nyrripgvsg atilgdgrvs livdigglvr
      661 slkvpqaa
//
LOCUS       WP_005915096             404 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Fusobacterium hwasookii].
ACCESSION   WP_005915096
VERSION     WP_005915096.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium hwasookii
  ORGANISM  Fusobacterium hwasookii
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 404)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Fusobacterium hwasookii"
                     /db_xref="taxon:1583098"
     Protein         1..404
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=45952
     Region          59..222
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mkkvflffcl lllitnsyte enlvtenkte niqvaveekp qkiivdvksv ydslnikdki
       61 dysifqkayl gyvqiqnknp gvliiidytk psneerfyvl dlnkkklvys trvahsknsg
      121 leiplefsdd pnsyqsslgf fvtlgeynga ygyslrlkgl eenvnanaed raivihggdi
      181 vedeyikkfg fagrslgcpv lpysltrqii dfikhgrvlf iygndeqyid dslylsklay
      241 vfegspkniv eiekpvivqk istppttvvt tspnttivad nktvnretvi aeanitkife
      301 iikqeakytn ntnykisyte llkgaiqerv nkttdikevt enkkqneeni eenidrqeki
      361 ietpttnvss eqkkeeetki tqknerkypv evtktslgig iklk
//
LOCUS       WP_005915804             123 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: endonuclease domain-containing protein [Xanthomonas].
ACCESSION   WP_005915804
VERSION     WP_005915804.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 123)
  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 123)
  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   3  (residues 1 to 123)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..123
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14162
     Region          17..110
                     /region_name="Endonuclease_DUF559"
                     /note="Putative endonuclease; cd01038"
                     /db_xref="CDD:411708"
     Site            order(21,50,67,73)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:411708"
ORIGIN      
        1 mrtgekirfa ktlrremtaa erllwyrlrd rrllgfkfrr qcpvgpyvad facleraliv
       61 eldgsqhlda psdaareafl hrkgfqllrf wnnevlvrtd avcdaiaqrl cvarfslpps
      121 gvr
//
LOCUS       WP_005915845             300 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Fusobacterium hwasookii].
ACCESSION   WP_005915845
VERSION     WP_005915845.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium hwasookii
  ORGANISM  Fusobacterium hwasookii
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Fusobacterium hwasookii"
                     /db_xref="taxon:1583098"
     Protein         1..300
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=34154
     Region          46..212
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkkilafisl lflmvacsst ekvvssssss srgssvsrnq stvrnmgkfq vdsssyvaig
       61 kneriqfivv hytaidnaas ikelttnkvs shflvldedd nkiynlvple qrawhagasa
      121 frgrtnindt svgieivsdg iakefisdpn pyhpydhyvd ykpiqiekva qiikyvaeky
      181 nvparnivah sdiapsrkkd pgakfpwkel ydkynigawy deadkqtfmd eekfkatsir
      241 eikdelrkyg yeinrfdewd keskdvvyaf qlhfnpknat gemdletfai lkalnkkype
//
LOCUS       WP_005915872             343 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Xanthomonas].
ACCESSION   WP_005915872
VERSION     WP_005915872.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..343
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37938
     Region          1..343
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mgirihrlrk qfetfaaldn idlevrqgel lallgpsgsg kttllrimag lehadggqvl
       61 fgdedatrms vqsrrvgfvf qhyalfkhmd vfeniafglr vrrgnarwae arirarveel
      121 lalvqlqgle qryptqlsgg qrqrvalara laieprvlll depfgaldaq vrrdlrrwlr
      181 elhertgltt vfvthdqeea leladrvail nrgrieqldt pamiydkpas pfvysfvgav
      241 nripgvlahg qiqvaghalp lanaalaagp vevyvrpedl vpdqagwpat vawsqrsgsr
      301 lrlramleps gnevevelpa sagsfqpgqq vrlaarqygi fpa
//
LOCUS       WP_005915984             712 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor family protein [Xanthomonas].
ACCESSION   WP_005915984
VERSION     WP_005915984.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..712
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=76987
     Region          38..710
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 msrltllaaa cglfatgats pvlaadpapp aatsiqrlpa vqvdaarvrg vddfdlpasf
       61 tvvaadddnr rgaqvselld gipglvardr qnyaqdtqls irgfgarstf gvrgvrllvd
      121 gipasmpdgq gqlshfnvla aqrvevlrgp fsalygnssg gvlqlwsadg qpddpwrlra
      181 tygsnatvnv gaqvlgqqga vhynvaanhf dtdgfrahsh akrdsvnakl gfdlaegrrl
      241 dlvlnyldap daqdplgltr aqfnadpaqa tsvatqfdtr ksvrqsqaga iftqrlddqt
      301 lrlmayggqr sveqflaipv avqrnplhsg gvidldsnye gadarwawqg ealgrplqlt
      361 vganvdrqrq hrtgyenfvg dtlgvkgalr rdqrdevenv dqfaqlwwqw sdrwsallgv
      421 rhsdvrfesd dhyivgrnpd dsgrrdysat tpvagivfra denlrfyasv grgfetptfn
      481 elgyrsdgga glaldlgaat srnyevgskw raqsgaalef avfradtdde lavasntngr
      541 styrnigatr rqgaelswqq pigatqqlql aytfvdatvr dgyltcassg catptaavas
      601 gsrlpgvprq qlfarwqwqp aqwqlaaesv asgatvvndl aterapgyal vnleasrrws
      661 tpqgalrtfa ridnvvdrqy vgsvivndgn gryyepgpgr tytvglqwdf gg
//
LOCUS       WP_005916376             248 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Xanthomonas].
ACCESSION   WP_005916376
VERSION     WP_005916376.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 248)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..248
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=27146
     Region          20..237
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mttlpvcnac rdgqdfptai tmafqpivdv strsiyagea lvrgingesa gsilaavder
       61 nryafdqacr ikaiecaaqi alpallsinf mlnavynpeh clratlsata qygwplnaii
      121 fevseqehlt dpahllgilr tyqargmkta iddfgagyag lgllaefqpd llkldialvr
      181 gidtdrsrqa ivrhvtrmce elgiaviaeg ieqpdqyral rdlgihlqqg ylfarpqige
      241 lpkvhwpe
//
LOCUS       WP_005918187             552 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Xanthomonas].
ACCESSION   WP_005918187
VERSION     WP_005918187.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 552)
  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   3  (residues 1 to 552)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..552
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=59269
     Region          6..547
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msavpddiaa dfiveaqeil drlgeqlvsl eqapeeadql navfrgfhtl kggagflaik
       61 pmvelchaae etlgmarsgq avlqahhfda aqqsldylqa mldamgsgea vphapatlia
      121 qfdaksappv lkaapqaaaa kpvaaahgdd ahapapkaag kgaaktgaea eqtvrvdtkr
      181 ldaivnlige lvlsrnrlkt lrtrlrdeel dravstldia tarlqtavmr trmqpvskvf
      241 arfpkvardv artlskevel eligaeteld rnlvealadp lvhlvrnaid hgiespalre
      301 atgkprsghv rlsaqqegdy vsieiqddga gidperlrei arnkglidae aaarlstdec
      361 lhlifmpgfs tkaevtdisg rgvgmdvvqs rirelsgqiq iqselgrgsr fmirvpltla
      421 ilptllvqag eavyalplar vvevlhapqt slgwfdgrav ldrrshtlpl idlrrwlgvp
      481 aeqpplltvv llqagetrfg lvvdqvrgre evvikplpra lrglpgyaga tligdgrmal
      541 ildvdglrss dh
//
LOCUS       WP_005919170             110 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Xanthomonas oryzae].
ACCESSION   WP_005919170
VERSION     WP_005919170.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (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   2  (residues 1 to 110)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..110
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11551
     Region          26..86
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mksftvvlks lllalllssn ayaldkvdin tasaeeldkv lvnvgrskae aivehrqang
       61 pfksaeelal vkgiglktve rnrdlievga tmapakkaak gaavkpvgrr
//
LOCUS       WP_005919262             669 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Xanthomonas].
ACCESSION   WP_005919262
VERSION     WP_005919262.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 669)
  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   3  (residues 1 to 669)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..669
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=71257
     Region          1..669
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdmnqlmqtf laesrdlled merhlleaer gesspdavna ifraahtikg sgglfdlpql
       61 vgfthvvesv ldlvrdeals lsseliglll vccdhihalv etaadpshad pvalaaeaep
      121 llaqlqtylq rsacgvtaaa vaqgapekqs gywritlklf adalrfgnsp lklirnlrsl
      181 gsvesintdi shlpafddld peanylgfqi llrsdadraa ieevfefvre dcdleivsvp
      241 apsdaadllt aetaassapn kplaavpsaa sapgraapda aarnadarsi rvdadkldrm
      301 idlvgeliia vsstnanaqr tgdaqllesa silaglvedv resalqlrmv kiggtfsrfq
      361 rvvhdvarel gkdialvvag edteldksvv ekigdplthl vrnamdhgie padvrvargk
      421 pargtvglna yhdsgsiviq itddggglnr drilakaler gliepgrqls drdvfamife
      481 pgfstaekvt nlsgrgvgmd vvkrnitalr gtveidsaag vgttisvrlp ltlaiingfq
      541 vgvgksvfvv pldvveecve ftpdyasdyi dlrgsvlpyv rlrelfalgg ktparesivv
      601 irqgaqrfgl vvdtllgewq tvikplskvf aqvkgisgss ilgsgdvali ldvpsliqql
      661 hpnqdalaa
//
LOCUS       WP_005919528             303 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Xanthomonas citri].
ACCESSION   WP_005919528
VERSION     WP_005919528.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas citri
  ORGANISM  Xanthomonas citri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Xanthomonas citri"
                     /db_xref="taxon:346"
     Protein         1..303
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33401
     Region          20..268
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mvstpehtav lavdsrcthg egvlwceqrq alywvdisek rlwrhhpasa htrhwtlpdr
       61 pgciglmddg rvlialakai givdpdtiee dvlpfeklad veadnpltrs ndgrvdrhgn
      121 lvfgtmdehd skaargafyq fslkhglral plpgvsipns icfsldgrtm yycdsvrpqi
      181 lccdydpeta qttntrvfts ldrddaepdg siidsegylw naqwrasrvv ryrpngsaer
      241 vvqlpvkhpt csafggaald rlhvissrld hsadelarmp eagslfvcdl aiaglpetrv
      301 asa
//
LOCUS       WP_005919621             224 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Pediococcus].
ACCESSION   WP_005919621
VERSION     WP_005919621.1
KEYWORDS    RefSeq.
SOURCE      Pediococcus
  ORGANISM  Pediococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 224)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Pediococcus"
                     /db_xref="taxon:1253"
     Protein         1..224
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24982
     Region          101..224
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(168..169,173,197..200,202)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkrrfeliig laivlfvgav ftsarayqkq vrhdakvelq ksakqkalpk ssakdtglag
       61 deaptaetak astktkmnpv nwkkssqkne ypdldkhpqa ylkvsiakqr vyvmdgkkvl
      121 ytmyastgsk dsptptgtfh iqkergdffy naaskegaky wvsfkdhgiy lfhtvptdkn
      181 gkfipkeaqq lgkeaqshgc vrlsvpdakw iyknvpegmk veih
//
LOCUS       WP_005917671             161 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Pediococcus acidilactici].
ACCESSION   WP_005917671
VERSION     WP_005917671.1
KEYWORDS    RefSeq.
SOURCE      Pediococcus acidilactici
  ORGANISM  Pediococcus acidilactici
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Pediococcus; Pediococcus acidilactici group.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 161)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Pediococcus acidilactici"
                     /db_xref="taxon:1254"
     Protein         1..161
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17269
     Region          9..153
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 msktiapiii dqidalltde phpianlana aallyseisd lnwagfylyd anadelilgp
       61 fqgkvacmhi qngsgvcgta lkqqstlrva nvhefpghia cdsasnseiv iplmvekqpi
      121 gvldidspsl nrfsatdeqv lndfvatlmk hidksvlral n
//
LOCUS       WP_005919690             399 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Pediococcus acidilactici].
ACCESSION   WP_005919690
VERSION     WP_005919690.1
KEYWORDS    RefSeq.
SOURCE      Pediococcus acidilactici
  ORGANISM  Pediococcus acidilactici
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Pediococcus; Pediococcus acidilactici group.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Pediococcus acidilactici"
                     /db_xref="taxon:1254"
     Protein         1..399
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43829
     Region          3..393
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mekiiainag sstlkfklfe mpeekvissg avdrigipgs nftiktadgh ktkieqpikn
       61 heeavdlllq qllkldiikd yheitgvghr vvaggeifqd salindqvlk diedlkeyap
      121 lhnpanatgi rafkkilpdi tsvavfdtsf hgtlpeknyl ysipyeyyek ygarkygahg
      181 tshryvagqa aklmqkpled lklitlhlga gssitaikdg ksfdtsmgft plagitmatr
      241 sgdidvslvv ylmeklnikd prkmleilne ksgllglsql spdlrdilda addgnhraev
      301 avdilvndiv kyigsyatem ggldgivfta gigensvpir qkvvnrlgif naklddelnq
      361 qcgerfinqa dsaikimvip tneelaiare verfkkmed
//
LOCUS       WP_005919844             321 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pediococcus acidilactici].
ACCESSION   WP_005919844
VERSION     WP_005919844.1
KEYWORDS    RefSeq.
SOURCE      Pediococcus acidilactici
  ORGANISM  Pediococcus acidilactici
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Pediococcus; Pediococcus acidilactici group.
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
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Pediococcus acidilactici"
                     /db_xref="taxon:1254"
     Protein         1..321
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=36239
     Region          5..317
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 msktmiefrh vkkifggrtv iddlnftvke geifvlvgts gsgktttlkm inqlfvqtag
       61 dilfngqrik dydlrnlrle igyvlqqial fptmtveqni slipemkrvd keevkrrvtq
      121 lledvdldpe ryrkrcprel sggeqqrigi lralaaqppv vlfdepfsal dplvraqlqd
      181 lvlklhqkfk ntivfvthdm dealklgdri gvmkdgkllq vatpkeiaqh panefvenff
      241 satvgknlyq tevekvvrtg fgvsapstte klpviprtas ldevfqqlae hpilqvvdeh
      301 gqttgwvdrp slfkylsetv h
//
LOCUS       WP_005920832             160 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Xanthomonas].
ACCESSION   WP_005920832
VERSION     WP_005920832.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..160
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16852
     Region          8..160
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfatssltgs kpeqyaqlta qaqalvhgep drianaanla alifhslpsl nwagfyfydg
       61 relvvgpfqg lpacvripld kgvcgaaast rqsqriadvd afpghiacds asrselvipl
      121 vkgdaligvl dldspeldrf daddqrglea iaqlfvdala
//
LOCUS       WP_005922267             343 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Xanthomonas
            citri].
ACCESSION   WP_005922267
VERSION     WP_005922267.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas citri
  ORGANISM  Xanthomonas citri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Xanthomonas citri"
                     /db_xref="taxon:346"
     Protein         1..343
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37929
     Region          1..343
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mgirihrlrk qfetfaaldn idlevrqgel lallgpsgsg kttllrimag lehadggqvl
       61 fgdedatrms vqsrrvgfvf qhyalfkhmd vfeniafglr vrrgnarwae arirarveel
      121 lalvqlqgle qryptqlsgg qrqrvalara laieprvlll depfgaldaq vrrdlrrwlr
      181 elhertgltt vfvthdqeea leladrvail nrgrieqldt pamiydkpas pfvysfvgav
      241 nripgvlaqg qiqvaghalp lanaalaagp vevyvrpedl vpdqagwpat vawsqrsgsr
      301 lrlramleps gnevevelpa sagsfqpgqq vrlaarqygi fpa
//
LOCUS       WP_005922397             297 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Xanthomonas citri].
ACCESSION   WP_005922397
VERSION     WP_005922397.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas citri
  ORGANISM  Xanthomonas citri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Xanthomonas citri"
                     /db_xref="taxon:346"
     Protein         1..297
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29291
     Region          188..253
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 myvralivvl ivlnagvalw walqppsapp sappqpsgva rlellptatg aggavlpaaa
       61 htgsgsaaes astapapsts tasglasvpt patsavagps tptsaaptsa ttaaaeaprs
      121 aseaaakpan gvattaaqss papsppaaer caslgpfaar adadaalarv rgqasrasvr
      181 edkdagistf rvmlpnvgdr aaaqalvkri aaagmgdyyv iaqgedntva lgqyqsrera
      241 errqaslvga gfpaqlvpsg ngqsrwwidv rtsaatsalq gaagatrqrs ldcaalr
//
LOCUS       WP_005923230             496 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [Bacteroides].
ACCESSION   WP_005923230
VERSION     WP_005923230.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..496
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54202
     Region          4..496
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 metkflkinp adnvavaivn lpageslsvd giditlnedv paghkfalkd faegediiky
       61 gypighakma krqgdwmnen niktnlagll eytynpiqvs ldiarkdltf kgyrrkngdv
      121 girneiwiip tvgcvngiin qlaeglrret qgkgvdaiva fphnygcsql gddhentkki
      181 lrdmvlhpna gavlvvglgc ennqpdvfre flgdydqdrv kfmvtqkvgd eyeegmdilr
      241 elyakavkde rtevplselr vglkcggsdg fsgitanpll gmfsdfliaq ggtsvltevp
      301 emfgaetilm nrcrnkelfe qtvklindfk eyflshgepv genpspgnka ggistledka
      361 lgctqkcgks yvegvlsyge rlqvkglnll sapgndlvaa talascgchm vlfttgrgtp
      421 fgtyvptmki stnstlaknk pgwidfnagv ivenepmekt cerfidyiik vasgefvnne
      481 kkgyreiaif ktgvtl
//
LOCUS       WP_005924058             116 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein, partial [Xanthomonas citri].
ACCESSION   WP_005924058
VERSION     WP_005924058.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas citri
  ORGANISM  Xanthomonas citri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Xanthomonas citri"
                     /db_xref="taxon:346"
     Protein         <1..116
                     /product="HNH endonuclease family protein"
     Region          <6..102
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 sggitmpqaw lthwplpeqd qvdeltkqka mvrrsvmlnt lgnltlitgk fnsslqnaaw
       61 ankrpellky skmnltryfh gkeaddwhea airtrtehlf aqllriwpaa gktans
//
LOCUS       WP_005924535             634 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Bacteroides salyersiae].
ACCESSION   WP_005924535
VERSION     WP_005924535.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides salyersiae
  ORGANISM  Bacteroides salyersiae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 634)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Bacteroides salyersiae"
                     /db_xref="taxon:291644"
     Protein         1..634
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=71768
     Region          68..551
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 madilkhldl nsadgtqlnl dalyqiapsa ftevrddktg eisrkvnfev lrrllgdhat
       61 dgdgemyqft wvgknaarae aakptdktlr pvmedsvdwd ntkniyiegd nlevlkllqr
      121 symgkvkmiy idppyntgnd fvyhddfart aaeedieagn vdelgyrfrk ntdtngkfhs
      181 dwcsmiyarl lvarsllted gvvfisiddn evrnlrnicd evfgehnfva qlvweraysp
      241 kndakyisns hdyilmfakq iedftigrle rteeanarys npdndprgvw kpsdmsvkty
      301 naacdypitt psgkiveppa grcwslskna fferlrdnri sfgvdgnsvp cikrflselk
      361 fdgmaptsil fykevghsqe gakevvslfg dkgvfdgpkp vrllqrlitl anlkedsivl
      421 dffsgsasta halmktnsdk dtdcrfimvq lpeevsdtkk dqgyknicei gkerirraga
      481 kikadfpltt qnldtgfrvy rldesnyekv sispkeykqd qldlfannik adrtdldlly
      541 gsmlawgvrl dlplqtetvd gctiyivneg dlvacfsegi tdkvvaamae ksplrvlfrd
      601 acfkedaqki niyeqfkqal dwadndafnn irvi
//
LOCUS       WP_005924616              91 aa            linear   BCT 20-JAN-2025
DEFINITION  zinc ribbon domain-containing protein [Bacteroides salyersiae].
ACCESSION   WP_005924616
VERSION     WP_005924616.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides salyersiae
  ORGANISM  Bacteroides salyersiae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 91)
  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 10577258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Bacteroides salyersiae"
                     /db_xref="taxon:291644"
     Protein         1..91
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10373
     Region          5..89
                     /region_name="Zn_ribbon_2"
                     /note="Putative zinc ribbon domain; pfam12674"
                     /db_xref="CDD:463667"
ORIGIN      
        1 meqkfcqscg mplsdatvlg tetngsknee yccycyadgh ftvdctmdem idhcaqfvde
       61 fnkdsemkmt keeavanmkq ffpllkrwkk a
//
LOCUS       WP_005925021             349 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Faecalibacterium prausnitzii].
ACCESSION   WP_005925021
VERSION     WP_005925021.1
KEYWORDS    RefSeq.
SOURCE      Faecalibacterium prausnitzii
  ORGANISM  Faecalibacterium prausnitzii
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Faecalibacterium.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Faecalibacterium prausnitzii"
                     /db_xref="taxon:853"
     Protein         1..349
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37463
     Region          1..346
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mslevniekk ldgftlraaf tagntstall gasgcgksmt lrciagivkp drgrivldgr
       61 vlfdsaqhid lppqqrgvgl lfqnyalfpn mtveqnilcg lktekdpaar rvacaemlra
      121 mrletlakry paqlsggqqq raalarilvg kprilmldep fsaldsylre evegevgsll
      181 anfvgtallv thnrdeayrl ckemivlneg qvlragttka vfadpqsiaa arltgcknil
      241 pctpldshtv rldgwdttlr lvlpvpagct avgirahdft pcaadapnai pvkavstsen
      301 pfdwnlicts pkgtaqlwwk vgktslsaaa peppqylcaa pesimplkg
//
LOCUS       WP_005925031             805 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Xanthomonas citri].
ACCESSION   WP_005925031
VERSION     WP_005925031.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas citri
  ORGANISM  Xanthomonas citri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 805)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 805)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 805)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..805
                     /organism="Xanthomonas citri"
                     /db_xref="taxon:346"
     Protein         1..805
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=86598
     Region          18..805
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mrqwlgrlll gigllvlaas lglyllmrgs lpqldgdsal sglaapvnvq rdrlgvvtid
       61 aanqldamra lgyvhaqery femdlmrrap agelselfga kavdldkrnr vhrlrarvqa
      121 sldiatgsqr talqaytdgv naglaalrvr pwpylllrqt prawtlddsi ltglamyadl
      181 qdsdnqtela aariravvpp alaalldhqg sswdaplfgp pqgdasvpda atldlrrlph
      241 ppaaphaetp tpgsnnfavd gsltadgrai vaddmhlglr apniwfrarl ryadsnapeg
      301 kvdvtgftlp glpavvvgsn ghvawaftns yidtadfari paptpghpqa ltrhvetirv
      361 agaapvqfev reaawgpvlh vnadgsalal rwaaqlpgai rldfaqmsta gdlqaafava
      421 drsgipaqnl lladrsgria wrligarpar nagcgpsgia elatstpape tassapaeaa
      481 atpsmsgtcl pwslrsdaap alidppshrl wtannrivda qqlatlgnag ydlgaraqqi
      541 redlfakqrf nerdllaiql ddravlltrw wqllrsvveh skdpalqqia hvtrhwdgra
      601 stdsasyriv rqfrsktiea veagllapak aalgaeflpp rraqlegiiw pllqqrpahl
      661 lspavasweq llddaarsaq sdliaedaqs eprgqhtwgq rntaaichpi aralpalakr
      721 wlcmpsdqlp gdrdmprvqg pafgasermv vspgheqdgi vhmpggqsgh plspfwgagh
      781 ddwvhgrptp flptatrytl qlrpq
//
LOCUS       WP_005926319             428 aa            linear   BCT 20-JAN-2025
DEFINITION  galactokinase [Faecalibacterium prausnitzii].
ACCESSION   WP_005926319
VERSION     WP_005926319.1
KEYWORDS    RefSeq.
SOURCE      Faecalibacterium prausnitzii
  ORGANISM  Faecalibacterium prausnitzii
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Faecalibacterium.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   McAuley,M., Kristiansson,H., Huang,M., Pey,A.L. and Timson,D.J.
  TITLE     Galactokinase promiscuity: a question of flexibility?
  JOURNAL   Biochem Soc Trans 44 (1), 116-122 (2016)
   PUBMED   26862196
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Holden,H.M., Thoden,J.B., Timson,D.J. and Reece,R.J.
  TITLE     Galactokinase: structure, function and role in type II galactosemia
  JOURNAL   Cell Mol Life Sci 61 (19-20), 2471-2484 (2004)
   PUBMED   15526155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Faecalibacterium prausnitzii"
                     /db_xref="taxon:853"
     Protein         1..428
                     /product="galactokinase"
                     /EC_number="2.7.1.6"
                     /GO_function="GO:0004335 - galactokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0005534 - galactose binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0046835 - carbohydrate phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=45457
     Region          38..426
                     /region_name="GalK"
                     /note="Galactokinase [Carbohydrate transport and
                     metabolism]; COG0153"
                     /db_xref="CDD:439923"
ORIGIN      
        1 mmksistwkq eltkgahaar laalycctpd etpaqaarya avldglettf gahteaglys
       61 apgrteiggn htdhqhgrvl agsvnidmia aaapnslnql rvqsegydlc vidlddltar
      121 keeenttasl lrgeceafrq rgaklsgldv yissnvpkgs gvsssaafev lvgvilndcf
      181 mdekvspiai aqigqwaenv yfgkpcglmd qmassvgnii tidfadkanp dvepvqvdfs
      241 kaglalcild sgadhadltd eyaaipnecr avaavcggev lrdvpfetfl anipacrkqc
      301 gdravlrafh fyadndrvpq qvaalregdf daflqmvtas gdssweylqn vipagykehq
      361 evavtiaaak hylggkgavr vhgggfagtv qafvpvemla dfkanmekil gagrchvlsi
      421 rpeggavl
//
LOCUS       WP_005926422             192 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Faecalibacterium].
ACCESSION   WP_005926422
VERSION     WP_005926422.1
KEYWORDS    RefSeq.
SOURCE      Faecalibacterium
  ORGANISM  Faecalibacterium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae.
REFERENCE   1  (residues 1 to 192)
  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 192)
  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   3  (residues 1 to 192)
  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   4  (residues 1 to 192)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 192)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Faecalibacterium"
                     /db_xref="taxon:216851"
     Protein         1..192
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21294
     Region          3..188
                     /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"
ORIGIN      
        1 mgralivsag ansneyiaar lsemgysrpv iipsgaearr rmsesdfeli vvnaplpdef
       61 ghelcitave qtdagvvflv kaaqaeqlla plneqgvlll skpfttplfl qamhmaaasn
      121 hrlqrlrqen arlqdkigql rlvsrakccl vehahmteae ahrylekqam dtrrdraeva
      181 qevleeyadr se
//
LOCUS       WP_005927244             342 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Bacteroides].
ACCESSION   WP_005927244
VERSION     WP_005927244.1
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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..342
                     /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=39958
     Region          1..281
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mqsdnkritf lditkcfaif cvilghviqq tfpgdpyhds wlfqfiysfh mplfmvvsgy
       61 fmekafamsp lyflkrrsiq lllptltfsi lfilfhniiy trftdkdsin ffaylsggwm
      121 wflkylfica viayaskkif rndilaaslp tilliiltrt tifrllpflw lgyflhkynd
      181 rlfrrplvpl igsliffiff lifwkgdyda ayriiffkda vrfdmqnfii tlirlgvgaa
      241 gsiffialfk illerikggk llqlcsetgr ntlgiyciqi yllefglehi afrfnfpgav
      301 iaqlvyaiiv lilcdalvrl vnknkwtalf mlgrwthksq tn
//
LOCUS       WP_005929209             212 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Xanthomonas].
ACCESSION   WP_005929209
VERSION     WP_005929209.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 212)
  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 212)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 212)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..212
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22842
     Region          1..200
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Region          93..119
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(95..96,99..100,102,126,129..130,133..134,136..137,
                     155,158..159,162..163,166)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          124..151
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          154..181
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 maiddlldeh eqgervrswl rkngaglvgg vllglalilg wqwwqtrtnt alveangrye
       61 avvksiqakd ldkaakdiva lddgkggiya elaalrlaka qvdagknaea iktlrdvpae
      121 gelkqivqqr larlltesgk pdeaikllad aqdhasleir adalvvqgkp dearalytka
      181 lttvdvaspq rrlletklmd vggkvpdpae qi
//
LOCUS       WP_005930032             261 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Xanthomonas].
ACCESSION   WP_005930032
VERSION     WP_005930032.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  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   3  (residues 1 to 261)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..261
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29546
     Region          45..257
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 msqgdtseld hdtdhlaegd eryllrnkrq irgllrqlld qraivtmhva grdmavptav
       61 levdedddcv ildgshndas nraiegakyl lcyaqlervn irfrlekaer idrdihvafr
      121 vdlpvamyhm qrresyrlet pitdspvcti rqdaaqgnef nlqlrvidis sgglavsltd
      181 gmpllelqrt yrncilqlpd tapitlpltv csqhkqalpn gsegfrigmq fsdlprgade
      241 tiqryifrvd rqrnarksgv f
//
LOCUS       WP_005930784             322 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Bacteroides salyersiae].
ACCESSION   WP_005930784
VERSION     WP_005930784.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides salyersiae
  ORGANISM  Bacteroides salyersiae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Bacteroides salyersiae"
                     /db_xref="taxon:291644"
     Protein         1..322
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37192
     Region          156..319
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mklllfplyy fsviryyvld miryvrysgi fhkknteikf isdiimsyhv lekgltmpdm
       61 rlgfgvervn alinlcneym srgyeksncq flhaigvide yrrthqaskf emntelldni
      121 dkliqkvgsv pclnqigytk esyfkendst feyfsasrhs lrnftseeid ieilkkaill
      181 aqnapsscnr qqarvyviqd kekikqvlnc qnghrgfghl snkliiltas veeysgiger
      241 nsayidgglf gmnllyclhy ykvgvctlna yfsyktekrm rqicdvppse vflmvlacgk
      301 vpeqfkvtls krndiskilh iv
//
LOCUS       WP_005930975             123 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Xanthomonas citri].
ACCESSION   WP_005930975
VERSION     WP_005930975.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas citri
  ORGANISM  Xanthomonas citri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 123)
  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 123)
  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   3  (residues 1 to 123)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Xanthomonas citri"
                     /db_xref="taxon:346"
     Protein         1..123
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14154
     Region          17..110
                     /region_name="Endonuclease_DUF559"
                     /note="Putative endonuclease; cd01038"
                     /db_xref="CDD:411708"
     Site            order(21,50,67,73)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:411708"
ORIGIN      
        1 mrtgekirfa ktlrremtaa erllwyrlrd rrllgfkfrr qcpvgpyvad facleraliv
       61 eldgsqdlea psdaareafl hrkgfqllrf wnnevlvrtd avcdaiaqrl cvarfslpps
      121 gvr
//
LOCUS       WP_005931032             305 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Bacteroides salyersiae].
ACCESSION   WP_005931032
VERSION     WP_005931032.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides salyersiae
  ORGANISM  Bacteroides salyersiae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Bacteroides salyersiae"
                     /db_xref="taxon:291644"
     Protein         1..305
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34993
     Region          143..304
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mslkktigif lkrilplkhy kiianggiiv psyyktiied tekyldyslk dshekdmllm
       61 rkyahiidkg lhrrdiepgh sklyykllke kiekirhtpf asdptvewaq skvefyeqlq
      121 tspqsflplq gkteappicy eqlselikqr rsnrffrein lsdeiinqls glvnwaansc
      181 nkqpirlfit ntpskanecl kcckggtgfs tfipsfwvfa adsrgyvwps evylpaidts
      241 lgaqnvflaa qtlgitgtil swaqkdkeee arlrmlldip qefiiifcav mgyashnylp
      301 pqrky
//
LOCUS       WP_005931313             577 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Faecalibacterium
            duncaniae].
ACCESSION   WP_005931313
VERSION     WP_005931313.1
KEYWORDS    RefSeq.
SOURCE      Faecalibacterium duncaniae
  ORGANISM  Faecalibacterium duncaniae
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Faecalibacterium.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 577)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Faecalibacterium duncaniae"
                     /db_xref="taxon:411483"
     Protein         1..577
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=62329
     Region          2..557
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 minkkllsfd rkalhyvgln vlfqwlgmlc nvvlvmtvsr liggvfagsl tgnalwqgml
       61 lclltvpvry gltlcasdms draskdvkrt lrssiyaklt rlgagysetv atseavmlas
      121 egveqidtyf akylpqlfys llapvtlfvl lvgvharsai lllccvplip lsivavqkfa
      181 kkllanywge yttlgdsfle niqglttlki yqadgwkhee mnaqaerfrk itmkvltmql
      241 nsvtlmdlma yggaglgiis aasafakgql sltsaltill laadfflplr llgsyfhiam
      301 ngaasaekif rllsaqeped gektadpads tlalehvtfg yekertilhd vtltipqgsf
      361 vslvgesgcg kstiaailsg artategevt lggipvsewk qadrlrlltl vphnaaifkg
      421 tveanlrmar pdaaeaelwa aleqvnladf crsqsglata lheggsnlsg gqrqrlamar
      481 allhdspiyv fdeatsnvda esendimkai hslagkktvi lishrlanvv dsdciyvlea
      541 griaeqgthn dllaaqgvys rlynaqkqle dlgevsa
//
LOCUS       WP_005934011             140 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Xanthomonas citri].
ACCESSION   WP_005934011
VERSION     WP_005934011.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas citri
  ORGANISM  Xanthomonas citri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Xanthomonas citri"
                     /db_xref="taxon:346"
     Protein         1..140
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15143
     Region          3..139
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mtyfslfvvs liaatllpaq seavlvalll dggsavglvv vaslgnvlgs linwwigrea
       61 vrfqgrrwfp ikpnallraq awyrrygkws lllswmpvig dpltlaagvm replravvpl
      121 lvvakttrya vvawatlava
//
LOCUS       WP_005934505             398 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Faecalibacterium].
ACCESSION   WP_005934505
VERSION     WP_005934505.1
KEYWORDS    RefSeq.
SOURCE      Faecalibacterium
  ORGANISM  Faecalibacterium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Faecalibacterium"
                     /db_xref="taxon:216851"
     Protein         1..398
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43196
     Region          1..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkvlvincgs sslkyqlidm dgekvlckgl cerigmessm itheanghka ttpaifptht
       61 eafaevvkkm ttgegkcind vseinaighr vvhggekfka sclitdevin tlrelsplap
      121 lhnpagilgi eaarkvfgni pmvavfdtaf hstmppkaym yaipyeyyek ygvrrygfhg
      181 tshkyvayka aeyleepier lklitchlgn gssiaavdqg kvvdtsmgmt plaglmmgtr
      241 cgdldpsvvn ylkytlnitg heldeilnkk sgllgisgvs sdkrdveeaa aagnkraqla
      301 sdmlnyqikk tigsyiaamg gvdaivftgg igehdaaara kichhmdwlg iridtdknkh
      361 iqgdvceita wgakvrtlvi atdeelmiar dtkevvek
//
LOCUS       WP_005938309             171 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Gordonia hirsuta].
ACCESSION   WP_005938309
VERSION     WP_005938309.1
KEYWORDS    RefSeq.
SOURCE      Gordonia hirsuta
  ORGANISM  Gordonia hirsuta
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 171)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Gordonia hirsuta"
                     /db_xref="taxon:53427"
     Protein         1..171
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=16983
     Region          82..168
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mnadrepnrl plragamlll avavvflllg iksasdsgke spqdklagag qsaqaasets
       61 asaapssspa sssvpsenig dtkicvlnag sipglagevs eelksagfpi gtdpanlpts
      121 sitentvfya egdedaakkv aeavpggasa eerpaaftrc dgeiavivvs k
//
LOCUS       WP_005938827             331 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Gordonia
            hirsuta].
ACCESSION   WP_005938827
VERSION     WP_005938827.1
KEYWORDS    RefSeq.
SOURCE      Gordonia hirsuta
  ORGANISM  Gordonia hirsuta
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Gordonia hirsuta"
                     /db_xref="taxon:53427"
     Protein         1..331
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=36054
     Region          1..321
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msisvigank hygdfaaldd vsidipagsl tsllgpsgsg kstllraiag ldsldsgvie
       61 ingrdvsqas pqqrdigfvf qhyaafkqmt vrenigfglk irkrpkaevr kkvdellevv
      121 glefvqkryp sqlsggqrqr malaralavd pqvllldepf galdakvrdd lrrwlrqlhe
      181 evhvttvlvt hdqqealdvs driailnkgr ieqvgtpddl ydrpdnvfva sflgsvsrln
      241 gqlvrphdir igrtpemtyp pedpsldtgv vratvnrvvn lgfetrvelt aaatgeefia
      301 qitrgdqnal elaagqtvya ratvvpklas g
//
LOCUS       WP_005939995              85 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Gordonia hirsuta].
ACCESSION   WP_005939995
VERSION     WP_005939995.1
KEYWORDS    RefSeq.
SOURCE      Gordonia hirsuta
  ORGANISM  Gordonia hirsuta
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 85)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 85)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 85)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Gordonia hirsuta"
                     /db_xref="taxon:53427"
     Protein         1..85
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8825
     Region          7..85
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 maedtstvav nyfaalvdav gcereqftla dptvgglrra igwrhgdrag elaahcsvld
       61 gdrllradte vigsqvdvlp pfagg
//
LOCUS       WP_005940696             422 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Gordonia hirsuta].
ACCESSION   WP_005940696
VERSION     WP_005940696.1
KEYWORDS    RefSeq.
SOURCE      Gordonia hirsuta
  ORGANISM  Gordonia hirsuta
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 422)
  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 422)
  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
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 422)
  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   5  (residues 1 to 422)
  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   6  (residues 1 to 422)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 422)
  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 15726307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Gordonia hirsuta"
                     /db_xref="taxon:53427"
     Protein         1..422
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43933
     Region          37..>108
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          114..394
                     /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 mtstldrrat lrqtrpatgv tvrpgqgark lrntvppagv aslqlstkaa alvlrtarvs
       61 gpvfrddaaa qtglsistvn rqvsallkag lireradltp pgavgrprvp feintgeflt
      121 vgihigyavt sitthdlqhr vvgainiptp qaatpdqvvt aighsarrfa drwsgkrllw
      181 ggvamggrvy gkgvvdhprl gwtgvrvgel iaqslglpvs vashveamaa aelvvnpads
      241 ghnflyfyar emagiafsvd gtvhtpaagp ptighfptgg trlldpdktg rleeaigdsg
      301 vlraaaaagl eidsleglrn aartgnavah dilaeraevl grtvalisdi fnpdhvvlgg
      361 qaftdypeal pvvskalrat svitnrdvrv arsaitvqqk aagaaaldav yadplealsh
      421 ta
//
LOCUS       WP_005940725             372 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Phocaeicola
            massiliensis].
ACCESSION   WP_005940725
VERSION     WP_005940725.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola massiliensis
  ORGANISM  Phocaeicola massiliensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 372)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 372)
  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 372)
  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 372)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Phocaeicola massiliensis"
                     /db_xref="taxon:204516"
     Protein         1..372
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42727
     Region          244..336
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(263,282..283,306,309,317..318,328,333)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 maarfkstig liilivigii gifyflvpsa eedihmlaer vlqetiiedy hvrsntksiy
       61 srpggrkikn yqietekgie tfsfkdside hranqlvtqy llaeyspinp dtfmaifnek
      121 mkkngitdsm giiyrykgqt qysnndslsp rtaycttiqf ldaretvsvq awvnyniwti
      181 ikyiplliif yvvcvlglga lliliytyyk nkkfnakdnf iaaevkases egeaaegnir
      241 lediildtnk tkaymgskel diskqafqll llfqkgtehf vsrdeikkgl wtneyetlge
      301 mnldrrvdss inrlrkvlqd ypqykikrir gagyqlvvns nlckngsvgq vdhykiivek
      361 ilnrlrncfk cl
//
LOCUS       WP_005941875             119 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Faecalibacterium].
ACCESSION   WP_005941875
VERSION     WP_005941875.1
KEYWORDS    RefSeq.
SOURCE      Faecalibacterium
  ORGANISM  Faecalibacterium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae.
REFERENCE   1  (residues 1 to 119)
  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   2  (residues 1 to 119)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Faecalibacterium"
                     /db_xref="taxon:216851"
     Protein         1..119
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12668
     Region          47..117
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mrethllvlq kkeklflals laavvlctvl afgfavplqa aepqvlpdtt gleqyvlvdl
       61 ntadlsalct lpgvgekraq tildyrtqng pfervedaan vpgltqtivd swagmatvs
//
LOCUS       WP_005945922             428 aa            linear   BCT 20-JAN-2025
DEFINITION  galactokinase [Faecalibacterium prausnitzii].
ACCESSION   WP_005945922
VERSION     WP_005945922.1
KEYWORDS    RefSeq.
SOURCE      Faecalibacterium prausnitzii
  ORGANISM  Faecalibacterium prausnitzii
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Faecalibacterium.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   McAuley,M., Kristiansson,H., Huang,M., Pey,A.L. and Timson,D.J.
  TITLE     Galactokinase promiscuity: a question of flexibility?
  JOURNAL   Biochem Soc Trans 44 (1), 116-122 (2016)
   PUBMED   26862196
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Holden,H.M., Thoden,J.B., Timson,D.J. and Reece,R.J.
  TITLE     Galactokinase: structure, function and role in type II galactosemia
  JOURNAL   Cell Mol Life Sci 61 (19-20), 2471-2484 (2004)
   PUBMED   15526155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Faecalibacterium prausnitzii"
                     /db_xref="taxon:853"
     Protein         1..428
                     /product="galactokinase"
                     /EC_number="2.7.1.6"
                     /GO_function="GO:0004335 - galactokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0005534 - galactose binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0046835 - carbohydrate phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=45517
     Region          38..426
                     /region_name="GalK"
                     /note="Galactokinase [Carbohydrate transport and
                     metabolism]; COG0153"
                     /db_xref="CDD:439923"
ORIGIN      
        1 mmksvsawkq elsssahaar laalyccape etpaqaarye avlngldatf gphaeaglys
       61 apgrteiggn htdhqhgrvl agsvnidmia aaapntlnql rvqsegydlc viglddlaar
      121 keeenttlsl lrgeceafrq rgaklagldv yissnvpkgs gvsssaafev ligvilndcf
      181 mtdkvspiei aqigqwaenv yfgkpcglmd qmassvgnii tidfadpahp dvepvavdfs
      241 kaglalcild scadhadltd eyaavpaecr avaavcggev lrdvpfetfl aklpecrkqc
      301 gdravlrafh iyadndrvak qvaalregdf dtflrlvnes ghssweylqn vipagykehq
      361 emgvtiaaak hylngkgavr vhgggfagta qafvpvemla dfkahmeail gegrchvlsi
      421 rpeggavl
//
LOCUS       WP_005946206             127 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Blautia
            hydrogenotrophica].
ACCESSION   WP_005946206
VERSION     WP_005946206.1
KEYWORDS    RefSeq.
SOURCE      Blautia hydrogenotrophica
  ORGANISM  Blautia hydrogenotrophica
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Blautia.
REFERENCE   1  (residues 1 to 127)
  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 127)
  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   3  (residues 1 to 127)
  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   4  (residues 1 to 127)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 127)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Blautia hydrogenotrophica"
                     /db_xref="taxon:53443"
     Protein         1..127
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=14784
     Region          <39..127
                     /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"
ORIGIN      
        1 mrfaidvcks kncvalllvr selhdeiyek vfpwgvftla kptsrtalir aldwmvstre
       61 rlrnlekkal sieekmeeir lvnhakwlli sqrqmnesaa hryiekqamn rcltkrevsl
      121 eiiqngs
//
LOCUS       WP_005946716             218 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Fusobacterium].
ACCESSION   WP_005946716
VERSION     WP_005946716.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 218)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..218
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24640
     Region          39..202
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mikkvllalt lfstlsfgae rnleedyiqk myndlnlnqk veytifrkay kgymqipdkr
       61 eglltivdyt kpsnverffv ldlnkrkiay styvthgkns gltsalnfsn nknsymsslg
      121 fymtndsyvg sngyslrlkg leaginsnal srnivvhgad yaepdfieky gflgrsegcp
      181 aipttisrdv idsikdrtvl fiigndrhyy ekssyasl
//
LOCUS       WP_005946718             198 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Fusobacterium varium].
ACCESSION   WP_005946718
VERSION     WP_005946718.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium varium
  ORGANISM  Fusobacterium varium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Fusobacterium varium"
                     /db_xref="taxon:856"
     Protein         1..198
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23141
     Region          68..165
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 mnnsifhkkk krstfpkiif iiiigivffk mkidkevgke ldslnnvkiy fngfpnksfg
       61 rnlaedgynl gmkyqcvefi kryyfeyynh kmpdtygnak dfydnklkda emnvkrgllq
      121 fsnpsfkkps vgdiiifkps llnpyghvai iskvdesaie iiqqnvwkkt resfnlinin
      181 nlwyieskri igrlslpe
//
LOCUS       WP_005947123             266 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Fusobacterium varium].
ACCESSION   WP_005947123
VERSION     WP_005947123.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium varium
  ORGANISM  Fusobacterium varium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
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
REFERENCE   2  (residues 1 to 266)
  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 266)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Fusobacterium varium"
                     /db_xref="taxon:856"
     Protein         1..266
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30540
     Region          27..80
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 madkvkmegi lergygiiak kvmrdrnlnv vskaiyayic syagkgkdaf psqkllcedl
       61 viskntlgky ikelkdssyi tvvqhkekgk ftrnlytinm vlctestkis eedvkstdrn
      121 skkkidnsli gemkeeieek eewrkgnlnn apveiqeilk kynelelpvf nyrpenyill
      181 kayrelgtek lfesltlmsq sefvknnmsi naifkienlk kalngnfkdk knnqknevkk
      241 kfvkpvyedf tgdfidkiln gtlggn
//
LOCUS       WP_005947426             159 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Blautia hydrogenotrophica].
ACCESSION   WP_005947426
VERSION     WP_005947426.1
KEYWORDS    RefSeq.
SOURCE      Blautia hydrogenotrophica
  ORGANISM  Blautia hydrogenotrophica
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Blautia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Blautia hydrogenotrophica"
                     /db_xref="taxon:53443"
     Protein         1..159
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=18266
     Region          49..147
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(62,105,107,132)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(62..63,75,82,88..89,91,97..98,100,109,117)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 manedkkdfn amlhdnkdmp kfqtitdqks iekyggnkmf fappidydqv mkkipygkvi
       61 tvgkireyfa klngadftep itagifvsiv awasdqrsen ktpywrtlka ngelnakype
      121 gikvqkekle aeghtiiqkg rkniryyvkd yenslfdlk
//
LOCUS       WP_005947592             220 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Fusobacterium].
ACCESSION   WP_005947592
VERSION     WP_005947592.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 220)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..220
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24413
     Region          42..204
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mdlgkklsai figlflsvav fangtvfqak elynemklng likydvfvqg vegfnkidkk
       61 ekniltivdf slpstekrmy vldlekkell fksyvshgkn tgdlyaesfs naaesnkssl
      121 gffmteapyk gsngyslrla glekgindna mkrnivvhga dyanpeiikt sgrlgrsfgc
      181 favpedmnne iidaikgrsi iyvyadklkl akeryvslnl
//
LOCUS       WP_005947788             243 aa            linear   BCT 20-JAN-2025
DEFINITION  3-deoxy-manno-octulosonate cytidylyltransferase [Blautia
            hydrogenotrophica].
ACCESSION   WP_005947788
VERSION     WP_005947788.1
KEYWORDS    RefSeq.
SOURCE      Blautia hydrogenotrophica
  ORGANISM  Blautia hydrogenotrophica
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Blautia.
REFERENCE   1  (residues 1 to 243)
  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 243)
  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 10118537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Blautia hydrogenotrophica"
                     /db_xref="taxon:53443"
     Protein         1..243
                     /product="3-deoxy-manno-octulosonate cytidylyltransferase"
                     /EC_number="2.7.7.38"
                     /GO_function="GO:0008690 - 3-deoxy-manno-octulosonate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0033468 -
                     CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27860
     Region          2..238
                     /region_name="CMP-KDO-Synthetase"
                     /note="CMP-KDO synthetase catalyzes the activation of KDO
                     which is an essential component of the lipopolysaccharide;
                     cd02517"
                     /db_xref="CDD:133010"
     Site            order(8..10,49,76,96,98)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133010"
     Site            order(121,138,144..146,152..153,155..161,169,194..195,
                     198..200,207..210)
                     /site_type="active"
                     /note="oligomer interface [active]"
                     /db_xref="CDD:133010"
ORIGIN      
        1 mrvvgvipar ygstrlpgkp lkeicgkpml vwvyervrqa krldavyvat dderiegmcr
       61 eyripvvmts pshptganrl qevsetvkad fyvqlngdep lldpslvdaa vpesvelkea
      121 fgtniitrmh spsevmdpan ikvvfdesfk alymsrtpip ypfksiefey ykhvgilgyn
      181 kkmldfyrds vpgrfekieg idtlrfidyg kklqfieveh crtlsvdtek dlervrrime
      241 ntl
//
LOCUS       WP_005948000             191 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Fusobacterium].
ACCESSION   WP_005948000
VERSION     WP_005948000.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..191
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21330
     Region          2..157
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 milktlenvr shrsftdrpl tktelskive garlgasakn sqsirffcvs dkklcdeife
       61 qikwaaavsw npvleespra yvilcacnpl tqtsepllhf dmgiasqnml lcaaemgfgg
      121 ciigaynkke veklialpek yksyfilalg epkdkvkiva aenkdtkyyr dtlnnhfvpk
      181 lslneiiign k
//
LOCUS       WP_005948256             297 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Fusobacterium varium].
ACCESSION   WP_005948256
VERSION     WP_005948256.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium varium
  ORGANISM  Fusobacterium varium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
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   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 297)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Fusobacterium varium"
                     /db_xref="taxon:856"
     Protein         1..297
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33336
     Region          36..90
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mnssaekkek ttganeakgi ykkgygtiak kvmkdknlni iskaiyayic syagkgkdaf
       61 psqklisndl ginigtlaky tqelkdsgyi tvkghkekgk fsknlytini elnmvspctv
      121 ktdtetteyg qidtnnnnin nniktnnnsv nnntltkgks kkniektted kkeklenapv
      181 eiqqilkkyk elelpdfdyr penyillray gelgavklfe altlmsqsef vknnmsinai
      241 fkienlkkal ngnfknkvnn kkgtktefkk pvyedftgel ideilsekig diedgkm
//
LOCUS       WP_005949218             173 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Fusobacterium varium].
ACCESSION   WP_005949218
VERSION     WP_005949218.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium varium
  ORGANISM  Fusobacterium varium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (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   2  (residues 1 to 173)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Fusobacterium varium"
                     /db_xref="taxon:856"
     Protein         1..173
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=20219
     Region          39..103
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkickgmfia vmlaiissft fgeesvkpfk limsenmlek kdnlidinta skedmvsqgi
       61 gigyankiln yrektggfek leelkrikgi geatyeklsk kfkienevek nplyineand
      121 evlkyfgfek keikkireyi nknnridnnl qlmeilskkr yekykkiiky dkf
//
LOCUS       WP_005949281             629 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Fusobacterium varium].
ACCESSION   WP_005949281
VERSION     WP_005949281.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium varium
  ORGANISM  Fusobacterium varium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 629)
  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 629)
  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 629)
  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 629)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Fusobacterium varium"
                     /db_xref="taxon:856"
     Protein         1..629
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=67719
     Region          11..626
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mekssnnirn yilntivvif igfqlylali kpldpmlqnp mhlilallvi fiinpadkns
       61 gkkwmtlldi pffagivfll yytivefprl sirvqyvdiv tnldkiatvi ciiilleavr
      121 rtlgkilfif illfiiydwl gmycpgilyf kgtnmrsfte tmmlgsggif gtplytsats
      181 lfyfilfgaf fsqcgggqll idfgmkfsnk saggpakaai issglmgmis gsavanvstt
      241 gvmtipmmkr vgyaphqaga ieavastggq imppimgvga fimaemlgvp yktvafaaii
      301 palayygsvf flvtfmakke aidsdkeavt ieikdpller vymiipaivl viyiisgksl
      361 mrsgmvgift vllcnlfskf ykggkyyqtl kttantaidg vkqasniaip taacgiiigv
      421 viqsglatrf sniiaqigts hlsialmiam lgcmllgmal ptvaaylvsn ilfvpvlikl
      481 nvnplsanmf vfyfgimaqi tppvclasyt aagiagadsl ktgftgfmya lvaflvpfvf
      541 vynpelllmg tpaeiakata ilffgtylla gaisgymvap lnkfnrailf igalcmiape
      601 pitdviglvi giyiiasgli kkkkvpvna
//
LOCUS       WP_005949367             389 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Fusobacterium].
ACCESSION   WP_005949367
VERSION     WP_005949367.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 389)
  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 389)
  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
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 389)
  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   5  (residues 1 to 389)
  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   6  (residues 1 to 389)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 389)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 389)
  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 20650276
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..389
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43436
     Region          11..50
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          76..370
                     /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 mkttsvkmkt lefiknsngi sraelakeln itpagigkiv ngflkkgiik eygegistgg
       61 rkplilkine enigvilgvs laprfiqisi gdingkvlrt ikyslkkrla qkennilktv
      121 eviikrelnk nkeitiisvi mngmvdseag isifsphynw kniklkelle kkfnrrvfie
      181 ndvrgmalte kifgsckekh nfvvlnigdg vggsiflnds lykgygsmsg elghmvvkrn
      241 ssekcscgkr gcletevsni aiikkiisqi klnnysslkn vlnekgtldm ediikavkek
      301 dmltlnimne aiyltahaid giisvinpek iilfgaifks sflfkmlvne vekvtlneqn
      361 yeikvsefsd tiyelspfav vnynifrei
//
LOCUS       WP_005950672              88 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: zinc ribbon domain-containing protein
            [Fusobacterium].
ACCESSION   WP_005950672
VERSION     WP_005950672.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 88)
  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 10577258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..88
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10256
     Region          5..86
                     /region_name="Zn_ribbon_2"
                     /note="Putative zinc ribbon domain; pfam12674"
                     /db_xref="CDD:463667"
ORIGIN      
        1 mnekycqscg mpmgntdely gtnadgkkns dyciycfeng kfkddvtmne miefcvphma
       61 eahpeiteek arqmmkeffp hlkrwkkd
//
LOCUS       WP_005951872             283 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Blautia hydrogenotrophica].
ACCESSION   WP_005951872
VERSION     WP_005951872.1
KEYWORDS    RefSeq.
SOURCE      Blautia hydrogenotrophica
  ORGANISM  Blautia hydrogenotrophica
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Blautia.
REFERENCE   1  (residues 1 to 283)
  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 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   3  (residues 1 to 283)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 283)
  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   5  (residues 1 to 283)
  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   6  (residues 1 to 283)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Blautia hydrogenotrophica"
                     /db_xref="taxon:53443"
     Protein         1..283
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32478
     Region          21..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..281
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mewidclnqa iryieehlte eidyeclgka accsayhfqr mfaymaevpl seyirrrrms
       61 laaadlkctd ekvvelalky gyqsptafnr afqsvhgitp saarktevpv ksyppisfkl
      121 mikgveemny rleqkeslri vgvrrklrkk leenfeivpk mwetvaedgt vprltalmdr
      181 epsgvlgisf cqepenwnym iavssgqepp egmeeaelps rtwaifsgeg ecpgaiqele
      241 rriytewmts sgyeydqgpd velylspnpq qakfevwvpv kkk
//
LOCUS       WP_005952624             218 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Fusobacterium necrophorum].
ACCESSION   WP_005952624
VERSION     WP_005952624.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 218)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..218
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=25252
     Region          41..203
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mkkcilifll liqgmvwgde irevpvinmq evyqklslhe kldfsifqka ylgflmipnk
       61 nsdylaiidy trpsnekrff lldmvnykiv sqtyvshakn tgldtalhfs ndrnsmqssl
      121 gfyltkdtyk geygyslvle gledninsna kerkivmhgg dfaeeeylkt ygflgrswgc
      181 pvlpkseita vidklknhhv lfiagndeyy rkhtrfkf
//
LOCUS       WP_005958336             580 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Fusobacterium
            necrophorum].
ACCESSION   WP_005958336
VERSION     WP_005958336.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 580)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 580)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..580
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=65286
     Region          2..556
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 miekqlyrfc getqkyikds vflscyrlla gigfsflfak lltdileknw ttnlflvmgg
       61 mliiilvkqw cmrkvasklg flvsevkenl rraiyqkvlr lgisyqetfq tqevihlavd
      121 gveqlenyfg gyltqfyycf asslilfcvi apwnvkaalv llimacsipl tlqlllrmvk
      181 qvqkkywsky asvgnlflds lqglttlkvy gtdgrreeei aelsegfrkq tmkvlkmqls
      241 siavinwiay ggtvaaviia ilayrrgdla lfgllfifml apeffipmrt ltaqfhvamt
      301 gvaaaenmmn flqkeeeksl geeeypkgsp ihvknlvyhy qdgtkaldgl nlslevgklt
      361 aivghsgcgk stfasllsge mqvgvkqifv gdtdirslka geitkhilri thdghifsgt
      421 vkenllmgnp eateemmida lekvsmwkfl qekdgldtll lsqgknvsgg qaqrlslara
      481 llhnaeiyif deansnvdie seeiilsviy elaktktvvy ishrlpsirk adkiyvmekg
      541 rvvqagkhes lyaeeglyqr mykeqeelen fqkggsheak
//
LOCUS       WP_005959553             272 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Fusobacterium necrophorum].
ACCESSION   WP_005959553
VERSION     WP_005959553.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..272
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31209
     Region          1..253
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mkvdlhihst asdgsfspkq vvqlammkkm raialtdhdt idglleakce adkwglefvm
       61 giefstywkn hevhilgyfl nledshfvqt ienlkflrek rnkkiiqllq nydiilnmts
      121 lqekypnqsi grvhiakemi kqgrvkdmke afskylaqgg layvqkeglt phmavqllke
      181 nsafsslahp kfiskdenei lqliqelkni glnaieanya gfksyeirky rswaktfdll
      241 vtggsdfhgs nrknieigmq gldysqfnkf rr
//
LOCUS       WP_005962260             374 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Schaalia cardiffensis].
ACCESSION   WP_005962260
VERSION     WP_005962260.1
KEYWORDS    RefSeq.
SOURCE      Schaalia cardiffensis
  ORGANISM  Schaalia cardiffensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 374)
  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 374)
  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   3  (residues 1 to 374)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Schaalia cardiffensis"
                     /db_xref="taxon:181487"
     Protein         1..374
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42201
     Region          249..353
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mntefvnqvh kaliittrkr rmplgerdtv kihrgvhlps tflhdlktpw eqrraisiar
       61 tlavlhrrqh aqpvarsaal lcgydifdtn psihihipqv ecksttdsal pavtldgvpi
      121 lgearchvhl heatlsaqdt efssrvltps psssalspdr aspqalspsa eeviglviqw
      181 tlidpgeeaf vftcqalrml tpsstrrlsg weqqeasirr hllrklftlp sgtrnlrrae
      241 wiirhasagc esigearllw ilqsrglagi vpqfevedsf vhyfidlaip hlkialefdg
      301 rlkygkdsee qlnvlreqiq rqkqlevrgw yvirfswadl fkpesiiqqi eeaachfrgk
      361 lkysakypvr ggvs
//
LOCUS       WP_005960268             320 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Fusobacterium
            necrophorum].
ACCESSION   WP_005960268
VERSION     WP_005960268.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium necrophorum
  ORGANISM  Fusobacterium necrophorum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 320)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Fusobacterium necrophorum"
                     /db_xref="taxon:859"
     Protein         1..320
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=36317
     Region          155..238
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mnmrkvyngi ilvliavlvi llyfnfrgnq islsdqdrml figkknlvav yedklavdip
       61 feihvnkelt fgdlvkkkey eevlrkvndi lpekiekyav vkygeieykv knakklpett
      121 idearyalas siysmfdely reantadvln qniivdvlna ngkggyarkt gelltqnlsm
      181 kynaanyekn qeesyiilnd isvdkardiv mtlpekyfki qakpvvptla nvvivlgken
      241 nlpfsisieg teanikkaas dlkkagykgv ktstktgnek sfieyqkedy fiaykiakil
      301 eiqdmvekds lsnkieihlp
//
LOCUS       WP_005963534             106 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Schaalia cardiffensis].
ACCESSION   WP_005963534
VERSION     WP_005963534.1
KEYWORDS    RefSeq.
SOURCE      Schaalia cardiffensis
  ORGANISM  Schaalia cardiffensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Schaalia cardiffensis"
                     /db_xref="taxon:181487"
     Protein         1..106
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11164
     Region          15..105
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mststhltpp vvmgeimsra devraivrah hgtgkiavfg sqvtgkatke sdidllvefg
       61 egtslldvva aeaelselfg rpvdimsfra sgyaadharr qavllv
//
LOCUS       WP_005964897             281 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Schaalia cardiffensis].
ACCESSION   WP_005964897
VERSION     WP_005964897.1
KEYWORDS    RefSeq.
SOURCE      Schaalia cardiffensis
  ORGANISM  Schaalia cardiffensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Schaalia cardiffensis"
                     /db_xref="taxon:181487"
     Protein         1..281
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30381
     Region          1..254
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mlridphths acsdgtdsps qlmveaarag ldcvglsdhd tfagwdeaea aisstgvali
       61 rgmemscaan gisvhllall pdpsnegllt cieraresra tralkmvenl sadypitweq
      121 vlafapeegp igrphiadal vaagafddrs aafvkvlhps spyyvrywap dpieavqlvl
      181 eaggvpvlah pkararqrll pesviedmke vglfgierdh rdhapedrea vdriakrldl
      241 rvfgssdyhg tgkpnrigen ltapaiidet verahlevlh p
//
LOCUS       WP_005964946             483 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Schaalia cardiffensis].
ACCESSION   WP_005964946
VERSION     WP_005964946.1
KEYWORDS    RefSeq.
SOURCE      Schaalia cardiffensis
  ORGANISM  Schaalia cardiffensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 483)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Schaalia cardiffensis"
                     /db_xref="taxon:181487"
     Protein         1..483
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=51575
     Region          88..196
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          363..482
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(435..436,439,455..458,460)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mshiapasra rsaprlligv glmlialvts aiacgayahs hegtampgvk vagedvtgmt
       61 rseiselven rfaastvtft vagksldipl vesgadides lvadaalkga tnpfsrllts
      121 vaprsvrlap tideegftal idrldalvge aplsasveld dsgtshrvip ghagrgvdre
      181 svrtalfeas esmestrvel evheiepevs teeatqaake mdalleaevs lqgpkrlhea
      241 saadkaswvg arrafgglta dvngsavrew ldgvvaaeer dpinaidevd angtllepar
      301 pgkvgidvtn ventaaelee avkkgtgfqg vltsreipfe teqrvvangp erfayrarag
      361 ekwvdvdltd stltlyqgqe riygpilinh ggvghetvtg vyhvylkfpa qdmgctpewp
      421 yceravpwvs ywhasyalhg apwveefgig tdesshgcin ipvdeakrvf dfaeigttvv
      481 thr
//
LOCUS       WP_005965235             174 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Fusobacterium periodonticum].
ACCESSION   WP_005965235
VERSION     WP_005965235.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium periodonticum
  ORGANISM  Fusobacterium periodonticum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (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   2  (residues 1 to 174)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Fusobacterium periodonticum"
                     /db_xref="taxon:860"
     Protein         1..174
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19954
     Region          41..103
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkkiigflif sclfansyav palnnndyrl imssqnmqne keelldinka seqdmlgrki
       61 sksyvskime yreitggfdk ledlkrikgi gdatyqklsk flkvgsaptk kvlninsane
      121 ltlkyyglsk keikkiqtyl dkndritdni efqklvkkkt yeelkdliny ggkk
//
LOCUS       WP_005965317             379 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Fusobacterium
            periodonticum].
ACCESSION   WP_005965317
VERSION     WP_005965317.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium periodonticum
  ORGANISM  Fusobacterium periodonticum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 379)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 379)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 379)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Fusobacterium periodonticum"
                     /db_xref="taxon:860"
     Protein         1..379
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43042
     Region          3..374
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mnkskslqvf ynekkvgtla lmknnivafe ydsnwitngf sispfslplk kqvfipridp
       61 fdglygvfsd slpdgwgrll vdrmlnsqni npreisqidr laivgetgmg alsykpeynl
      121 ledkdyqedy dnlalsckki lnteysadld nlfrlggssg garpkiltki dnedwiikfp
      181 sslddsnigk leylysvcak kckidipetk lfpskissgy fgikrfdrkk lstgairklh
      241 misvsgllet shripnldyn dlmqltlnlt ksfeeveklf rlmcfnvfsh nrddhsknfs
      301 fiynedlnkw elspaydlty sysingehat tingngvnpg lndilkvaek igldkkkaek
      361 iaieikeivk kdleiflsk
//
LOCUS       WP_005966894             298 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Fusobacterium].
ACCESSION   WP_005966894
VERSION     WP_005966894.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..298
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=34080
     Region          44..210
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkkilallsl lifmvacsss dtpvretkgi stsrrtssss igsmgkfkvd sdtyvslgrn
       61 eriqfvvvhy tatnneysik elisnrvsah flvldeddnm iynlvpldqr awhagassfr
      121 grtnlndtsi gieivsdgia rdrrndpnry ppydayleyk piqiekvaqi ikyvaaryni
      181 parnivahsd iapsrkkdpg akfpwkelye kydigawyne sdkqafmnee kfnatsisdi
      241 keelrkygye inrtnewdrd srdvvyafql hfnpknatgn mdletfailk alnkkypn
//
LOCUS       WP_005967525             188 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Fusobacterium periodonticum].
ACCESSION   WP_005967525
VERSION     WP_005967525.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium periodonticum
  ORGANISM  Fusobacterium periodonticum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Fusobacterium periodonticum"
                     /db_xref="taxon:860"
     Protein         1..188
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21344
     Region          2..150
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 miekikntrs hrkftdkkis keeilkileg arysssakns qflrysytvd dekckklfsa
       61 ialggllkle dkptleerpr ayilisakkd vnipdflqyf dvgiasqnia llanelgyga
      121 civmsynknv fkevlevped yetktvivlg eakdivklid skdendtkyf iengthyvpk
      181 lpldkill
//
LOCUS       WP_005947674             246 aa            linear   BCT 20-JAN-2025
DEFINITION  YaaA family protein [Fusobacterium varium].
ACCESSION   WP_005947674
VERSION     WP_005947674.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium varium
  ORGANISM  Fusobacterium varium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Prahlad,J., Yuan,Y., Lin,J., Chang,C.W., Iwata-Reuyl,D., Liu,Y., de
            Crecy-Lagard,V. and Wilson,M.A.
  TITLE     The DUF328 family member YaaA is a DNA-binding protein with a novel
            fold
  JOURNAL   J Biol Chem 295 (41), 14236-14247 (2020)
   PUBMED   32796037
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Liu,Y., Bauer,S.C. and Imlay,J.A.
  TITLE     The YaaA protein of the Escherichia coli OxyR regulon lessens
            hydrogen peroxide toxicity by diminishing the amount of
            intracellular unincorporated iron
  JOURNAL   J Bacteriol 193 (9), 2186-2196 (2011)
   PUBMED   21378183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006857
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Fusobacterium varium"
                     /db_xref="taxon:856"
     Protein         1..246
                     /product="YaaA family protein"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=28597
     Region          2..246
                     /region_name="YaaA"
                     /note="DNA-binding protein YaaA associated with the
                     oxidative stress response [Replication, recombination and
                     repair]; COG3022"
                     /db_xref="CDD:442258"
ORIGIN      
        1 mkiifspske mrdneilslp sspvffkekn fellkklqsf skeeiaeimk ikgklleetf
       61 eniknfdslk avsalslyng vsfknlelek yskdnieyan ntllilsafy gvlrpsdyvr
      121 kyrldmtmki dstslysfwn rivtdyiinl lqkdsdkvli nlasgeyskm ierknfpyki
      181 ididfkenkn gkfqsvssfa kqgrgsmlny liknkindae kikeyselgy slnielsdnn
      241 kfiftr
//
LOCUS       WP_005969024             326 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Fusobacterium
            periodonticum].
ACCESSION   WP_005969024
VERSION     WP_005969024.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium periodonticum
  ORGANISM  Fusobacterium periodonticum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 326)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Fusobacterium periodonticum"
                     /db_xref="taxon:860"
     Protein         1..326
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=36770
     Region          160..243
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 matkkkkkrg rapvlvlvlt aillvllfln frgnniklsk dekvliigkq nlfaiyedrl
       61 avkipyelyi dsdetvedlv strnyeqvle kinsivpekl tryiviksge ikldvenqrn
      121 ipetnigdkr filtssvyam fkdlyhekns vdeqnenilv dvlnangvgg yarktgelik
      181 tslgmkynaa nyettqdqsy vilndiskek aaeildklpe kyfkiktkst iptlanivvi
      241 igsekninfk idiygadsvl kdatdkvkkl gytdintsaa kegteqsvie ynkedyfial
      301 riakelgitd miennelvnr igvtik
//
LOCUS       WP_005970370             142 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Pectobacterium wasabiae].
ACCESSION   WP_005970370
VERSION     WP_005970370.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium wasabiae
  ORGANISM  Pectobacterium wasabiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Pectobacterium wasabiae"
                     /db_xref="taxon:55208"
     Protein         1..142
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15464
     Region          5..140
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 msefwavfsl fwssllsatl lpgssevllv tllladsakp ylliivatig ntlggltnif
       61 igrllpqpkq qaghtmamrw lqrygcaall fswvpvvgdl lcvlagwlrm pwvksavfig
      121 igkalryivl vgitlqgmaw ws
//
LOCUS       WP_005972366             188 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Fusobacterium periodonticum].
ACCESSION   WP_005972366
VERSION     WP_005972366.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium periodonticum
  ORGANISM  Fusobacterium periodonticum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Fusobacterium periodonticum"
                     /db_xref="taxon:860"
     Protein         1..188
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21462
     Region          2..150
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 miekikntrs hrkftdkkis keeilkileg arysssakns qflrysytvd dekckklfsa
       61 vslggllrle dkptleerpr ayilisvkkd lnipdflqyf dvgiasqnia llanelgyga
      121 civmsynkni frevlelsed yetravivlg eakdivklid skdendtkyf iengihyvpk
      181 lsldkill
//
LOCUS       WP_005972570             248 aa            linear   BCT 20-JAN-2025
DEFINITION  YaaA family protein [Fusobacterium periodonticum].
ACCESSION   WP_005972570
VERSION     WP_005972570.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium periodonticum
  ORGANISM  Fusobacterium periodonticum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Prahlad,J., Yuan,Y., Lin,J., Chang,C.W., Iwata-Reuyl,D., Liu,Y., de
            Crecy-Lagard,V. and Wilson,M.A.
  TITLE     The DUF328 family member YaaA is a DNA-binding protein with a novel
            fold
  JOURNAL   J Biol Chem 295 (41), 14236-14247 (2020)
   PUBMED   32796037
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Liu,Y., Bauer,S.C. and Imlay,J.A.
  TITLE     The YaaA protein of the Escherichia coli OxyR regulon lessens
            hydrogen peroxide toxicity by diminishing the amount of
            intracellular unincorporated iron
  JOURNAL   J Bacteriol 193 (9), 2186-2196 (2011)
   PUBMED   21378183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006857
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Fusobacterium periodonticum"
                     /db_xref="taxon:860"
     Protein         1..248
                     /product="YaaA family protein"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=28935
     Region          2..245
                     /region_name="YaaA"
                     /note="DNA-binding protein YaaA associated with the
                     oxidative stress response [Replication, recombination and
                     repair]; COG3022"
                     /db_xref="CDD:442258"
ORIGIN      
        1 mkiifspske mreenifenk kieftespfk dktnilidil kqksieeigs imklkadlla
       61 ktykdiqnyd klkhlpaism yygvsfkele leaysekslk ylknklfils alygfsqpfd
      121 llkkyrldmt msitdkglyn fwkkevndyi lssltknevl lnlasgefsk lidtkkinmi
      181 nidfkeekdg tyksvstysk kargkflnyl iinqidslee iekidldgys lnkdlsnskn
      241 liftrknf
//
LOCUS       WP_005973015             682 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Brucella melitensis].
ACCESSION   WP_005973015
VERSION     WP_005973015.1
KEYWORDS    RefSeq.
SOURCE      Brucella melitensis
  ORGANISM  Brucella melitensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 682)
  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 682)
  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 682)
  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 682)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Brucella melitensis"
                     /db_xref="taxon:29459"
     Protein         1..682
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=72905
     Region          16..681
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mteeqnakla pmeldevkar eleekfdsei hfrplapvaa rivgtlliil slfhyytagf
       61 gllpemihrg ihlafvlglv flvfpfsrkg ydepakpsll rplgisvidw glaiiavvav
      121 ihvplipldd lafrvgnpts tdvvlgslli lilleatrrs vgwplpiisv lfmlyalygp
      181 smpgilvhpg atvsqlvdhl ylttqgiygi algvvatyvf hfvlfgvfat riglgqlfld
      241 caawvagrfa ggpakvsifg salfgmisgs svanavtvgs ltipamirlg ykrhfaaave
      301 sasstggqit ppimgaaafl mieflnlpyt tiilaaivpa fmhffgvlmq vhfeakrtgl
      361 rgmtkeempd lkealkrdwp tiiplvvlia vllsgytpyl aafwgitlci avgllnprkr
      421 mtigevfegl rdgakyalav gaaaatvgii vgvvtltgvg fkisyivtst aaqlatyfgt
      481 ispvswfapq tltllftlvm tgmvcilmgc gipttanyii matiaapalg llgvepvvah
      541 ffvfyygvla ditppvalaa yaaagmagad pfktgntafr lglgkvlvpf vfvfspslll
      601 vtsnfnwpdf fiaffgcvig italgaalsg fflvrtkiwe nvllifaaml lvapeiyssi
      661 vglilllpvv vrhlvasrrp ay
//
LOCUS       WP_005973523             246 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Pectobacterium wasabiae].
ACCESSION   WP_005973523
VERSION     WP_005973523.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium wasabiae
  ORGANISM  Pectobacterium wasabiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 246)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Pectobacterium wasabiae"
                     /db_xref="taxon:55208"
     Protein         1..246
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=28000
     Region          14..239
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mntttlnidg kifrltaefq piihlpqnki fryealarfy nsegvlastq qtidkiekck
       61 aidevtdfmf dvvcqviknk ssmtisfnls hllfnntayl etlyqkcvmh kvspqnieie
      121 isekttrqql idgipflnqa kqygfmisld dfgagnlqvd slslfnfdti kidrsiidgi
      181 gkeetksqkl kvllnklipl gvniicegve katdlnrlnk yhpigiqgyi fyrpltfsql
      241 rllegf
//
LOCUS       WP_005974467             327 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Brucella melitensis].
ACCESSION   WP_005974467
VERSION     WP_005974467.1
KEYWORDS    RefSeq.
SOURCE      Brucella melitensis
  ORGANISM  Brucella melitensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 327)
  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 327)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 327)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 327)
  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   5  (residues 1 to 327)
  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   6  (residues 1 to 327)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Brucella melitensis"
                     /db_xref="taxon:29459"
     Protein         1..327
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36915
     Region          22..198
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          88..324
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 merhnitpgf vedalesvrq rgldtaplma aaglpqkvre pvtnvqygrl wwliaqtind
       61 effglaarpm rpgsfdllch avlhagtler alrralqfln vvlddprgel rirdgmahiv
      121 ltdaaghrpa fayraywlil mgvaswlvgr riplrtldfa cpapvhrqdy hkffgapvlf
      181 dqpatrlvfs stylalpiir sdvalenflr eapaniliry rhdhdissrv raqlnalpaq
      241 ewpsfddlak glrmsaptlr rrlkaegqsf gtikdelrfv iaqkllqekk lsiaevaael
      301 gysepsafyr afqkwvgrsp gqfrvep
//
LOCUS       WP_005975057             384 aa            linear   BCT 20-JAN-2025
DEFINITION  TerD family protein [Pectobacterium wasabiae].
ACCESSION   WP_005975057
VERSION     WP_005975057.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium wasabiae
  ORGANISM  Pectobacterium wasabiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Pectobacterium wasabiae"
                     /db_xref="taxon:55208"
     Protein         1..384
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=42113
     Region          1..384
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mnltpggnap vpnkalqvri lsgaavdasa frlfatgkvq gdtdmvfygq prnddgsvsl
       61 mheghntift idvtrlkpev qkvaftvace gsqtianlqr lniqveadne vlvngnvela
      121 grqeaalilg elyrrnndwk frfiaqgfng glqplaehfg vdvaapaaha eptpppappa
      181 tsrinlskvs ltkekpaisl ekrdnfgeir inlnwhreak asglrgmfgg sngvdldlga
      241 fvemqdghkt vvqalgnrfg dyqdepfvll kgddrtgdvs egewlhingr ewknlrqvli
      301 yafiyegvps wnktdgvvtl hipdqppiet rmtegqdsrs mcavarlvne ggsikverin
      361 qffrdhgemd nalgwgfrwk agsk
//
LOCUS       WP_005975836             258 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Fusobacterium
            periodonticum].
ACCESSION   WP_005975836
VERSION     WP_005975836.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium periodonticum
  ORGANISM  Fusobacterium periodonticum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Fusobacterium periodonticum"
                     /db_xref="taxon:860"
     Protein         1..258
                     /product="formate/nitrite transporter family protein"
                     /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=27578
     Region          6..258
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 madghktpte lvdyiikvgi dkatkplfkl mllgifggaf ialggagnii sastlvktdp
       61 gfakflgaav fpvglilvvt lgaelftsnc llsvafvnkk isfmqmirnl vivylfnyvg
      121 sfivayitvk ggsfnadsla ylqniathkv dasayalfik gilcnvlvcg aviqsytsrd
      181 tigklvgawl pimlfvligy dhsianmfyl taaklvdssl fgvsgilynl fyvtlgnilg
      241 alaiglplyf syykksdn
//
LOCUS       WP_005975837              94 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Pectobacterium
            wasabiae].
ACCESSION   WP_005975837
VERSION     WP_005975837.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium wasabiae
  ORGANISM  Pectobacterium wasabiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 94)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 94)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Pectobacterium wasabiae"
                     /db_xref="taxon:55208"
     Protein         1..94
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10792
     Region          1..76
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mgiplrrlse tinrvhgrnf sqvmneyrie eakrllsqtd aritdimles gfqtksnfnr
       61 eflrltgvsp svwrsqyplq eqatasarlp eesh
//
LOCUS       WP_005977248             229 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Fusobacterium ulcerans].
ACCESSION   WP_005977248
VERSION     WP_005977248.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium ulcerans
  ORGANISM  Fusobacterium ulcerans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Fusobacterium ulcerans"
                     /db_xref="taxon:861"
     Protein         1..229
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26674
     Region          10..>71
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mtflikkgwl enfveeikkg fgeriefigl qgshgrgeas kesdidvvvi ldklgmkdle
       61 kydeiiskme drekicgfis gkeelscwek advfqfyydt eplvgnldfi lptikksdir
      121 railvgscni yhvcghniih ekdleilfsl ykgasfvlqa kyyyetgryi kkkadllpkl
      181 seqdrkilei ymeikelent tkekflnfse elfnwasvli kehkmeeen
//
LOCUS       WP_005976983             291 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Fusobacterium
            ulcerans].
ACCESSION   WP_005976983
VERSION     WP_005976983.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium ulcerans
  ORGANISM  Fusobacterium ulcerans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
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   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 291)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Fusobacterium ulcerans"
                     /db_xref="taxon:861"
     Protein         1..291
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32931
     Region          32..79
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mdkvkmlgiy eegygvvakk vmrdktlnil skavyayics ytgkgkdafp sqnlicrdlg
       61 igkstlvkyi kelkdrgyvq hkekgkfaqn lytvnaipci vssdtvetdt nptargqvnt
      121 nnnslnnnkk nnnnikdkki nnthteveek addsaehkne iekeklsdap meiqdilkky
      181 kelglpeyny rpdnyvilgv wrelgavklf ealtlmsese fvknnmsvns ifkienlkka
      241 mngnfkdken kgkkknsskk efkrpeykdf teklidgaln gtlggnknde m
//
LOCUS       WP_005977742             251 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Fusobacterium].
ACCESSION   WP_005977742
VERSION     WP_005977742.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..251
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29016
     Region          25..208
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mvefqklspf ffpfidsdsr fagdfyydlh ihttasdsfi kpeflksfvk nkryllsvtd
       61 hneisgavel yekgigvvpg ielgcedgfe llvyfkkmad leefyvkeve qyknikrmak
      121 thrniyeyld vlqgwechks iphicgivqk nfinnkpyiy dviklvdsle thnhalslir
      181 nleaaelrer ygltatfgsd ahiireavsy ykysnmdqkn gdkvmdylyk igsvsgigqk
      241 hllhliknti l
//
LOCUS       WP_005977299             697 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Fusobacterium ulcerans].
ACCESSION   WP_005977299
VERSION     WP_005977299.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium ulcerans
  ORGANISM  Fusobacterium ulcerans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 697)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Fusobacterium ulcerans"
                     /db_xref="taxon:861"
     Protein         1..697
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=77611
     Region          11..697
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mskksigliw aalavaaygq qevdlgksvv ysttgfetem rktasnpsiv takeieekny
       61 ktvdeiladi psvnivkqgk dsiidlrgqg dkakqnvqil vdgvqmnsld tsmtatpint
      121 ispdsierie vlpgggsvly gsgtsggivn iitkkgtgrk atvgfdhgqy gsnktnvavg
      181 esfgnfdvnl aytknnakgy rdydksdsdy fqgdiryris dtqdigfkys ryeadetyps
      241 mltkeqvned rkqtgmysgk lgkeigttdt dkdeytltyn nkfsenldfn ltgfyqkttm
      301 dtkmssfaes ammdvsvwqd gkfedkkwgv kpklrysyge gsnlifgmdy innkatrysg
      361 tttlmsgkts lsettndlek etisgyvmnn yvwgnfefaq giryeranyd vgrktirssg
      421 knegvsvtsd ednfayelsa nylysdtgkt yiryergfts pppalltnkv tqagvaeyyl
      481 ndlksekydn feigvsdyig ftsfnasvfy titkdeitne masgmppawi nnynlgkter
      541 lgfelkaeqy lgkltlsqsy ayinakikdg ekgvydsngn ktgaadlsgn rianvprnkf
      601 niganyrftd nfnlgaevvy vddvylnnqn lggktnshtv anvranynfn fglslyagin
      661 nlfnekyyed vdysastgyt ydpaaernyy vgfrysl
//
LOCUS       WP_005978118             218 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Fusobacterium].
ACCESSION   WP_005978118
VERSION     WP_005978118.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 218)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..218
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24569
     Region          39..202
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mikkvllalt lfstlsfgae rnleegyikk mysdlnlnqk veytifrkay kgymqipdkr
       61 eglltivdyt kpsnverffv ldlnkrkvay styvthgkns gltsalnfsn nknsymsslg
      121 fymtndsyvg sngyslrlkg leaginsnal srnivvhgad yaepdfiery gflgrsegcp
      181 aipttisrdv idsikdrtvl fiigndrhyy ekssyasl
//
LOCUS       WP_005979484             628 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Fusobacterium ulcerans].
ACCESSION   WP_005979484
VERSION     WP_005979484.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium ulcerans
  ORGANISM  Fusobacterium ulcerans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 628)
  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 628)
  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 628)
  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 628)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..628
                     /organism="Fusobacterium ulcerans"
                     /db_xref="taxon:861"
     Protein         1..628
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=66837
     Region          12..619
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 megknknsql skillfiigl alalfhiyts yfgalpsyqh rvvhlalsmm lvplcynlfn
       61 iknekiknvf sigiiavvsv iglysysiad tmwkssgtms gleiilatil lilllsftwk
      121 tvgaampiia ilcilyalfg pnlprsiahr gytwvritev lfkgtngifn tplgvssiyv
      181 sifvifagvl easgagdifi rltqallggf rggpakvavv asslfgtisg savanvvgtg
      241 sftiplmkks gfdsefsgav etaassggql mppvmgaaaf imadyigsyq evltaaiipa
      301 ilfyialfim idlealkkdl kgqskdelpn fmeelkkgwl llmplvllvf llvgvrysaq
      361 ksaffsiifl vvimlvypgk krsvseilhl iassskgmvs valttgtagi ivgmlmltgi
      421 gyklssllis lsqgnvmlll iltmvtsvil gmgmptsaay vllatlivpa lenlgiakia
      481 ahffvfyfgi manvtppvav aaytaagiak gdamktgfva wrlslagflm pfmfcmnpal
      541 lgkgtngeii laimsaliga yglatavqry fkgnlswpkt ivvllgsvst mmpgiksdif
      601 gliclgsiya iqiikskksy degevnva
//
LOCUS       WP_005979864             386 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [Fusobacterium].
ACCESSION   WP_005979864
VERSION     WP_005979864.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..386
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=41127
     Region          <1..383
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mnflgyrrpd grvgvrnkif ilpasvcasd ttriiasqie gavtfnnqng csqvagdqql
       61 tmdvmagmaa npnvygiivv slgcencqmd lvvdairert nkpmetfiiq enggtittie
      121 ravragrkma qeasklqree fpiselivgt ecggsdptsg lasnvligel sdrlvalgst
      181 silsettefi gaehilaara ktpeikeriy eivhryekal qlvgeevrdg npspgniagg
      241 ittleekslg cihkgghtev tavydygkqv eekglvvmdt pgndpssvag mvaggaqviv
      301 fstgrgtptg npispvikit gnkitfanms dnididaspv iygpqtlkel geeflqevie
      361 vangkqtkae tlgytemaia rlcnyv
//
LOCUS       WP_005980516             324 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Fusobacterium ulcerans].
ACCESSION   WP_005980516
VERSION     WP_005980516.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium ulcerans
  ORGANISM  Fusobacterium ulcerans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 324)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Fusobacterium ulcerans"
                     /db_xref="taxon:861"
     Protein         1..324
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=36685
     Region          158..241
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mnkgigklkl iifvvgiiia lavflvinmn dgnrdldkns ryliigksnl iavyedklav
       61 kipyeinisk detvedlvkd knkeeimati nkilpekvdn ykvikfgdik lnvknaknip
      121 etnigdkryi ltsslysmfd tlytdtnran evneniivdi lnangragya rktgevlkkn
      181 lsmkynaany etfleesyvi mndiskektq evlmqldeky fkikdvpsip tlanvvvvlg
      241 keqnvdftve vvgntgtade mgkelkklgy kniknvknds kvessvieyn sedyfiayki
      301 aqkldikdmi ekdslknkim ifak
//
LOCUS       WP_005980653             238 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Fusobacterium ulcerans].
ACCESSION   WP_005980653
VERSION     WP_005980653.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium ulcerans
  ORGANISM  Fusobacterium ulcerans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
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   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   4  (residues 1 to 238)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Fusobacterium ulcerans"
                     /db_xref="taxon:861"
     Protein         1..238
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=27087
     Region          1..>236
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 miefvdinkn fgeyhiiknl smkiekgkit viigssgcgk tttlkminkl iiptsgkiyi
       61 dgedisqkdt iklrrnigyv iqqtglfphm tvkenielia kienidknkm nmrtrelmkm
      121 inldyekfse ryplelsggq qqrvgvaraf aldpaiilmd epfsavdpis rrqlqdelva
      181 iqkklektiv fvthdiqeav kiadkiclln ngeimqydtp eniiknpknd fvrkfvng
//
LOCUS       WP_005982380             286 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Fusobacterium ulcerans].
ACCESSION   WP_005982380
VERSION     WP_005982380.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium ulcerans
  ORGANISM  Fusobacterium ulcerans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 286)
  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 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   3  (residues 1 to 286)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 286)
  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   5  (residues 1 to 286)
  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   6  (residues 1 to 286)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Fusobacterium ulcerans"
                     /db_xref="taxon:861"
     Protein         1..286
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32993
     Region          22..102
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..284
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mdwifymqna idyiednlle sidyndvakr igfsnfhfhr tfallagmta neyirkrrls
       61 mageelsmsn akiidiafky gyetpesfsk afsrfhgfnp sdakksgtsl kkfsrfsikv
      121 kveggkimdy kieekgsmkf ltasksflne iinekgnrev sdfwtksfkn gtietlkkns
      181 vdsgiyglcl pvskesdsfk ygigvkstdi hnnvenfeiw tvkpsmwavf kcvgndgqci
      241 admwerifse flptspykmt eqadleyyye nnenifcelw ipverk
//
LOCUS       WP_005984630             284 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Actinomyces graevenitzii].
ACCESSION   WP_005984630
VERSION     WP_005984630.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces graevenitzii
  ORGANISM  Actinomyces graevenitzii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 284)
  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   2  (residues 1 to 284)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Actinomyces graevenitzii"
                     /db_xref="taxon:55565"
     Protein         1..284
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=27866
     Region          212..281
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mqdfirvays gdheqverpy rvamgakaal wggitlialg lliaawqlfi tssepsraqt
       61 gaktatshaq slgtarsasa asaqasarsp algpgggvts ptssggatas asggsaaggd
      121 gaagsgqivv dvdgavahpg lyklppgsrv qaalaaaggl spqadahrin raaklhdgqk
      181 lyvlsqgesa pplaasngqg cegqsctsad gadagsdaeg qglvnintan atqltqlpgi
      241 gpaiaqkiid yrtangpfts vddltkvpgi gaaklaqiks harv
//
LOCUS       WP_005985069             327 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Actinomyces graevenitzii].
ACCESSION   WP_005985069
VERSION     WP_005985069.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces graevenitzii
  ORGANISM  Actinomyces graevenitzii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Actinomyces graevenitzii"
                     /db_xref="taxon:55565"
     Protein         1..327
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=34854
     Region          89..>201
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mfrlrtalpa alalaltasl aapvgaanna pnidsnwmsd srvlsasqar qalaqlpdda
       61 papkswhgqg grlglfgpaw advdsngcdt rndilgrdlk qadysrapgi qgrtkgqgqg
      121 tsscrnatvw sgvlddpyta ktisykrgtq tsdavqidhv lplayvwahg awkwsaskrq
      181 qiandplnll avdgssnqak gacgpatcps gdsakgtwnp snsrgwwpen snyscnyarr
      241 fvsvasayql glpkadknyl skvlsncsdd gksttgnltk iikqqnpktl liagvaltiv
      301 gwlalymlrs hlsalggtkk rsrsrrr
//
LOCUS       WP_005985663             650 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Actinomyces
            graevenitzii].
ACCESSION   WP_005985663
VERSION     WP_005985663.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces graevenitzii
  ORGANISM  Actinomyces graevenitzii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 650)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 650)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 650)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..650
                     /organism="Actinomyces graevenitzii"
                     /db_xref="taxon:55565"
     Protein         1..650
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=68052
     Region          15..572
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mrgqtiptrs plgqrayrqi cvfsvvagas galsligfgk gvgapfnstv lahqvspfaa
       61 awpwlatavi fasicalsya aadyigrqna ldeesrlrvr tldhifaigh lprtgagads
      121 akttstgalv stlvdgserv skyeftflpq aisalitplv vlvlaaifid plsalelagg
      181 vavaigasla vsrltrgsaa gsrrqrsala aqyldavqgl stlvlarage ryaqrlaqrg
      241 eanrralmrl lagnqlvila tdlftsvfil masiaiaaag ldsgrldagd alalalvalv
      301 lldplnhvga ffyvgmsgra sqkaicnila tptpassapa pvpakassyq qeevdtaaif
      361 lrdvsvgwgd kdvlknvnlr velgehigiv grsgagkstl mallaghllp regygrlgpi
      421 rlrpanmsrv qrssalvsqr swlfgdtvaq nlrlakpeat teelwhalev aqldteiral
      481 pkgletmlgd sgmglsggqa qrlaiaravl anrpilllde ptsqvdlase aaiikalenl
      541 ganrtvvtis hrpaalihtd rtfkvskgrl heltprkpka kptgpaqptk aqadqllaak
      601 vsgdamttpl tsalaslaqm qkttktkkns akkptamdas sahsasgeed
//
LOCUS       WP_005985768             281 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Actinomyces graevenitzii].
ACCESSION   WP_005985768
VERSION     WP_005985768.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces graevenitzii
  ORGANISM  Actinomyces graevenitzii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Actinomyces graevenitzii"
                     /db_xref="taxon:55565"
     Protein         1..281
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30295
     Region          1..254
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mridphthss csdgtqtpaq lvasalecgl dvigltdhdt tdgwhqaaqa iegtslkllr
       61 gmeiscsyqg itlhllsylh dpdnvalnre lrrshearhe rarlmverls kdypitweev
      121 vaqtapgatl grphiadalv aagafknrse vfagplkpgs pytveryapd pvkacalvra
      181 aggvpvvahp raasrskrli pdevfarmae vglaglevyh rdhddaaraq alrlakdlgl
      241 gisgssdyhg agkpnrlgen lmpvefyerv veqgllpile g
//
LOCUS       WP_005986183             806 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Desulfocurvibacter africanus].
ACCESSION   WP_005986183
VERSION     WP_005986183.1
KEYWORDS    RefSeq.
SOURCE      Desulfocurvibacter africanus
  ORGANISM  Desulfocurvibacter africanus
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Desulfocurvibacter.
REFERENCE   1  (residues 1 to 806)
  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 806)
  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 806)
  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   4  (residues 1 to 806)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..806
                     /organism="Desulfocurvibacter africanus"
                     /db_xref="taxon:873"
     Protein         1..806
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89306
     Region          60..788
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mgkplslape rlraglqpea vpyadsrqip rrerfeppqp ralhalnlav nipgneynvy
       61 lsgeeslgrt yflrhflepv aakadvppdv lyvynfdded rpralqlppg qgrtfktdla
      121 kavallreri pgsleqdafv qrreallkty qstkddlytr medeaeskgf tlgmetegql
      181 slsprvkgkt lsleefekld setqrtlrgk rdellvamng mlrqvqaver gfteqersie
      241 refassevre klaplrgrfa sqvkvmdyla alekdvlanl erfatrpeqq pqpqpqqpqa
      301 epaqaedfcg ryeahllvdn sglkgapviv edhptyfnll gsmereselg alytdftlik
      361 pgalhranhg ylilkaddvl nspsawegll ralrsglarl edpsehseqv rtrtiepepi
      421 plqvkillvg tdeiyehlly hdsrfrklfk ikahlqshva rsegdilgfl qgcgtiiada
      481 gllpfdreal aglvdhasri vedqtklslh yplirelmie asamaklqgk dmvdaavlhe
      541 aqaardfran lyeeefmady dreiikvats gtavgrvngl svtyfgeyef glphhiactv
      601 gvgregivdl ereaelggpi htkammilks yllglfaydk plilsgslyf eqsyaevegd
      661 sasgaelaal lsalaeapie lslaftgavn qsgaimavgg vtrkiegffe vcrrrgltgr
      721 qgvlipadnv rnlmlkpevv ravddgkfsi hpvaciedal elltgipagk rgpdgtfpeg
      781 tlyrrvddrl galaraaaqf gqswri
//
LOCUS       WP_005987462             172 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Desulfocurvibacter africanus].
ACCESSION   WP_005987462
VERSION     WP_005987462.1
KEYWORDS    RefSeq.
SOURCE      Desulfocurvibacter africanus
  ORGANISM  Desulfocurvibacter africanus
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Desulfocurvibacter.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Desulfocurvibacter africanus"
                     /db_xref="taxon:873"
     Protein         1..172
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18954
     Region          7..156
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 merqnpvlta irerrsvrry tgdpvtreel lrileagrwa psglnnqpwr flviqagdar
       61 qealascsky apilrsasal icvfldream yheakdhqsa gaciqnmlla ahaldlggvw
      121 lgeiinhspq vmdalsldsr llelqavial grpahpgvss rkelaellle el
//
LOCUS       WP_005988271             799 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Xanthomonas vesicatoria].
ACCESSION   WP_005988271
VERSION     WP_005988271.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas vesicatoria
  ORGANISM  Xanthomonas vesicatoria
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 799)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 799)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 799)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..799
                     /organism="Xanthomonas vesicatoria"
                     /db_xref="taxon:56460"
     Protein         1..799
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=86148
     Region          7..799
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mrkwlarlml atvvlvlaag ltlylllrgs laqldgdtrl sglaaavsvq rdhngvvtid
       61 aksqtdamra lgyvhaqdry femdlmrrap agelsdlfgp kamdldkrnr vhrlrarvha
      121 nldtaagsqr aalqaytdgv naglaalpvr pwpylllrqt prawtlddsi ltglamyadl
      181 qdsdnqtela aariravvpp alaalldhqg sswdaplfgp ahgnavlpda aaldlrrlph
      241 ppaappaeqp tpgsnnfavd gsltadgrai vaddmhlglr apniwfrarl rypdtaaagg
      301 kvdvtgftlp glpavvvgsn ghvawaftns yidtadfari paatpghpqa ltthvetirv
      361 agaapvrldv reaawgpilh enpdgsllal rwaaqlpgai rldfaqmssa rdlqsafeva
      421 drsgipaqnl lladrsgria wrligarpar npgcgptgia elataappsa sppaqrdpqa
      481 sgctpwpvrs daapalidps shrlwtansr vvdtqqlatl gnagydlgar aqqirddlfa
      541 kqrfnerdll aiqlddrall ltrwwqllrg vvehskdpal qqieqatrqw dghasttsas
      601 yrivrefrsk tidkveagll apaqaalgeq flaprraqle givwpllqqr panllpptfa
      661 sweqllsdaa ssaqaelaaq adpgqpldtr twgerntaai chpiaralpd fakrwlcmpa
      721 dqlpgdrdmp rvqgpafgas ermvvspghe qdgivhmpgg qsghplspfw gaghedwvhg
      781 rptpflptat rymlelrpq
//
LOCUS       WP_005988796             978 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Xanthomonas vesicatoria].
ACCESSION   WP_005988796
VERSION     WP_005988796.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas vesicatoria
  ORGANISM  Xanthomonas vesicatoria
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 978)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..978
                     /organism="Xanthomonas vesicatoria"
                     /db_xref="taxon:56460"
     Protein         1..978
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=110908
     Region          160..605
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 matkktqkpg ksieqithpe akrkniptve hqsvmqqheq apvkvaypra nrhwltelca
       61 lhdgdkvspe fqqrlnrdld pqliwrgkdq qdwsdlvvna pplyiqekvk pkaliddlrr
      121 qteerreaaa pqqdtldlfg dfnglpegad rtefyqhegh wqnrfilgds lqvmaslaer
      181 eglrgkvqci yfdppygikf nsnfqwstts rdvkdgnadh itrepeqvka frdtwrdgih
      241 syltylrdrl mvardlltes gsifvqigge nlhrvravmd evfgeqnfca eiifrktart
      301 ssnllptend flvwfardke kikyrpifqk kdmtelksyk ylvssdtlva rsatvneksd
      361 assipegwkl aqlsfcvsgd pgkpedriys frgknydcga hrhwkttnpq gldnlwksqr
      421 lfglgsqlnf iryfddfsve systqwldtg sagfsnsdpk iyvvqtdslv vqrcilmttd
      481 pgdlvldptc gsgttatvse qwgrrwittd tsrvalalar arimgarypf ylladsregq
      541 lkeaeitrsv pssqptygni ahgfvyervp hitlksiann aeidviwdef qtmleplrad
      601 lnkalgkhwq eweiprdada kwseaakklh vdwwqqciar qkeidasiva kaefeylynk
      661 pyedkkkvrv agpftvesls phrvlgvdee delidhvaet qaqygqdfas lilanlrtag
      721 vqqahkadki eftslepwpg dlicaegryl engqvkragi lvgpefgtvt radlvdaare
      781 agdanfdvli acafnydapa sefsklgrih vlkarmnadl hmaedlkntg kgnlfvifge
      841 pdvdvldtqg rsirrydgkr dvievpadeq lvvringvdv fhpstgevrs dgadgiacwf
      901 ldtdyneesf fvrhayflga ndpykalktt lkaeidpdaw atlnsdtsrp fpkpsngrfa
      961 vkvinhlgde vmkvfkvn
//
LOCUS       WP_005989374             438 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin
            [Desulfocurvibacter africanus].
ACCESSION   WP_005989374
VERSION     WP_005989374.1
KEYWORDS    RefSeq.
SOURCE      Desulfocurvibacter africanus
  ORGANISM  Desulfocurvibacter africanus
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Desulfocurvibacter.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 438)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 438)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Desulfocurvibacter africanus"
                     /db_xref="taxon:873"
     Protein         1..438
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48563
     Region          5..416
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mstengayvf vwrsggfvpa gvlymveege evlqcrfqye pdylrrkdav pldpmslpls
       61 vgdaildspt gfrifpsfld qmpdawgqrv lgavaaekni pltyfdlivs gakdrigala
      121 ygdtpdgprw dyplqpgfme iaeldletll eaaerfqaqg fhdlpricke ylatgssvgg
      181 arpkslcmhr grhavakfka agddfnvcrv eyatmrlaga lglrvpevsl vsldngqsnr
      241 difiverfdr sgndrvhiis aatairastg lvklgtysyq divqalnvhg spshlqadrm
      301 elfrrmvfnm lvaneddhlr nhsflhdgtg wrlsplydvv pgfhgprhly lsagtqgglm
      361 slsnalskce afglyrkqak divgelvagf mdswenifle sgvppadmsq lrrlfdcarl
      421 adretdpear ellprqrn
//
LOCUS       WP_005989411             270 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Desulfocurvibacter
            africanus].
ACCESSION   WP_005989411
VERSION     WP_005989411.1
KEYWORDS    RefSeq.
SOURCE      Desulfocurvibacter africanus
  ORGANISM  Desulfocurvibacter africanus
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Desulfocurvibacter.
REFERENCE   1  (residues 1 to 270)
  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 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   3  (residues 1 to 270)
  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   4  (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   5  (residues 1 to 270)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Desulfocurvibacter africanus"
                     /db_xref="taxon:873"
     Protein         1..270
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30124
     Region          11..270
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <160..267
                     /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 mkpshnvrvw rdhdvpglev slvranshaf prhahdyysi glmehgggyy ldqcddcfil
       61 pgeialinpg qvhtgvpprg mrngyrmlyv ntewmrrlaa dlgrqgypef thwivglprv
      121 rdmllrltcl vadggellak esamvaafsl lmashatmrp slpgpggepe avrrakehlh
      181 arldgkvsle elaaetglsr yhllrvfkaa tgmspyayhl qlrveharrl llnglpfvqa
      241 aseagfsdqs hfsntfrhff gmtpgqylar
//
LOCUS       WP_005990633             547 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Solidesulfovibrio fructosivorans].
ACCESSION   WP_005990633
VERSION     WP_005990633.1
KEYWORDS    RefSeq.
SOURCE      Solidesulfovibrio fructosivorans
  ORGANISM  Solidesulfovibrio fructosivorans
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Solidesulfovibrio.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 547)
  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   3  (residues 1 to 547)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Solidesulfovibrio fructosivorans"
                     /db_xref="taxon:878"
     Protein         1..547
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=57934
     Region          3..532
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mveddkilel faescleqls gieaaildle sagpdalgpk vaavfraaht ikgdagavga
       61 anlaelahav esvldavreg rlpvtrglig ellavfdvik tmveapvags rrdvapemar
      121 maalleqheq ppaqpsqpve etapgeakad erirklaida reldilvdrv gelgiaqarl
      181 aalsarrpde elrdvaeeve rlaallrdqv lglrllpiki sfpkyrrlvr dtcatlgkda
      241 elvmdgente ldkavieqln tpcihllrna vdhgieppda rqalgksrrg tirlaarqdg
      301 ndvviaiadd gagidaaklw rkavaagrip pdrpydahaa leliflpgls tadrvgavsg
      361 rgvgmdavre gidalrgrie vastpgagsv ftirlpvsla iidclevrlg aetyylhldy
      421 veeclelppa tamhrgrgvm elrgepmplv clrhffglpg ptpetshvvt lrrdegragl
      481 vvdgvvgrkq avlkhlgral gkvagvlgat vtedgdmalv vdvpgllhaa laedkgtgdn
      541 aaatgis
//
LOCUS       WP_005991788             160 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Xanthomonas vesicatoria].
ACCESSION   WP_005991788
VERSION     WP_005991788.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas vesicatoria
  ORGANISM  Xanthomonas vesicatoria
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Xanthomonas vesicatoria"
                     /db_xref="taxon:56460"
     Protein         1..160
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16839
     Region          8..159
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfatssltgs kpeqyaqlta qaqalvhgep drianaanla alifhslpsl nwagfyfydg
       61 relvvgpfqg lpacvrisld kgvcgaaatt rqsqriadvd afpghiacds asrselvipl
      121 vkgetligvl dldspeldrf daddqhglea iaqvfvgalt
//
LOCUS       WP_005992235             275 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Solidesulfovibrio
            fructosivorans].
ACCESSION   WP_005992235
VERSION     WP_005992235.1
KEYWORDS    RefSeq.
SOURCE      Solidesulfovibrio fructosivorans
  ORGANISM  Solidesulfovibrio fructosivorans
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Solidesulfovibrio.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (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   5  (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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Solidesulfovibrio fructosivorans"
                     /db_xref="taxon:878"
     Protein         1..275
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30490
     Region          13..272
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <154..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 mprraasfap ellrrredpd lpglvarlaa yrrrafsrhi hdawcvglil sgatrvrrag
       61 cirritaget aliapgepha cnpepdgrla yvmfflerea vrlvgvgdep afraplvrdp
      121 vvaarlsgly ramtarrdrl ekqsllclal aplfsrtehl pgppgrgltr vrdylrehwr
      181 dkvsladlav laghspshvl rlfkreyglp phayqnflrv erakallagt dlpaaavaqe
      241 tgfadqshli rtftpqvgat pnqyrlslrr srpga
//
LOCUS       WP_005995262             727 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Solidesulfovibrio
            fructosivorans].
ACCESSION   WP_005995262
VERSION     WP_005995262.1
KEYWORDS    RefSeq.
SOURCE      Solidesulfovibrio fructosivorans
  ORGANISM  Solidesulfovibrio fructosivorans
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Solidesulfovibrio.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 727)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Solidesulfovibrio fructosivorans"
                     /db_xref="taxon:878"
     Protein         1..727
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76952
     Region          27..655
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mqqtvspake ggsggaaayr krilhgvmag vvgltaawll sltgivtsfe artfdwrarl
       61 laprdggsda vrlilldqps ldwaakengl swpwprevyg aildfcrrgg akavafdvly
      121 tepstygvad dtafaaagkk lgnfalpvfl gretgktnvw padvppdpla ikglkawldk
      181 vpvneapvyp kaafpvpeva agakilgnvs qdpefdgiyr rvnlfgifdg kavpslplaa
      241 rmlvepnlda aiaghalrlg pvtvplddag raiprwrrss dfpavsaaav irseltlleg
      301 gkpaldpnif rgryvlfgfs apglldlrps pvagvtsgve ihaqtlqsll tgdflrviph
      361 wagwwlaggl avvaglavtl ttgamagagv iilflplpll ialaayamgs wlplalpqla
      421 vagslvtavl igyategrqk rfiksafrqy lspdvieali ahpermslgg elreltiffs
      481 dlqgftgise gmtpqeltal lnkyltamtd iileeggtvd kyegdaiiaf wnapldqpdh
      541 aaravraalr cqdkltelrp afrersghdl hmrvglntgq avvgnmgsds rfdytmlgda
      601 vnlasrlegi nkqfgtytmi skatrdaagd afasrrlgrv avvgraepvd vyeplwpaaa
      661 aslaathday aaalaafiag dfqaalagft alaaadpaaa syvkrceali asppagewng
      721 vlvmtsk
//
LOCUS       WP_005997044             725 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Solidesulfovibrio fructosivorans].
ACCESSION   WP_005997044
VERSION     WP_005997044.1
KEYWORDS    RefSeq.
SOURCE      Solidesulfovibrio fructosivorans
  ORGANISM  Solidesulfovibrio fructosivorans
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Solidesulfovibrio.
REFERENCE   1  (residues 1 to 725)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 725)
  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   3  (residues 1 to 725)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..725
                     /organism="Solidesulfovibrio fructosivorans"
                     /db_xref="taxon:878"
     Protein         1..725
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=78021
     Region          28..713
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mseidpsigi yveetrellg elerglldle kdpgdmervd acframhtik gggamfgfee
       61 isrfthdvet vldrvrsgel pvtselltlt laakdhilal leapippgpe llaasdalle
      121 sfaaflphkg aaaakapvea ttgaqasdla cdteedvcya cepqpgppgi ywvrfrpspl
      181 ilhsgndpar lladldsvgi vrtlrhgpmp dldasdfnpe evygvfdmli rtpctpntlr
      241 dvfifvedds ditieyihqg nlrgddlrdl lhallgldaa ptdavldals ralanklssi
      301 saakakaeag raqavraeng kkrhgattgs ttlrvdaarl dsvvsmagel vilqsrlrqa
      361 vqardidaaa avdedlerlt damrdvalgl rmlpigtvfs qftrllrdls aslgksvefe
      421 alggdteldk tvidrikdpl ihllrnsldh gvespserqa agkpekgrit lsashsggnv
      481 viaisddgkg idpvgirnka vekgliapds dlpekavfel ifapgfstaq kisdisgrgv
      541 gmdvvkrnie alrgsvevds vlgqgttvti klpltlaiid gfsvvvgrds fivplvtlrg
      601 fqerfpagdv rtvenmermg elipvvslrk lfsvpgsqpg yervviteve gdmvgfcvdk
      661 vvgrqqavik slddcyrhlk wisgttingd gsislildvp qlvrfvreqe dsrlhavkas
      721 rtlaq
//
LOCUS       WP_005997647             201 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Desulfuromonas acetoxidans].
ACCESSION   WP_005997647
VERSION     WP_005997647.1
KEYWORDS    RefSeq.
SOURCE      Desulfuromonas acetoxidans
  ORGANISM  Desulfuromonas acetoxidans
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Desulfuromonadales; Desulfuromonadaceae;
            Desulfuromonas.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Desulfuromonas acetoxidans"
                     /db_xref="taxon:891"
     Protein         1..201
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22534
     Region          18..165
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 msdctlnncd frgliektrn yhyfvesekv teemlrelvd yarlapstsn lnlqplryli
       61 aceeerneki fetlswqgyl rgwggpikgv kptgyiivlg dktvcssyva dqgiaaqsil
      121 lgdtnkglgg ciaakvqrrk lrealdlptr yeillviaig kpgeeivleh qepgadaygw
      181 hddqgnyhlp krsldsiilk y
//
LOCUS       WP_005998164             227 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Desulfuromonas
            acetoxidans].
ACCESSION   WP_005998164
VERSION     WP_005998164.1
KEYWORDS    RefSeq.
SOURCE      Desulfuromonas acetoxidans
  ORGANISM  Desulfuromonas acetoxidans
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Desulfuromonadales; Desulfuromonadaceae;
            Desulfuromonas.
REFERENCE   1  (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   2  (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   3  (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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Desulfuromonas acetoxidans"
                     /db_xref="taxon:891"
     Protein         1..227
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26077
     Region          14..70
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msnllvnavw qlplprtakm tflaladqat degycfpsvv tiaeragftg knkeracrkv
       61 iadlrrenwl ttepryrqdg grtsngyqln tsklldiyrd yldqkksrkm irkgdakvhd
      121 nhaakleidd yvrlavkhkk yssvnddpda fqakikrrla sqgdlsaidr kqlyrwrese
      181 kkkllesatr kqpelqnkgi tdselkkgrs qirkimkqia genndlh
//
LOCUS       WP_006000259             774 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Desulfuromonas acetoxidans].
ACCESSION   WP_006000259
VERSION     WP_006000259.1
KEYWORDS    RefSeq.
SOURCE      Desulfuromonas acetoxidans
  ORGANISM  Desulfuromonas acetoxidans
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Desulfuromonadales; Desulfuromonadaceae;
            Desulfuromonas.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 774)
  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   3  (residues 1 to 774)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Desulfuromonas acetoxidans"
                     /db_xref="taxon:891"
     Protein         1..774
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=85105
     Region          11..106
                     /region_name="HPT"
                     /note="Histidine Phosphotransfer domain, involved in
                     signalling through a two part component systems in which
                     an autophosphorylating histidine protein kinase serves as
                     a phosphoryl donor to a response regulator protein; the
                     response regulator protein is...; cd00088"
                     /db_xref="CDD:238041"
     Site            order(51,54..55,70,73)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238041"
     Site            51
                     /site_type="active"
                     /db_xref="CDD:238041"
     Region          <101..>227
                     /region_name="FimV"
                     /note="Type IV pilus assembly protein FimV [Cell motility,
                     Extracellular structures]; COG3170"
                     /db_xref="CDD:442403"
     Region          195..773
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mtdelssdqi eiiqefvqes qdmieqlept iielgqttdn etinavfrlf hsmkgsagfl
       61 efnhitsvah aaeslldlvr sgkmslqpeh vtllceccdf tkealetvde hftdeamakq
      121 geamatrfhe amdsdsaapa deepvtqepq tvpepeaqae tvpqpqpesa seadaeeidp
      181 skieatddlt leitpemver fvqeadelle taeqsllewe kepdsqdhva lifrsihsfk
      241 gnsgffgygt leklshqien vldvvksggs fatenpfevl lnsvdalkdg lnaltedgrd
      301 dideidslid alkalpspri gevlvdkgvv deetvnaaln qqkkplgdvi vdmgkatkeq
      361 vdealttqtq tkkpaapapr akpkgsaikr qdirvdlekl dnlinligel viaenmlihn
      421 pdlegleles fnkaaqqmgk lvrelqemam iirmipvsgl frrmirlvhd lsvksgkkvd
      481 lklsgestev dktvietitd plvhilrnsm dhgleppder iaaekdetgv irlnacheeg
      541 evwitleddg rglnkekila kaitnglieg dgsdltdkei ynlifqpgfs tadkitdisg
      601 rgvgmdvvkq nlekikgkvd vdsipgkgtk iklripltla iidgmlvrvg tarcivpils
      661 ikeafrpqpd aitvtpdnee lvrvrenffp vvrlhellet tpehsdlvda ilivleyqgr
      721 siclmvdeim gqqqtvikgl seyignvrgc sgctilgngd vslildvgnl vemk
//
LOCUS       WP_006001422             805 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Desulfuromonas acetoxidans].
ACCESSION   WP_006001422
VERSION     WP_006001422.1
KEYWORDS    RefSeq.
SOURCE      Desulfuromonas acetoxidans
  ORGANISM  Desulfuromonas acetoxidans
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Desulfuromonadales; Desulfuromonadaceae;
            Desulfuromonas.
REFERENCE   1  (residues 1 to 805)
  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 805)
  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 805)
  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   4  (residues 1 to 805)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..805
                     /organism="Desulfuromonas acetoxidans"
                     /db_xref="taxon:891"
     Protein         1..805
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89523
     Region          72..798
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 msitplaadd lkwlccdqqf efdstkqlng ldgpigqera maaielslam pndgfnlfit
       61 gqtgtgrtsa irqileerak gepvpddwcy vhdleqgasp vafsvphglg kqlqedmael
      121 irrlseqlpk lfkskeyeqy kgktteefql kskklledle qeaaeqgfei qrsvsglvlv
      181 pakdgealtq aeydaldees rkeidqkggk lqkilngvla qtreiesevq qavskmeeqi
      241 vdmttshlfa elmdhyqdyd evvehldrcr rdivnnvsef rprkerqlif sggedlserf
      301 wsrfevnlli dnqalegapv vfennptyfn lfgriehvfr mgnattdftm ikagalhran
      361 ggylvlncrd llmnyfsyea ikrclrrgdv viediaeqar lismaslkpg pipfsgkivl
      421 vgdahlynll hhfdpdfgkf fkiradfnss idntwdnvtr yaqfiavqcr dhdlphfepg
      481 avsrvvehaa rltedqnkls skfldladli keagfyahqq grekvaaqhv llalesrryr
      541 nnriedelrr livegtimvd fagavvgqin glsvymqgdy qfglptrita ttsigrggvv
      601 averevkqsg avhdkgvmil sgffaqrfgq nkpltfsasl cfeqtyggvd gdsasstely
      661 alisslsgls lrqdiavtgs vnqhgqvqai ggvnekiegf ftlcnivglt grqgvmipra
      721 nvknlmlngd vvaacrdgrf hvwavstide glelltgtpa gefvdgqwse gsvnarvdqr
      781 lttmvetlma fakkndaate nhsgs
//
LOCUS       WP_006001648             192 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Desulfuromonas acetoxidans].
ACCESSION   WP_006001648
VERSION     WP_006001648.1
KEYWORDS    RefSeq.
SOURCE      Desulfuromonas acetoxidans
  ORGANISM  Desulfuromonas acetoxidans
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Desulfuromonadales; Desulfuromonadaceae;
            Desulfuromonas.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Desulfuromonas acetoxidans"
                     /db_xref="taxon:891"
     Protein         1..192
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21945
     Region          2..156
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mlkdlllrnr syrrfhadka iseeqltelv eltrycgcva nlqplrylls vdkerndrif
       61 nylgwagylk dwkgpaener psgyiviigd ktisdrfdgd sgiaaqsill gavekglggc
      121 migsiqkqkf reefkiptrf eivmvialgy paeevrlvdk eesgdikywr desgvhyvpk
      181 rtmdhlvlsw in
//
LOCUS       WP_006001677             702 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Desulfuromonas acetoxidans].
ACCESSION   WP_006001677
VERSION     WP_006001677.1
KEYWORDS    RefSeq.
SOURCE      Desulfuromonas acetoxidans
  ORGANISM  Desulfuromonas acetoxidans
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Desulfuromonadales; Desulfuromonadaceae;
            Desulfuromonas.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 702)
  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   3  (residues 1 to 702)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Desulfuromonas acetoxidans"
                     /db_xref="taxon:891"
     Protein         1..702
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76471
     Region          30..702
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          <242..>299
                     /region_name="nfrB"
                     /note="phage adsorption protein NrfB; PRK11234"
                     /db_xref="CDD:236884"
ORIGIN      
        1 mqdapqnafk eeayellsel edslleleeq pddhetiskv framhtikgs gamfgfttis
       61 efthevetvf dlvrngelpv tkqlvdlslk ardhilalld cdaeeqggya aqgadlvaqf
      121 qalagggsap atlaasvada dnadtkndyt tyrirfrpsl dimhngtsia qlldelaelg
      181 tcrtiahkan vraldelnae dcyaswdiil tsdcgedair dvfifveddc eliikaidlg
      241 sdedgmdrkr lgdilierge isqaeiddvl ahnkrigdll veanlvsrdq vdsalleqqe
      301 irklkekkke ksqgasslrv padklddlvn lvgemvtvqs rlsqvanqrh dadllsiaee
      361 verltedlrd stlnirmlpi gstfskfkrl vrdisadlgk evelkttgad teldktvieq
      421 lgdplvhiir nsmdhgiemp ddrvaagkpr tgqvhlsaeh sgdsviinis ddgkgmdpev
      481 irqkaiskgv igaddqlsht dllnlifapg fstaqqvtgl sgrgvgmdvv kraieslrgs
      541 itldsqkgqg stvslriplt laiiesllvq igdgryvlpl saveecielt aqdihdshgr
      601 nlakvrghlv pyvplreefa idgnrpavqq ivitqingqq lgfvvdnvig ehqtvikslg
      661 pmyrdvqcvs gatilgdgsv alildivylm qkaseegrvs qp
//
LOCUS       WP_006002949             716 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Glaciecola punicea].
ACCESSION   WP_006002949
VERSION     WP_006002949.1
KEYWORDS    RefSeq.
SOURCE      Glaciecola punicea
  ORGANISM  Glaciecola punicea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Glaciecola.
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Glaciecola punicea"
                     /db_xref="taxon:56804"
     Protein         1..716
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=79029
     Region          8..716
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mkrttlakav iaalisplsv saiaddtlal esnieqikii gsksqarkia gssayidqaq
       61 itveastdin qlmktipgvy ireedgeglr pnigiraasa grvskvtlle dgvmmapapy
      121 snpaayyfpt afrisaievl kgapllrygp qttggvinlv stpvpvkfgg evltqfgens
      181 srdihafvgg tngqfgalie tvqrssdgfk nidrsqrdag fniedyvakl ewtgdqssll
      241 akiqyseets netylgladv dffqdknrry glseidrmdn shnsytlnyn ydinneisin
      301 vlgyynefsr nwfkldggnn yvnaansgda ealailrgel detglnyknn nrkyeskgie
      361 fnvrwsldah diefgirdhs ddmdrfqpvd iydqingsll ftgtkaptgs nnrlegadat
      421 sfwitdrwqv tqalnlnlml ryedvesfrn qfadvertai astranstde llpgvsftyd
      481 innewqvlgg mhkgfsplgg gakanqepet snnfevgary nanalfaeai ifysdfsdtt
      541 qicsianpcd ngadsgsyvl geslvsgief hvsnsftyes flipvdfayt ytkgeisndn
      601 ttaglfdgde lrdipqnvfs lrlgldnneg wanyvvakym demcvsvgcn rgnsefdkte
      661 slfvtdfisr fdvnndmtvf lkiqnlfdeq nivarsphga rpnkpqtasi gleysf
//
LOCUS       WP_006003354             182 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Desulfuromonas acetoxidans].
ACCESSION   WP_006003354
VERSION     WP_006003354.1
KEYWORDS    RefSeq.
SOURCE      Desulfuromonas acetoxidans
  ORGANISM  Desulfuromonas acetoxidans
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Desulfuromonadales; Desulfuromonadaceae;
            Desulfuromonas.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Desulfuromonas acetoxidans"
                     /db_xref="taxon:891"
     Protein         1..182
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20281
     Region          3..170
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 melfdaiclr hsyrgpmept pvpredleri vgagirapsg knaqttqfii iddqevlsvl
       61 qglhpankam qqapamiaci idtqpdkiye gydfqledca aatenmllai talgyasvwi
      121 dgwlrvegra etvasllhlp agkkvqillp vgrpkeqwdq kerrpfstrv synrypqpqe
      181 pl
//
LOCUS       WP_006003518             153 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Glaciecola punicea].
ACCESSION   WP_006003518
VERSION     WP_006003518.1
KEYWORDS    RefSeq.
SOURCE      Glaciecola punicea
  ORGANISM  Glaciecola punicea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Glaciecola.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Glaciecola punicea"
                     /db_xref="taxon:56804"
     Protein         1..153
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16250
     Region          3..153
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mnskvsqyke lvsqvsaita getdsianma nisailfngm sgvnwagfyi ykdeqlvlgp
       61 fqgnpaciri pldkgicgra attksvqvie nvhdfaghia cdaasnsevv vpiikngqli
      121 gvldvdspsf arfdnidaey lskvvdiltn tln
//
LOCUS       WP_006003871             457 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Glaciecola punicea].
ACCESSION   WP_006003871
VERSION     WP_006003871.1
KEYWORDS    RefSeq.
SOURCE      Glaciecola punicea
  ORGANISM  Glaciecola punicea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Glaciecola.
REFERENCE   1  (residues 1 to 457)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Glaciecola punicea"
                     /db_xref="taxon:56804"
     Protein         1..457
                     /product="amidohydrolase family protein"
                     /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=50654
     Region          22..449
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mskfavffti mitfclvnlp manaqqtalv ggrlidgfgh qplansvili kdgiilkvgs
       61 idtlpvpndy kvvstegmdv lpglwenhah lmltghadyv hwrkeytskl aseimpasae
      121 qlllagitsa rdlgapleds ilikkqiesg eipgprlyvs gpflqhkpyp gtehyrwgid
      181 gvkdaklkvn kladagvdii klidhdmmti eeaqsivdqa hkrnlvvvah ahkpdeirrg
      241 leigvdnfeh tglttapeyp edvirllker takgriaggp lfwtptvegl wnyettvsnf
      301 erlddkcwhr glepstikdi rdslgnvgql eymqltplrk ptlkrkiqql kdtgvvmlig
      361 tdsgiptkfh cqstwnelsv wvnemdispm dtiraatywp svlmkvsdkt gtisagkyad
      421 iiavkgdvlr yinllqnvdm vmkggkvykl nglptad
//
LOCUS       WP_006005804             709 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Glaciecola punicea].
ACCESSION   WP_006005804
VERSION     WP_006005804.1
KEYWORDS    RefSeq.
SOURCE      Glaciecola punicea
  ORGANISM  Glaciecola punicea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Glaciecola.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Glaciecola punicea"
                     /db_xref="taxon:56804"
     Protein         1..709
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=79063
     Region          9..709
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 myqrttiaic iasalfassv havvtqvdpq kneierieik gqsgtfeafp fnintveegk
       61 ilagkkvsvv dlslqptfve pnlrqvfsrl pglfvsdqki psiynvnyrg lgnphesefv
      121 afyqngipla sdvfgyatiy ylppaqriqr aefirggggl lygpqigpti nfmttranpd
      181 aknsastehs igsdgfysty nevryakddf gfiaslehrq adgprtnedy evnsgyvgla
      241 ykgfddirig fdvdvyqsds geagrlssre faqnrdlvnt pfnrieidrv iasltydqql
      301 sndstlngkl yysyqdrfsr rsgaflepad epattnidqq efttvgldvr yaqawgannv
      361 ftagtmlyrg dsprtryvss nirsntqnad dllfdqdrvm tyssvfaenl frfgdlsvvp
      421 tlryervnyd lfeplkrasl ersainidkt snellfglga syrvnnatev yanvsesyrp
      481 qrfddlanpn aeltgangpg issaknfelg vrsmvidgln ldvslfridf ddkveqiqvn
      541 ivdvqrvnsg nsrhqgiefs aeydffhqqn ndskligfin gslldaeitq stnanlvgnt
      601 pgfapdyvlr agfiysqdkl nvaltatlvd eqfwqdsnqp rgagngqina iidayqvvdl
      661 sadydinqsw svqaginnll dedyysrvrn dgiepaaert lylgfkfql
//
LOCUS       WP_006006009             308 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Glaciecola punicea].
ACCESSION   WP_006006009
VERSION     WP_006006009.1
KEYWORDS    RefSeq.
SOURCE      Glaciecola punicea
  ORGANISM  Glaciecola punicea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Glaciecola.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Glaciecola punicea"
                     /db_xref="taxon:56804"
     Protein         1..308
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34420
     Region          7..269
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mvddptallk khgrsfnfar lflgaetgia aarlyrfcri iddiadened kieaeiqlae
       61 irssiiqnek dhpligdfll lceehsidrq ngiiliegvs edfslqalvn eqevvqyayk
      121 vagvvglmma pilgadqqgq kfaidlgigm qltniardvm edarmnrryi pgiwvnsita
      181 kqiaanqaqd qkniqdaivq llhlaqeyyq sglaglyylp krnqraiava ayvyreigkk
      241 llrqncrywn grvivstprk vtlacqalwd lsarniadgh ikhsqelhkh lttiplakak
      301 asklaist
//
LOCUS       WP_006006021             380 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Glaciecola punicea].
ACCESSION   WP_006006021
VERSION     WP_006006021.1
KEYWORDS    RefSeq.
SOURCE      Glaciecola punicea
  ORGANISM  Glaciecola punicea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Glaciecola.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Glaciecola punicea"
                     /db_xref="taxon:56804"
     Protein         1..380
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42428
     Region          1..269
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          265..353
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkfihtsdwh igrqfhnvsl ledqrhvlnq lldyiktekv daviiagdiy drsippasav
       61 dlldqvltai tmdlgvpvil ipgnhdsaqr vrfgsrqlkk sglhimgdls aitepvvias
      121 stgdvafygi pytdpetvrn vwsedvksfd eahtflvnki skatlanqan vlishcfidg
      181 aqtsdserpl siggsdrvsy qpcedfnyva lghlhapqqk gaphirysgs ilkysfseqh
      241 qkkgitlvel dkdgrasfth lplaplrnmr viegefatii eqgkldphkq dyvlirmtdr
      301 hailepmakl revypnvlml ekpgmlitgd qamnreklkr gelemfsdff eqvsgqamst
      361 dqqkavketi vslikqeqqa
//
LOCUS       WP_006006157             286 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Desulfovibrio piger].
ACCESSION   WP_006006157
VERSION     WP_006006157.1
KEYWORDS    RefSeq.
SOURCE      Desulfovibrio piger
  ORGANISM  Desulfovibrio piger
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Desulfovibrio.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Desulfovibrio piger"
                     /db_xref="taxon:901"
     Protein         1..286
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31548
     Region          1..254
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mqfidlhths qasdgtdspg qlvrnarmqg laavavtdhd tvsgldeaea aardlgldfv
       61 rgcelstste lgemhvlglw lprdlaplqd rlqylrrkrs ernvrivskl qglgveield
      121 evlhearges vgrphiaavl vrkgyvkdvs eafkeylgyy graylpkevl qpeeavevls
      181 slgatvclah pmlqklpegw leafierllp cgltaieayh sehseaasrr clelarhygl
      241 gvsggsdyhg tnkprirlgk gygslrvpys vledlremra rrglpc
//
LOCUS       WP_006006681              79 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Desulfovibrio].
ACCESSION   WP_006006681
VERSION     WP_006006681.1
KEYWORDS    RefSeq.
SOURCE      Desulfovibrio
  ORGANISM  Desulfovibrio
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae.
REFERENCE   1  (residues 1 to 79)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 79)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 79)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 79)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Desulfovibrio"
                     /db_xref="taxon:872"
     Protein         1..79
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8247
     Region          2..79
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 msilvklstt lrdyvpgydp eagitldape dataadvarm vglpleeiki vmingrqkev
       61 qskicdgarv affpavggg
//
LOCUS       WP_006007712             268 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Glaciecola punicea].
ACCESSION   WP_006007712
VERSION     WP_006007712.1
KEYWORDS    RefSeq.
SOURCE      Glaciecola punicea
  ORGANISM  Glaciecola punicea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Glaciecola.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Glaciecola punicea"
                     /db_xref="taxon:56804"
     Protein         1..268
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29835
     Region          97..250
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mqprhpvfae ayiletvicy hkaimtpglc ieekkwatdv lkeyfsvvih tkviakakal
       61 feaaiesedl kasavsqqsi prdrssypel diateqleal flrrrsvrwy lpkpvpqkki
      121 ieavnlasla psacnrqpye fyvvndmqra piiakcamgt tgfadnlpci vvvvgnlday
      181 paerdrhciy idgslaamqf mlaietlgla tcpinwpdie arerqlakel slsvdqrpvm
      241 liavgyadpd ggvpfsqkkn ntllirnv
//
LOCUS       WP_006008153             717 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Brumicola pallidula].
ACCESSION   WP_006008153
VERSION     WP_006008153.1
KEYWORDS    RefSeq.
SOURCE      Brumicola pallidula
  ORGANISM  Brumicola pallidula
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Brumicola.
REFERENCE   1  (residues 1 to 717)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 717)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 717)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..717
                     /organism="Brumicola pallidula"
                     /db_xref="taxon:56807"
     Protein         1..717
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=80723
     Region          12..713
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkyislkwfg yilalviasv fciayltlps mpdtrayiar atkydvevmr dglgiphiyg
       61 kkdidtafgl gyvqseddfe tlqsvllatr gtlaaeigyk aaetdfvvqf mgvwdavnan
      121 yetqvpenik qiaqayadgv nlyaaqnpeh vsryflpatg kdiiagftfk mpmfygfdqi
      181 lsdlvdpdvm hevaksqnal iwqptnalpi gsqgiaiaph rsedglthll inshqpltgp
      241 vawyevrlhs eegwnmvgst fpgapviihg hndhlgwant vnkpdlvdiy qltinpdnen
      301 qylldgqwkt fktkvakmti klfgplrwtv kkeinisehg pvmatekgsf alrwsgmnev
      361 gtlefmfaan katnkeqfea alklnsmpsi nfvyadkagn iahyynakfp kridgwqwdk
      421 ilpgnrsdli wtefydfsam pktvnpssgl vynanntpwl atdgdddaqe sqypesmgie
      481 tsvtnrvlqi eeklkgvkki skglfkevky dlfyhpksyq italrkwlaq qqsvdlsqie
      541 lgaldalrsw nlsthkdnqe aalavltmap iqkangkpve mkkitrafkn tvaqlvkyhg
      601 sytppygdvy rlkrgqknlp msggpdilra vygqemdqng qieniagdgf mmfvswdkng
      661 vvqsdaihqy gsatkdsnsv hyndqmemfv akqerrvlfq raelekqver ryrpgfr
//
LOCUS       WP_005994924             295 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein, partial [Xanthomonas
            vesicatoria].
ACCESSION   WP_005994924
VERSION     WP_005994924.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas vesicatoria
  ORGANISM  Xanthomonas vesicatoria
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Xanthomonas vesicatoria"
                     /db_xref="taxon:56460"
     Protein         <1..295
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          12..260
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 agggapsrct hgegvlwceq rqslywvdis ekrlwrhhpd saktrfwtlp drpgclglmd
       61 dgrllialak avgivdpdst endvlpfekl adieadnplt rsndgrvdrh gnlvfgtmde
      121 hdnktargam yqfslthglr alplpgvsip nsicfsldgr tmyycdsvrp qilccdydqe
      181 taqtsntrvf atldrddaep dgsiidaegy lwnaqwrasr vvryrpdgsv erivhlpvkh
      241 ptcsafggaa ldrlhvissr ldhsaeelar mpeagglfvc dvaivglpes rvasa
//
LOCUS       WP_006008612             728 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Brumicola pallidula].
ACCESSION   WP_006008612
VERSION     WP_006008612.1
KEYWORDS    RefSeq.
SOURCE      Brumicola pallidula
  ORGANISM  Brumicola pallidula
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Brumicola.
REFERENCE   1  (residues 1 to 728)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..728
                     /organism="Brumicola pallidula"
                     /db_xref="taxon:56807"
     Protein         1..728
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=79736
     Region          17..728
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mkfsklslgi ssilmgvvft ssavesttdt nsdsieqiti fgstaavskl pgsgayiske
       61 mldtyattdi qrilsstagv yfveedgygl rpnigmrgss sdrsekitim edgvlaapap
      121 yaspaayyfp tvgrmqavei lkggssieyg prtsggvinl vstavpqdal ggkfdlalgs
      181 dgfsklhtfv ggrnetsggl veiynyqadg fknlnsgqdt gfnktdlltk fdiyldddkr
      241 hqlefklkys dessdetyvg ltqqdfnenp yqrysatqld dmstehkhas vhydyiisen
      301 mdlsviayin dfgrnwykvs kingsslgsg aeeiasnfda tvsmggapdd itvtlkannr
      361 dylsrgiqgq falylnnhqi nigarvhnde mdrfqwvdqy alaadfsmsv lsagvpgtns
      421 nridsanays ffvkdkmtfg dfivtagvry envnlarddw gktdplrsad psernnevsa
      481 flpsvgttyq andnwvllag vqkafappsp gnnkadneeg wnyefggrfs ydsvngelig
      541 fvtkldnlhg nctasqgcni dligqqynag kvdisgvefv inhraefdsf avptrfnyty
      601 ssaefgetfe selglwgsve agfdipylpk vtwqlesgia gdnwqvlaai kyvdemrvva
      661 gnnnidenng idartvvdis anyqiddqqs lyavvdnlfd keyavtrqhg glqvgkprsl
      721 qvgyryqf
//
LOCUS       WP_006008827             298 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Brumicola pallidula].
ACCESSION   WP_006008827
VERSION     WP_006008827.1
KEYWORDS    RefSeq.
SOURCE      Brumicola pallidula
  ORGANISM  Brumicola pallidula
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Brumicola.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Brumicola pallidula"
                     /db_xref="taxon:56807"
     Protein         1..298
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33235
     Region          8..270
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mqdnpttllk khgksfnfar fflgsktgia aarlyrfcri vddiadened kveaaaqlkl
       61 lkqqiiqnhk tdptvgdflm lcseygidre hgitliegvs qdliplalts demliqyayr
      121 vagvvglmma pilgaqksgh sfavdlgigm qltniardvm edakmqrryi pqdwvkglsa
      181 aqitkseiae ravvqkaiqr llqlaetyyq sglaglyylp prnrraiava afvyrdigrk
      241 llnndciywq grvmvptskk lllasqalwq ltssklahtd cvhaselhlh ltaqmqtk
//
LOCUS       WP_006009053             256 aa            linear   BCT 20-JAN-2025
DEFINITION  3-deoxy-manno-octulosonate cytidylyltransferase [Desulfovibrio
            piger].
ACCESSION   WP_006009053
VERSION     WP_006009053.1
KEYWORDS    RefSeq.
SOURCE      Desulfovibrio piger
  ORGANISM  Desulfovibrio piger
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Desulfovibrio.
REFERENCE   1  (residues 1 to 256)
  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 256)
  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 10793788
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Desulfovibrio piger"
                     /db_xref="taxon:901"
     Protein         1..256
                     /product="3-deoxy-manno-octulosonate cytidylyltransferase"
                     /EC_number="2.7.7.38"
                     /GO_function="GO:0008690 - 3-deoxy-manno-octulosonate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0033468 -
                     CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28572
     Region          1..245
                     /region_name="PRK13368"
                     /note="3-deoxy-manno-octulosonate cytidylyltransferase;
                     Provisional"
                     /db_xref="CDD:184007"
     Site            order(8..10,49,76,102,104)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133010"
     Site            order(127,144,150..152,158..159,161..167,176,201..202,
                     205..207,214..217)
                     /site_type="active"
                     /note="oligomer interface [active]"
                     /db_xref="CDD:133010"
ORIGIN      
        1 mniiaiipar mgssrfpgkp lalihgvpmv ghvafrtams rclsatyvat cdtviedyck
       61 easlacvmtg dhhvrcstrt aeallkieaa tgrkadivvm vqgdepmvlp gmidaavepm
      121 lkdpsinvvn lmadmdtlee fedpnevkvv vdrnndalyf srepipsrkk gadkvpmrkq
      181 vciipfrrdy lirfnemees pleicesvdm mrilehgekv rmvptdartw svdtpedlar
      241 vtrlmegdvl mreyak
//
LOCUS       WP_006010722             699 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Brumicola pallidula].
ACCESSION   WP_006010722
VERSION     WP_006010722.1
KEYWORDS    RefSeq.
SOURCE      Brumicola pallidula
  ORGANISM  Brumicola pallidula
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Brumicola.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 699)
  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   3  (residues 1 to 699)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Brumicola pallidula"
                     /db_xref="taxon:56807"
     Protein         1..699
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76671
     Region          3..686
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msidlsqfip sfleesfegl elmessllnl dagdneiins ifraahsikg gagtfgfdnv
       61 tefthlvetl ldeirdgrrd itakdtelll vsvdcmrlli eaarddadyd qdkitetthl
      121 leqtleidgp ashieiaksd edtqepagki whitfipehh lvqtgndpll lfsaladlge
      181 ltlkaktdll paitemdate lyiswelsli sdaseedire vfewvedeck leivelevsp
      241 kssssetqds lrnsasvdpe isdsqtalvt eqpasaiqss ekiekieknk tktkqdsgsi
      301 rvgvdkvdsl inlmgelvit qsmlselgnd feiskleklk sgldqllqnt kelqesvmki
      361 rmlpisfafn rfprlvhdls iktgkeinlv irgeqteldk tvmeqigdpl vhlvrnavdh
      421 giessdmria ngkpksgtit ldayhqggni iieisddggg inreavlska iekglvdsga
      481 tlsdsqvfdl lfepgfstak eisdisgrgv gmdvvkrniq slggriqves qpgigskfkv
      541 nlpltlaild gqlvrvgtev yiiplitive slqakeefin kvsgdmtlyr lrddnvpvip
      601 iyqlfdlpad tkevnnallv vveadgqkvg llvddllaqq qvvikslkdn yqqvegisga
      661 tilgdgsvam ildvpgmiem amkraqekqn ehilegalv
//
LOCUS       WP_006011009             280 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Brumicola pallidula].
ACCESSION   WP_006011009
VERSION     WP_006011009.1
KEYWORDS    RefSeq.
SOURCE      Brumicola pallidula
  ORGANISM  Brumicola pallidula
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Brumicola.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Brumicola pallidula"
                     /db_xref="taxon:56807"
     Protein         1..280
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30973
     Region          1..275
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mkidlhchst csdgaltpve lvqraqqmqv dvlaitdhdt vagisaardy aknsniklni
       61 iagielstsw hgfdihvvgl rvdkddcvfl krlegqlaer dkraericek lakcghegiy
      121 daaleiagga qisrnhiara lvqrsicthp qqaftkylgk nkkahvtpkw isideaiqwi
      181 hdaggqavla hpghydmttk wlrklvaefa qaggdameit hpnmaaekkk llqeimfdna
      241 llasagsdfh fpsrftelgr rldiplsckp vwhswnlatt
//
LOCUS       WP_006011811             173 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Brumicola pallidula].
ACCESSION   WP_006011811
VERSION     WP_006011811.1
KEYWORDS    RefSeq.
SOURCE      Brumicola pallidula
  ORGANISM  Brumicola pallidula
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Brumicola.
REFERENCE   1  (residues 1 to 173)
  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 173)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 173)
  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   4  (residues 1 to 173)
  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   5  (residues 1 to 173)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Brumicola pallidula"
                     /db_xref="taxon:56807"
     Protein         1..173
                     /product="TRAP transporter small permease subunit"
                     /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=19131
     Region          6..170
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mslvgavssv satidvinkr igecvsyftf lmaavtfavv vlrygfnlgw iamqesvvyl
       61 haavfllgsa ytlqhdghvr vdvfyrgfsh rrkalvnlvg tlflllpvmi fitvvswhyv
      121 feswqtlegs mesgglpfly vlksfillfs ftmflqgvse aikqslilag vsk
//
LOCUS       WP_006013105             651 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Brucella ovis].
ACCESSION   WP_006013105
VERSION     WP_006013105.1
KEYWORDS    RefSeq.
SOURCE      Brucella ovis (Brucella melitensis biovar Ovis)
  ORGANISM  Brucella ovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 651)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 651)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 651)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 651)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Brucella ovis"
                     /db_xref="taxon:236"
     Protein         1..651
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=70429
     Region          28..651
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msgelngndt svqaavsags vlegaafade geqhnesmkt lvlgalgvvy gdigtspiya
       61 frealhaaat ngilarsdil gvvsfifwal tlvvtvkyvl fvlradnnge ggilslmalv
      121 rgalkgrpdl ilgvgicgaa lffgdavitp aisvlsameg leivapnltp fvvpatvvil
      181 vtlfsvqklg tgrvaivfgp imalwfvalg asglwhifdd ptvmaalnpy yavrfltvsp
      241 avafvtvgav flamtgaeal yadlghfgrk pivrawlwiv fpclllnyfg qaafilshge
      301 aaalpffqmi psfalwpmvl lataatvias qavitgaysv arqavqlnil prleiqhtse
      361 klhgqiyipr vnlllglavv ilvlgfekss nlaaaygiav tgnmlvttvl lyivmtriwn
      421 wrvsralpii lgflvidmlf fsaniikvhe ggwasigiat vlvlimwtwv rgtrhlfqkt
      481 rkaevpldli veqmakrppt ivpgtavflt gdpksaptal mhslkhykvl hennviltvv
      541 taskpwvala drarvsqyne rfmlvtltfg ymqqpnipra lglcrrlgwk fdimttsffl
      601 srrslkasvh sgmplwqdkl fillartasd ateyfqiptg rvveigtqvn i
//
LOCUS       WP_006014987             363 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Brumicola pallidula].
ACCESSION   WP_006014987
VERSION     WP_006014987.1
KEYWORDS    RefSeq.
SOURCE      Brumicola pallidula
  ORGANISM  Brumicola pallidula
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Brumicola.
REFERENCE   1  (residues 1 to 363)
  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 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   3  (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
REFERENCE   4  (residues 1 to 363)
  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 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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Brumicola pallidula"
                     /db_xref="taxon:56807"
     Protein         1..363
                     /product="CmpA/NrtA family 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=40422
     Region          2..260
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 msvevklgfv pltdsapliv aqelgyfrqf eldvklcpqn swstlrdklq tglldaaqll
       61 apiplasslg lggmqvqmtv pmvlsqngna islsralcde illdnklsel pfpmpsnllt
      121 kivqrrakkg ekklrfatvf pyschqyqll dwlkvenmhn vidvitipps emsgslesgl
      181 idgfcvggpw saksvregtg vtvltsyhiw qdkaekvlgt tdafyqkepe lmaklcaall
      241 lacewlqylp nrfeaaklms qsgylnepie viapsllgsc liqqnqspqh vphynrfyes
      301 nfivvnsptl elqqwllqkm ldshqisskd aqqvvvtqim qkivntacfd eavallakqr
      361 hky
//
LOCUS       WP_006015387             309 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Brumicola pallidula].
ACCESSION   WP_006015387
VERSION     WP_006015387.1
KEYWORDS    RefSeq.
SOURCE      Brumicola pallidula
  ORGANISM  Brumicola pallidula
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Brumicola.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Brumicola pallidula"
                     /db_xref="taxon:56807"
     Protein         1..309
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34614
     Region          23..273
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mnktqlpkkv gkllfsinsq cilaecalwn efeqviywvd iigakiqryc prthgvetfd
       61 mpyrigcfsf tpiknqiiaa fdigiarynl vteqlewlaq pekniktnrf ndgrtdrqgr
      121 fwagtmnesv aadddsnlnn ivlgnlycid ankqcdakvv nvsisnglcw skdgktlyha
      181 dspkrtisay dfdtrttqls nkrvfattqg hrfpdgsivd sedylwsahw gasqvvrynp
      241 kgkidlvvdm pvsqpssvai ggpqmdwliv ttakhslape rlmiepqsgn ifiyqlhgie
      301 gvaepvcvi
//
LOCUS       WP_006019735             507 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Afipia broomeae].
ACCESSION   WP_006019735
VERSION     WP_006019735.1
KEYWORDS    RefSeq.
SOURCE      Afipia broomeae
  ORGANISM  Afipia broomeae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Afipia.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Afipia broomeae"
                     /db_xref="taxon:56946"
     Protein         1..507
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=53732
     Region          4..507
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 maptpvirlh sddsvviart allpgaeiaq gvaateripa ghkvavkpia vgepvkrygq
       61 iigfatvpit pgqhvhvqni gmgefskdya ygvdvkptpn fdlpatfqgi rrpdgrvatr
      121 nyigiltsvn csahvaglva dvfkknpftg hdpladypnv dgvvalthkt gcgmtqlepl
      181 tvlrrtlggy arhvnfshvi ilglgcemnq iggfleeqrl agrlrsldiq dvggsrktve
      241 kavafvrevl aesnnikrep cpaselmval qcggsdgysg vsanpalgaa sdllvrhggs
      301 vilsetpety gaehlltrra vspevgeklv almrwwedyt rrngaemdsn pspgnkaggl
      361 ttilekslga makagstnlv dvvgyaepvt kkgftfmdtp gfdpvaatgq vagganlvcf
      421 ttgrgsvfgc kpspsiklat ntpmfrrmee dmdvncgtil dgdetvqqcg qrifelilrv
      481 asgeqtksea fdfgaaefap wvlgatm
//
LOCUS       WP_006020010             362 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein [Afipia].
ACCESSION   WP_006020010
VERSION     WP_006020010.1
KEYWORDS    RefSeq.
SOURCE      Afipia
  ORGANISM  Afipia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 362)
  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 362)
  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 362)
  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 362)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Afipia"
                     /db_xref="taxon:1033"
     Protein         1..362
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39654
     Region          1..354
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkrrdflkvt aagaaatava spaiaqsspe vkwrltssfp ksldtiygga eqlskyvaem
       61 tdnkfqiqvf aagevvpglq aldatsngtv emchtvsyyy vgkdptfaif asvpfglntr
      121 mqnswldqgg gnelanefyk kfgvmglpcg ntgtqmggwf rkeiktvadl qglkmriggi
      181 agqvlakvgv vpqqlaggdi ypslekgtid aaewvgpydd eklgfnkvak fyyypgfweg
      241 gptvhaftnl ekfnalpkny qailtnaaah tngwmparyd mqnpgalkrl vasgtqlrpf
      301 tnevldaclk atnelwaeis aknadfkkai damqayrsdq ylwwqvaeyt ndsfmirsrt
      361 rg
//
LOCUS       WP_006020037             633 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Afipia].
ACCESSION   WP_006020037
VERSION     WP_006020037.1
KEYWORDS    RefSeq.
SOURCE      Afipia
  ORGANISM  Afipia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 633)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 633)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 633)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Afipia"
                     /db_xref="taxon:1033"
     Protein         1..633
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68435
     Region          1..633
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 maasdtsadt pqevpvttgf waltlgsigv vfgdigtspl yafreavhna thggpvsrei
       61 vlgvlslilw slivvvtiky vllllradnn geggtlslma lgqralgrrs wvllalgvig
      121 gamflgdami tpaisvlsav eglkiaapal ehyvvplaiv ilvclfalqs rgtamvasaf
      181 gpvmiiwflt lgvmglmhis ddpgivhain pifavqfllt hgmiglvilg avflavtgge
      241 alyadlghfg rkpiqaawfy fvlpclllny fgqgalvlah peaienpfyr mvpesvlvpl
      301 iclataatvi asqavitgaf slvrqaiqlg llprfevryt sethagqiyl prvnvmllig
      361 vlllvglfrs ssnlasaygi avsttmvcdg lmcfvviwkl wnwraataaa livplvivdl
      421 tfltanllkl lqgawvpvlf gilmaglvwt wrrgtvilin ktrrtevpla dlikslekrp
      481 phivkgtavf ltsdpayvpt allhnlkhnk vlhehnvilt ihtaetprvd vadrvrmeki
      541 sdkfstvrlt fgfmespnvp kalaiarklg wqfdimstsf fvsrrslkps aqsgmplwqd
      601 hlfiamsrsa ndatdyfqip tgrvvevgtq vti
//
LOCUS       WP_006002626             484 aa            linear   BCT 20-JAN-2025
DEFINITION  type I restriction-modification system subunit M [Glaciecola
            punicea].
ACCESSION   WP_006002626
VERSION     WP_006002626.1
KEYWORDS    RefSeq.
SOURCE      Glaciecola punicea
  ORGANISM  Glaciecola punicea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Glaciecola.
REFERENCE   1  (residues 1 to 484)
  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   2  (residues 1 to 484)
  AUTHORS   Youell,J. and Firman,K.
  TITLE     Mechanistic insight into Type I restriction endonucleases
  JOURNAL   Front Biosci (Landmark Ed) 17 (6), 2122-2139 (2012)
   PUBMED   22652768
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Sistla,S. and Rao,D.N.
  TITLE     S-Adenosyl-L-methionine-dependent restriction enzymes
  JOURNAL   Crit Rev Biochem Mol Biol 39 (1), 1-19 (2004)
   PUBMED   15121719
REFERENCE   4  (residues 1 to 484)
  AUTHORS   Murray,N.E.
  TITLE     Type I restriction systems: sophisticated molecular machines (a
            legacy of Bertani and Weigle)
  JOURNAL   Microbiol Mol Biol Rev 64 (2), 412-434 (2000)
   PUBMED   10839821
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114514
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Glaciecola punicea"
                     /db_xref="taxon:56804"
     Protein         1..484
                     /product="type I restriction-modification system subunit
                     M"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=54424
     Region          7..143
                     /region_name="HsdM_N"
                     /note="HsdM N-terminal domain; pfam12161"
                     /db_xref="CDD:463478"
     Region          155..393
                     /region_name="HsdM"
                     /note="Type I restriction-modification system, DNA
                     methylase subunit [Defense mechanisms]; COG0286"
                     /db_xref="CDD:440055"
ORIGIN      
        1 myeaafknid dtlwkdagcs seldyieqts wvlflkyldd fesekeqaai lngekftrii
       61 dgefrwnewa apkkvdgsad ynaaltgddl rdfvnlklfp ylsnfklsad nprtinykig
      121 eifselrnkl qsgyalrevv nkvdelkfls nddkhelssl yedkiknmgn agrnggeyyt
      181 prpliksivk vinpqigetv ydgavgsagf lceayahmrg skelsaaeye tlqnstffgk
      241 ekkslayvig tmnmilhgie apnilhtntl aenitdiqqk drvdvvvanp pfggkeraei
      301 qqnfpiktse taylflqhfi kmlkvggrcg vvikntflsn tdnasvalrk qlleecnlfa
      361 vldlpggafi gtgvktvvlf fekgkptekv wyyqldvgrn mgktnplner dlaefvdmak
      421 tqelsekswl ididsvntkt ydltvnnpnr veevdertpl eiiaeieeld aqaaealqai
      481 kell
//
LOCUS       WP_006020325             562 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Afipia broomeae].
ACCESSION   WP_006020325
VERSION     WP_006020325.1
KEYWORDS    RefSeq.
SOURCE      Afipia broomeae
  ORGANISM  Afipia broomeae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Afipia.
REFERENCE   1  (residues 1 to 562)
  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 11482063
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Afipia broomeae"
                     /db_xref="taxon:56946"
     Protein         1..562
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=59490
     Region          37..562
                     /region_name="PRK06132"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:235709"
ORIGIN      
        1 mygnrlpasg dqrktlgits pfpgndissr plrsiglrta wlataltagf vlpadaqvyw
       61 pmdpgatyyp epqhhleprr prvarakpkl pdapkdtakp vgpivvaisi drqtlklydq
      121 nglfaespvs tgmrghstpm gvfsviqknk yhrsniysga pmpymqritw sgvamhagvl
      181 pgypashgci rmpmnfamrm wgwtrmgarv iitpgevspa dfshplliar kqgtkpvaaa
      241 avperhtett pksdrssivd aashdkpqlr ltsisedapv rtadasgalp qksdadsvva
      301 qawdasrggg swdagrggvt pepeaakdgp kenanppspn apkdgaaakd daaktdgnag
      361 asddkaagdk spdatpadkk seapktdkdq trvtdtgaap apvavasegs aefigpvkpr
      421 tghvavfvsa kenkiyvrqn fepwfetpvt iaasnrplgt hvftvradkd daealrwsvv
      481 slpsparvae eaprrrrgep vaaiaapapp ssptealdrl sipeetmtri asalapggsi
      541 tvsdrglgde tgrgtdfivq lr
//
LOCUS       WP_006020600             390 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein [Afipia
            broomeae].
ACCESSION   WP_006020600
VERSION     WP_006020600.1
KEYWORDS    RefSeq.
SOURCE      Afipia broomeae
  ORGANISM  Afipia broomeae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Afipia.
REFERENCE   1  (residues 1 to 390)
  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 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   3  (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
REFERENCE   4  (residues 1 to 390)
  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 390)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Afipia broomeae"
                     /db_xref="taxon:56946"
     Protein         1..390
                     /product="CmpA/NrtA family 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=41723
     Region          4..263
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mtgtplrigf iplvdaaall vavdkgftaa egldvtlvre vswsnvrdkl niglfdaahl
       61 lapvaiastl glsqvkvpii apfnlglngn aitvspalya aitgeadgdp anpmvtakal
      121 arvvaarrks gsepltfgmt fpfsthnyql rfwmaaggvd pdedvrlvvl pppymvdsla
      181 nghvdafcvg apwnsvavdl gvghilhyvs dileraaekv lavretwalk nsgvlarltr
      241 ahghaadfie npdnrtevsr ilgaperigv dpevirrtld grlkispggt iresgrylli
      301 gregaarpdp vqaawlyaqm vrwgqaaysr ealetarkvf rpdlydaalg apktpvramq
      361 dsvgafdgpl fdpndipahl asvtikrrql
//
LOCUS       WP_006020618             129 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein [Afipia].
ACCESSION   WP_006020618
VERSION     WP_006020618.1
KEYWORDS    RefSeq.
SOURCE      Afipia
  ORGANISM  Afipia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Afipia"
                     /db_xref="taxon:1033"
     Protein         1..129
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=13564
     Region          38..105
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mkkialvaas lavlagpala qtsgtapaea kfstvakdem fssklkglnv ynqkdekvge
       61 itdlaigkge qiqamilsvg gflgvgehyv avspssvrvs ynkdkdtwta kmnttkealk
      121 aapefkypk
//
LOCUS       WP_006022682              92 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Afipia broomeae].
ACCESSION   WP_006022682
VERSION     WP_006022682.1
KEYWORDS    RefSeq.
SOURCE      Afipia broomeae
  ORGANISM  Afipia broomeae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Afipia.
REFERENCE   1  (residues 1 to 92)
  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 92)
  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   3  (residues 1 to 92)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Afipia broomeae"
                     /db_xref="taxon:56946"
     Protein         1..92
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=10490
     Region          19..>92
                     /region_name="Endonuclease_DUF559"
                     /note="Putative endonuclease; cd01038"
                     /db_xref="CDD:411708"
     Site            order(23,52,69,75)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:411708"
ORIGIN      
        1 mrgpdhkatg iarklrglqt daetklwrhl rnrqisgakf vrqepvdryv cdfvcrelkl
       61 iveadggqhl esgtdavrdr nlseigyrvl rf
//
LOCUS       WP_006020749             722 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Afipia broomeae].
ACCESSION   WP_006020749
VERSION     WP_006020749.1
KEYWORDS    RefSeq.
SOURCE      Afipia broomeae
  ORGANISM  Afipia broomeae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Afipia.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Afipia broomeae"
                     /db_xref="taxon:56946"
     Protein         1..722
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=78949
     Region          10..722
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mfsvsirars illasaatvs tiplahaqta pqelppvvvq terqprpvrn rvatpapvqs
       61 gststaptat paplgvktad qarqeiqqtp ggvavvaaee yknnsvasti kdilgyvpgv
      121 faqpkwgddt rlsirgsgls rnfhlrsvql ymdgipints dgygdfqeid ptaykyvevy
      181 kganalqfga nslggainfv tptgrdfgvn sagidmgsfg yrrfqgsvgg angpwdafft
      241 asnqsaegfr dhsyghstra sgnigyqfsp dfetrfyida ndvrqripgs vtrasaltsp
      301 etaaavnvan dwqrnidtvr lankttvrfg attvefgafa vdrhlmhpif qwldysykdy
      361 ggfvkatddr iiggfrnrfv agvnilngti daqqyvntgg ykgalqsslt qkpenysgfa
      421 ensfyflpnv aaiagaqylf avrdqqvnfs lngdkngrss fslfspkggl lwdidptwqa
      481 fanvsrsaev psfgesvaps fqnpgyptip fydikpqtat tyeigtrgrr pdltweltgy
      541 raniknellc fysnfgncnv tnadrtvhqg ieaglgiamf rniftpdadk iwlnmaytfn
      601 dfrfdndpvf rnnqlpgapr hflraevlyk hangfyigpn iewvpqayyv dsantlttqa
      661 yaiwglkagv ddgkysmyle arniantayi asasiinqan atmplfepgt graiyagmkv
      721 rw
//
LOCUS       WP_006020046             157 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-hydroxyacyl-ACP dehydratase FabZ family protein
            [Afipia].
ACCESSION   WP_006020046
VERSION     WP_006020046.1
KEYWORDS    RefSeq.
SOURCE      Afipia
  ORGANISM  Afipia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (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 10101294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Afipia"
                     /db_xref="taxon:1033"
     Protein         1..157
                     /product="3-hydroxyacyl-ACP dehydratase FabZ family
                     protein"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=17397
     Region          6..126
                     /region_name="FabZ"
                     /note="FabZ is a 17kD beta-hydroxyacyl-acyl carrier
                     protein (ACP) dehydratase that primarily catalyzes the
                     dehydration of beta-hydroxyacyl-ACP to trans-2-acyl-ACP,
                     the third step in the elongation phase of the bacterial/
                     plastid, type II, fatty-acid...; cd01288"
                     /db_xref="CDD:238615"
ORIGIN      
        1 mqleyfqmvd ritdldvgkr titvesqvpe tstvfeghfp gyplmpgvll tetmaqtsgw
       61 lliallkfer mpflasvkea kmrdfvkpge lltinaslvh dgsgfavtda nvriggklkc
      121 natltfrhtp fphpdlrvhm eamakrigfp eqaiahd
//
LOCUS       WP_006023404             382 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Afipia broomeae].
ACCESSION   WP_006023404
VERSION     WP_006023404.1
KEYWORDS    RefSeq.
SOURCE      Afipia broomeae
  ORGANISM  Afipia broomeae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Afipia.
REFERENCE   1  (residues 1 to 382)
  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 382)
  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 382)
  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 382)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Afipia broomeae"
                     /db_xref="taxon:56946"
     Protein         1..382
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=41923
     Region          41..373
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mtkrhkdkts sdktssrrnf lkvaaagaaa tvatpalaqt gptnmrfqst wpakdifhey
       61 aqdyakkvnd mtggdlkiev lpagavvpaf qlleavskgt ldgghgvlay hygkqnalal
      121 wgsgpgyamd anmllawhky gggkqllekl ynsiganvvs fpygpmptqp lgwfkkpvtk
      181 addlkgvkfr tvgisidvft gmgaavnalp ggeivsamdr glldaaefnn assdrvlgfp
      241 dvskvcmlqs yhqnaeqfei mfnkdkynal pakiraildn aaeaagqdma wkaidrysrd
      301 yeemqskdkv kfyktpdsvl qkqleifdqv aekksaenpl fkeivesqla fakratqweq
      361 dtvvsrrlay nhyfgpnakk kt
//
LOCUS       WP_006024243             252 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Burkholderia].
ACCESSION   WP_006024243
VERSION     WP_006024243.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  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   3  (residues 1 to 252)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..252
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27819
     Region          43..250
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mnteqstsla esaaahsghd ygrrnpleig vqlrnlvnrg dfltvqyqgg qlvtrildvd
       61 vgartfvfdw galadqnagi laaprcvfha spdgvrvefs tappretrye nlpafeadfp
      121 dvlycvqrre yfrvdapild pyvcrgklpd gesflfevhn lslgglglrt gddrvaslep
      181 gttlpdveln lnghgklsld lqlvshrate tpsgarryql gfrflslpgn aentlqriit
      241 qlemkrrqla ra
//
LOCUS       WP_006024793             424 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Burkholderia].
ACCESSION   WP_006024793
VERSION     WP_006024793.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 424)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..424
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=46286
     Region          35..254
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 msmididpps fqsprpiagd dgnrrtvlyg dytvfsvfqp vfsvshrrai gyhaslrahd
       61 shgnqvpshe vftqaarrgd llelgrlaes lhlgnfhtfd shdewlflsl hpaalmdtvy
      121 gdallanlka lglppqrvvl evpeqagget prfaaivdgl rkagflialg gfgakhsnid
      181 rvwhlhpdiv tldrgilaqa sehshlervl pglvsllhes gqlvlmggit terealiale
      241 cdvdfvqgqy fagpsvepvq pqvaagimdt lsaalrlrva ersraqearl apyvaallra
      301 gallregrdl teaskellel peaarcflld asgrqigdnv lprvhasqra krfspllhse
      361 gaswerrpyf ieamrvpgrv hftppylsin eahlcvtasi atpaaqgmqv lcvdinweaa
      421 ahrd
//
LOCUS       WP_006026625             351 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Burkholderia].
ACCESSION   WP_006026625
VERSION     WP_006026625.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..351
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38181
     Region          1..349
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mgitvrnlhk rfgdftaldd vtldfpagel vallgpsgcg kttllrviag lehadsgqvv
       61 lqgldvasvg arerqvgfvf qhyalfrhmt vfenvafglr vkprrerpse aairakvhel
      121 lslvqldwla qrypselsgg qrqrialara lavepkvlll depfgaldak vrkelrgwlr
      181 rlhddlhist ifvthdqeea levadrivvl nhgrieqvgs pqdvydhprs afvyeflgaa
      241 nrldgtvsgq gfvahgaaqa iavdadfagp arayvrphdl elvaplarad giaadvrrvv
      301 plggsvrvel aartggvlea eldrnawral aldvgdaltv vpravrvfpv r
//
LOCUS       WP_006027098             353 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Burkholderia].
ACCESSION   WP_006027098
VERSION     WP_006027098.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 353)
  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 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   3  (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   4  (residues 1 to 353)
  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 353)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..353
                     /product="CmpA/NrtA family 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=37772
     Region          12..260
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mdparinqat pdapergrlr igfvalsdaa plvaakrlel gerygltlel crqpswasir
       61 dkllsgelda ahalyglvyg vqlgiggpra emavpmvlnr ngqaitfsnr ladahrasgn
      121 lkaalatlgr rpvfaqtfpt gthamwlyhw lashgvdplr dirsvvippp emvgalaage
      181 ldglcvgepw navaeargag rtvaatsevw rdhpekalac rrefvalypn aarllvrtll
      241 dacawlddpa hrmraaqwla kpdaigvpve qiaprllgdy gagpfaqppa pirfysngta
      301 nrpaasdglw flsqyrrwgm lsgdvddaai angvaqtaiy deavalagvr gvd
//
LOCUS       WP_006030704             256 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Moritella sp. PE36].
ACCESSION   WP_006030704
VERSION     WP_006030704.1
KEYWORDS    RefSeq.
SOURCE      Moritella sp. PE36
  ORGANISM  Moritella sp. PE36
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Moritellaceae; Moritella.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Moritella sp. PE36"
                     /db_xref="taxon:58051"
     Protein         1..256
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28209
     Region          10..93
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          173..253
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mksslefkli qpkgllspyi qgiwsasvhs seaiehwlhg dacsgiifnl gsaiklgdvs
       61 fptgvialpv skcaqkislp pgsklvglrf hpaigvgvlg krydepkivt adskmtlalq
      121 alsesltsir ghfacittly rwlidsldls cpipiqldqa lkaieksqtp tqlcnaitis
      181 qrqierqfqr wlgltpkhyq rilrvksvin vlreipdsnl adlalshgfs dqshmtreck
      241 kiakitpkvf tkrvhl
//
LOCUS       WP_006030976             682 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Moritella sp. PE36].
ACCESSION   WP_006030976
VERSION     WP_006030976.1
KEYWORDS    RefSeq.
SOURCE      Moritella sp. PE36
  ORGANISM  Moritella sp. PE36
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Moritellaceae; Moritella.
REFERENCE   1  (residues 1 to 682)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 682)
  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   3  (residues 1 to 682)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Moritella sp. PE36"
                     /db_xref="taxon:58051"
     Protein         1..682
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=75858
     Region          3..673
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdidlkqfhq vfieeclegl evmeaellkl npgsvdsevi ntifrvahsi kggagtfgfh
       61 qltafthvae tllddlraek ltlidghinl flqtvdclra wiqlladdse sipdaaeslk
      121 qqynqflqld vnqdlsstgd eplakppvmk glddgdwlih fvpgqdilkq gneprlifae
      181 lqdmgelkvm pkfdnipswn nlspediyvt wdlelisqvs eaqikeafew vedestiiit
      241 tpstrtqsia setlatdnkm laeskpspvt tnkitktksp etnsirvsid kvdalinmvg
      301 elvitqamle elgqdfsvek lpelkkgltq lsqhtremqd svmkirmlpi qfafnriprm
      361 vrdlsaqlgk nvvlrihgee teldkimlek lsdpivhlvr naldhgieti eerklagksd
      421 vayldinafh qggeiiveir ddgrglnrdk ihakaiekgi ankdqrysdn qidefifspg
      481 fstvetvsdi sgrgvgmdvv krnieslggd ikiesttgeg scfsirlplt lsimdgqlvk
      541 igsktyilpi msiieslqlk dgmvtkladd tevfklrdef isiirlykvl nhktnlkcit
      601 dgllvvvecg nqkygllvdd laaqqqvvik nleenfmkvs cvsgatilgn gtvalildia
      661 divkrvtner hqqqgprahv aa
//
LOCUS       WP_006031351             279 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Moritella sp. PE36].
ACCESSION   WP_006031351
VERSION     WP_006031351.1
KEYWORDS    RefSeq.
SOURCE      Moritella sp. PE36
  ORGANISM  Moritella sp. PE36
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Moritellaceae; Moritella.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 279)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Moritella sp. PE36"
                     /db_xref="taxon:58051"
     Protein         1..279
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=31704
     Region          35..257
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mdfmndyarl hnniieliee daeygfyity qdltftsvfq pifdrehniy gvealarifd
       61 angsavnphd yfesiihdde vsaiatlics tihmlnfsrs cyydkklfin vtpvifeils
      121 nhdiavntli rglkkigvsp tqlvyeiief egrnlesvln giqkladfgi evaiddygia
      181 ysteervrsi krdylkidks ivdllaafky skfhhavsig rsikaktiae gietkavfer
      241 cvesgadyfq gyylarpekl aksesvrqtt essegwkvl
//
LOCUS       WP_006031876             622 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Moritella sp. PE36].
ACCESSION   WP_006031876
VERSION     WP_006031876.1
KEYWORDS    RefSeq.
SOURCE      Moritella sp. PE36
  ORGANISM  Moritella sp. PE36
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Moritellaceae; Moritella.
REFERENCE   1  (residues 1 to 622)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 622)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 622)
  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 622)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..622
                     /organism="Moritella sp. PE36"
                     /db_xref="taxon:58051"
     Protein         1..622
                     /product="M4 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=67197
     Region          10..615
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mmannkfils avavsllgtv naiaaervnl rdniqqlasa aladpgilms apaqllglsw
       61 ndglsvikty rnskgdsitr yqqtyfglpi igeqaiiart skglfkrahg ailnniaddi
      121 vditpsittv nalrqakrls rpatplaenk svatenetsr lavwlgddgv aklvyevsff
      181 qradkpsrpy yiidahsgev llsydnlqta datgpggnek igeyrygsdf salnvtqagg
      241 icvmnnaqvk tvnlnhgteg sdafsftcpe ntvksingay splndahyfg giifdmykdw
      301 lnvspltsql vmrvhydkny enafwngesm tfgdgadify plvsldvsah evshgfteqn
      361 sglvysgksg glnesfsdma geaaefymhg rndwlvggqi lkangalrsm shppmdgssi
      421 dnqadyrfnm dvhhssgvyn kafytlatta gwdtqkafvl yaaanqyywt snsnwndagn
      481 gvmdaacdld ynvddvqasl tavgvvadvs dgsqcsvtkp pvsaidrtee nistsffrpa
      541 nfkqelgegy srlivtlagg tgnadlyvkh edkslfsksd cisktpgnie tcvidnpnag
      601 iwkidvrgyg stsgvilniq aq
//
LOCUS       WP_006033369             139 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Moritella sp. PE36].
ACCESSION   WP_006033369
VERSION     WP_006033369.1
KEYWORDS    RefSeq.
SOURCE      Moritella sp. PE36
  ORGANISM  Moritella sp. PE36
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Moritellaceae; Moritella.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Moritella sp. PE36"
                     /db_xref="taxon:58051"
     Protein         1..139
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15757
     Region          1..138
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mglwllffss ftsatilpgs seilltamli egswsywqlf vmatsgnvlg siltfymgyf
       61 ihakkpidfs ankhyqrvhd viqrwgwssl lfswlpifgd ilcllagwlr vnpllafmai
      121 mfgksiryai liwfmsavs
//
LOCUS       WP_006032198             243 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Moritella sp. PE36].
ACCESSION   WP_006032198
VERSION     WP_006032198.1
KEYWORDS    RefSeq.
SOURCE      Moritella sp. PE36
  ORGANISM  Moritella sp. PE36
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Moritellaceae; Moritella.
REFERENCE   1  (residues 1 to 243)
  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 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   3  (residues 1 to 243)
  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   4  (residues 1 to 243)
  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 243)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Moritella sp. PE36"
                     /db_xref="taxon:58051"
     Protein         1..243
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27606
     Region          1..239
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <138..239
                     /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 mkhpllidiq cndiespshg hdfhqlilpi sgdlvleieg dqakvnndvi afvsasnkhs
       61 fiaeqenrfi lanvplawrd tlrelppflk ltptvksyiy fiscqlqdla vsalnqeqil
      121 imlldliskp linnekidkr illaktfldd hvatsvsleq vamaahlsvr qlstlfkeql
      181 gftplnyire qrmkeaqill iqstlpitti aesvgyqnls afsdrfkkhf grspriyrqf
      241 dkq
//
LOCUS       WP_006035672             130 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Rickettsiella grylli].
ACCESSION   WP_006035672
VERSION     WP_006035672.1
KEYWORDS    RefSeq.
SOURCE      Rickettsiella grylli
  ORGANISM  Rickettsiella grylli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Rickettsiella.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Rickettsiella grylli"
                     /db_xref="taxon:59196"
     Protein         1..130
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14771
     Region          1..128
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mntagftlfe llivlviigi lttfstpiyr hlvkktrrse akialinlaq hmeiyylenn
       61 nsyekasfsk lhlknmtekk fyqltlksts ntyqlsakaq ftdpecylfm lnqlgektnk
      121 gsgssqcwsa
//
LOCUS       WP_006036466             288 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Paenibacillus curdlanolyticus].
ACCESSION   WP_006036466
VERSION     WP_006036466.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus curdlanolyticus
  ORGANISM  Paenibacillus curdlanolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Paenibacillus curdlanolyticus"
                     /db_xref="taxon:59840"
     Protein         1..288
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31552
     Region          4..261
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 maimgnadmh thtlasdgtn apavvvrlak eaglaavait dhdtisgwae amaegerigi
       61 evipgvelst vmngrdihil gywcnsddeq wqerlrsqqg frgkrnlmmi erlqalgidv
      121 tideiialar khgkqvegae qigrphlaev liargvvtdi reafdrylge sglaycnppr
      181 lqpfeaidwi reaggvsvia hpglygddel veaivrhgaq gieayhsdhd adqelryeam
      241 aqrygllvtg gsdfhgekqg vvfhgpighr svgmqvvdrl kqlirrdk
//
LOCUS       WP_006036606             687 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Paenibacillus curdlanolyticus].
ACCESSION   WP_006036606
VERSION     WP_006036606.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus curdlanolyticus
  ORGANISM  Paenibacillus curdlanolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 687)
  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   3  (residues 1 to 687)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Paenibacillus curdlanolyticus"
                     /db_xref="taxon:59840"
     Protein         1..687
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=74551
     Region          1..687
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          173..250
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 mdmnaylsmf idesndhlqa lnenllklen dpqdlsivqv ifrsahtlkg msatmgfedl
       61 aslthemenv ldlvrnskls mdsfifdtlf kgldaleamv qdvveggtgk advsalivsl
      121 qsivkgdykt nasaapsaaa naaegnlssg nelldifqls vlkqsieags kayyikvtlr
      181 edcvlkavra ymvfdvlern geviksdpsv qdieqdkfdr sfivflisss dqqalkdgie
      241 svsevelaev vlldaesiql ygpqneqspa pkaaapsavp qpqqeakqqv aaakaqtaaa
      301 atapvnrtir vdidrldslm nlfsellidr vrleqlssei krgdlsetve hmarvstdlq
      361 divlklrmvp vesvfnrfpr mvrdiaknld kkidlvitga eteldrtvid eigdplvhll
      421 rnsldhgvem padriaagks dtgtvhlraf hsgnhvfiev eddgngidaa kvsriaikng
      481 vlteeeakkl seeqlqmlif apgfstadki sdlsgrgvgl dvvkskitsl gghvsirskl
      541 gqgtifsiql pltlsiiaam likmgdekya iplssivetg iiqrdkiatv hgnqmiefrg
      601 svipvvslsr vldvesfned deqeteivvi rkgdklaalm idsfigqsei vlkslgkylp
      661 avkaisgati lgdgqvalii dpnafik
//
LOCUS       WP_006037350             354 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Paenibacillus curdlanolyticus].
ACCESSION   WP_006037350
VERSION     WP_006037350.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus curdlanolyticus
  ORGANISM  Paenibacillus curdlanolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Paenibacillus curdlanolyticus"
                     /db_xref="taxon:59840"
     Protein         1..354
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39801
     Region          1..333
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mhievrnlnk qfgdfhavrd vsftiekghl igllgpsggg ktsilrmlag letptsgdie
       61 flgkrvnelp pqergigfvf qnyalfkhmt vfdniafglk ikkqskeqir nrvmelvelt
      121 glkgfehryp hqlsggqrqr vafaralape pqlllldepf aaidakirge lrtwlkelie
      181 rvgitsifvt hdqeeaieva deimiinkgq leqkgspwdi ykspetpfva gfigestiie
      241 nigeirgfen angwsgtkal irpeyieigk pgeirlasaa mngrvkhlhf rgsewmveie
      301 vgaaklityr slekdalhpg eevnvlvhra ymfndsdswi menklkedpm pihi
//
LOCUS       WP_006038834             417 aa            linear   BCT 20-JAN-2025
DEFINITION  TerD family protein [Paenibacillus curdlanolyticus].
ACCESSION   WP_006038834
VERSION     WP_006038834.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus curdlanolyticus
  ORGANISM  Paenibacillus curdlanolyticus
            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 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Paenibacillus curdlanolyticus"
                     /db_xref="taxon:59840"
     Protein         1..417
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=45278
     Region          38..417
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mavavvkgqk vditktnpgl tqlkvaigwq sssavevdts afllgengmt sgdedlifyn
       61 qpsngfirye ngqapdqkqf vidlqrvpan ihrvafsltl ydeqqgfkqv kdayirfmng
      121 atgqeavryd lgnnfsveta vvvgefyryn gewkfnaigs gfsgglkalc anygiavqqd
      181 epakppvpss aptpspapaa svpppsspss agapvhlnlk kielkkkgdk inltkgpkgd
      241 lgeirinlnw nrqqgkggff sksrsvdldl aclyelndgr kgvvqalgns fgsldrapyv
      301 aldgddrtgt vatgenirin garvseikri liftfiyqga anwkdadgvv tieqqggpdi
      361 ivhmnehdnq kgmcaiamih nvgnetfsie rlvqfynghs eldraydwgm rwvagkk
//
LOCUS       WP_006039059             390 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Paenibacillus curdlanolyticus].
ACCESSION   WP_006039059
VERSION     WP_006039059.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus curdlanolyticus
  ORGANISM  Paenibacillus curdlanolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Paenibacillus curdlanolyticus"
                     /db_xref="taxon:59840"
     Protein         1..390
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43404
     Region          1..275
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          271..359
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mklfhtadwh lgklvqgvym tddqryvleq fvaavkeekp daviiagdly draippteav
       61 dlldellrrl imecettvla iagnhdspdr ldfgtrlmes rglhlagrlr adlkpvvlhd
      121 ehgevhvylv pyadpaqvrl tleddsirsh ddalraivar ieaeanphar rvfvghafvt
      181 qggepqpnts eserplaigg aehvnaahlr qfhysalghl hqahhvgder iryagsplky
      241 ssseanhrkg wlvvemdaag aiqiekrela plrdmrrvsa sieeieneha rsddyvfvtl
      301 lndnpvlfpm ekvravypna lhverrpass svqiedgads asrtarqaad pvelfaafyh
      361 evkgmplead krklfeetfa dvvkseggav
//
LOCUS       WP_006039214             405 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Paenibacillus curdlanolyticus].
ACCESSION   WP_006039214
VERSION     WP_006039214.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus curdlanolyticus
  ORGANISM  Paenibacillus curdlanolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 405)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Paenibacillus curdlanolyticus"
                     /db_xref="taxon:59840"
     Protein         1..405
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44343
     Region          1..398
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkvlvinags sslkyqlydm rdesvlasgr verigmdssi vtheppgkpe vrsvseileh
       61 ttavrrvidm lvdpnvgvia nmneidavgh rvvhggeafk qsvivtpevk leikklfdla
      121 plhnpahmmg ilaveanlpe vpqtvvfdta fhqtmpresy lypipmvlyr rhkvrrygfh
      181 gtshayvsaq aasflkqple slklitchig ngasctaikd gksfdtsmgm tpleglmmgt
      241 rsgdldpavv pfvmnkedls vsevnsmlnk hsglqaisgl ssdmreitea igegdknakl
      301 afdmytyrvr kyigayaaam ngvdtivfta gvgenssvlr kavcegltfl gleldeernn
      361 arskevrfit kdtsrvkvlv vptneellia rdtyalvneq seasl
//
LOCUS       WP_006039761             386 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Paenibacillus curdlanolyticus].
ACCESSION   WP_006039761
VERSION     WP_006039761.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus curdlanolyticus
  ORGANISM  Paenibacillus curdlanolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Paenibacillus curdlanolyticus"
                     /db_xref="taxon:59840"
     Protein         1..386
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=40029
     Region          <1..386
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mktfqgyara ngdfgirnhl liiptvicsn qvvnriaqlv pntvaiphqh gcsqigadkd
       61 rtfevlagtg mnpnvgavli vslgcevvdp eqlaaairrt gkaveffdiq svggsvkaiq
      121 hgadiakrlr veldaqplve vpysalrvgv kcggsdatsg lasnpalgva sdliianggg
      181 ivigetteii gaehiladrc vnaevsdkly aivnrferev ekvgadmrgg npspgniagg
      241 lstieekslg ciskcgtapi qgvieyaeql pgaglyfmds pgndiecvsg maaggahivc
      301 fttgrgtptg aavvpvikit anqrmyekms dnvdvnvcgl ltgeidlaea gawigqeiye
      361 vaagkltaae iighqefsin rigpsl
//
LOCUS       WP_006040113             184 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Paenibacillus
            curdlanolyticus].
ACCESSION   WP_006040113
VERSION     WP_006040113.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus curdlanolyticus
  ORGANISM  Paenibacillus curdlanolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 184)
  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 184)
  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   3  (residues 1 to 184)
  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   4  (residues 1 to 184)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 184)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Paenibacillus curdlanolyticus"
                     /db_xref="taxon:59840"
     Protein         1..184
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21032
     Region          <97..184
                     /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"
ORIGIN      
        1 mktilvideg nnsdllsrmr eggrtvhhva sdkdacslia vadaavmavk lermtdcqas
       61 laamrrlpif wycteqrlpq qmdwgfsldg vifpsmsstd iqhmlqfgar vhqqrkrwtd
      121 ereqllqrie erkwidqaka vlceirgine aeaydflrkq amndrkrige vaasivkvyq
      181 lihg
//
LOCUS       WP_006040384             296 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Paenibacillus
            curdlanolyticus].
ACCESSION   WP_006040384
VERSION     WP_006040384.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus curdlanolyticus
  ORGANISM  Paenibacillus curdlanolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 296)
  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 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 296)
  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   4  (residues 1 to 296)
  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 296)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Paenibacillus curdlanolyticus"
                     /db_xref="taxon:59840"
     Protein         1..296
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35103
     Region          43..290
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <191..285
                     /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 mlavnmewip ritlmgfvsy kslwmhfkrt sdehilyiik sgelhiqeeg qrfilregdv
       61 fmlephlehe gfemhicdyy fihfkhpdis altiedplsf aqaffledhe hqqhnrscfp
      121 kqmnltsnsa ksqiygglne mlrlyrrkny nraltalkls elfiwmsrey mmlvlqsnqk
      181 rttksnlkvy elldyihqhy askitserie sefdcnfdyi nrtfnqltgy siahyvnkvr
      241 idharellqt tklsigeiae lvgffdiyhf skvfkryvgv spttyfkgiq etvygl
//
LOCUS       WP_006040627             265 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Paenibacillus
            curdlanolyticus].
ACCESSION   WP_006040627
VERSION     WP_006040627.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus curdlanolyticus
  ORGANISM  Paenibacillus curdlanolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 265)
  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 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   3  (residues 1 to 265)
  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   4  (residues 1 to 265)
  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 265)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Paenibacillus curdlanolyticus"
                     /db_xref="taxon:59840"
     Protein         1..265
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30473
     Region          1..264
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <153..263
                     /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 mhmqiklpql elhkivnrfe nvphahesdy qltipthgtc hftyenkqvt lsageglllh
       61 prdrhsfhln deagviivvv kdqrlqplmd irrdeqavrh hfeptvitry frqwtstmfe
      121 vdaldrlaae etelrvlgdl qglladskpl qparlpvwss adphiarvle yvhahyteql
      181 didsmaaval qsrfhfirsf ksatgftpyq yvlylrmeqa kqwlaqtvdt vtdisfklgf
      241 ssasqfyraf eksvgttpeq yragi
//
LOCUS       WP_006043800             401 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Prevotella pallens].
ACCESSION   WP_006043800
VERSION     WP_006043800.1
KEYWORDS    RefSeq.
SOURCE      Prevotella pallens
  ORGANISM  Prevotella pallens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Prevotella pallens"
                     /db_xref="taxon:60133"
     Protein         1..401
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44021
     Region          1..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkilvlncgs ssikyklydm tdesvlaqgg aervgldeaf vkvtlkdgsk ekimhdmpdh
       61 kegvkfvfql lldpkygalk sldeidavgh rvvqggdlfe kscivtkkve egieslidla
      121 pvhnlghlrg iravdalmph tpqvtvfdna fhstmepyaf lyavpyemye kyhvrrygfh
      181 gtshryvshr aceflgvdyk sqkiitchig ngasmaaikd gkvidtsmgl tpleglmmgs
      241 rsgdidasav tymmeklgka pqemadylnk esgvlgitgi ssdmreieaa eatgnerail
      301 alkmysyrik kyigayaaam ggvdmivwta gvgenqtglr ldacqglefl gvkmdaeknk
      361 crgveriisa ddskvkvlli ptdeeiviar dtqelvsear k
//
LOCUS       WP_006047141             206 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Paraburkholderia].
ACCESSION   WP_006047141
VERSION     WP_006047141.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 206)
  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 206)
  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   3  (residues 1 to 206)
  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   4  (residues 1 to 206)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 206)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 206)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..206
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22836
     Region          13..196
                     /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"
ORIGIN      
        1 mnagarrifd dlrtlrvvvi hppgddrsvl eeqlrrigcp vraiwplpah lptdadviff
       61 lvgpeirnag nwsaadtqat lialsdyenp talkmlldtq ahgvitkpyr stgvlstlvl
      121 arassgyqqr lhakigklee aikarrhier amrilidahr lseneayehm rsratelrvt
      181 vgeiativid ahegmeklgl gkrskl
//
LOCUS       WP_006047323             277 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Paraburkholderia graminis].
ACCESSION   WP_006047323
VERSION     WP_006047323.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia graminis
  ORGANISM  Paraburkholderia graminis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 277)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 277)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Paraburkholderia graminis"
                     /db_xref="taxon:60548"
     Protein         1..277
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30743
     Region          18..101
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          127..276
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mnpvgkalwf ieshfaeelt lddiahcgcv srfhlarafe aatgvpvmry vrgrrlseaa
       61 rrladgapdi ltvaidagyg sheaftrafr eqfgltpeal rarghldnlv ivepikmdet
      121 llthlapprf edgrpflvag lserytcesa aaipsqwqrf neyfgkvpgq vgnvaygvcy
      181 naddagnidy lcgvevsdfs tlpaefsrlr iaaqryavfs hrehvstirr twntiwntwl
      241 pasghlpada pnferydakf dpvsgmggle iwlplka
//
LOCUS       WP_006048812             352 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Paraburkholderia graminis].
ACCESSION   WP_006048812
VERSION     WP_006048812.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia graminis
  ORGANISM  Paraburkholderia graminis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Paraburkholderia graminis"
                     /db_xref="taxon:60548"
     Protein         1..352
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38761
     Region          1..351
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mgitvrnlqk rfgdfvaldn vsldfppgel vallgpsgcg kttllrviag leyadggqve
       61 lqgqdvatvg arerevgfvf qhyalfrhmt vfenvafglr vkprkerpse avirekvhel
      121 lklvqldwla qrypselsgg qrqrialara lavepkvlll depfgaldak vrkelrswlr
      181 rlhddlhist ifvthdqeea levadrivvl nhghveqvgs pqdvydhpqt sfvyeflgaa
      241 nrlhgkvdas gfvvdgaalp vaigtdfsgp afayvrphdl qlypqsaghr egivvdvrrv
      301 vtlggsvrve lagregnlle aeldreswre lqlavgdgvt avpralrvfp aq
//
LOCUS       WP_006049393             341 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [Paraburkholderia].
ACCESSION   WP_006049393
VERSION     WP_006049393.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 341)
  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 341)
  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 341)
  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 341)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..341
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=37152
     Region          19..339
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mtnlarrall raaaaapmag algfpaivra asgpefvfky gnnlplthpl nvraqeaanq
       61 ireaskgrme irifpnnqlg gdtdmlaqvr sggiemftps alvvstlaps vainavgfaf
      121 ndynqvwaam dgklgayvra amqkaglesf ekmwdngfrq tttsngpits aqtmrglkir
      181 vpvsplsidm fkglgaapts lqfsevyssl qthivdaqen plpivqvakl yevqkycslt
      241 nhmwdgywfv lnprawqrlp kdlqgiasda fnqcalkqrd dvrklndaav adlqskglai
      301 nrpapdsfra alrqagfyaq wkgkfgneaw dlleqsvgkl a
//
LOCUS       WP_006038015             364 aa            linear   BCT 20-JAN-2025
DEFINITION  GerAB/ArcD/ProY family transporter [Paenibacillus curdlanolyticus].
ACCESSION   WP_006038015
VERSION     WP_006038015.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus curdlanolyticus
  ORGANISM  Paenibacillus curdlanolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Paenibacillus curdlanolyticus"
                     /db_xref="taxon:59840"
     Protein         1..364
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=40739
     Region          2..355
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 mitprqlast vilfligsss lfllggtaer dawmsvcigv magllllsfv tlhiqklepn
       61 rnlieifkly fgriagfafg lmyvvyysyk sirnvrefad lsimfllsdt plsilvlmic
      121 lisayavvgg pgvffrmaev llpillliyv flfclligag vidfsrltpm ldqgfkpvwd
      181 aaipeiisfp fgemtlflmf wrytetsefs qvvrmtvkgy lfagvfitvm nvitiaslgs
      241 fanwstvpll qatnfidign iferidpivs lllfsavyvk ltayylgasl afaylfgisl
      301 riaaipvgig ifigslsfrs ymqqvnfgfe qnlryhfpif qiaipillll vmrirtgvrt
      361 tker
//
LOCUS       WP_006049962             210 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: pilin [Paraburkholderia].
ACCESSION   WP_006049962
VERSION     WP_006049962.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..210
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=21387
     Region          43..177
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mivtlpyspy sqstlahsrf ararwsatla racrrvgsrl glgftlielm ivlaivgvia
       61 ayaipayqdy larsrvgegl slassarlav senaasgnaf gggyasppat rnvesvhvdd
      121 dsgqitvaft trvapagsnt itlvpsvpdn idaptarvsl akgavqagal awecfaggkt
      181 asslpapgag pmpaqaptlp shlsppecra
//
LOCUS       WP_006051213             661 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Paraburkholderia graminis].
ACCESSION   WP_006051213
VERSION     WP_006051213.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia graminis
  ORGANISM  Paraburkholderia graminis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 661)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..661
                     /organism="Paraburkholderia graminis"
                     /db_xref="taxon:60548"
     Protein         1..661
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=73324
     Region          35..572
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 makqntsdll enlkslnapq lrrllieqlt kqklglywes daierdaaln advvlprlip
       61 dashtptgtn hhrnliiegd nfdslrllra thagkirviy idppyntgnk dwvyndkfvg
      121 andrwrhsqw leflyqrltl ardlltsdgv ilvsindenr srlellmdev fprrragslv
      181 wrtkdtgndl sqrfshvheh vlvyanagfk fngratskhk frnpdkdsrg dwspqpltan
      241 ktlverpnty ypiqnpetgy wypcdpdstw rfasekeirk rldneevaiq aalgglrsdt
      301 ieqliekkli yfppcsssev mqfdtkqdll naisngkgpt lpkkktpllr edlpdldfwv
      361 gkpiaagrps rkelwtskpe serlaplgsw iagmneqvda leededdepv vlrsarggva
      421 tdevknilgs kafpypkpis likgllaqat tpgdivldff agsgttgqav lelnaedggq
      481 rrfilcsste attkepaknl crdvcaerlr rvmigyrdkp gysvaqggef aylqldkiea
      541 adiafdgkaq havsllcmre aaiapisved aeihliakgg dwlavlcaqi epetvdalaa
      601 lpsaygvtrl avycprpkal aglltdrgvd antysitdal legqvsnntk avdivpegas
      661 a
//
LOCUS       WP_006051312             209 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Paraburkholderia].
ACCESSION   WP_006051312
VERSION     WP_006051312.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 209)
  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 209)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 209)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..209
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22713
     Region          3..207
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 msyhdeqesi eglkawwaqw gnattwivlv alvaaagwng wnfwqrrqaa eaavlydqvq
       61 qavasgdkak isrvaadmed kfsrtayaqm talgaakaly aagdeagaka qlqwtidhak
      121 ddefkqiarl rlasllldek aydqglalla epqsdafkgi vangrgdlla aqgkrddara
      181 ayklaleslp kndsserqli qfkldalgg
//
LOCUS       WP_006051458             300 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Paraburkholderia].
ACCESSION   WP_006051458
VERSION     WP_006051458.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..300
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33330
     Region          14..264
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mpevrllvda nnhlgegplw dvkeerlywi dstaaeiysc radgsevkrf fvprhigsma
       61 lreqggavva langlhfydf daqtvqfiad pesddpetrf ndgkvdrrgr fiagtmsydf
      121 drydadrgqr strsgglyrl didgtlarld sgiscsngpc wspdnrtlyf tdtysremya
      181 ydydietgaa gnrrlfasar dmagtfdgat vdeegyvwsa lvfggrilrf apdgkldrvv
      241 efpvrnltsv mfggpnldtl yvttmgrpmw gipqkerekg glfavtglgv rglpeprfag
//
LOCUS       WP_006051877             306 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Paraburkholderia].
ACCESSION   WP_006051877
VERSION     WP_006051877.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..306
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32646
     Region          26..269
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mtasvdvrap ahapraallv dskctlgega twcattgrfy wtdiegarlw rydprdgrsm
       61 swtmperlat falcadphyl llglasrlaf fdlatgetrh ivdaepgrnt rvndgrcdrq
      121 grfvfgtkde gsplraiggf yrldrdltle rlplpapais nsiafspdga tmyycdsptr
      181 eiracdylad ggiandrvfa rltdatgepd gstvdrdggl wnaqwggarv vrygadgvet
      241 ervdvptvqp scvalggaql gtlyitsarv gldaaalagd sraggvfiat parrglpepv
      301 fagapa
//
LOCUS       WP_006052725             255 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Paraburkholderia].
ACCESSION   WP_006052725
VERSION     WP_006052725.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 255)
  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 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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (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   5  (residues 1 to 255)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..255
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28398
     Region          4..246
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <148..246
                     /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 mntlahqfpp deaplsamls hfrqlepvfd alpdvvffvk dadaryalvn rtlasrcgfk
       61 ektallgkta edvfprrfgr iytaqdegvi hvgnqmidql elhlypgrqp gwcltskqpl
      121 rdaagkiigl agisrdlrad esshpaysrl atvvqfiqen yvqplnlkql aamadmsvaq
      181 leryfhkvfh ltprqvllkt rldaatallv sndkvtdvaa lcgytdhsaf trqfkatvgv
      241 tpteyrmllh gtsrn
//
LOCUS       WP_006036815             241 aa            linear   BCT 20-JAN-2025
DEFINITION  phosphonate ABC transporter ATP-binding protein [Paenibacillus
            curdlanolyticus].
ACCESSION   WP_006036815
VERSION     WP_006036815.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus curdlanolyticus
  ORGANISM  Paenibacillus curdlanolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
REFERENCE   2  (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   3  (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   4  (residues 1 to 241)
  AUTHORS   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 241)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Paenibacillus curdlanolyticus"
                     /db_xref="taxon:59840"
     Protein         1..241
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=26893
     Region          1..241
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mirvshltkq ipggpkvldd lsfeieagef valkgasgsg ksmllrclal rekwskgtyi
       61 fdqvnvqeqf lkgrskvrre iayleesprl yqdktalrnv qigsvnqtpf wrrwtgmvrs
      121 ddymgamdti eklglldkah mkgnklsgge rqriaiaral vhgakvilad epvtgldphs
      181 adqvlgdlkr lckeqglivi aalhqgdyae rfadrtfgls ggkllfdvkg rrltemerrk
      241 l
//
LOCUS       WP_006059197             467 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Holdemania filiformis].
ACCESSION   WP_006059197
VERSION     WP_006059197.1
KEYWORDS    RefSeq.
SOURCE      Holdemania filiformis
  ORGANISM  Holdemania filiformis
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Erysipelotrichaceae; Holdemania.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Holdemania filiformis"
                     /db_xref="taxon:61171"
     Protein         1..467
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50187
     Region          13..>467
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mktnairgyv vdrlqyalnp ssvavigasr cpgkvghkvi dglqkwgyqg kiypvnprae
       61 kvaglkaypt lreieepvdl afiavpahlv ksiledcvak evkivviats afkeigrgel
      121 qdelteycra nelpligpnl vgmgspalnf ncgfipylpt lgpvamisqs ganllaalgt
      181 sqkdhygmsf fvglgnkadv dfsefiayag kddntkciav ymegldspea fieacqsvak
      241 pvvaikvgrs pigvkaafah tasenvrdda yydevfaqag alrattwqef ldvslalgtq
      301 palrgenvvm itngggsgll scdhfdrcgl plkelkeisp slagriraym pmfgsplnpv
      361 disgtasptq ykgafmqamr dpavdgilgs icptavtnvd avvdvvievh dryrrlgkpf
      421 imecqggeec qraimklrdh gipayptaeq avnamvalyr ygqmqkk
//
LOCUS       WP_006059723             156 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Holdemania filiformis].
ACCESSION   WP_006059723
VERSION     WP_006059723.1
KEYWORDS    RefSeq.
SOURCE      Holdemania filiformis
  ORGANISM  Holdemania filiformis
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Erysipelotrichaceae; Holdemania.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 156)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Holdemania filiformis"
                     /db_xref="taxon:61171"
     Protein         1..156
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16743
     Region          15..154
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mnenlttdld tlldnakalc sgetdriccl anlsalimqs mprinwagfy lmkqgelvlg
       61 pfqgkpacth ialgkgvcgt aaqkneclvv rdvhqfpghi acdeasrsei vvplvyqsev
      121 vgvldidapi pdrfgsveea vlrelgawig elfald
//
LOCUS       WP_006060570             422 aa            linear   BCT 20-JAN-2025
DEFINITION  galactokinase [Holdemania filiformis].
ACCESSION   WP_006060570
VERSION     WP_006060570.1
KEYWORDS    RefSeq.
SOURCE      Holdemania filiformis
  ORGANISM  Holdemania filiformis
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Erysipelotrichaceae; Holdemania.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   McAuley,M., Kristiansson,H., Huang,M., Pey,A.L. and Timson,D.J.
  TITLE     Galactokinase promiscuity: a question of flexibility?
  JOURNAL   Biochem Soc Trans 44 (1), 116-122 (2016)
   PUBMED   26862196
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Holden,H.M., Thoden,J.B., Timson,D.J. and Reece,R.J.
  TITLE     Galactokinase: structure, function and role in type II galactosemia
  JOURNAL   Cell Mol Life Sci 61 (19-20), 2471-2484 (2004)
   PUBMED   15526155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Holdemania filiformis"
                     /db_xref="taxon:61171"
     Protein         1..422
                     /product="galactokinase"
                     /EC_number="2.7.1.6"
                     /GO_function="GO:0004335 - galactokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0005534 - galactose binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0046835 - carbohydrate phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=46386
     Region          32..422
                     /region_name="GalK"
                     /note="Galactokinase [Carbohydrate transport and
                     metabolism]; COG0153"
                     /db_xref="CDD:439923"
ORIGIN      
        1 mnkselkaal eqqrpritsl ygqeqverqi arygqliddy erafgnmdca lfsapgrtev
       61 ggnhtdhqhg rvlaasvnmd aaaaagrreg evvfysegfe ikpvsladlf vhpeekntse
      121 alirgvlagf vqrgykiggf qavsnstvlk gsgisssaaf evlvgtilsh lyndgqvsaq
      181 eiakigqyae nvyfgkpsgl ldqmacsvgn fvtidfkdpq nvlveqvdfd fnhsqialcl
      241 vdtrqdhadl sdeyglmpae mrqvaayfga evlrqvdpae fyrrlrevrs qvqndrailr
      301 aihffeedar vplqvqalkd qdlkrffelv iesghssfmy lqnvtspsdi rhqslalala
      361 lsenvlkghg awrvhgggla gtiqafvpla lletyqkvmd dcfgagschv lsirpeggvr
      421 li
//
LOCUS       WP_006060689             157 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Holdemania filiformis].
ACCESSION   WP_006060689
VERSION     WP_006060689.1
KEYWORDS    RefSeq.
SOURCE      Holdemania filiformis
  ORGANISM  Holdemania filiformis
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Erysipelotrichaceae; Holdemania.
REFERENCE   1  (residues 1 to 157)
  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   2  (residues 1 to 157)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Holdemania filiformis"
                     /db_xref="taxon:61171"
     Protein         1..157
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17637
     Region          92..156
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mrkefllifc fvflllplip qrvvdldamr gqpitvtieg avrepvtltc ppytelgell
       61 dqvtllddad lspfsmtmiv kdhdvfqiph fqetprisin tasieqltql pgvgqataek
      121 ivayraehgl fqtledlmqv pgikqkkwea lkeficl
//
LOCUS       WP_006068829             712 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Borreliella valaisiana].
ACCESSION   WP_006068829
VERSION     WP_006068829.1
KEYWORDS    RefSeq.
SOURCE      Borreliella valaisiana (Borrelia valaisiana)
  ORGANISM  Borreliella valaisiana
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Borreliaceae; Borreliella.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 712)
  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   3  (residues 1 to 712)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Borreliella valaisiana"
                     /db_xref="taxon:62088"
     Protein         1..712
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79347
     Region          1..712
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdssdvidkf knsfkeesie nisdieqall nlelssdqdi vnsifrnlht ikgssgmfgf
       61 nftaslvhei etvldvvkdg ratfnqaaid atlmsvdfir eliegdevis eldfdkrkqf
      121 lvneikkvle isnvkdafqe tlkndfsnpn nsfiledvkv nsdnkfddea lrsefksyki
      181 lfspakgilf hghkpinlls klinlgsghv kakvdnipdl elispdnvyv dweirldtee
      241 sresiedifv fldsqskvdi qelekcfead kgdgvglesf nllhldrsik dsgnltfkks
      301 efaeksffng dksrfnvqdd tvrskvnias ikvdskkldh lvnlvgelvt iqsklskeae
      361 nrnsnvlnsi saefslline lrdyttglrt vpleilfvkf qrivkdlsts lgksivyray
      421 ggdtvldksi ieklneplvh lirnsidhgi espeereglg kdpkgiikls acqsgdsviv
      481 iieddgrgld knkilkkaie rniisdsvak tlsdidvynl ifepgfstas svtdisgrgv
      541 gmdvvkkqve slrghvvles elgkytrtkl ifpltlaiie gwlvrvkdeh fivplsnves
      601 clesnklisq idgvetknnv mnyrgsmisf irlreffqvs seksfneqvv vvntnsgkmg
      661 ivvdevlgqh qtvikalgki ysrvegvsga tilgdgslal vvdidaitkl mr
//
LOCUS       WP_006071094             651 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Brucella suis].
ACCESSION   WP_006071094
VERSION     WP_006071094.1
KEYWORDS    RefSeq.
SOURCE      Brucella suis (Brucella melitensis biovar Suis)
  ORGANISM  Brucella suis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 651)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 651)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 651)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 651)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Brucella suis"
                     /db_xref="taxon:29461"
     Protein         1..651
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=70384
     Region          28..651
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msgelngndt saqaavsags vlegaafade geqhnesmkt lvlgalgvvy gdigtspiya
       61 frealhaaat ngilarsdil gvvslifwal tlvvtvkyvl fvlradnnge ggilslmalv
      121 raalkgrpdl ilgvgicgaa lffgdavitp aisvlsameg leivapnltp fvvpatvvil
      181 vtlfsvqklg tgrvaivfgp imalwfvalg asglwhifdd ptvmaalnpy yavrfltvsp
      241 avafvtvgav flamtgaeal yadlghfgrk pivrawlwiv fpclllnyfg qaafilshge
      301 aaalpffqmi psfalwpmvl lataatvias qavitgaysv arqavqlnil prleiqhtse
      361 klhgqiyipr vnlllglavv ilvlgfekss nlaaaygiav tgnmlvttvl lyivmtriwn
      421 wrvsralpii lgflvidmlf fsaniikvhe ggwasigiat vlvlimwtwv rgtrhlfqkt
      481 rkaevpldli veqmakrppt ivpgtavflt gdpksaptal mhslkhykvl hennviltvv
      541 taskpwvasa drarlsqyne rfmlvtltfg ymqqpnilra lglcrrlgwk fdimttsffl
      601 srrslkasvh sgmplwqdkl fillartasd ateyfqiptg rvveigtqvn i
//
LOCUS       WP_006070176             331 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein [Vibrio].
ACCESSION   WP_006070176
VERSION     WP_006070176.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 331)
  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 331)
  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 331)
  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 331)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..331
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=36991
     Region          1..326
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mkklimatav smlalstsvm sattirighg anenyhlhra lekfkedvet ksegkfevqi
       61 fansqmgpdr emiegvqsgm lqmavspssf ysswdpsfdv velpfiypsk qaaldtvhsp
      121 agdqlltkln nmnlqgigwl engvrhvtnn srpvetpedl kglkirtmkv pahvktfnsl
      181 nasatpmnfg evysglqqgv idgqenpiah iyaqrfyevq dyvsltshvv tfyipvmnle
      241 fwhglsaedq elikgsmrda eiyqqelvsa eegqqieefk kqgtqvnals eeqlqlfida
      301 tepvrqeyke klgadvydaw matiqevtsk s
//
LOCUS       WP_006072032             312 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella suis].
ACCESSION   WP_006072032
VERSION     WP_006072032.1
KEYWORDS    RefSeq.
SOURCE      Brucella suis (Brucella melitensis biovar Suis)
  ORGANISM  Brucella suis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
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
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Brucella suis"
                     /db_xref="taxon:29461"
     Protein         1..312
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=34226
     Region          1..309
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 miefdritkn yngraavdev sftiephsia aivgtsgsgk ttllrmvnrl eeptsgeiri
       61 dgqsildepg helrrrigyv iqqhglfphr tvgeniatvp allgwpkqri earvdellel
      121 fqlepgayrd ryphelsggq qqrvgvaral aagpnillmd epfgaldpvi rakaqedlka
      181 iqrrfgttil lvthdmeeai slgdriavmd egkllqfgpp aeilarpate fverlvgtge
      241 rpfrllsltg lktvlqpgda sgeplpvtas qrdalaellw sgrralpvld edgrslgrvt
      301 lekllhqaer pa
//
LOCUS       WP_006073619             381 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: exonuclease SbcCD subunit D [Vibrio].
ACCESSION   WP_006073619
VERSION     WP_006073619.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..381
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43001
     Region          1..271
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          <288..356
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkfihtsdwh lgrqfhnvsl ledqkqvlnq itryvtenhi daliiagdiy drsvpptaai
       61 evldgflnhi vqdlnvpvim isgnhdgakr lgfgskqfdk aglhiissle qlctpveivs
      121 aqdsvvhfyg mpysdpetvr hhydiqinnh ddahaylasq ignvldkdvh nvvishcfid
      181 gaetcesert lsiggadrvs yehfksfdyv alghlhqaqk rgletirysg simkysfseq
      241 hhrksvtlve icdesgeitt ralplnaphd mrvlegelen llelgrsdan fddyllvrlt
      301 dkhaildpma klrevypnvl hlekpgmlvg vdkeisqarl grsevdmfrd fflevqgdem
      361 tdnqkdmlse vvmslkkqse e
//
LOCUS       WP_006073743             180 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit [Vibrio].
ACCESSION   WP_006073743
VERSION     WP_006073743.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 180)
  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 180)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 180)
  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   4  (residues 1 to 180)
  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   5  (residues 1 to 180)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..180
                     /product="TRAP transporter small permease subunit"
                     /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=20233
     Region          <39..169
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mrsliyierl fnkvadllgw lssilfllll vnvvydvvmr yvfndvsiaf qemewhlfsa
       61 vfllgvpyai kagghvrvdv fyerlsikaq aiidllgtfv flfpfcllva wfgidfakes
      121 yalgetsgdp gglpyrwiik amiplsfffm aiagvglvlh slnklfnphl iyakssgshe
//
LOCUS       WP_006074427             159 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: pilin [Vibrio].
ACCESSION   WP_006074427
VERSION     WP_006074427.1
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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..159
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=16512
     Region          6..148
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 myqginqkgf tlielmivva vigvlaaval pqyqkyigks eaasalatls glrtnieayt
       61 leqgsfpdte ttpalktrlg fpnaiieaie aeagvssagn iilsfdqvpn aspsvsnykl
      121 alarnaqggw acistatees gvlpkgcqys esvsvtvpe
//
LOCUS       WP_006074537             371 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Brucella suis].
ACCESSION   WP_006074537
VERSION     WP_006074537.1
KEYWORDS    RefSeq.
SOURCE      Brucella suis (Brucella melitensis biovar Suis)
  ORGANISM  Brucella suis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
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   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   3  (residues 1 to 371)
  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   4  (residues 1 to 371)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 371)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 371)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Brucella suis"
                     /db_xref="taxon:29461"
     Protein         1..371
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39255
     Region          27..358
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(99..101,122..123,172,224,248)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mrktlfsgva laaviafggs awadvlvgig ipvtgpnavy gaqiqkgaea aikevndagg
       61 ingekiaiti gddvsdpkqg isvankfaad gvkfvighfn sgvtipasqv yaengileis
      121 pgatnpqyte qglwntfrtc grddqqgtva gqyifdhfkd akiavihdkt pygqgladet
      181 kkklnelgtk etlyegvnvg ekdfsaliak lkqagvnvvy wgglhpeagl iirqmadqgl
      241 kaqfisgdgi vsndlasiag pavegtlntf gpdprnnpdn aelvkkfrda gfepeaytly
      301 syaavqslaq aakaagsndp qevakamkek gpfktvlgdl sydekgdpkl pgyvmykwek
      361 gadgkynyiq q
//
LOCUS       WP_006074540             157 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Vibrio].
ACCESSION   WP_006074540
VERSION     WP_006074540.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..157
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16907
     Region          4..151
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mnlenyerla kqataliese tdfianlsni sallfmeldd lnwagfylmk qgelvlgpfq
       61 gkpacvripv grgvcgtaae tntiqrvydv hafeghiacd aasnseivip fsiggevvgv
      121 ldidsptigr fseideeglk nfmnsvekvl nshtnaa
//
LOCUS       WP_006080397             271 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Shewanella baltica].
ACCESSION   WP_006080397
VERSION     WP_006080397.1
KEYWORDS    RefSeq.
SOURCE      Shewanella baltica
  ORGANISM  Shewanella baltica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 271)
  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 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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Shewanella baltica"
                     /db_xref="taxon:62322"
     Protein         1..271
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30658
     Region          27..265
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          189..265
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mlsrqldsin aiieqapnmp sfvktiemqk gyvdvlhqhc whqlifplqg llqteadgal
       61 flvphttalf vpagvihesv aitdtcfigv ylnpmygrdy gamikpvams aflrelvltl
      121 rkqcafntpi nvepmvqapi lrllevlydq insaggqtfk llipqdrrlk lifehltqtp
      181 aldfslvkwg ervgasertl srlfvrefgs sfvlwrqhlr liyslsllat dlsiqnvahq
      241 igyqndssyi kafkerfgmt pqrfrlgdhg i
//
LOCUS       WP_006081169             381 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Shewanella baltica].
ACCESSION   WP_006081169
VERSION     WP_006081169.1
KEYWORDS    RefSeq.
SOURCE      Shewanella baltica
  ORGANISM  Shewanella baltica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Shewanella baltica"
                     /db_xref="taxon:62322"
     Protein         1..381
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42092
     Region          1..268
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          267..354
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkfihtsdwh igrqlhnqsl lddqafvleq iialadehkv davivagdiy drsippanav
       61 allddvlnrl vqdlgvqvim iagnhdgher lgfaakqmaa sglhiigpls adihpitlss
      121 ssgdvvfypl pyaepatvrq vfeceasshe mamdvllekv rqhdsqglpk vvishcfldg
      181 gseseserpl siggadkisp klftefdyva lghlhgpqyk gaehvrysgs ilkysfseqh
      241 qhksvtlvel gtqtpidirl lpltsmrdvr ilegeldtll aqgktdakre dylmvrlldk
      301 haildamgkl ravypnvlhl ertglmagqq qvalsrdhik kgemdmfcdf fsqvsgeslt
      361 qaqqavmddl ltklhneerq a
//
LOCUS       WP_006081692             901 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Shewanella baltica].
ACCESSION   WP_006081692
VERSION     WP_006081692.1
KEYWORDS    RefSeq.
SOURCE      Shewanella baltica
  ORGANISM  Shewanella baltica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 901)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 901)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..901
                     /organism="Shewanella baltica"
                     /db_xref="taxon:62322"
     Protein         1..901
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=97494
     Region          1..714
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 msqrtlhslf kptsvaiiga sntekragnv lmknllssgf sgpimpvtpk yravmgvlay
       61 pnieslpikp dlavictrac rvpaivetla qfgckvaiim asgmaqefne dgvslldltm
      121 qnakrygmri lgpnslgmll pplglnasla hasalpgkia fvsqsaaict tvldwannkg
      181 igfssfislg datdinfdel ldylgrdsrt saimlyidsv nekrhflsaa raasrnkpil
      241 viksgrsaeg araaklhtgg vggndavyea afrragmlrv ndlielfaav eslahsnplq
      301 gerlgiisng ggpavlavde limrggklae lsddtiakle avlpntwsrq npidiigdan
      361 asryakalti lmdsneldai lvlhspsalg esveiadali svihahpkkn rlniltnwsg
      421 edsayqarkr ftkggistyr tpegavgafm hmveyrrnqk llqevpqsip dniptdsyta
      481 rtllqaaqak gksvlethea spilraygln tidtwfvkda deavaianea gyplalkvqs
      541 pnilhksdvh gvmlnltsae dirhaasait qrvhqanpea iiegmivqkm altagaqeir
      601 vavisdpvfg paiclgeggs ewdptndaav alpplnmala rymviqalkn hklkdrhlpl
      661 gldmnalcvm ltqishiiid cpeiasldln pvlaagenit lldvnirlhd anadsssrma
      721 impypkelee vaelknglkv mlrpilpede pkhlafdnsl sdedrykryf gvrskmthee
      781 mavltqidya remafiatak gpdgdditlg avrasidpdn teaefamavr gdhqgiglgk
      841 llleklikyy qandtpvltg ftmfenrnma slakslgfkv sfdmeehlik mhmdlkppsd
      901 e
//
LOCUS       WP_006037151             366 aa            linear   BCT 20-JAN-2025
DEFINITION  GerAB/ArcD/ProY family transporter [Paenibacillus curdlanolyticus].
ACCESSION   WP_006037151
VERSION     WP_006037151.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus curdlanolyticus
  ORGANISM  Paenibacillus curdlanolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Paenibacillus curdlanolyticus"
                     /db_xref="taxon:59840"
     Protein         1..366
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=40827
     Region          2..326
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 mrkeetitgr qlislvimtq lgtevlslph teaeiaghdt wlavllsgla aqvgilliww
       61 lgsryplrni ygylplivgk pigagvilly gcyyaisglv lillytdilk rwifvltptw
      121 viilmllivc gyaatstlkr laflsqsfmf fvyisfllii fsgiygldak nllpilpsgw
      181 spvikgiypa fssyvgyell lyaypyvktk skknlllamt langftivfy vavclictmk
      241 fglgqlnmip epivfilkny rvevlqsidi lfliyyasii sttiyvyyfl aanaflhlrs
      301 qglgkqhrwv wtivglgfig sffvtkrsdi lhfasiqdqa sviivvvlpi vllmisgirg
      361 larsgt
//
LOCUS       WP_006083232             257 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Shewanella baltica].
ACCESSION   WP_006083232
VERSION     WP_006083232.1
KEYWORDS    RefSeq.
SOURCE      Shewanella baltica
  ORGANISM  Shewanella baltica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 257)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Shewanella baltica"
                     /db_xref="taxon:62322"
     Protein         1..257
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=29115
     Region          24..241
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mdfparikqq tcmdclsgks lgfeirmafq piihwpsrei sgyealvrgp egegaawvfa
       61 rindsnkyyf dqacrvkaie tasklgldkm lsinflpnav ynpetcirat ieaadmygfd
      121 ihkimfevte geqivdrakl vrifesyakr gfitaiddfg sgfadlswld alrpqvlkld
      181 itlirdidvd kekqqavdei lriclelntr vlaegvesea elnylagigi eyfqgyyfak
      241 pklehlstye elnfhap
//
LOCUS       WP_006083940             372 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Shewanella baltica].
ACCESSION   WP_006083940
VERSION     WP_006083940.1
KEYWORDS    RefSeq.
SOURCE      Shewanella baltica
  ORGANISM  Shewanella baltica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 372)
  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 372)
  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 372)
  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 372)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Shewanella baltica"
                     /db_xref="taxon:62322"
     Protein         1..372
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40813
     Region          34..366
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mrkfgsvlvl mllmglsgcn pvasdaqnva vshaatddpq aipaiewrla tswpknfpgl
       61 gmaperfahl vddmsngrlk iqvygagelm pafaifdgvs qgkiqmahaa syywkgkapa
      121 aqffssipfg mtaqemngwl hygggmalwd evyrpfgiip laggntgmqm ggwfnkpint
      181 iadfkglkir mpglggevlk rvgaipvnma grelygalqt gsidaaewvg plndlafglh
      241 kvakyyyypg whepgsnmef linkaafesl pqdlqaivkv aarainqdml deyttrnvaa
      301 letlvndegv vlkafppkvl lelekiskqv ieeqanqdpl mrkvyaayha yeqgvrqyhk
      361 isedaygqqr qh
//
LOCUS       WP_006084332             677 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Shewanella baltica].
ACCESSION   WP_006084332
VERSION     WP_006084332.1
KEYWORDS    RefSeq.
SOURCE      Shewanella baltica
  ORGANISM  Shewanella baltica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 677)
  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 677)
  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 677)
  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 677)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Shewanella baltica"
                     /db_xref="taxon:62322"
     Protein         1..677
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=72739
     Region          12..669
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 msdpqqglsa ntgdwpkalf ytalifsifq iitaafhpvs tqvlrathig flllvvflsy
       61 pargksqpwq plawllglag mvtaayqwyf eadliqrsge ltdadmvigi tlivlvfeaa
      121 rrvmgwalpi icgiflaygl lgqylpgdlm hrgygfdqii nqlafgtegl ygtptyvsat
      181 yiflfilfgs fleqagmirl ftdfamglfg hklggpakva vvssalmgti tgsgvanvvt
      241 tgqftiplmk rfgyrsafag gveatssmgs qimppimgav afimaetinv pfieiakaal
      301 ipallyfcsv fwmvhleakr anlcglpkdq cpdpwaaike rwylliplfi lvyllfsgrt
      361 plfsgmvgla ltsivilgsa ivlrlssmam riafwialgv lcagffqlgi gvvfgviall
      421 vaicwfikgg ketltvclha lvegarhavp vgiacalvgv iigivsltgi astfasyila
      481 vgqdnlflsl vltmitclvl gmgiptipny iitssiaapa lldlgvpliv shmfvfyfgi
      541 madltppval acfaaapiak esglkislwa iriaiagfvi pfmavydpal mlqgdsllat
      601 afvvlkatvg igiwgviftg yllqklywwe rvigflagas lilatplsde igfglallfi
      661 vqhswrarkl krlaeqg
//
LOCUS       WP_006085377             122 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Shewanella].
ACCESSION   WP_006085377
VERSION     WP_006085377.1
KEYWORDS    RefSeq.
SOURCE      Shewanella
  ORGANISM  Shewanella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae.
REFERENCE   1  (residues 1 to 122)
  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   2  (residues 1 to 122)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Shewanella"
                     /db_xref="taxon:22"
     Protein         1..122
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12612
     Region          52..121
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mnitkcipai msamaltafl ttpaiaadtp tkaaakmqtq akteasdmas dakkampdaa
       61 qvnintasae qlqvlkgiga akaqaivdyr tkngkfnaid dlanvsgvga klieqnrhli
      121 kl
//
LOCUS       WP_006086068             682 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Brucella abortus].
ACCESSION   WP_006086068
VERSION     WP_006086068.1
KEYWORDS    RefSeq.
SOURCE      Brucella abortus (Brucella melitensis biovar Abortus)
  ORGANISM  Brucella abortus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 682)
  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 682)
  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 682)
  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 682)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Brucella abortus"
                     /db_xref="taxon:235"
     Protein         1..682
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=72999
     Region          16..681
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mteeqnakla pmeldevkar eleekfdsei rfrplapvaa rivgtlliil slfhyytagf
       61 gllpemihrg ihlafvlglv flvfpfsrkg ydepakpsll rplgisvidw glaiiavvav
      121 ihvplipldd lafrvgnpts tdvvlgslli lilleatrrs vgwplpiisv lfmlyalygp
      181 smpgilvhpg atvsqlvdhl ylttqgiygi algvvatyvf hfvlfgvfat riglgqlfld
      241 caawvagrfa ggpakvsifg salfgmisgs svanavtvgs ltipamirlg ykrhfaaave
      301 sasstggqit ppimgaaafl mieflnlpyt tiilaaivpa fmhffgvlmq vhfeakrtgl
      361 rgmtkeempd lkealkrdwp tiiplvvlia vllsgytpyl aafwgitlci avgllnprkr
      421 mtigevfegl rdgakyalav gaaaatvgii vgvvtltgvg fkisyivtst aaqlatyfgt
      481 ifpvswfapq tltllftlvm tgmvcilmgc gipttanyii matiaapalg llgvepivah
      541 ffvfyygvla ditppvalaa yaaagmagad pfktgntafr lglgkvlvpf vfvfspslll
      601 vtsnfnwpdf fiaffgcvig italgaalsg fflvrtkiwe nvllifaaml lvapeiyssi
      661 vglilllpvv vrhlvasrrp ay
//
LOCUS       WP_006087021             257 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Shewanella baltica].
ACCESSION   WP_006087021
VERSION     WP_006087021.1
KEYWORDS    RefSeq.
SOURCE      Shewanella baltica
  ORGANISM  Shewanella baltica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 257)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Shewanella baltica"
                     /db_xref="taxon:62322"
     Protein         1..257
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=29227
     Region          24..241
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mdfpaqikqq tcmdclsgks lgfeirmafq piihwpsrei hgyealvrgp ngegagwvfe
       61 rinesnkyyf dqacrvkaie tasklgldkm lsinflpnav ynpetcirat ieaadmygfd
      121 ihkimfevte geqivdrakl vrifesyakr gfitaiddfg sgfadlswld alrprvlkld
      181 mtlirdidvd kekqqavdei lriclelntr vlaegvesea elnylagigi eyfqgyyfak
      241 pklehlstye elnfhap
//
LOCUS       WP_006094337             288 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 5'-3' exonuclease [Bacillus].
ACCESSION   WP_006094337
VERSION     WP_006094337.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..288
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32206
     Region          1..277
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mkkvllvdgm allfrafyat svygqfmkrq dgtptngihg ymkhlltaaq aiepthivtc
       61 wdmgsttfrt esfsnykanr aappeelipq fdlvqemtsk lfipviglkg yeaddcigtl
      121 akeyaseaev yiltgdtdll qlvdtnvtvm llrkgignye yytpekiree kgvepwqivh
      181 akafmgdtsd nypgvkgige ktaykliqeh gtvaavleni aaltkaqrtk iendlenlni
      241 slqlaqihce vpiscsleeg lhtideekvr fvcdqmnwgr peifinml
//
LOCUS       WP_006094828             385 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: exonuclease SbcCD subunit D [Bacillus].
ACCESSION   WP_006094828
VERSION     WP_006094828.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..385
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44454
     Region          1..275
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          271..357
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkffhtadwh lgklvhgvym tedqrivldq fvqaveeekp daviiagdly draippteav
       61 dllndvlkki vidlqtpvia vagnhdspdr ihfgsslmkk qglhivgqfq fpyepvvlhd
      121 kygevhfhli pyvdpsivrh vmknedirsh ddamrifmne lsetmnqear hvfvghafvt
      181 ssgeaeents daerplsigg aeyvnshyfd kfhytalghl hqahfvrnet irysgsplay
      241 siseerhkkg yyiveldetg qveiekrlft prrqmrtvea kiddllkypt sedyvfvkll
      301 denpvlqpme kirsvypnam hversmqrre ftetnevtvs rhktddlsll kafyremkgs
      361 dlseekerlf ldvlqtvqer egerg
//
LOCUS       WP_006097154             554 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: M4 family metallopeptidase [Bacillus].
ACCESSION   WP_006097154
VERSION     WP_006097154.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 554)
  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 554)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..554
                     /product="M4 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=60388
     Region          52..554
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mktkkqslvv llsagivats islptssyaa tsnnvlstek yneaikstef isgqlttpss
       61 tktedvvfry vdenkdkykl gtksakesft vkkqeddtlg akvvrlqqty ngvpvwgstq
      121 vahvdnkgvl tvfsgtvipd ldqklqqpnq kisaneavsf aekelgfkpn ydvkptselv
      181 vyakddtvsy ayyvhlgfls pqpgshdyfv eaetgkildh ievlhaaknp rnitetvttg
      241 tgkdsfgntq nlnllksnnt yyladktrgq giytydaqnq gsdddtsflp gvlfsnntns
      301 ftsknaqaav dahtyagmvy dyykkvqgrn sydgngakiv ssvhfgqqyg nafwspelkq
      361 mvygdgdgst rsftaaidav ghelthavte sssnliyqde sgalneamsd ifgtlieyyn
      421 nskpdylige dlffqsgqal rsmsdptqyg dpdhyskryt gtnqsklvht nsgiinkaay
      481 lvaeggthyg vtvngigkdk mgkifyrant qyltesatfs qarqalvqsa adlygtqsae
      541 vtsvnkafda vgvk
//
LOCUS       WP_006097415             646 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Bacillus
            pseudomycoides].
ACCESSION   WP_006097415
VERSION     WP_006097415.1
KEYWORDS    RefSeq.
SOURCE      Bacillus pseudomycoides
  ORGANISM  Bacillus pseudomycoides
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Bacillus pseudomycoides"
                     /db_xref="taxon:64104"
     Protein         1..646
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=74550
     Region          48..646
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mnvsvlnflk rkqkkeekke kklinkefva qiqpqggiqf kevyvqggdg lqtcihvygy
       61 qttvndfwqe pimnmpnvit tmdiisdsrk vviesinksm aeqsvrhana kdnierieae
      121 qqfseletly qqvskgevlk rvhlriyisa rtmtelekqa kevmetlesy nfrgaiflne
      181 qeyewaslts sfemqkkyin krngkeipal slaggfpfhf tflndpygiy ygttktkgsv
      241 ifdlfhkdkq rksyngvvig kmgagkstll kkimsdnamk gykirgfdft gefegivqey
      301 ngkqialdgs qgqinplqvy ktaeteessf tqhlskmsif yrfiapeakd deikeyenll
      361 rklyvkkelw sdelgvqnni tslsakeypi fsdylhlvrl elyenletgk hrsnvsstrk
      421 krlelielnl anlvdnfghl fngvstiddf skeqivffsl rhlmslkpei yqaqifnvmn
      481 lmwdemleng kpqwkafdrk eiqfddviry liimdeahhl intsersqha vqfttkfsre
      541 arkyfagivf ashsirdfvp edsnltavee ikklfeltqy kfimqqdsnn ldmlrrvfag
      601 qistselnei pflptgdvll cisavknilf kvdvteeela lfggga
//
LOCUS       WP_006098126             496 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Coleofasciculus chthonoplastes].
ACCESSION   WP_006098126
VERSION     WP_006098126.1
KEYWORDS    RefSeq.
SOURCE      Coleofasciculus chthonoplastes
  ORGANISM  Coleofasciculus chthonoplastes
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Coleofasciculales; Coleofasciculaceae; Coleofasciculus.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Coleofasciculus chthonoplastes"
                     /db_xref="taxon:64178"
     Protein         1..496
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50697
     Region          4..250
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          198..447
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 makitgtdgn nilnalaqgf glednliigg lgddtliggr rndrlvggig sdimkgglgd
       61 dtyivdsddk pdnliessgg gfdkvistvs wtlgrnfenl llvgsgsing tgnnlnnril
      121 gnavenildg regndslngy qgndiligga gndklnggeg nddmtggvgd dsyfvdslld
      181 qvnenfgegn dvvfvvntaa nnytlpanve alflregvrn gngndlnnyi qgnsldnilt
      241 ggagndflna lggademrgg igddrygvgd lgdlviensg egfdtvtssi sytlpvnveq
      301 lillsgfgai ngtandngti ligndesnil tggvgsdtle gnagndellg gasndelvgg
      361 vgddeltggs gsdrleggeg ndrligdlgs ddgvdawigg sgsdlfvlgf gnttfyndgd
      421 pttagnkeya tirdftigsd kiqlganpty rlrlnasggt qvlldnpigs heiiaivrgv
      481 dliaagglas anfvfv
//
LOCUS       WP_006100239            2367 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Coleofasciculus chthonoplastes].
ACCESSION   WP_006100239
VERSION     WP_006100239.1
KEYWORDS    RefSeq.
SOURCE      Coleofasciculus chthonoplastes
  ORGANISM  Coleofasciculus chthonoplastes
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Coleofasciculales; Coleofasciculaceae; Coleofasciculus.
REFERENCE   1  (residues 1 to 2367)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 2367)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 2367)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..2367
                     /organism="Coleofasciculus chthonoplastes"
                     /db_xref="taxon:64178"
     Protein         1..2367
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=247386
     Region          373..624
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          508..759
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          644..894
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          876..1169
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          1100..1349
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          1305..1556
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          1585..1835
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          1719..1970
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          1982..2231
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 matdfnkvft qlieeggkir vlymngirtt edqfkenlig fdqiwniqgk lvlpekcisr
       61 gsidldkqyr nttdstgndw ldlgvfvgkf lfeyalsqis fggiieqank hkalkkkfeq
      121 lkkegkdvte iaeqlddlkd iadffgtint gielaesftk lsnpadlvkd ddftakailf
      181 ikevagflpg fgnivdvids mieaapedlk esleqywyae skfqdinntw tnsaqewlss
      241 hehnpfdnns lillghsqgn ffledglidm gaqndpsrir vlalasptsy lnagglnlyk
      301 gsavpnnnik nsgdpvtflq fesepfvwdk igkifnllag iggigqhpld kylerddvks
      361 ylkdtvyelh pkgyyfpssd tflrdgtqnd dwiegtsddd tingnerndv lrgqggddtl
      421 vggsgydfld geegedtany ssspnkinvr aekvddqdvy kvndgfgtvd tlgnievisg
      481 snhddimvgg dyqdifkgqd gndnfkgngg ddvfyggagd dqalggndnd dlrgedgndk
      541 lngedgndtl yggtgedqlv ggngddylhg edgndklsge dgndslyggt gedqllggng
      601 dddlrgedgn dklsgdnghd slyggageds lfggsgnddl rgedgndylk gedgndtlyg
      661 gnhndtllag tgedllhged gddilhgeqg ndtlyggndq dqlhggynhd ilygeagddq
      721 lhgnegndvl ygntgndqly gndgydyleg gdnqdylsgg ygfdtlygqa gndqlygnag
      781 ddfldggsha dqlyggtgrd llygqsgndf lngeadndvl dggsgvdtld ggtgedtlyg
      841 qtdddflygn aghdvleggd gndylegnsg ddilhgqann dqlygnqgnd elygetgddf
      901 lmgeagddli hggqdndtvs yetspngviv nineyrdyhh nrsdraaqei tdanpseyys
      961 dlepdftins gtaidgfgtt dtlknlehii gsefddilig nykdnqiqal agddlilsta
     1021 gndqfdggng tdtlsfrrdp ggvqvnletg rvmdgwgdmd iiiprpdnns lstienvigs
     1081 rhddqiigdn qanwitadkg ddtldgqagd dslygergdd qiigglgqdr ifgnqgtdti
     1141 ygdlqgvtdq gdadyirggd gddtihaggg ddwvkgdsgy gddliygddg ndtleggage
     1201 dfisggigsd rifgddeadq lygdagddhi vggtgddqld ggadndylea negndrllgq
     1261 agddflsggd gedslwggdd ndwlegeagd dylageagdd hlegadgdde lygqqgddhl
     1321 dggdgqdyli ggdgddvifg qtgedtldgg qgedvlisgd gddllmgqag hdildagagn
     1381 dslsggddtd flyghqgedt ldggqgddhl eagdgndqly gqtgddllda gtgndnlfgg
     1441 tgndqlfgrl gddfldagag ddhleagagd dslygqggnd flnggdghdr leggdgddel
     1501 iaeagidyld ggsgddslsg gddhdqllgq agndtldggs gddnliggdd qdqllgqagn
     1561 ddldggsgdd lllggdgndd lygqsgndtl dggagqdkly gddgddelig qagddyleag
     1621 dgndllsgge nndklygeag ddtlnggsgd drleagegdd qlsgdagfdy ldgglgndql
     1681 aggddndrly grqgndtldg gagvdylnag egedqilgga gndqlyadag ndtlaggadn
     1741 dyldggaged llsgddgndq lygqqgndtl eggtgddyle ggdgeddltg gtgndrlygk
     1801 rdrdtlnggd gndlldggds sdqlngddgn dtlygragld tltggvgnda lwggddadml
     1861 sgdagtdvlq ggdgndqlsg gegndrlygn adndtlegnt gndllnggag ddhllgndgf
     1921 drlygkkgnd wldggdgsdq lrgeagddtl fgqagtdyld ggsgddqlyg gtgrdrlygr
     1981 qgedvldgga dhdllqggsg ddqlygqtgn dilnggrgdd lvwggdhndt ldggtgddyl
     2041 dggsgddqin gggdndqifg qsgidilngg sghdyleggl dndqlsgdrg ndqlygqqgd
     2101 dslegnagnd yleggvgndt lagdrgndql ygqdgddiln ggtdddyldg gadndqllgg
     2161 kgndqlygqa gddlldsgeg ddyleggsgd dhllggkgdd qlygqqgtny ldggaghdyi
     2221 eggdgidtlf gqsgddylig gdgddildgg sgydwlegga gndqlyagsg ddildggagn
     2281 dqlyggngmd tfilgsgaga dtifnftvgm dwiglmggit fndlsisqgt nsqendtllt
     2341 iqdsgeqlat ltgvqantlt hfdftii
//
LOCUS       WP_006104486             312 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella abortus].
ACCESSION   WP_006104486
VERSION     WP_006104486.1
KEYWORDS    RefSeq.
SOURCE      Brucella abortus (Brucella melitensis biovar Abortus)
  ORGANISM  Brucella abortus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 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
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Brucella abortus"
                     /db_xref="taxon:235"
     Protein         1..312
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=34265
     Region          1..309
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 miefdritkn yngraavdev sftiephsia aivgtsgsgk ttllrmvnrl eeptsgeiri
       61 dgqsildepg helrrrigyv iqqhglfphr tvgeniatvp allgwpkqri earvdellel
      121 fqlepgayrd ryphelsggq qqrvgvaral aagpnillmd epfgaldpvi hakaqedlka
      181 iqrrfgttil lvthdmeeai slgdriavmd egkllqfgpp aeilarpate fverlvgtge
      241 rpfrllsltd lktvlqpgda sgeplpvtas qrdalaellw sgrralpvld edgrslgrvt
      301 lekllhqaer pa
//
LOCUS       WP_006098417             566 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Coleofasciculus chthonoplastes].
ACCESSION   WP_006098417
VERSION     WP_006098417.1
KEYWORDS    RefSeq.
SOURCE      Coleofasciculus chthonoplastes
  ORGANISM  Coleofasciculus chthonoplastes
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Coleofasciculales; Coleofasciculaceae; Coleofasciculus.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 566)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Coleofasciculus chthonoplastes"
                     /db_xref="taxon:64178"
     Protein         1..566
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=63349
     Region          36..>470
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mmsemrsfft qhpvgkgima fggtvvltsv vvtgvivglr qlgalegsel kaydqlvrsr
       61 pesepsdrvl vvgiseedir nynqfpitda tlatllkkla dyqpraigid igrdvpigeg
      121 redliqvieq ndnmvaacvm ssatepgtpp apgtppervg fadmqldrdq virrtalvsf
      181 ppfveplpen phlcqdpdsl lyslpfrlat syleqegiee elttpeefik ldstiflple
      241 dqsgnysytg afdyqiminw sgenaikqvt ltdvlegnid pnlvtdrvvl vgytastand
      301 dfatpfsaaa qdrvlmpgvv lhaqvvsqim ttvlegrpli wywsqgteil wiflwsvvgg
      361 tlawkirrpw illpaaivgs gilygicyal fvqqsgwipl vppavglvlt tfsvviidry
      421 gqvvaktvkk llrinieide tqkeeqvaqi letdsfqdiq iradqlrrrr qitkpktynn
      481 tvtdqvelnw eevpelgqyq qvlqrarvlr hqlnrvever devedveqtt ngssgrmptv
      541 kkqafnpede sylsqlqsrg rrmrnr
//
LOCUS       WP_006107072             651 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Brucella abortus].
ACCESSION   WP_006107072
VERSION     WP_006107072.1
KEYWORDS    RefSeq.
SOURCE      Brucella abortus (Brucella melitensis biovar Abortus)
  ORGANISM  Brucella abortus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 651)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 651)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 651)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 651)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Brucella abortus"
                     /db_xref="taxon:235"
     Protein         1..651
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=70300
     Region          28..651
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msgelngndt saqaavsags vlegaafade geqhnesmkt lvlgalgvvy gdigtspiya
       61 frealhaaat ngilarsdil gvvslifwal tlvvtvkyvl fvlradnnge ggilslmalv
      121 rgalkgrpdl ilgvgicgaa lffgdavitp aisvlsameg leivapnltp fvvpaavvil
      181 vtlfsvqklg tgrvaivfgp imalwfvalg asglwhifdd ptvmaalnpy yavrfmtvsp
      241 avafvtvgav flamtgaeal yadlghfgrk pivrawlwiv fpclllnyfg qaafilshge
      301 aaalpffqmi psfalwpmvl lataatvias qavitgaysv arqavqlnil prleiqhtse
      361 klhgqiyipr vnlllglavv ilvlgfekss nlaaaygiav tgnmlvttvl lyiamtriwn
      421 wrvsralpii lgflvidmlf fsaniikvhe ggwasigiat vlvlimwtwv rgtrhlfqkt
      481 rkaevpldli veqmakrppt ivpgtavflt gdpksaptal mhslkhykvl hennviltvv
      541 taskpwvasa drarvsqyne rfmlvtltfg ymqqpnipra lglcrrlgwk fdimttsffl
      601 srrslkasvh sgmplwqdkl fillartasd ateyfqiptg rvveigtqvn i
//
LOCUS       WP_006107511             360 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Brucella abortus].
ACCESSION   WP_006107511
VERSION     WP_006107511.1
KEYWORDS    RefSeq.
SOURCE      Brucella abortus (Brucella melitensis biovar Abortus)
  ORGANISM  Brucella abortus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 360)
  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 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   3  (residues 1 to 360)
  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   4  (residues 1 to 360)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 360)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 360)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 360)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Brucella abortus"
                     /db_xref="taxon:235"
     Protein         1..360
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36910
     Region          18..351
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(91..93,114..115,164,216,240)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mafaatigfa saayvditig viapltgpva afgdqvkkga etavevinka ggikgekvvl
       61 kfaddagepk qgvsaanqiv gdgikfvvgp vttgvavpvs dvlsengvlm vtptatgpdl
      121 targlenvfr tcgrdgqqae vmadyvlknm kdkkvavihd kgaygkglad afkaainkgg
      181 itevhydsvt pgdkdfsalv tklksagaev vyfggyhaeg gllsrqlhda gmqalvlgge
      241 glsnteywai ggtnaqgtlf tnakdatknp aakdaiqalk aknipaeaft mnayaavevi
      301 kagieragst ddsaavakal hdgkpietai gtltysetgd lsspsfdifk wddgkivgle
//
LOCUS       WP_006111726             371 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Brucella abortus].
ACCESSION   WP_006111726
VERSION     WP_006111726.1
KEYWORDS    RefSeq.
SOURCE      Brucella abortus (Brucella melitensis biovar Abortus)
  ORGANISM  Brucella abortus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 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   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   3  (residues 1 to 371)
  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   4  (residues 1 to 371)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 371)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 371)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Brucella abortus"
                     /db_xref="taxon:235"
     Protein         1..371
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39259
     Region          27..358
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(99..101,122..123,172,224,248)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mrktlfsgva laaviafggs awadvlvgig ipvtgpnavy gaqiqkgaea aikevndagg
       61 ingekiaiti gddvsdpkqg isvankfaad gvkfvighfn sgvtipasqv yaengileis
      121 pgatnpqyte qglwntfrtc grddqqgtva gqyifdhfkd akiavihdkt pygqgladet
      181 kkklnelgtk etlyegvnvg ekdfsaliak lkqagvnvvy wgglhpeagl iirqmadqgl
      241 kaqfisgdgi vsnelasiag pavegtlntf gpdprnnsdn aelvkkfrda gfepeaytly
      301 syaavqslaq aakaagsndp qevakamkek gpfktvlgdl sydekgdpkl pgyvmykwek
      361 gadgkynyiq q
//
LOCUS       WP_006100110             448 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Coleofasciculus
            chthonoplastes].
ACCESSION   WP_006100110
VERSION     WP_006100110.1
KEYWORDS    RefSeq.
SOURCE      Coleofasciculus chthonoplastes
  ORGANISM  Coleofasciculus chthonoplastes
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Coleofasciculales; Coleofasciculaceae; Coleofasciculus.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10792831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Coleofasciculus chthonoplastes"
                     /db_xref="taxon:64178"
     Protein         1..448
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=50957
     Region          52..445
                     /region_name="PRK06849"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:235876"
ORIGIN      
        1 mtnslilavl qnlgtltlla iafpfnltvv vvalvwdslt rpfqnpkvan pnpktimltg
       61 gkmtkslqla rsfyadghrv ilveshkywl vghrfsravd rfytvpapnk dpdgymegll
      121 aiakqenvdv yvpvcspvas yydslakpvl sgccevfhfd pdvtqllddk fafaqkaref
      181 glsvpksfki tdpqqvidfd frgekrkyil ksipydsvrr lnltklpckt psetaafvks
      241 lpisedkpwi mqefipgkey cthstvrnge lrlhcccess afqvnyenvd qpdilqwvsr
      301 fvqglnltgq asfdfikted givyaiecnp rthsaitmfy nhpgvaeayl sdtplpeplq
      361 plpeskptyw lyhevwrlne irsfgdirrw fktvfggkda ifqvndplpf lmvhhwqipl
      421 llldnlrrmq gwiridfnig klvelggd
//
LOCUS       WP_006116711             345 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Acetobacter].
ACCESSION   WP_006116711
VERSION     WP_006116711.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter
  ORGANISM  Acetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Acetobacter"
                     /db_xref="taxon:434"
     Protein         1..345
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37988
     Region          1..341
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msvnlhsftq yapgstrkil dninltvedg afialvgpsg agktsllrai gglspvyegq
       61 llidnlpigh sdlpkrktgf vfqnyalfrh msvarnisfg ldvlprkqrp drtaiaarvq
      121 dlleliqlph ladarpdqls ggqrqrvala ralatepkll lldepfgald pivrrtirrw
      181 lrelhdklgl ttilvthdhe ealdiadrlv vmqdgrivqd adadtlntsp qtpfvmqflg
      241 etlefageir kgefipedtd tlpfpvtakn gkttafirpc dvqfisgqga arilsrsrnp
      301 nglyhytvqt tertldittp mpteisegeq fglgishgki fsnll
//
LOCUS       WP_006115755             280 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Brucella abortus].
ACCESSION   WP_006115755
VERSION     WP_006115755.1
KEYWORDS    RefSeq.
SOURCE      Brucella abortus (Brucella melitensis biovar Abortus)
  ORGANISM  Brucella abortus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Brucella abortus"
                     /db_xref="taxon:235"
     Protein         1..280
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=29151
     Region          47..131
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
     Region          175..241
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mkrllattml aamvalpafa qggtpiftge kqhqpvtskn gyfvaspgql ltsdfigqpv
       61 yndpsddadn igtvndiilg adgtpqaivi gvggflgvge kdvaigcnhf swvdksggtr
      121 wlmvdadkeq lekapvfdrn aaftangasr aaektvttkk tsrvipegmk pianeglsae
      181 kligamvyda detkigtigd vlmsadgqte afvvdvggfl ginskpvais ianldvatgk
      241 dgklsvftqf tkkdlqaqpa fseaaykedp egailhgaae
//
LOCUS       WP_006118184             283 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Pantoea stewartii].
ACCESSION   WP_006118184
VERSION     WP_006118184.1
KEYWORDS    RefSeq.
SOURCE      Pantoea stewartii
  ORGANISM  Pantoea stewartii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 283)
  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 283)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Pantoea stewartii"
                     /db_xref="taxon:66269"
     Protein         1..283
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29567
     Region          1..283
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 myaamndlis qaaqkkyavl aincfnlesa raavkaaepq raplilnvyq ghsrhfppai
       61 avplvqalaa easvpialal dhgkafplig qafragftgl midasaepla enirqtarvv
      121 dmahtagvcv egelghiada ptyaladaav kmtqvadvlp fleqthidll avsvgtahgl
      181 ypagvqptid fqrladlhaa ssrplalhgg sgtpaddirr vsqhgvakin vgaavfeagk
      241 qalhqalkhp pttelpdlla lmesaccevv sdylswsgsa rqa
//
LOCUS       WP_006118919             420 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein [Pantoea
            stewartii].
ACCESSION   WP_006118919
VERSION     WP_006118919.1
KEYWORDS    RefSeq.
SOURCE      Pantoea stewartii
  ORGANISM  Pantoea stewartii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 420)
  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 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   3  (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   4  (residues 1 to 420)
  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 420)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Pantoea stewartii"
                     /db_xref="taxon:66269"
     Protein         1..420
                     /product="CmpA/NrtA family 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=45818
     Region          39..290
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mskspvslsr rqlllssaav gglwllpglr navwaagsda pekatvrvgf ipltdcapvv
       61 masvkgfdkk ygltlqpske aswaavrdkl isgeldaahv lysliyglql gvagpqhama
      121 nlmtlnnngq aislsnqlka qkvtdaaslk ksidsqakgs ltfahtfpts thamwlyywl
      181 anaginpfdd vrtvvvpppq mvmnmkignm sgfcvgepwn qrsisddigf tvatsqqiwp
      241 dhpekilgtr aawvkenpnt araltaavle tarwidasdd nrretaqvla grawintkpe
      301 ilqgrmlgqy englgqkwqd phamrffhdg svsfpylsdg mwfltqlkrw gmltqdpdyl
      361 avakqinqid iykqaasavg nvtlpgsemr sstlmdgkvw dglnpaayaa sfainhkers
//
LOCUS       WP_006119559             651 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Brucella abortus].
ACCESSION   WP_006119559
VERSION     WP_006119559.1
KEYWORDS    RefSeq.
SOURCE      Brucella abortus (Brucella melitensis biovar Abortus)
  ORGANISM  Brucella abortus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 651)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 651)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 651)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 651)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Brucella abortus"
                     /db_xref="taxon:235"
     Protein         1..651
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=70380
     Region          28..651
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msgelngndt saqaavsags vlegaafade geqhnesmkm lvldalgvvy gdigtspiya
       61 frealhaaat ngilarsdil gvvslifwal tlvvtvkyvl fvlradnnge ggilslmalv
      121 rgalkgrpdl ilgvgicgaa lffgdavitp aisvlsameg leivapnltp fvvpaavvil
      181 vtlfsvqklg tgrvaivfgp imalwfvalg asglwhifdd ptvmaalnpy yavrfltvsp
      241 avafvtvgav flvmtgaeal yadlghfgrk pivrawlwiv fpclllnyfg qaafilshge
      301 aaalpffqii psfalwpmvl lataatvias qavitgaysv arqavqlnil prleiqhtse
      361 klhgqiyipr vnlllglavv ilvlgfekss nlaaaygiav tgnmlvttvl lyiamtriwn
      421 wrvsralpii lgflvidmlf fsaniikvhe ggwasigiat vlvlimwtwv rgtrhlfqkt
      481 rkaevpldli veqmakrppt ivpgtavflt gdpksaptal mhslkhykvl hennviltvv
      541 taskpwvasa drarvsqyne rfmlvtltfg ymqqpnipra lglcrrlgwk fdimttsffl
      601 srrslkasvh sgmplwqdkl fillartasd ateyfqiptg rvveigtqvn i
//
LOCUS       WP_006120103             310 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Pantoea stewartii].
ACCESSION   WP_006120103
VERSION     WP_006120103.1
KEYWORDS    RefSeq.
SOURCE      Pantoea stewartii
  ORGANISM  Pantoea stewartii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Pantoea stewartii"
                     /db_xref="taxon:66269"
     Protein         1..310
                     /product="formate/nitrite transporter family protein"
                     /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=33841
     Region          34..284
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mkpsssisqg pndvdseeke qgkedievde dalpsraaai heeirhdgek elerdgmall
       61 wsaiaagllm gaslmakgif qvhldgvpga yllenlgytf gfvivimarq qlftentvta
      121 vlpvmhkptt snlglllrlw givllgnlig tafaalafne mpifdeatrq aftdismkvm
      181 ehtpgemfan avisgwiiat mvwmfpyaga aklfvivmmt wlvalgdlah ivvgsvevly
      241 lvfngsvpwt aflwpfavpt llgnltggtl ifalishaqi rndmgeaaqa kakaerrkae
      301 kkrqqqqeer
//
LOCUS       WP_006120308             166 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Pantoea stewartii].
ACCESSION   WP_006120308
VERSION     WP_006120308.1
KEYWORDS    RefSeq.
SOURCE      Pantoea stewartii
  ORGANISM  Pantoea stewartii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 166)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Pantoea stewartii"
                     /db_xref="taxon:66269"
     Protein         1..166
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17707
     Region          1..154
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mnktafyadl drdmrallag etaflaamgn fsallyegle gvnwagfyll teadtlvlgp
       61 fqgkiacvri pvgkgvcgta laqnqvqrvd dvhafpghia cdaasnaeiv iplkvnghvv
      121 gvldidsvey nrfdsddekg lvaltdglcd vlantdleky lqltrs
//
LOCUS       WP_006121118             376 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Pantoea stewartii].
ACCESSION   WP_006121118
VERSION     WP_006121118.1
KEYWORDS    RefSeq.
SOURCE      Pantoea stewartii
  ORGANISM  Pantoea stewartii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 376)
  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 376)
  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
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 376)
  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   5  (residues 1 to 376)
  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   6  (residues 1 to 376)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 376)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 376)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Pantoea stewartii"
                     /db_xref="taxon:66269"
     Protein         1..376
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41422
     Region          13..70
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          79..371
                     /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 mvhgysgrde velnrsekli lelvrrnhgi srsslvsqti lnqssvhriv dtltengfls
       61 lgespsqgrg kpspslslnp darysygisi nsdsvaasli nfrgdiieyc vldtlpgnpa
      121 rtlldlkrhy ldtlkhigis sekvcgvgys magflydsrk yfnppeplkn wmgidlrrei
      181 mtlfdrpvwi ennattaaha eaflgaglhy etfgylsfny gfgggiving kpfqgafgna
      241 geisrifsse egklrpalgi lidrlrnggi eihnirdlnn kfdpdwpiar qwvnevtpnl
      301 hramdalnav idpgaiilgg elprklgemf lamprvssgk rwnisaeypd illstiegds
      361 salgaaltpl retyfn
//
LOCUS       WP_006123348             302 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 5'-3' exonuclease [Streptomyces].
ACCESSION   WP_006123348
VERSION     WP_006123348.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..302
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32719
     Region          1..296
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mlldtaslyf rayfgvpdsv rapdgtpvna vrglldfigr lvhdhrpdel vacwdndwrp
       61 qwrvdlipty kahrvaeetp agqtdeeeip dtlspqvpii edvlaalgia rvgvtpyead
      121 diigtltara kgpvdivtgd rdlyqlvdda rqvrvlyplk gvgtlqvtde awlrekygvd
      181 gagyvdlall rgdpsdglpg vpgigektaa klldaygdld gimaavddpk akltpsqrkr
      241 ldesrayvav apkvvrvagd vplpdfdpal preprdpaal ealaeqwgls gaiqrlltvl
      301 qh
//
LOCUS       WP_006125127             272 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease family protein [Streptomyces].
ACCESSION   WP_006125127
VERSION     WP_006125127.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            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="HNH endonuclease family protein"
                     /calculated_mol_wt=28845
     Region          132..269
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 miaprtprrp thrrcthraa alpavgalvv lalasgcspd dlaadaggts ggtnggaqsa
       61 egfgvspldn pdgtkpglap ltgdadraaa rkliekvatk grgpktgyer dkfgyawkdg
      121 vdgiplarng cdtrndllar dgkdiehkag sdcivmamtl kdpytgetid wrkqqatkvq
      181 idhvmplsyd wqmgaarwna skreqiandp lnlipvdgpa nnakrdsgpa swlppykpir
      241 csyavrfaqv slkyelpvta adkramlaqc gg
//
LOCUS       WP_006125144             304 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Streptomyces].
ACCESSION   WP_006125144
VERSION     WP_006125144.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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   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 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 18542080
            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="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33652
     Region          1..>49
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
     Region          80..256
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 maalfgsrlr klrvaagltq aevgalahvv ssriaqlera tgakptlelt rvldkelvad
       61 ellvdlwpyv yreafpdwsq afiaysarat virqysshav pgllqtpeya rallsmghsl
      121 rdaehleerv aarldrqvrl tgpdrpelwi vldeavlrrp vggaavmrgq lekllrmaee
      181 pnitvqvlpf dqgghgalag slsvlvmpdg tkiaytegah hgqlteepde veqfdltydq
      241 lramalpplm sldlirsale vdyragsips rsdrrrlaqq qlqqrggrrl ragggriprr
      301 rprp
//
LOCUS       WP_006126185             361 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Streptomyces].
ACCESSION   WP_006126185
VERSION     WP_006126185.1
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 10007593
            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="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=40352
     Region          24..295
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mplpltseqp rptaaagape tgkppsdgrd hffdnakyla ivlvaighaw eplpsgrlve
       61 taytfvytfh mpvfiliagy fsrnfelrpd rvwklvtsll vpyvlfevly tlferaanrp
      121 dyalsllspy wllwflpalf lwrlstplwq svrfpvlvsl aiaalatlsp aadgslqiqr
      181 vlqflpfyvl glrlrpehfr llrstwvria svpvfavgll vaywlvprts tgwfyrksst
      241 drldmadwtg ptvtvllfaa aivlgacfla wvpqgkswmt algtctlygy llhgfvvrgl
      301 kyggfyddpf fgttlgtvtv tlgaiavitl lctppvrrll rplleprmaw arqkppaara
      361 s
//
LOCUS       WP_006129128             444 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Streptomyces].
ACCESSION   WP_006129128
VERSION     WP_006129128.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 444)
  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 444)
  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
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 444)
  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   5  (residues 1 to 444)
  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   6  (residues 1 to 444)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 444)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 444)
  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 20170230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..444
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=46867
     Region          <17..116
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          80..408
                     /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 maernrrtvr dlrrgnrarv lqrlyfdgpl srqelgpvtg lssgsisnvv aelsaeglle
       61 eagvvdsdgg rprtllrvap dggllvgidi getrvrvelf dlsltelart erllaqhgyd
      121 verivahvrt gvadvlrdag adprrllgig igvpgiierd gpegpdgtrg avvhgqtigw
      181 ravpfeqllr eavdvppevp lfidngaktl gqaemwfggg rgagaaaial igsgvgacvd
      241 hgdildedrt slalewghtt vqlrgrrcrc gsigcleaya gaealrerwr eaggplpega
      301 ddetalaall aaayparrgt ppdpvalall detaeclgaa ladlvnlflp eriliggwag
      361 lllgprllpe irryaneyal rhaaarttie mgrlgpdavt vgaatlplad fltrggsrpe
      421 pggsgapprt aveavrerhr tpvt
//
LOCUS       WP_006130556             276 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AfsR/SARP family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_006130556
VERSION     WP_006130556.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..276
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=29882
     Region          1..253
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mdisvlgpfr atlagvpvhl tavkprkvfa llalqadevv svaslveevw gespprsvqt
       61 tlqtyilqir hviaaalgde qaelpcgaks vlvtepggyr ldtqgglida reydalssag
      121 hraleqrdwa eassyfrral alwhgralad vqcgplleve atrldesrms vlhgrieadl
      181 rlgrhhelvg elsglaarhp lheglheqlm lalyragrrs dalevyhhlr talnqslgld
      241 pspaieqlhr avldssarle pagaphrgtp vlagpr
//
LOCUS       WP_006130568             264 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AfsR/SARP family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_006130568
VERSION     WP_006130568.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..264
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=28892
     Region          1..253
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mqikvlgslt ahergvpvvp taakprqlla llalhadrvv gvptlmeeiw geniprsast
       61 tlqtyilqlr rkiaaalhdd prrdakdvlv trlggyllrv spgqvdahef eqlaesgrta
      121 felgdyrsas delrraltlw qgpalvdvpa gsvlalevlr lneertaale rrieadlrlg
      181 ryaevvpelr vlaarhplhe gfcgqlmral hhtgsswral eayqrlrgcl vrelglepsa
      241 plqglhqavl sgdpdralha aaad
//
LOCUS       WP_006133797             376 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: aminoglycoside phosphotransferase family protein
            [Streptomyces].
ACCESSION   WP_006133797
VERSION     WP_006133797.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 376)
  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   2  (residues 1 to 376)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..376
                     /product="aminoglycoside 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=40344
     Region          98..309
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 myaasssvsa pprplrprps dsgpylapar patpvlgagn arrlagpgtq plsgrldlsg
       61 aqgaqlrtal asvhricpef apvqvlrrtg rsvllvgttg rstavakcll dhspawseri
      121 rheiaayrsf vrqrppvrap rliaadpdnc tlvierlpgr vaalqrhpve appradiraa
      181 lgaicrlnsw rppagtfdap ldyaarinry helglltdrd lgdlqkllhg iavatgrqgm
      241 gqfchgdall snilispagp vlvdwehagw ylpgydlatl wsvlgdapaa rrqisqiaqs
      301 agpasrdafl vnlmlvltre irtyetavqr smhepapaag qpggvpsgee qrlllrrlhd
      361 dcqlarravr aavgtr
//
LOCUS       WP_006134959             128 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Streptomyces].
ACCESSION   WP_006134959
VERSION     WP_006134959.1
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 10790320
            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="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=13625
     Region          19..120
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(40,68..69,71,93)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 msqeslpsdg gpeppdalpe yaervlevae lippgrvmty gdvaewlgeg gprqvgrvma
       61 lyggavpwwr vvradgvllp ghelralghy raegtplrea graaqghvpr ldmrrarwdg
      121 gagtgght
//
LOCUS       WP_006135513             218 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Streptomyces].
ACCESSION   WP_006135513
VERSION     WP_006135513.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 218)
  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 218)
  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   3  (residues 1 to 218)
  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   4  (residues 1 to 218)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 218)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 218)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..218
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=24048
     Region          22..214
                     /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"
ORIGIN      
        1 msapespqpa dvpddtshvp pmttrvviae dealirldlk emleeegytv vgeagdgera
       61 velarehrpd lvildvkmpk ldgisaaeki aeesiapvlm ltafsqrdlv erardagama
      121 ylvkpfsksd vvpaiemavs rftelkeler evadlsqrle trklvdraks vlqtqyglse
      181 paafrwiqkt smdrrmsmqq vaqaviddae ekkaakgd
//
LOCUS       WP_006137295             277 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Brucella melitensis].
ACCESSION   WP_006137295
VERSION     WP_006137295.1
KEYWORDS    RefSeq.
SOURCE      Brucella melitensis
  ORGANISM  Brucella melitensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Brucella melitensis"
                     /db_xref="taxon:29459"
     Protein         1..277
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30596
     Region          1..275
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mnqnethcla llreadrdry lsvlyapqek rgalaalyaf naeiarirdl vheplpgevr
       61 lqwwrdling eargsaeahp vaaalietie kyelpriafd nycearvfdl yddpmpsrnd
      121 legycgetas aliqlagfil drdaaqahae taghagvaqa vagllrllpi hrrrgqvyvp
      181 admfkaigvt rdmllssedk sateravtim lalarehlai fdkakaglpq tlhpaflpma
      241 lvpaylnave rlgaqaaqkv adisairkqw lmfranf
//
LOCUS       WP_006137572             284 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Streptomyces].
ACCESSION   WP_006137572
VERSION     WP_006137572.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            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="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29810
     Region          15..254
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mtyevevavr aeaelgegpt wdaaagrllw ldilrsrvht ldpvsghrtv rtteqhvgav
       61 kpraggglvl nlrdgiglvd tagdfrwlrh epvpgrrgnd aavapdgslw agtmrydeat
      121 gggtlsritg dgaaevvldd vtvsngtgws pdgrlmyyid tptrridvfd hdpatgrvsg
      181 rrplatvedg agypdgltvd adgcvwvalw dgaavrrytp sgeldrvvpl pvprvtacaf
      241 ggpeltdlyi ttarvglspa pplagslmvl pgagkgqtlp pfag
//
LOCUS       WP_006137872             211 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Streptomyces
            griseoaurantiacus].
ACCESSION   WP_006137872
VERSION     WP_006137872.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces griseoaurantiacus
  ORGANISM  Streptomyces griseoaurantiacus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            aurantiacus group.
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   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
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   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Streptomyces griseoaurantiacus"
                     /db_xref="taxon:68213"
     Protein         1..211
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22403
     Region          118..204
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(137,156..157,175,178,186..187,197,202)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mattrslsta stasaspvtg paargarhrl ravdrdevve iadflppgat wlpapphalp
       61 alpgrppmvg ylvlvpagqq ppfapaavpa gserpapaev taeapaperg aesgdplvri
      121 dpvrrtaevd grrldltyle fellahlvah phrvhtrdql vttvwgyghv gdgrtvdvhv
      181 arlrrklgae hraaiqtvrr vgykytpptg a
//
LOCUS       WP_006139290             442 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Streptomyces].
ACCESSION   WP_006139290
VERSION     WP_006139290.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 442)
  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 442)
  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
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 442)
  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   5  (residues 1 to 442)
  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   6  (residues 1 to 442)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 442)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 442)
  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 20170230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..442
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=46218
     Region          <20..>60
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          80..404
                     /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 magrngrtvr dlrrgnraev lqrlyfdgpl srfelgpvtg lssgsvsnvv aelvadglve
       61 eagsvdsdgg rprtllrvap tagymigvdv getrvrvelf dlaltelart ehplehhryd
      121 vdvvvghile giaevldttg laperllgvg igvpgivare edrgavvhgq tigwdavple
      181 allrsarllp dsvpyfadng artlgqaemw fgagrgarda vvvlfgsgvg acvvtgdmtg
      241 graveyghlt vrvggrrcrc galgcleaya gaeallarwr eaggevpeea deetaltall
      301 aaahpdegaa daegagtpdp vasavleeta eylgaglsdl inlfrperil iggwaglqlg
      361 arflpavrrh aaayslrypa ervsielgrl gpdavtvgaa ilpladffaa ggrrtgtpat
      421 perrppgwre aledrasggg ar
//
LOCUS       WP_006139736             551 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: M4 family metallopeptidase [Streptomyces].
ACCESSION   WP_006139736
VERSION     WP_006139736.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 551)
  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 551)
  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 11461404
            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="M4 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=57211
     Region          44..551
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mtplyarhkr ttlaiatava agallttgms tgaaaqtpad qggatlaaap lklsanarte
       61 liqraedaap etarkiglga keklvardvv kdadgtvhtr yertyaglpv lggdlvvhes
      121 aagatksvtr atkadikvas vtakvtaaka ekqaltaakd agsarteadh aprkviwaas
      181 gtpvlayetv vgglqddgtp nelhvitdaa tgkklyeyqg ietgtgktly sgsvtlsttk
      241 sgstyqlydt trgghktynl ahrtsgtgsl ftdaddvwgt gaasssstdq taaadaayga
      301 qetwdfykst fnrngiknng vgaysrvhyg nnyvnafwdd scfcmtygdg sgnnhpltal
      361 dvaghemshg vtaataglny sgesgglnea tsdifgtgve fyadnasdkg dyligekidi
      421 ngdgsplrym dkpskdggsa dywsssvgnk dvhyssgvan hffyllsegs gsktingvsy
      481 nsptyngstv tgigrakalq iwykalssym tsttkysgar tatlsaasal ygsssteyna
      541 vkaawsavnv n
//
LOCUS       WP_006141722             301 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 5'-3' exonuclease [Streptomyces].
ACCESSION   WP_006141722
VERSION     WP_006141722.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..301
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32265
     Region          1..295
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mlldtaslyf rayfgvpesl kapdgtpvna vrglldfidr lvkdhrpddl vacmdadwrp
       61 awrvelipsy kahrvaearp agpdteevpd tlspqvpiie avldalgiar vgvaeyeadd
      121 vigtftarat gpvdivtgdr dlyqlvddar gvrvlypvkg vgtllltdea vlrekygvdg
      181 rgyadlatlr gdpsdglpgv pgvgektaak llaefgdlpg vlaavedpka rltptqrrrl
      241 tealpyleva pkvvkvaddv plppvptalp htardpemve alasrwglgg slqrllttlr
      301 s
//
LOCUS       WP_006142782             399 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Streptomyces].
ACCESSION   WP_006142782
VERSION     WP_006142782.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 399)
  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   5  (residues 1 to 399)
  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   6  (residues 1 to 399)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 399)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..399
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40599
     Region          14..77
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          77..379
                     /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 metpgsqssl hranlervvr avrlagsltq aeiarttgls aatvsnivre lknngtvevt
       61 ptsaggrrar svslsgdagi vigvdfghth lrvaignlah qvlaeeaepl dvdasaaqgf
      121 draeevvsrl ieatgvdrtk iagvglgvpg pidveagtlg stailpgwtg arpaeelrer
      181 lgvpvhvdnd anlgalgelv wgsgrgvkdl ayikvasgvg aglviqgkiy rgpggtagei
      241 ghitldesgp vcrcgnrgcl etfasaryvl pllrsshgtd ltldgvvrla rdgdpgcrrv
      301 iadvgrhvgs gvanlcnlln psrvvlggdl aeagelvlgp iresvgryai psaarhlsvl
      361 pgalggraev lgalalalse mgdstlldgs apvaspaft
//
LOCUS       WP_006144683             369 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Brucella melitensis].
ACCESSION   WP_006144683
VERSION     WP_006144683.1
KEYWORDS    RefSeq.
SOURCE      Brucella melitensis
  ORGANISM  Brucella melitensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 369)
  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 369)
  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 369)
  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 369)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Brucella melitensis"
                     /db_xref="taxon:29459"
     Protein         1..369
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40400
     Region          38..360
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mketlsrrsf ltkgaaigaa aatsgaalat paiaaelptl rwrltsgfpn nldtiyggav
       61 ymadavskmt dgkfqiqvfq ageivpgpqa idavqantve mahtcgyyft gknptfaigt
      121 alpfgmntrl qnawlyhggg nelyneflsd ygivggntaa qmggwyrkei ksaedlkglk
      181 mriagvagev msrfgvvpqq lpggdiypsl ergtidaaew vgpyddeklg fyqiapyyyy
      241 pafweggasv hffinkkqye slpeaykval ntaaeaatqn mialydvknt aairslvskg
      301 vklqplprdv ldaaykvsfd lyaeyneknp awakiypawk kfrdegfewf rvaeytydsy
      361 vyaaqaagk
//
LOCUS       WP_006144805             162 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Streptococcus peroris].
ACCESSION   WP_006144805
VERSION     WP_006144805.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus peroris
  ORGANISM  Streptococcus peroris
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Streptococcus peroris"
                     /db_xref="taxon:68891"
     Protein         1..162
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18515
     Region          5..76
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mvytideika kikpiakryn vskvylfgsy argeedensd idialelgdi tkfmdvyghl
       61 stifsgnvdi llvsdllspk tnigslvkkn flndrvliyq kleeamvenl vnnprmrdit
      121 eynevtqnai keslekykte gitkssesid nyfermvren tk
//
LOCUS       WP_006144999             374 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Brucella melitensis].
ACCESSION   WP_006144999
VERSION     WP_006144999.1
KEYWORDS    RefSeq.
SOURCE      Brucella melitensis
  ORGANISM  Brucella melitensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 374)
  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 374)
  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
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 374)
  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   5  (residues 1 to 374)
  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   6  (residues 1 to 374)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 374)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 374)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Brucella melitensis"
                     /db_xref="taxon:29459"
     Protein         1..374
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39056
     Region          7..>48
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          72..353
                     /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 msihlgmvlk ilrdegpqsr aelarrcgls attlthltaq llkdgciaet dapvlpsgsp
       61 mpgrppvsvr lvpsahyvag vhigaeavqv aicdltaqlv tsaafdhaan dnplklthqt
      121 advlrnlvqa kgislgslvg igmgvpgpvd qvrrrnllsi ntgwrdvafa dameaelnip
      181 tvvehnvtam alaeahygig qgcpavlyvy lgtglgaglv vdgmpfrpgg hgavelghiq
      241 idpqgtlcac gnrgcletfv servlrerga gsaepllaal arnpalhdev aghfttalan
      301 avnlltpdli vlgghfaeap eafyarlrcd lpprvlphmr dvlrierggf gnnadavgaa
      361 avaldhlfys gvsr
//
LOCUS       WP_006146237             374 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LysM peptidoglycan-binding domain-containing protein
            [Streptococcus].
ACCESSION   WP_006146237
VERSION     WP_006146237.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus
  ORGANISM  Streptococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae.
REFERENCE   1  (residues 1 to 374)
  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 374)
  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 11443421
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Streptococcus"
                     /db_xref="taxon:1301"
     Protein         1..374
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=39555
     Region          <2..89
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          47..89
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
     Region          <106..261
                     /region_name="rne"
                     /note="ribonuclease E; Reviewed; PRK10811"
                     /db_xref="CDD:236766"
ORIGIN      
        1 mkkriilast valslaptla tqakevawsp rsveqiqndi sksenktsyt ikygdtlsti
       61 aealgvdvnv lanlnkitni dlifpetvlt ttvneneevt evevytpqev gsdvatatad
      121 ltnnqviind qtvqvedlsq pvettdsqva eevvaettvs tgepaveatt evatpavapv
      181 aeatteavte ttapvteapv aeettttvae vnateapvae vapepqsapa tyqaepsqga
      241 sttytapaap dyasiaasks enaglqpqta afkeevanlf gitsfsgyrp gdsgdhgkgl
      301 aidfmvpvss algdqiadya iqnmasrgis yiiwkqrfya pfdskygpay twnpmpdrgs
      361 vtenhydhvh vsmn
//
LOCUS       WP_006148689             165 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Streptococcus infantis].
ACCESSION   WP_006148689
VERSION     WP_006148689.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus infantis
  ORGANISM  Streptococcus infantis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Streptococcus infantis"
                     /db_xref="taxon:68892"
     Protein         1..165
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18186
     Region          4..156
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mlhsekesiy qivneqlssl legetnvlan lsnasallkm nfprtvfagf ylydgnelil
       61 gpfqggvscv rialgkgvcg esaascqtvi vgdvktypny iscdssarse ivlpmvkngq
      121 llgvldldss yvddydeidq kyleefvtil ldktewkfsm feeke
//
LOCUS       WP_006149751             265 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Streptococcus
            infantis].
ACCESSION   WP_006149751
VERSION     WP_006149751.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus infantis
  ORGANISM  Streptococcus infantis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptococcus infantis"
                     /db_xref="taxon:68892"
     Protein         1..265
                     /product="formate/nitrite transporter family protein"
                     /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=28829
     Region          4..260
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mvssefiski efackkkesl ysnskfkyai rsmfagaflt fstaagavga dlinkiatgs
       61 grflfpfvfa wglayivfln aelvtsnmmf ltagsflkki swrktaeill yctffnliga
      121 liagwgfahs aayanlthds fisgvvemkl arsnelvlle gilanifvni ailsfvlvkd
      181 ggaklwlvls aiymfvfltn ehiaanfasf aivkfsvaad sianfgigni lrhwgvtfig
      241 nfigggllig lpyaflnkne dtyvd
//
LOCUS       WP_006151731             265 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Streptococcus
            infantis].
ACCESSION   WP_006151731
VERSION     WP_006151731.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus infantis
  ORGANISM  Streptococcus infantis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptococcus infantis"
                     /db_xref="taxon:68892"
     Protein         1..265
                     /product="formate/nitrite transporter family protein"
                     /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=28839
     Region          4..260
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mvssefiski efackkkesl ysnskfkyai rsmfagaflt fstaagavga dlinkivpgs
       61 grflfpfvfa wglayivfln aelvtsnmmf ltagsflkki swrktaeill yctffnliga
      121 liagwgfahs aayanlthds fisgvvemkl grsnelvlle ailanvfvni ailsfvlvkd
      181 ggaklwlvls aiymfvfltn ehiaanfasf aivkfsvaad sianfgigni lrhwgvtfig
      241 nfigggllig lpyaflnkne dtyvd
//
LOCUS       WP_006157754             210 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Cupriavidus basilensis].
ACCESSION   WP_006157754
VERSION     WP_006157754.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus basilensis
  ORGANISM  Cupriavidus basilensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 210)
  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 210)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 210)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Cupriavidus basilensis"
                     /db_xref="taxon:68895"
     Protein         1..210
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23234
     Region          1..207
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 maydleeqeq leslkawwrq ygntvtwali agllvfaaws gwnywqrkqa geaallyeqv
       61 vkaaesrdve rikraagdle dkfgktaygp mtalvsakvl ydagdlaatk tqlqwaidhg
      121 egeyahlarv rlagvlldek ayeqglallk deppapfval yadrrgdlla aqekraears
      181 ayqkaldkls andaamrqii qfkldalgta
//
LOCUS       WP_006157882             693 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Cupriavidus basilensis].
ACCESSION   WP_006157882
VERSION     WP_006157882.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus basilensis
  ORGANISM  Cupriavidus basilensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 693)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 693)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..693
                     /organism="Cupriavidus basilensis"
                     /db_xref="taxon:68895"
     Protein         1..693
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=71997
     Region          1..618
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mpsldsllkp rsvavigast qpekvggmpi rllrelgyag rifpvhptas eiqglpayat
       61 laaigqavdl aivavpavat esvmaqlaqn gtraaiffts gfaevgdegl amqvalaesa
      121 rrhgvallgp nclgamnlre rmfatfspip ltgvppagdv glvsqsgafg ayafalarea
      181 glglsywvtt gneaglqvad viewmaqdpd trvilaymeg crdgarlrqa laaaraagkp
      241 vvitkvgtte agarsaqsht aslagedavy qavfdeygvh rahtledffr lgytlsrgrr
      301 parwdspsgl mgdavapvai vtvsggvgim madraeelgm pmppmpaaaa kalrtsipfa
      361 stanpidvtg qvvaqpavll damagvatcg eygsvvafla gganaprlwe elqrtigalh
      421 edkraaplll sgvvdddkra wleahgclvf repahaieav atlaraaale aaaarvpvae
      481 aaaplaallr dvpddasals efdamrllad agvpvaahgl ardadeaval aqrigypvav
      541 klcsaqvlhk sdvggvalnl tddaavrkaf aamqaalara saslpfegvl varmvrgwge
      601 lmvgvrrdpv fglvvlagir rnrrgdlpad glwpgavhrd gvvkklepta qpdtgtdrtr
      661 gwgttktgdk sscicklqgp rarrwqafsp psc
//
LOCUS       WP_006157988             129 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Cupriavidus basilensis].
ACCESSION   WP_006157988
VERSION     WP_006157988.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus basilensis
  ORGANISM  Cupriavidus basilensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Cupriavidus basilensis"
                     /db_xref="taxon:68895"
     Protein         1..129
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14026
     Region          1..104
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkrvrsrrlh gftlielvvv maiiglllti alprylrsid rgkeqvqrqn lavmrdaidk
       61 yfgdngeype nldelvlkhy lrsvpqdpvt ggtswtvias pdadkagvyd vapaseaaav
      121 paaavapek
//
LOCUS       WP_006104149             513 aa            linear   BCT 20-JAN-2025
DEFINITION  type I restriction-modification system subunit M [Coleofasciculus
            chthonoplastes].
ACCESSION   WP_006104149
VERSION     WP_006104149.1
KEYWORDS    RefSeq.
SOURCE      Coleofasciculus chthonoplastes
  ORGANISM  Coleofasciculus chthonoplastes
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Coleofasciculales; Coleofasciculaceae; Coleofasciculus.
REFERENCE   1  (residues 1 to 513)
  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   2  (residues 1 to 513)
  AUTHORS   Youell,J. and Firman,K.
  TITLE     Mechanistic insight into Type I restriction endonucleases
  JOURNAL   Front Biosci (Landmark Ed) 17 (6), 2122-2139 (2012)
   PUBMED   22652768
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Sistla,S. and Rao,D.N.
  TITLE     S-Adenosyl-L-methionine-dependent restriction enzymes
  JOURNAL   Crit Rev Biochem Mol Biol 39 (1), 1-19 (2004)
   PUBMED   15121719
REFERENCE   4  (residues 1 to 513)
  AUTHORS   Murray,N.E.
  TITLE     Type I restriction systems: sophisticated molecular machines (a
            legacy of Bertani and Weigle)
  JOURNAL   Microbiol Mol Biol Rev 64 (2), 412-434 (2000)
   PUBMED   10839821
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114514
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Coleofasciculus chthonoplastes"
                     /db_xref="taxon:64178"
     Protein         1..513
                     /product="type I restriction-modification system subunit
                     M"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=58746
     Region          6..147
                     /region_name="HsdM_N"
                     /note="HsdM N-terminal domain; pfam12161"
                     /db_xref="CDD:463478"
     Region          162..399
                     /region_name="HsdM"
                     /note="Type I restriction-modification system, DNA
                     methylase subunit [Defense mechanisms]; COG0286"
                     /db_xref="CDD:440055"
ORIGIN      
        1 msreqltndi wracdilrrd nncggvmeyv ehlswllflk fldgqedafe qeaksanrky
       61 trvisrqyrw snwvtkalgk kggkkgrrti pawddhqlme fvrgeliphl aslsgspere
      121 viagifrdrn viicdspdnl kdvlkivdqi dltnpddiyt vshiyedllk rlgsenkmag
      181 efytprsvir fmvevidpqi getvydpacg tcgflleafl htqkqektak dreilqrhtf
      241 vgqekkplpa llgtmnmvlh gvlvpdirrr ntlaedirdg sglfdetfdv iltnppfggk
      301 enariqknfp vkanatellf lqhvmkklkp kqgarcgivv pegtlfrgga fatvkkellh
      361 dfnlfmvvsl ppgtfapysd vkaallffer geqqkevlyq eialpddlkk fskvnsisde
      421 hfaearqvwq qmkdyhlgka nrptmtansw ledvkglvkn eydftaknsi ylkkeklphp
      481 seitaillkd qrelqirler lhkmlndrik sdd
//
LOCUS       WP_006158405             133 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Cupriavidus basilensis].
ACCESSION   WP_006158405
VERSION     WP_006158405.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus basilensis
  ORGANISM  Cupriavidus basilensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 133)
  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   2  (residues 1 to 133)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Cupriavidus basilensis"
                     /db_xref="taxon:68895"
     Protein         1..133
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13161
     Region          21..88
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mfkptltras rqvllaaavw fslsgaafaa vdvntadeaa lvslkgigpa tantivters
       61 rggpfrdaad ladrvkglgq ksvvrlqeag mtigaggaaa pkaavtapka avaaaapark
      121 dgkaetppak avr
//
LOCUS       WP_006160053             625 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Cupriavidus basilensis].
ACCESSION   WP_006160053
VERSION     WP_006160053.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus basilensis
  ORGANISM  Cupriavidus basilensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 625)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Cupriavidus basilensis"
                     /db_xref="taxon:68895"
     Protein         1..625
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=67360
     Region          1..625
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mpqasalidt paktrpglav mglsalgvvf gdigtsplyt lktvlalsgg kpsapvilgl
       61 lslliwtlii vttvkyvsfa mridnngegg ilalmsllgi kkrkrplvva aglfgaaliy
      121 gdgaitpais vlsaleglni vfpeaksfil patvailval faiqpmgtsr igrafgpvma
      181 lwflciavlg irgillhpsi lialnplygl aflfsngyts fliflcvtga ealyadmghf
      241 gprpirlaws aivfpsllln yagqaalvls gvdsthnify llcpppllvp lvilaavatv
      301 iasqsiitga fsmtrqaill gwlphlqirq tseqgygqiy vgtvnwllml vtvslalffk
      361 ssdqlasayg iavsltmlmt svllfiamrd iwgwnlwasa avsgvfliid sgffvanlak
      421 mldggyiplm laavvygvml iwhrgtaais aainedvmpi eaflgevqak niprvpgagv
      481 fltrtldgtp pvmlwhvkrn halqqkilal svvtqtvpwi kdaerltlte lmpdvwrlna
      541 rygfmerpdi pklllqpqvl pcaldlgait yymgletivl resdsrmprw qgklfalmvk
      601 ngmhvtdlfr lpsdqvveig rrvsi
//
LOCUS       WP_006160346             348 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Cupriavidus basilensis].
ACCESSION   WP_006160346
VERSION     WP_006160346.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus basilensis
  ORGANISM  Cupriavidus basilensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 348)
  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 348)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Cupriavidus basilensis"
                     /db_xref="taxon:68895"
     Protein         1..348
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38224
     Region          21..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          246..328
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtylvratal tnyvrvarev gldpykqlsk agirratlld pdamiaadal rsllaesasa
       61 agvedfglrm aetrqltdlg plgfaiqgep tlrkalesmm rylrlqsesv vmaieeldel
      121 vvireslltd gqapqrqsie lvvagvyrll rrflgetwkp rsicfshapp sgptgharvf
      181 gmpvlfnqef dgivcratdl daplaaydpl mawevrqhld tllagsdlaf pdvvrrlvla
      241 llpsgncsvd svaqhlrvdr rtvhrrlakd gesysgiyng vradlaarla rsearplael
      301 aallgfstas sfarwfgghf gctvsewrar hrarlttpts ldqpespr
//
LOCUS       WP_006161345             381 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Cupriavidus basilensis].
ACCESSION   WP_006161345
VERSION     WP_006161345.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus basilensis
  ORGANISM  Cupriavidus basilensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Cupriavidus basilensis"
                     /db_xref="taxon:68895"
     Protein         1..381
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=40833
     Region          1..268
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          264..353
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrflhtadwh lgrvfharsl ledqawvldq fvalarelrp davliagdvy dravpppeav
       61 allddvlari vvdagipvvm iagnhdsaqr lgfgarllta qglhvagite reatcvtlsd
      121 ahgevriyal pyaepaavrd afgmelpghe aalatrldai rashpahars vvvahafvig
      181 geaseserpl svggsgavaa gvfagfdlva lghlhrpqtf hqrihyagsl lkyslsevth
      241 aksvsliela adgkvsieai plsprrdlrv vegkladlla qgaedahrdd yvhavltdtg
      301 alldpmarlr qaypnalaie ravlartgea gaagqrlrql dtgelfanff kevadeeldd
      361 dkrrvldhvl egiaradres a
//
LOCUS       WP_006162612             204 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Cupriavidus basilensis].
ACCESSION   WP_006162612
VERSION     WP_006162612.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus basilensis
  ORGANISM  Cupriavidus basilensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Cupriavidus basilensis"
                     /db_xref="taxon:68895"
     Protein         1..204
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21336
     Region          9..201
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mtaagdgkpr rivvaitgat gavygvrlvq ilgaapgvea hllisaagvm nlqheldisk
       61 aeveafahvv hnvrdigati asgsfaaham vvapcsmrtl aavahglsdn litraadvtl
      121 kerrklvlmv retplnlahl rnmtavtemg giifppvpgf yqpgfyqkpq svaelvdhtv
      181 grvldlidvp qtlapswagl ngqa
//
LOCUS       WP_006162257             377 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Cupriavidus
            basilensis].
ACCESSION   WP_006162257
VERSION     WP_006162257.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus basilensis
  ORGANISM  Cupriavidus basilensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 377)
  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 377)
  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 377)
  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 377)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Cupriavidus basilensis"
                     /db_xref="taxon:68895"
     Protein         1..377
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=41549
     Region          44..371
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 merrsfllka savaatgala acgkeekaaa pvaagasapa vigsnpavew rlassfpksl
       61 dtiyggaell sqrvkeltdg kfnikvfaag elvpglqvld avqnntvqig htagyyyfgk
      121 nptlcfdttv pfgltsrqqn awmmqgngmk lmreffkeyn vvnflggntn aqmggwfrke
      181 iktvadlqgl kyriagfagv vlsrlgvvpq qiaggdiypa lekgtidaae wvgpyddekl
      241 gfykvapyyy ypgwwegsaq lsfyssatey eklpalykra letatievht nmmakydavn
      301 pqalarllen gvklrpfske imeacfkatq dayaeetakn psfkkiyddw rvfrnneaaw
      361 fnvaeqafsq fsfarkl
//
LOCUS       WP_006162904             829 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Cupriavidus basilensis].
ACCESSION   WP_006162904
VERSION     WP_006162904.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus basilensis
  ORGANISM  Cupriavidus basilensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 829)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 829)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 829)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..829
                     /organism="Cupriavidus basilensis"
                     /db_xref="taxon:68895"
     Protein         1..829
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89550
     Region          78..128
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          105..829
                     /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 mephqdadaf grlkrhplac aighaavamg ltatcllpgm araadtaaap asaatrpyni
       61 pagplegaln rlgreagill sfptdtaagl qskglhgrys vpdalaqllq gtglaavaqa
      121 nggyalvkhi etsatapaas gneaalppvt vradaareds yrppptasvm rsdtplldtp
      181 qvinvvpaqv lrdqrprnld dalgnisgit qgntlagtqd timkrgfggn rdgsvmhngm
      241 pliqgrglna aadsvevlkg pssllygimd pggvinivsk rpmlqqynai svlgstyghg
      301 kngagatlds tgpigtsgla yrlvvdqvde qywrnfgehr etlvapslaw ygkdtqvvls
      361 yeyrkflypf drgtaidpkt neplaipsrr rldepfnsmn gqshlvqlav dhqfnadwrg
      421 hfgysynres ydanqlrvfg vnattgvlsr sndathgals tdsygiayvd grftvaglrn
      481 dlqvgvdsey rriyradllr qnttrafnyl npvyglesps stvsasdsdq tdtlhdsslf
      541 fqdslhlsek wilvggarfl sysqvagrgr pfnvntding nkwlpraglv ykwteavsly
      601 gsytqslkpt stiaplssgv vidsgvlpee arswelgtkl dlpgsmtgsl affnidkknv
      661 lvsqyndvtr qtdwrtsgra rsrgieldva gqigerwnli gsyayidakt tedplyagnr
      721 lwnvaqhtaa lsavydfgqi fggdklrlga gahyvgnrpg dsansftlpa ytvadafaty
      781 etkvgqrklr fqlnvknlfn rtyypssvnk yfvsvgdarq vtllstfef
//
LOCUS       WP_006162926             148 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Cupriavidus basilensis].
ACCESSION   WP_006162926
VERSION     WP_006162926.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus basilensis
  ORGANISM  Cupriavidus basilensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Cupriavidus basilensis"
                     /db_xref="taxon:68895"
     Protein         1..148
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15966
     Region          1..148
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mqrvnrtsqr gftliealit vsiiailsai aypnyssyit kgrraeakaa lledmqlfer
       61 nfsqvnsyyg agttalwtgy ktwsgdsptt gsyqilavqc gasngqcvel qaspikpdst
      121 cgtlvyrstg ekynmltsgv yattagcw
//
LOCUS       WP_006163060             408 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Cupriavidus basilensis].
ACCESSION   WP_006163060
VERSION     WP_006163060.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus basilensis
  ORGANISM  Cupriavidus basilensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Cupriavidus basilensis"
                     /db_xref="taxon:68895"
     Protein         1..408
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43016
     Region          8..401
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msaihptilv vnagsssvkv svyavpeaah anadinpvls ahgqiegigv sphliasmad
       61 grvvaderfp vaqvsdhdaa frlirlvlsi glrdappvai ghrvvhggad fsaavkidde
      121 viaklealip laplhqphnl tairavraaa pallqvacfd tafhaghdpl aqllalpyey
      181 fergirrygf hglsyeyiar rlqqiapdla qgrvivahlg ngaslcamre grsvestmgl
      241 taldglpmgt rcgaidagai lwlsqqgmst kdietmlyqe sglkglsgvs sdmrallasd
      301 aprarlaidf ytyraaqeig klaatlggld alvftagiga nsppvrekic arlaelfgis
      361 ldagannegr qrvsrdnsrv pvlvlptdee gmialntari mmaqnala
//
LOCUS       WP_006169698             308 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [unclassified
            Synechococcus].
ACCESSION   WP_006169698
VERSION     WP_006169698.1
KEYWORDS    RefSeq.
SOURCE      unclassified Synechococcus
  ORGANISM  unclassified Synechococcus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="unclassified Synechococcus"
                     /db_xref="taxon:2626047"
     Protein         1..308
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=33844
     Region          124..303
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mvqnflnrcr eqpfsllrrh qktalsalai gsigfvvlgw slidgrmlsl vfdrpsllel
       61 ldqvsedkgt krkpsplgsv pvaplsrswr splarqcssi dkgirsrllt lqkrsgswrt
      121 fvpidstnfg krfsedafgr rldpsprviv lhetvysvss avntfqtphp rdedqvsyht
      181 lisrdgrvld lvdplmrayg agysaflgew aitnkrlkgs vnnfalhlsl etpssgahgg
      241 sghsgyssqq ydalalvlsg wmkafnlspt svtthrhvdi ggeradprsf dwsalqgrla
      301 algdlcvp
//
LOCUS       WP_006169950             390 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LysM peptidoglycan-binding domain-containing protein
            [unclassified Synechococcus].
ACCESSION   WP_006169950
VERSION     WP_006169950.1
KEYWORDS    RefSeq.
SOURCE      unclassified Synechococcus
  ORGANISM  unclassified Synechococcus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 390)
  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 390)
  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 11443421
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="unclassified Synechococcus"
                     /db_xref="taxon:2626047"
     Protein         1..390
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=39917
     Region          <28..126
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          151..195
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
ORIGIN      
        1 mrspqplrra laalvvalvl plpalagpqh vvksgetlse iaerygvsvk rllqlngikd
       61 pnlveagtrl klpegspaqa shtvsagetl seiaerygls vqklmelngl kdadlvqvgq
      121 rlkvptaksa aspakpakpa apaaagaktg rvhvvksget lseiaerydv pmarlvsmnk
      181 lespdnlqvg tklslgagsg tpatkpapak paaakpaask paaskpaaak papapqaaap
      241 kpaakpepkp apnppeqaeq papavatpaa qatpepeakp aaaapkptva aaqpqpkpkp
      301 kpkpdpsnta ppdwrtygpl qvdfsnwrpm ggsqvapaln sggqpvfvai ncaarkinat
      361 geagawtswe dpttdfeeql ikdvckqtag
//
LOCUS       WP_006170136             247 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [unclassified Synechococcus].
ACCESSION   WP_006170136
VERSION     WP_006170136.1
KEYWORDS    RefSeq.
SOURCE      unclassified Synechococcus
  ORGANISM  unclassified Synechococcus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 247)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="unclassified Synechococcus"
                     /db_xref="taxon:2626047"
     Protein         1..247
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=26646
     Region          96..240
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(189..190,193,214..217,219)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 maspmtperf qdrfeafrge pqqvsgvwtl haaiaalpgs eavldehapw altfsqkpaa
       61 ppapavpsgg ldprgseeag magpqlaapv qpgdsyllvn drdedmeayd htgqflwkip
      121 clargqgadt dwsrantdtp pglyklgqly adyeqnpnpp csdtamaygw ysfdmeeleg
      181 qevshgragi mlhgggsacg wpgawaaqqp lhptlgcvrl hnadlrdkvl plyrqgtvyv
      241 gvfqekk
//
LOCUS       WP_006172395             368 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Brucella].
ACCESSION   WP_006172395
VERSION     WP_006172395.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 368)
  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 368)
  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
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 368)
  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   5  (residues 1 to 368)
  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   6  (residues 1 to 368)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 368)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 368)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..368
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38319
     Region          1..>42
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          66..344
                     /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 mvlkilrdeg pqsraelarr cglsattlth ltaqllkdgc iaetdapvlp sgspmpgrpp
       61 vsvrlvpsah yvagvhigae avqvaicdlt aqlvtsaafd haandnplkl thqtadvlrn
      121 lvqakgislg slvgigmgvp gpvdqvrrrn llsintgwrd vafadameae lniptvvehn
      181 vtamalaeah ygigqgcpav lyvylgtglg aglvvdgmpf rsgghgavel ghiqidpqga
      241 lcacgnrgcl etfvservlr ergagsaepl laalarnpal hdevaghftt alanavnllt
      301 pdlivlgghf aeapeafyar lrcdlpprvl phmrdvlrie rggfgnnaga vgaaavaldh
      361 lfysgvsr
//
LOCUS       WP_006172550             441 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [unclassified Synechococcus].
ACCESSION   WP_006172550
VERSION     WP_006172550.1
KEYWORDS    RefSeq.
SOURCE      unclassified Synechococcus
  ORGANISM  unclassified Synechococcus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 441)
  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 441)
  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 441)
  AUTHORS   ter Beek,J., 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 441)
  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 441)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="unclassified Synechococcus"
                     /db_xref="taxon:2626047"
     Protein         1..441
                     /product="CmpA/NrtA family 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=47697
     Region          44..304
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mlnrrkflsv lsatlagtlm lnacgnppek gsgpasgtap vadagletkt itlgyvpile
       61 aaalvagvek gffakhglev klakqaswpa ardnvvigst gggidggqwq lpmphliteg
      121 iitngnkvpm yvlaqlssqg naiavsnslk kanlrvdltp aaptilgfpk tegrkfraah
      181 typnanqdlw irywlgaggi dpdkdiellt vpstetlqgm rngtmeafst gdpwpfrivt
      241 dnigytaalt aeiwpvhpee flgvradwvd khpkaavali kglleaqqwa dkaenkeala
      301 kmlssrqyfn tpvsvlvpal kadyklgadl kpstdpklgp lywasdrgvi sypykslslw
      361 flveslrwkf hpgkldtidq akalvdkvnr edlwrqaate lglpaadipt gssrgketff
      421 dgvvydpenp qayldslkik r
//
LOCUS       WP_006175102             761 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: penicillin acylase family protein [Brucella].
ACCESSION   WP_006175102
VERSION     WP_006175102.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 761)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 761)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..761
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=84405
     Region          3..760
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mnvasarpav arqinlqgls dtveidydlw giphiyahsm ddlffgngya haadrlwqmd
       61 aarrralgrf aawagkeals sdmlmrrldl atvsradyaa lspetqrmce ryaqgvnawi
      121 dsgqlpaeyr llgerperwe gwhcvlvmrq rgilmgslwf klwraaafar igpdclhllr
      181 yedggterfv vpqeqsadrw sisleelrpa ieglmklfph datgggsnnw avdarhsktg
      241 mpivagdphr ayeipgmyaq ihqtcdsfdv lglsvpgvpg fphfahneem awcvthafad
      301 ihdlyvedfs glphgayrte kgtekaqhrv eaiqvrgged vqidvwttrh gplilgspee
      361 gkgialksvq lqpgdrsldc llpmltassi tefydmmepw glidhnlvsa dkkgnigvlv
      421 rakipvrdrl ngwlpmpgwt gahewrgmlp ferspreenp asgivvtann rtvpddwpdy
      481 ictdchpatr akrirsrles etpfspsdml silhddvsap aaeiaqklra itpkseparh
      541 llsmlagwqg dmapnklapt aymairqemt rilarvsdla gvadteisrl ppgvspfthl
      601 wwalpdqlrr ndtsllggms wdellleave tvaqtfdpqp wgdahrpifr hplagafpeq
      661 aavlaptsry vggdgdcvla tgslpqsgat aaygpvakyi wdladwdass wvvfhgasgd
      721 pasphyrdqn erwargeqvp acysrenvra nsarhlimqp s
//
LOCUS       WP_006173745             372 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [Brucella].
ACCESSION   WP_006173745
VERSION     WP_006173745.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 372)
  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 372)
  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 372)
  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 372)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..372
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40649
     Region          38..363
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mketlsrrsf ltkgaaigaa aatsgaalat paiaaelptl rwrltsgfpn nldtiyggav
       61 ymadavskmt dgkfqiqvfq ageivpgpqa idavqantve mahtcgyyft gknptfaigt
      121 alpfgmntrl qkawlyhggg nelyneflsd ygivgivggn taaqmggwyr keiksaedlk
      181 glkmriagva gevmsrlgvv pqqlpggdiy pslergtida aewvgpydde klgfyqiapy
      241 yyypafwegg asvhffinkk qyeslpeayk valntaaeaa tqnmialydv kntaairslv
      301 skgvklqplp rdvldaaykv sfdlyaeyne knpawakiyp awkkfrdegf ewfrvaeyty
      361 dsyvyaaqaa gk
//
LOCUS       WP_006175388             385 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Enterobacter cancerogenus].
ACCESSION   WP_006175388
VERSION     WP_006175388.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cancerogenus
  ORGANISM  Enterobacter cancerogenus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 385)
  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 385)
  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   3  (residues 1 to 385)
  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   4  (residues 1 to 385)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 385)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 385)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 385)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Enterobacter cancerogenus"
                     /db_xref="taxon:69218"
     Protein         1..385
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40509
     Region          32..368
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(108..110,131..132,181,233,257)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mktvkisals aaillsgfas tgawaadset vviglagplt gpsarigkdl engaqlaidd
       61 inkqhptigg kavtfklqse ddqsdprtav avaqrlvdsg vagvvghwnt gtsipaarvy
      121 hdagiaqvap vatghaytkq gfdtsfrvmg hdddggqfag qyavntlkak riaviddrta
      181 fgqgladefi ksldaqgvki vdrqyvddkt vdfsavltai rsknadliff ggvdsqaapl
      241 arrikqlgmk atlmgaggfv sqtflqlaqk egegvvalep glpveqmpgg kafeqayqsr
      301 yhthielhap faydatrvlv aamekadsvd padylpalra isysgvtgqi afdkegnlts
      361 psftvykvvd gkwqpqtvlg gaksr
//
LOCUS       WP_006175876             415 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Enterobacter cancerogenus].
ACCESSION   WP_006175876
VERSION     WP_006175876.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cancerogenus
  ORGANISM  Enterobacter cancerogenus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 415)
  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 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   3  (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   4  (residues 1 to 415)
  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 415)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Enterobacter cancerogenus"
                     /db_xref="taxon:69218"
     Protein         1..415
                     /product="CmpA/NrtA family 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=45679
     Region          35..286
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 madlsrrrfl qasmlasgam llpgimqaaw aagsdrpeqq tvrigfiplt dcapvviaal
       61 kgfdkkygit ivptkeaswa avrdklvage ldaahilygl lyglelgiag kpqemanlmt
      121 lnqngqaitl ssdlaekgvr dldglkkrva qqppgtytfa htfptgtham wlyywlasag
      181 inpfddvrtv vvpppqmvmn mrignmvgfc vgepwnarai ndrigftaat sqsiwadhpe
      241 kilgtrrawv eknphtaral vsavleaarw idaspenkre taqilsrraw lnckeqyltg
      301 rmlgeydngl gqrwqddhpi rffndgavsy pylsdgtwfl tqfrrwgllk aapdynaiaq
      361 rinqtavwqd aatavgdist pssplrsstl mdgtvwngtd pdgyanrfai hrkga
//
LOCUS       WP_006176006             165 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Enterobacter].
ACCESSION   WP_006176006
VERSION     WP_006176006.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Enterobacter"
                     /db_xref="taxon:547"
     Protein         1..165
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17682
     Region          1..153
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mnksefyadl nrdfqalmag etsflatlan tsallferls gvnwagfyll edntlvlgpf
       61 qgkiacvrip vgrgvcgtav atnqvqrved vhafdghiac daasnseivl plvvkgqimg
      121 vldidstdfg rfsaedeqgl relvanlenv lattdyqkff asvag
//
LOCUS       WP_006176665             206 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Enterobacter].
ACCESSION   WP_006176665
VERSION     WP_006176665.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 206)
  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 206)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 206)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Enterobacter"
                     /db_xref="taxon:547"
     Protein         1..206
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22098
     Region          1..204
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 meiyenendq vdavkrffae ngkalvvgvi lgvgalmgwr ywnshqadsa rgaslayent
       61 vsdiradqpq tlaaaekfva dnkntygala alevaqqyvd kneldkaaaq lsqslaaasd
      121 enlkavinlr lariqvqqkk addalktldt ikgegfaaiv adlrgealls kgdkegarka
      181 wqagveskas palsemmqmk innlsv
//
LOCUS       WP_006178539             299 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Enterobacter cancerogenus].
ACCESSION   WP_006178539
VERSION     WP_006178539.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cancerogenus
  ORGANISM  Enterobacter cancerogenus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 299)
  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 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   3  (residues 1 to 299)
  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   4  (residues 1 to 299)
  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 299)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Enterobacter cancerogenus"
                     /db_xref="taxon:69218"
     Protein         1..299
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33439
     Region          28..171
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          207..288
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mnrddiclql tsqikhlidk qndlsallpd irllygtqpg trtpvmyqpg ivflfsghki
       61 gyinervfry dtneyllltv plpfecetfa teavplagir vnvdilqlqe llmdigedel
      121 fqpsmaasgi nsatlsdeil caverlldvm erpldarilg kqiireilyh vllgpgggal
      181 lalvsrqthf slisrvlkri esqytenlsv dqlaaeanms vsafhhnfks vtstsplqyl
      241 ktyrlhkarm lmihdgmkas aaamrvgyes asqfsrefkr yfgvtpgeda trirtmqga
//
LOCUS       WP_006186306             277 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phytoene/squalene synthase family protein [Brucella].
ACCESSION   WP_006186306
VERSION     WP_006186306.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..277
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30490
     Region          1..275
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mnqnethcla llreadrdry lsvlyapqek rgalaalyaf naeiarirdl vheplpgevr
       61 lqwwrdling eargsaeahp vaaalietie kyelpriafd nycearvfdl yddpmpsrnd
      121 legycgetas aliqlagfil drdaaqahae taghagvaqa vagllrllpi hrrrgqvyvp
      181 admlkaigvt rdmllssgdk sateravtim lalarehlai fdkakaglpq tlhpaflpma
      241 lvpaylnave rlgaqaaqkv adisairkqw lmfranf
//
LOCUS       WP_006188083             339 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Treponema vincentii].
ACCESSION   WP_006188083
VERSION     WP_006188083.1
KEYWORDS    RefSeq.
SOURCE      Treponema vincentii
  ORGANISM  Treponema vincentii
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Treponema vincentii"
                     /db_xref="taxon:69710"
     Protein         1..339
                     /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=38548
     Region          1..276
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mreridwidv akaigisfvi mghlhnperv safiyafhmp lffflsgmtf kkeknfidyl
       61 hkkirtllip yflfaiityi fwlilgrhfg edantgipii kpligifysn aidnwlafng
      121 plwyltclfv veiayyflsk vkksicsail ilcgivgyil sltsfirlpw sinvgltaiv
      181 fygfgnlfin giekislrri fngilcilfg iicyitsqmn glidmnsnfy gniilfylga
      241 vsgilaminf sklftnskil ifigrntlvi lalhgiigsv ikgvmvfvfh lklnilnrnv
      301 mlnlvftlit lllslpiilf inryipeltg kqrlsfist
//
LOCUS       WP_006188143             171 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Treponema vincentii].
ACCESSION   WP_006188143
VERSION     WP_006188143.1
KEYWORDS    RefSeq.
SOURCE      Treponema vincentii
  ORGANISM  Treponema vincentii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Treponema vincentii"
                     /db_xref="taxon:69710"
     Protein         1..171
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19073
     Region          4..170
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mnavidallt rvsvrkftdq kiedeklkli adcakaapsg knrqarkfti vhnrekiqel
       61 aqaiakvhnr sdyriydcda illisfaedd iygqcdssca ientylaaea lglgavwinq
      121 lrdkcnepdi rkvldsfhip snhvicgfva lgypaekpap kertepvefi q
//
LOCUS       WP_006188186             384 aa            linear   BCT 20-JAN-2025
DEFINITION  galactokinase [Treponema vincentii].
ACCESSION   WP_006188186
VERSION     WP_006188186.1
KEYWORDS    RefSeq.
SOURCE      Treponema vincentii
  ORGANISM  Treponema vincentii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   McAuley,M., Kristiansson,H., Huang,M., Pey,A.L. and Timson,D.J.
  TITLE     Galactokinase promiscuity: a question of flexibility?
  JOURNAL   Biochem Soc Trans 44 (1), 116-122 (2016)
   PUBMED   26862196
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Holden,H.M., Thoden,J.B., Timson,D.J. and Reece,R.J.
  TITLE     Galactokinase: structure, function and role in type II galactosemia
  JOURNAL   Cell Mol Life Sci 61 (19-20), 2471-2484 (2004)
   PUBMED   15526155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Treponema vincentii"
                     /db_xref="taxon:69710"
     Protein         1..384
                     /product="galactokinase"
                     /EC_number="2.7.1.6"
                     /GO_function="GO:0004335 - galactokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0005534 - galactose binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0046835 - carbohydrate phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=44015
     Region          1..384
                     /region_name="GalK"
                     /note="Galactokinase [Carbohydrate transport and
                     metabolism]; COG0153"
                     /db_xref="CDD:439923"
ORIGIN      
        1 mqkilpfhvd eygdepevtv avpgrfhllg ehtwfaqgnt lsmaidhyly lcvskrkdsn
       61 yrflslslke rkkvaavnlr yrkedrwans ikavilsfmd qgiemtglnf tilseipada
      121 glgtpnalkv atamalrkvf aprltkadlv dilenanvqh lktyphradi lcalyakagh
      181 cvrtnhrrkt adiypfpinn yriiltdsrv prllareeln hriqecmeay ervkkmpdip
      241 kdfsklaesd leelaipesv rrrvlyiire sisvddaida lkkndwvvfs rivtrsqenl
      301 rdrfeiscpe ldwlvkrame fvapdtndiv csrltgrgfg gctysilran diqtyieklg
      361 dyerifgfkp lyykvkpsgg vril
//
LOCUS       WP_006188354             177 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Treponema vincentii].
ACCESSION   WP_006188354
VERSION     WP_006188354.1
KEYWORDS    RefSeq.
SOURCE      Treponema vincentii
  ORGANISM  Treponema vincentii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Treponema vincentii"
                     /db_xref="taxon:69710"
     Protein         1..177
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19981
     Region          3..173
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdlqtcmeqr rsvrkyknqp vphelvreii qaailapswk nlqvsryyva egnaskelak
       61 cladfnqrnv qnapvlivst vvnkrsgftr dgeyethlkd gfqyydhgmq amnlclkahd
      121 lglatlimgi ydetairkff nidenqiiva viavgyadge tpkpkrktvd ditvfks
//
LOCUS       WP_006189411             529 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Treponema vincentii].
ACCESSION   WP_006189411
VERSION     WP_006189411.1
KEYWORDS    RefSeq.
SOURCE      Treponema vincentii
  ORGANISM  Treponema vincentii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Treponema vincentii"
                     /db_xref="taxon:69710"
     Protein         1..529
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=56537
     Region          <152..328
                     /region_name="rne"
                     /note="ribonuclease E; Reviewed; PRK10811"
                     /db_xref="CDD:236766"
     Region          451..527
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mikktitvls mlvlsaaliw avwegnaaag skedfpsglf assdlfpkyt lieitnleqn
       61 ttsraviign agadgvlvki spdlaaalsi qegstvrvrv svpplvaeeg adpvllskve
      121 dkpsvspass ekpeaeasdt vsseeapqee tpreeaqeih eeepvqnepa ppemsepvqp
      181 vpaeeekaae pviateaepv qpetenapek etlpiaevse pmppepease atstvaevte
      241 taeqpaqsed fteyawpvre vaaitvpeea avshtaetpv revlppaepq pesytelpvk
      301 evapiqeppa edtepaadtv etaaiaeaep ekdveepvde paliaaepaa adetvpetea
      361 pideaeneap aekgeepqde pelfasgepl peedntenet venyavlvps epkepiaedl
      421 plpkepekpa paaapiitqp aeepytastl kkgsfyvqig qfkdmlnaqs fvqrygkqyp
      481 vavekspaak gsdvfykvyi gplnkdeqga tletfqklgf kdaflkkap
//
LOCUS       WP_006189839             372 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [Brucella].
ACCESSION   WP_006189839
VERSION     WP_006189839.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 372)
  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 372)
  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 372)
  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 372)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..372
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40621
     Region          38..363
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mketlsrrsf ltkgaaigaa aatsgaalat paiaaelptl rwrltsgfpn nldtiyggav
       61 ymadavskmt dgkfqiqvfq ageivpapqa idavqantve mahtcgyyft gknptfaigt
      121 alpfgmntrl qnawlyhggg nelyneflsd ygivgivggn taaqmggwyr keiksaedlk
      181 glkmriagva gevmsrlgav pqqlpggdiy pslergtida aewvgpydde klgfyqiapy
      241 yyypafwegg asvhffinkk qyeslpeayk valntaaeaa tqnmialydv kntaairslv
      301 skgvklqplp rdvldaaykv sfdlyaeyne knpawakiyp awkkfrdegf ewfrvaeyty
      361 dsyvyaaqaa gk
//
LOCUS       WP_006190852             198 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Selenomonas sputigena].
ACCESSION   WP_006190852
VERSION     WP_006190852.1
KEYWORDS    RefSeq.
SOURCE      Selenomonas sputigena
  ORGANISM  Selenomonas sputigena
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Selenomonas.
REFERENCE   1  (residues 1 to 198)
  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   2  (residues 1 to 198)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Selenomonas sputigena"
                     /db_xref="taxon:69823"
     Protein         1..198
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=20411
     Region          72..198
                     /region_name="comE"
                     /note="comEA protein; TIGR01259"
                     /db_xref="CDD:213597"
ORIGIN      
        1 mpmfkksmlv llavvalaag gafyagihgq eeavtldagt tpqgealvke seivvyvaga
       61 vnhpgvvqla egarakdavd acggflptad tngvnlaqkl kdgmqvtvpe kspqgmavqg
      121 aaggvqagaa rplpegmvni ntadekeldk lpgigpamak riieyrteng afqspeeikr
      181 vkgigdakye kmkdkial
//
LOCUS       WP_006191542             374 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Brucella].
ACCESSION   WP_006191542
VERSION     WP_006191542.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 374)
  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 374)
  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
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 374)
  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   5  (residues 1 to 374)
  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   6  (residues 1 to 374)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 374)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 374)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..374
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39026
     Region          7..>48
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          72..350
                     /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 msihlgmvlk ilrdegpqsr aelarrcgls attlthltaq llkdgciaet dapvlpsgsp
       61 mpgrppvsvr lvpsahyvag vhigaeavqv aicdltaqlv tsaafdhaan dnplklthqt
      121 advlrnlvqa kgislgslvg igmgvpgpvd qvrrrnllsi ntgwrdvafa dameaelnip
      181 tvvehnvtam alaeahygig qgcpavlyvy lgtglgaglv vdgmpfrpgg hgavelghiq
      241 idpqgalcac gnrgcletfv servlrerga gsaepllaal arnpalhdev aghfttalan
      301 avnlltpdli vlgghfaeep eafyarlrcd lpprvlphmr dvlrierggf gnnagavgaa
      361 avaldhlfys gvsr
//
LOCUS       WP_006194216             437 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase [Cyanophyceae].
ACCESSION   WP_006194216
VERSION     WP_006194216.1
KEYWORDS    RefSeq.
SOURCE      Cyanophyceae
  ORGANISM  Cyanophyceae
            Bacteria; Bacillati; Cyanobacteriota.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Cyanophyceae"
                     /db_xref="taxon:3028117"
     Protein         1..437
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=50086
     Region          22..>372
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 matgitkkng hkskkqntis frleyegkip veeilktqpa rlrriisvdk kpinqliyge
       61 nlrvlsslik ndavvgkvgl iyidppyatg ssfesrkrdh ayhdimegae yleflrqrli
      121 llrellseeg siyvhldqnm acavkiimde ifgtknfrnw itrkkcnpkn ytrnqygnia
      181 dyilfytkte nyvwnqqfdp wtentakkey qyveertgri ykkvpihapg vrkgatgqpw
      241 rgmlpppgkh wqytpqtlde mdtrgeiyws stgnprrkvy ldnsqgisvq diwlnfkdah
      301 nqnikitgyp teknldfikr iilassnpgd lvldafagsg ttvavaeelg rkwiaidnss
      361 laittivqrl vkgteamgdf vnrnnptkye qqslintnri lhtgldlyfe etpelelisd
      421 taiknwnsql ncqanll
//
LOCUS       WP_006195981             227 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Nodularia spumigena].
ACCESSION   WP_006195981
VERSION     WP_006195981.1
KEYWORDS    RefSeq.
SOURCE      Nodularia spumigena
  ORGANISM  Nodularia spumigena
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nodulariaceae; Nodularia.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Nodularia spumigena"
                     /db_xref="taxon:70799"
     Protein         1..227
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25149
     Region          32..222
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mvvnfartst nadtlrqvfw svdaqscptl lnfhlhtvhs dgklqpstlm eqaiaiglqg
       61 laitdhhsik gyeaaqdwle nyrgnssent pylwsgvein anlldvevhi layafepehp
      121 sikpylqrkp ttgkeyqahn viaaiqqagg lavlahpary krshfdlvpa aaergidgve
      181 afyayknpkp wtpsaletqq vqqladeyql fntcgtdthg lsllqrl
//
LOCUS       WP_006194493             538 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Nodularia spumigena].
ACCESSION   WP_006194493
VERSION     WP_006194493.1
KEYWORDS    RefSeq.
SOURCE      Nodularia spumigena
  ORGANISM  Nodularia spumigena
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nodulariaceae; Nodularia.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 538)
  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 538)
  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 538)
  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 20073035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Nodularia spumigena"
                     /db_xref="taxon:70799"
     Protein         1..538
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=61230
     Region          7..>56
                     /region_name="di_4Fe-4S_YfhL"
                     /note="YfhL family 4Fe-4S dicluster ferredoxin; NF033683"
                     /db_xref="CDD:468141"
     Region          474..533
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
ORIGIN      
        1 mpytipnnnc vgcdncrpqc ptgaikiend eywidpnlcn ncegyypepq cvivcptnsp
       61 ipwqakkgrc kveprdapsp dlfangqnnp fasaiviwea cnvlaqrtsl nweinqagyl
      121 sygrkvkqgr gaiafhledp fpvnahasks itelaaiaal diratcihlm faayatsleq
      181 pweqefaide rqiekylgle krkdlsknak laliknivqq acslmisidw pqqgripgfs
      241 vtgsrlwdli niqhhfqedd lgckylvglt fkvkagiwaq yflnkqacke rtafyqygsl
      301 pktllttvms iwqqhegavr lmlwllfktk mgkeqritvp tllriaygee kvtiasrqre
      361 erkrllrtfe sdlevlnhhg ikpnfdpvty pleiqplwak lmgipedpee alefwtndgg
      421 gnnrltdsgp rgkwnllmna rilsfelppe weqrtsqlqk kprrtvksrr ktntisdlpg
      481 eqilqarknl qlsqrelakl tgksqswird vengrlkvka edqallrkvl nidsgisk
//
LOCUS       WP_006198001             113 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Nodularia spumigena].
ACCESSION   WP_006198001
VERSION     WP_006198001.1
KEYWORDS    RefSeq.
SOURCE      Nodularia spumigena
  ORGANISM  Nodularia spumigena
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nodulariaceae; Nodularia.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Nodularia spumigena"
                     /db_xref="taxon:70799"
     Protein         1..113
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12979
     Region          10..109
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mtkaetetvk qlaialpmna iqsfcqrwqi velsvfgsil rddfnaesdv dflyalktnt
       61 rwrlsdlida eeelekmlsr kvdlvgktti eqshnwlrkq nilssakviy ede
//
LOCUS       WP_006200455             501 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Mesorhizobium amorphae].
ACCESSION   WP_006200455
VERSION     WP_006200455.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium amorphae
  ORGANISM  Mesorhizobium amorphae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Mesorhizobium amorphae"
                     /db_xref="taxon:71433"
     Protein         1..501
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=51828
     Region          7..501
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mnaansills padnvavang rieigtvlpg gavaaaliep ghkvaikpia ageavvkyaq
       61 aigratqdia agehvhshnl vfesgrlpvv ppseaehate adrartfmgy rradgragtr
      121 nfigivasvn csatvchaia dqanrellpk ypgidgfvpi vhgqgcgmsg tgdgmmvlhr
      181 tlagyarhpn fggvlmvglg cevnqltlyg qkgvaagkrh fniqeaggsr ksvekamgvl
      241 aeiaeevgkl krepipvsei vvglqcggsd gmsgitanpa lgaavdilad vggigilset
      301 teiygaehll ayraaspeia arldgyikww edhvakhgas idnnpspgnk rgglttilek
      361 slgavakggq tplngvfgya ekvtghglvf mdtpgydpvs atgqvaggan vivfttgrgs
      421 cfgcrptpsi kvasnstmyh tmeedmdvnc gviasgekti agmgreifel ivetasgrkt
      481 kseafgygdn efvpwhlgat l
//
LOCUS       WP_006200340             189 aa            linear   BCT 20-JAN-2025
DEFINITION  transcription termination/antitermination protein NusG
            [Mesorhizobium amorphae].
ACCESSION   WP_006200340
VERSION     WP_006200340.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium amorphae
  ORGANISM  Mesorhizobium amorphae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Kang,J.Y., Mooney,R.A., Nedialkov,Y., Saba,J., Mishanina,T.V.,
            Artsimovitch,I., Landick,R. and Darst,S.A.
  TITLE     Structural Basis for Transcript Elongation Control by NusG Family
            Universal Regulators
  JOURNAL   Cell 173 (7), 1650-1662 (2018)
   PUBMED   29887376
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Liu,B. and Steitz,T.A.
  TITLE     Structural insights into NusG regulating transcription elongation
  JOURNAL   Nucleic Acids Res 45 (2), 968-974 (2017)
   PUBMED   27899640
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Steiner,T., Kaiser,J.T., Marinkovic,S., Huber,R. and Wahl,M.C.
  TITLE     Crystal structures of transcription factor NusG in light of its
            nucleic acid- and protein-binding activities
  JOURNAL   EMBO J 21 (17), 4641-4653 (2002)
   PUBMED   12198166
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415705
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Mesorhizobium amorphae"
                     /db_xref="taxon:71433"
     gene            1..189
                     /gene="nusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
     Protein         1..189
                     /product="transcription termination/antitermination
                     protein NusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
                     /calculated_mol_wt=21146
     Region          22..186
                     /region_name="NusG"
                     /note="Transcription termination/antitermination protein
                     NusG [Transcription]; COG0250"
                     /db_xref="CDD:440020"
ORIGIN      
        1 mlqsdlhyep lpeptrdsrd gkaarwcvvq thqhseslae rhllsqnfrt ylpkrkrtvr
       61 harsvktvcs ayfdcylfvs lavdqqswyp instvgvrkl vmshgvptpa pygvvealis
      121 atddegilhp dvllrpgqri ritdgpfseq lgvldyvgka gavrilldim nrsipitidr
      181 dnisivsqn
//
LOCUS       WP_006201464             622 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Mesorhizobium amorphae].
ACCESSION   WP_006201464
VERSION     WP_006201464.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium amorphae
  ORGANISM  Mesorhizobium amorphae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 622)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 622)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..622
                     /organism="Mesorhizobium amorphae"
                     /db_xref="taxon:71433"
     Protein         1..622
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=65593
     Region          13..611
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 msgralatli alilaglwga glgfahwrgn lgfldrveat mtdlrtlvrg takppeliti
       61 vaiddetvrv egsyplsrat larlvdsiar lepkaialdl llvdpgakdd daalarslgr
      121 sasviaaaav ypggrqwava egegplarvp daerflwplk afsdaaavgv vnvvtdrtgt
      181 prfvpllfra gdrleasfsl rvaalaaged paiapdhlsl gsrrvrtdig hilpltfygp
      241 rgtirtisaa tvlegqldrg iirdrivvig atatgagdvf ptpfdpvlpg vevmstaiah
      301 latddgivrd rsvrladagf avvlpmvlvg llawrrnaig laavagvvli wfvvnmtafs
      361 hhiwlsaalp maaavppall fgsaqlwlgr nraqyfaaqs ellqrveapg lgewlarhgd
      421 flkepvrada ailfidlsgf tglsetlgps atrellnafh glvnkevadc ggvvtsfmgd
      481 gamilfglpe paandafnaa rccarlssrt ndwlvslpas tasrlgfkig ahhgtivasr
      541 lggearqhia atgdtvnvas rlmeiaaeqn aevavsdkml eaagrdcalf ksgvlrgpve
      601 tqirgrsgsl aiwfwqsart lq
//
LOCUS       WP_006201728             292 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Mesorhizobium
            amorphae].
ACCESSION   WP_006201728
VERSION     WP_006201728.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium amorphae
  ORGANISM  Mesorhizobium amorphae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Mesorhizobium amorphae"
                     /db_xref="taxon:71433"
     Protein         1..292
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31866
     Region          16..256
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mrlhhahtvf dcnnqlgegc swsasdqslw wtdieaksvf rwddkrrvaa vrqlpnraaf
       61 vfprarggfv lgfpksivit dptftdfsqv aeiephlaqt rvndaaidpy ggivlgtyne
      121 rsrepvgsvy rlapdgevvt lfggvaaang lafspdgrim yftdttdgti rrfdlapqfa
      181 slteigplag anvapgspdg aivdieggyw sarlrggcvv ridrnghltd rvdmpsmapt
      241 cvalggedlr tlfitsrrir qppgellrfp esgnlfrvev dqagrlpfdc rv
//
LOCUS       WP_006201899             312 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Mesorhizobium amorphae].
ACCESSION   WP_006201899
VERSION     WP_006201899.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium amorphae
  ORGANISM  Mesorhizobium amorphae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
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
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Mesorhizobium amorphae"
                     /db_xref="taxon:71433"
     Protein         1..312
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=33691
     Region          1..309
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mieiegitkr ydattvvddv smvieprtia vivgtsgsgk ttllrminrl veptagiirl
       61 dgndnrsqpd yelrrsigya iqghglfphr tvaqniatvp vllgwdkari karvdelmtl
      121 yqldpeaygp ryphelsggq qqrvgvaral aaepnvllmd epfgaldpii rtkaqedlla
      181 iqkrfgttii lvthdmeeav rmgdkiavmd agklvqyakp aeilakpasd fvetlvgase
      241 kpfrllslgr vsdavekgta egeaipgdas qrdalaellw sgrsalpvkg edgkplgrvt
      301 vdglvkraar pa
//
LOCUS       WP_006202191             150 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Mesorhizobium amorphae].
ACCESSION   WP_006202191
VERSION     WP_006202191.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium amorphae
  ORGANISM  Mesorhizobium amorphae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 150)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Mesorhizobium amorphae"
                     /db_xref="taxon:71433"
     Protein         1..150
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=16026
     Region          38..149
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(101..102,105,118..121,123)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mhttisakli nitaaaltga alffgsgaah anqilarvsl sqqtmevlvd grptfawkvs
       61 tggrgyvtpt gsfkptrmhe mwyskkydna pmphsvffsg gyavhatyai knlgrpashg
      121 cvrlhpdnaa dfyqlveafg pantsivivk
//
LOCUS       WP_006202818             346 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Mesorhizobium amorphae].
ACCESSION   WP_006202818
VERSION     WP_006202818.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium amorphae
  ORGANISM  Mesorhizobium amorphae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Mesorhizobium amorphae"
                     /db_xref="taxon:71433"
     Protein         1..346
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38193
     Region          1..345
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mevrvanvrk efdrfpalhd vsldiksgel iallgpsgsg kttllrliag lerptkgaif
       61 fgdedasqks iqernvgfvf qhyalfrhmt vadnigfglk vrhgpsrppt qeirrrasel
      121 ldlvqlsgle krypaqlsgg qrqrvalara maiepkvlll depfgaldaq vrrelrrwlr
      181 dihdatghtt vfvthdqeea leladrvvvm sqgrieqvgs adeiydtpns pfvygfiges
      241 sslpvkvdng diwladrpig lsaahapsge amlyfrphdv elvdgcsgci agtvaasrrv
      301 agtrrvelei ggerqrveie lpvdhpaaqk srvafrprrw klfpaa
//
LOCUS       WP_006204134             404 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Mesorhizobium amorphae].
ACCESSION   WP_006204134
VERSION     WP_006204134.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium amorphae
  ORGANISM  Mesorhizobium amorphae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 404)
  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 404)
  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
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 404)
  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   5  (residues 1 to 404)
  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   6  (residues 1 to 404)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 404)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 404)
  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 15726307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Mesorhizobium amorphae"
                     /db_xref="taxon:71433"
     Protein         1..404
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42713
     Region          23..>88
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          85..382
                     /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 mnenssirak sgtnqegtsa hnrrvmieal rlngalsrad laratqltkq avsniiedle
       61 rdglvvaldt vrkgrgqpst pyrlvpegaf aiglqidrhl travvvdlvg svlaraeanl
      121 pldepsegvk vilglidgvr relagissqs esrlvglgva mpgpfglqns ddkwmmpawq
      181 kfplletlaa gtglnvglqn daaacataer ivgaahgvdh avslyvgygi aaglilngel
      241 ytggngnage igrallspag pgstplehra slaslyqhlg ldaadahlye rmdalalaed
      301 pkvmawikda ahdlrwsvhl ietifdpqtv iltsgapetl arrlleamqp llpsiadrpg
      361 rslprlqlgi tdpwsialga aaepisrafd prfsailktr sggf
//
LOCUS       WP_006207599             270 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Paenibacillus
            glucanolyticus].
ACCESSION   WP_006207599
VERSION     WP_006207599.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus glucanolyticus
  ORGANISM  Paenibacillus glucanolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 270)
  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   2  (residues 1 to 270)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Paenibacillus glucanolyticus"
                     /db_xref="taxon:59843"
     Protein         1..270
                     /product="aminoglycoside 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=30623
     Region          16..>168
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
     Region          <124..233
                     /region_name="CotS"
                     /note="Thiamine kinase or a related kinase [Coenzyme
                     transport and metabolism]; COG0510"
                     /db_xref="CDD:440276"
ORIGIN      
        1 mcdkeevlpg gnvnevvrig nnvhrttnws sfvhdllrhl dkqgfdgapk figidhsgre
       61 ilsfipgevp gnqypdfkpy iwsdhaliqs aallrryhda vqgfattsiq tesehnpqas
      121 gewddevich ndaalynivf rdevpvalid fdlaaqgpri wdmvymlyts vplasfainy
      181 ttgtsipyrs elhaadrthr islffksygi apppnmkewi irrikalcdt lttgaaqgnk
      241 ayqkmidegh vahyekeiqf lqahfeewyr
//
LOCUS       WP_006208990             222 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Paenibacillus vortex].
ACCESSION   WP_006208990
VERSION     WP_006208990.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus vortex
  ORGANISM  Paenibacillus vortex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 222)
  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   2  (residues 1 to 222)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Paenibacillus vortex"
                     /db_xref="taxon:71995"
     Protein         1..222
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=22427
     Region          <69..>156
                     /region_name="MSCRAMM_ClfA"
                     /note="MSCRAMM family adhesin clumping factor ClfA;
                     NF033609"
                     /db_xref="CDD:468110"
     Region          152..220
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkrislgwsl aatiagcgfi lfaggtdkgi egwqplndql eqvvgvegek gmktssansr
       61 ngavedaapa eagdvpdaak kadpdtgsep agntkdlsls ssqgaatvsg spgetsppas
      121 vqpesssgss qtdgdalqtq qrasasesav dspsssvqsg linvntadaa tlmelpgige
      181 akaqaiidyr kqfgpfrsia dlmnvkgigp kmlekmkpyv gl
//
LOCUS       WP_006207194             368 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Brucella suis].
ACCESSION   WP_006207194
VERSION     WP_006207194.1
KEYWORDS    RefSeq.
SOURCE      Brucella suis (Brucella melitensis biovar Suis)
  ORGANISM  Brucella suis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 368)
  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 368)
  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   3  (residues 1 to 368)
  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   4  (residues 1 to 368)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 368)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Brucella suis"
                     /db_xref="taxon:29461"
     Protein         1..368
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37822
     Region          26..359
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(99..101,122..123,172,224,248)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mnlkllssla faatigfasa ayaditigvi apltgpvaaf gdqvkkgaet avevinkagg
       61 ikgekvvlkf addagepkqg vsaanqivgd gikfvvgpvt tgvavpvsdv lsengvlmvt
      121 ptatgpdlta rglenvfrtc grndqqaevm adyvlknmkd kkvavihdkg aygkgladaf
      181 kaainkgait evhydsvtpg dkdfsalvtk lksagaevvy fggyhaeggl lsrqlhdagm
      241 qalvlggegl snteywaigg tnaqgtlftn akdatknpaa kdaiqalkak nipaeaftmn
      301 ayaavevika gieragstdd saavakalhd gkpietaigt ltysetgdls spsfdifkwd
      361 dgkivgle
//
LOCUS       WP_006209471             200 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Paenibacillus].
ACCESSION   WP_006209471
VERSION     WP_006209471.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..200
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21882
     Region          6..200
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 meatrrkswv vgitgasgsi ygvrltesll slgydvhlii snagwrvlke emdfqagnre
       61 emlsekfggy egkviyhpia digatiasgs ylvegmiimp csmgtlssva hgssdnlmgr
      121 aadvmmkegr alvlvpretp lhaihlenml klarlgvkii pampafyygp ktiddivnfl
      181 vgkvldslri ehqlykrwgd
//
LOCUS       WP_006210884             343 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: aminoglycoside phosphotransferase family protein
            [Paenibacillus].
ACCESSION   WP_006210884
VERSION     WP_006210884.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
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
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..343
                     /product="aminoglycoside 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=40317
     Region          <102..261
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mnnhdekfvn pqilvlvlsk mldktvvrad yqlkelqggt lgvvrlvtgm tetsdgeslp
       61 ykvvwktqkk werhgdpdsw rreydlyisd fakfftdslr wpecyygemn gdeiqlwmeh
      121 iegvsglnlt pemyeraaee lgrfqgklya kqsdvslnli nvsevdfvks sylryqswkv
      181 lydyirsddc eipkhlckml ididnhadei fsrieklpiv fchrdfwvan ifysdrkial
      241 idwdtagwgy mgedvaslia deadvchmve yyqkcipayy rgfseyvdvs hitdhcvhel
      301 iltmfgyrlv ewytfaespe dksmhldtlq kiyemrnisi kfd
//
LOCUS       WP_006211040             386 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Paenibacillus].
ACCESSION   WP_006211040
VERSION     WP_006211040.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 386)
  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 386)
  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
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 386)
  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   5  (residues 1 to 386)
  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   6  (residues 1 to 386)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 386)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..386
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42360
     Region          12..56
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          80..380
                     /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 mkkhdqdfmk rqnrltvfqi ikneqpisra aiakqtgmsp ttvsrivsel teegyvhete
       61 eqasagrgrk sslirlldta visigveldr hqanigfidv qgnvlcsgnf prssgdtpea
      121 tvariadiie elilecdidr rrivgigvgl pgiidveagi vnfsvqlgwk nvqlaerlke
      181 ltglqavvdn elkvkalaeq lkgsaygsnr tvllgfgngv gsalilegei yrgvtnsage
      241 ighttvdpeg mmcdcgkagc lqtyinipsl lseaskikpv rtieelfaer ragtrwacyl
      301 idralaymai tinnvvsmyn pdsvilsgei ldkfpevyee itnlcytqyi weplqdsfti
      361 vrsklhehgv iigsglvaqd ryfqln
//
LOCUS       WP_006211097             284 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Paenibacillus].
ACCESSION   WP_006211097
VERSION     WP_006211097.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..284
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31081
     Region          1..254
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mkvdlhchtn isdgslsfge ivalakqegv gylaitnhdt tkglgemvea gvksgveiip
       61 gmeisaydfe rnrrvhilgy yieeghpale eiceplremr hqaslvmtnr lieagykitw
      121 eqietyakdg tgvykqhimh alidngytds iygdlykelf argengkapg iafvpmkyvd
      181 artairavle aggipvlahp gqyrnfefvp elvesglagi evwhplhgpk dvarakdyaa
      241 eyglimtggt dfhgyygeke ialgsmnpvi nslnalkakk gvgl
//
LOCUS       WP_006212110             284 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Paenibacillus vortex].
ACCESSION   WP_006212110
VERSION     WP_006212110.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus vortex
  ORGANISM  Paenibacillus vortex
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 284)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 284)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Paenibacillus vortex"
                     /db_xref="taxon:71995"
     Protein         1..284
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32740
     Region          21..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..280
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mdwiqrmnea igymeahlte eidyaeaari accsvyhfqr mfpyitdvsl seyirrrrlt
       61 laayelqnsd ikvislalky gyespeafar afqnmhgttp taarqagtkl kaypriffqf
      121 smrgaaemny rieemkgfsi vgfqkqirtq qayedvpllw kdahaegifd klwnyrqddh
      181 pirgilgvca dgdygknedf dyimsvvsqh tppdpmvqrh vpaatwavfe megdpsgiad
      241 mwkrlytewv pshaydlapi paiecylppd enknelwipv irka
//
LOCUS       WP_006214440             196 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Brucella abortus].
ACCESSION   WP_006214440
VERSION     WP_006214440.1
KEYWORDS    RefSeq.
SOURCE      Brucella abortus (Brucella melitensis biovar Abortus)
  ORGANISM  Brucella abortus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Brucella abortus"
                     /db_xref="taxon:235"
     Protein         1..196
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20984
     Region          1..189
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mkrivigvsg asgsliplkl lerlavmeev ethlvisdaa qqtlryelga ngysllyrla
       61 artyavedvg aaiasgsvpt agmiiapcsm rtlsaiangy sdslltraad vhlkerrklv
      121 liaretplhl vhlrnmctvt emgaivmppv pafylqprtv edvasqvaar aidligvgtp
      181 qaqswnpeek prrkag
//
LOCUS       WP_006214237             386 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Kocuria palustris].
ACCESSION   WP_006214237
VERSION     WP_006214237.1
KEYWORDS    RefSeq.
SOURCE      Kocuria palustris
  ORGANISM  Kocuria palustris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 386)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Kocuria palustris"
                     /db_xref="taxon:71999"
     Protein         1..386
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40382
     Region          23..374
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 magqataleg qgagmhatga vararitgvg gyqpgepisn dvieelagel paevleglsi
       61 qqrfwlidpr tgehresnad matkaahral dsaglvpedi dgiilstgtp eytlpptvgy
      121 vqeqlglekv stmelrsaga gavqaleiar lqiaagtrrr vlvigsecis pvlagtylam
      181 pkekirmrdr vpiymfsdga gaivveasdd eskglepgae qaiggnrkpg ihavgggtfk
      241 plveqqrtkr lvdlrvdvvg ageftpvmvl ealsgtlaaa gatpadldwc lipegnvgwl
      301 ldsmeeqgtl nadfkalegk vfdnladtga cgsaavplfl dhawrsgmie vgqrvsligv
      361 eatkwiwagi tldwtapapa stgrda
//
LOCUS       WP_006214565             455 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: galactokinase [Kocuria].
ACCESSION   WP_006214565
VERSION     WP_006214565.1
KEYWORDS    RefSeq.
SOURCE      Kocuria
  ORGANISM  Kocuria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   McAuley,M., Kristiansson,H., Huang,M., Pey,A.L. and Timson,D.J.
  TITLE     Galactokinase promiscuity: a question of flexibility?
  JOURNAL   Biochem Soc Trans 44 (1), 116-122 (2016)
   PUBMED   26862196
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Holden,H.M., Thoden,J.B., Timson,D.J. and Reece,R.J.
  TITLE     Galactokinase: structure, function and role in type II galactosemia
  JOURNAL   Cell Mol Life Sci 61 (19-20), 2471-2484 (2004)
   PUBMED   15526155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Kocuria"
                     /db_xref="taxon:57493"
     Protein         1..455
                     /product="galactokinase"
                     /EC_number="2.7.1.6"
                     /GO_function="GO:0004335 - galactokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0005534 - galactose binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0046835 - carbohydrate phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=47899
     Region          30..407
                     /region_name="GalK"
                     /note="Galactokinase [Carbohydrate transport and
                     metabolism]; COG0153"
                     /db_xref="CDD:439923"
ORIGIN      
        1 mhqphpaepg saapewvphp dnaviarsgl enfervfgrr pegiwqspgr anlngehidf
       61 lggrclplal pygtlvaaap rtdgllrmrt leptldegiv evrvedigpg rpegwtgyva
      121 galwglheva ectpgisipe gfgadmlirs tlpvggglss saalecasil afagmitgsd
      181 ehddarraal ahacmmaevr vvgantggld qtaslrshag qvvsldcrdf sityrpadal
      241 ldghrligvd trtphwlggh efssrrldae aaarflgadr lrdllpetps qddvetvlrr
      301 wedaaptaeq lvgrdpgdaf rrlrhaltem lrseqidall agetgvsvpc avgriltsgh
      361 asmrddaeas faaadlivdt alsagadgar ligggfggsv lmlvpeqnve avteavaaav
      421 vkahlpsvrf ldiqpadsgh lvcrdcvela gmgcs
//
LOCUS       WP_006215772             283 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Kocuria palustris].
ACCESSION   WP_006215772
VERSION     WP_006215772.1
KEYWORDS    RefSeq.
SOURCE      Kocuria palustris
  ORGANISM  Kocuria palustris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Kocuria palustris"
                     /db_xref="taxon:71999"
     Protein         1..283
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30245
     Region          1..254
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mkidlhthss asdgtqlpge virsaaeagl dvvaltdhdt tagweeaaea arehavafvp
       61 gtevscqtdd gisvhllsyl qdpqdralde amqrarrsrr traermveli aedypisweq
      121 vldqvvgdat vgrphiadal vaagiaqtrs eafstvlhpr sgyyvghyap dpvtavrlvr
      181 qaggvpvmah plarvrgrtv gqevfdamie aglagleiah rdnppearav lsqmaaehdl
      241 ivtgssdyhg sgkpnelgen ltseqslrri maeagsgtqv vrp
//
LOCUS       WP_006216147             877 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: VirB4 family type IV secretion system protein
            [Achromobacter].
ACCESSION   WP_006216147
VERSION     WP_006216147.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter
  ORGANISM  Achromobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 877)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 877)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..877
                     /organism="Achromobacter"
                     /db_xref="taxon:222"
     Protein         1..877
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=97419
     Region          284..857
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mlltekdgyl ldagtlgeie sartqglast aellpwmfry neqvvvnkds almacfeytg
       61 pdtdsqssaq llglmhqaeh afqvasrnpl tfwfithrrr sdpyapasmp dpysqivede
      121 rsnafktksn yinrhylaia lsasagldrv agrffhamah ekvgpfravm halrgiwsdq
      181 adfaytsvel aaavkdfeeq ltrwraslpa ltltrlagee lggflascaa paaprrasva
      241 mvdfldesms hgevipaedy ilfkaegrkr igvvtaipaa hqfyparlrp halddllkvp
      301 geltishvyr iqdadasarm idqmgsyhrt naldlralaa vaansgdpny apredkgrve
      361 aadetedlkk gvsrgktsyg qytlsvtsls apfhsdqvee wdaameqart tagkvgdali
      421 gakflplvet lgalsswtas ipgawrdiar waplraavva ravplrtvaq gskenrhlaa
      481 tmkqpspala glptdygtpy fwtgfyhdig htlvsgetgl gkttivnlgw tlfrkylgsd
      541 vfvfdrtfss ripimmqggv ycdpedsseg rltvnplsli gdvrhlkfvk dwicmlaerr
      601 gyvatsadre elekailatr qlkrkdwrlh avhvqlsvgs fqnalsewvg ealnarwfdn
      661 aldifdeiaa graaavlgie mgkllaqpdv lipyliycfy riqdriesrr nsgliaptfi
      721 glpevwgfle epvfarklae widtlrkllg cvwmdaqspe ryinspiyas irdnvpnrii
      781 lpypaaktsp slrkaftelg lnpqqidqla egtpkqdyfl tqkdgfmrkv alrldprsla
      841 vlrseldaqa lfdhhrasgr qdwreayfee vvrgsnp
//
LOCUS       WP_006216382             447 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Achromobacter
            piechaudii].
ACCESSION   WP_006216382
VERSION     WP_006216382.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter piechaudii
  ORGANISM  Achromobacter piechaudii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 447)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 447)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Achromobacter piechaudii"
                     /db_xref="taxon:72556"
     Protein         1..447
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48999
     Region          2..396
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mkldvhvggr rvaqlyread qyvlsyvpgt pddafvslam pvrdaawrwp rdlhpffrqh
       61 lpegyllgvi relfgplmdg tdlsllaivg asgigrvavt aegalpgval pplsipdllt
      121 aentaprfha lvreyaqsai sgvvpkflap daqrhgrlet akatlrtpeh iikgsdektp
      181 ylgfneffsl rvlrrlgvvp vvdaqmsadg rllvvdrfdi daqgqrvigv edacsllglp
      241 phekyattte rvhkatrdyl psasmraqnv hfawhllany vvrnadchak nialyyttrg
      301 dvaytpvydv vttqaypefg nsapglsvdg rktwvpgntl akfmlarlgi nakqyqamve
      361 qlcesavevg revieaaknq pdwrwiakqm vhawnegmca lrsakldsky rsldaaisea
      421 gysaadapid ssrvigrseg laapkrt
//
LOCUS       WP_006216484             258 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Achromobacter piechaudii].
ACCESSION   WP_006216484
VERSION     WP_006216484.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter piechaudii
  ORGANISM  Achromobacter piechaudii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 258)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Achromobacter piechaudii"
                     /db_xref="taxon:72556"
     Protein         1..258
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=27835
     Region          29..246
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mipihgsaqp aasggschgc ksdeaasidm tfafqpivdl ksgdayayea lvrgpqgepa
       61 asvlsqvdda nryhfdqrcr ttaielaarl gmdrylsinf mpnavyqpaa cirttfeaae
      121 rhgfpvnqii fetvegesii drahlleifq ayksygfqta iddfgsgysg ltlladfqpd
      181 likldmalvr gidtnnarqr ivagvqrict dlgirviaeg ietagerdfl asqgislmqg
      241 ylfakpafqa mppisnag
//
LOCUS       WP_006217893             808 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Achromobacter piechaudii].
ACCESSION   WP_006217893
VERSION     WP_006217893.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter piechaudii
  ORGANISM  Achromobacter piechaudii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 808)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 808)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 808)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..808
                     /organism="Achromobacter piechaudii"
                     /db_xref="taxon:72556"
     Protein         1..808
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87002
     Region          69..117
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          94..808
                     /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 mstvtdlrls llaaalvalf stpgvraqse ggsrpvavdt anvlrtydip aqalgsslar
       61 iasesgeais vdaelvrgmq apavrgrysa eqaahaaieg sglellrtgs gswalrrlsq
      121 taggvvtlga vqvmgerdpa vtentgayta tgpsatgtpl alslketpqs vtvitrqrld
      181 dqklesiida lesttgvtaf rqgmgtdlsg lwsrgftisn flvdgipssl gassywrnta
      241 mydrievvrg atglmsgmgt paasinlvrk rptaegqasi taeagswdry glgadlsgpl
      301 sdngklrgrl vvdeenqhsw idryekrnrl vygiteldls rstlltvgls yeknendspl
      361 rtglpftysn gaptnfkrsa naapdwsyyd seltnlfasv khdfgkgwng kvevthtqyn
      421 ydsalyfltg sidqrtggga svwpvrwksn dkqttldaql sgpfdllgrq hevvagisls
      481 qlrsdtpdyg swlgpwtgyd gsiadfrhwd gasntpdfvk agqtntketq ysaylttrfk
      541 ladptsliag arvinwerka dtsvvgvpgs thadtretgv ivpyaglvhd lnenwtvygs
      601 ytrifspqsa strdvnntvl dpergtsyel gikssfledr lnaglalfkt rqsnlanyda
      661 atssyvalqg iqtkgaelel tgelsrgwni aagytystse dakgqraitq iprhsvklft
      721 tyrlpdalnk ltvggglnwq sasgyvgeaq qssytvvnam aryefskqfs atlnvnnvfd
      781 kayysglsmy ggiygaprnv vlsakyaf
//
LOCUS       WP_006218033             261 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Achromobacter piechaudii].
ACCESSION   WP_006218033
VERSION     WP_006218033.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter piechaudii
  ORGANISM  Achromobacter piechaudii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Achromobacter piechaudii"
                     /db_xref="taxon:72556"
     Protein         1..261
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=28296
     Region          2..>64
                     /region_name="Lipoprotein_16"
                     /note="Uncharacterized lipoprotein; cl19472"
                     /db_xref="CDD:473174"
     Region          39..177
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
     Region          203..257
                     /region_name="PG_binding_1"
                     /note="Putative peptidoglycan binding domain; pfam01471"
                     /db_xref="CDD:460223"
ORIGIN      
        1 mirlittlla tavlagcatr gpagldldts itavsqasrv rsivlhyttv ddatslklls
       61 rgkvsshyli tdtgrayrlv denraawhag asswygniam nstsigieiv npgwtegpdg
      121 kplwhayndr qvraltillr dliqrhgvap envvghsdia pqrkvdpgpl fpwktlaiag
      181 igrwydetga aehlarlqvq gmpdvawfqk qlqrlgyacg qdgkldaati ntlaafqmhy
      241 rpalhdgqpd letaaimlam p
//
LOCUS       WP_006218437             642 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Achromobacter].
ACCESSION   WP_006218437
VERSION     WP_006218437.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter
  ORGANISM  Achromobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 642)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 642)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 642)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 642)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 642)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Achromobacter"
                     /db_xref="taxon:222"
     Protein         1..642
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=70189
     Region          12..642
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msqatagapl ptgphaggvh apssraalil galgvvygdi gtsplytlra cltglsvhtd
       61 lepahllgvl silfwmlmvv vslkyvtlvl radnrgeggt lallelavrn rdgkmrwvli
      121 vlgifgaalf ygdsmitpai svlsalegig ivshtldawv vpialvvlva lfaiqshgtg
      181 lmgklfgpvm lvwfgtlaal ggwqiwqtpe vlaalnpmwg lrfvvefpli sfvllgavvl
      241 altgaealya dmghfgrpai rsawfsmvlp altlcyfgqg alllrdpeai rnpfflmapd
      301 wglvplvala tiativasqa visgaysvtr qavqlgfwpr mqilhtsave kgqiylpqvn
      361 alllcavlvl vllfrnsdnl aaaygfavtg tmlttsvlaf avlprgstgv krmlwfgvlg
      421 flllfdvllf sanvfkiheg gwlpllvaiv vftlmmtwrr grrllsdmqq rdrqplkefm
      481 eqleeyppsr vpgtaifmtm nsgnvppall hnlkhnkvlh dhvlfltirv advpyvspee
      541 rfdvnklsas swtatvnygf kedpdvpeal rlvaeaypel dlepmrtsyf lsrqtvvaar
      601 kpalwrwrra vfsfmarnst rstkffkipa nrvvemgmqv el
//
LOCUS       WP_006218684             656 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Achromobacter piechaudii].
ACCESSION   WP_006218684
VERSION     WP_006218684.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter piechaudii
  ORGANISM  Achromobacter piechaudii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 656)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Achromobacter piechaudii"
                     /db_xref="taxon:72556"
     Protein         1..656
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=71224
     Region          87..636
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mstlrrllfc tallvgfill gaqalgmiaa hrylntqlaq qseggasalt walahasssp
       61 deraaladdl yaqglyalvr itddngstli erqqsasasg rdgdwrrdwl nvqppaitra
      121 yvsmdggarg tvtvqadgql ardtlwqggv rvlglvlaag vfwslfafnl vrwieartsr
      181 dicqrvrals pdndalpvgs celagvdqal vdaqrrvaat veeqnakies lqseiyrdpi
      241 trlsnrkhfv dqfraaladk stdagghvlm frqrdlaqin rhlsraftdq wlrsssdrlr
      301 klvvefggps tqlarisgsd fallmprtsa pqasvlaerv rrelralrvp mdkygwcrwa
      361 lamaafapgd nmsdalarld halmcaesad ddqitlasqa adstrigeys whdalatale
      421 qhrfslsvqp lhavtgellh heasltlhdt tggdpvpasi fippavrlgl saecdiqair
      481 lgldwlfths ealtvpvsla slaqtsflsr lermladrpa ltgrliievd adglieqggd
      541 lrqlcdivta aggrvglsrl sqqfgamerl hefpvcylkl cgsfitgllh spgsqhlaat
      601 vmataatldm avyaedvpds atqdiledlg vrairgavvn fahtrelapd hqwvss
//
LOCUS       WP_006219461             132 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Achromobacter piechaudii].
ACCESSION   WP_006219461
VERSION     WP_006219461.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter piechaudii
  ORGANISM  Achromobacter piechaudii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Achromobacter piechaudii"
                     /db_xref="taxon:72556"
     Protein         1..132
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=14299
     Region          20..99
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mehqtnivgg pksspggpgp evmaagtleg ndvynsaged lgsikdimid vprgrvayav
       61 lsrggvlgig dklfaipwaa ltldtdrkcf vldideetlk napgfdkdnw psmadetwar
      121 nlhtyykqei yw
//
LOCUS       WP_006219477              96 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Achromobacter
            piechaudii].
ACCESSION   WP_006219477
VERSION     WP_006219477.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter piechaudii
  ORGANISM  Achromobacter piechaudii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 96)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Achromobacter piechaudii"
                     /db_xref="taxon:72556"
     Protein         1..96
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10912
     Region          13..89
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 maqrsdqwkn mpigsrslns ffqhcfglgp vqylhlrrlh hiraalrdmr epsatiadvf
       61 ewggypysay alsryraifg eppsetrars pvmqgt
//
LOCUS       WP_006219885             208 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Achromobacter].
ACCESSION   WP_006219885
VERSION     WP_006219885.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter
  ORGANISM  Achromobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 208)
  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 208)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 208)
  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   4  (residues 1 to 208)
  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   5  (residues 1 to 208)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Achromobacter"
                     /db_xref="taxon:222"
     Protein         1..208
                     /product="TRAP transporter small permease subunit"
                     /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=23375
     Region          1..170
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mlrlirlidr vstfvgktfa wlivvltlhv cwevaaryll nqpsawafdm qmmyygilfm
       61 magaytlakn ghvrgdilyg flpprvqggl dlilylvfff pgaialvwag wyyasysiai
      121 gehsslmang ppiypfkafi pvagavlllq gvaevlrcil clrrgawpar eedveevdvd
      181 klkqmvhvkd ediarldryv ttpgeaqr
//
LOCUS       WP_006220077             339 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Achromobacter
            piechaudii].
ACCESSION   WP_006220077
VERSION     WP_006220077.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter piechaudii
  ORGANISM  Achromobacter piechaudii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 339)
  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 339)
  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 339)
  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 339)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Achromobacter piechaudii"
                     /db_xref="taxon:72556"
     Protein         1..339
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=36933
     Region          6..337
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mklltrrsal rrlcavpava laggfpliar aadytlkygn nlpvthplnv raqeaadril
       61 kesngrvdik ifpnnqlggd tdmlaqvrsg gidfftpsal viatlvpvaa inavgfafkd
      121 ynqvwgamdg algahvraai aqrklyafek mwdngfrqtt sskapvstaa dmdglkirvp
      181 vsslpismfk glgaapaslq fsevysslqt kvvdaqenpl piiqvaklye vqkycsltnh
      241 iwdgywfian grmweglpad lktivargin eaglaqredi kklnasvqsd leskglkfnq
      301 papdsfreal rtagfykewq grfgneawsl leqsvgkla
//
LOCUS       WP_006220851             285 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Achromobacter piechaudii].
ACCESSION   WP_006220851
VERSION     WP_006220851.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter piechaudii
  ORGANISM  Achromobacter piechaudii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 285)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Achromobacter piechaudii"
                     /db_xref="taxon:72556"
     Protein         1..285
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=31100
     Region          90..217
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(175..176,194,210..213,215)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
     Site            order(194,213)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mmpqsetmia rtrlpraapa wlmaaaivaa tlgtgmpawa rmppdevara frqevspalv
       61 lpedeqtryg dlalqslhaa glvllapqyv lvvdrnvkvq aamlywmqpd appvyvgaap
      121 vstgrvgqfd hfetptgvft hglnnpdfra egtknangir gygakgmrvy dfgwqqarqg
      181 wtqngvstmr lqmhatdptl lepklgtpqs kgciripatl nqlidrlgll dadyelaadl
      241 vstpwvlrrd rvpadgagry liivettrdk rpawspppra vkgkp
//
LOCUS       WP_006220384             408 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Achromobacter piechaudii].
ACCESSION   WP_006220384
VERSION     WP_006220384.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter piechaudii
  ORGANISM  Achromobacter piechaudii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 408)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Achromobacter piechaudii"
                     /db_xref="taxon:72556"
     Protein         1..408
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=43179
     Region          159..398
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mmrdfnmtlp lrdsscgiel itfgpasvss davdallkng alrevraacg ldaliealcq
       61 qdadvilcev hgvpcealll pghlqrefda grlrrlpavl wisdlprsil eacagsfrta
      121 ggklqiatia tgvaasldlf akagrggapa aaaprfnded lilaldaedg irvvlqpqvd
      181 lktgrilgae altrwrhpql gevaaadvvq aisrlsmdpm lfhvvtervl dlhvqlavqg
      241 vatrisvnaa vstlstpgva lsleertlrr gispdqitve itesetisdk talkaglerl
      301 racgfgvsmd dfgtgastle rlsclpfsei kvdqtfvrrr rsepashavv daavglgral
      361 glaviaegie tpeeasllqs lgcrigqgfg larpmeidvf vekllsap
//
LOCUS       WP_006221688             292 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Achromobacter
            piechaudii].
ACCESSION   WP_006221688
VERSION     WP_006221688.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter piechaudii
  ORGANISM  Achromobacter piechaudii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Achromobacter piechaudii"
                     /db_xref="taxon:72556"
     Protein         1..292
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31369
     Region          15..262
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mpasaervgd llcsvgespv wraseqaytw tdipnrtlwr wspatgefae walpqmagci
       61 aprdagwlla mqdgvyrcdt lrpgepclpq rlagvthaap nmrfndgrcd rqgrflagtm
      121 vmdmgrtqpa grlyrldadg levllddliv pnglafspdg ktmylsdshp sramvwafdy
      181 dvdsgtprnr rpfiaalpag rpdgaavdad ggywicgnda griyrytpdg rldltfsvpa
      241 ckvamcafgg agmdtlfits irpadavpgs ldgavfalrp gargleetas tg
//
LOCUS       WP_006221959             802 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Achromobacter marplatensis].
ACCESSION   WP_006221959
VERSION     WP_006221959.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter marplatensis (Achromobacter spiritinus)
  ORGANISM  Achromobacter marplatensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 802)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 802)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 802)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..802
                     /organism="Achromobacter marplatensis"
                     /db_xref="taxon:470868"
     Protein         1..802
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87659
     Region          62..113
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          90..802
                     /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 mplptlnlry tplafsllla tlgaaaalpa haqqqtdaai pfdiaagpla palnryaqqa
       61 gvaisvdasr iqglttngln gryrvdegfr lllagsgfta arsaggyvlv aapvpgtttl
      121 pavrvsgqsv pgaldptsgl lastsssatk tdtplietpq svsvvtreqi deqkprsvte
      181 alrytpgaft glvgaadryd yvalrgfien stdntiydgl kllsdsgtfs siqidpyfve
      241 ridvfrgpss vlfgrsapgg lvqltskrpl fdpyrsvevs ygtqgqksag fdvagpvddn
      301 gkvayrvtgl grstdtqfdn treeryaiap qvmfnftpdt slllqaylqr dpsggfhsgv
      361 padasitndh agqrisrhfv dsdpdnnefk rnerifsyqf dhrfndrwtf rqnaryvssd
      421 valkqvygyg wangtelnry ysgadeslna faidnqlqgk fetgavkhtv llgldyqnrh
      481 adgrwdsgsa snlnafhpdy angnvqitsr tffdrrleqt gfylqdqlay drwrlilsgr
      541 qdevrttess rtgdyaskqs wsgskftkra glvylfdngv spyvsysesf npnaytdqqg
      601 nllpptqskq yeagvkfqpp gtenmvtlaa fdltqdnvan rvlaqtyytp agkvrsrgie
      661 legkarltdn ftmlaaytft amtyresteg ltgntpyqap rhmaslwgdy qfdsglgvga
      721 gvryvgtswa dsantlkvpa ytlvdlsvry dlgrlssslk gmsvrvaann lldktyvasc
      781 aslnycyyge ernvvatlky ef
//
LOCUS       WP_006222047             738 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Achromobacter
            marplatensis].
ACCESSION   WP_006222047
VERSION     WP_006222047.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter marplatensis (Achromobacter spiritinus)
  ORGANISM  Achromobacter marplatensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Achromobacter marplatensis"
                     /db_xref="taxon:470868"
     Protein         1..738
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=79266
     Region          51..738
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 makarnqnar agfplnrraa aiaaalagls smahaqtapp apaaatgqag elaavtvtgd
       61 wlgtpteekv lshpgartvv eqqqiqesgs ssvrdvlrqi pgvqvqdsng tggsdvslnv
      121 gvrgltsrls prstilmdgv pmayapygqp qlslapvslg nlesvdvvrg agsvrygpqn
      181 vggiinfvtr aipqdfttsl nvgseiyshg gnvkttpslf vggtndkglg gallysgthg
      241 dgyrssndst diddvilkga yrfsatddva vslhhfegkg rmpgglttaq ysedpfqstr
      301 qydqftgrrt dgslkythnd gvnnfevlty yvdsyrgsyi eqggtgatan qfrlttaprs
      361 yyyfgfepry srlfdsgsfv qevtvgyryl kesssevagr tayynpaagg dafdlnmpty
      421 qtsdggttah afyiddridi gkwtitpgvr fesistynnv tnfntatgav tsalspsids
      481 rvtlptlsvl yrvddkwslf anagksfgpq qysqlastte glhpetakty eigthfagqa
      541 wsgeltlfni dfdkelqltr sivgegmwtd lgatrhrgve salrydmgdl sdalrglsvy
      601 atytytqaia kagafegrdl plysrqvasv garyavqrwt fnadvfaqsk qrspgspdag
      661 agyvteedas grlgdipgfa tvalragydf grdmnnlkla vgvknlfdrr yytrstdnng
      721 gkfvgqprti ymqasmaf
//
LOCUS       WP_006222065             441 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Achromobacter
            marplatensis].
ACCESSION   WP_006222065
VERSION     WP_006222065.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter marplatensis (Achromobacter spiritinus)
  ORGANISM  Achromobacter marplatensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 441)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Achromobacter marplatensis"
                     /db_xref="taxon:470868"
     Protein         1..441
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=49143
     Region          13..430
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mararkhksv esqlfvyvdi rgeavlagvl tlddsdehhf faeftyvqsy vndprafald
       61 plnlplidak ttfrtesrye tlgaifdaap dawgrnvmrv dkagarvted evllrgrgmg
      121 vgalffsarq ltpnmrktyr lpeisqlesl adlltdidqg vkpkglyrdi lgsswdigga
      181 rpktivrdeq gemwiakfpr qgdsydrqrv efanlemara igltvpeihl tqthlgavll
      241 trrfdrerla aerggepvva rrhflsgasl ispsaqigkr eldgargkat ysyarladvv
      301 rrvssnpvqd lkelyarmil nvavhntddh lknvgfvkde gagtyrlspl fdvvtqegsa
      361 khylhigaag rdstfenclt eyrrfglrse avaqsildrv revvaeragf ydragmsrae
      421 itqveatlta wrlqggnksp l
//
LOCUS       WP_006222262             206 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Achromobacter
            marplatensis].
ACCESSION   WP_006222262
VERSION     WP_006222262.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter marplatensis (Achromobacter spiritinus)
  ORGANISM  Achromobacter marplatensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 206)
  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 206)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 206)
  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   4  (residues 1 to 206)
  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   5  (residues 1 to 206)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Achromobacter marplatensis"
                     /db_xref="taxon:470868"
     Protein         1..206
                     /product="TRAP transporter small permease subunit"
                     /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=22259
     Region          9..173
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mtqtehfrll ggllrraesf sraavwagga ltvasvllis fdvlarkflg fttggadels
       61 syafaistsw alafatlqra nvrvdvlyqy lpvrlsavld wismvamavf mvfltyyaye
      121 vvqtswaqks aantplatpl wipqglwllg lawmcitval mlarasaalv tgdielvkqi
      181 cgvrsaqeea deeaaagerm vkgepa
//
LOCUS       WP_006222323             877 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: VirB4 family type IV secretion system protein
            [Achromobacter].
ACCESSION   WP_006222323
VERSION     WP_006222323.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter
  ORGANISM  Achromobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 877)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 877)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..877
                     /organism="Achromobacter"
                     /db_xref="taxon:222"
     Protein         1..877
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=97673
     Region          284..857
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mlltekngyt ldagtlgele sarvrglast aellpwmfry neqivvnkds almacfeytg
       61 pdtdsqsaaq llslmhqaeh afqvasrnpl tfwfithrrr sdpyapavmp dpysqivede
      121 rsnafktksn ytnrhylaia lsasagldri agrffhamah ekvgplraai halrgiwsdq
      181 adfaytsvel aaavkdfeeq ltrmraslpa ltltrlvgde lgaflascaa paaprrsava
      241 mvdfldesms hgevipaedy ilfkaegrkr igvvtsipaa hqfypsrirp halddllkvp
      301 geltishvyr iqdanasakm idqmgsyhrt naldlralaa vaansgdpny apredrgrve
      361 aadeaedlkk gvsrgkasyg qytlsitsls apfqsdlved wdsamdqvrt tagkvgdali
      421 gakflplvet lgaisswtat ipgawrdiar waplraavva ravplrtvsq gskenrhlsn
      481 tmkrpspala glptdygtpy fwtgfyhdig htlvsgetgl gkttivnlgw tlfrkylgsd
      541 vfifdrtfss ripimmqggv ycdpedastn rltvnplsli gevrhlkfvk dwictlaerr
      601 gylatsndre elekallatr qlqrkdwrlh avyvqlpvgs fqhalaewvg dalnarwfdn
      661 gldifdeiaa graaavlgie mgkllaqpdv lipyliycfy riqdriesrr nsgliaptfi
      721 glpevwgfle epifarklae widtlrkllg cvwmdaqspe ryinspiyas irdnvpnrii
      781 lpypaaktsp slrkaftelg lnpqqidqla egipkqdyfl tqkdgfmrkv alkldtrtla
      841 vlrseldaqa lfdhyrasdr edwrdayfre vvrasnp
//
LOCUS       WP_006223872             832 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Achromobacter marplatensis].
ACCESSION   WP_006223872
VERSION     WP_006223872.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter marplatensis (Achromobacter spiritinus)
  ORGANISM  Achromobacter marplatensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 832)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 832)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 832)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..832
                     /organism="Achromobacter marplatensis"
                     /db_xref="taxon:470868"
     Protein         1..832
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90019
     Region          78..127
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          106..832
                     /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 mqggklkgai aggamaagvr gkrlpqpmpi svlaacvvaa taapeasraq avqqqeysie
       61 aqpldralrl fseqsrhqvl fdeavvtgrq apavqgkftp realdrllag sgvivnsarp
      121 dvftltritg paadssgavt lqavtvtgqg ertatteqtg sytspaltlg kwtqsiretp
      181 qsvsvitrqq lddrnlttle ealaqttgvt ksarnfgnhk fsirgfnvdn anymidgvpg
      241 tvyapvgwlp vdtavfdrve vlrgagglvl gaadpsgain mvrkrprgea hlemagsvgs
      301 wdnyrgelda ggplnadgtv rarfvtayqd rhffydgsas rapllygvid advgpntllt
      361 fgarrqestt dgywlfglpr ytdggaldvs rstsliqdwn rqkggvsevf aeaehrfagd
      421 wkakvsynht itdldqrvai pvggvdratg igssfydiyf nrmhlvsdgi danttgsfra
      481 lgrthqvlvg anwsrqrtgq qsadltantp idvfnpdhss ipeperpdwd srsslretqy
      541 glyanarlql adplhlilgg rlswleyrad dditgrktad yqqkheftpy aglvydldnq
      601 wsvytsyadt fqpqssyvts sgtpldpaig anyeagvkge lydgrlnvsa avfairksgl
      661 avvdeniaas cpgslasrdc yrnggnlrsk gfeleasgel apgwqvmagy tyltskddeg
      721 qsisaetprh llrlstsyql pgkwnavtig ggvsaqsgys ypayddtsvr mgapgravwd
      781 lraayrfnrh wtaavnvanv fdksyygmis qirrgnhyge prnvmltvrg tf
//
LOCUS       WP_006224174             208 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Achromobacter
            marplatensis].
ACCESSION   WP_006224174
VERSION     WP_006224174.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter marplatensis (Achromobacter spiritinus)
  ORGANISM  Achromobacter marplatensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 208)
  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 208)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 208)
  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   4  (residues 1 to 208)
  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   5  (residues 1 to 208)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Achromobacter marplatensis"
                     /db_xref="taxon:470868"
     Protein         1..208
                     /product="TRAP transporter small permease subunit"
                     /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=23181
     Region          3..172
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mqallalsrg idainlrmgr ivswvtllvv lvsagnaivr kffhfssnaw lemqwymfga
       61 mflltagytl lkndhvrvdi iasrlsrraq vgieifgvlf fllpacllim ylswpvfmds
      121 ylsnehssns gglirwpvkl lipvgfallv lagvshlikc igflmgrcrd preregaksa
      181 eeelaeeiar eaqareaaav reldnkgr
//
LOCUS       WP_006224337             207 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Achromobacter
            marplatensis].
ACCESSION   WP_006224337
VERSION     WP_006224337.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter marplatensis (Achromobacter spiritinus)
  ORGANISM  Achromobacter marplatensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 207)
  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 207)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 207)
  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   4  (residues 1 to 207)
  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   5  (residues 1 to 207)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Achromobacter marplatensis"
                     /db_xref="taxon:470868"
     Protein         1..207
                     /product="TRAP transporter small permease subunit"
                     /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=23313
     Region          1..170
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mirlirlidr istfvgqtfa wlivvlalhv cwevaaryll nrpsawafdm qmmyygilfm
       61 magaytlakn ghvrgdilyg flpprvqagl dlvlfivfff pgvialvwag wyyagysiai
      121 gehsslmadg ppiypfkafi pvagavlllq gvaevlrcvl clrrgawpsr eedveevdvd
      181 klkkmvhvkd ediaqldryv ttpkepr
//
LOCUS       WP_006225125             354 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Achromobacter marplatensis].
ACCESSION   WP_006225125
VERSION     WP_006225125.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter marplatensis (Achromobacter spiritinus)
  ORGANISM  Achromobacter marplatensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Achromobacter marplatensis"
                     /db_xref="taxon:470868"
     Protein         1..354
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39393
     Region          1..350
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msievrnlsk qfgqfralnd vslhietgel vallgpsgcg kttllriiag leapdsgsvl
       61 fagedatavd vrqrqvgfvf qhyalfkhmt vfenvafglr vkhrsqrppe dqirrkvhel
      121 ltlvqldwla drypaqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 rlhdelnvas vfvthdqeea levadrvvlm nagrieqvgt prevwegpat pfvygflgdv
      241 nqlqgvatrg vwegaglslp apelaqadaq ratayvrphe fdieryragg egiavrlsha
      301 ylagpsayle laredsdaii eaevpeylyr eldlrdgeal larprrarif avqp
//
LOCUS       WP_006225647             814 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Achromobacter marplatensis].
ACCESSION   WP_006225647
VERSION     WP_006225647.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter marplatensis (Achromobacter spiritinus)
  ORGANISM  Achromobacter marplatensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 814)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 814)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 814)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..814
                     /organism="Achromobacter marplatensis"
                     /db_xref="taxon:470868"
     Protein         1..814
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88869
     Region          74..124
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          102..814
                     /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 mslpffpshs aapaglrvka faalvlaama gaavspapaq aqsagavaaa rhsvnvpaga
       61 lgaalssfaq qtqvllsfdp alavgmetag lqggygvdqg faallagtgl eavrradgdy
      121 llqrvdgqqa tqlapvvvlg agattegtgl ytadwmrsan glvlsqretp qstsvltrqq
      181 mddrsitsvr dvmenatgmn vqqaeserls yysrgfsmdt fqfdgvvkpl ngiyqfgdgn
      241 ldpviydhve iirgatglms gtgnpggsvn firkrptref qgdfklsagt edtyrgevdl
      301 stpfnesgsv rgrivgaker rgdtmdlykk krdvlygiie advaeattis vggsvqrtrp
      361 sgiswgglpa ldangkpidw pkgqamgakw srwdtdshey faqidhgfan gwnarlsytr
      421 lenkfdapll ftsdvpvtid gfstppllrk fvggsdqdvv ggsmdgdfda fgrrhqfnmg
      481 fshsvikawn qswdtsdqat ypipdvknwt gdwpapnwdi lalsqtnrne qtgvygtlrl
      541 gltdrlhllt garwtrwest etswgvkgys htysevtpyv gvtydlndty tayasytnif
      601 qpqmvktqtw emagpayghn yeaglkasyl dgrlnasvav fqtdqkdvae yggydyahdd
      661 gwyyildgtr trgfeaevag evmpgwnvfl gytyrqskdn tgkkvqttqp eqllklstaf
      721 rlpgawnklt vgggvrwqsq tsaqtyyglq sgsivqkpya lfdlmaqynf sdktqlqlnv
      781 rnladkkyyr smgfynsvfy gegraalvtl tqrf
//
LOCUS       WP_006225813             323 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Achromobacter marplatensis].
ACCESSION   WP_006225813
VERSION     WP_006225813.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter marplatensis (Achromobacter spiritinus)
  ORGANISM  Achromobacter marplatensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 323)
  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 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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Achromobacter marplatensis"
                     /db_xref="taxon:470868"
     Protein         1..323
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35591
     Region          99..323
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          239..320
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 msfqsvytrq vysglepsqa fdvvyggrfe hrllssrdtv lhhqrliige lrletgcydf
       61 pviaqgcmpe dgicigfmva ggdrtkvntt algpdeiqiy paglellyha tgpsrwvnlt
      121 vphellqraa trrlgfsltl prqsarslql npggchaltc avddalnmar rmqpgglapd
      181 lacvihdsll ngyldafgda taaqgaarsi verrhhhlis scerlvlsge dadvaladia
      241 qrsgyslrsl elifrrsvgm tpsrwfmtar lngalrdmlt qgqalsvsei agkwgfrhms
      301 rfaqyfrqaf gesprdtlrr ars
//
LOCUS       WP_006226052             377 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Pseudomonadota].
ACCESSION   WP_006226052
VERSION     WP_006226052.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonadota (proteobacteria)
  ORGANISM  Pseudomonadota
            Bacteria; Pseudomonadati.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Pseudomonadota"
                     /db_xref="taxon:1224"
     Protein         1..377
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=39807
     Region          1..370
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mrvlainags atlkfgvfes artlplidsa idhpavdaat feeierhlhr agvttldgig
       61 hrvahggpll snavlvdeev ereigkasal aphhnpaala girltrerwp gvrhvavfdt
      121 afhddmpeya hsyavppswr aagvrrygfh glshqgvlaa vstelkrpps elrivschig
      181 sgasvcaidr grsvdtsmgm taleglvmgt rcgdldpgvp gfvaralglt laqieaalys
      241 dsglkglsge ssdlrivekr agegvgaaql amqvhayrvr kyigayaaam ggcdavaftg
      301 gagensaalr rrivdglefi gleldeernr ayspntevaq lqssrsavav lvvqareqla
      361 iaretfraln dqasglv
//
LOCUS       WP_006227791             787 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Achromobacter marplatensis].
ACCESSION   WP_006227791
VERSION     WP_006227791.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter marplatensis (Achromobacter spiritinus)
  ORGANISM  Achromobacter marplatensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 787)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 787)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 787)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..787
                     /organism="Achromobacter marplatensis"
                     /db_xref="taxon:470868"
     Protein         1..787
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=85824
     Region          49..97
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          75..787
                     /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 mlslrfpaac viaaaastah aqalhqydlp agqldvsltr iariagavis fraelvagks
       61 apaisgqltv eeataraltg sglelrrtad gsltvapsst ttlapvtvea ttpgvtegth
      121 syttpimsta tkfalspret pqsvsvvtrq qiedrgfqsl ddvardapgl ttrqiggger
      181 tqffsrgfei nsfladgvpl aydydtqgva tlamydhiev lrgaagmmtg agnpsgtinl
      241 vrkratavpq fsvttsagsw dnyrgevdgs gplneagtlr argvvayqds ntfkksyehq
      301 rqlfygtiea ditanttlsi ggyynrednp gadwnglptr rdgsfydfnr sirlspdway
      361 wnkentsffa eldhrfengw sgkltartlr akmnmlgsyl ypledstffg qglgqydydk
      421 tqysvdgyls gpftllgrth elvlggsflk nkdddgpggw pldynmtvdp ehwdssavek
      481 pafvypwsrk gyqrqmsgya ttrlsladpl mlmlgarldw yeydmnlksg dyvsppagyk
      541 vnheltpyag liydldrqhs vytswtsvfq pqgsqsasgt pldpvigtnl eagvkgeyfd
      601 grlnasaavf qirqrnrpva latsacspgv iecyapsgkv esrgfeleva galtpawqvs
      661 agytfnrsky ledsgaisag apydtqtprh lfklstmytl pgslnawrvg gavrvqsais
      721 lpaysvrqpg ysvwdvvvay rasqnldlrl nvynlfdkyy yqaigstqdn nhfgaprafl
      781 ltakytf
//
LOCUS       WP_006227895             381 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Achromobacter marplatensis].
ACCESSION   WP_006227895
VERSION     WP_006227895.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter marplatensis (Achromobacter spiritinus)
  ORGANISM  Achromobacter marplatensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 381)
  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 381)
  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   3  (residues 1 to 381)
  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   4  (residues 1 to 381)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 381)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 381)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Achromobacter marplatensis"
                     /db_xref="taxon:470868"
     Protein         1..381
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40703
     Region          29..365
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(105..107,127..128,177,229,253)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkfrttlkll aasiaavgmt aaanaadikf gfaapltgpq shygedmqng lnlaleeank
       61 kgikvdgqpa kfvlvsrddq adprvgvqva qqlvdqdvvg ilghfnsgtt ipasrvyhea
      121 glpqiamats peytkqgyet tfrmmtsdtq qgaavgkfiv qnlkakkvai iddrtaygqg
      181 ladevekavk aaggevvrre yttdkandft ailtnikgsa pdaifyggld aqsgpmkrql
      241 atlglkaplv sgemtrsdtf iklagdaadg tyaslagvpl dkmvagkdfe qryqarfkka
      301 pgvyapyayd gawnmitaie qagsakpeky lpvlakldrk gatsehisyd akgdlkeisv
      361 tiyevkngkw emvetmvsqa n
//
LOCUS       WP_006228800             392 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Photobacterium
            profundum].
ACCESSION   WP_006228800
VERSION     WP_006228800.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium profundum
  ORGANISM  Photobacterium profundum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 392)
  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 392)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Photobacterium profundum"
                     /db_xref="taxon:74109"
     Protein         1..392
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45281
     Region          1..386
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mrtlslpqar klallsqcis trslkgsayt etlnvferlg yvqidtisvv qrahhhtlws
       61 rnpryqvahl dqlvadkkvf eywshaasyl pmrdyrfslp rktalkmgqq shwykkdhkl
      121 madvlqries egplmakdfv skshktngwg skpskqalet lfmqgdlmia erknfhkvyd
      181 ltqrvlpndv dasipteqeq eqeqehgqfl vlsylrahgf gnlaeityll knvktlasqa
      241 lnvllergdi krviinefvy faccdallll dkrlnkkqvh ilspfdnlli qrkrtqsifn
      301 ykyllecyvp aakrqfgyfc lpvvwdgtlv tradckvdkq tstlnvihlf iessvkekei
      361 fftaleeklq afaqfnqcsh yaiqkasthk ci
//
LOCUS       WP_006228652             265 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Photobacterium profundum].
ACCESSION   WP_006228652
VERSION     WP_006228652.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium profundum
  ORGANISM  Photobacterium profundum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 265)
  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 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   3  (residues 1 to 265)
  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   4  (residues 1 to 265)
  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 265)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Photobacterium profundum"
                     /db_xref="taxon:74109"
     Protein         1..265
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29753
     Region          37..262
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <169..262
                     /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 mntkfkhsei vilpeqmehh nhgynqvvig lsgqtefdie gygnlvcpgq gclvtadseh
       61 afsglgrnei lvlnipvsqn sfeetyghlq psyaverver lfdqssyfhl dsqaqnlina
      121 ltvemtahpd dlllskactd tlmcvlqrhf kplasdrhia rlnmdivdqy iikhltrkis
      181 vtqlaglvfl gesqfhllfk nqtgvtphqy vlkkrlemak qlmeesqlsl aqvaqscgfs
      241 gqssftqafs rlygmpparf kkdnl
//
LOCUS       WP_006229811             166 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Photobacterium profundum].
ACCESSION   WP_006229811
VERSION     WP_006229811.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium profundum
  ORGANISM  Photobacterium profundum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 166)
  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   2  (residues 1 to 166)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Photobacterium profundum"
                     /db_xref="taxon:74109"
     Protein         1..166
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18060
     Region          95..165
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 miralfitll fllpfttqat tsstkaqiek cetkyksdtk kktdcinsvk kkaketakkd
       61 dvtkhktann dsrqntstkm hgntesrqle daqkksavtk nlkavnvnsa saedlaaslp
      121 gigdakakai vdyrkkngkf ksasdlakvp glgdksvgnm kkylky
//
LOCUS       WP_006230863             361 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Photobacterium
            profundum].
ACCESSION   WP_006230863
VERSION     WP_006230863.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium profundum
  ORGANISM  Photobacterium profundum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 361)
  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 361)
  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 361)
  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 361)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Photobacterium profundum"
                     /db_xref="taxon:74109"
     Protein         1..361
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39751
     Region          1..359
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mmrrsvkaiv aliasmlisa cdsndsasnv edistvewtl vtswpkgfpg lgeapehfae
       61 kvnilsrgrl qikvygagel vpsfdvfnav skgtaqmghs aayywqkkip aspffasipf
      121 gmtaqemnaw lhyggglelw qelyapfgvv plsggntgaq mggwfnkeit tlddlsglkm
      181 rlpgfgadvl kraggipvsl pggelftale tgaidatewv gpyndlafgl hnaakyyyyp
      241 gwhepgtnle flinkdalqa lpvdlrevik iaaravsqdm ldeytlknvq aldillnehn
      301 vllkvfpddv llrlkqltne llveksdsdp tlkkvydsyy rflidvrqyg rftenadvni
      361 d
//
LOCUS       WP_006230893             164 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Photobacterium
            profundum].
ACCESSION   WP_006230893
VERSION     WP_006230893.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium profundum
  ORGANISM  Photobacterium profundum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 164)
  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 164)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Photobacterium profundum"
                     /db_xref="taxon:74109"
     Protein         1..164
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18490
     Region          64..116
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mqdydydyep rpkggfkpfs pskmhnksss prphsnssai kkkprtthfd lmaplrdamt
       61 vsdltgierl vlwtlysrmd khgvcfpsya riskeagiad rtakkaiksl vektwltykk
      121 gsqisgkane ykldmnkldl tqvkirqetk takipalscd dgdf
//
LOCUS       WP_006231024             103 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Photobacterium profundum].
ACCESSION   WP_006231024
VERSION     WP_006231024.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium profundum
  ORGANISM  Photobacterium profundum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Photobacterium profundum"
                     /db_xref="taxon:74109"
     Protein         1..103
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11454
     Region          1..100
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(4..5,23..24,32,35,37..38,40,43..44,46,54,59,66)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(23,54..55,57,81)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mddfsaqiyt qvhqipygkv stygeiakfs gfpgyarhvg rlmatlpegs kipwyrvvna
       61 kgmisltgnd lirqreklla egidvsesgk islrhyrwng npv
//
LOCUS       WP_006232306             214 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Photobacterium profundum].
ACCESSION   WP_006232306
VERSION     WP_006232306.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium profundum
  ORGANISM  Photobacterium profundum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 214)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Photobacterium profundum"
                     /db_xref="taxon:74109"
     Protein         1..214
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=23632
     Region          49..213
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mkkaiclcil iffylpiqas asnvksssys nnnadivvqy vykktnlegv idyaifkqgf
       61 naytntkgkk kslltiidys kpstekrffv idlknhtlly ntyvshgvns ggkmaknfsn
      121 tvdsrksslg tyltsttyng gngyslkldg ltagindnar rryivihgad yatetfikrn
      181 gylgrswgcp alpkklskki idtikngsvi faha
//
LOCUS       WP_006234023              80 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyl carrier protein [Collinsella].
ACCESSION   WP_006234023
VERSION     WP_006234023.1
KEYWORDS    RefSeq.
SOURCE      Collinsella
  ORGANISM  Collinsella
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Coriobacteriales; Coriobacteriaceae.
REFERENCE   1  (residues 1 to 80)
  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 80)
  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 80)
  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   4  (residues 1 to 80)
  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 10011594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Collinsella"
                     /db_xref="taxon:102106"
     Protein         1..80
                     /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=8556
     Region          3..79
                     /region_name="acpP"
                     /note="acyl carrier protein; Provisional; PRK00982"
                     /db_xref="CDD:179197"
ORIGIN      
        1 mdrseifdki aevaadvlgv dvaeisdett fddldansle rlqlvtaied efnleiddet
       61 llslnsvada vdaieaakea
//
LOCUS       WP_006234303             392 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Collinsella aerofaciens].
ACCESSION   WP_006234303
VERSION     WP_006234303.1
KEYWORDS    RefSeq.
SOURCE      Collinsella aerofaciens
  ORGANISM  Collinsella aerofaciens
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Coriobacteriales; Coriobacteriaceae; Collinsella.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Collinsella aerofaciens"
                     /db_xref="taxon:74426"
     Protein         1..392
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42986
     Region          1..390
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mnvlvvnags sslkyqlldt dtrevfakgn cerigsdmgi fghsenggak qteevpfpdh
       61 rsaiarvlee lektdftidg ighrivqggw hfddsavvdd evmaeileva plaplhnyge
      121 aaaieycrek ypelpnvavf dtsfhmtmpe vaytyalpkd vcdkyhvrky gahgtshrye
      181 wmmakeilgs rchrllschl gngaslaaie dgvcrdttmg ltpldglmmg trcgsidpat
      241 vcylqreggy syqevddmmn kqsgllaisg isndardirt rasegdercl lafdmfayka
      301 mqqagsmias magvdtitft agigendwsi rkafcdcfew lgvridnnkn reavgngpqv
      361 isaagsavtv mviptdeeym iahdverltk nn
//
LOCUS       WP_006234304             360 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Brucella abortus].
ACCESSION   WP_006234304
VERSION     WP_006234304.1
KEYWORDS    RefSeq.
SOURCE      Brucella abortus (Brucella melitensis biovar Abortus)
  ORGANISM  Brucella abortus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 360)
  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 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   3  (residues 1 to 360)
  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   4  (residues 1 to 360)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 360)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 360)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 360)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Brucella abortus"
                     /db_xref="taxon:235"
     Protein         1..360
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36822
     Region          18..351
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(91..93,114..115,164,216,240)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 masaatigfa saayaditig viapltgpva afgdqvkkga etavevinka ggikgekvvl
       61 kfaddagepk qgvsaanqiv gdgikfvvgp vttgvavpvs dvlsengvlm vtptatgpdl
      121 targlenvfr tcgrdgqqae vmadyvlknm kdkkvavihd kgaygkglad afkaainkgg
      181 itevhydsvt pgdkdfsalv tklksagaev vyfggyhaeg gllsrqlhda gmqalvlgge
      241 glsnteywai ggtnaqgtlf tnakdatknp aakdaiqalk aknipaeaft mnayaavevi
      301 kagieragst ddsaavakal hdgkpietai gtltysetgd lsspsfdifk wddgkivgle
//
LOCUS       WP_006235441             223 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Collinsella].
ACCESSION   WP_006235441
VERSION     WP_006235441.1
KEYWORDS    RefSeq.
SOURCE      Collinsella
  ORGANISM  Collinsella
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Coriobacteriales; Coriobacteriaceae.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Collinsella"
                     /db_xref="taxon:102106"
     Protein         1..223
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24050
     Region          28..187
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mnetvpaapv saesmakqgc eklgldafda lvrrartcrr fdesmrvpre fllelaelah
       61 lapcganaqr lrfhvvsgae dcarvfdela wagalkdwpg paegerptgy iailaeravp
      121 gkpaapitdv dtgiaaqtmm laarsatpev aacmfkaftp haidamgldn dkyelklima
      181 fgvpaetqvi daidsnpdgs inywrdearv hhvpkrplad vll
//
LOCUS       WP_006236024             651 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Brucella abortus].
ACCESSION   WP_006236024
VERSION     WP_006236024.1
KEYWORDS    RefSeq.
SOURCE      Brucella abortus (Brucella melitensis biovar Abortus)
  ORGANISM  Brucella abortus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 651)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 651)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 651)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 651)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Brucella abortus"
                     /db_xref="taxon:235"
     Protein         1..651
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=70310
     Region          28..651
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msgelngndt saqaavsags vlegaafade geqhnesmkt lvlgalgvvy gdigtspiya
       61 frealhaaat ngilarsdil gvvslifwal tlvvtvkyvl fvlradnnge ggilslmalv
      121 rgalkgrpdl ilgvgicgaa lffgdavitp aisvlsameg leivapnltp fvvpaavvil
      181 vtlfsvqklg tgrvaivfgp imalwfvalg asglwhifdd ptvmaalnpy yavrfltvsp
      241 avafvtvgav flamtgaeal yadlghfgrk pivrawlwiv fpclllnyfg qaafilshge
      301 aaalpffqmi psfalwpmvl lataatvias qavitgvysv arqavqlnil prleiqhtse
      361 klhgqiyipr vnlllglavv ilvlgfekss nlaaaygiav tgnmlvttvl lyiamtriwn
      421 wrvsralpii lgflvidmlf fsaniikvhe ggwasigiat vlvlimwtwv rgtrhlfqkt
      481 rkaevpldli veqmakrppt ivpgtavflt gdpksaptal mhslkhykvl hennviltvv
      541 taskpwvasa drarvsqyne rfmlvtltfg ymqqpnipra lglcrrlgwk fdimttsffl
      601 srrslkasvh sgmplwqdkl fillartasd ateyfqiptg rvveigtqvn i
//
LOCUS       WP_006236119             254 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: aminoglycoside phosphotransferase family protein
            [Collinsella].
ACCESSION   WP_006236119
VERSION     WP_006236119.1
KEYWORDS    RefSeq.
SOURCE      Collinsella
  ORGANISM  Collinsella
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Coriobacteriales; Coriobacteriaceae.
REFERENCE   1  (residues 1 to 254)
  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   2  (residues 1 to 254)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Collinsella"
                     /db_xref="taxon:102106"
     Protein         1..254
                     /product="aminoglycoside 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=28704
     Region          38..237
                     /region_name="Bud32"
                     /note="tRNA A-37 threonylcarbamoyl transferase component
                     Bud32 [Translation, ribosomal structure and biogenesis];
                     COG3642"
                     /db_xref="CDD:442859"
     Region          114..>222
                     /region_name="CotS"
                     /note="Thiamine kinase or a related kinase [Coenzyme
                     transport and metabolism]; COG0510"
                     /db_xref="CDD:440276"
ORIGIN      
        1 mllpdsktel vrrgnkvvyd lgdkivkvfn etkpvsdvfn ealnlarine cgirspkale
       61 vsqlenangw alvtekvpgt tlaekmtaep qrfgeylemf vdlqieihgy tspllnrqrd
      121 kfarmidsld qlnattrynl qerldgmtke fkvchgdfnp snvivgddgq lyvcdwahat
      181 qgspaadvat tyllfalnsk dqaeaylely cdradmpmqv vrqwtsivaa selarkrnvn
      241 deflknwidv vdyq
//
LOCUS       WP_006237680              96 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Saccharomonospora xinjiangensis].
ACCESSION   WP_006237680
VERSION     WP_006237680.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora xinjiangensis
  ORGANISM  Saccharomonospora xinjiangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Saccharomonospora xinjiangensis"
                     /db_xref="taxon:75294"
     Protein         1..96
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10444
     Region          1..94
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(5..6,24..25,33,37..38,40,43..44,52,57,62)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(24,52..53,55,77)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mneelherir evvasvpegt vstygdvaar agastprlvg rvlaedghdl pwhrilradg
       61 tpaphlaseq larlraegva adggrvdlrr frwrtq
//
LOCUS       WP_006239058             371 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Saccharomonospora xinjiangensis].
ACCESSION   WP_006239058
VERSION     WP_006239058.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora xinjiangensis
  ORGANISM  Saccharomonospora xinjiangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (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   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Saccharomonospora xinjiangensis"
                     /db_xref="taxon:75294"
     Protein         1..371
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38017
     Region          1..346
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mtlraeltlt rgsfelsvsl svpeggvlav lgpngagkst vlsclaglvr aerahvrlgg
       61 rvldgdgvrv pahergvgll aqnallfphl svldnvafsp rsrgaskaea revarrwlde
      121 vdarefadrs paelsggqaq rvglaralag epglllldep laaldvdaap avrgvlrrvl
      181 resgrklatv lvthdpldal tladhvavla egriveqgpa revlaaprtv ftarlagvnl
      241 vpgtatrtgs gavvrtasgq sfhgvpardl adgdaavavf npgavavhph daevagsprn
      301 vvnavvtave phgpvvrlrt regisadltp asvadlalep gtpvrlavka avvavhaape
      361 pargpdpaig w
//
LOCUS       WP_006240143             761 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Brucella abortus].
ACCESSION   WP_006240143
VERSION     WP_006240143.1
KEYWORDS    RefSeq.
SOURCE      Brucella abortus (Brucella melitensis biovar Abortus)
  ORGANISM  Brucella abortus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 761)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 761)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Brucella abortus"
                     /db_xref="taxon:235"
     Protein         1..761
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=84436
     Region          3..760
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mnvasarpav arqinlqgls dtveidydlw giphiyahsm ddlffgngya haadrlwqmd
       61 aarrralgrf aawagkeals sdmlmrrldl atvsradyaa lspetqrmce ryaqgvnawi
      121 dsgqlpaeyr llgerperwe gwhcvlvmrq rgilmgslwf klwratafar igpdclhllr
      181 yedggterfv vpqeqsadrw stsleelrpa ieglmklfph datgggsnnw avdarhsktg
      241 mpivagdphq ayeipgmyaq ihltcdsfdv lglsvpgvpg fphfahneem awcvthafad
      301 ihdlyvedfs glphgayrte kgtekaqhrv eaiqvrgged vqidvwttrh gplilgspee
      361 gkgialksvq lqpidrsldc llpmltassi tefydmmepw glidhnlvsa dkkgnigvlv
      421 rakipvrdrl ngwlpmpgwt gahewrgmlp ferspreenp asgivvtann rtvpddwpdy
      481 ictdchpatr akrirsrles etpfspsdml silhddvsap aaeiaqklra itpkseparh
      541 llsmlagwqg dmapnklapt aymairqemt rilarvsdla gvadteisrl ppgvspfthl
      601 wwalpdqlrr ndtsllggms wdellleave tvaqtfdpqp wgdahrpifr hplagafpeq
      661 aavlaptsry vggdgdcvla tgslpqsgat aaygpvakyi wdladwdass wvvfhgasgd
      721 pasphyrdqn erwargeqvp acysrenvra nsarhlimqp s
//
LOCUS       WP_006240358             376 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Saccharomonospora xinjiangensis].
ACCESSION   WP_006240358
VERSION     WP_006240358.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora xinjiangensis
  ORGANISM  Saccharomonospora xinjiangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Saccharomonospora xinjiangensis"
                     /db_xref="taxon:75294"
     Protein         1..376
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=39630
     Region          1..357
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mrvltvnpgs sslklslvdg gvvtadehia ewdgvtrrel eefaaaqpsv davsvrivhg
       61 anraaptvld egvladlrgq vplaplhqpr slslarqald lpgrmpvvgc fdtafhvglp
      121 dqaatyplpr swrdrygirr ygfhglslah atraaaevlg epvrrlrlvc chlgagasvt
      181 avvggrsadt smgftpldgv amatrcgsid pgiplylqre hgftasdveh alnhdsglag
      241 lsgtggdvrd vlalrakgdp darlaldvyl hllrreiaaq avsvgkpdav vltggvaehq
      301 pelraelfgd tllgvridaa rnrgtgdrli seesstpavl vacreekela rlceevltgl
      361 agagplvfrh grkadp
//
LOCUS       WP_006240923             283 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Mycolicibacterium tusciae].
ACCESSION   WP_006240923
VERSION     WP_006240923.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium tusciae (Mycobacterium tusciae)
  ORGANISM  Mycolicibacterium tusciae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 283)
  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 283)
  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   3  (residues 1 to 283)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Mycolicibacterium tusciae"
                     /db_xref="taxon:75922"
     Protein         1..283
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31269
     Region          172..262
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mqpflgteal aagvvtryql atrydalfrn vyvpkgqavt pidraigawl wsgrrataag
       61 lsaaalhgcr widarlpael nqasrhrttg ivlhsdtlhe derclvkgvp vttaartafd
      121 lgrrpgtera viridaltqa trlkaeavda lverhrgarg lvnlrkalel sdpgaespqe
      181 trtrlvltaa glrpthtqid vfdrydhvgr idmgyltwkv gveydghqhw tdplvrsrdi
      241 erqaelealg wrivrvnadm lryrkpiiva rtraalraag aav
//
LOCUS       WP_006242980             694 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Mycolicibacterium tusciae].
ACCESSION   WP_006242980
VERSION     WP_006242980.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium tusciae (Mycobacterium tusciae)
  ORGANISM  Mycolicibacterium tusciae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Mycolicibacterium tusciae"
                     /db_xref="taxon:75922"
     Protein         1..694
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70891
     Region          29..684
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 maggtggagg qeaplpiams earrgavaam lgarsvavvg asprpdsfgs rmvieaqrgt
       61 arvhlvnpry drigdalcap sltdleddvd lvllgvpdea lleqlesava igargavlfg
      121 sahglseklt aiamnagiav cgagcmgfin nvrgvralgy lepdplpagg islithsgsa
      181 fstllrarrg fgfrlavssg qelvtntady veyalddpdt riiallmetp rdvprlrkal
      241 lraagqgvpv viltvggspr gkamvaahsg alagdraawd afcaatgaig vsdlaefadt
      301 lelfsatrrs rgggvatvhd sgaeralvad lahdlgvefa dltddtlatv galldeglaa
      361 snpldvwgtg adtrnlfgsc lramiddpgv gvtalavdlv tefdgdtaya davldvaelt
      421 eaplavlasv psaidtvtaq rlrdngvpvi egarsglaal ghlahwplpv eespspgrrr
      481 didpgasase vlaaygipvv gsrsadsldq alaaadavgy pvalktvgvl hktevggvvl
      541 gladtaalta aynamaqrlg pavtvetmvd ggveisvgfv rddafgplvv vaaggtlvel
      601 medrvvacpp lsrsgalrml drlrvaplla gwrgspavdi daladvivsv selavdhgde
      661 fdaveanpvi ttphgaiavd tvmiprhlrd qkie
//
LOCUS       WP_006243629             352 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Mycolicibacterium tusciae].
ACCESSION   WP_006243629
VERSION     WP_006243629.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium tusciae (Mycobacterium tusciae)
  ORGANISM  Mycolicibacterium tusciae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Mycolicibacterium tusciae"
                     /db_xref="taxon:75922"
     Protein         1..352
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=36073
     Region          16..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mtdvsvravv enrgvdlefa vaasevlavl gpngagksta vqviaglvrp ddgvvrvgdr
       61 vltdtaagth iathdrqvgl llqdpllfph lsvaanvafs prssradaar wleeveaadl
      121 adrmprqlsg gqaqrialar alaaepdvll ldeplagldv gaaaamrkll srvlvrggrs
      181 avlithdlvd vltladrvlv leagrtaeig stagilaapr skfgarfagv nlvagiagpd
      241 gvlttpsgvp whgvsapdtv sggstvalfs paavavyrdk phgsprntve vtiaeltshg
      301 pairiraeeq sdgapglaad itagsaaelr ltsgervyfs vkaqevtllp sp
//
LOCUS       WP_006244467             332 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Mycolicibacterium tusciae].
ACCESSION   WP_006244467
VERSION     WP_006244467.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium tusciae (Mycobacterium tusciae)
  ORGANISM  Mycolicibacterium tusciae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 332)
  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 332)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 332)
  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   4  (residues 1 to 332)
  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 332)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Mycolicibacterium tusciae"
                     /db_xref="taxon:75922"
     Protein         1..332
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36206
     Region          21..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          245..327
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mgnliratam wgypglvrel gadpavfldr fgvpsgaele edtfisfasf irileataee
       61 ltcpdfglrl sgrqglhiig pvaviarsas tvlsgieaie rflyihspal mlaaqprddg
      121 gvkfiyemte pgvpyiqgye lsmgvaariv rmlggpsarl davsfphpqq gtdaayrdal
      181 gcpvyfeppc sfelsaelaa rrndnadpqt hriateylea tylpasatla drvaelahrl
      241 lptgqctvea iagelamhpr tlqrrlgdeg trcqdiidra rrtqaaryfa epdlhfaqia
      301 gllgyaeqsa lnrscrrwfg rtprqcrega pv
//
LOCUS       WP_006245882              98 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Mycobacteriaceae].
ACCESSION   WP_006245882
VERSION     WP_006245882.1
KEYWORDS    RefSeq.
SOURCE      Mycobacteriaceae
  ORGANISM  Mycobacteriaceae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Mycobacteriaceae"
                     /db_xref="taxon:1762"
     Protein         1..98
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10680
     Region          5..96
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(27,55..56,58,80)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(27..28,35,38,40..41,43,46..47,55,60,65)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mtavtdeqve rvrtlvasip pgrvstygdi adaaslsspr ivgwimrtds sdlpwhrvir
       61 asgrpaphlt trqlallrae gvlaedgrip lrdvrhtf
//
LOCUS       WP_006246208             210 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Mycolicibacterium
            tusciae].
ACCESSION   WP_006246208
VERSION     WP_006246208.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium tusciae (Mycobacterium tusciae)
  ORGANISM  Mycolicibacterium tusciae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 210)
  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 210)
  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   3  (residues 1 to 210)
  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   4  (residues 1 to 210)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 210)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 210)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Mycolicibacterium tusciae"
                     /db_xref="taxon:75922"
     Protein         1..210
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=23070
     Region          13..205
                     /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"
ORIGIN      
        1 maaapeastg dekprrvlia edealirmdl aemlreegye ivgeagdgqe avdlaerltp
       61 dlvimdvkmp rrdgidaase iagkriapiv iltafsqrel verardagam aylvkpfnin
      121 dlipaievav srfgeiaale qevaelsdrl etrklverak gllqakqqms epeafkwiqr
      181 aamdrrttmk rvaevvvetl dtpkdaspsn
//
LOCUS       WP_006246207             405 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Mycolicibacterium tusciae].
ACCESSION   WP_006246207
VERSION     WP_006246207.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium tusciae (Mycobacterium tusciae)
  ORGANISM  Mycolicibacterium tusciae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 405)
  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 405)
  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   3  (residues 1 to 405)
  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   4  (residues 1 to 405)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 405)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 405)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 405)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Mycolicibacterium tusciae"
                     /db_xref="taxon:75922"
     Protein         1..405
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41954
     Region          80..404
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(151..153,174..175,224,275,299)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mrgsvarkaf aigsasllvl giagcqqqse pseggeaate lriveqvqid engaevpppa
       61 eetaanpagd gnaqcppvsl amagalngpd aalginikng iqlavdqhna anpgcqvqlk
      121 tfdtegdpqk atqiapqiin daftigligp afsgetnatg dvfnqaglva atasatnvtl
      181 sengwrtffr glgndgvqgp svanylkntl qqkkicvvdd stdyglglaq avretlgpva
      241 daacnisvkk gdkdfsaavt qikgaspdsv ffagyyaeaa pfvqqlkdgg fegvfvsadg
      301 tkdpqfvqqa gessqgails cpcgpatgsf aeeyskkfnq eagtysaegy dlgtillkgi
      361 dsgaitrpal lefvrnyngq gvarqyqwtp tgelttsliw iykvq
//
LOCUS       WP_006248316             413 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Mannheimia
            haemolytica].
ACCESSION   WP_006248316
VERSION     WP_006248316.1
KEYWORDS    RefSeq.
SOURCE      Mannheimia haemolytica
  ORGANISM  Mannheimia haemolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Mannheimia.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 413)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 413)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Mannheimia haemolytica"
                     /db_xref="taxon:75985"
     Protein         1..413
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48014
     Region          4..412
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mmnkriyvfa dwetfsqpel vgvlssdvvr gkenfrfsyd newlsspyvq qidpnlylyp
       61 geqystdtqn fhifldscpd rwgrllmkrr eaalasqenr kpklliesdy llgvhdmnrm
      121 galrfkteln gpfldnntrl aapplsslre lefaaiqles sdnvddpdyl kwlhmlispg
      181 sslggarpka svidelnqlw iakfpsrydd ydialweyla yrlaiqakie matcrierfn
      241 qehhtfltqr fdrhcgkrrh ftsaltqlgy ydgdyeasyl eiaqfltesg sntridlaql
      301 wrrivfniai sntddhlrnh gfiyaqegwi lspaydlnpv plsqglhlni tdsdnrldyq
      361 lafdvadffq lskqqavqiy devlkeinnw qnvakeigip rqeqeqmkfa fnv
//
LOCUS       WP_006248240             327 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Mannheimia
            haemolytica].
ACCESSION   WP_006248240
VERSION     WP_006248240.1
KEYWORDS    RefSeq.
SOURCE      Mannheimia haemolytica
  ORGANISM  Mannheimia haemolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Mannheimia.
REFERENCE   1  (residues 1 to 327)
  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 327)
  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 327)
  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 327)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Mannheimia haemolytica"
                     /db_xref="taxon:75985"
     Protein         1..327
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=37443
     Region          1..327
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mklktftkal lisslmftgs afaktiikig hynsdvhpsn ialqeyfkkt ieektegrye
       61 irifpnnqlg gedqivnglr ngtieggitg lllqnvdpif gvwewpylfk dnaeakkvle
      121 spiaqeigek mekygiklla ygmngfrvis snkkvenfdg fkglrlrvpl nslfvdwaka
      181 mhinpqsmpl sevftaleqk vidgqenpym likdsglyev qkyiiesnhi fspgllqlsl
      241 ktwnkmsked qtifleaakl yqekewelam kmeqdvkdff hkngkevivp seqfkadmlk
      301 asetlyqnfy qkydwakdvi skihaak
//
LOCUS       WP_006249473             166 aa            linear   BCT 20-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Mannheimia
            haemolytica].
ACCESSION   WP_006249473
VERSION     WP_006249473.1
KEYWORDS    RefSeq.
SOURCE      Mannheimia haemolytica
  ORGANISM  Mannheimia haemolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Mannheimia.
REFERENCE   1  (residues 1 to 166)
  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 166)
  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 11443472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Mannheimia haemolytica"
                     /db_xref="taxon:75985"
     Protein         1..166
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17306
     Region          19..165
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          123..165
                     /region_name="LysM"
                     /note="LysM domain; pfam01476"
                     /db_xref="CDD:396179"
ORIGIN      
        1 mkkslfvlsl isfalvgcss nsgestsave tteanatwqs adsiqtapmp asmnqpiatq
       61 ptyqqptysa pqpisaapap mpvssgsdss qvetvgncqv vrdannapiy sqitkgcyte
      121 shytvgksdt lyligyltgt nanqiaqlng lntgsplkvg qvlrvr
//
LOCUS       WP_006249745             274 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Mannheimia haemolytica].
ACCESSION   WP_006249745
VERSION     WP_006249745.1
KEYWORDS    RefSeq.
SOURCE      Mannheimia haemolytica
  ORGANISM  Mannheimia haemolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Mannheimia.
REFERENCE   1  (residues 1 to 274)
  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 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   3  (residues 1 to 274)
  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   4  (residues 1 to 274)
  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 274)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Mannheimia haemolytica"
                     /db_xref="taxon:75985"
     Protein         1..274
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30892
     Region          32..274
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <158..267
                     /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 mdslthlftq fqfrtdlfhl gqlcqigsfn eenkgylhfv rqgrfilnqa aerpitierp
       61 aiifsptnil hslhplddsg ldifcinfdf gkgirnplth tlhnivilel aqypelgvla
      121 dqifsevnqk gcgyqamihh lcayftlkva rqclekgyiq tgllkgladk qlgkvllaih
      181 naperdwnve elanvalmsr srfaayfkqt mgvspmdylt nwrlavaqhl lqkgipvalv
      241 aeqvgyshna alsrvfmrel glsptewlaq nkes
//
LOCUS       WP_006250514             413 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Mannheimia
            haemolytica].
ACCESSION   WP_006250514
VERSION     WP_006250514.1
KEYWORDS    RefSeq.
SOURCE      Mannheimia haemolytica
  ORGANISM  Mannheimia haemolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Mannheimia.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 413)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 413)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Mannheimia haemolytica"
                     /db_xref="taxon:75985"
     Protein         1..413
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48000
     Region          4..412
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mmnkriyvfa dwetfsqpel vgvlssdvvr gkenfrfsyd newlsspyvq qidpnlylyp
       61 geqystdtqn fhifldscpd rwgrllmkrr eaalasqenr kpklliesdy llgvhdmnrm
      121 galrfkteln gpfldnntrl aapplsslre lefaaiqles sdnvddpdyl kwlhmlispg
      181 sslggarpka svidelnqlw iakfpsrydd ydialweyla yrlaiqakie matcrierfn
      241 qehhtfltqr fdrhcgkrrh ftsaltqlgy ydgdyeasyl eiaqfltesg sntridlaql
      301 wrrivfniai sntddhlrnh gfiyaqegwi lspaydlnpv plsqglhlni tdsdnrldyq
      361 lafdvadffq lskqqavqiy devlkevnnw qnvakeigip rqeqeqmkfa fnv
//
LOCUS       WP_006250663             610 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Mannheimia haemolytica].
ACCESSION   WP_006250663
VERSION     WP_006250663.1
KEYWORDS    RefSeq.
SOURCE      Mannheimia haemolytica
  ORGANISM  Mannheimia haemolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Mannheimia.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Mannheimia haemolytica"
                     /db_xref="taxon:75985"
     Protein         1..610
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=70162
     Region          2..590
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mlnwagksta yqtlqtptsk tltpceeesv dfentqnifi egenldvlka lqksyfnsvk
       61 miyidppynt gndfiyndsf adtkadyaek vgdvdehgkl krafvrnske nghyhsnwln
      121 mmlprlhlak nllrddgvif isiddneqaq lkllcdevfg eenfvailsv ennpkgrkns
      181 kfisvsndfc iiyaknkemg kfvenipkna kdmcqdengh yvhasgkrvl vgenkfnqpv
      241 tdftsdkhys vyfnkldddi ilkfedsldd kdlnlinqgy vryisffdde fventytrfk
      301 flelfedesl eftedkiyek nfsdtirmks ilnnknykav sagnltnytl dvkttsagtl
      361 lkelfetklp vfsapknpnf lrhlitlfed knfisldffa gsssfphail esnridkgnr
      421 kfiavqypee idikskngkv akqfcqrknl plyiteiske rirragkqil qnnpenrpld
      481 vgfkvfklte shfkqwqspt senladqlem fidpvsekad tqavlyelll rlglkltakv
      541 rlenkvfwve englifalll naadeeiiqt viaqqpkkvi aldrlfngnd arkkntelqm
      601 qdagitffvi
//
LOCUS       WP_006251798             164 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Mannheimia haemolytica].
ACCESSION   WP_006251798
VERSION     WP_006251798.1
KEYWORDS    RefSeq.
SOURCE      Mannheimia haemolytica
  ORGANISM  Mannheimia haemolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Mannheimia.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Mannheimia haemolytica"
                     /db_xref="taxon:75985"
     Protein         1..164
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=18254
     Region          13..163
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mteyltsffs lffseqnqlf tmflsgflsa tllpgnseii fttlasqhli tygslssfsl
       61 fnlllvatlg nslgsittya iglllprpqn ttnrysqwal aksekygvlv llfswspivg
      121 difcgiagwl rfslwqsilf ivigkllryl fllatlysvl phil
//
LOCUS       WP_006253557             272 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Mannheimia haemolytica].
ACCESSION   WP_006253557
VERSION     WP_006253557.1
KEYWORDS    RefSeq.
SOURCE      Mannheimia haemolytica
  ORGANISM  Mannheimia haemolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Mannheimia.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Mannheimia haemolytica"
                     /db_xref="taxon:75985"
     Protein         1..272
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30291
     Region          1..272
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mkydlhahst asdgvlspte lvqraveqgv imlaltdhdt isgiqeaknf aqnqplelis
       61 gveisilwqe ksihlaalni denneelvkf ldnqaqlree raveigekla kvgianayeg
      121 akalatgevt rahygrflye qgyvrnieha fkrylgmgkp ayvkprwssl edavnvthts
      181 ggvisiahpl rykmtarwir rliadfkqag gdgievsgcg qtpdqrqlla rwakefdlyg
      241 svgsdfhypt gwielgksle lpqeckpiwt lf
//
LOCUS       WP_006253683             164 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Mannheimia haemolytica].
ACCESSION   WP_006253683
VERSION     WP_006253683.1
KEYWORDS    RefSeq.
SOURCE      Mannheimia haemolytica
  ORGANISM  Mannheimia haemolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Mannheimia.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Mannheimia haemolytica"
                     /db_xref="taxon:75985"
     Protein         1..164
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=18280
     Region          13..163
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mteyltsffs lffseqnqlf tmflsgflsa tllpgnseii fttlasqhli tygslssfsl
       61 fnlllvatlg nslgsittya iglllprpqn ttnrysqwal aksekygvlv llfswlpivg
      121 difcgiagwl rfslwqsilf ivigkllryl fllatlysvl phil
//
LOCUS       WP_006256811             335 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-oxoacyl-ACP synthase III family protein [Myroides].
ACCESSION   WP_006256811
VERSION     WP_006256811.1
KEYWORDS    RefSeq.
SOURCE      Myroides
  ORGANISM  Myroides
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 335)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Myroides"
                     /db_xref="taxon:76831"
     Protein         1..335
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36526
     Region          3..335
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mfrskisglg yyvpenvvtn ddlakimdtn hewivertgi herrhkalee dttsgmgvka
       61 ariameragv eaedidfvvf atlspdyyfp gpgvmlqrel glntvaaldi raqcsgfiya
      121 lsiadqyikt gmyknvlvvg sevhstgldm ttrgrgvsvi fgdgagaavl trseneeqgl
      181 lsthihsqge haeelallap gmggrwvtdi lkdndpddvs ytphmngqfv fknavvrfse
      241 vinegleang lqisdinmli phqanlrisq fiqqkfglsd dqvfnniqky gnttaasvpi
      301 alteaweagk ikegdlvvla afgsgftwgs viikw
//
LOCUS       WP_006257366             126 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SPOR domain-containing protein [Myroides].
ACCESSION   WP_006257366
VERSION     WP_006257366.1
KEYWORDS    RefSeq.
SOURCE      Myroides
  ORGANISM  Myroides
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Myroides"
                     /db_xref="taxon:76831"
     Protein         1..126
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14460
     Region          54..119
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mrflrnflvl ilvlftnhvi iaqsskttln epsaikelln kkkntntstt vndkykiqif
       61 ygknaearva lnnfrrlypd vnatiiytnp sykvlvgnyk trleaernlr aiqkdfelsl
      121 llrpgk
//
LOCUS       WP_006258108             272 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Myroides
            odoratimimus].
ACCESSION   WP_006258108
VERSION     WP_006258108.1
KEYWORDS    RefSeq.
SOURCE      Myroides odoratimimus
  ORGANISM  Myroides odoratimimus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Myroides.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 272)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Myroides odoratimimus"
                     /db_xref="taxon:76832"
     Protein         1..272
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=31530
     Region          <2..267
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 medvmldvlk mgtsaggarp kaiiaynkkt gkvksgqtla edgfehwlik fdeisdvqfg
       61 vsksygrvem ayykmatdfg iemtesrlie enkrvhfmtk rfdrvggnqk vhtqtlcalq
      121 hydfanitsy syeqvfqtmr llrltyaeae qmfkrmvfnv varncddhtk nfaflmdaqg
      181 kwklapaydi cfayrpdsmw vsqhnlsing krkdferkdl vtiaeqnsir npnkiidqal
      241 dlvknwnhya kmyqvdtala hqidrelike mk
//
LOCUS       WP_006259563             352 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-oxoacyl-ACP synthase III family protein [Myroides].
ACCESSION   WP_006259563
VERSION     WP_006259563.1
KEYWORDS    RefSeq.
SOURCE      Myroides
  ORGANISM  Myroides
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 352)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Myroides"
                     /db_xref="taxon:76831"
     Protein         1..352
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39311
     Region          1..351
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mnikiissgs yiptkvidnt nfdqfdfrde qgqplkdtnq rtayklqqit gieerryveh
       61 elttsdigti asehaiksag idpetldyii fahnfgdvkh gtlqsdivps lasrvkhnlk
      121 ianpscvafd vlfgcpgwlq gviqayafmk vgmakrclvi gaetlsrvid lhdrdsmiya
      181 dgagatilel tneeggilsv esasytldea ffihygksyn pdldentkyi kmfgrkiyef
      241 altnvplamk scvdksgidi nkikkvmihq anekmdeaiv krffelydme mpehimpmni
      301 qklgnssvat lptlydmiin kqldphqleq gdiilfasvg agmninafty qv
//
LOCUS       WP_006259806             111 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Myroides].
ACCESSION   WP_006259806
VERSION     WP_006259806.1
KEYWORDS    RefSeq.
SOURCE      Myroides
  ORGANISM  Myroides
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Myroides"
                     /db_xref="taxon:76831"
     Protein         1..111
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12281
     Region          2..105
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(7..8,26..27,35,38,40..41,43,46..47,49,57,62,69)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(26,57..58,60,86)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mdkqanffer vftvarqipv grvttygaia raigaarsar mvgyamnash dddtvpahrv
       61 vnrnglltgk fhfdgtnlmq qllenegvev vdnkvvnfke llweptvyeg e
//
LOCUS       WP_006259912             153 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CHAP domain-containing protein [Myroides].
ACCESSION   WP_006259912
VERSION     WP_006259912.1
KEYWORDS    RefSeq.
SOURCE      Myroides
  ORGANISM  Myroides
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Myroides"
                     /db_xref="taxon:76831"
     Protein         1..153
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16974
     Region          38..120
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 mrtqlvrqaq sqlhvqewpi knnkgpgvkk ylnsvglgeg yawcmafvyw cvqevctdyk
       61 lsnplkktgg vlaqwnaske lrvmkpevgd ifimdfgkgl ghtgiviavn gdvittiegn
      121 tndqasregy ivaekkrhiq tinkgfirvf sns
//
LOCUS       WP_006260285             261 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Myroides].
ACCESSION   WP_006260285
VERSION     WP_006260285.1
KEYWORDS    RefSeq.
SOURCE      Myroides
  ORGANISM  Myroides
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
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   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Myroides"
                     /db_xref="taxon:76831"
     Protein         1..261
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=28550
     Region          48..253
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Site            order(146..147,150..151,153,178,181..182,185..186,
                     188..189,215,218..219,222..223,226)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          146..170
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          175..206
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          214..239
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 matynkrgyk apkpeqeked nefeqynnid ssnsktaevf nsldqganrm eswvvrnqkv
       61 ifgivgaval atlgyvgydk fvvepkndda anemfqaqsy yndalmngta kdslfnlaln
      121 ggegklgflg iienyggtqs adlanyyagt aylhkgdfpk aiehlekfkg ndavlaplal
      181 gaigdafsel gqqeqaleyy qkaaakqknd fttprylnka glvalelgkk eealksfnei
      241 knnyqgsvey rgvdaligla q
//
LOCUS       WP_006261011             324 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Myroides odoratimimus].
ACCESSION   WP_006261011
VERSION     WP_006261011.1
KEYWORDS    RefSeq.
SOURCE      Myroides odoratimimus
  ORGANISM  Myroides odoratimimus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Myroides.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 324)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Myroides odoratimimus"
                     /db_xref="taxon:76832"
     Protein         1..324
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36757
     Region          3..324
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mtikqtcfyh ptsyetnecv iasfeqrnip mqriqqslgr kkrfildrns tettltmatk
       61 aakgalkecg lhiedidvia lvsatpellv psasiklhqm lnakkktmcf dlnancigaf
      121 ialdqltkyl qctpnmqral ivcaenlcri vdnnnpitaf cfsdsafafi ldkdgesigl
      181 kdvmyhtdsd iadtvsyppa gfsqfknedv lvwdrsfdgm gsvdfikkel llflernkms
      241 vedidlfmfs qfsyknvqli keyfnlgddk vpfyshelgy tgssspflal dqyqrrvrki
      301 kqgeqilfwt lgagyeaglm lwey
//
LOCUS       WP_006261999             261 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Myroides].
ACCESSION   WP_006261999
VERSION     WP_006261999.1
KEYWORDS    RefSeq.
SOURCE      Myroides
  ORGANISM  Myroides
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
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   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Myroides"
                     /db_xref="taxon:76831"
     Protein         1..261
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=28510
     Region          48..251
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Site            order(146..147,150..151,153,178,181..182,185..186,
                     188..189,215,218..219,222..223,226)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          146..170
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          175..206
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          214..239
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 matynkrgyk apkpeqeked nefeqynnid ssnsktaevf nsldqganrm eswvvrnqkv
       61 ifgivgaval atlgyvgydk fvvepkndda anemfqaqsy yndalmngta kdslfnlaln
      121 ggegklgflg iienyggtqs adlanyyagt aylhkgdfak aiehlekfkg ndavlaplal
      181 gaigdafsel gqqeqaleyy qkaaakqknd fttprylnka glvalelgnk eealksfnei
      241 knnyqgsvey rgvdaligla q
//
LOCUS       WP_006263317             427 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Myroides odoratimimus].
ACCESSION   WP_006263317
VERSION     WP_006263317.1
KEYWORDS    RefSeq.
SOURCE      Myroides odoratimimus
  ORGANISM  Myroides odoratimimus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Myroides.
REFERENCE   1  (residues 1 to 427)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Myroides odoratimimus"
                     /db_xref="taxon:76832"
     Protein         1..427
                     /product="amidohydrolase family protein"
                     /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=49250
     Region          17..408
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mhrfctflfl ttiqtltaqt pkvdyifkdv nvitmkddkv lrnhtvviqn gkiieittkt
       61 srdsdniida kgsyllpsma dahvhfpekn eeleqvmkln lingitklrs mrgewkdias
      121 rkqynnenqy ypklyltapp fhrsydltee qvesyvktak engidqikvl siknqrlfel
      181 lsetcekyni plgghfpmve dgvmadeilf qsfytsiehl ggligepdkv edrvnyikkn
      241 eifvcptmqw yaigygqygv demmnqrgmq yipekikkdw aekstnyrtk lgkegfeaek
      301 ekyalemqer fnmikrlhdh gvklllspds sskfivsgfg mleemklysk aglsnfdilr
      361 sattnfallf kenygiialg kdadfilvke npledlkale qvegvfynnf ylnkqklsei
      421 sksiipn
//
LOCUS       WP_006263965             337 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Myroides odoratimimus].
ACCESSION   WP_006263965
VERSION     WP_006263965.1
KEYWORDS    RefSeq.
SOURCE      Myroides odoratimimus
  ORGANISM  Myroides odoratimimus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Myroides.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 337)
  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 337)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Myroides odoratimimus"
                     /db_xref="taxon:76832"
     Protein         1..337
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39774
     Region          80..334
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          260..331
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mrfmfvnkia kkflseyily llllvfitfc lvfststigc mefnifpwmg siilislipi
       61 annrivlsel yrilmlgiai iiiqtffhle iwledslfnf fsiiyllfyf khiskikied
      121 kihrgyihfi nfflffdfil fnvdsllrll fnetialhik yidigidtvi lfiswitlfa
      181 liinklilkk alfryktssk kdfkveevkd qiinsqpvva ftekevviak kiadffekdl
      241 sylekdfsln rlceliiedn rstvsrvind ylgttfyelv gkyrviysle ilrskknwkl
      301 davanrcgfk svntfkkyfi asqgmtpney rmnyedg
//
LOCUS       WP_006265082             262 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Myroides odoratimimus].
ACCESSION   WP_006265082
VERSION     WP_006265082.1
KEYWORDS    RefSeq.
SOURCE      Myroides odoratimimus
  ORGANISM  Myroides odoratimimus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Myroides.
REFERENCE   1  (residues 1 to 262)
  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 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   3  (residues 1 to 262)
  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   4  (residues 1 to 262)
  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 262)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Myroides odoratimimus"
                     /db_xref="taxon:76832"
     Protein         1..262
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30376
     Region          47..261
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          183..261
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 msipinnkie eqklikiaif kkeirttkph khqgyfeliy lknttgyhci deqqyqlsth
       61 nlfiikkeqv hywnitsepf gyvilikrdf flqnidstlk qfffditqlt qidlpedtni
      121 dflfalllte ddqtaqgall kalfikirns titeqlplks giysaylhll nidhtpinkv
      181 nhyakllhtt pqnlnascqk niglsaaavl aqhiiaeakr lliytdfsin eislqlnftd
      241 ashftkyfkk httytpnnfr kl
//
LOCUS       WP_006269368             265 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Streptococcus
            constellatus].
ACCESSION   WP_006269368
VERSION     WP_006269368.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus constellatus
  ORGANISM  Streptococcus constellatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus anginosus group.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptococcus constellatus"
                     /db_xref="taxon:76860"
     Protein         1..265
                     /product="formate/nitrite transporter family protein"
                     /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=29443
     Region          9..260
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mseslfiski eyachkkeel fnrskakyai rsmfagaflt lstaagviva dlmngfasgt
       61 grfvfpfifa wglvyilfln aelttsnmmy ltagtflkki nwkkallill yctffnlaga
      121 lfigfifnqt sefthltsks flagiaehkl srpnqlvife givanifvni ailsylllkn
      181 stakilivis aiymfvfltn ehlaanfasf slvafnkiag qievfnllni lrhfsvtfla
      241 nwigggllig lsyaflnkde ttyvd
//
LOCUS       WP_006269601             710 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CHAP domain-containing protein [Bacteria].
ACCESSION   WP_006269601
VERSION     WP_006269601.1
KEYWORDS    RefSeq.
SOURCE      Bacteria (bacteria)
  ORGANISM  Bacteria
            Unclassified.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Bacteria"
                     /db_xref="taxon:2"
     Protein         1..710
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=80899
     Region          604..676
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 mgkklkkdfk erqrarieke rlqsnssiep eenklkhndd yrgkivhdkd rfqdkvhekv
       61 skrsaeteln gktskrnary rspetgsvsq eeigkadydt evkdgkiydp lgkdldndgi
      121 idrydndfrd sdyfestydv ednlqhkved tkgfsksqka qkknykrkny sdklytrkkd
      181 keakeekads kksgkeaild rekknrlske qerafknkts kvsalsglak gsetvrdyls
      241 hgsdenqgve agektadtss klihgiknys dkkkakkgyd ltnkdykirk rksklefrda
      301 keelkktqey qkannfkrfq krkqmkdsik rknksrlrdr ikegligslk sskevilrka
      361 kglmiifigl iilgtffinf agtgmtgfmn stssvlttsy lskpnvlsei nenfsemeke
      421 lqsevdnvee nypgydeyil nnteyighnv hellsyitsr cgevknasev ssvlnelfks
      481 mydleykeev eiryrtvtet ytdedgneyt esheepyeyk klivtlhkke mdsiirkvfa
      541 nypdnlkhye alflaqgnmg eafgnsdlia snggigggke yeastevqkk ivnaayitps
      601 pgagwcamwv sqvyqnaglg yiggnacdmy rnytftsdks klkvgmlvav essssgstag
      661 ltyghvgiyi gdgkvidnig rirvttlddw iasfcqhhpv gfgfppnvnr
//
LOCUS       WP_006269812             392 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptococcus constellatus].
ACCESSION   WP_006269812
VERSION     WP_006269812.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus constellatus
  ORGANISM  Streptococcus constellatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus anginosus group.
REFERENCE   1  (residues 1 to 392)
  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 392)
  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
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 392)
  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   5  (residues 1 to 392)
  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   6  (residues 1 to 392)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 392)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Streptococcus constellatus"
                     /db_xref="taxon:76860"
     Protein         1..392
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44102
     Region          14..62
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          75..386
                     /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 mnqtkkqael rtiildkiya kgpisridis ketgitpatv saitgsliqe kllyelgede
       61 ehtkvgrkki llgikkqhsy figcelseky fsfvlsdntg nvidkdkati tsekilaega
      121 dlfchlleqf ifrnnsytiq avgvaipgry lhndlittnn qtwkqfdlak iknefsfpiy
      181 fsnnvncmal akrlfsayql denfiyfhfa rgmhcsymyn gkiygksniv igeightvvc
      241 pdgevcgcgr rgclqtyase swlikkakii fetaelthlk slvtdkeeit iqtiltaynl
      301 gdqailnllh lafkylaqsl lnlsmmidak kiylhspilt ddkviaafyq eisqqpkllf
      361 kdlpeliiep yndftgatag valclqkell sv
//
LOCUS       WP_006271555             512 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Asticcacaulis biprosthecium].
ACCESSION   WP_006271555
VERSION     WP_006271555.1
KEYWORDS    RefSeq.
SOURCE      Asticcacaulis biprosthecium
  ORGANISM  Asticcacaulis biprosthecium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Asticcacaulis.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Asticcacaulis biprosthecium"
                     /db_xref="taxon:76891"
     Protein         1..512
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=53947
     Region          25..512
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mpedqatqka gcaglgarda arpgilrvhe ndhvavalgd ldagetvtvg avsvtlttdv
       61 pkghkialyd ipvgqavlkf gfvigratqa iaagehihsh nlatalsgve dytyepvpma
      121 kpavptgqfl gyrrgdgkvg irneiwilct vgcvartser larlaserfk gridgvhalt
      181 hplgcsqlgd dldhtrklia alamhpnagg vlivglgcen nqlsallkei drpadrlkyf
      241 aaqmvedete tglealeelv aiiekdqrep cdlsdlaigv kcggsdgfsg ltanplvgrv
      301 adrvafaggq aimteipeif gaerilmgra kneavfegvv svvndfkqyf ldhnqpvfen
      361 pspgnkaggi ttleekslga vqkggtspln evlrygerad ekglslleap gndavsstal
      421 taagavivlf ttgrgtplgf paptlkiasn salaqkkphw idfdagqvln dgldattdsl
      481 mdlilrtasg qpscnetnde reiaiwkngv tl
//
LOCUS       WP_006271771             411 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Asticcacaulis biprosthecium].
ACCESSION   WP_006271771
VERSION     WP_006271771.1
KEYWORDS    RefSeq.
SOURCE      Asticcacaulis biprosthecium
  ORGANISM  Asticcacaulis biprosthecium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Asticcacaulis.
REFERENCE   1  (residues 1 to 411)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Asticcacaulis biprosthecium"
                     /db_xref="taxon:76891"
     Protein         1..411
                     /product="amidohydrolase family protein"
                     /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=45170
     Region          2..407
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mvivgdrivr ieqggqggta gaeiidgkgk fllpgfidmh ahllfprchp graepqfdrg
       61 lsekalsrql efgittvrsp atptveglkl rddvnagrvr gpralasael indsaltdaq
      121 lraavrdalp nrpdyfkvya rlgpeqvatv ideahrhhip vighlqktsw aagarlgidh
      181 lahsvdwsve slppaarpay mkalearpgf rsridwleaf dpgsadqqql isllareris
      241 vdltliaydg kfspqedery rknpyltsfp elrndweqca datadwtaed yrrwtaarpk
      301 llrwvkamsd ggvllvtgtd ltnewitpge glhqefglla eagltpnqil rmtgasaaea
      361 lrrddigvve vgrradlvll sadprqsign trsimwvmqg gkivvraapr p
//
LOCUS       WP_006272012             502 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Asticcacaulis biprosthecium].
ACCESSION   WP_006272012
VERSION     WP_006272012.1
KEYWORDS    RefSeq.
SOURCE      Asticcacaulis biprosthecium
  ORGANISM  Asticcacaulis biprosthecium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Asticcacaulis.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Asticcacaulis biprosthecium"
                     /db_xref="taxon:76891"
     Protein         1..502
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50103
     Region          <12..>498
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
     Region          <17..188
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mpsrvsgksv iaaiwaggpd ndtytgsdsa dtiegrggdd lldgggghds iagedgndqi
       61 yggtgndtln ggdgddtawg gtghdmlngg fgddsltggt gndtyvvnav gdvideqsgq
      121 gadvvqasit fslagtyleh lvligianin gtgsasansl tgnnssnlld ggdgsdtltg
      181 aagwdtyvvn tasdvvieva gqgddlvqag vsytlgdyve rmtltgtgdi natgnsahnq
      241 lignsgnnvl dgatggdylt gglgndtyyl dhsgdkifel agegvdlays svsyvlvgtv
      301 venliltgta dlnatgngvg nkltgnsgnn vldglvgndt ltgglgddty yvqssgdkvv
      361 easgegydvv yasatytltg ryaeelrltg aadieasgns vgnvlvgndg dnvlnglggn
      421 dsltgglggd tflftagnrt dtvtdfsave gdminvnayt ggvdnaglvs qvglnvvidf
      481 gsgnvvtvln avqadvlshm vw
//
LOCUS       WP_006272405             292 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Asticcacaulis
            biprosthecium].
ACCESSION   WP_006272405
VERSION     WP_006272405.1
KEYWORDS    RefSeq.
SOURCE      Asticcacaulis biprosthecium
  ORGANISM  Asticcacaulis biprosthecium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Asticcacaulis.
REFERENCE   1  (residues 1 to 292)
  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 292)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Asticcacaulis biprosthecium"
                     /db_xref="taxon:76891"
     Protein         1..292
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31111
     Region          38..270
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mttsrrtala gltgialaat agtataatdv kkalkpwain ldtwfrelpf lerfapaaka
       61 gfttvefwpv nrdgvdavkv ralldqhglk vsqfapsapa fsdpakhael admikqaivd
      121 cntlgckait lvghavvpnl sreamvsgyt aglmriapll eaagvmalve pfntvnhpnh
      181 llngsrpavs icravnspmv klqwdfyhmq leegdliekf qagidqvgyv qlgdvpgrhq
      241 pgtgevnhvn llkairaagy tgvfgleymp ldqdndrafk daatlsiaag la
//
LOCUS       WP_006273598             836 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Asticcacaulis biprosthecium].
ACCESSION   WP_006273598
VERSION     WP_006273598.1
KEYWORDS    RefSeq.
SOURCE      Asticcacaulis biprosthecium
  ORGANISM  Asticcacaulis biprosthecium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Asticcacaulis.
REFERENCE   1  (residues 1 to 836)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 836)
  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   3  (residues 1 to 836)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..836
                     /organism="Asticcacaulis biprosthecium"
                     /db_xref="taxon:76891"
     Protein         1..836
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=89523
     Region          1..666
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mddliaeflt etaeslevvd aelvrfeanp serktldnif rlvhtvkgtc gflglsrlea
       61 vahagetllg rfrdgklevn adavtlvlhs idrikvilag legagiepeg ddndliaqle
      121 amaegqavdl tavqavevpv rpigseiepa elnlpttapa taapnlktgd vdpatgrtlr
      181 lgevseadle aafaaasgpe depkhlkagd ldpatgrvlr pgevseaele aafaaaeagi
      241 eipapapvae apkpapvaka apeplpasmg gedlaslnnt qsirvsvdvl eglmtlvsem
      301 vltrnqllqi srtredsafa tplqrlstlt gelqdsvmkt rmqpigaawk klprlvrdls
      361 helhkkidlv mdgegteldr qvlelirdpl thmvrnsadh gletteeria lgkpaigtik
      421 laafheggyi virisdngkg lntgkirekl vekglanrte letmsdqqvh ryifapgfst
      481 aakvtnlsgr gvgmdvvrtn ieqiggqidl nsvpgqgttf tikipltlai vsalivgagg
      541 qkfavpqtav melvrtgvta ehkierines lvlrlrekll plvqlgptlq leaaknedps
      601 fvmviqvger ryglvvndvl dteeivvkpl atvlrdvdvf sgatilgdgs vvlildpnam
      661 seragnmlee kqaeesestv dttndnrcam llfkagsgap kavelehitr lehievsqie
      721 rmdgraalqy rgklmpilnv gdystikdeg iqpllvftge gyamglavde ivdvvedrlq
      781 ielsadrpgv rgtavvagra ceivdvdyyh lrglaehqrh paplgagqss serava
//
LOCUS       WP_006275366             702 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Asticcacaulis biprosthecium].
ACCESSION   WP_006275366
VERSION     WP_006275366.1
KEYWORDS    RefSeq.
SOURCE      Asticcacaulis biprosthecium
  ORGANISM  Asticcacaulis biprosthecium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Asticcacaulis.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 702)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 702)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Asticcacaulis biprosthecium"
                     /db_xref="taxon:76891"
     Protein         1..702
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=69844
     Region          <2..692
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
     Region          139..407
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 msgltsktdk tapvlaatpd avltaavtas vteavytggt gndtytggnd ndtingaggn
       61 dslsgggghd rldggsgndt lvggagndty ytdvigdviv elegegrdlv vssrsfnmsg
      121 llvedvtllg ssdfsvtgng lsnvitgnsg ynalsggagh dtiyggsgrd titggdgnds
      181 ldgggsrdsm tggagndtyv vddssdrvve ligqghdqvy ttittslaay vedltllgtg
      241 gidgsgnaen nvvtgnsgsn rlfghggnds ldgdagddrl dggdgndtll ggagsdslqg
      301 yagtdsvsgg dgndslygyt gddtllgegg ndylygdagn dtltgdagnd tlfagggldl
      361 lmagagndrl qdnigeastl vggtgndtya iynastllte vagggldeiw sslatytlge
      421 hfenlridvn dgigignnkn nvitgnnaan rldgaagtdt laglngndty vidgndvvve
      481 ldgggtdqis asfsygladf venltltgtg nlegtgnsms nsltgnngnn llngdggsdt
      541 mtgglgndty yvqsagdvvv enagegrdmv aswvsyslfg tvvedltlig paglsatgnt
      601 lgntligndg nnvlngmasr dvltgglgad iflftagsgg dritdfnaaq ndridinayt
      661 agvantgivt qsganviial ggsnivtvld avradvlshi vw
//
LOCUS       WP_006277349             651 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Brucella suis].
ACCESSION   WP_006277349
VERSION     WP_006277349.1
KEYWORDS    RefSeq.
SOURCE      Brucella suis (Brucella melitensis biovar Suis)
  ORGANISM  Brucella suis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 651)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 651)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 651)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 651)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Brucella suis"
                     /db_xref="taxon:29461"
     Protein         1..651
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=70386
     Region          28..651
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msgelngndt saqaavsags vlegaafade geqhnesmkt lvlgalgvvy gdigtspiya
       61 frealhaaat ngilarsdil gvvslifwal tlvvtvkyvl fvlradnnge ggilslmalv
      121 rgalkgrpdl ilgvgicgaa lffgdavitp aisvlsameg leivapnltp fvvpatvvil
      181 vtlfsvqklg tgrvaivfgp imalwfvalg asglwhifdd ptvmaalnpy yavrfltvsp
      241 avafvtvgav flamtgaeal yadlghfgrk pivrawlwiv fpclllnyfg qaafilshge
      301 aaalpffqmi psfalwpmvl lataatvias qavitgaysv arqavqlnil prleiqhtse
      361 klhgqiyipr vnlllglavv ilvlgfekss nlaaaygiav tgnmlvttvl lyivmtriwn
      421 wrvsralpii lgflvidmlf fsaniikvhe ggwasigiat vlvlimwtwv rgtrhlfqkt
      481 rkaevpldli veqmakrppt ivpgtavflt gdpksaptal mhslkhykvl hennviltvv
      541 taskpwvasa drarvsqyne rfmlvtltfg ymqqpnilra lglcrrlgwk fdimttsffl
      601 srrslkasvh sgmplwqdkl fillartasd ateyfqiptg wvveigtqvn i
//
LOCUS       WP_006278191             136 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Cylindrospermopsis
            raciborskii].
ACCESSION   WP_006278191
VERSION     WP_006278191.1
KEYWORDS    RefSeq.
SOURCE      Cylindrospermopsis raciborskii
  ORGANISM  Cylindrospermopsis raciborskii
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Aphanizomenonaceae; Cylindrospermopsis.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Cylindrospermopsis raciborskii"
                     /db_xref="taxon:77022"
     Protein         1..136
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15766
     Region          50..133
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 meakmgelki rediyimfdy tkakqfyldk qrslqherhl lwqkakldse rivamiiqdy
       61 apkqiiqwgs vlapehfssv sdidlavlgi eplvflrlfa daeamtnfsl dlirwedihp
      121 afqqilllkg kviyas
//
LOCUS       WP_006278836             338 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Cylindrospermopsis].
ACCESSION   WP_006278836
VERSION     WP_006278836.1
KEYWORDS    RefSeq.
SOURCE      Cylindrospermopsis
  ORGANISM  Cylindrospermopsis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Aphanizomenonaceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Cylindrospermopsis"
                     /db_xref="taxon:77021"
     Protein         1..338
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37415
     Region          1..333
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mgivvenvsk yfgsfhaved vsleiasgsl vallgpsgsg kstllrliag letpdqgkif
       61 ltgkdatyqs vqernigfvf qhyalfkhlt vrqniafgle irklakkkiq grveqlldlv
      121 qlsglgeryp sqlsggqrqr valaralave pkvllldepf galdakvrkd lrawlrrlhe
      181 evsvttvfvt hdqeeameva nkiviinqgr leqmgtpaei ydhpasafvm sfigpvnvlp
      241 ssaqifqgsg fdspnpevfl rpqdviieka gngtnttaiv hriihlgwev qveltlddgq
      301 tftaylsrer fdelslepke rvyvkpkdak sfplyysi
//
LOCUS       WP_006280027             191 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Wolbachia].
ACCESSION   WP_006280027
VERSION     WP_006280027.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia
  ORGANISM  Wolbachia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Wolbachia"
                     /db_xref="taxon:953"
     Protein         1..191
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20999
     Region          4..188
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mnsrivigis gasgsiygvr ilealkdvdy ethlvisrag kitlaheike kleditslad
       61 fyyseekige kiasgsfkts gmivapcsmk tmseiasgvt snlltraadv tlkerrklvl
      121 mvresplhlg hlqnmlklte mgaiiappvp afyikpksld diinhsvgkv ldlfdiklpd
      181 fkewqgsdny y
//
LOCUS       WP_006241555             646 aa            linear   BCT 20-JAN-2025
DEFINITION  type I restriction-modification system subunit M [Mycolicibacterium
            tusciae].
ACCESSION   WP_006241555
VERSION     WP_006241555.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium tusciae (Mycobacterium tusciae)
  ORGANISM  Mycolicibacterium tusciae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 646)
  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   2  (residues 1 to 646)
  AUTHORS   Youell,J. and Firman,K.
  TITLE     Mechanistic insight into Type I restriction endonucleases
  JOURNAL   Front Biosci (Landmark Ed) 17 (6), 2122-2139 (2012)
   PUBMED   22652768
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 646)
  AUTHORS   Sistla,S. and Rao,D.N.
  TITLE     S-Adenosyl-L-methionine-dependent restriction enzymes
  JOURNAL   Crit Rev Biochem Mol Biol 39 (1), 1-19 (2004)
   PUBMED   15121719
REFERENCE   4  (residues 1 to 646)
  AUTHORS   Murray,N.E.
  TITLE     Type I restriction systems: sophisticated molecular machines (a
            legacy of Bertani and Weigle)
  JOURNAL   Microbiol Mol Biol Rev 64 (2), 412-434 (2000)
   PUBMED   10839821
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114514
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Mycolicibacterium tusciae"
                     /db_xref="taxon:75922"
     Protein         1..646
                     /product="type I restriction-modification system subunit
                     M"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=71175
     Region          11..144
                     /region_name="HsdM_N"
                     /note="HsdM N-terminal domain; pfam12161"
                     /db_xref="CDD:463478"
     Region          158..419
                     /region_name="HsdM"
                     /note="Type I restriction-modification system, DNA
                     methylase subunit [Defense mechanisms]; COG0286"
                     /db_xref="CDD:440055"
ORIGIN      
        1 madaanngtt arivwdtadk ylrhivdeed ygdyilpftv lrrlecmlgd tkqevtafva
       61 slagmpphli diavkdkfgl sfynvspldl atiasvddnv hkslqsyidg fsnniadiwt
      121 sfefnrrakv ladanrlhsv vkhfskldls pkelantamg dvfedvmyra fnkkgkaagn
      181 fytprdaikl mvdilitndd dglagesalr siydptagsg gmllvaqdal krmngkidvt
      241 lygqelmpsa falgkadlli qggrpdaikq gntliedlya dqtfdyvlsn ppfgndwead
      301 ekavkeqakv hgsrfshglp gtsdgqmlfl ahcasklspa akngqggraa vvsnqsplfn
      361 sdngpnsirq wlleedlida iiglptsmfy gtgiatyvwi ldtnkdpdrk gkiqlidgsg
      421 qwdsmrkpmg dkrremgknh rktlmeayka fdqadpaisr vmtpedfrfr dvpvykqarf
      481 gtcysdavve slrsrrdfte dhvgilrsld gtpwndlpka lpeaakvagv kasvglvdaa
      541 mkamavqdds appavdrkgq pvvagdwklt ervplsedlt ehmehevmpy apdamwdesk
      601 akhgtdipft rifyvpeepr plaaidadvq klmselaemf ttvsne
//
LOCUS       WP_006280878             280 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Brucella suis].
ACCESSION   WP_006280878
VERSION     WP_006280878.1
KEYWORDS    RefSeq.
SOURCE      Brucella suis (Brucella melitensis biovar Suis)
  ORGANISM  Brucella suis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Brucella suis"
                     /db_xref="taxon:29461"
     Protein         1..280
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=29079
     Region          47..131
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
     Region          175..241
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mkrllattml aamvalpafa qggtpiftge kqhqpvtskn gyfvaspgql ltsdfigqpv
       61 yngpsddadn igtvndiilg adgtpqaivi gvggflgvge kdvavgcnhf swvdksggtr
      121 wlmvdadkeq lekapvfdrn aaftangasr aaektvttkk tsrvipegmk pianeglsae
      181 kligamvyda detkigtigd vlmsadgqte afvvdvggfl ginskpvais ianldvatgk
      241 dgklsvftqf tkkdlqaqpa fseaaykedp egailhgaae
//
LOCUS       WP_006282510             303 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Segatella].
ACCESSION   WP_006282510
VERSION     WP_006282510.1
KEYWORDS    RefSeq.
SOURCE      Segatella
  ORGANISM  Segatella
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 303)
  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 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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Segatella"
                     /db_xref="taxon:2974251"
     Protein         1..303
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34806
     Region          95..303
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          222..296
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mptkmdlyin eandyardig apvwhphvsv ihydelgair htlnrynvyg lflqsefpen
       61 ltygigryhd aggsllalsp gqiggkhddg trrqyngwvl lfdthfiqgs eierrladyh
      121 ffsynaneal flteqeknvl sglmanvree lkahgnddvh ddiirdyill ildycrrfyi
      181 rqfkemtteg gdilsrfqqv linyydtgrq lkdglpsvry casqlclsag yfgdivreal
      241 gespkdyihg fivmkaknll lsgmqvtqvs eqlgfeypth ftrlfkqmtg qtpsqfyaeq
      301 rkk
//
LOCUS       WP_006284438             299 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Paenibacillus
            popilliae].
ACCESSION   WP_006284438
VERSION     WP_006284438.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus popilliae
  ORGANISM  Paenibacillus popilliae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Paenibacillus popilliae"
                     /db_xref="taxon:78057"
     Protein         1..299
                     /product="formate/nitrite transporter family protein"
                     /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=31124
     Region          4..258
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 magylkpqei aavtvetgtt karnplsvmv ilgflagafi algyllyirv tagappewgt
       61 itgligaslf piglilvllg ggelltgnmm avplarmkgr ittgevvrnl ivitvsnflg
      121 aifvayffgh ivgltadgvy lektvsvagh kleegflqaf vsgigcnwlv alavwlaygs
      181 ksfsgkilgi wfptmtfvai gfqhvvanmf vipaaifegy ygwgeyimnf ipvwlgnltg
      241 gavfvagayc laylrpnpda afpaqtsgtr asasavsaap aapdtpasss ssldhsvtg
//
LOCUS       WP_006285596             620 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Paenibacillus popilliae].
ACCESSION   WP_006285596
VERSION     WP_006285596.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus popilliae
  ORGANISM  Paenibacillus popilliae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 620)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..620
                     /organism="Paenibacillus popilliae"
                     /db_xref="taxon:78057"
     Protein         1..620
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=70917
     Region          63..528
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mnqltmksad ltqvnidkia elfpnviaea rdeqgkinra idfdllrqel snflvegeke
       61 ryqltwpgkk eailqanspi ektlrpvked svewektknm yiegdnlevl kllqeaylck
      121 ikyifidppy ntgrdfvykd dfsesvegyl eesgqvdang nrlfqntesn grfhsdwltm
      181 mysrvkiarn llredgvifi siddnevdnl skicdevfgr qnflgkiiwk kktngnnmgv
      241 ippvhdyicv yakninllgd igfpadieki qkdysnpdnd prgpwttmdl sanhkgpyfk
      301 iinplngdef wpsegrywvf nenevlkria dgriifgksg narpvqkifl kdkqfkkika
      361 esiwdnhgmn edatkelwdi lgepklfthp kpskllyhli klstdfdknd ivldffsgsa
      421 ssahavikln sedlgnrkyi mvqipeqtee sseaykagyk niceigkeri rrtakkikee
      481 tgadidygfr vyridssnmk dvyytpdklg qmnlddvasn ikedrtgedl liqvmlecgl
      541 elslpietke iegktvhyva gnsliacfdd evsesvikki avdqplrvvf rdssfsddsa
      601 rinveelfkl lsssteiqvl
//
LOCUS       WP_006288719             246 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Parascardovia denticolens].
ACCESSION   WP_006288719
VERSION     WP_006288719.1
KEYWORDS    RefSeq.
SOURCE      Parascardovia denticolens
  ORGANISM  Parascardovia denticolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Parascardovia.
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
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Parascardovia denticolens"
                     /db_xref="taxon:78258"
     Protein         1..246
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=27494
     Region          1..>236
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 miefknvskt fgdqtvitee sftinseeff vlvgpsgggk tttlkminrl vepssgrill
       61 dgrdissmpl rqlrltigyv lqqialfpnm tvgqnielip emkgwskdkr tqrakelltt
      121 vgldadsyyk rypqelsgge qqrvgilral vanpelilmd epfsaldpit raqlqdltld
      181 lhdklkttvv fvthdideac ymgdricvis dgevtqigsp keikghpanq fvadlfshnh
      241 krkdrd
//
LOCUS       WP_006289087             408 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Parascardovia denticolens].
ACCESSION   WP_006289087
VERSION     WP_006289087.1
KEYWORDS    RefSeq.
SOURCE      Parascardovia denticolens
  ORGANISM  Parascardovia denticolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Parascardovia.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Parascardovia denticolens"
                     /db_xref="taxon:78258"
     Protein         1..408
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43851
     Region          3..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 maktvlvins gsssikyqlv nlesgealas glvekigept dgaythkfdg ekhtftepik
       61 dheqglkkvl affdeygpnl kdyelvavgh rvvqggyifp tpalvtpqti qqvkdlavla
      121 plhngpeaig aevmtrllpd vpqgfvfdss fffqlpkass tyalnkevae kyhirrygah
      181 gtsheyvgsv vpevigkpae glkqivlhig ngasasaqis gkpvetsmgl tpleglvmgg
      241 rtgdidpavv fhlirnahmd vdqldtlfnk qsgmmgltgh gdmrdvdalr aqgdedaela
      301 fqiyvhrivs yignytaqmg gcdvitftag vgendaavre aicdklapfg vkldkekndt
      361 rsseprvisa pdssvviavv ptneelaiar kvaklaeegd aygnkfer
//
LOCUS       WP_006289521             336 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Parascardovia denticolens].
ACCESSION   WP_006289521
VERSION     WP_006289521.1
KEYWORDS    RefSeq.
SOURCE      Parascardovia denticolens
  ORGANISM  Parascardovia denticolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Parascardovia.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 336)
  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   6  (residues 1 to 336)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Parascardovia denticolens"
                     /db_xref="taxon:78258"
     Protein         1..336
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37855
     Region          3..182
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <128..309
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mfginvgeal reagapedlf srhrptleea ayyrfmdavg sqakdpqlpi riasadgves
       61 fspplfaayc senaktccer lseykriiap mryrtister tvevemaasg vglslpqflv
      121 esemvfllhi iraatrtvih piqihmtdpp ttgdlsryar cpirksgrnr iifqrtdmdk
      181 pfisynegmw dylapelqrr lyemkegdpa amkvrsaltg llpsgrttik dvastlgisp
      241 rtlerrlake nttfqqqlns trellakhyi rntdmssgdi afllgyqepn sflraftqwt
      301 glsvseyknt tttqqpknkt pttlsilknp ieerse
//
LOCUS       WP_006289827             210 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Parascardovia
            denticolens].
ACCESSION   WP_006289827
VERSION     WP_006289827.1
KEYWORDS    RefSeq.
SOURCE      Parascardovia denticolens
  ORGANISM  Parascardovia denticolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Parascardovia.
REFERENCE   1  (residues 1 to 210)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Parascardovia denticolens"
                     /db_xref="taxon:78258"
     Protein         1..210
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=21652
     Region          126..209
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 masdnrdkas iedeftqaag tpggahrgrk slgvrlrpyl ivlviaicla lllwawlsga
       61 iggartpsta ksattsvtqs akkstdsqat qtketpgska spstaksssp ssdqssssst
      121 avrkdtqiiv ynggftagla gknrdiltqa gftnvsannp ndrstlpera tvwyrgeenk
      181 ataeevaktl gisnveeatg iaapvvavvk
//
LOCUS       WP_006290810             245 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Parascardovia denticolens].
ACCESSION   WP_006290810
VERSION     WP_006290810.1
KEYWORDS    RefSeq.
SOURCE      Parascardovia denticolens
  ORGANISM  Parascardovia denticolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Parascardovia.
REFERENCE   1  (residues 1 to 245)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Parascardovia denticolens"
                     /db_xref="taxon:78258"
     Protein         1..245
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=26833
     Region          123..245
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(191..192,195,218..221,223)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mdqvhqtvsr irrngyeavi agalvavcli mgliiglrtt hgdntpqmrq aqtmgqeatt
       61 plkpkssvre psrkqsqpsq ptrpsqraqs ktggnkgqtl aidwrkptgg kqpnlaayrn
      121 lsvevdlakq rvyvlsgkkt iytavvstgm ngstprghfv agdhsdtprg asffntrekm
      181 gaknwiriqg dilfhsvptd ekesyitsea rklgrpashg cvrmsvadsk wffdqlpdgt
      241 pvriy
//
LOCUS       WP_006291194             560 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Parascardovia denticolens].
ACCESSION   WP_006291194
VERSION     WP_006291194.1
KEYWORDS    RefSeq.
SOURCE      Parascardovia denticolens
  ORGANISM  Parascardovia denticolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Parascardovia.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 560)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Parascardovia denticolens"
                     /db_xref="taxon:78258"
     Protein         1..560
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59321
     Region          303..422
                     /region_name="COG3942"
                     /note="Surface antigen [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443142"
ORIGIN      
        1 mpaheqehea sdslriqvst arvaakttvk tvkaaasvae apvavakktv kivsfaanap
       61 srvrafaksd gktkgrillg lgkkagkrvg rtalgvsqgv irgsakvada ginrffdlqt
      121 adgdettqva veeasrgltl akgsvkaagk tlahskrsir aasrsfkaar ksfkaakqsl
      181 daaraamhsa asamqalkai gsiiaavvtm vvntvtsvia vlapviaiiv avtmvisfiv
      241 nfltitsqqa saacvgdssy tinsagfnak sgaltgliyh ssggtkvvdf mkmgipasky
      301 dndpwsyayq qctwwaayrr kmlgqpvdkq mgngnqwass aktkgyktgt sprlgavisy
      361 psgvlgaspv yghvsvveqi dpngdiwvsq agtgffstyg gpvvskiskr qleenktltf
      421 iydstgsgng lavqgtqtdl nsddcnvpap pagnvgkevt aaknyakgrl saygwkesef
      481 naldqlwthe sgwkwdadnp tsdaygipqa lpgnkmsskg adwktnpktq iewglqyikd
      541 ryktpsaawr qwqsrspnwy
//
LOCUS       WP_006291931             357 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Parascardovia denticolens].
ACCESSION   WP_006291931
VERSION     WP_006291931.1
KEYWORDS    RefSeq.
SOURCE      Parascardovia denticolens
  ORGANISM  Parascardovia denticolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Parascardovia.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Parascardovia denticolens"
                     /db_xref="taxon:78258"
     Protein         1..357
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37432
     Region          241..356
                     /region_name="COG3942"
                     /note="Surface antigen [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443142"
ORIGIN      
        1 mshgahvsps srhtmrsqag rkasgagkhv dlatggssls vtshrpkpgr hlapavpidt
       61 tpahapsfav rhdldlalle klnsapvtrk dlrlmeqksa rrgqfmvasa atmlmgtigt
      121 vyasaanqtl aahgssssqv vesqslgsss vsrhedrqsq psatetasvt edssarwnld
      181 tnssnvdtak lsvstqkakv esvvkpstsa lvasqadsts kpttlfsyta paaetmkvnh
      241 atgdsgnaye fsqctwwayl rrhqlglpvg shfgnggqwa asargmgyav dnkpqvgdvm
      301 vfapgqegsd psyghvaive svnpdgtvti secgavwqgv ihirtisnps nfqfihs
//
LOCUS       WP_006292166             305 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Parascardovia denticolens].
ACCESSION   WP_006292166
VERSION     WP_006292166.1
KEYWORDS    RefSeq.
SOURCE      Parascardovia denticolens
  ORGANISM  Parascardovia denticolens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Parascardovia.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Parascardovia denticolens"
                     /db_xref="taxon:78258"
     Protein         1..305
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=32952
     Region          157..285
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 msdrrghagv gvgkyigytl aavltiavvv asggwktfsd algfgrgvsd vsalkardrs
       61 rpfdlsrqaq egrqalsgvk vpsppqgkps vsvphslpqq lsrslpqaay spvsyaqalq
      121 wakampvaap hpagydrery fgtwqksprl cgtgtsrdyi lkrdlaspvm dsrcrvvsgv
      181 lddpytgtvi dfrrgvntsg lvqidhvval qdawasgass wtqdrrvsya ndpdvllasq
      241 gaanmakgng vdwkaaadpv wlpsyrpyrc dymakrvsik hkyglsmskp ereqtvrlle
      301 acpak
//
LOCUS       WP_006293000             493 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Scardovia inopinata].
ACCESSION   WP_006293000
VERSION     WP_006293000.1
KEYWORDS    RefSeq.
SOURCE      Scardovia inopinata
  ORGANISM  Scardovia inopinata
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Scardovia.
REFERENCE   1  (residues 1 to 493)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Scardovia inopinata"
                     /db_xref="taxon:78259"
     Protein         1..493
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=53211
     Region          93..198
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          368..483
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(436..437,440,456..459,461)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 migsqhgknk skarkkgkar lvvffvvlal iltvgggtfa ayrffqdrva pgvslgqtsl
       61 tgktqaevek lvsqlkekti isitgtdgkk hlvslddlgv rvkinktaqt avdakrdksd
      121 ferfspaalq kltlsattde tvmqnyldkt fvgnstgaqe pqviysqsqa kfivrpgksg
      181 ksvvldsvrs avskalsqpg htqkakaqvr lmqpaisdsq avaaaaaana rlstiikisn
      241 gstksytips sliaswmtfs sdkqtktmtl sydydavyss lktvlpqnln qtlvnqqqti
      301 dhknrlvavq vkgingitvt dtsqpasqvv aalkagrnav itapvqtkay stkstvvyry
      361 dipdgdpwal vnlseqkaya ysgttlkktf nvstgkpstp thpgtytvyi klntqtmrgk
      421 dyvtpnvkwi syfhggegfh aapwnqsgia qgrpmshgcv nmnpqdakwl ydflpmkamv
      481 kitgstptka vrg
//
LOCUS       WP_006296074             371 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Hylemonella gracilis].
ACCESSION   WP_006296074
VERSION     WP_006296074.1
KEYWORDS    RefSeq.
SOURCE      Hylemonella gracilis
  ORGANISM  Hylemonella gracilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Hylemonella.
REFERENCE   1  (residues 1 to 371)
  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 371)
  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 371)
  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 371)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Hylemonella gracilis"
                     /db_xref="taxon:80880"
     Protein         1..371
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40869
     Region          8..363
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mtqskttrrr sllkgaavaa gamsvpmisn aqttslrlqs twpaqdifhe yaqdfakkvn
       61 dmaggrlkie vlpagsvvpa fqlleavnkg tldaghgvva yhygkqsala lwgsgpafgm
      121 dpnmvlawhn ygggkallde iyksinmdvv sylygpmptq pfgwfkkpia kvedvkgmkf
      181 rtvglavdiy tamgaavnpl pggeivaald rglidgaefn nassdrvlgf pdvakncmlq
      241 sfhqsgeqfe ilfnksklet lppelraivd yavqaasadm swkaidrnsk dyqelkkqgv
      301 kfyktpdail raqldawdki mekksaenpl fkkvldsqra faqrtkqwqn dymvdfnmay
      361 nryfgrgakk a
//
LOCUS       WP_006296082             372 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Hylemonella
            gracilis].
ACCESSION   WP_006296082
VERSION     WP_006296082.1
KEYWORDS    RefSeq.
SOURCE      Hylemonella gracilis
  ORGANISM  Hylemonella gracilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Hylemonella.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Hylemonella gracilis"
                     /db_xref="taxon:80880"
     Protein         1..372
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=41221
     Region          1..361
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msieirkvnk hfgdfralhd vdldiasgel lallgpsgcg kttllriiag letadsgsif
       61 fsgedttdkh vrdrhigfvf qhyalfrhmt vadnvafglr mkpraerpse kqikakvmdl
      121 lklvqldwla drypsqlsgg qrqrialara lavepkvlll depfgaldak vrkelrrwlr
      181 rlhdelhvts ifvthdqeea levadrvvlm nrgvveqvgs pqdvwehpas pfvygflgdv
      241 nlfhgraheg tlhldgissd itiaapehvd ardaqafayv rphefdvrrw ssgapgiaar
      301 lsraivvgpi arlellpees tpslrqavie vqipasqyre lgltegella vtprkarvfv
      361 egkpdlaast tt
//
LOCUS       WP_006297129             421 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Hylemonella gracilis].
ACCESSION   WP_006297129
VERSION     WP_006297129.1
KEYWORDS    RefSeq.
SOURCE      Hylemonella gracilis
  ORGANISM  Hylemonella gracilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Hylemonella.
REFERENCE   1  (residues 1 to 421)
  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 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   3  (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   4  (residues 1 to 421)
  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 421)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Hylemonella gracilis"
                     /db_xref="taxon:80880"
     Protein         1..421
                     /product="CmpA/NrtA family 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=45621
     Region          46..296
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mqdpkianvg gnhgslsrrt llqaaaagaa gispalravv haagsdapek kevkigfipl
       61 tdcasvvmas vlgidqkygv kiipskeasw psvrdklvng eldfahvlyg lvygvhlgig
      121 gpkkdmavlm nlnhngqait lskqladkga vdaaslatlm tkekreytfa qtfptgtham
      181 wiyywlasag inpftdakvi tvpppqmvan mrvgnmdgfc vgepwnhrai ldgigvtaat
      241 tqeiwkdhpe kvlgttgdfv kqypntarav taaileagrw idasaanrqk maetvadksy
      301 vntgvdaiqd riqgryqngm gktwddpnhm kfyndgavny pylsdgmwfl tqhkrwgllk
      361 dhpdylavak qinqteiykq aaaaakapvp ksdlrsskli dgvvwdgkdp kkyadsfkvk
      421 v
//
LOCUS       WP_006297510             420 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Hylemonella
            gracilis].
ACCESSION   WP_006297510
VERSION     WP_006297510.1
KEYWORDS    RefSeq.
SOURCE      Hylemonella gracilis
  ORGANISM  Hylemonella gracilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Hylemonella.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 420)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 420)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Hylemonella gracilis"
                     /db_xref="taxon:80880"
     Protein         1..420
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=45428
     Region          9..405
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mspvpytprd elflwwladp aqprlvgrlr lvrrtaghpg gvsleydpaw laeglalsed
       61 lplrpgeflp vendaaagav ddarpdrwge rvirhlykpt rlstleylyf agderfgalg
      121 vsssaqryep qpravlpvvg dvpalyelvr rieagepvdd alqrlvapgt tlggarpkaq
      181 ieidghpwvl kfadagdpnd spliehaamt latragitvc etrpiplvdg havavrrfdr
      241 agaghggrrl halsahvalr aaasdggype lalllrrrgd ptqiaangaq vfrrmvfnvl
      301 idntddhekn hallvqgrsy alapaydvlp agqalgyqqf rvgaqgldas aenllsepaa
      361 fglrrpqaqa larevaevve gwqthfaacg vsagdlgrla eqidrpyllg errallresa
//
LOCUS       WP_006298112             169 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Hylemonella gracilis].
ACCESSION   WP_006298112
VERSION     WP_006298112.1
KEYWORDS    RefSeq.
SOURCE      Hylemonella gracilis
  ORGANISM  Hylemonella gracilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Hylemonella.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 169)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Hylemonella gracilis"
                     /db_xref="taxon:80880"
     Protein         1..169
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17988
     Region          13..167
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 msftvadqld mstpaakraa yellsaqlqs llegerdria nlaqfsally qvlpdlnwag
       61 fylaqgetlv lgpfqgkvac vripfgrgvc gtcaatgqvq ivpdveafpg hiacdsasrs
      121 elvlplrsgs qflgvldlds pelarfdeid aqgltrmvat lvagtdwar
//
LOCUS       WP_006298311             209 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Hylemonella gracilis].
ACCESSION   WP_006298311
VERSION     WP_006298311.1
KEYWORDS    RefSeq.
SOURCE      Hylemonella gracilis
  ORGANISM  Hylemonella gracilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Hylemonella.
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   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   3  (residues 1 to 209)
  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   4  (residues 1 to 209)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 209)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 209)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Hylemonella gracilis"
                     /db_xref="taxon:80880"
     Protein         1..209
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=23111
     Region          13..193
                     /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"
ORIGIN      
        1 mssslrrlye dlrsisvtvv yppgedrdvv vqqlqrigcr lkvvwpfpae ppagvdvilf
       61 qvsqdlegrs awnasavdaa fvalsdyesp ttlkllldtr ahgvitkpfr ssgilstlvl
      121 arasqgfqqr qqgkiekles tiksrrqiek airvlvdyqr mtetqayehm reratglrvt
      181 vaevaamlle aheameklgf atakpasgk
//
LOCUS       WP_006298850             714 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Hylemonella gracilis].
ACCESSION   WP_006298850
VERSION     WP_006298850.1
KEYWORDS    RefSeq.
SOURCE      Hylemonella gracilis
  ORGANISM  Hylemonella gracilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Hylemonella.
REFERENCE   1  (residues 1 to 714)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 714)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..714
                     /organism="Hylemonella gracilis"
                     /db_xref="taxon:80880"
     Protein         1..714
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=77946
     Region          50..657
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mgrdtragka glsdseaska rgaakvsrga lggrwvslll allavtavvw lyyaqndfle
       61 gfearsydlr fkslrgplpv qsditiiaid dksiaalgry pwtrqqyvrl ldkleaskpr
      121 vvlfdvffpe penpavdaal aqalaragnv vlastfsfdt qgrvtgrmgs lpaleaaaag
      181 rahinlrped dgvnrrndlr iayldgasgq trlmpslgls aalfmlgads fgaepfrvwi
      241 argqellrsv pvnadgalwi nylgsagayp rvsfvdvleg radpallrdk avflgatalg
      301 vydmrvtpfh pntpgvevha avadnilsqr yvhrtgmqal fdllmivlig flsffitarm
      361 rlqramavvl glvvcylgla ywmflqgqwv smvyppvaal lalmlgggwr fmvlersarq
      421 mramfssyvs sklvsqleqn pdaariggds revtvlftdi kgfttfsern paevvvdrln
      481 eylsamvqii hahdgtvdkf mgdgimaywg aplpqadhar lalrcalgmk akmaeltdaw
      541 rargvepfqi rggilsgrvv agnigssgqk meytvigdtv nqasrlegag ktygidftvg
      601 estkrlvdad gefgfrrldc vrvvgktepv elfelrpaap sadqggadpl vdrfeaalgh
      661 yrarrwegav nsfrklvadf pqdgpsalyl qrciefqarp psadwdgvfn rqek
//
LOCUS       WP_006298970             718 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Hylemonella gracilis].
ACCESSION   WP_006298970
VERSION     WP_006298970.1
KEYWORDS    RefSeq.
SOURCE      Hylemonella gracilis
  ORGANISM  Hylemonella gracilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Hylemonella.
REFERENCE   1  (residues 1 to 718)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 718)
  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   3  (residues 1 to 718)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..718
                     /organism="Hylemonella gracilis"
                     /db_xref="taxon:80880"
     Protein         1..718
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76602
     Region          15..718
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 maegyqesgg gdgldltqfy qiffeeagen ldqmeqmlln lnletaddea lngifrcahs
       61 vkggaatfgf sdvaelthqm eslldklrrh elqpnplmvd vllesadasr lllarhqtgd
      121 tsdppstagl vqriselaag gvpmmadpvv evapvappap vpvappaapa vapaasapkv
      181 pqsrllevrl gplerteqad gvkdlfrdiv glgriaevas dkpeirvfkv rtssaneell
      241 dlfvfhvsre qvqiqqlpee egivgwldle dppadapvap apgygffena pggfnstptp
      301 apapkaatpa paatrpaggg saaasahavq peaatirvai skvdqlinlv gelvitqaml
      361 aqnsqsldpa vnqqllagla dldrntrdlq esvmsirmip msivfsrfpr mlrdlasklg
      421 kkvdfvtqge ateldkglve kitdplthlv rnscdhgiel pedrvtagkp etgtitlsaa
      481 hqggsiviev rddgrglsre kilqkarerg levsdsmsdp dvwqlifapg fstaevvtdv
      541 sgrgvgmdvv kkniaalngt veidsvfgqg mkvsvrlplt laimdgmsvg vgeevyilpl
      601 ssvvesfqvk edavntiaqg srlvkvrdey mpvielekvf qvprhgsdka sdimvvveae
      661 gsrvallvde llgqqqvvvk nletnyrkvp nvsgatilgd gqvalildts alvrrsrh
//
LOCUS       WP_006299431             990 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Hylemonella gracilis].
ACCESSION   WP_006299431
VERSION     WP_006299431.1
KEYWORDS    RefSeq.
SOURCE      Hylemonella gracilis
  ORGANISM  Hylemonella gracilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Hylemonella.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Hylemonella gracilis"
                     /db_xref="taxon:80880"
     Protein         1..990
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=111496
     Region          134..>537
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 matrkpkapl qvetlkhdda trkniptaey qsilrdedka pirvayerrn qdldpqlvwr
       61 gkdvqdwsdl vvhapplyiq ekvhpkvlid dlkrqteaaq aaaatqqqgf vadlfadfng
      121 lpsneaktef yqhdahwanr milgdslavm aslaereglr gkvqciyfdp pygikfnsnf
      181 qwsttsrdvk dgnaghitre peqvkafrdt wrdgihsylt ylrdrltvar dlltdsgsif
      241 vqigdenvhr vravmdevfg denciteilv kkkgsqkggt ldpvndfilw ygkqkkssnq
      301 lkirpiyevr sqfelledfp fielsdgrrl rlteleeldg fkysddlaal errypasklf
      361 aanplksggn rrqqshdfkf rgrtfpikpg qcwkhtvied dgstpgmerl gradrlhpqn
      421 tdvrfvrhsp qpsireisnw wdgfggasnq iyvvqtnerv vqrclllatd pgdlvlditc
      481 gsgttayvae qwgrrwitid tsrvalalar arimgarypy ylladsregq lkvaevtqra
      541 passpvrsdv rlgfvyehvt nttsgdiann ieidviwekf qavleplrfk lnelteqqwq
      601 ewevprdiep hiptwltsgf qqrvtttpvd rnarvqeirk lhadwwaqri arqkeidasi
      661 aakaefefly dkpyedkkkv rvagpftves lsphrtlgvd engdvmdgnk aaepeagygg
      721 tsvrdfaaii lenlrtagvq qahkqdrisf taltpwpgsy vcgegryteg eggaekraai
      781 figpefgtvs rpdlvsaake agdagfdvlv acafnydahs sefeklgrip vlkarmnadl
      841 hmaedlkntg kgnlfvifge pditildaat dqpfkagera tgelkvkvng vdvfdpstge
      901 vrsdgadgia cwfidtdyne esffvrhayf lgandpyksl kttlkaeinq eawdslnsdv
      961 srpfdkpssg riavkvinhl gdevmkvfrv
//
LOCUS       WP_006299998             656 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Aminomonas paucivorans].
ACCESSION   WP_006299998
VERSION     WP_006299998.1
KEYWORDS    RefSeq.
SOURCE      Aminomonas paucivorans
  ORGANISM  Aminomonas paucivorans
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Synergistaceae; Aminomonas.
REFERENCE   1  (residues 1 to 656)
  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 656)
  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 656)
  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 656)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Aminomonas paucivorans"
                     /db_xref="taxon:81412"
     Protein         1..656
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=69254
     Region          16..647
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mepkekpvdl lsidpmndek iqrlvekyda esryrrltgl pgklvtllla gmslfhlyta
       61 gigilpitiq ravhltfaiv avyllypmtq kgsktqtpwy dwilaaaslv avgyialffn
      121 diarrgaepi gyelwlgala mvlvleagrr vvgnvlpvms llflsycyyg ayapgmfqir
      181 gysvsriiqh myltpegifg valgvsatfv itfiifgafl gksggarffn elalalagsr
      241 pggpakvavv asgllgting ssvanvattg tftiplmkrv gykpeyagav eacastggql
      301 mppimgagaf imseflgmsy lriaaaaalp avlyytaifv nvhvrarkrg lrglskdelp
      361 aagqvlkqdg hllipviavi aallmkytpi kaaflgvlav vvvsqfraht rmgfkaivea
      421 leegargglg valacalvgf vvgtstltsl gltlsnniie isggkllptl vmamvaslvl
      481 gmglpttany ivcstiiapa ligmnvfpla ahlfvfyfgi madltppvcl aaftgagiag
      541 anpaktgfta tkialasyll pysfiyspmi llenvvyldl avilvagvag ilglaagleg
      601 wmfrslkple rvaiilvsvg aflphdlpkl valgavvaaf lffrktagee iqpeta
//
LOCUS       WP_006300056              98 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Aminomonas paucivorans].
ACCESSION   WP_006300056
VERSION     WP_006300056.1
KEYWORDS    RefSeq.
SOURCE      Aminomonas paucivorans
  ORGANISM  Aminomonas paucivorans
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Synergistaceae; Aminomonas.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Aminomonas paucivorans"
                     /db_xref="taxon:81412"
     Protein         1..98
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10734
     Region          1..97
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mdidrvrdil rqnnalllqh hvrslsvfgs vvrgeagpds didllvefqp nvavglfefi
       61 rlknelstll gmkvdlgtpd alhpalkeei lkeavhva
//
LOCUS       WP_006300579             198 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Aminomonas paucivorans].
ACCESSION   WP_006300579
VERSION     WP_006300579.1
KEYWORDS    RefSeq.
SOURCE      Aminomonas paucivorans
  ORGANISM  Aminomonas paucivorans
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Synergistaceae; Aminomonas.
REFERENCE   1  (residues 1 to 198)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Aminomonas paucivorans"
                     /db_xref="taxon:81412"
     Protein         1..198
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=21661
     Region          35..169
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(126,129,142..145,147)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mslsrfalll lvlgvllplg taqaapfvpg peeywikvdk srlrlylfqg kdtlvksypv
       61 avgrgvgdvk kdrldlitpe gvfkvrrvlq dasqlvydpa wfdepgepqk gvygsklisf
      121 ynpwqiaihg tnsprsvgrr athgcirmkn rdintlvayv kpgmkiwivg kdgkappggk
      181 tappgtpnle pgverdtl
//
LOCUS       WP_006301797             101 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Aminomonas paucivorans].
ACCESSION   WP_006301797
VERSION     WP_006301797.1
KEYWORDS    RefSeq.
SOURCE      Aminomonas paucivorans
  ORGANISM  Aminomonas paucivorans
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Synergistaceae; Aminomonas.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Aminomonas paucivorans"
                     /db_xref="taxon:81412"
     Protein         1..101
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11421
     Region          10..96
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mslqtspvpe elaafcrrhh irrlalfgsa lgpgfressd idllvefrpe hipgllgmar
       61 lerelsafwg grrvdlrtpe dlspyfrqqv leeakeqyae g
//
LOCUS       WP_006301846             420 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Aminomonas paucivorans].
ACCESSION   WP_006301846
VERSION     WP_006301846.1
KEYWORDS    RefSeq.
SOURCE      Aminomonas paucivorans
  ORGANISM  Aminomonas paucivorans
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Synergistaceae; Aminomonas.
REFERENCE   1  (residues 1 to 420)
  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 420)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Aminomonas paucivorans"
                     /db_xref="taxon:81412"
     Protein         1..420
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=44561
     Region          58..279
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mdvaskayqn llkrrplnvr arfgneplgl vsgrdiasam neagaialaa narnalvikg
       61 vlkaakklda avllelakse stycgatyen ipdyalqysa elghgvvfgl hvdhygikgp
      121 ddvlkgaahl ghvlargfts valdashlpd yenlratrdl adwipsglgl evevgeikga
      181 gelstveeal yfigglnawg vfpdylaisn gslhgtydpa agqvegidla rtveiaaaia
      241 pygvsiaqhg isgtpldkvg tfrnygirkg nvatlfqnvi fglkmdpatg naviqdgsyv
      301 kepgrgiptd lwnqivawcd akgygrksgd ykkanlpfhd pildlppsvq epiveeiaww
      361 aerflvafga agtaervmei varrpdhnaa pertilhrrd afgpgaapgg gvkgegdysd
//
LOCUS       WP_006303034              78 aa            linear   BCT 20-JAN-2025
DEFINITION  acyl carrier protein [Fannyhessea vaginae].
ACCESSION   WP_006303034
VERSION     WP_006303034.1
KEYWORDS    RefSeq.
SOURCE      Fannyhessea vaginae
  ORGANISM  Fannyhessea vaginae
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Coriobacteriales; Atopobiaceae; Fannyhessea.
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   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 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   4  (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 10011594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Fannyhessea vaginae"
                     /db_xref="taxon:82135"
     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=8439
     Region          4..78
                     /region_name="acpP"
                     /note="acyl carrier protein; Provisional; PRK00982"
                     /db_xref="CDD:179197"
ORIGIN      
        1 mdssqvfetv tniisteldv dkqsltpqte fkdlgadsfd llslitafed efgstlnddi
       61 lqniktinda vdaivnaq
//
LOCUS       WP_006303741             224 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Fannyhessea
            vaginae].
ACCESSION   WP_006303741
VERSION     WP_006303741.1
KEYWORDS    RefSeq.
SOURCE      Fannyhessea vaginae
  ORGANISM  Fannyhessea vaginae
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Coriobacteriales; Atopobiaceae; Fannyhessea.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 224)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 224)
  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 224)
  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 224)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Fannyhessea vaginae"
                     /db_xref="taxon:82135"
     Protein         1..224
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25182
     Region          136..222
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(154,173..174,192,195,203..204,214,219)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mhhknilfva etrrcvpimr elkqaldvsi lssasatlpq alnsehvfdc iiidmqdiqn
       61 dvytridayi aehptvgtlv vqdknalnkl rffnntkndf ivsdasahef qarcallmwn
      121 ggeeapddei sidnmtinla tyqvyiddkp vdltlmeysl lsflashpgr aysrekllhq
      181 vwgfeycggt rtvdvhirrv rskvgpqvas higtvrgvgy lfra
//
LOCUS       WP_006303511             389 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Fannyhessea vaginae].
ACCESSION   WP_006303511
VERSION     WP_006303511.1
KEYWORDS    RefSeq.
SOURCE      Fannyhessea vaginae
  ORGANISM  Fannyhessea vaginae
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Coriobacteriales; Atopobiaceae; Fannyhessea.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 389)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Fannyhessea vaginae"
                     /db_xref="taxon:82135"
     Protein         1..389
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42463
     Region          1..389
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mnilvinags sslkyqllnp ntkevfakgn cerigidgsf igheemgsek qklvvdlpth
       61 keaikhvfsi ikplgkevdg ighrvvqggw yisessivtd evmkhvreva plaplhnpve
      121 advidicrtm fpsipnvivc dtsfhyhmpe kasryalprk vedelhirky gmhgtshrfi
      181 wqatsafthg ethklvschl gsgaslcaih egksvdttmg ltpldglimg trtgtldpav
      241 vfylvrvggy tideidtmmn kesglkglsc lssdsrdiea aaekgdknci qtlemyyyrt
      301 aaliaemaqa mhgfdtiafs agvgensdim ragivdelgw lgvsidpekn svrsdqvrdi
      361 saptsrvrvl vvptneelmi aldvqalia
//
LOCUS       WP_006304011             145 aa            linear   BCT 20-JAN-2025
DEFINITION  division/cell wall cluster transcriptional repressor MraZ
            [Fannyhessea vaginae].
ACCESSION   WP_006304011
VERSION     WP_006304011.1
KEYWORDS    RefSeq.
SOURCE      Fannyhessea vaginae
  ORGANISM  Fannyhessea vaginae
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Coriobacteriales; Atopobiaceae; Fannyhessea.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Chen,S., Jancrick,J., Yokota,H., Kim,R. and Kim,S.H.
  TITLE     Crystal structure of a protein associated with cell division from
            Mycoplasma pneumoniae (GI: 13508053): a novel fold with a conserved
            sequence motif
  JOURNAL   Proteins 55 (4), 785-791 (2004)
   PUBMED   15146477
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449500
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Fannyhessea vaginae"
                     /db_xref="taxon:82135"
     Protein         1..145
                     /product="division/cell wall cluster transcriptional
                     repressor MraZ"
                     /GO_function="GO:0000976 - transcription cis-regulatory
                     region 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=15999
     Region          3..140
                     /region_name="MraZ"
                     /note="DNA-binding transcriptional regulator and inhibitor
                     of RsmH methyltransferase activity [Translation, ribosomal
                     structure and biogenesis]; COG2001"
                     /db_xref="CDD:441604"
ORIGIN      
        1 myltgtykhs ldakfritlp svfrkqlgdv iclvplnnav ygftpeshra wiqsffpqgv
       61 nprdqravgl rtallsrtlt ldldsagrla lgkldpkqle avnikkdvav vgvddhfeiw
      121 daatfdaqsa mfdanlddlm ygvsq
//
LOCUS       WP_006304817             184 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Centipeda periodontii].
ACCESSION   WP_006304817
VERSION     WP_006304817.1
KEYWORDS    RefSeq.
SOURCE      Centipeda periodontii
  ORGANISM  Centipeda periodontii
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Centipeda.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Centipeda periodontii"
                     /db_xref="taxon:82203"
     Protein         1..184
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=19996
     Region          1..184
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mkkivvgitg asgsiyavrl vdvlreqgie vhavitdsgr cvldyecgvt teelarrvdv
       61 lypnddvgaa iasgsfrmda mvilpcsmkt agaiahgvtd dlltraadvt lkegrrlllv
      121 pretpmheih lenlmrlara gavimpaapg fyhkpetldd lvnmmvgkil drlgieaelf
      181 trwr
//
LOCUS       WP_006304657              79 aa            linear   BCT 20-JAN-2025
DEFINITION  acyl carrier protein [Fannyhessea vaginae].
ACCESSION   WP_006304657
VERSION     WP_006304657.1
KEYWORDS    RefSeq.
SOURCE      Fannyhessea vaginae
  ORGANISM  Fannyhessea vaginae
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Coriobacteriales; Atopobiaceae; Fannyhessea.
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]
REFERENCE   4  (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 10011594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Fannyhessea vaginae"
                     /db_xref="taxon:82135"
     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=8650
     Region          3..72
                     /region_name="acpP"
                     /note="acyl carrier protein; Provisional; PRK00982"
                     /db_xref="CDD:179197"
ORIGIN      
        1 mdnaaitdkv felistelev dkatltletr fkedlgcdsf dllslvtafe defartlddd
       61 slqhivtvgd avravqqsl
//
LOCUS       WP_006305029             639 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Centipeda periodontii].
ACCESSION   WP_006305029
VERSION     WP_006305029.1
KEYWORDS    RefSeq.
SOURCE      Centipeda periodontii
  ORGANISM  Centipeda periodontii
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Centipeda.
REFERENCE   1  (residues 1 to 639)
  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 639)
  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 639)
  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 639)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Centipeda periodontii"
                     /db_xref="taxon:82203"
     Protein         1..639
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=67083
     Region          1..638
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mtdhktaeav lkkydresnt vhyaglpkki iaaiaitfsv fqlytatfgi ldaqlqravh
       61 lgfglalayl lypfrrawtr dsffhpidvi favlgaaapa yiviqyrelv tragaiaptd
      121 vvvggigill vieatrrvvg lpmvtvvlff layaflgpym pgvlahrgls ieqlvshlyf
      181 ttegifgipl gvsstfiflf ilfgaylest glgkffidla navagwasgg pakvavlssg
      241 lmgtvsgssv anvvgtgslt ipmmkklgyh pnfagaveaa astggqlmpp vmgaaaflma
      301 efvgvsyiev vkaaaipall yftgvwlgvh feakrknlkg iprnelpnpl tlikerghla
      361 iplvvivyll vsgytpmraa lvaivlsiac amlrkstrmk pieivygler gakavlgvli
      421 acaaagiiig vvtktgvglr lasgliemag gmllpamfft mitaivlgmg vpttanyvit
      481 stiaapalvq mgvpilaahm fvfyfgiiad vtppvalaay agagisggna lktgvhaskl
      541 aiaafiipyi fvlspvilmv datpltliva tlsallgmia vssalcgfla dhcrlyervl
      601 livagllmik pggmtdmigl aifavilamq ytrakkaea
//
LOCUS       WP_006305322             132 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Centipeda periodontii].
ACCESSION   WP_006305322
VERSION     WP_006305322.1
KEYWORDS    RefSeq.
SOURCE      Centipeda periodontii
  ORGANISM  Centipeda periodontii
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Centipeda.
REFERENCE   1  (residues 1 to 132)
  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 132)
  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   3  (residues 1 to 132)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Centipeda periodontii"
                     /db_xref="taxon:82203"
     Protein         1..132
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15406
     Region          15..114
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mrnynqkvkq yakemrhcmt peerrlwydf lsksayhfrr qqpvgnfivd fysvalkfai
       61 evdggqhfee dvrgydvnrt aclsergirl vrftnqqirr dflsvceaid naiadivsdg
      121 eiacteddgh iy
//
LOCUS       WP_006309456             153 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Facklamia languida].
ACCESSION   WP_006309456
VERSION     WP_006309456.1
KEYWORDS    RefSeq.
SOURCE      Facklamia languida
  ORGANISM  Facklamia languida
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Facklamia.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 153)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Facklamia languida"
                     /db_xref="taxon:82347"
     Protein         1..153
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=17534
     Region          2..130
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(7..10,41..43,46,73,112,126)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mlvihidasy dpktkeagla fhiqagaesi srkyylaqia dnhvaefqtl illldylkei
       61 qtdpnqliqi ksdskilvas iakryvkspq yqpyfniilq emtaypllfv dwvaekfnrg
      121 adqlakqalr qqgkviqlne etllhkwkkp iqh
//
LOCUS       WP_006310096             367 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [unclassified Agrobacterium].
ACCESSION   WP_006310096
VERSION     WP_006310096.1
KEYWORDS    RefSeq.
SOURCE      unclassified Agrobacterium
  ORGANISM  unclassified Agrobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 367)
  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 367)
  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 367)
  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 367)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="unclassified Agrobacterium"
                     /db_xref="taxon:2632611"
     Protein         1..367
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40126
     Region          1..357
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mdrrsfirka gavgagvtat alaapaiaqe npkitwrmts sftkgldilf gagqlvadhv
       61 keasggnfvi qhfaggeivp alqaadavta gtvemahtcs yyyvgkdptf algtsvpfgl
      121 narqtnawfn qaggnellne flaqhniysi llgntgaqmg gwfrkeinti ddlkglkmri
      181 agltgqvmqk vgvtpqqiag gdvyaalekg tidatefvgp yddqklgfyk vakyyyypaw
      241 weggpavhaf vnlqkfndlp enykrilkda caagsasmle rydarnpkal kelvaqgail
      301 rpfsqeildv chkaaqdtya eisaknesfk kiyesqqafk kdaylwaqia eytydtymmi
      361 qqrngtl
//
LOCUS       WP_006312557             154 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Caldisalinibacter kiritimatiensis].
ACCESSION   WP_006312557
VERSION     WP_006312557.1
KEYWORDS    RefSeq.
SOURCE      Caldisalinibacter kiritimatiensis
  ORGANISM  Caldisalinibacter kiritimatiensis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Thermohalobacteraceae; Caldisalinibacter.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 154)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Caldisalinibacter kiritimatiensis"
                     /db_xref="taxon:1304284"
     Protein         1..154
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=17535
     Region          <7..139
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mkkkncqlll dsnfsqlkfe itetqiltle nenvknlkel mnlgieisld dfgtgyssir
       61 nmaffpvsev kidkgfidyi iedekmeklv sliivtahkl gytvtaegve ykgqlnklle
      121 yscdkiqgfy lakpmsaqdi vefirysnln elsk
//
LOCUS       WP_006314553             122 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: endonuclease domain-containing protein
            [Agrobacterium].
ACCESSION   WP_006314553
VERSION     WP_006314553.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium
  ORGANISM  Agrobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 122)
  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 122)
  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   3  (residues 1 to 122)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Agrobacterium"
                     /db_xref="taxon:357"
     Protein         1..122
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14080
     Region          17..119
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mphakvkpqh reharqmrka ltdaelkfwn avrahrlagl sfrrqlpvsg yivdfacpsh
       61 kiiveldgfq haedaaaayd rqrtrtleel gwtvlrfwnd dilkdidnvc lhiirtaeen
      121 qp
//
LOCUS       WP_006315175             365 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [Agrobacterium].
ACCESSION   WP_006315175
VERSION     WP_006315175.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium
  ORGANISM  Agrobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 365)
  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 365)
  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 365)
  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 365)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Agrobacterium"
                     /db_xref="taxon:357"
     Protein         1..365
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40084
     Region          1..355
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mdrrsfmkkg alagaaatal aapaiaqqnt kinwrltssf pksldtiygg aediakhvaa
       61 atdgnftiqp faageivpgl qaadavssgt vemchtcsyy yvgkdptfai gtaipfglna
      121 rltnswfyeg ngnkllnefy akhnlygmis gntgaqmggw frkeintvdd fkgvkmriag
      181 lagkvveklg vvpqqiaggd iypalekgti daaewvgpyd dhklgfqkva kyyyypafwe
      241 ggpvihsfvn ldkwnslpkn yqmvlqdaca fantsmmaky daknpiaikq lvsegavlrp
      301 fsqeileacy kaalevyani sasnpdfkki yedqvafkre gylwmqlaey tfdtfmmiqq
      361 rngkl
//
LOCUS       WP_006315177             179 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Rhizobium/Agrobacterium group].
ACCESSION   WP_006315177
VERSION     WP_006315177.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium/Agrobacterium group
  ORGANISM  Rhizobium/Agrobacterium group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae.
REFERENCE   1  (residues 1 to 179)
  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 179)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 179)
  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   4  (residues 1 to 179)
  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   5  (residues 1 to 179)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Rhizobium/Agrobacterium group"
                     /db_xref="taxon:227290"
     Protein         1..179
                     /product="TRAP transporter small permease subunit"
                     /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=19941
     Region          4..166
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mksllklsal idlvsealgk vagylvlicc lvsagnamvr yalnyssngw leiqwymfaf
       61 ivligasytl rmnehvrvdi iygaisprsr lwvdiigivl flipacfyla wlswpmftls
      121 whqgemssna gglirwpvkl vifagfallv lqgfselikr vgalnglyal dtkyekplq
//
LOCUS       WP_006316267             684 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Caldisalinibacter kiritimatiensis].
ACCESSION   WP_006316267
VERSION     WP_006316267.1
KEYWORDS    RefSeq.
SOURCE      Caldisalinibacter kiritimatiensis
  ORGANISM  Caldisalinibacter kiritimatiensis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Thermohalobacteraceae; Caldisalinibacter.
REFERENCE   1  (residues 1 to 684)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 684)
  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   3  (residues 1 to 684)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Caldisalinibacter kiritimatiensis"
                     /db_xref="taxon:1304284"
     Protein         1..684
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76843
     Region          1..684
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          175..254
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 mdmnqyleif iveakehlen lnenllslek dpdnkdllne ifrashtlkg magtmgfmki
       61 kdlthemenl lhalrndkfk vnseivdilf ealdtledyi nyvsesgeeg dldssklvkn
      121 ineliennge lavtveqaqi qkeaenrdkq pvfidhnqyv inllkkakkr glnafditit
      181 lkkncmlksa rafivfktle knaeivqsnp svediedekf dntfsvtivt kadeanmkkd
      241 imlvseiesv qisevnlede isneskitde sdsnhiaekt lnvkkddiik kqknkrkesr
      301 rlgktvrvdi drldnlmnlv seliiiktrm edasgdlekk gnmneaieyl erittslhda
      361 vmkvrmvpie rvfnrfprmv rdlskelgke inlemsgeet evdrtvidei gdplihlirn
      421 sidhgiespe erikagknka gvvklcaypd gnnvvieved dgdgidiekv rqkgiakglv
      481 deekaytlsd devidllfna gfstadnitd isgrgvgldv vktkiesigg nvevetergk
      541 gtkftirlpl tlaiiqallv klenetfaip lssikeispi mskdirkvqg qeiilfrnkt
      601 lpiirlnell glnsntenqk eelitvivkk gdkeagliid dligqqeivi kslgkylngi
      661 kylagatilg ngeislildi nslf
//
LOCUS       WP_006315910              98 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein [Agrobacterium].
ACCESSION   WP_006315910
VERSION     WP_006315910.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium
  ORGANISM  Agrobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Agrobacterium"
                     /db_xref="taxon:357"
     Protein         1..98
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=10432
     Region          19..76
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mdhtnhvrlv eteltpsvle gatvygaddh kvgkvdhvhg vgaattaiid vggflgigak
       61 pvavplsdld fmrdedgdvh avtswtkdql kempehrh
//
LOCUS       WP_006319632             237 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Serratia inhibens].
ACCESSION   WP_006319632
VERSION     WP_006319632.1
KEYWORDS    RefSeq.
SOURCE      Serratia inhibens
  ORGANISM  Serratia inhibens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (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   3  (residues 1 to 237)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Serratia inhibens"
                     /db_xref="taxon:2338073"
     Protein         1..237
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26954
     Region          63..235
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mehndnglfi krerfevlai lreickqrtp lrvvnqqqqf qslllsvgpd nivfsgdkad
       61 svadgeftvv ieshdakief tvgqpkftdq lgvqvcstcl pkelvyiqrr rqfrvttphw
      121 rqflcsgeya dgtayqlrih dlsaggvglr fdgplpdklq pgilfkkall dlgsygsfkv
      181 nmelmvined qeldeddkpv hfsrlscrfi nlglamerki qsavfafeld fnkkkkr
//
LOCUS       WP_006315876             370 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [Agrobacterium].
ACCESSION   WP_006315876
VERSION     WP_006315876.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium
  ORGANISM  Agrobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 370)
  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 370)
  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 370)
  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 370)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Agrobacterium"
                     /db_xref="taxon:357"
     Protein         1..370
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40345
     Region          31..361
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkdnpgrrqf lsggvlagaa aaastlatpa iaqsspsvrw rltsgfpnnl dtiyggavvm
       61 analramtgg kfdiqvfqag eivpgaqaid avkantveis htcgyyftgk dptfaigsti
      121 pfglnarqqn awlyhgggne ayneflsdyg vigipggatg aqmggwyrke ikgiedikgl
      181 kmriagvagq vlaklgavpq qlpggdiypa lergtidaae wvgpyddekl gfyqiapyyy
      241 ypafwegglt ihffvnkdqy aalpdeykaa ldtackaani nmqalydvkn kdairslvsk
      301 gtqlrplprd vldaaykatf elydeytqky pawakiypgw kkfrdesyew frvaeytyds
      361 ygyamqtagk
//
LOCUS       WP_006319646             386 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Serratia inhibens].
ACCESSION   WP_006319646
VERSION     WP_006319646.1
KEYWORDS    RefSeq.
SOURCE      Serratia inhibens
  ORGANISM  Serratia inhibens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 386)
  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 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   3  (residues 1 to 386)
  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   4  (residues 1 to 386)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 386)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 386)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 386)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Serratia inhibens"
                     /db_xref="taxon:2338073"
     Protein         1..386
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40720
     Region          34..369
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(109..111,132..133,182,234,258)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mnkitrfkpl alaaavlatl gaaapawaad tiliglagpl tgpsarigkd lengaqlaia
       61 danaqkptln gkpvtfklls eddqsdprta vavaqrlvde gvagvvghwn tgtsipaari
      121 yhdagiaqva pvatghaytq qgfdtsfrvm ghdddggnya geyavkvlka kriaiiddrt
      181 afgqgladef ikslaaqgvq pvareyvddk tvdfsavltt vrsknadlif fggvdsqaap
      241 larrikqlgm ntqlmgaggf vsqtfltlaq kegegvvale pglpleqmpg gkafeqayrd
      301 rykthielha pfaydatrvl iaaieqagsa npadylpklr aihyqgvtgn iafdpqgnlq
      361 qpsftlykvv dgkwqpqsvl ggaktq
//
LOCUS       WP_006319652             626 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Serratia inhibens].
ACCESSION   WP_006319652
VERSION     WP_006319652.1
KEYWORDS    RefSeq.
SOURCE      Serratia inhibens
  ORGANISM  Serratia inhibens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 626)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 626)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 626)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 626)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Serratia inhibens"
                     /db_xref="taxon:2338073"
     Protein         1..626
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68093
     Region          1..626
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mtaeneleqt pkmslpllag galgvvfgdi gtsplytlkt vlylsgdaps apvilgllsl
       61 ifwtlvivts lkyamfamri dnrgeggima lmsllvskks arpmvvfagl fgaaliygdg
      121 aitpaisvls aleglnivlp esqpyilpaa vvilvslfai qplgtarigk vfgpimalwf
      181 fsiavlgvwg iiqhpavlma lnplyginfl fsngvtsflv lggvflcvtg aealyadmgh
      241 fgkrpiwlaw fgivfpslll nyagqaalil sgadvtqnif frlcppimqi plvilatlat
      301 iiasqaiisg afsmtrqaiq lgwlprlrvk qtteesygqi yigainwllm avtvfltvff
      361 kssdnlaaay giavsltmim tsgllfvamr evwrwgftas llvaggffiv dlsflvanls
      421 kvlqggyvpl llaslvygvm liwhrgvaaa srtlgeksmp lvdflaqiev qaiprvpgta
      481 ifltrnmngt ppvmkwhvkr ngslhadvlt lnimivnepr vanaerlvmr qqspgfwcgv
      541 asygfmerpn iprllhhaea qktglnfdda tyylghetvv rreddsrlpa wqrsifalmv
      601 rngmhvtdyy ylpsdqvvei srrvpv
//
LOCUS       WP_006319692              91 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Anoxybacillus flavithermus].
ACCESSION   WP_006319692
VERSION     WP_006319692.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacillus flavithermus
  ORGANISM  Anoxybacillus flavithermus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Anoxybacillus.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Anoxybacillus flavithermus"
                     /db_xref="taxon:33934"
     Protein         1..91
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10328
     Region          3..87
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 msknldmwsk kygvkriglf gsysrgeqre ssdidvlvef iddamtfdny mdlklsledh
       61 fqkkvdlvii ddikpslmst ilgsakyaer a
//
LOCUS       WP_006319773             277 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Anoxybacillus flavithermus].
ACCESSION   WP_006319773
VERSION     WP_006319773.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacillus flavithermus
  ORGANISM  Anoxybacillus flavithermus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Anoxybacillus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Anoxybacillus flavithermus"
                     /db_xref="taxon:33934"
     Protein         1..277
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31250
     Region          1..275
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 merehlllid gmallfrsfy ataprwmins rgvptnavyg vvkqieaatn alrpthvvcc
       61 wdmgsttfrt ewfpdykanr gepphelmpq fdlaketvam lgipnigvlg aeaddcigsl
      121 vkqyrehmqi simigdrdlf qllservtvy llakgignye aytlerfieq kgiqphqlid
      181 vkalmgdpsd nypgvrgige kqafklvqqy gsiegilenl anltnaqqqk itehldllhl
      241 srklatihcd ipislrleea kwdgerkrfa evleair
//
LOCUS       WP_006319839             372 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Serratia inhibens].
ACCESSION   WP_006319839
VERSION     WP_006319839.1
KEYWORDS    RefSeq.
SOURCE      Serratia inhibens
  ORGANISM  Serratia inhibens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 372)
  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 372)
  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   3  (residues 1 to 372)
  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   4  (residues 1 to 372)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 372)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Serratia inhibens"
                     /db_xref="taxon:2338073"
     Protein         1..372
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39702
     Region          29..363
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(103..105,126..127,176,228,252)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 msskfikspl aalligclgs afyaqadivi gvagpfsgpn atygdqywrg asqaaadina
       61 aggikgekik lvqgddacep kqavsvanrl vdqdkvsavv ghfcssstmp asevydeagi
      121 iaitpgstnp qitergmtnm frmcgrddqq gviatdymln tlkakriavi hdkdtygqgl
      181 adaaraemnk rgvkevlyeg lsrgekdfna lvtkiasvkp dvvyfggchp eagplvrqmr
      241 eqgvtakffs gdcvvteelv taaggpqytn gvlmtfgndp rqipegkavi akfrasgfep
      301 egytlysyas iqaiaaafsa tggkdsakas ewlkshdvdt vmgkkawdkk gdlkvsdyvv
      361 yqwddkgkyh ql
//
LOCUS       WP_006320006             420 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Serratia
            inhibens].
ACCESSION   WP_006320006
VERSION     WP_006320006.1
KEYWORDS    RefSeq.
SOURCE      Serratia inhibens
  ORGANISM  Serratia inhibens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 420)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 420)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Serratia inhibens"
                     /db_xref="taxon:2338073"
     Protein         1..420
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47240
     Region          9..412
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mngqrqvesv qalalmlhqv rigvlahysg gkniltfdpq ylalpeasrp lftlrqrahp
       61 gyleqvlmss lrlppvlsnl lpegalrswl aqslkthvde efplmawtga nlpgaleara
      121 laaneipawa ltsrgeleav qidvgletqk fslagvqmkf sslrkdgrfn issqvgadsw
      181 iiktpstvhr nvpeneytam rlaqaigvdi pdielvavgq ldnlpdirla depyayairr
      241 fdrsesgrvh aedfaqifei yahdkyrgkn yeqiaaylyd wgsdpladvq qmarrllani
      301 llangdahvk nwsmiypnqt gvrlspaydi vttrvyipge sevalnmare krwamismqt
      361 ferwaervgi pwpairvhll daidkartlw pdllenlpmv aehqsvlrqh waslssdfrl
//
LOCUS       WP_006326065             419 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Serratia plymuthica].
ACCESSION   WP_006326065
VERSION     WP_006326065.1
KEYWORDS    RefSeq.
SOURCE      Serratia plymuthica
  ORGANISM  Serratia plymuthica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 419)
  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 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   3  (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   4  (residues 1 to 419)
  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 419)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Serratia plymuthica"
                     /db_xref="taxon:82996"
     Protein         1..419
                     /product="CmpA/NrtA family 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=45568
     Region          42..293
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mthtkhpgle ltrrrflags aalggsmllp glmntawaag sdapekkeir vgfipltdca
       61 svvmaavkkf dekygikiip skeaswaavr dkllsgelda ahvlygmvyg lqlgvagpqh
      121 dmavlmtlnn ngqaitlsnq lkqagvtdag alkkhvdasa kgtytfaqtf ptgthamwly
      181 ywlanagihp fddvrnvvvp ppqmvmnmki gnmsgfcvge pwnqraiaen igftavttqe
      241 iwpdhpekvl gttgnwvaan pnsaraltaa vldaarwids sdanreetaq vvagrayint
      301 kpevitgrml gqyqnglgks wqdahamrff hdgevnypyl sdgmwfltqh rrwgllsaep
      361 dylavaqkin rieiykqaas avggvnlpgs dmrastlfdg krwdgsnpae yansfslkr
//
LOCUS       WP_006326190             200 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Mesorhizobium sp. STM
            4661].
ACCESSION   WP_006326190
VERSION     WP_006326190.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. STM 4661
  ORGANISM  Mesorhizobium sp. STM 4661
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 200)
  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 200)
  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   3  (residues 1 to 200)
  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   4  (residues 1 to 200)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 200)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Mesorhizobium sp. STM 4661"
                     /db_xref="taxon:1297570"
     Protein         1..200
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21592
     Region          17..193
                     /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"
ORIGIN      
        1 mskvpripnl ggaktfvlhr phptvqaitr qlsaigletv gcwpelpaev laadfvffda
       61 dlgfdeqfpw kpgeapmplv aligseapgr iewalshqad aqllkpvgna gvysalliar
      121 qsfearklqa seisslrlrv aerqtivrav ealskgagdg rayaqlrsla mswqisveea
      181 arrivamtee eggddqshra
//
LOCUS       WP_006307027             273 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Caldisalinibacter
            kiritimatiensis].
ACCESSION   WP_006307027
VERSION     WP_006307027.1
KEYWORDS    RefSeq.
SOURCE      Caldisalinibacter kiritimatiensis
  ORGANISM  Caldisalinibacter kiritimatiensis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Thermohalobacteraceae; Caldisalinibacter.
REFERENCE   1  (residues 1 to 273)
  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 273)
  AUTHORS   Magnet,S., Arbeloa,A., Mainardi,J.L., Hugonnet,J.E., Fourgeaud,M.,
            Dubost,L., Marie,A., Delfosse,V., Mayer,C., Rice,L.B. and Arthur,M.
  TITLE     Specificity of L,D-transpeptidases from gram-positive bacteria
            producing different peptidoglycan chemotypes
  JOURNAL   J Biol Chem 282 (18), 13151-13159 (2007)
   PUBMED   17311917
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   4  (residues 1 to 273)
  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 13744852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Caldisalinibacter kiritimatiensis"
                     /db_xref="taxon:1304284"
     Protein         1..273
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region 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=31535
     Region          82..134
                     /region_name="SH3_3"
                     /note="Bacterial SH3 domain; pfam08239"
                     /db_xref="CDD:462405"
     Region          159..273
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(220,223,246..249,251)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkirlfillm cmtlllvgce negfqkpnve etinvveddk easkelndta ntendgknee
       61 nkdkeeakky igqaldtlew dkvvevykek skkseviykm kdleeielie tvpygwfkvr
      121 ledgtegyvd aryvrtkevp pheynenieg yalvfthqdq tlriykdgql vkesigssgl
      181 wdhftprgif qiekgrrgkw ayiprfnqgf kywvgfkgvy lfhsvpydkn gqviqeeaek
      241 lgqpashgci rlpvdvakfi yenvpegslv liy
//
LOCUS       WP_006327601             372 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Mesorhizobium sp. STM 4661].
ACCESSION   WP_006327601
VERSION     WP_006327601.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. STM 4661
  ORGANISM  Mesorhizobium sp. STM 4661
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 372)
  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 372)
  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   3  (residues 1 to 372)
  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   4  (residues 1 to 372)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 372)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Mesorhizobium sp. STM 4661"
                     /db_xref="taxon:1297570"
     Protein         1..372
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /function="1.4 : Pyruvate family"
                     /function="7.1 : Amino acids, peptides and amines"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38739
     Region          27..358
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(99..101,122..123,172,224,248)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mrksllsava ltalvafggs awadvligva gpitgpnaaf gaqlqkgtea aaadinaagg
       61 ingeqiklsi gddvsdpkqg isvankfvgd gvkfvvghfn sgvsipasev yaengileit
      121 psatnpkfte rglwntfrtc grddqqgsia gaylaanfkd gkiavihdkt tygqgladet
      181 kkamnaagvt evmyegvnvg dkdfsaliak mkeagvsiiy wgglhteagl iirqaadqgl
      241 katlvsgdgi vsnelasiag davagtlntf gpdprlipan kelvekfraq gfepeaytly
      301 syaamqaiaa aataaksndp qevakalkan gpfktvlgdl sydekgdpkl pgyvmyewkk
      361 gddgkytyiq km
//
LOCUS       WP_006329787             292 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Mesorhizobium sp. STM
            4661].
ACCESSION   WP_006329787
VERSION     WP_006329787.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. STM 4661
  ORGANISM  Mesorhizobium sp. STM 4661
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Mesorhizobium sp. STM 4661"
                     /db_xref="taxon:1297570"
     Protein         1..292
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31978
     Region          13..255
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mkievvvdvk ttlgegplwd veqqrlywid sfdgrvfrat adgreirswd vpmkigsmal
       61 rkdgsgavvs lqrgfhlldf asgdvtlihd pepdkpmnrl ndgkvdrrgr ffagsmdtme
      121 egpsgglyrl dpdfsvtrid sgiicsngpc wspddrtfyf adtwtgeiwa ydydiatgaa
      181 tnrrtftrvd tsrggaadgs tvdaegflwn alvydgrlvr yapdgsidri idmpvkkits
      241 vmfggpkldi lyvtsmakpp lprfpgdgvl rgslfaitgl gvtgtpeprf gg
//
LOCUS       WP_006330004             708 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Mesorhizobium sp. STM 4661].
ACCESSION   WP_006330004
VERSION     WP_006330004.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. STM 4661
  ORGANISM  Mesorhizobium sp. STM 4661
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 708)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Mesorhizobium sp. STM 4661"
                     /db_xref="taxon:1297570"
     Protein         1..708
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72416
     Region          7..704
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 migfaasrea mralmaprsv avigaterad asssyvmrnl kafgfsgaii pvhpkaetvf
       61 giaaipsldr ldapadvavi gigaahvlga ledagkagvk aavvlasgfa etdgegkarq
      121 qalvgiarky gmaicgpncl glfnlqsgaa lysstlspnl rrgqlailsh sgasaialan
      181 tgrfglshiv scgnsaatdl pdylsyladd eatrviglvv eairdpaaft samraahatg
      241 kqvialragk sskgaeaaaa htgslaaane ayevffrrtg vievadmdef vetaalclsl
      301 karlarkgva vvgvsgggva hvsdiaeqvg idlpefsqnt iarlkavlpp fatprnpvdt
      361 tgvvfadggi yrgvleilaq dpavglivaa qdapvgldaa gaaeyagiad avaaytkdat
      421 vpvafisnls sghhpavrer lagvpvlngt raalnavrrl ldatgvtipn apaiesagen
      481 dpwaerlatg gkltereakq llaenglpvt rerlavtaqe aveaaeaigf pvvlkiespd
      541 iphkteaggv rlgigsaaea aeafaaimqs arahapdael rgvvvqemag rgvealvgli
      601 rhepfglgiv vgvggvlvel vkdaafdllp idrvsaeali drtrlaallk gfrgapqadr
      661 aalvetimal sdfagryghl ieavdlnpvv vfekgvsvld alvisrga
//
LOCUS       WP_006330110              98 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Gordonia rhizosphera].
ACCESSION   WP_006330110
VERSION     WP_006330110.1
KEYWORDS    RefSeq.
SOURCE      Gordonia rhizosphera
  ORGANISM  Gordonia rhizosphera
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Gordonia rhizosphera"
                     /db_xref="taxon:83341"
     Protein         1..98
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10426
     Region          5..98
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(27,55..56,58,80)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(27..28,36,38,40..41,43,46..47,55,60,65)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 masvsdddve rvrelvaaip vgrvttygdl aaaaglsspr ivgwimrtds adlpwhrvis
       61 asgrpaahla drqlerlrae gvavhagrva lrahrwap
//
LOCUS       WP_006330371              82 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Gordonia rhizosphera].
ACCESSION   WP_006330371
VERSION     WP_006330371.1
KEYWORDS    RefSeq.
SOURCE      Gordonia rhizosphera
  ORGANISM  Gordonia rhizosphera
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 82)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 82)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 82)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 82)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Gordonia rhizosphera"
                     /db_xref="taxon:83341"
     Protein         1..82
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8474
     Region          2..82
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mqitiryfaa araaagadst vvdvtadttl gdlettlard npdlrsvlar csylrdsial
       61 cdrtvalgac etidvlppfa gg
//
LOCUS       WP_006330674             373 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Gordonia rhizosphera].
ACCESSION   WP_006330674
VERSION     WP_006330674.1
KEYWORDS    RefSeq.
SOURCE      Gordonia rhizosphera
  ORGANISM  Gordonia rhizosphera
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 373)
  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 373)
  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
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 373)
  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   5  (residues 1 to 373)
  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   6  (residues 1 to 373)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 373)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 373)
  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 15726307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Gordonia rhizosphera"
                     /db_xref="taxon:83341"
     Protein         1..373
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38281
     Region          20..>75
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          82..346
                     /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 mspsgvvpaa lqvgalpaaa vlqavrvngp vtrdhlaaat tlspatinrq vtnlcglglv
       61 verpelvdpg gigrpknplt ldrdhlcvag mhigarrtll aiadlggrtl yshavrtprd
      121 aaevgdlciq lrdlaarfsg rrllwggvaa ggavdassgv vdhpvlgwrr vavgpmlada
      181 lgvpvsvceh vqamaaaell ltyprefegt glffyaretv gmamtidgkv hmplhgagsi
      241 ahlpvdapvl vpggrarlqq viggrvdrea aerlgvaaga svivderadv lgtvvammrd
      301 vinpdavvva gdafaahpdg lapvqaafda atttsrtlei spsrfgirvq esaavvvals
      361 viyadpvaat stg
//
LOCUS       WP_006331131             352 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Gordonia rhizosphera].
ACCESSION   WP_006331131
VERSION     WP_006331131.1
KEYWORDS    RefSeq.
SOURCE      Gordonia rhizosphera
  ORGANISM  Gordonia rhizosphera
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 352)
  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 352)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 352)
  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   4  (residues 1 to 352)
  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 352)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Gordonia rhizosphera"
                     /db_xref="taxon:83341"
     Protein         1..352
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39213
     Region          20..206
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          248..328
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msvirgsvlt gyreqvaelg adpdvllraa glrpedagnh dvfipylshi kavesaaeat
       61 gaidfgrqla arrqgveilg plgvalrtap kvsdafdiav kyvsaygpal aislqptgsg
      121 ervfyeirpl ldrlpphaqt qelalgmslk vfrfllgpey splqvhhthr alaprkdyla
      181 yygggprfeq pragftlrar dlerplsrdr aanevirryl dtvlppsetg ltfratelvs
      241 rllptgatld mvakqfamhp rtfqrrleah gttfadlvdd vrrdvaeryl rdtdlsftyi
      301 arelgyseqs tltracqrwf gtsprnyrkr vttetpsrvt sdvknqssrv kf
//
LOCUS       WP_006331499             343 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Gordonia rhizosphera].
ACCESSION   WP_006331499
VERSION     WP_006331499.1
KEYWORDS    RefSeq.
SOURCE      Gordonia rhizosphera
  ORGANISM  Gordonia rhizosphera
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 343)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Gordonia rhizosphera"
                     /db_xref="taxon:83341"
     Protein         1..343
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36736
     Region          10..339
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mttttpqesi ldlatylpet rvpadyfvqy aeddalidnv mfrapefrhh aadgetsadm
       61 mvtaahvltd rhgddffddv davlthsqlp evpirgcgge vahrlglrps tvldvhnggc
      121 vafihlidla gallranggr ralialaqns aaqiftqeqv rgkaqaaipg dgaavavlta
      181 etdsgspilg lschsygqys gdmtgvtepp rkyweagtgq lhigfteaki akvlargnrm
      241 vpeaaievad svgiapadld wlvtnqpnri flrnwreale lpeerhpdtf decgnmfavg
      301 ipvtldtais dgriregdvv mmaafahagd fagaaalrwa grr
//
LOCUS       WP_006332580             339 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Gordonia rhizosphera].
ACCESSION   WP_006332580
VERSION     WP_006332580.1
KEYWORDS    RefSeq.
SOURCE      Gordonia rhizosphera
  ORGANISM  Gordonia rhizosphera
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 339)
  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 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 339)
  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   4  (residues 1 to 339)
  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 339)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Gordonia rhizosphera"
                     /db_xref="taxon:83341"
     Protein         1..339
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36502
     Region          24..209
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          252..334
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mvhwdlprap tsalmmtqvg aehgvpvevc lrgtrlrpdd lddpqreisa qqelavvvnl
       61 lgalgnppgl gldagvhyhl ttygiwgfal issptlrsal dlglrfvdlt fslgrirgre
      121 eademqlvld apdvpltvrr flierdaaai qtlqselfat pipvhrisfa fpppaggngr
      181 aaeifgvvpt fdaaeniiaf dpelldaplp qasehtatva adqcrdllar rqartglagq
      241 vrdtlvarla dppgadqvaa rlnisgrtlr hrlaaegtsf ralldeareh maeellvnag
      301 ltvaetaqrl gyvevssfsq afrrwkgvgp rayraghgg
//
LOCUS       WP_006332589             331 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Gordonia
            rhizosphera].
ACCESSION   WP_006332589
VERSION     WP_006332589.1
KEYWORDS    RefSeq.
SOURCE      Gordonia rhizosphera
  ORGANISM  Gordonia rhizosphera
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Gordonia rhizosphera"
                     /db_xref="taxon:83341"
     Protein         1..331
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=35812
     Region          1..321
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msisvidank rygdfaaldn vsidipegsl tsllgpsgsg kstllraiag ldtldsgtvi
       61 isgndvsras pqkrdigfvf qhyaafkhln vrdniafglk irkrskaein akvdelldvv
      121 gltvfqkrfp aqlsggqrqr malaralavd pqvllldepf galdakvred lrkwlrrlhd
      181 evhvttvlvt hdqqealdvs driavlnkgr ieqvgtpgdl ydrpanefva sflgstvrln
      241 gelvrphdir igrnpelalp aadqsldtgv ikatvtrvvh lgfevrvelv aattgdefqa
      301 qitrgdanal nlqpgeaiya ratkvaalsd t
//
LOCUS       WP_006335933             407 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Gordonia
            rhizosphera].
ACCESSION   WP_006335933
VERSION     WP_006335933.1
KEYWORDS    RefSeq.
SOURCE      Gordonia rhizosphera
  ORGANISM  Gordonia rhizosphera
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 407)
  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 407)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Gordonia rhizosphera"
                     /db_xref="taxon:83341"
     Protein         1..407
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45724
     Region          1..405
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mgrtdlsaaq arrialaaqg ftdrrpsgkp tlahlrrvls riglfqmdsv niaarahylp
       61 mfsrsgpydr aildraawrp grgerllvey waheaalipv tdwplfgwrr eefrdgryrh
      121 trdimrrnrd lardvhaviv dagastprqi edhlgidrsp gvrggwwhrg evkhlcealf
      181 aagelsaird enftrhydlt grivapelve dtvdraeahr rltaraarsl gvatiadlad
      241 yyrtkpaevr gavadlvdtg elapvgvegw rdpaylrpea aiprrvdrsa ilspfdplvf
      301 frpraerlfd fryrieiyvp ehkrvhgyyv lpylmgsdiv arvdlkadrk gstllvlaaf
      361 vepgrskdav aesltadlas marwlglgrv sigdrgdlvd slrrvsg
//
LOCUS       WP_006336422             275 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Mesorhizobium sp. STM 4661].
ACCESSION   WP_006336422
VERSION     WP_006336422.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. STM 4661
  ORGANISM  Mesorhizobium sp. STM 4661
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (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   5  (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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Mesorhizobium sp. STM 4661"
                     /db_xref="taxon:1297570"
     Protein         1..275
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30773
     Region          27..275
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <170..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 mteairlywg rfghvsvlnv asdfvthahv eahiiiwleg tagemtigre tvrlgpgtaa
       61 ginsfqphsh alsrdgtpgl flafyidpdw arrrrdlpss aplfstpait lepwlhkaaa
      121 nlldhlsdne siddianyei erfidsvlda adasapqavr arintmqdfr vrkaiqlmka
      181 nvcericfdd varsvglsrp hffalfkeqt nltpnvywnt lrmeeavrql qwsqeplisv
      241 acnlgfttqg nfsrffrdhv gvpptlyrea araia
//
LOCUS       WP_006337082             367 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Gordonia
            rhizosphera].
ACCESSION   WP_006337082
VERSION     WP_006337082.1
KEYWORDS    RefSeq.
SOURCE      Gordonia rhizosphera
  ORGANISM  Gordonia rhizosphera
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Gordonia rhizosphera"
                     /db_xref="taxon:83341"
     Protein         1..367
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38576
     Region          17..346
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msglhasirc dtpavsvdid iddgatlaim gpngagksta lsvlaglrrs astvtvgdev
       61 vqdgrrflpa hrrsvvllaq rpklfphlsv rrnvafgpsa lrlqrgevte rtdrwldavg
      121 vadladrmpg qlsggqaqrv alaralacep rvllldepfa aldvsvtqqi rsllrdllgq
      181 rsgvtvlvth dlidavslad dvavmdagrv vdagrtrevl ttpghpftas lsglnlfvgr
      241 hvdhavddde ghrvvggvve dvpegspcaa afspravavy lapphgsprt mmrarvtdvv
      301 prgdhavvrt lvgrqivdae vtwsavrdlg lvvgqdvvlv lkasevriyg vaspgapvsa
      361 ievgdpl
//
LOCUS       WP_006336831             122 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Mesorhizobium sp. STM
            4661].
ACCESSION   WP_006336831
VERSION     WP_006336831.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. STM 4661
  ORGANISM  Mesorhizobium sp. STM 4661
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 122)
  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 122)
  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   3  (residues 1 to 122)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Mesorhizobium sp. STM 4661"
                     /db_xref="taxon:1297570"
     Protein         1..122
                     /product="endonuclease domain-containing protein"
                     /function="18 : Unknown function"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=13956
     Region          17..113
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mthypvppvn rgnarkmrka mtdaelklwn eirahrlmgl sfrrqmpian yivdfacpdk
       61 kliveldgsq hadaqvarld tartarleal gwtilrfwnd dvlrdidnvc qhivieagmd
      121 rc
//
LOCUS       WP_006344669             339 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-oxoacyl-ACP synthase III family protein
            [Streptomyces].
ACCESSION   WP_006344669
VERSION     WP_006344669.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 339)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            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="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35996
     Region          8..329
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mtaepgvpgi gitgwgrylp egrltnaela arfgvdeewi vqrtgirerr vvgpgettas
       61 laveagrral akaglrpdqi shlilasgtp eqlspatsaf vqrelgtagg ahdvnaecag
      121 faygfvvaag lmaidprpil ligtdthslv vnpedrdlgv ligdgagavv lephdrswlr
      181 swdmgcdgsk vdslripagg srmpasettl reklhyaqik gneiylnavr ftvgsvkrtl
      241 rsaglapqdi dhllphqanm rivdsilehs gvprerlitn ieyygntgaa smpialaeal
      301 dagriqrgdr vlfaafgagm vwltalvewg ageptgwds
//
LOCUS       WP_006338778             292 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Gordonia rhizosphera].
ACCESSION   WP_006338778
VERSION     WP_006338778.1
KEYWORDS    RefSeq.
SOURCE      Gordonia rhizosphera
  ORGANISM  Gordonia rhizosphera
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 292)
  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 292)
  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   3  (residues 1 to 292)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Gordonia rhizosphera"
                     /db_xref="taxon:83341"
     Protein         1..292
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32040
     Region          177..274
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 medldypgvl aagfgvaswk qlrtagmtrt elraalknst lrgvrrgwya tpwadanvvs
       61 avaaggvlsc lsalrlqkvw vpgtsetvha rarasahrtp gaqfcqqygr peselssvde
      121 ltvavrhalk clddegivvv cdsilnkdll elsdlktvfr saparirrll drcdgaaqsg
      181 tesmtrlhlr srgigvrtqv diagvgfvdm vvgarliiev dgyehrsske qfekdrerdr
      241 kavglgyivi rltyhqvvhe wpaaeesimd ivrrgehlkp pvpttelvsd dt
//
LOCUS       WP_006345838             398 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Streptomyces].
ACCESSION   WP_006345838
VERSION     WP_006345838.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 398)
  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 398)
  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
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 398)
  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   5  (residues 1 to 398)
  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   6  (residues 1 to 398)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 398)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 398)
  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 18624027
            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="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40161
     Region          14..>59
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          77..379
                     /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 metpgsqtsl hranlervvr avrmagsltq adiarstgls aatvsnivre lkesgtvevt
       61 ptsaggrrar sislssdagv vvgvdfghth lrvaianlah evlaedaepl dvdssagtgf
      121 draermvgrl iaatgagpgk vlgvglgvpg pidgesgvig atsmlpgwvg snpgkemser
      181 lgvpvhvdnd anlgalgelv wgaargvadl ayvkvaggvg aglvmggriy rgpggtagev
      241 ghltldesgp vcrcgnrgcl etfaavpyvl pllepahgpg ltmdrvvala regdpgcrrv
      301 iadtgrhvav gvgalcnlln prvvvvggei aeagelllep lrsaltryti ptaarhltvv
      361 kgalgaraev lggialvlse mgepallpgs apgirpvl
//
LOCUS       WP_006346786             290 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Streptomyces].
ACCESSION   WP_006346786
VERSION     WP_006346786.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..290
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30315
     Region          1..257
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mridlhthst asdgtdtpae lvrnaaaagl dvialtdhdt trghaeaiaa lpgldrpltl
       61 vtgaelscav dgiglhllay lfdpdepell arrellrddr vpraraivar lrelgapvsw
      121 eqvariagdg svgrphiaaa mvelgvvptv sdaftaewia dggrawvakh eldpftairl
      181 vkaaggvavi ahpaavkrgr tisdatiael aeagldgiev dhqdhdeptr arlrglaael
      241 gllttgssdy hgsrkdiplg hfttdpeiyg eitrratgaf pvpgaggspa
//
LOCUS       WP_006348646             743 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate--CoA ligase family protein [Streptomyces].
ACCESSION   WP_006348646
VERSION     WP_006348646.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 743)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..743
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=78129
     Region          53..739
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mlgsthgtlt sglrarvvac gepphdtvhd aasvvasagd tdvsgrplya pvpdldrffr
       61 pssvavvgas daegrpntgi trqlvawagr vgarlhpvhp srsevfgipc vprigavaep
      121 vdlavllvgd plplvdelae akvkfavafa agyaetgedg aaaqarlaaa veragirllg
      181 pntnlnafee frddldgpai alitqsghqg rpvftlqelg irlshwaptg neadletadf
      241 isyfaerpev gaiacyvegl kdgrafllaa draarrgvpv vavkvgrtet gartaashtg
      301 kltgadrvvd samrqygvir vdgldelqdt sallararap ladgvvvysi sggtgahfad
      361 lataagltlp rlsaarqtel hqwipddlnv anpvdngghp vgdwrgrkii dailadpavg
      421 vlicpitgpf ppmsdrlaqd lvdaaertek lvcvvwgspv gteaayretl lgssrvatfr
      481 tfancitavr ayldhhrftt gylspfdeap rshspsfrka qallkpgarl sehgakqllr
      541 aygirvpreq lvtsaaaavr aagqvgypvv mkasgsllah ktelglvkig ltsasqvrda
      601 yrelteiarc egtdldgilv cqmvergaem vvgvtqdalf gptvtvglgg ilvevlrdta
      661 vrvppfgevq aramlaelrg ralldgvrgg ppldvdalve vilrvqrmal elggelseld
      721 inplmvlprg qgavaldala vcr
//
LOCUS       WP_006348828             250 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease family protein [Streptomyces].
ACCESSION   WP_006348828
VERSION     WP_006348828.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            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="HNH endonuclease family protein"
                     /calculated_mol_wt=26530
     Region          110..247
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mensrktpit yaiallgaav lltgcesdts pdaegargsg pgavgplanp dgtrpglapv
       61 adgdraaark ligslatkgr gpgtgyerek fgrawsdtad gvplarngcd trndllrrdg
      121 relrfrdgsd cvvvamtlad pytgkdivwk kakaaevqid hvvplaygwr mgaarwpadk
      181 rerfandaln llpvdgranq akrdsgpasw lppnkgvrca yavrfaqvak eyalpvtapd
      241 rnmmlkqcgs
//
LOCUS       WP_006350508             385 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: exonuclease SbcCD subunit D [Streptomyces].
ACCESSION   WP_006350508
VERSION     WP_006350508.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..385
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41167
     Region          1..270
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          266..357
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrflhtsdwh lgrslhrvsm lgaqsafldh lvdraraldv davlvagdvy dravpplaav
       61 elfdralhrl adagvptvmi sgnhdsarrl gvaagliera gihlrtdpag catpvvltdd
      121 hgdialyglp ylepalvkde fgvararhet vlgaamdrvr adlatrptgt rsvvlahafv
      181 aggaasdser ditvggvaav ppavfdgvdy aalghlhgcq tltdrvrysg spiaysfsea
      241 ahrktmwlid lgaggavtae ridcpvprpl arltgrlddl ledpaherhe dsfveatltd
      301 pvrpaepmar ltrrfphtls lvfaperppe ddtpsyarml rgrtrqqiae dfvahvrgag
      361 pddaeravls aafdavrtae aeaag
//
LOCUS       WP_006350769             436 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TerD family protein [Streptomyces].
ACCESSION   WP_006350769
VERSION     WP_006350769.1
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 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..436
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=45539
     Region          31..436
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 msmlkgantp vtarrvrvel swstgpsvpe vdvsallldt gsgrvrsdrd fvfynqpeha
       61 sgavrhegre tgpgtatdav avdldrvepg igrivlaasa gggsfgrvpg lsvrvvdaas
      121 gaelarydst datvetalla gelyrrqgaw kfravgqgys tglaglatdf gitvdaarpa
      181 appppvttrp aapapaattr tpapapvpps prpapaappa pssapvrltk vtltkeaptv
      241 sltkqggtsg alkvnlswqv rkqfkgwgak lgraialhgd ldldlcalye ladgskgvvq
      301 algnafgslh rppwihldgd drtggssgen ltvnldhsrd frrilvfvtv yegarsfadl
      361 datvtlrpqh gasidfslge ctvpstvcal alitntgsdl vvqreanflv pqrgvspqrt
      421 vdhaygwgmn wtpgrk
//
LOCUS       WP_006351645             304 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Lactobacillus
            amylolyticus].
ACCESSION   WP_006351645
VERSION     WP_006351645.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus amylolyticus
  ORGANISM  Lactobacillus amylolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 304)
  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 304)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10097223
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Lactobacillus amylolyticus"
                     /db_xref="taxon:83683"
     Protein         1..304
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33187
     Region          7..284
                     /region_name="TBP_aldolase_IIB"
                     /note="Tagatose-1,6-bisphosphate (TBP) aldolase and
                     related Type B Class II aldolases. TBP aldolase is a
                     tetrameric class II aldolase that catalyzes the reversible
                     condensation of dihydroxyacetone phosphate with
                     glyceraldehyde 3-phsophate to produce tagatose 1; cd00947"
                     /db_xref="CDD:238477"
     Site            order(28..30,33,53,56..58,63,67,70..71,231..232,234..235,
                     238,242,245)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238477"
     Site            order(86..87,176..178,180,206..207,209,228,230..231)
                     /site_type="active"
                     /db_xref="CDD:238477"
     Site            order(87,177,206)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238477"
     Site            order(176,178,180,207,209)
                     /site_type="other"
                     /note="Na+ binding site [ion binding]"
                     /db_xref="CDD:238477"
ORIGIN      
        1 mayfdngnqi fkdarrehya vgayntnnle wtraelraae etrtplliqv stgaakymgg
       61 ykfvkdmvad qidsmnisvp vilnldhgdy esakecialg yssvmfdgha lpveenlakt
      121 keiiklaher gisveaeigk igenqgadgg elasvedait fykagvdkla cgignihgvy
      181 pegwkglnfd rlkeiadavp vplvlhggsg ipedqvkkai slgiakvnin tefqlafqka
      241 trkyiedkkd ldtankgydp rklllpgtea itaamkemis wlgtksidde lkdasfdras
      301 lnee
//
LOCUS       WP_006357360             275 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Gordonia alkanivorans].
ACCESSION   WP_006357360
VERSION     WP_006357360.1
KEYWORDS    RefSeq.
SOURCE      Gordonia alkanivorans
  ORGANISM  Gordonia alkanivorans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Gordonia alkanivorans"
                     /db_xref="taxon:84096"
     Protein         1..275
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30551
     Region          94..261
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mkprrdtfae dyiretvaav ldaandsnfs qlelcwfedv lnayfdatvs sssniiaear
       61 rqyafrlnqa pagrelcapr rvsdgkspvs iedlreladl resvrhytse pvptcvvdea
      121 idvalqspta cnrvpwqirv ftnssevhei asiamgtagy ikslshiavl vgdlsayshd
      181 rdrhliyidg slaamsfila lraqnisscc inwpdirnre irmakrlglq pyqkvvmlia
      241 fgyadedaiv pfsgkrdles vrkfgelsvs gdevn
//
LOCUS       WP_006330746             180 aa            linear   BCT 20-JAN-2025
DEFINITION  transcription termination/antitermination protein NusG
            [Mesorhizobium sp. STM 4661].
ACCESSION   WP_006330746
VERSION     WP_006330746.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. STM 4661
  ORGANISM  Mesorhizobium sp. STM 4661
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Kang,J.Y., Mooney,R.A., Nedialkov,Y., Saba,J., Mishanina,T.V.,
            Artsimovitch,I., Landick,R. and Darst,S.A.
  TITLE     Structural Basis for Transcript Elongation Control by NusG Family
            Universal Regulators
  JOURNAL   Cell 173 (7), 1650-1662 (2018)
   PUBMED   29887376
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Liu,B. and Steitz,T.A.
  TITLE     Structural insights into NusG regulating transcription elongation
  JOURNAL   Nucleic Acids Res 45 (2), 968-974 (2017)
   PUBMED   27899640
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Steiner,T., Kaiser,J.T., Marinkovic,S., Huber,R. and Wahl,M.C.
  TITLE     Crystal structures of transcription factor NusG in light of its
            nucleic acid- and protein-binding activities
  JOURNAL   EMBO J 21 (17), 4641-4653 (2002)
   PUBMED   12198166
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415705
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Mesorhizobium sp. STM 4661"
                     /db_xref="taxon:1297570"
     gene            1..180
                     /gene="nusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
     Protein         1..180
                     /product="transcription termination/antitermination
                     protein NusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
                     /calculated_mol_wt=19704
     Region          14..179
                     /region_name="NusG"
                     /note="Transcription termination/antitermination protein
                     NusG [Transcription]; COG0250"
                     /db_xref="CDD:440020"
ORIGIN      
        1 mdkantssqr pavspatrwy aasvfpgkes iaewhlqrqg fhsfvpryek ttrharrlet
       61 rsaayfpgym fvaldvtlqr wrsvngtlgv rslvmqrdrp lpvpsglver fialtgkdgl
      121 ldfrgglaag asvkivsgpf aemigrldrl dpagrarvlv aimngevpvd ldardlvaia
//
LOCUS       WP_006357410             292 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Gordonia alkanivorans].
ACCESSION   WP_006357410
VERSION     WP_006357410.1
KEYWORDS    RefSeq.
SOURCE      Gordonia alkanivorans
  ORGANISM  Gordonia alkanivorans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Gordonia alkanivorans"
                     /db_xref="taxon:84096"
     Protein         1..292
                     /product="formate/nitrite transporter family protein"
                     /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=31421
     Region          2..265
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msyvnpsefa vkmvdageak vflstrdtii raymagaila laaafavtvt vrtgepllga
       61 llfpvgfcll ylmgfdlltg vftlvplali dkrrgvtvks mlrnwswvfl gnflgaftva
      121 vmmavivtyg fsvdpdevgr qlgeighsrt vgyaehgaag mltlfirgvl cnwmvstgvv
      181 gammstslpg kvlamwmpvm vffymgfehs ivnmflfpsg lmlggdfsig dylvwneipt
      241 vignlvgglt fvgftiyith artaadrrpv shdetaevdv aapaeiesvk tv
//
LOCUS       WP_006358106             161 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LytR C-terminal domain-containing protein [Gordonia].
ACCESSION   WP_006358106
VERSION     WP_006358106.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 161)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..161
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=16340
     Region          69..154
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mnadrepnrl plragammlf avavvfiglg whsaatsgse pqatettata tptpasttss
       61 tsassttkrv cvinagqvsg lasdvsdllk ekgytmaqpg nytaggfsen tifydsdsdk
      121 aqadelakal ggtvsveerp ssftrckggv pvivvtavsg s
//
LOCUS       WP_006359323             331 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Gordonia
            alkanivorans].
ACCESSION   WP_006359323
VERSION     WP_006359323.1
KEYWORDS    RefSeq.
SOURCE      Gordonia alkanivorans
  ORGANISM  Gordonia alkanivorans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Gordonia alkanivorans"
                     /db_xref="taxon:84096"
     Protein         1..331
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=36027
     Region          1..321
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvigank rygdfaaldd vsidipdgql tsllgpsgsg kstllraiag ldtldsgivr
       61 indndvsqks pqkrdigfvf qhyaafkhlt vrdniafglk irkrpkkevd akvdellevv
      121 glavfqhrfp aqlsggqrqr malaralavd pkvllldepf galdakvrdd lrrwlrrlhe
      181 evhvttvlvt hdqqealdvs driailnkgr ieqvgtpddl ydrpanefva sflgstvrln
      241 gelvrphdir igrtpemasp aadasldtgv ikatvlrvvn lgfetrvelv aattgdefaa
      301 qitrgdqnal nlqagetvya ratkvaalte a
//
LOCUS       WP_006360079              99 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Gordonia].
ACCESSION   WP_006360079
VERSION     WP_006360079.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..99
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10512
     Region          5..96
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(27,55..56,58,80)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(27..28,36,38,40..41,43,46..47,55,60,65)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 maaiteeqve avralvaeip vgqvstygdl agaaglsspr ivgwimrtdt adlpwhrvvp
       61 asgrpaphla nrqlerlaae gvpivggrir lrecrwaip
//
LOCUS       WP_006361408             401 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Slackia exigua].
ACCESSION   WP_006361408
VERSION     WP_006361408.1
KEYWORDS    RefSeq.
SOURCE      Slackia exigua
  ORGANISM  Slackia exigua
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Slackia.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Slackia exigua"
                     /db_xref="taxon:84109"
     Protein         1..401
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44055
     Region          1..398
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkilvlnags sslkyqliet dtqtmlakgl cervgsknsy ikhgadkder ifhqfmadhe
       61 ealrvvfdal thsdrstits idqidaighr ivhggdffde svlidqdvid kiarlsplap
      121 lhnppalaci evcqklapgm pqtavfdtaf fqtlppsaym yplpyelcrv hrirkygahg
      181 tshryiahrc aallgrpied lkivtchlgn gcsisavdhg iavdtsmgft pldglmmgtr
      241 cgsidpaiip flienenlsa aevndimnkk sgllgvsgis ndvrdvtdaa msgneravla
      301 ydmyahsirk ylgqyivema gvdaivltag vgenaerirr lifaglqplg ivldqeknrl
      361 rhngkerfis rdespvkiiv iptneefmia qdtydivsrl p
//
LOCUS       WP_006361679             212 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Stenotrophomonas maltophilia].
ACCESSION   WP_006361679
VERSION     WP_006361679.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas maltophilia
  ORGANISM  Stenotrophomonas maltophilia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas; Stenotrophomonas
            maltophilia group.
REFERENCE   1  (residues 1 to 212)
  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 212)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 212)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Stenotrophomonas maltophilia"
                     /db_xref="taxon:40324"
     Protein         1..212
                     /product="YfgM family protein"
                     /function="Uncharacterized protein conserved in bacteria"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22326
     Region          1..200
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 maiddlldeh eqservrswl rkngasilgg vviaigaiag wqwyqkdqgg klasanveyq
       61 kalvglqqnk lddaskavka leagpssiyg dlaalqlaka qvdagkneea latlravkve
      121 gdlqrvvdqr varllvatgk sgeaikllgs atdsssleih gdalmaqgkr ddaraqyeka
      181 lktldvaapq rrlletkvmd aggtvaapae sv
//
LOCUS       WP_006362236             367 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Slackia].
ACCESSION   WP_006362236
VERSION     WP_006362236.1
KEYWORDS    RefSeq.
SOURCE      Slackia
  ORGANISM  Slackia
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Slackia"
                     /db_xref="taxon:84108"
     Protein         1..367
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=40630
     Region          1..364
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mslridirkk lasfdlevaf evesetlgfl gasgcgksmt lrciagveep degiievngt
       61 tyfdsaagid lspqkrktal lfqsfqlfph ltvadniaag igrdageadr aaavarqirr
      121 fsleglekrf pyrlsggqqq rvalarmiaa qpgilmldep fsaldahlks eleqdllalf
      181 esfegsilyv shdideafrf cdriavveeg hireiapkrd ivsdpqtlat irlsgckntt
      241 eaqkagdhev flpsfgvtvr caqnvpddvr ffgvrafrir rarhegrnvf rvrvdrasds
      301 rfertvmvsf ldgapissga adeserfaqt hlqwkvdkla tceadvpckg dellieipee
      361 fvyvvtr
//
LOCUS       WP_006364448             378 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Gemella sanguinis].
ACCESSION   WP_006364448
VERSION     WP_006364448.1
KEYWORDS    RefSeq.
SOURCE      Gemella sanguinis
  ORGANISM  Gemella sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Gemellaceae;
            Gemella.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Gemella sanguinis"
                     /db_xref="taxon:84135"
     Protein         1..378
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43737
     Region          1..265
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          262..352
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkfihtadwh igrklqgidl lldqqfvlen liadikkdni dfiiiagdly drsvpskeat
       61 illqellvel niennipifa isgnhdsrer lavgeawfsk hdfylhtelk qafnkieykd
      121 adiyllpyfe pyearayfdd dsltthnsat krvideiykn ldetrinilv ahtfvaggle
      181 tdsereisvg tvenvaveif ekfdyvalgh lhnpnalnne kikysgspla ysfseakntk
      241 gyrlvdiskd tlneefielk qkrkmhnvva dyndifskef qekfnykedf fsmelsgleg
      301 vtdpmprike yypntlqlks ktkkensdkn ydkkeiltks pleliegfyr deigeelskk
      361 qrdtlvtlvk evevdetn
//
LOCUS       WP_006365153             257 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Stenotrophomonas maltophilia].
ACCESSION   WP_006365153
VERSION     WP_006365153.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas maltophilia
  ORGANISM  Stenotrophomonas maltophilia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas; Stenotrophomonas
            maltophilia group.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  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   3  (residues 1 to 257)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Stenotrophomonas maltophilia"
                     /db_xref="taxon:40324"
     Protein         1..257
                     /product="flagellar brake protein"
                     /function="Predicted glycosyltransferase"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28968
     Region          44..253
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 msdgndtavh dvhaadaade rflvrnprql rqllrslidq rslinahidg rdrsfptall
       61 eldededyll ldgspqeasn raaeqadhll cfaqlervlv rfrlqelqrv dndghvafra
      121 pmpdelvhlq rrelyrletp vtdspqlqlp aaedrseals mrvvdisggg lavvvptdca
      181 vfslqkrypa vlslpdgpdl eielvvcnll pqrqpngiei krvgmrfdil prggdsaiqr
      241 yifridrqrk arrngel
//
LOCUS       WP_006365572             348 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Chlorobium
            ferrooxidans].
ACCESSION   WP_006365572
VERSION     WP_006365572.1
KEYWORDS    RefSeq.
SOURCE      Chlorobium ferrooxidans
  ORGANISM  Chlorobium ferrooxidans
            Bacteria; Pseudomonadati; Chlorobiota; Chlorobiia; Chlorobiales;
            Chlorobiaceae; Chlorobium/Pelodictyon group; Chlorobium.
REFERENCE   1  (residues 1 to 348)
  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   2  (residues 1 to 348)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Chlorobium ferrooxidans"
                     /db_xref="taxon:84205"
     Protein         1..348
                     /product="aminoglycoside 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=38635
     Region          18..>200
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
     Region          187..302
                     /region_name="CotS"
                     /note="Thiamine kinase or a related kinase [Coenzyme
                     transport and metabolism]; COG0510"
                     /db_xref="CDD:440276"
ORIGIN      
        1 magaaapart dlmsfamesl elfcarfgie apftlnpvrs grnsevllig kgrkkwivkh
       61 yfqqgrdkrd rlaaefgflt flnnagvagv srplginqsl haalysflpg krpeivtarh
      121 itqaadfign insfrnsaaa rsllpaadac fsqqghirla etridrllaa lspesgveae
      181 acrfvkerlr plyerlkarv saqrspsqla eplspeeril spsdfgfhnt lelngalsfl
      241 dfeyagwddp aklicdficq pelpvsaiqa rqfteelgis lplsgslsar velllpfhrl
      301 kwcgillnef reearnrrlh agvesegmld lqlvkskryy sehlailt
//
LOCUS       WP_006367969             159 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Gordonia].
ACCESSION   WP_006367969
VERSION     WP_006367969.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            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="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16770
     Region          6..159
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 msfdiataqt gtytelaeaa aglvagehdr ianaanisal vyhslpqlnw vgfyffdgte
       61 lvvgpfqgkp acvrigldrg vcgaaartrt tqrvadvhav pdhiacdaqs rselvvplvg
      121 addeligvfd ldspvperft addqrgleai aavfvdslr
//
LOCUS       WP_006367320             357 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Chlorobium
            ferrooxidans].
ACCESSION   WP_006367320
VERSION     WP_006367320.1
KEYWORDS    RefSeq.
SOURCE      Chlorobium ferrooxidans
  ORGANISM  Chlorobium ferrooxidans
            Bacteria; Pseudomonadati; Chlorobiota; Chlorobiia; Chlorobiales;
            Chlorobiaceae; Chlorobium/Pelodictyon group; Chlorobium.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Chlorobium ferrooxidans"
                     /db_xref="taxon:84205"
     Protein         1..357
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=40054
     Region          1..351
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mgielqnitk kftdytaldn islniasgel iallgpsgcg kttllriiag lesadsgkii
       61 legkdttnlp preknvgfvf qhyalfrrln vyenvafglk vlprskrpsk seikdrvehl
      121 lklvqmewal krypsqlsgg qrqrvalara lavnprvlll depfsaldak vrqelrrwlr
      181 klhdeihvts ifvthdqeea leladrivvi nkgkieqqgt pqevydhpan afvynflgnv
      241 nvfhgrvheg mvtlgghsvd apdelknsae ktsqtfvrph eigiskirse gndlegtire
      301 irllggqigl niecegfdqp idaeiprely lnlqlkkgdr vfvtfnkvkv facdyei
//
LOCUS       WP_006368035             319 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Gordonia
            polyisoprenivorans].
ACCESSION   WP_006368035
VERSION     WP_006368035.1
KEYWORDS    RefSeq.
SOURCE      Gordonia polyisoprenivorans
  ORGANISM  Gordonia polyisoprenivorans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (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   2  (residues 1 to 319)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Gordonia polyisoprenivorans"
                     /db_xref="taxon:84595"
     Protein         1..319
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34811
     Region          27..100
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
     Region          162..297
                     /region_name="DinB_2"
                     /note="DinB superfamily; cl46334"
                     /db_xref="CDD:480674"
ORIGIN      
        1 mtdpgrdrvr elldavladd nvslsgmaag ahssefhfsr qvsrfagesp vamrrrvmle
       61 racwylrqgs svtevafdsg ydtvegfsra ysrafghpps sagadssrgh wlpapngihf
      121 hsptglyved cdgagtsagy getagnpval mvrhdlddvt alldaatgle aaeyerirlp
      181 ehrisdwqgp ddsiahvlah lvadkvpwla aieghdapad iptgldalia lhqevsgrwl
      241 alireidrhh awadrvidai ceppesflls eivahvltfa ahrrvlvrmm mrdagvdlsp
      301 dhrdpdpimw hrnrtggls
//
LOCUS       WP_006368960             270 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Gordonia
            polyisoprenivorans].
ACCESSION   WP_006368960
VERSION     WP_006368960.1
KEYWORDS    RefSeq.
SOURCE      Gordonia polyisoprenivorans
  ORGANISM  Gordonia polyisoprenivorans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 270)
  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 270)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Gordonia polyisoprenivorans"
                     /db_xref="taxon:84595"
     Protein         1..270
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28547
     Region          6..266
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mvdtsritvn csilltdlpl lhrpqaarda gfgavefwwp faaavpadrd vdafvtaved
       61 agvrlthlnf aagdlsager gllshpatga efrdsvdvai gigsrlgvvg fnalygnrig
      121 dlamevqddl aaenlafaar aaatidagil leplsgipty pltraahaid vcdrlardhg
      181 vdnaalladl yhlavngenl ddvidtvadr ighvqiadvp grgepgtgsl dlsrplaala
      241 ardypgwisl eyiptrsdtf dwvpdfpafr
//
LOCUS       WP_006371388             411 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Gordonia
            polyisoprenivorans].
ACCESSION   WP_006371388
VERSION     WP_006371388.1
KEYWORDS    RefSeq.
SOURCE      Gordonia polyisoprenivorans
  ORGANISM  Gordonia polyisoprenivorans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 411)
  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 411)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Gordonia polyisoprenivorans"
                     /db_xref="taxon:84595"
     Protein         1..411
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46330
     Region          1..410
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 maaalttaqa rrialtaqgf sdrpptgavt mrlvervvar tklfqmdsvn iavrahylpl
       61 fsrlgpydqa lldraawrpg rgrrllteyw aheaalipvd dwplfgfrma eyrdgryrht
      121 rdtmrrnrel addvraviae agpvtprrie evlgierapq aaggwwnrge vkhlceamfa
      181 sgefaatrdd vfgrhydlae rvvgadrvdr rverddahre lvrraasalg vatvadlady
      241 yrlktadvrp aiadlidsgv lqpvsvdgwr dgaylhtaat vparvrtanr ergailspfd
      301 plvffrprte rifgfhyrie iyvpehkrvh gyyvhpyllg deivarvdlk adrqrgvlmv
      361 pgvfseagqr lseiasalrr dlqvladwlg mesveigsrg dladtlrhlf d
//
LOCUS       WP_006372932             102 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Gordonia].
ACCESSION   WP_006372932
VERSION     WP_006372932.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..102
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11068
     Region          5..99
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(27,55..56,58,80)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(27..28,36,38,40..41,43,46..47,55,60,65)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 msavteddve rvralvaaip sgrvstygdl aaaaglsspr ivgwimrtds adlpwhrvis
       61 asgkpaphla hrqldrlrde gapirdgkvl mrecrweidv ld
//
LOCUS       WP_006375546             754 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate--CoA ligase family protein [Streptomyces].
ACCESSION   WP_006375546
VERSION     WP_006375546.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 754)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 754)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..754
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=80128
     Region          49..748
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mlgsthgtft tdsrrarvla cgeqpspvvh grpadvddld vsgrplyagv pdldrffrpe
       61 slavigasdt egrpntgitr qllawaervg arlhpvhptr eavfgipcfp svadlpeqid
      121 lavllvadpl pvveelaeak vrfavafasg faetgeagae aqarlsdavr rsglrllgpn
      181 tnlnafenfr edldgpaial itqsghqgrp vfalqelgir lshwaptgne adletadfis
      241 yfserpevga iacyveglkd grafllaadr aarrgvpvva vkvgrtetga rtaashtgkl
      301 tgadrvvdaa mrqfgvirvd gldqlqdtsa llararrpla dgvavysisg gtgahfadla
      361 teaglnlpql sagrqaelhq wipdylnvan pvdtgghpvg dwrgrkiida iladpavgvl
      421 vcpitgpfpp msdklaqdlv daaeqtdklv cviwgspvgt esayretllg ssrvatfrtf
      481 ancvtavrah ldharftasy rspfdeaprt pspsfrkara lmrpgetlse haaklllray
      541 girvpreqlv tsaaaavraa glvgypvvmk asggqiahkt elglvkiglt sasqvrdayr
      601 eltdiaryeg vdldgvlvcq mvergvemvv gvthddlfgp tvtvglggvl vevlqdtavr
      661 vppfgeeqar dmltelrgra lldgvrgrpp adldalvevv mrvqrmalel gdelaeldin
      721 plmvlprgqg avaldalavc gpgpdgqdvn qqpl
//
LOCUS       WP_006375867             308 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Streptomyces].
ACCESSION   WP_006375867
VERSION     WP_006375867.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..308
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31403
     Region          113..303
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mraqrriatv attalaltla lgsaaltast aqaatpnags lrhtdgelwy kanagqanrl
       61 tvsvkietre nefdayyilt frdrapisid aaaaaqdecv ypsaddhtva rcavgiplgs
      121 ddsddydvdl gdgndtvtia anssayatiy ggkgndvltg tssevlygqd gndrlvgggg
      181 iwgagaygga gndvftgcsv achggagndt ltgstdpdgn enslfgddgn dvlhgqagan
      241 flyggkgndr lyggndndrl ygeqgndtly gekgndtlyg nsgndvlhgg agkdtlsggp
      301 gtnkvyqn
//
LOCUS       WP_006376153             400 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator, partial [Streptomyces
            turgidiscabies].
ACCESSION   WP_006376153
VERSION     WP_006376153.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces turgidiscabies
  ORGANISM  Streptomyces turgidiscabies
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Streptomyces turgidiscabies"
                     /db_xref="taxon:85558"
     Protein         1..>400
                     /product="AfsR/SARP family transcriptional regulator"
                     /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]"
     Region          1..254
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mefkvlgpme vvsggrslpl ggvkqravlg llllranqvv atsqlldalw peesrpvtar
       61 kmvqnavwgl ralletgdge rpdgstppql ltrapgyvlr vdperldatr feravtagra
      121 rldagepaea avllggalae wrgsalsdla eegmewaelt alrqlrldam edrfeaelac
      181 grhhavlgel tslaeaeplr erlcgqlmla lyrcgrqaea lsvfsgvrla lveeygleps
      241 aglqtlqhri lrhdqtlasp aggraepggt etrasrrhpv aeagrvrtpa riaavasaap
      301 gtgaaadtgp qtvpahdfap peeeeprasr plgvaeagav aerrdvcvlv vctesaadaa
      361 tmeseqldts lhdavtvlte svearsgtvv gsmgglcaal
//
LOCUS       WP_006376187             703 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Stenotrophomonas
            maltophilia].
ACCESSION   WP_006376187
VERSION     WP_006376187.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas maltophilia
  ORGANISM  Stenotrophomonas maltophilia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas; Stenotrophomonas
            maltophilia group.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Stenotrophomonas maltophilia"
                     /db_xref="taxon:40324"
     Protein         1..703
                     /product="TonB-dependent receptor family protein"
                     /function="Outer membrane receptor proteins, mostly Fe
                     transport"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=76731
     Region          34..702
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mslsphrltp sllflavslv lasttaaapq attldavqvt aaadasaqah ealkrvpgas
       61 nvidvakads rlsssadvla yqpgisaqsp gnegtkisir gsginrgpga hasgiavsid
      121 glpltgpggt pyelleplwl srvevlrgan gfergalalg gaidyvsrsg rdsagvqlhy
      181 eagsrgyqkr giswggvngd vdyflaytdt efdgyqrhar gdgkgamani gwqitpglqt
      241 rffvryretn hetpgrltrd qirndpraan aanlaidarr pqpgstwvgn vttlqideds
      301 slqaglvyht ypmdlnesly rqqldyanln atldyrhrhr lfgldsettv glrvthdlda
      361 dvreslrfas ngygagtrtr dfrhhgtdst lhvgniltfn drlrmqtgla lintrrdvqv
      421 twpssggrlr dhdwdyaprl gftwqhsaqt qwfgnlsrsv eaphpwsmiw gsnqyfgpgn
      481 gpstgrqrap vpmqnqtatt lelgargdag lgrweltgyy ahvnhellsv elqpvpnlfi
      541 aennasptvh rgieagldst lwqaapgrls lrqaytfsdf ryrhdarfgs nrlpglpmhs
      601 yqaelrfdha sglyaalnse yasriavdya nsywadshvi fgsrigydap ggrwqawaem
      661 rnignrhyaa tvtpgyddag kdvarstpge grgiyagvrl rfd
//
LOCUS       WP_006376235             326 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Streptomyces].
ACCESSION   WP_006376235
VERSION     WP_006376235.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (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   2  (residues 1 to 326)
  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 326)
  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 10617438
            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="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35034
     Region          17..70
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
     Region          <92..249
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
ORIGIN      
        1 msiqlmiaaa ylppdvlsqs qklalmkiad saddetrlar pgltrlaawv gvtdkraiti
       61 vteliakglv ervevgkagr savyrifplg vpptpttpel kerlearkaa pknpnkarpg
      121 vtrsvpakpa mtyqdvddre aarrekaess qveagfhagn pdeeagfhgg npdgedgrvp
      181 pvepdefhgg nplgssggtp sfpgsssvlp spptptadaa gefasappdg saaergeppr
      241 gctkhrgrpa ascrgcgtnp ragrrreqee akeeeqrvhg rfwddwyeea arrrqrveeh
      301 peaadearka araavraqke rsqrkt
//
LOCUS       WP_006345012             305 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces sp.
            SID5473].
ACCESSION   WP_006345012
VERSION     WP_006345012.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. SID5473
  ORGANISM  Streptomyces sp. SID5473
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 305)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Streptomyces sp. SID5473"
                     /db_xref="taxon:2690299"
     Protein         1..305
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=33072
     Region          21..269
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mrtrsvmdga attppapapa evrlnllgpl evtrgpdvls lggprrraal gclllrcnev
       61 vpasrlital wgagappsar kgvqnvvwhl rtalsaadgs tgprlltrpp gyllragtdq
      121 vdllrfqela argralcadg llpaasrtwr ealelwrgpa lsdlvetgvs wpelraleea
      181 rldvfedyvd aelrlghhhh vlpklrrvar darhrerlpa hlmtalyrcg rrnealavyr
      241 dfttgladel glepgrelrd lhrailshdp gllrpshets aligaarrps ghpalpagqd
      301 gpvhp
//
LOCUS       WP_006378307             416 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Streptomyces].
ACCESSION   WP_006378307
VERSION     WP_006378307.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 416)
  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 416)
  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
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 416)
  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   5  (residues 1 to 416)
  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   6  (residues 1 to 416)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 416)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 416)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..416
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42202
     Site            order(9..10,14..16,27..29,38..41,43..44,47..48,50..51,
                     64..66,71..73)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Region          11..55
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Site            order(27,30,80)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
     Region          76..396
                     /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 mpaspstara indrlalrll qqegplaawq lkqltglsrp tvadlverlt vagliavvge
       61 sgeqrrgpna kvygivadla hlaaldvrte gvsvvvtdlv ggvlaeasvp igddtgtgpa
      121 veqavalver aakeagavgv ppregvrawg rlhtvgigap glidpatgel rdtgglpvwh
      181 rrlvtalqer lpetrviven etnlaalaeq rdgaardrdt fvllwlghgt gaavvldgtl
      241 rrgasggtge igflpvagtg rlpsatdceg gfhslaggaa ivqlagaqgl vadidvhepy
      301 aatlvraava spgtpahvrf ldalaervai gaasvvavld pgcvvlggev graggdvlaa
      361 rveerlsrms plpaqvrasa lgggavlrga lltardraqe elfggsvgqr gnwagg
//
LOCUS       WP_006379045             293 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: aminoglycoside phosphotransferase family protein
            [Streptomyces].
ACCESSION   WP_006379045
VERSION     WP_006379045.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 293)
  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   2  (residues 1 to 293)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            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="aminoglycoside 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=31698
     Region          35..254
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mtdaappppg lrawarrqvg pitavrdvsh prpgsrvwhl elggrldvfl kaasgpvayr
       61 resfayrhav palgqgsapq liessaqhlg llltaipgrp laeldvppav rheayrqagv
      121 llarlhqage lrgehrteae ealrrtahga ekhlaaagdr vsgaerrlvl rlagellvlg
      181 pvllgflhgd awernmlwsg rrtawvdfer arfgavvqdl vamycgawse epglrpaffr
      241 gfgrelsaqe ehaltclsal davsclgwap gqgdlqvaar grraldrlmg aya
//
LOCUS       WP_006379969             713 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: molybdopterin oxidoreductase family protein
            [Streptomyces].
ACCESSION   WP_006379969
VERSION     WP_006379969.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 713)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 713)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..713
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=76274
     Region          5..709
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 metpvtpthc pycalqcgmn ltpvagggvt vservdfpvn rgalcgkgrt apallsptlr
       61 lteplvrrdg vlvpasweea ldrvaegltr trtehgpdac gvfggggltn ekayalgkfa
      121 rvvlgtsqid yngrfcmssa aaagnkafgm drglpfpmed ipktgcvilv gsnlaetmpp
      181 alryfaelke nggtlividp rrtrtaeqad lhlaprpgtd lalalgllhl vvsqgrtdea
      241 fieertsgwe etraaamahw peyveritgv pvpqlreavr mfcaptdamv ltargpeqqs
      301 kgtdtvsawi nlclatgrsg rpysgygclt gqgngqggre hgqkadqlpg yrkltdpear
      361 rhvagvwgvd pdslpgpgls ayelldalgs dirslllmgs npvvsapraa hiqqrlesld
      421 flavadvvls etaaladvvl pvtqwaeetg tttnlegrvl lrrqavtppd gvrsdlyvlh
      481 qlaaragvek gfpvdpeevf eelrrasagg iadysgityr rlaeengvfw pcpapdeqeg
      541 gregpqqggh gdvaprtaph pgsprlfldr fatedgrarf apvtyrpiae epdaeypvll
      601 ttgrvvaqyq sgaqtrrvde lnaaapgpfv elhprlaarl gagegdaiav vsrrgravap
      661 arittsirpd tvfmpfhwpg egrantltnp aldptsrmpe fkacavrlet vrp
//
LOCUS       WP_006382616             214 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease family protein [Streptomyces].
ACCESSION   WP_006382616
VERSION     WP_006382616.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..214
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=23146
     Region          <116..208
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mpkfyarrrl silaaltgli asvgllngpt asaalptpvs aatartylas ltvkaenrtg
       61 ydrdlfptwi tisgtcntre yilkrdgsnv vtnsactats gswyspydga twtaasdldi
      121 dhlvplaeaw dsgasawtta qrqgfandvt rpqliavtdn vnqsksdqdp aewmpsltsy
      181 rctyvrawvq vkyyydlsvd saeksaltsy lasc
//
LOCUS       WP_006383308             296 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Streptomyces].
ACCESSION   WP_006383308
VERSION     WP_006383308.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..296
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28466
     Region          94..>289
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mgrkallrvm vvaamagsav tltggpasaa tgvfksgtni vvnaaqgran nitvslsgnf
       61 viiqdtadtl taglnctllv ngtvacpvav nsdtvvvnag dgndvitktg nvrgdlkges
      121 gndvinggps pgsnilngga gndtlnggvt fdllnggpga drlsggggts diasyfesgs
      181 gvvvdidnaa ddgiggegdn vltdveivyg sqfgdtltgg tagdilsgfa gndllvggag
      241 ndtlvggagn dthsggagnd tldgvdsvfd ndslnggant dtctadtsdt ksacea
//
LOCUS       WP_006383813             553 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Streptomyces turgidiscabies].
ACCESSION   WP_006383813
VERSION     WP_006383813.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces turgidiscabies
  ORGANISM  Streptomyces turgidiscabies
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 553)
  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 553)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Streptomyces turgidiscabies"
                     /db_xref="taxon:85558"
     Protein         1..553
                     /product="M4 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=57711
     Region          36..553
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 msrtqrtphv qrirgsrlaa agttvgvaal laaalsptad aadrptrdta irnavtalad
       61 qathlgltsl qntkvrdviv dkdgsqhvry drtyrqlpvl ggdfvvhlap ggayrsasra
      121 ttrpislati spsvsapkaa dlavsalraa npgetlnktt skpqlvvdal hgtpklawqt
      181 namaldsvgn pvartvltna rtgaqidawd sietatgdgk slyggtvple ttvsgstyql
      241 kdptrgntyt gdaengtdlc ifgicirrap atlftdtdnh wgtgatadra saavdaqygt
      301 dmtwdyyknt fgrsgikgng vgsynrvhyg snynnafwdn scfcmtygdg dgttfgplvs
      361 ldvaghemth gvtsstanlt ysgepgglne atsdifgtlv efsaanstdl gdyligekvv
      421 rsgfgkpalr ymdqpskdtk sancwssavg sldvhyssgv anhfayllae gsgakslngv
      481 dynsptcngs tvagigrakl gaiwykaltt ymtsstnyag artatlnaar dlygtgstey
      541 aavgaawsav svg
//
LOCUS       WP_006384199             371 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein, partial [Achromobacter
            xylosoxidans].
ACCESSION   WP_006384199
VERSION     WP_006384199.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter xylosoxidans
  ORGANISM  Achromobacter xylosoxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 371)
  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 371)
  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 371)
  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 371)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Achromobacter xylosoxidans"
                     /db_xref="taxon:85698"
     Protein         1..>371
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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]"
     Region          8..359
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mqhvtkprrk fisgaaaaga aalafpavtr aqnapislrf qstwpandif hefardyaqk
       61 vndmaggqlk ievlpagavv kafdlldavs agtldgghgv vaywygknta valwgsgpsf
      121 gmdanmllaw heygggkell veiqkamgvn vvslmygpmp tqpfgwfkrp iskiedvkgv
      181 kfrtvglaid mytamgaavn alpggeivpa ldrglldgae fnnassdlal gfqdvskicm
      241 lqsfhqsaeq fevlfnkaky dalpehlkhi lsyaaqassa dmswkasnry sqdyvklqkd
      301 hnvkfyktpd ailqqqlkiw demiakrsae nplfkkvlds qrafaervgr whgdttvnyr
      361 mafnhyfsrg g
//
LOCUS       WP_006384200             207 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Achromobacter].
ACCESSION   WP_006384200
VERSION     WP_006384200.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter
  ORGANISM  Achromobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 207)
  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 207)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 207)
  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   4  (residues 1 to 207)
  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   5  (residues 1 to 207)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Achromobacter"
                     /db_xref="taxon:222"
     Protein         1..207
                     /product="TRAP transporter small permease subunit"
                     /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=23324
     Region          1..170
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mirfirfidr istfvgktfa wliviltlhv cwevgaryll nqpsawafdl qmmyygilfm
       61 magaytlakn ghvrgdilyg flpprvqagl dlilfivffi pgvialvwag whyagysiai
      121 rehsslmang ppiypfkafi pvagaflllq gvaeilrcvl clrrgawpsr eedveevdvd
      181 klkemvhvkd ediarldryv ksggpaq
//
LOCUS       WP_006384979             805 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Achromobacter xylosoxidans].
ACCESSION   WP_006384979
VERSION     WP_006384979.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter xylosoxidans
  ORGANISM  Achromobacter xylosoxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 805)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 805)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 805)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..805
                     /organism="Achromobacter xylosoxidans"
                     /db_xref="taxon:85698"
     Protein         1..805
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87669
     Region          54..101
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          82..802
                     /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 marmqlkavp alvawalaap vaqaqpqaap mqfsiaaqpl dralrlfseq srhqvlfdea
       61 avagqqapai egrytpreal drllagtnvr vngsrpdvft ltaigrpssd avtlqpvtvs
      121 ggslrdptte ltgsytsgal tigkltqsir etpqsvsvit rqqlddknlt tldealaqtt
      181 gvtktarnfg nhkfsirgft vddnnylvdg vagivyapvg wlpidtavfd rvevlrgagg
      241 lmlgsadpsg ainmvrkrpr geghlemntt agswdnyrme fdgggpinaa gtvrgrlvta
      301 yqdrhyfydg tksrsplfyg vidadvgqht tltfgarhqa tdtdgywlfg lprytdggal
      361 dikrstsliq dwnrqtgqvd eifaeaehrf skdwkarlsl nstevdldqr vaipiggvdr
      421 asgrgssfyt vyfnrarvrs dgvdlnttgn fqalggshqi llgaswarqr inqksaslda
      481 dmpidvydpd hsaipkparp awdsketarg eqaalygnlr lqladplhll lggrlswlky
      541 qstngltgar trdyqqrhef tpyaglvydl drqwsvytsy adtfqpqssy vtssgspldp
      601 aiganyeagi kgelydgrln lsaavfavkk sgiavvdesn pggctgslas sdcyrngstl
      661 rskgfeleas gelspgwqvm agytfvtsrd degetisaet prhlfrlstt yrlpgrwnaf
      721 svgggvsaqs gysypayddt svrmgapgra vwdlragyri dkhwslalnv anvfdkhyyg
      781 mvsqirrgnh fgeprnvmlt lrgtl
//
LOCUS       WP_006385222             265 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Achromobacter].
ACCESSION   WP_006385222
VERSION     WP_006385222.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter
  ORGANISM  Achromobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  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   3  (residues 1 to 265)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Achromobacter"
                     /db_xref="taxon:222"
     Protein         1..265
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29309
     Region          75..265
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mldasdpefl ltrpedmraa lfelthpdsh ilvrdaadre mavlvlgadk qtrqffwrpr
       61 dyagadfeqs dsmgllsgtt fhfnataygg vqirfrvarp evihfddgsa almspfpdrl
      121 ariqrrkmfr aslvssasrc haswrpapaa kpisfsvrdi svdgvglrve lavptlpqrg
      181 avledvqldf gelgklnanl evrnvypvsg qpmiqaaspd epapthvslt gepplshvga
      241 vflnldarqe nwlqqvvwrl eknar
//
LOCUS       WP_006385434             682 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate--CoA ligase family protein [Achromobacter].
ACCESSION   WP_006385434
VERSION     WP_006385434.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter
  ORGANISM  Achromobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 682)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 682)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Achromobacter"
                     /db_xref="taxon:222"
     Protein         1..682
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=71765
     Region          11..679
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mfysselnla dvlfrprsia lvgasdrrds pagrplallr easyegrvyv vnpkfsvvqg
       61 eqtwddlsdl petpdhvyll gssttvlaav qacvalevpv vtilasgfse sgpqgvalen
      121 eiraallgsr trllgpsslg vvnfqngcrl sanaacagef pvgqqlvvsh sgsiigalvt
      181 rarsrgagfa glvsvgseid ltmadicast lsepsitgyi lflehlrdad rlrrfaaear
      241 sqgksvvayk lgrtaeaakl svshtgamvg edqfaatflr esgiarihhi dalpeavtla
      301 rvlgdipqqr tvslavvgtt gggsamlvde malrgvhvsr lsassvqdls qsgirygdgs
      361 vldltlagtk aevmsraldv vagsgdfdlv lvvlgssahs rpqatvapvi eafqkascai
      421 avlvmphape alalllaagv pafnapevca daiqavfkar yrdrpenpla iparrrpeel
      481 ldaigiarpp evlaswdtee plalpfdypv vmkvygegll hktdvggvvl giatpyeaaq
      541 vlaqwkasev fdgkevriqi qpmvrgvvae vlvgflrdre vgpvvtvamg gilaelseqr
      601 vlrlapvsva earemisela plkvldgyrg kprgdreala eaiaalsrla acrevveaei
      661 nplmvlaegk gvaavdvlvq gk
//
LOCUS       WP_006385601             394 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Achromobacter xylosoxidans].
ACCESSION   WP_006385601
VERSION     WP_006385601.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter xylosoxidans
  ORGANISM  Achromobacter xylosoxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Achromobacter xylosoxidans"
                     /db_xref="taxon:85698"
     Protein         1..394
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42661
     Region          3..392
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msdtilvina gsssikfyly didgkqalap rlggqlegig tghprlrvrd aagqtlverd
       61 iapshapdvp ngqevvgtwl sghlggapla vghrvvhggp dlsepvlidd ailakldtft
      121 plaplhqpnn lapirvirer rpwipqvacf dtafhrshsd vadryalpen lyqqgvrryg
      181 fhglsyeyia qrlrqalpei amgkiiaahl gsgvsacamh qgrsvdstmg ftaleglpmg
      241 trpgrldagv vlwmmeqgms hddiehvlyh dcgmkglsgi sndmrellas dapsarlalk
      301 yfawrvaegm iglgcamngi dgivftagvg ensaeirqai sehwgwlgik ldpernahhg
      361 prissddsri gvyvvrtnee liiaqhtlal vkqr
//
LOCUS       WP_006385790             791 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Achromobacter xylosoxidans].
ACCESSION   WP_006385790
VERSION     WP_006385790.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter xylosoxidans
  ORGANISM  Achromobacter xylosoxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 791)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 791)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Achromobacter xylosoxidans"
                     /db_xref="taxon:85698"
     Protein         1..791
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87361
     Region          40..91
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          68..791
                     /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 mlcpaatlaq palqadsrav dipagplgpa laayaqrmrv llsfrpaqtd glstpglsgs
       61 yaveegfarl lsgtalrvrr lpddsyalea aaaegisqla avtvlgagat tegtgaytad
      121 wmrsanglvl aqrdtpqsts ivtrqqlddq amgsvrdvme natgmnvqqs etdrlsyysr
      181 gfqmdtmqfd gvvkpldgty qfgegnldpv iydhveiirg atglmsgtgn pggsvnfirk
      241 rptrefqgsl ramggsydty rgeidlsspl tasgairari vgakerrgdt ldfyskkrdv
      301 aygiveadla pattlsagas tqrsrpkgvm wgglpifdtn gdqvdwkkgq tvgakwttwd
      361 tdsteyfaql ehgfangwng rlsysrldnd fdasllfaad fpvdadtgyl sgtptlrkyr
      421 grskqdvygg sltgdfgllg athefnlgfs hsrtrsrtkg wnssdqatyp vpnihdwhgd
      481 wpepvwdlav sdqqlrttqt gifgtarfnl gsrlhlltga rwtrweadey rwnqwspdsa
      541 pitlsqsqry seitpylgvt ydlddtytay vsytnifqpq myktrdwnmt gpayghnyea
      601 gikasylegr lngsfavfqt nqkdvaeyag fdaarneswy emldgtrtrg felelagevs
      661 pgwnlflgyt yrvskdnagr kvqttqpeqm lkasttyrlp galrdlvigg glrwqsrtra
      721 vgyygeqsaa veqqpyalfd lmaqydlgrq tqlqlnvrnl adkryyramg fynsvyygeg
      781 rttlvtlthr f
//
LOCUS       WP_006387034             337 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [Achromobacter].
ACCESSION   WP_006387034
VERSION     WP_006387034.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter
  ORGANISM  Achromobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 337)
  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 337)
  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 337)
  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 337)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Achromobacter"
                     /db_xref="taxon:222"
     Protein         1..337
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=36860
     Region          28..334
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mnttrrnlmr aagggallal apfqrtlaap qfrykyannl ppshpmnlra neaaqnilkd
       61 tggrfelavf pssqlgsdtd tlsqlragav efftlsglil stlvpsasis gvgfafpdya
      121 svwkamdgdl gahirading kglfvmdriw dngfrqvtts sraitgpddf rdlkirvpvs
      181 plwtsmfkal gsspasinfn etysalqtrv vdaqenplai iqtaklyevq kycsmtnhmw
      241 dgfwflgnrr aweklpadir evvakhinaa gmaeradvla lnnqlqakla eqglafntpd
      301 papirdalrr agfyaswkek ygdkawglle qaagsls
//
LOCUS       WP_006387856             212 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Achromobacter].
ACCESSION   WP_006387856
VERSION     WP_006387856.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter
  ORGANISM  Achromobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 212)
  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 212)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 212)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Achromobacter"
                     /db_xref="taxon:222"
     Protein         1..212
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22503
     Region          1..209
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 maydleeqek ldaikawwar ygtlvmllva avalawggww gakayqshka nqamgyfeal
       61 edaarlggad ssvrikaaaa tlreqygstg yatrgalvaa qalqaqkdvd garqqlewla
      121 gqsknpsmqa varlrlagll ldqkqydaal aqlnnapaaf aalfadrrgd ilaaqgkrde
      181 araawqsaid glgtanpltq vvqlkldals ga
//
LOCUS       WP_006388286             354 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Achromobacter xylosoxidans].
ACCESSION   WP_006388286
VERSION     WP_006388286.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter xylosoxidans
  ORGANISM  Achromobacter xylosoxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Achromobacter xylosoxidans"
                     /db_xref="taxon:85698"
     Protein         1..354
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39199
     Region          1..350
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msievrnlsk rfgqfralnd vslhietgel vallgpsgcg kttllriiag lesadtgsvl
       61 fagedatavd vrqrqvgfvf qhyalfkhmt vfenvafglr vkhrsqrppe dqirrkvhdl
      121 lnlvqldwla drypaqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 rlhdelnvas vfvthdqeea levadrvvlm nagkieqvgt prevwegpat pfvygflgdv
      241 nqlqgvasrg vwegaglslp apelaqaeaq ratayvrphe fdieryraga agipvrlsha
      301 ylagpsayle lasedsdavi eaevpehlyr elglrdgdvl larprrarif avqa
//
LOCUS       WP_006388516             642 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Achromobacter].
ACCESSION   WP_006388516
VERSION     WP_006388516.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter
  ORGANISM  Achromobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 642)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 642)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 642)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 642)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 642)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Achromobacter"
                     /db_xref="taxon:222"
     Protein         1..642
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=70134
     Region          12..642
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msqgsvsvpp ssnghaaggh apssraalvl galgvvygdi gtsplytlra cltglsvhtd
       61 lepahllgvl silfwmlmvv vsfkyvtlvl radnrgeggt lallelavrs regklrwvli
      121 vlgifgaalf ygdsmitpai svlsalegig ivshtldawv vplalvvlva lfaiqshgtg
      181 amgklfgpvm llwfgtlaal gawqvwqtpe vlaalnpmwg lrfivefpwi sfvllgavvl
      241 altgaealya dmghfgrpai rsawfsmvlp altlcyfgqg alllrdpsai rnpffmmape
      301 wglaplvala tvativasqa visgaysvtr qavqlgfwpr mqilhtsave kgqiylpqvn
      361 alllcavlvl vllfrnsdnl aaaygfavtg tmlttsvlaf avlprgttga krmlwfvvlg
      421 llllfdvllf sanvfkiheg gwlplvvaiv vftlmmtwrr grrllsdmqq rdrqplkefm
      481 eqleayppsr vpgtaifmtm nsgnvppall hnlkhnkvlh dhvlfltirv advpyvsede
      541 rftvqkmsas swaatinygf kedpdvpeal rlvaeaypel dlepmrtsyf lsrqtvvaar
      601 kpalwrwrra vfsfmarnst rstkffkipa nrvvemgmqv el
//
LOCUS       WP_006388816             796 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Achromobacter xylosoxidans].
ACCESSION   WP_006388816
VERSION     WP_006388816.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter xylosoxidans
  ORGANISM  Achromobacter xylosoxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 796)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Achromobacter xylosoxidans"
                     /db_xref="taxon:85698"
     Protein         1..796
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86532
     Region          56..104
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          83..796
                     /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 mfcfrspasr alaalafasa vpvqaqvaqe vrsyriaagp ldvaltqiar tagavisysp
       61 elvagkmapa vagdltlrqa agraladsgl elstaadgtl tlrrsaagva tlapvnvega
      121 tlgpvtegsg aytigsmsta tkfqlsqret pqsisvvtrq qmddrgfqsl devardttgl
      181 ttrqiggger tqffsrgfei ssfladgvpl aydydtqgva tlamydhvev lrgasglmtg
      241 vgnpsgtinl vrkrptstpq fsvttsagsw dnyrgevdgs gplnasgsvr argvvayqds
      301 rtfkkayehq rqlyygtiea dlganttlsv ggyynrednp gadwnglptr rdgsfydfnr
      361 strltpdway wnkensslfa eldhrfangw kgrvtarvlr skldmlgtyl ypledsedfg
      421 qgagqyaydk tqhsidgyls gpfqllgrth elvlggsfrr nkdddgpggw ptdynvivdp
      481 mnwdssavpk paftypwsrk ghqrlssaya ttrlsladpl tlmlgarvds yeyrmtlksg
      541 dyvdpagykv sneitpyagl vydldahhsv yaswtsifqp qnyqtatgal ldpvtgtnle
      601 agvkgeyfdg rlnasaaifq inqrnlpvtq lqstcanptq scysqagevr srgvelelag
      661 tltpgwqvma gytynqstyl kdsengpagt rydtqtprhl fklstmvtlp galnawrvgg
      721 avrlqgpisl prynvrqagy givdtvvsyq asrnldlrln vynifdkyyy qaigstqdnn
      781 hfgaprsfll takytf
//
LOCUS       WP_006389158             814 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Achromobacter xylosoxidans].
ACCESSION   WP_006389158
VERSION     WP_006389158.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter xylosoxidans
  ORGANISM  Achromobacter xylosoxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 814)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 814)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 814)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..814
                     /organism="Achromobacter xylosoxidans"
                     /db_xref="taxon:85698"
     Protein         1..814
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88240
     Region          67..118
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          94..814
                     /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 mpsvpllrhs aklaplarav aialtvlgat psaqaqavss aqasrhyevp pgplglalsr
       61 faaqagvvls fdatltqgrq saglqgdygv aaglaamlsg tgleavnqgg nryglraana
      121 qtlapvevlg arepapsegt dsytvgvsnt atrlpmtlre tpqsvsvmtr qrltdqglnt
      181 ledaivntpg ltfkkkgsad dnekglyarg meitnmqvdg vpthkdfnal gldtalydri
      241 evvrgstgll sgagnpaasi nlvrkrptre feagvgasvg swdykrtefd lgspldasgk
      301 lrgrlvgawq eggsfidrvk qdsqllygvi eadlsertll tlgaeyqrkk ctacsyfgfp
      361 ayyadgsktn frqrfnsatn wsrqertryn vfatldhefs slwkgsltls rtgddndrty
      421 gwfssngwan pqtgqgasvw vakwpipktq naldaslsga fdalgrrhdl vlgvslsrtr
      481 gdydtyplwt apgydpvipd vrawdgdmpq pqwqatgkry ytekqnavyg alrlrptdal
      541 svilgsrvtw wdqqasytyn dgsaypdnmr eqgvytpyag lvydltptls ayasytsifl
      601 pqqaqtvsgs giapikgnty eiglksawld grlngalalf rtrqdnyamv dgdklapngd
      661 sayvaangav lrgveaelsg elapgwqmql syayvdrrlp tgfstqvglp rhiaklytty
      721 rlpgdwsalt vgggvrwesq sgftsrgpgs qqldssqsgy alldlmaryq fnrqwsatln
      781 lnnvldkkyy astniysnyy gapfsamlgv nyry
//
LOCUS       WP_006389463             674 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Achromobacter xylosoxidans].
ACCESSION   WP_006389463
VERSION     WP_006389463.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter xylosoxidans
  ORGANISM  Achromobacter xylosoxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 674)
  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 674)
  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 674)
  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 674)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..674
                     /organism="Achromobacter xylosoxidans"
                     /db_xref="taxon:85698"
     Protein         1..674
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=72154
     Region          5..669
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 meidhektqq laekydseir frplhksatw ivsgllvals lfhyytagfg llreathrgv
       61 hlafvlslif lvfgfskahy qrepkstwya pggvplydwi iaialalsvl yipyifedla
      121 frvgnplpid vlmgsillig lleatrramg wplpiialvf mayaafgpyf pgllqhagnt
      181 wsqivnhmyl tsqgvygvav gvvgtyvfhf vlfgvlatri glgqlfldva stvagryagg
      241 pakvsvfgsa mfgmlsgssv anavtvgslt ipamirigyp rhfaagveaa sstggqitpp
      301 imgaaaflmi eflgipyqqi aiagifpafl yffgmfmqvh feakreglrg ltaeempklk
      361 qsfkmrwptl iplilligvl asgrtpylaa fagitgciiv gllnpfqrlh wrdlyeafet
      421 gakyalavga aagtvgivig vvtltgvgfk isyivisaaq siagvagaii petianaqsl
      481 tlvaalimtg vvcilmgcgi pttanylimv avaaptlvql gvqpiaahff vfyfgiladi
      541 tppvalaaya aagmagsdpf ktgntafrlg itklivpfvf vfspsllisv qgftwydffv
      601 tlfgcmvglv llsaafsrym lvgmkswerw lctlgallti lpgltsglig laicipvfir
      661 qlaqlklesa pkta
//
LOCUS       WP_006389901             174 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Achromobacter xylosoxidans].
ACCESSION   WP_006389901
VERSION     WP_006389901.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter xylosoxidans
  ORGANISM  Achromobacter xylosoxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Achromobacter xylosoxidans"
                     /db_xref="taxon:85698"
     Protein         1..174
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=18973
     Region          16..171
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 meesllsavh wllgllalps vglpaifavs lisatllplg sepavfgylk lspdmfwpai
       61 lvatagntig gaisyamglg aekaverwke rhphapaerr mrgrwherah dwihrmgppa
      121 lllswlpavg dplcavagwl rlpfwpcvay maigkflryl gmtasllwlf pgqv
//
LOCUS       WP_006390133             340 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Achromobacter
            insuavis].
ACCESSION   WP_006390133
VERSION     WP_006390133.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter insuavis
  ORGANISM  Achromobacter insuavis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 340)
  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 340)
  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 340)
  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 340)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Achromobacter insuavis"
                     /db_xref="taxon:1287735"
     Protein         1..340
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=36966
     Region          30..338
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mklltrrsal rrlcalpaaa algggfplia raadyslkyg nnlpvshpln iraqeaadri
       61 lkesngrvdi kifpnnqlgg dtdmlaqvrs ggidfftpsa lviatlvpva ainavgfafk
      121 dygqvwgamd galgahvraa iaqrrlyafe kmwdngfrqt tsskapvtka admdglkirv
      181 pvsplpismf kglgaapasl qfsevysslq tkvvdaqenp lpiiqvakly evqkycsltn
      241 hiwdgywfia ngrmweglpq dlktvvargi neaglaqred ikklnasvqa dlegkgltfn
      301 qpaadsfrdq lrkagfygew qqrfgqeawg lleqavgkla
//
LOCUS       WP_006390856             394 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Achromobacter insuavis].
ACCESSION   WP_006390856
VERSION     WP_006390856.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter insuavis
  ORGANISM  Achromobacter insuavis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Achromobacter insuavis"
                     /db_xref="taxon:1287735"
     Protein         1..394
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42686
     Region          3..392
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msdtilvina gsssikfyly diddkqalap rlggqlegig tshprlrvrd aagqalverd
       61 iapshapdvp ngqevvgtwl sghlggapla vghrvvhggp dlsepvlidd ailakldtft
      121 plaplhqpnn lapirvirer rpwipqvacf dtafhrshsd vadryalpeh lyqqgvrryg
      181 fhglsyeyia qrlrqalpei amgkiiaahl gsgvsacamh qgksvdstmg ftaleglpmg
      241 trpgrldagv vlwmmeqgms hddiehvlyh dcgmkglsgi sndmrellas dapsaklalk
      301 yfawrvaegm iglgcamngi dgivftagvg ensaeirqai sehwgwlgik ldpernahhg
      361 prissddsri gvyvvrtnee liiaqhtlal vkqr
//
LOCUS       WP_006390912              83 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Achromobacter].
ACCESSION   WP_006390912
VERSION     WP_006390912.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter
  ORGANISM  Achromobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Achromobacter"
                     /db_xref="taxon:222"
     Protein         1..83
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8583
     Region          5..83
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mngatinlly farvaelvgk rseawpldge stgaqllaal gerypqlapa grlklainqt
       61 hakpsapira gdevavfepv tgg
//
LOCUS       WP_006391296             326 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Achromobacter insuavis].
ACCESSION   WP_006391296
VERSION     WP_006391296.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter insuavis
  ORGANISM  Achromobacter insuavis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 326)
  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 326)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Achromobacter insuavis"
                     /db_xref="taxon:1287735"
     Protein         1..326
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35154
     Region          54..203
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          231..310
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqlpeemkev arscdespaa aglpgpgelt gallraarqy adarldgegv aatpiegmfi
       61 lretapsplq yaitrplval vlqggkrvgm gersftfgag esllitmdvp tvsqvitasa
      121 aapyyslvve ldaavitelv gemgelplqp dhpvrvgrte aevadaalrl lrlldrprsl
      181 avlgrqlvre lhywllagrh ggairvlgva dghgrriara iemlragyar plrietlaea
      241 agmslsvfht hfrnittltp lqfqkqlrll earrrmlaeg vaigaaahgv gyesvtqftr
      301 eyarmfgqpp arniremral ahsats
//
LOCUS       WP_006392214             787 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Achromobacter insuavis].
ACCESSION   WP_006392214
VERSION     WP_006392214.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter insuavis
  ORGANISM  Achromobacter insuavis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 787)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 787)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 787)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..787
                     /organism="Achromobacter insuavis"
                     /db_xref="taxon:1287735"
     Protein         1..787
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=85844
     Region          49..98
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          75..787
                     /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 mlslrfpaac viaaaastah aqalrqydlp agrldvaltq iariagavis fradlvagks
       61 apavsgqlsv eeataralag sglelrrtpd gsltvapara ttlapvtvea atlgvtegth
      121 syttpvmsta tkfalspret pqsvsvvtrq qiedrgyqsl ddvardttgl ttrqiggger
      181 tqffsrgfei ssfladgvpl gydydtqgva tlamydhiev lrgaagmmtg agnpsgtinl
      241 vrkratavpq fsvttsagsw dnyrgevdgs gplnesgtlr argvvayqds ntfkkayehq
      301 rqlfygtiea ditanttlsi ggyynrednp gadwnglptr rdgsfydfkr strlspdway
      361 wnkentsffa eldhrfengw sgkltartlr akmnmlgsyl ypledstlfg qglgqyaydk
      421 tqysvdgyls gpftllgrth elvlggsflk nkdddgpggw pldynmtvdp ehwnssavek
      481 pafvypwsrk gyqrqvsgya ttrlsladpl tlmlgarldw yeydmqlksg dyvsppadyk
      541 vkheltpyag liydldrqht vytswtsvfq pqsnqstgga pldpvigtnl eagikgeyfg
      601 grlnasaavf qirqrnrpva letsacspgv iecyapsgkv qsrgvefeva gaitpgwqvs
      661 agytynqsky ledsgnlrag aaydtqtprh lfklstmytl pgslnawrvg gavrvqsais
      721 lpaynvrqpg ysiwdavvay ratpnldlrl nvynlfdkyy yqaigstqdn nhfgaprsfl
      781 ltakytf
//
LOCUS       WP_006392540             275 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Achromobacter insuavis].
ACCESSION   WP_006392540
VERSION     WP_006392540.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter insuavis
  ORGANISM  Achromobacter insuavis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (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   5  (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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Achromobacter insuavis"
                     /db_xref="taxon:1287735"
     Protein         1..275
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29664
     Region          20..275
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <176..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 mkddvryqpv pgtpglvlgv arlvdfefdr hyhvdyhigl vtqgvqrqnf rgrstllgpg
       61 gialmppgev hdgagvadyg qsytlktfrl spdlmrdfia evsggapger flgtlieepa
      121 laarfmalha swmadaaagp lahesaslal mgalfartga vtpqavrggl slphqravld
      181 ycqahlgdki gledlarlcg lsryqflrrf alsvgltpha wltrlrlera caalararap
      241 iaqvaadvgf ydqshfnraf rtaygvppsa yrraa
//
LOCUS       WP_006393334             709 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Achromobacter insuavis].
ACCESSION   WP_006393334
VERSION     WP_006393334.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter insuavis
  ORGANISM  Achromobacter insuavis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Achromobacter insuavis"
                     /db_xref="taxon:1287735"
     Protein         1..709
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=77604
     Region          25..709
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mtspllrqla ssltlgvlgl saahaqslpp atadravpsl apvvvsgesa trgldpgpqr
       61 vqaeqqavpg gtnlilpqqe vrlvtlrdal dyqpgvvvqe ffggldqprl nirgsgiqsn
      121 plsrgillmq dglplndadg sfvisllepr naglvavrrg analspgatt lggevdfqsl
      181 tgtqsdlvrl gtgsfgtrsv tlskgfeger ldgrfsfgyd ksdgyrhhsa serssfqgnl
      241 gfrrgtfenr tylsytdlkf dipqpvpkar myadprgvlg dgnspqdlan nvynrdphrd
      301 tsqfrianrs ywgddslnqt aglywqrtnd dftnpqvanv tdgdtyglaw qlagkagsvd
      361 yrvaldwqrs nmdrdlyair padgrrlqrf gnyaltaenr salvgldwhl tgqlslvgdl
      421 kytqavrdar ergsgktldq dwnyatprlg ivwqpaqtqr wyanvsrsne aptfweivng
      481 evpapmnpat avtsmskldl qraltyeigg dgtfdvagrd lrwtvslyrs rvqdelmsvt
      541 nangtpagty nyrgrtrhqg ieaglsgslp apgdglldyr vaytfsdfrf regefqgnri
      601 agvprhllsa elmyrkggwr vgpnlrwlms dtetnhanap gtqqnayall gfkiayehda
      661 hwsayaqadn ltdktyassy airnsataam piflpgngra fsagvtyrf
//
LOCUS       WP_006393977             212 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Achromobacter].
ACCESSION   WP_006393977
VERSION     WP_006393977.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter
  ORGANISM  Achromobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 212)
  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 212)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 212)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Achromobacter"
                     /db_xref="taxon:222"
     Protein         1..212
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22446
     Region          1..209
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 maydleeqek ldaikawwar ygtlvlslva avavawggww gskayqshka nqamgyfeal
       61 edaarlggad ssvrikaaaa tlrdqygstg yatrgalvaa qalqaqkdvd garqqlewla
      121 gqtknpsmqa varlrlagll ldqkqydaal gqlnnapaaf aalfadrrgd ilaaqgkred
      181 araawqsaid glgtanpltq vvqlkldals ga
//
LOCUS       WP_006394346             800 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Achromobacter insuavis].
ACCESSION   WP_006394346
VERSION     WP_006394346.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter insuavis
  ORGANISM  Achromobacter insuavis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 800)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (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
REFERENCE   3  (residues 1 to 800)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..800
                     /organism="Achromobacter insuavis"
                     /db_xref="taxon:1287735"
     Protein         1..800
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87201
     Region          63..111
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          88..800
                     /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 mfpvrpapql aaaffialav pagiaqaqag aqsgaptaqr ydlpaaplae tltriarqsg
       61 havsvdpalv agrqapavag tytpeqalrq alagsglelr itangtfsar plpqaggatl
      121 lepvrvtgaa esssgplhgy aarvsatgtk tdtpiietpq sitvvgaeei etlkaqslqd
      181 algyvagvsr aegqdrtsds lflrgfrgsq gnyyrdgtly tvniyngrqe lyglervefl
      241 kgaasvlyga appggvintv skrptteplh elnveagnfr rkqisgdfgg alddegkwsy
      301 rltalkrdsd tfidhvpddr tyvapalkwq psdatsltll aeyqedrtvy vyglpgqgtv
      361 lpnpngripr nrftgepgfd kfimkrysig ylfehaftdq lklrnsvryf hadstyfstd
      421 iwqlqadqrh tadrgamprw drssavvtdt slqydattgp lrhtllagld yslprheter
      481 ylrsntnidl ydpvygvplg patpfpwsss ktdmkrlgvy lqdqikiadk wvlllggrhd
      541 wvtvnernff tgekvadnek sqaftgragv vyladnglap flsysesfep tsgqdrqgsr
      601 fkpttgeqye aglryqpags dtmlsaavyq ltrknvnvad pfdtnyeiqa gqartrglel
      661 eartrvgrha nliaayaytd artlkasplq pdevgkrlns vpfnqfsvwg dygfgafglp
      721 glrvgagvry vgstrgmahg tavevpsftl fdamvsyttg pwrfalnatn ladktyigsc
      781 tygcfygepr rvigtatyrw
//
LOCUS       WP_006394479             286 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Achromobacter insuavis].
ACCESSION   WP_006394479
VERSION     WP_006394479.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter insuavis
  ORGANISM  Achromobacter insuavis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Achromobacter insuavis"
                     /db_xref="taxon:1287735"
     Protein         1..286
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29582
     Region          208..283
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mgffkrkdpa dqaqpskraa vpsevqaael rgrarrrlag aialvlaavi ilpmvldsqp
       61 tpvadnipik vperntpfqp qvsepqanap aapaqgatpg esstiptppp vtsgpqasap
      121 qaatpstttp pvttppvttp pattppavtp patvtpprtp ppkpepkpep kpatpkpetr
      181 sddgaralal legrsapaat palkpqaakg nfvlqiaayt tsedaqsrrd klhqagvtna
      241 fveqasiggk qqyrlrvgpf psreaaqaaq arlrtlgydn gfiaaq
//
LOCUS       WP_006394650             120 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Achromobacter
            insuavis].
ACCESSION   WP_006394650
VERSION     WP_006394650.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter insuavis
  ORGANISM  Achromobacter insuavis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
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   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
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   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Achromobacter insuavis"
                     /db_xref="taxon:1287735"
     Protein         1..120
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12872
     Region          21..110
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(40,59..60,84,87,95..96,107)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mghvlltcip esgdrlhfad leldllrcra yrdgeplllt pkefgllaml mgspgavfss
       61 wqlaesvwqa kapglgaghv kcqavaiamr rlrrkvdggs rprllhvirg gsfmlaagpl
//
LOCUS       WP_006394734             206 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Achromobacter insuavis].
ACCESSION   WP_006394734
VERSION     WP_006394734.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter insuavis
  ORGANISM  Achromobacter insuavis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 206)
  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 206)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 206)
  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   4  (residues 1 to 206)
  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   5  (residues 1 to 206)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Achromobacter insuavis"
                     /db_xref="taxon:1287735"
     Protein         1..206
                     /product="TRAP transporter small permease subunit"
                     /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=22280
     Region          9..173
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mtrtehfrll ggllrraetf srvavwagga ltiasvllis fdvlarkflg fntggadels
       61 syafaistsw alafatlqra nvrvdvlyqk lpvrlsavld wismvalavf mvfltyyaye
      121 vvqmswaqks aantplatpl wipqglwllg lawmcitval mlarasaalv tgdielvkei
      181 cgvrsaqeea deeaaagerm vkgata
//
LOCUS       WP_006395166             801 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Achromobacter insuavis].
ACCESSION   WP_006395166
VERSION     WP_006395166.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter insuavis
  ORGANISM  Achromobacter insuavis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 801)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 801)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 801)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..801
                     /organism="Achromobacter insuavis"
                     /db_xref="taxon:1287735"
     Protein         1..801
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87371
     Region          59..109
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          88..801
                     /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 mhvrpfrypl laralatalt apaallaaap aqaqapagfq iapgplsqal sqfasqagvt
       61 lsldgrlvag kqspglsgay svdqgfgrll dgtglraerr sdnvytvrpl tsgdsaaqle
      121 pvtvvgasta egayqpepva svtrsplavl dqpqavnvvp aqvlrdqrpr nlddalanvs
      181 gitqgntlag tqdtlmkrgf ganrdgsimh ngmplvqgrg lnaaadsvev lkgpasllyg
      241 imdpggvini vskrpqltpy haltltgssy aqgrdgvgat ldstgpigds rlayrlvvdt
      301 mnedywrdfg rrrdtlvaps lawygqdtqi vasyehrdyl ypfdrgtald pttgkpldip
      361 srrrldepyn nmwgstelaq vtvdqrvtdn wkahlgyswn qerydanqvr vtaidpvagt
      421 ikrsndgtrg alstdhyvig yvdgrvdigg lrndlqvgad yerrkifrsd lirqnlskpf
      481 syvnpvydrq dpgntvvasd sdqtdklrat sfflqdslhl gerwilvggl ryqhyeqlag
      541 rgrpfktntd ieggkwlpra glvykwtpev slygsytesl kptstiapls sgtvidsgva
      601 peqakswelg lkwdmpgqtt gtlalfdirk rnvlvsqynd ltkltdwrts gaarsrgvel
      661 dvsgslsarw dfmasyayld arttddpqyq gnrlwnvaqh tgslalvyna gqigegrlrl
      721 gtaaryvgtr pgdsansfvl paytvvnafa tydtriagrk vqfqlnvnnl fdrtyytssa
      781 nqyfismgda rqfvlstrme f
//
LOCUS       WP_006396569             403 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Burkholderia
            multivorans].
ACCESSION   WP_006396569
VERSION     WP_006396569.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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 403)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..403
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45853
     Region          17..403
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mptlslaaar alhlaaqgll tpprrkatka dvldtirrma qlqidtihvv arspylvlfs
       61 rlgafrpqwl dehlaearlf eywsheacfl pieqfglmry kmldpsgmgw kyaadwhaqh
      121 rdeiarllvr irsegpvrsa dfvradgtkg ngwwdrkpek rhlevlfttg dlmvaerrnf
      181 qriydvrerv lpdwddardl ppreavlptl ldytcralgi vradwvadyy rlprrsyrae
      241 lerlaqagel ipvqvadwke payvhrslea llpaaaadtl rstvttllsp fdpvvwdrrr
      301 aatlfdfdyt iecytpahkr rygyfclpvl hrgrligrvd akahralgtf elksvhiepg
      361 vrvgsglaad vakavrklaa whgtpqitva happelahal rda
//
LOCUS       WP_006397153             143 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Burkholderia multivorans].
ACCESSION   WP_006397153
VERSION     WP_006397153.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..143
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15555
     Region          3..143
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mpellsyggl favsmlaatl fplqseavla glllagrepv walvlvasvg nvagstlnwa
       61 lgrgierfre rrwfpvkasa laraerwyar ygrwslllsw apvigdpltm iagvlreplp
      121 sflaivtiak vgrylaiawl vlh
//
LOCUS       WP_006397995             371 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Burkholderia multivorans].
ACCESSION   WP_006397995
VERSION     WP_006397995.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
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   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   3  (residues 1 to 371)
  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   4  (residues 1 to 371)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 371)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 371)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..371
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38943
     Region          27..362
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(103..105,126..127,175,227,251)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mklkcmiavl alggftigaa haervvtiaf sgpltgpqav sgkddenglr lavetlnrtp
       61 itvdgqpvrf rivaeddqad prtgvqvaqr lldrqpaaff gpensgvaip varltnaarv
      121 pmltvasnpq ltalgydnvf rtgasdsvlg asmaafaagk lgaktaavid drtaygqgla
      181 eqfiakaksl glqvvareft hsqatdflai latikgknpd viffggytaq aapmakqmvq
      241 rgvrarllgg dgicsanmgt vaqtasrnvf camsgagldr teagrdyvar yrarfksepq
      301 tygityydgm lllaktmasa qttdpaklig alrsashegv agtyaftvrg ellnapttvf
      361 tfedgqmvpv r
//
LOCUS       WP_006398508             424 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Burkholderia multivorans].
ACCESSION   WP_006398508
VERSION     WP_006398508.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 424)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..424
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=45787
     Region          35..254
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 msmldidppg fqpprpvagd dgnrrtvlyg gytvfsvfqp vfsvshrrai gyhaslrahd
       61 eenrqiashe vftqaarrgd llelgrlaes lhlgnfhafd shdewlflsl hpaalmdtvy
      121 gdallanlkt lglpphrvvl evpeqagget pryaaivdgl rkagflialg gfgakhsnid
      181 rvwhlhpdiv tldrgilaqa sehshlervl pglvsllhes gqlvlmggla terdaliale
      241 cnvdfvqgqy fagpsvdpvq pqaaagcmdt lsaalrlrva qrertqaerl apyvaaleea
      301 sarlgagdtl iaaaagvlgl pdtarcflld asgrqigdnv largsvsqra krfrpllhse
      361 gaswerrpyf idamrtpgrv hltspylsin eahlcvtasi aapgatgmqv lcvdinweaa
      421 lnre
//
LOCUS       WP_006399937             638 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Burkholderia].
ACCESSION   WP_006399937
VERSION     WP_006399937.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 638)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 638)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 638)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 638)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..638
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=69107
     Region          18..638
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mndtthaada ahaphpmhqh slralaiaai gvvfgdigts plyslkeafs pahgipltes
       61 silgvisllf waiilvvgvk yllfvmradn ngeggvlalm alslrpldpk trvagalmal
      121 gifgacmfyg davitpaisv msavegleia tphlshlvlp itivilialf wiqrhgtatv
      181 gklfgpimvl wfiaiaalgv yhivrapgiv aainpyyaas fmsehllqay vvlgsvvlvl
      241 tgaealyadm ghfgakpirl aayglvmpsl vlnyfgqgal liqnpraien pffllapdwa
      301 llplvvlstv atviasqavi sgaysltsqa iqlgyvprmk vlhtselaig qiyvplvnwl
      361 llfvilcivi gfkssdnlaa aygiavtatm vittvlacvv mvkvwnwnrl lvgaiiavfl
      421 tidlgffgan llkvaqggwl plgigallff llmtwykgrh ivkertaadg iplepflqgl
      481 lahpphrvsg taiyltgndk lvpvsllhnl khnkvlhert lfmtfvtrdi pyvrddkrls
      541 ardaggglyi vkaeygfnet pdvkavleef grthdmtfel mdtsfflare tvvptqlpgm
      601 siwrervfaw mhqnaakptd ffaipanrvv elgtkiei
//
LOCUS       WP_006400504             198 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Burkholderia].
ACCESSION   WP_006400504
VERSION     WP_006400504.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..198
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21250
     Region          8..195
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mvspsaprrr livaitgatg aiygvrlldl lraaggveth llisnagwln iqhelklsks
       61 dvesradvvh svrdvgatia sgsfathgmv iapcsmktla siahglsdnl itraadvtlk
      121 errrlvlmvr etpfnlahlr nmtavtemgg ivfpplpafy ampktidelv dqtvtrvldl
      181 fapdtplttp waglrhaq
//
LOCUS       WP_006401244             167 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Burkholderia].
ACCESSION   WP_006401244
VERSION     WP_006401244.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 167)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..167
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18095
     Region          10..160
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mftlshdpda skadqyatlv eqaralvese rdlianaanf salvyhsldr lnwagfyffd
       61 gtelvvgpfq gkpacvrial gkgvcgtaaq tretqvvrdv hafpghiacd aaseseivvp
      121 lvaddgtlig vwdvdspvaa rfddedrrgm ealcrvfveh awqktrg
//
LOCUS       WP_006401226             382 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Burkholderia].
ACCESSION   WP_006401226
VERSION     WP_006401226.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 382)
  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 382)
  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   3  (residues 1 to 382)
  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   4  (residues 1 to 382)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 382)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 382)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..382
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40246
     Region          33..369
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(109..111,132..133,182,234,258)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mklrhsllsv siasalalfs qqaaqaadel dvkvgfaapl tgvnagygkd lqngvqlald
       61 davaqkvqia gkpahfsliv qddqadprvg vqaaqalvdk nvsvvvghfn sgttipasvv
      121 ydkagipvid paatnptlts rglanmfmvi atdgqnagna gkyavevtka kriaivddrt
      181 afgqgeadef ekavkaaggt iiareftnnq avdfraqits lkgknpdlif fggldalaan
      241 fikqmrqlgl naqfvggggv kdnefikiag paaegamawe ygrpldelpq gkdfeqrfkk
      301 rfgvdvlsya qfgydatwaa ikamqaagst dpnvyrpalk kidfegitgr isfakdgslk
      361 sgmstlyqvk ngawktivtk gg
//
LOCUS       WP_006402895             387 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia multivorans].
ACCESSION   WP_006402895
VERSION     WP_006402895.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 387)
  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 387)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 387)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 387)
  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   5  (residues 1 to 387)
  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   6  (residues 1 to 387)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..387
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43411
     Region          80..259
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          139..387
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 masqgradga vrratrpvvr arrrqplqyn asrsidgdam tgsdsptarp gralpppsat
       61 vpislvngfl asagvqhdiv erylreagip telrsephar vteeqfstly rmlaieldde
      121 mpgifsrplr ggtlkylcls lldarnleta qhrfgqffhi llddffvesk rdglvaqvll
      181 rpnpavgpig algqelmlkl vhgvcswlig qripllqief acprprhavd hlyffsgpvq
      241 fdcertlmrf sadyldapir qskrnlrkfl arapgdwife tfseqrvchr vrqylsealp
      301 dlpvieqaae hlhcsvrtls rhlaaegttf qalkdelrrd iaiqrltdtq dtiaaigadi
      361 gfddpsafhr afrhwtgstp gtyrrra
//
LOCUS       WP_006400718             118 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Burkholderia].
ACCESSION   WP_006400718
VERSION     WP_006400718.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (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   2  (residues 1 to 118)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..118
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11566
     Region          20..79
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mirkwfaaaa lfgafasawa avdvnsaned almgikgigp arakailder gargpfkdaa
       61 dlasrvkgmg ghtverlqke gltvgaagps aagspaagka aspaaakpag aptrtaqk
//
LOCUS       WP_006399750             323 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia multivorans].
ACCESSION   WP_006399750
VERSION     WP_006399750.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 323)
  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 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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..323
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35219
     Region          38..189
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          218..297
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mnatqadrrg gerapdrrnr ivalsaalap regynltalp svrilrsdra lartpvlydp
       61 givivcqgrk rgyfgdalyl yderhylavs vpvpfsmetd atparpllal ylhldfamaa
      121 elaaqidrag gtppvhaprs mmstpmdepm htsvlrllda ltrpleaavl gpgllrelyf
      181 rvltgaqgps mraalamrgq fgrigralra ihagyaqpld vaqlareagm svpsfhshfk
      241 avtqvspmqy vkstrlhqar llmvrqglta eaashavgya spsqfsrefk rlfgatpase
      301 tkrmresfal ppafadaeyv ssh
//
LOCUS       WP_006403439             347 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Burkholderia].
ACCESSION   WP_006403439
VERSION     WP_006403439.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
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
REFERENCE   4  (residues 1 to 347)
  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 347)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..347
                     /product="CmpA/NrtA family 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=36695
     Region          7..255
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mntsppaape rchlrigfva lsdaapliva qrlklgaahg ltlelsreps waavrdklls
       61 geldaahtly glvcglqlgi ggpqadmaal mvlnrngqai tlsrtladay rahgsvrdaf
      121 atlgrkplla qtfptgtham wlnawlashd vdplhdvrsv vipppemvaa laggeldgfc
      181 agepwhavad acgagrtvav tseiwpdhpe kvlasrrdfv alypatsral irtlvdacaw
      241 ldsaahrrea adwlaspdal gvparliapr llgdygagpf aqpplpirfh dggavnrpdp
      301 rdgrwflaqy rrwgmldgph ddagiaaaia qtalydaava ergttga
//
LOCUS       WP_006404696             301 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Burkholderia].
ACCESSION   WP_006404696
VERSION     WP_006404696.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..301
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31962
     Region          20..261
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mqqnrpaaaa slladcrnal gegatwcdat ntlywtdieg arlwrcradg salaqwpmpe
       61 rlacfaltdd pdvllvglat hlaffdlrsg altrivdvep dlptrlndgr cdpfgafvfg
      121 mkdeggeppr avggfyrlgs dlalerlalp paaiansiaf spdgtkmyfc dsmvreifvg
      181 dysragvsgv rsfarltdpd gdpdgatvdr dgglwsaqwg grrvvrygpd gietervdvp
      241 taqpscpald gegrlyvtsa rvgladdala ddphaggvfv aatrhaglpt arfalkrgvg
      301 t
//
LOCUS       WP_006403832             388 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Burkholderia].
ACCESSION   WP_006403832
VERSION     WP_006403832.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 388)
  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 388)
  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   3  (residues 1 to 388)
  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   4  (residues 1 to 388)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 388)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 388)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 388)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..388
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40219
     Region          34..369
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(109..111,132..133,182,234,258)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkiarftvgf alsafalvas vtagaqsapq tiliglaapl tgpsarigkd lqngaqlaid
       61 danakhptig gkpvvyklva addqsdprta vavaqqlvdq hvigvvghwn tgcsvpasrv
      121 yrdagipqia pastghqytq qgyatafrim ghddaggnft gayavktlka kriaviddrt
      181 sfgagladqf ikgvqanggt ivdrqyvndk ttdfsgvlta ikgkradlvf fggldaqaap
      241 iarrmrqlgv nvpllgaggf vsqtflslag kdgdgvtale pglplermpg gkafdaqyqa
      301 rfrapielha pfaydaaatl iaaaqkagst qpaklvaavr eidrpgvtge iafdkegnlk
      361 npaftiyqvr ggkwtvvdvl ggartaak
//
LOCUS       WP_006404434             383 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Burkholderia].
ACCESSION   WP_006404434
VERSION     WP_006404434.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 383)
  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 383)
  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   3  (residues 1 to 383)
  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   4  (residues 1 to 383)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 383)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 383)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 383)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..383
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40091
     Region          33..369
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(109..111,132..133,182,234,258)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mtfrlrllsa aaltvanlal ptgaahaqea ivkvgvavpl tgggaaygkd iengvrmavd
       61 eanaarttig gkpvkfvvts qddqsdprig vqaaqqltdg qvavvighfn sgttlpaski
      121 yakagipmit psatnpditr aglgtvyrvi atdtqnagna gayaasitka kriaiiddrt
      181 afgqgeadef ekavkanggt ivareftndk avdfsaqltk iksvnadlvf fggldaqsam
      241 lvkrmrqlgi raqflagggv mnanfiklag saaegaavwe ygqplsrlak gklfetkfkq
      301 kygvdmlaya pfaydatwia inamqkanst kpadfnaalk rtqydgitgt iaftetgdlk
      361 npsstlyevk naawqpvttk sad
//
LOCUS       WP_006405425             384 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Burkholderia].
ACCESSION   WP_006405425
VERSION     WP_006405425.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 384)
  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 384)
  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   3  (residues 1 to 384)
  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   4  (residues 1 to 384)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 384)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 384)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..384
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39902
     Region          36..369
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(112..114,135..136,184,236,260)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mersivgmrc kplitaalav aafgaasgal adqvvkigsv epttggiahl gkdnengarl
       61 aveeinakgl tiggqkitlq fdpqddaadp rqatqvaqkl vddkvvavig hlnsgtsipa
      121 skiysdagiv qispsatnpt ytqqgfktty rvvatdaqqg palasyaqsn gvktvavvdd
      181 staygqglan efekkakalg lkvlshdatn dkavdfrail tkikgenpda imyggmdatg
      241 gplakqakql glrakilsgd gvctdqlaql agpaadnvlc sqagaaiekm pggaafvaky
      301 qkrfnqgikf dapfaydavy ivvdamkran stdpakilaa mpatkyegvi gtttfdskgd
      361 lthgiisiyg yksgkktfld qvrm
//
LOCUS       WP_006405986             312 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia multivorans].
ACCESSION   WP_006405986
VERSION     WP_006405986.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
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
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..312
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=33346
     Region          1..309
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mieidrvgkr fgdivavddv sltmkqgtit alvgasgsgk stllrminrl iaptsgtiri
       61 dgtdtagvpp eqlrrrigyv iqghglfphw svarniatvp rllgwrpdri rarvtellel
      121 fhlapaefad klphelsggq qqrvgvaral aaepamllmd epfgaldpii rnkaqddlla
      181 lqrrlgitvv ivthdieeal klgdtiavmd ggrllqvatp adilgnpaag vveqlvagvd
      241 rplrllaltp vdavaeagha dgapieaart lrdaisellw rgvdalpvdd ghgrpsrrit
      301 ldairahark pa
//
LOCUS       WP_006406208             403 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Burkholderia].
ACCESSION   WP_006406208
VERSION     WP_006406208.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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 403)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..403
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45904
     Region          17..403
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mptlslaaar alhlaaqgll tpprrkatka dvldtirrma qlqidtihvv arspylvlfs
       61 rlgafrpqwl dehlaearlf eywsheacfl pveqfglmry kmldpsgmgw kyaadwhaqh
      121 rdeiarlldr irsegpvrsa dfvradgmkg ngwwdrkpek rhlevlfttg dlmvaerrnf
      181 qriydvrerv lpdwddardl ppreavlptl ldytcralgi vradwvadyy rlprrsyrae
      241 lerlaqagel ipvqvadwke payvhrslea llpaaaadtl rstvttllsp fdpvvwdrrr
      301 aatlfdfdyt iecytpahkr rygyfclpvl hrgrligrvd akahralgtf elksvhiepg
      361 vrvgsglaad vakavrklaa whgtpqitva happelaral rda
//
LOCUS       WP_006406882             378 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Burkholderia].
ACCESSION   WP_006406882
VERSION     WP_006406882.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 378)
  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 378)
  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   3  (residues 1 to 378)
  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   4  (residues 1 to 378)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 378)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 378)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..378
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40051
     Region          28..364
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(104..106,126..127,176,228,252)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mklkvshval aaacalsgah aiaadvvkig faapltgpqs nygtdmqkgv qlaiadfnat
       61 nptiggkpvt fqldsqddqa dprtgttvaq rlidnnvrgi ighfnsgtsi pasdlydrag
      121 lpqismatsp qytargyktt yrlltsdaqa grivgtyavk nlhfkriaii ddrtaygqgi
      181 adefakavqa aggtivkrdf tndkaldfsa iltnlkginp davfygggda qsspmirkmr
      241 qlgmksafvt gemsrsptfl kvggdaaega ivymgglpke kmpgfagyaa rykarfnedv
      301 ityspysydg tmalltamkn anstdpkvyt pylgkvsikg vsadriayda kgdlkdapvt
      361 iyrvehgafk pvdtiagn
//
LOCUS       WP_006407455             350 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia multivorans].
ACCESSION   WP_006407455
VERSION     WP_006407455.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 350)
  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 350)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 350)
  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   4  (residues 1 to 350)
  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 350)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..350
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38413
     Region          32..214
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          258..337
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mdnarrfmtv wnfarspasv llmiefgrsr aiappallkg sqltlkqlad pdftvqaaqe
       61 ltvasnllrl agneagvglk vglsyqlsay gllgyglmss atgrdaivlg srylaltytf
      121 vgmryrrvgt hdavvfepsp elstqlqrff veramgatcr vlrdvmgptf alatfdlays
      181 aepgsrqqvl gtkvryaqpa smitfehaql erplpqanaa taamcermca ellsrrrtrv
      241 divsflneyl athaferppq lkdvaallnt sertlkrrlq eegacfrdis navrkaraqa
      301 lvaegrlsik eiaqelgfsd mssfsqaykr wtgvapsmsr qgravrsagl
//
LOCUS       WP_006408813             576 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein/permease
            [Burkholderia].
ACCESSION   WP_006408813
VERSION     WP_006408813.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 576)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..576
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=59895
     Region          1..558
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mqrhlwrlag vvyadiaisv aiglavtacy agqalclalg iaaiwsgasl rglsgwafgf
       61 aafalarial mwagevaalr tasrtkarlr arllpqalal gahggagrta elqhaivggv
      121 ealetyygry ipavcvalvg caavigavaw idplsasvla acvlavpvid rvwlrlcrpr
      181 asglmasigr fgatmldslq giatlkafda agsrraslva aaaglrream gilyatlmrn
      241 gvtglfglgc vaavaalnas raasgvlpat talitlflar eafrpvdrld ktfhiawgaa
      301 saagpiaall daeppvrepv sprapgehad vvfddvtftw pgsdrpalkh vsltigqref
      361 vgivgpsgag kstlgallir madpqhgsvr iggvdlrdlp laamrekvga vfqdivlfdg
      421 siednlrfar pdadadaird aarvahvhdf ieglpqgyat pvgeraaqls ggqrqrlaia
      481 rawlkgapil lldeatsnvd psseqaiqas ieacagqral vviahrlatv rhadrivvvd
      541 dgriveegdh dtlkarggly arllaaqage tgeesv
//
LOCUS       WP_006409094             347 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Burkholderia multivorans].
ACCESSION   WP_006409094
VERSION     WP_006409094.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
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
REFERENCE   4  (residues 1 to 347)
  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 347)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..347
                     /product="CmpA/NrtA family 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=36721
     Region          7..255
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mntsppaape rchlrigfva lsdaapliva qrlklgaayg ltlelsreps waavrdklls
       61 geldaahtly glvcglqlgi ggpqadmaal mvlnrngqai tlsrtladay rahgsvrdaf
      121 atlgrkplla qtfptgtham wlnawlashd vdplhdvrsv vipppemvaa laggeldgfc
      181 agepwhavad acgagrtvav tseiwpdhpe kvlasrrdfv alypatsral irtlvdacaw
      241 ldsaahrrea adwlaspdal gvparliapr llgdygagpf aqpplpirfh dggavnrpdp
      301 rdgrwflaqy rrwgmldgph ddagiaaaia qtalydaava ergttga
//
LOCUS       WP_006412533             388 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Burkholderia multivorans].
ACCESSION   WP_006412533
VERSION     WP_006412533.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 388)
  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 388)
  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   3  (residues 1 to 388)
  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   4  (residues 1 to 388)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 388)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 388)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 388)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..388
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40340
     Region          34..369
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(109..111,132..133,182,234,258)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkiarfsvgf alsafalvaa vpafaqsapq tiliglaapl tgpsarigkd lqngaqlaid
       61 danakrptig gkpvvyklva addqsdprta vavaqqlvdq hvigvvghwn tgcsvpasrv
      121 yrdagipqia pastghqytq qgyatafrim ghddaggnft gayavktlka kriaviddrt
      181 sfgagladqf ikgvqanggt ivdrqyvndk ttdfsgvlta ikgkradlvf fggldaqaap
      241 iarrmrqlgv napllgaggf vsqtflslag kdgdgvtale pglplermpg gkafdaqyqa
      301 rfrapielha pfaydaaatl iaaaqkagtt qpaklvaavr eidrpgvtge iafdkegnlk
      361 npaftiyqvr ggkwtvvdvl ggartttk
//
LOCUS       WP_006412719             423 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Burkholderia multivorans].
ACCESSION   WP_006412719
VERSION     WP_006412719.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 423)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..423
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=46224
     Region          32..253
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mkssrdlsld slldrltptp ggwvatyrgt tlrsafqpvl sithkrvvgy eallrvvdan
       61 gtlisptalf drtrndadsl lldrlarclh tanfvaqgig dgwlflnvtp rvldsglvqr
      121 efvealcrhf slspnrivle vieqpardea alartidmiq hrdfliaidd fgtgfsnfdr
      181 vwrarpdivk ldrslverst wspedrrimh hlvsmlhqag amvlaegves ddalqalmda
      241 didfvqgfqf gqpdtsiaha saavpamlda awqrfiarrh appapaqpgf daierlvlag
      301 aaafaasgdl hdaaqrvfav paarrvfvtd eigeqflpsi gapgpagttr laplfpeths
      361 nwsrrpyfqr aiaapgrval mgphfslteg rdcytaavat hargklvvfc vdfvldsagt
      421 vmr
//
LOCUS       WP_006412726             143 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Burkholderia multivorans].
ACCESSION   WP_006412726
VERSION     WP_006412726.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..143
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15567
     Region          7..141
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mpelltyggl favsmlaatl fplqseavla glllagrepv walvlvaslg nvagstlnwa
       61 lgrgierfre rrwfpvkasa laraerwyar ygrwslllsw apvigdpltm iagvlreplp
      121 sflaivtiak vgrylaiawl vph
//
LOCUS       WP_006413215             123 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Burkholderia multivorans].
ACCESSION   WP_006413215
VERSION     WP_006413215.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (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   2  (residues 1 to 123)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..123
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11958
     Region          20..79
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mfrkwfaaaa lfgafasawa avdvnsaned almgikgigp arakaileer gargpfkdaa
       61 dlasrvkgmg ghtverlqke gltvgaagsg aagpagspaa gkaasaspaa akpagaptrt
      121 aqk
//
LOCUS       WP_006413530             269 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Burkholderia multivorans].
ACCESSION   WP_006413530
VERSION     WP_006413530.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..269
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=30914
     Region          4..71
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mlrsikelhg savrakdgdi ghvnqayfdd dnwcirylvv atgdwlhdkq vlispysvkh
       61 tdsrsstlhv dltrhqveds pdldihkpvs rqheieylry yqypsywggp nlwgvdaypv
      121 fhsatvsqdl eaghplptrs tpadaptdth lrstgkvkgy rleatagrig rvtdfiydde
      181 awvirylair trnwwltnkd vliathwldq vdwstetvst tltrdairqs peyddsqpvy
      241 rsdeialyqf yrkrgywlna esstargal
//
LOCUS       WP_006414518             233 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Burkholderia
            multivorans].
ACCESSION   WP_006414518
VERSION     WP_006414518.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..233
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=25456
     Region          1..>219
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mslvvdirkt yataerrftl dvsftattqr vvlfgpsgag ksmtlqaiag llapdegtia
       61 lngeplfdaa rridvptrar rvaylfqdya lfphlnvrqn iafgltaglr nprakalppe
      121 vaywlrafdl eplaaqypsq lsggqkqrva laralvaqpr illldepfaa ldgamrqrmr
      181 helaelqarl dipmvlishd pddvaafgdq vvqlndgrvq paaphagwpa rvm
//
LOCUS       WP_006414796             323 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia multivorans].
ACCESSION   WP_006414796
VERSION     WP_006414796.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 323)
  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 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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..323
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35239
     Region          38..189
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          218..297
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mnatqadrrg gerspdrrnr ivalsaalap regynltalp svrilrsdra lartpvlydp
       61 givivcqgrk rgyfgdalyl yderhylavs vpvpfsmetd atparpllal ylhldfamaa
      121 elaaqidrag gtppvhaprs mmstpmdeam htsvlrllda ltrpleaavl gpgllrelyf
      181 rvltgaqgps mraalamrgq fgrigralra ihtgyaqpld vaqlareagm svpsfhshfk
      241 avtqvspmqy vkstrlhqar llmvrqglta eaashavgya spsqfsrefk rlfgatpase
      301 tkrmresfal ppafadaeyv ssh
//
LOCUS       WP_006415007             251 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Burkholderia multivorans].
ACCESSION   WP_006415007
VERSION     WP_006415007.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  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   3  (residues 1 to 251)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..251
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27464
     Region          42..246
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mnietstaps ldsghsgpdy arrnpleigv qlrnlvnrgd fltveypggq lvtrllevdv
       61 gartftfdwg alseqnasil gaahcafsaa pegvrveftt gtpretryeg lpafvadfpd
      121 vlvciqrrey frvdapvvdp flcrgalpdg erfqfevhnl slggvglrta dervealalg
      181 tvlpdvelel nghgklsldl qlvsqratql pngarryqlg frflslpgsa entlqrlitq
      241 lemkrrslar a
//
LOCUS       WP_006416731             199 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Burkholderia multivorans].
ACCESSION   WP_006416731
VERSION     WP_006416731.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..199
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=20308
     Region          32..198
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mfeafsvslf rrlaadlrra rrpaalrawr agftlielmi vlaivgvvaa yaipayqdyl
       61 arsrvgegla lassarlava dnaasgtgld ggysapaatr nvesiridae tgqitvayta
      121 rvaaagantl vlvpsapdkp dtptarvplk kgemqagaia wecfaagkda sslpapgagp
      181 lpgtaatlpa kyapaecra
//
LOCUS       WP_006417066             143 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Burkholderia multivorans].
ACCESSION   WP_006417066
VERSION     WP_006417066.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..143
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15551
     Region          1..140
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 marrtgftll elmivlaivg lpagwgipsy rehmarthra savsalyraa hyletldvgl
       61 pravpeafah appdgrpvyr ialrprqqsd aaaatdelna tpldtgpmrd dacgtfilrs
      121 dgtkgnrkrd gteewepacw gvr
//
LOCUS       WP_006418338             101 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Eremococcus coleocola].
ACCESSION   WP_006418338
VERSION     WP_006418338.1
KEYWORDS    RefSeq.
SOURCE      Eremococcus coleocola
  ORGANISM  Eremococcus coleocola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Eremococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Eremococcus coleocola"
                     /db_xref="taxon:88132"
     Protein         1..101
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11128
     Region          5..100
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(27,58..59,61,82)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(27..28,36,39,41..42,44,47..48,50,58,63,70)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 maqlnedldf evlavvseip rgkvatygqi arligqpnqa rlvgkilsra eyfgdypchr
       61 vvnqagrlvp gwadqawllq aegipfkkkg yvdmaaaqwe d
//
LOCUS       WP_006418503             459 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Eremococcus coleocola].
ACCESSION   WP_006418503
VERSION     WP_006418503.1
KEYWORDS    RefSeq.
SOURCE      Eremococcus coleocola
  ORGANISM  Eremococcus coleocola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Eremococcus.
REFERENCE   1  (residues 1 to 459)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Eremococcus coleocola"
                     /db_xref="taxon:88132"
     Protein         1..459
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=51054
     Region          211..311
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          336..459
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(410..411,414,432..435,437)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkkflklvmg vfvlfgliyc ggffyfqdhf nfnsqyagid isnltvkaas dkvekqllak
       61 eykliedgqt vkkiqladlk ptfnlnksik qafkqqdhan wmsemltdkv yadslgqevd
      121 ldvadlasdl nqselkgnkr kpaiqaelay deakgyyate gqagteiqae kleevldqal
      181 ttketdikle eaydqpiave dnkklqdklt kidkiannef sfelggdtve tdkkkieswm
      241 tlsdddeiql dreaiaaylt elnekystfn kyrefnstnf gkvevqpgil gweidveaet
      301 eaiasaleag esvpaepvfy stggiagaad digdtyvevd lanqtmylyy egtlitetpi
      361 vsgkdgaetv pganavneml tdtnlvgynq fynveystpv sywirfddka qgihdapwqs
      421 afggdvhtya gslgcintpy dqvsliysyv dygtpvivf
//
LOCUS       WP_006418447             471 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Eremococcus coleocola].
ACCESSION   WP_006418447
VERSION     WP_006418447.1
KEYWORDS    RefSeq.
SOURCE      Eremococcus coleocola
  ORGANISM  Eremococcus coleocola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Eremococcus.
REFERENCE   1  (residues 1 to 471)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Eremococcus coleocola"
                     /db_xref="taxon:88132"
     Protein         1..471
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=52810
     Region          220..324
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          348..471
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(424,426,444..447,449)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mqtkqiipll kklraknkqt falqvilall iilyiigiif yqnhylpntf aagvpignrd
       61 qqealaevks klgqevvdfq eggkdlgfvq lnqfeldypn sfdwqeglak qwawvwpiqi
      121 lrgnrqleaq psllandsqv dqliqglgid nsqreatqna rlteaedgsl qvieekygnn
      181 idsesmrqai aqglsqgldk idlktaykqp kytkdgkgiq dlqadyqake atqitlefnh
      241 esvtipqdqi kawlhlddqg qaqvdqeaik dyiyqlnety sslfgkhefq styqglvtve
      301 sgtfgwyidp daeapviaen ilkggsykre paiagqgyma eneignsyve vdlshqmmlv
      361 ylegalvlet pivsgnigtl tvpgayqvwq klektdlrgy nprtekeyvq pvdywiafdn
      421 ngqgihdaqw qsqfggnvyq ssgslgcint plsamqevfq ivyvgmpvmi f
//
LOCUS       WP_006426307             277 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Dorea].
ACCESSION   WP_006426307
VERSION     WP_006426307.1
KEYWORDS    RefSeq.
SOURCE      Dorea
  ORGANISM  Dorea
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Dorea"
                     /db_xref="taxon:189330"
     Protein         1..277
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31113
     Region          1..179
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mkidmhchvr egsvdsrvsl deyittlkek gfdgmlitdh dtyhgyrhwk yhmkgkvhed
       61 fvvlkgieyd tldaghiici mpegvkmrll evkglpvsvl idfvhrhggi lgpahpcgek
      121 ylsftntsrf ykspelikrf dfieafnace saesnegark laekykkpgi ggsdahrpdc
      181 igtgytilpe rvtcetelia lirskaaiea ggvlygktak dkmgpahkil tysfwfynkg
      241 gallkkhkrt lkgkienpat pidpieipyl hnikkqk
//
LOCUS       WP_006428406             369 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Dorea].
ACCESSION   WP_006428406
VERSION     WP_006428406.1
KEYWORDS    RefSeq.
SOURCE      Dorea
  ORGANISM  Dorea
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 369)
  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 369)
  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
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 369)
  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   5  (residues 1 to 369)
  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   6  (residues 1 to 369)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 369)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 369)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Dorea"
                     /db_xref="taxon:189330"
     Protein         1..369
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41127
     Region          10..54
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          74..363
                     /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 magrnekkni tkskivnyii nnkitskael aqnlslsmpt vlsnvnelid rnmvieigey
       61 estggrkakr iginpaykya vgvvitanhl givllnmqye iektirmrlk fstetsyclk
      121 vaemvedflk dvedrekilg igisipgiid qanrmvvksh alqlenfsls fleqvfsypv
      181 yfandanaam maedmheyqd avylslnntl ggafcingkl vagqnqkage fghmilvpgg
      241 kkcycgkagc adaycaasal tdeeqemtle qfmekveqkn tktvekwnqy ldnlailisn
      301 lrmaydtdii lggevggyls eymiplgekv mayngfehdv rylkncsykr easavgaakh
      361 flseyiqhl
//
LOCUS       WP_006428598             338 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Dorea longicatena].
ACCESSION   WP_006428598
VERSION     WP_006428598.1
KEYWORDS    RefSeq.
SOURCE      Dorea longicatena
  ORGANISM  Dorea longicatena
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Dorea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Dorea longicatena"
                     /db_xref="taxon:88431"
     Protein         1..338
                     /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=38566
     Region          11..273
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 meekkvtvsv rdsqmdnika illflvalgh tldvykdvwn vnmylmkyiy lfhmplfafi
       61 tgyftkntek arnfaiekcl ipyillqsly vimgklmihm glanfnsgvf ngsllvpssa
      121 fyyllavfvw kltakefmnl rhpfiisval gllvsvtkmq efhmgygavf allpffvagv
      181 lcdeklllri rnskkifsil ilglciipav klpysihsvr ssyqtagfsd ifgigyriif
      241 yiiallmgya visitsrkrn vfthigeasi lvyagstfla phgylilnki fgfsknnwin
      301 litmmiycii liwvcaiptf lklynwilsk inyilfkk
//
LOCUS       WP_006428865             188 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase
            [Stenotrophomonas].
ACCESSION   WP_006428865
VERSION     WP_006428865.1
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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..188
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /function="Negative regulator of beta-lactamase
                     expression"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=20889
     Region          18..186
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mpnpllpglq lqplpyhdrl plrdpatlem vvihctelpd lamareyger vlydsgagns
       61 ghfyidrdgr vvqyvaperv ahhvrgmnah tlgielvntg ryphwfdsrh qamdepytea
      121 qlvalealll alvarypslr riaghdqldl eqvpasddaa ltvarkrdpg plfpwarila
      181 kvplqglg
//
LOCUS       WP_006431543             204 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Stenotrophomonas].
ACCESSION   WP_006431543
VERSION     WP_006431543.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..204
                     /product="YqaA family protein"
                     /function="Predicted membrane protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22387
     Region          3..171
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mkifgplyer amkwaahera ptyltvlsff eaiifpvmpe vmlapmcvaq pkrgwwfatl
       61 slagsmvgav vgyalghfaf eaikplfeal gmlpaieqgi ttvqakmaes pwavftflvl
      121 ggfmpipmkv ftwasgivgv pmpqyllsml igrgkrvyvl aaviriggar aeaalrrwie
      181 plgwiatalv vvliawlvwr skfa
//
LOCUS       WP_006433947             713 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Borreliella spielmanii].
ACCESSION   WP_006433947
VERSION     WP_006433947.1
KEYWORDS    RefSeq.
SOURCE      Borreliella spielmanii (Borrelia spielmanii)
  ORGANISM  Borreliella spielmanii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Borreliaceae; Borreliella.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 713)
  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   3  (residues 1 to 713)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Borreliella spielmanii"
                     /db_xref="taxon:88916"
     Protein         1..713
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79101
     Region          1..713
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdssdvidkf knsfkeesie nvsdieqall slevssdqdi insifrnlht ikgssgmfgf
       61 nftaslvhei etvldvvkdg raifnqaaid atlmsvdfir eliegdeais eidfnkrkqv
      121 lvneikkile tsnvkgdfqe alkndfsksg nssvleevar vdpdnkfdde alrsefksyk
      181 ilfspakgil fhghkpinll sklinlgngy vrakvdnipd lelispdnvy vdweiilnte
      241 esresiedif vfldsqskid iqeldkcfes dkgdnaglkn fnllgldrna kdlansslkk
      301 sdfveksfss gdknkfnvqd dtvrskvnia sikvdskkld hlvnlvgelv tiqsklskea
      361 enrssnvlns isaefsllin elrdyttglr tvpieilfvk fqrivkdlsa nlgksilyha
      421 yggdtvldks iieklneplv hlirnsidhg iesseererl gkdpkgiikl safqsgdsvi
      481 vaieddgrgl dkdkilkkai ernivsdssa ktlsnidvyn lifepgfsta ssitdisgrg
      541 vgmdvvkkqv eslrgnvvle selgkytrik lifpltlaii egwlvrvkne hfivplsnve
      601 sclesnnlis qidgvetksn vmnyrgsmis firlreffqv sdeksfneqv vvvntnsgkm
      661 givvdevlgq hqtvikalgk iysrvegvsg atilgdgsla lvvdidaitk lir
//
LOCUS       WP_006434876             212 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Stenotrophomonas].
ACCESSION   WP_006434876
VERSION     WP_006434876.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 212)
  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 212)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 212)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..212
                     /product="YfgM family protein"
                     /function="Uncharacterized protein conserved in bacteria"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22370
     Region          1..200
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 maiddlldeh eqservrswl rkngasilgg vviaigaiag wqwyqkdqgg klasanveyq
       61 kallglqqnk lddaskavka leagpssiyg dlaalqlaka qvdagkneea latlrgvkve
      121 gdlqrvvdqr varllvatgk sdeaikllgs atdsssleih gdalmaqgkr ddaraqyeka
      181 lksldvaapq rrlletkvmd aggtvaapae sv
//
LOCUS       WP_006435331             293 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Gordonia amicalis].
ACCESSION   WP_006435331
VERSION     WP_006435331.1
KEYWORDS    RefSeq.
SOURCE      Gordonia amicalis
  ORGANISM  Gordonia amicalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 293)
  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 293)
  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   3  (residues 1 to 293)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Gordonia amicalis"
                     /db_xref="taxon:89053"
     Protein         1..293
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32450
     Region          175..273
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mtsdsgvytl kelatmdwsp dditrarrsg tlipvahgwv rsatadprvv aavaaggals
       61 cvgalrfhqt hgsseiwvpp gytethvrls khmkgrprps gpfrwcqgyg qplpvvtavd
      121 siplalgcaa rcltaeewva tvdsvlnstd wtipdiqaem grvaravmam fgrcdarsqs
      181 gtesiarlrl iaagfevevq pgigthehad lrigalliec dgrayhsdve tfrndrrrdr
      241 mtmidrwltm rltyddvlyn wdgvledvra vtrsdrhrir rdndprrrgn asi
//
LOCUS       WP_006436524             212 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Gordonia].
ACCESSION   WP_006436524
VERSION     WP_006436524.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..212
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23411
     Region          3..201
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 melseamrtt gtcryfsdkp vedevfyqaf ddarfgpqgg nrqpvrwvvv rddatkkala
       61 dlylpfwepy ynsilegskk vgavpkties anyfahhlae vpalvvvcae meglhptdhe
      121 lgrlsvvgga siypsvqnlt lalrqqgvat alttllcaae ndvkellgip ddyitaahia
      181 vgyprdgfpr kltrspvedi ayldrfdnrm fa
//
LOCUS       WP_006437273             399 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: exonuclease SbcCD subunit D [Gordonia].
ACCESSION   WP_006437273
VERSION     WP_006437273.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..399
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42692
     Region          1..269
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          267..>315
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrivhtsdwh lgrtfhgvdl ladqrralsh laalvaaesa dvvivagdvy drsvpsadav
       61 riyddglaei aaagaqivvt pgnhdsatrl gagssfaaag glhlrtsida iacpivlsde
      121 ygevavygip ylepdtarrh lgveevcght avldaamsri radlatrqsr svvvahafvs
      181 gaaasgsers isvggvetvp aetfsgvdyv alghlhspqr vtdtvrysgs llpysfgert
      241 hrkavwvidl dadgvteirr nelpvvrels slrgtldell aaeeyataeg hyveatltdt
      301 vrpldamrrl rerfpfavhv qwdrphtgsg vdyrsrvrgr sdaeiinsfv edvrdsptkg
      361 ervlieralr avvgepeada gadgelalfa ldafvaeta
//
LOCUS       WP_006437318             207 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Gordonia amicalis].
ACCESSION   WP_006437318
VERSION     WP_006437318.1
KEYWORDS    RefSeq.
SOURCE      Gordonia amicalis
  ORGANISM  Gordonia amicalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
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   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   3  (residues 1 to 207)
  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   4  (residues 1 to 207)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 207)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 207)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Gordonia amicalis"
                     /db_xref="taxon:89053"
     Protein         1..207
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22941
     Region          20..205
                     /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"
ORIGIN      
        1 mvtvtdsatt tagettkthr vlvaeddsli rmdliemlre egydvvgeap ngqvavelte
       61 slrpdlvimd ikmpirdgid aateiaekrl apvvmltafs qrdfiekvrd agamaylvkp
      121 ftkadlvpai evavsryhel kllerevatm nerletrklv erakgllmqk qglsepeafk
      181 wiqraamdrr ttmkavaqvv vetlgan
//
LOCUS       WP_006439682             351 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Peptacetobacter hiranonis].
ACCESSION   WP_006439682
VERSION     WP_006439682.1
KEYWORDS    RefSeq.
SOURCE      Peptacetobacter hiranonis
  ORGANISM  Peptacetobacter hiranonis
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Peptacetobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Peptacetobacter hiranonis"
                     /db_xref="taxon:89152"
     Protein         1..351
                     /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=39880
     Region          4..277
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mdnsktktrl tyidiargia illvvighmn qfyrnnlnis npqmlsfiyt lhiplffiis
       61 gmlfseksfk dvsftkflik kiktlivpyl flditgglfn vfvysdvtlv niknvvvntl
      121 tlhcniganw fisalfigei ilyffmkfym piykyiawip fllinvfypf shwiniavrg
      181 viaftfillg yylkeffksd lnkrwymili slvitymvsk fngqidiwgs tignpflcvl
      241 gglagsyavi gisklisskl lvfigqntmt vmgthmliif fiwpllsksv faafpsltts
      301 avgailffai viavdlpimy lydrfipfli gkpskpvvke keavksvqdi a
//
LOCUS       WP_006440178             466 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Peptacetobacter hiranonis].
ACCESSION   WP_006440178
VERSION     WP_006440178.1
KEYWORDS    RefSeq.
SOURCE      Peptacetobacter hiranonis
  ORGANISM  Peptacetobacter hiranonis
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Peptacetobacter.
REFERENCE   1  (residues 1 to 466)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Peptacetobacter hiranonis"
                     /db_xref="taxon:89152"
     Protein         1..466
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=52524
     Region          82..197
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          223..328
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          348..466
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(418,421,439..442,444)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mgilsrkgtk dipkkkiaai ivgviaviyi glavfftnhf yfgtvinges csgktvadve
       61 emfgkvsddy sltltdkrnk eftikskdid ltfhdegqiq kikdsqssfg wivgifknkd
      121 ynadivrydn akleklyngf elfdknyvie pksaypeysr ktnsyeirpe iygnkvnkea
      181 lykemqksil sgnkainide aglyvqpknk adssklakav eelnkkvkmk vtydfedrke
      241 vfsgyeiaql lncdsegnyd itinrdrmie llrglskqys tygdprkfka ssgkeitiyg
      301 gsygwlidke keadeltkvl eagksvtrep vysqtalhrt kddigntyve islggqylwy
      361 yrdgklvtsf pvvtgntsrg hgtpggiypl nykerdtyln grnysshvny wmpfngnigl
      421 hdatwrssfg ggiyrsngsh gcvncpysga atiyktiekg tpiily
//
LOCUS       WP_006440713             181 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Peptostreptococcales].
ACCESSION   WP_006440713
VERSION     WP_006440713.1
KEYWORDS    RefSeq.
SOURCE      Peptostreptococcales
  ORGANISM  Peptostreptococcales
            Bacteria; Bacillati; Bacillota; Clostridia.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Peptostreptococcales"
                     /db_xref="taxon:3082720"
     Protein         1..181
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20369
     Region          3..178
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mnfencvker rsvrkfteek ishetfekii elarfapswk nsqtaryhii edtdiktkva
       61 eeavmnfvfn ektikrapal vvltavgkks gyeedgsfst skedrwevfd agiacqtfcl
      121 saynegvgsv vlgifddkkv keiceipeee nvmaliavgy rdgeakaape rlevkdlvsf
      181 k
//
LOCUS       WP_006441439             287 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [[Clostridium] hylemonae].
ACCESSION   WP_006441439
VERSION     WP_006441439.1
KEYWORDS    RefSeq.
SOURCE      [Clostridium] hylemonae
  ORGANISM  [Clostridium] hylemonae
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 287)
  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 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   3  (residues 1 to 287)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 287)
  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   5  (residues 1 to 287)
  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   6  (residues 1 to 287)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="[Clostridium] hylemonae"
                     /db_xref="taxon:89153"
     Protein         1..287
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32723
     Region          21..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          134..287
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mkqysplera leyieehlnd niglnevske tgysyyymtr lftsvlgesv gryinrrkly
       61 nasrklidtd ervldiavdc gfasseafsr afksefgssp aeyrkagadl vvnakrelvp
      121 edvyhiahni srspeiimtd etkvagvrgt tslsdnripe iwkqfllfpk elfdgadvgy
      181 gicetkravy trdgdvlftv maagavdtfe slprtldrki lsagkyavft hrgtfanlhr
      241 tyryifgtwl ktageelddr edfemyqrki vsyddpdnev kifipik
//
LOCUS       WP_006442926             290 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [[Clostridium] hylemonae].
ACCESSION   WP_006442926
VERSION     WP_006442926.1
KEYWORDS    RefSeq.
SOURCE      [Clostridium] hylemonae
  ORGANISM  [Clostridium] hylemonae
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 290)
  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 290)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="[Clostridium] hylemonae"
                     /db_xref="taxon:89153"
     Protein         1..290
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=31956
     Region          1..287
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mivtlqdmlk daenknyava cinattyegl rgiieaaeel napvilghaq vhetvapide
       61 fgplivqeav kakvpvvvhl dhgmdyeyai kavragfnsi mydcsvlsle knieevrrft
      121 klahkmgvav egevgcmpsn ivgqggctef gkeiinikdy ytkpeearrf veetgvdmlt
      181 vsfgtvhgvf vdkpeldiql ltdihketda ylvmhgssgv dqdqmlaavd hgvrkinhyt
      241 svgtapaspl meavqraedp vyyhdlakms kdiikekske iiallrshmr
//
LOCUS       WP_006443133             289 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [[Clostridium] hylemonae].
ACCESSION   WP_006443133
VERSION     WP_006443133.1
KEYWORDS    RefSeq.
SOURCE      [Clostridium] hylemonae
  ORGANISM  [Clostridium] hylemonae
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="[Clostridium] hylemonae"
                     /db_xref="taxon:89153"
     Protein         1..289
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31522
     Region          17..262
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mktnkmvlkt gpeeaacdlh vhtacsdgsa sveyvldyak raglryiavt dhdtfagsrk
       61 araaagpggp evipgaeisa rddkrgrnvh mlcycpkded glqrfmdgtl kkrrqqklqm
      121 awkisrlypg ftveaveqqa aesesiyech imqvlcdlgy tntaigplme elissrgscy
      181 vpnsypsara aaeairdagg iavvahpeqf dsfalveela qsgliqgvev whprnseaar
      241 trlrqlarqy dlaetggsdy hgqyaktpnp lakctctpqq aeklkerag
//
LOCUS       WP_006443454             447 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [[Clostridium] hylemonae].
ACCESSION   WP_006443454
VERSION     WP_006443454.1
KEYWORDS    RefSeq.
SOURCE      [Clostridium] hylemonae
  ORGANISM  [Clostridium] hylemonae
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 447)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="[Clostridium] hylemonae"
                     /db_xref="taxon:89153"
     Protein         1..447
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=51581
     Region          199..441
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 minffksgta erqkpaketp dspegvqrlg srellekeys dvaemanevl viiqlnrfnh
       61 lntifgmemi etivkilsgl iadyaersgg kayslqmdli avitpygerd tflaglqeqv
      121 kkmeevnfrd edivysnhyt ftyivyfldf dksyipdiki ildnmllklk qigngnstrg
      181 evyngagdpn wrlldslsre vkrgwenref ipyyqliyel ktgtpvgael ltrwnhperg
      241 iltpneflsv lekqglilnl dlymleeack kiknwieeel vtvpitvnvs klnlhredfl
      301 pkvldivkry dipgvllile ieesiivtel dselihtine lrdygiqism dkfaateyss
      361 lnvlryvpid mikvnpsffp ggdadrreki fvrnvfrmlr dlgiravaer aetmediakf
      421 ekygcecaqg fyyskpmcde efekiif
//
LOCUS       WP_006444772             283 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [[Clostridium] hylemonae].
ACCESSION   WP_006444772
VERSION     WP_006444772.1
KEYWORDS    RefSeq.
SOURCE      [Clostridium] hylemonae
  ORGANISM  [Clostridium] hylemonae
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 283)
  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 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   3  (residues 1 to 283)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 283)
  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   5  (residues 1 to 283)
  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   6  (residues 1 to 283)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="[Clostridium] hylemonae"
                     /db_xref="taxon:89153"
     Protein         1..283
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31695
     Region          21..101
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..280
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mewierlnka vnyieenite eldyaqaart accstyhfqr mfafmagvpl seyirrrrmt
       61 laaadlqnkg akvldialky gyasptafnr afqsihgitp ssakkegavl ksfppisfqi
      121 tikgveemny rieakesfri igiseplhkd ieenfsvvpg lwqkaaadgt igalakmmng
      181 rpmgllgvsa chdedewryy lavssdmelt gsleeyhvpa atwaiftgsg tnrsiqeleq
      241 rivtewlpgs gyeyadapdi evylnadpdn aqyevwipvr qkd
//
LOCUS       WP_006445334             276 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Alicyclobacillus].
ACCESSION   WP_006445334
VERSION     WP_006445334.1
KEYWORDS    RefSeq.
SOURCE      Alicyclobacillus
  ORGANISM  Alicyclobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Alicyclobacillaceae.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 276)
  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 276)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Alicyclobacillus"
                     /db_xref="taxon:29330"
     Protein         1..276
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31062
     Region          29..80
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mvnqgrvkkg wtenwfrtpn siyevdyvsg yakavyiflc rcadaegqsf pgynaiakai
       61 gfgrtrtiea ikeletvgll ikehrrneet geyysnlytv ihpddvplgg glssgdrpis
      121 pydrpvshgd iplsshdrpv spddrpmsrg vrevrskdqd plvktyldth keaasaiemt
      181 nqrqvpydsh nevcdsinqs llqlgiraqr ktilnwlqia qpeeiieaay latregvksp
      241 agyigsilrn gliqvektns tkldprynef yklfpr
//
LOCUS       WP_006445326             639 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Alicyclobacillus
            hesperidum].
ACCESSION   WP_006445326
VERSION     WP_006445326.1
KEYWORDS    RefSeq.
SOURCE      Alicyclobacillus hesperidum
  ORGANISM  Alicyclobacillus hesperidum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Alicyclobacillaceae; Alicyclobacillus.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 639)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Alicyclobacillus hesperidum"
                     /db_xref="taxon:89784"
     Protein         1..639
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=73424
     Region          49..623
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mfgrkktkri lehdpsvige haptlhdlmt ladgievrts evyvspsgyt ktfyvtglps
       61 tvhfgylqrf frvgadvhis mhvepadsal aiskrtklmt kieaeilaeq kagtnkqlaf
      121 lqqeyhllek ereelrlgae rlfyvtvvla vsspdrhefe aaceriereg fegflireaf
      181 kehdlgfrsv apigenvlrh piemtasala nsfpftnsrf sheygvpigv dwssghlnry
      241 dawhkklvna naviigkags gksffvkglv arsaamgirh aivdyegeyt pmvqalggvv
      301 iridenspyk fnpfeleeee ekqsdgtirr fvdvkekisd merlivsmah lhaghdllds
      361 ytrnaindml qelyeldfgf tpdpeslyer hetwqrdakg drlvrrvkrp qprfsdfyak
      421 learaandsr leelamrlrr freggtegmf dcysnvelqd vpvvsfdlsr lpeksmarkl
      481 gmqvvlewim ekfikknvhl kkrviideaq kmlehpeham fmedinrrir krsgsavaas
      541 qdfrkfaese qgrailqnsd tkvllrqdkl dkeavienfg leehefeeli afrdgqarww
      601 vggevfynql vpfadefelf ttrfvqsdae lamqrrwla
//
LOCUS       WP_006445745             821 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Stenotrophomonas sp. Sm6012].
ACCESSION   WP_006445745
VERSION     WP_006445745.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. Sm6012
  ORGANISM  Stenotrophomonas sp. Sm6012
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 821)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 821)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 821)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Stenotrophomonas sp. Sm6012"
                     /db_xref="taxon:3002745"
     Protein         1..821
                     /product="TonB-dependent siderophore receptor"
                     /function="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89101
     Region          72..121
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          98..818
                     /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 mgymkikral varafstgvq atrlpllavc issalaapai aqaqpaqrmp fnipaqplda
       61 alrrfseqsr qqvlfsesav agrrapavtg sytpqealar llegsgvrvn atrpgvftla
      121 qdaasparsk daqttlqtvn vtangpgdgs yttrelslgk lgqsirqtpq svsvitrqql
      181 ddrnlttlde alaqttgvtk tarnfgnhkf sirsftvdds nylvdgvagi vyapvgwlpi
      241 dtavlervev lrgaggmmlg aadpsgainm vrkrprdqah ldlaatlgsw dnyrlevdgg
      301 gplnaagsvr grlvaayqdr dyfqrgtssk tpvaygvida dlgqdttltf glrhqasdtd
      361 gywlfglpry tdggaldikr stsliqdwnr qegsvdeafa eaehrfnerw karlsvnrte
      421 sdldqrvavp vggvdratgi gsrfydiyfn rsrvrsdgid lhttgsfdaf grthqlllga
      481 mwsrqrtrqs sadlaidvpi dvyapdhsai aqplqpawdw senaraqqsg vysnlrlqla
      541 aplhltlggr lswvkyqsnd gftgarsrdy eqkheftpya glvydlgpqw svyasyadtf
      601 qpqssyvtss gavldpaiga nyelgvkgel ndgrlnvsaa vfsirktgna vvdasdsgsc
      661 pgslassdcy rnggklrskg feleasgela pgwqmmagyt hvtsrddega tisaetprhl
      721 lrlstsyqlp grwnafsvgg gvsaqssysy payddpdwrm gaagravwdl ragyrinprw
      781 svgvnvanlf dtryyamisq irrgnffgep rnvmltlrga l
//
LOCUS       WP_006446980             338 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Alicyclobacillus hesperidum].
ACCESSION   WP_006446980
VERSION     WP_006446980.1
KEYWORDS    RefSeq.
SOURCE      Alicyclobacillus hesperidum
  ORGANISM  Alicyclobacillus hesperidum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Alicyclobacillaceae; Alicyclobacillus.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 338)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Alicyclobacillus hesperidum"
                     /db_xref="taxon:89784"
     Protein         1..338
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=37555
     Region          95..326
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 msceacaasp vrvvlripes dltavraslg nnageiwlgg gmmslppeav tarirywqef
       61 fdtslwaagl gnnrglgtee lqpfdvwaqg lppvwldell argglrmaiq pivdvgsgsi
      121 vacemlvrav saagdfispg alfqaardqs rlfaldracr ieaiaaatql psdwyvfinf
      181 vptsiyvpeh clrstveatr khglaksrlv fevvetelve dlehlrrild fyrregwqya
      241 lddfgegysd etmlraiqpd vvkldrqfvd hvdadpakrr vaeglaqvak slgvrllaeg
      301 verpqealll rdlgylwqqg ylygrptfdv pvehinwr
//
LOCUS       WP_006447032             665 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Alicyclobacillus hesperidum].
ACCESSION   WP_006447032
VERSION     WP_006447032.1
KEYWORDS    RefSeq.
SOURCE      Alicyclobacillus hesperidum
  ORGANISM  Alicyclobacillus hesperidum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Alicyclobacillaceae; Alicyclobacillus.
REFERENCE   1  (residues 1 to 665)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 665)
  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   3  (residues 1 to 665)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Alicyclobacillus hesperidum"
                     /db_xref="taxon:89784"
     Protein         1..665
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=72405
     Region          1..665
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdisqyldsf laesednlat lddlclaler dgasddtlaa mfraahtlkg msatmgfmam
       61 adlthhmeda lghirnhpte fqpsvvdtll aaidaltanl dqirdrgsee gidhsailqr
      121 laavvetqns rsvegsteag ppvafrdrva eilrsgrepl viqiafapec tmkavrllmv
      181 eravesfgec aavypdvqal eadadastay lamlvahqda dalltairei seittavvve
      241 lesivsasge remnqarqet aatvavatan etpahhaaap stggkvrdqt lrvpvsride
      301 fmnvlselvi aktrlellaq rgdhalrevt eqiarltssl qdgvmqmrmm pveslfqrfp
      361 rmmrdlqktl grefefvmtg letemdrtvm demgealvhl lrnaadhgle ppevrerngk
      421 prkgtirlsa yasgghvyle vaddgagidr drvlnsaigk glvdersaqn wtdaqvydll
      481 fasgfstaek vsdisgrgvg ldavrgkves lggdirvesv pgqgttfvie lpltlailpa
      541 mlvqldnyiy aiptgsveev arlsaedids iqeqpvyryr dgvvpivdlg drffdapcrg
      601 dypwnavick egkrrlaliv ddivdelgiv nkplgrylgq vemfsgatil gdgrvaliid
      661 vrqlf
//
LOCUS       WP_006448511             666 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Xanthomonas].
ACCESSION   WP_006448511
VERSION     WP_006448511.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 666)
  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   3  (residues 1 to 666)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..666
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=70836
     Region          3..659
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msmdlqrfha tffeesregl dameagllsl eegnrdpeii nsvfraahsi kggaatfgfe
       61 avaglthvle tlldelrsnk rqlapnavda mlgsvdvlra llreaehgtp adpaavkavh
      121 trlnavlage apvaavvakp keeepeawhi gftpapslfm sgndplriir elehlgplqi
      181 aarlermpgf enidpleayl awdlgligki prskiedtfa wvvddceldi rpmavpgppp
      241 slavdaadta avavaataaa epaaavatpa kaaaaeaess irvsvdkvda linlvgelvi
      301 tqamlkqvst gldpahaeql fagldllern trdlqeavig vrmlpvdavf rrfprlvrdl
      361 ssrlgkqvrl rtigesteld kgliekiadp lvhlvrnsid hglempdarr asgkdetgti
      421 tlaashqggh ivievsddgr glnrakilek aaergiavpd nptdaqvwdl ifapgfstad
      481 avtdlsgrgv gmdvvrrniq glggevqles sagsgtrvli rlpltlaild gmtvsvaget
      541 lilplsyvle alqpapedvr smagdgrvlr vrgeylpils ltnyygfggq qsskeslvvv
      601 vegdgqkial evdellgqqq vvvknienny rripgvsgat ilgdgrvsli vdigglvrsl
      661 kvpqaa
//
LOCUS       WP_006449132             362 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Xanthomonas hortorum].
ACCESSION   WP_006449132
VERSION     WP_006449132.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas hortorum
  ORGANISM  Xanthomonas hortorum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Xanthomonas hortorum"
                     /db_xref="taxon:56454"
     Protein         1..362
                     /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=39258
     Region          26..305
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mttapyssaa rhdssgaraa papaltrdwq idaakalaiv lvvlghasgm paayklfays
       61 fhvplffvls gwvgerfgrr amtvatikkl artllipyla fflvayacwm lmgvtsraah
      121 pshslpwwdp faglfwanga slyvlpalwf lpalfvttla yialrarlst tvlaatclpl
      181 alawagwfps lqlrlpfald vlpvalffia vggwlsryad alrslgamaw alalpvlaaa
      241 wwwlaawngq vdvnnlqfgq saavfllvsl lgtamtlcva yfvrqwrwlq wigantllil
      301 cthtlvflvl tsvvartgvi apsmigtpaw amslcpvaiv asvpmravlv riapwmlglk
      361 gk
//
LOCUS       WP_006448713             354 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Xanthomonas hortorum].
ACCESSION   WP_006448713
VERSION     WP_006448713.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas hortorum
  ORGANISM  Xanthomonas hortorum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 354)
  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 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   3  (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   4  (residues 1 to 354)
  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 354)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Xanthomonas hortorum"
                     /db_xref="taxon:56454"
     Protein         1..354
                     /product="CmpA/NrtA family 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=38372
     Region          2..251
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 msqanlpvlr vaymplidca pliaaqrlgl drahglqlel qrqaswagvr drllagevda
       61 ahalaslvya idlgiagpqc pmallmtlnh ngqaitlapa laqaladghg lpqvltglgr
      121 ravfaqtfpt gthalwlyyw laacgvdpmr dvdvlsippp qmpealasgl vdgycsgepw
      181 aavaeaqgsg rrvirsgelw aghpekvlac rrefaalqpe lterltacvl eacrwldaap
      241 gnrtqcaqwl aepqhigvsa ahlaacldad iemhandata lafhrngavn mpwlsdgewf
      301 ltqfqrwgwh dihdddiarl rdihrldnyr raaasvgvav pdddhrsnrl fdal
//
LOCUS       WP_006450491             351 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Xanthomonas hortorum].
ACCESSION   WP_006450491
VERSION     WP_006450491.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas hortorum
  ORGANISM  Xanthomonas hortorum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 351)
  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 11482063
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Xanthomonas hortorum"
                     /db_xref="taxon:56454"
     Protein         1..351
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=36797
     Region          1..343
                     /region_name="PRK06132"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:235709"
ORIGIN      
        1 mpmrplltsv flctllicgh alavpfwgar qsspaetapa qlkpgewiwg gvskgwgpma
       61 vivslteqra yayrngilig vstissgkpg hetptgvfti lqkdkdhrsn iynaapmpyq
      121 qrltwdgval hagglpgype shgcvhlpse farllfdnsn mgmvvvvaqa gmdadavvhp
      181 ralspidptt gaqrallplp ngqafawqpe laptgpisml vsssdqqlvv yrngveigra
      241 qvalhaqpga aplgtqafiv gqgflpgevp glpgqrmpnw mrigipgssa aagqaldadt
      301 iarlqvppaf lagllplltp gvvlvatdqr ilpettggkl qvlnsdppea p
//
LOCUS       WP_006450645             326 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Stenotrophomonas].
ACCESSION   WP_006450645
VERSION     WP_006450645.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 326)
  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 326)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..326
                     /product="AraC family transcriptional regulator"
                     /function="AraC-type DNA-binding domain-containing
                     proteins"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35623
     Region          67..321
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          235..317
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mvdggvgdsd dsglrsidla tlsgvlrvcd velllldgng praafasrvh eealfcsisc
       61 gfhcrgrfml ppdwamlgyl hatdetlswc hgipltpgma ltvmpegise ftlspgthlt
      121 lmlvpvarvq rkltelslrs tppagqalsl fnlssesapl arhyqqlhvq lgqggnlepe
      181 eaerllhehv qallgagaad rpgcsrarrt hyliaqraen fmrlnlrrni ymneicdaag
      241 vserglryaf edlfgtspnr ylsmlrlcaa crslsmadss rrsvkaials cglwdlsrfa
      301 dnyrkvfgel prdtlmrapa qigqpa
//
LOCUS       WP_006451574             261 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Xanthomonas hortorum].
ACCESSION   WP_006451574
VERSION     WP_006451574.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas hortorum
  ORGANISM  Xanthomonas hortorum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  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   3  (residues 1 to 261)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Xanthomonas hortorum"
                     /db_xref="taxon:56454"
     Protein         1..261
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29391
     Region          45..257
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 msqgdtseld hdadhlaegd eryllrnkrq irgllrqlld qragvtmhva grdmavptav
       61 levdedddcv ildgshneas nraiedakyl lcyaqlervn irfrletpdr lerdihvafr
      121 aalpdamyhm qrresyrlet pitdspicti rqdeaqggtl nlqlrvidis sgglavaivd
      181 gmpllepqrt yrnctlqlpd tapitlpltv csqykqslpn gsegfrvglq fsdlprgade
      241 tiqryifrvd rqrnarksgv f
//
LOCUS       WP_006451663             382 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Xanthomonas hortorum].
ACCESSION   WP_006451663
VERSION     WP_006451663.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas hortorum
  ORGANISM  Xanthomonas hortorum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 382)
  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 382)
  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
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 382)
  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   5  (residues 1 to 382)
  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   6  (residues 1 to 382)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 382)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 382)
  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 20170230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Xanthomonas hortorum"
                     /db_xref="taxon:56454"
     Protein         1..382
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39577
     Region          <18..>66
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          86..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 mssiatsavp lhspsfpgls lnerdmlerl rlagvltrad lsrgtgltvq tavrlieglq
       61 argmvhmgsg varagrgkpg vavslnpahg htlgisiatd altlalvdfa gqvlavsela
      121 ldagsadavl mqlqagdaal larldhapgp rlgiglamsg fftgengcin ppeplralgd
      181 falapwlaqa caqpvwmdnd gsvaaageam lgvgqrhrdf aylylsyglg gglvidgqvm
      241 rgargnagef agmlpaqkle ratlellrel laddgvefad vrsllaaydp awpaierwia
      301 rsapgvsliv saitavcdpe aivfggrlpa dlaqrliaav qidnqprrgq grpmplllpa
      361 eapadacaig aatlplkary fr
//
LOCUS       WP_006454898             921 aa            linear   BCT 20-JAN-2025
DEFINITION  AAA family ATPase [Synechococcus sp. PCC 7335].
ACCESSION   WP_006454898
VERSION     WP_006454898.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus sp. PCC 7335
  ORGANISM  Synechococcus sp. PCC 7335
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 921)
  AUTHORS   Liu,Y., Sung,S., Kim,Y., Li,F., Gwon,G., Jo,A., Kim,A.K., Kim,T.,
            Song,O.K., Lee,S.E. and Cho,Y.
  TITLE     ATP-dependent DNA binding, unwinding, and resection by the
            Mre11/Rad50 complex
  JOURNAL   EMBO J 35 (7), 743-758 (2016)
   PUBMED   26717941
REFERENCE   2  (residues 1 to 921)
  AUTHORS   Chen,Z., Luong,T.T. and Lee,C.Y.
  TITLE     The sbcDC locus mediates repression of type 5 capsule production as
            part of the SOS response in Staphylococcus aureus
  JOURNAL   J Bacteriol 189 (20), 7343-7350 (2007)
   PUBMED   17704228
REFERENCE   3  (residues 1 to 921)
  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   4  (residues 1 to 921)
  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
REFERENCE   5  (residues 1 to 921)
  AUTHORS   Hopfner,K.P., Karcher,A., Craig,L., Woo,T.T., Carney,J.P. and
            Tainer,J.A.
  TITLE     Structural biochemistry and interaction architecture of the DNA
            double-strand break repair Mre11 nuclease and Rad50-ATPase
  JOURNAL   Cell 105 (4), 473-485 (2001)
   PUBMED   11371344
REFERENCE   6  (residues 1 to 921)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..921
                     /organism="Synechococcus sp. PCC 7335"
                     /db_xref="taxon:91464"
     Protein         1..921
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=105724
     Region          1..917
                     /region_name="PRK03918"
                     /note="DNA double-strand break repair ATPase Rad50"
                     /db_xref="CDD:235175"
ORIGIN      
        1 mqilsvaltn fkthkeqqfd fqlgtnaicg engagktsil eaiawvlfny qgsykkedli
       61 rngassaqvr vvfissrdsr tyevqrstth gytlydpqla eklpytrikd evlpwlrqnl
      121 gvapgtdlgq lfantigvpq gtftadflls tekrkpifdi ilkveeyqet yrqsnglrry
      181 aesqvqrlkd lieqyedslk swdelknrqq qlqseitqge sylerlevkr talfeqrqql
      241 idqaeeiqql rqqqqqlnnq iksqeqtqer ivssltqaqq sanicqeqqs tyeafiaieq
      301 qieklteegk arqqldqqqh tieqslsqsq qelsrlevkl eqfsaareel aslaavisaq
      361 skleaqrdtl qqqqqkfasv rlqckalkqq qenilrevae veseigrlnr lkekqgdieq
      421 weqqltrtre qlsrltaaqq feqeirtmld rgkssqdeyr hqvaaalktl dswaqhidel
      481 sveaiapvkd alfqggllsk gtldriksil ndltqqtdkr qlekqsktlq switqaykqr
      541 aelvslptqe skrvqlsarq eqiaqqlsql tqlltteeti gcsltqveeq lrrldnpkgk
      601 qqliernler qdavdqqykt lnatrvaqvq qletvtaklk afarldeqlq aqqqlrqthq
      661 agyllylqnq qaaqqaaslq lesealalac qqsqsqkaqv dkqlavltkd fdpnaftivd
      721 kqymdvnsqa drlrgslpql kqrlieltgq idrlkataek rdqaqkeike rdrlkrfiny
      781 arkvykeagp riteryvqsi sreadrlfre llgrtnvala wsadyeitvq egahtrrfin
      841 lsggeqmcaa lavrlallkv ladidvaffd epttnmdrar raslaeaitr iksfkqlfvi
      901 shddtfehvt etvitverdp d
//
LOCUS       WP_006455287             424 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Synechococcus sp. PCC
            7335].
ACCESSION   WP_006455287
VERSION     WP_006455287.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus sp. PCC 7335
  ORGANISM  Synechococcus sp. PCC 7335
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 424)
  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 424)
  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   3  (residues 1 to 424)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Synechococcus sp. PCC 7335"
                     /db_xref="taxon:91464"
     Protein         1..424
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47462
     Region          308..414
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 msvdqqqtgf vnklslhqsr rnqsiptlst lvggtaathl lwvrwmrqtg rctavctyes
       61 lpslfcawls taisycdlqs laltrtaqla ereveqlskw layvgeyqkn qfwqhltalf
      121 pqalwlrali slgmnhpakc metltlegit lqeddptvva qgfavvsnll pdttipglli
      181 hlpsgcself frysvlpalt rlvesvpaip vgllfslsqs delieqlpes rekavvrggm
      241 vklttpkeee lrqwlgehgl hqedkiqpil haarqygatk eiliaavgla ktvsqnepan
      301 ssgdiyrshp erllfqylea rpatagqfqv naqvditfgn ramevdflad kakvvieldg
      361 syhhlrslds yrrdrrkdfa lqqegfwvlr flsedvithl edilnaidqa lalrlaeapv
      421 qmet
//
LOCUS       WP_006455610             533 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Synechococcus sp. PCC
            7335].
ACCESSION   WP_006455610
VERSION     WP_006455610.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus sp. PCC 7335
  ORGANISM  Synechococcus sp. PCC 7335
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 533)
  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 533)
  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 533)
  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 18628020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Synechococcus sp. PCC 7335"
                     /db_xref="taxon:91464"
     Protein         1..533
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=61321
     Region          1..>62
                     /region_name="COG2768"
                     /note="Uncharacterized Fe-S cluster protein [Function
                     unknown]"
                     /db_xref="CDD:442050"
     Region          481..533
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
ORIGIN      
        1 mnytikenci acdvcqplcp qdaikpnses dgywidptlc dgcpdleipl cvsacdtgal
       61 kplppkkgrc kssllpvaip siflnrktsp fasclvmwet cnilaqrqal pwtrddddri
      121 cyrrpvnrnr gemrfrlaad aetnspkpms mgageeaian fdiratcihl ifaayvmtid
      181 cpwqnafvln dqhianylgl dkrkdltkld kltliknlvh qscqvlvtln wpqqgrvgaf
      241 rleehfvwql ldtqyhfekd skghrhligl sftiksglwa khflnkqkyr sqtafyqygt
      301 lpqsllrevm grwqqhqgai rillwslfkl rlggdqrvkv rtlmrvayge eqlhqaatvr
      361 gahkrllraf esdleaicqy glkplfdpkt ypldiqplwv rvasipddvd eevnfwadda
      421 nqafgltdsa prdkwqrlln arllgfeise ewqenirrrk pkkrrkpsks wtvtqtekls
      481 gsdinlarqr qklsqrslae rlgksqswvr diengrfkvs rddqallrke ldl
//
LOCUS       WP_006459275             802 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Thiomicrospira aerophila].
ACCESSION   WP_006459275
VERSION     WP_006459275.1
KEYWORDS    RefSeq.
SOURCE      Thiomicrospira aerophila
  ORGANISM  Thiomicrospira aerophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Thiomicrospira.
REFERENCE   1  (residues 1 to 802)
  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 802)
  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 802)
  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   4  (residues 1 to 802)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..802
                     /organism="Thiomicrospira aerophila"
                     /db_xref="taxon:92245"
     Protein         1..802
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89008
     Region          68..797
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mqklrvdqly rqtqidtdaf eknetgaeaf mqrfhprayq slnfglhlkr nhnhifimge
       61 pgvgrigmtk allnkaaaak pmpddvvlva dlkeppktry lyfpagqghe fkvaieqfia
      121 qlkhqlplvf dghgyqlrsq qlerkmaaeq eevlrpafel aeqlsidilq tennfvlhai
      181 vdgkkmrlae lkslpaedqa rytealdlve aqlnegltrf ptiqhefmee gkklntqvae
      241 eqvtplikkl ksrfenevvg qylddlaqav laklhlfwdq sadqvttsnn ggsgggsasp
      301 leelmldqqg lsqfgvnllv dhrglehapv iyeqnaslpk lfgyaiqsgh qglggdtlgl
      361 amnhqagllq kanggflmls mqsilkdpei wsslkaalms rqlsfdvpst nsvvpyhlpd
      421 fplnvtlvll gqaahfyalq eidaqfsrlf kvqvefevel drtpehelal vqqlasevan
      481 wddlpvelsa yerlteyasr laedknrlyt nkailrdvla eanafarakg asqvtrdtve
      541 atiaqrefht glmedyyhra iieqqvlisl tgehigqvng ltvmtvgrqs fgqpvritaq
      601 asagdegvvd iereiemagp ihskgmlils gyvrgrymry ralgfsasiv ieqtydgieg
      661 dsasspelya llsaiaqvpm rqdlavtgsv nqfgeiqpvg ginekiegff kvckargltg
      721 qqgvvipqan vrhlmlnaev rdavdqgvfh iyaiehvdeg lallsnlevg elneeghyps
      781 hsfnghllqa lermnekpsd sd
//
LOCUS       WP_006459402             663 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Thiomicrospira aerophila].
ACCESSION   WP_006459402
VERSION     WP_006459402.1
KEYWORDS    RefSeq.
SOURCE      Thiomicrospira aerophila
  ORGANISM  Thiomicrospira aerophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Thiomicrospira.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Thiomicrospira aerophila"
                     /db_xref="taxon:92245"
     Protein         1..663
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=75850
     Region          61..616
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mnqikpeila dnsettinsq qvatlkkhfp qcfdkegnfi aeklneiiss sgtafskesy
       61 glswlgksya rllanenplt llaedkehnq kpenqdsenl likgdnlevl khlkgaysec
      121 ikmiyidppy ntgsdgfvyq ddrkftpdql aelagieqne akrileftqs kanshsawlt
      181 fmyprlyiar ellkddgvif isidnneqaq lrvicdevfg eanylglicw knvtdnnptn
      241 iateheyivv yakskdsvkp vwksflsdvk dlliqigdef nkkykdqdkl qkaytkwfre
      301 nkfqlgeldr ykyideegvy tgsqsvhnpg kdgyrydvih pdtgkpckep lmgyrfpest
      361 mkelldndrv lfgkdhnkii elkvyakdfk dklssifvld grvgatelrd lfpdvktift
      421 npkpvellkr lisfatdhgd ivldffggsg ttahsnlaln sedngsrkfi iiqidektds
      481 kkdahkagfn tifeitkari kkaaekirae npdyngdlgf qifetlpvfe gyldnietle
      541 geqgelfdgs alsddqlehl lstwkvydgi pltqrlietd lagyiayrhd rvlylmhqgf
      601 rteslkafls rldetdgddk nfdvekvvlf gynfdsknql eineavrqyq nrkektvsvl
      661 vry
//
LOCUS       WP_006460319             382 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Thiomicrospira aerophila].
ACCESSION   WP_006460319
VERSION     WP_006460319.1
KEYWORDS    RefSeq.
SOURCE      Thiomicrospira aerophila
  ORGANISM  Thiomicrospira aerophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Thiomicrospira.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Thiomicrospira aerophila"
                     /db_xref="taxon:92245"
     Protein         1..382
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42374
     Region          2..269
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          265..352
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mikllhtadw hlgrvlhhhs lladqahvln qimdyavahq vdavlvagdi ydrsmplada
       61 vrllnqtinr faelaiplim isgnhdsaer lgfaatqlhk tglhiltdiq hvaepvwlrk
      121 adtalqifgi pfadpervrh vfnqsvtdyd aahnllldqv kaardphfpa llmshcfvdg
      181 adtsesektl svggsdrvsy epmlafdyva lghlhspqsk gashiryags plkysfsehl
      241 hkkgvtllsf nsaglvaqah lplqplremr vlegtlnvll aqgqqdpqrd dyimvrltdt
      301 talldpmgrl revypnvlhl ekrllqtepl aqanpnhikl daaqlvrdfy aqiqgepltd
      361 aqsdiinatl tkllqpnqdn sl
//
LOCUS       WP_006460834             172 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Thiomicrospira aerophila].
ACCESSION   WP_006460834
VERSION     WP_006460834.1
KEYWORDS    RefSeq.
SOURCE      Thiomicrospira aerophila
  ORGANISM  Thiomicrospira aerophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Thiomicrospira.
REFERENCE   1  (residues 1 to 172)
  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 172)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 172)
  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   4  (residues 1 to 172)
  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   5  (residues 1 to 172)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Thiomicrospira aerophila"
                     /db_xref="taxon:92245"
     Protein         1..172
                     /product="TRAP transporter small permease subunit"
                     /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=19287
     Region          3..172
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mhflqlfifw qnrfqqsvgh avawlslalv lttaaavllr ygvnfsaskl desliymhat
       61 lfmlgiayty qqnqhvrvdv fyqrcslrtq twinllgail fvlpvmvfii waglsyvgas
      121 waiqekslda sglpyvyllk tlilimpglv ilqtlgliaq slltllhvee pa
//
LOCUS       WP_006461785             733 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Herbaspirillum frisingense].
ACCESSION   WP_006461785
VERSION     WP_006461785.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum frisingense
  ORGANISM  Herbaspirillum frisingense
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 733)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 733)
  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   3  (residues 1 to 733)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..733
                     /organism="Herbaspirillum frisingense"
                     /db_xref="taxon:92645"
     Protein         1..733
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79965
     Region          1..722
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mkkdsardav vqearellva meaallqiem egptrecina ifraahtikg saglfafdsi
       61 vqfthqvehl ldlvrqdrlp lnghlmslll qcgdyigelv daiergqeae epnaerrtal
      121 laelalvalt astadaaeaa gagqpaaagd avagqregtg aideltaqap adypywhlsl
      181 qfnenvlrdg ldplsflhyl rslgrivail pvesgipdaa smdaescylg veicfasgss
      241 rqtledvfef vrddsridil sphsvladya tvlqrlared aarlaglwrh hglfnetqwr
      301 clgaatvdea aapvvpvavp dtrqrprlld erraqeqkfi kievskldql idlvgelvia
      361 gasarliarr rkdsqfeeat qaidglmeqi rdaaltlrmv qinevfqrfp rivrdiardl
      421 dkdidlimtg sdteldksmv erladplmhi vrnaidhgie panerlaagk ppkatlrlna
      481 thesgsvlie vmddgrgmdr drilekavaq gltsgdedls dadiyrfvfe pgfstarqvt
      541 elsgrgvgmd vvkrniealh gevsidtegg rgtvvrirlp ltlaiisgfq vvvgnavfvi
      601 pldmvvecid mpphqsgshi vavrdeplpf vplrelfdlp erqqgrarks lvivqygqlr
      661 agllvdgllg ecqavikplg rlfgkvkgls gstilgdgrv alildiphlv hhtqqqeqgn
      721 tavyaergvt saq
//
LOCUS       WP_006462024              96 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Herbaspirillum frisingense].
ACCESSION   WP_006462024
VERSION     WP_006462024.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum frisingense
  ORGANISM  Herbaspirillum frisingense
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Herbaspirillum frisingense"
                     /db_xref="taxon:92645"
     Protein         1..96
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10275
     Region          1..96
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mkpsealash raairhvves hhalnarvfg svahgqdteg sdldilidpt petslmdvaa
       61 iqvelqhllg vsvdvltpra lpeemrrqil seaipv
//
LOCUS       WP_006461978             752 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Herbaspirillum frisingense].
ACCESSION   WP_006461978
VERSION     WP_006461978.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum frisingense
  ORGANISM  Herbaspirillum frisingense
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 752)
  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   3  (residues 1 to 752)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Herbaspirillum frisingense"
                     /db_xref="taxon:92645"
     Protein         1..752
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=80739
     Region          156..745
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mhldsasaaa rsatedsldp vagrinaslr qtllplltiv rqqdgvwrsc lgkghagavp
       61 plyrrtlltl rdcarsvgav pladiasqli mlleqhtpds plapprllqi eqgldqlarl
      121 lespgspavl tlpgseaprp imgnvmtphd vidpgllpvf leeaqelmas igetmlalpp
      181 ghrhtpadtd llaelarplh tlkgsarmvg amrlsqcvhe mesalqrlqt gevaqnadvl
      241 tallalydqt mehfsnleqa aasvpaasrs gglqsplqpp sqphfraapv lrirttvldr
      301 llnqvgevsi mrarldneva alqddvrilg dhlrtladqv gqlqrdtgaa pvaahelqav
      361 tyamdtvlaq awrqqkhlhd gvgraceglr qqgryarelq qdlmharmik fnsmesrlqh
      421 larqlaaetg kplvldlsdc rlqidraile rlmgplehll rncavhgied taarraagkp
      481 psgqlrvqag hegneavirv sddgrgldlv airgkarqrg lpaaqdasda glaelifapg
      541 fstsaqvsal agrgigmdva raevaalggr mtvhsrpgqg vlftlylpls lavqqvcllq
      601 qgrqqyaips tlidsvlqlr seqarqaleq rvlevngrrl alyplhhllr eqlepeqdad
      661 leveakaadq adtdsafall iksgdelmvi madhvngnre vvvkpvgpql atlaglvgat
      721 vlgdgqivli lnplllagsr hadssvvtpg vq
//
LOCUS       WP_006462211             811 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Herbaspirillum frisingense].
ACCESSION   WP_006462211
VERSION     WP_006462211.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum frisingense
  ORGANISM  Herbaspirillum frisingense
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 811)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 811)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 811)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..811
                     /organism="Herbaspirillum frisingense"
                     /db_xref="taxon:92645"
     Protein         1..811
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88288
     Region          66..112
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          93..811
                     /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 mpstpflsln srtagitrma ltalllalgg lglwpaeama qdrrhyeiaa gpleqalnhf
       61 arqagitlsy apdmvqgrqv valaatlave dglaqllags glqavraang syglqwrtgm
      121 geggapmpvr qqtqrlkdvi idgrgeqaef aegsegyava asqsatrtvt plleiaqsls
      181 vvtraemear gadsildvlr ympganteth gvdprgydyf nlrgfinaqn tsnylnglrq
      241 pvagfgtfrt eayglervev lrgaasasfg qadpggvvnr iskvagddap neiqagigsf
      301 qrrqlaadls atlddagrvq grlvglalds ntqfsygngs avpndrlyla pslklqlggd
      361 shlilladyl rdrsgsgrwt avrpdgslth tlvgdpgtdh qrgeqwslgw mldqrldatw
      421 rlqqnfrhaa lrsdysvlnp gslsgsvlsr ssaryqtqlt stqidtrlqg rwqqgpldht
      481 vllgldlmqm rqdeqryrgt apaldlaqpv ygmpialast lyaqlheemr qtgvyvqdqi
      541 rdgawvwtlg srhdrvtdst rndigpsrld sraqawshrl glawthypal vpylnystaf
      601 lpqagqdaag qpfapaygrq levglkfqpq gqrllytaal yqvskdnvlt adpqhanayl
      661 tqsqvrsrgv eleakgrlhp glniaaayay tqaintrhvd palqgkspvl vprhaaslwl
      721 dyspgpvwsg wgigggvryv grnyanadns vrnaavllld amlrldqghw ryalnisnlt
      781 nrqstsclae ptltcfwaee rmallsaryr w
//
LOCUS       WP_006462327             154 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein, partial [Herbaspirillum frisingense].
ACCESSION   WP_006462327
VERSION     WP_006462327.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum frisingense
  ORGANISM  Herbaspirillum frisingense
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Herbaspirillum frisingense"
                     /db_xref="taxon:92645"
     Protein         1..>154
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
     Region          <6..154
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mtltwgtdai tienyfltgy yyiekitfdd gttwaysdla srltqtgtsg nenwtgfgdq
       61 nnrmlgmagn dvltggrlad tieggsgddt lyggdgddtl sgdkgndyln gglgndiyvf
      121 nqgdgvetin dydnnvgnid tlrlgkgika adtv
//
LOCUS       WP_006464496             359 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Herbaspirillum].
ACCESSION   WP_006464496
VERSION     WP_006464496.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum
  ORGANISM  Herbaspirillum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Herbaspirillum"
                     /db_xref="taxon:963"
     Protein         1..359
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39737
     Region          1..350
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msievhhiqk rfgsftalnd vslnfpagel tallgpsgcg kttllriiag lespdsgqvl
       61 ldgedasarh vrerqvgfvf qhyalfkhmt vfeniafglr vkpraqrpse aairekvksl
      121 lelvqldwla dryppqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 rlhdelhvts ifvthdqeea levadqvvlm nkgqveqigt peavynhpas pfvygflgnv
      241 nlfhgrlheg vldaagarfe apghddtrda sgvgyvrphd ldveryapga qgivvqlrra
      301 haigplaqle lerddnaeli eavipnerfa qlglkngdtl vvrprrlqvf aqqeggtar
//
LOCUS       WP_006464874             378 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Herbaspirillum].
ACCESSION   WP_006464874
VERSION     WP_006464874.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum
  ORGANISM  Herbaspirillum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae.
REFERENCE   1  (residues 1 to 378)
  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 378)
  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   3  (residues 1 to 378)
  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   4  (residues 1 to 378)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 378)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 378)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Herbaspirillum"
                     /db_xref="taxon:963"
     Protein         1..378
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39867
     Region          31..367
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(107..109,129..130,179,231,255)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mfkrvsglni iaaslalipa famaqeaqvv kigfsspltg pqasagkdnq gglmmaverl
       61 naqpitvggk kikfeviaed dqadpkqgva vaqkladqgv kaivgpynsg vtipasrvyn
      121 dagivvatva snpkitqqgf atlfrvaasd sqlggkmaly aakelklkrv aviddrtayg
      181 qglaeefakv akangievvs kdftndkatd ftailtsikg kkpdavflgg yapqggpikr
      241 qmkqlgidvp lmggdgicsp emgrlggdai getvyctqgg tmldkakdgk ifsddyqkky
      301 srpaetyavs fydgmmliaq amkqansiep kafgpalaki sykgvagqyd fdanhdlkqs
      361 pvtvyrfkdg lpvpltsy
//
LOCUS       WP_006465246             101 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein
            [Herbaspirillum].
ACCESSION   WP_006465246
VERSION     WP_006465246.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum
  ORGANISM  Herbaspirillum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Herbaspirillum"
                     /db_xref="taxon:963"
     Protein         1..101
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10708
     Region          1..96
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mrpsvaldmk rvavreavgr frtanlrvfg svlhgtdgdg sdidllvdal pgatlldlgd
       61 ledelksllg vdvdlltped lpptfrakvl aealplfpsk d
//
LOCUS       WP_006465189             293 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Herbaspirillum
            frisingense].
ACCESSION   WP_006465189
VERSION     WP_006465189.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum frisingense
  ORGANISM  Herbaspirillum frisingense
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Herbaspirillum frisingense"
                     /db_xref="taxon:92645"
     Protein         1..293
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31622
     Region          13..258
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mnaqllvdgh helgegvlwc ersqtvfwtd ihasrlwnhd pqsgatrswp mperlccfaf
       61 tadperllig lasrlaffnl gtgaitpicr ieddlpttrl ndgrcdrqgr fvfgtlneda
      121 grapiasfyr lnadlslerl plpgiaisns icfspdgtrm yhcdsmegki mvcdydpasg
      181 aianqrvfad laqqpggpdg stvdadghvw naqwggarvv rftpdgridg ivdmptaqps
      241 cvafggaald tlfvtsaheg msarqreqda lagalfavpe tgvrglpevr fag
//
LOCUS       WP_006465502             342 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Herbaspirillum frisingense].
ACCESSION   WP_006465502
VERSION     WP_006465502.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum frisingense
  ORGANISM  Herbaspirillum frisingense
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 342)
  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 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 342)
  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   4  (residues 1 to 342)
  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 342)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Herbaspirillum frisingense"
                     /db_xref="taxon:92645"
     Protein         1..342
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38171
     Region          66..220
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          249..327
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mdldlhavqd sapllllehd ssptsvaptr seadlaavar fhamqqellq llerytagse
       61 gmlataipdl eiyritcptg pkhavqkpvf aviaqgskri fvgdeiyeyd pmhylvasvd
      121 lpvvgkvmvt spdepylglr leldtqeige ligdenlpaa ahltegaarg lyvnrldvel
      181 ldavlrllrl hesprdvail apmirreily rllmngqgal lrqtvlqdsq mnrvakairl
      241 ikdgydqalr iedvarevhm svsslhhhfk mvtamsplqy qknlrlqear kliltadasv
      301 ataahrvgye sssqfsreys rlfgapplrd krrwqeeeap ml
//
LOCUS       WP_006466849             198 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein [Brucella].
ACCESSION   WP_006466849
VERSION     WP_006466849.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..198
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=20002
     Region          66..150
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mfrttllttt calliggsaf aqtatpspap aeapattqdm pvsskdmfgk pitgeagkvg
       61 fvepkegqll vssfigrsvy esdapdaqsv gklndliasp dgqieaaiig vggflgvgek
      121 dvavspdqlq latrsdgktw lvikankqql ndapafdrsk ffadgvadps aatetnapat
      181 dtpasgtapa paspapaq
//
LOCUS       WP_006467646             196 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Brucella].
ACCESSION   WP_006467646
VERSION     WP_006467646.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            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="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21726
     Region          1..165
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlrrlydwti slaarksaew wlaiiafves svflvpadvl flpmalarpe rawryafiat
       61 vssvlggiag wylgyhayeq iakpvlemyg kldtfeqlrg ttsadaillm litsglahlp
      121 pikvvtilsg aaginiwlfi asaiaargar ffflawllrr ygepirhfie krlgliasvv
      181 avalialffa vkylha
//
LOCUS       WP_006467669             284 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein [Brucella].
ACCESSION   WP_006467669
VERSION     WP_006467669.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            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="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=29688
     Region          47..131
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
     Region          179..259
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mkrflastal aalialpafa qdrspifsde kqekpiasen gyfvaspgql lvsgfigqav
       61 yngpsndaan igtvndmilg adgspqavvi gvggflgvge knvaigfdrl swvvredgkr
      121 wlivdatkeq lekapafdrn tafaadgapr aeppaaekti ttqkadrvmp egmkpvpseg
      181 lsadkligat vfgadetkig tvgdvlmsad gqteafvvdv ggflginskp vavsianldv
      241 asgkddklnv ftqftkeqle aqpaysdeay kkdpegtilh geae
//
LOCUS       WP_006469998             705 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter permease [Brucella].
ACCESSION   WP_006469998
VERSION     WP_006469998.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 705)
  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 705)
  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 705)
  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 705)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..705
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..705
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=75273
     Region          1..699
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 maqsektaae taiesaehip gwgsgagari lfaiavafsv fqlwtsaysp lpsqvvrsvh
       61 vgflllllfg lyanaatdaa rrtvfwlaav vafalslyhw ifyedllira gepshtdivi
      121 gvlavglvfw agkkmmgwtl plicliflay glfgqylphp fnhrgydfeq vvevlflgte
      181 giygtpiyvs ssyiflfilf gafleragmi qlfndiamgt vgasrggpak vsvissalmg
      241 tingsgvanv vttgaftipl mkrsgfrpaf aggveavasm ggqimppvmg avafimaetl
      301 glpyveivka aivpailyfi tvfvmvdlea rrlrmkglnk sempsaleai rrrwflilpl
      361 aalvwllfsg ytplfagtvg lsltaliilg vpvsgglsmp lrvlfwialg vmsaaafgtt
      421 fnifgyalrg itliillval lvainfavrg gretlslcle slaegaknal pvgiacalvg
      481 viigilaltg agstfarviv svgenslffs lvltmlaclv lgmgiptipn yiitssiagp
      541 allhlevpll vshmfvfyfg imadltppva laafaaapia resgmkigmq airiavagfa
      601 vpfmavyepv imlqeggplt ekygfwlafa ymlvkallsi llwgaaaigh lrtplqlwer
      661 iwafvaialm latypysdel gfaacaafli whfwrsrpsv vassg
//
LOCUS       WP_006469997             683 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter permease [Brucella].
ACCESSION   WP_006469997
VERSION     WP_006469997.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 683)
  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 683)
  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 683)
  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 683)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..683
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=72555
     Region          16..678
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 msedqnvkla pmeldevkar eleeqfdtei rfrplaplsa rivggllivl slfhyytagf
       61 gilsemvhrg ihlsfvlglv flvfpfsrtg ydkpavssll rplgisiidw alaivavvav
      121 lhvplipldd lafrvgnptt tdvvlgglli lilleatrrs vgwplpiisi lfmlyalygp
      181 smpgilvhpg atvsqlvnhl ylttqgiygi algvvatyvf hfvlfgvfat riglgqlfld
      241 caawvagrfa ggpakvsifg salfgmisgs svantvtvgs ltipamirlg ykrhfaaave
      301 sasstggqit ppimgaaafl mieflnlpyt tiilaaivpa fmhffgvlmq vhfeakrngl
      361 rgmtreelpd lkeafkrdwp tviplivlig vllsgytpyl aafwgitlci avgllnprkr
      421 mtvseifdgl rdgakyalav gaaaatvgii vgvvtltgvg fkisyivtst agqlaaffgt
      481 vlpaswfgpq tltllftlim tgvvcilmgc gipttanyii matiaapalg llgvepivah
      541 ffvfyygvla ditppvalaa yaaagmagad pfktgntafr lglgkvlvpf vfvfspslll
      601 vtsgfnwadf llaflgcaig italgaalsg fflvrtkawe nvlmivgaml lvapeiyssa
      661 vgllllvpvl irhlaarkep aai
//
LOCUS       WP_006470287             363 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Brucella].
ACCESSION   WP_006470287
VERSION     WP_006470287.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
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   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   3  (residues 1 to 363)
  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   4  (residues 1 to 363)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 363)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 363)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 363)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..363
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37840
     Region          32..341
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(96..98,119..120,172,224)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mielgkrpaa altsiilsll assvlaqaad mriglaapls gtfaplgnql aegariaaat
       61 kgaelvisdd rcdaeggrea aehfvrenvr ivtgflcpda leaalpvlaa gniaivasgv
      121 septlterra papmavfrla tgldketqat gsflgslwra qafaviddgt iegreraarv
      181 laslkeqqlq pvftdtyrpg ldnqnalvar lrragathvy vggerddiaa igasaaalnh
      241 pltiaggsll daapgaqpls qgtlmiapvr pqdlstakpa idalhqaakl adayaiigya
      301 saeiaadail radekkqpvl dtlrtgsfet vlgtikfddn girtdnpnrl qrfdgkrfvl
      361 adk
//
LOCUS       WP_006470323             219 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Brucella/Ochrobactrum
            group].
ACCESSION   WP_006470323
VERSION     WP_006470323.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..219
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22138
     Region          <1..195
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 matleggayd dvlfgsrfdd firahggddl vfggdgndtv fggngndilf ggtgndtlfg
       61 engndilfgn egndvlsggn gsdvlyggng ddilqggngs dllyggahnd ilyggngndi
      121 ldggagndvl iggngsdtfl fnggggndvi ldfnpgedil qiqkgingld issaddladr
      181 vtqvggnvvv dlgngdtvtl vntnaddvqa hpdqyftvh
//
LOCUS       WP_006470631             193 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase
            [Hyphomicrobiales].
ACCESSION   WP_006470631
VERSION     WP_006470631.1
KEYWORDS    RefSeq.
SOURCE      Hyphomicrobiales
  ORGANISM  Hyphomicrobiales
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Hyphomicrobiales"
                     /db_xref="taxon:356"
     Protein         1..193
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20512
     Region          3..189
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mstqrliigi tgasgaaygi ralelaraag vethlvvsrs alltlnqelg lqkadlegra
       61 dviypvadig atiasgsfrt mgmliapcsv rtmseittgv tstlmsraad vvlkerrrlv
      121 lmlretplhl ghietmaalt rmgaiimppv pafyakpqsl delvthssar aldlfdidtg
      181 avrrwgglke slt
//
LOCUS       WP_006471261             371 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Brucella].
ACCESSION   WP_006471261
VERSION     WP_006471261.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
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   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   3  (residues 1 to 371)
  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   4  (residues 1 to 371)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 371)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 371)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..371
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39223
     Region          27..358
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(99..101,122..123,172,224,248)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkksllagva laavmsfggs awadvilgig apltgpnavy gaqiqkgaea aikevndagg
       61 ingekitisl gddvsdpkqg isvankfaad gvkyvighfn sgvsipasev yaengileis
      121 paatnpvyte rqlwntfrtc grddqqgiva gqyifdhfkd akiavihdkt pygqgladet
      181 kkklnelgtk ealyegvnvg ekdfsaliak lkqagvtvvy wgglhpeagl iirqmadqgv
      241 kaqfisgdgi vsnelasiag pavegtlntf gpdprnnpnn aelvkkfrda gfepeaytly
      301 syaavqslaq aakaagsndp qeiakalkek gpfktvlgdl sydekgdpkl pgyvmykwek
      361 gadgkytyvq q
//
LOCUS       WP_006471521             302 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Brucella].
ACCESSION   WP_006471521
VERSION     WP_006471521.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 302)
  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 302)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 302)
  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   4  (residues 1 to 302)
  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 302)
  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 12071874
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32510
     Region          19..169
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          197..278
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 maslirqlap heghtkslld gvrlmradhp lgrtpvlyep sivivcqghk rgylanqvyh
       61 ydaqhylvls vplpfstete aspeepllav svrldmtava dliievdqqa tspasppagi
      121 vstpldatla dttvrllral csplearvlg paivrelcfr vlvggqggai raalashgnf
      181 griarvlrri hsdyaqqldv sslaseagls tpafhahfka vtatspiqyi ksvrlhqarl
      241 mmirddvtaa gaaarvgyes asqfnrefkr lfgrspgeea remrsafalm apaqleavaa
      301 th
//
LOCUS       WP_006472956             443 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Brucella].
ACCESSION   WP_006472956
VERSION     WP_006472956.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 443)
  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 443)
  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
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 443)
  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   5  (residues 1 to 443)
  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   6  (residues 1 to 443)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 443)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 443)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..443
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=47964
     Region          61..113
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          125..428
                     /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 mvrhkverep dsgsaesvpa tpsgiisrtl sgtpgpamqq fagpganvnr gsnqigvray
       61 nerlvlalvr rhgalaradi arltglsaqt vsviiralek dglitqgerv rgrvgqpsmp
      121 mrlaadgvfs fglkigrrsa eiilmdflga irerrhityr wpvpdeirsf tidsvnafta
      181 aleparrdri aglgialpfe lwnwveevga paedldawlg adlvsdfaha fsfpvfiqnd
      241 gtaacgaelt fgrgpeftdf vyffigsfig ggvvlnntly pgrtgnagal gsmpmrmrgt
      301 wergetlqli dtaslfvler mlqerhlpsd dlwlspenwr nfgtpldewv alaarglaha
      361 avaaasvidf paavidgwlp gnvrhrivea trvelscldl qglrapeiie gkvgvhakam
      421 gaaslplsnr ylfdqsvlfk das
//
LOCUS       WP_006473606             397 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Candidatus Endoriftia persephonae].
ACCESSION   WP_006473606
VERSION     WP_006473606.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Endoriftia persephonae
  ORGANISM  Candidatus Endoriftia persephonae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Candidatus Endoriftia.
REFERENCE   1  (residues 1 to 397)
  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 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   3  (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   4  (residues 1 to 397)
  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 397)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Candidatus Endoriftia persephonae"
                     /db_xref="taxon:393765"
     Protein         1..397
                     /product="CmpA/NrtA family 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=43978
     Region          43..324
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mkqsnngnhg rrgflkksll alatasvigg milgsaavra eigdpekeel kfgfikltdm
       61 aplaiayekg yfedeglyvt leaqanwkvl ldgtidgqld gahmlagqpl aatigfgtka
      121 hiitpfsmdl ngngitvsne twkqmkpyvp kqpdgksvhp ikadalkpvv dkfkeegkpf
      181 kmgmvfpvft hnyelrywla agginpgyya phkgdtsgtm kadallsvtp ppqmpatlea
      241 gtiygycvge pwnqqavfkg igvpvvtdye iwkdnpekvf gmtkafteky pnttvrvvka
      301 liragkwldd nnnanrpeav kilsqsnyvg adydviansm tgtfeyekgd krevpdfnvf
      361 frynatypyd sdavwyltqm rrwgqisdry rhspgyh
//
LOCUS       WP_006475222             190 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Candidatus Endoriftia persephonae].
ACCESSION   WP_006475222
VERSION     WP_006475222.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Endoriftia persephonae
  ORGANISM  Candidatus Endoriftia persephonae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Sedimenticolaceae; Candidatus Endoriftia.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Candidatus Endoriftia persephonae"
                     /db_xref="taxon:393765"
     Protein         1..190
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21476
     Region          3..164
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mrlfsalysr amqwsrhpha prylaglsfa essffpippd vmlapmslaq pnrawylaal
       61 ttaasvlggl lgyfigvfaf eliepwlhel gywekylhtk iwfdewgfwa iflagfspip
      121 ykvftitagv iamalfpfll aslvgrgarf flvaglmawg germevalhr yvdrlgwmli
      181 vlfaviflim
//
LOCUS       WP_006476469             167 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Burkholderia cepacia
            complex].
ACCESSION   WP_006476469
VERSION     WP_006476469.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 167)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..167
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18021
     Region          8..160
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mftlsndpta skadqyatlv eqarslvese rdltanaanf salvyhsldr lnwagfyffd
       61 gtelvvgpfq gkpacvrial gkgvcgtaaq tretqvvrdv hdfpghiacd aaseseivvp
      121 lvaddgtlig vwdvdspvaa rfddedrtgm ealcrvfveh awqkarg
//
LOCUS       WP_006477067             198 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Burkholderia].
ACCESSION   WP_006477067
VERSION     WP_006477067.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..198
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21147
     Region          8..193
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 maspsapprr livaitgatg viygvrlldl lraaggveth llisnagwln iqhelklpka
       61 dvesradvvh svrdvgatia sgsfatdgmv iapcsmktla svahglsdnl itraadvtlk
      121 errrlvlmvr etpfnlahlr nmtavtemgg ivfpplpafy ampktieelv dqtvtrvldl
      181 falsaplttp wpgirhaq
//
LOCUS       WP_006477221             672 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase [Burkholderia
            cepacia complex].
ACCESSION   WP_006477221
VERSION     WP_006477221.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 672)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..672
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=74542
     Region          67..542
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mektmqklda aspqamstdf tadnvarlka lfpelvtegp dgasvdvdvl kalvgertvd
       61 daderygfhw hgkraarqaa ltpstgtlrp cpddsvawdd trhlviegdn ldvmkllhks
      121 yagkvklvyi dppyntgsdf vypddfsdsi rhylamtgqt eagvkrstnt eangrfhtdw
      181 lnmmyprlkl ahallsdegl iavhidehev halvlmlrei fgeenelgva vwdkrnpkgd
      241 argvayqhes lvlfarnaet lleraplkrp krnaqrmlda ahdavyrsgn pkdaqkayra
      301 wmkaqtnlsg gevmydrlsp egrvyrlvsm awpnkkkapd eyftplihpv tgkpcampar
      361 gwrnppatmq allergqief gpdettqpqr iyyldenmye nvpsvlpfag sddallktlg
      421 ipfdlpkpvd faaavigwct rgddivldcf agsgstghav mqvnatdgga rryilvqlpe
      481 aldrrdktqt aaadfcaklk kpltlaeitk erlrraaqqv ardypesygd lgfrvyrldt
      541 tnviewdprr ddfdhalfas vehvktgrte ddllaeltlk lgldlctpve hhqvagktvh
      601 ligraivacf darisrddag pladgivdll dasgasrdvt clfrdsgfvd dvaklnlaal
      661 leqhgvkrvr sl
//
LOCUS       WP_006477293             379 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Burkholderia cenocepacia].
ACCESSION   WP_006477293
VERSION     WP_006477293.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   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 379)
  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   3  (residues 1 to 379)
  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   4  (residues 1 to 379)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 379)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 379)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 379)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..379
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39964
     Region          29..365
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(105..107,127..128,177,229,253)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mqhtmkkvag atfvavmsla gtahaddvki gyagpmtgaq ahygkdmqng ivlaledfna
       61 tnpkiggkav kfvldtqddq adprtgttva qklvddgikg mlghfnsgtt ipasriyana
      121 gipeiamata peytqqgykt tfrmmtsdtq qgsvagtfas kdlgmkkiai vddrtaygqg
      181 ladqfekaak aggativdre ftndkavdfk ailtklkaak pdlvyyggad sqaapmvkqm
      241 ktlgitaplm sgemvktptf lkiagnaaeg tiaslaglpl eempggkaya dkykkrfged
      301 vqtyspyayd gamamlnamk kadstdpaky lpvlaktdma gvtsthvayd akgdlknggi
      361 tmykvekgew kplksiggk
//
LOCUS       WP_006478689             638 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Burkholderia].
ACCESSION   WP_006478689
VERSION     WP_006478689.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 638)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 638)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 638)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 638)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..638
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=69014
     Region          10..638
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mndtthatda ahsphstqqh smralaiaai gvvfgdigts plyslkeafs pahgiplteg
       61 silgvisllf waillvvgvk yllfvmradn ngeggvlalm alslrpldsk trvagalmal
      121 gifgacmfyg davitpaisv msavegleia tphlshlvlp itivilialf wiqrhgtalv
      181 gklfgpimvl wfvviaalgv yhivrvpgii aainpyyaas fmadhllqay vvlgsvvlvl
      241 tgaealyadm ghfgakpiry aayglvmpsl vlnyfgqgal liqnpkaien pffllapewg
      301 llplvvlstv atviasqavi sgaysltsqa iqlgyvprmk vlhtselaig qiyvpvvnwl
      361 llavilcivv gfkssdnlaa aygiavtatm vittvlacvv mvkvwnwnrl lvgaiiavfl
      421 aidlgffgan llkvaqggwl plgigallff llmtwykgrh ivkertaadg iplepflqgl
      481 lahpphrvsg taiyltgndk lvpvsllhnl khnkvlhert ifltfvtrdi pyvrddkrqs
      541 ardaggglyi vkaeygfnet pdvkavleef grthdmtfel mdtsfflare tvvpthlpgm
      601 siwrervfaw mhqnaakptd ffaipanrvv elgtkiei
//
LOCUS       WP_006479118             143 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Burkholderia].
ACCESSION   WP_006479118
VERSION     WP_006479118.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..143
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15505
     Region          7..143
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mselltyggl favsmvaatl lplqseavla glllagrepv walvlvasvg nvagsainwa
       61 lgrgiehfre rrwfpvkpsa laraerwyar ygrwslllsw apvigdpltm iagvlreplp
      121 tflaivtiak vgrylavawl vmh
//
LOCUS       WP_006479456             233 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Burkholderia
            cenocepacia].
ACCESSION   WP_006479456
VERSION     WP_006479456.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..233
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=25557
     Region          1..>226
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mslvvdirkt casaerrftl dmsftattqr vvlfgpsgag ksmtlqaiag lltpdagtit
       61 lngeplfdaa rridvptrer rvaylfqdya lfphlnvrqn iafgltsglr npraktvppe
      121 vaywlrafdl eslagqypsq lsggqkqrva laralvaqpr illldepfaa ldgamrqrmr
      181 helaelqarl dipmvlishd pddvaafgdq vvqlsegrvq aspphaewpt rvt
//
LOCUS       WP_006480841             402 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Burkholderia cenocepacia].
ACCESSION   WP_006480841
VERSION     WP_006480841.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..402
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42540
     Region          5..390
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mrhpvlvlna gssslkfsvy dtredrslda glhgqvenlh dtphlfvtda hgatlvdsav
       61 arpghqgaie alhawfaahv greaafdgvg hrvvhggpyf tapvridahv ldaiaslapl
      121 aplhqphhvd airavaavap nlpqvacfdt afhatvpale refalpralt eqgivrygfh
      181 glsyeyiama laaldpswmq hrtvvahlgn gaslcalang rsvattmgft avdglpmgtr
      241 tgaldpgvil ylqrhsgrsl devehliyae sgllgvsgvs sdmrtllasd apsaahavel
      301 fayraarela alagvlggld tlvftagige haprvreric rraawlgivl ddaanaaglp
      361 vissdasrvt vrviptdenl miarhtrrvl ddaipstpyp tr
//
LOCUS       WP_006480723             285 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Burkholderia
            cepacia complex].
ACCESSION   WP_006480723
VERSION     WP_006480723.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 285)
  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 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   3  (residues 1 to 285)
  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   4  (residues 1 to 285)
  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 285)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..285
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31259
     Region          35..278
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <169..278
                     /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 mttdakavgt tdhwlvarrd aetgieslha hfnghaydah dhddmlvgft eqgvqrfqch
       61 rslhtsvpgr ailiepgamh dghapeaggf tygmlylpqa wveraarrld lpglgsveat
      121 fghtlvddrg lvdairnaff aihdnegrla rdqtldrllt rlgsqlggpl alesgvvppa
      181 iarvrdllhe hmdgnlglde lasvagidrf rltrmfqraf gtsphaylvr lrlraarkll
      241 aagrtpaqaa advgfadqsh lgrwfrrayr itpaayrqlc tnvpd
//
LOCUS       WP_006480844             403 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Burkholderia cepacia complex].
ACCESSION   WP_006480844
VERSION     WP_006480844.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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 403)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..403
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45964
     Region          1..402
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mltlspasar alhlaaqgll tpprrkatka dvldtirrma qlqidtihvv arspylvlfs
       61 rlgdfsphwl dehlaearlf eywsheacfl pieqfglmry kmldpsgmgw kyaaewheqn
      121 rpeierllar ireegpvrsa dfaredgvkg ngwwdrkpek rhlevlfttg dlmvserrnf
      181 qrvydvrerv lpdwddtrdl ppreavlpal ldytcralgv vradwvadyy rlprrsyrae
      241 lerladagdl ipvqiddwke payvhrslda llpaaaadtl rstvttllsp fdpvvwdrrr
      301 astlfgfdyt iecytpehkr rygyfclpvl hrgrlvgrvd akahralgtf elkavhvepg
      361 vrfgagiaad vakavkklaa whgtpevtva happalveaf trt
//
LOCUS       WP_006481059             280 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Burkholderia
            cenocepacia].
ACCESSION   WP_006481059
VERSION     WP_006481059.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..280
                     /product="formate/nitrite transporter family protein"
                     /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=29666
     Region          2..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mayltpnefv trmvdagesk lsmstrdtli raymagaila laaafavsit intgnalvgs
       61 llfpvgfcml yllgfdlltg vftlaplavi drrpgatwgg vfrnwtlvff gnfagaltva
      121 lfmaiiftfg fseapnaigq kiggigeart lgyaahgaag mltlfvrgvm cnwmvstgvv
      181 aammstsvpg kviamwmpil vffymgfehs vvnmflfpsg lmlgahftvv dyllwneipt
      241 vlgnlvgglv fvgaalysth yktapkrapa spvgvvarka
//
LOCUS       WP_006481705             373 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Burkholderia cenocepacia].
ACCESSION   WP_006481705
VERSION     WP_006481705.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 373)
  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 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   3  (residues 1 to 373)
  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   4  (residues 1 to 373)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 373)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 373)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..373
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38541
     Region          28..363
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(103..105,125..126,175,227,251)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mrhfltalsv avaagaltsa haqevvmigh sapltgpqaa ngkdnengar lavdelnkag
       61 ikvagkavtf klvseddqad pkagvqvaqn lvdkgvvavl gpynsgvaip asrvystagv
      121 pilpvasnpa ltkqgfknif rigasdeqlg gtmatfaakt lnaktaavid drtaygqgva
      181 eqfmnvakan gikivdqeyt nssatdflgi ltkikasnpd viflggyaaq gapmakqmkq
      241 rglrakllgg dgicsadmgk vageaasivy caqggvalek taagreflkk yhdtyhtdtq
      301 vygvnyydgm klladamvka gtttdkakls aqlaksnyag vagtysfdan gdlkgapttv
      361 yvirnglpep yak
//
LOCUS       WP_006483393             329 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_006483393
VERSION     WP_006483393.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 329)
  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 329)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 329)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 329)
  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   5  (residues 1 to 329)
  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   6  (residues 1 to 329)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..329
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36819
     Region          18..198
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          88..329
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mnrfaispgw qvvmvdlglr adellrhaql padlftrpen glttreyfrm wramedmanm
       61 pavalrildl lsveafdppl faalcspnle iairrisqfk pligpirlrv sheadaltla
      121 vdflerevpp pgmlvaaelg ffvklarlat rtelparavt lprdvrphpg yarffgvtpq
      181 ygdapsvsma lqdarrpfvt anhamwqife pdlrrrldal saeagiverv raallelipg
      241 glattdgvar tlaiskrtlq rrlgdeganf ktllaevrek lawhyldrsd lpysqiafll
      301 gyqdpnsffr afsewtgmtp eaarsrtar
//
LOCUS       WP_006483644             334 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_006483644
VERSION     WP_006483644.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 334)
  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   5  (residues 1 to 334)
  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   6  (residues 1 to 334)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..334
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36727
     Region          22..197
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          90..330
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mgpqmispdf vddalaclrr rglptvpvlr aaglpaavhe pvtpqqygrl wlaiagaldd
       61 effglaarpm rrgsftllch avlragtldk alrralkflr vvldephgel vvadgqaqiv
      121 laqsgapypa fayrtfwlil lgvacwligr riplqridfa cpsagqrsdy hqffgvpvhf
      181 drpdsrlafn aaylalptir seqalktflr gapgnllvry rhdtgwvakt rahlkarpaa
      241 ewpdfdtlav rldttpatlr rrlrsegqsf aaikdelrga laqsllrgha lsvaeiaael
      301 gftepsafhr afrkwtgtsp gafrrdvhaa qaes
//
LOCUS       WP_006484057             202 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Burkholderia cenocepacia].
ACCESSION   WP_006484057
VERSION     WP_006484057.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 202)
  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   2  (residues 1 to 202)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..202
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19357
     Region          24..76
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mlkkllmlfv alslslaagl aaavevntad qaalesvkgl gpvkskaiid ertkngpfkd
       61 addlanrvkg lgtksvghle engltiggas tppkgvklsk paattsatts tttsagtast
      121 sttatagttt aapaptasap eaaakpaktk raskkekaaa aaasadagas apaaasstka
      181 tkgskkkskk dkaasaaaas ga
//
LOCUS       WP_006484314             382 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Burkholderia].
ACCESSION   WP_006484314
VERSION     WP_006484314.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 382)
  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 382)
  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   3  (residues 1 to 382)
  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   4  (residues 1 to 382)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 382)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 382)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..382
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40123
     Region          33..369
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(109..111,132..133,182,234,258)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkfrhsllsv siasalalls qqaaraadat dvkvgfaapl tgvnagygkd lqngvqlald
       61 davaqkvqia gkparfnlvv qddqadprig vqaaqalvdq nvsvvvghfn sgttipasvv
      121 ydkagipvid paatnptlts rglanmfmvi atdgqnagna gkyavdvtka kriaiiddrt
      181 afgqgeadef ekavkaaggn ligreftsnq avdfraqits lkaknpdlif fggldslaan
      241 fikqmrqlgl naqfvggggv kdnefikiag paaegamawe ygrpldelpq gkdfearfkk
      301 rfgvdvlsya qfgydaawaa ikamqaagst dpkayrpalk kidfegvtgr isfandgslk
      361 sgmstlyqvk ngawktivtk gg
//
LOCUS       WP_006484341             360 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_006484341
VERSION     WP_006484341.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 360)
  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 360)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 360)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 360)
  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   5  (residues 1 to 360)
  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   6  (residues 1 to 360)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..360
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39854
     Region          42..225
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          122..355
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mlvisgqidm tspsrkdrlg lrrptipvay trlllqalaa rgvdlaavra gtglrdavla
       61 epdarvapsq wgrlvlnaie iggdpgigla lglllkptvh gflgyatlta rdirealsvt
      121 qryfrmrnrq yrltyaeder gatlelhgvq anpvlqhhvm fefvltglaq nisqwsgrvs
      181 ppirlqfawp epayfaryrd qlppvafgca analwiarda ldwplplade vahrqalvqv
      241 ereyaqvrqe egdlvervra elaraagdyp gpdtladall vstrtlrrrl eeagssyrql
      301 ldearfrdak qllaasdldl ktiaerlqft dpanftrafr rwagqtpsaf reaaagtara
//
LOCUS       WP_006486934             383 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Mesotoga].
ACCESSION   WP_006486934
VERSION     WP_006486934.1
KEYWORDS    RefSeq.
SOURCE      Mesotoga
  ORGANISM  Mesotoga
            Bacteria; Thermotogati; Thermotogota; Thermotogae; Kosmotogales;
            Kosmotogaceae.
REFERENCE   1  (residues 1 to 383)
  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 383)
  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
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 383)
  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   5  (residues 1 to 383)
  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   6  (residues 1 to 383)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 383)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 383)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Mesotoga"
                     /db_xref="taxon:1184396"
     Protein         1..383
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41271
     Region          <8..60
                     /region_name="COG3398"
                     /note="Predicted transcriptional regulator, contains two
                     HTH domains [Transcription]"
                     /db_xref="CDD:442625"
     Region          82..376
                     /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 mitkpgdlre knmgrviqll lanpdisrve iarkteltkt tisaiiaall dlniveetpg
       61 lktglvgktp ipmrvrgdaa vaigvnlarg stsgvvmtac gkllesvske vsnltradat
      121 ahlfevvqrl lnkcfrngid vdaigigaps pldkekgviy apyglsdwkd fpvgeitrek
      181 fglpvflvnd adgaafgmkc fgkcrdirsf ismyfdegvg agiilndeiy sgssgysgqi
      241 syaliksfcn gqvensrfsl dtvvsdlnke igvncrkidd fldrrfnggq kmnsvlsrvg
      301 delgriaalv snivgpeavv vngrlldfgk vffaalkdsf esnlfsrgsv qlikgftnqf
      361 rafstgaasy aifsylmdkv lsn
//
LOCUS       WP_006490067             789 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Mesotoga prima].
ACCESSION   WP_006490067
VERSION     WP_006490067.1
KEYWORDS    RefSeq.
SOURCE      Mesotoga prima
  ORGANISM  Mesotoga prima
            Bacteria; Thermotogati; Thermotogota; Thermotogae; Kosmotogales;
            Kosmotogaceae; Mesotoga.
REFERENCE   1  (residues 1 to 789)
  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 789)
  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 789)
  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   4  (residues 1 to 789)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..789
                     /organism="Mesotoga prima"
                     /db_xref="taxon:1184387"
     Protein         1..789
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88075
     Region          45..787
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mrkvawkdid lkivlpedvk stecvgelee figqeraira letglhidak gynvfvsgtt
       61 ntgrrtfvsr ylkkkvegtk tpgdwiyvyn fddprspnsi sleagtgkif qkemndfvei
      121 ainsigesfq sedyqqkvts lqneqsekrs nmlkelieka kekdytvqin qtgvatipiw
      181 ngkpltqevy ealpedyqkq itkkgeevre lvnsyllkls kmekdfgeky kelnrkvasf
      241 aveghiremk drfseskevv dfiesmkkdl ldnlgvffsq eidskaffgk ryavnlfvdn
      301 sgiegkpvve vtnanysslf grieyvakmg mldtdhtmir pgaihssngg ylvldaknvl
      361 sepyvwqtlk qvlfsglegi enlehkigll stvslkpepi pldikivmig epwiysmlst
      421 ldtdfkklfk vkaefdwemt iqndtvdklc glmcnivkan slrpleregi ievikraifl
      481 sgsrkkvstq fgaleqille ssavaevsgh emiqaddvst aweemhkrvs lyqdkikemf
      541 qnstlmvqte gelvgeingl tviqtedlsf gipvkitakv gpgnsgivdi qkeselsghi
      601 hnkasltiqg ymsskyaqqf plslngsisf eqvysavegd sasvaetiaf lsaiaevpik
      661 qsiavtgsin qsgrvqpvgg vqykiqgfyd lckikgfngq qgvivpeans dnvilndeii
      721 gaikegrfnv wtietvdeai eiltgmkpgk igkngqyssg sfnrlvvdrl kkfyeiasrt
      781 hdrsgkdad
//
LOCUS       WP_006491727             280 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Mesotoga prima].
ACCESSION   WP_006491727
VERSION     WP_006491727.1
KEYWORDS    RefSeq.
SOURCE      Mesotoga prima
  ORGANISM  Mesotoga prima
            Bacteria; Thermotogati; Thermotogota; Thermotogae; Kosmotogales;
            Kosmotogaceae; Mesotoga.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Mesotoga prima"
                     /db_xref="taxon:1184387"
     Protein         1..280
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31127
     Region          1..252
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mfvdfhchsd hsdgtdsvaa ivqkaadkgi silsvtdhdt lagqnearel clragikyir
       61 gveiscdfhe tldvlgygmv feassmeeel rqlrlkrdlr ntrilsrlrs lgvqitdeel
      121 essfpgeslg rphianlivr kgysdstena fkeflgkdgk ayvekeklsi ksaielilsa
      181 ggvpvlahpl smmldrketi eiiramiryg lkgmevfykt yeettreelf eisrnlglia
      241 tggsdyhgkh kkdlelgidi pdsavsrfle slpadnglny
//
LOCUS       WP_006494491             380 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Burkholderia cenocepacia].
ACCESSION   WP_006494491
VERSION     WP_006494491.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 380)
  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 380)
  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   3  (residues 1 to 380)
  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   4  (residues 1 to 380)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 380)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 380)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..380
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39744
     Region          31..367
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(107..109,130..131,180,232,256)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mnrhhktvfa tavaltcalp agaaqaddvv righvapltg aiahlgkdse ngarlaveei
       61 nakglviggr kvtlqldaqd dagdprtatq vaqrlvddkv vgvvghhnsg tsipasrvyr
      121 dggvvqisqa atnptytqqg fkttyrvvat daqqgpalam yaaknmgirt vavvddstay
      181 gqglatefek aakaagmkvv srdatndkai dfrailtkik ganpdaimyg gmdatggpla
      241 kqarqlgmra qilagdgvcs tdlpklagpa senvvcseag ialekmpgga afakryeary
      301 hqpmqvyapf sydavyiivd amkranstdp akvlaampat dyrgvigets ftpqgdlkhg
      361 aisvftyksg rkalldivrm
//
LOCUS       WP_006496027             360 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_006496027
VERSION     WP_006496027.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 360)
  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 360)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 360)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 360)
  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   5  (residues 1 to 360)
  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   6  (residues 1 to 360)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..360
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39803
     Region          42..225
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          122..348
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mlvisgqidm tspsrkdrlg lrrptipvay trlllqalaa rgvdlaavra gtglrdavla
       61 epdarvapsq wgrlvlnaie iggdpgigla fglllkptvh gflgyatlta rdirealsvt
      121 qryfrmrnrq yrltyaeder gatlelhgvq anpvlqhhvm fefvltglaq nisqwsgrvs
      181 ppitlqfawp epayfaryrd qlppvafgca analwiarda ldwplplade vahrqalvqv
      241 ereyaqvrqe egdlvervra elaraagdyp gpdtladall vstrtlrrrl eeagssyrql
      301 ldearfrdak qllaasdldl ktiaerlqft dpanftrafr rwagqtpsaf reaaagaara
//
LOCUS       WP_006496393             203 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Burkholderia].
ACCESSION   WP_006496393
VERSION     WP_006496393.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 203)
  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   2  (residues 1 to 203)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..203
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19428
     Region          24..76
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mlkkllmlfv alslslaagl aaavevntad qaalesvkgl gpvkskaiid ertkngpfkd
       61 addlanrvkg lgtksvghle engltiggas tppkgvklsk paattsatts tttsagtast
      121 sttatagttt aapaptasap eaaakpaktk raskkekaaa aaaasadaga sapaaasstk
      181 atkgskkksk kdkaasaaaa sga
//
LOCUS       WP_006497594             280 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Burkholderia].
ACCESSION   WP_006497594
VERSION     WP_006497594.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..280
                     /product="formate/nitrite transporter family protein"
                     /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=29636
     Region          2..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mayltpnefv trmvdagesk lsmstrdtli raymagaila laaafavsit intgnalags
       61 llfpvgfcml yllgfdlltg vftlaplavi drrpgatwgg vfrnwtlvff gnfagaltva
      121 lfmaiiftfg fseapnaigq kiggigeart lgyaahgaag mltlfvrgvm cnwmvstgvv
      181 aammstsvpg kviamwmpil vffymgfehs vvnmflfpsg lmlgahftiv dyllwneipt
      241 vlgnlvgglv fvgaalysth yktapkrapa apvgvvarka
//
LOCUS       WP_006497989             329 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_006497989
VERSION     WP_006497989.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 329)
  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 329)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 329)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 329)
  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   5  (residues 1 to 329)
  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   6  (residues 1 to 329)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..329
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36815
     Region          18..198
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <148..329
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mnrfaispgw qvvmvdlglr adellrhaql padlftrpen glttreyfrm wramedmanm
       61 pavalrildl lsveafdppl faalcspnle iairrigqfk pligpirlrv sheadaltla
      121 vdflerevpp pgmlvaaelg ffvklarlat rtelparavt lprdvrphpg yarffgvtpq
      181 ygdepsvsva lqdarrpfvt anhamwqife pdlrrrldal saeagiverv raallelipg
      241 glattdgvar tlaiskrtlq rrlgdeganf ktllaevrek lawhyldrsd lpysqiafll
      301 gyqdpnsffr afsewtgmtp eaarsrtar
//
LOCUS       WP_006498196             565 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: M4 family metallopeptidase [Burkholderia].
ACCESSION   WP_006498196
VERSION     WP_006498196.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 565)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 565)
  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 565)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..565
                     /product="M4 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=59804
     Region          1..565
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mkklsrllpi taitlaslsa faqagdqpaa vdkalqliqq npsafslaag gtartlkfag
       61 pqagaptdgd qfqvrdvivd pdgtehvrfd rfhaglpvig gdvvvhsskg qlkqasvtql
      121 apinlagsig kvgnravirn apdvgatrar hiaaarfnsd vrrvddaelv vfardvtptl
      181 ayavrvygka tethgdavly yvdartgtll daqdliktaa atgtgrslyy gnltlttdqt
      241 gtnayrmldp srgggsvydg rglssdeveq atdlpiftss tnvwgnnttt drqtvaadid
      301 yglaltwdyy ktthnrngif ndgrgvksya hvvfntgsgt tganaawlss rvmaygdgep
      361 gtrlpkpvvs vdvaghemsh gvteatanln ysgdagglne stsdifgtlv kfyannpndp
      421 gnyvigarvv sgglrkmykq dldgrsfscy psggfswsnp rhdphftsgv gnrffyllse
      481 gpsvpptdtg lsrtqlvcng dttfsglgrd kagkiwyrtl tvylnanssy pnarrasiqa
      541 andlygansa esatvaraws avgvn
//
LOCUS       WP_006498836             344 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Burkholderia].
ACCESSION   WP_006498836
VERSION     WP_006498836.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 344)
  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 344)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 344)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 344)
  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   5  (residues 1 to 344)
  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   6  (residues 1 to 344)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..344
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37757
     Region          25..207
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          85..340
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkqedkgtva islvaysval atrrgvaaep llaqagiapa llgqprarvs aqqygalwna
       61 iartlddeff gqdrhpmrsg sfiamsqaal sardglhama ravnfmhcvl ddlhaeldan
      121 pqrvrlrfvh rnngatpamf tyatyfiivy gltcwligrr ipllhasfrc dtppadheyp
      181 smfcddmrfn epesyvdfdp efatlpvvqn aktlktflrn apasfivkyr npnalaqrvr
      241 avlrgmppaa wpgaggmaar lhvaeatlrr klhqeghayq sikdtlrrdl afealadpar
      301 tiadvaaatg faepsafyra frkwsgrspa efreealarg ggag
//
LOCUS       WP_006498979             403 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Burkholderia].
ACCESSION   WP_006498979
VERSION     WP_006498979.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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 403)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..403
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45995
     Region          17..401
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mltlspaaar alhlaaqgll tpprrkatks dvldtirrma qlqidtihvv arspylvlfs
       61 rlgdfspqwl dehlaearlf eywsheacfl pieqfglmry kmldpsgmgw kyaaewhaqn
      121 rpeierllar iraegpvrsa dfaredgvkg ngwwdrkpek rhlevlfttg dlmvserrnf
      181 qrvydvrerv lpgwddtrdl ppreavlptl ldytcralgv vradwvadyy rlprrsyrae
      241 lerlaeagdl ipvqiddwke payvhrslda wlpaaaadtl rstvttllsp fdpvvwdrrr
      301 astlfgfdyt iecytpehkr rygyfclpvl hrgrlvgrvd akahrtlgtf elkavhvepg
      361 vrfgtglaad vakavkklaa whgtpevtvr happelvkal adt
//
LOCUS       WP_006501327             407 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Austwickia chelonae].
ACCESSION   WP_006501327
VERSION     WP_006501327.1
KEYWORDS    RefSeq.
SOURCE      Austwickia chelonae
  ORGANISM  Austwickia chelonae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermatophilaceae; Austwickia.
REFERENCE   1  (residues 1 to 407)
  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 407)
  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
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 407)
  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   5  (residues 1 to 407)
  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   6  (residues 1 to 407)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 407)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Austwickia chelonae"
                     /db_xref="taxon:100225"
     Protein         1..407
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41846
     Region          28..>85
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          88..394
                     /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 madsllgsad stpgagsqsa lrsantrrvl acltesgpmt qvalskstgl spatisnlva
       61 klrsegvvat spttssgrra vlvelggvpq ckvavgidmg rrhlrialct lnrevvaeka
      121 vglpadhhae dsigladrvl tilleragle rsqvvgcgvg ipgpidagsg kiahgvilpa
      181 wvdfrpidrl revlrrpvyl dndanlggla eitwgpyaea ghllyvkvgt gigaglvlsg
      241 qvyrgamgit geighipvae hglvcrcgnr gcletvasts vmvealvkag vlehdagiar
      301 lvetvragdp aagrvaedag malgqvlgmm vnvlnpavvv iggslvglgg dllgpvrrgi
      361 rrfasptvsa rtevvlsslg eraevlgacs lvfqqesent wllpsrc
//
LOCUS       WP_006501688             427 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Austwickia chelonae].
ACCESSION   WP_006501688
VERSION     WP_006501688.1
KEYWORDS    RefSeq.
SOURCE      Austwickia chelonae
  ORGANISM  Austwickia chelonae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermatophilaceae; Austwickia.
REFERENCE   1  (residues 1 to 427)
  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 427)
  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
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 427)
  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   5  (residues 1 to 427)
  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   6  (residues 1 to 427)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 427)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 427)
  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 11973053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Austwickia chelonae"
                     /db_xref="taxon:100225"
     Protein         1..427
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44047
     Region          <25..82
                     /region_name="COG3398"
                     /note="Predicted transcriptional regulator, contains two
                     HTH domains [Transcription]"
                     /db_xref="CDD:442625"
     Region          93..401
                     /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 meetgrpmga rsirragair prtglrsevg pgallavire sggltrrdli dmtgfaratv
       61 esrldallgs gliverarqg gsggrppkvf sfneqagyll svvlgsshtr igvsdlgcrt
      121 valedldvdm sagpgvvlga vgtrlrrmle qrgieprtvl gvgvgvpspv elggrmarpp
      181 ergglsdlgg qwadvviare imaflpglgv eavpvvvdkd animalgewr ttwpdvrdli
      241 vfkvgitlac givanacvvr gvggiagdlg hvpdpasdvr crcgqsgcae avasgeairr
      301 algergrglk rgrdivellh agdpevaehv vragrhigrv igdaistlnp elvvvggtla
      361 ednpllidsi rsvaasrvhp laaastqiva stikedtgvi gaallaleea ldpvvvdamv
      421 gagrsag
//
LOCUS       WP_006507572             178 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein, partial [Xenococcus sp. PCC 7305].
ACCESSION   WP_006507572
VERSION     WP_006507572.1
KEYWORDS    RefSeq.
SOURCE      Xenococcus sp. PCC 7305
  ORGANISM  Xenococcus sp. PCC 7305
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Pleurocapsales;
            Xenococcaceae; Xenococcus.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Xenococcus sp. PCC 7305"
                     /db_xref="taxon:102125"
     Protein         1..>178
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
     Region          <1..178
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 maniigtsgd dflngtfedd iirtglgvdt vdggagidll eidyslsanr isyssnsvpa
       61 lgsgrlsggg nivefsnvei ynitgsqfnd elfggdfsdt lsggngrdti dggqgadvld
      121 ggegsdtlsr nlsifnqgsv vdntlstmtl idgttasnfe nlditlgsgd dtirtglg
//
LOCUS       WP_006507639             173 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Xenococcus sp. PCC 7305].
ACCESSION   WP_006507639
VERSION     WP_006507639.1
KEYWORDS    RefSeq.
SOURCE      Xenococcus sp. PCC 7305
  ORGANISM  Xenococcus sp. PCC 7305
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Pleurocapsales;
            Xenococcaceae; Xenococcus.
REFERENCE   1  (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   2  (residues 1 to 173)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Xenococcus sp. PCC 7305"
                     /db_xref="taxon:102125"
     Protein         1..173
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19441
     Region          38..>65
                     /region_name="HHH_3"
                     /note="Helix-hairpin-helix motif; pfam12836"
                     /db_xref="CDD:463723"
     Region          106..172
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mvlsslrkka isykilndpy yrfqsleeit iagelgikin vnqasvddwl rlpgisihqg
       61 rslvelvgmg vqllciedva aalsfpvtrl lplepilhfe yydrlsvlsp qkvnpnrasv
      121 aeigqipile idlasliike renngsyrnl adlqrrlkld sqlianlmhy itf
//
LOCUS       WP_006507765             116 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Xenococcus sp. PCC 7305].
ACCESSION   WP_006507765
VERSION     WP_006507765.1
KEYWORDS    RefSeq.
SOURCE      Xenococcus sp. PCC 7305
  ORGANISM  Xenococcus sp. PCC 7305
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Pleurocapsales;
            Xenococcaceae; Xenococcus.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Xenococcus sp. PCC 7305"
                     /db_xref="taxon:102125"
     Protein         1..116
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13351
     Region          24..112
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 msslkpvinq nqieqrlgvs lltvtqfcqr wqitelalfg svlrddfnpn sdldflvtfs
       61 pdakiglaev nemeqelknm vkrkidliwk ksieasqnwi rrqniletak viyger
//
LOCUS       WP_006508677             101 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Xenococcus sp. PCC 7305].
ACCESSION   WP_006508677
VERSION     WP_006508677.1
KEYWORDS    RefSeq.
SOURCE      Xenococcus sp. PCC 7305
  ORGANISM  Xenococcus sp. PCC 7305
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Pleurocapsales;
            Xenococcaceae; Xenococcus.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Xenococcus sp. PCC 7305"
                     /db_xref="taxon:102125"
     Protein         1..101
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11164
     Region          6..101
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mnnsdkladl lqdkrdeiia iaakhgafnv rifgsvarne adqdsdidfl vdyslddisp
       61 wfpaglkldl ekllnhkvdl ategalkeri rekilseavs l
//
LOCUS       WP_006509347              90 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Xenococcus sp. PCC 7305].
ACCESSION   WP_006509347
VERSION     WP_006509347.1
KEYWORDS    RefSeq.
SOURCE      Xenococcus sp. PCC 7305
  ORGANISM  Xenococcus sp. PCC 7305
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Pleurocapsales;
            Xenococcaceae; Xenococcus.
REFERENCE   1  (residues 1 to 90)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 90)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 90)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 90)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Xenococcus sp. PCC 7305"
                     /db_xref="taxon:102125"
     Protein         1..90
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=9943
     Region          11..90
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 meltgnwsmv nvkvklfaay qevcgkselt lsfpeattvg dvlnyliqer pelekwrevt
       61 rfginlqfvs aetvirdgde ivlippvsgg
//
LOCUS       WP_006509408             103 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Xenococcus sp. PCC 7305].
ACCESSION   WP_006509408
VERSION     WP_006509408.1
KEYWORDS    RefSeq.
SOURCE      Xenococcus sp. PCC 7305
  ORGANISM  Xenococcus sp. PCC 7305
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Pleurocapsales;
            Xenococcaceae; Xenococcus.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Xenococcus sp. PCC 7305"
                     /db_xref="taxon:102125"
     Protein         1..103
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11270
     Region          8..103
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 msnstqntia nllkakreei iaiaakhgaf nvrvfgsvar neasnesdid flvdysveei
       61 spwfpaglml dleallgrkv dvateaalke rirerilqea isi
//
LOCUS       WP_006509369             282 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Xenococcus sp. PCC 7305].
ACCESSION   WP_006509369
VERSION     WP_006509369.1
KEYWORDS    RefSeq.
SOURCE      Xenococcus sp. PCC 7305
  ORGANISM  Xenococcus sp. PCC 7305
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Pleurocapsales;
            Xenococcaceae; Xenococcus.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Xenococcus sp. PCC 7305"
                     /db_xref="taxon:102125"
     Protein         1..282
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31427
     Region          2..280
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mklllidgds lahrcyysnv nkekiltnsd gcpiaicsgf lislrslltr lnpshlaiaf
       61 nspvhsfryq vcpeykqnrd htkpedflid lrnlrcllge mnicnlnisg fevgdllati
      121 tertscpivi hsndkkilql vsdrvsvhyt hgkthqiytp dlvvqefgfs peliplfkai
      181 agnssdnikg vagigkitaa qmiqkygdla nifanlaelk prmqkkmqdn qllitqllki
      241 tnlatnvpls fsvdncqitq iktnvdiaqe leiqhlvdkl pd
//
LOCUS       WP_006509727             378 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Xenococcus sp. PCC
            7305].
ACCESSION   WP_006509727
VERSION     WP_006509727.1
KEYWORDS    RefSeq.
SOURCE      Xenococcus sp. PCC 7305
  ORGANISM  Xenococcus sp. PCC 7305
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Pleurocapsales;
            Xenococcaceae; Xenococcus.
REFERENCE   1  (residues 1 to 378)
  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 378)
  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 378)
  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 378)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Xenococcus sp. PCC 7305"
                     /db_xref="taxon:102125"
     Protein         1..378
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=42513
     Region          1..370
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkrrkfltkt glgaigatal gacnsqsekp titrantpkt dtrqpsfrwr matswpkslq
       61 ilfeaadllc qkvnnmtngr fvitpyaage ltdglkvlqa vqdnmvecgh tasyyyldyg
      121 salafgttlp fgltasqqna wlyyggglea mrrlyqnlgi infpggntgt qmggwfkqev
      181 ntiedfrglr mrvpglggki lqrlgveiks lpgnriftal eqntidaaew knphadqtlg
      241 lnkvapfyyy pgwwepgtsy efqvnleqwn klpveyqeif qaaatdintk mlaqfnavng
      301 evleglvlsg tkllpfssei lqasykeafi myeemaskdq dfrniyrqwq efrnqiyawn
      361 nmnelgfanf alkhpnla
//
LOCUS       WP_006509728             375 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Xenococcus sp. PCC
            7305].
ACCESSION   WP_006509728
VERSION     WP_006509728.1
KEYWORDS    RefSeq.
SOURCE      Xenococcus sp. PCC 7305
  ORGANISM  Xenococcus sp. PCC 7305
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Pleurocapsales;
            Xenococcaceae; Xenococcus.
REFERENCE   1  (residues 1 to 375)
  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 375)
  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 375)
  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 375)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Xenococcus sp. PCC 7305"
                     /db_xref="taxon:102125"
     Protein         1..375
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=42030
     Region          1..367
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkrrhllgat ssigamgafa lysprtqaqs ptstlsnlns lpsirwrmat swpksldilf
       61 ggaericsqv tamtngkfsi tpyasgeive gfgvldavae gevecghsas yyyfhknpal
      121 afgtnipfgl taeqqnswly ygggqelinr iyadlgiisf pagntgvqmg gwfrrkinqv
      181 tdlqglkmri pglgsevmsr lgvevqilpi dqiasalikg kidavewnnp yddeiiglhd
      241 sapyyyypgw wepgatyele vnlaewkklp keyqevlqva atnanitmla eynakngkvl
      301 qrlnqrgtnf lpfsdeilea ayqqtltile eyssqdktfr eiyrqwqkfr sqvyhwnqin
      361 elsftnftfq aanlt
//
LOCUS       WP_006510302             217 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Xenococcus sp. PCC 7305].
ACCESSION   WP_006510302
VERSION     WP_006510302.1
KEYWORDS    RefSeq.
SOURCE      Xenococcus sp. PCC 7305
  ORGANISM  Xenococcus sp. PCC 7305
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Pleurocapsales;
            Xenococcaceae; Xenococcus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Xenococcus sp. PCC 7305"
                     /db_xref="taxon:102125"
     Protein         1..217
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22514
     Region          <29..137
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mdtffdssds lsllssgdls estpseesna lfgqegddnf nggegndtlf ggggrdslfg
       61 grgrdsldgg qdhdflvgga hddtlvggag hdtmlgqsnm dylyggaghd qlkggdgndt
      121 lsgadgldsl yggagfdqfe vwrsgwdnqn iiadyedgqd kiaihdgqis gfenlsitqt
      181 gssvtiqdan dsniyyatvn dilasdltas dflfaas
//
LOCUS       WP_006511749             235 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Xenococcus sp. PCC 7305].
ACCESSION   WP_006511749
VERSION     WP_006511749.1
KEYWORDS    RefSeq.
SOURCE      Xenococcus sp. PCC 7305
  ORGANISM  Xenococcus sp. PCC 7305
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Pleurocapsales;
            Xenococcaceae; Xenococcus.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Xenococcus sp. PCC 7305"
                     /db_xref="taxon:102125"
     Protein         1..235
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22620
     Region          <4..194
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 maqifgtaia dslpgtledd iiigdgegdf iggdegddli lggdgedaiy gnlgddillg
       61 gshadllvgn egadtidggs gadlifgnqg sdflsggada dvisggagad lilgdegddi
      121 lagdggndhl iggadhdmlw geggddtlng gagsdnlfgg agadtfvlea gngedaiagy
      181 fdgtdifslg ggltyeelai gggpaaatis vaatgevlvs vlgvdssfig aedfa
//
LOCUS       WP_006512327             301 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Xenococcus sp. PCC 7305].
ACCESSION   WP_006512327
VERSION     WP_006512327.1
KEYWORDS    RefSeq.
SOURCE      Xenococcus sp. PCC 7305
  ORGANISM  Xenococcus sp. PCC 7305
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Pleurocapsales;
            Xenococcaceae; Xenococcus.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Xenococcus sp. PCC 7305"
                     /db_xref="taxon:102125"
     Protein         1..301
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31547
     Region          3..223
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mkivgtlnad llqgnsednl leglqgndti fggsgndtil gqkgddllvg esgfdviqgg
       61 ngndtiyvkt tevklfatat sesnlaygnq gddrifgseg ndtiygnqgq dvivgmagdd
      121 slygglgddt isgingrnri fggegndslv ggngkdimag ghdddtirgg rqndtllggn
      181 gndtldgegn ddvlvgnndl iepssnnqdv wtggagkdsf qlgnedtvfy qqnaesdlai
      241 ikdftsedki ilhgspsdyl iaingsdsei ysgsteklel iakvenntnl dlneayfdfk
      301 e
//
LOCUS       WP_006520530             193 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Desulfoscipio gibsoniae].
ACCESSION   WP_006520530
VERSION     WP_006520530.1
KEYWORDS    RefSeq.
SOURCE      Desulfoscipio gibsoniae
  ORGANISM  Desulfoscipio gibsoniae
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfallaceae; Desulfoscipio.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Desulfoscipio gibsoniae"
                     /db_xref="taxon:102134"
     Protein         1..193
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21184
     Region          4..188
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mnniienilt rrsirafked qipeedlnti lmagsyapng mgmqnwkfta iqnaaaikkv
       61 nkairqtlls ipvvpethpy vvsliekakd enadflyhap tfiivsnlkd dgnsmpdsal
      121 aignmmlaah slgigscwln qlpglthmpl irelltdldi senhivygsv vigyaaeesk
      181 paaprknvih iir
//
LOCUS       WP_006520896             352 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Desulfoscipio
            gibsoniae].
ACCESSION   WP_006520896
VERSION     WP_006520896.1
KEYWORDS    RefSeq.
SOURCE      Desulfoscipio gibsoniae
  ORGANISM  Desulfoscipio gibsoniae
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfallaceae; Desulfoscipio.
REFERENCE   1  (residues 1 to 352)
  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 352)
  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 352)
  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 352)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Desulfoscipio gibsoniae"
                     /db_xref="taxon:102134"
     Protein         1..352
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40249
     Region          1..340
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mnsrkftila tltlflislt flygcggqdn ksgtqvnsnq qqaeeqykir lnhglpqehf
       61 maleiqewad lveqksdgrl kiemypsaql ykdpdliqav rsgvieagat ynflfenlip
      121 efeplvfpri mtstrhmhnv ingdvgnilm srveendmkv lswlywpvet tgtisnkpih
      181 vpsdmkgmkf rttggiqavl lkkvgasssy isgaemymal qrrtidgglq nnfahvldrk
      241 fyevspyyti tkmgqtvdli iinkkfydsl pvdlqqilvd sgremqeksv tiaedryekl
      301 lpemksvmke villtkeeee swdklsqevw qetldkadpe trkiadeiik mr
//
LOCUS       WP_006521974             716 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Desulfoscipio gibsoniae].
ACCESSION   WP_006521974
VERSION     WP_006521974.1
KEYWORDS    RefSeq.
SOURCE      Desulfoscipio gibsoniae
  ORGANISM  Desulfoscipio gibsoniae
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfallaceae; Desulfoscipio.
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 716)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Desulfoscipio gibsoniae"
                     /db_xref="taxon:102134"
     Protein         1..716
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76521
     Region          11..716
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mitadlknel nsltplfqpn siaiigasqn pakpsgqplv sltrygfkgr vypvnpnydt
       61 lhglpcyptl qdipdqvdlc iiavpahmtm galkecadkg vrgviiftsg faevsadgaa
      121 iqqqitalar stgmrvcgpn cmgifsarna lmanffitel ptkvlvpdyl gfisqsggfg
      181 vaifqivkek gygfshfvgt gneadlefsh ylgymaadah trviggyleg vkdgpkflna
      241 ldmalanekp vllmkagsyp asaraaasht gamvgsekvy savfkqkgvv rvesleefqn
      301 mlsllhngki prgkrvaiia ssggigvmla dkcahyglev vtlqdktrsa laallpdfas
      361 tanpvditsa imtqpglleq caqivindpq vdmmivaywt elgdkgnldq mirvaqqtnk
      421 pvfnltwgpd kavfealqym nsqlapaare ldsivkglaa ladyhnfvrs rrksklvape
      481 vpsdarekva allgnlprga klsehsakql lqaygipttr eqlattgeea adaaeaigyp
      541 vvmkiespdi lhktdaggvl lnantpdevr sgfnrlldna raykadadik gvlvqqmlpa
      601 giemivgiar dsvfgstvlv gmggifveal kdaalrvvpv apldamemle elkgrrvldg
      661 lrgmppsdki amveviqrvs rlaqdfpqia eldinplivf segrgacaad aiivle
//
LOCUS       WP_006522232             100 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Desulfoscipio gibsoniae].
ACCESSION   WP_006522232
VERSION     WP_006522232.1
KEYWORDS    RefSeq.
SOURCE      Desulfoscipio gibsoniae
  ORGANISM  Desulfoscipio gibsoniae
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfallaceae; Desulfoscipio.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Desulfoscipio gibsoniae"
                     /db_xref="taxon:102134"
     Protein         1..100
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11183
     Region          3..90
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mnngnailak ietnmikikg fgvkkiglfg sfargeqndt sdidilvefy qnhktfdnym
       61 dlkfyledll nrkvdlviae aikpdlkpni tgsvryaqgi
//
LOCUS       WP_006523058             185 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Desulfoscipio gibsoniae].
ACCESSION   WP_006523058
VERSION     WP_006523058.1
KEYWORDS    RefSeq.
SOURCE      Desulfoscipio gibsoniae
  ORGANISM  Desulfoscipio gibsoniae
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfallaceae; Desulfoscipio.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Desulfoscipio gibsoniae"
                     /db_xref="taxon:102134"
     Protein         1..185
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20018
     Region          1..185
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mkivvgisga sgaiygiral ealrqcgvet hlvisksaki tismetnyri ndvealadyv
       61 yenenigaai asgsfkhdgm ivapcsiksl saiansyndn llvraadval kekrkllviv
      121 retplhighl rllvtlaelg gtilppvpaf yhqpktiddi vnqtvgkald qfgiehqlfr
      181 rwegs
//
LOCUS       WP_006523144             388 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Desulfoscipio gibsoniae].
ACCESSION   WP_006523144
VERSION     WP_006523144.1
KEYWORDS    RefSeq.
SOURCE      Desulfoscipio gibsoniae
  ORGANISM  Desulfoscipio gibsoniae
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfallaceae; Desulfoscipio.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Desulfoscipio gibsoniae"
                     /db_xref="taxon:102134"
     Protein         1..388
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=41772
     Region          <7..388
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mssykfpkff gyrrengrvg irnyvailsl ddlsnaacea vsnnikgtla lphaygrlqf
       61 gedldltfrt ligfgsnpnv aavvvigiep ewtkvivdgi aktgkpvtgf aierngqhkt
      121 ieraswkaqe yvqwaseiqr vecsvdelyv sikcgesdtt sglasnptvg rsverlleag
      181 atvsfgetse itgaedicka haatpevgda yykmwkeynd fivsqgvdlv gsqptkgnia
      241 gglttieeka lgnlqkigna kyvgvlgpae apnskglwym dtssaaaeav tlwaasgavv
      301 hlfptgqgni ignpiepvik lsanpltvvd mkehvdvdvs gilrremdld qasdalldmm
      361 irvcngrftc aealghrefi itklyrsa
//
LOCUS       WP_006523733             108 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Desulfoscipio gibsoniae].
ACCESSION   WP_006523733
VERSION     WP_006523733.1
KEYWORDS    RefSeq.
SOURCE      Desulfoscipio gibsoniae
  ORGANISM  Desulfoscipio gibsoniae
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfallaceae; Desulfoscipio.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Desulfoscipio gibsoniae"
                     /db_xref="taxon:102134"
     Protein         1..108
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=11767
     Region          6..83
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mvhndmvevr gfsflkeifd qrgwpfpvqv pldgectaee larrmdlpre kiegvfingl
       61 agpldrtvhp gdrvafvppg tpgpyrvilg lvktskeqnn svpgdagn
//
LOCUS       WP_006524120             180 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Desulfoscipio gibsoniae].
ACCESSION   WP_006524120
VERSION     WP_006524120.1
KEYWORDS    RefSeq.
SOURCE      Desulfoscipio gibsoniae
  ORGANISM  Desulfoscipio gibsoniae
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfallaceae; Desulfoscipio.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Desulfoscipio gibsoniae"
                     /db_xref="taxon:102134"
     Protein         1..180
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18881
     Region          3..176
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mntldaiakr ksirkykaeq ikdsaleeii kagktapnag pfqitviqna kllakiteia
       61 laamknsgnd flmsraalpg ytplygaptl lvlsapqanp ysmantsnaa tnmtiaatdl
      121 glgscymitp qlaftadpsl akeanipegf svicavavgy sdgnafster sdvdnvnyvk
//
LOCUS       WP_006524268             197 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Desulfoscipio gibsoniae].
ACCESSION   WP_006524268
VERSION     WP_006524268.1
KEYWORDS    RefSeq.
SOURCE      Desulfoscipio gibsoniae
  ORGANISM  Desulfoscipio gibsoniae
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfallaceae; Desulfoscipio.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Desulfoscipio gibsoniae"
                     /db_xref="taxon:102134"
     Protein         1..197
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=22733
     Region          13..197
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mkhidkiqev leqnngvita sqvtaanipr hylkkmmdmk llvkldrgiy skpeiwedem
       61 yilqykysrg ifshetalyi hgltdrtplk yvmtfpygyh vkslkqenvi irksvqdlye
      121 lglttgispc gnpirlydve rtlcdivkgn ntcdiqivnq amkqyakmpg knipklfdya
      181 gkirvkpkil nymevll
//
LOCUS       WP_006525905             151 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Solobacterium moorei].
ACCESSION   WP_006525905
VERSION     WP_006525905.1
KEYWORDS    RefSeq.
SOURCE      Solobacterium moorei
  ORGANISM  Solobacterium moorei
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Erysipelotrichaceae; Solobacterium.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 151)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Solobacterium moorei"
                     /db_xref="taxon:102148"
     Protein         1..151
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16828
     Region          5..131
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mktilnkqic afleesdkia alsnvsaciq msykninwvg fyfvkddqli lgpfqgkpac
       61 tripfdkgvc gkcyrdksvq ridnvlafsg hiacdcdsrs elcvpiivng kcvgeidids
      121 pitsrfgqee enemlqaayd iaqaylqhhw i
//
LOCUS       WP_006525977             710 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Solobacterium moorei].
ACCESSION   WP_006525977
VERSION     WP_006525977.1
KEYWORDS    RefSeq.
SOURCE      Solobacterium moorei
  ORGANISM  Solobacterium moorei
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Erysipelotrichaceae; Solobacterium.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Solobacterium moorei"
                     /db_xref="taxon:102148"
     Protein         1..710
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=80710
     Region          604..676
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 mgkklkkdfk erhkaslere mfnsktdtip eesklkhndd yrgkivheke rfqdkvhekt
       61 skvsadneks ygtskrneky rtsdkgdvns aietgrsdyi tevkdgkiyd plgkdldndg
      121 iidrydndfr dsdyfestyd vednlhhkae ntnsfsksqk aqkknykrkn yteslytrkk
      181 ddvlkenkpe dkktgkdtas kkvhssiyke qkkklkkdmv kvsalsglak gsetvrdyls
      241 hgsdenqgve agektadtss klihgikkys dkkrakrgyd ltnkdykirk rksklefrda
      301 kkelkktdey krasaykrfq kknqvkaaif renksrlrdr ikegligtlk sskdmiirka
      361 kglmlifigi iilgtfvinf agtgmtgfmn stssvlttsy lskpnvlsei nqnfsameke
      421 lqnevdnvks nhpgydeyil nnteyighnv hellsyitsr cgevksasev esilkelfds
      481 mydleyreei eiryrtvtkt ytdedgneyt esheepyeyk klivtlhkke mdsiirkvfa
      541 nypdnlkhye alflaqgnmg eafgnsdlis anggigggke yeastevqkk ivnaayitps
      601 pgagwcamwv sqvyqnaglg yiggnacdmy rnytftsdrs klkvgmlvav essssgssag
      661 ltyghvgiyi gdgkvidnig rirvttlddw iatfckhhpv gfgfppnvkk
//
LOCUS       WP_006526158             257 aa            linear   BCT 20-JAN-2025
DEFINITION  prolipoprotein diacylglyceryl transferase [Solobacterium moorei].
ACCESSION   WP_006526158
VERSION     WP_006526158.1
KEYWORDS    RefSeq.
SOURCE      Solobacterium moorei
  ORGANISM  Solobacterium moorei
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Erysipelotrichaceae; Solobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002130
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Solobacterium moorei"
                     /db_xref="taxon:102148"
     Protein         1..257
                     /product="prolipoprotein diacylglyceryl transferase"
                     /EC_number="2.5.1.145"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008961 -
                     phosphatidylglycerol-prolipoprotein diacylglyceryl
                     transferase activity [Evidence IEA]"
                     /GO_process="GO:0009249 - protein lipoylation [Evidence
                     IEA]"
                     /GO_process="GO:0042158 - lipoprotein biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28881
     Region          1..245
                     /region_name="Lgt"
                     /note="Prolipoprotein diacylglyceryltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0682"
                     /db_xref="CDD:440446"
ORIGIN      
        1 mfndwfkigp vtvhgygfmi avgilfafwl serlakkqgl eyekidgmif fiiifgfiga
       61 kllyiftvwd sfvknpvvil snegfvvygg iiagiiaawi yckwkkwdfm kyanvlmpav
      121 slgqgfgrig cffagccygi rttawygvef paeslgpgag ikviptelis sagnflifaf
      181 llrnllkgkh pedtaawylv lyglgrflve flrgdlirgq iwifstsqfi sifvflagaf
      241 llwyrqnhsd lkkevaa
//
LOCUS       WP_006526472             158 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Solobacterium moorei].
ACCESSION   WP_006526472
VERSION     WP_006526472.1
KEYWORDS    RefSeq.
SOURCE      Solobacterium moorei
  ORGANISM  Solobacterium moorei
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Erysipelotrichaceae; Solobacterium.
REFERENCE   1  (residues 1 to 158)
  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   2  (residues 1 to 158)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Solobacterium moorei"
                     /db_xref="taxon:102148"
     Protein         1..158
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17382
     Region          34..>69
                     /region_name="SLBB"
                     /note="SLBB domain; pfam10531"
                     /db_xref="CDD:463136"
     Region          87..157
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mrllltvflc liilssgqfh iidinqynks siqvtvhggv lrqgvisldp yatiedllsk
       61 aglsedadls slnletvlhd kdvltiptks ndirinqisi ntadlngllq ipkigektaq
      121 aiidyrnqyg lfqaledlmk vkgigqakfd fikdkicl
//
LOCUS       WP_006527228             618 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Gloeocapsa sp. PCC 73106].
ACCESSION   WP_006527228
VERSION     WP_006527228.1
KEYWORDS    RefSeq.
SOURCE      Gloeocapsa sp. PCC 73106
  ORGANISM  Gloeocapsa sp. PCC 73106
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Chroococcaceae; Gloeocapsa.
REFERENCE   1  (residues 1 to 618)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 618)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 618)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..618
                     /organism="Gloeocapsa sp. PCC 73106"
                     /db_xref="taxon:102232"
     Protein         1..618
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=63817
     Region          60..>371
                     /region_name="AidA"
                     /note="Autotransporter adhesin AidA [Cell
                     wall/membrane/envelope biogenesis, Intracellular
                     trafficking, secretion, and vesicular transport]; COG3468"
                     /db_xref="CDD:442691"
     Region          330..550
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          383..443
                     /region_name="choice_anch_Q"
                     /note="choice-of-anchor Q domain; NF041518"
                     /db_xref="CDD:469403"
ORIGIN      
        1 mlskkstklw ipisiskkif ilnkpkiftn ffsdrilrnp cktnrstsls prqtiefdss
       61 ltgetivlts grlilsseit inglgaeelt ldaggnsslf avndgnpesn ievgingiti
      121 tggqqrvaga ienrenltit essiannssl lggaivnesg eltiidsnis nntagngggg
      181 ifvrggntni adsifsnnqs gsfgggifia apedsvnnin nsvisdnvst lsgagftnfg
      241 geinitnsti lgnrstngsg gailnvadln itnstisgnt afnrggainq aslglltisn
      301 stitgnsatn tagglasyag pnntsqviva ntiisgnfnt pdvalfgsep ltnnitssgg
      361 nligtgnvle ffnqptdqin iinpglaplg dnggptpthl pladspaida gvnalippgv
      421 ttdqrgldri fnetvdvgav eiqvsesned qeiqgtfrnd tltgglgndt ilgltgndsl
      481 lglegndsii gglnndtlvg glgndtlvgg lgrnwfrfds peegidtitd frvrnnliav
      541 sgsgfdnfgt plisnsslpp elfaqlgsit seavfvydpt dgdlfyrrgs ietpetiqla
      601 slspglnlns snfwvtsv
//
LOCUS       WP_006527401             243 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Gloeocapsa sp. PCC 73106].
ACCESSION   WP_006527401
VERSION     WP_006527401.1
KEYWORDS    RefSeq.
SOURCE      Gloeocapsa sp. PCC 73106
  ORGANISM  Gloeocapsa sp. PCC 73106
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Chroococcaceae; Gloeocapsa.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Gloeocapsa sp. PCC 73106"
                     /db_xref="taxon:102232"
     Protein         1..243
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25250
     Region          <2..192
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 matingtnas dtitpssiss gvtggfptsg nddifaldgn dyadggsgnd klvgwrgndt
       61 lfgnsgndnl fgdtgvdyly ggsgndvirg ftnnsqairv lgrndsgnfl ygesgndsiy
      121 ggssndfiyg gterdflqge ggsdtywfls sndsviasyd tisgytager idlgvsdqvv
      181 sssgtltnlt diyflsfssg tsraynvsgq sgifvfhnpd gtnfdsndfv vqlqgyngaa
      241 tiv
//
LOCUS       WP_006529589             730 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Gloeocapsa sp. PCC
            73106].
ACCESSION   WP_006529589
VERSION     WP_006529589.1
KEYWORDS    RefSeq.
SOURCE      Gloeocapsa sp. PCC 73106
  ORGANISM  Gloeocapsa sp. PCC 73106
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Chroococcaceae; Gloeocapsa.
REFERENCE   1  (residues 1 to 730)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 730)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 730)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Gloeocapsa sp. PCC 73106"
                     /db_xref="taxon:102232"
     Protein         1..730
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=81010
     Region          1..710
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mvdsvktlcp ycgvgcglev ssprfsgtgn ptdeqgnpiw kvtgdrahps sqgmvcikga
       61 titeslyknr leypmmrdsl eepfrrcswd qaltrivdhi kllrstqgad aicmygsgqf
      121 qtedyyiaqk llkgclgtnn fdansrlcms savsayiksf gsdgppccye dlehtdcafl
      181 igtntaechp ivfnrlqkyl rknrkarliv vdprttktae aahlhlaikp gtdidllngi
      241 ahillewgei ntffidectk gfyeyaevir hyppelvaak cgisvpqlkk aarywakanr
      301 vlslwsmgin qssegtakar tlinlhlmtg nigkpgagpf sltgqpnamg greagglshl
      361 lpgyrsvlna ehrrdveqfw klepgrispt pgrdawrmit gletgdvgll wiaatnpavs
      421 mpdlsrtkaa llkspltvyq dayyptetsa yahillpaaq wsektgtmtn servvtlcpq
      481 frlppgeaka dwqifaevgk rlgftsqfnf kdsaevyaef vqltrdrfcd ltgishqall
      541 rsgpiqwpcp qdhsreskrl ytdfrfptpd graqfaayhs kglaeppdpe ypfiltvgrl
      601 yghwhtqtrt ghipkitkmy pyprleihpq daariniadg ewlevrsrrg kacfltqitr
      661 aitpgtvfvp mhwgalwaqh aeanllthse acpislepel kacavqlipv lassatlidv
      721 selnsklanf
//
LOCUS       WP_006530439             522 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Gloeocapsa sp. PCC 73106].
ACCESSION   WP_006530439
VERSION     WP_006530439.1
KEYWORDS    RefSeq.
SOURCE      Gloeocapsa sp. PCC 73106
  ORGANISM  Gloeocapsa sp. PCC 73106
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Chroococcaceae; Gloeocapsa.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Gloeocapsa sp. PCC 73106"
                     /db_xref="taxon:102232"
     Protein         1..522
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53116
     Region          4..223
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          247..461
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mnpvnyitgf liseiirgld rqnfisatag ndyvtgfgdd dtiiggsgnd lifgdvnflg
       61 qpsapsnsgn dvifvgegnn aaignggsdy ivggpdndal ntvfsatdgp gndtifgggg
      121 idfvagatgm dllfgeegdd lmvgygnsdt ldggsgddil fgeegndlli gnsgfdfvgs
      181 ssgndifvls dddgidcfvd ftvgqdvial tetlavediq idlpfrgvss fnvishattk
      241 evlalvistt sapisisdlt rfdqtiddtp mnppsgrgrn fssqivsnqf nirgtsgndm
      301 lngsnndeei lggdgidfis agsgddsvfg egdedfligq egddlinaga gpdglnggsg
      361 ddtligeqgs dflragdgnd vldggpgfga lvgeegddll lggnavdnlk ggpgedsleg
      421 nnssdylngg sgddfldggl asdifiggtg rdtfviglsd gpdvildfed rldvialssg
      481 lsfgdlqfvp ngnsvdvyts anipvfnlag vnaslisaad ft
//
LOCUS       WP_006531529             189 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Streptococcus infantarius].
ACCESSION   WP_006531529
VERSION     WP_006531529.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus infantarius
  ORGANISM  Streptococcus infantarius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 189)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Streptococcus infantarius"
                     /db_xref="taxon:102684"
     Protein         1..189
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=21286
     Region          68..189
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mgkkfskkvl illltftnlv vgyglcrqlm vthqesevkl deyafeksmk ktqkkiypdl
       61 skydhlsilv sisqqkmivy skndvifktk vstgakdtpt ptgkfaieae rgdfsyddsl
      121 nrgvcywvsf kdhgacqfqs lptdwkgkvl kgetkklgka ctdgnvrlsk edakwlfenm
      181 pegvivsvh
//
LOCUS       WP_006533427             206 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Proteus].
ACCESSION   WP_006533427
VERSION     WP_006533427.1
KEYWORDS    RefSeq.
SOURCE      Proteus
  ORGANISM  Proteus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
REFERENCE   1  (residues 1 to 206)
  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 206)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 206)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Proteus"
                     /db_xref="taxon:583"
     Protein         1..206
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22148
     Region          1..204
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 mevysteneq vdaikqffkn ygltivlaav igfggvfgwk ywqshqtnrl qesagafati
       61 sealakptpe nialaekfvt etndiygala slelaqiaid andlvsgerh ltnavakvkn
      121 dafadmlnlr larvqlaldk tdaalvsleq vkgkawngmk nyirgdvlak kgdnagaaaa
      181 yrsaltdena gairslvelk lnnlsn
//
LOCUS       WP_006540953             349 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Parafrankia sp. EUN1f].
ACCESSION   WP_006540953
VERSION     WP_006540953.1
KEYWORDS    RefSeq.
SOURCE      Parafrankia sp. EUN1f
  ORGANISM  Parafrankia sp. EUN1f
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae; Parafrankia.
REFERENCE   1  (residues 1 to 349)
  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 349)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 349)
  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   4  (residues 1 to 349)
  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 349)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Parafrankia sp. EUN1f"
                     /db_xref="taxon:102897"
     Protein         1..349
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37457
     Region          82..310
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          229..310
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mpvpgrpdvd teavaqerve repgerepge qvdehvrvap apnlrpyvaw ysgyrqrglp
       61 pavhrglpsp altliftlde plvlldppga garrrsfdsl igglhtapal ithqgaqsgv
      121 qlalrplgar allglpagel aaldlpadav lggagrrmsd rlreargwpe rfavldqelt
      181 glvradrpra grfgdvgrvg qierevpael rhawnllrrg hgnvpiavia aevgwstrhl
      241 sdrfrvelgl apkaaarvir fdrarrllvs rdrrwrladl aaecgyfdqa hlardfralt
      301 gcspsgwlaa efrnvqadgy gfdesldgpg psspgtgtgt gtgtgtgtg
//
LOCUS       WP_006541278             448 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Parafrankia sp. EUN1f].
ACCESSION   WP_006541278
VERSION     WP_006541278.1
KEYWORDS    RefSeq.
SOURCE      Parafrankia sp. EUN1f
  ORGANISM  Parafrankia sp. EUN1f
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae; Parafrankia.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 448)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Parafrankia sp. EUN1f"
                     /db_xref="taxon:102897"
     Protein         1..448
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=46827
     Region          198..424
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 maesghrgdt mappcpvrpe sdskrepdpe rpaglepvag pepvpaavag llatargcle
       61 vdvcwlsrli ggtqvieacs gdaasfgvrp gstvrygdrr hshghtghpp apagqaspgt
      121 gtgtsaaegq vsgrlgagsy lgvpvvladg rlygmlccls hdrvltargr qarslillag
      181 vlaeslscqp pdlearrgrf rqlidnggpr mtfqpvfelp smdcmgaeal arfppgfggp
      241 ercfaeaael gldialevsa irvalralpq lppefglgfn aspttivsga iakiivglpa
      301 drlvleiteh dhiedypaid raldvlrrag vrvavddvgr gsaglrhlvq lrpdfikmdr
      361 cltqhidvdp arralatalv sfaretdglv laegvetaae ldvligagvh qaqghllarp
      421 gplplppnad qahpqpdtsp peptsehs
//
LOCUS       WP_006541716             199 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Frankiaceae].
ACCESSION   WP_006541716
VERSION     WP_006541716.1
KEYWORDS    RefSeq.
SOURCE      Frankiaceae
  ORGANISM  Frankiaceae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales.
REFERENCE   1  (residues 1 to 199)
  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 199)
  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   3  (residues 1 to 199)
  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   4  (residues 1 to 199)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 199)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 199)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Frankiaceae"
                     /db_xref="taxon:74712"
     Protein         1..199
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21915
     Region          8..199
                     /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"
ORIGIN      
        1 msqpsstprr vliaedeali rldlremlqe egyevvgeag dgetavalag klrpdlvild
       61 vkmpkmdgid agakiakdri apvviltafs qrelverare agamayvvkp fqkkdllpti
      121 emamsrftei vsleaevedl qgrlearkii erakgvlqte hsmtepdafr wiqrtsmnqr
      181 rtmravaeav lsgealpgs
//
LOCUS       WP_006541770             742 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Parafrankia sp. EUN1f].
ACCESSION   WP_006541770
VERSION     WP_006541770.1
KEYWORDS    RefSeq.
SOURCE      Parafrankia sp. EUN1f
  ORGANISM  Parafrankia sp. EUN1f
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae; Parafrankia.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 742)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Parafrankia sp. EUN1f"
                     /db_xref="taxon:102897"
     Protein         1..742
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=77427
     Region          26..742
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mpepdvdsas paaperapal rridwsrlfs prvvavvgat dtegspqraq wtqvrerlga
       61 lgadvvpvhp kkpdilgvra ypsvaelpad pdvvvvlvrd plpaveeava rgagfvivfs
      121 agfaelgtae gdaaearlre laagstriig pntnlnifep wqqglpgrkl aiitqsgyqg
      181 rpitqgqvlg igiemwatlg netdiewadv aghlatrpgv gviatyvegf qdgrafmlaa
      241 dacvragipv iaikvgrsee gramaaahtg hltgpdavhd avfdqygvir vddideviei
      301 sglfchagll pgaggvavya msggtashva dlcglagvpv phftpetvaa lgeyipwylk
      361 rdnpvdsggv itarpenrrv leimlddpnv dvlfapitgv fpgmsdalar dlialheraq
      421 agegkpvvaa wtspirddda yralcaagvp lfhsfgaavr glgelgrfsr lvreyrspfa
      481 pgaetgtgae teadaeaeae agvprpsaga ttrarallat rsgalnevds kqllaaygip
      541 vvaerlttsp deavatatel gfpvvlkias adiahksdlg lvavgvrdaa dvraayarlt
      601 startaapda ridgvvvaem vtdavaevil glshqppfgp titfglggvf tevfadvafa
      661 vppfdadrar aviestrgvr llrgargrpa gdidalveti mrlqvlavdv gdqiaeldin
      721 pvmvrpagrg vvavdalvip rr
//
LOCUS       WP_006541864             170 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase, partial [Parafrankia sp. EUN1f].
ACCESSION   WP_006541864
VERSION     WP_006541864.1
KEYWORDS    RefSeq.
SOURCE      Parafrankia sp. EUN1f
  ORGANISM  Parafrankia sp. EUN1f
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae; Parafrankia.
REFERENCE   1  (residues 1 to 170)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Parafrankia sp. EUN1f"
                     /db_xref="taxon:102897"
     Protein         <1..170
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
     Region          49..169
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(115,126,129,142..145,147)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 npnengaprv flvqakmpgw wqvllpvepn gstgwvkaaq vnasqtpyri evargahvlr
       61 lfsgdqkiae ekvaigtsdt ptpggrfflm ellrpsnpng aygpyafgls gfstslddfg
      121 grdpvigihg tndpsslgrd vshgcirlsn dsitrlaqtv plgtpveiva
//
LOCUS       WP_006543394             655 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Parafrankia sp. EUN1f].
ACCESSION   WP_006543394
VERSION     WP_006543394.1
KEYWORDS    RefSeq.
SOURCE      Parafrankia sp. EUN1f
  ORGANISM  Parafrankia sp. EUN1f
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae; Parafrankia.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 655)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 655)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 655)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 655)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 655)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Parafrankia sp. EUN1f"
                     /db_xref="taxon:102897"
     Protein         1..655
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=70410
     Region          29..655
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mtdrqqaape papaqpsdah ippsrdvvrl alvvgalgvv fgdigtspiy tlqtvfnped
       61 phpvpvstds vfgvvsmvfw svmiivtvty vllamradnd geggimalit llrrlgtqrs
      121 rratavlagl gifgaalffg dsmitpaisv lsaveglkiv kpsfddlvvp ltaaiivvlf
      181 lvqrrgtaav grifgpvmia wfvtvgvlgv agitghpail kalsptyaas flvhhisigf
      241 falaavvlav tgaealyadm ghfgrraitr awlllvfpac vlsylgqgal llehpdriss
      301 pffllapgwa rlplvllata atviasqavi tgaysvasqa aelgylprlr iahtsestig
      361 qiyipwinwl lmvsvltlvf afrssaalay afgmavtgti tittlmffyv arlrwhtprw
      421 llglgasvll lvdllfvaan ltklvhgawl pllialtaft vmttwqrgrq ivtaqrhtre
      481 gslrdfveel hattsptaqv pgtavflnrg kqtaplalra nvehnhvrhd lvlimsvetl
      541 pvprvpangr iavddlgyad dgishitarf gymdkpdvlg alraldpati egqrlnlgqa
      601 syflskielr vgdapsmarw rkrlfiatsy itadaaehfg lprdrtvimg ahiei
//
LOCUS       WP_006524728             160 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Desulfoscipio gibsoniae].
ACCESSION   WP_006524728
VERSION     WP_006524728.1
KEYWORDS    RefSeq.
SOURCE      Desulfoscipio gibsoniae
  ORGANISM  Desulfoscipio gibsoniae
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfallaceae; Desulfoscipio.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Desulfoscipio gibsoniae"
                     /db_xref="taxon:102134"
     Protein         1..160
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17159
     Region          33..127
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 mslstfvqta ngevgytegp nndtkyglwf glnyqpwcsi fvawcaneag ilttaatase
       61 pnvyktasvq tlynwyasnr rnltpstnps sanypkvgdl afidgtsnhv giivavssts
      121 ittvegnisd qvtkvtysms tlrnsngnti sylgsnnthy
//
LOCUS       WP_006546432             490 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Gleimia coleocanis].
ACCESSION   WP_006546432
VERSION     WP_006546432.1
KEYWORDS    RefSeq.
SOURCE      Gleimia coleocanis
  ORGANISM  Gleimia coleocanis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Gleimia.
REFERENCE   1  (residues 1 to 490)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Gleimia coleocanis"
                     /db_xref="taxon:103618"
     Protein         1..490
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=53109
     Region          92..195
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          <254..332
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          367..489
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(441..442,445,462..465,467)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mdavesvepv aakktglklk itagiaavla itlggssvay gmyfedralp svtiagqdvs
       61 gmkeaeiakm itdqagkqkl kfkvgekevt atyaeigvet daeataknvl kanqsiwnrf
      121 tayfnptkqq vvtkfnetkf ndflgtlekt ldkprqdaal nvnaetgefs vvpgkmgevv
      181 dkedlrtqve aqvmnltsep iitkivslep eltdaevtaf qqkatelanl dltffegeed
      241 itieylqkvg lisfkdaagk tvepkydadk vrefvaklae qtneepepal hnvngagkvl
      301 avakegkpgw kvnnasavad aavnslaagk afrgeftydk iqqkvetrli adgaenlayq
      361 aapgerwidi nlsnytmtay egatpvfftd qivpganetp tvvgkfavyl kynvqdmrgt
      421 nfdgtpyltk gvpwvtyfhg gyaihgapwr svfglghggn gthgcintpt gnakwiydws
      481 qmgdpvvvhy
//
LOCUS       WP_006547274             207 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Gleimia coleocanis].
ACCESSION   WP_006547274
VERSION     WP_006547274.1
KEYWORDS    RefSeq.
SOURCE      Gleimia coleocanis
  ORGANISM  Gleimia coleocanis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Gleimia.
REFERENCE   1  (residues 1 to 207)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Gleimia coleocanis"
                     /db_xref="taxon:103618"
     Protein         1..207
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=22648
     Region          92..176
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 metqntepqe aprapqitpr vayrkrrqrr qgkvfnvivv lmgisslval liltgllkfp
       61 yynsfnkver faekgniacv gknvkpadlt gvkikvfngt sragladtvg talagvglef
      121 tekanydgqf fgnirivtng knvvnaysla rlfegasvyy dpdaadviqi ivgdaftemk
      181 paeelkaiae krdvefenpe gclkvke
//
LOCUS       WP_006547450             286 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Gleimia coleocanis].
ACCESSION   WP_006547450
VERSION     WP_006547450.1
KEYWORDS    RefSeq.
SOURCE      Gleimia coleocanis
  ORGANISM  Gleimia coleocanis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Gleimia.
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
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Gleimia coleocanis"
                     /db_xref="taxon:103618"
     Protein         1..286
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=31369
     Region          1..>248
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 miefknvskq fpnssqkavd dfsyvipsre ihvflgssgc gkttllrcvn rmeiptsgqi
       61 lwddqdvael npvelrrsig yvmqsaglmp hrtvldnvtt vlrlrngeak lskeqirsrg
      121 lemlelvgld pqlasrypaq lsggqaqrvg varalapnpr vvlmdepfaa vdplvrtqlq
      181 dlvrdlqrel kttilfvthd vdeavrladk iivlseraqi rqagtarell sqpadqfvad
      241 flginrelpl elgaqnlvfn pdgrplghls fpegvagsvt daeagi
//
LOCUS       WP_006547800             204 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Actinomyces urogenitalis].
ACCESSION   WP_006547800
VERSION     WP_006547800.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces urogenitalis
  ORGANISM  Actinomyces urogenitalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Actinomyces urogenitalis"
                     /db_xref="taxon:103621"
     Protein         1..204
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21924
     Region          12..201
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 msetvlrgar rrervvvait gasgtvygvr llqalaattv ethlvispsg qltrsletdw
       61 skeeveslad vvwkpsdmaa aissgsfrtr gmvvapcsmr tlgeiasgvt sslvscaadv
      121 tlkerrrlvl varesplsli hlrnmtavte agavvvppvp gfytrpatve qivdqtvgrc
      181 ldlldiepae gwqrrrwgeg elar
//
LOCUS       WP_006554494             332 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Rhodococcus
            pyridinivorans].
ACCESSION   WP_006554494
VERSION     WP_006554494.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus pyridinivorans
  ORGANISM  Rhodococcus pyridinivorans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Rhodococcus pyridinivorans"
                     /db_xref="taxon:103816"
     Protein         1..332
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=35687
     Region          2..321
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mitvtgarkn ygdfaaladv didipsgslt allgpsgsgk stllrsiagl etldagtvhi
       61 agkdvtgvtp qkrdigfvfq hyaafkhmtv renvafglki rkrpkaeitk rvddlleivg
      121 lggfqrrypa qlsggqrqrm alaralavdp qvllldepfg aldakvradl rtwlrrlhde
      181 vhvttvlvth dqeealdvad riavmnagri eqvgtpeely drpansfvms flgtvsklng
      241 vlvrphdirl arqpalsdts ggsvgvtrat vervvrlgfe vrvelrndat geqfttkitr
      301 gethdlglva gdtvyahapa asetaplgta aq
//
LOCUS       WP_006556346             196 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Veillonella seminalis].
ACCESSION   WP_006556346
VERSION     WP_006556346.1
KEYWORDS    RefSeq.
SOURCE      Veillonella seminalis
  ORGANISM  Veillonella seminalis
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Veillonella.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Veillonella seminalis"
                     /db_xref="taxon:1502943"
     Protein         1..196
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=22253
     Region          11..196
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 msekcilkla yenngvvtsa rvseanisrn ylaqlvkank lekvsrgvyt lpdvwedkfl
       61 naqvkykkgi fslgtalylh gftdrtpmrl hftfpegynt saplkngfkc nkvkkdvfef
      121 gveevktpsg nlvraynier tlcdivkttn rveiqvitda fkqymnsksk nipllssyak
      181 llkvdkkirp ylevlq
//
LOCUS       WP_006557919             355 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Acetobacter
            tropicalis].
ACCESSION   WP_006557919
VERSION     WP_006557919.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter tropicalis
  ORGANISM  Acetobacter tropicalis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Acetobacter tropicalis"
                     /db_xref="taxon:104102"
     Protein         1..355
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38513
     Region          1..>287
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msvliqnlvr capgtrkrll ndvsldvptg afvalvgpsg agkttllrai agldtcesgs
       61 llldgqkven mqdrarkigf vfqnyalfph mtvarnisfg ldvqpramrp sqgeiaarvq
      121 elldlmqlpd mgkayparls ggqrqrvala ralatgpgll lldepfgald pivrrtirsw
      181 lrslhdrlgl ttilvthdqe ealevadriv vmqqgsimqd aspeeldkep atafvmeflg
      241 esatfrgvvq dgwftpeedg vlpfavaaei apgpadamir pfeitiasad lvqgqtvpis
      301 sqgvrngyrh ylarlkdrti avhipdytgg nvlsessgvl disrarlfrd gkrys
//
LOCUS       WP_006558553             814 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Acetobacter tropicalis].
ACCESSION   WP_006558553
VERSION     WP_006558553.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter tropicalis
  ORGANISM  Acetobacter tropicalis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter.
REFERENCE   1  (residues 1 to 814)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 814)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 814)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..814
                     /organism="Acetobacter tropicalis"
                     /db_xref="taxon:104102"
     Protein         1..814
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=88588
     Region          11..811
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mthratalsr rhvllggvaa slagigtral arkaasprll glegltapve vfedqwgvph
       61 vraasvpdaf fangyliard rlwqldfdyr rstgrlaevf gpdfvpsdta nrlflfrgda
      121 qaefaalppt vqacarayva ginayleqvr atgeklppef tifsyqplqw dvldlvrira
      181 eatgntkaei rrarlaaqga ldydalimpl rpahtlrvpd gldvhavteq dlglfgvlqa
      241 slplsglhap psaseddhrr anegsnawvi aptrtatgrp ilandphlsf gspgprhvih
      301 ltapgldvig ggsagmpgvm qghnahfafg rtnfhidqed lfilrthpah pdryfhngrw
      361 vemertetti avrdeaartv tlhyaaqgpv vstnaarnra vavsatwlyp gangmlanig
      421 inlaqdwtsf realklhtsp tnftyadtag nigwqaaggl persggydgl mpapgdgryd
      481 wkglqpldal pnsfnpargw fgtsnelnlp adypyeqrcv syewkdpyry nrvaevlaas
      541 phatlaqsva lqhdtlshla lsvvkllpdv padiraeadl lrrwdgrvea tsaaaalyev
      601 wwtrlntlfy qalvpenlra llpqplnasv llaflqkpdg rvgdkpeaar dallvkafqq
      661 aveeardrmg pvaaawqwgt lhtlqlrhpl haveavakaf lpiggetths ggdpytvmar
      721 wynpdlsqka lahghnpyav tggasylmvc dvgawdhslf lnfpgqsalp dsghyedflq
      781 pwlkgamqpl vfsasavqaa arhhavlypk gktp
//
LOCUS       WP_006559786             196 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Acetobacter tropicalis].
ACCESSION   WP_006559786
VERSION     WP_006559786.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter tropicalis
  ORGANISM  Acetobacter tropicalis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Acetobacter tropicalis"
                     /db_xref="taxon:104102"
     Protein         1..196
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20774
     Region          3..187
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 markrivvgi tgasgfqygv dvlsllrdad ieshlvmsrg aqltrehetg lsaedvyala
       61 tyihspgalg apissgsfrt egmiiapcsm htlgaiasgv tdnlvtraad valkerrrlv
      121 lmtreaplhl ghlrnmqavt eyggiifppv paiyaaprts adiirhsaar alsllgvhvp
      181 dmprwgetls avsaek
//
LOCUS       WP_006564137              73 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Helicobacter suis].
ACCESSION   WP_006564137
VERSION     WP_006564137.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter suis
  ORGANISM  Helicobacter suis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 73)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 73)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 73)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 73)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..73
                     /organism="Helicobacter suis"
                     /db_xref="taxon:104628"
     Protein         1..73
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=7954
     Region          1..73
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mvyvkflgpi keetfeveas nleglrqilh ekqnlhswls vsavaingel iedihtplra
       61 gdevvflppv cgg
//
LOCUS       WP_006564874             768 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Helicobacter suis].
ACCESSION   WP_006564874
VERSION     WP_006564874.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter suis
  ORGANISM  Helicobacter suis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 768)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..768
                     /organism="Helicobacter suis"
                     /db_xref="taxon:104628"
     Protein         1..768
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=86526
     Region          1..768
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mrrvtlflcg csllissaqa iktktlkkiq tteaiqdeda pkswhsngvk nylgsrtvis
       61 nkqltheanm sieqalqnvp gihirnftgv gampsfsirg fgggspghsn telvlvngip
      121 iyvapyalig isifpvtfqs vdrisvikgg esvqygpnaf ggviniitkp ipekwsnqia
      181 qrvtywgrsr nggfitptst plnkslgnnf lyntylksgg mfnkyvgvma qtnyitgqgf
      241 rynspttiqn ymldgiyqin atnkitvsyq yykyfltdpg slgqaaydqn rfqndrpnnt
      301 ksgdanrwsa vyqtlfgdsd kvggdftlty wghdmsrdfq mdsnylnint npakglvytn
      361 dnyagffivn harhflvnsi epnvnlnint ksmkqtikvg mrvmtsdill hplqstcqns
      421 divngkcnmp tptpllksse emnnnytaay vsdkmeflng kliftpglry trvnynqkvp
      481 ekpdytrmqt lkrefnewsp avnigykpmq nwlfyfnyrr sfippqnrmi alyssnynqi
      541 fdgieagsry gykdllsfna syfitfaqry ysggyspgpv narsqgvele lyytpirglq
      601 fhvaytyina vvtnnviddt nwfigivdhp fsikgkklpy vspdqfifga mytyrnttig
      661 issyfysray ssvlnqakse tvcfhtdpak tggvsfgcns vgllpwywlw niqvsqtfwq
      721 sgrhkivgsl qvnnifnmky yfrgigtspt gmepgpgrsv taylsyqf
//
LOCUS       WP_006566877             497 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Anaerostipes].
ACCESSION   WP_006566877
VERSION     WP_006566877.1
KEYWORDS    RefSeq.
SOURCE      Anaerostipes
  ORGANISM  Anaerostipes
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 497)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Anaerostipes"
                     /db_xref="taxon:207244"
     Protein         1..497
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=57196
     Region          377..496
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(447..448,449,469..472,474)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 makikqkyly imgaaavavi aaltavhiyy kdrwypgssi dglkvsgmty eesldelket
       61 adrysitvkg rekgtltikg rdiglkvksl dsvkelyqkq hkqsvifsfm kkeqknlkdt
      121 idfsekklsg lvkksvlvtg ddgykltkpe daaieyskek kygvlkkeie gnildqkafv
      181 rrlseaikel ktsmdltdqk typgvykepg lriddseltr mqetynqyll hwiqwdmgnd
      241 tketmtpevl kdcirvntkk rtvkldksav edwvekfclk yktvgiarkf tthsgkkikv
      301 eggdygwrid ydkeiarvlk llkkapskkl metyqkdpsd knqkamtvnl kpvyfnkayr
      361 kdyqnpqndw dhknysevdl saqevfvykn gkrvfsanci tgkptpdrit rtgtyyvkek
      421 rltktlvgad ysvdtkywvr imwtgtgyhw skrsdwglws pgrykvtgsh gcvnlqlsda
      481 aaiyklvesg dpvfihy
//
LOCUS       WP_006568148             160 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Anaerostipes caccae].
ACCESSION   WP_006568148
VERSION     WP_006568148.1
KEYWORDS    RefSeq.
SOURCE      Anaerostipes caccae
  ORGANISM  Anaerostipes caccae
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Anaerostipes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Anaerostipes caccae"
                     /db_xref="taxon:105841"
     Protein         1..160
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=18224
     Region          49..147
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
ORIGIN      
        1 manedkkdfn kmlyedkgmp kiqivtdeat ikryggermy fappvtydei mkkipcgkvi
       61 tvgtirvyla kkndadftdp itagifvsia awascqrsed etpywrtlka rgelnpkypg
      121 gieaqkerle aeghtivqrg rknikyyvqd yenvlfdleg
//
LOCUS       WP_006568638             102 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Anaerostipes caccae].
ACCESSION   WP_006568638
VERSION     WP_006568638.1
KEYWORDS    RefSeq.
SOURCE      Anaerostipes caccae
  ORGANISM  Anaerostipes caccae
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Anaerostipes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Anaerostipes caccae"
                     /db_xref="taxon:105841"
     Protein         1..102
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11472
     Region          6..101
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(28,59..60,62,83)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(28..29,37,40,42..43,45,48..49,51,59,64,71)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mkkilderli yeilsvveei prgkvatygq iarligrekn arlvgrvlsm aeyygsypch
       61 rvvnhagrlv pgwhdqglll leegavfkdn ghvdlkacqw de
//
LOCUS       WP_006569003             349 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Anaerostipes
            caccae].
ACCESSION   WP_006569003
VERSION     WP_006569003.1
KEYWORDS    RefSeq.
SOURCE      Anaerostipes caccae
  ORGANISM  Anaerostipes caccae
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Anaerostipes.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Anaerostipes caccae"
                     /db_xref="taxon:105841"
     Protein         1..349
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39788
     Region          1..347
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mslyvdiekh lpefhlktsf eagneilsil gasgcgkslt lkciagietp drgrivlngr
       61 vlfdsqkrin lpardrkvgy lfqnyalfph mtvreniacg lpsrdrsltd swiekfylsg
      121 lgdhypsqls ggqqqrtala rmlasapsli mldepfsald dylkwqmeqe lmhiirdfpg
      181 talfvshnrd evyrmsdria vmgngrlkti qrkkelfqnp esleaalltg cknishaeyi
      241 ddhtffasdw nivltssvpv pkdikyagfr ahyfsiepda tlpntmectv tniiedtfsm
      301 illfrekqnk ksgdwtglrf elpktlwdgq ikkdtvflrf pkdkflfmk
//
LOCUS       WP_006572084             194 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Pseudoflavonifractor
            capillosus].
ACCESSION   WP_006572084
VERSION     WP_006572084.1
KEYWORDS    RefSeq.
SOURCE      Pseudoflavonifractor capillosus
  ORGANISM  Pseudoflavonifractor capillosus
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Pseudoflavonifractor.
REFERENCE   1  (residues 1 to 194)
  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 194)
  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   3  (residues 1 to 194)
  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   4  (residues 1 to 194)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 194)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 194)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Pseudoflavonifractor capillosus"
                     /db_xref="taxon:106588"
     Protein         1..194
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21612
     Region          4..189
                     /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"
ORIGIN      
        1 mgkdgisvvi addepisrmd lkellteggy tvlsevsdgf daveqcklyh pdlvildikm
       61 pfldgisaak iiyeedladt iimltayser efidqakgcg vsgylvkpid ekslvpsiel
      121 avarsqelkr lrkdmekvse rlksrsviek akgiimqeqg mteqeaydyi rklsldkhls
      181 mrrvaeiilv kngg
//
LOCUS       WP_006572644             399 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Pseudoflavonifractor capillosus].
ACCESSION   WP_006572644
VERSION     WP_006572644.1
KEYWORDS    RefSeq.
SOURCE      Pseudoflavonifractor capillosus
  ORGANISM  Pseudoflavonifractor capillosus
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Pseudoflavonifractor.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Pseudoflavonifractor capillosus"
                     /db_xref="taxon:106588"
     Protein         1..399
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42710
     Region          1..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkvlvinags sslkyqlmdp atrdvlakgl cerigidgrl thkvpakdqk feaeiampth
       61 aeaieavlqa ltdsdhgvia smdeidavgh rvlhggmaft esciiddaci eaikeciplg
      121 plhnpanlmg ieacqkvmpt kpqvavfdta fhmtmpekaf tyaipyeyye kdkvrrygfh
      181 gtshryvsar aaalmgrdpk glklischlg ngsslaaivd gkcvdttmgl gplagvpmgt
      241 ragdmdatil eylmgrygyd ikemltilnk ksgvlgisgv ssdfrdlesa aaegnhrarl
      301 aldvfyydvk kyigayaaam ggvdgiifta gvgenaagtr maiasgleym gvkmdeeknn
      361 trgkeaiisa ddskvtvmvi ptdeelmias dtaeivskl
//
LOCUS       WP_006572715             141 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein
            [Pseudoflavonifractor capillosus].
ACCESSION   WP_006572715
VERSION     WP_006572715.1
KEYWORDS    RefSeq.
SOURCE      Pseudoflavonifractor capillosus
  ORGANISM  Pseudoflavonifractor capillosus
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Pseudoflavonifractor.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 141)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 141)
  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 141)
  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 141)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Pseudoflavonifractor capillosus"
                     /db_xref="taxon:106588"
     Protein         1..141
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16528
     Region          42..133
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(61,80..81,100,103,111..112,125,130)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 milelherdt evleqilsil knhpeiekfe ideepmvslp gleifpsrrk vfrdrqeiql
       61 takeyrilll laankgrvlt yaqiyeqvwg dfttgnennt igfhicnlre klyranpdap
      121 fyirsvrevg ycleafterl e
//
LOCUS       WP_006572726             138 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein
            [Pseudoflavonifractor capillosus].
ACCESSION   WP_006572726
VERSION     WP_006572726.1
KEYWORDS    RefSeq.
SOURCE      Pseudoflavonifractor capillosus
  ORGANISM  Pseudoflavonifractor capillosus
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Pseudoflavonifractor.
REFERENCE   1  (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   2  (residues 1 to 138)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 138)
  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 138)
  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 138)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Pseudoflavonifractor capillosus"
                     /db_xref="taxon:106588"
     Protein         1..138
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16047
     Region          42..133
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(61,80..81,100,103,111..112,125,130)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 milelherdt evleqilsil knhpeiekie vdeepmvslp gleifpsrrk vfrdrqeiql
       61 takeyrilll laankgrvlt yaqiyeqvwg dfttgnennt igfhicnlre klyqanpdal
      121 fyirsvrevg ycldvdep
//
LOCUS       WP_006572981             147 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Pseudoflavonifractor capillosus].
ACCESSION   WP_006572981
VERSION     WP_006572981.1
KEYWORDS    RefSeq.
SOURCE      Pseudoflavonifractor capillosus
  ORGANISM  Pseudoflavonifractor capillosus
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Pseudoflavonifractor.
REFERENCE   1  (residues 1 to 147)
  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   2  (residues 1 to 147)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Pseudoflavonifractor capillosus"
                     /db_xref="taxon:106588"
     Protein         1..147
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15553
     Region          31..>101
                     /region_name="PRK13042"
                     /note="superantigen-like protein SSL4; Reviewed"
                     /db_xref="CDD:183854"
     Region          73..145
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkisrlefvl llltaaclaf fagwflggqp vpgtvritar hspepsvmas lpvsqtpeps
       61 etgpvetetq tpapspsape qqsglinint adsetlqtlp sigekraaai iayreehgpf
      121 riveditnvs gigegilsqi idyitve
//
LOCUS       WP_006573111             118 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein
            [Pseudoflavonifractor capillosus].
ACCESSION   WP_006573111
VERSION     WP_006573111.1
KEYWORDS    RefSeq.
SOURCE      Pseudoflavonifractor capillosus
  ORGANISM  Pseudoflavonifractor capillosus
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Pseudoflavonifractor.
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   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
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   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Pseudoflavonifractor capillosus"
                     /db_xref="taxon:106588"
     Protein         1..118
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12924
     Region          47..>95
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mdeiiviraa dpdgsvfqav mdalkgkrae midvveqsas vlrigdleih heqrrvlmag
       61 revelnhgey amlycmassp gqmfskaqly eaawgggisk rdklrgeyhl aaetetgt
//
LOCUS       WP_006574057             180 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Pseudoflavonifractor
            capillosus].
ACCESSION   WP_006574057
VERSION     WP_006574057.1
KEYWORDS    RefSeq.
SOURCE      Pseudoflavonifractor capillosus
  ORGANISM  Pseudoflavonifractor capillosus
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Pseudoflavonifractor.
REFERENCE   1  (residues 1 to 180)
  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 180)
  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   3  (residues 1 to 180)
  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   4  (residues 1 to 180)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 180)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Pseudoflavonifractor capillosus"
                     /db_xref="taxon:106588"
     Protein         1..180
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=19885
     Region          3..175
                     /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"
ORIGIN      
        1 mekiivafak eessrrirei lessgtaacv vcrsaaevkr vvskqrisav vcgykfhdes
       61 aehlfedlpp acamlmiaaq smlemcesdd ifklaspvsr gdliasvrll lqvghrlekm
      121 trprrseeek avveqakavl mssrgiseee ahrylqkrsm dsgsrlldta rqvlsedcga
//
LOCUS       WP_006574837              76 aa            linear   BCT 20-JAN-2025
DEFINITION  acyl carrier protein [Pseudoflavonifractor capillosus].
ACCESSION   WP_006574837
VERSION     WP_006574837.1
KEYWORDS    RefSeq.
SOURCE      Pseudoflavonifractor capillosus
  ORGANISM  Pseudoflavonifractor capillosus
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Pseudoflavonifractor.
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   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 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   4  (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 10011594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Pseudoflavonifractor capillosus"
                     /db_xref="taxon:106588"
     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=8125
     Region          1..76
                     /region_name="acpP"
                     /note="acyl carrier protein; Provisional; PRK00982"
                     /db_xref="CDD:179197"
ORIGIN      
        1 mtfeemrdii vetlscdaed vtmeaklsed lgadslaave lsmaleeasg vtiedddlpn
       61 mktvgdlmay ieshka
//
LOCUS       WP_006575909             270 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Cupriavidus].
ACCESSION   WP_006575909
VERSION     WP_006575909.1
KEYWORDS    RefSeq.
SOURCE      unclassified Cupriavidus
  ORGANISM  unclassified Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (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   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="unclassified Cupriavidus"
                     /db_xref="taxon:2640874"
     Protein         1..270
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29563
     Region          3..101
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          175..249
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mfqviapcpa lapyvngywf vqdlegmyeg qpivtcpypg avlsvnfgrp nameggptvp
       61 kvsllgfqsa srrwrswsdt yfvmamlgav glarlfpgig adckdrlmdl agylgdgaac
      121 aleadlsaaw spgriarqld dwllrrldai rapmelptla aahallrqgr qvqdiarlta
      181 vdrrqlhrwf erhlglgpkq lmdlerlqss iqavqrgdgd alsgysdqah qirnwrrrla
      241 qtpggyarag psplaehfga qstdgpafyl
//
LOCUS       WP_006576880             251 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Cupriavidus].
ACCESSION   WP_006576880
VERSION     WP_006576880.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  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   3  (residues 1 to 251)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..251
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27741
     Region          46..250
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 msshesidrp eaaaasdaas deqyrlthas qigtvlrdla wqkctlnvrs grgretvssv
       61 lhvdpasrtf ifdwcrteee aravleaeen tisaslrgvp vnfaigrpep vqyqggpafk
      121 apfpdklyhf qrrrhfrart lvtrgygceg rlddgtvvkl disdlslsgv glrsrtvgda
      181 qlpvgtriar arldfrelgk ldldlqvvgh wlvgrddsai hhfgcafvnp dgrlentlqr
      241 lvfalelahr g
//
LOCUS       WP_006578584             292 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Cupriavidus].
ACCESSION   WP_006578584
VERSION     WP_006578584.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 292)
  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   3  (residues 1 to 292)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..292
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30564
     Region          87..283
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mipltpndlp vgqplpwsll dgqgnlllgs gkvladgrdv alvfrhgsvc rpdplppdda
       61 apvgavrvdp vpaqasgplg lqvgtllqik apddggraaa srligfieqg lfvswpqfgg
      121 ndatfqagee vllrgftgqs ihsfrctvta vcrspfrylv lsvptevqqv pvrssprvqt
      181 rlaaqlmdqd gdaagaprla vlsdlsagga lvqtagptpa pgtrlqlrfv lrtagtdsei
      241 tvdawarnpa rddgdaefpa fgvafdllge reaallhcyi yeqllaaasm tv
//
LOCUS       WP_006547968             450 aa            linear   BCT 20-JAN-2025
DEFINITION  ferrochelatase [Actinomyces urogenitalis].
ACCESSION   WP_006547968
VERSION     WP_006547968.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces urogenitalis
  ORGANISM  Actinomyces urogenitalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Ferreira,G.C.
  TITLE     Ferrochelatase
  JOURNAL   Int J Biochem Cell Biol 31 (10), 995-1000 (1999)
   PUBMED   10582332
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Ferreira,G.C., Franco,R., Lloyd,S.G., Moura,I., Moura,J.J. and
            Huynh,B.H.
  TITLE     Structure and function of ferrochelatase
  JOURNAL   J Bioenerg Biomembr 27 (2), 221-229 (1995)
   PUBMED   7592569
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Taketani,S.
  TITLE     Molecular and genetic characterization of ferrochelatase
  JOURNAL   Tohoku J Exp Med 171 (1), 1-20 (1993)
   PUBMED   8122254
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Cole,S.P. and Marks,G.S.
  TITLE     Ferrochelatase and N-alkylated porphyrins
  JOURNAL   Mol Cell Biochem 64 (2), 127-137 (1984)
   PUBMED   6390167
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11477763
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Actinomyces urogenitalis"
                     /db_xref="taxon:103621"
     Protein         1..450
                     /product="ferrochelatase"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0004325 - ferrochelatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47275
     Region          28..404
                     /region_name="hemH"
                     /note="ferrochelatase; Reviewed; PRK00035"
                     /db_xref="CDD:234585"
ORIGIN      
        1 mpestaptht aasagrqasa paspdplapy davlilsygg pmgpddvlpf mrnatagrgv
       61 pdsrllevsg hygrfegvsp inarnaemle alraelarrg srvpvaignr nwhpfvseam
      121 rsladagarh vltmttsayg sysgcrqyre dtaaalalla agadgetgqg wevdaaarvg
      181 gaggapvela vdktrpfynt pgmleanvda ivdayrqled rgvdaagvrl vlvthsvplg
      241 meedssphaa eraagvspav aepgvapdls teisyveqhr rlaevllpqv rerlgmaedp
      301 qtdlvycsrs gppqarwlep dvndhleala agrltdgtav avpagvvvap igfvadhmev
      361 vfdldteare taerlhlpyv raatagthpa fissladilv eraavargee vepdsttgtg
      421 pfhtvcpdvc crpgvrrrph arpggphgqd
//
LOCUS       WP_006578738             829 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Cupriavidus sp. HPC(L)].
ACCESSION   WP_006578738
VERSION     WP_006578738.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. HPC(L)
  ORGANISM  Cupriavidus sp. HPC(L)
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 829)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 829)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 829)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..829
                     /organism="Cupriavidus sp. HPC(L)"
                     /db_xref="taxon:1217418"
     Protein         1..829
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=90794
     Region          9..818
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mhwlkrlawl tvilaglvla aaiggyawyr qasqpavagt valaglhgrv tivrdrhaip
       61 rieagdplda yfglgfvhaq drlwqmqmnk riasgrlaei lgasalptdr flrtigvrrn
      121 aeaafaastp etraalqaya dgvnagiash kgplppefai lrtvperwep adtlawqtmm
      181 awdlsanwsr evlrmrlaqt lplsrinell apypgeqplr ttdypalyrq laplttamag
      241 veaaappglv egmgsnnwvv sgahtrsgkp llandlhlgl qapalwyfat lrapgldvtg
      301 atlpgmpvvv ightpriawg ftntapdlqd lyierlrpgr peqyqtpngw adfsvreeti
      361 rvkdqsdvti rvrstrhgpv isdvadqlaa avaplgaqyv vsfqwvalrp ddrtvqaglk
      421 lnrahdwasf tealrdfhtp qqsavyadvd gnigflapgr vplrnaandl kglapapgwd
      481 arydwsgfip feklprslnp pggvvvtanq kivpddypff ltsewtvpyr hdrirallaa
      541 rrphtldtfa aiqkdelsla vkdalplllg asiaaddsrp arerelfaal arwdgtmsad
      601 rteplvataw lrelsrgmfe gkvgdgvfar mweqrnvqqa mlnilrssrg lgrfwcddpk
      661 tpapedcndq mgaawkraia dlqqrygddp rrwrwgqaha araehrpfar vpslagffnv
      721 kvptggdtyt vnagrhnigd eqapfenvhg asvraiydla dlsasrfitp tgqsgnvlsp
      781 hyrdwteqwa rgeyvtirga ghpagakafe tlvltpaagd ggrtsgasr
//
LOCUS       WP_006579690             383 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Cupriavidus].
ACCESSION   WP_006579690
VERSION     WP_006579690.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 383)
  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 383)
  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   3  (residues 1 to 383)
  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   4  (residues 1 to 383)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 383)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 383)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 383)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..383
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40292
     Region          33..369
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(109..111,131..132,181,233,257)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mnttfhktal tvaltiaglt aasaafaqaq eiklgfaapm tggqaqygkd mqngvvlaie
       61 qmnatkpkig gkevkfvlls eddqadpktg svvaqklvdn giqgmlghfn sgtsipasmv
      121 ynragiaqia matapeytrq gfkttfrmmt sdtqqgsvig tfvvkklgak niaivddrta
      181 ygqgladefe kaakaaggki vrreytndka vdfkavltni krsnpdiiff ggaetqsapm
      241 akqikelglk aplvsgemsk tdnflklagp aaegtvvsla glpleqmpgg akyaqdyekr
      301 fkskvqtysp yaydgatalm tamvkagsad parylpvlaa tnmpgvttkt laydargdlk
      361 dggitvykvv ggkwtvletl ggk
//
LOCUS       WP_006580346             710 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor family protein
            [Acinetobacter].
ACCESSION   WP_006580346
VERSION     WP_006580346.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..710
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=78568
     Region          35..706
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 msllrldrlh ycilmsmgci ssplvwaedl nsdvaklptl hveatrtdtt ylqtpasvfr
       61 ieapqadnss qvnltevvkg ipslqirnre nyaqdlqlsm rgfgarstfg vrgirlyvdg
      121 ipatmpdgqg qtsnidlssl dhvevltgpf sslygnssgg tiltstkegq gkdsielsys
      181 ggsqdksrag lvlqggakga nepsyiisss yfdtdgyreh sgaekilnna klswnlddgs
      241 kinwvtnyvk inaddpqglt hdqwnanpkq qvpflkqfnv rkdieqtqtg mtwskpindk
      301 nelyamaylg nrqvtqyqsi pkstqdasin haggvidfdr nyygadfrwt gkellpnttv
      361 slgvaldamd edrkgfenfn lvngqpsygv kgklrrdedn tlwnidpylq aswqflptwr
      421 idtgvrysnv hykskdnyls ngddsgktdy skvlpslals wqilpelmay msyakgfetp
      481 tftemayqtd ttksgfnfdl kpstsdtyea glksqnqlgd ftlavfqtkt kndivsagss
      541 ngrstfrnad ktlregvefa wnkklwrdlt atasyaylda tfdadipalg niaqipagna
      601 ipgiaknqay islawqpshg lyggvdvqym dkvyvndtns daapsysvts anigyawdlg
      661 twkvksfarv dnlfdknyag svivndgndr yfepadgrnw saglrvikqf
//
LOCUS       WP_006581785             443 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: replicative DNA helicase [Acinetobacter
            calcoaceticus/baumannii complex].
ACCESSION   WP_006581785
VERSION     WP_006581785.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus/baumannii complex
  ORGANISM  Acinetobacter calcoaceticus/baumannii complex
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Acinetobacter calcoaceticus/baumannii complex"
                     /db_xref="taxon:909768"
     Protein         1..443
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=49532
     Region          9..426
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 msfnsnihdv nmeqcvlaal matslslesi gqeldaecfy sdrhqqiyka ivelsesnhp
       61 ydvvmvsnyl kgknvlhlmg gedyliqlmq dapssfynae syvtqlkklk thrkieqigf
      121 riaamakdtt vpdafieaen llsqidkted gdmgasfgda ltsalaqmie ksekktknql
      181 sgvrfnlvtl dkmlgtvqng hfcvvggrpg sgkstlaqmm aidtamvkke gvlfisaemd
      241 ketlsnrmfs slssipydnl hnatlydgll keyaryrevy sglpiwiepk qkpsisevra
      301 yarrakrrfa kagiklgcii vdylqlvrdp skkdrfqevg sisrelksma kefecpvval
      361 vqlnresekg kkpkasdike sgqieqdadq iilvnpltdd ktlqplgvte liiaknrhgk
      421 rgavrvqehl dmcrfkaiqe lee
//
LOCUS       WP_006582151             267 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Acinetobacter calcoaceticus/baumannii complex].
ACCESSION   WP_006582151
VERSION     WP_006582151.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus/baumannii complex
  ORGANISM  Acinetobacter calcoaceticus/baumannii complex
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Acinetobacter calcoaceticus/baumannii complex"
                     /db_xref="taxon:909768"
     Protein         1..267
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30185
     Region          19..67
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msidatnwaw napvktspqr villsladra gedhkcypsn kriakdtvln iktvqkvvne
       61 lielglisdt gerkghtkqv rvlqligvns rednkpnfgt aeqtqkrnnt kigndtdngl
      121 vkdgqtnpnl egnepkngig ndpkigignl plnllmnlsc ehdwipeekt lveilkmkgq
      181 qrnlklifgl pdfefqlgaf nahyeykeqt esskhyafan witdkfeqhi krnpdyteiq
      241 nhqdnipveq pqtqfkgvak kfkgmdq
//
LOCUS       WP_006582201             232 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Acinetobacter
            calcoaceticus/baumannii complex].
ACCESSION   WP_006582201
VERSION     WP_006582201.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus/baumannii complex
  ORGANISM  Acinetobacter calcoaceticus/baumannii complex
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 232)
  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 232)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 232)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Acinetobacter calcoaceticus/baumannii complex"
                     /db_xref="taxon:909768"
     Protein         1..232
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=25760
     Region          3..210
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 mslsdeeqfd slksfakkyg samisgilia liaffgweyw qkrnlatsqt etakvqqlmd
       61 eanatadnpn alasitasad klvkddidsv qaiqtqfvla klayekqdya aaekalkkve
      121 nskvkdegli qvvklrlada qlaqnkydea lktlsgnvdp afkatveelr gdifvakkdi
      181 dsakkeyqaa wdsllerkqe rqilqikles vgvlvedpqi erpiletqve es
//
LOCUS       WP_006582563             187 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Acinetobacter].
ACCESSION   WP_006582563
VERSION     WP_006582563.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..187
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=20617
     Region          3..>103
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mlkqraftli elmitlivta vlaaitypny rrymekrdla vaqqeaqhla selerfkakn
       61 fsykgfdasy iynagtvtpy dattsslllp ldatsttaky tltlldatqh lplsilkgsd
      121 gnetadsakv qglnwviive raknssgepk qannydllin sdgfrcmtkv knvvngytdc
      181 gsnsetw
//
LOCUS       WP_006587110             238 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Lactobacillus].
ACCESSION   WP_006587110
VERSION     WP_006587110.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus
  ORGANISM  Lactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
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   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 238)
  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 238)
  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 238)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Lactobacillus"
                     /db_xref="taxon:1578"
     Protein         1..238
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27554
     Region          148..237
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(167,186..187,205,208,216..217,229,234)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mtkkflilsq npdlttklkq likkkkenyr hlttptslvv alnddddsys gifwditksn
       61 ldttlatlll irnqvagpii iftnshsdrt lnklykakvd fvadleinek lllrifeqrl
      121 wsytfkiqpe ekklakrane eiietgniki ninkysvfkn nepvvltpke fqllvylaqn
      181 kgnvisreql lqkiwgydll gssrivdihi shlrdkledd sshpqhiltk rgfgyrfi
//
LOCUS       WP_006588032             285 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Lactobacillus jensenii].
ACCESSION   WP_006588032
VERSION     WP_006588032.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus jensenii
  ORGANISM  Lactobacillus jensenii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Lactobacillus jensenii"
                     /db_xref="taxon:109790"
     Protein         1..285
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=33721
     Region          149..264
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mcsnqedkki lkselqlpdi qkrlvtlnqd ltntdfdsvn sefigliikn iqvqkgifis
       61 lafpkfcpyn hkkilepill yyiryrtkeh fetkftnfif kviaeaclry fslkdvssfl
      121 dkvtkevies dypdfkfkes yqanddwken lrrpvktprn yrkkqrlvlv llaaemqldy
      181 vdllkkdiev ehiypqagen dddriytign ltllekklng kasnhdfcdk knnyqkskit
      241 itqelyemds wdfdeidsrt edlisdlegi fgqwqddyre llntn
//
LOCUS       WP_006588287             338 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Lactobacillus jensenii].
ACCESSION   WP_006588287
VERSION     WP_006588287.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus jensenii
  ORGANISM  Lactobacillus jensenii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Lactobacillus jensenii"
                     /db_xref="taxon:109790"
     Protein         1..338
                     /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=39602
     Region          4..276
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mkfkriewid fgrgftiflv vvghvlsgiy tnhiypnsdg llmffgefif lfimpvffsl
       61 sgyffkapen mvdyivmikk kawnilvpyi vfsfvyvlln qlggkskeys wgdllkiwyh
      121 pisylwflyi lffifilvga fsllkvslrl qlliyfigfi lvqvlkinfy ifnvfgwvvf
      181 fclgllfkkd lncikskgil saslvlsilg yllmikfvgl shayyndvsl vnfipkvifd
      241 illfsfflni deesklfkyf kqygkyslii ymvhapvlsa iraiilkftm pnvfvlmvvl
      301 liigwvsclv viwmnnrfrl infifnayan vkkiknkr
//
LOCUS       WP_006590121             314 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Bartonella birtlesii].
ACCESSION   WP_006590121
VERSION     WP_006590121.1
KEYWORDS    RefSeq.
SOURCE      Bartonella birtlesii
  ORGANISM  Bartonella birtlesii
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Bartonella birtlesii"
                     /db_xref="taxon:111504"
     Protein         1..314
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=35839
     Region          1..227
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 myqidynsyr siksfnrrvr flvmhytsld fkesvmaltg envsahylvp dpsektyiea
       61 gfkdmrifnl vdenkrawha gmsswagrnn lndtsigiei vnlangdtdf seqayvkail
      121 kdvrvlnpvn kdeselqtdv clwtegsdvn gtalqlekvn lvtynhrgft fpsynptqid
      181 avkelalnil qrypdimptd vvghsdiaig rksdpgaafp wkelymagig awydderkgy
      241 yqeqfcksfp tkediltklk cygydisvac teigyknlir afqlhfrqen ydgildieta
      301 aiiyalvdky fpsh
//
LOCUS       WP_006590177             146 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Bartonella birtlesii].
ACCESSION   WP_006590177
VERSION     WP_006590177.1
KEYWORDS    RefSeq.
SOURCE      Bartonella birtlesii
  ORGANISM  Bartonella birtlesii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Bartonella birtlesii"
                     /db_xref="taxon:111504"
     Protein         1..146
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=15830
     Region          58..132
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mkkiayttli svlmasstya qsfevlskpe iisstgivqv gsdmsaryvt platdfvass
       61 liganvynie nenigevkdi ilrenniagf vvavggflgi gesyvvvspe tiqmtndygk
      121 wklitnatkd slreaptfky egywar
//
LOCUS       WP_006591516             396 aa            linear   BCT 20-JAN-2025
DEFINITION  ferrochelatase [Kineosphaera limosa].
ACCESSION   WP_006591516
VERSION     WP_006591516.1
KEYWORDS    RefSeq.
SOURCE      Kineosphaera limosa
  ORGANISM  Kineosphaera limosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermatophilaceae; Kineosphaera.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Ferreira,G.C.
  TITLE     Ferrochelatase
  JOURNAL   Int J Biochem Cell Biol 31 (10), 995-1000 (1999)
   PUBMED   10582332
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Ferreira,G.C., Franco,R., Lloyd,S.G., Moura,I., Moura,J.J. and
            Huynh,B.H.
  TITLE     Structure and function of ferrochelatase
  JOURNAL   J Bioenerg Biomembr 27 (2), 221-229 (1995)
   PUBMED   7592569
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Taketani,S.
  TITLE     Molecular and genetic characterization of ferrochelatase
  JOURNAL   Tohoku J Exp Med 171 (1), 1-20 (1993)
   PUBMED   8122254
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Cole,S.P. and Marks,G.S.
  TITLE     Ferrochelatase and N-alkylated porphyrins
  JOURNAL   Mol Cell Biochem 64 (2), 127-137 (1984)
   PUBMED   6390167
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11477763
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Kineosphaera limosa"
                     /db_xref="taxon:111564"
     Protein         1..396
                     /product="ferrochelatase"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0004325 - ferrochelatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42130
     Region          8..352
                     /region_name="hemH"
                     /note="ferrochelatase; Reviewed; PRK00035"
                     /db_xref="CDD:234585"
ORIGIN      
        1 msaqnplapy dallylsfgg perqedvmpf lrnvtagrgi pderleevat hyrarggrsp
       61 indenravlt rleaelaara vqvpvvwgnk ffdpytveal rsaqeagarr lltvvtsafp
      121 sysgcrsyre dlaaaraele asaaaagaes lqidvlrpyg qtrafvepmk tltvaglrdl
      181 caqagltpeq vrilfvthsi peamnaasgp teepstyitm httvcdelaa gvraetgvav
      241 pwqlvycsrs gpptqpwlep dvndaiaaia adrdehpgeg gvggvlivpm gfvsdhmevv
      301 ydldeeamat agehglaalr vptvrddqrf vsglvdllle raraereapa tpglrcpagc
      361 cagrspakpt vsdeaspada eisphsgesv aargcr
//
LOCUS       WP_006591972             418 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Kineosphaera
            limosa].
ACCESSION   WP_006591972
VERSION     WP_006591972.1
KEYWORDS    RefSeq.
SOURCE      Kineosphaera limosa
  ORGANISM  Kineosphaera limosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermatophilaceae; Kineosphaera.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 418)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Kineosphaera limosa"
                     /db_xref="taxon:111564"
     Protein         1..418
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=45227
     Region          38..407
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mttseataae drpvrafawa wlpnatepvl tgridvvgdr hfftyarsyl arsdaislyv
       61 pelplqrgpq gpanglalag clrdaapdaw gqrvilaehh grltrssdtg dlsiltylle
      121 sgsnrigald ftdaaddyqp rhtdasldel qkaaglldsg eplsptlaaa lvrgtsigga
      181 rpkalvtqag qhwvakfsst tdhypvvkse alalalarrv gvnvpagels rslgrdvlll
      241 qrfdrtpagg rrllvsaltm lgldemfgry atyvdladlv rsrftrpdpt lrelfsriaf
      301 nicigntddh arnhaafwdg qaltltpayd lcpqprsgse aaqamayspa gerasrlgql
      361 vsaahvyhld egsaqdivns qvegirmswn eaaeaahltq verdllwgrq ilnsfifs
//
LOCUS       WP_006592189             376 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Kineosphaera
            limosa].
ACCESSION   WP_006592189
VERSION     WP_006592189.1
KEYWORDS    RefSeq.
SOURCE      Kineosphaera limosa
  ORGANISM  Kineosphaera limosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermatophilaceae; Kineosphaera.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Kineosphaera limosa"
                     /db_xref="taxon:111564"
     Protein         1..376
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38220
     Region          27..370
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msvepaagrg artgraasap dvladvtfde rdvqvrldva ggevvallgr ngagkstllq
       61 aisglsvpde grvvvggqtf vdtaagifrp ahtrglgvlt qdpllfphls vaanvafgpr
      121 srgrgrraah tsalrwldal gvadlaarrp gqlsggqaqr vglaralave pavllldepl
      181 aaldiavaaq lrpllrqicr eqgrttlivt hdlldvlala driavieggr ivevgtttqv
      241 laaprsafaa rlagvnlvpg ladagpavrt adggrvvgvg dvpdgqhava vfapsavsvf
      301 pepptgsprn iwpavvtela pavagdgavh lrarvegvgl iaadvtpaaa aelrlepgaa
      361 vylavkaqev aihart
//
LOCUS       WP_006592778             311 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Kineosphaera limosa].
ACCESSION   WP_006592778
VERSION     WP_006592778.1
KEYWORDS    RefSeq.
SOURCE      Kineosphaera limosa
  ORGANISM  Kineosphaera limosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermatophilaceae; Kineosphaera.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Kineosphaera limosa"
                     /db_xref="taxon:111564"
     Protein         1..311
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32863
     Region          1..304
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mtsrapvlll dsaslyfraf fgvpdrrenp ddppnnavrg fldmiatlvt ahrpsglvac
       61 wdddwrpafr veaipsykth rlaenspvse espeeltpqv pvivaalaal giprvgaagy
      121 eaddvigtlt trfagegrsv dvvtgdrdlf qlvddaadvr vlytarggvr dpdlvdqafl
      181 rstydvasgd ayadfavlrg dpsdglpgvr gvgpksaaal lhahgdlagi raalaagdps
      241 ikgaqrtrll egsdyldaap rvvrvvrdid lgpvepglpt qvadpalmsr lavdyrltga
      301 ftrvvtalgi a
//
LOCUS       WP_006593407             341 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Kineosphaera limosa].
ACCESSION   WP_006593407
VERSION     WP_006593407.1
KEYWORDS    RefSeq.
SOURCE      Kineosphaera limosa
  ORGANISM  Kineosphaera limosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermatophilaceae; Kineosphaera.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 341)
  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 341)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Kineosphaera limosa"
                     /db_xref="taxon:111564"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35814
     Region          18..200
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          245..324
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 miraaalrgf aplvtelgge paeylqragl dpavlgddea lvpverfaaa lalagaeldc
       61 phlglllsqr qdlevlgpla vvlesaptmg ealhsaerfl fvhsstagvq llpdprgepg
      121 viaveltpad mplglelglg llhriagmft ggdyglrgvh lpgppvates vyaqvfgapv
      181 rfrtgrgllr vpatlpeqrl rtgdellhrm avqyletnaa thaattsgqv trvlagslss
      241 nvpligtvag llglhprtlq rrlaaegttf aqvldevrrd rayylivstd lpfrqisaqv
      301 glsdpaaltr acrrwfaapp ralrqaasga gsptapksap k
//
LOCUS       WP_006595797             103 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Streptococcus australis].
ACCESSION   WP_006595797
VERSION     WP_006595797.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus australis
  ORGANISM  Streptococcus australis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Streptococcus australis"
                     /db_xref="taxon:113107"
     Protein         1..103
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11480
     Region          1..96
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(5..6,24..25,33,36,38..39,41,44..45,47,55,60)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(24,55..56,58,79)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mndlfeekvl kvvaqvplgr vatygqiaql igyprharqv gkvlatstkd vaypchrvvt
       61 stgrlapdwe eqgtllwaeg verkkngcvd lkkykwkaee tql
//
LOCUS       WP_006596101             292 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Streptococcus
            australis].
ACCESSION   WP_006596101
VERSION     WP_006596101.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus australis
  ORGANISM  Streptococcus australis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 292)
  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   2  (residues 1 to 292)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptococcus australis"
                     /db_xref="taxon:113107"
     Protein         1..292
                     /product="aminoglycoside 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=34446
     Region          8..226
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mnfsskiain kgwsddkkyc vtdqnqqkyf lrvsdkekld skkfefdmme kvaslgipmc
       61 kpisielcdd evhslhewid gkdaretilt vskeqqytyg veagrilrki hslpvtevre
      121 dwesffnrki ddkikkykec pvqyengqif ieflnanrew lkdrpqvfqh gdyhignfmi
      181 gedrkiyvid fdrfdlgdpw eefnrivwsa qvspsfasgm idgyfdhkvp dlfwkllaiy
      241 ilnnlvgalp waipygaeei svmqhqarei lewyddlnqi ipswylnkkk te
//
LOCUS       WP_006597138             242 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Streptococcus australis].
ACCESSION   WP_006597138
VERSION     WP_006597138.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus australis
  ORGANISM  Streptococcus australis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
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
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptococcus australis"
                     /db_xref="taxon:113107"
     Protein         1..242
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=26781
     Region          1..>237
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mieykhvalr ytdkdilkdv nlciedgefm vlvgpsgsgk ttmlkminrl leptdgniym
       61 drkrikdyde relrlstgyv lqaialfpnl tvadnialip emkgwtksqi askteelldk
      121 vglpaaeyan rkpselsgge qqrigivrai iaepkillmd epfsaldais rkqlqaltkd
      181 lhkefgmtti fvthdtdeal klgdriavlq egeivqvads dtilaqpand fvadlfggah
      241 hv
//
LOCUS       WP_006597215             397 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Streptococcus australis].
ACCESSION   WP_006597215
VERSION     WP_006597215.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus australis
  ORGANISM  Streptococcus australis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Streptococcus australis"
                     /db_xref="taxon:113107"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43775
     Region          3..395
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msdkilaina gssslkfqll empseaviak gifdrigfkd gkvkyqtkrn qvqknvcips
       61 hefavqvllg tlvesgeihs ieeivgvghr vahggesfkg svlvdeknee iisdlgdlap
      121 shnpislsvi ksfkthfpsi knvavfdtsf hqtmepvhyl yplpyslyek fhvrkygfhg
      181 ishayiaetv ekifqqeeha kenvkiisch lgngasicai keqqsvntsm gftpidglmm
      241 gsrcgsidpm iipylverqk mpihevkkll neasgllgis emsndmrdli qavtkgnqka
      301 ilaiemfvnr vahtiasyiv dldgldalvf tggigenaal irslvvdklq vfgmsvnkel
      361 nengslyiqd anskckilvv qtneelmiar etyrlsl
//
LOCUS       WP_006597881             398 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Pseudoramibacter alactolyticus].
ACCESSION   WP_006597881
VERSION     WP_006597881.1
KEYWORDS    RefSeq.
SOURCE      Pseudoramibacter alactolyticus
  ORGANISM  Pseudoramibacter alactolyticus
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Eubacteriaceae; Pseudoramibacter.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Pseudoramibacter alactolyticus"
                     /db_xref="taxon:113287"
     Protein         1..398
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43474
     Region          1..396
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkvlvinags sslkyqlldm dterllakgl aerigiegsv vthepvgkdk vkferpmeth
       61 kealdiimra lvneqygvik slneidavgh rtvhgaesfa ssvvindevi ekmeecsvla
      121 plhnpanlig iracqevlpn vpmvgvfdta fhqtmpkeay iyplpyelye kyrirkygfh
      181 gtshryvslr aaellnqdln qlklischlg ngasiaairy gksidtsmgl tplaglamgt
      241 rcgdidpeim iflrqhgytt eeldhimnke sgilgisgis sdfrdveqaa dtgnkraqla
      301 ldvfhyrvrt tigayvaamd gvdgiiftag lgensastrs aicsgltylg iklnaeknsk
      361 rgeemvista dsatnvmvip tneelmiard tvelvqgk
//
LOCUS       WP_006598337             172 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein, partial
            [Pseudoramibacter alactolyticus].
ACCESSION   WP_006598337
VERSION     WP_006598337.1
KEYWORDS    RefSeq.
SOURCE      Pseudoramibacter alactolyticus
  ORGANISM  Pseudoramibacter alactolyticus
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Eubacteriaceae; Pseudoramibacter.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Pseudoramibacter alactolyticus"
                     /db_xref="taxon:113287"
     Protein         <1..172
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          92..171
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 gehismdgep sliirsrkei dhilneiyti danirqpycl ikvmelllfl sslerkdtqr
       61 pcsfsrpile atqdcygylv qhpfewihvk elagmfaise sglkicfqyi sgkaigsfmr
      121 enrikeaael lirkpdlsig eisetagyen qskftkafkt iigktpsefr kd
//
LOCUS       WP_006602609             339 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Streptomyces auratus].
ACCESSION   WP_006602609
VERSION     WP_006602609.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces auratus
  ORGANISM  Streptomyces auratus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 339)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Streptomyces auratus"
                     /db_xref="taxon:114687"
     Protein         1..339
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36897
     Region          45..334
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mttvsltdva sylpgepvpa kfyteypgae dklrdhpmfr vpplrhhvaa detnadmver
       61 avqplierhg rdeirgvdvl lvhsqlpdlp fvgagtevar rlglnpewlv dvansgcasf
      121 vymlklarqi lttteaksal icnaqstagq wftqsqvrrl aqaavpgdgc gvgyvttssd
      181 apildvatrh iaeyagdmtv vlddgrkywe pgesqlrigf teasvakvla rgnrlvpevv
      241 tnlcrrlgva tadidalitn qpnrtflrnw realhlpaer hlhtfdeygn lfgaaipitl
      301 draissrqve dgdlvvlggf ahagdfagav avrwhsgrt
//
LOCUS       WP_006605188             390 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Streptomyces auratus].
ACCESSION   WP_006605188
VERSION     WP_006605188.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces auratus
  ORGANISM  Streptomyces auratus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   3  (residues 1 to 390)
  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   4  (residues 1 to 390)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Streptomyces auratus"
                     /db_xref="taxon:114687"
     Protein         1..390
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=40985
     Region          1..297
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mikfdavskr ypngttavdg lsldlpeggv tvlvgssgcg ktttlrmvnr mveptsgtis
       61 vggrdiletd aaelrrgigy viqqsglfph rtildniatv plllgwgrrk araraaelle
      121 lvglpadagk ryphqlsggq qqrvgvaral aadppvllmd epfgavdpvv rtqlqnellr
      181 lqeelrktvv fvthdideav rlgdriavfr tggrlvqcae paellarpad dfvagflgae
      241 rglkllsltd ladvphapgg eiradepvgg iprdgdrwrl vtsprseplg wldtdalpag
      301 gtageaplep vrplrdsdsl lsalneavss paaavarvta dgvltgltsr daiheragrs
      361 haeagraaag qrtpedaapg taeaaterpa
//
LOCUS       WP_006605718             273 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces auratus].
ACCESSION   WP_006605718
VERSION     WP_006605718.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces auratus
  ORGANISM  Streptomyces auratus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 273)
  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 273)
  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 273)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Streptomyces auratus"
                     /db_xref="taxon:114687"
     Protein         1..273
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30047
     Region          1..64
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          98..264
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 manasrqaaw efwgtelkrr redagltqea lggmvfvsgg yigqfeqair kpqldvairi
       61 dgilqtdgff ermwrklina sgftdyfaaa aqlealatki cefesvlvpg llqtaaymra
      121 vmladnpfvs ndeldgwvaa rleraktlkg panptywaii hehalrtpvg gpacmaeqle
      181 hvatlarcrr vlvqvvpytq gahagmsksm rlmefedapp tlytegmywg qlldepttvk
      241 raqatydlir aaalspeasl sliesaaesy rsp
//
LOCUS       WP_006605885             214 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Streptomyces auratus].
ACCESSION   WP_006605885
VERSION     WP_006605885.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces auratus
  ORGANISM  Streptomyces auratus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Streptomyces auratus"
                     /db_xref="taxon:114687"
     Protein         1..214
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=23189
     Region          <117..210
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 makvyarrvs iaagaaaalv gtlvfsgqsa qaappsppda atartyladi keqpegsldg
       61 ysrdkfphwi dqgkncntre vvlkrdgtdv qqdsscaats gkwvspydga twtkaadldi
      121 dhvvplaesw rsgaaqwtta rrqelandlt hsqliavtdn vnqekgdkdp akwlppkasy
      181 hceyarmwvw vkheygmtad saekaalkki ldgc
//
LOCUS       WP_006606029             207 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Streptomyces
            auratus].
ACCESSION   WP_006606029
VERSION     WP_006606029.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces auratus
  ORGANISM  Streptomyces auratus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 207)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 207)
  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 207)
  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 207)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Streptomyces auratus"
                     /db_xref="taxon:114687"
     Protein         1..207
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21664
     Region          116..202
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(135,154..155,173,176,184..185,195,200)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mtnvrtltap sptapaphah rhrlravapd ealpspatap gggashpgap svaellnsaa
       61 twlpapqhsl palpgqppmv gylvlvpaeq apapppgaap gptaapptap tgdeivridp
      121 errtaqvqgr pldltylefe llahlvahph rvhtrdqlvt tvwgyghvgd grtvdvhvar
      181 lrrklgaahr ssivtvrrvg ykyvpgi
//
LOCUS       WP_006606016             281 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces auratus].
ACCESSION   WP_006606016
VERSION     WP_006606016.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces auratus
  ORGANISM  Streptomyces auratus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 281)
  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 281)
  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 18542080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces auratus"
                     /db_xref="taxon:114687"
     Protein         1..281
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31591
     Region          22..80
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
     Region          98..264
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mevqnmtggt gsgepestds lktfgavvka freragltqe glallvrfsp qtvasieqgr
       61 rlpppdfier aeevldafgv lraaavhlar kpgiaawfrq waaleerais lytyecrlip
      121 gllqteaysr alfteqlppl ddeqieaqwa araerqrllr erpntaysfi leehlflrrt
      181 ggaevtreli ehvletvear nveiqimple rkthagldgp mqlletpenq wfaynegqrg
      241 glfisdpkev svlqmryarm rsqalsldds lsllkqmrga l
//
LOCUS       WP_006608562             299 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Mycoplasmopsis columbina].
ACCESSION   WP_006608562
VERSION     WP_006608562.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis columbina (Mycoplasma columbinum)
  ORGANISM  Mycoplasmopsis columbina
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Mycoplasmopsis columbina"
                     /db_xref="taxon:114881"
     Protein         1..299
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34113
     Region          6..286
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mktnnakken fllidgnllm fqsfyasynp nninylmksp kgiyvngvhv flislaklie
       61 afdpkylfia fdangktkrh nefegyksgr nkapeiifeq falikdiltg lnikwfeqig
      121 deaddliatl aktketnnii fskdkdllql vnentiiaqn akneygyriv nldnfetifg
      181 ilpsqipdfk glagdasdnl tgvngigdkg avkllnefgs leniyqnieq ikgkqkekll
      241 ndknnaflck klallnkdvd mdtniknyeh flytnnekgk ellkehkltk cyeyifnry
//
LOCUS       WP_006606237             218 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Streptomyces].
ACCESSION   WP_006606237
VERSION     WP_006606237.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 218)
  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 218)
  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   3  (residues 1 to 218)
  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   4  (residues 1 to 218)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 218)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 218)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..218
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=24319
     Region          24..212
                     /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"
ORIGIN      
        1 msaaepeqpv adddqshvpp lttrvviaed ealirldlke mleeegytvv geagdgqtav
       61 elarehrpdl vildvkmpvl dgisaaevic eesiapvlml tafsqrelve rardagamay
      121 lvkpfsktdv vpaiemavsr ftelrtleke iedltqrlet rklvdraksi lqtqygltep
      181 aafrwiqkts mdrrlsmqqv aeaviedaee kkqqkkde
//
LOCUS       WP_006609141             640 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Bradyrhizobium sp. ORS 285].
ACCESSION   WP_006609141
VERSION     WP_006609141.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. ORS 285
  ORGANISM  Bradyrhizobium sp. ORS 285
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 640)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 640)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 640)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 640)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 640)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 640)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Bradyrhizobium sp. ORS 285"
                     /db_xref="taxon:115808"
     Protein         1..640
                     /product="potassium transporter Kup"
                     /function="16.1 : Circulate"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68986
     Region          14..640
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mtadiaatpa etpatnghgd ahstasftal tlgsigvvyg digtsplyal reavmaasss
       61 gepaphavmg vislilwali vvvtlkyvvi llradnhgeg gtlalmalaq rgvtrgasii
      121 vllgiisgal fygdavitpa lsvlsaiegv klvtaafdpy vvpmtiiilv mlfavqvrgt
      181 akvaaffgpi mllwfvvigv aalppilrhp evlwainpfn avtfmlhhgi igfitlgavf
      241 lavtgaealy adlghfgkrp iqtawlfivl pslalnylgq galviadaka ienpfflmfp
      301 dwalipmval atvatviasq avitgayslt rqaiqlgllp rfeirhtsea hsgqiyipri
      361 tklllvsvvl lvllfksssa lasaygisvt gtmvvtammg fvviwkvwrw spfaaaalia
      421 pflfldltfl sanllkvleg gwvplalggf vmtlmytwrr gsrllfeksr klefpladlv
      481 emlekrppqr vagtavflts dplsaptalm hslkhykvlh eknviltiet aptpridpse
      541 rvrleqispt fskvtlrfgf mespnvpral aiarklgwqf dimstsffls rralkpaahs
      601 gmprwqdhlf itmsrsanda tdyfqipsgr vvevgtqvti
//
LOCUS       WP_006609969             362 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Bradyrhizobium sp. ORS
            285].
ACCESSION   WP_006609969
VERSION     WP_006609969.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. ORS 285
  ORGANISM  Bradyrhizobium sp. ORS 285
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 362)
  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 362)
  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 362)
  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 362)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Bradyrhizobium sp. ORS 285"
                     /db_xref="taxon:115808"
     Protein         1..362
                     /product="TRAP transporter substrate-binding protein"
                     /function="16.1 : Circulate"
                     /GO_component="GO:0005886 - plasma 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=39572
     Region          1..355
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkrrdfikvt glgaagaaai aapaiaqsmp elkwrmptsw pksldtlygg aemmakmvae
       61 atdnkfqiqp faageivpgl qvvdavqngt veightasyy yfgkdptftf gssvpfgpnm
      121 rinqawymlg ggreilnefy akynvvslla gntgcqmggw frkeltsvnd lkglkfrvgg
      181 fagrvlqklg avpqqiaggd iypalekgti daaewvgpyd deklgfvkva phyyypgwwe
      241 ggpmllafvn qdrwnalpkh yqkileqagh fannwmmaky dqsnpaalrr llaagaklhg
      301 fspeimqaci kaarelhgev aatnpdfkkt lesltafagn gyswfqvaei gydafmarnp
      361 la
//
LOCUS       WP_006611517             743 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Bradyrhizobium sp. ORS 285].
ACCESSION   WP_006611517
VERSION     WP_006611517.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. ORS 285
  ORGANISM  Bradyrhizobium sp. ORS 285
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 743)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Bradyrhizobium sp. ORS 285"
                     /db_xref="taxon:115808"
     Protein         1..743
                     /product="CHASE2 domain-containing protein"
                     /EC_number="4.6.1.-"
                     /function="16.12 : Sense"
                     /function="16.3 : Control"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016849 - phosphorus-oxygen lyase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=82558
     Region          34..665
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mkrlravprw farrfgyarv iclllliafa alrvadpalv qelrlrtfdn fqalsprvkt
       61 irpvtivdid eksvadpklg qwpwprtria eivdrltelg alviafdvvf aepdrlnpal
      121 aaetfpnlde atreklkalp sndqvladav rrsrvvlget asrdvraepd ktlpetgfae
      181 lgdpvpfmep fpgllrnvpl iehaaagrgl ftieperdgi vrrvpmvmra qdvkmlalsf
      241 etlrvvagvd tvrvkadtgg itsigfgplq iptdgnakiw vhyanhdpsi yvsaidvleg
      301 rvppekiark liligpsaig lsdikttpvy aampgvevha qvlesvltgs iltrpywgiv
      361 veffgavllg llvivfaprl gavtlvlvga vfasallgvs wyfykqhril idftypmlst
      421 tsvyltlifa sfireqqqrr eirgwfaqym spvlveqlaq speklvlgge eremtimfsd
      481 vrgftsises ykhdpqglta lmnrfltplt daiiarkgyv dkymgdaima fwnaplddre
      541 hhlnactaal dmldridevn rereqeaahg ghvyiplnvg iglntgigvv gnmgselkkn
      601 ysvlgdsvnl asrlegqtke ygfpiivgaa tamavkdrla ileldfimvk gktepeviya
      661 itgredvmys erfqllrnlt iemlaayrsr dwdealaaia rgrkkdeake laklfdlyee
      721 rirayqqnpp pdnwngahal tsk
//
LOCUS       WP_006611952             168 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Bradyrhizobium sp. ORS 285].
ACCESSION   WP_006611952
VERSION     WP_006611952.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. ORS 285
  ORGANISM  Bradyrhizobium sp. ORS 285
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Bradyrhizobium sp. ORS 285"
                     /db_xref="taxon:115808"
     Protein         1..168
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=17592
     Region          67..140
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mrtpnhrcrl gaasalaava lltlqmnaaa aqqaspvpvt ketpapakep apppsvtilg
       61 ardahgvlgr dvrsstgedm ghivdvivdl tgtvraavid fggflgvgsr kivvdwtald
      121 fkhiteksdq vtldltkeqv kaapeykedk pvvvlgaagk lspwdfdh
//
LOCUS       WP_006611886             239 aa            linear   BCT 20-JAN-2025
DEFINITION  prolipoprotein diacylglyceryl transferase [Bradyrhizobium sp. ORS
            285].
ACCESSION   WP_006611886
VERSION     WP_006611886.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. ORS 285
  ORGANISM  Bradyrhizobium sp. ORS 285
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002130
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Bradyrhizobium sp. ORS 285"
                     /db_xref="taxon:115808"
     Protein         1..239
                     /product="prolipoprotein diacylglyceryl transferase"
                     /EC_number="2.5.1.145"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008961 -
                     phosphatidylglycerol-prolipoprotein diacylglyceryl
                     transferase activity [Evidence IEA]"
                     /GO_process="GO:0009249 - protein lipoylation [Evidence
                     IEA]"
                     /GO_process="GO:0042158 - lipoprotein biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=25424
     Region          <60..227
                     /region_name="Lgt"
                     /note="Prolipoprotein diacylglyceryltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0682"
                     /db_xref="CDD:440446"
ORIGIN      
        1 mdgaalhaif dvaawlsaaa agwwlargag vrfpkqstew pyvaalvfga glgaylfgtl
       61 nlwlsgmtgl arsvegalag givavelykw rhgialrtga rfalplavgi avgrigcyla
      121 glddftygtp ttlpwghdfg dgvlrhpvql yeslamaafa alyivavkrr neaiitngfy
      181 lallvyglqr fvweffkpyg pvigpltlfh llslaiaaya avmlatapqa kvlheraaa
//
LOCUS       WP_006613142             697 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Bradyrhizobium sp. ORS 285].
ACCESSION   WP_006613142
VERSION     WP_006613142.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. ORS 285
  ORGANISM  Bradyrhizobium sp. ORS 285
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 697)
  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 697)
  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 697)
  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 697)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Bradyrhizobium sp. ORS 285"
                     /db_xref="taxon:115808"
     Protein         1..697
                     /product="TRAP transporter permease"
                     /function="16.1 : Circulate"
                     /GO_component="GO:0005886 - plasma 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=74151
     Region          22..692
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 metpvkvefd nfehgfpegf gpgrwgylay giglafalfq lyvaafnylp sqvvrgvhvg
       61 flllltfgli gnftaktdag riagwaigai gflcglyqwi fyadliardg dptradlvvg
      121 tllavlifeg trrlmglalp lmcgacllyw ffgqylpspl nhrgydfdqv ithlsfgteg
      181 fygvpiyvsa tyiflfilfg sflehagmiq lftdvslglf grtrggpakv avfasgmmgt
      241 isgsgvanvv tvgqftiplm irfgyrrafa agveatasmg gqimppvmga vafimaetlg
      301 vdysvivkaa vipailyfts afwmvhleag khgltgmkps eipsawkalv arwylvlpla
      361 alvymlfegf tplyagsmgl altvalilgt sitmgfsnqv lryvfwigla lvvgalsrng
      421 lqivpvasvv valvvitafv rggmgtlhac rdslaesaks altvgmacai vgviigmmtq
      481 tgvgsifgsw viglgktslf aalimtmlls illgtgipti ptyiitaala apalaklgvp
      541 liashmfafy ygimadlspp valaalaaap iakenpdkig weamrialag yvipflfvys
      601 palmlqagdp meaqigfyga vayafvkali siglfgmvai gflytrmtli erllafvasv
      661 cllgefpysd vlgfalavvi vawqwwqrpp ttvaasa
//
LOCUS       WP_006613323             725 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Bradyrhizobium sp. ORS
            285].
ACCESSION   WP_006613323
VERSION     WP_006613323.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. ORS 285
  ORGANISM  Bradyrhizobium sp. ORS 285
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 725)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..725
                     /organism="Bradyrhizobium sp. ORS 285"
                     /db_xref="taxon:115808"
     Protein         1..725
                     /product="TonB-dependent receptor family protein"
                     /function="16.1 : Circulate"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=78870
     Region          87..725
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 msrsvtalca atclvtlssp cfsqarepsn lptvtvdpar psasrparpa nndqparrar
       61 aprsaaapqt ataapagpap srtapntqta tqriqqiaga vavvpdtafk ngsaqtikdv
      121 ldyvpgvfaq pkwgddtrls irgsglsrnf hlrgtqltld gipintadgy gdfqeidpta
      181 yryvevykga nalrygansl ggavnfvtpt grdasafesr ldggafgflr gqastggvtg
      241 aadyfvtgsa srvdgyrdhs wgqsergsan lgyqvspdfe trfylnantv rqripgevsk
      301 tsalnspeta aannvlndwq rnidtvrvan kstlhldnid iefgvfavdr hlmhpifqwl
      361 dyryhdyggf vravddreig dhrnrftvgl niqngtidad qfvnigvnkg aqtfaavqrp
      421 enytlyaena wyvtpavsli agaqylhavr eqrvdlttdp tkksgssvfd lfspklgllw
      481 dvdpgwqvfa nisrsgeaps fgegngavip fydikaqtat tyeigtrgrr pdvtwdfaly
      541 hadirnelqc fyssfgncnv tnadktmhqg veaglglsll kglavksdap drvwlnlayt
      601 yndfrydnda twgnnrlpga pphflraell ykhpagfavg pnvewvpqsy fvdsantlst
      661 esyllwglka tyddgknfsa ylegrnlank ayiattsiid ratptstlfn pgngrgvyag
      721 lrykl
//
LOCUS       WP_006614201             286 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Bradyrhizobium sp. ORS
            285].
ACCESSION   WP_006614201
VERSION     WP_006614201.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. ORS 285
  ORGANISM  Bradyrhizobium sp. ORS 285
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Bradyrhizobium sp. ORS 285"
                     /db_xref="taxon:115808"
     Protein         1..286
                     /product="formate/nitrite transporter family protein"
                     /function="16.1 : Circulate"
                     /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=30659
     Region          31..284
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msskataptf spaddvegvs deqrqqikaq srpnaalihe tiraegesel errwwaills
       61 glaaglsisl slivqgefha fvsdeaarrl faplgytagf lvvvlgrqql ftentltpil
      121 pllhhrdlkt lgqvarlwsl vltanvagtw aaaaalaytd vfeprvvdaf teisrhtveg
      181 pfsttfarav fagwlialma wllpavraar ahivvvmtyl valgqfahvv agsvecaflv
      241 fkgdvslady agafflptll gnivggttlv ailnygqvaa eldqdd
//
LOCUS       WP_006615221              73 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Bradyrhizobium
            sp. ORS 285].
ACCESSION   WP_006615221
VERSION     WP_006615221.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. ORS 285
  ORGANISM  Bradyrhizobium sp. ORS 285
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 73)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 73)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 73)
  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 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   5  (residues 1 to 73)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..73
                     /organism="Bradyrhizobium sp. ORS 285"
                     /db_xref="taxon:115808"
     Protein         1..73
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=8217
     Region          2..72
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(4,23..24,46,49,57..58,64,69)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mkltrneqai fdllskrspe vvsredivav crssranasq fgfsniadvh iknlrrkidr
       61 eitsvrgvgy rle
//
LOCUS       WP_006623489             541 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Limnospira].
ACCESSION   WP_006623489
VERSION     WP_006623489.1
KEYWORDS    RefSeq.
SOURCE      Limnospira
  ORGANISM  Limnospira
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Sirenicapillariaceae.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Limnospira"
                     /db_xref="taxon:2596745"
     Protein         1..541
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55729
     Region          217..451
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 msafgfgtma qdinisplsd ltdiidqesi reeeedpeig lldnsdndtl pvdngdngdn
       61 gdngdngdnd tlpvdngdng dngdngdngd ngdngdngee eeeeipfipe pappipqptp
      121 apfeptpppv aqptppppvp iptppptptp tpaptptptp tptptptptp tptptpsqpt
      181 ptptpsqptp tptpseptpt pseptpsept ptptlpsadh vfeggdgnsl ilgtegndll
      241 yggggnntly gftgndtlig gggndllygg qnndfldggn gnntlyggln ddtllggigr
      301 dllfgeagnd fldggdgndt lyggedndtl lggngndllf gnqgndsldg gpgddtlygg
      361 kgddtllgsq gddillgnqg ndilyggdgd dclyggqgdd tlyggrgrdy lsgdrgndfl
      421 vgvdtsadfp glttidtlvg gegfdtfvlg nekgpfydng nddingvady alilnfnsat
      481 dvillsnddy lfstdipqpl pqgtaifrrt pgeneliail egvvdlqfdg tnlddgpirf
      541 i
//
LOCUS       WP_006623707             127 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [Limnospira].
ACCESSION   WP_006623707
VERSION     WP_006623707.1
KEYWORDS    RefSeq.
SOURCE      Limnospira
  ORGANISM  Limnospira
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Sirenicapillariaceae.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Limnospira"
                     /db_xref="taxon:2596745"
     Protein         1..127
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14496
     Region          19..118
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 miflpmmdlg eldvnvdmiq taialpmeei aefcqkwkvt efalfgsilr ddfhgnsdvd
       61 vmvqfhpeah ptlfdlaeme eelkqlferd vdlitrkgie nsrnylrrqa ilssarviye
      121 tgcsila
//
LOCUS       WP_006623734             282 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Limnospira].
ACCESSION   WP_006623734
VERSION     WP_006623734.1
KEYWORDS    RefSeq.
SOURCE      Limnospira
  ORGANISM  Limnospira
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Sirenicapillariaceae.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 282)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Limnospira"
                     /db_xref="taxon:2596745"
     Protein         1..282
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=31813
     Region          36..278
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mrrsatlkng lsgqskvicl pggdldgcgd rihqinrlkk trsaqrfgly tqeaislnsg
       61 eskryceili rfidepeqvv paswlvpiit qgyglaekid rwvietvldl lsetspenre
      121 kyrfainiss rtlydyrqwr klereilkrd ltpdlfcwei aestilanpq kaadaianlq
      181 iqgyyvtvdq vggryssldy lnyvtvdylk iaddlvkdia qdlgdrsivq iiqlvaqsla
      241 ietiangvet spafetlrdl eidyaqgyyl tqphplaakf lg
//
LOCUS       WP_006624758              96 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [Limnospira].
ACCESSION   WP_006624758
VERSION     WP_006624758.1
KEYWORDS    RefSeq.
SOURCE      Limnospira
  ORGANISM  Limnospira
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Sirenicapillariaceae.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Limnospira"
                     /db_xref="taxon:2596745"
     Protein         1..96
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10577
     Region          1..96
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mnlperlqek reeilalaaq ygasnirvfg svargeadad sdvdflvemq pgrslldmgg
       61 llmelqellg crvdiitekg lrprirqqvl aeairl
//
LOCUS       WP_006625238             124 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [Limnospira].
ACCESSION   WP_006625238
VERSION     WP_006625238.1
KEYWORDS    RefSeq.
SOURCE      Limnospira
  ORGANISM  Limnospira
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Sirenicapillariaceae.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Limnospira"
                     /db_xref="taxon:2596745"
     Protein         1..124
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14355
     Region          31..120
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mmnqefvnsd rlaywkqrmt qqaaqnkklv nqarsdvdti vemlvsqfgv rrvilfgslv
       61 rgrfretsdi dlaveglrkk dyflavaean dltrrwvdlk pfedlephfr drvlqtgecv
      121 yeag
//
LOCUS       WP_006625456             107 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Limnospira].
ACCESSION   WP_006625456
VERSION     WP_006625456.1
KEYWORDS    RefSeq.
SOURCE      Limnospira
  ORGANISM  Limnospira
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Sirenicapillariaceae.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Limnospira"
                     /db_xref="taxon:2596745"
     Protein         1..107
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11023
     Region          <28..>95
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 msqfietpqi eelpdgslif rgatepqnff aggsgddiit ggdsddtlyg gpgndtidgr
       61 ggndlilgee ghdsliggsg ddtiyggegn dtidgqersg imddyyv
//
LOCUS       WP_006627221             668 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CHAP domain-containing protein [Bacillota].
ACCESSION   WP_006627221
VERSION     WP_006627221.1
KEYWORDS    RefSeq.
SOURCE      Bacillota (firmicutes)
  ORGANISM  Bacillota
            Bacteria; Bacillati.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 668)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Bacillota"
                     /db_xref="taxon:1239"
     Protein         1..668
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76013
     Region          562..634
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 mgkklkkdfk erhkasiere ilhsetgitp eesklkhndd yrgkivhdke rfqdkvhkkt
       61 skindddnpl gkdldndgii drydndfrds dyfestydve dnlhhkaent nsfsksqkaq
      121 krnykrknyt eslytrkkdd vlkenkpedk ktgkdtaskk vhssiykeqk kklkkdmvkv
      181 salsglakgs etvrdylshg sdenkgveag ektadasskl ihgiknysnr krakkgcdlt
      241 kkdykirkrk sklefrdake nlkktdeykr asaykriqkk nqvkaairre nksrirdrik
      301 egligtlkss kefivrkakg lmiifiglii lgtffinfag tgmtgftnst ssvlttsyls
      361 kpnvlseinq nfsamekelq nevdnvksnh pgydeyilnn teyighnvhe llsyitsrcg
      421 evkeafevns ilkelfesmy dleyreevei ryrtvtktyt dkngnehtes heepykykkl
      481 ivtlhkkemd siirkvfanh pdnlkhyeal fvaqgnmrea fgnsdlsasn ggvgggkeye
      541 asdevqkkiv raayitpspg agwcamwvsq vyqnaglgyi ggnacdmyrn ytftsdrskl
      601 kvgmlvaves sssggsaglt yghvgiyigd gkvidnigri rvttlddwia tfckhhpvgf
      661 gfppnvrr
//
LOCUS       WP_006627489             569 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Bulleidia extructa].
ACCESSION   WP_006627489
VERSION     WP_006627489.1
KEYWORDS    RefSeq.
SOURCE      Bulleidia extructa
  ORGANISM  Bulleidia extructa
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Erysipelotrichaceae; Bulleidia.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 569)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Bulleidia extructa"
                     /db_xref="taxon:118748"
     Protein         1..569
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=64225
     Region          1..551
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mllidrllme ygkrswlwiv givglrlfil vgitqfslll gkvlatmtvs tigfviglcl
       61 sislfillvs lvqgeleyql qartrtmmrn emvkktleld sgqleeigpt sssiaaldav
      121 emalpyvsvy lpslvysfva plylffevck yqigiayill avswlllpih nlfrknierl
      181 rkkywlslem mtrlyldglr gmttlkiynq skahvkkleq ysqelnrdih afmkinfssf
      241 lvtewimygt lflvvlwgiq sqlslannls llllgyayfa sirqlmsath daltaisast
      301 kmqsilqkkt arvyefipan qeegiqfenv sfsyegrnev iqdlnldikk gevlalvgls
      361 gcgkstiasl alrfidpkkg hirldgqdyr slseeilrkk lvmvpqrvhi fsgtirsnlm
      421 lgketasdee lfavlkkvrl edfvktlphq ldeevgengs rlsggqkqkl gmarallsda
      481 pymvldeats avdpkneeei wriihtlfhe ktlllishrl stiqqadriv vmeegkivee
      541 gthdqlmana glyaqmvdqq ealeggfgd
//
LOCUS       WP_006631891             260 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Microcoleus vaginatus].
ACCESSION   WP_006631891
VERSION     WP_006631891.1
KEYWORDS    RefSeq.
SOURCE      Microcoleus vaginatus
  ORGANISM  Microcoleus vaginatus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae;
            Microcoleus.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Microcoleus vaginatus"
                     /db_xref="taxon:119532"
     Protein         1..260
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26922
     Region          4..213
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 maltvnnlig dvtgfpvfag ggprllgfat pdeinvgngn lssfpwgvwg ldgndtiggs
       61 sdsnerllgn ngsdiigggg gndiiyggkd ddrldgndgn dvvrgdagnd lifggfgndl
      121 lrggqgdddl egnegndfla gdrgvdvltg glgadifvlr sndeafging advitdfnfd
      181 egdrigltdg lteldlffed dnliaydndg iindmvieni ingqivgivl ntnnfeltga
      241 feqaspfala vngsqfqfla
//
LOCUS       WP_006633026              49 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Microcoleus vaginatus].
ACCESSION   WP_006633026
VERSION     WP_006633026.1
KEYWORDS    RefSeq.
SOURCE      Microcoleus vaginatus
  ORGANISM  Microcoleus vaginatus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae;
            Microcoleus.
REFERENCE   1  (residues 1 to 49)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 49)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 49)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 49)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..49
                     /organism="Microcoleus vaginatus"
                     /db_xref="taxon:119532"
     Protein         1..49
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=5519
     Region          7..>49
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 msnlpititv klftpyqeae glselklefp ketpvsqvle rlsanrqrf
//
LOCUS       WP_006632838             739 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Microcoleus
            vaginatus].
ACCESSION   WP_006632838
VERSION     WP_006632838.1
KEYWORDS    RefSeq.
SOURCE      Microcoleus vaginatus
  ORGANISM  Microcoleus vaginatus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae;
            Microcoleus.
REFERENCE   1  (residues 1 to 739)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 739)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 739)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Microcoleus vaginatus"
                     /db_xref="taxon:119532"
     Protein         1..739
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=81228
     Region          1..702
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 metiktlcpy cgvgcglevv pdkkqswkvr gdrnhpssqg mvcikgatva esirsdrlly
       61 pmmrdtldqp frraswdeal daivnriqti rstsgpdalc vygsgqfvte dyyvaqklmk
      121 gclgtnnfda nsrlcmssav sgyvqsfgsd gppccyddle ltdcafiigs ntaechpivf
      181 nrlakyhkkh phvkmivvdp rrtptaeaad lhlaikpgtd idllngiayl llhrqaidsn
      241 fiqectanfs afaevissyt pefvasrcgi tvseletaan yweqsqrvls lwsmginqss
      301 egtakvrsli nlhlmtgqig kpgcgpfslt gqpnamggre agglshllpg yrfvknaehr
      361 tqveefwgia pgsispnpgr tawdmitgle tgevellwia atnpvvsmpd lertkaallr
      421 spftiyqeay yptetsayah illpatqwse ktgvmtnser rvtfcpgfdt psgearddws
      481 ifaevgrrlg faqhfafdsv gdvykeyvql tqgqpcditg lsheylrteg pqqwpcpenl
      541 pphpaneakr lytdrrfhtp dararfsayh srglaeppdp nypfvlttgr vyghwhtmtr
      601 tgrtekinql hpdpfleihp rdaaklqike gdllevrsrr gkaqfpakvt kaiapgtlfv
      661 pmhwgclwae gaeanamtha ascpdskqpe lkacavqlsl vgaetaaevv aevaaevaae
      721 vaaevgefnw akstlavts
//
LOCUS       WP_006634473             649 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Microcoleus vaginatus].
ACCESSION   WP_006634473
VERSION     WP_006634473.1
KEYWORDS    RefSeq.
SOURCE      Microcoleus vaginatus
  ORGANISM  Microcoleus vaginatus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae;
            Microcoleus.
REFERENCE   1  (residues 1 to 649)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 649)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Microcoleus vaginatus"
                     /db_xref="taxon:119532"
     Protein         1..649
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=71878
     Region          33..638
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mpkffnriyh klgegrwknl tyffpfpdlq plaiiwivvt gtllgvrhlg glqplelnay
       61 dlmvqlrpdp gpdprllive vtdpdintie kwplsdrvla kaiaeiarle ptaigldiir
      121 dipyepgnae latqlknpkv fpitfigtsk ydrvqpppni pdqrvgfndl yldpdgilrr
      181 nvisigdgkk tfysfpsrla fayfdsrkie skgtknnefl vnkivfsklr snsggyqnip
      241 aqgyqillny rsakkiaetv titqvlqgkv dpklvkgkiv ligvtaptvk difstpysat
      301 kngniptpgv lihatatshi lsavldgkgl fwywdewhei lwiavwsavg gclawrleks
      361 lnliaiaiaa cgslfgftff lfmqqgwipl maptlgllit agvavtykye qsrqqqgivm
      421 kllgqqtspa ianalwkerv hllesgllpg qkvtativlt dlqgfstise klppevvmsw
      481 lneylsamaq evqahqgvin kftgdgmlav fgvpiprttp eeiaedarla vscalaissr
      541 lpemnqnwlt rglpaakmrv giftgpvmvg slggttrley gvigdsvnia srlescekdr
      601 qegtcrilia eetflhladk feveswgllp lkgreqkvnv yrilgrkkk
//
LOCUS       WP_006635406             638 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Microcoleus vaginatus].
ACCESSION   WP_006635406
VERSION     WP_006635406.1
KEYWORDS    RefSeq.
SOURCE      Microcoleus vaginatus
  ORGANISM  Microcoleus vaginatus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae;
            Microcoleus.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 638)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Microcoleus vaginatus"
                     /db_xref="taxon:119532"
     Protein         1..638
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59764
     Region          367..596
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mppsdsfnpg assssssssq sssfvdssga gstssataas ptgsstssqt aytagatsss
       61 gsaaasastv appttsatas apaaapapap apaptpaptp appptpaplg dssgasssss
      121 tatsptgnss saqtasapgd ssssasasas sgldtpptts atasapaatp tptpapapap
      181 tpapaptpap ladssgasss sstatsptgn sssaqtasap ggtsssasas assgldtppt
      241 tsatasapap apaptpapla dssgasssss tatspagssg saqtasapgg tsssasasas
      301 sgldtpptts atapapapap apapepapap aapaatdsap vinitpptpt pptptpptpt
      361 pptptpsnnd gatftpvtgg tssnssssns ysdstgtgge stiiseptdn snsnnsialp
      421 ahntnnsnae ttpppemiap enypgaltit ydsngdgywl gtsdsdviic gsgvdqifag
      481 sgddivtsnr gddaidggdg ndtvrggkgq dwliggngdd flcgdfgsdt liggsgadtf
      541 afrpetasaa anplladrvv dfnpaqgdri gligglsvtd ltlvafdtdg dgttdatlvk
      601 fssnngdril gvvlgtvnaa gattlsnadf islpndil
//
LOCUS       WP_006636624             291 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Bacillus].
ACCESSION   WP_006636624
VERSION     WP_006636624.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 291)
  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 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   3  (residues 1 to 291)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 291)
  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   5  (residues 1 to 291)
  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   6  (residues 1 to 291)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..291
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33306
     Region          21..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..287
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mdmlkhmnea mkyiennlan didykeaakr afcseyhfkr mfsflagisl seyirrrrlt
       61 laafelkgsq akvidiavky gyhspdaftr afqklhgmtp tearsgaqtl kaypemtfql
      121 tikggnemny rienkapfri vgikkrvpiv fhginpeiaa mwktlnnemi tqlktlsnme
      181 pqgllqasvn fsesrmeekg eldhyigvat tqqcpdhfvq levpastwav feaagpfpet
      241 lqdvwgriys ewfpssnyeq tegpeilwne skdldspsfk sqiwvpvlqk r
//
LOCUS       WP_006637198             367 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GerAB/ArcD/ProY family transporter [Bacillus].
ACCESSION   WP_006637198
VERSION     WP_006637198.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..367
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=41134
     Region          1..364
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 metakvspkq lftlivlfef gtalivplgi gakqdawlae ligmiggtvl ffhyyylykq
       61 ypkllptryf qkilgkhlgf liglsyvlff iygasrdlrd ssellllqyn qtpmyivsgi
      121 tmllvcyaly kgievlarta elifplllfl iiltfvflaa snvirfenll pvlengwepv
      181 vttaflervf fpygelvcft vifpyinrsr ngmkfgltam ifagfvlimt ivleiavlgv
      241 ygwststfpf lrfvekinig gfiqglqgfa mivlvvgnff kvaifsyaai icsadlfnlk
      301 hhasliapig fiiltvsmas aasyvehieq akivlrsifv lfefiipfll tavvmvkkhf
      361 ggstrhs
//
LOCUS       WP_006638102             302 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Bacillus].
ACCESSION   WP_006638102
VERSION     WP_006638102.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 302)
  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 302)
  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 302)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..302
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33367
     Region          1..69
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          218..277
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mtelgnrlke areekgmsld dlqaatkiqk ryltaleegn ydiipgkfyv rafikqyaea
       61 vglnsenlfe efkkdipdsy ndevsdklss ikpqrelpks askalellpt llvsagvivv
      121 iaiiyvivqa vigggnqnsa dqtkteetqs kydvskdspl tkenqksgdn ekaadkdkke
      181 ngddeqadek kelniktvss qgssttyevs gadklelevk ttgdswvrvq dakgnslkeg
      241 tmkkgetfqk nitdqdqidl rigyapgvei kingkvlsye ldpknvmtqn itiqnkkeek
      301 ss
//
LOCUS       WP_006638088             221 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Bacillus].
ACCESSION   WP_006638088
VERSION     WP_006638088.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 221)
  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   3  (residues 1 to 221)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..221
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25293
     Region          8..217
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mlslgniiti efenenqenv iakskvssie envlkvhypv dvetgrtvii ptntiatihf
       61 vnaqqipykf tsviqgreiy hnipvlnmyl peedqmtkiq rrqffrvntt ipvtvrpygs
      121 gsmfktyttn isaggaalii eetqkhepee dlnlsislpn kgddeividv htqvkrtyld
      181 rrtnkqimtv efismnehdk qtlvhycikc qliekkklks e
//
LOCUS       WP_006638153             678 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Bacillus].
ACCESSION   WP_006638153
VERSION     WP_006638153.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 678)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 678)
  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   3  (residues 1 to 678)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..678
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..678
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=75218
     Region          1..678
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          166..245
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 mdmnqyldvf ieeskehlqt cnekllelek npsdlqlvhd ifraahtlkg msatmgfedm
       61 ahlthslenv ldairneemt itsewmdvmf ealddleaiv lsiieggdgk rdvsevcakl
      121 dvtganketa aaaeapeaas skskwsydef qrtviaeaee qgfncyeisv slkddcllkg
      181 vrvymvfeql neigevvkti petevlesed fdsefvicfl skhdkqeifn kvngvseiek
      241 vevtelkidi apsenekpae ekeaapkete kkpekpakqp kqsngkkepa kpaagggtkt
      301 irvnidrlds lmnlfeelvi drgrleqiak eldhgeltet vermtrisgd lqsiilnmrm
      361 vpvetvfnrf prmvrqltke lnkkieltif gaeteldrtv ideigdplvh llrnsldhgi
      421 eapevrvkng kpetgqvtlk ayhsgnhvfi eveddgagin rkkvlekale rnviterdae
      481 tiedheidal ifapgfstad qisdisgrgv gldvvkskle slggsvsits tegkgslfsi
      541 qlpltlsiis vllvkleket faipissiie tavidkkdil fthdrevidf rghivpvvyl
      601 keqfnvedsa ddldqlhaiv vkkgdkltaf vvdsfigqqe vvlkslgdyl tnvfaisgat
      661 ilgdgqvali idcnalik
//
LOCUS       WP_006638464             341 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Bacillus].
ACCESSION   WP_006638464
VERSION     WP_006638464.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..341
                     /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=39225
     Region          2..272
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 msnsrdsyfd nakflliflv vfghiirsyi ndndvllhiy kfiytfhmpa filisgyfak
       61 gfnrpgymkk ialklivpyl ifqgiytvfy sfiddqslsa anpfepqwsl wfllslffwn
      121 lllfpftalp gkwafaasla iavlvgyvda vsdtlslsrt fvffpvflag yylkkdhfkm
      181 lkgwkgkqaa lavlaatfvf yffvdfdysw lfgskpysef gdvgiksgln rvallvltfa
      241 stfgfmalvp ekryfftlwg trtfyvyllh gfiiksfrkt gaeewladyq sltvliiata
      301 vltfflsssf vktvaqpvie lkmtnlmkwl kkqgrynays k
//
LOCUS       WP_006639759             390 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Bacillus].
ACCESSION   WP_006639759
VERSION     WP_006639759.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 390)
  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 390)
  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
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 390)
  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   5  (residues 1 to 390)
  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   6  (residues 1 to 390)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 390)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 390)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..390
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41577
     Region          17..57
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          76..381
                     /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 mqrgtfqlmk svnksiilnk irtsepisra eiaketkitp ptvssivkel igqglvkest
       61 rghssggrkp tmlhintgaf yvigidagpe tvecvltdla ggilqrtssl lkkpltnemf
      121 idvlkenida ilgradvdqe kiigigiamh gvvdaetgms riapilnltn ipikdvleqe
      181 fnltvrvend aramalgesw fggrddagsm aavnigrgvg agivingkly hgaegiagel
      241 ghmiidinge kcecgnrgcl qtivsgkaia ergkkrlkes pdsltakdlf emaengcqtc
      301 ielfretgvi igigltnfih lvnpgkivlg ggvmkggrfi lpairetiqq kaltaearqt
      361 evtitklgde atlygavsll laelfdpvlk
//
LOCUS       WP_006643704             413 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein, partial [Photobacterium sp.
            SKA34].
ACCESSION   WP_006643704
VERSION     WP_006643704.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium sp. SKA34
  ORGANISM  Photobacterium sp. SKA34
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Photobacterium sp. SKA34"
                     /db_xref="taxon:121723"
     Protein         1..>413
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          4..>413
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mdgmrrllkp ksitvigasd npsragnvvi rnllsdqfrg pimpvtpkyd avagilaypd
       61 iaslprvpdl aivctraeln idiveqlgkk gvkaaiilaa gmnnqqlnpa pftpnhqpsl
      121 edqmlakake ygmrligpns mglilpwlnl nasfspisan kgniafisqs aavcttildw
      181 aknksigfst flslgdacdi nfaelldtlc qdskteaill yidsvkdarr fmsaaraaar
      241 nrrilvlksg rtqagssaah ihtggdigld avydaairrs gmlrvnnthe lfaavetlsh
      301 svplrgerla iltngggpai mavdalsdrg grlaqlspet inrlsavlps cwshsnpidi
      361 igdaditryq qaikilldsd dfdallimhs psaiapdtat anvlvetlhq hpr
//
LOCUS       WP_006644067             486 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [unclassified Photobacterium].
ACCESSION   WP_006644067
VERSION     WP_006644067.1
KEYWORDS    RefSeq.
SOURCE      unclassified Photobacterium
  ORGANISM  unclassified Photobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 486)
  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 486)
  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 486)
  AUTHORS   ter Beek,J., 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 486)
  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 486)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="unclassified Photobacterium"
                     /db_xref="taxon:2628852"
     Protein         1..486
                     /product="CmpA/NrtA family 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=53878
     Region          59..340
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mapkplflnr ssgfyflswv gnimaikglm qlikksygvs lsallfgalt vnasplvlge
       61 pekeelklgf ikltdmapla iayekgyfed eglyvsleaq anwkvlldrv idgeldgahm
      121 lagqplgati gigtkapiit afsmdlngna itvsnevwqq ikpqlpvden gkvihpikae
      181 alkpvlehyk dtgkpfqmgm vfpvsthnye lrywlaaagi npgfyapekg dnsgqreaei
      241 llnvtpppqm patmeagtiq gysvgepwnq qavakkigvp iiadndiwkn npekvfgvte
      301 swakenpnth irlvkalira aawldhngne nraeaskila rseyvgadek viansmtgsf
      361 eyeagdirpa pdfnvffryn atypyysdav wsltqmrrwg qipqakpdsw yidiakqvyr
      421 pdiyrlavna lisdglmkqs dfsdvdnetg frpphnhfid nitydgrspn ayleqfsigl
      481 kgdqqi
//
LOCUS       WP_006644548             262 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Photobacterium sp. SKA34].
ACCESSION   WP_006644548
VERSION     WP_006644548.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium sp. SKA34
  ORGANISM  Photobacterium sp. SKA34
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 262)
  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 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   3  (residues 1 to 262)
  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   4  (residues 1 to 262)
  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 262)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Photobacterium sp. SKA34"
                     /db_xref="taxon:121723"
     Protein         1..262
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30236
     Region          5..258
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          179..257
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mknvyqplfd dnnppsdiff ghtiflpntg tmkhahpwgq lqlisggiie lkaetkhfla
       61 ppqyalwvpp aiehqsyirr slnycsmnit kpladalpdy scllevsplm qamvndlrer
      121 rivipetpqd krlvkvlfdq vlmskeheqy lpttedkllq smlieleknp tnnttlaewa
      181 kqlhttertl arhfkdklgm sftewrqrrk fiyslhllrs glsvkeiaft lgyhqaspfi
      241 tafkkqsgst pdqyrqrlgt ek
//
LOCUS       WP_006644624             607 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Photobacterium sp. SKA34].
ACCESSION   WP_006644624
VERSION     WP_006644624.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium sp. SKA34
  ORGANISM  Photobacterium sp. SKA34
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 607)
  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 607)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Photobacterium sp. SKA34"
                     /db_xref="taxon:121723"
     Protein         1..607
                     /product="M4 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=67218
     Region          10..600
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mnlqrqtsck iavllgtsvg fsvhaaemvk vndnkflfqs lraqstsitp letgfseikk
       61 vvlpngktkv ryqqtylgvp vfntsvvatl snnkpsdvyg lmakgvnrdl psitpklsek
      121 eailaaitsh qlvannnhni enknaklmvk lddnqtakiv ylvnfyiase hperpfyivd
      181 aingvilehw dglnhakasg mgpggnikts eyiygfdfdg lpiskvgttc tlenaavktv
      241 nlnnategnt ayqynciddd nynyfryvng afsplndahy fgnvvfdmyq dwmntsplnf
      301 qltmrvhygs eyenafwngs smtfgdgkdr fyplvdinvs ahevshgfte qnsglvykdm
      361 sggineafsd iageaaeyyl rgkvdwivgs difksegglr yfdqpskdgq sidhasqyyd
      421 gmnvhfssgv fnrafyllan kpnwgvrkgf eiftlanqly wtanstfdeg acgvvkaaed
      481 fgytvkdves afnsvgvdas cgspipndnv likwepitdl sgsensktyy ifnvdkastv
      541 mvsmaggkgd adlyiranrk pttsafdcss nrsgndemcy lyaqpgityy vlihgytryt
      601 kltlrld
//
LOCUS       WP_006646412              97 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Photobacterium sp. SKA34].
ACCESSION   WP_006646412
VERSION     WP_006646412.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium sp. SKA34
  ORGANISM  Photobacterium sp. SKA34
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 97)
  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   2  (residues 1 to 97)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Photobacterium sp. SKA34"
                     /db_xref="taxon:121723"
     Protein         1..97
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10462
     Region          35..95
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 myayrlfkai tlvgglalvp lshaadnmhe gidikinint anveqldtll igigaekaqa
       61 iinyrkvngk fasvddltkv kgigeatvdk nrkriel
//
LOCUS       WP_006646797             745 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Photobacterium sp. SKA34].
ACCESSION   WP_006646797
VERSION     WP_006646797.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium sp. SKA34
  ORGANISM  Photobacterium sp. SKA34
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 745)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 745)
  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   3  (residues 1 to 745)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..745
                     /organism="Photobacterium sp. SKA34"
                     /db_xref="taxon:121723"
     Protein         1..745
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=80180
     Region          6..744
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msfdldedil qdflieagei lellseqlve lerspddsel lnaifrgfht vkggagflsl
       61 telvdachga envfdllrtg krsvtselmd vilealdcin vmfeqvkehq pldraeqrll
      121 dalhyysqpa tadelapiyk paevpsvdii aevtpepait snndnvttgs svddmtqdef
      181 drlldelhgt gqspskpttp eptapnnvda qlnfdsgdit ddeferllde lhgsgkgpgn
      241 sdtpasdvai psssisssvt psstvpedtg agdsddlmtd deferlldel hgagkspsle
      301 eqasaaqsta ndlteieatv psaqstamvt ptpavhqppa ersakpvavk ekskpqadat
      361 vrvdtstldt imnmvgelvl vrnrlvslgl ntndeemska vsnldvvtad lqgavmktrm
      421 qpikkvfgrf prvvrdlars lkkdivlemr geetdldknl vealadplvh lvrnsvdhgi
      481 empdvrelvg kprtgtvlls asqegdhill tieddgggmd aeklrsiave rgvmdadaas
      541 ritdneaynl ifapgfstkk eisdisgrgv gmdvvktgin qlngsihids vlgkgtridi
      601 kvpltlailp tlmvgvgeqp falplasvne ifhldlnktn tvdgqltiiv rdkaiplfyl
      661 qdwlsnmtvg tnkdrghghv vivqighqri gfvvdtligq eevvikplds llqgtpgmag
      721 atitsdghia lildvpsllk hyagh
//
LOCUS       WP_006655559              73 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Helicobacter canadensis].
ACCESSION   WP_006655559
VERSION     WP_006655559.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter canadensis
  ORGANISM  Helicobacter canadensis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 73)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 73)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 73)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 73)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..73
                     /organism="Helicobacter canadensis"
                     /db_xref="taxon:123841"
     Protein         1..73
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=7870
     Region          1..73
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mievellgpl gnqkftsnak dfyalkqelq qdsniqawlk dcaialndei vqsldtplkd
       61 gdkvvilppv cgg
//
LOCUS       WP_006656410             499 aa            linear   BCT 20-JAN-2025
DEFINITION  type I restriction-modification system subunit M [Helicobacter
            canadensis].
ACCESSION   WP_006656410
VERSION     WP_006656410.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter canadensis
  ORGANISM  Helicobacter canadensis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 499)
  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   2  (residues 1 to 499)
  AUTHORS   Youell,J. and Firman,K.
  TITLE     Mechanistic insight into Type I restriction endonucleases
  JOURNAL   Front Biosci (Landmark Ed) 17 (6), 2122-2139 (2012)
   PUBMED   22652768
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Sistla,S. and Rao,D.N.
  TITLE     S-Adenosyl-L-methionine-dependent restriction enzymes
  JOURNAL   Crit Rev Biochem Mol Biol 39 (1), 1-19 (2004)
   PUBMED   15121719
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Murray,N.E.
  TITLE     Type I restriction systems: sophisticated molecular machines (a
            legacy of Bertani and Weigle)
  JOURNAL   Microbiol Mol Biol Rev 64 (2), 412-434 (2000)
   PUBMED   10839821
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114514
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Helicobacter canadensis"
                     /db_xref="taxon:123841"
     Protein         1..499
                     /product="type I restriction-modification system subunit
                     M"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=56759
     Region          1..140
                     /region_name="HsdM_N"
                     /note="HsdM N-terminal domain; pfam12161"
                     /db_xref="CDD:463478"
     Region          153..389
                     /region_name="HsdM"
                     /note="Type I restriction-modification system, DNA
                     methylase subunit [Defense mechanisms]; COG0286"
                     /db_xref="CDD:440055"
ORIGIN      
        1 mqntidritd ilrrddgisg amhyseqisw ilflkflddy erelkdeafl ndvpyasild
       61 sqyawqswaa pkkdgkldvk nalsgsdlle fvnnelfpyl ksfknnedfk siaykiggif
      121 efidnriang htlrevinli delsfskesd vfalgdvyek llkdmgsdgg nsgefytpra
      181 lvkvmvevin pkpkeriydp acgscgflve sflhilyedr akgqkanlsv eeleflqkda
      241 lfgkektpls yamgvmnmil hgikspniik tntlskritd iteseryevi lanppfggke
      301 keqiqgnfiv psnatellfl qhilkslktn grcaiivpeg vlfqnsnafv kvkqdlieny
      361 nlecvlslps gvflpysavk tnvlffskgl rgivdeqdsn vyyyelippy kltknkpley
      421 vhfkeflecy kqrkitphsy lvsleelkar nydlsaknpn tkeekslrev gaileslhnt
      481 qnqvmtllge letqihtki
//
LOCUS       WP_006657643             456 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Providencia alcalifaciens].
ACCESSION   WP_006657643
VERSION     WP_006657643.1
KEYWORDS    RefSeq.
SOURCE      Providencia alcalifaciens
  ORGANISM  Providencia alcalifaciens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Providencia.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Providencia alcalifaciens"
                     /db_xref="taxon:126385"
     Protein         1..456
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=50480
     Region          3..429
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mvnnqieasv iggllkdglt lnasdvlatl kpeafavhfy retykviqkq aktrglidlm
       61 mvaeamgdky fadimqvakd cpsaanlkgy atmvtdnhnr remirlmddh rhiiefgsid
      121 aaaeamdkli kkanelraan deikpvhtke liadftdvle qrltngdesd tlktgiheld
      181 eitgginsvd lviiaarpam gktelalrit egvasqvdkq tglkkgvlif smemssrqim
      241 erqiagasgl svsslrnpak mddegwarvs ngigriqdld vwivdaskln veqiraiakr
      301 hkqqypslal ilvdylglie kpkaerndla igyissnlkn makelltpvi slsqlsrdve
      361 krpnkrpvng dlrdsgsieq dadsiimlyr davynenssa apyaeiivtk nrfgktgtvy
      421 qrfknghfmd vdqmeaanac qqsnkpqqrr yqgadv
//
LOCUS       WP_006660862             283 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Providencia
            alcalifaciens].
ACCESSION   WP_006660862
VERSION     WP_006660862.1
KEYWORDS    RefSeq.
SOURCE      Providencia alcalifaciens
  ORGANISM  Providencia alcalifaciens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Providencia.
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   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 283)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Providencia alcalifaciens"
                     /db_xref="taxon:126385"
     Protein         1..283
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31353
     Region          <29..70
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msnkiqgyvw dacavsgvkg tklmimvrla dyssdegvsy psvetisrqi gagvstirsa
       61 cneleqdgwl vkkmrrngnr nasnlyflnv dklekialee naklrklrek askshhpese
      121 rsdsdrtenn ekvrfdppvs gvqggfhppe sggdpsvnsk hdpsvnsked psvqvepkks
      181 kksfdaklak pknvsdevws dwinfrkeik kpltetmckq qakklagcsd adavicnsia
      241 ngwqgifpek sitkfnkpns htgfgdkhye sqdphwfvgg kna
//
LOCUS       WP_006668715             474 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Limnospira maxima].
ACCESSION   WP_006668715
VERSION     WP_006668715.1
KEYWORDS    RefSeq.
SOURCE      Limnospira maxima
  ORGANISM  Limnospira maxima
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Sirenicapillariaceae;
            Limnospira.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 474)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Limnospira maxima"
                     /db_xref="taxon:129910"
     Protein         1..474
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48022
     Region          42..293
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          179..451
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mtaelipnpt qpessrpnpn aidggliieg fmnqenrlig tggsdlitgg dlndviyggd
       61 ggnntlsgga gddliyggqg ndiiyggegk ntisagegnn tllggagddl vyggkdddii
      121 yggkgsdtiy agegnnllfs nlgddlvygg qgndiiyggq gddtiyggeg nntllgdkgn
      181 dliyggqgnd iiyggegknt isagegnntl lggagddlvy ggkdddiiyg gkgsdtiyag
      241 egnnllfsnl gddlvyggqg ndiiyggqgd diihggegnn tllgdkgndl iyggtgndti
      301 ygvegnntil ggpgnnlifg gknddvihsg kgdntvyggq gndrisagkg nslltggkgs
      361 dtfslvsgnp dksfsiqelf gldtitdftv gedriqldad ifdalggagn ladsqfttia
      421 nfdptnptnt gganlvynst sgvlyyidgt gqaipilnlg eglddldsds fdli
//
LOCUS       WP_006669557             303 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Limnospira].
ACCESSION   WP_006669557
VERSION     WP_006669557.1
KEYWORDS    RefSeq.
SOURCE      Limnospira
  ORGANISM  Limnospira
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Sirenicapillariaceae.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Limnospira"
                     /db_xref="taxon:2596745"
     Protein         1..303
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31083
     Region          2..229
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mssvgviidp rildelfgvd tlpadliipp egsvngetnn sgdnlgngts dfgetlssng
       61 svneitvtds agetvrgtga adriiggdgp dsllggsnnd tiygkagsdt llgeagndll
      121 fgnqgrdlly ggngndtlyg gqeadtlyge agddllfgnl andwlyggdg ndtlfggknd
      181 dilyggdgnd llsgdtgadt liggegrdsf vvsslsggvn ireadvimdy trsddqillt
      241 gglrstnlef vsgtsvgleg eledstvirl rqsfdpnraf vaivvgvdnl tsadftaidq
      301 iti
//
LOCUS       WP_006670157             134 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Limnospira].
ACCESSION   WP_006670157
VERSION     WP_006670157.1
KEYWORDS    RefSeq.
SOURCE      Limnospira
  ORGANISM  Limnospira
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Sirenicapillariaceae.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Limnospira"
                     /db_xref="taxon:2596745"
     Protein         1..134
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13782
     Region          <50..>134
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mfsdiitqng ltfamaspan dfmivselpd eqiarlsspg lpqaiallpg ddylvndaqg
       61 rillghqgnd tiignsgndt iyggqnddyl nggsgddllf gnrgndtiyg gsgndtiygg
      121 vgndwivggs gnnv
//
LOCUS       WP_006670862             535 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Limnospira maxima].
ACCESSION   WP_006670862
VERSION     WP_006670862.1
KEYWORDS    RefSeq.
SOURCE      Limnospira maxima
  ORGANISM  Limnospira maxima
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Sirenicapillariaceae;
            Limnospira.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 535)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Limnospira maxima"
                     /db_xref="taxon:129910"
     Protein         1..535
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=60191
     Region          31..>509
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 msgkwlqvfk nkradlkeii acaianaivi lailllkqag glqtleliaf dimvrlrndl
       61 epdprllivg iteedivafn rwplsdevia qlldrlsqlq pqaigldiyr dipyepghqs
      121 liqqldnpki itikalgdae vqgtlapptv ppsrvgfndl lldpdgvvrr nlmlatiede
      181 pfysfsmrla lrywqkqgie ptnsplhpdd irwgaaeflp ldrtsggyqt iddqgyqill
      241 dyrsrkplar vvsvsevlyg nipsswvedk ivligtiaps gkdlfltpys psrrispkmp
      301 gvlihaqmvs qlldvvager slfvfwppwa efvwaigwgv vgvmvvvvvr hplvwifcpp
      361 lmlgvlwmgg fylflnsvwv pmvtpsltll ftsviviiyl gfraqrqqqv vmgllgqnas
      421 peiakalwns rdrlmtngkl pgeklvatml ftdirnfsti seqippeqli ewlneylatl
      481 tqcvhshrgi inkfmgdgim aafgvpiart teqkllkmpm rrwlvlwkwa ivsws
//
LOCUS       WP_006674642             802 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Paenibacillus dendritiformis].
ACCESSION   WP_006674642
VERSION     WP_006674642.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus dendritiformis
  ORGANISM  Paenibacillus dendritiformis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 802)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 802)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 802)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..802
                     /organism="Paenibacillus dendritiformis"
                     /db_xref="taxon:130049"
     Protein         1..802
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=89988
     Region          25..802
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkllaavtvp svkrrkkrwp rvtgiiflvl vlliacaggy vywfvnkslp vvqgklnisg
       61 lekevtvwrd asgvphieaq nehdlyiaqg yvtaqdrmfq mdlsrrqasg qlsevvgaka
      121 idrdkffraf slrraaevsl eayskesrqv lqwyadgvnn yikhakaars lpvefailgy
      181 epaewqpvds ltigkymayd lagnwegqaf ryamaqklss ekfqsvmpty pkdgaliiqa
      241 ltehpvdlta laatavprdp fngsnnwvvs geksasgkpm landphlgls tpsiwyethl
      301 sapelnvsgv ifagvpgiil ghndmiawgv tnlspdvqdl yiekrnpdnp hqfeymgkwe
      361 dakvykeeik vkgedpvpye vvvtrhgpii sefahdqrqe talamkwtal natteleavq
      421 mfakarnwed fkqalehfea paqnfvfast dgtiayrgng lipirkkgdg svpvpgwtde
      481 fewtgyipwd elpttvnpke gfiatannkv igdsypyhlt dvwsqpyrea riqqvlsakd
      541 nltvedmkkl qfdrhnlhae efldeliaki kdspdlrqid rdtlsllqdw nkvndpeqaa
      601 plgyelwmqs fddvlfkpei nadmmelfnn ksvvkdemlr ralqgerepw idekggiekv
      661 alqafqlaad qaaslqgklp dkwrwgkfhq vdfahplsav kpldlifnak svpmgggrvt
      721 vgaagwnaes gevthgapwr tvidmsdptr slnvvgpgqs ghvlskwyhd qvddwttgqy
      781 hitsnvpney rkagnelklv pe
//
LOCUS       WP_006674917             274 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Paenibacillus
            dendritiformis].
ACCESSION   WP_006674917
VERSION     WP_006674917.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus dendritiformis
  ORGANISM  Paenibacillus dendritiformis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (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   2  (residues 1 to 274)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Paenibacillus dendritiformis"
                     /db_xref="taxon:130049"
     Protein         1..274
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31078
     Region          21..272
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          27..121
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
ORIGIN      
        1 mdtkpnrepd vrgmlyaaag eqkfritrhl papdlrhfvk hywmiawdlr gqppyvqevl
       61 qhpgvnlvfe rdntavygiv sgrsqrvleg qgrvagvlfq pagfyplyre pmsrlaghtl
      121 pfrdvfgids gpmeqalfal edgeamsrii dgflrerlpe aednvklvnr iietvvdgrd
      181 itrvqelaer fslhtrslqr lflhyvgvsp kwviqrsrih eaagmaaaga vpdwaalaad
      241 lgyhdqahfi kdfkafvgvs peeyarklrh reqi
//
LOCUS       WP_006677056             296 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Paenibacillus
            dendritiformis].
ACCESSION   WP_006677056
VERSION     WP_006677056.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus dendritiformis
  ORGANISM  Paenibacillus dendritiformis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Paenibacillus dendritiformis"
                     /db_xref="taxon:130049"
     Protein         1..296
                     /product="formate/nitrite transporter family protein"
                     /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=30719
     Region          4..258
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 magylkpqei aaatvetgta karnplsvmv ilgflagafi algyllyirv tagappewgt
       61 itgligaslf piglilvllg ggelltgnmm avplarmkgr ittgevarnl ivitlsnflg
      121 aifvayffgh ivgltadgvy lektvsvagh kleegflqaf vsgigcnwlv alavwlsygs
      181 ksfsgkvlgi wfptmtfvai gfqhvvanmf vipaaifegy yswgeymmnf ipvwlgnltg
      241 gavfvagayc laylrpssda alpaqtsgtr astsaasaap atpasssgsl dhsvtg
//
LOCUS       WP_006678173             247 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Paenibacillus
            dendritiformis].
ACCESSION   WP_006678173
VERSION     WP_006678173.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus dendritiformis
  ORGANISM  Paenibacillus dendritiformis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 247)
  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 247)
  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 247)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Paenibacillus dendritiformis"
                     /db_xref="taxon:130049"
     Protein         1..247
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27000
     Region          156..245
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(175,194..195,213,216,224..225,237,242)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mqsfedngsv ddgkamtfad delgqfcett rrvvivspfp asirslfval tircydvllf
       61 hqehdpmlqt mnsdlvivdr tkavpadpsa tipgshgail llqgedlgtg pdeqgrevmi
      121 wpcpieaals rieelasrnd aqpavagsel lrfkdvvvdl kritvhqaga kieltrtefd
      181 vlkglllngg gvmtrqqime fvwgesyigg snsidvhiks lrqklgdapk hpkyivtvrg
      241 igyriad
//
LOCUS       WP_006680688             273 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein
            [Actinomycetaceae].
ACCESSION   WP_006680688
VERSION     WP_006680688.1
KEYWORDS    RefSeq.
SOURCE      Actinomycetaceae
  ORGANISM  Actinomycetaceae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales.
REFERENCE   1  (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   2  (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   3  (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   4  (residues 1 to 273)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Actinomycetaceae"
                     /db_xref="taxon:2049"
     Protein         1..273
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=29321
     Region          1..273
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mitfdhishv fpngttaldd vslhvephtt tvllgtsgsg kttlmrmvnr mlsptsgrvv
       61 vrgqdvadvd pvklrrsigy vlqdaglfph rsivdniatv prlegasrre sakralelmd
      121 lvgldrglak rypaqlsggq rqrvgvaral aneadillmd epfgaldplv radlqrelrd
      181 lrdrvgttil fvthdldeaf mlgdqiavlq tggvlaqvgt senlvtnpan dfvasfvgss
      241 gqrrlsmkst pagtlvsdpd grplgllpeg elr
//
LOCUS       WP_006680858             471 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase family protein [Actinomycetaceae].
ACCESSION   WP_006680858
VERSION     WP_006680858.1
KEYWORDS    RefSeq.
SOURCE      Actinomycetaceae
  ORGANISM  Actinomycetaceae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales.
REFERENCE   1  (residues 1 to 471)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Actinomycetaceae"
                     /db_xref="taxon:2049"
     Protein         1..471
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=49404
     Region          77..178
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          <228..315
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          351..470
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(423..424,427,443..446,448)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mtrmkwliaa iigvlvvvgg agtayasyys dkalptasvg ghnvnamnrd elvawindqa
       61 sqvsididvd gtpskaslad lgvtvdaqas adqvlassds vwerfvglfk rsdyplvsst
      121 dkktfnayma slvksvgeap ksatvsvdeq gafvvtpgvp giaidaqpln davatalqtl
      181 ssqaisvsps tqdpivsdkq aqkvadaata lvahsvtisd gikdytaetv draawvalpg
      241 vddvegtpsi dpeavqawvd ktaeatnvap tpainnvdga gnvlaesmpg kegeavnnsa
      301 qvgadvvaal nagtdysgsf dydkvpppte trpvmagyea ypyamhegek widinlttnr
      361 ltayegqtvv hdpiavnhga pghetvtgty hiylkyekqd mgctpewpyc akdvpwvsyf
      421 tgsyaihgap wvrqfglgsv ggshgcvnlp vaeahyvfsw adsgtavvth y
//
LOCUS       WP_006683444             398 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Citrobacter youngae].
ACCESSION   WP_006683444
VERSION     WP_006683444.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter youngae
  ORGANISM  Citrobacter youngae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 398)
  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 398)
  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
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 398)
  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   5  (residues 1 to 398)
  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   6  (residues 1 to 398)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 398)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 398)
  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 20682457
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Citrobacter youngae"
                     /db_xref="taxon:133448"
     Protein         1..398
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44387
     Region          14..53
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          82..393
                     /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 mqiaglnnqt vrqhnrraim aliwrykrls ksqlathtgl sipaiskild elvgerklsh
       61 ssenlssrgm nsghyqipnd gplilcmnvt ptsiesqlid aqmtpvgdfl htqvnaptpe
      121 alltaiedlw rqqqkhcpgr hinlalgvhg qvdpdtgvsq tmpqapwkkp veikylleer
      181 lrvsvrvdnd cimlalaekw qngsnrqdfc ivnvdygigs sfvingqiyr gmlngsgqig
      241 htifdrdgia cdcgrygcle tvaslsalkk qarvwlksrp tppgldpqti tsrqlidawh
      301 sgdeqvvqwv eqaanaiglt lynllnilni nqiwfygrsc efgdrwlqti yrqigftpfd
      361 qgdavrtrqt qigfgnltrq qqitgigylf veaalara
//
LOCUS       WP_006683605             313 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Citrobacter youngae].
ACCESSION   WP_006683605
VERSION     WP_006683605.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter youngae
  ORGANISM  Citrobacter youngae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Citrobacter youngae"
                     /db_xref="taxon:133448"
     Protein         1..313
                     /product="formate/nitrite transporter family protein"
                     /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=34826
     Region          37..289
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mndiekekid rhsdelqves deksegkkie vdedrlpsra maihehirqd gekemerdam
       61 allwsaiaag lsmgasllak gifhvqlegv pggfllenlg ytfgfiivim arqqlftent
      121 vtavlpvmqn ptlgnfgllm rlwgvvllgn iigtgiaawa feympifdee trdafvkigm
      181 dvmknsptem fanaiisgwl iatmvwmfpa agaakivvii lmtwlialgd tthivvgsve
      241 ilylvfngtl hwgdffwpfa iptlagnicg gtfifalmsh aqirndmsnk rkeearlhak
      301 reekkdkiqk kqa
//
LOCUS       WP_006685614             231 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Citrobacter youngae].
ACCESSION   WP_006685614
VERSION     WP_006685614.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter youngae
  ORGANISM  Citrobacter youngae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 231)
  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   3  (residues 1 to 231)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Citrobacter youngae"
                     /db_xref="taxon:133448"
     Protein         1..231
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26595
     Region          32..221
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 msfglakdnk feiiailree lhkktklevl censsvitql ekvdferfvi sghedivpek
       61 vqyfilhses givkfsarfe qnpsagaeag lsylipdmif faqqrqnqrf sflkgydffc
      121 fgrykngeny sfkiknisqg gcalivkdvn arfvykdavi knaslefdtf gslrldlkvi
      181 dvvtinefde dnqlyschqi scefdfknrr eeaevekiii kflmsnkiks l
//
LOCUS       WP_006687643             283 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Citrobacter youngae].
ACCESSION   WP_006687643
VERSION     WP_006687643.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter youngae
  ORGANISM  Citrobacter youngae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 283)
  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 283)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10097223
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Citrobacter youngae"
                     /db_xref="taxon:133448"
     Protein         1..283
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29931
     Region          5..281
                     /region_name="TBP_aldolase_IIB"
                     /note="Tagatose-1,6-bisphosphate (TBP) aldolase and
                     related Type B Class II aldolases. TBP aldolase is a
                     tetrameric class II aldolase that catalyzes the reversible
                     condensation of dihydroxyacetone phosphate with
                     glyceraldehyde 3-phsophate to produce tagatose 1; cd00947"
                     /db_xref="CDD:238477"
     Site            order(26..28,31,51,54..56,60,64,67..68,141,233..234,
                     236..237,240,244,247)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238477"
     Site            order(81..82,177..179,181,208..209,211,230,232..233)
                     /site_type="active"
                     /db_xref="CDD:238477"
     Site            order(82,178,208)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238477"
     Site            order(177,179,181,209,211)
                     /site_type="other"
                     /note="Na+ binding site [ion binding]"
                     /db_xref="CDD:238477"
ORIGIN      
        1 mfadmksmvt kawreqyall aincmnlesa raavrvaekh rapiilnlyq ghldhfpapi
       61 aaavvktlae eaavpvalal dhgkdpvrir qafragfsgl midasafale enirqtravv
      121 elaasvslcv egelghlada prydhaanad lmtqaadvep fiqqtgidll avsvgtahgm
      181 yapgvtpaid fqrlediarl stvplalhgg sgtpfdqlqr cpafgvakin vgaavfeagk
      241 aallhtlcrd tsgelvdala lmeqaceeai ipylqasgai nka
//
LOCUS       WP_006686891             506 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Citrobacter youngae].
ACCESSION   WP_006686891
VERSION     WP_006686891.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter youngae
  ORGANISM  Citrobacter youngae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Citrobacter youngae"
                     /db_xref="taxon:133448"
     Protein         1..506
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54358
     Region          4..500
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mntaypviki nsnddvvvar fpvkegtwla heettvnvdi paghkialrd iavgeavkry
       61 gqvigfashd ikqgdhvhth nlsmgdftrd yafgedtvvl ppaekidtfm girrrdgrva
      121 trnfigilts vncsatvara iedhykkvgl eqypqvdgvv alpqsfgcaf gfnsetmavm
      181 rrtlsgyarh vnfagvviig lgcesnqikd liqtegleeg kflhsltiqe tggtqktidk
      241 giaiidamlp eannitrepv pvsevilale cggsdsysgi sanpvlgyva dkivqqggta
      301 ilsetseifg aehlltrrai tpevgkklia rikwwedyca rtksemnnnp sagnkagglt
      361 tvlekslggi akggtsnlve vyeyaepvta kglvfmdtpg ydpmavtgqi agganllcft
      421 tgrgsafgsk ptpslkiatn nalwqrqqed mdlncgdvae gietiaqage rlyaqvlama
      481 sgqktksekf gygslefvpw tmnaim
//
LOCUS       WP_006687955             495 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Citrobacter youngae].
ACCESSION   WP_006687955
VERSION     WP_006687955.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter youngae
  ORGANISM  Citrobacter youngae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Citrobacter youngae"
                     /db_xref="taxon:133448"
     Protein         1..495
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=53995
     Region          1..495
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mqyikihald nvavaladla egtevtvdgq vitlrqavtr ghkfalrnia qgenvvkygl
       61 pightlvdva agehihahnt rtnlsdldty syqpdfqtqe aqpadrdvqi yrrangevgv
      121 rnelwilptv gcvnamarqm qtrflketnd aegidgvhlf shtygcsqlg ddhvntrtml
      181 qnmvrhpnag avlvvglgce nnqvdafret lgeydpervh fmvcqhqede veagiehlhq
      241 lynvmrndkr epgklgelkf glecggsdgl sgitanpmlg rfsdyviang gttvltevpe
      301 mfgaeqllmd hcrdeatfgk lvtmvndfkq yfiahdqpiy enpspgnkag gittledksl
      361 gctqkagssn vvdvlryger lktpglnlls apgndavats alagagchmv lfstgrgtpy
      421 ggfvptvkia tnselaakkk hwidfdagql ihgkampqll nefvdaivdf angkqtcner
      481 ndfrelaifk sgvtl
//
LOCUS       WP_006690074             679 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Selenomonas flueggei].
ACCESSION   WP_006690074
VERSION     WP_006690074.1
KEYWORDS    RefSeq.
SOURCE      Selenomonas flueggei
  ORGANISM  Selenomonas flueggei
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Selenomonas.
REFERENCE   1  (residues 1 to 679)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 679)
  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   3  (residues 1 to 679)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..679
                     /organism="Selenomonas flueggei"
                     /db_xref="taxon:135080"
     Protein         1..679
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=73494
     Region          1..679
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdnqymdmfl deshehlqsl negllrleen meeisavndi frnahtlkgm satmgfakia
       61 elthemedvl dlvrkeqlkl nedimdtlfk cldsleqmvd svgngeaedv vdvsdlvakl
      121 ssiskgtpap aeaapsaaaa paadgassdl giddididvm kkakeagmni fhvkvtlmes
      181 cvlkaarsvm vmhaldevgd viksvppaed leqekfehsf dvviatsadt eavknavdtv
      241 seiedigvee ldpdalgkqi epapaqtapa aapaakkpaa pakkagaksa paakkphqsq
      301 svrvdiekld tlmnlmgelv inkvrleqig qthrmsdlme tleqmdrvtg dlqnivmkvr
      361 mvpvsavfnr fprmvrdvsk elgkeinlti egeeteldrt videigdpim hllrnsldhg
      421 vespdareak gksrvgevgl iarhegnnvv imitddgagi dadkirrkav ekgmisqsea
      481 dslddadavr liflpgfsta eqitdisgrg vgmdvvrski ealsghvdve thidegsifk
      541 iklpltlaii qamlvrvqee myaipltsid stinieptdi qtvqnkeviv lrgeiipiir
      601 meealqvpht kdsdehfvvv vhageakagi vvdnligqqe iviktlgnlf aglklfggat
      661 vlgdgrvali ldvatmiqq
//
LOCUS       WP_006690076             231 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Selenomonas flueggei].
ACCESSION   WP_006690076
VERSION     WP_006690076.1
KEYWORDS    RefSeq.
SOURCE      Selenomonas flueggei
  ORGANISM  Selenomonas flueggei
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Selenomonas.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 231)
  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   3  (residues 1 to 231)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Selenomonas flueggei"
                     /db_xref="taxon:135080"
     Protein         1..231
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25960
     Region          25..223
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 magelvears ilaigqrlei ffenteegtp gytsriediv gdelviampv derlipvipr
       61 pgenlyvlag gdgchyrffs vhrshghydg hiptlritip efaekfqkrg lfrikvnlma
      121 tirhvdaegt idapervpii dlsgsgmsfa wtrrvsvgtg valdindipg vgtlelmskv
      181 mrvtriered dmpiyhigiq fqavsrsmrd kiirylfqvq raqvervdnd e
//
LOCUS       WP_006690765             113 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Selenomonas flueggei].
ACCESSION   WP_006690765
VERSION     WP_006690765.1
KEYWORDS    RefSeq.
SOURCE      Selenomonas flueggei
  ORGANISM  Selenomonas flueggei
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Selenomonas.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Selenomonas flueggei"
                     /db_xref="taxon:135080"
     Protein         1..113
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12982
     Region          5..95
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 milsideird kirpicekyk iekvwlfgsy argearedsd vdvyaessnh vslldliafr
       61 mdledavakd vdmitripne ypifakyver dkvllydaqs egrtdsanyr svl
//
LOCUS       WP_006692174             386 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Selenomonas infelix].
ACCESSION   WP_006692174
VERSION     WP_006692174.1
KEYWORDS    RefSeq.
SOURCE      Selenomonas infelix
  ORGANISM  Selenomonas infelix
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Selenomonas.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Selenomonas infelix"
                     /db_xref="taxon:135082"
     Protein         1..386
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=40725
     Region          <1..379
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mefwgykrkd gragirnhvl ilpacacgse ssrivasqvr gavsivfntg csdvaantam
       61 sqkvltgfac npnvygvvii glgcetvphr klrekieamt skpvvsfgiq eeggtlktie
      121 kavraarema saagmqqker cgiselllgi ecggsdatsg lasnpavgel sdrlvdlgas
      181 tmmsesiewi ggehvlakra atpeihdqii rvcedyeahl kaagqdcrag qptpgnkdgg
      241 lstidekslg cirkggtrpi vevlaqaerp tkrgaivmdt agydissvts mvaagcnviv
      301 fttgrgtptg naivpvlkvt anahtyswme dnmdvdlsgi lrgeesisas gerlltrihe
      361 vangrltkae aygfsdiavd hvcrfv
//
LOCUS       WP_006692351             339 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Selenomonas infelix].
ACCESSION   WP_006692351
VERSION     WP_006692351.1
KEYWORDS    RefSeq.
SOURCE      Selenomonas infelix
  ORGANISM  Selenomonas infelix
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Selenomonas.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Selenomonas infelix"
                     /db_xref="taxon:135082"
     Protein         1..339
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=38581
     Region          63..>334
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mermkmhsrd nvvahieavg rlfpnaltev mrdgkvvqai dfdvlrqela reivegreer
       61 yaftwpdkqq ailaanapia atlrpvveds vgrdgkegaf dsenlyiegd nldvlkllqe
      121 tylgkvkmiy idppyntgnd afvydddfam adgdffaask vydedgnrty dfranngsng
      181 rfhtdwlnmi yprlrvaksl laddgvifis vdynenfnmr kvadeilgeq sfigeiywes
      241 ktksqntkta ynklqpkaem ilvyakdrqr rfhliekgvk eysfsdergv yreypvevmn
      301 asgvrgrgsm iyeisdtvst vfppagkqwk lgqaqvaty
//
LOCUS       WP_006692463             132 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Selenomonas infelix].
ACCESSION   WP_006692463
VERSION     WP_006692463.1
KEYWORDS    RefSeq.
SOURCE      Selenomonas infelix
  ORGANISM  Selenomonas infelix
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Selenomonas.
REFERENCE   1  (residues 1 to 132)
  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 132)
  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   3  (residues 1 to 132)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Selenomonas infelix"
                     /db_xref="taxon:135082"
     Protein         1..132
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15486
     Region          15..114
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mrdyktktkq yakelrqhmt peerrlwydf lsqnschfrr qqpignyiad fyapsirlvv
       61 evdgsqhfee tgqrydaars eflrqqgvrv lrftneqiqr rfpsvceavg raiadiragk
      121 eigdveddgh vy
//
LOCUS       WP_006692835             230 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Selenomonas infelix].
ACCESSION   WP_006692835
VERSION     WP_006692835.1
KEYWORDS    RefSeq.
SOURCE      Selenomonas infelix
  ORGANISM  Selenomonas infelix
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Selenomonas.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  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   3  (residues 1 to 230)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Selenomonas infelix"
                     /db_xref="taxon:135082"
     Protein         1..230
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26084
     Region          18..223
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 magelvqars ilaigqrlei ffenseegds gytsrvedii gdelvvampl derrvpiipr
       61 vgenlyvlag gdgchyrffs vhrshgrheg ripvlhisip evaerfqkrg lfrikvnlta
      121 tvrlvdregk idapkrvpvi dlsgsglafv wpkqvshdme aaleindipg igtlelmtrv
      181 mrctriered dtpiyhigvq fqeisrsmrd kiirylfqvq raqvervknd
//
LOCUS       WP_006693874             348 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Selenomonas
            noxia].
ACCESSION   WP_006693874
VERSION     WP_006693874.1
KEYWORDS    RefSeq.
SOURCE      Selenomonas noxia
  ORGANISM  Selenomonas noxia
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Selenomonas.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Selenomonas noxia"
                     /db_xref="taxon:135083"
     Protein         1..348
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38444
     Region          1..345
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mklvvniekr lrsftlaanf tltdttlall gasgsgksmt lkciaglerp drgqillngr
       61 tlydsekgin lppqargvgy lfqnyalfpn mtvheniifa ldgtreeker ilaenvarfs
      121 legienaypa rlsggqqqra afarilarga dlllldepls aldthlkwqi etalreilsa
      181 qnlaailvth drdeafriaq eiavvdrgrl tppidkhelf rrpgtraati ltgcknisaa
      241 rradaehvea tdwgitlrta estsdvqhia irahslmpaq tdgenvfpar vteviestft
      301 yivmlrfadg avpirwetdk avwrslhaae gavlhfrfpa eelmllad
//
LOCUS       WP_006694214             380 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Selenomonas noxia].
ACCESSION   WP_006694214
VERSION     WP_006694214.1
KEYWORDS    RefSeq.
SOURCE      Selenomonas noxia
  ORGANISM  Selenomonas noxia
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Selenomonas.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Selenomonas noxia"
                     /db_xref="taxon:135083"
     Protein         1..380
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41916
     Region          1..268
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          265..354
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrfihtadwh lgklfgqrhm tedqayvlee llalckdvrp dalviagdvy draipppeav
       61 elfneiltrl aaqgirvlfi agnhdsavrl gfgaqllras giylagavrs aeppvilsdk
      121 hgdvyfslip ygdpphvrea falnenvsfd galvvqiaaa raqipssars vavahafvig
      181 gqtsesehal svggsdhvsa ehfaaysyta lghlhapqra gaenvrysgs llkysfdeah
      241 qkkgielvel naagaashtf ypltprhdvr ivrgmmdeim tdtdplphdd yicvelfdtd
      301 avlaaheklr riypnlftit rpninvnrls stersyergk sdlhlfsdff aevtdeqmte
      361 terdelirii dsmeqgerae
//
LOCUS       WP_006694420             303 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Selenomonas noxia].
ACCESSION   WP_006694420
VERSION     WP_006694420.1
KEYWORDS    RefSeq.
SOURCE      Selenomonas noxia
  ORGANISM  Selenomonas noxia
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Selenomonas.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 303)
  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 303)
  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 303)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Selenomonas noxia"
                     /db_xref="taxon:135083"
     Protein         1..303
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31846
     Region          2..67
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          188..251
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mvgdilrkar ekqgltiadi eegtsirkly iehiergnid alpgmvyakg fvrnyaaflh
       61 ldaehlvqqf aeengappap vpaepetkpr rislssvgde slsqisiggr rssyagifgk
      121 lalgiivlaa lvgggaalis ainspaketa apaptkteqp aptsvaaead asdaartaaa
      181 saqdvrvsvh lterswmevq vdgnvvlegi iesgrtenwq andaiiirag nagalevtan
      241 gkklgrfgne gevverrftk etkdlrdtlp papsqeapaa qqgqsratga kdargtkgtr
      301 nqq
//
LOCUS       WP_006697273             382 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Bradyrhizobium lupini].
ACCESSION   WP_006697273
VERSION     WP_006697273.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium lupini
  ORGANISM  Bradyrhizobium lupini
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 382)
  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 382)
  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
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 382)
  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   5  (residues 1 to 382)
  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   6  (residues 1 to 382)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 382)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 382)
  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 15726307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Bradyrhizobium lupini"
                     /db_xref="taxon:136996"
     Protein         1..382
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42302
     Region          16..>77
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          83..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 mntdqrqhpn fdrqplasan erhildivrr hgpiprawit ghtnltqqsv hrliegllkr
       61 gllqasapik gtrgqpspti elvpeaaysl gvsintdsvv iciadfrcdv iveeklkmlp
      121 edreetlaal alalerlqae hgiprerllg lgfsmsgffv sedrafnape plrdwslmdl
      181 kpvlekrfhl pvwlennatt gaigeslrgv gswcqtfayl sfnygfgggl ilggqpfhgf
      241 hgnagefsgi yspdespkrp alqyliatlq kngvdihsie plyqqfdptw pgveewldet
      301 mpqvdrlvas liavldpqai vfggqlpral gqmmikrthm psqrehrygv gpkeaklvls
      361 etkgdpsaig aallplrvry fl
//
LOCUS       WP_006697287             408 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Bradyrhizobium lupini].
ACCESSION   WP_006697287
VERSION     WP_006697287.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium lupini
  ORGANISM  Bradyrhizobium lupini
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 408)
  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 408)
  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
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 408)
  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   5  (residues 1 to 408)
  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   6  (residues 1 to 408)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 408)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 408)
  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 15726307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Bradyrhizobium lupini"
                     /db_xref="taxon:136996"
     Protein         1..408
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42661
     Region          25..>107
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          87..351
                     /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 mtvhtvdayp vaigknpers rehnrrvvld ivrrhgslgr aeiakithlt pqavanivde
       61 lmgeellkel grrrsgrgqp piqfsvnpdg gatigveiaa dhmvtvgldl agvlrtqrit
      121 plsdttpeai fktfaaehdg vaknlgcrll gtgvvmpgpf eidgmtsvgp ttlsgwggid
      181 arqmlgeacg qpvvvendat aaavgerlfg aglaipnfcm iyfgvgiglg iiqdgapyrg
      241 afgnageigh vtvsprgrpc pscgqrgcle ayasvyvlke klvcagvadt elddlealfk
      301 aghpvvrewi deaaahlapm vamlenildp qtvilggalp eviigeiiar mgplptsvas
      361 rrqrelprvi hgksgqltaa lgaaalplfd ivtpkletsm gaaaqapg
//
LOCUS       WP_006699239             409 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Bradyrhizobium
            lupini].
ACCESSION   WP_006699239
VERSION     WP_006699239.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium lupini
  ORGANISM  Bradyrhizobium lupini
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 409)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 409)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Bradyrhizobium lupini"
                     /db_xref="taxon:136996"
     Protein         1..409
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=45301
     Region          5..394
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mpkftvldvr lygepvatlt nlqdgrtifa fndpyiedek rptlslslkd pfgalitkfr
       61 pyntvvppff snllpegplr kyladragvk psreffllwm lgrdlpgavt vhpsegddap
      121 pddeqaivea rpnalrfsla gvqlkfsafk ndkkggglti paegtggswi vklpsqqysg
      181 vpenefammt iarmmgmdvp elqlvdldav sglpqgvgel hgqalaikrf drtpegavhv
      241 edfaqvfgvf pdhkydrgny rmigrvlgie tstadvaefi rrlvfstlig ngdmhlkncs
      301 liypdrrtpa lspaydllst ipyiegedta alnfsrtkkm aalskdelth laakaelsek
      361 lvidtaretv erfrtvweae kknlpmaakv ietidthapk velyrefak
//
LOCUS       WP_006699572              98 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein
            [Hyphomicrobiales].
ACCESSION   WP_006699572
VERSION     WP_006699572.1
KEYWORDS    RefSeq.
SOURCE      Hyphomicrobiales
  ORGANISM  Hyphomicrobiales
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Hyphomicrobiales"
                     /db_xref="taxon:356"
     Protein         1..98
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10810
     Region          1..97
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mkkadaiskl kqhaqavesm gatslylfgs tardeaiass dldifidydp grrfslldlv
       61 gikqfleeel avevdvttrn slhpllrndi eqsavrif
//
LOCUS       WP_006699921             195 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Hyphomicrobiales].
ACCESSION   WP_006699921
VERSION     WP_006699921.1
KEYWORDS    RefSeq.
SOURCE      Hyphomicrobiales
  ORGANISM  Hyphomicrobiales
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria.
REFERENCE   1  (residues 1 to 195)
  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 195)
  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   3  (residues 1 to 195)
  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   4  (residues 1 to 195)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 195)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Hyphomicrobiales"
                     /db_xref="taxon:356"
     Protein         1..195
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21668
     Region          4..194
                     /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"
ORIGIN      
        1 mtlrdltilv idenairasi ieeglreagy qrvtvihevn gvartietlq pdvifidlen
       61 pnrdmmehlf qltrtvgrpi amfvdrsdta sieaaveagv sayvvdglkk ervkpildma
      121 vsrfnafsrl qreladaksa leerkviera kgilmkmrgl seeeafallr qtamnekkki
      181 seiaqsvvta agllm
//
LOCUS       WP_006700359             151 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Bradyrhizobium lupini].
ACCESSION   WP_006700359
VERSION     WP_006700359.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium lupini
  ORGANISM  Bradyrhizobium lupini
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Bradyrhizobium lupini"
                     /db_xref="taxon:136996"
     Protein         1..151
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=15295
     Region          63..138
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mkinvialat aaalsssvaf aqtaatapaa gadatlsgpg itmgtkatgp lkfvnvqktd
       61 ltasqldgmd iynaqnenig eiedvvigdg kaviglvasv ggflgidksy vvldpasvav
      121 hndngtwkaf vdttkdalqn apkldydkld d
//
LOCUS       WP_006700988             458 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Falseniella ignava].
ACCESSION   WP_006700988
VERSION     WP_006700988.1
KEYWORDS    RefSeq.
SOURCE      Falseniella ignava (Facklamia ignava)
  ORGANISM  Falseniella ignava
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Falseniella.
REFERENCE   1  (residues 1 to 458)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Falseniella ignava"
                     /db_xref="taxon:137730"
     Protein         1..458
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=51231
     Region          73..187
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          <249..309
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          335..458
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(411,413,431..434,436)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mrktlgtiva sfiivlviym agigfyadrf vpmtqfyhid isnltmaqae qkiekelgqr
       61 qftlteaekt lgqldlssma ptfkvdkelk elfyqqnpnv wlskllepdq agteleevel
      121 dqealveqlk kigidntkre pvqeaqikyd kksgyysvpg krgtkvdpll mkeaiaqaii
      181 enkdsisles tyerplnegn sevidevldt idriasvsit yelageeiti pkqeieswly
      241 fgegndlivd eeavraylve lddkyatfnk yrefestwrg vvtvepgilg wgidietetr
      301 nlvndvqsgh dvtrtpalvs vgnyagqade igptyieidl anqymflyvd hqlvvetpiv
      361 sgqpgaetvp gagaviemlt dtklrgtnpf lnvdyatpvk ywirfddkdq gihdaswqga
      421 yggdvwtyag slgcintpld avitiynyvt ygtpvivf
//
LOCUS       WP_006701327             202 aa            linear   BCT 20-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Falseniella
            ignava].
ACCESSION   WP_006701327
VERSION     WP_006701327.1
KEYWORDS    RefSeq.
SOURCE      Falseniella ignava (Facklamia ignava)
  ORGANISM  Falseniella ignava
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Falseniella.
REFERENCE   1  (residues 1 to 202)
  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 202)
  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 11443421
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Falseniella ignava"
                     /db_xref="taxon:137730"
     Protein         1..202
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=22241
     Region          <113..202
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          158..201
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
ORIGIN      
        1 mpkdnendyr gtegmnhdsp sqsaqepwdn kfeednlker qfsrsvrnqp akearnlskv
       61 llliiivgfi tpfllyiivn ggkkndqiat rpatevridr nsttkeetke ttaneitlat
      121 revtneties ttaqpqttqa ppaeptpapq tpsqgsgtyt vqagdswfai arnygidvyq
      181 laqfngasid splfpgdtiq ip
//
LOCUS       WP_006701956             195 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Falseniella ignava].
ACCESSION   WP_006701956
VERSION     WP_006701956.1
KEYWORDS    RefSeq.
SOURCE      Falseniella ignava (Facklamia ignava)
  ORGANISM  Falseniella ignava
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Falseniella.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Falseniella ignava"
                     /db_xref="taxon:137730"
     Protein         1..195
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=22974
     Region          8..194
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mntlkeyiqe nliitnkeae elgytrhnls eltkcgqler lrpglyqlkg kviddfvlis
       61 snsnriifsy qtalylhdls drtpnvfhis vpqgynashi kkryedlqvh yvkkdlyeig
      121 kteikspqgn pipvydiert vcdiiidrek idkqifteai kryfksqnkn lrrlikygrl
      181 fkiedeirky mevls
//
LOCUS       WP_006704826             212 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Candidatus Regiella insecticola].
ACCESSION   WP_006704826
VERSION     WP_006704826.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Regiella insecticola (Candidatus Adiacens aphidicola)
  ORGANISM  Candidatus Regiella insecticola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; aphid secondary symbionts;
            Candidatus Regiella.
REFERENCE   1  (residues 1 to 212)
  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 212)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 212)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Candidatus Regiella insecticola"
                     /db_xref="taxon:138073"
     Protein         1..212
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23748
     Region          1..212
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 meiytteneq adavrrffse nakilvvsvl liitvligwh ywqnnqntam knaassyqqv
       61 seiltdnkka avtksddntn dvaeqfvren dnnyavfial elanrfvvqk ifdkaeqqlm
      121 laltktkdtn llsltnlrla klqlqlkkpd qalktlnsve geawvamaed vrgdiflnkg
      181 dipaaraayt katevnaaqt lqtllrlkld nl
//
LOCUS       WP_006705648             212 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Candidatus Regiella insecticola].
ACCESSION   WP_006705648
VERSION     WP_006705648.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Regiella insecticola (Candidatus Adiacens aphidicola)
  ORGANISM  Candidatus Regiella insecticola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; aphid secondary symbionts;
            Candidatus Regiella.
REFERENCE   1  (residues 1 to 212)
  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 212)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 212)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Candidatus Regiella insecticola"
                     /db_xref="taxon:138073"
     Protein         1..212
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23819
     Region          1..212
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 metytteheq adavrrffse nakilvvsvl liiavligwh ywqnnqntam knaafsyqqv
       61 seiltdnkkt avtksddntn dvaeqfvren dnnyavfial elanrfvvqk lfdkaeqqlm
      121 laltktkdtn llsltnlrla klqlqlkkpd qalktlnsve geawvamaed vrgdiflnkg
      181 dipaaraayt katevnaaqt lqtllrlkld nl
//
LOCUS       WP_006710162             204 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Vibrio ichthyoenteri].
ACCESSION   WP_006710162
VERSION     WP_006710162.1
KEYWORDS    RefSeq.
SOURCE      Vibrio ichthyoenteri
  ORGANISM  Vibrio ichthyoenteri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 204)
  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 204)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 204)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Vibrio ichthyoenteri"
                     /db_xref="taxon:142461"
     Protein         1..204
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22101
     Region          1..202
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 melydteeqq veaikdwwke ngkavifgav iglgglfgwr fyqdttleaq eaasasytka
       61 meslaatgaq aetqvqsfie angeseysil aalqlakvqv eanqldeait qlqwakdatq
      121 dqallavinf rlarlqaeqg dfdsaiaqla nitdagwtgr veelkgdill rkgdaegaya
      181 ayteaqqagd atevlkmkld dlak
//
LOCUS       WP_006708476             206 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Serratia symbiotica].
ACCESSION   WP_006708476
VERSION     WP_006708476.1
KEYWORDS    RefSeq.
SOURCE      Serratia symbiotica
  ORGANISM  Serratia symbiotica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 206)
  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 206)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 206)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Serratia symbiotica"
                     /db_xref="taxon:138074"
     Protein         1..206
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22586
     Region          1..204
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 mevytteneq vdalrrffae ngkalavgvv lgiaalvgwr ywqnhqsvdl maasqsyqev
       61 sdrlaagkpd dvaaaekfvq ansnsysvla alqlakhfve qndvakaeqq lvqaqsqtrd
      121 dnllsqinlr larvqlqekk wdhalktlde vkdagwaalv qdtrgdvlla kgdaqgahea
      181 yskglesnvs qalevllrik lnnlsn
//
LOCUS       WP_006710987             122 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit, partial [Vibrio
            ichthyoenteri].
ACCESSION   WP_006710987
VERSION     WP_006710987.1
KEYWORDS    RefSeq.
SOURCE      Vibrio ichthyoenteri
  ORGANISM  Vibrio ichthyoenteri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 122)
  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 122)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 122)
  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   4  (residues 1 to 122)
  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   5  (residues 1 to 122)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Vibrio ichthyoenteri"
                     /db_xref="taxon:142461"
     Protein         <1..122
                     /product="TRAP transporter small permease subunit"
                     /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]"
     Region          <1..114
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 flfsavflig vpyaikaggh vrvdlfyerl snkaqaiidl lgtvffllpf cllvawygvd
       61 fakesyalge tsgdpgglpy rwiikgmipl sflfmavsgi glmlhslnri vnphlmhaqa
      121 sk
//
LOCUS       WP_006712280             157 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Vibrio ichthyoenteri].
ACCESSION   WP_006712280
VERSION     WP_006712280.1
KEYWORDS    RefSeq.
SOURCE      Vibrio ichthyoenteri
  ORGANISM  Vibrio ichthyoenteri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Vibrio ichthyoenteri"
                     /db_xref="taxon:142461"
     Protein         1..157
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16946
     Region          2..151
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mkiehyqrlt kqalallese snfianlsnl sallnmelid lnwvgfylme egelvlgpfq
       61 gkpacvripl gkgvcgtaaa tntvqrvydv hefaghiacd aasnseivip fsingkiagv
      121 ldidspnigr fseedeqglt flmaevenll nshaika
//
LOCUS       WP_006712659             815 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Herbaspirillum frisingense].
ACCESSION   WP_006712659
VERSION     WP_006712659.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum frisingense
  ORGANISM  Herbaspirillum frisingense
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 815)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 815)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 815)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..815
                     /organism="Herbaspirillum frisingense"
                     /db_xref="taxon:92645"
     Protein         1..815
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87447
     Region          87..135
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          114..815
                     /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 mrhqslrsta tthrargttg atrplralst tahvlmagsl llagvalvmp asaatpvaae
       61 qslplsipag pldqslnrla asarrllvvd pallrgrqap avegnlsvsr aleqllsgsg
      121 lvadqredgs ihvrklpaqs sslpaltvva tsavdpgagl qrpassgalg srslletpfs
      181 itvvdkddiq erqvttveqa frydpsvtsa sgeygrgssl lvrglgiddt ngfkmdglal
      241 pgwgndllpm evfervellk glsgfmygfg spggimnyvl krptdenlfa vdvgyktgsl
      301 fskhidmggr agddqrlgyr inlvqeqggt yfkggsldrt vaslatdlrl tqdlklsfdt
      361 vyarrksngn afwgmslasg ldlptaidpr trqqpegayf snenivvstg lewqlnpdwk
      421 ssfnyryare dvdyvygdis indalgnttt qvygglysfq yqqlqamleg klktgaighq
      481 lvfgasrqqy evlsdrasts talgsgniys dsrlsvggis naghsqyrgs eivqnalfas
      541 dtlslgeqws ligglrytrf dqrgynrvgv qtttyqrspv tptvalmfkp laglttyvsy
      601 vealerggta gettanagev mpplkskqie agvkveqanw sataavfrmq raaeyvnaan
      661 tlvqdgetry qgldlsgrya ltpalnlegg lmwldakyqs dsadlagkqv vgaprmqata
      721 gvryrvagva glsvngglrh vgrskldtga pqrelsaytv mdvgavyrtr lsgkdvtfna
      781 qvqnladrry wvyngdsyif agaprtlsln arvef
//
LOCUS       WP_006713400             265 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio ichthyoenteri].
ACCESSION   WP_006713400
VERSION     WP_006713400.1
KEYWORDS    RefSeq.
SOURCE      Vibrio ichthyoenteri
  ORGANISM  Vibrio ichthyoenteri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 265)
  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 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   3  (residues 1 to 265)
  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   4  (residues 1 to 265)
  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 265)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Vibrio ichthyoenteri"
                     /db_xref="taxon:142461"
     Protein         1..265
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30401
     Region          20..262
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <164..262
                     /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 mdrvkysnti sesinlidar yqqfafqrhy hldfhiglit qgeqrfhhqg qqhhigqgqv
       61 vimapdelhd gnsvlergyq tkvfaidpnw ltqlaqytqp dqilsfrqti isntaifnql
      121 yqlhlllgdd sqsqlakdcl plegfdqlfa qfgygqqekv tplghqsiat lksfildnlg
      181 qairleqlan lchltptqfq rhfkmqmgit pyawlsrlrl ehamrllqqg hnatyvahqv
      241 gfydqahfsk afksnfgvpp tqine
//
LOCUS       WP_006714091             271 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio ichthyoenteri].
ACCESSION   WP_006714091
VERSION     WP_006714091.1
KEYWORDS    RefSeq.
SOURCE      Vibrio ichthyoenteri
  ORGANISM  Vibrio ichthyoenteri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 271)
  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 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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Vibrio ichthyoenteri"
                     /db_xref="taxon:142461"
     Protein         1..271
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29735
     Region          17..271
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <175..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 msndktvqlk sssdkilspr paelvtlpsy mdchdhsytq iviglkgqae fevngygnlv
       61 gpgqgcvvts gsghafggvi gqsdilvlnm psachqdplm lqklnelnqa dvyfqldgqi
      121 qkliqmlvae mhaspedlll sracndtvma llhrhisalq isrkesrfdl eaidryierh
      181 isykisvaql agsvflgesq fhslfkeqlg itphqyvlsk ridmakqlie qghltlgqva
      241 elsgfsgqst fahafarlqg ispsqykkqi s
//
LOCUS       WP_006715266             199 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Desulfitobacterium
            metallireducens].
ACCESSION   WP_006715266
VERSION     WP_006715266.1
KEYWORDS    RefSeq.
SOURCE      Desulfitobacterium metallireducens
  ORGANISM  Desulfitobacterium metallireducens
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfitobacteriaceae; Desulfitobacterium.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Desulfitobacterium metallireducens"
                     /db_xref="taxon:142877"
     Protein         1..199
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=22781
     Region          8..>65
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 msevkilgef yfsqilnkpi ldaqgrrvgr vrdmvmrwds laphvtgikt akgaqavipi
       61 elvsfmnhre irlsvdfssn itvplqedet figkwlldkq iidlegsklv rvndltlswi
      121 trnhkqimvl vavdiglrgv frrlgveflv rrvknnflgw qyikplesrs salqitreke
      181 qlrelhpadi adlletmgy
//
LOCUS       WP_006716279              74 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Desulfitobacterium metallireducens].
ACCESSION   WP_006716279
VERSION     WP_006716279.1
KEYWORDS    RefSeq.
SOURCE      Desulfitobacterium metallireducens
  ORGANISM  Desulfitobacterium metallireducens
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfitobacteriaceae; Desulfitobacterium.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 74)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 74)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 74)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Desulfitobacterium metallireducens"
                     /db_xref="taxon:142877"
     Protein         1..74
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8047
     Region          2..74
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mnvkiklfat fregrfkvee refpeesqvg dvlqslgiap eevaiclvng rdakedrile
       61 egdtlslfpp vggg
//
LOCUS       WP_006716541             398 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Desulfitobacterium
            metallireducens].
ACCESSION   WP_006716541
VERSION     WP_006716541.1
KEYWORDS    RefSeq.
SOURCE      Desulfitobacterium metallireducens
  ORGANISM  Desulfitobacterium metallireducens
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfitobacteriaceae; Desulfitobacterium.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Desulfitobacterium metallireducens"
                     /db_xref="taxon:142877"
     Protein         1..398
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43041
     Region          1..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mnilvincgs sslkyqlldt etkqpsakgl verigmpgsv lthrkaggek eiitaeitnh
       61 tiaiklvlda lvnpeygvvk dlkeieavgh rvvhggekfa qsvliddevi kaieecvela
      121 plhnppniag ieackdlmpg vpqvavfdta fhqtmppeaf iyglpyelye qykirkygfh
      181 gtshkyvsqr aaallgrple dlklischlg ngssitaidg gksvetsmgf tpleglmmgt
      241 rsgdldpaiv syimqkedlt skrvndflnk kcgvlgvsgv ssdfrdiega aeegnyraql
      301 alnvfahdvk kyigsyaavl ngadaiifta glgensatmr esiagnlsyl gveidpeknk
      361 irgqeidist edarcrvlvi ptneelmiam dtyevvkg
//
LOCUS       WP_006718712             339 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein
            [Desulfitobacterium metallireducens].
ACCESSION   WP_006718712
VERSION     WP_006718712.1
KEYWORDS    RefSeq.
SOURCE      Desulfitobacterium metallireducens
  ORGANISM  Desulfitobacterium metallireducens
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfitobacteriaceae; Desulfitobacterium.
REFERENCE   1  (residues 1 to 339)
  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   2  (residues 1 to 339)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Desulfitobacterium metallireducens"
                     /db_xref="taxon:142877"
     Protein         1..339
                     /product="aminoglycoside 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=39735
     Region          31..241
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
     Region          <206..304
                     /region_name="CotS"
                     /note="Thiamine kinase or a related kinase [Coenzyme
                     transport and metabolism]; COG0510"
                     /db_xref="CDD:440276"
ORIGIN      
        1 mlheqlaqdi inyvnrayfr rsmniqtpir vqflaqgeyn lnyllqtdsq nyvlrvntgs
       61 qmnlanqiry eyqalqllkp sgvtpipyyl ddrqkeipyg vlvmeylpga plnynadltk
      121 aaetfarihs isfnrgennf lvkanapfsa ilgevknllt ryfdcseanp evknlferiy
      181 lmgeekrkee syflkepwra vintevnshn fivnqekksc hlidwekpiy gepaqdlsmf
      241 lirtttlwka nvllsaeqed lflkrytqel iscpyvktlp ervqifkffn tlralswcam
      301 awteytkper plinedtfek inmyldpnfi kgcfpeifk
//
LOCUS       WP_006719011              74 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Desulfitobacterium metallireducens].
ACCESSION   WP_006719011
VERSION     WP_006719011.1
KEYWORDS    RefSeq.
SOURCE      Desulfitobacterium metallireducens
  ORGANISM  Desulfitobacterium metallireducens
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfitobacteriaceae; Desulfitobacterium.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 74)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 74)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 74)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Desulfitobacterium metallireducens"
                     /db_xref="taxon:142877"
     Protein         1..74
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8176
     Region          3..73
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mdvnvklfgd lregrfeqqi thleensrvi dvikkhnlpl dkvaiclvns nnvefeqvlq
       61 ngdtvafspp vggm
//
LOCUS       WP_006720239             117 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Collinsella stercoris].
ACCESSION   WP_006720239
VERSION     WP_006720239.1
KEYWORDS    RefSeq.
SOURCE      Collinsella stercoris
  ORGANISM  Collinsella stercoris
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Coriobacteriales; Coriobacteriaceae; Collinsella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Collinsella stercoris"
                     /db_xref="taxon:147206"
     Protein         1..117
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12751
     Region          14..114
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(17..18,36..37,45,48,50..51,53,56..57,59,67,72,80)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(36,67..68,70,96)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mdahpatkes prrdegffer vyevveqipr gcvatygqva almgaprcar qvgyalhanp
       61 rpgivpchrv vfadghiceg fafggaeaqr elleaegvaf kddthvdmkr srwqagl
//
LOCUS       WP_006720394             389 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Collinsella stercoris].
ACCESSION   WP_006720394
VERSION     WP_006720394.1
KEYWORDS    RefSeq.
SOURCE      Collinsella stercoris
  ORGANISM  Collinsella stercoris
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Coriobacteriales; Coriobacteriaceae; Collinsella.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 389)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Collinsella stercoris"
                     /db_xref="taxon:147206"
     Protein         1..389
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42642
     Region          1..389
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mnvlvlnags sslkfqlmnt ktreiftkgn cekigleegi fghseggekv ketvvlpdhg
       61 tavrmvidli nehgfemdai ghrivqggwh ftdsalvddd vlakiyevap laplhnyaea
      121 gviefcreay psipnvavfd tsfhmgmpem sytyplpkev rekyhvrkyg ahgtshryew
      181 ktakemlgdr chrllschlg ngsslcaied gvcrdttmgl tpldglmmgt rcgsidpatv
      241 cylqrvggyt adevdtmmnk qsgilamyek tsdardirea alkgdekalf tldlfaykam
      301 lhsgsmifsm agvdtitfag gigendwatr qafceffewl gvrvdraknk ecvggkggvi
      361 saagssvtvv viptdeeymi sldverlak
//
LOCUS       WP_006722170              88 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein, partial
            [Collinsella stercoris].
ACCESSION   WP_006722170
VERSION     WP_006722170.1
KEYWORDS    RefSeq.
SOURCE      Collinsella stercoris
  ORGANISM  Collinsella stercoris
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Coriobacteriales; Coriobacteriaceae; Collinsella.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 88)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 88)
  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 88)
  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 88)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Collinsella stercoris"
                     /db_xref="taxon:147206"
     Protein         <1..88
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          1..86
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(18,37..38,56,59,67..68,78,83)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 idlgahglav ggeavpltpt eyaiceylar hpgqvmsraq ireavlgwes daddaaismq
       61 vsrarrklse agadpiatvw gmgykwql
//
LOCUS       WP_006722431             368 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Collinsella
            intestinalis].
ACCESSION   WP_006722431
VERSION     WP_006722431.1
KEYWORDS    RefSeq.
SOURCE      Collinsella intestinalis
  ORGANISM  Collinsella intestinalis
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Coriobacteriales; Coriobacteriaceae; Collinsella.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Collinsella intestinalis"
                     /db_xref="taxon:147207"
     Protein         1..368
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=40332
     Region          1..365
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mslsmaikkr ypgftldval evgeervall gasgcgkslt lrciagvetp degrivvngv
       61 tffdseagvn lspqerktal lfqnyqlfph mtvlenvcag magprlglgg rmdgeaarre
      121 sralrfleif gvstfadrfp tqlsggqqqr valarmlaar pgilmfdepf saldsylksa
      181 leqnlldvfs vvdrtvlyvs hdideacrlc dricvmhngr veesgtagel iarpqtlagm
      241 rltgckntsr arkvsdtvve aldwgmtfdm grevpddvay lgvrarhihr draraagelg
      301 rnsfdlhvar vsdarferlv llepplggsr sriqwkvdil daptgslpea getlrlhfda
      361 srlllvnr
//
LOCUS       WP_006724100             667 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Agrobacterium albertimagni].
ACCESSION   WP_006724100
VERSION     WP_006724100.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium albertimagni
  ORGANISM  Agrobacterium albertimagni
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 667)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 667)
  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   3  (residues 1 to 667)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Agrobacterium albertimagni"
                     /db_xref="taxon:147266"
     Protein         1..667
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=72279
     Region          1..665
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mnnldpiavf rteaaeqlev ieaglldltr nlddkaqida vfrglhtlkg sgsmfgfdql
       61 aafthhceta fdrvrkgeap atseliaavl dtqghmqall dhpngdhdav smklleqlhk
      121 avgrevsadr ktasptlaaa mqqtglrtwq ldfqlpagam ingtnplgli delrelgect
      181 igvstgslpe ldaldprqly lgwsativtd rprsdiedvf ifvmddmvmg lkdvtpqtqa
      241 adpspaevpa pqikpgetva areeqrlpan dpksqrqsdn vrvpalrlde mmdrvgelvi
      301 aqsrlsrmag saidlglrsv seeierlage lrdtmmvlrm mpvaslfsrf rrlvhdlare
      361 tgkeielvts gestevdktv idrladplvh lvrnsidhgl elpqdrvaag kpavgqvtls
      421 ahqtgsevvi tikddgrgid rarvrakaea ngliqpgqpl sdqellqqif qpgfstaekv
      481 tnlsgrgvgm dvvkktieal rgsidvksde gsgseialri pltlaiidgl lvrvgngsyv
      541 iplsaveecl qlsieedlrs rgrsfislrd dlvpflrlre lfrtgtqpdp hqkvvvistg
      601 rervglvvdq iigdhqtvik smsklhdqvs sfsgatilgd gnvalildva hliaagqqqe
      661 aqmraag
//
LOCUS       WP_006725334             195 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Agrobacterium
            albertimagni].
ACCESSION   WP_006725334
VERSION     WP_006725334.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium albertimagni
  ORGANISM  Agrobacterium albertimagni
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 195)
  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 195)
  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   3  (residues 1 to 195)
  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   4  (residues 1 to 195)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 195)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Agrobacterium albertimagni"
                     /db_xref="taxon:147266"
     Protein         1..195
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21459
     Region          6..194
                     /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"
ORIGIN      
        1 mnhldltilv idenavraai iedglreagh rhvtvalgvq giaktvetla pdviiidien
       61 pnrdmmehlf qltrsvsrpi amfvdrsdsa sieaavdagv sayivdglrk ervkpildma
      121 vsrfnafsrl qrelaeakna leerkiiera kgilmkmrgm seeeafalmr qtamnekkkl
      181 vdiaqsvvta aglll
//
LOCUS       WP_006724812             389 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Agrobacterium
            albertimagni].
ACCESSION   WP_006724812
VERSION     WP_006724812.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium albertimagni
  ORGANISM  Agrobacterium albertimagni
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 389)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Agrobacterium albertimagni"
                     /db_xref="taxon:147266"
     Protein         1..389
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42275
     Region          33..303
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mtdthpsyse ahlarptirr pillnygfsg dfedqracsa airrgsksfh laslllpgpt
       61 reaaralyaf crhsddlidd prsgmpalqr lrerldliya gdpapfacdr afarvvhdha
      121 iakpvveall dgfamdldgr rhatiddvka yatcvaasvg lmmasvmgvs draalaraad
      181 lgiamqltni ardvgedarn grlylpldwl eeqgidvaaf lenpqftpal glvvrrllde
      241 aarhyrlgha girslpkpcr hairtaalvy eaigqgiadn gydsvnhrat tglstkigll
      301 lkarsddsrw tatavrdlha stepvaralv tlsgvlresa pmqradkpts daetavgrvt
      361 dillrlhnda rletlrrrea arekaasla
//
LOCUS       WP_006725435             411 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Agrobacterium
            albertimagni].
ACCESSION   WP_006725435
VERSION     WP_006725435.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium albertimagni
  ORGANISM  Agrobacterium albertimagni
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 411)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 411)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Agrobacterium albertimagni"
                     /db_xref="taxon:147266"
     Protein         1..411
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=45872
     Region          6..402
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mpdlsvlsvr lygedigtit yvgtektlfa fndayvenrd rptlglqfkd slgdlitdfr
       61 pykiklmpyf snllpeghlr ryladradih idreffllwv lgqdlpgait vvpadgeewp
      121 deahnilege aakeaaedam rfslagvqlk fsavqsasgg ltiptsgvgg nrivklpsre
      181 fanvpenefs mmslarmvgi hvpaiglidv rsignlpdgi ekigqqafvi erfdrnedgs
      241 vthiedfaqv fnvypedkyk kasyrnlisv vasesdqddv aefirrltfn vligngdmhl
      301 knwsliypdr rnarlapayd fvstipyian dksaltfsrt keftgfttde lahlsakanl
      361 pkklvldtak etvalfmerw eaeksnlpmh qdvveaidkh lktlpvvtgk e
//
LOCUS       WP_006726519             330 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Agrobacterium albertimagni].
ACCESSION   WP_006726519
VERSION     WP_006726519.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium albertimagni
  ORGANISM  Agrobacterium albertimagni
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 330)
  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 11482063
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Agrobacterium albertimagni"
                     /db_xref="taxon:147266"
     Protein         1..330
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=35427
     Region          36..330
                     /region_name="PRK06132"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:235709"
ORIGIN      
        1 mrnkergrrd fisglaalaa vagpggtlag evmkeiaalk pgeftwhpeh qrtgpvavvv
       61 slpeqrvhvy rngiriavst cstgkpghet ptgvfvvlqk dkhhksstyd dapmpnmnrl
      121 twsgialhag nlpgypashg cvrlpmafse rlfdithlgt pviiagstqd pqalthpgmv
      181 lgayaarefs davtalhgkq rpndwtdlsk qpvvsvimst fdgkallven seiraegrit
      241 vngrdklgsh vflldgldea trgmrwiafa npnddegvvn maanllaris adptfvstmq
      301 rllhpgavli ltdaplapdt rtgkdfvima
//
LOCUS       WP_006726630             633 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Agrobacterium albertimagni].
ACCESSION   WP_006726630
VERSION     WP_006726630.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium albertimagni
  ORGANISM  Agrobacterium albertimagni
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 633)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 633)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 633)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Agrobacterium albertimagni"
                     /db_xref="taxon:147266"
     Protein         1..633
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68518
     Region          6..633
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mqqidhqpsa gpkdarslfl lalgsvgvvy gdigtsplya frealkpigv dgitrveiig
       61 lvslmiwslt iivtlkyvlf llradndgeg gtlsllalls ktanghgpvl mvlgligaal
      121 flgdsmitpa lsvlsavegl klvapdmsdy ivpislaili glfavqsrgt gavarffgpi
      181 tavwfivmaa ggimhifddi gifsafnpwy avsfllregf lgiivlgavf ltvtgaealy
      241 adlghfgrkp iqlawfalvf palvlnylgq galvlsdpst asdpfflmfp swallpivil
      301 atfatiiasq avitgafslv rqaihlgflp rmqilftset qsgqiylpsv ntlllvgvls
      361 lvllfessea lataygisvt gamvvttvma fefvrkrwnw slalaaavlt pllllelvfl
      421 ganllkihdg gyipvlfaaa ftvvmwtwrr gtailfqktr rddvpleafi amiekkgehg
      481 ptcvagtaif ltsdptcapa almhnlkhnh viherniilt irtlgrpria evdrfaveel
      541 serfsrveir fgfmetqnvs ktlaslrrgg lkfdimstsf ylgrrklvag qgmgmphwqd
      601 rlyialaeaa adpsdyfrlp anrvielgsh vii
//
LOCUS       WP_006726737             395 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Agrobacterium
            albertimagni].
ACCESSION   WP_006726737
VERSION     WP_006726737.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium albertimagni
  ORGANISM  Agrobacterium albertimagni
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 395)
  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 395)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Agrobacterium albertimagni"
                     /db_xref="taxon:147266"
     Protein         1..395
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45851
     Region          1..392
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 msipvpntla rkiflerqgl srspsralgr qglydlihdl gfvqvdsiqw verahhqilf
       61 srnqtyrpkd lqhllekdrs lfehwthdas vipsaffpyw khrfvrreer irqnwakwqg
      121 egfdqafeet yarirdhgpv mardvkaedh ksggwwnwhp sktaleflwh tgklsiarre
      181 gfqkvydlse rvipaehhaa evehdafvdw acraaltrlg fatsgeiaaf fdivtpdeak
      241 awviahrdel qelaletidg kprasfafad nvaslldtpe pparirvlsp fdplirdrnr
      301 terlfgffyr ievfvpepkr qygyyvfpll egdrligrid mkaerkegvl nirrlwlepg
      361 vkptagrldk leaelqrvar fagmeavrlq pgwlg
//
LOCUS       WP_006727097             828 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Agrobacterium albertimagni].
ACCESSION   WP_006727097
VERSION     WP_006727097.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium albertimagni
  ORGANISM  Agrobacterium albertimagni
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 828)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 828)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 828)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..828
                     /organism="Agrobacterium albertimagni"
                     /db_xref="taxon:147266"
     Protein         1..828
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89980
     Region          68..119
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          98..828
                     /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 mghgirrrvf ngkvralata llvstaigvg ltapvdqafa qssaqssfsv pagplhnalt
       61 vfgrqaglqv tylsaaangk tspgfsgsat reqalaeila gsgltysfpn agtvaisapa
      121 sgadnvaadg stqlntievq genawgpvdg ivatqsatgt ktgtplkntp qavnvvtrdq
      181 meaqgaatvt qvlrytpgvv aqysdtdvrh dwltvrgfvp gryrdglrlp fgargysqpk
      241 iepyglerae ilkgpasvly gqglpggmln mvskrprdee irevelqygs hdrfqaafdv
      301 ggkldeegtl lyrmvgvgrl sdtqydyvee rkgyiapslt fqpdegtslt ilgeyqnids
      361 pggggapalt angtlytnvy aelprdaflg epgydrfrne qafigyefah efdetwtfkq
      421 nlrygyvdtd tqrvqaycls aascnpssly ryawafpess rlftvdnqai arfatgdmsh
      481 taifgldysf edsrfeesal svitrpfnvy dpvygatsit rpatalridq drsqagiyaq
      541 dqiewgnavf slggrydwan tetrertssk datveqkdgk ftwrtglvyn fdngfspyas
      601 ystsfnpasg tsrlavpfdp ttgeqfevgl ryqpegmnsf islsayqltq qnvltpdpvn
      661 tsyrvqtgev rmrglelegk aelndafsvi asyaytdsei trdnpnssgi snqgkrlafv
      721 peqqaalwld ysiqsddawg glsfgggary vgqtygdnan vydvpgytlf daairydfgk
      781 adpkleglka slnvsnlfdk kyvsscigtt gcywgegrti ygtlkysw
//
LOCUS       WP_006727971             131 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein
            [Rhizobium/Agrobacterium group].
ACCESSION   WP_006727971
VERSION     WP_006727971.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium/Agrobacterium group
  ORGANISM  Rhizobium/Agrobacterium group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Rhizobium/Agrobacterium group"
                     /db_xref="taxon:227290"
     Protein         1..131
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=14708
     Region          23..99
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mlhenrntaa sqdpyvkdtp sliasdkveg tavygrdgdr igsiqrvile kkggrvayav
       61 lgfggfwgig ddyyplpwek ltydesldgy ridltkeqve gapratddsd dwyrnngrsv
      121 ydyygvppyw i
//
LOCUS       WP_006728053             380 aa            linear   BCT 20-JAN-2025
DEFINITION  threonine synthase [Agrobacterium albertimagni].
ACCESSION   WP_006728053
VERSION     WP_006728053.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium albertimagni
  ORGANISM  Agrobacterium albertimagni
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 380)
  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 380)
  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   3  (residues 1 to 380)
  AUTHORS   Parsot,C.
  TITLE     Evolution of biosynthetic pathways: a common ancestor for threonine
            synthase, threonine dehydratase and D-serine dehydratase
  JOURNAL   EMBO J 5 (11), 3013-3019 (1986)
   PUBMED   3098560
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10107605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Agrobacterium albertimagni"
                     /db_xref="taxon:147266"
     Protein         1..380
                     /product="threonine synthase"
                     /EC_number="4.2.3.1"
                     /GO_function="GO:0004795 - threonine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009088 - threonine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39844
     Region          21..347
                     /region_name="Thr-synth_1"
                     /note="Threonine synthase is a pyridoxal phosphate (PLP)
                     dependent enzyme that catalyses the last reaction in the
                     synthesis of threonine from aspartate. It proceeds by
                     converting O-phospho-L-homoserine (OPH) into threonine and
                     inorganic phosphate. In plants; cd01563"
                     /db_xref="CDD:107206"
     Site            order(39,44..45,68,91,107,110..111,117,133..139,141..143,
                     155..156,192,303..305,307..308,343)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:107206"
     Site            order(74,100,206..210,341)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:107206"
     Site            74
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107206"
ORIGIN      
        1 mvyrravgrp pvgsdrslps lwryadslpf drqdaislge gltpllpapk lgaaigvpgl
       61 lvknegnnpt wshkdrfstv aitaavqsga klvatsstgn agaslaayaa raglpcvvat
      121 lagsagpmlt qirkygaevv pfenksdrwt flaegvakfg wfatspyrhp vvgshpigie
      181 gyktiafeiv eqmggkapdw calpvcygda lagvwlgfre mlqrgaidrm pkllaaevhg
      241 sleqaiaqqt dripdmpaaf dalavsigat rstfqalkal retkgaalai snaglvslqe
      301 kvaateglfl elsstipiaa irearqrgii dcdetvvavv tasglkdtdr saspdtaspf
      361 gdvesalsvf angglhrhrp
//
LOCUS       WP_006728335             189 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit, partial [Agrobacterium
            albertimagni].
ACCESSION   WP_006728335
VERSION     WP_006728335.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium albertimagni
  ORGANISM  Agrobacterium albertimagni
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 189)
  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 189)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 189)
  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   4  (residues 1 to 189)
  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   5  (residues 1 to 189)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Agrobacterium albertimagni"
                     /db_xref="taxon:147266"
     Protein         <1..189
                     /product="TRAP transporter small permease subunit"
                     /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]"
     Region          24..189
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 agirddetrt aqafraggkl mlqalqtyvr ivdafnrrvg rivmygvfvm mgillyssis
       61 kglflpahwt lemaqfvmag yyllggaysl qldshvrmdl lygrwspktk avvdvitimm
      121 lfvylffllw ggvsstsyal qygetsyssw spymapvkiv mvigifltfl qatsifikdl
      181 avamgrpia
//
LOCUS       WP_006729768             393 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Lactobacillus iners].
ACCESSION   WP_006729768
VERSION     WP_006729768.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 393)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..393
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=45384
     Region          130..230
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          267..393
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(344..345,348,366..369,371)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mrkkarsykf sliillllsf llvifllian nkrkhnrikq inqtviynkt hfnpcvkiyg
       61 vdvskltidq ayrkvnkkav nalmidgrdi klirkdfeti trkkvedyfn eqktrlpnyq
      121 kyifrnkell dlkgkaknia dakvvfeilg kkyifsrkky ypkvecynka fhflddsllk
      181 arierlnqey stlhkkyhfe tpehgmilvr nesygwains kqlieaiksa yinkhsvlkg
      241 hnfvygigys sygkgygkgn nglgntyiav sipnqeawfy khgklvlkin nivtgtaank
      301 ldatpkgvwy ihykqspsvl rgknsdgtpy asrvrywmpf tlsgcglhda awrtdwskta
      361 yikngshgcv nikpslikav wnvvekdepv viy
//
LOCUS       WP_006734858             403 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Lactobacillus iners].
ACCESSION   WP_006734858
VERSION     WP_006734858.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..403
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44679
     Region          5..400
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 memmkkilav nagssslkfk lfllkdeqvl ahgqadrigl pestfvlkla ngevyqdkte
       61 irtqedavek llswltkski vndlseiagv ghrvvaggey fahstlidqd nlqkiyelne
      121 yaplhnchea dgikafmkll pnvpqvgvfd tsihqtldqv hymyslpyey yekykvrkyg
      181 ahgtsvryvs qriasilkrp ldelnmvich lgsgvsitav kngqsydtsm gfsplagvtm
      241 ssrsgdidps alqyilgket dlnfdqmidi lnnksgllgi sgispdmrdi rkaisqgder
      301 aslarnifin rivryigayy lelqgidvia ftagvgendi girkeimnqm scyglipdyd
      361 anqingieki isapnskiva mviptneelm iardvvriak isd
//
LOCUS       WP_006734989             223 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Lactobacillus iners].
ACCESSION   WP_006734989
VERSION     WP_006734989.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 223)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..223
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=25029
     Region          95..220
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 miifnktnln ikikhfkfgy iavsivvvfa mamascvfar kntkhsstlr tskislqkkl
       61 frpypdptdl vkegewqkss ekkaypnlkk vkklvirvsv kgnrvylldn nkviytmlas
      121 cgkykngksl tplgkyqiig grgdkffnsk lnegalnwvs wtencvylfh svpicknqki
      181 nkseaaklgk qpasngcirl slpdskwlmd nvptgtpvvi kth
//
LOCUS       WP_006735481             399 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Lactobacillus iners].
ACCESSION   WP_006735481
VERSION     WP_006735481.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..399
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44050
     Region          2..396
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkkilainsg sssfkyklfn ypseevvaqg qaqriglags tfslkladgs kyeseikipd
       61 hktaiqlllt wlpkynvind lkeiagighr vvaggeifse salidkeklq qiydlsdyap
      121 lhnpyeadgi rdfmqllpgv pqvavfdtsf hhtldpvhyl yslpykyyek yrarkygahg
      181 tsvryvshra aellnkplnt lkmivchlgn gasitaikdg ksydtsmgfs pvagitmstr
      241 sgdidpsvlq yvmkkenisd fnkminilnn ksgilgisdy spdmrdirkr aaagdvkakl
      301 akdifvnrii kyigsyyvdm ggldalvfta gigeneslyr qaivdklsvl glkidekans
      361 vngekvisav dskakiliip tneelviard vvrlakink
//
LOCUS       WP_006736783             396 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Lactobacillus iners].
ACCESSION   WP_006736783
VERSION     WP_006736783.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 396)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..396
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=45757
     Region          133..233
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          270..396
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(347..348,351,369..372,374)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mrkkarsykf sliillllsf llvifllman nkrkqnqhnr irqinqaviy nkshfnpcvk
       61 iygvdvsklt idqayrkvnk kavnalmidg rdiklirkdf etitrkqved yfneqktrlp
      121 nyqkyifrnk elldlkgkak niadakvvfe ilgkkyifsr kkyypkvecy nkafhfldds
      181 llkarierln qeystlhkky hfetpehgmi lvrnesygwa inskqlieai ksayinkhsv
      241 lkghnfvygi gyssygkgyg kgnnglgnty iavsipnqea wfykhgklvl kindivtgta
      301 ankldatpkg vwyihykqsp svlrgknsdg tpyasrvryw mpftlsgcgl hdaawrtdws
      361 ktayikngsh gcvnikpsli kavwnvvekd epvviy
//
LOCUS       WP_006736052             403 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Lactobacillus iners].
ACCESSION   WP_006736052
VERSION     WP_006736052.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..403
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44575
     Region          5..400
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 memikkilav nagssslkfk lfslkdeqvl ahgqadrigl peatfvlkla ngevyqdkte
       61 irtqedavgk llswltkski vndlseiagv ghrvvaggey fahstlidqd nlhkiyelne
      121 yaplhnchea dgikafmkll pnvpqvgvfd tsihqtldqv hymyslpyey yekykvrkyg
      181 ahgtsvryvs qriasilkrp ldelnmvich lgsgvsitam kngqsydtsm gfsplagvtm
      241 ssrsgdidps alqyilgket dlnfdqmidi lnnksgllgi sgispdmrdi rkaisqgder
      301 aslarnifin rivryigayy lelqgidvia ftagvgendi girkeimdqm scyglipdyd
      361 anqingieki vsapnskiva mviptneelm iardvvriak isd
//
LOCUS       WP_006737598             381 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Lactobacillus iners].
ACCESSION   WP_006737598
VERSION     WP_006737598.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..381
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=43929
     Region          7..>346
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mmqdnipvft evkereikak densynflle gdnlhslkll ekthagkidv iyidppyntg
       61 nkdfiyddsf vdktdgyshs kwlsfmserl eiaklllsee gvifisiddh eqaqlkllcd
      121 svfgadnfia esidasnssk nnsnyiavnh eyllcyakni sgvkkgwlvk knqideferr
      181 aktllnmnls pekihnellq lvkypcfydf dhytyvdqhg vystfepggv kngnfdteil
      241 hpitgkpcvk psggwrysea tlqelvkkdg infgkdetvi prikrylhdy pmqvpkstlf
      301 fdsqattkwl kreniafdfp ksidyikhil sytqdnsatv fdffvgfrvi imtqansqvn
      361 irvlellpkf kikkmnrwca v
//
LOCUS       WP_006737841             223 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Lactobacillus iners].
ACCESSION   WP_006737841
VERSION     WP_006737841.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 223)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..223
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=25090
     Region          95..220
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 miifnknnln ikikhfrlvy iaisivvvfa mtlascvfar knskhsstlr tskislqkkl
       61 frpypdptdl vkegewqkss ekkaypnlkk vkklvirvsv kgnrvylldn nkviytmlas
      121 cgkykngksl tplgkyqiig grgdkffnsk lnegalnwvs wtencvylfh svpicknqki
      181 nkseaaklgk qpasngcirl slpdskwlmd nvptgtpvvi kth
//
LOCUS       WP_006738065             403 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Lactobacillus iners].
ACCESSION   WP_006738065
VERSION     WP_006738065.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus iners
  ORGANISM  Lactobacillus iners
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Lactobacillus iners"
                     /db_xref="taxon:147802"
     Protein         1..403
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44667
     Region          5..400
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 memikkilav nagssslkfk lfslkdeqvl ahgqadrigl pestfvlkla ngevyqdkte
       61 irtqedavek llswltkski vndlseiagv ghrvvaggey fahstlidqd nlqkiyelne
      121 yaplhnchea dgikafmkll pnvpqvgvfd tsihqtldqv hymyslpyey yekykvrkyg
      181 ahgtsvryvs qriasilkrp ldelnmvich lgsgvsitam kngqsydtsm gfsplagvtm
      241 ssrsgdidps alqyilgket dlnfdqmidi lnnksgllgi sgispdmrdi rkaisqgder
      301 aslarnifin rivryigayy lelqgidvia ftagvgendi girkeimnqm scyglipdyd
      361 anqingieki isapnskiva mviptneelm iardvvriak isd
//
LOCUS       WP_006740169              74 aa            linear   BCT 20-JAN-2025
DEFINITION  acyl carrier protein [Streptococcus urinalis].
ACCESSION   WP_006740169
VERSION     WP_006740169.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus urinalis
  ORGANISM  Streptococcus urinalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 74)
  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 74)
  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 74)
  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   4  (residues 1 to 74)
  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 10011594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Streptococcus urinalis"
                     /db_xref="taxon:149016"
     Protein         1..74
                     /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=8321
     Region          1..74
                     /region_name="acpP"
                     /note="acyl carrier protein; Provisional; PRK00982"
                     /db_xref="CDD:179197"
ORIGIN      
        1 mavfekvqei iveelgkepe evklettfed ldadsldvfq viseiedefd iqieteegln
       61 tvgdlvayve ektk
//
LOCUS       WP_006740283             505 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Streptococcus urinalis].
ACCESSION   WP_006740283
VERSION     WP_006740283.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus urinalis
  ORGANISM  Streptococcus urinalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Streptococcus urinalis"
                     /db_xref="taxon:149016"
     Protein         1..505
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55122
     Region          16..>226
                     /region_name="ROM1"
                     /note="RhoGEF, Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases [Signal transduction
                     mechanisms]; COG5422"
                     /db_xref="CDD:227709"
     Region          <28..110
                     /region_name="DMP1"
                     /note="Dentin matrix protein 1 (DMP1); pfam07263"
                     /db_xref="CDD:462128"
     Region          395..504
                     /region_name="COG3942"
                     /note="Surface antigen [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443142"
ORIGIN      
        1 mkkqkiftlm mlmavlspna nvlqayaeet naneshltse esvksvpenn esssektqts
       61 qslstdlsqs stvptsqslt kpsdsngnak tettsqsqdv nanqtsktse mpdkleetkn
      121 kkstqvpksd svsqqvipsk tvspnlsqek tntvpvvket ntqqlssaif dtinlpsvnv
      181 adayvehwss gnaythhlms krygitaqql dgylqstgih ydsnringqk llewqkisgl
      241 dvraiiaiai aesslgtagv athkganmfg yaafdsnpnf arhfndekal vkltqetilq
      301 nqnqsfaiqd qkakklsqgf ldvaldggvy ftdtsdsgkk rarimeeidr widqhggtpa
      361 ipeslklkss tsfdmvpvgf ktmkanvvin ytaatyawgq ctwyvynran elgyhydpym
      421 gnggswqhka gyttshkaev gyavsfspgq agadrtyghv aiveqvredg svlisesncl
      481 glgvisyrtf taeqasqlty vigkk
//
LOCUS       WP_006741398             333 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio antiquarius].
ACCESSION   WP_006741398
VERSION     WP_006741398.1
KEYWORDS    RefSeq.
SOURCE      Vibrio antiquarius
  ORGANISM  Vibrio antiquarius
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio diabolicus subgroup.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 333)
  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 333)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Vibrio antiquarius"
                     /db_xref="taxon:150340"
     Protein         1..333
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37495
     Region          20..201
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <152..331
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          245..327
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 myivrsgaad kfdslvselg qnpqeimaav glsaaqfrdp dtylayprla elleeaaarc
       61 kqplfgalla erqnlqslgd lpmlvsraet vgnalarvnd ylylhssgvt lnmtpqddwv
      121 rlslnidvns drgiaqlmql svshlamfia slldieashf alhltqhatl eveqskfaqq
      181 nklrfgdkfd gillkaslln akdhqdedal drhfqqhlky lqtrypnnls dqaanmigrl
      241 lstgecsver varaldlhpr mlqsklkqqe tsyrqllqqv rqdfaeqrls eniqsitdia
      301 lqlgyaetav fsrhfrswtg kspsqwrlen ris
//
LOCUS       WP_006742256             293 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Vibrio
            diabolicus subgroup].
ACCESSION   WP_006742256
VERSION     WP_006742256.1
KEYWORDS    RefSeq.
SOURCE      Vibrio diabolicus subgroup
  ORGANISM  Vibrio diabolicus subgroup
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 293)
  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 293)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 293)
  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   4  (residues 1 to 293)
  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 293)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Vibrio diabolicus subgroup"
                     /db_xref="taxon:2315253"
     Protein         1..293
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32991
     Region          27..179
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          209..292
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mhtladimqq yvenqglhdl egmkktaidg vwfyrsskgn hrqpfvyqsg iivlgqghkn
       61 ihigdtpvqy gpddylvvgv pmpleceafa tnnepllgis idisptllhk lvkkleaekf
      121 snkcldttrc glksvhmseg mldackrlms alcneldvvm lgdllleeiv yrtlvskegy
      181 vlfdlahqeg syarvakaln rvhqayheql svqtlaeean msvsafhqaf rnvtlesplq
      241 yikkvrlnka reliqlegrr vndaarlvgy tspsqfsrey krhfnetprs tka
//
LOCUS       WP_006743074             265 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Vibrio].
ACCESSION   WP_006743074
VERSION     WP_006743074.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 265)
  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 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   3  (residues 1 to 265)
  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   4  (residues 1 to 265)
  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 265)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..265
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30305
     Region          24..265
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <167..262
                     /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 meqiqyyatd hdqlslieak yqkfafqrhy hldfhlglit hgtqkfqyqg cshqvghgqi
       61 vimppdelhd ghsklesgye vnvfaiephl lsdladlsqn gqiirfneli isdpqifsql
      121 snlhallrre nlsqltkdcl pfegfnqlfd rygslarqkv vplgkqslht lkdylmanld
      181 qtvrldalse lcqlsptqfq rhfkaqtgmt pyawfarlrl eqgmkllqag wcgtdvayqv
      241 gfydqahfsk afkqtygvsp sqvar
//
LOCUS       WP_006743698             155 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Bacteroides].
ACCESSION   WP_006743698
VERSION     WP_006743698.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..155
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17067
     Region          7..155
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdaliqflid wgywgmfisa vlagsvvpfs seavlaalvh pstgldpmwc liaasignii
       61 gsstcfalgh lgkmdwlvky fhmkpekiek mqaylnrksa lmaffaflpi vgtlivvalg
      121 fmrsnfwvvl vsmsigkvlr yaiviyvaqg ifnyf
//
LOCUS       WP_006746250             816 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Thioalkalivibrio paradoxus].
ACCESSION   WP_006746250
VERSION     WP_006746250.1
KEYWORDS    RefSeq.
SOURCE      Thioalkalivibrio paradoxus
  ORGANISM  Thioalkalivibrio paradoxus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Thioalkalivibrio.
REFERENCE   1  (residues 1 to 816)
  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 816)
  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 816)
  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   4  (residues 1 to 816)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..816
                     /organism="Thioalkalivibrio paradoxus"
                     /db_xref="taxon:108010"
     Protein         1..816
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=90243
     Region          80..813
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 msdarrdrfl pdspvaeklg pdalrlacpp daldfetted ledldrvlgq dralealnlg
       61 ieiphqgynl yvlgstglgr rtlvnrmlre aaqgrpvpsd wcyindfeap hrpralrlpp
      121 glgqalrrdm qqvmeaiita latafqseay raqaqeihdd lkerderafa alrekaearn
      181 vallrtpggy tlapmrdgei lsaeefgklp eseqkateea veelkqdlrq liaqvprwqr
      241 evrerqkeln lsvssltldq hlgelrrkyq elpevqrfid avredllens eqirslgede
      301 qggpnpagqa arqlnrykvn vlvdhahhqg apviyednpt yqnlvgrveh tvqygtlvtd
      361 ftlikagala ranggylild vdrllghpfa wqalkralra helrveslet mlslastttl
      421 epepipldlk vvlvgdrlly yllqeydpef grlfkvaadf sedvrrdada trlyarliat
      481 qqragglrpl trdavarvie qaarrisdge rlslhlgsld dllreadywa gkadskrvde
      541 ahvdravdar irrlsrired vheaitrgiq lvdldgdavg qvnglsvigl gefsfgrpsr
      601 itatarlgeg evvdvereve lggaihskgv lilssylawr ystdqplsls aslvfeqsyg
      661 lvegdsasva elcallsvla aapvrqslav tgsvnqhgvv qaiggineki egffdvcsrr
      721 gltghqgvvm pasnrphlml rrdvvdavrd grfhvhavhh vdqaaelltg lpagepdeeg
      781 rwpagslhar vharldelar lrqafsargg ggddsa
//
LOCUS       WP_006747438             117 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Thioalkalivibrio paradoxus].
ACCESSION   WP_006747438
VERSION     WP_006747438.1
KEYWORDS    RefSeq.
SOURCE      Thioalkalivibrio paradoxus
  ORGANISM  Thioalkalivibrio paradoxus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Thioalkalivibrio.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Thioalkalivibrio paradoxus"
                     /db_xref="taxon:108010"
     Protein         1..117
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13180
     Region          24..117
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mmktdpdpra lstpteapsr slvraavleq lrrfkqarga efrvsrlgvf gsvardeaga
       61 esdvdvvfet ddpnlfrtah lrqeleewlg cpvdivrlrp tmnaslreri lrearyv
//
LOCUS       WP_006747700             403 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Thioalkalivibrio paradoxus].
ACCESSION   WP_006747700
VERSION     WP_006747700.1
KEYWORDS    RefSeq.
SOURCE      Thioalkalivibrio paradoxus
  ORGANISM  Thioalkalivibrio paradoxus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Thioalkalivibrio.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Thioalkalivibrio paradoxus"
                     /db_xref="taxon:108010"
     Protein         1..403
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43511
     Region          6..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mpgdllvlns gssslkfavy tvdhatgnre parrlrgqit gldatprfrv kdadgktias
       61 gdpangargf dqddafdfll dwldrepggq alhaaghrvv hggqaftdav ritdevitql
      121 qalvplaplh qphniapmri larsrpdliq iacfdtafhh tqsaverrla lpraiteqgv
      181 mrygfhglsy efiaeslasr mgraetgrvv vahlgsgasl aalrdgvsva ttmgftaldg
      241 lpmstrcgal dpgavlyllr ekamspedvt allheqsgll gisgisgdmr tlldsrepaa
      301 eeavavfvhr avreigalva mlggldhlvf tggigehasp vrericerle wlgvdidrda
      361 ngrhaeqvqs ersrvgvwii ptdeermiar hslrvlreht pil
//
LOCUS       WP_006748259             233 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Thioalkalivibrio paradoxus].
ACCESSION   WP_006748259
VERSION     WP_006748259.1
KEYWORDS    RefSeq.
SOURCE      Thioalkalivibrio paradoxus
  ORGANISM  Thioalkalivibrio paradoxus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Thioalkalivibrio.
REFERENCE   1  (residues 1 to 233)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Thioalkalivibrio paradoxus"
                     /db_xref="taxon:108010"
     Protein         1..233
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=25288
     Region          40..207
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 msmtlrrllp aavialmlwn paaaataera lvedlaaeap alnrvvlaka vaamhcavsn
       61 gtgpadrlav idfslpssep rlwifdlpgr gllleelvah gqgsgdnfat qfsnvrgshq
      121 ssiglfrtqe syygrhgysl rmdglepgin dnartraivi haadyvdpaw ierqgrigrs
      181 qgcpavrpei adavvdhlkd gqfmfsyypd qewlasseyl ncqpellasl mqp
//
LOCUS       WP_006748762             444 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Thioalkalivibrio paradoxus].
ACCESSION   WP_006748762
VERSION     WP_006748762.1
KEYWORDS    RefSeq.
SOURCE      Thioalkalivibrio paradoxus
  ORGANISM  Thioalkalivibrio paradoxus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Thioalkalivibrio.
REFERENCE   1  (residues 1 to 444)
  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 444)
  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 444)
  AUTHORS   ter Beek,J., 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 444)
  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 444)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Thioalkalivibrio paradoxus"
                     /db_xref="taxon:108010"
     Protein         1..444
                     /product="CmpA/NrtA family 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=48351
     Region          43..304
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mgnkgnsngg itrrrflggm aaaagaamlg patagrvlas aggkpetraa klgfialtda
       61 aplfvavekg ffrkhgmtdv evlkqaswgt trdnlvlgsr rngidgahil tpmpylistg
      121 avtpnnqpvp myilarlnls gqcisvgrey adlevgtdas gfkealaaka sggspvraam
      181 tfpggthdlw irywlaaagi dpnrdiativ vpppqmvanm rvgsmdtfcv cepwnmqlin
      241 qgigytanit gelwhnhpek afalradyvd anpnaalalt maimeaqmyc eepqnreeva
      301 ricsrrrwih apfddivdrm qgnfdygtgr vvenhpaqmr ywrdhasypf qshdlwflte
      361 nirwgylppd ldtrtliarv nredlwreaa gtlgvdtadi pestsrgiet lfdgkvfdpd
      421 npqayldsla lkrlagsspv payv
//
LOCUS       WP_006748969             713 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Thioalkalivibrio
            paradoxus].
ACCESSION   WP_006748969
VERSION     WP_006748969.1
KEYWORDS    RefSeq.
SOURCE      Thioalkalivibrio paradoxus
  ORGANISM  Thioalkalivibrio paradoxus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Thioalkalivibrio.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Thioalkalivibrio paradoxus"
                     /db_xref="taxon:108010"
     Protein         1..713
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=77903
     Region          47..713
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 marktilgrr sgvaqmpvrt gklalavava isgmagtgtv kaeesdaase erasvvlpri
       61 dvvapgltdv satpgavtiv tegeiketrp rstedvlrrv pgmyikredd saivtnygvr
      121 gipadqyktt vledgvpvqp gifvgnqryy nprvqrmdgv eilrgaaslr ygpassggvi
      181 nyqtrtpddg lavtgtvgsw ntrevtveag gsspsgdalf glvvtdassd gwmdkewdmt
      241 dvmikvgsai gdnqflgakf syyendaais yrgyfqdafd agatfnpapd drfetertaf
      301 dvnhewdisp dmrlktvayw mettrdywrf nvdgtttnad ghtvwnftdi legrnrdfer
      361 igvdsrlfln hsafginnma efglrymeee mhdtrpratr aaprspiavd gqglrrdrld
      421 sakswagfae nrfdvtdqls vtaglrvety eqkrkdrqtg gpadtfsnte flpglgatyq
      481 lnpalqfygs vyrafqppvv gsvigaddap tdaetsvnle lgmrgatgpw nyeaaafqmd
      541 fsnqvdpgis girnpnegsa liqgleaamg yvlpagfrld gnvtwvptae fredrvegia
      601 agnrlpyspe wvanvalsye qgplttalmy nytgsvfgtg dnrreidpen hgfsglvpsh
      661 ytvdltasyd fnprfavfga vknltderyi aglrqgiyag persfeigar yef
//
LOCUS       WP_006749013             194 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Thioalkalivibrio paradoxus].
ACCESSION   WP_006749013
VERSION     WP_006749013.1
KEYWORDS    RefSeq.
SOURCE      Thioalkalivibrio paradoxus
  ORGANISM  Thioalkalivibrio paradoxus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Thioalkalivibrio.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Thioalkalivibrio paradoxus"
                     /db_xref="taxon:108010"
     Protein         1..194
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21548
     Region          3..164
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mkifeplydr vmgwsrhrha prylaalsfa essffpvppd vmlapmaaar preglrlaal
       61 ttlfsvlggv lgyligalay elvspwivea gygermelak ewfavwgvwi vliagfspip
      121 yklftitaga lampllpfil asvigrgsrf favsllmawl gphadrhlrp ymerlgwlsv
      181 fvlvsimayl tfid
//
LOCUS       WP_006749218             272 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Burkholderia ambifaria].
ACCESSION   WP_006749218
VERSION     WP_006749218.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..272
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=31155
     Region          10..76
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
     Region          158..>206
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mlrstkalhg savrakdgdi ghvnqayfdn dwcirylvvk tedwlherqv lispycikht
       61 dsrsstlhvd ltrqqvgdsp dldthqpvsr qheieylsyy hyprywdgpn rwgmdaypts
      121 gsatlsrele agnplpsltm psdvpadapt dthlhgtsrv kgyrleatag righvsdfvy
      181 ddeawviryl aistrnwwlt nkeiliathw ldrvnwatet vstalnrdsi rhspeyddsq
      241 pvyrsdeial yqfygkhgyw lnaesstarg tr
//
LOCUS       WP_006749230             156 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Burkholderia ambifaria].
ACCESSION   WP_006749230
VERSION     WP_006749230.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..156
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=16945
     Region          30..109
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mtipnqthrp stsdtgasiv gsgtgegpgp nvmeadtlkg nklftsdrvd igkiseimld
       61 vrsgriayav lssggflgig gklyaipwsa ltldtdekcf rldvtadhvk napafdkdhw
      121 psmadeqwgs slhqfynrqp ywlatrdvvt nrppeh
//
LOCUS       WP_006749576             383 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Burkholderia ambifaria].
ACCESSION   WP_006749576
VERSION     WP_006749576.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 383)
  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 383)
  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   3  (residues 1 to 383)
  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   4  (residues 1 to 383)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 383)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 383)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 383)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..383
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40082
     Region          33..369
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(109..111,132..133,182,234,258)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mtfrirslsg ialtaailaf qtgvahaqet vikvgvavpl tgggaaygkd iengvrmavd
       61 eanaahttig gkpvkfvvas qddqsdprig vqaaqqltda qvavvighfn sgttlpaski
      121 yakagipmit psatnpditr aglgtvyrvi atdaqnagna gayaasvtka kriaiiddrt
      181 afgqgeadef ekaakanggt ivareftndk avdfsaqltk ikstnadlvf fggldaqsam
      241 lvkrmrqlgi raqflagggv mnanfiklag naaegasvwe ygqplsrlak gkqfetkfrq
      301 kygvdmlaya pfaydatwia inamqkanst kpadfngalk gtrydgitgt iaftntgdlk
      361 npsstlyevk naawqpvttq tad
//
LOCUS       WP_006751777             379 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Burkholderia].
ACCESSION   WP_006751777
VERSION     WP_006751777.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 379)
  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 379)
  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   3  (residues 1 to 379)
  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   4  (residues 1 to 379)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 379)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 379)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 379)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..379
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39982
     Region          29..365
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(105..107,127..128,177,229,253)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mqhtmkkvag atfvavmsla gtahaddvki gyagpmtgaq ahygkdmqng ialaledfna
       61 tnpkiggkpv kfmletqddq adprtgttva qklvddgikg mlghfnsgtt ipasriyana
      121 gipeiamata peytqqgykt tfrmmtsdtq qgsvagtfas kdlgmkkiai vddrtaygqg
      181 ladqfekaak aggativdre ftndkavdfk ailtklkaak pdlvyyggad sqaapmvkqm
      241 kalgmaaplm sgemvktptf lkiagnaaeg tiaslaglpl dempggksya ekykkrfged
      301 vqtyspyayd gamamlnamk kadstdpaky lpvlaktdma gvtsthvayd akgdlknggi
      361 tmykvekgew kplksiggk
//
LOCUS       WP_006751859             167 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Burkholderia ambifaria].
ACCESSION   WP_006751859
VERSION     WP_006751859.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 167)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..167
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18067
     Region          10..160
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mftlsndpha skaelyvtlv eqaralvese rdltanaanf salvyhsldr lnwagfyffd
       61 gselvvgpfq gkpacvrial gkgvcgtaaq tretqvvrdv hefpghiacd aaseseivvp
      121 lvaadgtlig vwdvdspvaa rfddedrngm ealcrvfveh awqktrg
//
LOCUS       WP_006753390             233 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Burkholderia
            ambifaria].
ACCESSION   WP_006753390
VERSION     WP_006753390.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..233
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=25245
     Region          1..>226
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msvavdirkt yasaerrftl dvsfaataqr vvlfgpsgag ksmtlqaiag llspdegtit
       61 lngeplfdsa rgidvptrar rvaflfqdya lfphlnvrqn iafgltpglr npraktappe
      121 vaywlqafel dalagqfpsq lsggqkqrva laralvaqph vllldepfaa idgamrqrmr
      181 helaelqarl dipmvlishd pddvaafgdq vvqlsegrvq aatphaewpt rvv
//
LOCUS       WP_006753625             198 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Burkholderia ambifaria].
ACCESSION   WP_006753625
VERSION     WP_006753625.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..198
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21061
     Region          8..193
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 maspsapprr livaitgatg avygvrllel lraaggveth llvsnagwln iqhelklska
       61 evesradvvh svrdvgatia sgsfatdgmv iapcsmktla svahglsdnl itraadvtlk
      121 errrlvlmvr etpfnlahlr nmtavtemgg ivfpplpafy ampktieelv dqtvtrvldl
      181 falgtpmttp wagirpaq
//
LOCUS       WP_006755370             373 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Burkholderia ambifaria].
ACCESSION   WP_006755370
VERSION     WP_006755370.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 373)
  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 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   3  (residues 1 to 373)
  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   4  (residues 1 to 373)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 373)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 373)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..373
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38575
     Region          27..363
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(103..105,125..126,175,227,251)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mrylitalsv avaagaltsa haqevvtigh sapltgpqaa ngkdnengar lavdelnkag
       61 vkvagktvtf klvsdddqad pkagvqvaqs lvdkgvvavl gpynsgvaip asrvyanagv
      121 pmlpvasnpa ltrqgfknif rigasdeqlg gtmatfaakt lnaktavvid drtaygqgva
      181 eqfanvakan gikivdqeyt sssatdflgi ltkikasnpd viffggyaaq gapmakqmkq
      241 rglrakllgg dgicsadmgk vageaasivy caqggvalek tsagraflkk yhdtyhtetq
      301 vygvnyydgm klladamvka gtttdkakli aqlaksnyag vagtysfdeh gdlkgapttv
      361 yvirnglpep yak
//
LOCUS       WP_006756002             198 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Burkholderia].
ACCESSION   WP_006756002
VERSION     WP_006756002.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 198)
  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 198)
  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   3  (residues 1 to 198)
  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   4  (residues 1 to 198)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 198)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..198
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21810
     Region          9..191
                     /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"
ORIGIN      
        1 mstpvpplrl rvllvtdtdk pigelgdala rlgyemlndv atparlpaav eeqrpdvvii
       61 dtdspsrdtl eqlavmhata prpvlmfshd adqdlihaav gagvsaylve glsaerlapi
      121 levalarfsh ddalrrrlad verelaerkl idrakrllmd qrklsehday aflrkramdq
      181 glrivdvarq lhdassqs
//
LOCUS       WP_006756459             379 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Burkholderia ambifaria].
ACCESSION   WP_006756459
VERSION     WP_006756459.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   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 379)
  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   3  (residues 1 to 379)
  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   4  (residues 1 to 379)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 379)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 379)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 379)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..379
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40001
     Region          29..365
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(105..107,127..128,177,229,253)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mqhtmkkvag atfvavmsla gtaraddvki gyagpmtgaq ahygkdmqng ialaledfna
       61 tnpkiggkpv kfmletqddq adprtgttva qklvddgikg mlghfnsgtt ipasriyana
      121 gipeiamata peytqqgykt tfrmmtsdtq qgsvagtfas kdlgmkkiai vddrtaygqg
      181 ladqfekaak aggativdre ftndkavdfk ailtklkaak pdlvyyggad sqaapmvkqm
      241 kalgmaaplm sgemvktptf lkiagnaaeg tiaslaglpl dempggksya ekykkrfged
      301 vqtyspyayd gamamlnamk kadstdpaky lpvlaktdma gvtsthvayd akgdlknggi
      361 tmykvekgew kplksiggk
//
LOCUS       WP_006756544             338 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_006756544
VERSION     WP_006756544.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 338)
  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   5  (residues 1 to 338)
  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   6  (residues 1 to 338)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38079
     Region          27..206
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          96..338
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mndaqdkgtt sislvreail vaaqrnldvs avlqhagiaa ellnaprarv palafsrlwa
       61 alsdlmddef fgldshplrr gsyalmchav lhadnlehal rrmlkflrav lddihgelrc
      121 egehavivlh ddgrtrrlfa ygtwfilvhg facwlarrri pliemrfras apsddsdyrm
      181 rfcedvtfsa eetlirfdrs fldlklsgte aslraflena panilvkyrn essttaqvrr
      241 rlrnqapddw pdldalsrll nlsaatlqrr llaegtnyrq lkdelrrdia ielfsstslt
      301 vaevaartgf qeasafhraf rkwtgaspgm yrhgkana
//
LOCUS       WP_006757159             507 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Burkholderia ambifaria].
ACCESSION   WP_006757159
VERSION     WP_006757159.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..507
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=52845
     Region          5..507
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mndrmvvilh gddnvavalr tfeagtpiev sglstiavts ipaghkmatr rivrgspvik
       61 yrqtigvaln diapgehvha hnvgmpeyhp hrpahidagh alapadrpet fqgfvredgq
      121 vgtrnyigvi asvncsasvc haiadafkgd amapfewvdg vvaithqsgc gmsatgdgma
      181 vlrrtltgya cnpnfaavll vglgcevnqv galatsvett iaapvrtlvv qdeggvretv
      241 ahgiaivrem ltaanrmtrt evpaarlkvg lqcggsdgys gitanpalga avdllvrhgg
      301 tailsetpei ygaehlltar asgvvaerll dklrwwerya gesggdmnnn pspgnkaggi
      361 ttilekslga vskggssaln avydyadrvs esglvfmdtp gydpvsatgq iagganlvcf
      421 ttgrgsvfgs kpvptiklat ttglfermrs dmdfnggeiv dgslsigqag aqlfrlmldv
      481 asgartcseq ngmgdrefvp wlrgpim
//
LOCUS       WP_006760725             403 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Burkholderia
            ambifaria].
ACCESSION   WP_006760725
VERSION     WP_006760725.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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 403)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..403
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45525
     Region          17..403
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mltlspaaar alhlaaqgll tpprrkatka dvldtirrma qlqidtihvv arspylvlfs
       61 rlgdfapqwl dehlaearlf eywsheacfl pieqfglmry kmldpsgmgw kyaaewheqn
      121 radierllar irdegpvrsa dfiredgakg ngwwdrkpek khlevlfttg dlmvserrnf
      181 qriydvrerv lpgwddardl pprdavlpal ldytcralgv vradwvadyy rlprrsyrae
      241 lehlagagel lpveiagwke payvhrslea llpaaaadtl rstvttllsp fdpvvwdrrr
      301 astlfgfdyt iecytpahkr rygyfclpvl hrgrligrid akahrvlgtf elkavhvepg
      361 vrfgtglaad vakavkrlaa whgtpdvtva happeltkal aga
//
LOCUS       WP_006760807             380 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Burkholderia].
ACCESSION   WP_006760807
VERSION     WP_006760807.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 380)
  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 380)
  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   3  (residues 1 to 380)
  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   4  (residues 1 to 380)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 380)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 380)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..380
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39635
     Region          32..365
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(108..110,131..132,180,232,256)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mnikmqkllp itaaamlcva aagnaaadqv vkighvaplt ggiahlgkdn engarlavee
       61 inakgltvgg qkvtlqldaq ddaadprqat qvaqklvddk vvavvghlns gtsipaskiy
      121 sdsgivqisp satnpvytqq gfkttyrvva tdaqqgpala nyahskgiks vavvddstay
      181 gqglanefek kakalglkvv shdatndkav dfrailtkik genpdaimyg gmdatggpfa
      241 kqakqlglra kifagdgvct ekladlagda tdnvvcseag aslekmpggs afkakyekrf
      301 gqpiqiyapf tydavyiiad amkranstdp akilaampat nytgvigttt fdakgdlrhg
      361 vislynyksg kktlldevkm
//
LOCUS       WP_006760955             424 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Burkholderia].
ACCESSION   WP_006760955
VERSION     WP_006760955.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 424)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..424
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=45890
     Region          35..254
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 msmididppg fqpprpvagd dgkrrtvlyg aytvfsvfqp vfsvshrrai gyhaslrahd
       61 eesrqvashe vftqaarrgd llelgrlaes lhlgnfhafd shdewlflsl hpaalmdtvy
      121 gdallanlka lglpphrvvl evpeqagget pryaaivdgl rkagflialg gfgakhsnid
      181 rvwhlhpdiv tldrgilaqa sehshlervl pglvsllhes gqlvlmggls terdaliale
      241 cdvdfvqgqy fagpsvdpvq pqaaagcmdt lsaalrlrva qrertqaerl apyvaaleea
      301 sqklaagepl idaagavlgl petarcflld asgrqigdnv largsvsqra krfrpllhse
      361 gaswerrpyf shamrapgrv hltppylsin eahlcvtasi aapvatgmqv lcvdinweaa
      421 lnre
//
LOCUS       WP_006761057             322 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Burkholderia ambifaria].
ACCESSION   WP_006761057
VERSION     WP_006761057.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..322
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=33829
     Region          117..192
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
     Region          <226..278
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 msgglpfpas rmsfpsstvf lvlaaaalls gcgllptqnp papisealie pveetagkpl
       61 tmppvpplvq peepeapkkp hreatrpkpv qraepptppp ppppplvatr pldrtqihal
      121 ldsevarrng kvigravdmv idasgkprem ivnlqgfmgi gdrkvifpwn vfrftpggkq
      181 epivldvpsg dlppaarpka vplsgsaaas patrlpmlds dverpngtki grvvdvlidr
      241 aaqpqaivld lgglvnpdrr siaaswgalr fvtrdkalhp qldlndaqik aappyaadkp
      301 ivavyppvap apaqassasa tr
//
LOCUS       WP_006761353             388 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Burkholderia ambifaria].
ACCESSION   WP_006761353
VERSION     WP_006761353.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 388)
  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 388)
  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   3  (residues 1 to 388)
  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   4  (residues 1 to 388)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 388)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 388)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 388)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..388
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40220
     Region          34..369
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(109..111,132..133,182,234,258)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkiaflparl afsaaaliaa vpafaqsapq tiliglaapl tgpsarigkd lqngaqlaid
       61 danakhpsig gkpvvyklva addqsdprta vavaqqlvdq hvigvvghwn tgcsvpasrv
      121 yrdagiaqia pastghqytq qgyatafrim ghddaggnft gayavktlka kriaviddrt
      181 sfgagladqf ikgmqanggt ivdrqyvndk ttdfsgvlta ikgkradlvf fggldaqaap
      241 iarrmrqlgv napllgaggf vsqtflslag kdgegvtale pglpldrmpg gnafdaqyra
      301 rwhapielha pfaydaaatl iaatqkagtt qpakvvaavr aidrpgvtgr vafdsegnlk
      361 dpaftiyqvr ggkwtvvdvl ggarpatk
//
LOCUS       WP_006761460             198 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Burkholderia
            ambifaria].
ACCESSION   WP_006761460
VERSION     WP_006761460.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 198)
  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 198)
  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   3  (residues 1 to 198)
  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   4  (residues 1 to 198)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 198)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..198
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21791
     Region          9..191
                     /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"
ORIGIN      
        1 mstpvpplrl rvllvtdtdk pigelgdala rlgyemlndv atparlpaav eeqhpdvvii
       61 dtdspsrdtl eqlavmhata prpvlmfshd adqdlihaav gagvsaylve glsaerlapi
      121 levalarfsh ddalrrrlad verelaerkl idrakrllmd qrklsehday aflrkramdq
      181 glrivdvarq lhdassqs
//
LOCUS       WP_006763028             672 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase [Burkholderia].
ACCESSION   WP_006763028
VERSION     WP_006763028.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 672)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..672
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=74551
     Region          67..542
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mektmqklda anpqamstdf tadnvarlka lfpelvtegp ngasvdvdvl kalvgdrtvg
       61 daderygfhw hgkrsarqaa ltpstgtlrp cpddsvawdd trhlmiegdn ldvmkllhks
      121 yagkvklvyi dppyntgsdf vypddfsdsi rhylsitgqa eggvkrstnt eangrfhtdw
      181 lnmmyprlkl vhallsdegl ivvhidehev halvlmlrei fgeenelgva vwdkrnpkgd
      241 argiayqhes lvlfarnaet lleraplkrp krnaqrmlda ahdamyrsgn pkdaqkayra
      301 wlkaqtnlsg gevmydrlsa dgrvyrlvsm awpnkkkapd eyftplihpv tgkpcampar
      361 gwrnppatmq allergqief gpdettqpqr iyyldenmye nvpsvlpfag sddallkalg
      421 ipfeqpkpvd faaavigwct rgddivldcf agsgstghav mqvnatdgga rryilvqlpe
      481 aldrrdkaqq aaadfctklk kpptlaeitk erlrraaqqv ardypesygd lgfrvyrldt
      541 tnviewdprr ddfdhalfas vehvktgrtd ddllaeltlk lgldlctpve hhvvagktvh
      601 ligreivacf dariarddag pladgivdll dasgatrdvt clfrdsgfvd dvaklnlaal
      661 ldqhgvkrvr sl
//
LOCUS       WP_006763493             199 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: pilin [Burkholderia].
ACCESSION   WP_006763493
VERSION     WP_006763493.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..199
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=20311
     Region          32..198
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mfeafsvslf rrlaadlqqr trrrahrgrp agftlielmi vlaivgvvaa yavpayqdyl
       61 arsrvgegla laasarlava dnaasgapld ggysspaatr nvesvridgd tgqitvaftt
      121 rvaaagtntl vlvpsapdka dtptarvalk kgtmqagaia wecfaagksa sslpapgsgp
      181 lpseaatlpa kyapaecra
//
LOCUS       WP_006765852             143 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Burkholderia].
ACCESSION   WP_006765852
VERSION     WP_006765852.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..143
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15538
     Region          7..141
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mpelltyggl favsmvaatl fplqseavla glliagrepa walvlvasvg niagstinwa
       61 lgrgierfre rrwfpvkpsa laraerwyar ygrwslllsw apvigdpltm iagvlreplp
      121 tfiaivaiak vgrylaiawl vth
//
LOCUS       WP_006767510             323 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Burkholderia].
ACCESSION   WP_006767510
VERSION     WP_006767510.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 323)
  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 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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..323
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35885
     Region          38..190
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          218..299
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msaeysptrd pspasrnrer lvalllelap hegynltalp svrilrsnra lsrtpvlydp
       61 givivcqgsk rgyfggeryl ydehhylavs vpvpfsmetd atpdrpllal ylhldfalaa
      121 elaeridreg gaelvqaprs mmstpmddam hasvlrfvea mhrpleaail gpallrelyf
      181 rvltgaqgra mrsalamrgq fgrigrslrr ihadyaqpld vrqlaaeagm svasfhshfk
      241 aitqvppmqy lkstrlhqar llmvredlta eaagyavgyt spsqfsrefk rlfgltpake
      301 tkrmrdsfai papfadaeyv ssh
//
LOCUS       WP_006767523             373 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Burkholderia].
ACCESSION   WP_006767523
VERSION     WP_006767523.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 373)
  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 373)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 373)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 373)
  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   5  (residues 1 to 373)
  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   6  (residues 1 to 373)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..373
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41304
     Region          66..245
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          133..372
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mrpgapeiar aplkynasgs tdgdamtgsd spsarpgral sspsatvpis lvngflasag
       61 vqrdvveryl rgagipikll gepharvtee qfstlyrtla idlddempgi fsrplrggtl
      121 kylclsllda rnletalhrf gqffhilldd ffveskrdgl vaqvllrpnp avgpigalgq
      181 elmlklvhgv cswligqkip llqiefacpr prhavdhlyf fsgalqfdre rtlmrfsady
      241 ldapirqskr nlrkflarap gdwifesfse qlvshrvrqy lsaalpdlpv ieqaaehlhc
      301 svrtlsrhla aegttfqvlk delrrdiaiq rltdtadtia aigadigfdd psafhrafrh
      361 wtgstpgtyr rrv
//
LOCUS       WP_006768112             379 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Corynebacterium efficiens].
ACCESSION   WP_006768112
VERSION     WP_006768112.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium efficiens
  ORGANISM  Corynebacterium efficiens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Corynebacterium efficiens"
                     /db_xref="taxon:152794"
     Protein         1..379
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=40714
     Region          6..>62
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mteatpnkse iralfdatai dksgdklgsi kevfvddrtg qptfvevghg lfgmssslvp
       61 lrgsslsgdt lhlgfskdai kdapdldadn glsveeenri yehyqltdar dvdyfhadtt
      121 ntstdrnrsd ltgadrdvdt htdrgavsdd sghvtttdhd dyvipadgtr datgvdggrr
      181 dpmearntgd patpgvsavp gdvgaplddh lrdragtdtr ddattprask lpsdvsapvd
      241 eelvrreeet varnrtpdde raaadttvta egardetfvd rlrgsrvdtt ddvdnyantg
      301 mgagaaggav rsdtdttite etdvnasrdv deanahgrht kddvvnevve gkapgdfqtq
      361 qdrfrlrrys drqtgtvkd
//
LOCUS       WP_006768374             253 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Corynebacterium
            efficiens].
ACCESSION   WP_006768374
VERSION     WP_006768374.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium efficiens
  ORGANISM  Corynebacterium efficiens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 253)
  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 253)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Corynebacterium efficiens"
                     /db_xref="taxon:152794"
     Protein         1..253
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27629
     Region          1..249
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mpkfaanlsl lftelpfper faaaantglf eavefqfpyd hdlktltqta qqaglpvali
       61 nappgdtfgq aalnstdfes sitealryat algaeklhvm agitepspda talyrrnitt
      121 aarmaaergv livvepinhh tvpgyflhdl dqalgliqni pnvkilfdif hiqqihgdlt
      181 rrltalhqqd llghlqvaav psrhepgtge vddarlfeli dalpwpgfvg aeyhpadttv
      241 eglgwlqpwv tyh
//
LOCUS       WP_006769221             183 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Corynebacterium efficiens].
ACCESSION   WP_006769221
VERSION     WP_006769221.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium efficiens
  ORGANISM  Corynebacterium efficiens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Corynebacterium efficiens"
                     /db_xref="taxon:152794"
     Protein         1..183
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=20294
     Region          <70..160
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mttftrllav ftfllllyta lpylttsgte lpavepvpqr vriigydrdq mfgtwlpgvr
       61 esiveaagat dpytgepldl staevdhilp lsaawdlgah rwtalerief andpvnlvlv
      121 nraenqqksd qlpsqwlptd rsvrcwyvgr lftvaaaydl plpepdirag rrscglailq
      181 tpd
//
LOCUS       WP_006772477             432 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: galactokinase [Hungatella].
ACCESSION   WP_006772477
VERSION     WP_006772477.1
KEYWORDS    RefSeq.
SOURCE      Hungatella
  ORGANISM  Hungatella
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   McAuley,M., Kristiansson,H., Huang,M., Pey,A.L. and Timson,D.J.
  TITLE     Galactokinase promiscuity: a question of flexibility?
  JOURNAL   Biochem Soc Trans 44 (1), 116-122 (2016)
   PUBMED   26862196
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Holden,H.M., Thoden,J.B., Timson,D.J. and Reece,R.J.
  TITLE     Galactokinase: structure, function and role in type II galactosemia
  JOURNAL   Cell Mol Life Sci 61 (19-20), 2471-2484 (2004)
   PUBMED   15526155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Hungatella"
                     /db_xref="taxon:1649459"
     Protein         1..432
                     /product="galactokinase"
                     /EC_number="2.7.1.6"
                     /GO_function="GO:0004335 - galactokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0005534 - galactose binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0046835 - carbohydrate phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=47373
     Region          34..410
                     /region_name="GalK"
                     /note="Galactokinase [Carbohydrate transport and
                     metabolism]; COG0153"
                     /db_xref="CDD:439923"
ORIGIN      
        1 mkvcdtiqml eseksrklma alygetavea nieryqnlvk sfqkkfaeed itlfsspgrt
       61 eisgnhtdhn hgkvlagsin ldcvgvaakn nsskvhiise tfnqsfiidl ndlspsdkka
      121 gtidlvkgll qgfkesgyev ggfnayitsn visaagvsss asfemllcsi lntffnegrm
      181 dtvayahigk ysenvywdka sglldqmaca vgglitidfm epaspvveki dfdfssqnhs
      241 liivntgkgh adlsadyssv piemkkvaef fgkevcaqit eeeviehlae vrayagdrsv
      301 lralhffeen krveaevkal kegrftdflm nitasgnssw kwlqncftns ayqeqgitva
      361 laltelfiae kqrgacrvhg ggfagvimam lpndlvdeyv ayiekalgeg nayrmsirpy
      421 gaicfdtvme eq
//
LOCUS       WP_006773274             348 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Hungatella].
ACCESSION   WP_006773274
VERSION     WP_006773274.1
KEYWORDS    RefSeq.
SOURCE      Hungatella
  ORGANISM  Hungatella
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Hungatella"
                     /db_xref="taxon:1649459"
     Protein         1..348
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39904
     Region          1..344
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mslkveikkk lrdmtlsvaf dtdrdsgitg ilgasgcgks mtlkciagif tpdegrieln
       61 grvlfdsekg invkiqdrgv gylfqnyalf phmtirenve malscpkrer rqaamryldm
      121 yhigeladry psrlsggqqq raalarimas kpevlmldep fsaldyylke klqleqleel
      181 knydgdvllv thsrdeiyrf cstihvineg eivvsgavke vfkepetvsa akltgcknil
      241 dikyvddhtf yvpnwdmqvi irdrnvpkaa pfigirahyf taareeaevn vmecrlkqll
      301 ddpfevtlil endlwwkipk arwkdemker vperlvvpee sifflkdr
//
LOCUS       WP_006776016             145 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein, partial [Hungatella hathewayi].
ACCESSION   WP_006776016
VERSION     WP_006776016.1
KEYWORDS    RefSeq.
SOURCE      Hungatella hathewayi
  ORGANISM  Hungatella hathewayi
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Hungatella.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Hungatella hathewayi"
                     /db_xref="taxon:154046"
     Protein         1..>145
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          14..>145
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 msnkiylipe tgtfykanlh chtihsdgrl tpeevkkaym eagysvvayt dhrkyqwhre
       61 lmddhfvala acevdinehf qvpgdfsrvk tyhinlydak peefseekkq iplperrygd
      121 yhyineyidq mkaygffacy nhpyw
//
LOCUS       WP_006776348             401 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Hungatella].
ACCESSION   WP_006776348
VERSION     WP_006776348.1
KEYWORDS    RefSeq.
SOURCE      Hungatella
  ORGANISM  Hungatella
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
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
REFERENCE   3  (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   4  (residues 1 to 401)
  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   5  (residues 1 to 401)
  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   6  (residues 1 to 401)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 401)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 401)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Hungatella"
                     /db_xref="taxon:1649459"
     Protein         1..401
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44106
     Region          14..54
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          78..390
                     /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 mykgkkkkas nrsrileciy rnapiartdi aeeteitpat vtmnvttlis egfvrelgev
       61 stdeassgrk rvlidiipdr aysigleftq kalvicitdl kgrirfqrte pfneelagri
      121 tdaiiggvkd lvaesgiswd eivgigaavp ghmngsassl itnrktwqnf dpkrieqelp
      181 lpivcennar cmalgeylfs pqespdsfaf fhvgmgmfca svvdgemflg enyvageigh
      241 tivseggrrc ecgkygclqt yasenhlirn arllyrntpn tilrslvsdd sqitietitt
      301 aysmgdpvig myiaealkyl gitisniaii tnpgkiflhg qlfdnqdiqn elmdyierql
      361 ifvdrtyagn veilpygaad gavgasalai lrffirpvmg e
//
LOCUS       WP_006776676             276 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Hungatella].
ACCESSION   WP_006776676
VERSION     WP_006776676.1
KEYWORDS    RefSeq.
SOURCE      Hungatella
  ORGANISM  Hungatella
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Hungatella"
                     /db_xref="taxon:1649459"
     Protein         1..276
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30417
     Region          1..258
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mkvdyhmhtl csdgiyevet vvdmavnngi lamavtdhdt lagigrarqr cqgrvrymtg
       61 teltcaerpw gslpvpqsih llgygfdend etlcallssr kertetvyrd laeavtasgc
      121 plripdvpks cgnvlqlrdv mahvrktfps vseetirlid sfsknltean itvedgiaai
      181 hhaggkavwa hpyhsyhlfq kqtlqadevs vmlnelvrmg ldgleteypa fslpeksfln
      241 glaadyqlft tagsdfhgsa srnrmgmeta qnsffl
//
LOCUS       WP_006778893             328 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Hungatella hathewayi].
ACCESSION   WP_006778893
VERSION     WP_006778893.1
KEYWORDS    RefSeq.
SOURCE      Hungatella hathewayi
  ORGANISM  Hungatella hathewayi
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Hungatella.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Hungatella hathewayi"
                     /db_xref="taxon:154046"
     Protein         1..328
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36816
     Region          14..210
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mkrniegfkg rgnwykgnlh shtvnsdgkl tpaesvklfq dngyhflcls ehdlytdyrk
       61 efdspefiil pgleasavlf ekedgihrkk vhhihgilgt elmqqkavkp lfrhmerlev
      121 pvyygewdga avaqqladel aargcittyn hpvwsrveer efvdtdgifg leifnyntvn
      181 esgtgydtah wdvmlrkgrr ihgfasddnh neglfddacg gyvwvkadgl thdniisalv
      241 egnyysssgp eiydwgireg vvyvdcspvn rvnviaggyv nggrtvmcgs lqetmtraey
      301 plngdetyvr vecvdasgrt awsnaifl
//
LOCUS       WP_006779504             182 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Hungatella hathewayi].
ACCESSION   WP_006779504
VERSION     WP_006779504.1
KEYWORDS    RefSeq.
SOURCE      Hungatella hathewayi
  ORGANISM  Hungatella hathewayi
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Hungatella.
REFERENCE   1  (residues 1 to 182)
  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 182)
  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   3  (residues 1 to 182)
  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   4  (residues 1 to 182)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 182)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 182)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Hungatella hathewayi"
                     /db_xref="taxon:154046"
     Protein         1..182
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=20459
     Region          1..178
                     /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"
ORIGIN      
        1 mtnvivafsk pedaksikni lmrngfsvva vctsgaqaln cmdglnggil vsgyrfedml
       61 yrelreclpa gfemllvasp arfsgglpgd lvylpmplkv hdlintlemm tqaqtkrkkk
      121 drqkprerde eerqlitrak ellmernnmt eteahryiqk csmdsgtnmv etaqmvmsli
      181 hl
//
LOCUS       WP_006779229             412 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Hungatella hathewayi].
ACCESSION   WP_006779229
VERSION     WP_006779229.1
KEYWORDS    RefSeq.
SOURCE      Hungatella hathewayi
  ORGANISM  Hungatella hathewayi
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Hungatella.
REFERENCE   1  (residues 1 to 412)
  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 412)
  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
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 412)
  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   5  (residues 1 to 412)
  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   6  (residues 1 to 412)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 412)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 412)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Hungatella hathewayi"
                     /db_xref="taxon:154046"
     Protein         1..412
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45800
     Region          21..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...; cl46857"
                     /db_xref="CDD:481197"
     Region          102..404
                     /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 mdknstgfkp knlrtnnskl iidlfrkqee lsiqdltnav glsktsiiki vhqlmddgiv
       61 isagkgsste eggkrpniyr lnpsylycis vlftdyeytg kiidlklqti htitlsydcp
      121 hsyeevvdni vkiiqelmkm gnllpeqlcg itigmpgvin akkgvivrpt refsceqnap
      181 lrqnvadrlp fetniyfdna crfggyyell dneerqsrsv vvietfeksv ggcliqqgel
      241 iqgdngfvge fghiktdykt srrcascgnt gcfeatvcsd glvadagsrd ytgsalepfl
      301 eshtlnadii fqeanrgdel aqkvvdyavn qfwaliqnir fvcdpseiii qglysaagey
      361 fhdnllkelv smtyydssnv ptitfsdvds mlslhsgaal ycidqyfgln pd
//
LOCUS       WP_006779669             493 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Hungatella hathewayi].
ACCESSION   WP_006779669
VERSION     WP_006779669.1
KEYWORDS    RefSeq.
SOURCE      Hungatella hathewayi
  ORGANISM  Hungatella hathewayi
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Hungatella.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Hungatella hathewayi"
                     /db_xref="taxon:154046"
     Protein         1..493
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=53007
     Region          1..493
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mqdiirinqa dnvavalrpi nkgetldigg navtaaedip qghkmaikpi ksgeevvkyg
       61 frigyakeei gvgqwihvhn vktalgdlle yeyqpagsgl eetehayfeg frradgkvgv
      121 rneiwiiptv gcvnsiaqal ekaskklvtg siedvvafph pygcsqmgdd qehtrtvlad
      181 minhpnaggv lvlglgcens nipvlkeyig dydeqrvkfl qcqdvedeme tamemleela
      241 vyagafsrek idaseliigm kcggsdglsg itanpvvgaf sdiliskggt tiltevpemf
      301 gaetllmnrc etpelfektv nlindfknyf tshnqtiyen pspgnkkggi stledkslgc
      361 tqksgsalvk gvisygepvk tkglnllsap gndlvaatal avsgahivlf ttgrgtpfas
      421 pvptvkissn salagkknnw idfnagrmve dkskeelaqe lfdyvievas grkvkaeeag
      481 fhdmaifkqg vtl
//
LOCUS       WP_006781803             546 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Hungatella hathewayi].
ACCESSION   WP_006781803
VERSION     WP_006781803.1
KEYWORDS    RefSeq.
SOURCE      Hungatella hathewayi
  ORGANISM  Hungatella hathewayi
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Hungatella.
REFERENCE   1  (residues 1 to 546)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Hungatella hathewayi"
                     /db_xref="taxon:154046"
     Protein         1..546
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=58669
     Region          <148..217
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          <320..400
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          420..543
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(496..497,500,518..521,523)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 msnqqkrnnq veaywtpvrq veacwetara nlwklvltvm vlagicamnt waeepeqfvn
       61 gttindisvg kmtvdeakak iqktytesyk lsivekggkk eqiaggdigy saavpeglqa
      121 ildeqnatgr rwgpsidnsh tmeipavyde kaleaavgrl ncisgseivk tmdarvseyq
      181 egqpftiipe vqgndvdear vmalikeava sgkqevnles ggcyrtvkvk asdeklkaqc
      241 qvmnqcrdmv itytfgetag sgtageeasa gsganavgtv dagtasasen veaasggsve
      301 sstgaetaag aartevltge tictwltgte ngeisvnrds aaayvamlae kydtagtsri
      361 fhtstgkdve ltgpygwkid qageidalia airtgqsqtr eplyakkaas rtlpdwgnty
      421 veidlgsqyv smfqngervw ssgcvtgnvs knyttpegiy sltykeksrv lrgakkadgt
      481 yeyesyvdfw mpfnggiglh danwrgqfgg tiyktngshg cvnlppvkak dlyelvytgi
      541 pvicfn
//
LOCUS       WP_006781656             292 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Hungatella hathewayi].
ACCESSION   WP_006781656
VERSION     WP_006781656.1
KEYWORDS    RefSeq.
SOURCE      Hungatella hathewayi
  ORGANISM  Hungatella hathewayi
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Hungatella.
REFERENCE   1  (residues 1 to 292)
  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 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 292)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 292)
  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   5  (residues 1 to 292)
  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   6  (residues 1 to 292)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Hungatella hathewayi"
                     /db_xref="taxon:154046"
     Protein         1..292
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33285
     Region          21..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          134..292
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mnyldtlqra ivyieehlge nitveevaha tgysyyhltr qfqavlgeni gsylkgrrla
       61 eaakrliyse qriidiamey gfesseafsr afkavyrmsp svyrknrldl iisnkeklge
      121 elirhraasi tvhpklvelp dikaaglrgr ttlrdnvipk lwqefmavrn eiphpkaggl
      181 glgiceacre dnslltmndd ilfsevagie vdsfedlpep fvaktlkggr yavfthkgsl
      241 gslkktfdyi wgtwvfntke llddredfeg yderflgfdn pdsemdiyip ir
//
LOCUS       WP_006782027             396 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Hungatella hathewayi].
ACCESSION   WP_006782027
VERSION     WP_006782027.1
KEYWORDS    RefSeq.
SOURCE      Hungatella hathewayi
  ORGANISM  Hungatella hathewayi
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Hungatella.
REFERENCE   1  (residues 1 to 396)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Hungatella hathewayi"
                     /db_xref="taxon:154046"
     Protein         1..396
                     /product="amidohydrolase family protein"
                     /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=43119
     Region          21..396
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 milencklva elcdagvpqm advvidgnki taivpcgtpv egehermdih gatllpglid
       61 ahvhlfmgka tagdrdritv paqwafdcyn yarffldngy ttirdvgdel hysglatrna
      121 inegimqgpr iygsgvtivp vtagfdayey fcglystked vrrmardqfn hgadflklyg
      181 tgsmlvddsl pgkrimlede iaeavtmaks kgsycachch gaeaigvmie qgvrtiehas
      241 fitdesckkl dgrkdmgivp tiacscpeal gitedagaay ekfsrvsaer dacirnayen
      301 ydilmgwgtd mdlgsmqanp ymewqtrknr lgisnldllk qatinsavlm gvdnkigtvs
      361 vgkladfivv dgdpiadita mykkpvhvik dgevir
//
LOCUS       WP_006782277             384 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Hungatella hathewayi].
ACCESSION   WP_006782277
VERSION     WP_006782277.1
KEYWORDS    RefSeq.
SOURCE      Hungatella hathewayi
  ORGANISM  Hungatella hathewayi
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Hungatella.
REFERENCE   1  (residues 1 to 384)
  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 384)
  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
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 384)
  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   5  (residues 1 to 384)
  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   6  (residues 1 to 384)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 384)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 384)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Hungatella hathewayi"
                     /db_xref="taxon:154046"
     Protein         1..384
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42734
     Region          23..63
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          85..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 mayrlngnki lntmavkkin esrileliyw nqgltqqdik nelglsaptv iqalqqfrel
       61 gligdggelv ssggrkpktl qfyydarvaa gveirrshie avvidlkgnv lwsetqekkf
      121 ehvdaywewl nqylkenvvi pygkemllgv giafpgevsp dgtsisrstv lgiqnmplan
      181 ikqhfdypvy ieyganaagf gavwsrrgey dikdavyliv tnngvagtvi qdnhifkgsr
      241 graaafghmt lnpngrqcfc gakgcwsayc glhnlsdgtd gslerffeel dagkeearkq
      301 weeyltyfaq alvnirlsfd lniiiggkla gyldsrleel yrkifshptm adegkfmeld
      361 tieesaqavg aaliyvekll sgef
//
LOCUS       WP_006782584             128 aa            linear   BCT 20-JAN-2025
DEFINITION  zinc ribbon domain-containing protein [Hungatella hathewayi].
ACCESSION   WP_006782584
VERSION     WP_006782584.1
KEYWORDS    RefSeq.
SOURCE      Hungatella hathewayi
  ORGANISM  Hungatella hathewayi
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Hungatella.
REFERENCE   1  (residues 1 to 128)
  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 12181465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Hungatella hathewayi"
                     /db_xref="taxon:154046"
     Protein         1..128
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14688
     Region          20..125
                     /region_name="zinc_ribbon_15"
                     /note="zinc-ribbon family; pfam17032"
                     /db_xref="CDD:465334"
ORIGIN      
        1 mfficgidtr tkeipysktv icaqcggygr yqvfmtyscl slffipifkw nrhyyvrmsc
       61 cdtlyemsqe lgkriaggdl vditessltl vqsgrrkeng wtekkccgnc gyettedfey
      121 cpkcgqkf
//
LOCUS       WP_006783428             355 aa            linear   BCT 20-JAN-2025
DEFINITION  GerAB/ArcD/ProY family transporter [Turicibacter sanguinis].
ACCESSION   WP_006783428
VERSION     WP_006783428.1
KEYWORDS    RefSeq.
SOURCE      Turicibacter sanguinis
  ORGANISM  Turicibacter sanguinis
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Turicibacteraceae; Turicibacter.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Turicibacter sanguinis"
                     /db_xref="taxon:154288"
     Protein         1..355
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=40608
     Region          38..310
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 mkkplstaql villffcrhy slltytnseq aletslyaiv iadiinllfl ipvflllkkn
       61 hsrnlmaiaq dispflnkli ylvlfvffil ttfisltefg tfmtttifpt tssaiilfsm
      121 lifcmyaain gletiaktas lllpmiiigi llitffsmsn idfdnfrpil enpiltiikr
      181 awtisirnie lvaliyllpf fngsnkkvvg gflgsytvsh allifmtiav lgeyayvqqy
      241 psysiatvak fsifqrldsl ymgiwvftgf irislnlwls ihllkylvpa kyhkflllmt
      301 siilfivsly rnyffnisla esiflihtvl fitcliffpl llliiqkifk kesys
//
LOCUS       WP_006783525             591 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Turicibacter
            sanguinis].
ACCESSION   WP_006783525
VERSION     WP_006783525.1
KEYWORDS    RefSeq.
SOURCE      Turicibacter sanguinis
  ORGANISM  Turicibacter sanguinis
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Turicibacteraceae; Turicibacter.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 591)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 591)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Turicibacter sanguinis"
                     /db_xref="taxon:154288"
     Protein         1..591
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=65881
     Region          3..572
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mminkrlisi ceeskkymfl tllcswigii cniaiifmmg lfinamvage tlskglshfy
       61 ltkhltlava ipliiillia kfiahhyygk fsykssakar stlrsliyek llrlgmdyqk
      121 sqptstivqi siegveqlei yfgkylpqff ysllapltlf vvistiswkv alvfiacvpl
      181 ipisiialmk vakrimkdyw nnyadlgdtf lenlqglttl kvygqddikh lemneeaekf
      241 rritmkllsm qlnsinimdl iafggsalgt ivalyqfqkg ainvgelivi illsseffip
      301 mrllgsyfhi amngmaasdr ifalldteev avknpcdfkk dssvkieven infsydgerq
      361 vlndisfdlt nggltaivge sgsgkstmat lligqkrpts grilingvdl tqlktealye
      421 hvslvsahsh ifkgsikenl lmakrdatse evnqalkmar ldqfiaglpk gletevseng
      481 sslsggqkqr lalarvilan rdviifdeat snidveseea iwdaiyelsq qktilvishr
      541 lasvkrakai hvfklgtlve sgthdhlmsq ngvyahmves qqqlemirev e
//
LOCUS       WP_006785355             160 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Turicibacter sanguinis].
ACCESSION   WP_006785355
VERSION     WP_006785355.1
KEYWORDS    RefSeq.
SOURCE      Turicibacter sanguinis
  ORGANISM  Turicibacter sanguinis
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Turicibacteraceae; Turicibacter.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Turicibacter sanguinis"
                     /db_xref="taxon:154288"
     Protein         1..160
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17671
     Region          8..159
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfqkeaytgt leenyelvla qlkaliages dlianlsnas allnvfleei nwvgfylvkn
       61 nqlvlgpfqg lpaciripfd kgvcgyvatt kqtalvqnvh efvdhiacds atnseivvpi
      121 ikdnelmgvl didspllnrf sktdqhylek fvqilvesli
//
LOCUS       WP_006785124             264 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Turicibacter].
ACCESSION   WP_006785124
VERSION     WP_006785124.1
KEYWORDS    RefSeq.
SOURCE      Turicibacter
  ORGANISM  Turicibacter
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Turicibacteraceae.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Turicibacter"
                     /db_xref="taxon:191303"
     Protein         1..264
                     /product="formate/nitrite transporter family protein"
                     /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=28381
     Region          6..253
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mqqprmlsak eianevvevs kykvsrknsv vlisgmlagl figlgytvyl lvygqmsdpy
       61 vgkvvgsflf pialilillt gadlftgntl iakacfkkev kvsayiknlv lvwvgnllgi
      121 lcaigllyga rlftngvspt vaenimhiae vkihtlstse vffrailcni liaggvyvsy
      181 aakdvtgkvl lnvivvavfa lmgvehcian mfvlgmgkvl gaditfggig wnlfiatign
      241 ivggfiiaip yyfnfihayk kqqv
//
LOCUS       WP_006785907             747 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Turicibacter].
ACCESSION   WP_006785907
VERSION     WP_006785907.1
KEYWORDS    RefSeq.
SOURCE      Turicibacter
  ORGANISM  Turicibacter
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Turicibacteraceae.
REFERENCE   1  (residues 1 to 747)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 747)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 747)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Turicibacter"
                     /db_xref="taxon:191303"
     Protein         1..747
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=87809
     Region          <564..743
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mgasisrkql lsffiqasyl ldkfysikes fnfdsiseds lekiievers hqnfdylvsl
       61 lilseqyfve qkeyhtaivy lieclsllee ldfnnilkvy iylelgyife snqfykeaen
      121 yykralevsv ekknpllvty sfeklsqiil kscnrkgiir fnslvqlyge nfvpasivfv
      181 fdllnlyvnq dydkilevls yhqdyqdlgv nreflmiiyv iqtqsfykln kfeeikwldf
      241 shdssiskhn pylmlydlty qliykkdeig qyiadvtqkl senhqyyllr vfyyyllgee
      301 sivkdkecyl kiyellgqnr qilfyeegil ktkiqnvyqt ykqyynqlds vkfddkyriv
      361 swqqmgahyq reynsqtvvg flmvddcfcs efsqelkesl innlnaiiqg eltfcfhdhg
      421 lwfyfkactg evklkqklns llkplydnlq rkytvafclp rftssdfskt mrivytsfyg
      481 mvvhteleqn ysvsfcqess sylalsedih nlllkaykek nfiidkkhfy neggqqlfgi
      541 efkgilsdln lvidnldgdk eviresllme vematleigc qlikeayqti hsnpylfikl
      601 sretlmnkli vgrilnclkr ynlnynqiii sinedvlfeq neflkklinr lhelgvgval
      661 ddygtgsltg sirnlninyl klspsliqyl sstyhysgmm kslisvcsny nvkiccsdid
      721 nksshdlisn fgidvvsgsy yqrklvv
//
LOCUS       WP_006786401             399 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Thiorhodospira sibirica].
ACCESSION   WP_006786401
VERSION     WP_006786401.1
KEYWORDS    RefSeq.
SOURCE      Thiorhodospira sibirica
  ORGANISM  Thiorhodospira sibirica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Thiorhodospira.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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   3  (residues 1 to 399)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Thiorhodospira sibirica"
                     /db_xref="taxon:154347"
     Protein         1..399
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44884
     Region          284..389
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mailahleaq qqqrqrqtpr vsvlvgevta anaiwadwhq qralpavyws lhhprsstsh
       61 wletvfasha ptqaawryva qlsqqnlpal qaqlgaqsiy qrklwyehwi nlddpvlaal
      121 lrgllesama htpptllqal gwvhkfqpyg speqhlmasl atlipqtqlp gllwtdlpad
      181 pavlsrwleg aarlaeavpa lplavtlsat sytqymqsip esrhkalire gylplaplda
      241 arpdtpppsv tnilrhyhva egvwhqatal hqtlaatppl dadrarsqae rflfnllqsi
      301 pefkdrfvln arlpiqfgqe tmevdfladp pglvleldgy yhfqdavcyr rdrrkdlllq
      361 qhgytvvryl aedvvshlee ilatirhalv hapgrpidr
//
LOCUS       WP_006787192              92 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Thiorhodospira sibirica].
ACCESSION   WP_006787192
VERSION     WP_006787192.1
KEYWORDS    RefSeq.
SOURCE      Thiorhodospira sibirica
  ORGANISM  Thiorhodospira sibirica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Thiorhodospira.
REFERENCE   1  (residues 1 to 92)
  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   2  (residues 1 to 92)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Thiorhodospira sibirica"
                     /db_xref="taxon:154347"
     Protein         1..92
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9619
     Region          22..90
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkhylsivlf vvglalstav waqavqteav dintadaqti aqvmkgvgpa kataivtyre
       61 engpfasvyd ltkvrgigak tveanldvit id
//
LOCUS       WP_006786996             113 aa            linear   BCT 20-JAN-2025
DEFINITION  PilZ domain-containing protein [Thiorhodospira sibirica].
ACCESSION   WP_006786996
VERSION     WP_006786996.1
KEYWORDS    RefSeq.
SOURCE      Thiorhodospira sibirica
  ORGANISM  Thiorhodospira sibirica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Thiorhodospira.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 113)
  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   3  (residues 1 to 113)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 113)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Thiorhodospira sibirica"
                     /db_xref="taxon:154347"
     Protein         1..113
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12438
     Region          1..113
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mppgqgilnl aikdknslym aympyvkngg lfiptqkryr lgdevfmlls lmeekdripv
       61 agkivwvtpp rsqgnrtpgi gvqfnpqdng strnriegll ggalqsdrlt htl
//
LOCUS       WP_006787627             247 aa            linear   BCT 20-JAN-2025
DEFINITION  3-deoxy-manno-octulosonate cytidylyltransferase [Thiorhodospira
            sibirica].
ACCESSION   WP_006787627
VERSION     WP_006787627.1
KEYWORDS    RefSeq.
SOURCE      Thiorhodospira sibirica
  ORGANISM  Thiorhodospira sibirica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Thiorhodospira.
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   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 10118537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Thiorhodospira sibirica"
                     /db_xref="taxon:154347"
     Protein         1..247
                     /product="3-deoxy-manno-octulosonate cytidylyltransferase"
                     /EC_number="2.7.7.38"
                     /GO_function="GO:0008690 - 3-deoxy-manno-octulosonate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0033468 -
                     CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27379
     Region          4..238
                     /region_name="CMP-KDO-Synthetase"
                     /note="CMP-KDO synthetase catalyzes the activation of KDO
                     which is an essential component of the lipopolysaccharide;
                     cd02517"
                     /db_xref="CDD:133010"
     Site            order(8..10,49,76,96,98)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133010"
     Site            order(137,143..145,151..152,154..160,170,196..197,
                     200..202,209..212)
                     /site_type="active"
                     /note="oligomer interface [active]"
                     /db_xref="CDD:133010"
ORIGIN      
        1 mrsvvmipar ygssrypgkp lvpllgkpmi lwvaelsara vgaenvyvat edrrivevve
       61 aagfqsvmtt ddaltgtdrl aqaaeqvead iyinvqgdep ladpadilkv rdaklaymda
      121 iingvswvgd nedphsvnip kvitnerdel vymswvalpg fkdakcapkr ykkqvciyaf
      181 tleelaafra fgrkseleha edieilrfle lgktirmvet qpgslavdvp edvekveeal
      241 krmvrei
//
LOCUS       WP_006788133             136 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Thiorhodospira sibirica].
ACCESSION   WP_006788133
VERSION     WP_006788133.1
KEYWORDS    RefSeq.
SOURCE      Thiorhodospira sibirica
  ORGANISM  Thiorhodospira sibirica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Thiorhodospira.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Thiorhodospira sibirica"
                     /db_xref="taxon:154347"
     Protein         1..136
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14511
     Region          5..104
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mlsptrrrgf tlievmivva iigilaaiay psymryvers hisegktall qaaqwmerry
       61 tqansypdda afqagfgsgg tdyytlsita rtntsytlta tsaakkvgtk cntmtitntg
      121 vttgstggaa dnscwn
//
LOCUS       WP_006787472             195 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Thiorhodospira sibirica].
ACCESSION   WP_006787472
VERSION     WP_006787472.1
KEYWORDS    RefSeq.
SOURCE      Thiorhodospira sibirica
  ORGANISM  Thiorhodospira sibirica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Thiorhodospira.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Thiorhodospira sibirica"
                     /db_xref="taxon:154347"
     Protein         1..195
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21519
     Region          3..164
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mklfgplydq vlhysahpha prylaglsfa essffpvppd vmlapivlar pdqawrlali
       61 ttvfsvlggl lgyvlgylay gliapwvisl gygdaltqar lwfdtwgvwv vlvagfspip
      121 yklftftaga mamlllpfii asligrglrf favalliswl gprivpklrp ymewlgwmtv
      181 lllviavvil hvfns
//
LOCUS       WP_006788418             711 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Thiorhodospira sibirica].
ACCESSION   WP_006788418
VERSION     WP_006788418.1
KEYWORDS    RefSeq.
SOURCE      Thiorhodospira sibirica
  ORGANISM  Thiorhodospira sibirica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Thiorhodospira.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 711)
  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   3  (residues 1 to 711)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Thiorhodospira sibirica"
                     /db_xref="taxon:154347"
     Protein         1..711
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=78253
     Region          5..709
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          <249..>323
                     /region_name="nfrB"
                     /note="glycosyl transferase family protein; PRK15489"
                     /db_xref="CDD:237974"
ORIGIN      
        1 msatmadalq tffaeannll semeeallal kegpaedtel ihalfraaht ikgsaglfgl
       61 daivafthqv esvldqvrdg nigldatlla tlmrahdhif allehedrpl deamqatdqa
      121 lvrelcrylg teipattata tdsppaasps paqegdiwhi slrfgedvlq ngmdplsflh
      181 ylqtfgeivh lvtlpdrlpp aaqmnpehcy lgfeirfasc adkaqiegaf dfvrdssair
      241 ilppgsrlhd yvemienlpe kasrlgellv gcgaitrrel devlnlqarq dgedrpllgd
      301 vlvqeqlvqr elvdaalhrq qevrnrqhqe hkllrvqahk ldslidlige lviahaglrl
      361 lvensqdsdm lesvsevthl veeirdtamh lrmveigetf srfrrvvrev sketgkeiel
      421 linggdteld ktvvdrigdp lthlirnaid hgieptqtrl qrgkpaqgtv alnayhesgg
      481 ivievsddgs gldrerilrk aqqrglvqnt qvlsdeqick lifeagfsta eqvsnlsgrg
      541 vgmdvvkrsi eglrgtieid sqagqgstfr irlplslaii dgflmrvadg hyvvpldmvl
      601 ecvefdprkl tqgqayldlr geilpllrlr eyyklsgkrh grqnvvvvqw gqrkagfvvd
      661 elkgelqavi kplgpvfsal kgiagstilg sgevalvldv stlldqaagl h
//
LOCUS       WP_006788850             158 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Thiorhodospira
            sibirica].
ACCESSION   WP_006788850
VERSION     WP_006788850.1
KEYWORDS    RefSeq.
SOURCE      Thiorhodospira sibirica
  ORGANISM  Thiorhodospira sibirica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Thiorhodospira.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 158)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Thiorhodospira sibirica"
                     /db_xref="taxon:154347"
     Protein         1..158
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18106
     Region          74..153
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 miqqidafag daallqaagf ndqvyrllam alqpevflkq tdylaaqrvd tlaaferyve
       61 ehlqkpvalt eiermlgvsa ralqyaclkr hgcspmayir nrkldysyqy llqsqndinl
      121 aklsaelyfs iqskfsryfr erygvlpsef masrsqkk
//
LOCUS       WP_006799415             320 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Dysgonomonas gade].
ACCESSION   WP_006799415
VERSION     WP_006799415.1
KEYWORDS    RefSeq.
SOURCE      Dysgonomonas gade
  ORGANISM  Dysgonomonas gade
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Dysgonomonadaceae; Dysgonomonas.
REFERENCE   1  (residues 1 to 320)
  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 320)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 320)
  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   4  (residues 1 to 320)
  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 320)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Dysgonomonas gade"
                     /db_xref="taxon:156974"
     Protein         1..320
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37552
     Region          <120..317
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          240..317
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mkiikndviy lhpilrrdkt emedktkmyg ekkalskdkk nsvysfgydf nicmgesalp
       61 vtytqtylpi gilglctegs aiidvymqeh hlskgelmvi lpgqivslks kspdfsinyf
      121 tvshllindv lsgvarlspl ffihmrrkyh yklskdevyr fsqyynlsys wvkpadnlfq
      181 reyivnllrl fyldlynnyr nnllsknair didsrkekit ydffllimqy frenreiafy
      241 aeklhitpky ltsvvkdvsg rpakdwivey simeiksllk npalniqeit vktnfsnqas
      301 lsrffkkhtg lsptqyrmdk
//
LOCUS       WP_006800080             685 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate--CoA ligase family protein [Dysgonomonas].
ACCESSION   WP_006800080
VERSION     WP_006800080.1
KEYWORDS    RefSeq.
SOURCE      Dysgonomonas
  ORGANISM  Dysgonomonas
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Dysgonomonadaceae.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 685)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Dysgonomonas"
                     /db_xref="taxon:156973"
     Protein         1..685
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=74109
     Region          4..685
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 miyeqlinpk sivvvgasdn ilkpggsvlh nlttgtfdkd lyvvnarggs iqntkayvsi
       61 edipqtdlai isvpanqclq tveylakkkg vkafivfsag fseesedgak lekdlvdivn
      121 kagaimigpn csgyfntkhq siftrpipnl dpqgvdiiss sggtityiie samriglrfn
      181 sawsignaaq vgvedilefl dnefdpessp kikllyleki adpdrflnhs aslirkgcki
      241 aaiksgssss gsraasshtg aiassdsave alfrkagiir cysreelanv aavltlkeik
      301 grnlaiitqa ggpaviltda lskgnidvpe mnkelaaelk khllpgaavs npidiigtgt
      361 gehmatcidf cekrfkeidg iaviygnpgv snvaeayeil dqkiktcklp iypilpsvia
      421 asqemdnfvk kghvnftdey alanalskvv swtppsvgkm edikidipri rniidnasdg
      481 yidsdtirkl fdaagipqvq elvtnnkeea isfankidyp ivakcvgpvh ksdvggvvln
      541 irsddhlale fdrlmkipet tevmiqpmls gqelfigaky eskyghivlc glggifveil
      601 kdvasglapl sfneassmir slraykiiqg trgqkglner lfteiivrls illrfateik
      661 emdinpllan edkviavdar iriek
//
LOCUS       WP_006800320             147 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Dysgonomonas gade].
ACCESSION   WP_006800320
VERSION     WP_006800320.1
KEYWORDS    RefSeq.
SOURCE      Dysgonomonas gade
  ORGANISM  Dysgonomonas gade
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Dysgonomonadaceae; Dysgonomonas.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Dysgonomonas gade"
                     /db_xref="taxon:156974"
     Protein         1..147
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16263
     Region          7..146
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mldgfveygy iglflasfla atilpfgsef vfagllaigm nawgcvivas vgnwlggmtn
       61 yylgrlgkie wiekylkvdr gkiekmqqwl egkgaimaff sfmpvvgdii alalgymran
      121 iyivnvamfs gkllryilim ygvswii
//
LOCUS       WP_006801633             167 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SPOR domain-containing protein [Dysgonomonas].
ACCESSION   WP_006801633
VERSION     WP_006801633.1
KEYWORDS    RefSeq.
SOURCE      Dysgonomonas
  ORGANISM  Dysgonomonas
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Dysgonomonadaceae.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Dysgonomonas"
                     /db_xref="taxon:156973"
     Protein         1..167
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18636
     Region          81..146
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mkksiyiflv lclfsgfala qddnktiide lnsskwgqgn ikvmqdeavq nilgvrqiav
       61 idttktvgvi dptanftkvr gfkiqvfsgn nqqrskreae skqaqvksaf peletvvsfq
      121 spfwrlrvgn ftsradadgv lkemkktfpa fgremyvvpd vvkkpvq
//
LOCUS       WP_006802782             283 aa            linear   BCT 20-JAN-2025
DEFINITION  class 1 fructose-bisphosphatase [Helicobacter winghamensis].
ACCESSION   WP_006802782
VERSION     WP_006802782.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter winghamensis
  ORGANISM  Helicobacter winghamensis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Marcus,F., Gontero,B., Harrsch,P.B. and Rittenhouse,J.
  TITLE     Amino acid sequence homology among fructose-1,6-bisphosphatases
  JOURNAL   Biochem Biophys Res Commun 135 (2), 374-381 (1986)
   PUBMED   3008716
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10013175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Helicobacter winghamensis"
                     /db_xref="taxon:157268"
     Protein         1..283
                     /product="class 1 fructose-bisphosphatase"
                     /EC_number="3.1.3.11"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0042132 - fructose 1,6-bisphosphate
                     1-phosphatase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31072
     Region          1..281
                     /region_name="PRK09293"
                     /note="class 1 fructose-bisphosphatase"
                     /db_xref="CDD:236458"
     Site            order(41,64..65,83..87,228)
                     /site_type="active"
                     /db_xref="CDD:238814"
ORIGIN      
        1 mdsiltkikq asleiysilq kslgeytqst natgdtqlka dvqadlivqn tlktlpcvkq
       61 icseeqtsai tlydngtysi aydpldgssl mganlsvgsi fgiyqgdflp qnlvasayvv
      121 ygmvvgigft sllkegvdyf tydgekfglq kclklsekgk lnatggtqkn wskthkekme
      181 slfdagyrlr ysggmvpdlh hilvkggglf sypatsdapk gklrmlfevf pfafiferag
      241 gkavfidele skitpllelk pthlhdttpc yfgsiweief vsr
//
LOCUS       WP_006802806             402 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Helicobacter winghamensis].
ACCESSION   WP_006802806
VERSION     WP_006802806.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter winghamensis
  ORGANISM  Helicobacter winghamensis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Helicobacter winghamensis"
                     /db_xref="taxon:157268"
     Protein         1..402
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43826
     Region          1..398
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mdvlvincgs sslkyqlint qteevlasgi cdrigikggq fsykpkdgsk ttqnvempdh
       61 evaiklvlna lvdpkdgilk sldeikatgh rivhggehft esalvndevi rhieecadla
      121 plhnpahllg iracqhlmpn kpmvavfdta fhqtmppray iyglpyeyye kykirrygfh
      181 gtshsyvskr taeflgiple nskiitchlg ngssicaien gksidtsmgl tpleglvmgt
      241 rsgdldpaii dyiaqkenln tkevinilnk ksgvlgisgi ssdfrdllaa deegnlkarf
      301 arevfayhva kyigsytaal tgvdaitfca gvgenakfir gkivshlqfl gitldekanl
      361 etigkegiis tkdskvkvcv iptneelmia rdtralvagk hl
//
LOCUS       WP_006803019             298 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Helicobacter
            winghamensis].
ACCESSION   WP_006803019
VERSION     WP_006803019.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter winghamensis
  ORGANISM  Helicobacter winghamensis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Helicobacter winghamensis"
                     /db_xref="taxon:157268"
     Protein         1..298
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=33011
     Region          2..>227
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 miildfekrl lsaqgeivlk vactlkeqdl itlfgksgag kttilrilag lvepdfgrvq
       61 vgdkvwfeka kearkasinl ppqqrtigfv fqdyalfpnm sveenlsfal pkgadkkkvv
      121 elleitelqa lakqkpntls ggqqqrvala ralvrnpeil lldepfsald svmahklqke
      181 llkihrhfnl ttflvshnfs evfflsnfvl fiekgiihkq gsphsvflqd lpsgkfrhsg
      241 vvleikksgl vyvlsvlign eiaqitaqee evvdlksgdc vmlsskawnp vvtkianl
//
LOCUS       WP_006806240             398 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Pseudoleptotrichia
            goodfellowii].
ACCESSION   WP_006806240
VERSION     WP_006806240.1
KEYWORDS    RefSeq.
SOURCE      Pseudoleptotrichia goodfellowii
  ORGANISM  Pseudoleptotrichia goodfellowii
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Leptotrichiaceae; Pseudoleptotrichia.
REFERENCE   1  (residues 1 to 398)
  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 398)
  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
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 398)
  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   5  (residues 1 to 398)
  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   6  (residues 1 to 398)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 398)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 398)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Pseudoleptotrichia goodfellowii"
                     /db_xref="taxon:157692"
     Protein         1..398
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45037
     Region          14..58
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          78..385
                     /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 mqkieskkir klnrtdyril ekvmkdsevs rtdlakemel tsaaiskaik klmlqniime
       61 hatlestggr prkslivnke ykkiigvnlg agfinivash lngeiiqirq rkfvyktqek
      121 vldllyegis dmvekfgees iigiglathg lvdrkkgtvi fsphfkwkkl dirrelerkf
      181 nlkvivendv ramltaehmy gcagnmknfm llyirngvga aiflngkife gsnysagevg
      241 hfivneksti qcrcgkfgcl etecseqali nkvvwelekk dkneskekit idkiysrskh
      301 keepyysivk eaayetgkvi gnilnildid nvvvagdiim teklymnnfr kgvdrmiled
      361 fnkkvkivss alddmigiyg aislvtsnlf vgeklmkg
//
LOCUS       WP_006810364             274 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Enterobacter
            cloacae complex].
ACCESSION   WP_006810364
VERSION     WP_006810364.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae complex
  ORGANISM  Enterobacter cloacae complex
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 274)
  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 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   3  (residues 1 to 274)
  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   4  (residues 1 to 274)
  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 274)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Enterobacter cloacae complex"
                     /db_xref="taxon:354276"
     Protein         1..274
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31638
     Region          16..274
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <156..270
                     /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 mqgvpeqftd erdsarfrhl aqlpglelyh ahisdyafep htheafgigt ietgaerfry
       61 rgsqhlaaek svvtmnpdei htgesategg wryrmvyiep dlleevtglr hwwfndvtrh
      121 dplrsqqigq liyglwhtnd plaqkgllld liqtfqplah hapvmqeaah rfdrvrdylh
      181 dnymraltld elanvvslsp yhfqrqfkah fhvtphqmlm airlwrakaf lthgmpaaev
      241 aaatgltdqs hltraftrry gitpvryqkq vmpr
//
LOCUS       WP_006811962             299 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Enterobacter
            cloacae complex].
ACCESSION   WP_006811962
VERSION     WP_006811962.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae complex
  ORGANISM  Enterobacter cloacae complex
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 299)
  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 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   3  (residues 1 to 299)
  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   4  (residues 1 to 299)
  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 299)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Enterobacter cloacae complex"
                     /db_xref="taxon:354276"
     Protein         1..299
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33515
     Region          28..179
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          207..288
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mnrdaicrql tsqikrlinn enttadllpd irllygtqpg prtpvmyqpg ivflfsghki
       61 gyinervfry dtneyllltv plpfecetfa teavplagir vnvdilqlqe llmeigedel
      121 frpsmaasgi nsatlseeil caierlldvm erpldarilg kqiireilyh vlmgpgggal
      181 lalvsrqthf slisrvlkri esqytenlsv dqlaaeanms vsafhhnfks vtstsplqyl
      241 ktyrlhkarm lmihdgmkas aaamrvgyes asqfsrefkr yfgvtpgeda srirtmqga
//
LOCUS       WP_006813161             340 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Providencia
            rustigianii].
ACCESSION   WP_006813161
VERSION     WP_006813161.1
KEYWORDS    RefSeq.
SOURCE      Providencia rustigianii
  ORGANISM  Providencia rustigianii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Providencia.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 340)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 340)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Providencia rustigianii"
                     /db_xref="taxon:158850"
     Protein         1..340
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=38433
     Region          <55..330
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mnekhclinl kklnneelef gysqvginel fgknsltlel pftrsqfiqd qpanqtgmsi
       61 sgfqpklslr lengslyvan nkgtfilkps peaypflaen ehatmtvmkr lkfptppfgl
      121 ipfqssldkp kefafiiqry drlgndvqkl hqeqldgamg indkygnvdg tksvsyekaa
      181 kfiienvdds laskrdlflr iiyayvlgnn dyhlrnisil lpqnkkpsla piydfvsivp
      241 ypsvfteyla lplleleend sdiapglnsq ygeytgadfi llaqgigirn elakklllrv
      301 ikshqlitdt yteshlpdvd klaiikyisr rmtllgimrf
//
LOCUS       WP_006821363             231 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Corynebacterium casei].
ACCESSION   WP_006821363
VERSION     WP_006821363.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium casei
  ORGANISM  Corynebacterium casei
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 231)
  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   2  (residues 1 to 231)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Corynebacterium casei"
                     /db_xref="taxon:160386"
     Protein         1..231
                     /product="ComEA family DNA-binding protein"
                     /function="1.10 Transformation/competence"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=23759
     Region          163..230
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mtqkpgisqr lseltaptge epildvsypa prlkiapwqa ivaaiaaiva vllwlalssp
       61 ksdgqlppie aaqapeistv tseealpaev vvsvvgaveq qgililpqga riadalevsg
      121 lapdadivsi nhaqllvdge qiyvsrigee ppaqveaged ggargsnssk inlnsataae
      181 ltqlpgvgev taesivshrd tvgsftsveq lldisgigpa kfeklqdlvt v
//
LOCUS       WP_006818283             299 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Yokenella regensburgei].
ACCESSION   WP_006818283
VERSION     WP_006818283.1
KEYWORDS    RefSeq.
SOURCE      Yokenella regensburgei
  ORGANISM  Yokenella regensburgei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Yokenella.
REFERENCE   1  (residues 1 to 299)
  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 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   3  (residues 1 to 299)
  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   4  (residues 1 to 299)
  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 299)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Yokenella regensburgei"
                     /db_xref="taxon:158877"
     Protein         1..299
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33580
     Region          28..179
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          207..288
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mnreaiclql teqikslinn qqrlsellpd vrllygtqpg trtpvmyqpg ivflfsghkv
       61 gyinersfry dtneyllltv plpfecetfa tpevplaglr lnvdilqlqe llmdigedeh
      121 frpavaasgi nsavlnedil caaerlldvm drpldarilg kqiireilyh vltgpcggal
      181 lalvsrqthf slisrvlkri esqytenlsv dqlaaeanms vsafhhnfks vtstsplqyl
      241 ktyrlhkarm mmvhdgmkas aaamrvgyes asqfsrefkr yfgitpgeda arirmmqgl
//
LOCUS       WP_006823417             267 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Corynebacterium casei].
ACCESSION   WP_006823417
VERSION     WP_006823417.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium casei
  ORGANISM  Corynebacterium casei
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Corynebacterium casei"
                     /db_xref="taxon:160386"
     Protein         1..267
                     /product="HNH endonuclease family protein"
                     /function="5.2 Protein of unknown function similar to
                     proteins from other organisms"
                     /calculated_mol_wt=29255
     Region          <157..>228
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mgkpgntphr trpstpsqpy hvtvfttpts rarkfttsdt pstfedaael arkaalvari
       61 rntfliilti atalfalsml sprlhpysqe glpnlktslq nidtiparhk ilgykrevfg
      121 adwaiapgss cdtrqvviss qspsvsdctt estelfdpys qslipnanie vdhifplsaa
      181 wdhgayawdd dtrkhfandp lnlvatsrtl nqsksdslpg ewippnpaah cwyaervagv
      241 aaaysltlae tdittmkrrc qlgipfm
//
LOCUS       WP_006823809             135 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Corynebacterium casei].
ACCESSION   WP_006823809
VERSION     WP_006823809.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium casei
  ORGANISM  Corynebacterium casei
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Corynebacterium casei"
                     /db_xref="taxon:160386"
     Protein         1..135
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /function="3.3 DNA recombination, and repair"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=14710
     Region          5..96
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(29,56..57,59,79)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 msepaepsev aqrvlyiagl ippgnvstyg evgkaadata rqvgsimrlw gsriswwrvi
       61 kadgsshdfd rakshwedeg iqlrgmkvrm dlcgldhrdl rdivkhmppa aaesvnlaag
      121 cklggyerhr stdlg
//
LOCUS       WP_006829344             388 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Planococcus antarcticus].
ACCESSION   WP_006829344
VERSION     WP_006829344.1
KEYWORDS    RefSeq.
SOURCE      Planococcus antarcticus
  ORGANISM  Planococcus antarcticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Planococcus.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Planococcus antarcticus"
                     /db_xref="taxon:161360"
     Protein         1..388
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44147
     Region          1..275
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          271..355
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkffhtadwh lgklvqgiym teeqqfvleq fmdaikeqqp daiiiagdly dravpptdav
       61 nlldevlaki vlelktpvla vagnhdspgr lnfgsrlmkm neihiaghvh kdhqavvlsd
      121 qfgevhfhli pytdpsmvry efeddairth neamkaiten ikaaydpqar hvfvghafvt
      181 hhgeqeents dserplsigg aehvdahhfe gfhytalghl hkahyvlnet irysgsplky
      241 siseehhqkg fhivemdarg evsvekrlfs prrnmrtveg tineilrhei sddfvfvtll
      301 ddapvlfpme kvrsvypnam hverknfsgs mlqsevgsrr kmdslslfht fyeevkgeka
      361 saetadifke vlqeflqeep akteevks
//
LOCUS       WP_006829996             159 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Planococcus antarcticus].
ACCESSION   WP_006829996
VERSION     WP_006829996.1
KEYWORDS    RefSeq.
SOURCE      Planococcus antarcticus
  ORGANISM  Planococcus antarcticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Planococcus.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Planococcus antarcticus"
                     /db_xref="taxon:161360"
     Protein         1..159
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17340
     Region          13..159
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mftqtdysgs nleqytmlsk qldallegen nsianlsnas allnqflert nwvgfylmee
       61 gelvlgpfqg lpacvriplg kgvcgtavsd kktmlvkdvq afpghiacda asrseivipl
      121 mkedqvigvl didspelsrf teedqqglel fatvlmkhl
//
LOCUS       WP_006832795             165 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Erythrobacter sp. SD-21].
ACCESSION   WP_006832795
VERSION     WP_006832795.1
KEYWORDS    RefSeq.
SOURCE      Erythrobacter sp. SD-21
  ORGANISM  Erythrobacter sp. SD-21
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Erythrobacter/Porphyrobacter
            group; Erythrobacter.
REFERENCE   1  (residues 1 to 165)
  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 165)
  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   3  (residues 1 to 165)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Erythrobacter sp. SD-21"
                     /db_xref="taxon:161528"
     Protein         1..165
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18429
     Region          46..138
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mtdrktlqlr dpsetadtap alkkkgrgwe isekrldalh eqardmrrhs teahkalaek
       61 fakadmgpft fkrhavvgsa ivdfnchklg maimideegq detlakrrdk sleavgirvm
      121 riaakdiled mdavlqritl gmrsriadkr erraahnass rgvps
//
LOCUS       WP_006834479             796 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Erythrobacter sp. SD-21].
ACCESSION   WP_006834479
VERSION     WP_006834479.1
KEYWORDS    RefSeq.
SOURCE      Erythrobacter sp. SD-21
  ORGANISM  Erythrobacter sp. SD-21
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Erythrobacter/Porphyrobacter
            group; Erythrobacter.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 796)
  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   3  (residues 1 to 796)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Erythrobacter sp. SD-21"
                     /db_xref="taxon:161528"
     Protein         1..796
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=86770
     Region          1..546
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdelladfva etremleqsg selvaweadp sdkkridtif rfvhtvkgnc gffdfprleq
       61 lshaaedala ecragrrepd salvtavlai idrisemtda ieagedfpag gdealiaals
      121 pdaeievqsd veiveetlae apaegdapaa ptkaprqtvq rsirlpvdll devmkgvsdm
      181 vlarndlarr lreageqpti dgpferlsai ladvrnsitr mrmqrlehlf sslprlvrdl
      241 snelgkqvmv dfegseveld remiemvrdp lthiirnaid hgletpaarl kvgkreigll
      301 kfaarqsgnq islvitddgg ginvdkvvak aianglysrs eidkmsdkqk enlifepgls
      361 taeqvssvsg rgvgmdvvrs niervggsie vsskpgegts fhlqlpltls iiaaltvgsg
      421 dqryaiprsy veeivfgnss hvefaqagdr rlvtfrgqrv pclalgevlg geanetcrwe
      481 dktlilvrla sgdvfalavd rvfdhedvvv kpiapaimet rlyagttlld dgrpmmlidl
      541 psiaqmrgmv ggvrtkpvgi ekeertqksk avpvmlfagl dgrhravrle lvrridtisr
      601 eaidiegdra qavidgeimt laghdtgplp eercrllrls dgehelvyav kevldaadit
      661 ddvvpseadt aiegvtligg kpiplldgha vfaryraark idhtltcrip egsewartil
      721 eplvqaagyr iageddevea dlaialaeda apitagaret irlrpepeda gddtiyrydr
      781 dallaalkri rtgraa
//
LOCUS       WP_006804238             243 aa            linear   BCT 20-JAN-2025
DEFINITION  YaaA family protein [Leptotrichia hofstadii].
ACCESSION   WP_006804238
VERSION     WP_006804238.1
KEYWORDS    RefSeq.
SOURCE      Leptotrichia hofstadii
  ORGANISM  Leptotrichia hofstadii
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Leptotrichiaceae; Leptotrichia.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Prahlad,J., Yuan,Y., Lin,J., Chang,C.W., Iwata-Reuyl,D., Liu,Y., de
            Crecy-Lagard,V. and Wilson,M.A.
  TITLE     The DUF328 family member YaaA is a DNA-binding protein with a novel
            fold
  JOURNAL   J Biol Chem 295 (41), 14236-14247 (2020)
   PUBMED   32796037
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Liu,Y., Bauer,S.C. and Imlay,J.A.
  TITLE     The YaaA protein of the Escherichia coli OxyR regulon lessens
            hydrogen peroxide toxicity by diminishing the amount of
            intracellular unincorporated iron
  JOURNAL   J Bacteriol 193 (9), 2186-2196 (2011)
   PUBMED   21378183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006857
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Leptotrichia hofstadii"
                     /db_xref="taxon:157688"
     Protein         1..243
                     /product="YaaA family protein"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=28268
     Region          2..242
                     /region_name="YaaA"
                     /note="DNA-binding protein YaaA associated with the
                     oxidative stress response [Replication, recombination and
                     repair]; COG3022"
                     /db_xref="CDD:442258"
ORIGIN      
        1 mkiiispskt kkinslpikd sgsltekepf yleitneiie kiknfsveei ekkfklknek
       61 aqnllgfyqn yeneksgnal asytgvayka ikietfdksd feyleshlvi lsalygiltp
      121 ytnvkeyrld mtnsifesks lyevwkssin eyfekedvil nlaskeyskl insdklidfe
      181 fwedsngklk qvstnskkmr gftlnyivkn kisdvkklrn itldgyvfde dmsderkfvy
      241 vkk
//
LOCUS       WP_006834616             249 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Erythrobacter sp. SD-21].
ACCESSION   WP_006834616
VERSION     WP_006834616.1
KEYWORDS    RefSeq.
SOURCE      Erythrobacter sp. SD-21
  ORGANISM  Erythrobacter sp. SD-21
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Erythrobacter/Porphyrobacter
            group; Erythrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Erythrobacter sp. SD-21"
                     /db_xref="taxon:161528"
     Protein         1..249
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=28024
     Region          22..171
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mssdfgelga glpeakdelv drkilspnhd erklpitmvv ihytemedkg faierlcdpe
       61 akvsanylig kggevvrlvp eekrawhagv sywrgikdvn sasigieldh pghkygycef
      121 pdaqfealvp lvarmvkqyd ipranvvghs dvaparkidp gelfpwdrla eyglclprpt
      181 klergdpfdn dasfylaler fgydisdghk aveafqrrwr pekidgvidg qvrailfqll
      241 ldrdrghar
//
LOCUS       WP_006835730             663 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Bacillus sp. SG-1].
ACCESSION   WP_006835730
VERSION     WP_006835730.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. SG-1
  ORGANISM  Bacillus sp. SG-1
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 663)
  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 663)
  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 663)
  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 663)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Bacillus sp. SG-1"
                     /db_xref="taxon:161544"
     Protein         1..663
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=71233
     Region          12..655
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mdnnskhfes ltaeqqqell ekydpesstr kfksgivkwi vffgllafsl fqltasifqf
       61 iprqlllsih lgfalslifl lfpaskkrsr kdkvawydii lallsivvgs ywtimqddiv
      121 srigimttad ftvgiiavvl vleatrravg lpitiiagsf llymyygrim pgflahrgyd
      181 idaivktmff tsegilgtpl yvsatfiflf llfgaflvkt gvgqyfndla vslagkrtgg
      241 pakvaifssa lqgtisgssv anvvtsgsft ipmmkklgyr kefaggveaa astggqlmpp
      301 imgaaaflmv efiggvsywe iakaaaipal lyftgiwimt hfeakriglr gltdeempdr
      361 kevfkkiyll lpiltviill fsgmsvmraa lwsivatiai sairkdtrid wrdavdalvd
      421 gartalsvaa ataaagiivg vvtktglglt manglvdlag dltnsaqgkl lltlfftmva
      481 siilgmgspt tanyvitsti aapaiillga pelaahlfvf yfgiiaditp pvalaafaaa
      541 gvsggepirt glnsaklaia afiipymfvl spellmidtt ipyllwvvft aitgmmaiga
      601 amigfwyrkv taiervlcla agimliypeg mtdifglilf vimlalqffi kgkssgdkep
      661 ata
//
LOCUS       WP_006836413             350 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Bacillus sp. SG-1].
ACCESSION   WP_006836413
VERSION     WP_006836413.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. SG-1
  ORGANISM  Bacillus sp. SG-1
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Bacillus sp. SG-1"
                     /db_xref="taxon:161544"
     Protein         1..350
                     /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=40882
     Region          2..276
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mkkernhyfd nakviliflv vfghfirsfi endpyvlaly ktlytfhmpa fiivsgffak
       61 gfykkgyipk lvkklilpyl lfqviysiyy yflynkhslt idiynpqwsm wfllslfcwn
      121 illylfvrkw klpqnkglfi afavgisigf vdgvsnylsl srtfvffplf llgyymrkeh
      181 fsklrmgkvr iaatvipaav lvfmflvpef sdkwllgsks yeqlggkdll splarsmvyv
      241 lniamsfsff afvpksrhff tkwgastlyv ylihgffvkf frespyqdll ppiqsitllv
      301 aasfiltvvl ssrpltsltq plielktskl tellkdlkns kkkyieqtkf
//
LOCUS       WP_006837839             219 aa            linear   BCT 20-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Bacillus sp.
            SG-1].
ACCESSION   WP_006837839
VERSION     WP_006837839.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. SG-1
  ORGANISM  Bacillus sp. SG-1
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 219)
  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 219)
  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 11443472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Bacillus sp. SG-1"
                     /db_xref="taxon:161544"
     Protein         1..219
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=25406
     Region          75..215
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          170..215
                     /region_name="LysM"
                     /note="LysM domain; pfam01476"
                     /db_xref="CDD:396179"
ORIGIN      
        1 mrrdpyraqa eklrqkierv epkpeqepeq rrtlpkrsel hqekrkkiky plikgmlaff
       61 vllpilmygl yttldsnqng nrsivtekgq leevtyetkd ieekvksgts sidedkpede
      121 teqlaeeqet sggqetpaek vdeenliqlt eqvepvqete yqenvqvieh vvkpqetlfr
      181 iamnyynsqa giekikewnn ienhdleagq vlkiplpvd
//
LOCUS       WP_006838532             103 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Bacillus sp. SG-1].
ACCESSION   WP_006838532
VERSION     WP_006838532.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. SG-1
  ORGANISM  Bacillus sp. SG-1
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Bacillus sp. SG-1"
                     /db_xref="taxon:161544"
     Protein         1..103
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11508
     Region          1..101
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(4..5,23..24,32,35,37..38,40,43..44,46,54,59)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(23,54..55,57)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mtpftenvvn iiksiptgrv mtygqiagla gspraarqvv rilhsmsgky klpwhrvina
       61 kgqialqdde afyeqkmnle megvevglhg kinlekyrwn pns
//
LOCUS       WP_006839788             214 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Corynebacterium].
ACCESSION   WP_006839788
VERSION     WP_006839788.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 214)
  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   2  (residues 1 to 214)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..214
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21719
     Region          153..212
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 msrpsrpsst dritellrpt geedrlavef ppprvrvepl haavavavvl alvagwaflr
       61 paapepqwdt aaveappaqv vvsvvgevan pglvtleqga rvadalklaa plpqadlisl
      121 nqaqllvdgq qihvqavgaa pagpaaqppa pglvslnsas aaelttlpgv gdataaaiia
      181 hreangpfas veqlmdvkgi gpakfealkd lvgv
//
LOCUS       WP_006840659             667 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Corynebacterium
            lipophiloflavum].
ACCESSION   WP_006840659
VERSION     WP_006840659.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium lipophiloflavum
  ORGANISM  Corynebacterium lipophiloflavum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 667)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Corynebacterium lipophiloflavum"
                     /db_xref="taxon:161889"
     Protein         1..667
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=74426
     Region          9..>464
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 magakqllel twfnkdkali pseegkyaye wvdpkdpryc etrtlvidev vtgsqspkev
       61 gtqyskradl eptddnllil gesgdvleal trvpefreky lgkvkciyid ppfntaqtfa
      121 nyednlehsv wltmmrdrlv hlrkllsddg siwvhldyae nhrmrlllde vfgsgnflse
      181 fvwqkadgpr ndptyfstdq dtiiayrksd nfsvnrlprp dsmntrfsnp dkdpkgpwvk
      241 gdpcapdapn nqpmvyaiqh pitgelmyps qgscwrmspa tmfeemskwa tyelrdigdr
      301 ekraavsgvp vtearntvpa mmlaeplevs gdrvrakias getlpelvft knglgrimrk
      361 aripskgvvp rtlllneevs hsrgakkelv slfpgttafs tpkperller iihiatnpgd
      421 ivldvfagsg ttaavaqkmg rrwvtcelvd dtfnsftrpr lekvvldndp ggvtftnere
      481 pkpgvevpek fdtkkmedaa kllravrseq dlsledeaai ktalkliatr pstvrnwrgg
      541 ggftvahlsp qcfdyspeln lvtlseaatg ptlvnsvaan lnfaltpdnr nfdgkrgsmf
      601 lkviegrldr ekveellrhl gegegatlaa telepgvrqf arttdqpcqi vhipndifsy
      661 sgtqegk
//
LOCUS       WP_006842081             521 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Dysgonomonas mossii].
ACCESSION   WP_006842081
VERSION     WP_006842081.1
KEYWORDS    RefSeq.
SOURCE      Dysgonomonas mossii
  ORGANISM  Dysgonomonas mossii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Dysgonomonadaceae; Dysgonomonas.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Dysgonomonas mossii"
                     /db_xref="taxon:163665"
     Protein         1..521
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=60236
     Region          3..511
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mptlnwigkd kvinhhldvp yrilekqyth naegsenkii hgdnlealks llpeyegrik
       61 ciyidppynt gnegwvyndn vndpkikkwl gevvgkesed ltrhdkwlcm myprlkllhr
      121 lladdgaifi siddnefanl klicdeifgt ngfksvfiwk srqivdsrnq tmiskdheyi
      181 ltygksesfs lkgrisdksk ysnpdnderg awmsnsilgl ankeqrpnlh ysildpdtgi
      241 eydcppdtgw rysretmeqk ikekriffpt kkngrprekk ylnelaseft gfstilpedv
      301 gytmngtril reivpeskfn fpksfelvkt lieqatdkds ivldsfagsg ttahavlnln
      361 kqdggnrkfi lvemedyadd itaervkrvi dgygegksve gtggdfsyye lgqpmfiend
      421 ylneelplqe ihryiwytet acpfdestke hphllgvndn ssyyffydkd slttlnhefl
      481 qtikqksdty viyadncvlp kefmaknnii fkkiprditr f
//
LOCUS       WP_006842679             306 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Dysgonomonas mossii].
ACCESSION   WP_006842679
VERSION     WP_006842679.1
KEYWORDS    RefSeq.
SOURCE      Dysgonomonas mossii
  ORGANISM  Dysgonomonas mossii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Dysgonomonadaceae; Dysgonomonas.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Dysgonomonas mossii"
                     /db_xref="taxon:163665"
     Protein         1..306
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35704
     Region          219..298
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 minntqqnqt kvmlekgsne lgyslenefe lyknahslpv phsafcttfg ivgichegsi
       61 tievhqrqee hrfvegemiv llpnqtisvk dksddfkvdy fllsqtmtnd ilggisrfsp
      121 lffiymmqkh fykltkdems ryseyynlvn erlltsdsmf qreyivslir lfyldvyysf
      181 knsvlsanat pcsrkenlay qffllilkhy kenkemsfya kqlditpkyl skvikdvsgr
      241 sakdwiveyt lleiksllnn ttlniqqitl dthfstqasl grffkkhtgq spseyrlrld
      301 vqpsmf
//
LOCUS       WP_006843472             315 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Dysgonomonas mossii].
ACCESSION   WP_006843472
VERSION     WP_006843472.1
KEYWORDS    RefSeq.
SOURCE      Dysgonomonas mossii
  ORGANISM  Dysgonomonas mossii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Dysgonomonadaceae; Dysgonomonas.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 315)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Dysgonomonas mossii"
                     /db_xref="taxon:163665"
     Protein         1..315
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34566
     Region          3..313
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mfinsigcyv pktripndyf teingltsdw inqrtgiltr srasqeetid ymsskaiesa
       61 lpdlpynied idliifasyt psdtivttgh yvqrkynisn akvffvssac ssglnaieii
      121 ysfftsqiae kallicadrn stysddtdci sghlwgdgat ayffstesys ekdpqiidit
      181 tqglghigla sravylnpke dglkmphgkd vfiqactyma qntkdivemn gyslddltff
      241 ighqanmril knvakqlaip eekvlsniee lgntgstsal lvlaqnikki argdlicisv
      301 fgggystgsc likip
//
LOCUS       WP_006843901             403 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Dysgonomonas mossii].
ACCESSION   WP_006843901
VERSION     WP_006843901.1
KEYWORDS    RefSeq.
SOURCE      Dysgonomonas mossii
  ORGANISM  Dysgonomonas mossii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Dysgonomonadaceae; Dysgonomonas.
REFERENCE   1  (residues 1 to 403)
  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 403)
  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
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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   5  (residues 1 to 403)
  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   6  (residues 1 to 403)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 403)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Dysgonomonas mossii"
                     /db_xref="taxon:163665"
     Protein         1..403
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44564
     Region          18..61
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Site            order(33,36,85)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
     Region          81..396
                     /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 mniqllqeie rgtksalikk niinyyiqng sstitelske ldlsiptvtk ligemyddgy
       61 indygklett ggrypnlygl npesgyfigv dikqsavnig linfkgdmid ltmgvsyqmq
      121 ntpealnrlc niildfidkq tvdknkilni nvnisgrvnp esgysysify feerpladii
      181 seklngykvt idndtramty geylagcvns ekniifvnvs wglaigiiid gkvytgksgf
      241 agefghmkiy dneiichcgk kgcleteasg hamhrrlfel aqeggsslls ekilkgdnvt
      301 ldeiiaavnk edvlcidlve eigrklgeqi aglinvfnpe mviiggtvsm tedyimqpik
      361 tairkyslnl vnkdstisis klkdkagvvg acllartrlf eiy
//
LOCUS       WP_006844272             453 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Dysgonomonas mossii].
ACCESSION   WP_006844272
VERSION     WP_006844272.1
KEYWORDS    RefSeq.
SOURCE      Dysgonomonas mossii
  ORGANISM  Dysgonomonas mossii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Dysgonomonadaceae; Dysgonomonas.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 453)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Dysgonomonas mossii"
                     /db_xref="taxon:163665"
     Protein         1..453
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=52959
     Region          364..442
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mshcflqvng klkysskykr iisyililvl vvighyflmq islesfrytr rsimsmlcil
       61 clggvmmlmi rtnggraril faflmfmvgl tnllslingl itgyvgvvey kfmsipmliy
      121 gaiyayifll ypiesfrpgw ltlrralllf lpiivvvgvy lfvsriqnvp mpvpainnwi
      181 flihnfwnfn vwfgllilay pilgltimlr yqnkykewce nnyasiedmd vkwlsdyifs
      241 nfvitlscgi ivfsndvrsi lmhniiflff flygfyrvll rkspypegyf kesldeaklg
      301 areameldee ckckdiqidi sendlstkll fvnklpeymc klelwmqtek pylrkdfklt
      361 damailplnr sylsrlfneg ygesfyqfvm ryriaesknl llsrpdlnit siadlsgfss
      421 lsvfgraftr etncspmqwr nkemaekyne psf
//
LOCUS       WP_006845776             337 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Weissella koreensis].
ACCESSION   WP_006845776
VERSION     WP_006845776.1
KEYWORDS    RefSeq.
SOURCE      Weissella koreensis
  ORGANISM  Weissella koreensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Weissella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Weissella koreensis"
                     /db_xref="taxon:165096"
     Protein         1..337
                     /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=39059
     Region          1..274
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mkriewidia kgqtiflvvl vhvlegiykt nlfpeaklgl ecsmsgifli impiflalsg
       61 ylykvpqnrk yfidqfkkka wnllwpsiif sviyvglqqc aggdvheghq wsslltmgit
      121 pigylwflet lfltwllmsa lfslkiniwf qaliyvglvf vgwhvqgpli lqdvcvwsif
      181 fflgyliknn skimlqsgvv igslivllmt lyaqsqipte wydtngptpl imlgklasvi
      241 vafkffqvlh lkrtkmywln agknsliiyl vhaplasilr illlklginn fylltflili
      301 ftwelsrwva wislryrplq iifyptrwws drtkers
//
LOCUS       WP_006846597             498 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [Segatella].
ACCESSION   WP_006846597
VERSION     WP_006846597.1
KEYWORDS    RefSeq.
SOURCE      Segatella
  ORGANISM  Segatella
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Segatella"
                     /db_xref="taxon:2974251"
     Protein         1..498
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54005
     Region          6..498
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 meqssfikin padsvvvclr pmkkgetiev dgktitllqd tpaghkvlin daaegtdilk
       61 ygypighakt glkagewvne nnlktnlagt leytynpvne qlniakenrt fmgyvrknge
      121 vgvrnevwvv ptvgcvngva eklvellkke tgcegidaih awhhnfgcsq lsgdhentrk
      181 vlrdiclhpn agavlvlslg cennqpddfm kmlgdydhdr ikllvtqkve gdeleegmki
      241 lrnlyalake dkreevpvsk lrvglkcggs dgfsgitanp lvgefsdwlv aqggtsilte
      301 vpemfgaeti lmnrcenkel fdktvhlind fkeyflshge pvgenpspgn kaggistled
      361 kalgctqkcg rapvsgvlqy gdrlettgln llsapgndlv aatalasagc qlvlfttgrg
      421 tpfgtfvptm kistnsnlak nkpnwidfna galvegvemk dlvskfidki iavasgeear
      481 neyngyreis ifkngvtl
//
LOCUS       WP_006849058             215 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Segatella copri].
ACCESSION   WP_006849058
VERSION     WP_006849058.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..215
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24578
     Region          132..208
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mkqfvtllim ilcstftana qnyldhlkkk epgkgvvtvn qskaidelvn gkqvipqddk
       61 tkttpqkkek epetqhkqep dslkktepqh heanrenahv nnaqkaenkk eetetpvvdm
      121 rkkvmrksyk vtgyrvqafa ggnsrndrlk aeqtgnqlkv hfpeqpvyvh fysprwicrm
      181 gnfrslaeaq kmlakvrslg yrqaclvkgq itvqy
//
LOCUS       WP_006849969             215 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Synechococcus sp. WH 8109].
ACCESSION   WP_006849969
VERSION     WP_006849969.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus sp. WH 8109
  ORGANISM  Synechococcus sp. WH 8109
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Synechococcus sp. WH 8109"
                     /db_xref="taxon:166314"
     Protein         1..215
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23290
     Region          22..211
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mthplkavle kvgpsscptt hnfhchtvcs dgslepikli qqaterglkh lavtdhhssh
       61 ahreiqawld qqratgvlvp tvwsgmeisa llkgclvhvl algfelnhpv lqpynrgdav
      121 vgellraeav vkaihdaggl avlahparyr lghdvlidea arlgfdggea wydyemqptw
      181 saspliceai drqlsnlgll rtcgtdthgi dlcgr
//
LOCUS       WP_006851774             295 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Synechococcus sp. WH
            8109].
ACCESSION   WP_006851774
VERSION     WP_006851774.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus sp. WH 8109
  ORGANISM  Synechococcus sp. WH 8109
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Synechococcus sp. WH 8109"
                     /db_xref="taxon:166314"
     Protein         1..295
                     /product="formate/nitrite transporter family protein"
                     /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=31597
     Region          2..274
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mdyvlpnelv dgmiaaggkk stvsvknlli rgfysgailg lavilaltvg itvkapfvgs
       61 llfpfgfasi vlfgmelvtg nfallpmatw agkstwgatf rnwvwvwign wigtavvavi
      121 maisltsgtm dgaadnigpp iwdavaqkim alnqinvekk yealgsmgff laflrglvan
      181 wlvclgvtma lvsksvpgki lacwlpitaf qsmgmehivv nqflhtagpi lgsgvpftkv
      241 ifwnflpvtl gnivggmvfi gmlfysthrt pmdnvlpteh deklerelaa elgar
//
LOCUS       WP_006850255              55 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Synechococcus sp. WH 8109].
ACCESSION   WP_006850255
VERSION     WP_006850255.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus sp. WH 8109
  ORGANISM  Synechococcus sp. WH 8109
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 55)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..55
                     /organism="Synechococcus sp. WH 8109"
                     /db_xref="taxon:166314"
     Protein         1..55
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=6040
     Region          <6..52
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(6..7,10,27..30,32)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 msaneaiclh atpwqentgk pfgvprshgc vrmpmkharw lfhntpkgtp itmqa
//
LOCUS       WP_006853569             293 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Synechococcus sp. WH
            8016].
ACCESSION   WP_006853569
VERSION     WP_006853569.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus sp. WH 8016
  ORGANISM  Synechococcus sp. WH 8016
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Synechococcus sp. WH 8016"
                     /db_xref="taxon:166318"
     Protein         1..293
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31404
     Region          13..257
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mtcrcvlpia aglaegpcww sernillwvd ieasriglfd patgnndfly lpahvgavvp
       61 tsvgdlllat aaglmrmdps sgavtllldp evdrpgnrfn dgkcdpwgrf wagtmaydfe
      121 pmagalwrld gdgritrqrr qltisnglaw sqdrgtlyfi dsptlkvmaf pltssgeiaa
      181 epsicvqipe dwdavpdgmc idaegmlwia lfgggavtrw dpisgqlldr lavpcrqvts
      241 ccfggphldq lfmttarrem daaaiaaepl agglfqadvg vkglpadtfq vaa
//
LOCUS       WP_006855252              98 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [Roseburia].
ACCESSION   WP_006855252
VERSION     WP_006855252.1
KEYWORDS    RefSeq.
SOURCE      Roseburia
  ORGANISM  Roseburia
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Roseburia"
                     /db_xref="taxon:841"
     Protein         1..98
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10955
     Region          8..92
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mcqldpaikk diiacckkyn ankvilfgsr argdngpysd idlaikgadn fdrlfaelky
       61 neftlldmdi idldgrvsep lmkdilndgh ilyertgk
//
LOCUS       WP_006855893             342 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Roseburia intestinalis].
ACCESSION   WP_006855893
VERSION     WP_006855893.1
KEYWORDS    RefSeq.
SOURCE      Roseburia intestinalis
  ORGANISM  Roseburia intestinalis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Roseburia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Roseburia intestinalis"
                     /db_xref="taxon:166486"
     Protein         1..342
                     /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=38299
     Region          1..283
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mkryqyldva rgfglllvii shscglsrfl inyyiplffv vsgyiykegr sykeniehka
       61 krllipyfgy savllavyvl mgrtlaetka safgilysry clydttvvkd nvylftvang
      121 amwyltaffa aslvyhlvid rclsdrkfli gtlivltait maladipvll pwsidlacvg
      181 tifmiagtll graqffekkw nipliaavfv iyiltscldp ginmsireyg iygafsvpff
      241 iivgltgsll ciwfgklien tapgrfiayv gkntifllaf hifalevver iaskfiaipv
      301 pggavvpfvl yhalritaav lgclafseil nrlkkrlrrk tr
//
LOCUS       WP_006855282             128 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Roseburia].
ACCESSION   WP_006855282
VERSION     WP_006855282.1
KEYWORDS    RefSeq.
SOURCE      Roseburia
  ORGANISM  Roseburia
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 128)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 128)
  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 128)
  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 128)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Roseburia"
                     /db_xref="taxon:841"
     Protein         1..128
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14849
     Region          26..115
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(45,64..65,83,86,94..95,107,112)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 msyaneeiev lkhddfckek lhfeglcidk fkrivvrdgn eieltytefe illllaqnag
       61 ivfskeqiyn svwkepyfgd ynivmshirn irekiednps kpiyiqtvwg vgyklneklk
      121 cagiaesl
//
LOCUS       WP_006856573             219 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Roseburia intestinalis].
ACCESSION   WP_006856573
VERSION     WP_006856573.1
KEYWORDS    RefSeq.
SOURCE      Roseburia intestinalis
  ORGANISM  Roseburia intestinalis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Roseburia.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Roseburia intestinalis"
                     /db_xref="taxon:166486"
     Protein         1..219
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=25690
     Region          37..219
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mrrerrngvi msesyavnek relilqkvke fivahggivk knqleelhid yrrildfvek
       61 gdliriksgy ytirigdyse delivklfpd avltmecaly aygyikrkpy gyqiavdknt
      121 sksrfklefp qvtpfyaepe tlqsgvdrid fgnakmqifd kdrliceclk yedkmeravf
      181 qegvlsyikd ekknianlmk yarerrvvkk vqsmigvwl
//
LOCUS       WP_006857292             611 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: VirB4 family type IV secretion system protein
            [Lachnospiraceae].
ACCESSION   WP_006857292
VERSION     WP_006857292.1
KEYWORDS    RefSeq.
SOURCE      Lachnospiraceae
  ORGANISM  Lachnospiraceae
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales.
REFERENCE   1  (residues 1 to 611)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 611)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..611
                     /organism="Lachnospiraceae"
                     /db_xref="taxon:186803"
     Protein         1..611
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=69718
     Region          41..607
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mnnnrkkktq tqtpgeerlk sfldmiapsv iqfytdhyic gntfrsvwal reyptatdeq
       61 ailrhlgekd gvtlriytrq vtpaeekkii snaanknrmk qgntenlqet vtaasnlqdv
      121 tniiatmhrn repllhtavy lelsaadmdk lkllqtevlt elirsklnvd klllrqkqgf
      181 lcvhpagrnv fleqferalp assvanlfpf nysgktdkng fyigrdkfgs nvivdfnqra
      241 ddktnanili lgnsgqgksy llkliqtilr esgmkvicld peheyvdltg nlggcfvdlm
      301 sgeyiinvle pktwdengsp edteapyafr cssklsqhis flkdffrsyk nftdsqldti
      361 eimlaklyek wnigddtdfg rltpkdypil sdlydlmeee ykhydakkkq lytaellqei
      421 clglhsmckg aeskffnght nitdssfltf gvkgllqask nvkdamlfnv lsymsnellt
      481 nghtaacide fylfltnlta veyirnfmkr vrkkdsavil asqnledfni dgireytkpl
      541 fsipthvflf nagnidsrfy idtlqleqse ynlirypqrg vclykcgner ynlmvhapey
      601 keklfgsagg r
//
LOCUS       WP_006858930             240 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Roseburia intestinalis].
ACCESSION   WP_006858930
VERSION     WP_006858930.1
KEYWORDS    RefSeq.
SOURCE      Roseburia intestinalis
  ORGANISM  Roseburia intestinalis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Roseburia.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Roseburia intestinalis"
                     /db_xref="taxon:166486"
     Protein         1..240
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26748
     Region          6..203
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mqingylydt hvhtsegsac gqntgaemar ayqkagyagi vvtdhffygn taadrslpwk
       61 dwveqfckgy ehakeegdki glqiffgwes gyhgtefliy glnkewlleh peikdadvke
      121 qyelvhaggg ivshahpfre edyipeirlf pdcvdavegi nathespast shknilynek
      181 aiayakehgl pitagsdqht trmigggmlf drklsdekdf cravlageak aywngsefyg
//
LOCUS       WP_006860491             382 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Marvinbryantia formatexigens].
ACCESSION   WP_006860491
VERSION     WP_006860491.1
KEYWORDS    RefSeq.
SOURCE      Marvinbryantia formatexigens
  ORGANISM  Marvinbryantia formatexigens
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Marvinbryantia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Marvinbryantia formatexigens"
                     /db_xref="taxon:168384"
     Protein         1..382
                     /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=41946
     Region          1..327
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mkqreyaydn lkfllivlvi aghladfyte pggnasgsla vaarglygli yifhmpafif
       61 vsglfaksal sdksramkrt geflvlyilc klllglpsml lrctfdfqll sesgipwfml
      121 smalwyamay vlekcrvilk kwnvpvilaa nialacilgy tgvigdflcl sktivffpff
      181 wmglhmdagk ltdkvskpvc ravgavgill fvlaaviqpe flyalrplln grgdayaqva
      241 enfanmypqv daaagiagta glmtgtvsga gitgllakpa ygvfwrlahy aaaafliycl
      301 lavipkkkla vsvcgertlq vyflhyifly plkivpvvek mqtvlptavc llfilvvsal
      361 lavllsarfi tvlferfhri wk
//
LOCUS       WP_006859919             283 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Marvinbryantia
            formatexigens].
ACCESSION   WP_006859919
VERSION     WP_006859919.1
KEYWORDS    RefSeq.
SOURCE      Marvinbryantia formatexigens
  ORGANISM  Marvinbryantia formatexigens
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Marvinbryantia.
REFERENCE   1  (residues 1 to 283)
  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 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   3  (residues 1 to 283)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 283)
  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   5  (residues 1 to 283)
  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   6  (residues 1 to 283)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Marvinbryantia formatexigens"
                     /db_xref="taxon:168384"
     Protein         1..283
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31908
     Region          21..102
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..279
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mewierlnda mdyleghlte eidyeklgki accssyhfqr mfaymagvpl seyirrrkms
       61 laavdlqsgn mkiidvagky gynsptafnr afqsvhgmap savknegisv kafppvrfki
      121 tvkgveemny rietkeafri vgvsvplhkd ieknfaaipp kweeisangt lqkligmmdt
      181 ppmgvlgist cndtepwryy iavstsqenn dleeyvvpaa twavfpgegt nqsiqelerr
      241 ivtewlptsg yeygdapdve vylnpdpqna qyevwipvvk ken
//
LOCUS       WP_006861216             246 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Marvinbryantia
            formatexigens].
ACCESSION   WP_006861216
VERSION     WP_006861216.1
KEYWORDS    RefSeq.
SOURCE      Marvinbryantia formatexigens
  ORGANISM  Marvinbryantia formatexigens
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Marvinbryantia.
REFERENCE   1  (residues 1 to 246)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Marvinbryantia formatexigens"
                     /db_xref="taxon:168384"
     Protein         1..246
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=26892
     Region          154..231
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mrkwlwtvfl lficiagiaa slylykqddr qgpvitvese nvtyyaggdt svllkgvtam
       61 detdgdlten imieaiypsa dgtsaeiiya vmdksnnvtk akrnvkyvde sqqtqgetda
      121 ggqiketepq itetqeasek aeavgresel keaklaiing snvagvaaml qerfreegfq
      181 nisigsyqgq ieetviyten velgellkey fpeanienem vssgidisvt lmdaciivgq
      241 tdaekl
//
LOCUS       WP_006862474             338 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Marvinbryantia formatexigens].
ACCESSION   WP_006862474
VERSION     WP_006862474.1
KEYWORDS    RefSeq.
SOURCE      Marvinbryantia formatexigens
  ORGANISM  Marvinbryantia formatexigens
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Marvinbryantia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Marvinbryantia formatexigens"
                     /db_xref="taxon:168384"
     Protein         1..338
                     /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=38367
     Region          9..288
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 medrlkindn iktammlavv lyhccmfftg swfdrstpvf sanylsvfar ylntfhvqtf
       61 amasgflfya lkkeygkysg nfrvdigkrt krlllpyait nivwvlpfyi vfsgfdvkai
      121 vykyvfgcap sqlwflpmlf wlfllayvvf rkhrpsevgl iasvlisigg gyilstigvk
      181 nvlqivtavr yamyyyfgty lyekeikpst sltvmsvifs vggfalssql agsnlfvlka
      241 vnilvssfts fagifmvygf anligckedn riwrglkkns fgvylfhqql iypcimllng
      301 rvnpviqvvi cfmvlgfiss giteflrkwk atkvmfgl
//
LOCUS       WP_006862237             253 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Marvinbryantia
            formatexigens].
ACCESSION   WP_006862237
VERSION     WP_006862237.1
KEYWORDS    RefSeq.
SOURCE      Marvinbryantia formatexigens
  ORGANISM  Marvinbryantia formatexigens
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Marvinbryantia.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Marvinbryantia formatexigens"
                     /db_xref="taxon:168384"
     Protein         1..253
                     /product="formate/nitrite transporter family protein"
                     /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=26339
     Region          9..252
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mfqedykaas ntalaksnfl kknpagyfis smmaglyiaf gsilmgivgg ymtgqpaqkl
       61 vcgiifsvgl cfvtvagael ftgnnfvmsv galkktvtwa qtakvwvvcy lgnlvgsvva
      121 agiftmtgip gsgdvgaffe ntavakatgt panlfakail cnilvcvaiw cgtrlksega
      181 kivmnfccvg tfvtcgfehs ianmtflsvg mmngaavglg gflynllivt lgnmvggivf
      241 valpyyfisk eka
//
LOCUS       WP_006863668             102 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Marvinbryantia
            formatexigens].
ACCESSION   WP_006863668
VERSION     WP_006863668.1
KEYWORDS    RefSeq.
SOURCE      Marvinbryantia formatexigens
  ORGANISM  Marvinbryantia formatexigens
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Marvinbryantia.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Marvinbryantia formatexigens"
                     /db_xref="taxon:168384"
     Protein         1..102
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11229
     Region          8..98
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 menticqktg ikekvlaalk qyaqecnier vilfgsrarg dfkersdidl avfggntdkf
       61 tiladeeapt llkfdivnlg aavepelraa ikeegillye ki
//
LOCUS       WP_006864729             318 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 5'-3' exonuclease [Gordonia].
ACCESSION   WP_006864729
VERSION     WP_006864729.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..318
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33495
     Region          1..309
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mlldgaslwf rsfyalpekm tspdgrpvna vrgfidtian lvtrehptrl vvcldldwrp
       61 efrtalipty kahrvavedg atdatgteti dveevpdtlt pqvdmimnvl aaagiatsga
      121 vgceaddvig tlaweeakdp vivvsgdrdl lqvvsddpvp vrvlyvgrgl akaemmgpve
      181 vgekygvpad ragigyaems mlrgdpsdgl pgvqgigekt aakliseygs ldaleeaard
      241 ssskvptrar kallaaadyl eaartvvsvr tdaetidsgp dllpsepadp ealaalveel
      301 gigasvsrls kalgwpka
//
LOCUS       WP_006865241             393 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Gordonia].
ACCESSION   WP_006865241
VERSION     WP_006865241.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 393)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..393
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=42860
     Region          150..388
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mnrdatviav svdpyhravv ayghrsavsi aelfveqvlm pisprarfer rsdlqwlisl
       61 saddgghdal idaarrklga htvsdgdrsa fldvcmgvav sadlravsde tdlvrhadaa
      121 lcvaltrrvh vefahpgmvr qisaevdlaa wltrsverdf svfyqpivam adrrvvgyes
      181 llrwhtesgv lapdaflava egisllapig rhaigeaird lagdisemag eeafvslnls
      241 gqqlsdeglv ryidglirdh hvepsrvwie vredqvirle tsaartvngl hdlgcticvd
      301 dlgagfsalr yvrdlpvdvl kvdrtliaql vhshsdravv raisemaaat glrmvaegie
      361 sddvlevlte fgfdyaqgff fgrpeplasw tgq
//
LOCUS       WP_006866443             184 aa            linear   BCT 20-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Gordonia
            namibiensis].
ACCESSION   WP_006866443
VERSION     WP_006866443.1
KEYWORDS    RefSeq.
SOURCE      Gordonia namibiensis
  ORGANISM  Gordonia namibiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 184)
  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 184)
  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 11443472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Gordonia namibiensis"
                     /db_xref="taxon:168480"
     Protein         1..184
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=19436
     Region          <63..182
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          133..181
                     /region_name="LysM"
                     /note="LysM domain; pfam01476"
                     /db_xref="CDD:396179"
ORIGIN      
        1 mrtatlidpv rstvpvrstv pvrgdvlqrp rpmrrgdgrr pvdgrpvses avrvrriast
       61 qcaspvglrg rgpvvpasrp aqtapsavir rrrrtatail agvglalavw viavvgqnya
      121 atvtpssvgt evvhvrsgds lstiasrvap empreavvde ivqlndlpss glrvgqplla
      181 pryh
//
LOCUS       WP_006866531             360 aa            linear   BCT 20-JAN-2025
DEFINITION  DNA polymerase domain-containing protein [Gordonia namibiensis].
ACCESSION   WP_006866531
VERSION     WP_006866531.1
KEYWORDS    RefSeq.
SOURCE      Gordonia namibiensis
  ORGANISM  Gordonia namibiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Zhu,H., Nandakumar,J., Aniukwu,J., Wang,L.K., Glickman,M.S.,
            Lima,C.D. and Shuman,S.
  TITLE     Atomic structure and nonhomologous end-joining function of the
            polymerase component of bacterial DNA ligase D
  JOURNAL   Proc Natl Acad Sci U S A 103 (6), 1711-1716 (2006)
   PUBMED   16446439
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Zhu,H. and Shuman,S.
  TITLE     A primer-dependent polymerase function of pseudomonas aeruginosa
            ATP-dependent DNA ligase (LigD)
  JOURNAL   J Biol Chem 280 (1), 418-427 (2005)
   PUBMED   15520014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Gordonia namibiensis"
                     /db_xref="taxon:168480"
     Protein         1..360
                     /product="DNA polymerase domain-containing protein"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=40424
     Region          4..314
                     /region_name="LigD"
                     /note="Eukaryotic-type DNA primase [Replication,
                     recombination and repair]; COG3285"
                     /db_xref="CDD:442515"
ORIGIN      
        1 masrspaeel dvdgvavrls npdkiyfpel genggrkrdl vgyyrtlalg vddsgdgplm
       61 ratrdrptfl qrfpdgvege eiyqkhiakk rpehvqstpi vfpskrtgda irptmpadlv
      121 waanlgtvtf htwptlhpdn dhpdqlridl dpqpgttfdd vrnvaidglk plldelgftg
      181 fvktsggrgi hvyvpieplw dfiatrrcvi aiarelerrd pdrvttswwk eergerifid
      241 ynqnardrtm aspysvrrsa igrvstpvtw deladvdpdd ctmatvpkll edrgdpwagi
      301 adhrrgienl lemvqeddan gladmpypps ypkmpgeppr vqpskkvaeh wdekgnrigd
//
LOCUS       WP_006867795             206 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Gordonia].
ACCESSION   WP_006867795
VERSION     WP_006867795.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..206
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22435
     Region          17..201
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mtellpldpd qllsttrsvr krldydrpvp ldvvkealev alqaptgsns qtwhwivltd
       61 pelkqkvady yaqsfakyya aqqprdetgk rvassaqyla dtmgqvpvlv igaiytggdl
      121 pegnqagvwg sllpgawslq lalrarglgs awttlhlaye keiaellgip agihqgvllp
      181 vayytgtdfk paprkpldsv lhidgw
//
LOCUS       WP_006867814             341 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Gordonia namibiensis].
ACCESSION   WP_006867814
VERSION     WP_006867814.1
KEYWORDS    RefSeq.
SOURCE      Gordonia namibiensis
  ORGANISM  Gordonia namibiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 341)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Gordonia namibiensis"
                     /db_xref="taxon:168480"
     Protein         1..341
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36285
     Region          5..337
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mtpnpvglvd latylpekvv raayyaqyae edtladnvmf rapafrhhaa dgetsadmmi
       61 satrdllerh gddflddvdv vlthsqlpev pvrgcggela hrlgirpstv ldvhnggcaa
      121 fifmieiaga llraggghka llglaqnsag qvftqeqvrg kaqaaipgdg aavavltldd
      181 vdaspilglr chsfgqysgd mtgvsdpprk yweagsgqmh igftdskiak vlargnrmvp
      241 evaievadei gispsdldwf vtnqpsrifl rnwrealelp dshhpdtfde cgnlfavaip
      301 vtldaaisdg rigegdvvmm aafahagdfa gaaamrwagr p
//
LOCUS       WP_006869208             328 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Legionella
            drancourtii].
ACCESSION   WP_006869208
VERSION     WP_006869208.1
KEYWORDS    RefSeq.
SOURCE      Legionella drancourtii
  ORGANISM  Legionella drancourtii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 328)
  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   2  (residues 1 to 328)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Legionella drancourtii"
                     /db_xref="taxon:168933"
     Protein         1..328
                     /product="aminoglycoside 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=37820
     Region          56..238
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mnqdnpnrei inwgyntlks lgftlksslp ekvqdtpwsc vmrfitdqgl iylkqtpeql
       61 alealitqvl ytqyqapvpe iiahhtelhc flmkdagrpl reilktrfdv nlfrhameqf
      121 sllqimvaar idaffamgvp dwrldnlpnl yrqllsqkei lladgllevd idelkrllpt
      181 vsslcnqlsd yaiqetlvqc dfhdnnilie eqsknstfid lgeivishpf fslvgclrqv
      241 kthhaltdkd eaylqliday lgnyinfdfk erllealqla qvlwciyeal aqyrlrlace
      301 ptrfmlvqrh gklsgrlkef mslvhgcs
//
LOCUS       WP_006869288             107 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Legionella drancourtii].
ACCESSION   WP_006869288
VERSION     WP_006869288.1
KEYWORDS    RefSeq.
SOURCE      Legionella drancourtii
  ORGANISM  Legionella drancourtii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (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   2  (residues 1 to 107)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Legionella drancourtii"
                     /db_xref="taxon:168933"
     Protein         1..107
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11284
     Region          29..100
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkvvpfiaaa lalsiailpa hasaspkkap ekqtvvatnk idlnkadass ltgsfkgigk
       61 kradaiiayr dshqgfksie elaevkgigq hfmaanrekl nevfvin
//
LOCUS       WP_006870854             201 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Legionella drancourtii].
ACCESSION   WP_006870854
VERSION     WP_006870854.1
KEYWORDS    RefSeq.
SOURCE      Legionella drancourtii
  ORGANISM  Legionella drancourtii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 201)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Legionella drancourtii"
                     /db_xref="taxon:168933"
     Protein         1..201
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=22303
     Region          <102..184
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mnkllwagll lclgltscve ydestlitdd agyvhrtvhy tkdkrgrnyf pmkikatgek
       61 rfvfdpkasa waaydeegnr lltgagsagv dtceenstqs crtvtgtfhi ynkkglncrs
      121 geypvdtrgg akmpycmyfy qgftihaayd vpehpsshgc vrvfpsaakw lnenfmrvgt
      181 kviilaypdq ngvysstaqs f
//
LOCUS       WP_006871304             423 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Legionella drancourtii].
ACCESSION   WP_006871304
VERSION     WP_006871304.1
KEYWORDS    RefSeq.
SOURCE      Legionella drancourtii
  ORGANISM  Legionella drancourtii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 423)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Legionella drancourtii"
                     /db_xref="taxon:168933"
     Protein         1..423
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=47026
     Region          66..233
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 msalllwila vtsaylpplp vdfpqqkkaa tedfhlisvv apvlsagqvs aqaisdlelm
       61 lhnqaptlnq qvinkvlmtl kcateynvdh nniltvidys lpsnekrlwv fdlkekkllf
      121 htyvshgiks galvsnyfsn kynskassig vyqtqkayyg rdglslrldg ldrsfndnas
      181 nrsvvmhsgw yveegfikky grpgrswgcp alpltnsqai intikdksll viyypsdnwf
      241 sksrflncdk laaaqitnnf tleipatapd dqrdailfvg sgykgkrtes npvavisadm
      301 yqrifhtsap ltrmlrrqin saeyialsrt elnylannsn vataeqaegl nvisfvipvi
      361 kevrggyyet qmqivnlgki kevkvnggsp rennsgnsft vyfegkpain lnatsqfirw
      421 vgl
//
LOCUS       WP_006872871             224 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Legionella drancourtii].
ACCESSION   WP_006872871
VERSION     WP_006872871.1
KEYWORDS    RefSeq.
SOURCE      Legionella drancourtii
  ORGANISM  Legionella drancourtii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 224)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Legionella drancourtii"
                     /db_xref="taxon:168933"
     Protein         1..224
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24506
     Region          42..209
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mntlltiist vlltsnmtts ppsfatgsdi ntlvqhlgsk aprldknvlk laltayknas
       61 rkgavkkpvl tvidyslpsn kqrmwvfdvn rerllyntyv ahgknsgnnr ashfsnvnss
      121 kesslgtyit kgtymghkgy slnlqgldkg fndnaysrrv vihgawyvep dfikksgrag
      181 lswgcpaiaq tlakpvinti kngsvifayf pdkkflshsg ylva
//
LOCUS       WP_006872575             234 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Legionella drancourtii].
ACCESSION   WP_006872575
VERSION     WP_006872575.1
KEYWORDS    RefSeq.
SOURCE      Legionella drancourtii
  ORGANISM  Legionella drancourtii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 234)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Legionella drancourtii"
                     /db_xref="taxon:168933"
     Protein         1..234
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=26262
     Region          2..219
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mdlscafqpi vdvnenkvfs yealvrgknn esasyvfsqi pkedllifdq qakkvaiala
       61 aklkigcyin lnflpctlqs tgsyiseile faeqhhlarn qiivevteee visdpqnfsr
      121 finkyramgi kvaiddfgag yaglnllvdf lpdiikldin lirnihnhgs lqaivkailq
      181 icidlgidvi aegietldey ywlkshnikf fqgflfakpg feslplvfyp dllv
//
LOCUS       WP_006873371             387 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Anaerotruncus colihominis].
ACCESSION   WP_006873371
VERSION     WP_006873371.1
KEYWORDS    RefSeq.
SOURCE      Anaerotruncus colihominis
  ORGANISM  Anaerotruncus colihominis
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Anaerotruncus.
REFERENCE   1  (residues 1 to 387)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Anaerotruncus colihominis"
                     /db_xref="taxon:169435"
     Protein         1..387
                     /product="amidohydrolase family protein"
                     /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=39887
     Region          1..340
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mssiviknig tilsgdidnp ilkgdtivvt dgkiaaigga eiangieaek vidaagstvt
       61 pglfdthvht slgdyahrqf asnfiegelh ggvttiisag echtpgrpkd pagtkalail
      121 ahksfaalkp ggvkvhggsv ilekglvekd feemakegvw tvgeiglgsv kdpadaapmv
      181 ewahkngmkv qmhtggtsip gsstvtaaqv matkpdvish inggptaipl sevdklmdet
      241 dfameivqcg npkvtdyvar rakekgqlgr iifgndapsg tgiiplgilr nicqvasvsd
      301 ipgeialcma tgnsakvynk lntgiiavgr eadlvfmdap mgsvantave afecgdipgl
      361 siimvdgvik aaksrntppc kraakvi
//
LOCUS       WP_006874119             636 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Anaerotruncus colihominis].
ACCESSION   WP_006874119
VERSION     WP_006874119.1
KEYWORDS    RefSeq.
SOURCE      Anaerotruncus colihominis
  ORGANISM  Anaerotruncus colihominis
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Anaerotruncus.
REFERENCE   1  (residues 1 to 636)
  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 636)
  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 636)
  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 636)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Anaerotruncus colihominis"
                     /db_xref="taxon:169435"
     Protein         1..636
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=68365
     Region          2..629
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 meeskktgfd lkldraisiv aivmsayhli acnynifqag qhinlhilfs liivflqavk
       61 ikngkptwqs wcmiallaas vvtclyihfh yynfmtalga qpfdkvfsgv cilliiliat
      121 qrtwgwvipv isiiallygy fgpwlpnpff hgglpfsrli tyvttnfdgv ygmlasvsan
      181 tiilftifgg lmdafgaiga imnvamsast kirsggaqva vvsagligsi tgsvaanitl
      241 tgsvcmplmr krgysaefta ateaaastgg ailppvmnaa afiiaswtgi pyitlvfvgv
      301 tpallyylgi slsvyikack lgdekmkkel lpqfhhayvn lmvfliplvl lvtlmimges
      361 pqkalslail glavvgllqq fiireanpir sfakkfvagl enggrtvasi avvmacmgvv
      421 vqmmtatgls skisqfalsi agdnliilal vvaltctlfg mgmpsasayi laallgapal
      481 vsfgvplvva hffvfyfaem saltppvaig clvasglana kflktcvial rlaimgfvlp
      541 flflyrpall lqgtafewfw avlmvvcflf cfiivcekyf riqttlaeri aagvgalcci
      601 ipvyvmdfig lalflflivs qqrrvkregl asrsqa
//
LOCUS       WP_006875817             386 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Anaerotruncus colihominis].
ACCESSION   WP_006875817
VERSION     WP_006875817.1
KEYWORDS    RefSeq.
SOURCE      Anaerotruncus colihominis
  ORGANISM  Anaerotruncus colihominis
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Anaerotruncus.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Anaerotruncus colihominis"
                     /db_xref="taxon:169435"
     Protein         1..386
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=41103
     Region          <1..384
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mtfmgykrpd glvgirnhvl ilptcacase tcrvvsqqva gsihiinnsg caevkanedm
       61 tqtilrgfaa npnifgtvvi glgcenvghr elreaiekit nkpivsfgiq eeggtpntir
      121 lavraaremv aaasiqkrep cgmsnlilgl ecggsdatsg faanpalgyv sdkliamgas
      181 tvmaetieli gaehvlarrg atreihdqii tickdfedyl hamgqdcrhg qptpgnkegg
      241 lstleekslg cinkggtspi vevvaegrrp tkkgaiimdt pgydiacnta miaggcqmia
      301 fttgrgtptg haiapifkit gnratfermk dnievdvsal ttgeisiera geiiyhemme
      361 iiegkltkae tygfsdtaid ricrfi
//
LOCUS       WP_006876445              84 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Eubacteriales].
ACCESSION   WP_006876445
VERSION     WP_006876445.1
KEYWORDS    RefSeq.
SOURCE      Eubacteriales
  ORGANISM  Eubacteriales
            Bacteria; Bacillati; Bacillota; Clostridia.
REFERENCE   1  (residues 1 to 84)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   3  (residues 1 to 84)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Eubacteriales"
                     /db_xref="taxon:186802"
     Protein         1..84
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9569
     Region          11..64
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mnsfrniyns nlshraksvy mylkdradse grcwpairti alelglsrst vkralddlcr
       61 agllqkdprw rengsltsnl yhvv
//
LOCUS       WP_006876509             344 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Anaerotruncus colihominis].
ACCESSION   WP_006876509
VERSION     WP_006876509.1
KEYWORDS    RefSeq.
SOURCE      Anaerotruncus colihominis
  ORGANISM  Anaerotruncus colihominis
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Anaerotruncus.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Anaerotruncus colihominis"
                     /db_xref="taxon:169435"
     Protein         1..344
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37394
     Region          6..341
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mietavqkrf rgfsletaft thggclgilg asgcgksmtl rciagierpd agrvvvngrv
       61 lydssvrlnl ppqkrrvgyl fqnyalfphm tvaenivcgm hgekngreqm ikellarfhl
      121 eglggrypgq lsggqqqraa larmlasepd villdepfsa ldahlreqmq mqvlellesy
      181 gkdavlvths rdeayrlcge llvmdagrpi ahggtkelfr spglvqvarl tgcknisrak
      241 kagahrveal dwgisfdtad pvpedvshvg vrahsffpps gasapnliai edcgssegpf
      301 ewnilfraag tasekiwwki gkhayagvpd hlavspedvl vlre
//
LOCUS       WP_006878979             282 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Vibrio brasiliensis].
ACCESSION   WP_006878979
VERSION     WP_006878979.1
KEYWORDS    RefSeq.
SOURCE      Vibrio brasiliensis
  ORGANISM  Vibrio brasiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Vibrio brasiliensis"
                     /db_xref="taxon:170652"
     Protein         1..282
                     /product="formate/nitrite transporter family protein"
                     /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=30104
     Region          5..267
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mstdfkpaef vqtminvgea ktktstrdll lrgtmagiil slavvvaitt ivqtgmgvvg
       61 alvfpvgfvi lsvmgydlvt gvfglaplak fenrpgitws rvfrcwglvg lgnligsliv
      121 avlvavsltg nfslepnava qkfiavstar slgfenmgmd gwitcfvrgi fcnlmvclgv
      181 ignmtgrtla griammwfpi fiffalvfeh tvvnmflfpl gmilgadfgi atwlnfnlip
      241 tilgnivggl lmtciplylt haktapalse qeevnakpvl ak
//
LOCUS       WP_006879066             343 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio brasiliensis].
ACCESSION   WP_006879066
VERSION     WP_006879066.1
KEYWORDS    RefSeq.
SOURCE      Vibrio brasiliensis
  ORGANISM  Vibrio brasiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 343)
  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 343)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 343)
  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   4  (residues 1 to 343)
  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 343)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Vibrio brasiliensis"
                     /db_xref="taxon:170652"
     Protein         1..343
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38507
     Region          <83..215
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          259..340
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqviahyqpt dqrhqlgvmd valllnaves fgvrseslvn eaglaeidwy seqsqityad
       61 klklfghvnr qwpglglgll vgeqatlshf gilgyailss rtvqdaintg fkyldlngpv
      121 fsvtveverd iaairlenvl dvgemlpfcs eyflssiasl fleltgqqfk vnvihlpyqa
      181 peyharyqqr faceaefnqd elalyfnagq lalpltthna dklshylksc dslvaalqsp
      241 ylltnqikai lyqsagafpt feslavqfgc sertlrrqld qhktsyqall nevrgdlake
      301 yllgtrltve eigfrlgysd sanfrrafkr wtgmtpqqfr aev
//
LOCUS       WP_006879347             457 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein [Vibrio
            brasiliensis].
ACCESSION   WP_006879347
VERSION     WP_006879347.1
KEYWORDS    RefSeq.
SOURCE      Vibrio brasiliensis
  ORGANISM  Vibrio brasiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 457)
  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 457)
  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 457)
  AUTHORS   ter Beek,J., 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 457)
  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 457)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Vibrio brasiliensis"
                     /db_xref="taxon:170652"
     Protein         1..457
                     /product="CmpA/NrtA family 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=51173
     Region          30..311
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mkwktlakqs fsavtlttlf ylpssfaeig epeledlkfg fikltdmapl avayekgffe
       61 deglyvtlea qanwkvlldr vidgeldgah mlsgqplgat igigtkaevi tafsmdlngn
      121 aitvsnktwq qmkphipmqa dgkpvhpika dalkpvvesy ldqgkpfnmg mvfpvsthny
      181 eirywlaagg ihpgyyapda gdnsgqinae vmlsvtpppq mpatmeagti egysvgepwn
      241 qqavfkgigv pvvtdyeiwk nnpekvfgvs kswaekypnt hirvvkalir aahwlddnnn
      301 anraeavkll akseyvgadf dviansmtgt feyekgdvre vpdfnvffrh natypyysda
      361 iwyltqmrrw gqisqqkpdq wymdvakkvy rpdiyqqaaq alvedgvlse kdfpdfdqed
      421 gfrapqthfi dnivydgrtp ndylkqfsig lkgkdkv
//
LOCUS       WP_006879508             324 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Vibrio
            brasiliensis].
ACCESSION   WP_006879508
VERSION     WP_006879508.1
KEYWORDS    RefSeq.
SOURCE      Vibrio brasiliensis
  ORGANISM  Vibrio brasiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 324)
  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   2  (residues 1 to 324)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Vibrio brasiliensis"
                     /db_xref="taxon:170652"
     Protein         1..324
                     /product="aminoglycoside 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=37122
     Region          23..236
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mnqdfylpli selgyrnins levlqtlwgg ygqlvrlhld ggsiivkhiq lpqpahhprg
       61 wntelshqrk lrsyqvelnw yqntagncfa rvpkplkviq hddelllvme dlkqagfsev
      121 vtqaskshls aclrwlaefh aqhightgee lwevgtywhl dtrpdellal kdselkqqak
      181 ridqvlrdap yqtlvhgdak lanfcftpdg qqaaavdfqy igrgcamkdv alfissavep
      241 eqceeleewl ldeyfahles avkthqpels aedvelawrp lfaiawadfq rfvkgwspgh
      301 wkinpytegl keraldmlka yper
//
LOCUS       WP_006879574             738 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Vibrio brasiliensis].
ACCESSION   WP_006879574
VERSION     WP_006879574.1
KEYWORDS    RefSeq.
SOURCE      Vibrio brasiliensis
  ORGANISM  Vibrio brasiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 738)
  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   3  (residues 1 to 738)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Vibrio brasiliensis"
                     /db_xref="taxon:170652"
     Protein         1..738
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=78322
     Region          6..737
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msydldedil qdflveagei lellseqlve lennpedkdl lnaifrgfht vkggagflsl
       61 telvdtchga envfdilrng qrqvsaslmd tmlkaldtvn eqfqavqdre plpraeqdll
      121 delhrlsspe sadeavaeap pvveepvaae pvipepvvet paeqtsvsag sideitqdef
      181 eklldelhgs gtapgassaa spapaapapa asadmsgdit ddefekllde lhgvgkapge
      241 neaeaptppp apaapaapaa gsadsdlmtd eefekllddl hgsgkgpsve eleaatkpaa
      301 anpppapeak papapqpava tapkeqpkpp akkeasppaa qakkpqaeat vrvdtstldt
      361 imnmvgelvl vrnrllslgl nsndeemska vanldvvtad lqgavmktrm qpikkvfgrf
      421 prvvrdlars lnkditlemr gedtdldknl vealadplih lvrnsvdhgi empearvasg
      481 ksrtgkvils asqegdhiel aivddgggmd pdklrgiavk rgimdedaas rltdkecfnl
      541 ifmpgfsske qisdisgrgv gmdvvktain tlngsidids emgkgtkiti kvpltlailp
      601 tlmvgvaghp falplasvne ifhldlsrtn vvdgqltiiv reksiplfyl qnwlapragq
      661 velrkghghv vivqigsqrv gfvvdtligq eevvikpldn llqgtpgmag atitsdghia
      721 lildvpdllk qyaaasri
//
LOCUS       WP_006880147             294 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio brasiliensis].
ACCESSION   WP_006880147
VERSION     WP_006880147.1
KEYWORDS    RefSeq.
SOURCE      Vibrio brasiliensis
  ORGANISM  Vibrio brasiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 294)
  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 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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Vibrio brasiliensis"
                     /db_xref="taxon:170652"
     Protein         1..294
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33020
     Region          27..179
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          210..290
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtlaelmqdy verkqlhqle giteteikgv hfyrsskgns rqpfvyqsgv ivlgqgtkni
       61 ylgnepvryg pddylvvgvp mpleceafae ngepllglsi didpqllhrl vnkldsmhcf
      121 qsrhevstnp glksvamdem mldvckrlmk alcnpietai langlmeela frvllsqegy
      181 vlfdlarheg hyarvaksld ylhknyteav tvqdlaeqan msisafhqaf rsvtletpiq
      241 yikkvrlnka keliqleglk agdaarlvgy nstsqfsref krhfnetpka nvsa
//
LOCUS       WP_006882102             841 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: VirB4 family type IV secretion system protein
            [Enterobacteriaceae].
ACCESSION   WP_006882102
VERSION     WP_006882102.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 841)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 841)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..841
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..841
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=94837
     Region          222..797
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mstnksnars inkkalegki phyrypvtds ismigdnklm atvkiagypy eladdselys
       61 nynlfrtylv sigkdmagql glwtyidkre ilvndvyksn nvfiqkfvdk ymerfntggr
      121 yyesvyyitl iynygqssie dgikkldsvi kmsekicgpf glsvlqndgy mnesanflsw
      181 linhhdfkvp lvedpiykvv gnserifgyd islirnanda qdkycvsytl rsfpakikpg
      241 aldfilsipc eltfaqsyiy trqltaisii dgqankinst naaideegta lnsiknlvqn
      301 gevflgdyhg vvsvygktak eaydnailve sgfsaagyvl lratdeqedv fisslpdakk
      361 rplntvrsts tladqfslhn fsvgkrtgnp mgdgtammpv etlqggihyl sttdsdpakd
      421 vvgepesghg iflgqtgtgk ttlqasltsf verfnpmlfg idfkqsmrlp mmmlgaqyfv
      481 lregeftgln pfqldeikma tddngivdqa faeqikerir qfcyswveri ganseggldd
      541 gdsakivrav davmelpreg rrfsnvlemi aasplrnrlm efsayanggr mgryawavds
      601 penkfdpllf drvafdstvi lkkqpngkph paaeillavl ffykdlmkin prkkgrwtif
      661 sceefwmpan fpltqeqlkq slkagrmdye mcwlisqqpv daincaifne ineqttirvl
      721 lpnpnakwqh ykeigitrke frklkslakt srtflikksn tsvfgtmdlh gfdeflpvls
      781 gdkygvqaae eiikrigssd pndwipifiq enarnhklrk aehddeeegi eyedteyeda
      841 e
//
LOCUS       WP_006886584             192 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Mycoplasmopsis anatis].
ACCESSION   WP_006886584
VERSION     WP_006886584.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis anatis (Mycoplasma anatis)
  ORGANISM  Mycoplasmopsis anatis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Mycoplasmopsis anatis"
                     /db_xref="taxon:171279"
     Protein         1..192
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=22707
     Region          11..192
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mlevffsknd lltvreaknl gisryklfnl vkkgylerlk ngiykkretl ndefaaisvk
       61 nenvvfsyht alflydlsdr vpnifhisvp qgynvrhikk htnsirvhyi krenfelgis
      121 eiktpygnkv kiydlertic divsqrrnid rqiyvdalkg yfkrndknlr klikysvilg
      181 veeeirkyie il
//
LOCUS       WP_006886905             143 aa            linear   BCT 20-JAN-2025
DEFINITION  division/cell wall cluster transcriptional repressor MraZ
            [Mycoplasmopsis anatis].
ACCESSION   WP_006886905
VERSION     WP_006886905.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis anatis (Mycoplasma anatis)
  ORGANISM  Mycoplasmopsis anatis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Chen,S., Jancrick,J., Yokota,H., Kim,R. and Kim,S.H.
  TITLE     Crystal structure of a protein associated with cell division from
            Mycoplasma pneumoniae (GI: 13508053): a novel fold with a conserved
            sequence motif
  JOURNAL   Proteins 55 (4), 785-791 (2004)
   PUBMED   15146477
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11478503
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Mycoplasmopsis anatis"
                     /db_xref="taxon:171279"
     Protein         1..143
                     /product="division/cell wall cluster transcriptional
                     repressor MraZ"
                     /GO_function="GO:0000976 - transcription cis-regulatory
                     region 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=16303
     Region          1..123
                     /region_name="PRK00326"
                     /note="transcriptional regulator MraZ"
                     /db_xref="CDD:234728"
     Site            order(73,75,103,110,119..120,123)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293784"
     Region          81..85
                     /region_name="DXXXR"
                     /note="DXXXR [structural motif]"
                     /db_xref="CDD:293784"
ORIGIN      
        1 mfgtverkid dknrivlptn frdllgsdfy ltigfdgnge lrskenfiey trtieqqsmf
       61 nknaralrrs ilgrainitl dssgrfllpk nilenlaiqk dvvfvgvgsi veiwskeryd
      121 efestydndt isqiaqelsn les
//
LOCUS       WP_006887147             224 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Rothia aeria].
ACCESSION   WP_006887147
VERSION     WP_006887147.1
KEYWORDS    RefSeq.
SOURCE      Rothia aeria
  ORGANISM  Rothia aeria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Rothia.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Rothia aeria"
                     /db_xref="taxon:172042"
     Protein         1..224
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=26224
     Region          85..215
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mpnnewrpaa lwafkayegd kdflnyflkk lerfvaglli rrihsnyraa kyaellrqll
       61 ngdgleakaf dlsaeekqem mkqlnteiyl qpqyicryil mhlnslaagh yevsnnkkia
      121 iehvlpqhpd pdsgwsqnft epaveywtnr lgnllplnrk krrteaqgfe fekkkevyfg
      181 sivsdsiift lteqvinete wtptvvearh rhmlntlydv wslk
//
LOCUS       WP_006887939             262 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YaaA family protein [Rothia].
ACCESSION   WP_006887939
VERSION     WP_006887939.1
KEYWORDS    RefSeq.
SOURCE      Rothia
  ORGANISM  Rothia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Prahlad,J., Yuan,Y., Lin,J., Chang,C.W., Iwata-Reuyl,D., Liu,Y., de
            Crecy-Lagard,V. and Wilson,M.A.
  TITLE     The DUF328 family member YaaA is a DNA-binding protein with a novel
            fold
  JOURNAL   J Biol Chem 295 (41), 14236-14247 (2020)
   PUBMED   32796037
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Liu,Y., Bauer,S.C. and Imlay,J.A.
  TITLE     The YaaA protein of the Escherichia coli OxyR regulon lessens
            hydrogen peroxide toxicity by diminishing the amount of
            intracellular unincorporated iron
  JOURNAL   J Bacteriol 193 (9), 2186-2196 (2011)
   PUBMED   21378183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006857
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Rothia"
                     /db_xref="taxon:32207"
     Protein         1..262
                     /product="YaaA family protein"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=28092
     Region          2..227
                     /region_name="YaaA"
                     /note="DNA-binding protein YaaA associated with the
                     oxidative stress response [Replication, recombination and
                     repair]; COG3022"
                     /db_xref="CDD:442258"
ORIGIN      
        1 mlillppseg ktaaeatnap vqfadlsfpe ltgeretvle qlaavsaqet aleqlkvgas
       61 leaevrrntr llhepahaai qtytgvlfea ldygsfspae rqlaqrtili ssalwgvvrp
      121 edaipayrls mgvklgelgq lanfwrgals salapvvage lvldcrsaay akswvtpgaq
      181 tlavrvervs adgtrkvvsh makhyrgela rylvrsglae rdftadadga aalvealean
      241 wdvewvagte rkagtltvli rq
//
LOCUS       WP_006890310             191 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Methylobacter].
ACCESSION   WP_006890310
VERSION     WP_006890310.1
KEYWORDS    RefSeq.
SOURCE      Methylobacter
  ORGANISM  Methylobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Methylococcales; Methylococcaceae.
REFERENCE   1  (residues 1 to 191)
  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 191)
  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   3  (residues 1 to 191)
  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   4  (residues 1 to 191)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 191)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Methylobacter"
                     /db_xref="taxon:429"
     Protein         1..191
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21454
     Region          1..191
                     /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"
ORIGIN      
        1 mntlnillie dettdqllek tliakgysvt ntvpsetnip slamtnktdl vifnidspkk
       61 yfphihylnr nqplpiiifa addtsdtikq ivkagvsayv vngletsrin siiniavarf
      121 keqqrltnel ektksrleer klidrakgil iktrgftedd ayhtlrklam drniaigema
      181 kniiamaell k
//
LOCUS       WP_006888353             402 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Rothia aeria].
ACCESSION   WP_006888353
VERSION     WP_006888353.1
KEYWORDS    RefSeq.
SOURCE      Rothia aeria
  ORGANISM  Rothia aeria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Rothia.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 402)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 402)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Rothia aeria"
                     /db_xref="taxon:172042"
     Protein         1..402
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44594
     Region          6..395
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mpeiladvyk kgilaghfsr tddgatayty astyletssk plsptlplst dsyrreggal
       61 ppfftgllpe grrltglrkh lktsaddelg mliavgedtv gdvqivspnt qpaqlvipda
      121 geliqsedfq titfselinr hsiidpaaip gvqdkvsgkm ltlplrssed fyllkisppe
      181 ypqvvenesf flkaasriha spqvvshrlv hdatgrsgil irrfdryide hgiahrlaae
      241 dacqlsnryp sdkylltaeq csealltqvf spriaapevf rqfvyawltg ngdlhaknls
      301 ivenrkgqye lspiydipst apygdksmal llsgkkdgls rrrfltfahn igvssrvaeh
      361 vleevltgte hlaeqareel pfdshrmkel lkvlknrrrs ll
//
LOCUS       WP_006890887             740 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Methylobacter tundripaludum].
ACCESSION   WP_006890887
VERSION     WP_006890887.1
KEYWORDS    RefSeq.
SOURCE      Methylobacter tundripaludum
  ORGANISM  Methylobacter tundripaludum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Methylococcales; Methylococcaceae; Methylobacter.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 740)
  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   3  (residues 1 to 740)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Methylobacter tundripaludum"
                     /db_xref="taxon:173365"
     Protein         1..740
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=80358
     Region          1..727
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          <269..>332
                     /region_name="nfrB"
                     /note="glycosyl transferase family protein; PRK15489"
                     /db_xref="CDD:237974"
ORIGIN      
        1 mipdeylqtf vveckelleq meealliveq aeqdpeiina ifraahtikg sagmfgldpv
       61 vefthaaesv ldrvrsgeva mtsvlaalfi eahdhlkeli ghvaegshpa eatdnhgktl
      121 iarleaylge tpaeqpgnsg ssdnsgempv iqtanvereh sdavvgtdlw hlslrfgpev
      181 frngmdpfsf vrclaslgsi eelvtvidai paaaqmdpes cylgfeisfs sdadklaids
      241 lfnfvrsdcf irilpprska seyqrliqel peqemrlgei lvkcgtltpe eldnilrlqs
      301 qhgdapqrpi gevlveqqmv sspvveaala kqqqvkdnkk seaslirvda ekldelinlv
      361 geliiagagt nliarragma elmestatls rlvedvrdsa lalrmvqigg tfnrftrvvr
      421 dvskelgkdi dlvisggdte ldktvvekig dplthlvrns mdhgieaael rlargksakg
      481 tlrlnayhda gsivievsdd ggglnkekil nkaierglva eganlsdkei ynlifeagfs
      541 tadavsnlsg rgvgmdvvkr niqalrgsvd ldsiegqgst irirlpltla iidgfmvgvg
      601 nasyvipldm vvecvelnaw asdegdgqyl nlrgevlpyr rlrdhfvidg dmvqrenvvv
      661 vrygehkagl vvdklmgefq tvikplgklf sseksiggft ilgsgevali vdvpglmgqi
      721 ehereagevv pftrsgvvmh
//
LOCUS       WP_006891755             628 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Methylobacter tundripaludum].
ACCESSION   WP_006891755
VERSION     WP_006891755.1
KEYWORDS    RefSeq.
SOURCE      Methylobacter tundripaludum
  ORGANISM  Methylobacter tundripaludum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Methylococcales; Methylococcaceae; Methylobacter.
REFERENCE   1  (residues 1 to 628)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 628)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 628)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 628)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 628)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 628)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..628
                     /organism="Methylobacter tundripaludum"
                     /db_xref="taxon:173365"
     Protein         1..628
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=69107
     Region          4..628
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msissqghsk rqvtvlalsa igvvfgdigt splyavkevf gshlpidkph vlgvlslifw
       61 sltlvvttky aifimrannk geggimalma lalqsandnp kkarfiitig llgaalfygd
      121 siitpaisvl saveglqiia pslshyvlpi aitvlsalfi vqakgtgavg kmfspimclw
      181 failgilgin niintpavla avnpyyavhl llelgwhgfl imgavvlait gaealyadmg
      241 hfglkpirya wfsfvfpall lnyfgqgall ldhpeavknp fylmaptwam ypllilstla
      301 sviasqavis gafsvtrqai qlgycprmni shtsgqevgq vyipainwll mvsvfvvvls
      361 fesssalasa ygiavtgtmi vdtllafivi kgiwqwkksa svaflttflt vdflflssns
      421 lkiptggwlp liigavlflm mttwikgral laeymderrv lfedledkii shqavtvkgs
      481 aiylaksvhg vpqvflhnfe hnhvlheqim vltivtkdep yvdvahriki rafgknnnfy
      541 rvklyygfmq npdvrqaleq caqeglnidf kqtsffigse rvsfrkkspm pkwrrplfrf
      601 lfhnassaie ffkipvervi elgiriel
//
LOCUS       WP_006891767              77 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Methylobacter tundripaludum].
ACCESSION   WP_006891767
VERSION     WP_006891767.1
KEYWORDS    RefSeq.
SOURCE      Methylobacter tundripaludum
  ORGANISM  Methylobacter tundripaludum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Methylococcales; Methylococcaceae; Methylobacter.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 77)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 77)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 77)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Methylobacter tundripaludum"
                     /db_xref="taxon:173365"
     Protein         1..77
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8214
     Region          2..77
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 msikvryfas lkesigrsed nlefsgpatv gdvwhranpd ktlpdnslaa vnmdyvelns
       61 avkdgdevaf fppvtgg
//
LOCUS       WP_006893481             733 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Methylobacter
            tundripaludum].
ACCESSION   WP_006893481
VERSION     WP_006893481.1
KEYWORDS    RefSeq.
SOURCE      Methylobacter tundripaludum
  ORGANISM  Methylobacter tundripaludum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Methylococcales; Methylococcaceae; Methylobacter.
REFERENCE   1  (residues 1 to 733)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..733
                     /organism="Methylobacter tundripaludum"
                     /db_xref="taxon:173365"
     Protein         1..733
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=79887
     Region          48..733
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mkfirsnrpv tllqlssplf isfllvnags aamaqeqpkt vkagkkttea vspvelktme
       61 vteksdrkle tasaevalsp ggvslvnine lhdrnvssva dffryvpgvw atsqsgndev
      121 fitgrgsnld annfagsgvk flqdgmpvta adgnnhnrmi dplassfatv arggnafkyg
      181 asalggaidf tsptahdspt arlslsggsf gqflgrgtvs kvfndsfdgl ltlegkewdg
      241 yrdhnkqdrf glysnfgwqi sdsvvnrtfv syiknnqqlp gqltraqfda npyqastqai
      301 ggnyqlntet ervankttwt iddkssfdvg fsfenqhlyh pivdtvhffp gdtadrfsll
      361 vdsvqqdwgt sarynlrlds helllgvnyg tnsdkggnyt nvggmrgpmt nqitkeadnv
      421 eifaqdhwhi tdkwtltpal qgvfahrevn narlpipqda nfnvysqggn psndysginp
      481 slglmynltk ssslygnvsr lyapptnyni sdnitaglnt tnlkamegts veigtrgtqk
      541 lgnlntvnwd lslyyswlnn eilsttppgg sakaanfdnt ihagieglig gsfaldgkgt
      601 htikpmltyt inhfnfdndr nyannalpaa pkyflkgeai yhhasgffmg ptfdvvgkrw
      661 gdyantykid aygllgmrtg wsndhykvfl egrnlldtky vantnimnaa tatdamlnag
      721 aplsfyggie ity
//
LOCUS       WP_006893605             797 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Methylobacter tundripaludum].
ACCESSION   WP_006893605
VERSION     WP_006893605.1
KEYWORDS    RefSeq.
SOURCE      Methylobacter tundripaludum
  ORGANISM  Methylobacter tundripaludum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Methylococcales; Methylococcaceae; Methylobacter.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 797)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 797)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Methylobacter tundripaludum"
                     /db_xref="taxon:173365"
     Protein         1..797
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=88124
     Region          9..796
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mvkirkiily ggltlasvaa ialgggfwvm hrsmpqldgt vqldrltaev rvqtdahgmp
       61 vinaanrvda vralgyvtar drlfqmelmr rksagrlaei fgdmaldsdi rartygfhre
      121 akailaklpp ahqqylqsya dgvnrymaes gklpfeftvl gyqpgpwtpe dsllvvlgmc
      181 enltageerg ermlsvmekt lpdaamrflt pdtdfyteql qkqaeslrpa qaipvealat
      241 althqssdtp plaqlvqqsd lmvgsnawav ggkktwdgra ilandmhlgi svpntwyrie
      301 lnygavhaag ltlpgtplli agsnrhiawg atnlsgdfld lvrleinpan pdqyrvgeqw
      361 qrfdeypeti ivkgsaakqi vvkqtrwgpv anqplldqpv aihwtaldad afnlnlfdle
      421 qgetleeavt ivngsggpql nvlladdkgs iawtvmgkip krfgndglvs rswadgrvgw
      481 ngyvepedlp rvidppegil asandrrfgk nypyvighqf gngyrayrit rqltqmprig
      541 ewamfdlqld tesefyvfyq qlalnsltaa viarqpdlae ardyllawng radtgslgfa
      601 llvefrkqli eavftpllsa srdadknfsy swtyidtplq allnekppra lpdaahyrnw
      661 ddfilgqlkh glqqvqaqhp gvplmelnwg eqnkvkqshp fskalpilsd lldmprealp
      721 gcgfcvraag pgfgaserlv vspghfedai lhmpggqsgq plspyyrdqq gywlkglsmp
      781 ltagkpehml llqphgk
//
LOCUS       WP_006895292             263 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Gordonia].
ACCESSION   WP_006895292
VERSION     WP_006895292.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 263)
  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 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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..263
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28301
     Region          1..262
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          183..261
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mtrpdvpsdr gvlrpeslpe fhrlpaigat adlvrwfwic rwqlptgrvs rqevigfgal
       61 nlvvqhdhvv vagattrish rdlagtgwav gallrpaaag alpirpaehl dtvtvvsapd
      121 lhaavstemt tgmgsppdpa aaaetvgrwl rarasltdea llanravtal esdpalirvd
      181 qsaelfgise rtlqrltaky vglspaalir rrrlqeaahr vrtrpdesla eiaaelgytd
      241 hahmtrdfas vlgftpsryr agg
//
LOCUS       WP_006897926             205 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Gordonia].
ACCESSION   WP_006897926
VERSION     WP_006897926.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 205)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..205
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=21728
     Region          84..203
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(153..154,157,177..180,182)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 maevasgnrl rsgvrgyaap lalataalvv tvalllhltw ntnsaavqpa thaaavpast
       61 isdpaairaa gsaecrtnap grrlirvsls qqamwmcdgr rpvssspvtt gnvargdgtp
      121 tgtwtvqsre tnrdlvgpgy rdhvrywlpf fgdfgfhdap wqktafgdre afktagsrgc
      181 vhvpgpemkh lydwaevgtt vtvae
//
LOCUS       WP_006899428             316 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Gordonia paraffinivorans].
ACCESSION   WP_006899428
VERSION     WP_006899428.1
KEYWORDS    RefSeq.
SOURCE      Gordonia paraffinivorans
  ORGANISM  Gordonia paraffinivorans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Gordonia paraffinivorans"
                     /db_xref="taxon:175628"
     Protein         1..316
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33179
     Region          1..309
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mlldgaslwf rsfyalpekm tspdgrpvna vrgfidtian lvtrehptrl vvcldldwrp
       61 dfrtelipsy kahrvavedg atdptgasti dveevpdtlt pqvdmimdvl aaagiatsga
      121 vgceaddvig tlaydeakdp vivvsgdrdl lqvvaddpvp vrvlyvgrgl akaemmgpve
      181 vaekygvpve ragmgyaems mlrgdpsdgl pgvagigekt aakliseygs ldaleaaand
      241 passlptrar kallasadyl ekartvvcvr tdadtidsgp dtlpsepadp ealdalveel
      301 gigasvgrls kalgws
//
LOCUS       WP_006899802             331 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Gordonia
            paraffinivorans].
ACCESSION   WP_006899802
VERSION     WP_006899802.1
KEYWORDS    RefSeq.
SOURCE      Gordonia paraffinivorans
  ORGANISM  Gordonia paraffinivorans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Gordonia paraffinivorans"
                     /db_xref="taxon:175628"
     Protein         1..331
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=36145
     Region          1..321
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msikvigank rygdfaaldd vsidipdgql tsllgpsgsg kstllraiag ldtldsgtvi
       61 indtdvskks pqkrdigfvf qhyaafkhlt vreniafglk irkrpkkevd akvdqllevv
      121 gltvfqkrfp aqlsggqrqr malaralavd pkvllldepf galdakvrdd lrrwlrrlhd
      181 evhvttvlvt hdqqealdvs driavlnkgr ieqvgtpddl ydrpanefva sflgstvrln
      241 gelvrphdir igrtpemasp ttdpnldvgi iratvqrvvn lgfetrvelv sastgeefaa
      301 qitrgdqnal nlqpgetvya ratkvaaldg v
//
LOCUS       WP_006895609              78 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Gordonia].
ACCESSION   WP_006895609
VERSION     WP_006895609.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 78)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 78)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 78)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..78
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=7755
     Region          1..78
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 miiryfagaa eaagrseqta dgsaavgdlk arlsgelgpe fervlsccsi lvdgvratde
       61 tvaaadatvd vlppfagg
//
LOCUS       WP_006899989             791 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Gordonia paraffinivorans].
ACCESSION   WP_006899989
VERSION     WP_006899989.1
KEYWORDS    RefSeq.
SOURCE      Gordonia paraffinivorans
  ORGANISM  Gordonia paraffinivorans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 791)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 791)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Gordonia paraffinivorans"
                     /db_xref="taxon:175628"
     Protein         1..791
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=85275
     Region          7..768
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 msitgspvie atveilrdah giphvlastp egavygqgra caldrrwqie wmrlraegrt
       61 aevfgascve wdvfarrael dvaarrihda ssertrrllq ayadgvnstl sefgnadgat
      121 hpealefeal dhtprpwqpw tpisvfimhh vlfgrfttkl frlhacrflg ldalafwdfe
      181 kreadptvpa mpnqafldei laltdptgtp atgetldlgd pmsgsnawgv sagrsstgsp
      241 ivagdphrfl elpgiyqqfh lastdpsasf dmlgfafagv pgvphfaqgp eiawgitnam
      301 adyqdlyieq ltrddsgall veapggervp artrseqidv rdaepvavqv ittpngtvvf
      361 ggpdetfams lrspllseev tfdapldllf artvadveaa lsawvepvnr aviahadgtv
      421 athlagrvpa rapenhwlpv pgwderyqwr gyepgtlhep gfdatlpdgg vtvtanqris
      481 gvpplqptst ecvehfrasr itarldelts vspedcadih rdvrldqaav vqgllarvvg
      541 ntpaaeeirq rildwdrtmt adstdaylfa efrsqlvrav aatdalaplr gphgfptvlq
      601 pwfvpeprla taitsvveks aligidieav alsaldavvt rvealggape wgtvhvlapi
      661 hgfdlvgasp dhpelfarlr ptplplagdt ecvfanasav gthvcitgsa aryvwdlsdp
      721 sasrwivplg asgdprsghf qdqaadwaag rllpverdwd vlrgpttdph tapattstpt
      781 slstqedscq p
//
LOCUS       WP_006902887             298 aa            linear   BCT 20-JAN-2025
DEFINITION  prolipoprotein diacylglyceryl transferase [Thermaerobacter
            subterraneus].
ACCESSION   WP_006902887
VERSION     WP_006902887.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacter subterraneus
  ORGANISM  Thermaerobacter subterraneus
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiales Family XVII. Incertae Sedis; Thermaerobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002130
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Thermaerobacter subterraneus"
                     /db_xref="taxon:175696"
     Protein         1..298
                     /product="prolipoprotein diacylglyceryl transferase"
                     /EC_number="2.5.1.145"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008961 -
                     phosphatidylglycerol-prolipoprotein diacylglyceryl
                     transferase activity [Evidence IEA]"
                     /GO_process="GO:0009249 - protein lipoylation [Evidence
                     IEA]"
                     /GO_process="GO:0042158 - lipoprotein biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33040
     Region          6..252
                     /region_name="Lgt"
                     /note="Prolipoprotein diacylglyceryltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0682"
                     /db_xref="CDD:440446"
ORIGIN      
        1 mevnwdpvli qigplairwy gffmavsmaa glyvlvrdgi rrgydeefly nasaliivgg
       61 ivgarlvyvl tnpgdyfapg rygeiirvdh gglslhgall ggglagwwyi rrrlpgpawp
      121 hfqrlldlav pgvaigymlv rignlfngev lgnfttalpf prhpvqlyas aaglgllllh
      181 qrlarrrppa gylfwsflyy yqwwrvavee tvrdapiawp vyanpaygie iltvtqvttw
      241 pllvlawwlr krsleqdidp vwepgdpare pgdgvgldga tradgaprat edgsegeq
//
LOCUS       WP_006903042             665 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Thermaerobacter subterraneus].
ACCESSION   WP_006903042
VERSION     WP_006903042.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacter subterraneus
  ORGANISM  Thermaerobacter subterraneus
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiales Family XVII. Incertae Sedis; Thermaerobacter.
REFERENCE   1  (residues 1 to 665)
  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 665)
  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 665)
  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 665)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Thermaerobacter subterraneus"
                     /db_xref="taxon:175696"
     Protein         1..665
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=69401
     Region          27..660
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mardgaegig pvrareaapa vapgpvpgsd dvdelverye gvtrrprgpl avvirvlavv
       61 malyhvwatf ayipahpmra ihlgfglali lllypasgrq drhripwvdg vlallavvtm
      121 aylvvfyrev ayriirpetp dlvlgtlall lvleaarrtt gwvlpllava flaygflgpy
      181 fpgmwghggy sfsrligqmy lslegifgvp lgvsatfiil ftlygallda sgagrffvdl
      241 slalvgrhra gpgravtaas fllggpsgsg vatavtlgai twpllrragy saeragalls
      301 aggigavisp pilgaasfii aeilrvsyld virwavvptv lyylcillmi eldaargavr
      361 pvvaeapplg rllrgygfhl tslvaivafl lagytaayav mwsmalavav sylrrdtalt
      421 prklvealdr garsalsvva ttavagiivg vlnltglglk fsslvlalsg gqlvptllls
      481 avvllllgla lpitasyiva avtvapalvq vgvpepaahm ftfyyavlse vspptalscf
      541 avsaitggnp frtmwltwry alpaflvpfl ftlspagmnl lldgpglavl ratltavagl
      601 aalvagvagw lrgparwyer vllvaggmal mypgshvdla glvlgaaava lhlaggrsra
      661 paaaa
//
LOCUS       WP_006903045             723 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Thermaerobacter subterraneus].
ACCESSION   WP_006903045
VERSION     WP_006903045.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacter subterraneus
  ORGANISM  Thermaerobacter subterraneus
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiales Family XVII. Incertae Sedis; Thermaerobacter.
REFERENCE   1  (residues 1 to 723)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 723)
  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   3  (residues 1 to 723)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..723
                     /organism="Thermaerobacter subterraneus"
                     /db_xref="taxon:175696"
     Protein         1..723
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=75279
     Region          11..701
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mtgdpwldls deerqlflae ggelldqlea glldletgqa gpgtvhavfr aahtlkgsaa
       61 tvgldgmaql thamenrlda wrqgqaapap geisrllaav dslramlaav aagntppppp
      121 aelvsalasp pppdaaaple epaagtaaag parwlveael dpaclmpavr alqvllalee
      181 qatlvasepp rdgleatwag nrvrawvedt gpaerlqqmv aavpdvaavr vvpaeggrqp
      241 apapagaplq dpgaaprpag avhapaaana vptgegaepe gpvlaglpdp apagaaagpl
      301 aagrpapapa gedrtirvdv alldrllnlv gelvvergrl gqlgqelgrr pavhdladel
      361 frvtgqiari tgalqdavlq armlpvarif rrfprlvrdl almlgkevel elvgedteld
      421 rtlhevvadp llhlvrnald hgieapeerr ragkpatgrv rlvaareghh vlirveddgr
      481 gldpqrlrra avekglispd raaalsdrea fdlmflpgfs taarvtgvsg rgvgldvvrq
      541 rleqaggrve vhsrlgqgta ftlvlpltla tlrallvevg dyvyalplsd vgeavrvtpg
      601 elrslqgrwv ttvrgqvvpl lwlrqfgdpr fgpqpgdepl vavlverrgq piglvvdrll
      661 geqevvvkgl gellagtrgl sgatilgdgr lalildtptl vaelaaaaag paaaragegg
      721 ppr
//
LOCUS       WP_006903071             503 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Thermaerobacter subterraneus].
ACCESSION   WP_006903071
VERSION     WP_006903071.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacter subterraneus
  ORGANISM  Thermaerobacter subterraneus
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiales Family XVII. Incertae Sedis; Thermaerobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Thermaerobacter subterraneus"
                     /db_xref="taxon:175696"
     Protein         1..503
                     /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=53242
     Region          35..>225
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mtggnpgsgd aavlrrpqrg varagrqpls pcparvaald varglsislv vlghtplpaw
       61 ingplstlrl pllffvsgyl fnwdrygtrp gqlvrqrarr lllpylaggl mtylfwllar
      121 raaspeaqav pwwwplagwl ygsasagwlv fnlplwylpa afcgqvlfwg llrlvarrpp
      181 llqaaaalaa glagialgrh aplpwsldva laaqpffwag wfarqagrtr pgrpgprpwp
      241 raaeaaeaeg aaggaggllp gdataapgrc gtdhdagpet gwttvapamp altggraraq
      301 aagpsllpgr lgrpgavllg lglwlvalve ngavaintrq yghpfwfysg giaacvlalh
      361 latalarlpl acrtlaylgq hsmvvlvfhv glafpvlawl laalagdpll dawglywlwg
      421 lgftaalarl vqpfprltla legampqrag slwprrpeqr aptagrpapa raardrksgh
      481 pgrpagraqp ghhpqtrwhg aad
//
LOCUS       WP_006904159             151 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Thermaerobacter subterraneus].
ACCESSION   WP_006904159
VERSION     WP_006904159.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacter subterraneus
  ORGANISM  Thermaerobacter subterraneus
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiales Family XVII. Incertae Sedis; Thermaerobacter.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Thermaerobacter subterraneus"
                     /db_xref="taxon:175696"
     Protein         1..151
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=16261
     Region          20..147
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkgmsrpgag rdagsrqecr trrqrgftli elgvvlavla ilvaiavpty lrmvararea
       61 eaqqawsmvr aelwsyflqn gefpqpsgtw psgidqptpp nwdftarggg tqitvvaqpt
      121 dlnsggetlc wtldqdgqvs tnrgdacnpp s
//
LOCUS       WP_006904205             207 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Thermaerobacter
            subterraneus].
ACCESSION   WP_006904205
VERSION     WP_006904205.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacter subterraneus
  ORGANISM  Thermaerobacter subterraneus
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiales Family XVII. Incertae Sedis; Thermaerobacter.
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   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   3  (residues 1 to 207)
  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   4  (residues 1 to 207)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 207)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 207)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Thermaerobacter subterraneus"
                     /db_xref="taxon:175696"
     Protein         1..207
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=23299
     Region          1..190
                     /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"
ORIGIN      
        1 mnkpevivfg fdpagpggrl pgalldtgwp ilvqvgwpse qwlarqqadl fvmrpagier
       61 paertrtlgr vtgrpvlwmv dpgdpepegl wqhlasedwp vwallpadap kwqlvavcra
      121 lmgsagrlqq arqmvdeamr kledrkiier akgilmdrfd laeseaykrl rdtamrqrkp
      181 lreiaqsiie ftaldetgsr rsgrgrr
//
LOCUS       WP_006905403             649 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Shuttleworthella satelles].
ACCESSION   WP_006905403
VERSION     WP_006905403.1
KEYWORDS    RefSeq.
SOURCE      Shuttleworthella satelles
  ORGANISM  Shuttleworthella satelles
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Shuttleworthella.
REFERENCE   1  (residues 1 to 649)
  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 649)
  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 649)
  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 649)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Shuttleworthella satelles"
                     /db_xref="taxon:177972"
     Protein         1..649
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=69395
     Region          9..641
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 msdmnqtvss aevdavmkky dresntriwt grpglvikcv mvgfslfciy vtlfatflee
       61 irltsfmali immgflvypa krgeqrenhm pwydliftil gtgsylyftf naksivlqgt
      121 hftvlqilvg ivavaaliev trrcvgipil lvagffilya afygltnpdf fgrvrylirn
      181 lfytkegifa tpvnvaskyi vifiifgafl ertgisgffi dlansiagrf sggpakvavi
      241 ssalcgmvsg ssvgntvttg svtipmmkkt gyrpefagav eaasstggqi mppimgaaaf
      301 lmadfvgvpy sdiisraiip aflyfagifi tvhleakrlg lkgeepenlp rvkelfkkiy
      361 lllplvmlvy wvsanvmtmq kaaaicills ilvslfhkdn ritpgkivda lmaggqssit
      421 vgaacgvagi isgiitmtgl anelvngivg lagnrliial lltmlvcivl gmgvpttany
      481 aimaattapi lirmgvptla ahffvfyfgi vaditppval aayagsaiar snpmktafna
      541 srlaiaifiv pyvfcynpal llinttvpti iqitvtslig ifgvasafeg yllarihpvv
      601 rvlfalgglm lidpraltdi igivviavcv liqylasrss kggaamaga
//
LOCUS       WP_006906959             710 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Shuttleworthella satelles].
ACCESSION   WP_006906959
VERSION     WP_006906959.1
KEYWORDS    RefSeq.
SOURCE      Shuttleworthella satelles
  ORGANISM  Shuttleworthella satelles
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Shuttleworthella.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Shuttleworthella satelles"
                     /db_xref="taxon:177972"
     Protein         1..710
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=80518
     Region          98..>197
                     /region_name="pol2"
                     /note="DNA polymerase (pol2); TIGR00592"
                     /db_xref="CDD:273159"
     Region          604..676
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 mgkklkkdfk erhkasieke mlhsetniip eesklkdtdd yrgkivheke rfqdkvhekt
       61 skvsadneks ygtskrneky rdsdkgdvns aietgrsdyi tevkdekiyd plgqdldndg
      121 iidrydndfr dsdyfestyd vddnlhkkde figsssknhk aqkknykrkn ytdslytrkk
      181 edvpkenkse gkktgkdvag ekeysslskd qkkklkkdmv kvsalsglak gsetvrdyls
      241 hgsdenqgve agektadtss klihgikkys dkkgakrgyd ltnkdykirk rksklefrda
      301 kkelkktdey krasaykrfq kknqvkaais renksrlrdr ikegligtlk sskdmivrka
      361 kglmlifigi iilgtfvinf agtgmtgfmn stssvlttsy lskpnvlsei nqkfsdmeve
      421 lqsevdhvke nypgydeyil nnteyighnv hellsyitsr cgevksvsev esilkelfds
      481 mydleyreei eiryrtvtkt ytdedgneyt esheepyeyk klivtlhkke mdsiirkvfa
      541 nypdnlkhye alflaqgnmg eafgnsdlis anggigggke yeastevqkk ivnaayitps
      601 pgagwcamwv sqvyqnaglg yiggnacdmy rnytftsdrs klkvgmlvav essssgssag
      661 ltyghvgiyi gdgkvidnig rirvttlddw iatfckhhpv gfgfppnvkk
//
LOCUS       WP_006907803             139 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Facklamia hominis].
ACCESSION   WP_006907803
VERSION     WP_006907803.1
KEYWORDS    RefSeq.
SOURCE      Facklamia hominis
  ORGANISM  Facklamia hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Facklamia.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 139)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Facklamia hominis"
                     /db_xref="taxon:178214"
     Protein         1..139
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=15696
     Region          2..130
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(7..10,41..43,46,73,112,126)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mltiymdaaf dpktgeagla yviidgqsrq ynkyycsklm dnhqaefvcl rqvlrdlllv
       61 ksslnqvlai ktdskivads fdkgyvksnn yqaylseilq ladqfdlifv twlpekknrq
      121 adglakqalh rqglvevls
//
LOCUS       WP_006908636             195 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Facklamia hominis].
ACCESSION   WP_006908636
VERSION     WP_006908636.1
KEYWORDS    RefSeq.
SOURCE      Facklamia hominis
  ORGANISM  Facklamia hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Facklamia.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Facklamia hominis"
                     /db_xref="taxon:178214"
     Protein         1..195
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=23015
     Region          8..194
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mntlkkyiqe nliitnkeae elgysrhnls eltkngqler lrpglyqlkg kviddfvlis
       61 snshriifsh qtalylhdls drtpnvfhis vpqgynashi kkryedlqvh yvkkdlyelg
      121 kterkspqgt lipvydiert icdiiidrer idkqifteam kryfkspnkn lrrlikysrl
      181 fkiegeirky mevls
//
LOCUS       WP_006908378             267 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Facklamia hominis].
ACCESSION   WP_006908378
VERSION     WP_006908378.1
KEYWORDS    RefSeq.
SOURCE      Facklamia hominis
  ORGANISM  Facklamia hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Facklamia.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Facklamia hominis"
                     /db_xref="taxon:178214"
     Protein         1..267
                     /product="formate/nitrite transporter family protein"
                     /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=28978
     Region          13..264
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 menlntqsaf istiagavak kealfeqska ryfvrsmyag amlvlataag vyaadyinim
       61 npqvgkfiys flfafglsfi lflhhelvts nmmyltvgmy hqlikpkkac qilafctlgn
      121 llgaivaall vsntgafshl taesfivttv agklskglmq vfieaiaani fvniailgyl
      181 laktefakll lvfgaifmfv flgyehvvan fgsfamvafs syesdfiqvi pvllawvvaw
      241 vgnyiggglv mglvyawlnd eglslrd
//
LOCUS       WP_006909139             374 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Cyanobium sp. PCC
            7001].
ACCESSION   WP_006909139
VERSION     WP_006909139.1
KEYWORDS    RefSeq.
SOURCE      Cyanobium sp. PCC 7001
  ORGANISM  Cyanobium sp. PCC 7001
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Prochlorococcaceae; Cyanobium.
REFERENCE   1  (residues 1 to 374)
  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 374)
  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 374)
  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 374)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Cyanobium sp. PCC 7001"
                     /db_xref="taxon:180281"
     Protein         1..374
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40315
     Region          29..363
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mtlprrqllq aaaagssaal lgactirrag tttgaalpsv rwrmatswph aldtiyggae
       61 tvsrrvaems egrfqiqpfa agelvpglev leavqsgsve cghtasyyyv gknpalafgt
      121 avpfgltaqq qnawlyeagg leaingvyad fgvisfpagn tgaqmggwfk rrldgpaslr
      181 glkmripglg gkvmaalgvn vqvlpggeiy laldrgaida aewtgpydde klglaraary
      241 yyypgwwepg ptltalvnrq awrrlpkayq tmfsvacqea nlgmlsryea lnavalkrll
      301 qsgtqlvnyg eailtaaaea seqllaemaa gdrgfreihd qwrtfrrqvq dwnevneysl
      361 srftyrgkag ggds
//
LOCUS       WP_006911240             216 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Cyanobium sp. PCC 7001].
ACCESSION   WP_006911240
VERSION     WP_006911240.1
KEYWORDS    RefSeq.
SOURCE      Cyanobium sp. PCC 7001
  ORGANISM  Cyanobium sp. PCC 7001
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Prochlorococcaceae; Cyanobium.
REFERENCE   1  (residues 1 to 216)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Cyanobium sp. PCC 7001"
                     /db_xref="taxon:180281"
     Protein         1..216
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=22892
     Region          <132..208
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(165..166,169,182..185,187)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mhraatliga alalagcges qapqrqaaai tgpikielhp ndpslsfgvl prgeertvfk
       61 vgfgrngitc agsrfeegyt pvgrfkvnai lsddrfvmep alvarsgkse aelkaslfrn
      121 mnaidfdgdg etgeygigyv slapvdsvpq pfafntydgr frwysfaihg snndarigqq
      181 vtggcvnvae pvlrtlldtv klgdevvisa kgpctp
//
LOCUS       WP_006912241             107 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Salinisphaera shabanensis].
ACCESSION   WP_006912241
VERSION     WP_006912241.1
KEYWORDS    RefSeq.
SOURCE      Salinisphaera shabanensis
  ORGANISM  Salinisphaera shabanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Salinisphaerales; Salinisphaeraceae; Salinisphaera.
REFERENCE   1  (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   2  (residues 1 to 107)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Salinisphaera shabanensis"
                     /db_xref="taxon:180542"
     Protein         1..107
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11272
     Region          17..83
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mknvfvliia tvllcmsava maavninsad aetlsqlpyi gesksasiie ereangefes
       61 vddltrvngi gsktvdrird qvtvdgdsam sddgmseddt adeaqdn
//
LOCUS       WP_006912403             204 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Salinisphaera shabanensis].
ACCESSION   WP_006912403
VERSION     WP_006912403.1
KEYWORDS    RefSeq.
SOURCE      Salinisphaera shabanensis
  ORGANISM  Salinisphaera shabanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Salinisphaerales; Salinisphaeraceae; Salinisphaera.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Salinisphaera shabanensis"
                     /db_xref="taxon:180542"
     Protein         1..204
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21663
     Region          8..200
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 madpgstlta lierrhsvre ysdaaidrva lerivhcaqg gsalgkrnap sahalyplrl
       61 faviqrlnep eyapglyald tpegrlgewv ktvppealra taladdvwle laavvlvvaa
      121 dyaaarahfa dhqpdgrrge ryvhietgav lqnmhlatla qdlggvivag fddarlssll
      181 nlhaplqpva lfcigapaep sagl
//
LOCUS       WP_006912557             158 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Salinisphaera shabanensis].
ACCESSION   WP_006912557
VERSION     WP_006912557.1
KEYWORDS    RefSeq.
SOURCE      Salinisphaera shabanensis
  ORGANISM  Salinisphaera shabanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Salinisphaerales; Salinisphaeraceae; Salinisphaera.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Salinisphaera shabanensis"
                     /db_xref="taxon:180542"
     Protein         1..158
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=16131
     Region          8..141
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mtqpsplqsg ftlievmivv aiigilaaia vptysnyvar aqfsealtlv sgvktavada
       61 yqsrddldgi dngvgsipaa saitgtyven vvvadgiita tfktdsaldg ktmtliptin
      121 kdalawqctt tappakapst cneatpnnig sdtvpitd
//
LOCUS       WP_006912695             730 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Salinisphaera shabanensis].
ACCESSION   WP_006912695
VERSION     WP_006912695.1
KEYWORDS    RefSeq.
SOURCE      Salinisphaera shabanensis
  ORGANISM  Salinisphaera shabanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Salinisphaerales; Salinisphaeraceae; Salinisphaera.
REFERENCE   1  (residues 1 to 730)
  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 730)
  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 730)
  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 730)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Salinisphaera shabanensis"
                     /db_xref="taxon:180542"
     Protein         1..730
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=76727
     Region          25..713
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mnqakqapda vepavadpet lekydresrv rhalpkrvmq fvialsvlla lfhlytsfsg
       61 plvdvvqrsi hlyvllgltf vlypwamrga rdrvavgdvi lavaafaigi ymvfsadrvi
      121 asagrintld mivglaalal vidaarrvtg wglpglaivf liygfyakls fypqltesiv
      181 lastrqivsh lvyitegllg taiavsasyi ilfilfgafl vksglgrlfn dlalalagps
      241 rggpakvavv asgflgsing saianvvttg aftiplmkrt gyranfagav eaaasvggqi
      301 lppimgaaaf imaevlavpy tqvmlagiip allfylgilf qvhlramrnd legiprselt
      361 plksvllerg hlllpmvvll wlifdgrapf faafwsiaat ilicgtrnlv vglaavlval
      421 vfepqiwali esrplpglpa srlwlfaiia vpmainairn rlglesevmn lvdcrdamte
      481 gvrnsipvai acaavgivvg iatltgiald aadavvnlgq aipsemlrll vtlaltmgas
      541 ivlgmglpsi pcyiitstma apillnlplf relagsndta ifvahmfvfy fgifanltpp
      601 valaayagag isggspnatg vqamklaiag fvvpymfvfa hsmlmidatw mnvatvavtg
      661 vvgvgllava vegylrrpla apwrvlalig alaliypgwi sdglgaliav alfmtggvgg
      721 tkgrdaahsa
//
LOCUS       WP_006912722             190 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Salinisphaera
            shabanensis].
ACCESSION   WP_006912722
VERSION     WP_006912722.1
KEYWORDS    RefSeq.
SOURCE      Salinisphaera shabanensis
  ORGANISM  Salinisphaera shabanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Salinisphaerales; Salinisphaeraceae; Salinisphaera.
REFERENCE   1  (residues 1 to 190)
  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 190)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 190)
  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   4  (residues 1 to 190)
  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   5  (residues 1 to 190)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Salinisphaera shabanensis"
                     /db_xref="taxon:180542"
     Protein         1..190
                     /product="TRAP transporter small permease subunit"
                     /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=21305
     Region          4..177
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mnillgvsra idgfstfvgr mmwwltvamv ligaynvitr ylgqylgvql sanvylelqt
       61 yafdlifllg aayllredgh vrvdivysrl gprarawidi fgtlfflvpf cifglyfclg
      121 yverswavme qspnpgglar ypiktvmlva famlilqgis elikniayla rqpgfaenea
      181 hratqetegl
//
LOCUS       WP_006912758             287 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Salinisphaera shabanensis].
ACCESSION   WP_006912758
VERSION     WP_006912758.1
KEYWORDS    RefSeq.
SOURCE      Salinisphaera shabanensis
  ORGANISM  Salinisphaera shabanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Salinisphaerales; Salinisphaeraceae; Salinisphaera.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Salinisphaera shabanensis"
                     /db_xref="taxon:180542"
     Protein         1..287
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=31383
     Region          54..202
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 miaseldpcp rqpgagrlll llglvvaiag ctpatlkqrn gywadqaqta qafnhrvrfl
       61 vlhytggdea raikvltgps vsshyvvadq pprrggnpvv yqlvdehara whagrsawgg
      121 rthlndssig ieivnpgpvd tpsgtvwrgf dggqieavtt lardiiaryd iapenvvaha
      181 dispgrkidp gpafpweqly rqgigawpde ptvnayrerf ryampgiaai qsalsrygyd
      241 idttgvldqp thsvvvsfqm hfrpgrydgi pdletvarlw alndkyr
//
LOCUS       WP_006912777             260 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Salinisphaera shabanensis].
ACCESSION   WP_006912777
VERSION     WP_006912777.1
KEYWORDS    RefSeq.
SOURCE      Salinisphaera shabanensis
  ORGANISM  Salinisphaera shabanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Salinisphaerales; Salinisphaeraceae; Salinisphaera.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  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   3  (residues 1 to 260)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Salinisphaera shabanensis"
                     /db_xref="taxon:180542"
     Protein         1..260
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28554
     Region          30..232
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mttspryaei dtpqavadtf veltwnthev tirfdgtmiq ypatvvsvdr tlgrcvldmt
       61 gtadieqllk akqsfvlyar qhsaalqsga mhcigvaqss arlsvcaslp dsvallkrrg
      121 qfraalndsm avivllaspt grewqttlrd lsaggcllsl pqdeqdglev gvdgysvqal
      181 fpngetfevl ghvshryvnt etqqcylgma fdirvdkaar evwryvreve revarqtspr
      241 semrplapsp lfttptktak
//
LOCUS       WP_006912791             122 aa            linear   BCT 20-JAN-2025
DEFINITION  PilZ domain-containing protein [Salinisphaera shabanensis].
ACCESSION   WP_006912791
VERSION     WP_006912791.1
KEYWORDS    RefSeq.
SOURCE      Salinisphaera shabanensis
  ORGANISM  Salinisphaera shabanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Salinisphaerales; Salinisphaeraceae; Salinisphaera.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (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   3  (residues 1 to 122)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Salinisphaera shabanensis"
                     /db_xref="taxon:180542"
     Protein         1..122
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13423
     Region          1..122
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mseqnlaiqs givrldiadr aelcaaympf itngglfvkq qyltnayydm gadvfllmhl
       61 veqnermpva gkvvwvtprn tgsprppgig vqfaaqdnga tqqrletlla gmlenrrtsy
      121 tm
//
LOCUS       WP_006915453             111 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Salinisphaera shabanensis].
ACCESSION   WP_006915453
VERSION     WP_006915453.1
KEYWORDS    RefSeq.
SOURCE      Salinisphaera shabanensis
  ORGANISM  Salinisphaera shabanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Salinisphaerales; Salinisphaeraceae; Salinisphaera.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Salinisphaera shabanensis"
                     /db_xref="taxon:180542"
     Protein         1..111
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12170
     Region          11..107
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(15,33..34,42,45,47..48,50,53..54,56,62,67,74)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(33,62..63,65,91)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mphshdrqag adntyaavfd avrripagrv ttygriarli grpraarqvg yamhrcpsgl
       61 pwhrvinaqg rislpaasta alaqrrrlee egvvfiggkv dldrfgwpdr d
//
LOCUS       WP_006912950             343 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Salinisphaera
            shabanensis].
ACCESSION   WP_006912950
VERSION     WP_006912950.1
KEYWORDS    RefSeq.
SOURCE      Salinisphaera shabanensis
  ORGANISM  Salinisphaera shabanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Salinisphaerales; Salinisphaeraceae; Salinisphaera.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 343)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Salinisphaera shabanensis"
                     /db_xref="taxon:180542"
     Protein         1..343
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36517
     Region          1..336
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 maavidaiey mlpartesie eiaarfpnwp lekiaektgi rarhvasdde casdfgviaa
       61 rdllertgtd vgdidylifc tqspdylapt taclvqerlg lgthigaldi nlgcsgyiya
      121 lgvakaliet gqskklllit adtyskfvnp gdksvralfg daaaatlmsa rdgdeaigpf
      181 vygtdgsgaq dlivpnsglr nravdrpvee ytdrhgntrs dhniymngra vieftlrevp
      241 kaidalceka gvsldeidav vphqasatvl egirkkldlp perfvvcmed igntvscsip
      301 iavkraaakg qikpgallll vgfgvglswg atlvrlpedf aaa
//
LOCUS       WP_006916519             189 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Limosilactobacillus coleohominis].
ACCESSION   WP_006916519
VERSION     WP_006916519.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus coleohominis
  ORGANISM  Limosilactobacillus coleohominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 189)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Limosilactobacillus coleohominis"
                     /db_xref="taxon:181675"
     Protein         1..189
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=21640
     Region          63..187
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(132..133,136,160..163,165)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkftrrliil ivlvcmvllg gryffhqhle ntsithqtpt snqwqhsset kpypnvsqyp
       61 hlwilvskkr qrvylinhgr tlytmyastg sgkdnntptg tyhiqaergq sffnaksgeg
      121 arywvswknh geylfhsvpv nrqgqylvse aqelgktans hgcvrlsipd arwlyqnikq
      181 gtkvvitns
//
LOCUS       WP_006916758             358 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Limosilactobacillus coleohominis].
ACCESSION   WP_006916758
VERSION     WP_006916758.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus coleohominis
  ORGANISM  Limosilactobacillus coleohominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Limosilactobacillus coleohominis"
                     /db_xref="taxon:181675"
     Protein         1..358
                     /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=40958
     Region          3..292
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mrtkkriewi dlargiaiva vvighslgky fpgyfgnfif afhmpiffvl sgylyknksk
       61 rlllknsfln llipylttiv ielvllffyk ifpnsiiaps ktssvkefli ssiyasggav
      121 kvpyfnitli pigalwflva mffatqifnl vmtiplkksv elkrsiifla lsfigtysar
      181 fiflpfsiqp allaqiflyf gylikqynvm khiklwmsmv mlvmwlvdar ynlfafegas
      241 anhivfaivi gclsslsvmi fcqklgktyh gsiinsvlif wgrgsllmlc fhlvdldfvq
      301 iwpvvisilv pisyllaiiv gmiyrvifas fwtyliprlp ilknlydnrs qpikkifq
//
LOCUS       WP_006917216             222 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Limosilactobacillus coleohominis].
ACCESSION   WP_006917216
VERSION     WP_006917216.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus coleohominis
  ORGANISM  Limosilactobacillus coleohominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 222)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Limosilactobacillus coleohominis"
                     /db_xref="taxon:181675"
     Protein         1..222
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24936
     Region          90..220
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(166..167,170,194..197,199)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mtnwkknliy ccfcvvvlyf gavrplthqa shvaksrtsq taneksprsh hskhhqqaaa
       61 eqsirrpinw kkssetkpyp dltkvknfnv lvkikknrty lrdgkkviyt myssagnyhr
      121 daqtgsqtsd tptgtfyvqa erganffnss lneganyyvs wlnhgeylfh svptsadgsy
      181 nlkeakklgk stgshgcvrl svadaqwmme hlpvgtkvti ed
//
LOCUS       WP_006922827             796 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: penicillin acylase family protein [Bacillus].
ACCESSION   WP_006922827
VERSION     WP_006922827.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 796)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..796
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=89916
     Region          18..796
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mevvikkkrk rgkrifiwas sivlllvisa aiflniytlk smpkidgtik ledlqqavtv
       61 krdskgvphi ksenahdlyf sqgyvqaqdr lfqmdlsrrq asgmlsevvg eaavdrdklf
      121 rtlglrraae asvsqyngea kdalqsfadg vnafireake ekklpvefti lgyepaewsi
      181 vdtltigkym afdlgghwhg qafrywalkn lpkeqanelf paypkdaprl laelkntnvd
      241 vaqsfsktii ppefngsnnw vvsgeksasg kpiladdphl slatpsiwyq trlemkglnv
      301 sgvifagvpg vilghndkia wgvtntgpdv qdlyiekrnp nneneflynd kwekatvvde
      361 sikvkggkti pynvtitrhg pvisefadkg kektktvfsl kwtalepsae lkavlnmnka
      421 kdwnefetal qdfhtptqnf vfasndgtia ykangnipvr kkgdgslpvp gwtdeyeweg
      481 yipfdqlpkv inpkqgfist annkivdddy pyhisntwaq pyrqmriqef lqekekytvk
      541 dleelqmdqk nlygkeftpi flkelnkapl nevekegvdq ltkwnfydsk deaaplifhl
      601 lmkeisntlf skeipkdvle lfegksqvvd elirkevage nsvwftkygg ftkvvhtsye
      661 nvmkklqkey gpdvgewkwg dyhqlafthp isksssmlal lafnrekpvp iggsqvtvqa
      721 asygengivn hgaswrfiid tkdmsngyhi vgpgqsghfr sdwyhdqidd wvngtyhttt
      781 lntegiegkv ltlqpk
//
LOCUS       WP_006924115             313 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Candidatus Bartonella
            washoeensis].
ACCESSION   WP_006924115
VERSION     WP_006924115.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Bartonella washoeensis
  ORGANISM  Candidatus Bartonella washoeensis
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Candidatus Bartonella washoeensis"
                     /db_xref="taxon:186739"
     Protein         1..313
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=35322
     Region          1..226
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 myqidynsyr svksfnrrir flvmhytsid fkgsitaltg savsahylvp dpsektylea
       61 gfkdmrifnl vdenerawha gvsswagrnn lndtsigiei vnlatghtdc feetyieagf
      121 kdmrgfspvd rneseaagvr lpsegsnlnd kvvklgtidl atynneaftf ppynpiqiea
      181 vkelalnilq rypdiiptdv vghsdiaigr ksdpgaafpw kelyeagiga wyddelkdhy
      241 qkqfckslpd kadilaklkq ygydtlvact ergyrdlira fqlhfrqeny dgvldtetaa
      301 iiyalvdkyf psn
//
LOCUS       WP_006925447             286 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Candidatus Bartonella
            washoeensis].
ACCESSION   WP_006925447
VERSION     WP_006925447.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Bartonella washoeensis
  ORGANISM  Candidatus Bartonella washoeensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Candidatus Bartonella washoeensis"
                     /db_xref="taxon:186739"
     Protein         1..286
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32474
     Region          5..278
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 minflpysfd ilratdrdry isvlfapkkk rralaalyaf naevarires vhdpligeir
       61 lrwwydsian nemqesknnp ilsdlftais lfslpktafl rycdaqildl yhnpvetlhd
      121 lefycgetas ivlqlscqil dpdveqdfad ayehggiaqg lsgilrllsf mpsryqyylp
      181 adilkvlgvn rkeleancis neqkchiiea mvalsrehyn rfyehfsvlp ttlkpaflpl
      241 aiipaslqka lqlgaavfqe satlpllhry wlitkaavsg hlpkvl
//
LOCUS       WP_006925890             293 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Bacillus].
ACCESSION   WP_006925890
VERSION     WP_006925890.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 293)
  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 293)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..293
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33466
     Region          8..>126
                     /region_name="COG3355"
                     /note="Predicted transcriptional regulator
                     [Transcription]"
                     /db_xref="CDD:442583"
     Region          34..92
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mgslynlmkp ysefrskeef ntyqkqvlnc yrfqlnktda iiihflgkya vnekqktvgv
       61 acplmetiat nvgksirtvr rsiakleelg iikrvatker hkrggysanl yvfltsaidr
      121 mddrmqmsgc ktennatgcs kneqksaget ilsknilqik ekrkgtyeld etycrhdipk
      181 pfiyalvpmt snpkkinifw skvelaykks glleqgvlle qiladeevyg nliwrvksvv
      241 raykygeirk digallystv rdlfleigle wgaalrrskg islfdpfkke pcv
//
LOCUS       WP_006927028             201 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Caldithrix abyssi].
ACCESSION   WP_006927028
VERSION     WP_006927028.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..201
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21976
     Region          1..200
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mkrivvgisg asgmlyaarf lravpadyev hlivssvaqk ilqvelgwdv kkqpfaqfwe
       61 tfseepylga aivvhpaenh fapvasgsfi tkgmviipcs aktlsgvasg yaanlmerta
      121 dvhlkerrpl ilvlretpys lihienmkka tlagatilpa spgfyhqpqs vndlvdfvaa
      181 rvmdhlnieh qlskrwgend g
//
LOCUS       WP_006927215             401 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Caldithrix abyssi].
ACCESSION   WP_006927215
VERSION     WP_006927215.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..401
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43808
     Region          1..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mivlvinags ssvkyqvidp eeqrslargv verigmsgai lthrkegeke vrlsgeildh
       61 kmaieyvlgi llsknhgvik dkseidavgh rvvhggevfs gsvliteevm aemrrcidya
      121 plhnppnlkg inaamqllpg vpqvgvfdta fhqtmpkhay lyglpyalyk khgirrygfh
      181 gtshrfvsdr aakmlgrpke elriitchlg ngasaaaiky gksidtsmgf tpleglmmgt
      241 rsgdldpaii lqimhkeelt pndattllnk hsgligvsgl ssdmreieee yetnarakla
      301 hdiftyrlkk yigayaaamg gvdaivftgg igensslvrk nalseleflg ikldhhknee
      361 kskgerdisa aesgvkvlvi ptneelviam dtmqivsqlk k
//
LOCUS       WP_006928781             197 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_006928781
VERSION     WP_006928781.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..197
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=22482
     Region          9..197
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mqnvidifkq hygyaylkdl kaqgihtdti rklltggkie kikpglyrla dftmmshqgf
       61 vdacmaipka viclhsalsy yeltttvpav vmvavpreak aprlqyppvk vfyfshsnye
      121 egiervhtet gdfriyniek tivdcfryrk rlgedvaveg lknylrskda ninklfsyar
      181 kgrmhgvikp yvealii
//
LOCUS       WP_006928786             676 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Caldithrix abyssi].
ACCESSION   WP_006928786
VERSION     WP_006928786.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..676
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=78364
     Region          70..516
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 makieikkte lvwkgkydea grlkpvekpg pypfqivevv nqprvekgag htqlsifdyy
       61 kgdegesfee gwrnkliwgd nkmvmsslle nfagkidliy idppfatgad ftvdipvges
      121 getlhkehsi ieekayrdtw grgldsflqm myerlvlmke llsedgsiyv hldwrvnsyi
      181 rimldeilgv dnfkneiiwq kikavkaqss sygnvidsil fysksektif nqirkehkee
      241 ylkqmyryvd engrryrlhd ftqkgsgppr yfgnkgliap pegkhwiwsq ekideglkkn
      301 livfsktgmp qvkrfldeve gealsnlwnd inpigsvshe ridyptqkpe alleriiras
      361 snegdlvadf fcgsgttcav aeklgrrwig vdlsryaiht trkrlleieh sksledpkkk
      421 ygkkarpfei lnlgkyerqf wqvkafgkkd ekealyeyla filklyeaep isgsshihgk
      481 kgnalvyiga vdapvtiqev idalkdtrel gmkelhvlgw ewemglndai qevakdmgir
      541 lklriipmdv tdpravqkgd irffelayfk adiqtssrti kvklqdfvip htdliprevq
      601 dsirkwsdwi dywaidfdfr ndtfnngwts yrtkknrqlv lqaehkyekp gkykifikii
      661 difgidtsqi yeievk
//
LOCUS       WP_006929199             290 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Bacillus].
ACCESSION   WP_006929199
VERSION     WP_006929199.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 290)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 290)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..290
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32910
     Region          21..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..286
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mdslknmnaa mryiednltn eidfkevarl alcseyhfkr mfsflagisl seyircrrlt
       61 laafelknsn vkvidiaiky gynspdsfar afqnlhgitp searnsshsl kayspmtfql
      121 siqggnemny rieekepfri igitkrvpiv fngvneeias mwkslnpesi qtlkslsnie
      181 ptgiisastn fsegrmeekg eldhyigvat tkdcpeqfvq levaastwai feavgpfpda
      241 lqnvwgriys ewfpssnyel aegpeilwne qkdisspnfk seiwipflkk
//
LOCUS       WP_006929222             247 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: aminoglycoside phosphotransferase family protein
            [Bacillus].
ACCESSION   WP_006929222
VERSION     WP_006929222.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 247)
  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   2  (residues 1 to 247)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..247
                     /product="aminoglycoside 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=28391
     Region          6..217
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mvlgnpiakg ntaeiyltdd kvvklfkdyl pdtesmneak kqkyayscgl pvpnvfevkk
       61 iqnrqaiime hvkgdnigdl llnnlneaer yislcvneqk kihaihvntd emelmrerle
      121 rqiksvhkld ekqkenilnk leaikfehrl chgdlhpfnl ilsnsnvkii dwvdatsgdi
      181 gadvfrtyll yaqasvelae mylhiycrnt rlsrneifqw apiiiaarlt ekvsanniel
      241 lnklmiq
//
LOCUS       WP_006930221             355 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Caldithrix abyssi].
ACCESSION   WP_006930221
VERSION     WP_006930221.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..355
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=40221
     Region          172..326
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mneidlyisv llkfltasll lervieffdk fltligvasg kknllmrlad ipfsydeqsq
       61 rtlkkvllvq tagiiigtai cyfsglgilk elklvdsvhs rwfdillsgi fisggsepih
      121 qlinflkghk eqlaatnlkk mqeigrlssv nlqrpgqkig ityqgglypd rpghglrkan
      181 ptyivihhsg tstkasfedv vnkekqerkn argayrldps fhsvitydgv ihnycrwdsi
      241 gwhvakgprv snanslglcf vgnfrnrssg knkpseqqie agarllalwr ylydieeknv
      301 vrhsdvrrgk iicpgenfpm erlvarstql lkswkqddti lkdleqfkkq ryiyv
//
LOCUS       WP_006930613             287 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Caldithrix abyssi].
ACCESSION   WP_006930613
VERSION     WP_006930613.1
KEYWORDS    RefSeq.
SOURCE      Caldithrix abyssi
  ORGANISM  Caldithrix abyssi
            Bacteria; Pseudomonadati; Calditrichota; Calditrichia;
            Calditrichales; Calditrichaceae; Caldithrix.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Caldithrix abyssi"
                     /db_xref="taxon:187145"
     Protein         1..287
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31788
     Region          1..257
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mavdlhlhtt hsdgsltpsq lvqllkklgv ktfaitdhdt isaikqadra ahkngmrlit
       61 gvelsieypl pgsahlhllg lfidvqneel nfalkklree rknrahliir kleqmgielp
      121 ssqkeklvln nsvarphiaq illqeglvks meeafqkyig rnapayvpkk kfqlkeaidl
      181 vhragglaiv ahpvslgakt daelrdhlda lvscgidgle ayyplhdppl tryllnyaee
      241 krlavsggsd fhgeakkeiq pvigdgrlnv pdeivtqlda fyrekyg
//
LOCUS       WP_006931106             332 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Rhodococcus].
ACCESSION   WP_006931106
VERSION     WP_006931106.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 332)
  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 332)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 332)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 332)
  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   5  (residues 1 to 332)
  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   6  (residues 1 to 332)
  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 12117664
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36593
     Region          23..207
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          87..332
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtapatipsd fvrrsvvlaa angvdlapal daarisravl ahpharltpe qvtrftqktw
       61 eltgdelfgl gpgpvprgtf rvmcltlihc rdlaqalerm ievnrvlptl prlrltpgpq
      121 ttrlevvlpe pcddktrvii dfllillhrf aawlvggrvr lasvtvpyge pdpvlaknyd
      181 aifgvpvtfd adgaaleidn aalrspivqt eetledylre spnlmmserd ydstaasqvr
      241 rifesgiegr tataeevaem lsvsaphlrr llrqegtslg qlreevlrdt aiaglrrgep
      301 vdalsarlgf sepsafrraf krwtgktpra yr
//
LOCUS       WP_006931673             405 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Roseibium
            aggregatum].
ACCESSION   WP_006931673
VERSION     WP_006931673.1
KEYWORDS    RefSeq.
SOURCE      Roseibium aggregatum
  ORGANISM  Roseibium aggregatum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 405)
  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 405)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Roseibium aggregatum"
                     /db_xref="taxon:187304"
     Protein         1..405
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46721
     Region          4..399
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mnvsslprlp nrlarhlfle rhglasapkg sgkgddlaav idqlgfvqid sintvarahh
       61 milaarrpay keknlkllte rdrhlfehwt hdasviptef frhwrlrfsr dkenlinrwr
      121 nwhqneferk fdeilkrisd hgpvtsatvg edeerssggw wewhpskaal eflwrtgels
      181 vsgrngfqkv ydltervipv qhlnaahdfd ettdwaaraa ldrlgfatsg eiaafwdlit
      241 pqeakdwcta alaegtiaei evecvdgswr kvfaypetln tldalpepps rvrilspfdp
      301 alrdrkraer lfgfsyriei fvpepkrqyg yyvfpvlegd rligridmka lrsedrlhvr
      361 aywpeqgira skgrevklqa elertarfag vsdityepdw qrtal
//
LOCUS       WP_006931744             122 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Roseibium aggregatum].
ACCESSION   WP_006931744
VERSION     WP_006931744.1
KEYWORDS    RefSeq.
SOURCE      Roseibium aggregatum
  ORGANISM  Roseibium aggregatum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 122)
  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 122)
  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   3  (residues 1 to 122)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Roseibium aggregatum"
                     /db_xref="taxon:187304"
     Protein         1..122
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14033
     Region          17..117
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mphqsvskql rsnakrlrsq mtdaekklwh virahrlegi sfrrqmpieg vivdfaapah
       61 rlimeldgsq haelqgqvrd iardrkfral gwttlrfwna evmqdldgvc rkilnacgke
      121 nf
//
LOCUS       WP_006932266             344 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Roseibium aggregatum].
ACCESSION   WP_006932266
VERSION     WP_006932266.1
KEYWORDS    RefSeq.
SOURCE      Roseibium aggregatum
  ORGANISM  Roseibium aggregatum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 344)
  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 344)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 344)
  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   4  (residues 1 to 344)
  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   5  (residues 1 to 344)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Roseibium aggregatum"
                     /db_xref="taxon:187304"
     Protein         1..344
                     /product="TRAP transporter small permease subunit"
                     /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=37351
     Region          166..332
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mtaldnvqdg spvmnsggqa spesarffrl cgwivlaimt ayllnnylty wqdlpgiapi
       61 fggaangsmp ilwswvqlal yaalmllafg yvrtngntlr edsvrisnin ayliracffa
      121 vlivglvdsa isflriegfl pdvvgqalad dlgksqfrgp ylhmplials lviaaftrtl
      181 gftwlallvv aaelmivigr fvfsyeqafl adlvrfwyaa lflfasaytl leeghvrvdi
      241 lyagmstrak givnavgsvv lgislctvil vigmggkqni inspiltyet tqagfglyvk
      301 ylmagflgvf avsmmiqfva yfldavadir gepggrdhds htvq
//
LOCUS       WP_006933422             404 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Roseibium aggregatum].
ACCESSION   WP_006933422
VERSION     WP_006933422.1
KEYWORDS    RefSeq.
SOURCE      Roseibium aggregatum
  ORGANISM  Roseibium aggregatum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 404)
  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 11482063
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Roseibium aggregatum"
                     /db_xref="taxon:187304"
     Protein         1..404
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43997
     Region          1..404
                     /region_name="PRK06132"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:235709"
ORIGIN      
        1 memnsrsrrk rsllnltgaa visvaamssa fardaapetd vasepplhml vslddqkikv
       61 yrgldlievs sissgkrghs tptgvfsile kkrkhfsnly ddapmpfmqr ltwsgialhv
      121 grlpgypash gcirlpkafa qslysmterg mhvvvtrgda nplgvhhavl pqpyvaetev
      181 asltdetias dpalrgaiqe aplqanlpav qpenpyfdqp lrmiitpqka psriqvlqql
      241 lnqmgfnagp edgvmgrktr aaislyqega elpvtgqltn alegrihada gyeepqnatl
      301 rirrkfrdvy sapvtikdid qeigthvfta mdfkpgdtsv dwiavsaeee rggsatdvld
      361 rievsrkval evstmltpgs sltvtdrnft rntglgtdfv vitr
//
LOCUS       WP_006933775             273 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Rhodococcus].
ACCESSION   WP_006933775
VERSION     WP_006933775.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 273)
  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   2  (residues 1 to 273)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..273
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26961
     Region          207..271
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mgssdehdlv rsrldaiars agdrasaapt iphqadddph pwydpagtve ppgplerlra
       61 arwqtgrgga galaavgvva vlatlvvvwg drpvaepvpp lpavevaapa adpvasrqdt
      121 apdevvvsvv glvgkpglvr vapgarvada laaaggtldg adlttlnlaq rladgdqvvv
      181 gasppvppas gvsgsggegg vgepgappga gpvnlntade atldalpgvg pvtaaaivaw
      241 rrdngpftdv eqlaevdgig parlarlrtl vvv
//
LOCUS       WP_006934409             352 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Rhodococcus].
ACCESSION   WP_006934409
VERSION     WP_006934409.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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 11438136
            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="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=36055
     Region          6..346
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mtglrlrarv gsrdvdlava vesgrvlavl gpngagkstl lnviagllqp ddgrieldgc
       61 vltdtaagva vpphrrgval laqqpllfph lsvldnvafa prsagrgrsa araaalrqla
      121 avdateladr rphqlsggqa qrvaiarala adprllllde pmaaldvtaa pavrsllrtv
      181 lrgpgrtalv vthdpldala ladravvldd griveegtvr dvlsrprsaf aariaglnll
      241 agtviadgld tpvgrvrgvl dddcapgnsa vavftpaava vypgephgsp rnsfavvvge
      301 levhgatvlv raaesgitae vttsaaadla lapgatmwfv vkatevriha ar
//
LOCUS       WP_006935357             611 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Roseibium
            aggregatum].
ACCESSION   WP_006935357
VERSION     WP_006935357.1
KEYWORDS    RefSeq.
SOURCE      Roseibium aggregatum
  ORGANISM  Roseibium aggregatum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 611)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 611)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 611)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 611)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 611)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 611)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..611
                     /organism="Roseibium aggregatum"
                     /db_xref="taxon:187304"
     Protein         1..611
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=67553
     Region          205..601
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mlylvgenld rsrahyqaet gkivqlmrgi yvdagadadv dvlrhsiria rylyprayls
       61 aasavllapt rdgrlfisgp rsqrtrirtl eiiqnvapeh pavataiidd gmgefhanvs
      121 svrqrflegf rlrsehaasi deamradiar rlvdeygtpk aaadalwala renqwyrege
      181 qaeryllhtg akieirneaa ldfivawhgt highllydgf ewrwkpdegf dlpliqqrvp
      241 gqlppfilsl lpegwlervl qenderavlr sgkrymsnit istkaadlda lpadiltcrl
      301 ndfktdgift gtyagpsrgd iehsfeekla rlyasadtpr lsgvqikapm flgedgklvp
      361 stglpfthil kpagtsgfqa lpvieflama lgrhagldtp stalvampdg mppaliverf
      421 dirtspddkr rialedlcsv ldlppeakyd gtieriarav rplssepead lllllkralf
      481 awlvadgdmh lknlallkva qpdtssfetv rvaplydavt tvvfpglehd rmalkingkd
      541 nrlrradflr taaiagltas aanqaidavl trlragidav iipdvpgidq ditakaeqml
      601 rlcrervdaf e
//
LOCUS       WP_006936528             369 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Roseibium aggregatum].
ACCESSION   WP_006936528
VERSION     WP_006936528.1
KEYWORDS    RefSeq.
SOURCE      Roseibium aggregatum
  ORGANISM  Roseibium aggregatum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 369)
  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 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   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 369)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Roseibium aggregatum"
                     /db_xref="taxon:187304"
     Protein         1..369
                     /product="CmpA/NrtA family 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=39052
     Region          11..265
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mntnlkpvia gfiplldsav ivaaaelgfa eregialkli retswanird risvghfdva
       61 hmlapmpiaa slnltslavp mlapmllglg gnaitvsnal wadmaaagad pegdpastga
      121 alarviasrq ksglpmlhfg vvhpfsghay elrywlaaag idpdqdveit vlapqvmada
      181 laegqldgyc vgepwntaav eagtgriaty kqaiwpdspe kvlgvtrkwa danpdtlaal
      241 mrafsaaanw cadpknnvel agvlarpdll acpaeiclaa lsgrirldqa svkdvpdflt
      301 fsggikaapm pvygkwfyeq mvrwgqvqps keaeqevekv fsptvyleam glsgvatdat
      361 iemfddars
//
LOCUS       WP_006937053             191 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Roseibium aggregatum].
ACCESSION   WP_006937053
VERSION     WP_006937053.1
KEYWORDS    RefSeq.
SOURCE      Roseibium aggregatum
  ORGANISM  Roseibium aggregatum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 191)
  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 191)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 191)
  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   4  (residues 1 to 191)
  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   5  (residues 1 to 191)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Roseibium aggregatum"
                     /db_xref="taxon:187304"
     Protein         1..191
                     /product="TRAP transporter small permease subunit"
                     /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=20997
     Region          18..180
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mpdnpdvsdl edngqanlrt gldrliagsa klfswaifla faisvyevva ryvfdsptyw
       61 ahesttflia aifliggpva lardkhirvr miydsvspkv rrwldivnsv iamiffaglg
      121 yagvtmawka thrpngdfhl egtgtawnpp tpallkiiil icvclmfvqt lmhlikairg
      181 ddaayskrgg k
//
LOCUS       WP_006937220             309 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Roseibium aggregatum].
ACCESSION   WP_006937220
VERSION     WP_006937220.1
KEYWORDS    RefSeq.
SOURCE      Roseibium aggregatum
  ORGANISM  Roseibium aggregatum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Roseibium aggregatum"
                     /db_xref="taxon:187304"
     Protein         1..309
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=32754
     Region          55..123
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
     Region          213..287
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mlrhllatta lvaglstaai agdtaamkdg gqtgakndtg vyefelhtla pdattgilat
       61 nmvgkpvlts rnadgeeigd indvvfgrdg tvravivgvg gflgmgekev aldftrlsfv
      121 sgqenqlivv tdvsrqeleg atpyerpdyi phwmtaegar eqmdkvtasa kdtyetvrke
      181 aidpakqrld eamadpwtae ktevdaasvs tdelidstvy tnqdtdigdv aevligkdgk
      241 aqavvidvgg flgfnakpva vsysslkmfe tengdllvta pftkeqlena ptyepaayks
      301 npdavllkg
//
LOCUS       WP_006937742             100 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Rhodococcus].
ACCESSION   WP_006937742
VERSION     WP_006937742.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..100
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10546
     Region          4..95
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(28,55..56,58,80)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(28..29,37,38,40..41,43,46..47,55,60,67)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mvtrdetsii davreavaai ppgsvasygd igkrigagpr qvgramslld dnvpwwrvvy
       61 adgttaschg grapalllee gtpvagkrvd mqrarqgwmd
//
LOCUS       WP_006938287             192 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Roseibium].
ACCESSION   WP_006938287
VERSION     WP_006938287.1
KEYWORDS    RefSeq.
SOURCE      Roseibium
  ORGANISM  Roseibium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Roseibium"
                     /db_xref="taxon:150830"
     Protein         1..192
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21295
     Region          1..163
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mirrlydwtl slaagprapa algtvsfves svfpippdil lipmviarre kawwyallct
       61 ltsvaggilg yviglflfeq vavpiltfyg kmgfvdefkd iyhqygwwfv fiagltpfpy
      121 kvitiasgal glslpvfiaa sivsrgirff vvsgllylfg ppirdfiekr lglmftifvv
      181 llvggflvlr yi
//
LOCUS       WP_006938344             363 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Roseibium aggregatum].
ACCESSION   WP_006938344
VERSION     WP_006938344.1
KEYWORDS    RefSeq.
SOURCE      Roseibium aggregatum
  ORGANISM  Roseibium aggregatum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 363)
  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 363)
  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
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 363)
  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   5  (residues 1 to 363)
  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   6  (residues 1 to 363)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 363)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 363)
  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 11513304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Roseibium aggregatum"
                     /db_xref="taxon:187304"
     Protein         1..363
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39072
     Region          <45..85
                     /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; cd00092"
                     /db_xref="CDD:238044"
     Site            order(45..47,56)
                     /site_type="other"
                     /note="non-specific DNA interactions [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            56..62
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            order(57..58,62)
                     /site_type="other"
                     /note="sequence specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238044"
     Site            57..58
                     /site_type="other"
                     /note="putative cAMP binding site [chemical binding]"
                     /db_xref="CDD:238044"
     Region          93..>244
                     /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 mpdmrfappn plriadcasg lnavsvrsyn erlvlslllq hssttrleig eqtglsaqtv
       61 svlvrsleqe glvakgeaqk grvgpptvpl tlnpegaysi gisvgnrhtd ivlidfvgki
      121 rfhktlpnpq laqgsnhsef letiasavkl lpdaererla gvglalprrl sggmdeeayf
      181 kalqaeieeq lgiavfvqnd itaaasgesm fgaaktlsdy mffylgadlh grlvlnhqiy
      241 ngnsevsfdv giaalerdls aqdkevdplw drsgswpdyg alvtdweerl isqmraslhg
      301 vgqfveietv ilssyapesi cqdicrklea aapdikaiag nivpapkaig aaslpfssrf
      361 mvs
//
LOCUS       WP_006938542             170 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Roseibium aggregatum].
ACCESSION   WP_006938542
VERSION     WP_006938542.1
KEYWORDS    RefSeq.
SOURCE      Roseibium aggregatum
  ORGANISM  Roseibium aggregatum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Roseibium aggregatum"
                     /db_xref="taxon:187304"
     Protein         1..170
                     /product="TRAP transporter small permease subunit"
                     /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=18805
     Region          1..163
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mhilvifler vvrlvgqaga lflpllmiti lvnvvaryvf gigsieieel qwhlnavavm
       61 sclawayqrd ahvrvdalha rmsprtravv elcgvlflll pflwfvtgss wkifeyswkl
      121 kegspmpsgl paryiikfvm aaglsllfvq giavalksil tllpssarkg
//
LOCUS       WP_006939207             783 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Roseibium
            aggregatum].
ACCESSION   WP_006939207
VERSION     WP_006939207.1
KEYWORDS    RefSeq.
SOURCE      Roseibium aggregatum
  ORGANISM  Roseibium aggregatum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 783)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 783)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..783
                     /organism="Roseibium aggregatum"
                     /db_xref="taxon:187304"
     Protein         1..783
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=86348
     Region          234..776
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mllgtfltga aavgaaalvs srgrkyllge veqdwlanel efdqlladnq tvslkdgsfv
       61 rvfslsglsy etrniseqea largrastfh qflsagsslr vfgikrrrdv sfqadwpsvt
      121 lkevgeaeqr lyqnayslvw ymvlttktsa elektsrgll sgftdynirp vpaaqehnqp
      181 celtrvlnyl vcgelkpeia rlsagisanl pasdihvstd gaidtftphq tlnrviavrg
      241 wpetvsgmlv srllalsgel evcqivkpld stkqialftr qiteqkhnyf gtgavlaele
      301 avnedllnns gqlqetqfqi tvrarneael tslidqvtsl ldnarirycc etvgaatawf
      361 nrmpgrdkll rplkitesnv aalwpfqfsp iglwsspfgd rpvrlfktpt gqnyafqfhv
      421 sdkpqspgny lmfaptgggk stlilhllgg lakfhgvrny vfdskdgarf mieafggiyq
      481 gyqdlalnpl didltdksar hrvrlilqam lgeafdedmd dylhaaldma aelepglrtl
      541 dniygaafpa qseirrafak wvngedgaeg qfshvfnapr dqitgflqks flvginmnea
      601 lmdpvlgppv vahisaaisa aakhgeggfs ifideaanll rnngfrsvvr emyqeyrkln
      661 glvglafqep gallefdgas amienaqtlf flpnsqarpe nlqpfnlsne qiafikgegd
      721 mkggrqvlvv krfeaanfne stildvdlsg lgdalrfyrs gpsavkelek tkqewgdqwl
      781 akl
//
LOCUS       WP_006940602             349 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Roseibium aggregatum].
ACCESSION   WP_006940602
VERSION     WP_006940602.1
KEYWORDS    RefSeq.
SOURCE      Roseibium aggregatum
  ORGANISM  Roseibium aggregatum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 349)
  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 349)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 349)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 349)
  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   5  (residues 1 to 349)
  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   6  (residues 1 to 349)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Roseibium aggregatum"
                     /db_xref="taxon:187304"
     Protein         1..349
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38752
     Region          24..207
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <163..341
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 metrlalvra thlntyisvl rdmgapidre laqsrlpkyi eetpdlyvsl pvamewvart
       61 grdlpamelg ligaqaasls slrptqqaai mtaqtglkrl ealsalsrfe dsalemsirq
      121 eaddvrvtcn mrgmerhphv cfaewlnlqa visvlrsvvg ptwypselcf tsthrlpdgv
      181 hvafpdtril vgqafasilv eraclalsts vlathrpapq tpgpvpsdge qigrsedwef
      241 vtllrkmvqp yladrrtnva fiaemagisk rtlqrrlklc gssysgllqe arfelarqnl
      301 enpalkvidv ammagyespq hftrafrrft gitptdyrhq nfvmgsaai
//
LOCUS       WP_006943419             100 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Dermacoccus sp. Ellin185].
ACCESSION   WP_006943419
VERSION     WP_006943419.1
KEYWORDS    RefSeq.
SOURCE      Dermacoccus sp. Ellin185
  ORGANISM  Dermacoccus sp. Ellin185
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermacoccaceae; Dermacoccus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Dermacoccus sp. Ellin185"
                     /db_xref="taxon:188626"
     Protein         1..100
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10542
     Region          5..99
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(28..29,37,38,40..41,43,46..47,49,55,60)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(28,55..56,58)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mtggardels esvaevvadv ppgrvttyga vaavvgtgar qvgriladgr pgwpwwrvtn
       61 argllpealr aqafeqyeae gtptraegvd lrragwvppf
//
LOCUS       WP_006943535             703 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Dermacoccus sp. Ellin185].
ACCESSION   WP_006943535
VERSION     WP_006943535.1
KEYWORDS    RefSeq.
SOURCE      Dermacoccus sp. Ellin185
  ORGANISM  Dermacoccus sp. Ellin185
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermacoccaceae; Dermacoccus.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 703)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 703)
  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 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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Dermacoccus sp. Ellin185"
                     /db_xref="taxon:188626"
     Protein         1..703
                     /product="M4 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=73247
     Region          40..641
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
     Region          <662..>702
                     /region_name="COG4412"
                     /note="Bacillopeptidase F, M6 metalloprotease family
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:443532"
ORIGIN      
        1 mkrttltvaf aaacsfslvp avaqsasads patrqasfqs asahsslvgs aqsqsaalvk
       61 avglsadnaf kikdvlkdtd gsthvrvdra fkgipvvggd lvihrdasgk vtghdgmfdg
      121 aitvdtapai pkatgeakgl aaakahkkse gldaakgags tlvirvdeag kqqlaymvkt
      181 tgmqkdrtps rvrsfinadt gavissfdei ahatgngiyd knvtlttsgs sgsyklsnpn
      241 tgnyttdsnn qkingttmtd adnvwgdgsn snrqsagvda qygadttfdy yksvmgrngi
      301 wnngngarsr vhydnnyvna fwdgtqmtyg dgdrnanplt eldvaghems hgvtentagl
      361 dysgdaggln eatsdifgtg vewyanlasd kpdfllgeei dingdgtplr ymdkpskdga
      421 sydcysssvg sadphyssgp lnhwyflasn gsgaktingv synsstcdss svtgagradi
      481 ekvwyrtlst kltstsnyka aregaiksav elyggssqvc ksvesafnai nvpkgtaacs
      541 tstdptptpt ptpapgtnav tngdfeagqt gwtgtdgpit nnarqaahgg swkmwlggng
      601 ststeyeqqs vkvpasgklt yyvhvdtaet trstkydtak vqvingttts tvstfsnlda
      661 asgyvaktvd lsafagktvt lkftasedsv sqtsfvfddv vvk
//
LOCUS       WP_006944105             388 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Rhodococcus].
ACCESSION   WP_006944105
VERSION     WP_006944105.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 388)
  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 388)
  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
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 388)
  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   5  (residues 1 to 388)
  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   6  (residues 1 to 388)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 388)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 388)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..388
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39668
     Region          18..80
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          82..383
                     /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 mredtdhpgs qsslrsanqq rvvrvlqsgg eltqaeiarr tglapatvsn lvrelttsgl
       61 vevaaaerpg qrgravkltr saglavgidf ghrhltvava dlsheilaek rvelatghra
      121 edgitragal lddalvelgc grdavaavgm glpapvesat hriggpsilp gwvgvdpaal
      181 aaerlalpvh vdndanlgal aehiwgagcg vddlayikls dgvgaglvld grlyrgragt
      241 ageightsld efgqvcrcgn rgcletmvas hvviglleps rgpgltiadv valaeagdag
      301 carvladtgr hvgvaaaslc nllnpqllli ggelalagel lleplrraie ryavpsaart
      361 vqvrtaalga raqvlgaval glraaspr
//
LOCUS       WP_006946607              81 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein, partial [Dermacoccus sp.
            Ellin185].
ACCESSION   WP_006946607
VERSION     WP_006946607.1
KEYWORDS    RefSeq.
SOURCE      Dermacoccus sp. Ellin185
  ORGANISM  Dermacoccus sp. Ellin185
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermacoccaceae; Dermacoccus.
REFERENCE   1  (residues 1 to 81)
  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   2  (residues 1 to 81)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Dermacoccus sp. Ellin185"
                     /db_xref="taxon:188626"
     Protein         <1..81
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          21..80
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 avagptapga pgggaaaggv vnvntadats ldalpgvgpv laqrivewre kngrfssvde
       61 lgevsgigdk mldrlrskvt v
//
LOCUS       WP_006947213             308 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 5'-3' exonuclease [Dermacoccus].
ACCESSION   WP_006947213
VERSION     WP_006947213.1
KEYWORDS    RefSeq.
SOURCE      Dermacoccus
  ORGANISM  Dermacoccus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermacoccaceae.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Dermacoccus"
                     /db_xref="taxon:57495"
     Protein         1..308
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32942
     Region          1..302
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mtprrlmlld saslyfrafy gvpertaadg tpnnalrgfa dmiatlltty eptdivacwd
       61 ndwrpafrve aipsykahrv qegsdvaees penltpqvpl irellelagi trlgvdgyea
      121 ddvigtlthr frdagpvdvv tgdrdlfqlv ddamgvrviy takggvrapd lvdesflmar
      181 ygvatgraya dmavmrgdts dglpgvagig ektaaaliae fgslaairda iasgdprikg
      241 arrtrleaas dyldvaprvv dvaldvrvph dlvttrpqgv adgagfadfa arwdmggsae
      301 rlsaalar
//
LOCUS       WP_006951039             697 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Sphingobium indicum].
ACCESSION   WP_006951039
VERSION     WP_006951039.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium indicum
  ORGANISM  Sphingobium indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 697)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 697)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Sphingobium indicum"
                     /db_xref="taxon:332055"
     Protein         1..697
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72748
     Region          3..693
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mnhnlhiffq prsvvlvgat dksawsqlih gnfgamgydg qvwlvnkrgt pahgraavts
       61 crdlpavpdi ayifvptdav realedvaea girhalilss gyaeagpdgt qkqdgliaya
      121 rdkgvtllgp nslgfinyvh dipvspfpvg keylrghlai vsqsgattnv ianfaqqqgi
      181 glsyaiatgn eadldtarvi dylaqdeatr viavfaetik dpaafrtaar kaaaagkpli
      241 ilkvgrtela sqlaqahtgs vtgddrifda vcaqdniirv tsieelvvta gvlahtgpie
      301 ggvaiisisg gaceviadta dlaglalppf aeatratlqa viadygaifn pldvtgaavr
      361 dpslferilt ilaadpaigl tacvydlprd ggdfvdrtal tcigaglaas ktpgiminqa
      421 irpvsafsrn lmaelgipav tggldlavra laaaqrwser rvrkgkadtg lsrqaaitsa
      481 rpaseyetli ylqgqgapvi qveraptade aveawraigg pvvlkiassa iqhksdiggv
      541 rlnldsevai rdafaaimta araaypdapi dgclvapmrp vgielfvgia qspwgpviva
      601 glggvwiell adtslrllpi detearamld elrarrildg yrgapaadlg avaeamckig
      661 naalalgpdl vtleinplla rgdevealda lavwrdg
//
LOCUS       WP_006951551             134 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Sphingobium indicum].
ACCESSION   WP_006951551
VERSION     WP_006951551.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium indicum
  ORGANISM  Sphingobium indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 134)
  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 134)
  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   3  (residues 1 to 134)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Sphingobium indicum"
                     /db_xref="taxon:332055"
     Protein         1..134
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15161
     Region          15..112
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mlygpkdtqr rartlrqtmt lpeillwqal rerpanlrfr rqhpagiyvl dffcprhrla
       61 ievdgeihgr gdqperdavr dawlkgegik vvripatdvl rdleavvchi iastgrelpl
      121 rqpcglpppl sged
//
LOCUS       WP_006952762             647 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Sphingobium indicum].
ACCESSION   WP_006952762
VERSION     WP_006952762.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium indicum
  ORGANISM  Sphingobium indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Sphingobium indicum"
                     /db_xref="taxon:332055"
     Protein         1..647
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=71046
     Region          3..647
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mvvaptraqt vvpasgadda tivvigriaa ndaegrvhat pggssvvtye dyadkslvsl
       61 rdtlafapgv ytqprfgqei risirgsgls rgyhmrgltl lqdgvpinla ddngdfqele
      121 paffdhlevy rganalrlgs gtlggaingi tprgdrshgl yarldfgsfd mvrglasfgf
      181 gdrdtngwla asadtqrgdr dharrhslrl ngnaglrlsd tivtrfylsa nsinqqlpga
      241 ltraaalaap rtgnfsgdqa rdidslrmqn rttfelgrat ldvgaflntk hlfhpiyqvi
      301 dqdstdrgvf arldyaagpv emtlggetrw gtnrakrfln vdgqrgaltf darqtartst
      361 lyaefrlrpa adlqliagai yadgyrrqtq svpapvlgea syhsfsprfg llweptrsiq
      421 vyanfsrsae fptfvelaqi aafvpvreqr awtveigtrg tagwvswdvs lyraklqgem
      481 lqfalgrdvp astfnadrtl hqgieagltl epnawlrirq iwqysdfrfr ddaqfgsnrl
      541 pvvprhvlrt eirlgtdalh iapnlewvpe gawadyantt rapgyamlgl tvgaklgrnl
      601 difvdarnvt drkaigdisa virsspasei yypverraiy agfrvri
//
LOCUS       WP_006953498             239 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Prevotella micans].
ACCESSION   WP_006953498
VERSION     WP_006953498.1
KEYWORDS    RefSeq.
SOURCE      Prevotella micans
  ORGANISM  Prevotella micans
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Prevotella micans"
                     /db_xref="taxon:189723"
     Protein         1..239
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27137
     Region          149..227
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mkkllttlai lflgilsiaa qgtvtishss didalvnkkq ttktkeqika ekkaakkaek
       61 ekkklekeqq knkrtvelkp qqanpsatlk qevkkitvpk iseiqeelpr vkreptqpmq
      121 rtklvkkrvk hepvgtqkvt rrvlkgitkt rgfrvqaytg gntraarqea erigqqvkml
      181 fpeepvyvhf ysprwmclvg nytdyeqark vlrklqrngi pkagiirmmv tattsvpie
//
LOCUS       WP_006953927             253 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Idiomarina baltica].
ACCESSION   WP_006953927
VERSION     WP_006953927.1
KEYWORDS    RefSeq.
SOURCE      Idiomarina baltica
  ORGANISM  Idiomarina baltica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Idiomarina.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Idiomarina baltica"
                     /db_xref="taxon:190892"
     Protein         1..253
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=28184
     Region          140..250
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mqrithliar aykplltavi vsaalllsvt pitvnaqtsp vkmsnskich dtsspyyert
       61 knfkaydsit acldaggrlp kgqkaprars ssefssssey srsafagwld edgdclntrh
      121 elllelstgp ttkssdgcrv vrgrwndpys gtvffdsskm dvdhlvplaw awrngasswp
      181 eserdrfand pinlfavsas lnrskgaqgp dswlppnekf hcqyvtrfyr vllkyefped
      241 vrsrakvimd skc
//
LOCUS       WP_006954454             382 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Idiomarina baltica].
ACCESSION   WP_006954454
VERSION     WP_006954454.1
KEYWORDS    RefSeq.
SOURCE      Idiomarina baltica
  ORGANISM  Idiomarina baltica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Idiomarina.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Idiomarina baltica"
                     /db_xref="taxon:190892"
     Protein         1..382
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43125
     Region          1..269
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          265..356
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkilhtsdwh lgrlfhqqsl leqqiellqq iveiidqqav daviiagdiy drsvppsaai
       61 safndfieev avsrqktiia isgnhdgaer lgfatsllkq snlhlvtelp qalepivlnd
      121 sattidiwcv pfhdplqvnn wldtdckefn tahqmivdri naernpahln mivshcyldg
      181 aseseserpl siggadrvdw qlfkdfdyaa lghlhqpqhk gmehirysgs lmkysfsevn
      241 qsksitlldv nekgvqniqq islkpsrdmr vlkgtlaeli aqaehdpqrn dfiqailtdk
      301 qailypmakl rahypnlmql rkeqlehirk asdtsgqeql kkadselihd fftevygtpl
      361 nadqkasinq viqqieqees es
//
LOCUS       WP_006954468             710 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Idiomarina baltica].
ACCESSION   WP_006954468
VERSION     WP_006954468.1
KEYWORDS    RefSeq.
SOURCE      Idiomarina baltica
  ORGANISM  Idiomarina baltica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Idiomarina.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Idiomarina baltica"
                     /db_xref="taxon:190892"
     Protein         1..710
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=77839
     Region          6..710
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mnkapialai asllssplvi aeenteieti kiigsteqar qiagssavid eeqmrvevpt
       61 dinqlmktlp gvyvleedgf glrpnigira anagrvskvt lledgvmmap apysnpaayy
      121 fpttmrmasv evlkgapllr ygpqttggvl nlvstpipeq aisgqvlaqw gefssndiha
      181 yvggtqgawg flletvqres ngfkaidrsh gdsgydiqdy taklsfdqgp hhllfkaqys
      241 eeisnetylg ltdadfaetp nrrygissid qmdnshkgfn laygfdvnsd vtlnavayrn
      301 efkrdwfkln gggsyvsaan qgdmlaqgil dgtedafdle ykhnnrayes ygielnaqwq
      361 lgahalevgg rdhtdemdrf qpveifdqin gslvyqstvs psgsnnrieg adatslwvtd
      421 swqvnqalkv nlalryedvs sfrnqydeaa rttapafrsn ssdewlpgas ftydlsdswq
      481 vlagihkgfs plgggatenq epetsinyea glryqqqntf veaiafysdf sdttqlcsia
      541 tpcdngaesg tyvlgesvvq glefqaqhtf aagkflipvd iaytytqgei skdnavsglm
      601 dgdrlndipe htanvrisld nntgwvnyln fkyidsmcvs vgcnnstaaf neteslfvtd
      661 avsryelntq tsvyvkveni fdqqaivart pdgarpnkpq tvwmgidykf
//
LOCUS       WP_006954901             708 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Idiomarina baltica].
ACCESSION   WP_006954901
VERSION     WP_006954901.1
KEYWORDS    RefSeq.
SOURCE      Idiomarina baltica
  ORGANISM  Idiomarina baltica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Idiomarina.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 708)
  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   3  (residues 1 to 708)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Idiomarina baltica"
                     /db_xref="taxon:190892"
     Protein         1..708
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=77195
     Region          5..708
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          <210..>298
                     /region_name="PspC_subgroup_1"
                     /note="pneumococcal surface protein PspC, choline-binding
                     form; NF033838"
                     /db_xref="CDD:468201"
ORIGIN      
        1 msfemdeeil qdflieaaei leqlseqlvq lendpenkdl lnaifrgfht vkggagflav
       61 salvdtchga envfdtlrng qrtvtsdlmd vilqaldtin aqfaqlqare epeaadsell
      121 etlhklsqpe seddtadaaa adddadvrra sgatndaent vddiqedefe alldelhgkg
      181 qgpgasktan kkeapnthtd ndeitddefe alldelhgsg kaptsaekqq eeqksasksd
      241 sdeitddefe allddlhgkg kapkvnkaae kpaqqpaaak kpepqkaapk qpepkkaeps
      301 keqakqpakk paappppppe ttvrvdtkrl deimnmvgel vlvrnrllsl snsddqkhee
      361 mskaianldv vtgdlqgsvm ktrmqpikkv fgrfprvvrd larslkkein lemhgeetdl
      421 dknlvealad plvhlvrnsv dhgiempder qakgkpregm vtlsasqegd himlsikddg
      481 agmdaeklkq iaikrgvlde daaarmsned aynlifaagf stkeqvsdis grgvgmdvvk
      541 tkisqlngsi kieselgkgt ellikvpltl ailptlmvev kdqtfalpla vvseiidldm
      601 aktntvdgql tlivrkraip lfflehwltr rpernkrnen ghvvvvqign qqvgfvvdal
      661 igqeevvikp ldkllqgtpg magatitsdg gialiidvps mlkyyakr
//
LOCUS       WP_006955580             417 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Idiomarina baltica].
ACCESSION   WP_006955580
VERSION     WP_006955580.1
KEYWORDS    RefSeq.
SOURCE      Idiomarina baltica
  ORGANISM  Idiomarina baltica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Idiomarina.
REFERENCE   1  (residues 1 to 417)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Idiomarina baltica"
                     /db_xref="taxon:190892"
     Protein         1..417
                     /product="amidohydrolase family protein"
                     /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=45823
     Region          24..417
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mnkltwiiga gavaallwll pepapvedns ftigpinvfd gekvlrahyv sveegvivrv
       61 esqppkavqr vyptkpdqwi ipglidshvh twgdareral dfgvttvidl fghpselrra
      121 rqqrnsvqlq qeadmwgagr lvtapdghgt qfgfsphpla dddsaesavs erlaegsdfi
      181 kivytaedvd yphrpsisyq qlqrviqaah dqqvlavvhv adhlsaehav tagadglvhg
      241 ffdqpiseql idkmeqlqvf ivptniiyeh lvhgefnkqv llpacgdcfn qqklnnlsrg
      301 ganmastsfy nnlktntrll deseldvlvg sdapnpgteh gisliaelmw leaqavnwqv
      361 aihsatalaa erwrikgrgr iavgqradmv ligpspaqgm hllldpqavw kngyqvr
//
LOCUS       WP_006955610              83 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Idiomarina baltica].
ACCESSION   WP_006955610
VERSION     WP_006955610.1
KEYWORDS    RefSeq.
SOURCE      Idiomarina baltica
  ORGANISM  Idiomarina baltica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Idiomarina.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Idiomarina baltica"
                     /db_xref="taxon:190892"
     Protein         1..83
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=9231
     Region          <4..80
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlagyllhqg fmqtrlkvyk anliraeaif rkfgrwtllf awlpiigdpl tlfaglsrvn
       61 fglflllvsv gkvaryavma tsv
//
LOCUS       WP_006956066             409 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Sphingobium indicum].
ACCESSION   WP_006956066
VERSION     WP_006956066.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium indicum
  ORGANISM  Sphingobium indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 409)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Sphingobium indicum"
                     /db_xref="taxon:332055"
     Protein         1..409
                     /product="amidohydrolase family protein"
                     /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=43955
     Region          10..403
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 msgpveptfd lvfqdawifd gertlpkpts vgitdgriak isqshlsgrq tvnaaglwlt
       61 pglieshihl fdfqnainpe amghyikeel pknlrsfldy gitsvksvgd plpeigdvrn
      121 rlasgdlsgp rllmtgvgit apgghpsatv ygrnpwyrlr aaseigsvde ardvvnamae
      181 kgvdaiklll qggcrcsgep dykwhgmvsi qrmkpevlea avaearrlgf kttvhtfeee
      241 raiealeaga dgvehgvvat risdkrfidl llkndasyvp tlwvypraea mhnlalvrda
      301 gvrivlgsds faptvqiegl esgmfgansi veaermalsg ltateilrsa tglaavhlgr
      361 sdigviaegr qadllllqad ptvsvenlks plkviqggri vvdraeqqa
//
LOCUS       WP_006956330             522 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Idiomarina baltica].
ACCESSION   WP_006956330
VERSION     WP_006956330.1
KEYWORDS    RefSeq.
SOURCE      Idiomarina baltica
  ORGANISM  Idiomarina baltica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Idiomarina.
REFERENCE   1  (residues 1 to 522)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Idiomarina baltica"
                     /db_xref="taxon:190892"
     Protein         1..522
                     /product="amidohydrolase family protein"
                     /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=58774
     Region          39..501
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mkmikticll cgfiiassal aqqgppkape rdrgegpyer lilrgatlvt gegapprgpv
       61 diviendriv nivsvghpgv piksdgrpea rsgdkemdvs ghyilpgfvd mhahiggsae
      121 gipseyvlkl wlahgittir epgsfngldw vkwhqqraad nritaprivp yvgfgmgree
      181 piytaeqard wvryiksqga agikffgasr rvmeaaldea nkqglgtmmh haqlnvksmn
      241 aldsarlglt smehwyglpe alfedqtiqn ypadynynde qnrfeeagrl wkqaaepgse
      301 kwnavrdeli eldftidptl tiyeasrdlm rerqavwhed ytlprlwdff epsryahgsy
      361 wfdwttedei awkhnyqkwm tflndfhnhg grltlgsdag yiykiygfgy iremellqea
      421 glnpleviya asmggaealn mdddigsvai gkkadmvivk enplanfkvl ygtghfklne
      481 dnqpirtqgi rytikdgivf daqqllkdvr eivakekasr es
//
LOCUS       WP_006957079             153 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Vibrio].
ACCESSION   WP_006957079
VERSION     WP_006957079.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..153
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16989
     Region          5..153
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mleafnaafe sialwfsdsa lwvlflsgfl satllpggse agliatlsln qfstlsiiav
       61 atvgntlggl tnywlglwlp nrtqnekhgh kalqwlskyg ywsllfswlp vigdtlclaa
      121 gwlrmrfwpc lwlimigkal rysllaalyy gff
//
LOCUS       WP_006958855             363 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein [Vibrio].
ACCESSION   WP_006958855
VERSION     WP_006958855.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 363)
  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 363)
  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 363)
  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 363)
  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 10008687
            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="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40835
     Region          28..358
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mslirqslkr vlkgtamaaa lavaatsvna aekvyrlkla etwgpnfpif gdatknmakm
       61 aeemsngrlq iridsankhk aplgvfdmvk sgqydmghsa syywkgkvpn tlyftsmpfg
      121 mlpteqyawf yygggmelme kvysphnlms fpggntdtqm ggwfqkeins vddlkglkmr
      181 ipgfageila elgakptnia pgelytsler rtidalewvg psldlrmgfh kiapyyytgw
      241 hepgtelqfl inkrtwnrlp ddlkailqva mktaaydmyt qskhesgknw asikseypnv
      301 qvknfpaevm talreanerl lkehadkdem akeiqasqaa yieqvrpwsd ishraylnsq
      361 aqq
//
LOCUS       WP_006958964             342 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Vibrio].
ACCESSION   WP_006958964
VERSION     WP_006958964.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 342)
  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 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 342)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 342)
  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   5  (residues 1 to 342)
  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   6  (residues 1 to 342)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..342
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38988
     Region          32..212
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          111..341
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 meviaeylpv dhryqlgild islllsvvee ygldadslln hsglsdidwh sqeshisysd
       61 klllfhyvqk yfpniglgll lgeratlshf gilgyavlss rtvfeaikag fkyldlngpv
      121 fsvrvsrdde tasieiendl eigellpfct eyffssitsl fleltglqlv lqklelpysk
      181 pdyathyadr frcnvifeqp rcvltfkanv mdwqlashns dllcaylhsc esvmavlqsp
      241 trlsnqikaf lyqsvgmfps iddiavqhgc svrtlrrllt qeqtsyrelv devrfelske
      301 flvrthltie eiafrlgysd sanfrrsfkr wsgkapscfr al
//
LOCUS       WP_006959027              98 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Sphingobium indicum].
ACCESSION   WP_006959027
VERSION     WP_006959027.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium indicum
  ORGANISM  Sphingobium indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Sphingobium indicum"
                     /db_xref="taxon:332055"
     Protein         1..98
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10557
     Region          1..97
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mdsstaiarl kaheaelram gvvslslfgs targeqrads dvdvaaqlvn dgriglfela
       61 gigervrell gvgvdfvsep trkarfqaei drdrirvf
//
LOCUS       WP_006959440             764 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Vibrio].
ACCESSION   WP_006959440
VERSION     WP_006959440.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 764)
  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   3  (residues 1 to 764)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..764
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=80765
     Region          6..763
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msyeldedil qdflveagei lellseqlve lennpddkdl lnaifrgfht vkggagflsl
       61 telvdtchga envfdilrng qrqvtaslmd tmlnaldtvn eqfqavqdre pltpadqall
      121 delhrlskpq tedeaeptae apaapvveep iveepvasep vaaspeapst qavsagside
      181 itqdefekll delhgegsap gtseaaaate apaapsvldg dmsgditdde feklldelhg
      241 sgkapgegsa atpappppsk petpapaaaa sggdsdlmtd aefekllddl hgsgkgpsve
      301 eldaatkpat qnveqgpepa kpasaqkaaa papkaaapaa stvasapkpk ekaappakke
      361 aappatqakk pqaeatvrvd tstldtimnm vgelvlvrnr llslglnsnd eemskavanl
      421 dvvtadlqga vmktrmqpik kvfgrfprvv rdlarslkkd inlemrgedt dldknlveal
      481 adplihlvrn svdhgvempd drvkagkprt gkvilsasqe gdhielaivd dgggmdpdkl
      541 rgiavkrgim dedaasrltn kecfnlifmp gfsskeqisd isgrgvgmdv vktaintlng
      601 sididsemgk gtkitikvpl tlailptlmv gvaghpfalp lasvneifhl dlsrtnvvdg
      661 qltiivreks iplfylqnwl apqagdvelr kghghvvivq igsqrvgfvv dtligqeevv
      721 ikpldsmlqg tpgmagatit sdghialild vpdllkqyaa asri
//
LOCUS       WP_006959622             145 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Vibrio].
ACCESSION   WP_006959622
VERSION     WP_006959622.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            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="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15966
     Region          1..144
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 migvnnckqs kqsligmtll ellivvtlig ilamfaypsh ldqvrkshri taiadlariq
       61 lelessyngq ydwhkvissg kctvclseqs rfvfsvtssa naayiikata qansqqnlds
      121 clqeynvdyl sldasnkafp lscwq
//
LOCUS       WP_006960567             185 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit [Vibrio].
ACCESSION   WP_006960567
VERSION     WP_006960567.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..185
                     /product="TRAP transporter small permease subunit"
                     /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=20808
     Region          17..180
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mndnvphppq qqdgqprnfl draiikisnl lswlfiftvf isfyevlmry afnapttwvh
       61 etasfiggsl fivggiyafa ankhvrvvli ydsvseqtrk ylnivhhlmg lafagmlaya
      121 sfamakeswy apwgelrlet sgsvlnapyp allkglifvv lcilviqfvl hliqevmglr
      181 knndv
//
LOCUS       WP_006960859             193 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator [Vibrio].
ACCESSION   WP_006960859
VERSION     WP_006960859.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 193)
  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 193)
  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   3  (residues 1 to 193)
  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   4  (residues 1 to 193)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 193)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            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="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21606
     Region          11..193
                     /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"
ORIGIN      
        1 mqkkisktpt ivccdsleeq arlttllaqd yddvigcqls qfeallqrep ganvvagwkq
       61 psaelrliid vcrekqrpll vvikqflsnd inrlpermdy vllpadsdls lkpwlehaai
      121 arasllames eieslagkle erkmiekakg llmkmhnvde esaykamrks amqssqtlaq
      181 vaknilitle tlk
//
LOCUS       WP_006960880             376 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: exonuclease SbcCD subunit D [Vibrio].
ACCESSION   WP_006960880
VERSION     WP_006960880.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..376
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42324
     Region          1..269
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          266..355
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkflhtsdwh lgrqfhnvsl lddqkavlaq lidylqsnsv dalviagdiy drsvpptaai
       61 elmnefvhqv cnelklpiil ipgnhdgaqr lgfgssqmkg aglhiisnfk emlepvvlnt
      121 dvgevafygm pyndpelvrh hfdqpvsthd dahrllseei ksqfkpgqkn vlishcfvdg
      181 aieseserpl siggsdrvsh ehfvdfdyva lghlhqpqkk gedyirysgs lmkysfseqh
      241 qkkgmtlvel neqgfvsath idltaphqmr iiegeldevi aagktdpnnh dyllvrlldk
      301 hailnpmekl ravypnvlhi ekpgmlvgie qemaqaklar sevdmfkdff leaqnselne
      361 dqnhaitdii kqlvkq
//
LOCUS       WP_006962135             157 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Vibrio].
ACCESSION   WP_006962135
VERSION     WP_006962135.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..157
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17114
     Region          2..151
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mkiehyhrlt kqavallese kdlianlsnl sallnmelee lnwvgfylmk egelvlgpfq
       61 gqpacvripv grgvcgtava tntvqrvydv hqfeghiacd aasnseivip fsingqivgv
      121 ldidspkvgr fseideeglt flmseveklf nshaisa
//
LOCUS       WP_006962641             275 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: class II fructose-bisphosphate aldolase [Vibrio].
ACCESSION   WP_006962641
VERSION     WP_006962641.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 275)
  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 275)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..275
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=30319
     Region          1..274
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mlvnlkdllp eaaagdfavp cfnvfgyeda kavveateet nrsvilacnk dvvdfygvet
       61 aasmflnlak qssapvclhl dhtyeeeivf ralkagfssv mfdgsqltld enirrtrnva
      121 rvahalgasv egeigsvpye egrdhiksiy tspqdaqrfa eeseadcvai svgnihrltq
      181 pvceidfgll dqiaaqvdip lvihgtsgir evdmlklkqs rvakfnigtc lrqafghglr
      241 dllnqepdkf drlyfmqkvi pavrqeairn feila
//
LOCUS       WP_006965381             197 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Desulfotignum].
ACCESSION   WP_006965381
VERSION     WP_006965381.1
KEYWORDS    RefSeq.
SOURCE      Desulfotignum
  ORGANISM  Desulfotignum
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfobacteraceae.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Desulfotignum"
                     /db_xref="taxon:115780"
     Protein         1..197
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21466
     Region          2..184
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mknrlivgia gasgviygvr llevlkqtdi ethlimseag klniqietsy dvddvlsmad
       61 vtytnadiaa svasgsfqtl gmviapctvk tlsgiansfn enlliraadv qlkekrklal
      121 mfretplhig hlrlltlaae mgahivppvp afyhhpetid diinqsvgkv ldymgiahtl
      181 fkrwdnsale klkseln
//
LOCUS       WP_006965511             302 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Desulfotignum phosphitoxidans].
ACCESSION   WP_006965511
VERSION     WP_006965511.1
KEYWORDS    RefSeq.
SOURCE      Desulfotignum phosphitoxidans
  ORGANISM  Desulfotignum phosphitoxidans
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfobacteraceae; Desulfotignum.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Desulfotignum phosphitoxidans"
                     /db_xref="taxon:190898"
     Protein         1..302
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32734
     Region          7..281
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mthlifadlh nhtqasdgdf tpgqlvarak alglkaiait dhdtlkgiep glaageqagi
       61 qvipgvevsv rfrrpfftgt lhllcyfsqk rlsdikfvte fetlmskgrg qglvrarivr
      121 ineefgpqgk tpllarelvf qdiadysana srrhfalals eklgiteket inriignasp
      181 aylpsgiela dvarfmtqhp llavlahpaa gsypgnghyk evlppieive tllpefldag
      241 lqgievfypg htkacqeill gwatrydlvi tggsdchdag erplgvagit eslfrrfeaa
      301 la
//
LOCUS       WP_006967573             278 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Sphingobium
            indicum].
ACCESSION   WP_006967573
VERSION     WP_006967573.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium indicum
  ORGANISM  Sphingobium indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 278)
  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   2  (residues 1 to 278)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Sphingobium indicum"
                     /db_xref="taxon:332055"
     Protein         1..278
                     /product="aminoglycoside 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=30182
     Region          14..181
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mdnsatmpas sgetlssias gasaelfdlg gnqvlklfrd svsdemivre ieasihavgs
       61 nvptvaaiar qdrngrrgiv yprldggtvm dwvrrnpmra gwaldqmgsi hsaihraegg
      121 tlrsvkqvlt tdiahgpapl lvqraaiayl dmlpdgkmlt hgdfhlgnvm mtpqgmivid
      181 wskaaaghpa adavrsemlm rfgigpsdwv tnlwrdwaag rlrrawlaal pgvtareldq
      241 wrpvvalawl rardaertpa fmcylnkaln raglptlr
//
LOCUS       WP_006967804             345 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Desulfotignum
            phosphitoxidans].
ACCESSION   WP_006967804
VERSION     WP_006967804.1
KEYWORDS    RefSeq.
SOURCE      Desulfotignum phosphitoxidans
  ORGANISM  Desulfotignum phosphitoxidans
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfobacteraceae; Desulfotignum.
REFERENCE   1  (residues 1 to 345)
  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 345)
  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 345)
  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 345)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Desulfotignum phosphitoxidans"
                     /db_xref="taxon:190898"
     Protein         1..345
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=38959
     Region          11..344
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mqktfarsii lsifsllial vmvfpganta eskekitmst atpmypafae qiginlyina
       61 iigmtethpd lkkyefkifd kgmlygnqse aleavsngai qmtysaphfl eeldpawklg
      121 etpgvfeswd hymrsmntpe wkalhdkmak ekgvtiikwl fdtgtwylft dtgpiksvad
      181 vegqkirfag geafakalka lkvtpialpy tevvtalqtn mieglltdft ggvgyfelar
      241 htkyavlipf gnqpicmvan tkwweglpen vretlsttfd qidaskyyek feqesiekwd
      301 adpklsalkf ekeeiakwqk lmrdsfadmy ekldpelika idtar
//
LOCUS       WP_006968175             140 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Desulfotignum phosphitoxidans].
ACCESSION   WP_006968175
VERSION     WP_006968175.1
KEYWORDS    RefSeq.
SOURCE      Desulfotignum phosphitoxidans
  ORGANISM  Desulfotignum phosphitoxidans
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfobacteraceae; Desulfotignum.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Desulfotignum phosphitoxidans"
                     /db_xref="taxon:190898"
     Protein         1..140
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16056
     Region          3..140
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 misvlllfcs aflaatilpf ysevllfall rqghdphllf wvatfgntlg svvnwwmgry
       61 llrfqhrawf yfsptqiaka qawfqrygvw tlllawlpig gdpltlvagi mnvrfkvfiv
      121 lvavgkglry vaviwfsaww
//
LOCUS       WP_006968697             670 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Desulfotignum phosphitoxidans].
ACCESSION   WP_006968697
VERSION     WP_006968697.1
KEYWORDS    RefSeq.
SOURCE      Desulfotignum phosphitoxidans
  ORGANISM  Desulfotignum phosphitoxidans
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfobacteraceae; Desulfotignum.
REFERENCE   1  (residues 1 to 670)
  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 670)
  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 670)
  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 670)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..670
                     /organism="Desulfotignum phosphitoxidans"
                     /db_xref="taxon:190898"
     Protein         1..670
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=71277
     Region          25..662
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mtdldipekq vtpdetftsa gqnptlvtft arvvmaiavg lslyqlytag vvaltalvqr
       61 sihlgailtl vfltrsvfag mkknnlsvlv vldwvlagls iyctyyicgn lseifdrqgd
      121 wlfqdrvvsi vgvllvleac rrvigvfmtg icalsivyam fgpympelii hkgysieria
      181 ttlwlttegi fglpigvaat fvfvfvlfga ilettgggaf fidmayaltg rfsggpakas
      241 vvasgfmgsv sgsavgnvaa tgsftipmmk kvgyrphmag aieaaastgg qlmppimgag
      301 aflmaeftnt syltiikval vpavmyyltv lvfvhyeakk fglkgqpket lpkitkvikn
      361 glhfiipvvi liyvlvsnys pmmagfiavv stlgisilvn firwiitten rmrlsgfaak
      421 eggllvkale ngaknavmvs vacaaagiiv gmvsltgmgl kfsslvmels fgiktlaill
      481 iavaslvlgm glpvtasyiv latlagpalm dmgvpvlvah mivfwysqds nvtppvslas
      541 fagaaiakas pmrtafaswk lakglyiipl vmayrpllgm gdnyellhwe viltmitttl
      601 glvafasale rfciraatgl etglfwlaaa gllwtsywte aagfilllia lalqkwsfgr
      661 qkagsssvip
//
LOCUS       WP_006970292             407 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein, partial [Plesiocystis pacifica].
ACCESSION   WP_006970292
VERSION     WP_006970292.1
KEYWORDS    RefSeq.
SOURCE      Plesiocystis pacifica
  ORGANISM  Plesiocystis pacifica
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Nannocystales;
            Nannocystaceae; Plesiocystis.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Plesiocystis pacifica"
                     /db_xref="taxon:191768"
     Protein         <1..407
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
     Region          <144..321
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 saetgpvlrv raltpsltla llaiglagcs fdasgsgqtg agdgesetan adevgedses
       61 ssegnddttd stdadttete tetetgetea gdtttgdtte tgteettees teesteeste
      121 esteeesttg epdpncmgip dcetvdvipi vndegdpled lepdlgpwsg vggaeimgtd
      181 sgenlvgsna adtifglaga dtingnggsd liwagsgpdd vfggdgndrl iggggddeln
      241 gendadwisg qagvdtidgg ggadllegds gddvinggqd adwlfggddl dtligdegdd
      301 llfgeagddd lqgggdsdtl vggggddtlg ggagsdfyvw sngegddeit getsgsdvlw
      361 ivgfgpddvi qlkigddlvv qlptgsvtlv gyyngqneie eirtefl
//
LOCUS       WP_006970441             319 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Plesiocystis pacifica].
ACCESSION   WP_006970441
VERSION     WP_006970441.1
KEYWORDS    RefSeq.
SOURCE      Plesiocystis pacifica
  ORGANISM  Plesiocystis pacifica
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Nannocystales;
            Nannocystaceae; Plesiocystis.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Plesiocystis pacifica"
                     /db_xref="taxon:191768"
     Protein         1..319
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36080
     Region          17..299
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mahslsktma qrfeqlrsas vklvrkrskr sssnfkfafl flaanqrkgl eyvykfcrvv
       61 ddivderppg eagraqaere ldewmaelar iydpeqrpts klgvglqqtv atfnlprfaf
      121 eeivagcamd ldtstyadle slelycyrva scvgilcigl fgdqspaaqr yarhlglalq
      181 ytnilrdige dasrarvyvp rdllarhrln erdmlecryd arfltmaeef adiaeaeyqr
      241 awaelphven rrallpaevm grtyyellge vrahnynvft hraalrrvdk lkvagvslal
      301 talpvdlpgp fgamrsalt
//
LOCUS       WP_006970485             323 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Plesiocystis pacifica].
ACCESSION   WP_006970485
VERSION     WP_006970485.1
KEYWORDS    RefSeq.
SOURCE      Plesiocystis pacifica
  ORGANISM  Plesiocystis pacifica
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Nannocystales;
            Nannocystaceae; Plesiocystis.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 323)
  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   6  (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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Plesiocystis pacifica"
                     /db_xref="taxon:191768"
     Protein         1..323
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34764
     Region          12..194
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          115..321
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mslgqlldde ygiaagelfg plgwtldala tpsarltaaq agellarave ltkdpglgir
       61 lgarapvpil glmgfalmts atlgdalrql vellpaqsda frldfvsgeg qatlylsvpg
      121 dfgrcqdial vasivgvqgv ashltgrvvp ivgelavaap egwrevglpe gmrctfdape
      181 hrvvfrtedl erpvvsaepv anrlivgqvr eqlarlpegq slaersrrll edeprlrsaa
      241 qlaralgvse ralrrrlaea gtsfreqrda alrrraiall eqpeislsdi aerlgfadsp
      301 sfsrafarwv geppgrfrkr rnp
//
LOCUS       WP_006971329             138 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Plesiocystis pacifica].
ACCESSION   WP_006971329
VERSION     WP_006971329.1
KEYWORDS    RefSeq.
SOURCE      Plesiocystis pacifica
  ORGANISM  Plesiocystis pacifica
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Nannocystales;
            Nannocystaceae; Plesiocystis.
REFERENCE   1  (residues 1 to 138)
  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   2  (residues 1 to 138)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Plesiocystis pacifica"
                     /db_xref="taxon:191768"
     Protein         1..138
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14487
     Region          58..126
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mtkitskrtt ilrtlatsfa lamtllagas asaslpegag aledvvenvi enideaqpeg
       61 vavtldgtin ineasaaele llpgvgpaia qrivdyradr pfkqlnhlmr vkgvgkktyl
      121 kvkpyiaieg dttlriag
//
LOCUS       WP_006972181             271 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Plesiocystis pacifica].
ACCESSION   WP_006972181
VERSION     WP_006972181.1
KEYWORDS    RefSeq.
SOURCE      Plesiocystis pacifica
  ORGANISM  Plesiocystis pacifica
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Nannocystales;
            Nannocystaceae; Plesiocystis.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Plesiocystis pacifica"
                     /db_xref="taxon:191768"
     Protein         1..271
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30909
     Region          3..249
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mqlreailgr httnghfkpd pvslehqhrl meaasrapsh fnsqpwrfvl idddatrgqi
       61 aeiagrtmhq lmaggkfftr yrryfrfskq emaerrdgif idklpgplrp fvkhvfsetg
      121 qkvvntlrvp ntlgkdnrkl vegsplllaa mltreeyreg elsgfysllg mgmaieniwl
      181 ttldlgmgiq fistpmefpe awaelrellq ipeeleliam yrlgylpdda krptidwtss
      241 hrkrlsqyvf rntcatpead adpnfgevpg s
//
LOCUS       WP_006972398             400 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Plesiocystis
            pacifica].
ACCESSION   WP_006972398
VERSION     WP_006972398.1
KEYWORDS    RefSeq.
SOURCE      Plesiocystis pacifica
  ORGANISM  Plesiocystis pacifica
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Nannocystales;
            Nannocystaceae; Plesiocystis.
REFERENCE   1  (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   2  (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
REFERENCE   3  (residues 1 to 400)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Plesiocystis pacifica"
                     /db_xref="taxon:191768"
     Protein         1..400
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45305
     Region          4..398
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 martqsiraa tarrialaaq gfrdprpkga adrrhlrrvm rrlqllqlds ipivirtqym
       61 ppfsrlgpya pelldrvayr ddewfeawch easllpvede pllrwqkart ergetwkhla
      121 kficeneayl devlaqvker pmapgelddp rprdgewwgg rsggsvaldc lfrlgklgir
      181 rrpgfvkefd llerivpapi laaptpteed ahrellmraa asygiataad lvdyhrlpkr
      241 pakarvaelv eegrlvevev egwsrpgllh pdaklprrvd acallspfdp vvwfrdraar
      301 lfdfhykiei ytpaakrvyg yyvlpfllgd rlvarvdlkt drdagvlrvl gafaepgvdk
      361 aevveglgra ldelsafvga erwqvsgrkg dlstalrrlr
//
LOCUS       WP_006974206             346 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Plesiocystis pacifica].
ACCESSION   WP_006974206
VERSION     WP_006974206.1
KEYWORDS    RefSeq.
SOURCE      Plesiocystis pacifica
  ORGANISM  Plesiocystis pacifica
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Nannocystales;
            Nannocystaceae; Plesiocystis.
REFERENCE   1  (residues 1 to 346)
  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 346)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 346)
  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   4  (residues 1 to 346)
  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 346)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Plesiocystis pacifica"
                     /db_xref="taxon:191768"
     Protein         1..346
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37698
     Region          41..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          257..337
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 maeptilarl ldplvatcqe lggaglaiel geraaklddp dpdarvplvr yyellefahe
       61 rcgepllgar mslamdpaal gilgflavts pdlgttfdrf iryqnllveg erstleregd
      121 evvfrvenwg pprlahqvwn eaaivdmivn grrlagasfe vrevrlrhla hagasalael
      181 ldapvrfgae dnamvvdaaa lalpmpsadp amfaffdrea srrlseqwaa rpgvsegrst
      241 reqvravvev alpegvpsve aiaarlelsp rtlqrrlhde gsslrklvda lrhelalrhl
      301 aggvsiaevs fllgfsepsa fhrafrrwtg stprawraar lspega
//
LOCUS       WP_006976366             254 aa            linear   BCT 20-JAN-2025
DEFINITION  phosphonate ABC transporter ATP-binding protein [Plesiocystis
            pacifica].
ACCESSION   WP_006976366
VERSION     WP_006976366.1
KEYWORDS    RefSeq.
SOURCE      Plesiocystis pacifica
  ORGANISM  Plesiocystis pacifica
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Nannocystales;
            Nannocystaceae; Plesiocystis.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
REFERENCE   2  (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   3  (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   4  (residues 1 to 254)
  AUTHORS   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Plesiocystis pacifica"
                     /db_xref="taxon:191768"
     Protein         1..254
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=27162
     Region          6..252
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mtspaptlel rgaqrrwger lalgpvdlri apgervalag psgggkttll rllaaalras
       61 ggsvaidgrs vaamrphqir dhrrrcalid qgatlipevs vhdnvlagra pawpwwrvla
      121 salwplerea vaallgqvdl rerqwdrvga lsggqrqrva iaralaseps vlladeptaa
      181 ldpttaaevi allsretrrr eltlivsthr lsqvlgevdr viglregrvs ldapadqidd
      241 atlaalyags rers
//
LOCUS       WP_006976412             105 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Plesiocystis pacifica].
ACCESSION   WP_006976412
VERSION     WP_006976412.1
KEYWORDS    RefSeq.
SOURCE      Plesiocystis pacifica
  ORGANISM  Plesiocystis pacifica
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Nannocystales;
            Nannocystaceae; Plesiocystis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Plesiocystis pacifica"
                     /db_xref="taxon:191768"
     Protein         1..105
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11305
     Region          4..101
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(9,27..28,36,39,41..42,44,47..48,50,58,63,70)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(27,58..59,61,85)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mtlspehshr rilaavstip rgrvasygqv aamadlpgra rlvgrvlsll apgskvpwqr
       61 vlnaqgkisl pdergrrqra lleaegvefr asgrvdlrrf gigae
//
LOCUS       WP_006976947             218 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Plesiocystis pacifica].
ACCESSION   WP_006976947
VERSION     WP_006976947.1
KEYWORDS    RefSeq.
SOURCE      Plesiocystis pacifica
  ORGANISM  Plesiocystis pacifica
            Bacteria; Pseudomonadati; Myxococcota; Polyangia; Nannocystales;
            Nannocystaceae; Plesiocystis.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Plesiocystis pacifica"
                     /db_xref="taxon:191768"
     Protein         1..218
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=23662
     Region          26..188
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mneaqaqdpa anpetsapep ekkrnvvrrl ydwvlswaet pyglpalfil avaessffpi
       61 ppdvlllalg laaptkafrf alwctigsvl ggilgyyigw glwasvepti iprlfsaekf
      121 ehatalyhey gvaivfaagf spipykvfti aagvakinlp afigtsivgr garfflvagv
      181 vrrfgdqard lidryfnlvt laftvllvga flllkvvl
//
LOCUS       WP_006977394             345 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Chthoniobacter flavus].
ACCESSION   WP_006977394
VERSION     WP_006977394.1
KEYWORDS    RefSeq.
SOURCE      Chthoniobacter flavus
  ORGANISM  Chthoniobacter flavus
            Bacteria; Pseudomonadati; Verrucomicrobiota; Spartobacteria;
            Chthoniobacterales; Chthoniobacteraceae; Chthoniobacter.
REFERENCE   1  (residues 1 to 345)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Chthoniobacter flavus"
                     /db_xref="taxon:191863"
     Protein         1..345
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=36290
     Region          31..168
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cl49639"
                     /db_xref="CDD:483979"
     Site            order(135..136,139,152..155,157)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mqghpyigaf iaavlfasva aadeivpyvp qvsivisipe qkltvlkdgc fwkkypists
       61 kygsgdsygs yktpvgnlrv cekigedlas gavikkrhat gevlpanspg rdpivtrilw
      121 legleeqnhn arargiyihg tteeeklgkp vsygcirmrs kdvlevfdda aidtpvsiit
      181 dkfphyakyv qpkpqvivsa papaskpaav avttpapvps papaavaant rpaskgttvv
      241 veptklfpsa pssmatnspr hsagkgamlp pvadfgapiv eseshssftv snvshstvah
      301 amegsmlsag lpngpkieta pkdvtrfgql apnpktkprs lsldq
//
LOCUS       WP_006977746             345 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Chthoniobacter flavus].
ACCESSION   WP_006977746
VERSION     WP_006977746.1
KEYWORDS    RefSeq.
SOURCE      Chthoniobacter flavus
  ORGANISM  Chthoniobacter flavus
            Bacteria; Pseudomonadati; Verrucomicrobiota; Spartobacteria;
            Chthoniobacterales; Chthoniobacteraceae; Chthoniobacter.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Chthoniobacter flavus"
                     /db_xref="taxon:191863"
     Protein         1..345
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38353
     Region          12..302
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mafqtkdlgg pllasvsrsf ylsirllpsk lrapvglayl larasdtiad spevpeatrl
       61 hhlasfarmi rtgktdglae lqqdihttha getmllcnld rclqwlehvd nkdrseivdv
      121 leriirgqtl dlerfsvggv hvvalqsaee ldeytylvag cvgefwtrvc lnhlpgcssl
      181 gladlrklge eygkglqlvn ilrdftedlr ngrcylpepe lraagtsptp lldapvkaqp
      241 vydrwlerat qqldagyeyi stlrsarlrm acflpwyigl rtlrllakpg tltkpgkvkv
      301 srmtvrfafi yalasafspk alawsykrat gktrpvapge enllr
//
LOCUS       WP_006979604             237 aa            linear   BCT 20-JAN-2025
DEFINITION  prolipoprotein diacylglyceryl transferase [Chthoniobacter flavus].
ACCESSION   WP_006979604
VERSION     WP_006979604.1
KEYWORDS    RefSeq.
SOURCE      Chthoniobacter flavus
  ORGANISM  Chthoniobacter flavus
            Bacteria; Pseudomonadati; Verrucomicrobiota; Spartobacteria;
            Chthoniobacterales; Chthoniobacteraceae; Chthoniobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002130
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Chthoniobacter flavus"
                     /db_xref="taxon:191863"
     Protein         1..237
                     /product="prolipoprotein diacylglyceryl transferase"
                     /EC_number="2.5.1.145"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008961 -
                     phosphatidylglycerol-prolipoprotein diacylglyceryl
                     transferase activity [Evidence IEA]"
                     /GO_process="GO:0009249 - protein lipoylation [Evidence
                     IEA]"
                     /GO_process="GO:0042158 - lipoprotein biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=26467
     Region          5..227
                     /region_name="Lgt"
                     /note="Prolipoprotein diacylglyceryltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0682"
                     /db_xref="CDD:440446"
ORIGIN      
        1 mrstaygwlm lagilisvlw wsrlakrder lliiyfvalf saflgakvvy faaegwmfwd
       61 dpqrwiiwat gktilgallg gyvgvevtkk ilgytqvtgd wfaliapfgi algrvgclih
      121 gccvgrkcyp awytirdshg iarwpsvpve igfnvaailv figlrrwrlf pgqhfhlyli
      181 gyglfrffhe flratprlag nysgyqiaal avaalgivgf vrrrnapnvt qdvsavs
//
LOCUS       WP_006980794             181 aa            linear   BCT 20-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein
            [Chthoniobacter flavus].
ACCESSION   WP_006980794
VERSION     WP_006980794.1
KEYWORDS    RefSeq.
SOURCE      Chthoniobacter flavus
  ORGANISM  Chthoniobacter flavus
            Bacteria; Pseudomonadati; Verrucomicrobiota; Spartobacteria;
            Chthoniobacterales; Chthoniobacteraceae; Chthoniobacter.
REFERENCE   1  (residues 1 to 181)
  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 181)
  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 11443421
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Chthoniobacter flavus"
                     /db_xref="taxon:191863"
     Protein         1..181
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=19114
     Region          15..169
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          124..166
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
ORIGIN      
        1 mifmrrflpl imalglslat vpglhaedav atqkldelrq aveaqsrqis ilaeqvgklt
       61 kaletqkvpe ptvkinevpp taapapspvp aasaegtkpt setapeapkg eaipkaeavp
      121 gtkhvvtkge tltsiakhyn isiadlknan kidnerklqi gqilsvptak tpeptdkken
      181 p
//
LOCUS       WP_006980421             186 aa            linear   BCT 20-JAN-2025
DEFINITION  transcription termination/antitermination protein NusG
            [Chthoniobacter flavus].
ACCESSION   WP_006980421
VERSION     WP_006980421.1
KEYWORDS    RefSeq.
SOURCE      Chthoniobacter flavus
  ORGANISM  Chthoniobacter flavus
            Bacteria; Pseudomonadati; Verrucomicrobiota; Spartobacteria;
            Chthoniobacterales; Chthoniobacteraceae; Chthoniobacter.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Kang,J.Y., Mooney,R.A., Nedialkov,Y., Saba,J., Mishanina,T.V.,
            Artsimovitch,I., Landick,R. and Darst,S.A.
  TITLE     Structural Basis for Transcript Elongation Control by NusG Family
            Universal Regulators
  JOURNAL   Cell 173 (7), 1650-1662 (2018)
   PUBMED   29887376
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Liu,B. and Steitz,T.A.
  TITLE     Structural insights into NusG regulating transcription elongation
  JOURNAL   Nucleic Acids Res 45 (2), 968-974 (2017)
   PUBMED   27899640
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Steiner,T., Kaiser,J.T., Marinkovic,S., Huber,R. and Wahl,M.C.
  TITLE     Crystal structures of transcription factor NusG in light of its
            nucleic acid- and protein-binding activities
  JOURNAL   EMBO J 21 (17), 4641-4653 (2002)
   PUBMED   12198166
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415705
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Chthoniobacter flavus"
                     /db_xref="taxon:191863"
     gene            1..186
                     /gene="nusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
     Protein         1..186
                     /product="transcription termination/antitermination
                     protein NusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
                     /calculated_mol_wt=20841
     Region          16..180
                     /region_name="NusG"
                     /note="Transcription termination/antitermination protein
                     NusG [Transcription]; COG0250"
                     /db_xref="CDD:440020"
ORIGIN      
        1 mrpessiptl lpaeipeakw yclraqpkhe hiaaarlrqc eeiqvfcprv riqrstrrgl
       61 vwftealfpn ylfarfewvq shalvrscqg vsgivrfgdh vpevpagtld dlraymedae
      121 lktvsfnide gddveivegp frgqngvvkq llparervkv llevlggate vdlcltsvfk
      181 eaavlv
//
LOCUS       WP_006982554             299 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Chthoniobacter flavus].
ACCESSION   WP_006982554
VERSION     WP_006982554.1
KEYWORDS    RefSeq.
SOURCE      Chthoniobacter flavus
  ORGANISM  Chthoniobacter flavus
            Bacteria; Pseudomonadati; Verrucomicrobiota; Spartobacteria;
            Chthoniobacterales; Chthoniobacteraceae; Chthoniobacter.
REFERENCE   1  (residues 1 to 299)
  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 299)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Chthoniobacter flavus"
                     /db_xref="taxon:191863"
     Protein         1..299
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32678
     Region          43..284
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mspstsrrsf lqtgalaals vaalrqrlea adaasglkgh ihhsvckwcy pkvsledlca
       61 agkdmgltsv ellqpadypt lqkhglacam tsnptikrpd gkdlgpipra fnrkehhdll
      121 vqayepqiaa vadagftnli cfsgnrdgld detglkncae glkrlmalce kkkvilcmel
      181 lnsrvnhpdy mcdksawgie lckqvgsanf kllydiyhmq imegdviati kknheffahy
      241 htggvpgrhe iddtqelnya aimraivetg hqghvaqefi parpdvissl kqavgicdv
//
LOCUS       WP_006980861             268 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Chthoniobacter flavus].
ACCESSION   WP_006980861
VERSION     WP_006980861.1
KEYWORDS    RefSeq.
SOURCE      Chthoniobacter flavus
  ORGANISM  Chthoniobacter flavus
            Bacteria; Pseudomonadati; Verrucomicrobiota; Spartobacteria;
            Chthoniobacterales; Chthoniobacteraceae; Chthoniobacter.
REFERENCE   1  (residues 1 to 268)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Chthoniobacter flavus"
                     /db_xref="taxon:191863"
     Protein         1..268
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=28445
     Region          30..166
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cl49639"
                     /db_xref="CDD:483979"
     Site            order(131..132,135,148..151,153)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mfrqiargll aaalafglas catkpnphli risvpdqkmv lfehgveiar ydistskfgv
       61 gdrpgsyatp lgemevreki gsgqpsgmkf knrrptgeiv rpntpgrdpi vsrilwlrgl
      121 epqnhrafdr diyihgtaee wsigtpasyg cirmrshdvi qlfdrigvgt rvevvnnhfp
      181 sgmvvgngat apaghynmet nppttaatta apastpvpma ataaptpaks kvtkkrsngs
      241 tapsagptpi pisrpasagl testktrs
//
LOCUS       WP_006982718             149 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Chthoniobacter flavus].
ACCESSION   WP_006982718
VERSION     WP_006982718.1
KEYWORDS    RefSeq.
SOURCE      Chthoniobacter flavus
  ORGANISM  Chthoniobacter flavus
            Bacteria; Pseudomonadati; Verrucomicrobiota; Spartobacteria;
            Chthoniobacterales; Chthoniobacteraceae; Chthoniobacter.
REFERENCE   1  (residues 1 to 149)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Chthoniobacter flavus"
                     /db_xref="taxon:191863"
     Protein         1..149
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=16317
     Region          2..148
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(104..105,108,121..124,126)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mhirvhvpsq tldllddage tircyaists rhglgtepgs fktptgrfri vekigdgapp
       61 geifvsrvpt gkigqegddh dhvqtrilwl dgldddnknt hdryiyihgt naesrlgipa
      121 sfgcvrmnnl dvidlydrvp agttveiqp
//
LOCUS       WP_006983170             739 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Chthoniobacter
            flavus].
ACCESSION   WP_006983170
VERSION     WP_006983170.1
KEYWORDS    RefSeq.
SOURCE      Chthoniobacter flavus
  ORGANISM  Chthoniobacter flavus
            Bacteria; Pseudomonadati; Verrucomicrobiota; Spartobacteria;
            Chthoniobacterales; Chthoniobacteraceae; Chthoniobacter.
REFERENCE   1  (residues 1 to 739)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 739)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 739)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Chthoniobacter flavus"
                     /db_xref="taxon:191863"
     Protein         1..739
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=82125
     Region          31..720
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 makltlseeq yielygptpn rsptydfhdg epdklvkthc cfcgvqcgiq lkvkynkvig
       61 fepwdefpvn qgklcpkgvl rymqndhpdr llsplirted gfraagwyes lnktadslka
      121 iqdkhgkdav aflggasmtn ekaylngkfa rialqtanid yngrlcmvsa gaanrmafgv
      181 draanpwsdi llaktiiltg tnlaecfpil tdyvwrardn gakiividpr itpigrtadl
      241 flpvrpgrds alangilhvm iergwtdekf iaehthdfdk vrelvkkytp evteklsgvp
      301 akniikaaem wgpaetsmll hargiehhtk gvenvltyin lvlatgrigk pgcgygtitg
      361 qgngqggreh gqrcnqlpgg rdinkpehrq fiadfwkipe pelpkqglta ceiidaierg
      421 eikgllsisi nplvsipdsn rtraalekle ffacidffls etaryadvvl agslqeedeg
      481 tvttgegrcv rlrnsvpppv darvdwwiir elakrlgkek wfnyskaeei fdelaaaskg
      541 gpidysgmty ekiennmgif wpcpapehpg tprlfeggkf hhpdgkakfh ayeyrppaed
      601 vdveypifft tgrvvsqyls gtqtrrigal vdqypeplce ihpllatklg ienrdmvkvs
      661 trrgeitlpa lvvqtirpdt ifipyhwagk kaanqvtnrv ldpiskipef kvcacrlekv
      721 aappakanaa wppvslenk
//
LOCUS       WP_006983390             198 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Chthoniobacter flavus].
ACCESSION   WP_006983390
VERSION     WP_006983390.1
KEYWORDS    RefSeq.
SOURCE      Chthoniobacter flavus
  ORGANISM  Chthoniobacter flavus
            Bacteria; Pseudomonadati; Verrucomicrobiota; Spartobacteria;
            Chthoniobacterales; Chthoniobacteraceae; Chthoniobacter.
REFERENCE   1  (residues 1 to 198)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Chthoniobacter flavus"
                     /db_xref="taxon:191863"
     Protein         1..198
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=21305
     Region          23..156
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(115..116,119,129..132,134)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mrfpvvlffa scvaaravap laididlglq kafllqdgkv vyespicsgr pghltptgdf
       61 qvlekdenhl sslygrivdt ngktlvrdad admsvpkgak fvqapmkhfl rfdgatglhs
      121 gylpgypash gcvrmpevka elfysiaevg tpvkvhgtpp arpepekpkv aaapaatpap
      181 tppphkwwqi lqhtppre
//
LOCUS       WP_006983462             185 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Chthoniobacter flavus].
ACCESSION   WP_006983462
VERSION     WP_006983462.1
KEYWORDS    RefSeq.
SOURCE      Chthoniobacter flavus
  ORGANISM  Chthoniobacter flavus
            Bacteria; Pseudomonadati; Verrucomicrobiota; Spartobacteria;
            Chthoniobacterales; Chthoniobacteraceae; Chthoniobacter.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Chthoniobacter flavus"
                     /db_xref="taxon:191863"
     Protein         1..185
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=19993
     Region          1..182
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mklvlaatga sgaiylqrll dlldpkehei hlvlsgyarq vineelggel lvaasvrqhs
       61 dktmnvpfvs gsarfdamvv vpcsmgtlgr iaagtsetti lraadvflke rrklilvpre
      121 tpwnliharn vvtvmeagai vlpaspgfys rpkkieelvd tvvarildql glpaqgafrw
      181 aenae
//
LOCUS       WP_006984047             279 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Cardiobacterium valvarum].
ACCESSION   WP_006984047
VERSION     WP_006984047.1
KEYWORDS    RefSeq.
SOURCE      Cardiobacterium valvarum
  ORGANISM  Cardiobacterium valvarum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cardiobacteriales; Cardiobacteriaceae; Cardiobacterium.
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   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   4  (residues 1 to 279)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Cardiobacterium valvarum"
                     /db_xref="taxon:194702"
     Protein         1..279
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=30898
     Region          9..>243
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mqperiplie fknvskryds haavselnlt iyqgeffvlv ggsgsgkstt lrminaltep
       61 tdgdvyfngr rikdydirpl rhrigyvlqq ialfptmtva qnielmpdil gwdkaqrkar
      121 asellelvgl spaqyqnryp helsggeqqr vgilraiaak pdillmdepf saldplaras
      181 lqetvslihk klgttivfvt hdmaealkla crigvmhqgr lvqvatpqdi qnhpaddyvr
      241 slfsatqtnd naasiiamie qlnsaeqaki raycarqag
//
LOCUS       WP_006987071             127 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Gillisia limnaea].
ACCESSION   WP_006987071
VERSION     WP_006987071.1
KEYWORDS    RefSeq.
SOURCE      Gillisia limnaea
  ORGANISM  Gillisia limnaea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Gillisia.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Gillisia limnaea"
                     /db_xref="taxon:195907"
     Protein         1..127
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14593
     Region          17..117
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mqnsnlvpte ndyisfmkik dsiqaklidf ttlcklynvk nlyafgsatt dqfdenssdi
       61 dllieieend plergeklla iwdkleeffq rkvdlltqss lknpilrkni datkiliydg
      121 krqevsl
//
LOCUS       WP_006985232             124 aa            linear   BCT 20-JAN-2025
DEFINITION  PilZ domain-containing protein [Cardiobacterium valvarum].
ACCESSION   WP_006985232
VERSION     WP_006985232.1
KEYWORDS    RefSeq.
SOURCE      Cardiobacterium valvarum
  ORGANISM  Cardiobacterium valvarum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cardiobacteriales; Cardiobacteriaceae; Cardiobacterium.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (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   3  (residues 1 to 124)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 124)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Cardiobacterium valvarum"
                     /db_xref="taxon:194702"
     Protein         1..124
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13495
     Region          1..124
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 msepapatqg qsklkqgvik iniddlkdly qyympyvdgc gifvpteety nleqevfifl
       61 klpgdlgkfa asgrivwlnp pkkasrrmpg vgvqlrgkea prireiieag lgkslasglp
      121 tatm
//
LOCUS       WP_006987955             336 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Gillisia limnaea].
ACCESSION   WP_006987955
VERSION     WP_006987955.1
KEYWORDS    RefSeq.
SOURCE      Gillisia limnaea
  ORGANISM  Gillisia limnaea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Gillisia.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 336)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Gillisia limnaea"
                     /db_xref="taxon:195907"
     Protein         1..336
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36867
     Region          4..336
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 myqskiaglg sylpenvvtn ddlsklmdtn dawiqertgi kerrhikkgd gnstatmgak
       61 aariaiersg iakddldmiv fatlspdyyf pgcgvqvqei ldiktipald vrnqcsgfiy
      121 alsvadqfik tgmyknilvi gsenhsggld ftdrgrsisv ifgdgagaav ltrtnhisqg
      181 ilsthlhseg knamelslra psteywvpqi iaenpqgddi pyypymngqf vfknaiqrfs
      241 evimeglkan glevsdidml iphqanlris qfvqqkfkls deqvynniqk ygnttaasip
      301 ialteaweng kikegdlvvl aafgsgftwg saiiew
//
LOCUS       WP_006987991             292 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Gillisia limnaea].
ACCESSION   WP_006987991
VERSION     WP_006987991.1
KEYWORDS    RefSeq.
SOURCE      Gillisia limnaea
  ORGANISM  Gillisia limnaea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Gillisia.
REFERENCE   1  (residues 1 to 292)
  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   2  (residues 1 to 292)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Gillisia limnaea"
                     /db_xref="taxon:195907"
     Protein         1..292
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33762
     Region          150..221
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
     Region          232..290
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mknfkshfif trseqngifl lvlivvvlql vyffvdftps ekryekqeke ltefqkiids
       61 ikdsekenvg aeifpfnpnf itdykgytlg mtpeeidklh ifraeekwvn saedfqkitg
      121 isdslfneis pyfkfpdwvn sekpsylkra pvtsktqpkn rkdlnlatle dltgiygige
      181 vlagriinyr nkiggflddi qlkdiyglnf evrselqsqf tvltipshtv hdineatvle
      241 laavpyigye lareiinyrl lnekidnfee lakikdfpse kidrialyls vk
//
LOCUS       WP_006988285             245 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein [Gillisia
            limnaea].
ACCESSION   WP_006988285
VERSION     WP_006988285.1
KEYWORDS    RefSeq.
SOURCE      Gillisia limnaea
  ORGANISM  Gillisia limnaea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Gillisia.
REFERENCE   1  (residues 1 to 245)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Gillisia limnaea"
                     /db_xref="taxon:195907"
     Protein         1..245
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=27504
     Region          66..230
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mtykiftvia vltasfaftt tdghnnseip iipetllrat nenttldeei hqlydvfven
       61 npnvpnlksf kngmmgyykl sdknlfdkei ltiidfslss tkkrmwvldm knnkvlfhnl
      121 vahgkntgge fatqfsntvn slqsslgffv taetyyggng ysmfidgmee efnskarery
      181 vvvhgakyan pefinnvgrl grsygcpalp tgltqeiidv iknksvlyih sadknyakks
      241 emira
//
LOCUS       WP_006988641             154 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Gillisia limnaea].
ACCESSION   WP_006988641
VERSION     WP_006988641.1
KEYWORDS    RefSeq.
SOURCE      Gillisia limnaea
  ORGANISM  Gillisia limnaea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Gillisia.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 154)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Gillisia limnaea"
                     /db_xref="taxon:195907"
     Protein         1..154
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17127
     Region          1..153
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mpfqklkpqi kailktgess velrllkice llkenisyyn wvgfyfkngd keelklssya
       61 geptdhtiip fgkgicgqva vsnknfvvad vkaqdnyiac sinvkaeivv plfidgenvg
      121 qididsntpd pftqdderfl ewvneqvaev ltap
//
LOCUS       WP_006989461              99 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Gillisia limnaea].
ACCESSION   WP_006989461
VERSION     WP_006989461.1
KEYWORDS    RefSeq.
SOURCE      Gillisia limnaea
  ORGANISM  Gillisia limnaea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Gillisia.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Gillisia limnaea"
                     /db_xref="taxon:195907"
     Protein         1..99
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11620
     Region          2..97
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mkllenhiek lnqlcdtyhv dkmylfgsal nsnfsdesdi dflvkfkpfd laeyfenymh
       61 fkenlkkllg rdidlieeqt lknpilinsi nktkeliyg
//
LOCUS       WP_006990605             255 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Paraglaciecola mesophila].
ACCESSION   WP_006990605
VERSION     WP_006990605.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola mesophila
  ORGANISM  Paraglaciecola mesophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 255)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Paraglaciecola mesophila"
                     /db_xref="taxon:197222"
     Protein         1..255
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=28437
     Region          25..242
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 meegstladk sfcrqcvdag dlgfdftmaf qpivnlklre vfgyealvrg lnnesafsvi
       61 sqvnqdnlyl fdqqcrvkai alaaklgits ilsinflpna vykpqrcirt tldaatrygf
      121 ptnkimfeft egekisdtqh vkgiveyyre qgfitaiddf gegysglgll anfqtnivkl
      181 dmglirgids dtvrqsivrh svnmfrdlni eplaegietv sesnwlleag idlqqgylfa
      241 kpgfeclpqv dfmfs
//
LOCUS       WP_006991045             296 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Paraglaciecola mesophila].
ACCESSION   WP_006991045
VERSION     WP_006991045.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola mesophila
  ORGANISM  Paraglaciecola mesophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 296)
  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 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 296)
  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   4  (residues 1 to 296)
  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 296)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Paraglaciecola mesophila"
                     /db_xref="taxon:197222"
     Protein         1..296
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32389
     Region          27..180
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          210..291
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mstlvdgihl fadkagllnl eghvetalpg vrffraskgs prqplvyqsg iiivvqgrkv
       61 ihfpdhhiqy gagdylvlgv pmpleceafv dnglpimgls idvkpallhq lvnhmqqhqr
      121 ytqsepcsqi scaqaakvda pleniiqrll vilsnpvetd ifgadvikel vyrvlcgsqg
      181 ktlfglaqhd ghyarvaral aslhanyasp itvetladev nmsvsafhra fkqvtfespl
      241 qylkkvrlvk akdlitangs raseaafqvg ytsasqfsre fkrhfnqsps evsmsa
//
LOCUS       WP_006991225             358 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Paraglaciecola
            mesophila].
ACCESSION   WP_006991225
VERSION     WP_006991225.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola mesophila
  ORGANISM  Paraglaciecola mesophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 358)
  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 358)
  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 358)
  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 358)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Paraglaciecola mesophila"
                     /db_xref="taxon:197222"
     Protein         1..358
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40178
     Region          18..352
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkakhlllta lvltlglsat asaadgkkyr wrlaetwgpn fpifgdaskn makmvkemsd
       61 grltiridsa nkhksalgif dfvksgqyqm ghsasyywkg kdfntmfftt vpfgmtapeq
      121 yawfyygggm elmketydqy gilsfpggnt gvqmggwfrk einkvedlkg lkmripgfag
      181 evlaklgasp tnipsaelyt alerntidal ewvgpsldlr mgfhkiapyy ytgwqepate
      241 lqfmvnqkay dslpadlqki ltvamktaay dmysqsthen gvnlkalqse ypnvkirtfp
      301 qpvmnairda ndellaefaa kdketakilk siksyqeqvr awtkfadqay lesfesne
//
LOCUS       WP_006991497             344 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Paraglaciecola mesophila].
ACCESSION   WP_006991497
VERSION     WP_006991497.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola mesophila
  ORGANISM  Paraglaciecola mesophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Paraglaciecola mesophila"
                     /db_xref="taxon:197222"
     Protein         1..344
                     /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=37881
     Region          7..274
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mnnatlslsk nkdlridtlr glaclflvfy hiigngsdsg lkiqegllrd fndllayirm
       61 plftflsgyv yalrpftsgs vtfikgkarr lllpmlvagt lfaiiqsitp gsnsevnnwl
      121 tlhiipvahf wfvealflif laivvlekcn lfatrnsasv vallaialfl spinsryfal
      181 sgalyllpff lagmyvkrfn iypkpmlgla llvvvaiall svspnfrvsk ydrdalvliv
      241 gvaaclsfls fgwksaplaf igkfsysiyi yhvfftagcr ivllklgies ltplilisll
      301 ggisgpiise liinksnygk tlflgkrfvs sknqspeekn ikvl
//
LOCUS       WP_006991981             342 aa            linear   BCT 20-JAN-2025
DEFINITION  formate dehydrogenase accessory sulfurtransferase FdhD
            [Paraglaciecola mesophila].
ACCESSION   WP_006991981
VERSION     WP_006991981.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola mesophila
  ORGANISM  Paraglaciecola mesophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Paraglaciecola mesophila"
                     /db_xref="taxon:197222"
     Protein         1..342
                     /product="formate dehydrogenase accessory
                     sulfurtransferase FdhD"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0097163 - sulfur carrier activity
                     [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36648
     Region          57..341
                     /region_name="FdhD"
                     /note="Formate dehydrogenase assembly factor FdhD, a
                     sulfurtransferase [Energy production and conversion];
                     COG1526"
                     /db_xref="CDD:441135"
ORIGIN      
        1 msrvktfpit rlvstnltge qgnslelann lelanshera nsleltekpe reqssvgrla
       61 iddtiaseep leiwlkhplk qggnaslllt tmrspgddva lvtgwlhssg llansadiqs
      121 vthtgserik gneanqilvt lhpqsdfdit sgqsqsgshi eyvnsgcgvc gqrsidvlld
      181 kipqrdmpnn asllnnevls lanalrqqqt afaatggshg aglfalpesa dlnapqtgan
      241 rlidvredig rhnaldklig anlpmllven tpektkeygv vissrisfdl vqkaamanig
      301 milamgapst laielakecd iclvgfisqk rinvytcdhr iv
//
LOCUS       WP_006992003             279 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Paraglaciecola mesophila].
ACCESSION   WP_006992003
VERSION     WP_006992003.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola mesophila
  ORGANISM  Paraglaciecola mesophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Paraglaciecola mesophila"
                     /db_xref="taxon:197222"
     Protein         1..279
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31778
     Region          1..275
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mkidlhchty ysdgqlspve lvdrannmqv dvlaitdhdt vqaldearah qakqkrkmhi
       61 vngielstsw hnfdihilgl nvdkddevfr qrlveqkner daraqkmsdk lakagvenvl
      121 ddakllageg qltrahfarv lverkevrdf egafkkylgk gkrahvkpqw itieeaiewi
      181 hdaggkavla hpghydmttk wlrrlvlefk qaggdgiett harinpekrk livelamehn
      241 lqasagsdfh fvsrwtelgk nlgvpehltp iwhdwsfvd
//
LOCUS       WP_006992143             253 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Paraglaciecola mesophila].
ACCESSION   WP_006992143
VERSION     WP_006992143.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola mesophila
  ORGANISM  Paraglaciecola mesophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Paraglaciecola mesophila"
                     /db_xref="taxon:197222"
     Protein         1..253
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=28592
     Region          149..>198
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mlaglrdiqr ftiaatdgdi giikdflfdd rawtirymyv dthkwlplge kvlispislr
       61 eidtddekih valskqqvke spsideektv sreyeeilfs ylgygyywtg pgawgeyahp
      121 talvnqqale qansnleehd kskanhlrsi delqgydvia ggetvghihd lildtdnwev
      181 pmltidthnw lpggkkllla pkhiddinwl eqrvhctlsa kdvelcpecd hdllndadyk
      241 lkvksalqsl pga
//
LOCUS       WP_006992846             304 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Paraglaciecola
            mesophila].
ACCESSION   WP_006992846
VERSION     WP_006992846.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola mesophila
  ORGANISM  Paraglaciecola mesophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 304)
  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 304)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Paraglaciecola mesophila"
                     /db_xref="taxon:197222"
     Protein         1..304
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33421
     Region          53..290
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 msnsrrnmlk gialssaala astvvsgcas sesneidnna nqpgvakfkg ninhsvarwt
       61 ygdlsieelc kvvkslgfsa idligpegwp ilkrygidss mcngaelnlv dgfihpefhd
      121 elekrylkhi dlvaqagykn licfsgnarg mskeqglkna vaglkrilpy aeekgvviqm
      181 elfnskvdhp dymadsskwg vdlckalgse hfkllydiyh mqvnegdiir tiqdnhqyfg
      241 hyhtagvpgr heigdnqely ypaiaraikd vgftgylaqe fipaaetkag kieslreaih
      301 icdv
//
LOCUS       WP_006993183             102 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Paraglaciecola mesophila].
ACCESSION   WP_006993183
VERSION     WP_006993183.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola mesophila
  ORGANISM  Paraglaciecola mesophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (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   2  (residues 1 to 102)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Paraglaciecola mesophila"
                     /db_xref="taxon:197222"
     Protein         1..102
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10766
     Region          31..100
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkkfiatlff agvllagyvg nvvaeakvdk ssvsqmksqk inlntataeq lvtlpgigkk
       61 kaaaiiayrd ksgkftkvsd ltnvkgigkk mvakltdhvq vk
//
LOCUS       WP_006995271             192 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Haemophilus].
ACCESSION   WP_006995271
VERSION     WP_006995271.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus
  ORGANISM  Haemophilus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Haemophilus"
                     /db_xref="taxon:724"
     Protein         1..192
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21497
     Region          3..164
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mkifgtmydk tmewskhrfa vswlsfvsfi eaiffpippd vmlipmsmsk pkgavkfafy
       61 taiasviggi igyaigfyat dwvenivqqw gyaahwakav swfeqwgvlv vfvagfspip
      121 ykvftlcsgv mqmaffpfvi tafvsrlarf llvaklaawg gekfaaklrk sieiigwsvv
      181 vlaiiayfil kn
//
LOCUS       WP_006996129             204 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Haemophilus].
ACCESSION   WP_006996129
VERSION     WP_006996129.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus
  ORGANISM  Haemophilus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae.
REFERENCE   1  (residues 1 to 204)
  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 204)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 204)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Haemophilus"
                     /db_xref="taxon:724"
     Protein         1..204
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22559
     Region          1..204
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 maysieeeqe inqlkdwwke ngktiivafi lgvggmfgwr ywqahqveqi sqasvqydal
       61 insvqqneqa kkanieqfvq ansktayavf alldeskkat ekqdfaaagv nlkqalmqsq
      121 devltsival rlsavqfqlg qldnalttln qvkgesfnar kailtgdiqv akgdkvaakn
      181 sfeqaqqsgs qleqqmakmk lnnl
//
LOCUS       WP_006989017             307 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Gillisia limnaea].
ACCESSION   WP_006989017
VERSION     WP_006989017.1
KEYWORDS    RefSeq.
SOURCE      Gillisia limnaea
  ORGANISM  Gillisia limnaea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Gillisia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Gillisia limnaea"
                     /db_xref="taxon:195907"
     Protein         1..307
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=34176
     Region          59..206
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mnmllrstyl ifvaslvisc atnpyaatnk ihkkqskllt dqlntfpteq pegeallpyg
       61 ehwagttnfn lrkpnfvilh htaqdslaqt lttftkvptq vsahyvigkn geiyqmlndy
      121 yrawhagagk wgnttdlnsa slgieldnng fepfsplqin slikllkvlk erynipaanf
      181 ighsdiapgr kvdpnpkfpw kllaeegfgl wydeievpvi vldgrpktgn lnipvvtegn
      241 ivpeptesdl attsvdpkma lriigydtsn meaaikafkl hfiqsevnge lnamdllile
      301 nlykkym
//
LOCUS       WP_006995245             343 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [Haemophilus].
ACCESSION   WP_006995245
VERSION     WP_006995245.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus
  ORGANISM  Haemophilus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 343)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Haemophilus"
                     /db_xref="taxon:724"
     Protein         1..343
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=39587
     Region          <55..330
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mnfcrillkp lkknealsgy saeglhyltg nkhfnpelpf srqefitvkp qkqqgmsisg
       61 fqpklqliik dghfdsvnqq gnyilkpspe eypflaeneh atmrimkelg fdvpenglvs
      121 fageqnhkef afvikrfdrd eqqkpmhqeq ldgamnirdk ygkigadneq yvsyeqiakf
      181 ilqhtenhla qqreifrrii yayllgnndl hlrnfsfiyp knshpklapi ydfvsvspyp
      241 eifnstllal pllareegna tlakgfntqy geyigddfve fgeniglnkn viiqklipei
      301 tqekekveqi ysqsfmpqph idcvlktyrk rlallnllne pel
//
LOCUS       WP_006994611             795 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Paraglaciecola mesophila].
ACCESSION   WP_006994611
VERSION     WP_006994611.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola mesophila
  ORGANISM  Paraglaciecola mesophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 795)
  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 795)
  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 795)
  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   4  (residues 1 to 795)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..795
                     /organism="Paraglaciecola mesophila"
                     /db_xref="taxon:197222"
     Protein         1..795
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89172
     Region          64..795
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mhlkyalslk eitakpsrrl inhalkddka lqatfigqar arealdfglg lnakgynlyv
       61 mgeqatgrft lvheyiakyv qkvltpddwc yinnfedere pfalrlppge skrlvkemgk
      121 lvdelldtfp aafdnpgyqr kkvaitrefd qrydhaidsv eqlaqaqnva lyeengnisf
      181 spivdgkpit dadfaklsde erqryyqlid elenrlgeal ielpkwkras seqlrhlkkd
      241 taeqgikpll kelehlyasd lgilkflrql kphlvetive iladdkkddk hdeydrrsvl
      301 eeqylpnilv shelnsgapv iyeanpthqn lfgrveytnv sgsvftnyrm irpgalhran
      361 ggyllldvdk lilqpyawet lklvlksgyl kmdlpqpdvg mvnsitlnpq hipinvkvvl
      421 lgsrelyynl qdfddefyem frvlvdfdhe iqldkktlyd fvgrvrhqvs qlglssispk
      481 amyrlveysl rmaehqqrls arfsdviell neslyfcrqg haldldvthi eaalsaktrr
      541 tgrvseavld dikqgqilia tegvdvgkvn gltvlevgds lfgtparits tvyagangvv
      601 dierevelgq pihskgvmll tgylghkyaq lfpltlsani aieqsyghid gdsaslaelv
      661 alisaltnip trqdlaitgs inqygqvqsv ggvnekiegf fklcqhrglt gnqgaiipks
      721 nqislmldke vvaavklgkf hicvvetvdq alellmnkev gvmntkgryp kgtinymavs
      781 sllnianvvn gadde
//
LOCUS       WP_006996675             211 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Candidatus Pelagibacter communis].
ACCESSION   WP_006996675
VERSION     WP_006996675.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Pelagibacter communis
  ORGANISM  Candidatus Pelagibacter communis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Candidatus Pelagibacterales; Candidatus Pelagibacteraceae;
            Candidatus Pelagibacter.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Candidatus Pelagibacter communis"
                     /db_xref="taxon:198252"
     Protein         1..211
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=23315
     Region          1..>52
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkvinnkkgf tliellvvva iigilssvgv vayngytaga kesackgnfr tivksvyeni
       61 mwcelnptin flwnttqsle ydcnnmfvgg rdtvyteytk nekiarltid qiaihdlslp
      121 gdiargkktk sgsrstltsm tnpyagktgy gvfnvsgtre lyegdeydlr gqvtlrkqds
      181 sgneiaanee gqlflitkcg dkviehdfdf y
//
LOCUS       WP_006996982             205 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Candidatus Pelagibacter communis].
ACCESSION   WP_006996982
VERSION     WP_006996982.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Pelagibacter communis
  ORGANISM  Candidatus Pelagibacter communis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Candidatus Pelagibacterales; Candidatus Pelagibacteraceae;
            Candidatus Pelagibacter.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Candidatus Pelagibacter communis"
                     /db_xref="taxon:198252"
     Protein         1..205
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=23148
     Region          1..>52
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkvinnkngf tliellvvva iigilssvgv vayngytaga kesackgnfr tivksvyeni
       61 mwcelnptin flwnpeqswe ydcntmfigg rdvvyqygyt kneklarlti neititdlsr
      121 kadsnigsrt tlngmanpyn rygvfhptgt relyegdkyd mrgnvslrkr dssgnelsnn
      181 wqsegqlfli tkcgdkvieh dfdfy
//
LOCUS       WP_006997053             219 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Candidatus Pelagibacter
            communis].
ACCESSION   WP_006997053
VERSION     WP_006997053.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Pelagibacter communis
  ORGANISM  Candidatus Pelagibacter communis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Candidatus Pelagibacterales; Candidatus Pelagibacteraceae;
            Candidatus Pelagibacter.
REFERENCE   1  (residues 1 to 219)
  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 219)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 219)
  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   4  (residues 1 to 219)
  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   5  (residues 1 to 219)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Candidatus Pelagibacter communis"
                     /db_xref="taxon:198252"
     Protein         1..219
                     /product="TRAP transporter small permease subunit"
                     /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=25364
     Region          38..219
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mvkkkshsag vketlditde liaerrtslk mpkdmvpwma ktiefidlnm lrigkvicwm
       61 viplifamtf evigrhffnr ptlwaydvtr miagaffmlg agyalskgih iradflyrnw
      121 nvktqakvdl flyllfffpg fivffwvsfd yaytsicgrs ilaecldgkv riqramdttw
      181 mpvmwplksc mpigafllli qgiselfkty yafvkgrwp
//
LOCUS       WP_006997486             198 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Candidatus Pelagibacter communis].
ACCESSION   WP_006997486
VERSION     WP_006997486.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Pelagibacter communis
  ORGANISM  Candidatus Pelagibacter communis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Candidatus Pelagibacterales; Candidatus Pelagibacteraceae;
            Candidatus Pelagibacter.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Candidatus Pelagibacter communis"
                     /db_xref="taxon:198252"
     Protein         1..198
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22445
     Region          1..167
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlnelyqktl klaahkksnt ylailsftes sffpippdvm iapmviakkn dylkifliat
       61 lfsslggilg yfigsyffdl gmivvefyny eekvinlkns lsegsglyvw latlflagft
      121 plpfkvftit sgmigfnlpi ffiiclfsrg lrffivsyls ykfgdifskf mktdaakwft
      181 ilgiiivlif tliyfaik
//
LOCUS       WP_006996595             486 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase [Haemophilus].
ACCESSION   WP_006996595
VERSION     WP_006996595.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus
  ORGANISM  Haemophilus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Haemophilus"
                     /db_xref="taxon:724"
     Protein         1..486
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=55764
     Region          1..377
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 miyidppynt gedsfkyndk fshstwltfm knrleiaktl laddgvifvq cddkeqaylk
       61 vlldetftre nfinciavkm sepsgnkmah tshrlpkike yiliyknkni klnpireqks
      121 ewddeynifl dnftqedkkf idlivnsqte nkeingntlk eidillkkis pisvnqklaq
      181 lnikdnevik wkldnayriv rtaasssvkk ladekkgncq qqffsviskr drllyivksd
      241 yskdakaprv qvlfaedyls islcdlwtni nttgleaegn velkngkkpe slietiikla
      301 tnesdivldy hlgsgttaav ahkmnrqyig ieqmdyietl averlkkvid geqggiskav
      361 nwqgggefvy aelapfneta kqqilacess ddiktlfnel ceryflkynv svkefsqiie
      421 epefqslpld eqkqmvleml dlnqmyvsls emddeqfadc lndddkalsr afyqsvknqa
      481 ekkdge
//
LOCUS       WP_006997610             138 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Candidatus Pelagibacter communis].
ACCESSION   WP_006997610
VERSION     WP_006997610.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Pelagibacter communis
  ORGANISM  Candidatus Pelagibacter communis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Candidatus Pelagibacterales; Candidatus Pelagibacteraceae;
            Candidatus Pelagibacter.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Candidatus Pelagibacter communis"
                     /db_xref="taxon:198252"
     Protein         1..138
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15491
     Region          3..137
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 miylslftis flaatilpfs seltlaglia tsnydnlill ivasfgntlg svvnwvlgfy
       61 srnlitkkwf pfkdkqiens srwfskfgkw sllftwvpil gdpitlvagl lrvrfldfvi
      121 lvaigkvsry lvvfylig
//
LOCUS       WP_006997874             247 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Candidatus Pelagibacter
            communis].
ACCESSION   WP_006997874
VERSION     WP_006997874.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Pelagibacter communis
  ORGANISM  Candidatus Pelagibacter communis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Candidatus Pelagibacterales; Candidatus Pelagibacteraceae;
            Candidatus Pelagibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Candidatus Pelagibacter communis"
                     /db_xref="taxon:198252"
     Protein         1..247
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=28917
     Region          10..158
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 malktilnys pnfnpkkrts kqikfiifhy tgmksesdal krlteiqsev schyliknng
       61 eivkivpdly iawhagkssw knykslnqns igieitnpgh eygyknftqk qittlvkfsk
      121 flikkykinp knilghsdia vlrkkdpgek fpweylaknk igiwhtlnkq dllknrklki
      181 skveeniffr nlfkigyskt fpknigrnky lieliksfqr rfrqelvdgk idqesllink
      241 slikayn
//
LOCUS       WP_007001921             313 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Teichococcus cervicalis].
ACCESSION   WP_007001921
VERSION     WP_007001921.1
KEYWORDS    RefSeq.
SOURCE      Teichococcus cervicalis
  ORGANISM  Teichococcus cervicalis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Roseomonadaceae; Roseomonas.
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
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Teichococcus cervicalis"
                     /db_xref="taxon:204525"
     Protein         1..313
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=33390
     Region          1..310
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mirfegatrr yagrtvvdrv tlevpaghlc vllgesgsgk stllrmvnrl vepsagrvlv
       61 egrdvaqaep ealrrrigyv iqsvglfphw rvadniatvp rllgwqapri aarveellgl
      121 vglepaqfrd ryphelsggq aqrvglaral aadpplllmd epfsaldpgt rrglqgelrr
      181 ihqatgktil fvthdveeal aladglavld qgrlvaqgrp aqvvepgapp pvralfgeeg
      241 lafhrlatlp aaeftrpgal pgltllphda slkqallrll aegaeslaia pgpahpggtl
      301 rwedvprgag mrg
//
LOCUS       WP_007002336             192 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Teichococcus cervicalis].
ACCESSION   WP_007002336
VERSION     WP_007002336.1
KEYWORDS    RefSeq.
SOURCE      Teichococcus cervicalis
  ORGANISM  Teichococcus cervicalis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Roseomonadaceae; Roseomonas.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Teichococcus cervicalis"
                     /db_xref="taxon:204525"
     Protein         1..192
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=20681
     Region          1..163
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlhalyeril rlaahrhagg wlaaisfaes svfpippdam llpmclarpe rawryatict
       61 iasvlggiag yalgyflfea vaqpvlaayg haealqsfra wfdrwgaavi likgltpipy
      121 kvvtiaagaa afdpwvflla sivtrgarff llaallrryg apvrgfvekr ltllttlaai
      181 ailggfaair li
//
LOCUS       WP_007002518             689 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Teichococcus cervicalis].
ACCESSION   WP_007002518
VERSION     WP_007002518.1
KEYWORDS    RefSeq.
SOURCE      Teichococcus cervicalis
  ORGANISM  Teichococcus cervicalis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Roseomonadaceae; Roseomonas.
REFERENCE   1  (residues 1 to 689)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 689)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..689
                     /organism="Teichococcus cervicalis"
                     /db_xref="taxon:204525"
     Protein         1..689
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70380
     Region          1..683
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 msalrallrp rsvavigasa daakmtgrpv gylqkygfsg diwpvnprad siaglpcyae
       61 iaalpgapda aivllgpera eaavrdlaar gcqaaivlas gygeanedga rrqqalkdaa
      121 gpmrllgpnt iglvnltdrm mlsatgalev gdlaagrisv vsqsggilgs llsraadrgi
      181 gfaklvstgn eadidssemi ahlvedeatd viavymeglr rpelfkqaar raaalgkpiv
      241 vykvgrsesg aqaatshtga lagadrvyda lfrqhgvira esftdlldip aalasgrrmr
      301 gdrvailtst ggagtlladn cglagiavpa pdapttqrla tllgedpaai grnpvdvtla
      361 glrpdlfrga idalldspgy daavvvigss alatpdivag aivecqarsd kpvlayvsph
      421 aphllrllns qgipafatpe scasvlralh rpalapppqp vaadpsvlag lpagnlneae
      481 skalfarfgv pvtreyvaad adgalaaara lggevvlkll sraiahksdl ggvrvglaae
      541 avpeacatml rrlaaagapa pegflvqeri rggvemilgf hrdpqlgpvi llgsggvaae
      601 lfqdttlrll piaradaeam vgelkaarll rgyrgapaad ipalvdavma faamagaage
      661 rlleaeinpl fvlpegqgar aadglavlr
//
LOCUS       WP_007002805             270 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Teichococcus cervicalis].
ACCESSION   WP_007002805
VERSION     WP_007002805.1
KEYWORDS    RefSeq.
SOURCE      Teichococcus cervicalis
  ORGANISM  Teichococcus cervicalis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Roseomonadaceae; Roseomonas.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 270)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Teichococcus cervicalis"
                     /db_xref="taxon:204525"
     Protein         1..270
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=28689
     Region          37..259
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mghafaprpa prfapsgeag rggcagcrtp aapvpplsma fqpilrcdag ghglfayeal
       61 vrgpggegaa svlsqihdgn ryafdqacrv raielaarlg lldgpallsi nflpnavyep
      121 racirtslea arrvglphdr lvfeftehea mlepahllri laeyrevgfr taiddfgagh
      181 sgltllaefr pdvvkldmal lrgmdadpvr rtilrhivam caelgcqvva egvetpgefa
      241 alralgvtlf qgyllgrpqf ealpsatcpg
//
LOCUS       WP_007003022             510 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Teichococcus cervicalis].
ACCESSION   WP_007003022
VERSION     WP_007003022.1
KEYWORDS    RefSeq.
SOURCE      Teichococcus cervicalis
  ORGANISM  Teichococcus cervicalis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Roseomonadaceae; Roseomonas.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Teichococcus cervicalis"
                     /db_xref="taxon:204525"
     Protein         1..510
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54172
     Region          7..510
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mdalsetpfi rlhpedsvmi arraapegtp vapgiatavr ippghkvair phapgeavkr
       61 ygqiigfatq piapgdwvht qncgmgdfdk dyawgadakp tlyvpqpasf qgivrpdgrv
      121 atrnyigivt svncsahvas miadafkrnp ftgsdplaef pnvdgvvalt hktgcgmgdn
      181 dglrllrrtl agyarhvnfs hviaiglgce vnqisgllqe qnlagrlrnm diqemggtrk
      241 tveagiafvr evlaeanqvh rqsvpashlt ialqcggsdg ysgitanpal gaasdllvrh
      301 ggtvilsetp etygaehllt rratsravge klvglmrwwe eyaergqael nsnpspgnka
      361 gglttileks lgamakagtt nltavynyae pvtekgfvfm dtpgydpvaa tgqvagganm
      421 vcfttgrgsv fgckpapsik latnsamyer meedmdvncg tilsgresve ecgerifqli
      481 lrvasgertk seqydfgaae fapwpigatm
//
LOCUS       WP_007005144             394 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Teichococcus cervicalis].
ACCESSION   WP_007005144
VERSION     WP_007005144.1
KEYWORDS    RefSeq.
SOURCE      Teichococcus cervicalis
  ORGANISM  Teichococcus cervicalis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Roseomonadaceae; Roseomonas.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Teichococcus cervicalis"
                     /db_xref="taxon:204525"
     Protein         1..394
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=41160
     Region          5..391
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msgrailvln agsssikfql ydeaggaltr rfkgrlegig tarprllawa agdvaledra
       61 ldpartadge aaqaalggwi adhmggppda vghrvvhggg rftgpalvdd tvlaeltalv
      121 plaplhqphn lapirsirar rpdlpqvacf dtafhatlpe larrfaiper lhaegvrryg
      181 fhglsyeyis srlpelapei aggrvvvlhl gsgasacamr agrsvestmg ftaldglpmg
      241 trpglldagv vlylaqqgrg aaeiehilyh esglrglsgl sgdvrdllas dapaarlald
      301 yfayrtaqsi aalasalggl dglvftagvg enaapvrami aercawlgir ldpaanaaha
      361 prihapgslp vhiiptneer mvarhvldml gaap
//
LOCUS       WP_007006152             404 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA, partial [Teichococcus cervicalis].
ACCESSION   WP_007006152
VERSION     WP_007006152.1
KEYWORDS    RefSeq.
SOURCE      Teichococcus cervicalis
  ORGANISM  Teichococcus cervicalis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Roseomonadaceae; Roseomonas.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 404)
  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   3  (residues 1 to 404)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Teichococcus cervicalis"
                     /db_xref="taxon:204525"
     Protein         <1..404
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <15..404
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 ampeaaaape prapqtttlr vdqaridqlm nligelivak nslayllrka eagagarela
       61 rdikdqhavv nrlaedmqga imairmlpvs hvfqrfprlv rdvarklgkq velvlegeet
      121 eadkgmieal aeplihmvrn sldhgleppe erlaagkpaq grvwlsaasl nesilltird
      181 dgrgidparl rrkavergml epeaaaalse aealrlifap gfstaeqvsd lsgrgvgmdv
      241 vratvekagg wvdveseigr gtairvtlpl smavtrimti ecggqlfgip mgavvesvrl
      301 paaaihrlrd reafvlrdri vpllrlaall elpappataq edapvlvlra gsatvglvig
      361 afrermeaiv rpldgalagl rgfagttllg dgrvllildv geli
//
LOCUS       WP_007007047             305 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Nitratireductor
            aquibiodomus].
ACCESSION   WP_007007047
VERSION     WP_007007047.1
KEYWORDS    RefSeq.
SOURCE      Nitratireductor aquibiodomus
  ORGANISM  Nitratireductor aquibiodomus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Nitratireductor.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Nitratireductor aquibiodomus"
                     /db_xref="taxon:204799"
     Protein         1..305
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32566
     Region          29..270
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 maaivrdyeg gkpvarevwt rlegercvlg egptydrhsd tvwwfdilek alfehcfadg
       61 vtrrhilpel ssalarvddn rqllvtesgl ylrnvadgsl slhrpleadn pqtrsndsrv
      121 hpsgafwigt mgknaeegag siywyrrgev krlysgitvt naicfspdgs vgyftdtptl
      181 qimqvsldpq tglpvgepsp faapsrdgep dgavvdaegn lwvarwgghg vevyspggll
      241 lrkidlpaal ttcpafvgpq adgllvtsas igvdpdssda asaggvfmsd lgapagklep
      301 dvlid
//
LOCUS       WP_007008800             193 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Nitratireductor aquibiodomus].
ACCESSION   WP_007008800
VERSION     WP_007008800.1
KEYWORDS    RefSeq.
SOURCE      Nitratireductor aquibiodomus
  ORGANISM  Nitratireductor aquibiodomus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Nitratireductor.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Nitratireductor aquibiodomus"
                     /db_xref="taxon:204799"
     Protein         1..193
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21467
     Region          1..163
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlrklydwtm slaatrhaek algsvsfies svfpippdvl lipmvlsera rwlryafict
       61 issvlgallg yaigaflyet vgqpilafyg kenafeqvag wynewggwgv lfaavtpfpy
      121 kvltifsgat glnllvfvvv svigrglrff lvswllyrfg apirvfiekn lgllftlfmv
      181 lliggfvair yvf
//
LOCUS       WP_007008848             202 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Nitratireductor
            aquibiodomus].
ACCESSION   WP_007008848
VERSION     WP_007008848.1
KEYWORDS    RefSeq.
SOURCE      Nitratireductor aquibiodomus
  ORGANISM  Nitratireductor aquibiodomus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Nitratireductor.
REFERENCE   1  (residues 1 to 202)
  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 202)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 202)
  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   4  (residues 1 to 202)
  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   5  (residues 1 to 202)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Nitratireductor aquibiodomus"
                     /db_xref="taxon:204799"
     Protein         1..202
                     /product="TRAP transporter small permease subunit"
                     /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=22776
     Region          4..180
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 magllglsrl idainqfigk qvswlilvav lvsaynaiir flgdglpayl piprasnsll
       61 elqwylygtv fllasaytlq rnehiridiv sslftkrtrd widlfchvff llpfvslivw
      121 lswpwfqrsf isgeisanas gliiwpakfm vlagfillta qavseivkry avlrglidep
      181 npqhemhpaa eaaiemeekr dd
//
LOCUS       WP_007010898             217 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein, partial [Nitratireductor
            aquibiodomus].
ACCESSION   WP_007010898
VERSION     WP_007010898.1
KEYWORDS    RefSeq.
SOURCE      Nitratireductor aquibiodomus
  ORGANISM  Nitratireductor aquibiodomus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Nitratireductor.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 217)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Nitratireductor aquibiodomus"
                     /db_xref="taxon:204799"
     Protein         <1..217
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <9..166
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 lgslsetasl fvnfdpshfv daasaasalr dvqvvlrdsg itaervvcei teqetgsdet
       61 llgfvqalkg yghrvavddy gadssdlrri ealgpdivkf dgawtghlla sapgvamlte
      121 mvrafsekgi rtvfegietg qqlelaescg vsmvqgfala rpqlapgafk efeaareser
      181 rralagtaer leqgkaektr rdvspnrsgr tfgrrgt
//
LOCUS       WP_007011750             739 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Novosphingobium pentaromativorans].
ACCESSION   WP_007011750
VERSION     WP_007011750.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium pentaromativorans
  ORGANISM  Novosphingobium pentaromativorans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 739)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 739)
  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   3  (residues 1 to 739)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Novosphingobium pentaromativorans"
                     /db_xref="taxon:205844"
     Protein         1..739
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76687
     Region          1..739
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mspeeiqqif faeceeslaa aesglaacqa gtqdadtvna vfravhsikg gagafgyval
       61 qaythtfetl lsdvreglva iesklvdlll raldtlsdhv eaareggdap adaaliseme
      121 asmaanagga peaavepave pevsepdttd sdaegsadye ldldallddl tagfdpapak
      181 aaeaapekrw kvhlrphsga mrngsepllm vreiaslgge cvhcdvsqvp pldafdpaqg
      241 ylgwtfsmpe aasedsvrei fdfigddcal afgedadipe vkivaaapkp apapapaapa
      301 pvseakvaap qpatpvaaaq pepvpvqeap gdvgakaaqa appappaggq siridlfkld
      361 rlidlvgelv iaqamlvqrl gangitanee lslletltrd iqesamsira qpissvfsrv
      421 prilrelass tgkhvkldvi getteldktv ierlgeplth lirnavdhgi esaedriaag
      481 kapegtltls aehrsgrili siaddgagin rervlakave kgivsaeaql saeeidnlif
      541 apgfstaqtv snisgrgvgm dvvrqnvkdl ggritidstp gkgttfiltl pltlaisdgm
      601 ivnvgdqtlv vplasvvesl rpgdgevqgl gsnrnmlnvr grfipivslr salgassgal
      661 tpdegvlivv dtestgqaal lvdeiqdqrq fvikslatnf rpvdgvagat ilgdgrvali
      721 vdvdglvsna vpgqerqaa
//
LOCUS       WP_007011610             234 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Novosphingobium
            pentaromativorans].
ACCESSION   WP_007011610
VERSION     WP_007011610.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium pentaromativorans
  ORGANISM  Novosphingobium pentaromativorans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Novosphingobium pentaromativorans"
                     /db_xref="taxon:205844"
     Protein         1..234
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=26456
     Region          8..158
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mnrwlvnhvv aspncnmrkr pismvvlhyt gmksaqeale rmcdpqaevs ahymidedgi
       61 vtnlvpeekr awhagrsywr gevdvnsasi gielvnpghe fgyrpfpepq mdallpllad
      121 imdrhdipra nvvghsdiap arkqdpgeyf dwarlgelgl aldiprakmn lfydnpgafy
      181 lalerfgydi tdgraavraf qrrwrpeiid geidgeiggi lfelllerdt grar
//
LOCUS       WP_007013054              80 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Novosphingobium pentaromativorans].
ACCESSION   WP_007013054
VERSION     WP_007013054.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium pentaromativorans
  ORGANISM  Novosphingobium pentaromativorans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 80)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 80)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 80)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Novosphingobium pentaromativorans"
                     /db_xref="taxon:205844"
     Protein         1..80
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8205
     Region          2..80
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mslnlvflgr ledvagrgkl svpvmpcida vidsldpqlg qalkaprvkl avngilvqdt
       61 dapvlkdgde iaflppvsgg
//
LOCUS       WP_007013218             293 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Novosphingobium
            pentaromativorans].
ACCESSION   WP_007013218
VERSION     WP_007013218.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium pentaromativorans
  ORGANISM  Novosphingobium pentaromativorans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Novosphingobium pentaromativorans"
                     /db_xref="taxon:205844"
     Protein         1..293
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31759
     Region          13..259
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mkvenvlnad nylgetpvws pseqtllwvn ceqpaelirw hpasgkvdrw pmpkriggfv
       61 lagngkalvv lsdgvydfdl tsaeltlraa spldpiiplh ecvtdrqgrl wvggfdhnff
      121 tdrgssqaiy frldgdkltp viegitvang lafspdgrti yagdsprrrv dqwdldpadg
      181 svsnrrpfvt fadddpghid gatvdaeggy wiaavgaaev rrytpdgkld rtielpfsnp
      241 tkpafggpdm ktlyitstrm ainvdhpgyg angplyacsp getgvadtly ses
//
LOCUS       WP_007014203             217 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Novosphingobium pentaromativorans].
ACCESSION   WP_007014203
VERSION     WP_007014203.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium pentaromativorans
  ORGANISM  Novosphingobium pentaromativorans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 217)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Novosphingobium pentaromativorans"
                     /db_xref="taxon:205844"
     Protein         1..217
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=23275
     Region          49..214
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mlfagatlat galmkrssls pvptipvasa rpakvpalar kpvkesrfdv nphllekama
       61 aldahsarie dnsrialvdf svsssrrrmy fldieggkas lilvahgsgs dpdhtgfver
      121 fsnavgsnas segtfltddy yvgkhgrsqr ligldptndn aldraivlhs awyanedmid
      181 thgmlgrsqg cfavgekhld dlfsflgkgr miyagra
//
LOCUS       WP_007015801             404 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Novosphingobium
            pentaromativorans].
ACCESSION   WP_007015801
VERSION     WP_007015801.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium pentaromativorans
  ORGANISM  Novosphingobium pentaromativorans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 404)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Novosphingobium pentaromativorans"
                     /db_xref="taxon:205844"
     Protein         1..404
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44557
     Region          4..397
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 midaaaldil lhdrrigtla rldgdrsift fddayladed rpvlslayrd pyggivntpr
       61 ayqtriepff snllpegmlr dylarragvk avreyplltq lggdlpgavq aipvdaldgl
      121 sddvedgsia gqarhalrfs lagvqlkfsa lknkgknagl titvsgtggd wivklpsarh
      181 pdvpenefaa mslasklgid vpdidlvpld tieglpdgit rygasayair rfdrseegai
      241 hvedfaqvfg vyaddkyena syrqilsvla ieadeasave fvrrltysvl igngdmhlkn
      301 wsliypdrrr pilapaydlv stvayipged salkfhrsre wesftyrele tiadkarlps
      361 hlvistaket veqfdalwdq ekahlpfsge vaaaidrhrk rlav
//
LOCUS       WP_007016178             728 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Bermanella marisrubri].
ACCESSION   WP_007016178
VERSION     WP_007016178.1
KEYWORDS    RefSeq.
SOURCE      Bermanella marisrubri
  ORGANISM  Bermanella marisrubri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Bermanella.
REFERENCE   1  (residues 1 to 728)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 728)
  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   3  (residues 1 to 728)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..728
                     /organism="Bermanella marisrubri"
                     /db_xref="taxon:207949"
     Protein         1..728
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=78031
     Region          6..728
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msldadeeil qdflveagei lellseqlvd lenrpddqdl lnsifrgfht vkggagflqi
       61 nplvdlchva envfdilrng qrqvdadlmd vvlsaldsvn dmfetvrgge mpepadqsli
      121 ddlkifsqpa gaapapkaea aptpptsapd tsneatssgd sgditddefe glldaldgnd
      181 aapakddktt ssdddlfdvg stpaasdede itedefeall dqlhgsgngp sktddvgsss
      241 eqaetaapaa paadgneeit esefeelldk lhgkgkgpse tgaesqvtse pepqaqkpda
      301 epakaeapkq eapapvakae rpaakkpekk qespsaeatv rvdtkrldei mnmvgelvlv
      361 rnrlvrlgln sndeamskav snldvvtgdl qtsvmktrmq pikkvfgrfp rvvrdlarnl
      421 kkevtlelrg eetdldknlv ealadplvhl vrnavdhgve mpdereasgk srngtvilsa
      481 eqegdhills iqddgkgmdp kklqsiavek gvmdqdaadr lsdsesynli fapgfstkte
      541 isdisgrgvg mdvvktkitq lngtinidsq lgkgskivik vpltlaimpt lmvmledqaf
      601 sfplvsvsei fhldltktnv vdgqevvvvr ekaiplfylk rwvipnshnv evteghvvvi
      661 nvgsqrvgfv vdqlvgqeev vikplgkmlq gtpgmagati tgdgrialil dvpsmlqhya
      721 krsgvvaa
//
LOCUS       WP_007016488             457 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Bermanella marisrubri].
ACCESSION   WP_007016488
VERSION     WP_007016488.1
KEYWORDS    RefSeq.
SOURCE      Bermanella marisrubri
  ORGANISM  Bermanella marisrubri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Bermanella.
REFERENCE   1  (residues 1 to 457)
  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 457)
  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 457)
  AUTHORS   ter Beek,J., 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 457)
  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 457)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Bermanella marisrubri"
                     /db_xref="taxon:207949"
     Protein         1..457
                     /product="CmpA/NrtA family 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=51203
     Region          31..311
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mkaksilkrf irytslsvgl svglmnsvsa dypekedlkf gfikltdmap laiakekgff
       61 edeglyvqle aqanwkvlld rvitgeldga hmlagqplga tigfgtqahi itafsmdlng
      121 ngitvsndvw ekmkkniphk ngkpvhpika dylkpiiddy kkdgkafnmg mvfpvsthny
      181 elrywlaagg ihpgyyaphk gdnsgtinad amlsvtpppq mpstleagti egycvgepwn
      241 qqavfkgigv pvitdyeiwk nnpekvfgvs kkwadeypit hksvvkamir aakwlddnnn
      301 anrpeavkil sqsnyvgady eviansmtgt feyekgdkre vpdfnvffry natypyysda
      361 iwyltqmrrw gqiaehkdds wymdiakkvy rpdiyaeaak eliaegkmna adfpdfaked
      421 gfkppqtefi dnvtydgskp naylnklsig lkekdvl
//
LOCUS       WP_007016654             320 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Bermanella marisrubri].
ACCESSION   WP_007016654
VERSION     WP_007016654.1
KEYWORDS    RefSeq.
SOURCE      Bermanella marisrubri
  ORGANISM  Bermanella marisrubri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Bermanella.
REFERENCE   1  (residues 1 to 320)
  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 320)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 320)
  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   4  (residues 1 to 320)
  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 320)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Bermanella marisrubri"
                     /db_xref="taxon:207949"
     Protein         1..320
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36638
     Region          75..313
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          231..312
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mmlptqeayp malfshhlgk dvdllrkaid dyivnvdvts ldtqvsldgy ladissedmq
       61 vsyvrfgmnv nvacfhddvy clvvplagea riqiplwqrp ldkqkafflp phvtldmnys
      121 adcghvvlrf ptsdfyqqvf apvldagall sdqqvrnvvh avhyfvnact flkdmasida
      181 ltnelkqdiv daihnesfvl enrtlvhnek lksavdfiih hpewdykiee lvavtnvpir
      241 tlywsfkhyl gitpyrffvv nrlkrvrldi lkhgkrmtit qialahgfvh lsrfsnqykg
      301 lfgelpietq nkyfkysala
//
LOCUS       WP_007016915             435 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Bermanella
            marisrubri].
ACCESSION   WP_007016915
VERSION     WP_007016915.1
KEYWORDS    RefSeq.
SOURCE      Bermanella marisrubri
  ORGANISM  Bermanella marisrubri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Bermanella.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Bermanella marisrubri"
                     /db_xref="taxon:207949"
     Protein         1..435
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=49575
     Region          2..434
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 maiqfaevvl wgttiavvrw deqaqladfq ytdefiglsq rfdiqvapvv mpvrsapyrf
       61 pnlaretfkg lpgmladvlp dkfgnalidq wliaqgrepk dfnpverlcy tanramgale
      121 fkptqryfdg dpmrdievek mvklasqvlq kkhfeiehed dlnsedleqi lqigtsagga
      181 rakaiinwnq ndhrilpghl eppegfdgwl ikfdgvsenk dkeladpmgf grieyayhll
      241 aveagiemmp crlleegsra hfmtqrfdri hnekrhmtsl cglghfdfnd psstsyeqaf
      301 vlarklevpr ahveqlflrm vfnvvfrnqd dhtkniaflm drqgqwtvsp afdvaysfnp
      361 kglwtskhqm singkrddft lddlkaages tglskrkism lmeqimaskp mwgefsekag
      421 vdverangia ktfrf
//
LOCUS       WP_007016944             319 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Bermanella marisrubri].
ACCESSION   WP_007016944
VERSION     WP_007016944.1
KEYWORDS    RefSeq.
SOURCE      Bermanella marisrubri
  ORGANISM  Bermanella marisrubri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Bermanella.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 319)
  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 319)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Bermanella marisrubri"
                     /db_xref="taxon:207949"
     Protein         1..319
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35698
     Region          1..189
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          233..312
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msiqdlladt gvsvqslesl sdsdqwvter qelqalqnvl ntrgdpfiig wqlgqryqlt
       61 sygiwgyall ssaslrkamd lglrylglty alchielier ngkveliftp kaqgdlgtlv
      121 lvrdisallv iqrelfaggf pvfeihltls eqelpsvvtd ltqglgfelv lnsdqsavif
      181 danlldrplp ranaqtaktc edqcrqllqq qnqyrdiaqd vrdkllslgl yasmeqvass
      241 marttrtlhr qlkeegmswr lvrdevrmgm aeallansis fdeiaerlgy sdaanfshaf
      301 krwkgvspkt yrdglymat
//
LOCUS       WP_007016992             340 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Bermanella marisrubri].
ACCESSION   WP_007016992
VERSION     WP_007016992.1
KEYWORDS    RefSeq.
SOURCE      Bermanella marisrubri
  ORGANISM  Bermanella marisrubri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Bermanella.
REFERENCE   1  (residues 1 to 340)
  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 340)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 340)
  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   4  (residues 1 to 340)
  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 340)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Bermanella marisrubri"
                     /db_xref="taxon:207949"
     Protein         1..340
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38261
     Region          30..211
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          255..336
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 merpnlsldl hpkiavqpvr alinyaerhg lkrsqlleqg slsesqlnds rllidvmrfe
       61 almhfvsgqi cdehlgfhlg qqfepdrwgi lglialtcpn vmaaldaqyr fqslsgnmga
      121 pmlsadesks ilqwvpaydc shnvsemiia glvsltrvli nqpdyspikv tfthsvagnv
      181 aeyseyfgcp vefssqsnsl eidngllqsp lrhgdgetyq ilmqhaksll tqqsfssple
      241 vikdfllktl pdhvpdieev aeymgmsvrs tqrklsefgt sysqvldgir kelamtylkq
      301 tqnpmifise rlgfseqsaf qrafkrwtgv tpkqfrtmrh
//
LOCUS       WP_007017007             213 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Bermanella marisrubri].
ACCESSION   WP_007017007
VERSION     WP_007017007.1
KEYWORDS    RefSeq.
SOURCE      Bermanella marisrubri
  ORGANISM  Bermanella marisrubri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Bermanella.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Bermanella marisrubri"
                     /db_xref="taxon:207949"
     Protein         1..213
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23445
     Region          7..210
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mensmnftqa lqwryapkql ngnavpastl griidaahla pssyglqpys vivvqnknll
       61 nqiflkacpq aqiqgssell vfasktqvnd elvdnyirgl adakkqpean fsefssamka
      121 ainsmesnda kkewanrqay islglavsaa alekvdaapm egfdpealdd llglkeqgls
      181 svvllalgyr deddsyakqp kwrkpynefi qwr
//
LOCUS       WP_007017344             276 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Bermanella marisrubri].
ACCESSION   WP_007017344
VERSION     WP_007017344.1
KEYWORDS    RefSeq.
SOURCE      Bermanella marisrubri
  ORGANISM  Bermanella marisrubri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Bermanella.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Bermanella marisrubri"
                     /db_xref="taxon:207949"
     Protein         1..276
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30038
     Region          3..273
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mlfdlhchsl rsdgqlsptd lvnrayeqgv thlaltdhdt inglqeakqa akplgleiih
       61 gieistvwng mgihvvglnf daehpamlaa ierqencrle raktiakkle kqgaegiwea
      121 aqkvangaqi grphfaqali dmgkvnnmaa afkrylgagk sgdvktlwpe mseavqwivd
      181 aggtavlahp dkykltrtkl rlllnafkea gggavevttg gmessfaqrm aqycdefgll
      241 gsqgsdfhgp rpwselgkfp pmpksvtpvw hdwyad
//
LOCUS       WP_007017722             339 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Bermanella marisrubri].
ACCESSION   WP_007017722
VERSION     WP_007017722.1
KEYWORDS    RefSeq.
SOURCE      Bermanella marisrubri
  ORGANISM  Bermanella marisrubri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Bermanella.
REFERENCE   1  (residues 1 to 339)
  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 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 339)
  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   4  (residues 1 to 339)
  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 339)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Bermanella marisrubri"
                     /db_xref="taxon:207949"
     Protein         1..339
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38410
     Region          23..210
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          258..336
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mehlgfassg avlqylktaa dygldarali aqvginsdll dnklkrisge sfqellalli
       61 ektqdpcfgl kssryvqpgs ysvlgymlmn cnglqealek tptyerlvgd mgtsqinrla
      121 ddntemrwic nypnpkvrph mianvlgswv nfarflvdkp ngkpkavyfe fpqpdatslr
      181 qfqsmfncpi yfnqsssali iddhllslpm rqpdqqllkt lenhadilma dindkqplpm
      241 qtknvirgll legiprkemv skrlgltert lqrklqafec syqqlldevr eeqakellie
      301 selsiqdiaa rlgfseprsf hrsfknwtgm tpgefrqak
//
LOCUS       WP_007017618             160 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Bermanella marisrubri].
ACCESSION   WP_007017618
VERSION     WP_007017618.1
KEYWORDS    RefSeq.
SOURCE      Bermanella marisrubri
  ORGANISM  Bermanella marisrubri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Bermanella.
REFERENCE   1  (residues 1 to 160)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Bermanella marisrubri"
                     /db_xref="taxon:207949"
     Protein         1..160
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=17626
     Region          3..160
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cl49639"
                     /db_xref="CDD:483979"
     Site            order(114..115,118,131..134,136)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mreicisian qtlttienge tikvfsvsta lngpgeqngt gqtptgshyv rakiggdqpk
       61 csvfrgrrpt geiysddlak aypkrdwils rilwlcgkev gknrlgnvdt maryiyihgt
      121 pdteamgqal shgcirmrnd dvielfdwap iqcpvlitke
//
LOCUS       WP_007018156             174 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Bermanella marisrubri].
ACCESSION   WP_007018156
VERSION     WP_007018156.1
KEYWORDS    RefSeq.
SOURCE      Bermanella marisrubri
  ORGANISM  Bermanella marisrubri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Bermanella.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Bermanella marisrubri"
                     /db_xref="taxon:207949"
     Protein         1..174
                     /product="TRAP transporter small permease subunit"
                     /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=19540
     Region          1..>132
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 msslltlcre itertglitr ylggilvlit flvvllrygf nyapialqet mtylhaalfm
       61 lgaaytlkhn ghvrvdvfyq nmsvrkqawv nifgtlfllf ptclfvliic wpyvadswsi
      121 qersiegsgl pflyllktll ilqplllmiq gvaiiiengv kltqtkpvqn eggq
//
LOCUS       WP_007018375             257 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Bermanella marisrubri].
ACCESSION   WP_007018375
VERSION     WP_007018375.1
KEYWORDS    RefSeq.
SOURCE      Bermanella marisrubri
  ORGANISM  Bermanella marisrubri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Bermanella.
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
REFERENCE   2  (residues 1 to 257)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Bermanella marisrubri"
                     /db_xref="taxon:207949"
     Protein         1..257
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28888
     Region          12..102
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          <75..253
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          176..253
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mdkqgfhfql sqpsgrlsam iqgfwvasvd qaeaitkply sdagsgivln lnggveiegq
       61 sipsgiimlp tsmqaehvcm qpgclfvgir fhpaigygvl grhyieptll akeddifqlh
      121 slhtslknep diqqyipmly ewaeqnldft dvipqtleks lqyisqaasl stlqsevdvs
      181 qrqierickl wlgmtpkhyq rilrirkaie clrenpsanl advahdfgfs dqahmtrefr
      241 tiarltpkqv lqkkvir
//
LOCUS       WP_007018782             338 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Bermanella marisrubri].
ACCESSION   WP_007018782
VERSION     WP_007018782.1
KEYWORDS    RefSeq.
SOURCE      Bermanella marisrubri
  ORGANISM  Bermanella marisrubri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Bermanella.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  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   4  (residues 1 to 338)
  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 338)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Bermanella marisrubri"
                     /db_xref="taxon:207949"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38833
     Region          22..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          253..331
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mrtstiashy vscaiagakr qgldvhdilr raditpdiln epkarifpdk makllrilvs
       61 elndeflgld dkpsprgsfe tlcqlivpcs tlrealllgt qfyglfdmal etqyadsqyg
      121 gmlravekrp cldehhylte fqlvlwhrla cwltgkripi elaefnyakp ehsdeyrlff
      181 ygerlfqrpq talhfkssyl dlpivrtrnd lpellkeapy vflvkpnntt sinaqirril
      241 qgnmddselp dfetvahkln tstqtlrrrl keentsfqai kdqvrrdmai yylgdpnisi
      301 neialkvgft epstfhrafk kwtgmtpgdy rseqaqpa
//
LOCUS       WP_007018735             278 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Bermanella marisrubri].
ACCESSION   WP_007018735
VERSION     WP_007018735.1
KEYWORDS    RefSeq.
SOURCE      Bermanella marisrubri
  ORGANISM  Bermanella marisrubri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Bermanella.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Bermanella marisrubri"
                     /db_xref="taxon:207949"
     Protein         1..278
                     /product="formate/nitrite transporter family protein"
                     /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=29900
     Region          2..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msyvvpsefa tkmvdagesk lfmstrdtli rafmagaila laaafavtva vqsgsfliga
       61 ilfpigfcml ylmgfdlltg vfmltplall dkrpgvtvpt ilrnwglvfc gnfagaltva
      121 fmiafiltmg fntepgavge klssvgeart lgyaeygtag wfaifirgml cnwmvsmgvv
      181 gamistnvsg kvlamwmpim lfffmgfehs vvnmflfpsa mimggdfsim dyliwneipt
      241 vlgnlvggla ftgltlyvth yktgtkrpqp emkaataq
//
LOCUS       WP_007020129             708 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Neptuniibacter caesariensis].
ACCESSION   WP_007020129
VERSION     WP_007020129.1
KEYWORDS    RefSeq.
SOURCE      Neptuniibacter caesariensis
  ORGANISM  Neptuniibacter caesariensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Neptuniibacter.
REFERENCE   1  (residues 1 to 708)
  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 708)
  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 708)
  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 708)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Neptuniibacter caesariensis"
                     /db_xref="taxon:207954"
     Protein         1..708
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=75847
     Region          6..703
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mstentvtdh evseklkgle laqrseqstt gkliywigvv falahiyfnt lgtwselyvs
       61 aihfggfalm calmvpmfkg gnraqkslal vldlllgiaa ivcalyligf edalydrgvk
      121 faqwdwvfsv caifialema rrttgwfipc lilvaltyvf wwgkyidgif gfaglsletl
      181 lyrsyfsseg mfgqiarisw tyvfmfilfg aflvksgagd fiielsrcaa grfvggpgfv
      241 avlgsglmgs vsgssvantv stgvitiplm rkagfparfs agveaaastg gqlmppvmga
      301 gafimasytq isyldiisia alpallyfls vgffvrveak rshahaveld trpigevfrg
      361 gwhfllplvv lvalliygft ptyaagisii svivsswlsk npmgikeild alaqgsknma
      421 ttamllisvg lvvnvvamtg igntfslmvt dwaggsllit lvlvalasli lgmglpvtaa
      481 yivlatlsap alyglmaesr lldlmvagql peaaktifml vdmekvalls apmapadaqa
      541 llslvpadfk gqlleqalap etlamillsa hmiifwlsqd snvtppvclt afaaaaiakt
      601 ppmatgftaw kvakglyivp llfaytnfig geplevlsif ifavfglygf vgfmegyleg
      661 rlnlisralc gvtamallwp hgelminlla mlafavifwl srrnseta
//
LOCUS       WP_007020430             815 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Neptuniibacter caesariensis].
ACCESSION   WP_007020430
VERSION     WP_007020430.1
KEYWORDS    RefSeq.
SOURCE      Neptuniibacter caesariensis
  ORGANISM  Neptuniibacter caesariensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Neptuniibacter.
REFERENCE   1  (residues 1 to 815)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 815)
  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   3  (residues 1 to 815)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..815
                     /organism="Neptuniibacter caesariensis"
                     /db_xref="taxon:207954"
     Protein         1..815
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=89095
     Region          3..797
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msidlsqfig tfleesyegl evmessllal dsadeetint ifraahsikg gagtfgfsev
       61 adfthvvetl ldemrsgkqe vtpplvnlll esvdcikmll eatqdgpaad anqinqvqer
      121 lqkaldgdvs dnassggtet svataevsvs spsqlaweie fkphpgllqs ghepafmfea
      181 lqdlgelnvv aklkkvpdls sldpeqifik wqlnlisncs keeieeifew vedecdlsiv
      241 qkeveaekpa vaesqqtdsr evreilfkpd asllatgnep sflfqaladl geleievdss
      301 glpdldqldp eklllswrfk lrsdcpeeei teifewvede celtiqgask vstqpaetet
      361 qpvaseqpve aasdkpatpa avqstspaas prkakpaaes ssirvetdki dalinrvgel
      421 vitqamlgqv gdelsdlvsg seierlqsgl eqlerntrdl qedvmrvrml pisfvfnrfp
      481 rlvhdvsgkl gkkveliitg eqteidktvm ekigdpmvhl irnsldhgle speervaagk
      541 petgkvqlda yhqggfiiid iiddgrglnt ekiyqkalek glvttdqnls dseinelifk
      601 pgfstaeavs dlsgrgvgmd vvrrnieslg ghvrvksepg hgstftvslp ltlaildgql
      661 irvhnetyiv plisivetil adksslspia genkllhfrd eyiplinlrs lfklpmqeeq
      721 mescliaive nggqkvgliv delfgqqqvv ikslevnfkr iegfagatil gdgsvalild
      781 iaglmkrgld hetartakkr ndqtrtddsl qgvva
//
LOCUS       WP_007020673             359 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Neptuniibacter
            caesariensis].
ACCESSION   WP_007020673
VERSION     WP_007020673.1
KEYWORDS    RefSeq.
SOURCE      Neptuniibacter caesariensis
  ORGANISM  Neptuniibacter caesariensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Neptuniibacter.
REFERENCE   1  (residues 1 to 359)
  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 359)
  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 359)
  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 359)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Neptuniibacter caesariensis"
                     /db_xref="taxon:207954"
     Protein         1..359
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39932
     Region          7..355
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 msiynykkvl tgaalccsmf aassamaadk vyklklaetw gpntpilget tkkmaaladt
       61 msngrlkiti dsankhkapf gvfdmvragq ydighsasyy wkgkvpntly fttmpfgmta
      121 peqygwfyyg egqalmnevy gkfgmlsfpg gntgvqmggw fqkeinsled vkglkiripg
      181 fageiwaklg akpvniapgd lytslerktv davewvgpsl dirlgfhkia pyyytgwhep
      241 aselqfmvnk kkfeklpedl qtilttamrt aaydmyiqsy hesgvnwdtm kkefpnikvk
      301 sfpaevisam reandallke aaakdpltkr iqesqaayma karawtdisd kaylnslsk
//
LOCUS       WP_007020892             356 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Neptuniibacter
            caesariensis].
ACCESSION   WP_007020892
VERSION     WP_007020892.1
KEYWORDS    RefSeq.
SOURCE      Neptuniibacter caesariensis
  ORGANISM  Neptuniibacter caesariensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Neptuniibacter.
REFERENCE   1  (residues 1 to 356)
  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 356)
  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 356)
  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 356)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Neptuniibacter caesariensis"
                     /db_xref="taxon:207954"
     Protein         1..356
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=38782
     Region          26..349
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkkfakslis aavvtaavag ttapaqaadk lllktpiafg shlpalgtpi vwvadqlklv
       61 sdgkvkmkiy epgklvspke ildavssgkv nsgystagyw qgkmpaaalf savpfgpeag
      121 eymawlyygn gmnlyqemyd tagynvkvlp caiispetsg wfskpiekpe dlkglnmrff
      181 glgasvmekl gvgtvqlpgg eifgalekga idasefsqpa idqrlgfhki vkynyfpgwh
      241 qqatvfelli nkdtwgkmsk gqqalvettc kasmtnaiae geamqfpvmq kaadngvqir
      301 ywnqtmldtf kstwdevvae ktaadpffkk vwddmstfrs gydlweanaf lpratk
//
LOCUS       WP_007021118             711 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Neptuniibacter caesariensis].
ACCESSION   WP_007021118
VERSION     WP_007021118.1
KEYWORDS    RefSeq.
SOURCE      Neptuniibacter caesariensis
  ORGANISM  Neptuniibacter caesariensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Neptuniibacter.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 711)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 711)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Neptuniibacter caesariensis"
                     /db_xref="taxon:207954"
     Protein         1..711
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=80542
     Region          135..706
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mpevleidgn allekygngq krqrlrknvq llflgltaee taplitllrt srisprgkqv
       61 nseqefldal serswdlilc tidrdkftsk havshlkrld kdipviqiip ssdsqlllqg
      121 lknhlqavvp ldekelvlis irreldhldy rrrlrkaeas laeetkrsqq lmdssrnaig
      181 cchdgklsyv nesfcelfgi enkdkalgkn laefftyedr hefieqlqli erqesndllv
      241 qltaqrsdrs efaanlelap ieikdalgvr aifrvdehnv shllsedldf vsglfnkdhl
      301 qkqleqitqk alrgghdcsl iyieldqldq ikakfghegs dqlirdvsal lqkkvnkahl
      361 lthptenafv ivfkdpniqt aqsfsenlck viaknrssaa gvevqstcsi giavindntp
      421 pptellqrat taianlrees pqgdgvllhi peslsneced defecirnsi ennefkllfq
      481 pivnltaedq tahhyeallr lkndeqgels pnefmsaigd setaikvdrw vieqglkhlk
      541 rslnqehknv lfinvsahal gdkklltwls gvlrknnipa drlvfqises disisprqaq
      601 ifaeklnkih crvcvkhfgs vpnydnmlts ihsdfvkldg sfisdlgkdp eqdeqfmsma
      661 aqlkslnkvt iapmveqtkt mahlwkagid yvqgyylqpp rekmdydffa e
//
LOCUS       WP_007022600             459 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Neptuniibacter caesariensis].
ACCESSION   WP_007022600
VERSION     WP_007022600.1
KEYWORDS    RefSeq.
SOURCE      Neptuniibacter caesariensis
  ORGANISM  Neptuniibacter caesariensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Neptuniibacter.
REFERENCE   1  (residues 1 to 459)
  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 459)
  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 459)
  AUTHORS   ter Beek,J., 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 459)
  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 459)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Neptuniibacter caesariensis"
                     /db_xref="taxon:207954"
     Protein         1..459
                     /product="CmpA/NrtA family 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=51174
     Region          32..313
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mlkkkkalls kvissavlaa slvtvpawaa igepekedlk fgfikltdma plaiayekgf
       61 fedeglyvtl eaqanwkvll drvidgqldg ahmlagqplg atigfgtqsh iitafsmdln
      121 gnaitvsndi wsqmkqhvpm gadgkpvhpi kadalkpvve kyqdegkpfn mgmvfpvsth
      181 nyelrywlaa ggihpgyyap hkgdtsgtid adallsvtpp pqmpatmeag tiygycvgep
      241 wnqqavfkgi gvpvvtdyei wkdnpekvfg vsktwadenp nthlrvvkam iraakwlddn
      301 nngnrpeave ilsrseyvga dydviansmt gtfeyekgdk revpdfnvff rynatypyys
      361 daiwyltqmr rwgqiaepks drwfmdiakk vyrpdiyaea akelieegkm tadmfpdfat
      421 edgfkspqth fidgitydgs kpneylkkfe iglkpedki
//
LOCUS       WP_007022602             341 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Neptuniibacter caesariensis].
ACCESSION   WP_007022602
VERSION     WP_007022602.1
KEYWORDS    RefSeq.
SOURCE      Neptuniibacter caesariensis
  ORGANISM  Neptuniibacter caesariensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Neptuniibacter.
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
REFERENCE   4  (residues 1 to 341)
  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 341)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Neptuniibacter caesariensis"
                     /db_xref="taxon:207954"
     Protein         1..341
                     /product="CmpA/NrtA family 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=37913
     Region          8..264
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mtaptelekt kltlgfvall dcaplvvare kgffnkygls vvlskesswa tirdkvsfgi
       61 ldgaqmlapm plaatlglng nktpmvtala lsqngtaitl gkelflalsq hvtdwdndet
      121 vgsqfkalik smgrkpviat vypysnhhyq lrywlkkhni sfaddvelva ipptkmlenl
      181 snglidgycv gepwnslali nqsggllttg yriwgtqiek vlgvtaqwad enplthqalv
      241 raiyeacewl sqsenkdeli ellslppyld rsanlikgft ppysmeqrff gnevnlpgqq
      301 qgqflleqmq acgqlsdeqi dlfsiskqvf redlyrewct n
//
LOCUS       WP_007022603             199 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Neptuniibacter
            caesariensis].
ACCESSION   WP_007022603
VERSION     WP_007022603.1
KEYWORDS    RefSeq.
SOURCE      Neptuniibacter caesariensis
  ORGANISM  Neptuniibacter caesariensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Neptuniibacter.
REFERENCE   1  (residues 1 to 199)
  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 199)
  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   3  (residues 1 to 199)
  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   4  (residues 1 to 199)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 199)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 199)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Neptuniibacter caesariensis"
                     /db_xref="taxon:207954"
     Protein         1..199
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22063
     Region          1..189
                     /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"
ORIGIN      
        1 mkhlnvliid eeadrvqalk dalhqlghhv vchlsdtsdl nhhvesfhpd iviidmdspd
       61 rdtlesmatm sqnnprpivf faeqqndrrt maaainagvs ayiadglqad rvkaimdtai
      121 ahfdahslir teleeartql adrkviekak gmlmkhqgcd enqayqtlrk iamdrgqklp
      181 dvaasvievl natngllkk
//
LOCUS       WP_007024272             308 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Saccharomonospora
            iraqiensis].
ACCESSION   WP_007024272
VERSION     WP_007024272.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora iraqiensis
  ORGANISM  Saccharomonospora iraqiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 308)
  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 308)
  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   3  (residues 1 to 308)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Saccharomonospora iraqiensis"
                     /db_xref="taxon:52698"
     Protein         1..308
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33600
     Region          193..295
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mtslphglhg ahlrsdlaal igrgalraal regrltsfsr tvvvearrvg efhtraaaal
       61 ltvgdtavls gqsalavhgc aaaetapvhl lvpytrrtyr rtglvthqgt vdgadvdava
      121 glrvhvpqaa laevlcrgsr rtalacadat lrllaehere afrtlvagrv drrpdirgrr
      181 qahelltlas glaespaesg vlltlvdggl pvpeqqvpvl dhrgvvlyrl dfawrevrva
      241 veydgyrwhe grrdsdaard edlrrrgwtv vradardlve parlrsevre llrrrglplw
      301 ngsgdsrv
//
LOCUS       WP_007024957              98 aa            linear   BCT 20-JAN-2025
DEFINITION  TOBE domain-containing protein, partial [Saccharomonospora
            iraqiensis].
ACCESSION   WP_007024957
VERSION     WP_007024957.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora iraqiensis
  ORGANISM  Saccharomonospora iraqiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 98)
  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 10506755
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Saccharomonospora iraqiensis"
                     /db_xref="taxon:52698"
     Protein         <1..98
                     /product="TOBE domain-containing protein"
                     /GO_process="GO:0015689 - molybdate ion transport
                     [Evidence IEA]"
     Region          32..88
                     /region_name="TOBE"
                     /note="TOBE domain; pfam03459"
                     /db_xref="CDD:427310"
ORIGIN      
        1 apdlepggpa vavfapgava vypagtdpvg sprnvvdtvv tavephggal vrvrtaasvt
       61 aevtpaavad lglepgtpvr lavkaaaitl hpaaqaig
//
LOCUS       WP_007025324             228 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Saccharomonospora
            iraqiensis].
ACCESSION   WP_007025324
VERSION     WP_007025324.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora iraqiensis
  ORGANISM  Saccharomonospora iraqiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 228)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Saccharomonospora iraqiensis"
                     /db_xref="taxon:52698"
     Protein         1..228
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=22719
     Region          134..221
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mslfdgvsrp mraaglglia vavvatalgg vsvvtggdpa dtaatgsaep dpgagggdhg
       61 dtpddpgrge ngpdsddgas gddgasgddg adggepgrdt ggdktgaedg dadgdgtdgd
      121 rgddrqasve etavrvynns disglatdag ddlrargwnv vevanysdgi ipnstvyfrp
      181 gtdeerlaha lgedfdlrve prfdgisdas pglvvivtrd ydgpvdpk
//
LOCUS       WP_007028690             912 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Amycolatopsis decaplanina].
ACCESSION   WP_007028690
VERSION     WP_007028690.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis decaplanina
  ORGANISM  Amycolatopsis decaplanina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 912)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..912
                     /organism="Amycolatopsis decaplanina"
                     /db_xref="taxon:208441"
     Protein         1..912
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=101022
     Region          131..590
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 markqaakgp tpvdaikhgd krtniptada hefvdptlee vrkvrysrde tldpqlvwrg
       61 kyppigdads tdndlvtdap piyiqekidp rvlienlrrt seheaeqpel alfesfdgld
      121 emdqidfyrh danwsnrmil gdslqvmssl aererlrgkv qmiyldppyg ikfgsnwqas
      181 arsrdvkdgk ledaareaeq ikafrdtwed giqsylsylr drlfaardll tesgscfvqi
      241 gdenvhlvrs lmdevfgsen fisqivlktt sgagspsggt lalagvsdhi iwygkdreql
      301 kyrqiltgks rgqgsdlykr vrlpdgssra atkdelneps llpegarlfr pdnltsqssg
      361 apqffdvkin dtvypvgksg wktsrsgmdr lvaadrifit rngtlqyvrf lddfpampin
      421 nvwtdvgtgs fteekiyivq sntkviqrcm lmctdpgdlv ldptcgsgtt afvaeqwgrr
      481 witidtsrva ltlarqrimg akypwyllad saeghakaqs mtaqtlpqqe ftddirhgfv
      541 yervqhvtlk siannpdike gmsrseidva ikrhadfell ydkpyenkkr lrvsgpftve
      601 slsphrslaf pggsgdtthe sggeteaakd adapnfeqsi ldnlakagiq ngtrseritf
      661 asfesyagey iqavgeqagd eatrvalaig pqygtvspsy vkkaareain aedvdllcil
      721 gfafdaqvtg ltdddgvtve asdegfanva airklgript lmvrmnadll mgeelkktga
      781 gnlftvfgep dieldetadg lvvhlngvdv ydpttgevrs kdtgqialwm idtdyneesf
      841 fvrhcyftgg ndpykglkra lkadidadaw eslysitsqp fakpetgkia vkvindygde
      901 vmkvfgvgdg ar
//
LOCUS       WP_007027685             113 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein, partial [Saccharomonospora
            iraqiensis].
ACCESSION   WP_007027685
VERSION     WP_007027685.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora iraqiensis
  ORGANISM  Saccharomonospora iraqiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (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   2  (residues 1 to 113)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Saccharomonospora iraqiensis"
                     /db_xref="taxon:52698"
     Protein         <1..113
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          46..>89
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 gtdpavaavl aarqrrdkar evvasdplma relrigrpdl rpdyddgglv dlnnapasal
       61 aevceldpgt aerivearsa rggfltvddv ftavdvplga wemirdravv ipr
//
LOCUS       WP_007029010             362 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Amycolatopsis decaplanina].
ACCESSION   WP_007029010
VERSION     WP_007029010.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis decaplanina
  ORGANISM  Amycolatopsis decaplanina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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
REFERENCE   3  (residues 1 to 362)
  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   4  (residues 1 to 362)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Amycolatopsis decaplanina"
                     /db_xref="taxon:208441"
     Protein         1..362
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=38239
     Region          3..299
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mtiefrgvtk rypdgtvavd dlnltvedgt itvfvgpsgc gkttslrmin rmveptsgtv
       61 lldgkdvsdg dpallrrgig yviqhaglfp hrtvldnvat vpllsgwdkg karkraaell
      121 etvglpaelg krypaqlsgg qqqrvgvara laadspvllm depfsavdpi vreelqdell
      181 rlqsqlgkti vfvthdidea vrlgdkiavl rvggvlaqyg tpsdvlrhpv ddfvasfvgk
      241 drgyrglsfl saegivveev ervevgkpap gpsddwrvav naegqprgwl rpgstvdggl
      301 aetdlvaggs lylqgspirg aldaalsspa slgvvvdadq kvlgvvrakq vlevieapsl
      361 ss
//
LOCUS       WP_007031572             341 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Amycolatopsis
            decaplanina].
ACCESSION   WP_007031572
VERSION     WP_007031572.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis decaplanina
  ORGANISM  Amycolatopsis decaplanina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 341)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Amycolatopsis decaplanina"
                     /db_xref="taxon:208441"
     Protein         1..341
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36151
     Region          4..326
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mpaahivstg talpgdaidn eimagklgis aewiemfigt rkrhfaidle tgkpthtlad
       61 lgaqagaqal aragiepeel dfvilatatp dtlmpatvnl iasrlcvnhv styqlqsgca
      121 gavqaldlar rllddqhrlg lviggdvsvk hfvadremqg vstaelvnyv lfgdgagaiv
      181 vtadavpgsl llrqvlnrft glgrapgqvv rwfgagdlar tesepdppfe edykaieerv
      241 pplakealde vlsstgwdre sasyllppql sgrmtsriaa dlalghaaei scvaetgntg
      301 natpffqldl lydrirpger avaiaiessk wikgaftveg m
//
LOCUS       WP_007032061             102 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Amycolatopsis decaplanina].
ACCESSION   WP_007032061
VERSION     WP_007032061.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis decaplanina
  ORGANISM  Amycolatopsis decaplanina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Amycolatopsis decaplanina"
                     /db_xref="taxon:208441"
     Protein         1..102
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11670
     Region          2..99
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mhesielrkr eieelcrths vrrldlfgsa vddrfdlvss dvdvlvefda gpgfdyfgty
       61 fdlkeglerv lgrpvdlvsv tsirnpyfkq qvletrelly aa
//
LOCUS       WP_007032326             362 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Amycolatopsis decaplanina].
ACCESSION   WP_007032326
VERSION     WP_007032326.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis decaplanina
  ORGANISM  Amycolatopsis decaplanina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 362)
  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 362)
  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
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 362)
  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   5  (residues 1 to 362)
  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   6  (residues 1 to 362)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 362)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 362)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Amycolatopsis decaplanina"
                     /db_xref="taxon:208441"
     Protein         1..362
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38402
     Site            order(9..10,14..16,30..32,41..44,46..47,50..51,53..54,
                     60..62)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Region          18..67
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          78..347
                     /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 mpetgvnlrg lrqhnrtlll thilraggls rvelaertrl tqqavskivp elleagllde
       61 erqpasgvgk prtllrvrad arhalgaqld rdsfrvvmtg ltgkiiasrg gplspgftpg
      121 qavaalgeat ealldgvere rvlglgvgsv gpldhlegvv rdatnmpgwh hvplrellak
      181 rtglpvrldk ntnaaafaqh wpegdraata vvlvgtgigv gllidgrlyr gprtnagefg
      241 httlafdgpr cacgrrgcve vlhnaaatte eaagllgigl adlvqvldle rvvltgravr
      301 aepevyrdtv aarlrellpl phwqriqvdl demgddvvaf gaaaevlagf ydsgditgws
      361 pg
//
LOCUS       WP_007033329             314 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Amycolatopsis decaplanina].
ACCESSION   WP_007033329
VERSION     WP_007033329.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis decaplanina
  ORGANISM  Amycolatopsis decaplanina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 314)
  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 314)
  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   3  (residues 1 to 314)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Amycolatopsis decaplanina"
                     /db_xref="taxon:208441"
     Protein         1..314
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35626
     Region          191..295
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mprnhyaeva dfsgpflgsr avsegdltrs qlrsgpynrl fqnvyvpiri pqdhvlrcka
       61 ailaapasav ltgcsaatvr gfpfaldndp vefvipeeeg fhfqrgmhlk rsrligedfe
      121 pwrdgriatp lrmtmdilan trlhrsfprv vglvdaliha gfvereqler yfehrhdhgi
      181 vrarkalels dgraesipes evrtwlrihd ieaepqvevy rgerflgrld laireaklai
      241 eydgawhleg eqprldaerr tlmeadgwrf ivitkeelyg dpkamvarvr dalrasplpq
      301 vgdqlrghrc psig
//
LOCUS       WP_007033426             211 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Amycolatopsis
            decaplanina].
ACCESSION   WP_007033426
VERSION     WP_007033426.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis decaplanina
  ORGANISM  Amycolatopsis decaplanina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 211)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Amycolatopsis decaplanina"
                     /db_xref="taxon:208441"
     Protein         1..211
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=21026
     Region          115..203
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mslfsglsrp mkaaglalvg vaviaavigg itltsgggds dtatppgttp ttsdgapqps
       61 spapgspsas tppassapps sapassappa sqpgqtggpg pgqpggdqqa shkwvtvrvy
      121 nnstiqglae qaakdfrasg wnvsevkgyp grlpetvayy rpgtdeeaaa kalalefgfr
      181 aeprfeeikn igpgvivilt kdykandkdg s
//
LOCUS       WP_007034293             313 aa            linear   BCT 20-JAN-2025
DEFINITION  DNA polymerase domain-containing protein [Amycolatopsis
            decaplanina].
ACCESSION   WP_007034293
VERSION     WP_007034293.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis decaplanina
  ORGANISM  Amycolatopsis decaplanina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Zhu,H., Nandakumar,J., Aniukwu,J., Wang,L.K., Glickman,M.S.,
            Lima,C.D. and Shuman,S.
  TITLE     Atomic structure and nonhomologous end-joining function of the
            polymerase component of bacterial DNA ligase D
  JOURNAL   Proc Natl Acad Sci U S A 103 (6), 1711-1716 (2006)
   PUBMED   16446439
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Zhu,H. and Shuman,S.
  TITLE     A primer-dependent polymerase function of pseudomonas aeruginosa
            ATP-dependent DNA ligase (LigD)
  JOURNAL   J Biol Chem 280 (1), 418-427 (2005)
   PUBMED   15520014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Amycolatopsis decaplanina"
                     /db_xref="taxon:208441"
     Protein         1..313
                     /product="DNA polymerase domain-containing protein"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=34207
     Region          6..284
                     /region_name="LigD"
                     /note="Eukaryotic-type DNA primase [Replication,
                     recombination and repair]; COG3285"
                     /db_xref="CDD:442515"
ORIGIN      
        1 mcerdgvklt nldqplfega tkrdlvdyld avagriipvl enrplsvirv lrgqepfmqk
       61 nlpkytpdwv krygmwaets krqvsyalcd drrtllwfan qraveyhptl mtadvdagpt
      121 hlvldldppp gddfthvvka avlvrqalsd sglvgtvkts gskgvhifvp ltpgqgfedv
      181 aaatralaar aekidpalat tayivedreg kvyldstrag gntvaaaysp rlrpgltvsf
      241 pvawevlenv vpadftvhta pgllgdkdpw aesmpvpqtl padlveqght ipiarvvamh
      301 egkrrarsrd rks
//
LOCUS       WP_007037015             331 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Enterocloster bolteae].
ACCESSION   WP_007037015
VERSION     WP_007037015.1
KEYWORDS    RefSeq.
SOURCE      Enterocloster bolteae
  ORGANISM  Enterocloster bolteae
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Enterocloster.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Enterocloster bolteae"
                     /db_xref="taxon:208479"
     Protein         1..331
                     /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=38348
     Region          9..284
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 meqsrckevd ifkglliilv vvghydsdiv hdviflfhmp lffiisglll krehimegtk
       61 yirtkiqnlm ipysvyliid lflirrdyav gsivralwgg ravpgvywyi tcflfslilf
      121 fgllrkfsdk tvkrvilifg gggvieshiv ekvhflqspg ipwnldvsli alvyvgigff
      181 ykdkiknlle sdsrkydava gvtafglvmf swfiyrdgnr lyyfdmkpay ykelllavli
      241 pcafgivfar faywlekeky feilkrflyl cgratipimf mhvplnhwkd cvgygrleym
      301 vigigiplmi ifafnensvm rkvlgipkln r
//
LOCUS       WP_007038711             903 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Enterocloster
            bolteae].
ACCESSION   WP_007038711
VERSION     WP_007038711.1
KEYWORDS    RefSeq.
SOURCE      Enterocloster bolteae
  ORGANISM  Enterocloster bolteae
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Enterocloster.
REFERENCE   1  (residues 1 to 903)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 903)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..903
                     /organism="Enterocloster bolteae"
                     /db_xref="taxon:208479"
     Protein         1..903
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=102206
     Region          315..902
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mriipkktrv smeffkgiel ldiviaaagv tltlfmllsn lplrwmaali vfivfsasii
       61 plddekayks lyyairyams ykefvkhpek kgqipvagvt pftgisdmfi eygtsylgvv
      121 veipsiefrf lteprqnqli dqvygsilrt vndtdsaamv kldrpvlyds fiegeekkme
      181 dlkaayirgl mtdeeltvri giiqdrmsql elfnnketvy lpfhymvffg rdrgrlteqa
      241 qnmvdtlgph giecrilkeq elaiflkyny sgvfdereaw kltpdqymdw ilpdklavts
      301 rtvaydglvt hnlrvtdypi vvpnawghal fnrpdvrvtl kmrpidrykg ikqidraide
      361 lreqgastgk tsrlmelgsh idtlaevlsl lqgdneilmd vnifitaydy easpellgpg
      421 yrppgqgigm krqirrelse wgfkssdmfm rqfdayasgh isafdafskd grgihsgsva
      481 aafpyvykvm mekkgiclgk sagrpvfldf farnkervns nmvvigksgs gksyatksil
      541 anlaaenski fildpeneyl glarslkgki idvgsategr lnpfhiitgl sdeedeldgd
      601 eeenqipgak vsfnmhmqfl eefyrqilpg ieadaleyln nitirmyeak gidaetdlsg
      661 ltpgdyptfd dlyekilndf qmstgdyskk nltvllnyis kfatggrnag lwngeasist
      721 qenfivfnfq sllanknntv anaqmllvlk wldneiiknr dynlrygasr kiiivideah
      781 vfidskypva ldfmyqmakr irkyngmqii itqnikdfvg teelarksta vinacqysfi
      841 fplspndmhd lcrlyekaga ineseqdeii nngrgrafvv tspserssid ietpkdierl
      901 fgi
//
LOCUS       WP_007039085             172 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Thiorhodococcus drewsii].
ACCESSION   WP_007039085
VERSION     WP_007039085.1
KEYWORDS    RefSeq.
SOURCE      Thiorhodococcus drewsii
  ORGANISM  Thiorhodococcus drewsii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiorhodococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Thiorhodococcus drewsii"
                     /db_xref="taxon:210408"
     Protein         1..172
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=18581
     Region          11..172
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mlalipgaga sarpidlivi hatggpgckh grlwhapggt lesnlrhfat hpnigyhyli
       61 grdgetvagt petqvafhar grnsssigie lvndgngkdp fppaqinali dllarllhry
      121 dltpdrilgh sevdrrafvc gkkryklkid pggeypgssg nfpwkrvrea lr
//
LOCUS       WP_007040408             144 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Thiorhodococcus drewsii].
ACCESSION   WP_007040408
VERSION     WP_007040408.1
KEYWORDS    RefSeq.
SOURCE      Thiorhodococcus drewsii
  ORGANISM  Thiorhodococcus drewsii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiorhodococcus.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Thiorhodococcus drewsii"
                     /db_xref="taxon:210408"
     Protein         1..144
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14891
     Region          10..142
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mhatrsqlig ftlielmitv aivgilaaia ypsyqdsvrk swranaaacl selaqgmerr
       61 ftgsssyvgg lppsgcpneg gmgnryafsf tsaatatafs lqavpvasgp qandscgtlt
      121 inqmgqkgvt saangydaat cwrr
//
LOCUS       WP_007040626             273 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Thiorhodococcus
            drewsii].
ACCESSION   WP_007040626
VERSION     WP_007040626.1
KEYWORDS    RefSeq.
SOURCE      Thiorhodococcus drewsii
  ORGANISM  Thiorhodococcus drewsii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiorhodococcus.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Thiorhodococcus drewsii"
                     /db_xref="taxon:210408"
     Protein         1..273
                     /product="formate/nitrite transporter family protein"
                     /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=29586
     Region          24..273
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msrskpsagl sreerhevse rlslrslqvf eivrqegvee lsrpinslfw sgiaaglsls
       61 lsvycmaflh qalegsrlqp alvgfgysvg fvivilgrlq lftentitvv lpvlsdisrf
      121 kiqrtlrlwa vvfianmigt lvsarvaisg gmlppeqlea allvsqhllq ysalqillyg
      181 ipagfmvasi vwlipnakgg efwiivlity misvgglthv vagstewfll amdgdctwvh
      241 avfsgilpal ignviggtgl falityaqvk dei
//
LOCUS       WP_007041481             208 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Thiorhodococcus drewsii].
ACCESSION   WP_007041481
VERSION     WP_007041481.1
KEYWORDS    RefSeq.
SOURCE      Thiorhodococcus drewsii
  ORGANISM  Thiorhodococcus drewsii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiorhodococcus.
REFERENCE   1  (residues 1 to 208)
  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 208)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 208)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Thiorhodococcus drewsii"
                     /db_xref="taxon:210408"
     Protein         1..208
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22089
     Region          3..204
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Region          123..153
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
ORIGIN      
        1 msyetdeekv eaiktwwken glsviagavi glgviygwry wvgyqadqaa masnafevll
       61 netragtaet vakqaqtlrd dygstpyaal gslvsaktly edgktdeaia alesviadap
      121 dpaiariaal rlariqvaen kldaaekiid kyddspafag dfaavrgdla largdtakar
      181 aayeeaidkg tglsqlvrlk ldnlpsas
//
LOCUS       WP_007046637             403 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Subdoligranulum variabile].
ACCESSION   WP_007046637
VERSION     WP_007046637.1
KEYWORDS    RefSeq.
SOURCE      Subdoligranulum variabile
  ORGANISM  Subdoligranulum variabile
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Subdoligranulum.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Subdoligranulum variabile"
                     /db_xref="taxon:214851"
     Protein         1..403
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44107
     Region          1..401
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkilvincgs sslkyqlidm egekvlckgl cerigmessm itheanghka ttpaifptht
       61 eafgevvkkm ttgegkvied vseidaighr vvhggekfkk sclitpdvvk airdlsplap
      121 lhnpaailgi easykvfgqd kpnvavfdta fhstmppkay myaipyeyye kygvrrygfh
      181 gtshkyvshr aaeyleepie rlklitchlg ngssiaavdq gkvvdtsmgm tplaglmmgt
      241 rcgdldpsvv nylkytleit ghqldeilnk ksgllgvsgv ssdmrdvesa akdgneraqm
      301 aldmlnyqik ktigsyiaam ggvdaivftg gigehddesr akichhmdwl giridtdknr
      361 gvrsqhkdvv eitawgarvr tlvvetneel miardtkevl sae
//
LOCUS       WP_007047519             244 aa            linear   BCT 20-JAN-2025
DEFINITION  3-deoxy-manno-octulosonate cytidylyltransferase [Subdoligranulum
            variabile].
ACCESSION   WP_007047519
VERSION     WP_007047519.1
KEYWORDS    RefSeq.
SOURCE      Subdoligranulum variabile
  ORGANISM  Subdoligranulum variabile
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Subdoligranulum.
REFERENCE   1  (residues 1 to 244)
  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 244)
  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 10118537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Subdoligranulum variabile"
                     /db_xref="taxon:214851"
     Protein         1..244
                     /product="3-deoxy-manno-octulosonate cytidylyltransferase"
                     /EC_number="2.7.7.38"
                     /GO_function="GO:0008690 - 3-deoxy-manno-octulosonate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0033468 -
                     CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27429
     Region          2..237
                     /region_name="CMP-KDO-Synthetase"
                     /note="CMP-KDO synthetase catalyzes the activation of KDO
                     which is an essential component of the lipopolysaccharide;
                     cd02517"
                     /db_xref="CDD:133010"
     Site            order(8..10,49,76,96,98)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133010"
     Site            order(121,138,144..146,152..153,155..161,169,194..195,
                     198..200,207..210)
                     /site_type="active"
                     /note="oligomer interface [active]"
                     /db_xref="CDD:133010"
ORIGIN      
        1 mktiavipar yastrmpgkp ladvlgkpmi wwvyqaakac pklddvliat dderiadack
       61 qyemqylmts pdhdtptgri wevstkvead lylqlmgdep lvnpaafdli lpdtlpedpy
      121 yvavltnime hpadvidfsn qkvvtnaare illisrspip ypkgtldfey ekvtgiqlys
      181 kqalafyhet pksilekaee ndmmrfieng hkvhaivspy ktvsvdtpkd lalvneilke
      241 khha
//
LOCUS       WP_007048258             189 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Subdoligranulum
            variabile].
ACCESSION   WP_007048258
VERSION     WP_007048258.1
KEYWORDS    RefSeq.
SOURCE      Subdoligranulum variabile
  ORGANISM  Subdoligranulum variabile
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Subdoligranulum.
REFERENCE   1  (residues 1 to 189)
  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 189)
  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   3  (residues 1 to 189)
  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   4  (residues 1 to 189)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 189)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 189)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Subdoligranulum variabile"
                     /db_xref="taxon:214851"
     Protein         1..189
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=20684
     Region          1..189
                     /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"
ORIGIN      
        1 makalivsag tnaneylarh iaelgytrpv ivpsggearr qmdgkdfevi vintplpdef
       61 ghelgtdavq ktdagvilla ksgtaeqisa klqdfgvlvl skpfsgpqfr qavqiaasny
      121 krlallraen qklldkiaql rlvdrakcfl iekrgmtete ahrlieknam dtrrsrgeva
      181 qeilesaee
//
LOCUS       WP_007048410             129 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Subdoligranulum
            variabile].
ACCESSION   WP_007048410
VERSION     WP_007048410.1
KEYWORDS    RefSeq.
SOURCE      Subdoligranulum variabile
  ORGANISM  Subdoligranulum variabile
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Subdoligranulum.
REFERENCE   1  (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   2  (residues 1 to 129)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 129)
  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 129)
  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 129)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Subdoligranulum variabile"
                     /db_xref="taxon:214851"
     Protein         1..129
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15137
     Region          38..123
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(57,76..77,95,98,106..107,115,120)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 msnaialqet fvteskprty pllrrasrkl tefrfkdlfi dlrahrvfrq eeevaltpre
       61 yalletlvrn rnialtrsql ltdawgydyi gesrtvdvhi nrvrrklgle qeiqtvfkvg
      121 yrlntrgll
//
LOCUS       WP_007048751             881 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Subdoligranulum
            variabile].
ACCESSION   WP_007048751
VERSION     WP_007048751.1
KEYWORDS    RefSeq.
SOURCE      Subdoligranulum variabile
  ORGANISM  Subdoligranulum variabile
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Subdoligranulum.
REFERENCE   1  (residues 1 to 881)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 881)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..881
                     /organism="Subdoligranulum variabile"
                     /db_xref="taxon:214851"
     Protein         1..881
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=101257
     Region          317..879
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mttqkylcpp rlqkkfllww wtvpelilia tlvvatfylt slellaltlf vaigaarvdf
       61 ehnlfgalrt rtlyqlftkt ftanekhaan keekrkrkrl vkqmrsrlpi qdliqfrftd
      121 ggiyggrdgk elfrfyryyp pntdvmtdee iaqeieqlcr lfdslrcpft mfgtdkiedm
      181 salkeyyrsl prrydhilad vvneiestet kssavqrayy fiykaqseed diytlivgkg
      241 ykidrvknde mavllrnylv refinvdiyt iaeevknypn makakpaiyn keiqrrlcpn
      301 ridftrdhae qsglmrrtlm iknfpaqipp ralytvasmr gtsftmrmtp lqkdnarkli
      361 deqirnkavi ggksqateqm daaqetmdik nfyaevtrnq ntiysvnvyi eiygktledl
      421 anleqqvkie lagvgitydq lnyeqrngfs svqplgsdhf ilcsnnlpsk tvaalypfsy
      481 sslihphgmp lgrtdrggpv yadifqrddq itngvffisg sagqgksylq kkiltfmvtr
      541 gvhcyvmdpe neysdvtrgl ggvvidcasg nhkinifevr rikleddvee gaelpeisne
      601 spmflqhlsw lkdefrimmp empdstlral milvqgmyas vgidqhtdfd rlqhqdyptf
      661 stlydfvqkq lgknsypmlt kemisevlly indptygels nifngtttid vknnplicfs
      721 mgallegseq rlqavennln tyiwsivllr efqvllsfde lymyleqplm akyisyfarr
      781 srkynacigv atqqlqdcld esvrrysspi inmssfkflf ysgqvdlqdm kealkltdge
      841 aacisvsnkr hcllkagngk yymevgtlpf eaelfgdkgg i
//
LOCUS       WP_007049302             102 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Anaerofustis stercorihominis].
ACCESSION   WP_007049302
VERSION     WP_007049302.1
KEYWORDS    RefSeq.
SOURCE      Anaerofustis stercorihominis
  ORGANISM  Anaerofustis stercorihominis
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Eubacteriaceae; Anaerofustis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Anaerofustis stercorihominis"
                     /db_xref="taxon:214853"
     Protein         1..102
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11469
     Region          13..100
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(28,59..60,62,83)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(28..29,37,40,42..43,45,48..49,51,59,64)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mgkvldddli flvlsiveei pegkvatygq iagladrpnn arlvgkilgm seyygeypch
       61 rvvnhngrla pnfhtqkekl esegikfknd ehvdlkkhkw ii
//
LOCUS       WP_007050595             189 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Anaerofustis
            stercorihominis].
ACCESSION   WP_007050595
VERSION     WP_007050595.1
KEYWORDS    RefSeq.
SOURCE      Anaerofustis stercorihominis
  ORGANISM  Anaerofustis stercorihominis
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Eubacteriaceae; Anaerofustis.
REFERENCE   1  (residues 1 to 189)
  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 189)
  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   3  (residues 1 to 189)
  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   4  (residues 1 to 189)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 189)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 189)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Anaerofustis stercorihominis"
                     /db_xref="taxon:214853"
     Protein         1..189
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21568
     Region          3..183
                     /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"
ORIGIN      
        1 mdkilivsan ekskdtlcel lkeyddiqiv tttsaskarr yasnnelsia iintplreef
       61 gtelsmdlsr lnigtllivk sevseeisad vesfgvlvis kpiikslfyq sfrlqmsvkn
      121 rlislkkend klknkieeik ivdraklvli enenlsenea hkyiekeamn rrlsryqiak
      181 eilvkynis
//
LOCUS       WP_007051368             247 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Bifidobacterium longum].
ACCESSION   WP_007051368
VERSION     WP_007051368.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium longum
  ORGANISM  Bifidobacterium longum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Bifidobacterium longum"
                     /db_xref="taxon:216816"
     Protein         1..247
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=26487
     Region          95..234
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 marrnahfrr rfnasgpler vlilivlava igvtiglllp qvssdvakit ggytatgsaa
       61 dtlnalavdd nqsssgydrd sfgfrtadvd gngcdvrddv lardltdity kyagscvves
      121 gtladpytaq tihfvrgrat sakvqidhvv alenawqsga rdwstakrhe fgndpynlla
      181 vdgpanqekg sasaaywlpt nadyrcdyva rqigvkdkyq ltvtsqekda mlavlhtcpg
      241 qavpade
//
LOCUS       WP_007051509             284 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Bifidobacterium].
ACCESSION   WP_007051509
VERSION     WP_007051509.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..284
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=30382
     Region          3..139
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mvnstwigsp nhyagrngye vthitlhimv grlagtdatf qnpvrqasst ygigstglih
       61 qyvretdapw tdsnyasncq tisieheggm agvpctkacm dasaalcadi arrygwprlw
      121 hdglkgnvwl hreipgsdha gcpdraangl dvdyvinkan qlltgagtvs aqdlyetkgn
      181 dgrnlfdgii qtrnelkdra adaliqtkgn dgrnvldsvi qarydiadlk tqltaqtaai
      241 ealskalgan padiskivad avrakldsle isvtatdktt ekeg
//
LOCUS       WP_007051792             209 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LytR C-terminal domain-containing protein
            [Bifidobacterium].
ACCESSION   WP_007051792
VERSION     WP_007051792.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 209)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..209
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=22416
     Region          82..166
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mtyqvderea rkayvrrrqt ivfsisgavl avvlviallf nfhvfglgev etpasqpnyg
       61 naapcavkds sgkaqyvsna svgirvmngt shgqfakavg ealanrgfsv qkidnysstd
      121 verttiyfgk nainqaytli gnftdatmim taredqlidv vigatfndlq dtnsspqsgk
      181 titniegcka adsmtklpad tkhdaytaq
//
LOCUS       WP_007051932             461 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Bifidobacterium
            longum].
ACCESSION   WP_007051932
VERSION     WP_007051932.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium longum
  ORGANISM  Bifidobacterium longum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 461)
  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 461)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Bifidobacterium longum"
                     /db_xref="taxon:216816"
     Protein         1..461
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=51030
     Region          17..67
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mswqctswal reapaptata rlvlialadr cqpdgrsawp tvdtlmaeah tsessvkral
       61 kaleetgcir rgnqklaqwd ehgnyvpdpy rsvvweccmn vtlehvsekp grqaraerae
      121 raerdgdgna eqagkadrfr gvkmtpleng gnkpksrgvk mtplnperea rgvtsdtpiv
      181 rtntskqisp lppteasprt gesrdgknqt ahiieaasap deanrpmgep dderwqdagp
      241 epeervpagi rarwildrle nrraamgltp kpagrrdtda vtrlverlda agepdtsglm
      301 ervldhaldn gfqakrvdtg rrfarlfdel rddltcdqrt lerrrrehad asqpagsdtg
      361 esrpaepesy etrarrmlad rigadadgpt airaladrlr ldpdpdpgqa sryaelalra
      421 grktraeqar lhaersrelh dyrashggsc fagnwqleqa t
//
LOCUS       WP_007052028             409 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Bifidobacterium].
ACCESSION   WP_007052028
VERSION     WP_007052028.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..409
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44055
     Region          3..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 maktvlvins gsssikyqlv dlesgeglas glvekigepv dghykheyng ekheleepih
       61 dheqglkrvl gffeeygpnl seagivavgh rvvqggsifp kpalvtnkti nqvkdlavla
      121 plhngpeakg aevmrsllpd vpqifvfdss fffqlpkaas tyalnkeiad qyhirrygah
      181 gtsheyissv vpdvvgkpae glkqivlhig ngasasaevs gkpvetsmgl tpleglmmgg
      241 rtgdidpavv fhlirnahmn vdeldalfnk rsgmmgmtgy gdlrevhrlv segnedakla
      301 ldvyvhrivs yignytyqmg gcdvitftag vgenddvvrk mvcdklapfg vkldeeknat
      361 rskepriist pdssviiavi ptneelaiar ksaaiaeagt dtygntfak
//
LOCUS       WP_007052144             531 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Bifidobacterium].
ACCESSION   WP_007052144
VERSION     WP_007052144.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 531)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..531
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=56810
     Region          393..530
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(480..481,484,503..506,508)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mtehlddstq qfaplfgann avsgtvadsv daaasdsiqg demrrrriwp wvviacllva
       61 lgaacgggvw ffqdhvlpgt tlwgnsvtgk teqeivdlin dqvdntavra kyqgqsatft
      121 lkdlgievdg eaiasdvina qrgdawwqqy afwithdvap qinpeladgs vvdkalnida
      181 qepvdaqval ndnnsgfnvi agengqgana tsiakqaist veslgsvqpq tvrveldvte
      241 ptitnaiade akttletlvn navaikvadk diatvnasml gsamridanq qsklkdnevr
      301 ngyvvfdadk lqqyydeqik pnlkleredk kvvvnnagev lsteteghdg iviadgadte
      361 vgarlaqvla tgtgsvnvdg kvdpkqevkv thrvaidlsd rklyayendt vvktlnvvva
      421 egndnvtgec vgmmctptgd fnvwqklpsq dmsgtlnlad gtvetwdvkd vgfvnyfssg
      481 caihriaggy vadavmpsia ngshgcvgig wdvaewfynw cnmgtsvhiq v
//
LOCUS       WP_007052353             318 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CHAP domain-containing protein [Bifidobacterium].
ACCESSION   WP_007052353
VERSION     WP_007052353.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..318
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32862
     Region          185..318
                     /region_name="COG3942"
                     /note="Surface antigen [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443142"
ORIGIN      
        1 mkhashkatt vsrqkfslak alfasgkgsh svravravqs agsdavvlgl dpaiaekine
       61 iapqtrrsir eaaraaerrs hilasaslaa lvgtaagala fsnnedatns fvadpatttt
      121 qikrisdvta asrseartdl ssssvtaqst neggwglsns dstldaklmn rnnannpvvs
      181 alvdadgdav pagfnpnhav gtnsnnypwg qctwyayqrr aelglpssgn fgnggawaas
      241 asalgywvdn tprhvgdavv fapgqadadg ayghvavlek inadgsieis esnakglgvi
      301 strtfsaaea gkfqyvhy
//
LOCUS       WP_007052490              95 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein
            [Bifidobacterium].
ACCESSION   WP_007052490
VERSION     WP_007052490.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..95
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10450
     Region          4..91
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mvpiehvydq irafaadaga rkvvlfgsra kgvnrpksdi dlavagcpdf nrleqnlqdn
       61 lwsllkvdvi nldepisssl raeiersgkv lyekv
//
LOCUS       WP_007052684             259 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Bifidobacterium].
ACCESSION   WP_007052684
VERSION     WP_007052684.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 259)
  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   2  (residues 1 to 259)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..259
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=27327
     Region          188..257
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mgvshnhrad haanrlrafs rqsaampqpr verpttpppp pgharirpag hppqraqsgl
       61 rqatrdkral sdligvrsad avgesarltr dqprlsftig halavillli valgislall
      121 vqqsmnmaml sqptamqttg gsagdqtmps qnttdekrtd pqqsehsdat anpesdttqs
      181 phmqtdgsda gasthglinl ntataeelqs ikgigpvtaq riidhrtaig gytsvdqlld
      241 vkgigsktle tmrgqvtvg
//
LOCUS       WP_007053800             397 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Bifidobacterium longum].
ACCESSION   WP_007053800
VERSION     WP_007053800.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium longum
  ORGANISM  Bifidobacterium longum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 397)
  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 397)
  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
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 397)
  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   5  (residues 1 to 397)
  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   6  (residues 1 to 397)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 397)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 397)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Bifidobacterium longum"
                     /db_xref="taxon:216816"
     Protein         1..397
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43784
     Region          20..70
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          76..363
                     /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 mrampstavk ahnrsamtqy lyghshvtkq elerelglsl ptitqnlral eddglirkgk
       61 lqdstggrka qnyefnpdhr taigvvmrsn elrlcainly gnviekrnda lpyrntnvyy
      121 qriggiinnf aadvekkhgk vlgvsfaiqg ilspdattii fgtimgntgl tletisqsvh
      181 ypcmmihdsd asamaelwfd stltdavcvy lerrpggavi aggklyqgpn qcngaiehmt
      241 lvpggrecyc gqrgcmdtyc spetlpedye sipgffsvle qgerhhrerm dewldyvaqa
      301 ivnarfiiag dvivggeaaq hledsdiedl ktrviarspf gtdhfnlrks ycaedqniig
      361 aalrfaenyl dgicgaaerg rksrastksd ntstmev
//
LOCUS       WP_007054041             297 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Bifidobacterium].
ACCESSION   WP_007054041
VERSION     WP_007054041.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..297
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32207
     Region          19..271
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 megmtgyvmp leppavgwdi hchtafsdgt etpatlaeqs kalglkgvai sdhdttagwp
       61 eaeaaahrvg lpllrgteit atdenvsvhm lgyqydptnq hitdlfantr aarlqrtqrm
      121 vellsrdypi twqsvlaqvk egskttigrp hiadalvsag vyrtrseafa davsasskyy
      181 iptpsptshe vvaavkgagg viliahagdv srnrrllsdd qiealisegl dglevwhrgn
      241 speqrerllt icrrhqllvt ggsdwhgkgk pnklgenltd eatveeivhr gvlplyr
//
LOCUS       WP_007049429             322 aa            linear   BCT 20-JAN-2025
DEFINITION  gluconeogenesis factor YvcK family protein [Anaerofustis
            stercorihominis].
ACCESSION   WP_007049429
VERSION     WP_007049429.1
KEYWORDS    RefSeq.
SOURCE      Anaerofustis stercorihominis
  ORGANISM  Anaerofustis stercorihominis
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Eubacteriaceae; Anaerofustis.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Gorke,B., Foulquier,E. and Galinier,A.
  TITLE     YvcK of Bacillus subtilis is required for a normal cell shape and
            for growth on Krebs cycle intermediates and substrates of the
            pentose phosphate pathway
  JOURNAL   Microbiology (Reading) 151 (Pt 11), 3777-3791 (2005)
   PUBMED   16272399
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Anaerofustis stercorihominis"
                     /db_xref="taxon:214853"
     Protein         1..322
                     /product="gluconeogenesis factor YvcK family protein"
                     /GO_function="GO:0043743 - LPPG:FO 2-phospho-L-lactate
                     transferase activity [Evidence IEA]"
                     /calculated_mol_wt=35644
     Region          8..319
                     /region_name="YvcK_like"
                     /note="family of mostly uncharacterized proteins similar
                     to B.subtilis YvcK; cd07187"
                     /db_xref="CDD:132873"
     Site            order(13..15,192..193,197,227..228)
                     /site_type="other"
                     /note="phosphate binding site [ion binding]"
                     /db_xref="CDD:132873"
     Site            order(39,43,57,60,93)
                     /site_type="other"
                     /note="putative substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:132873"
     Site            order(86,91,94..95,98..99,101..102,112,115..116)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:132873"
ORIGIN      
        1 mkfkdknivi igggtgnsvl lkefkkhtdn itaivtvsdd ggstgklrkd lgilavgdir
       61 ncitalaede stmtelmeyr ftkgalkkhs fgnlflaaln eisesfpkai kdisdvlaik
      121 gevvavsknd ditlcalldn tavvngeski pkqavkmrsk ikkvfmtpsd akvndyavek
      181 ienadiiils pgslytsiip nllikdipya idknkkakky fvanimtqhg etdgfdvwkh
      241 vteidkhipr gckifdeviy sttvldedvi krykkkhadv veanitdemk slykftgldl
      301 areingvmrh nsevlvdylk nt
//
LOCUS       WP_007054421             404 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Bifidobacterium longum].
ACCESSION   WP_007054421
VERSION     WP_007054421.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium longum
  ORGANISM  Bifidobacterium longum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 404)
  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 404)
  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
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 404)
  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   5  (residues 1 to 404)
  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   6  (residues 1 to 404)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 404)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 404)
  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 11513089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Bifidobacterium longum"
                     /db_xref="taxon:216816"
     Protein         1..404
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42842
     Region          14..>66
                     /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"
     Region          81..364
                     /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 matntthats qasvsesnrs rivkhlyhng issraqiaka leltpaaitk itarlieagm
       61 ieetgdlegs knrrsiglkl ntthfriigi kfarslvqig vfdlcgntls fenlptvcdn
      121 tindsivtih qrveqlldnd psivaigmav pgpylrnvgr tavvsnmqgw rkinfidefa
      181 tafrvpvfie qdaragalah ylfdpsvhad dnlayylvge gvglgvidng rlingflgaa
      241 teighisidv ngrpcdcgnv gclerycstp aihdtliadg tvvpgaadmt haeaaralfa
      301 kagdgdeaai aivrevaryv gygcvtifng ynpehiiigd ivseagpill devratvaer
      361 aipeinasts islstlsada avsgaaavav tqflehpsvf fdvs
//
LOCUS       WP_007054423             374 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator
            [Bifidobacterium].
ACCESSION   WP_007054423
VERSION     WP_007054423.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 374)
  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 374)
  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
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 374)
  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   5  (residues 1 to 374)
  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   6  (residues 1 to 374)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 374)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 374)
  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 20283677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..374
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39949
     Region          <41..70
                     /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(41..43,52)
                     /site_type="other"
                     /note="non-specific DNA interactions [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            52..58
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            order(53..54,58)
                     /site_type="other"
                     /note="sequence specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238044"
     Site            53..54
                     /site_type="other"
                     /note="putative cAMP binding site [chemical binding]"
                     /db_xref="CDD:238044"
     Region          96..370
                     /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 msylglnttt ddhaakaspa dvrrknrqli frllfptnqy sraelgrrtg lsrvavsdvv
       61 grmleegllr etgqapsggk gkrgtllsid idrlriisid ltqehllhga vtnllgqplr
      121 haevtlntgs fvsvdviiel iekmlgmsdg evigigvasp gvvdngvvrs stmrgwnnld
      181 lstpiaehfg levnvsndat aamlterffg qggpnmlfvr iergigsail lsdtpvigel
      241 haagelghis idldgplcpc gkhgcletmi sgtalkkqls aadveqhqgi laragrylgq
      301 alsmpvglld madvcvygqp niinetfida aqqyldaats ssfhkhtvir rcecgpditv
      361 qgeaiavvfq hlak
//
LOCUS       WP_007054616             402 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Bifidobacterium longum].
ACCESSION   WP_007054616
VERSION     WP_007054616.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium longum
  ORGANISM  Bifidobacterium longum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 402)
  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 402)
  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
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 402)
  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   5  (residues 1 to 402)
  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   6  (residues 1 to 402)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 402)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 402)
  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 20650276
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Bifidobacterium longum"
                     /db_xref="taxon:216816"
     Protein         1..402
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42347
     Region          18..66
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          101..397
                     /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 msdanaipqw fsgsehthrv aaaiaqygpi arttlaqmlg lsqgalsrit sdliyagvie
       61 elpaeagpsg klperftpre ssdrrgrpqt slvlcsnart figvkvhgms ivaaavnahg
      121 evvsgrhevp igadqsaeyv vsaitrlvre csadiassgl psptavgvav gghvvddsiv
      181 tfapflhwdg atdlgtmvte atglpcgvfn didsllvdas wfgpgvgvdm favvtigvgv
      241 gyslavngkp vqypdksygl vghvlidpeg prctsghigc sqcltddsia eqysaivgra
      301 vsfedfarda kervpqatql vnrtcfrlgs lvatvaniam pghvmiages aflaklgtds
      361 lrdgirfyrh sqtqpvkfti mnhdwqlwak aaasrvivkh ig
//
LOCUS       WP_007054849             247 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease family protein [Bifidobacterium].
ACCESSION   WP_007054849
VERSION     WP_007054849.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..247
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=26498
     Region          95..234
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 marrnahfrr rfnasgpler vlilivlava igvtiglllp qvssdvakit ggytatgsaa
       61 dtlnalavdd nqsssgydrd sfgfrttdvd gngcdvrddv lardltdity kyagscvves
      121 gtladpytaq tihfvrgrat sakvqidhvv alenawqsga hdwstakrhe fgndpynlla
      181 vdgpanqekg sasaaywlpt nadyrcdyva rqigvkdkyq ltvtsqekda mlavlhtcpg
      241 qavpade
//
LOCUS       WP_007055188             337 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Bifidobacterium].
ACCESSION   WP_007055188
VERSION     WP_007055188.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..337
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38792
     Region          166..333
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mkalmkrllp esalawlrgc esdmklrret lhqmkrfrrn yarrgstrks hletrivfft
       61 hqiekglsht dfrygfgkkv laqmaplmet lrttdpdiah nevyrtalsa lheyrvrhea
      121 kqfdltyakd lfsqriwnei estndrsggd liirstdkrd naelsfsqlm eqrhsvrefa
      181 etpvtveeim navrvamrtp svcnrqptrv hiitdaelik kamplqggfr gypmppalvl
      241 itgdnqtmmn qdernecytd gglfgmslll aleeqqiaac plntmlpmkr deatrellhi
      301 pdseflvmyi avghfrdevk tcksqrfsad eivtvha
//
LOCUS       WP_007055313             389 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator
            [Bifidobacterium].
ACCESSION   WP_007055313
VERSION     WP_007055313.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 389)
  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 389)
  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
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 389)
  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   5  (residues 1 to 389)
  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   6  (residues 1 to 389)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 389)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 389)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..389
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40851
     Region          <28..80
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          88..380
                     /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 matrlfgsqt slreanranl lasihkfgam tqvelaevtg lstatvstlv hqlvdedqle
       61 tkntvrngrr atlvtlarhq glgvglwiar rhltlsivdf sksiiaehtl plplghkadt
      121 tleramllin etlssidaea selvgigvav aapvatsdht iaipgilpgw dgvditaplr
      181 tafnvpvyvd ndanfaayge srmgvaagkr nfvyisandg vgagivinge imhgvtglag
      241 eighiqvdpl gaicscgnrg cldtvvaenr lvqllsvthg nmtlddlvsf anegdpgcrr
      301 iiadtavrig qvaadlcisv dpevivlggk lamtgdvfiq pfnealqrml fpdavapidv
      361 lvsshpndnc alggalcaie fsvrndvsq
//
LOCUS       WP_007056447             574 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Bifidobacterium longum].
ACCESSION   WP_007056447
VERSION     WP_007056447.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium longum
  ORGANISM  Bifidobacterium longum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 574)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Bifidobacterium longum"
                     /db_xref="taxon:216816"
     Protein         1..574
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=60612
     Region          <2..>120
                     /region_name="PknB_PASTA_kin"
                     /note="Stk1 family PASTA domain-containing Ser/Thr kinase;
                     NF033483"
                     /db_xref="CDD:468045"
     Region          424..547
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(496..497,500,521..524,526)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mandtfsfss pddqetavlq pvatdglfaa adsgtatpqq sdngtnnhad ntayvgehvm
       61 asttakshgk aariaiitif avllaaliay ffvgrwyfqd kaapgvhlgn vsvmgqtree
      121 lantvkqqln nttvtftaeg nsvkaslkdl gvtvdtdktv dallnaktgd vaklnifdqp
      181 hialtattdk etaeqfvtag lvdeadraqi atvvynkstk qfdytagqdg kgpdtnvvna
      241 avkeavatpg enatvpvklq taknpiddas aqqtqfdana rlglkltvdn gvnksvtipa
      301 dtiasflkpt vnkaegtmsl vvdrdaitky vtsdsvtkel tvpkvtrevy itpkdeggve
      361 igadktlgvd gievtgagda perlataieq nqstdstvav kdspydvkqv evphnfdtan
      421 gdkwvhvdlt nqtatayqgt tvvkkfnias gkptadgsml sdtgtfyvyl kyesqtmvge
      481 gynqpgtpwv syynggealh gvpaymwgeh piyvqqgipg shgcinmqva dakwmydfat
      541 igtrvvvdgt tptsgqalrp agadatgwqg gnas
//
LOCUS       WP_007057052             469 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Bifidobacterium
            longum].
ACCESSION   WP_007057052
VERSION     WP_007057052.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium longum
  ORGANISM  Bifidobacterium longum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 469)
  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 469)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Bifidobacterium longum"
                     /db_xref="taxon:216816"
     Protein         1..469
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=51985
     Region          17..67
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mswqctswal reapaptata rlvlialadr cqpdgrsawp tvdtlmleah tsessvkral
       61 kaleetgcir rgnqklaqwd ehgnyvpdpy rsvvweccmn vtlehvsekp grqaraerae
      121 raerdgdgna eqagkadrfr gvkmtpleng gnkpksrgvk mtplnperea rgvtgdtsrg
      181 vtsdtpivrt ntskqisplp pteasprtge srdgknqtah iieaasapde anrpmgepdd
      241 erwqdagpep eervpagira rwildrlenr raamgltpkp agrrdtdavt rlverldaag
      301 epdtsglmer vldhaldngf qakrvdtgrr farlfdelrd dltcdqrtle rrrrehadas
      361 qptgsdtges rpaepesyet rarrmladri gadidastai raladrlrld pdpdpgqaar
      421 yaelalragr ktraeqarre sersrelhdy rashggscfa gnwqleqae
//
LOCUS       WP_007058071             121 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein, partial
            [Bifidobacterium longum].
ACCESSION   WP_007058071
VERSION     WP_007058071.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium longum
  ORGANISM  Bifidobacterium longum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (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   2  (residues 1 to 121)
  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 121)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Bifidobacterium longum"
                     /db_xref="taxon:216816"
     Protein         1..>121
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          17..67
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mswqctswal reapaptata rlvlialadr cqpdgrsawp tvdtlmleah tsessvkral
       61 kaleetgcir rgnqklaqwd ehgnyvpdpy rsvvweccmn vtlehvsekp grqaraerae
      121 r
//
LOCUS       WP_007059756             187 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Clostridium carboxidivorans].
ACCESSION   WP_007059756
VERSION     WP_007059756.1
KEYWORDS    RefSeq.
SOURCE      Clostridium carboxidivorans
  ORGANISM  Clostridium carboxidivorans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Clostridium carboxidivorans"
                     /db_xref="taxon:217159"
     Protein         1..187
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21542
     Region          3..184
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdtikaieer rsirkfqnki ipketlenll elsskapsgk nrqpwrfvvl qnkkknelvn
       61 imrnvsnlyk nqnksigsfe lstnsineas avvlvfntfs nfeedynhhr lltdtqsiga
      121 siqtlllaaq dfklgalwic difycdkeic swldrkdelm aavaigypdq spyprprkpl
      181 qeitewf
//
LOCUS       WP_007059051             174 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Clostridium carboxidivorans].
ACCESSION   WP_007059051
VERSION     WP_007059051.1
KEYWORDS    RefSeq.
SOURCE      Clostridium carboxidivorans
  ORGANISM  Clostridium carboxidivorans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Clostridium carboxidivorans"
                     /db_xref="taxon:217159"
     Protein         1..174
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19191
     Region          4..167
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mnetmktlln rrsirkykse qikdeelkav leagkyapsg anqqsalfiv vqnkdiikki
       61 skmnaavmek envdpyygap tvilvladks katpvedasi algnmynaay slglgscwih
      121 rtremfesge gkkllkewgv egdyigvgsc ilgypdcelp kpaprkdnfv imvk
//
LOCUS       WP_007060386             466 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Clostridium carboxidivorans].
ACCESSION   WP_007060386
VERSION     WP_007060386.1
KEYWORDS    RefSeq.
SOURCE      Clostridium carboxidivorans
  ORGANISM  Clostridium carboxidivorans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 466)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Clostridium carboxidivorans"
                     /db_xref="taxon:217159"
     Protein         1..466
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=53628
     Region          87..195
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          207..320
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          344..462
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(414,417,435..438,440)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mrninvkkff kskdkaniai lifsiiliyl lisvyftnhf ffntvingad vslksyddan
       61 niirnytrny klqlverngq ieeivgqdig lkynetnnvf kichkkssfk wvislfknqk
      121 yyvndlfiyn qdslenkink lnclnkaiie phnvnfkysn gsykvikevy gnkinkgkmn
      181 eaikmsileg ktkldlnkef cyenpkytln snkvsktkdl lnkyvstkit yifenkneil
      241 dgniinewls vdenletvid ekavdkyvqg lakkydtvgi arkfktsigk ivevegglyg
      301 wkinctaetk vllenirfge tlekepiyiq kslprgedei gktyvevnit rqhlwfykng
      361 rlisegdivt gdpnrgcstv lgtymlnykq ngatlsglny etevsywmpf fgnigihdat
      421 wrysfggdiy krngthgcvn vpldlakaif dnieegtpii cyeeqe
//
LOCUS       WP_007060585             345 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Clostridium carboxidivorans].
ACCESSION   WP_007060585
VERSION     WP_007060585.1
KEYWORDS    RefSeq.
SOURCE      Clostridium carboxidivorans
  ORGANISM  Clostridium carboxidivorans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Clostridium carboxidivorans"
                     /db_xref="taxon:217159"
     Protein         1..345
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=39959
     Region          75..>345
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 manlienkin nlegikekni ettekisgqs ldivkenilk lkeifpevfc edkidferlq
       61 dvlgnyiddk eeryrfewyg ksqairmaqt psrgtlrpfr eesknwdtte nlyiegdnle
      121 vlkllqksyq nkikmiyidp pyntgndfvy kddykdnlqn yfevtgqvdd dgnktstnse
      181 ssgryhtnwl nmmyprlrla rnllkddgvi fisiddnefg nlkkvcddif gednflgniv
      241 ratgqttgqd sgglgssfdy vlaytkisgv dlsglplteh dlkrfdnede rgkyaydqmr
      301 ktgsndrred rpnmyysikd pdgndiypia aagyescwrf rkkni
//
LOCUS       WP_007061692             392 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Clostridium carboxidivorans].
ACCESSION   WP_007061692
VERSION     WP_007061692.1
KEYWORDS    RefSeq.
SOURCE      Clostridium carboxidivorans
  ORGANISM  Clostridium carboxidivorans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 392)
  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 392)
  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
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 392)
  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   5  (residues 1 to 392)
  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   6  (residues 1 to 392)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 392)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Clostridium carboxidivorans"
                     /db_xref="taxon:217159"
     Protein         1..392
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44418
     Region          16..59
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          83..382
                     /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 msrlksvdqe tirvlnqkki lnliyrnntl tkqeisqkln isiptvisns kelieqgfle
       61 eagvaestgg rkptilkflp ysrysfgvcv tkdkvriila nlnfeivhem dfnmpeklkd
      121 fndiickvse nveyiinkfn ipydrilgig fslpgtvdek nlllknvpnl klknisfkef
      181 qtcfkfpifi eneanasaya etfinfndik sslvfisite gigtgivien nvykgfnkra
      241 gefghmtivk dgkkcncgkk gcwelyaskk allseyrnaf ddmngtlddf lkrskndlki
      301 ksildiyidf laegikniil aldpknilig geifsykdfl eeelikkvfk dnsfydetqc
      361 nimfsslgen aavfgaallp mesvfflndn vi
//
LOCUS       WP_007062233             189 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Clostridium
            carboxidivorans].
ACCESSION   WP_007062233
VERSION     WP_007062233.1
KEYWORDS    RefSeq.
SOURCE      Clostridium carboxidivorans
  ORGANISM  Clostridium carboxidivorans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 189)
  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 189)
  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   3  (residues 1 to 189)
  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   4  (residues 1 to 189)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 189)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 189)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Clostridium carboxidivorans"
                     /db_xref="taxon:217159"
     Protein         1..189
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21723
     Region          1..189
                     /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"
ORIGIN      
        1 mnnykivvad sdstcrklis ellkkrgynv yqagdggevl rvsrriyphl vimdinllgi
       61 ngyktakiie edrissvifs annidsafye klktmnifay ivkpinpeql yqtvefsinn
      121 idkvnslqek iqhletelvn rkkidkakgi vmeklrvsen eaykylrkks mdycismdvl
      181 aekiikkyg
//
LOCUS       WP_007064150             695 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Clostridium
            carboxidivorans].
ACCESSION   WP_007064150
VERSION     WP_007064150.1
KEYWORDS    RefSeq.
SOURCE      Clostridium carboxidivorans
  ORGANISM  Clostridium carboxidivorans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 695)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Clostridium carboxidivorans"
                     /db_xref="taxon:217159"
     Protein         1..695
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=78388
     Region          1..691
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mkkiqstcny caldcnldfy vednkivkvi ptkgypvnng fscikgisld kqqtivrest
       61 lprlrqkdgs fkripwdday klvadkflel qekygresva glgtgqlale efalfghvmr
      121 nylkanvdgn trlcmatsvv ahkqsfgfda ppytlkdael sdtiiligan pvlahpilwg
      181 rikenknkkl ividprkset aqnadywygi kgktdlilly avankliekg yidneyvkny
      241 tegfedfkef vkgytlakaa eatgiseasi lelvelihkg krvsfwwtmg vnqgyeavrt
      301 aqaiinlalm tgnigkpgtg ansitgqcna mgsraysntt mlyaggdfdn tdrrkrvaev
      361 lgvnedvlad kptlpynvii ekiisgeika lwivctnprh swtnnetfke aikklelfvv
      421 qdiygdtdss kdcdiylpav pgikkegtyi nterrisamr pvlkkseder sdyeiiygig
      481 kalgmgnlld kwktprdafn lmkecsrnmp cdmtgvsydg lvnsngiqwp fregevltdd
      541 qrrlyednmy ytpskkakfi feevrenplv atkdfpytln tgrgsvgqwh tqtrtrevaf
      601 vedvsvkday iyintklake idikenemik vssvngkhsn fmvkltdnvr ydelyaplhy
      661 lecnnltpsl ydsyskepsy kttpiniski kmggi
//
LOCUS       WP_007065315             737 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Fulvimarina pelagi].
ACCESSION   WP_007065315
VERSION     WP_007065315.1
KEYWORDS    RefSeq.
SOURCE      Fulvimarina pelagi
  ORGANISM  Fulvimarina pelagi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Fulvimarina.
REFERENCE   1  (residues 1 to 737)
  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 737)
  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 737)
  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 737)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Fulvimarina pelagi"
                     /db_xref="taxon:217511"
     Protein         1..737
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=77623
     Region          29..719
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 masdpngttt rsdvpsdtav dretlekydr esafrhslpk pialvvtvlc valaafhlyt
       61 svsgplvdva qrsihlytll gltfilyplt ksgprdrlpi ydwitaaaaf ailvymlvva
      121 drviasggri tmtdaviglv aillvidasr rvtgwgltil cviflaygfy aklafynqln
      181 eaivlatfkq viahlvyite gllgtaigvs asyiilfilf gaflgksglg qlfndlalav
      241 aghskggpak vaviasgflg singsaianv vttgaftipl mkktgykpnf agaveasasv
      301 ggqilppimg aaafimaevl svpytqiila giipallyyl gvlaqvhlra lrnelegipr
      361 sqltpvkqvm aerghllvpm vvllwllfeg yapfyaafws iaatvlvcgt mpvvvftaal
      421 sallilepqi maivsgyqip gfrtsrwllv vmvvvpilvn iarrrigpil etmdftslrd
      481 amedgvrssi pvamacgavg iivgvatltg ialeaadavv elgnaipydt lqllatlflt
      541 mvasivlgmg lpsiptyiit stmaapilln lplfqelags nataifvahm fvfyfgifan
      601 ltppvalaay agagisggdp natgvqamkl alagfivpym fvfshamlmi datvtnilwv
      661 lvtsicgvll lavaaegyfr rplpiwlrlv alagalaliy pglitdliga aaivalilie
      721 gakptskaek aksapag
//
LOCUS       WP_007067908             365 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Fulvimarina pelagi].
ACCESSION   WP_007067908
VERSION     WP_007067908.1
KEYWORDS    RefSeq.
SOURCE      Fulvimarina pelagi
  ORGANISM  Fulvimarina pelagi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Fulvimarina.
REFERENCE   1  (residues 1 to 365)
  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 365)
  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 365)
  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 365)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Fulvimarina pelagi"
                     /db_xref="taxon:217511"
     Protein         1..365
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39946
     Region          1..355
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mdrrkfisga atgalgatal atpaiaqesp klqwritssf pksldtiygg aetvakyvte
       61 atdgqfeiqv faageivpgl qaadavrdgt vemahttsyy yvgqddayal gttvpfglna
      121 rqmnawyyyg ggndlmneff atkglyglps gntgaqmggw yrneintlnd lkglklriag
      181 lagrimerlg avpqqlaggd iypalekgvi dgaefvgpyd deklgfvkva pfyyypgwwe
      241 ggptvhtfvn ldqwnelpdn fkgvltaacq aancdmlasy dyknpaairr lvnegaklrs
      301 fsqdvmqaay daakeiyadi sssneafkki ydsqiefkrd aylyaqlsey tydtfmmiqq
      361 rngai
//
LOCUS       WP_007067991             392 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Fulvimarina pelagi].
ACCESSION   WP_007067991
VERSION     WP_007067991.1
KEYWORDS    RefSeq.
SOURCE      Fulvimarina pelagi
  ORGANISM  Fulvimarina pelagi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Fulvimarina.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Fulvimarina pelagi"
                     /db_xref="taxon:217511"
     Protein         1..392
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=42534
     Region          <2..392
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mpintnrkfq gyrrengrvg vrnhvvilpv ddisnaccea vannikgtla lphaygrlqf
       61 gadldlhfrt migtganpnv aacivvgiep gwtqkiadgi aetgkpvaaf sieqngdlkt
      121 imdvsrkake fvqwatelqr secdvselwv stkcgesdtt tglgscptvg nmydklipeg
      181 iygvfgetse itgaehickt ravdeevger wykmwkayqd dvifahatnd lsesqptkgn
      241 iegglstiee kalgnlekig reckyidild paeapqkgng lyfmdtssaa aecvtlmaaa
      301 gyvihtfptg qgnvignpiv pvikitanpr tvrtmsehvd vdvsgilrrd mtidqagdsl
      361 ienimrtang rmtaaealgh refvmtklyr sa
//
LOCUS       WP_007068009             196 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Fulvimarina pelagi].
ACCESSION   WP_007068009
VERSION     WP_007068009.1
KEYWORDS    RefSeq.
SOURCE      Fulvimarina pelagi
  ORGANISM  Fulvimarina pelagi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Fulvimarina.
REFERENCE   1  (residues 1 to 196)
  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 196)
  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   3  (residues 1 to 196)
  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   4  (residues 1 to 196)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 196)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Fulvimarina pelagi"
                     /db_xref="taxon:217511"
     Protein         1..196
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21801
     Region          4..195
                     /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"
ORIGIN      
        1 mdaelsilvf dentvraaii eaglreaght kvatvtelvg lvrrietlqp dvivvdlenp
       61 nrdqlehffq vsrsvkkpia mfvdrsdssa ireaveagvs ayvvdglrke rvkpildmav
      121 srfnavhrln celeqarsql aerklidkak gilmrrrgls epeayrllqr samnenrria
      181 dvarslisas sllgdl
//
LOCUS       WP_007068571             214 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Fulvimarina pelagi].
ACCESSION   WP_007068571
VERSION     WP_007068571.1
KEYWORDS    RefSeq.
SOURCE      Fulvimarina pelagi
  ORGANISM  Fulvimarina pelagi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Fulvimarina.
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   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   3  (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   4  (residues 1 to 214)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 214)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Fulvimarina pelagi"
                     /db_xref="taxon:217511"
     Protein         1..214
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=23571
     Region          10..197
                     /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"
ORIGIN      
        1 msgdlidglr dlnvlvvqph dgsteellkq igrigcnata vwpfpqsipd gtdmifmeit
       61 hpldanavrl lgvesvdapt vvgiiayenp svlkgiidlk idtvlakpir pfgvlshmlm
      121 arsvclarrr deeelqklrr kiqaiqkiad akfilmrhhs ineteaykii rsqamakrts
      181 tleiaqsvin aesilsgmap hdltarmqsq tded
//
LOCUS       WP_007070846             191 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Dialister invisus].
ACCESSION   WP_007070846
VERSION     WP_007070846.1
KEYWORDS    RefSeq.
SOURCE      Dialister invisus
  ORGANISM  Dialister invisus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Dialister invisus"
                     /db_xref="taxon:218538"
     Protein         1..191
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21632
     Region          11..155
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdfhtlcigc rtyrrfkqkq ipeeildell enariansam ngqplryvlv ktpeavrkiq
       61 scfhfaaalp kelgqpkege qptafiilct egretpwtgi digiavrtmn lnayiygvgs
      121 ciignaefek vkeilsvpet wdpklalalg ypshksslve lpedgsikyy ldeerqyyvp
      181 krkrkdisii r
//
LOCUS       WP_007070726             659 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Dialister invisus].
ACCESSION   WP_007070726
VERSION     WP_007070726.1
KEYWORDS    RefSeq.
SOURCE      Dialister invisus
  ORGANISM  Dialister invisus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 659)
  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 659)
  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 659)
  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 659)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Dialister invisus"
                     /db_xref="taxon:218538"
     Protein         1..659
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=70062
     Region          21..659
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mdehqsgvkl eealeakkel dakaqkilee keadsrmrty tgplgravav llcvwtafql
       61 yfttigaisa vnlraihcif llvftfllfp tfkketrkrk lpplwdvafi lcsagsllyl
      121 ilnytriart ggrisdmeaa ialvavvcvf eaarrasgnl avlagiflay nwfgaylpgy
      181 lghngftlkr vlitqfwgtq gilgtgigvs atyiflfvvf gaflkysgfs kfindfsltl
      241 vgttsggpak vaviasglmg mingsaianv attgtitipl mkrtgyksef agaveavast
      301 ggqftppimg avgfvmaefl nlsytyvala avtpallyyi glllavhfea krlglsgiar
      361 enipdalsvi keqghlvlpl vsliglmftg ftplyaavis ifitvaaswl rketrmtgdk
      421 iiaaviegar savsvgvccv iigviigtvt ltsmglnmgy lilsllqdnh vylagflvmi
      481 msailgmgvp gvaayvivqa vavpvlikag vlpliahmfc liyaclsnit ppvamsayva
      541 sgiagsdqtk tglmavrlgl igfiipfffl dnpvlligvd paatavetlw avfsaavgtf
      601 alvgalegwi lckcgwaeri vlfiasplll fpgtmtdfvg fagiaavigf qflqrrket
//
LOCUS       WP_007069354             198 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Dialister].
ACCESSION   WP_007069354
VERSION     WP_007069354.1
KEYWORDS    RefSeq.
SOURCE      Dialister
  ORGANISM  Dialister
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae.
REFERENCE   1  (residues 1 to 198)
  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 198)
  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   3  (residues 1 to 198)
  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   4  (residues 1 to 198)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 198)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Dialister"
                     /db_xref="taxon:39948"
     Protein         1..198
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22425
     Region          5..188
                     /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"
ORIGIN      
        1 msetyrivia ddeaiicmdl keileeaghe vvgicadgvr alelvkeekp dlvildvqmp
       61 kldglqaakl iahddlapvv lltaygdaet vekakrshvf gyvmkpveer nlfpalqiav
      121 sqyrsrheia hrvkemerel asrkiinrak gllmdyyhis deeayhkmqq tsmrrgillt
      181 dvaqkvikei mvrknmls
//
LOCUS       WP_007071579             167 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Micromonospora
            sp. ATCC 39149].
ACCESSION   WP_007071579
VERSION     WP_007071579.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. ATCC 39149
  ORGANISM  Micromonospora sp. ATCC 39149
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 167)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 167)
  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 167)
  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 167)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Micromonospora sp. ATCC 39149"
                     /db_xref="taxon:219305"
     Protein         1..167
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18002
     Region          76..164
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(95,114..115,133,136,144..145,156,161)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 msgkppltig iassathrrh laelfggaea flivssvdqa rrllgvtgkp pappsppaev
       61 athrpvvavd apasalsids drrvlrwrnr eigltplehd llrclvgtpg htwthrrlhr
      121 evwgterlgr gsdlhsvvrr vrrklarlgg patidavrgv gfrlavs
//
LOCUS       WP_007072094             206 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Micromonospora sp. ATCC
            39149].
ACCESSION   WP_007072094
VERSION     WP_007072094.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. ATCC 39149
  ORGANISM  Micromonospora sp. ATCC 39149
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 206)
  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 206)
  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   3  (residues 1 to 206)
  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   4  (residues 1 to 206)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 206)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 206)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Micromonospora sp. ATCC 39149"
                     /db_xref="taxon:219305"
     Protein         1..206
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22409
     Region          10..194
                     /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"
ORIGIN      
        1 maetqtdaer rrvliaedea lirldlaeml veegyevige agdgetavrl aeelkpdlvi
       61 ldikmpimdg laaaeriaga riapviilta fsqrdlvera raagamaylv kpfqksdlvp
      121 aveialsrys eiaaleaeva gltdrleirk tverakgalm ttygmtepqa fkwiqrtamd
      181 hrmtmkevae rilaetagge vaqpas
//
LOCUS       WP_007072782             386 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Micromonospora sp. ATCC 39149].
ACCESSION   WP_007072782
VERSION     WP_007072782.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. ATCC 39149
  ORGANISM  Micromonospora sp. ATCC 39149
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Micromonospora sp. ATCC 39149"
                     /db_xref="taxon:219305"
     Protein         1..386
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=40500
     Region          2..372
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msrvlvlncg sssvkyrlyd geevlrkgtv ervgepgggp adhetavrei ldgldqldpt
       61 gltavghrvv hggrrfaepv lvddavfaai eelvplaplh npanlagirv arealpgvpq
      121 vavfdtafhh tlpeaaatya idrdtarryd irrygfhgts hayvsrrtae llgrpyaeln
      181 titlhlgnga sacavaggrs vatsmgmspl eglvmgtrsg dldptvifhl rreagmgvde
      241 iddllnhrsg llglagvndm revlarrdag dpaatlaldv ytrritgyvg ayyallgrvd
      301 avtftagvge haagvraaal aglgrlgiav dparndgdgd rvispagaev avcvigtdee
      361 reiareartv aeaatadwgg pagrrp
//
LOCUS       WP_007073363             337 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp. ATCC
            39149].
ACCESSION   WP_007073363
VERSION     WP_007073363.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. ATCC 39149
  ORGANISM  Micromonospora sp. ATCC 39149
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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   4  (residues 1 to 337)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Micromonospora sp. ATCC 39149"
                     /db_xref="taxon:219305"
     Protein         1..337
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=35845
     Region          25..334
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mdvtpetrpt aghepaeaha aaialegigk rypdgteavr glslrvrage lvvligpsgc
       61 gkstvlrmin rlieptagri llgdedvtrv dpvalrrrig yviqnvglfp hqtvvanvgt
      121 vprllgwpsn rirrrseell elvgldpgrf grryphelsg gqrqrvgvar alaadpvvll
      181 mdepfsavdp ivrtrlqeef lrlqaevrkt ivlvthdlde avrlggriav lsqggrleqy
      241 dtpaallaap asdfvrdfvg adrgiralav tpvtrdalep apadpaglpe valgtsayda
      301 lavmltsgad rvlvtadgrp agvltrqral aggrdaa
//
LOCUS       WP_007075467             382 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Micromonospora sp. ATCC 39149].
ACCESSION   WP_007075467
VERSION     WP_007075467.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. ATCC 39149
  ORGANISM  Micromonospora sp. ATCC 39149
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Micromonospora sp. ATCC 39149"
                     /db_xref="taxon:219305"
     Protein         1..382
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41077
     Region          1..281
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          279..362
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkilhtsdwh vgkvlkgqsr aeehkqvlag vidvaraeqp dlvivagdly dtaaptpeat
       61 rlvtraltal rrtgadvvai ggnhdngqal dalrpwaeaa gitlrggvrd npdehvidgt
      121 taggerwrva alpflsqrya vravemyelt aaeatqtyad hlgrvlgrlt egfaepdrvh
      181 lvtahltvvg aatgggerda htvlgyavpa tvfpgtahyv alghlhrsqr vsgpcpirys
      241 gsplavdfge qenvpsvtiv evtatsaari revpvpaavp lrtvrgtldq laeiappdgw
      301 lrvfvreqpr aglreqvqel lpraleirid pemvpapgsg artaqragrs prelfadyld
      361 srghgdsdvr elfdelleev dr
//
LOCUS       WP_007075640              75 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Micromonospora].
ACCESSION   WP_007075640
VERSION     WP_007075640.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora
  ORGANISM  Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae.
REFERENCE   1  (residues 1 to 75)
  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 75)
  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 75)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 75)
  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   5  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10164212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Micromonospora"
                     /db_xref="taxon:1873"
     Protein         1..75
                     /product="winged 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=8158
     Region          5..70
                     /region_name="WHTH_GntR"
                     /note="Winged helix-turn-helix (WHTH) DNA-binding domain
                     of the GntR family of transcriptional regulators; cd07377"
                     /db_xref="CDD:153418"
     Site            order(5,7,30,32..33,41..45,47..48,51,61..62,64..67)
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:153418"
ORIGIN      
        1 mprqpvyeqv iddvtasirs gtlkpgdklp sitelceqyr asatpirlal rildergwie
       61 vhqgkgsfva qsppa
//
LOCUS       WP_007076378             169 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Micromonospora
            sp. ATCC 39149].
ACCESSION   WP_007076378
VERSION     WP_007076378.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. ATCC 39149
  ORGANISM  Micromonospora sp. ATCC 39149
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 169)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 169)
  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 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   5  (residues 1 to 169)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Micromonospora sp. ATCC 39149"
                     /db_xref="taxon:219305"
     Protein         1..169
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18415
     Region          72..157
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(91,110..111,128,131,139..140,149,154)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mlgelaesge galltgsaeq sgrtaaepwp psarrphpve frpaeadpag prptvprvfa
       61 aappppedpd evrilaasrv vrrgarvisl triefdllhf laanprrvft rpqllsnvwg
      121 yehavartvd vhvrrlrakl gntipmvttv ygvgyrlade arvsvdphr
//
LOCUS       WP_007077513             697 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Aeromicrobium
            marinum].
ACCESSION   WP_007077513
VERSION     WP_007077513.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium marinum
  ORGANISM  Aeromicrobium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 697)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 697)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 697)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Aeromicrobium marinum"
                     /db_xref="taxon:219314"
     Protein         1..697
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73967
     Region          2..694
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mtdthcpyca lqcaqtlseg dadtlvavpr afptnvngmc qkgwtstell tvrdrltvpl
       61 rrtvdgdfve vgwdealddi aarvravres agpdgvavfg gggltnekay qlgkfarlal
      121 rtrlidyngr fcmssaaaaa nrtlgvdrgl pfpltdlnda dvvvlfgsnl adtmppavqh
      181 lggvrsrggl vvvdprrsat arltddgage hvqlvpgtdl vlvlgllhvv faeslvdtgy
      241 ladrvdgvda vrrsvaewwp ervaattgvs etqvrrmarl ladasphrgg ggaflltgrg
      301 seqhtdgtdt vtavidlala lglvgaergg ygaitgqgng qggrehgqks dqlpgyrmia
      361 dpaarehvaa vwgvrpdqip gpgvpavell aslgtpdgpr alfvhgsniv vsapdagavr
      421 rrlesldlvv vcdivpseta mladyvlpvt qwaeedgtmt slegrvlrrr qavrapagvr
      481 seleifadla rrleapgtwa teprevfdel rrasaggrad yagisydrld agealhwpcp
      541 tddhpgtprl fadsfptpsg rasmvavrqt gpaevvsada pvwlvtgrvl qhyqsgaqtr
      601 rvaklngsmp rayveihpal aqrigvegvd eisitsvrgs mraqarispd irpdtvfvpf
      661 hfadeglvna vtlaavdpvs gmpefkvcav svartrt
//
LOCUS       WP_007077761             307 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Aeromicrobium marinum].
ACCESSION   WP_007077761
VERSION     WP_007077761.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium marinum
  ORGANISM  Aeromicrobium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Aeromicrobium marinum"
                     /db_xref="taxon:219314"
     Protein         1..307
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32806
     Region          1..297
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mpgrlllldt aslyyraffg lpdtlkapdg tvvnavrglv dfvatlvnre gaeavvacwd
       61 ddwrpawrve lvptyktqrl adgssdaeqt pddlspqvpl iaealtllgi pvvgapdaea
      121 ddvigtlvdr wdgpvdvvtg drdlfqlvdd aaahrvlyta rgvskldevd eawirekydi
      181 daaryvdyav lrgdasdglp gvagigekta aallgafgdl dgilaaaqdp staitprprr
      241 slveqadyva aarqvvavrr dldlpevapl prltsgqvee frefattwgl ggaadrvlta
      301 lqaesel
//
LOCUS       WP_007077548             205 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Aeromicrobium marinum].
ACCESSION   WP_007077548
VERSION     WP_007077548.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium marinum
  ORGANISM  Aeromicrobium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 205)
  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 205)
  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   3  (residues 1 to 205)
  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   4  (residues 1 to 205)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 205)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Aeromicrobium marinum"
                     /db_xref="taxon:219314"
     Protein         1..205
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22233
     Region          15..197
                     /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"
ORIGIN      
        1 mpsdeqtmtp pgaprvvvae dealirldlv emlrdegydv vgeagdgera valtaellpd
       61 vvlmditmpr ldgieaaaqi agrrlapvvl ltafsqrelv drareagama ylvkpfqqsd
      121 lppaiemars rfaeitalag evddlteqla arkaveraks llqesfgise aesfrwiqka
      181 amdlrlsmre vaeqvidkgt diarg
//
LOCUS       WP_007078392             350 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Aeromicrobium marinum].
ACCESSION   WP_007078392
VERSION     WP_007078392.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium marinum
  ORGANISM  Aeromicrobium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Aeromicrobium marinum"
                     /db_xref="taxon:219314"
     Protein         1..350
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=36026
     Region          16..342
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mtlhaeivlt ardvsvavdv gdgetvallg pngagkssll gavagllrpd agvvvldgrv
       61 lvddstwvpp hargvamlaq dpllfphlta lhnvafgprs tghgraeatr rarewleald
      121 vghladrrpa elsggqaqrv algralaaep rlllldepma aldvavapql rqvlqtvlhd
      181 rttvvvthdp ldallladrv vvieagrvve sgptrevlar prsafaaria glnlvsgrvv
      241 tggvrtregs vvagvaapgl aagsdavavf spaavavhrd ppggsprnvl pvrvtelepr
      301 gelvrvragd lsadvtlsaa adlalvpgtp vlfvvkarev alhpaglrad
//
LOCUS       WP_007078506             322 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Aeromicrobium marinum].
ACCESSION   WP_007078506
VERSION     WP_007078506.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium marinum
  ORGANISM  Aeromicrobium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Aeromicrobium marinum"
                     /db_xref="taxon:219314"
     Protein         1..322
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=35474
     Region          1..313
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mgieitgitk rfgdfvaldd inlsvpsgql tallgpsggg kstllrvvag lesadtgrie
       61 iegidttdlp aqkrnvgfvf qhyaafkhls vrrnvafgle irkqpkdqit akveellelv
      121 hltqwgdrlp sqlsggqrqr malaralaie psvllldepf galdakvrke lrdwlrrlhd
      181 evhvttvfvt hdqeealeva dtivvinegr ieqvgtpddl yddpasefvl sflgpvtrlg
      241 grlirphdie isryeqaata dgpitrwtri gfevrlevtp tdplhpepvq vvitrteana
      301 lglhlgdhvw lrpqvgaqtv ra
//
LOCUS       WP_007080133             679 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Rhodanobacter fulvus].
ACCESSION   WP_007080133
VERSION     WP_007080133.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter fulvus
  ORGANISM  Rhodanobacter fulvus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
REFERENCE   1  (residues 1 to 679)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 679)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 679)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..679
                     /organism="Rhodanobacter fulvus"
                     /db_xref="taxon:219571"
     Protein         1..679
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=75240
     Region          119..679
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mkkdlvikil fiensleeae qiisllrnsg iavrparatn aeqvqaalde lgpdivmfdp
       61 aittlsqrev vklmdaygrd yallglvdsm dnqlvadlfv ggargvaart hpkqltavlq
      121 refdslqarr qlrrleaslr eserrcdall dsstdaiayv hegmhvranr ayletfgyde
      181 fddllgmpvl dmidsthade fkailrgpqg qeklpnqlsl rarradashf datvefapat
      241 fegepclqiv frrqlvdpat laqlqrdpvt glfnrahtle ridtavaaaa ngkkgqalll
      301 iepdnwssiv asiglgkade liagfadrir illgttdvag mlaehtfgvv ldsrqdeair
      361 ewisklqhsv sneifdagsr sitvntsigg sllgeknant dlllnqasqa lrnaqsqggg
      421 kvelhdpaar ekadeerehy wlgllkdala ndglmlyhqq aislqdadgd fseillrmng
      481 pqgevlpgff mpiaekhgln gdidrwvlkq tiktlrerdk hgqsttffvk ltaaslqdeh
      541 llpwlgeqla aanlkhgriv lemteskvmt llrptqefvn gwkklggkfa leqfgsglns
      601 fqllnhvdad yvkidrsyma elprhpenqk kvteicqqar elnrqtiaew vedatstsll
      661 facgvdfvqg nflqppqrl
//
LOCUS       WP_007080544             371 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Rhodanobacter fulvus].
ACCESSION   WP_007080544
VERSION     WP_007080544.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter fulvus
  ORGANISM  Rhodanobacter fulvus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
REFERENCE   1  (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   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Rhodanobacter fulvus"
                     /db_xref="taxon:219571"
     Protein         1..371
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=40478
     Region          1..350
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mtlelshlhr ryagfaaldd vslciepgef lallgpsgsg kttllrilag ldypdsgsvr
       61 qndrdllavd arerkvglvf qhyalfrhlt vsenvafglr irprksrpgr aeinerverl
      121 lkrvqlddlg krytsqlsgg qrqrvalara lavepdllll depfgaldaq vrvalrrwlr
      181 nlheelglts vfvthdqeea leladrvavm nrgrieqigt peaiyqqpat pfvcefigkn
      241 nriplqrang vltggqrqlg adpwpgnavg saigyvrpeh llvsstpstd gwaaqlrhiy
      301 laggvahlel dvpalgqvle admssdevaq rglqpgqslv vqprlitafp ldargaadaa
      361 arhvlqpqaa s
//
LOCUS       WP_007080906             410 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Rhodanobacter fulvus].
ACCESSION   WP_007080906
VERSION     WP_007080906.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter fulvus
  ORGANISM  Rhodanobacter fulvus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
REFERENCE   1  (residues 1 to 410)
  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 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   3  (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   4  (residues 1 to 410)
  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 410)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Rhodanobacter fulvus"
                     /db_xref="taxon:219571"
     Protein         1..410
                     /product="CmpA/NrtA family 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=44133
     Region          13..263
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mnaptpsgsg tapklrigml rltdsapvvt ahefgffade gvevelmvep swaniadkla
       61 fgaldaaviv pplafavqlg lrgvaqpmli pytlsvggva itlerelatr vralgesddl
      121 dplpalaacl rqqpltlgvv hafsthnllc rywlasvgie vdrdvklavv ppsravealr
      181 ekqisgfcag apwgevarrn svghsiagsq qiwsnapeka favsarwanq hpealsgvlr
      241 alhrssrfcd daentayias llsrrrylnl gshailaslp ggaetsngcv fhrgaatfpw
      301 rsqglwflsq mrrwqlidds idlrslaerv yrpdlyraal salgeslpla dwkvegahaa
      361 pwsldatpqp ipmppdrfcd gaifdpaalp slgesampir arndendatr
//
LOCUS       WP_007081580             302 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Rhodanobacter fulvus].
ACCESSION   WP_007081580
VERSION     WP_007081580.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter fulvus
  ORGANISM  Rhodanobacter fulvus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Rhodanobacter fulvus"
                     /db_xref="taxon:219571"
     Protein         1..302
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32368
     Region          15..261
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 msiaaqsvva adnrlgegvq wcprtqalyw tdilastlwr ytphdgatrq wtmperlasf
       61 alceadgwll lglasqlaff hldsgelqpi vdvepdlltr vndgacdrqg rfvfgtmhep
      121 egdapkqaig gfyrlntdls lerlplpsva isnslafspd gatmyfcdsp tqriqccdya
      181 vdgrlgtprt fvdlagiegd pdgstvdaeg glwnaqwgms rvvryradgr edtvvplpar
      241 qptrpalgga aldtlyitsa rdglpadcvr deprngalfs apapagvhgl aearfggsps
      301 lg
//
LOCUS       WP_007082240             138 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Rhodanobacter fulvus].
ACCESSION   WP_007082240
VERSION     WP_007082240.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter fulvus
  ORGANISM  Rhodanobacter fulvus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Rhodanobacter fulvus"
                     /db_xref="taxon:219571"
     Protein         1..138
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15026
     Region          1..136
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mrrqlgftll elmivvviis ilsalaissy rsyvvrthrt daqrtlldla grqerfyysh
       61 naytdtladl sgsntmvgng qyytisipsa sstdytitat aagnqrrdda lcqtlslers
      121 gtqsstgsta ndpkcwgn
//
LOCUS       WP_007082292             146 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Rhodanobacter fulvus].
ACCESSION   WP_007082292
VERSION     WP_007082292.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter fulvus
  ORGANISM  Rhodanobacter fulvus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Rhodanobacter fulvus"
                     /db_xref="taxon:219571"
     Protein         1..146
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14985
     Region          1..145
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mknmqkgftl ielmivvaii ailaaiaipa yqdyiirsqv segstladga ktavaefysn
       61 tgrmpstnas aglakaesit gsyvsqvava dgkitatfak aspqkantai dtktlvlspv
      121 tsagstswtc nggtvsnkyl psscrk
//
LOCUS       WP_007082987             125 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Rhodanobacter fulvus].
ACCESSION   WP_007082987
VERSION     WP_007082987.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter fulvus
  ORGANISM  Rhodanobacter fulvus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
REFERENCE   1  (residues 1 to 125)
  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 125)
  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   3  (residues 1 to 125)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Rhodanobacter fulvus"
                     /db_xref="taxon:219571"
     Protein         1..125
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14454
     Region          10..111
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mdnlanaktm rseqtpaeqh lwyhlranrf mglkfkrqkp mgpyivdfic lergviievd
       61 ggqhgddvay dqrrdrwlas qgfivlrfwn hdvlnqtesv lerirqvvde rafparlpsp
      121 paplp
//
LOCUS       WP_007083113             369 aa            linear   BCT 20-JAN-2025
DEFINITION  GerAB/ArcD/ProY family transporter [Neobacillus bataviensis].
ACCESSION   WP_007083113
VERSION     WP_007083113.1
KEYWORDS    RefSeq.
SOURCE      Neobacillus bataviensis
  ORGANISM  Neobacillus bataviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Neobacillus.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Neobacillus bataviensis"
                     /db_xref="taxon:220685"
     Protein         1..369
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=41316
     Region          6..365
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 mnqqpgklgi reyvsiailm vslkatentp ailfnkvqna awmvpilsag lffiplflll
       61 ktmslfegkn lifliqkllg kyigffvclf ifiitsfgms fesrtytdii rafyfsttpv
      121 yvlysvlmav caygakkgiq hvgsvaylvi fwviisffia lglstqdsni qgilpiwgpg
      181 kleivkkstq slnlcadffl ltmlvpylks nkdfrkgtwi afilvsiqis vatllflclf
      241 dqslggigyp fhsairyisl gsyipnieii ffviwiisaf irfsaflyin alvfghifki
      301 kdfeflipsl aaiylligii pespvevmle wrsmvqsiig psfaaislil wlaallkgef
      361 khannkngl
//
LOCUS       WP_007083697             396 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Neobacillus bataviensis].
ACCESSION   WP_007083697
VERSION     WP_007083697.1
KEYWORDS    RefSeq.
SOURCE      Neobacillus bataviensis
  ORGANISM  Neobacillus bataviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Neobacillus.
REFERENCE   1  (residues 1 to 396)
  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 396)
  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   3  (residues 1 to 396)
  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   4  (residues 1 to 396)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 396)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 396)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 396)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Neobacillus bataviensis"
                     /db_xref="taxon:220685"
     Protein         1..396
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42015
     Region          40..379
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(114..116,137..138,187,239,263)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mklkkslall ltgglaasif lagcgsksgd ngksgssmik iatqtplsgg satigeaikl
       61 gaqmkldeek kkfkdlgfdl qlvpyddqgd pkkgvanaql igadksimav vghfnsgvai
      121 pssevyekya ipmvspansa vevtsrglkt vnrivarddf qgpagaefav ntlkakkifi
      181 iqdktaygtg laeafkkaae ekgaeilgfe gitigekdfn gvlnqvvskk pdlvyfggiy
      241 aegglvikqa rekginvpfl ggdgldastl veiaggaikd tyitslagds tksedgkkft
      301 vsykekfnkn tesysvygyd tmgvvlkgie daikannnkm ptreqvrdav rgvkdyqgvl
      361 tkvsfddigd nnyakvfiys fkeakypael vgevnk
//
LOCUS       WP_007083713             357 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Neobacillus
            bataviensis].
ACCESSION   WP_007083713
VERSION     WP_007083713.1
KEYWORDS    RefSeq.
SOURCE      Neobacillus bataviensis
  ORGANISM  Neobacillus bataviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Neobacillus.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Neobacillus bataviensis"
                     /db_xref="taxon:220685"
     Protein         1..357
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=40045
     Region          1..352
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqiqnisk sfgafkaldk inidiqtgel iallgpsgsg ktsllriiag lenanqgail
       61 fgeedmthig tkerkvgfvf qhyalfrhmt vfdnvayglr vrprkarpsk qeikekvtel
      121 lelvkleafa nrypshlsgg qrqrvalara lavepkvlll depfgaldak vrkelrrwlr
      181 klhdnyqits ifvthdqeea ldvadrivvm negkieqigt pdevyehpnn pfvynflgnv
      241 nlfkgrldqg klrhgsievd aplefagkin teavgyvrph ditikrvass dsvaakisyi
      301 hlvgaavqve lirqdngefv eaeiakdyfr slelktgeev fikpkqlkvf ipedysi
//
LOCUS       WP_007083970             381 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Neobacillus bataviensis].
ACCESSION   WP_007083970
VERSION     WP_007083970.1
KEYWORDS    RefSeq.
SOURCE      Neobacillus bataviensis
  ORGANISM  Neobacillus bataviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Neobacillus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Neobacillus bataviensis"
                     /db_xref="taxon:220685"
     Protein         1..381
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43025
     Region          1..266
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          <289..355
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkfihtadwh lgklvhgvym tenqrevleq fveivaeekp davviagdly drsvpptdav
       61 elldeilfki nvelktpiva iagnhdsaer lsfgsswykh sqfylsgkls nsfkpvqigg
      121 vnfflvpyae pgvvrqllrd esihshqdam kaligkmees inpneanvlv ghafvlggqt
      181 sdservlsvg gsgcvgaelf epfsytalgh lhspdaithh kvkysgsllk ysfseakqrk
      241 sisiiemnek gkfthryrsl tpkhdmrele ghleelldph fyekeqlhdy lkitlldega
      301 lldpinklrq vypnvlhler kiditdlknk qsfhahrsek kseielfeqf yaemttseft
      361 gdkkavmadi idkvlregna i
//
LOCUS       WP_007084755             373 aa            linear   BCT 20-JAN-2025
DEFINITION  GerAB/ArcD/ProY family transporter [Neobacillus bataviensis].
ACCESSION   WP_007084755
VERSION     WP_007084755.1
KEYWORDS    RefSeq.
SOURCE      Neobacillus bataviensis
  ORGANISM  Neobacillus bataviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Neobacillus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Neobacillus bataviensis"
                     /db_xref="taxon:220685"
     Protein         1..373
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=42845
     Region          13..367
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 mkvnlhpkks mlfnafflmf iihsvqagvg vvglprivfl eakhdawisv ilggvfvaii
       61 lwfmmmmlnq yesadlygih vdvfgkwlgn flsilymlym staffiimmn yieivqvwif
      121 stlptwqlaf vlilisvyav yggirvvvgv aflsvmgtaw liliqivplr yadiahifpi
      181 mnvdikhllk gvksttfsmm gfelilfvyp fikekrkahl yaqignaftt ltftiltfis
      241 iiffaedslk nviwpvismf kvvklpnler fefivvsfwm lvilpnlcay lwaaskgfsr
      301 ifkrkqkwgv wiiailafst tffikaryqe nvvtdivaki afyaaycypi vlsiivflkk
      361 rlsrrkktha egs
//
LOCUS       WP_007087060             252 aa            linear   BCT 20-JAN-2025
DEFINITION  phosphonate ABC transporter ATP-binding protein [Neobacillus
            bataviensis].
ACCESSION   WP_007087060
VERSION     WP_007087060.1
KEYWORDS    RefSeq.
SOURCE      Neobacillus bataviensis
  ORGANISM  Neobacillus bataviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Neobacillus.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
REFERENCE   2  (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   3  (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   4  (residues 1 to 252)
  AUTHORS   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Neobacillus bataviensis"
                     /db_xref="taxon:220685"
     Protein         1..252
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=27290
     Region          6..245
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 msskimiean nltknferki alsslsftik qgelvaligp sgagkttlln sigglvpiss
       61 gellldgksl sahkkgksfa kkvgvirqqf dligplavih nvlagklsew gtmkslfsll
      121 vpqekdlaik alervglhgk afeitstlsg geqqrvamar lmvqrpeiil adepvasldp
      181 araddilaml tkivteekqt litslhsvey akkyftriis mrngeiffdl ptekvtddll
      241 aelyqlksgv ma
//
LOCUS       WP_007088647             294 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Thalassospira xiamenensis].
ACCESSION   WP_007088647
VERSION     WP_007088647.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira xiamenensis
  ORGANISM  Thalassospira xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 294)
  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 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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Thalassospira xiamenensis"
                     /db_xref="taxon:220697"
     Protein         1..294
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32128
     Region          36..280
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <183..280
                     /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 mseqtrnlse rdilsdvfgv nhprgnafft gtlcgrsdhq grddkpliqq gilhvlrsgs
       61 vrvfidgrqt hfldrpglil fgkatrheie tpktgsgivc anllfhdagp gpallgipdc
      121 lvltfdempg lemitgqlfn eafeiqpgtr tavnllidll flmvmrhcqk hglmragils
      181 alrdprisrv vgalynrpgh gwsvesqael agmsraafaq lfrdllgisp geflqtirle
      241 rahallqagq rlqfvagevg yrsstalara ilqkygvspr mlqgdlktas vair
//
LOCUS       WP_007088958             387 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [Thalassospira].
ACCESSION   WP_007088958
VERSION     WP_007088958.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira
  ORGANISM  Thalassospira
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae.
REFERENCE   1  (residues 1 to 387)
  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 387)
  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 387)
  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 387)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Thalassospira"
                     /db_xref="taxon:168934"
     Protein         1..387
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=42321
     Region          16..380
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkkiptpedv kskqvsrrsf ltkgatgvva ggaaasglfa apavhaqpap lvvkmqtswp
       61 ssdiwmtfak qyadrveams ggrlkvdllp agavigafqv ldgvndgvid iahsvpvywy
      121 gknkaaslfg tgpvfggsat tmlswfyagg geefyreltq dvmglnvigl lgfpmpaqpf
      181 gwfkgevnsv adiqgfkyrt vglaadllqs mgmsvaqlpg geivpamerg vidafefnnp
      241 ssdmrfgaqd vaknyylssy hqasesfefi fnrdfyedle pdlqailryg veaastsnta
      301 lamdnyssdl qkladegvti hrtskeilaa qleawdklip qleedpfmkk vldsqrawve
      361 rvtyyelmns pdyqlaydhy fpgklkl
//
LOCUS       WP_007089024             195 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Thalassospira xiamenensis].
ACCESSION   WP_007089024
VERSION     WP_007089024.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira xiamenensis
  ORGANISM  Thalassospira xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Thalassospira xiamenensis"
                     /db_xref="taxon:220697"
     Protein         1..195
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21372
     Region          1..163
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlrslydwtl glaahrhaai alfiiafves svfpippdvl lipmiiaapt rawryalicl
       61 vgsvlggiag ygigyflfes igqpvlqlyg ysakfdifrd yynewgawav fiagispfpy
      121 kvitilsgvt aldpaifmva svlarglrff iiaaliwkfg pvirdfierr lglvftifvv
      181 vlvggfaaik liphg
//
LOCUS       WP_007089150             407 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Thalassospira
            xiamenensis].
ACCESSION   WP_007089150
VERSION     WP_007089150.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira xiamenensis
  ORGANISM  Thalassospira xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 407)
  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 407)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Thalassospira xiamenensis"
                     /db_xref="taxon:220697"
     Protein         1..407
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46269
     Region          6..393
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mindkaaisv sarqarnlal aaqgfdqdes rpvtkrrimk airqtgmlqv dsvnvltrah
       61 ympvfsrlgv ydpadldqls wgnsrqrrlf eywgheasmi pvedyglyrw rmadaaegkg
      121 twgqiakmir dhpefvrsil driekegala asdleqegas sskwwgwskt ktameflfws
      181 gqvmarkrrt sfervydlpe riigpealep pmpraeaqra lirngiaamg iateadlrky
      241 frlptddaka rvaemvedgt llqanvegwk qpgylcphvn prcrakptal mvpfdpimwe
      301 rdrverifgf nyrieiyvpa ekrqygyyvl pfmqngefva rvdlkadrqe gvlrvqsahl
      361 edgcdavtva gdlmmhlsrl arflglsgvv vvpynpfsvy lgrqnqg
//
LOCUS       WP_007089618             281 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Thalassospira
            xiamenensis].
ACCESSION   WP_007089618
VERSION     WP_007089618.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira xiamenensis
  ORGANISM  Thalassospira xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Thalassospira xiamenensis"
                     /db_xref="taxon:220697"
     Protein         1..281
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31791
     Region          7..278
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mtdtpklsyc adyvrrndkd rflcslfasp dkreslftly afnqevsktr emvsdtmlgh
       61 irlqwwrdtl aeieqgkirk hevveplsvv iqsgrldard letliaaref dladkapanq
      121 aeldhyidqt sghlavmate llgvddadar haarlagnay glvgilramv fhgrakrlyl
      181 phdrmehygv gqgdifefrk tdtvkaltre iaelaqnrir earkyrkylp snalaaalpv
      241 vladgylrkl ekagfdpfsa efglarpasf rltvkaflnr y
//
LOCUS       WP_007089639             281 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Thalassospira xiamenensis].
ACCESSION   WP_007089639
VERSION     WP_007089639.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira xiamenensis
  ORGANISM  Thalassospira xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Thalassospira xiamenensis"
                     /db_xref="taxon:220697"
     Protein         1..281
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29552
     Region          198..280
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mneeqgfglr aeqryqgagk kapggglakg vgtivlglvi iggglggagy wlynqgqpaq
       61 eegklpillp dplpiklrpd dpggmevphr dttiyeqlds nqpedqvvlq elpdmpkvpd
      121 vipspdntge pavieqtpea eivanaaqig sgkdvnasak tpaetaivap sdaekaiava
      181 kakeqatapa atsasgisek dfriqlasvr dtsgaeaewk rlsyknkdll gslqmylkra
      241 dlgdkgvfyr lqagplpdaa aaetlcrnlk qrnvgclivr p
//
LOCUS       WP_007089694             397 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Thalassospira
            xiamenensis].
ACCESSION   WP_007089694
VERSION     WP_007089694.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira xiamenensis
  ORGANISM  Thalassospira xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 397)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 397)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Thalassospira xiamenensis"
                     /db_xref="taxon:220697"
     Protein         1..397
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44377
     Region          9..394
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 marlrygivt fkgnragilr eepgnatsfe ydlgfdhdia cclpaaqrth fhpnglhpff
       61 shlgpegwlr erqsafedld tnddfgilla fagdcigavg iidpeakqdr rlktstlspm
      121 dqaanterti sgvqakilcn etddgklhpa kqdepapiia kfssenlpdl vtneagtmal
      181 cktllpkgev ahtwrtfvtg ipdaalavrr fdrqgaamqt klrcedfaqi lgvtpgrdhr
      241 gkynasygdi gralsfssap lidarrafir lavyvllgnv dchiknwsll etpnglrlsp
      301 aydvlngyiy gaqgyttrfg llvndqrlqw enydrdlllr iapefglprk aaesalkqly
      361 rkkeplfknl kdrillseek sfryantvke aweriyd
//
LOCUS       WP_007091180             771 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Thalassospira xiamenensis].
ACCESSION   WP_007091180
VERSION     WP_007091180.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira xiamenensis
  ORGANISM  Thalassospira xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 771)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 771)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..771
                     /organism="Thalassospira xiamenensis"
                     /db_xref="taxon:220697"
     Protein         1..771
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=84471
     Region          37..709
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mtdqpntpgr lsrarvtlwl hylvplavll vcvvlrwqdv plvgqlrmsv fdtyqriapr
       61 afedagvrii didersldem gqwpwprtrl aeliyrlrla gaqvvgfdiv faepdrtspa
      121 rvvhdwpknd nsdalaklae tlpdhdllfa efingvgqvv taaqltsqpf stlprqvgnf
      181 svggeagrhl adfipvlsga tanlsvieea aagnaiinvs peqdgvvrrv plmlaldhee
      241 pligkpvypt lsmevfrilq daprtmnvrl sgasgttrwt taegveairv gevtiptdqs
      301 ghmwvhfagh raeryisaad vikgnlpera lentvvligt saaglldlrs tpldpvlpgv
      361 eihaemleqm llgqfltrpy wvaeietlvl llvglffvla ipklgavwpa iiggtmtvaa
      421 ggfswwayss hqilidpvyg avslvavyli assigfmrte gerkqvraaf anylspalve
      481 qlarhperlk lggetrdmtl lfcdvrgfts isegfksnpq gltrlinrll tplskaildr
      541 egtidkymgd cimafwnapl dvpaharrac esalamfdal ehlnarraee ateegqdylp
      601 lnigiginsg nclvgnmgsd qrfdysvlgd avnlasrleg qsknygvgiv igeetarqaa
      661 dgfaileldl iavkgkseav riftllgdst iahsaefadl ldrhmemiqs yrlqdwdgte
      721 rlidecinla tdmigqfdla glyglyrdri atfraspppp dwdgvfvats k
//
LOCUS       WP_007091252             201 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Thalassospira xiamenensis].
ACCESSION   WP_007091252
VERSION     WP_007091252.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira xiamenensis
  ORGANISM  Thalassospira xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Thalassospira xiamenensis"
                     /db_xref="taxon:220697"
     Protein         1..201
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21802
     Region          28..180
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mekedksqnq nnkglvgwwr vwqqrlekla agrkglggia vasflettii pipieiliap
       61 imaasrrrgv ivatvtllgs vagavflyli ayglsgeliq piietaggqq efqkveqqfe
      121 eggfwvvfai siapipmqla alaagattyp fwlflvaigi sralryyglw llvlgfgvgi
      181 arlfegkkpd rlekaekgds v
//
LOCUS       WP_007091384             398 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Thalassospira].
ACCESSION   WP_007091384
VERSION     WP_007091384.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira
  ORGANISM  Thalassospira
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae.
REFERENCE   1  (residues 1 to 398)
  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 398)
  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 398)
  AUTHORS   ter Beek,J., 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 398)
  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 398)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Thalassospira"
                     /db_xref="taxon:168934"
     Protein         1..398
                     /product="CmpA/NrtA family 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=43770
     Region          4..265
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mslkqvrlgf vplvdcalpv varakgfaee enidltlire mswaairdkl sygvydaahl
       61 lagiplaarl glggmpsqri avpmalgrgg naitvstrly qrmleadpaa mhgprglsar
      121 alkkvidedr adgrpimsfa tvfpysshny elrywmaagg idpdkdvnig viapprmfds
      181 lrngwvdgyc vgepwnqrav fhgdgvival kediwarspe kvlgvredwv qsnpdtvdal
      241 vralvrsaew adqpenrtel aqllsgenhv gasfdilras llgrpvlkpg dnpieapdrh
      301 vfyrytatfp wlsqgawvgt qmqrwgqvda svdfgtlisd iyrpdlyrra vkgldvalph
      361 ddwrvegand aadrafvgpd afldnsifdm rsfagvge
//
LOCUS       WP_007091420             424 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Thalassospira xiamenensis].
ACCESSION   WP_007091420
VERSION     WP_007091420.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira xiamenensis
  ORGANISM  Thalassospira xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Thalassospira xiamenensis"
                     /db_xref="taxon:220697"
     Protein         1..424
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44268
     Region          <4..152
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          123..382
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mveliygtdg advlvgteqd dhifgragsd yirglggndr fyeigpgddt ldggaghdhf
       61 hasigddtll ggsgndkldg gpgadvidgg pgrdeirfsy sndsakegvi vnlatgigvg
      121 gdadgdryfn iedirdsryg diligddgnn affqtgagdg dvmnggggdd tfyaaygsaf
      181 seeqtsifig gegsdtisyi agwgndapyg eygpqpvinl etgtgrtgdh fisienvdgs
      241 nqsdliigdd ndnrlignkg gdtiygrdgd dvivgenihg eagndtltge wydvslyggd
      301 ghdtldagpi aheafsdnil sggggndwlq gnigddtfvf daeassrdrv vdfesgndgd
      361 tllltadlqa rsgitdfdsl ldhatetdgg dlyidfsngd pwtfgvived iskddltpdn
      421 vefg
//
LOCUS       WP_007092074             207 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Thalassospira].
ACCESSION   WP_007092074
VERSION     WP_007092074.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira
  ORGANISM  Thalassospira
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae.
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   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   3  (residues 1 to 207)
  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   4  (residues 1 to 207)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 207)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 207)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Thalassospira"
                     /db_xref="taxon:168934"
     Protein         1..207
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22803
     Region          11..199
                     /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"
ORIGIN      
        1 mkranripnf rgwhawvlhr psaaidpllr hlerlgmtvd rywpelpgld daqskgadil
       61 ffdadmgmde qfpwtpdhtp mpsvaligse apgrlewvls rqsgahlqkp vstagvfsaa
      121 vlavhafeqq qklraeicel rrrlklrpvv akvlmtvmls hnidehgalk airaeamkkq
      181 qtiedycaai vasgrtgsgd gatiapn
//
LOCUS       WP_007092191             364 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Thalassospira
            xiamenensis].
ACCESSION   WP_007092191
VERSION     WP_007092191.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira xiamenensis
  ORGANISM  Thalassospira xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 364)
  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 364)
  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 364)
  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 364)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Thalassospira xiamenensis"
                     /db_xref="taxon:220697"
     Protein         1..364
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39484
     Region          1..346
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkrrqflkga gigagaavaa tvaapaivsa qeslnwrmvm pwpkgtpglg tnaekfaamv
       61 kemsngrlni svfgageivp pfecmdaveq gvvemahgtp yywqgknpal nffstipfgl
      121 tawelsawlr fgggqelwee ayaefnvvpf yagnsgmqag gwfnkeinsv edlkglkary
      181 aglggeamrr lganitmlpp geilpamqsg aidaaewvgp wndlafglyq vakfyytpaf
      241 hepgpgleif iskekfdalg kdmqaiirya aqaiaentla dftfnnlqsy qplidkgvev
      301 rqfsddvila laeqsnaavq eiaakndlsg riaesylalv kkaarygkef eatgllhrak
      361 vwgy
//
LOCUS       WP_007092192             364 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [Thalassospira].
ACCESSION   WP_007092192
VERSION     WP_007092192.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira
  ORGANISM  Thalassospira
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae.
REFERENCE   1  (residues 1 to 364)
  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 364)
  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 364)
  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 364)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Thalassospira"
                     /db_xref="taxon:168934"
     Protein         1..364
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39415
     Region          1..345
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkrrqfltga smaagafvas saapsiakad eqihwrmvmp wpkgtpglga ngekfaervt
       61 kmsggrlkit vygagelvpa fecmdaveqg vaelahgtpy ywagkdagvn ffstipfglm
      121 gwelsgwlrf gggqelwdel yaqfnvkpfa agntglqagg wfnkeintvd dikgikmrya
      181 giggeamrrl ganvtmlpaa eilpamqsga idaaewvgpw ndyafgltqv gkyyytpafa
      241 epgtgievfv nkdkfaelpe dlqeifavaa qanleqtlad ftfhniqsyq avlakgaeir
      301 hfsddviaal atevkaavke iadqnelngr iyasymdfvk kaapygkefe atgllqranv
      361 waea
//
LOCUS       WP_007092470             376 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Thalassospira
            xiamenensis].
ACCESSION   WP_007092470
VERSION     WP_007092470.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira xiamenensis
  ORGANISM  Thalassospira xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 376)
  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 376)
  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 376)
  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 376)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Thalassospira xiamenensis"
                     /db_xref="taxon:220697"
     Protein         1..376
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=41070
     Region          5..365
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mtnlkrrdfl tksalgtavv gaaagaavfa tphiaraqes fnwkmtnayg pgspfyvtgp
       61 gspedfckrv temsngrlni qhfaagelip alegfdavqa gtvemnaana yfwagkifaa
      121 qyfttvpfgl nfqgmnawly hagglelwhe lyqpygliaf pmgntgvqmt gwfrepiesl
      181 ddfnglkmri pglagkvyqq igvevkllpg geifpalerg vidaaefvgp yqdrrlglqk
      241 aakyyyttgw hepsnvtell inqkaweslp adlqaivkna aqacnldshs wceannaaal
      301 rdlvenegvi aqtlpddvvn klkgitndtl eaeaakdplt kkvhdafmaf rdthrewaav
      361 sekpyhgiis skdgms
//
LOCUS       WP_007092208             334 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Thalassospira
            xiamenensis].
ACCESSION   WP_007092208
VERSION     WP_007092208.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira xiamenensis
  ORGANISM  Thalassospira xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  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 334)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Thalassospira xiamenensis"
                     /db_xref="taxon:220697"
     Protein         1..334
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=36333
     Region          39..94
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mtslhthaqi rkgaaqpapv gtsavarwqw vqneifdhad lstseicvav vlashvndrt
       61 qdcfpkieti areaglserk vrqalvrleq lglihrrvrc igrlrnrnay qlvglggkpe
      121 sgalkpasds gikpapgags nmntdkddnt dekeqshatt gtgavilpav ddqclvlare
      181 wqrlcadpwt lanaclrvne aidrvgfdav rqaledvkrr gkrpsrlgll dildglvsev
      241 svsadesvfp avcdpsdppe wqeicqvvaq sdipgcrnpr iwlsqiravl sgntielkar
      301 nrcvqdiarh hllaiiepva errglqigav scvs
//
LOCUS       WP_007092534             796 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Thalassospira
            xiamenensis].
ACCESSION   WP_007092534
VERSION     WP_007092534.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira xiamenensis
  ORGANISM  Thalassospira xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Thalassospira xiamenensis"
                     /db_xref="taxon:220697"
     Protein         1..796
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=87458
     Region          232..789
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 miwpdvittg lvtgmagglv vpagrrlllg dieqdwlqde leldgidpvd gvtvrgkdgs
       61 lsriwhlqgt sydarieseq qslllgrqsl lqelgkrkia vrlfavkrqr eiaahanwpn
      121 tvleeigtae arqykssyfi dwylmataqa mqplldaeek ipailseyrp ellarseddr
      181 pclltgflng lvsgeyrrdl paisrnlsan lpasdlhcdk vtgtitthvp aqqfhkvitv
      241 tlwpetvsgh ligeilalqg dieicqicdp wgsdqamlvn krrmagesns wfgnpaaaae
      301 vstlldllae gktalfatqf qiipraeted klaslirkit eilgnkrigy alqtrgapvc
      361 wfnrlpvisk rkirlpgsqf mapldlrdqn iaalwalphs atgmlasqfg papvrwfktp
      421 tgqsyafqfq vvnkpfslgn flvfapsgvg kstlimhlmg glakfenvrs yifdskegtr
      481 fmveamggly qaydglslnp ldvgddtpkn rervyailks lagidledad ldalnhavdl
      541 afqiepphrt lnaiypfafa rrsalrrafa qwvtddkgnt glrshifnap hdslggllnq
      601 shmvginmne aladpalggp vvghiseais ksvagrnggf vifideaakl lsnpgfrdlg
      661 aemyreyrkl ggavgmafqd paglgktgaa eaiientatm iffpnskvte eslkpfnlne
      721 eqklfvqgrt rarkkddrrv liikrdeasg feesaildvd laplgdavrf yrsgpdannd
      781 laaiqtkwgd awqshl
//
LOCUS       WP_007092938             492 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Kordia algicida].
ACCESSION   WP_007092938
VERSION     WP_007092938.1
KEYWORDS    RefSeq.
SOURCE      Kordia algicida
  ORGANISM  Kordia algicida
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Kordia.
REFERENCE   1  (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   2  (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   3  (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
REFERENCE   4  (residues 1 to 492)
  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 11467355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Kordia algicida"
                     /db_xref="taxon:221066"
     Protein         1..492
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=56889
     Region          28..472
                     /region_name="COG3800"
                     /note="Predicted transcriptional regulator [General
                     function prediction only]"
                     /db_xref="CDD:443013"
ORIGIN      
        1 meqeyiklif glklkqirtd knlslfglsk itglsksyln eiekgkkypk pdkivilsek
       61 ldvpydqmvs lkldknlapi gellqskilk eiplelfgik esnlidivan apakvnafis
      121 tiieiaqhyn fsresfflas vrsfqeannn yfndletqvl sfskayqvdl trpissnyle
      181 eilieeygyt ihknelssye alenlrsvfv pktktlllad gideaqrtfv yakeiaynfl
      241 kitdrlytfp wikfesfdev lhnfyasyfa galiipkdtl tlqletlfak etfdkksflq
      301 ilqtfnaspe sfyqrltnil pkafniqnlf flrfthkags ekfhlkkelh lshqhspran
      361 etnehycrrw islqvlkdis enknshefni qisnyeddga kyllfssatn dpfkedtyrs
      421 isvgllinkq lerklkfled ptikqqsvgv tcercaikdc elrhapaivl ekeaknkkie
      481 hivnelnakf ts
//
LOCUS       WP_007093646             287 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Kordia algicida].
ACCESSION   WP_007093646
VERSION     WP_007093646.1
KEYWORDS    RefSeq.
SOURCE      Kordia algicida
  ORGANISM  Kordia algicida
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Kordia.
REFERENCE   1  (residues 1 to 287)
  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 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   3  (residues 1 to 287)
  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   4  (residues 1 to 287)
  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 287)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Kordia algicida"
                     /db_xref="taxon:221066"
     Protein         1..287
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34050
     Region          39..283
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          206..283
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mkllpvynis qfqeketskh lycnrfkehl rthpfiekph rhdfhllvif tkgtgthvvd
       61 fntfditags vfalqpgqmh hwnlsedidg yilfhskefy nvhfqhkqin dypfyfstyn
      121 tpelclnhqq tanvssffem ilteyssksl fkehailnil dliyielsrh yvtptqlqik
      181 ryhtilrnfe vileqfykhe kkpsfyasrl nitlkhlnri cretldktat tvitdriile
      241 akrllltpel sineianllg fedysyfsrl fkqktgqtps efrsldf
//
LOCUS       WP_007097088             127 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Synechococcus sp. RS9916].
ACCESSION   WP_007097088
VERSION     WP_007097088.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus sp. RS9916
  ORGANISM  Synechococcus sp. RS9916
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 127)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Synechococcus sp. RS9916"
                     /db_xref="taxon:221359"
     Protein         1..127
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=13740
     Region          8..126
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(78..79,82,99..102,104)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mieliaslvv dlsdqkltvy dhndqvvrvi pvstgkastp tptglgavrt kyrsvtmrgr
       61 gyvapgvpya mcitanemic lhgapwqeda gqafgvprsh gcvrmptaqa rwlfentrkg
      121 tevliql
//
LOCUS       WP_007097808             217 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Synechococcus sp. RS9916].
ACCESSION   WP_007097808
VERSION     WP_007097808.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus sp. RS9916
  ORGANISM  Synechococcus sp. RS9916
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 217)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Synechococcus sp. RS9916"
                     /db_xref="taxon:221359"
     Protein         1..217
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=23154
     Region          96..205
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(169..170,173,186..189,191)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mlpdrlsrll ilisagvsfa spgqaltlne alairlatpn ettrssvaar shsdtqqhra
       61 spaellaklq eegtsvlvle kthrrlpstg dpiwslrlei pgqpvrqfda vsgranrqsa
      121 drdrlgsrap lpaghyilgp veplaagayp elgpiwigie ptfptgrrvl gihqdpsagl
      181 gansgtlgci glikrndlle larqvnkaki relvvtn
//
LOCUS       WP_007098012             257 aa            linear   BCT 20-JAN-2025
DEFINITION  phosphonate ABC transporter ATP-binding protein [Synechococcus sp.
            RS9916].
ACCESSION   WP_007098012
VERSION     WP_007098012.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus sp. RS9916
  ORGANISM  Synechococcus sp. RS9916
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
REFERENCE   2  (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   3  (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   4  (residues 1 to 257)
  AUTHORS   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 257)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Synechococcus sp. RS9916"
                     /db_xref="taxon:221359"
     Protein         1..257
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=27937
     Region          3..248
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mtavlelrdv slrgrdtarl dhvslslqag etvallgpsg agkssllsia ngslkpdagg
       61 vywrgtelhl rprqerrqig tlwqdlrlve elnvaqnvns galgrrsllw altnlllple
      121 reacgrclkq aglqpdlldr pvtslsggqr qrvalarlfr qrpglvlade plssldpalv
      181 edllttllrq splddhdvlp sttviclhrp dliqrfnrvi glkqgrmvld apakaitdre
      241 lkdlygpain takgaqa
//
LOCUS       WP_007098459             160 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Synechococcus sp. RS9916].
ACCESSION   WP_007098459
VERSION     WP_007098459.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus sp. RS9916
  ORGANISM  Synechococcus sp. RS9916
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Synechococcus sp. RS9916"
                     /db_xref="taxon:221359"
     Protein         1..160
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=16807
     Region          16..124
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mtplnsrfql allnrkkgkn liekgftlve lmivivivgi lsavalpnfl sqttkakvse
       61 asaklsgllk eghaeyqyks dptavqtvma ssittansag nfdyaitgtl tgtsavlpmt
      121 atgndndael edkvlsgcvn fktgkvdint qldvtpptcl
//
LOCUS       WP_007098622             279 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Synechococcus sp.
            RS9916].
ACCESSION   WP_007098622
VERSION     WP_007098622.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus sp. RS9916
  ORGANISM  Synechococcus sp. RS9916
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
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   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 279)
  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 279)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Synechococcus sp. RS9916"
                     /db_xref="taxon:221359"
     Protein         1..279
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29807
     Region          21..91
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          199..259
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 masrdsfsvd pqsdaqqevi tdlqhvgqal qrareaqglt lhqladalhm gdeqlkalet
       61 gdrdhlaetv fvratvrrva sklrldpepl iaalqsldgp npshrqsgsg rtdaaktqtr
      121 pqqeppagrr rgwlrvataa taivatiaag wswgqstllr qakeneaaps dasslgaskp
      181 lsqasapina aptspqtlti htsqpswiav rnqdgeelfa gmldkektfa asegleiyag
      241 rpdlvsvksa gnqqsplgpi dqirwyrisa apepinptl
//
LOCUS       WP_007100104             103 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [unclassified
            Synechococcus].
ACCESSION   WP_007100104
VERSION     WP_007100104.1
KEYWORDS    RefSeq.
SOURCE      unclassified Synechococcus
  ORGANISM  unclassified Synechococcus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="unclassified Synechococcus"
                     /db_xref="taxon:2626047"
     Protein         1..103
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11398
     Region          1..95
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mslalaqpql dtiadacrrh hvarldafgs vlrpdyrpge sdidllvefq pldpatlyka
       61 yfallnelri glasrvdlvm adavrnpyvk qtieasrqqi yaa
//
LOCUS       WP_007101273             631 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CHASE2 domain-containing protein [unclassified
            Synechococcus].
ACCESSION   WP_007101273
VERSION     WP_007101273.1
KEYWORDS    RefSeq.
SOURCE      unclassified Synechococcus
  ORGANISM  unclassified Synechococcus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 631)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 631)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="unclassified Synechococcus"
                     /db_xref="taxon:2626047"
     Protein         1..631
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=68295
     Region          7..607
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mswkrwllpy vaasallvgf qaspaaetln lllydlvasl retqhspddg aitvvgidea
       61 dlkafkwpip drhlcgaiqr letlgasaig ldlyrdpigt dsatclstli qtnprlisih
      121 nmadaipaip gtpprqqafn dlvvdsdrvv rrdlvhvggq seavrslplr lletargnpn
      181 lhrqlealpa eiwlqpqsgg yqrldasgyq tmlpvhppgr fpivslrall sgrvdassiq
      241 drivligsta pslkdqfeip qsrldqgerf lalpgvelha qrlaslqall rdgqapirta
      301 salqrhllla vmlllgiaia erphrirrss lllglsalal fgtsvlllle gvwigialpl
      361 sglilfgstg ilrrgaisqr hqqemarllg qatspavaqq lweqradliq dgrfagreqp
      421 vtilftdtch ftrvseqlsp aalmdwlnag maisvdavts rggmvnkftg dgmlavfgap
      481 isaglerdas qaleaaraiq tgiarlnrdl qargawplkl rigihsglvl tgslgsrsrl
      541 eyavigdtvn casrlesldk drhqgwvrvl isaeslslag vnpkddavid wgevhvkgrt
      601 eplrvfewrd qvnvetaind tpqgsspate n
//
LOCUS       WP_007102983             113 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Paraglaciecola polaris].
ACCESSION   WP_007102983
VERSION     WP_007102983.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola polaris
  ORGANISM  Paraglaciecola polaris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Paraglaciecola polaris"
                     /db_xref="taxon:222814"
     Protein         1..113
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12689
     Region          1..102
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(6,24..25,33,36,38..39,41,44..45,47,55,60,66)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(24,55..56,58,84)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mvnqhynqiw qtvcaipkgk vasygqiadl aglpgrarlv gkslgyipkd mfvpwyrvir
       61 ssgqlafsag sdqalhqtgm lqeenvvvfr nrvklrvfqw qptldemlwk lng
//
LOCUS       WP_007103308             795 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Paraglaciecola polaris].
ACCESSION   WP_007103308
VERSION     WP_007103308.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola polaris
  ORGANISM  Paraglaciecola polaris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 795)
  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 795)
  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 795)
  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   4  (residues 1 to 795)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..795
                     /organism="Paraglaciecola polaris"
                     /db_xref="taxon:222814"
     Protein         1..795
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89359
     Region          64..795
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mhlkyalslk ditakpsrrl inhalkdeqa tqatfigqar arealdfglg idakgynlyv
       61 mgeqatgrft lvheyiakyv rkvltpddwc yinnfddere pfalrlppge skrlvknmeq
      121 lvdelldtfp aafdnpgyqr kkvaitrefd qryeqaidtv eqlaqaqnva lyeengnisf
      181 spivdgkpit dadfaklsdd drqqyyhlid elenrlseal ielpkwkras seqlrhlkkd
      241 taeqgikpll kelehqyaad lgilkflrql kphlvetive iladdkkdek hdeydrrsvl
      301 eeqylpnilv shelnsgapv iyepnpthqn lfgrveytnv sgsvftnyrm irpgalhran
      361 ggyllldvdk litqpfawet lklvlksghl kmdlpqadvg mvnsitlnpq qipinvkvvl
      421 lgsrelyynl qdyddefyel frvlvdfdhe iqldkqtlyd fvgrvrhqvt qlglnsispk
      481 amyrlveysl rmaehqqrls arfsdviell neslyfcrks qdldldvthi eaalsaktrr
      541 tgrvseavld dikqgqilia tegvdvgkvn gltvlevgdc lfgtparits tvyagangvv
      601 dierevelgq pihskgvmll tgylghkyaq lfpltlsani aieqsyghid gdsaslaelv
      661 alisaltnip trqdlaitgs inqygqvqsv ggvnekiegf fklcqhrglt ghqgaiipks
      721 nqinlmldkd viaavklgkf hicvvetvdq alellmdkdv gtmntkgryp kgtinymavs
      781 sllnianvvn gsdde
//
LOCUS       WP_007104543             154 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Paraglaciecola polaris].
ACCESSION   WP_007104543
VERSION     WP_007104543.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola polaris
  ORGANISM  Paraglaciecola polaris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 154)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Paraglaciecola polaris"
                     /db_xref="taxon:222814"
     Protein         1..154
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16534
     Region          2..154
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mtlsktdlyk evaqqaqalm agekdlianl anvsallymr lptlnwagfy llkeqelvlg
       61 pfqgkpacir iplgrgvcgt aaetglaqci ydvhefaghi acdaesnsea vlpvfkngkl
      121 lgvmdldsph tgrfdqedmt glqnlvnilq daia
//
LOCUS       WP_007105275             102 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Paraglaciecola polaris].
ACCESSION   WP_007105275
VERSION     WP_007105275.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola polaris
  ORGANISM  Paraglaciecola polaris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (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   2  (residues 1 to 102)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Paraglaciecola polaris"
                     /db_xref="taxon:222814"
     Protein         1..102
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10795
     Region          31..100
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkkfiatlff agvlltgyvg nvvaeaqvdk ssvsqmksqk inlntataeq lvtlpgigkk
       61 kaaaiiayre ksgkftsidd ltnvkgigkk mlakladhvq vk
//
LOCUS       WP_007105594             389 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Paraglaciecola
            polaris].
ACCESSION   WP_007105594
VERSION     WP_007105594.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola polaris
  ORGANISM  Paraglaciecola polaris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 389)
  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 389)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Paraglaciecola polaris"
                     /db_xref="taxon:222814"
     Protein         1..389
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44685
     Region          1..385
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mpetlspqqa rklilhaqrl pagkqttkpi satlaaieal gyvqidtisa ierahhhtlw
       61 nrtstyqpqh leqlveqkqv feywahaaay lpmsdyrytl vrkaalqsge lahwyprnnk
      121 lmadvlarit aegplmakdf dkdeavikrk padwaskpak raleflfmqg dlmiakranf
      181 hkvydlterv lpcsvntsip sddayfrfli trflsanglg kaseiaylrk nskraiqkkl
      241 namleeksli evtvagesyv tlteqletle rpikrnklhi lspfdnlliq rkriqalfnf
      301 dyllecyvpq akrqygyfsl pilwdtnlva rmdcrvdrkt kilhihhlvl eanlqktaaf
      361 hlalqqslta flifnqcdey vlhktthls
//
LOCUS       WP_007105604             370 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Paraglaciecola polaris].
ACCESSION   WP_007105604
VERSION     WP_007105604.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola polaris
  ORGANISM  Paraglaciecola polaris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 370)
  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 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   3  (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   4  (residues 1 to 370)
  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 370)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Paraglaciecola polaris"
                     /db_xref="taxon:222814"
     Protein         1..370
                     /product="CmpA/NrtA family 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=40723
     Region          3..265
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mikleqpdit lgfipltdsa plivakelgf ferwglnvtl qkqnswstlr dklhagvlda
       61 aqmlapmpia salglgapsa nvitplvlsl ngnaitlseg llqevlkene itnvtlpmag
      121 yllqkvvekr khrglaklkf atvfpyschy yqlrdwlkaa kvnlddvdll vippinmvec
      181 lengdidgfc vggpwnakav ragigmtalt sfdiwqdspe kvlglldswh qknpnsvlal
      241 caalkqacsw lesvpnrfea arllsqseyl daeldviaps llgsclthks mpprsipsyn
      301 qfsvsnngci nqpelvrgew likhmvsagq ippnvtipld ligkvfrpdi yqkmrllied
      361 kgvqfyrrsg
//
LOCUS       WP_007106630             190 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Paraglaciecola polaris].
ACCESSION   WP_007106630
VERSION     WP_007106630.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola polaris
  ORGANISM  Paraglaciecola polaris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Paraglaciecola polaris"
                     /db_xref="taxon:222814"
     Protein         1..190
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21348
     Region          1..163
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mvaylkrktk qfiesknmym alviasfles iivpipleav liplmqakre kiwflaflat
       61 lgcvfgaiig ygvgyflfdq faaqianwfs dpqqlenvkt qmqeqgfwyv lsvgiipipf
      121 qiamlaagaa kyslfmflla tliarsiryf glallvklag nqaeaifkky kiptaivltl
      181 vvvliwwvkh
//
LOCUS       WP_007111142             270 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Vreelandella
            boliviensis].
ACCESSION   WP_007111142
VERSION     WP_007111142.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella boliviensis (Halomonas boliviensis)
  ORGANISM  Vreelandella boliviensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Vreelandella boliviensis"
                     /db_xref="taxon:223527"
     Protein         1..270
                     /product="formate/nitrite transporter family protein"
                     /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=29428
     Region          2..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msylmpsefv tklvdqgesk vymgtrdtli rsfmagatla lavifaitia tqtgnfliga
       61 llfpvgfvml ylmgydlltg vftlvplawl dkrpgvtlpr mlkcwalvgl gnlggalfia
      121 tfgylnftmg gteeinavgq tmmtvgesrt vgyqeaglag wivlflrgmf cnwmvsmgvv
      181 gaaisttvsg kimamwmpii vffylgfehs vvnmflfpig lmmgadftly qyimwneipt
      241 vlgnlvgglt lvglvlytth vrtqpkkvfs
//
LOCUS       WP_007111305             269 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Vreelandella
            boliviensis].
ACCESSION   WP_007111305
VERSION     WP_007111305.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella boliviensis (Halomonas boliviensis)
  ORGANISM  Vreelandella boliviensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Vreelandella boliviensis"
                     /db_xref="taxon:223527"
     Protein         1..269
                     /product="formate/nitrite transporter family protein"
                     /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=28711
     Region          2..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msyllpaefa akmvdageak lhmstrdali rafmagaila iaavfavtva vqtgypiiga
       61 ilfpvgfsil ylmgfdlltg vfvltplawl dkrpgvtinr ilkhwgivfv gnfggaltva
      121 flmaivftyg fstepsevgr vigevgegrt vgykeygagg matifirgvl cnwmvslgvv
      181 gamisttvsg kviamwmpim lffgmgfehs vvnmflfpsg lmmggnfsim dyliwneipv
      241 vlgnliggla ltgltlytth vrtapqkal
//
LOCUS       WP_007111529             276 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Vreelandella boliviensis].
ACCESSION   WP_007111529
VERSION     WP_007111529.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella boliviensis (Halomonas boliviensis)
  ORGANISM  Vreelandella boliviensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 276)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Vreelandella boliviensis"
                     /db_xref="taxon:223527"
     Protein         1..276
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=30439
     Region          21..238
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 msqcarvngs ckrcegdlpf eftmafqpiv dlslaqivty ealvrgshge sagsviaqvt
       61 ddllyrfdqa crvkaiemas alnmqtdlsi nflpnavyep eaciqatlev skrvgwptnr
      121 lifeiteter vrdrqhlcni idayrsmgfk talddfgngy anldlltelt pdklkidrel
      181 vmhcdsdfrr qallnaiill aqeldmtlia egvetraeal wlaragivcq qgfyfakpai
      241 nslgadispl ltelkselag lksevesgsg avhern
//
LOCUS       WP_007112397             143 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Vreelandella boliviensis].
ACCESSION   WP_007112397
VERSION     WP_007112397.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella boliviensis (Halomonas boliviensis)
  ORGANISM  Vreelandella boliviensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Vreelandella boliviensis"
                     /db_xref="taxon:223527"
     Protein         1..143
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15946
     Region          1..141
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlslffvalv satllpggse vwlarlwclg epplglwlva tagntlgsmi nvamgryarr
       61 fqdrrwfpas prslaraegw yhrfgelsll iswapiigdp ltvlagvfrl pwwralawiv
      121 vakgtryalv lllaqqwlep lcq
//
LOCUS       WP_007112748             173 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Vreelandella boliviensis].
ACCESSION   WP_007112748
VERSION     WP_007112748.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella boliviensis (Halomonas boliviensis)
  ORGANISM  Vreelandella boliviensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 173)
  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 173)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 173)
  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   4  (residues 1 to 173)
  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   5  (residues 1 to 173)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Vreelandella boliviensis"
                     /db_xref="taxon:223527"
     Protein         1..173
                     /product="TRAP transporter small permease subunit"
                     /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=18501
     Region          19..170
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mapatthnal erggiiggyi rvmdklsris aylacamfia gvlvicqmvf iryllgmsts
       61 wqteftifsv taamlmgspy vlmtgghvai tivpdalggi trtimrlias lfglgfcaal
      121 ayaswvyvae afhgewttgs vwtpplwpal lpmaigstll slqyvaeilr ges
//
LOCUS       WP_007113573             381 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Vreelandella boliviensis].
ACCESSION   WP_007113573
VERSION     WP_007113573.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella boliviensis (Halomonas boliviensis)
  ORGANISM  Vreelandella boliviensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Vreelandella boliviensis"
                     /db_xref="taxon:223527"
     Protein         1..381
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42790
     Region          1..268
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          265..351
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrllhtadwh lgrlfhnlsl lddqrhvldq lieiidrenv davliagdiy drsvppsaav
       61 tlldevlhal ceerklpvim isgnhdgaer lrfgarhlrq aglhilsdla dyatpvtlti
      121 kgievdvfgi pyadpehvrs qfevdtrdfd aahrylveri seqrhptrpc vlmshcfvdg
      181 gsasdserpl tlggaesvaw epmqgfdyva lghlhgpqyr ggehirysgs llkysfsean
      241 qrkgvtlvdi dvsgvtqieq iplipsrevr vlegeidtli aqgrtdphad dyllvrltdr
      301 haildpmgkl revypnvlhl ekpgmldarg kqqldrerqr fdaldmfsdf fnqtsgeams
      361 deqasamael itqlqrdeaq q
//
LOCUS       WP_007114767             111 aa            linear   BCT 20-JAN-2025
DEFINITION  PilZ domain-containing protein [Vreelandella boliviensis].
ACCESSION   WP_007114767
VERSION     WP_007114767.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella boliviensis (Halomonas boliviensis)
  ORGANISM  Vreelandella boliviensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 111)
  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   3  (residues 1 to 111)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 111)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Vreelandella boliviensis"
                     /db_xref="taxon:223527"
     Protein         1..111
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11946
     Region          2..111
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 maaqkalslt vpdvptllsa ympfldhggi fvptqthyvl gqqvfllltl pgeserlsvt
       61 gqvvwvspeg vsgrrmpgig lhfsqqdypv rdrietllag qldkaapsft l
//
LOCUS       WP_007117445             142 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Sulfitobacter indolifex].
ACCESSION   WP_007117445
VERSION     WP_007117445.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter indolifex
  ORGANISM  Sulfitobacter indolifex
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Sulfitobacter indolifex"
                     /db_xref="taxon:225422"
     Protein         1..142
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15557
     Region          18..140
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlallslffa allaatlipa qsealllglm wsgshavall wlvatvgnvl gsvlnwllgr
       61 ylshhadhrw fpfsakqmar asdgyqrwgy wsllaswvpv igdpltlaag ilreplwrfi
      121 livtfakggr ylvliliarg sm
//
LOCUS       WP_007117936             118 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Sulfitobacter indolifex].
ACCESSION   WP_007117936
VERSION     WP_007117936.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter indolifex
  ORGANISM  Sulfitobacter indolifex
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Sulfitobacter indolifex"
                     /db_xref="taxon:225422"
     Protein         1..118
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=13050
     Region          11..87
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mtdqttpasl vssdnvngta vfsadgteig hidhlmidkk sgkvayavmg fggflgmgee
       61 hypvpwnald ydpardgfmt nideatvkga pertdrwdsd rawqertfdh ygvpyywl
//
LOCUS       WP_007117667             311 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Sulfitobacter indolifex].
ACCESSION   WP_007117667
VERSION     WP_007117667.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter indolifex
  ORGANISM  Sulfitobacter indolifex
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
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
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Sulfitobacter indolifex"
                     /db_xref="taxon:225422"
     Protein         1..311
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=33734
     Region          1..308
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mieidritkt yagiravdsv smtvetgtit vivgtsgsgk ttllrminrl eeptsgevri
       61 ngestlsvkp hilrrrigya iqghglfphh tvgrnigavp qllgwprdki narvdellel
      121 fsmdpaqfrd rypaelsggq qqrvgvaral asrpdlllmd epfgaldpii rtraqedlrr
      181 iqqrlgstim lvthdmeeai rlgdrvavmd ggklvqhatp aeiiakpate fvanmvgdve
      241 rplrllslis vrelvedgta egdplpagas lrdalsaclw tgrtsvpvee dgtplgrvtl
      301 dairaragqh a
//
LOCUS       WP_007118129             328 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Sulfitobacter indolifex].
ACCESSION   WP_007118129
VERSION     WP_007118129.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter indolifex
  ORGANISM  Sulfitobacter indolifex
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Sulfitobacter indolifex"
                     /db_xref="taxon:225422"
     Protein         1..328
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33845
     Region          16..233
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mlalfalpal lglglifnii dddseedrpe dppeppdtlf vpddvesfrg sdgddiivar
       61 ddggfiagre gddtitgsdn vddiaghdgn dvidarggdd rvwgdfgddt itlgdgadrg
      121 iggngddnin ggagddhisg endddtligg agndtltggy gddliymgeg ddsgaayglv
      181 nwgndtvygg tgddvilegr gydalygeag ddviraldgt sspdtvdgga gndhlllddg
      241 digtggdged lfslnhsdya eepaiiitdf ntdddllsid tystdpveli hdpdraavlv
      301 qrtgvtlgil eglseadipn islvefaa
//
LOCUS       WP_007118454             188 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Sulfitobacter indolifex].
ACCESSION   WP_007118454
VERSION     WP_007118454.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter indolifex
  ORGANISM  Sulfitobacter indolifex
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 188)
  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 188)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 188)
  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   4  (residues 1 to 188)
  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   5  (residues 1 to 188)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Sulfitobacter indolifex"
                     /db_xref="taxon:225422"
     Protein         1..188
                     /product="TRAP transporter small permease subunit"
                     /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=21559
     Region          3..187
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mrfmrgyirr idamnrrigr immygifalm gvllwstvsk affvpslwtl emaqfvmvgy
       61 yilggpysiq lgsnvrmdll ygdwslrrka wfdlitvffl ifylcvllyg aisstayslg
      121 ywgtepfsff sglvtgaeei ghmeksssaw rpylwpikvv mivgiflmll qclsellkdv
      181 lrlkgeai
//
LOCUS       WP_007118596             404 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Sulfitobacter
            indolifex].
ACCESSION   WP_007118596
VERSION     WP_007118596.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter indolifex
  ORGANISM  Sulfitobacter indolifex
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 404)
  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 404)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Sulfitobacter indolifex"
                     /db_xref="taxon:225422"
     Protein         1..404
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45994
     Region          1..398
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 msrptlgnga arrlflarhl lsdppqgpak gaallkvihd lgfvqldsin tvarahdlil
       61 farrpryrpa alkrlyekdr alfehwthda avipmqfypq whlrrtrdaa kllnrwkdwq
      121 rhdfeaqmqs vlaqvraegt vtssdvgrde prssggwwew hpsktaleyl wrsgalavag
      181 renfrkrydl tervvpaalh dpanapdttq tidwccdqal trlgfatage leafwahisp
      241 aeargwcave qtagrleein ieaadsslrp afvrpgwand paltreppkr lrvlspfdpa
      301 lrdrkraarl fgfdyrievf vpeaqrkygy yvfpllqgdr mvgrvdmkah rdvdelrita
      361 lwpergtgwg kgrqaafeae lqrllplagv sqlrfvdgwl rdpv
//
LOCUS       WP_007118748             152 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Sulfitobacter indolifex].
ACCESSION   WP_007118748
VERSION     WP_007118748.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter indolifex
  ORGANISM  Sulfitobacter indolifex
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Sulfitobacter indolifex"
                     /db_xref="taxon:225422"
     Protein         1..152
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=15819
     Region          2..134
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mtvdyqtlak tiaalteged davalmatia cevhqsddrf dwtgfyrvta pevlkigpyq
       61 gghgclvipf srgvcgaaar tgevqlvedv dafpghiaca sstrselvlp vwngagdllg
      121 vfdidsdqpn aftqadadal aailkdsfaa aa
//
LOCUS       WP_007118977             280 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Sulfitobacter indolifex].
ACCESSION   WP_007118977
VERSION     WP_007118977.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter indolifex
  ORGANISM  Sulfitobacter indolifex
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 280)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Sulfitobacter indolifex"
                     /db_xref="taxon:225422"
     Protein         1..280
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=31017
     Region          35..264
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mprrfqrpia dippggdspl nhavtqrdas tlemvrvava hrqtllafqp vmrasdptri
       61 afheglirll dptgrvipak dfmpviedte tgrqvdvlal rlglnalhsh pglrlsinms
      121 arsigyqdwn rvlrhwlard atlgerlile itessammvp elvanfmdql qpygicfamd
      181 dfgagqtair yfkdfyfdil kldgqfirgi atnpdnralt aalmsiathf dmltvaecve
      241 naadaavlte mgidclqgyh yaapttrpdw fdlgharatg
//
LOCUS       WP_007120330             429 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Sulfitobacter
            indolifex].
ACCESSION   WP_007120330
VERSION     WP_007120330.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter indolifex
  ORGANISM  Sulfitobacter indolifex
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 429)
  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 429)
  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 429)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Sulfitobacter indolifex"
                     /db_xref="taxon:225422"
     Protein         1..429
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45754
     Region          22..92
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          312..379
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 migrwasksa kdetvepkgf dafelrlgdv mrgeratlgk slldvqrelr ikasyiaaie
       61 ncdpgafdtp gfiagyvrsy arylnmdpdr aftafckesg favahgmsae asvvkkpsfe
      121 errksvkedd lfarpntpfv ptgdgllsri epgavgssmv lialisaigf ggwtvlkevq
      181 rvqvapvdqt pivlsdldpl dgalarapdt dddsaapqsv esprsdaldr lyrpqaldvp
      241 vlvardapia sidprsvsnf ptpdrpepsg qaaavaendt innaidealm lanadtdlpk
      301 pqvveplgek vrmvaaypsw vrvraadgtv ifegvmnkgd twdvpvteep ptlrtgesga
      361 lyfamadgcf gpvgargavt snvalqaqal adryqpvdpt aeqslsrmfa dlegsldpsv
      421 laampcqgq
//
LOCUS       WP_007120362             192 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Sulfitobacter indolifex].
ACCESSION   WP_007120362
VERSION     WP_007120362.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter indolifex
  ORGANISM  Sulfitobacter indolifex
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Sulfitobacter indolifex"
                     /db_xref="taxon:225422"
     Protein         1..192
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=20867
     Region          1..163
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mirrlydwtl glaqhrhalw alavvafves sffpippdil mipmiiarpn rawliagval
       61 lasvlggllg yaigalafes lgqpilaslg kadamaefst rfndmgfwav lvagvtpfpy
      121 kvitimsgwt gmplgifimt silarglrff vvagllwrfg apirdfierr lglmftlava
      181 lliggfmvvk vl
//
LOCUS       WP_007120525             194 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Sulfitobacter indolifex].
ACCESSION   WP_007120525
VERSION     WP_007120525.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter indolifex
  ORGANISM  Sulfitobacter indolifex
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 194)
  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 194)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 194)
  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   4  (residues 1 to 194)
  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   5  (residues 1 to 194)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Sulfitobacter indolifex"
                     /db_xref="taxon:225422"
     Protein         1..194
                     /product="TRAP transporter small permease subunit"
                     /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=21895
     Region          1..170
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mvsfirfadn lsawfgksfa wlillmslgt gyevfvryvl ndptawaldv sfimygtlfm
       61 mggaytlsrg ghvrgdflyr llqpktqaki divlyiffff pgvtalilsg wkyaarswqy
      121 gevsvnspag vpiyqfkavi vaagillfiq gmaqvcrcil amrnnywlea yedvfetedl
      181 lmraankaek dhit
//
LOCUS       WP_007121900              81 aa            linear   BCT 20-JAN-2025
DEFINITION  acyl carrier protein [Limosilactobacillus gastricus].
ACCESSION   WP_007121900
VERSION     WP_007121900.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus gastricus
  ORGANISM  Limosilactobacillus gastricus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
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   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 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   4  (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 10011594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Limosilactobacillus gastricus"
                     /db_xref="taxon:227942"
     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=9178
     Region          3..76
                     /region_name="acpP"
                     /note="acyl carrier protein; Provisional; PRK00982"
                     /db_xref="CDD:179197"
ORIGIN      
        1 mtkeeifasv kevvveeldl dedqvtldak ikedldadsl dvfeimnele dkfdiqldvd
       61 envqtigdvv dfvkkqmdeq a
//
LOCUS       WP_007123556             274 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Limosilactobacillus antri].
ACCESSION   WP_007123556
VERSION     WP_007123556.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus antri
  ORGANISM  Limosilactobacillus antri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 274)
  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 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   3  (residues 1 to 274)
  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   4  (residues 1 to 274)
  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 274)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Limosilactobacillus antri"
                     /db_xref="taxon:227943"
     Protein         1..274
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31189
     Region          32..271
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          187..265
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mdelhhenvv vntnigirfw rsqvntsgyv pfhwhssiei vcvlagrldf tingqqlavt
       61 adqfivipsg vvhdvanlpn tayvlqvplk vlkpyvahpe qvifannqla spayaqaldl
      121 ikkfaklqlh hppafrfdse itfaallkil ftrlndpdrq vpntnnvkql iifinnhsta
      181 pltvaalarr fgynpsylsr rfkeqvgisl ihyiyvvkln hlyndlintd tdikqlfqkn
      241 gltnprtark ffremfgklp ndvrrekksk ksah
//
LOCUS       WP_007123600             220 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Limosilactobacillus antri].
ACCESSION   WP_007123600
VERSION     WP_007123600.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus antri
  ORGANISM  Limosilactobacillus antri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 220)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Limosilactobacillus antri"
                     /db_xref="taxon:227943"
     Protein         1..220
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24533
     Region          87..219
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(164..165,168,192..195,197)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mklavknriy agiylvvaiv gmgpelrksh rqspkparqa qlatdhqqav hrshsparss
       61 kmrvpidwrk ssetvpypdl aktkdfwvkv slkknrtyly dgqkllytmy stggmykrnp
      121 qtgkmesmtp tgtyyaqser gdsffnssln eganyyvswl dhgtylfhsv ptvaggnynv
      181 aeakklgkst gshgcirlsv pdaqwmsthl pvgtkivivn
//
LOCUS       WP_007124003             372 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Limosilactobacillus antri].
ACCESSION   WP_007124003
VERSION     WP_007124003.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus antri
  ORGANISM  Limosilactobacillus antri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 372)
  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 372)
  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
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 372)
  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   5  (residues 1 to 372)
  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   6  (residues 1 to 372)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 372)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 372)
  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 11973053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Limosilactobacillus antri"
                     /db_xref="taxon:227943"
     Protein         1..372
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41208
     Region          <16..79
                     /region_name="COG3398"
                     /note="Predicted transcriptional regulator, contains two
                     HTH domains [Transcription]"
                     /db_xref="CDD:442625"
     Region          76..361
                     /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 mrtktmqsiq qsnysniyhl lmhndklskq miadelglsl ptvtsnlnrl sdqqlimkng
       61 qleskigrra taysinhnaf lsigievfqk yatitvinlk hevlaihtvn ipfansdqya
      121 aaladqvrwv lqnngyneka ilgagigiqg lidsagttvl wgkildctgm raerfsqflp
      181 fpvrfyhdad cvaaaeyaan phdgivlsig ehfgsamiva gkilrsttgr dgtmehisin
      241 prhgrpcycg rrgcietycs lssllqptet lnsffanlkq ddpavkkrfa eyldylaesi
      301 ynlhmfidvp iiiggrlskf itspvleelr krlraisvfp eneryvkvgh vadnavaiga
      361 aipfidekls si
//
LOCUS       WP_007124498             193 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Limosilactobacillus antri].
ACCESSION   WP_007124498
VERSION     WP_007124498.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus antri
  ORGANISM  Limosilactobacillus antri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 193)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Limosilactobacillus antri"
                     /db_xref="taxon:227943"
     Protein         1..193
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=21346
     Region          62..191
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(137..138,141,165..168,170)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mnvvrvsiek iiyqflvifg ilgccslfta sanasrmrtp idwqkssetg aypdlaktpd
       61 lwlkvslkhn rtyvysghkl iytmystagk fqkdpasgkv ksvtptgtfq vqptrgdwvy
      121 npnlklgany yvswngdylf htvvtgpdhr yikseaaklg kepsspgcvc lsvpdakwlk
      181 dslptgtkiv idn
//
LOCUS       WP_007124751             398 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Limosilactobacillus antri].
ACCESSION   WP_007124751
VERSION     WP_007124751.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus antri
  ORGANISM  Limosilactobacillus antri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Limosilactobacillus antri"
                     /db_xref="taxon:227943"
     Protein         1..398
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43378
     Region          6..393
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msksiavnag sstlkfklfd mpseevvaeg tierigekmg hakikyagqk heddqpfgdh
       61 gaaikylldq lialgivqny deitavghrv vaggeyfkds avitddvikk idslaeyapl
      121 hdpaelmgik afrkalpnaf aiavfdtsfh aempkknaly sipyewyeky garkygahgt
      181 shryvaaqaa kmlkkpledl klitmhigag asitavkngk sfdtsmgftp lagitmatrs
      241 gdvdpslvaf veekagmssd emidtlnhks gllgiselsp dmrdildaad kgnekaqlal
      301 diyvnrikry igayiaemdg vdaivftagv gensipvrkl vtdnldcfgi kidqeknqcr
      361 gverdlsaad akvktllipt neelmivrdi erlkkeak
//
LOCUS       WP_007125009             397 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Lactobacillus ultunensis].
ACCESSION   WP_007125009
VERSION     WP_007125009.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus ultunensis
  ORGANISM  Lactobacillus ultunensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Lactobacillus ultunensis"
                     /db_xref="taxon:227945"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43746
     Region          2..392
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkkvlavnsg sssfkfklfs fpdekviakg mgdrigleds tfsitladgt kytkeiaipd
       61 qeaavsilik dlqkyhvlks lneivgvghr vvnggeyfkd stvidknklq kildlsdfap
      121 lhnppeargi eafmhvlpkv pqvavfdtsf hetldpvhyl ysipyeyyek yrarkygahg
      181 tsvhyvtlea akmmhedlse skliichlgn gasitavkng ksydtsmgfs plsgitmgtr
      241 sgdvdpsllq hlmhktgmsm demidvlnqk sgllgisgis sdmrdlkynk kprailarki
      301 flnrivryig sfiaemggvd aivltagvge gdvgmrkaim dsfkymgvdp dyeanetngq
      361 kfitkpdski qvmiiptnee lmiardvvrl tncatla
//
LOCUS       WP_007125580             401 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Lactobacillus ultunensis].
ACCESSION   WP_007125580
VERSION     WP_007125580.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus ultunensis
  ORGANISM  Lactobacillus ultunensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 401)
  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 15774123
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Lactobacillus ultunensis"
                     /db_xref="taxon:227945"
     Protein         1..401
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=44991
     Region          <3..148
                     /region_name="PknB_PASTA_kin"
                     /note="Stk1 family PASTA domain-containing Ser/Thr kinase;
                     NF033483"
                     /db_xref="CDD:468045"
     Region          123..245
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          273..400
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(351..352,355,373..376,378)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mneelrkknk rnniillvig lviivailag fgihsyneat rtaaekfaqt hfnpnvkidg
       61 vkvgkltvak atdkvnknak nqielknnkl eysysttiqt ideaetrslf kkqqtkmpsn
      121 ksysfttkdl atakkklsdl knatikyqin gesydlkake lvdnvtyrdg kyqfgdtakl
      181 tdklnqidke vsslhksykf tvpkgdkvkg ktitvknktw gwgvyvkkar rlllealeqg
      241 kttfngadai ygvgystyah gygksnheig ktyavvslkk qevwlvrngk lkvhlrdvvt
      301 gtmegskgdq tprgvwyihy kqspstlrgt nddgssyasp vkywmpftls gcgfhdaswr
      361 tdwsktaylr ggshgcvnvk pseirsvwnn isknepviiy e
//
LOCUS       WP_007125680             256 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Lactobacillus ultunensis].
ACCESSION   WP_007125680
VERSION     WP_007125680.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus ultunensis
  ORGANISM  Lactobacillus ultunensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
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   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   4  (residues 1 to 256)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Lactobacillus ultunensis"
                     /db_xref="taxon:227945"
     Protein         1..256
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=28593
     Region          6..250
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mtnstikfvh vnkkfgknqi isdlnfeikr gefvtvlgss gsgktttlkm inglekpttg
       61 qvivngkdvs scnlvelrrh igyvvqsigl fphmtiaqni avtpkllgwn kdkinqkvds
      121 llkqvglepe qykkrypiql sggqqqrvgv aralstnppi llfdepfsal daiirqnlqq
      181 eikslhqkls dktfffvthd inealflgdk vmvmnhgqie qfdtpealvs kpatdyvaql
      241 ldtvrqnkal wehlnd
//
LOCUS       WP_007125729             255 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Lactobacillus ultunensis].
ACCESSION   WP_007125729
VERSION     WP_007125729.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus ultunensis
  ORGANISM  Lactobacillus ultunensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
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   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   4  (residues 1 to 255)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Lactobacillus ultunensis"
                     /db_xref="taxon:227945"
     Protein         1..255
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=28525
     Region          6..250
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mtkeiikfnh vrksfgrnev ipdltfsisq gefvtvlgss gsgktttlkm inglekptsg
       61 dilisdknlk dtnlvdlrrh igyvvqsigl fphmtiaqni avtpkllgwt qekinsrvne
      121 lletvglhsa dfakrypaql sggqqqrvgv aralatnppi mlfdepfsal daitrqklqv
      181 evkqlhqqlk dktfffvthd inealylgdr vmvmnqgnie qfaspqevvn hpaseyvknl
      241 idtvrtnqkl wenlk
//
LOCUS       WP_007127639             290 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Paenibacillus].
ACCESSION   WP_007127639
VERSION     WP_007127639.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 290)
  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 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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..290
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33684
     Region          35..287
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <184..284
                     /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 mdhtlrepmt mpdpqfpikv hlcqfegrgq vmfnrhyheh leilyfvsge amlecgsstl
       61 haregdlivi nrnelhygis qsdhlfyyal ivdfsllqsh sldapemkfi tpitqnrlvf
      121 anrvngddvl ssmlaiiqel ekrefgyela ikselyrllt lllrgyvatv ltqdeyverm
      181 knverfapif kyieehykee lsvellsgma glsryhfsrl fkelsgrtvt eyvnetrink
      241 adyllrsspl tvseiavatg fkdiyyfsri fkkykrlaps flrknsavsh
//
LOCUS       WP_007128650             190 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Paenibacillus].
ACCESSION   WP_007128650
VERSION     WP_007128650.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..190
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20902
     Region          2..186
                     /region_name="VdcB"
                     /note="non-oxidative hydroxyarylic acid decarboxylases
                     subunit B; NF041206"
                     /db_xref="CDD:469110"
ORIGIN      
        1 mklivaitga tgamfgvrll qflkstdvet hlvlsswaaa tiqsetpfta kevskmadys
       61 ysnkdlgsri ssgsfqvdgm ivipctmktl asiriglgdn liaraadvil kerkklvlvt
      121 retplndihl enmlflsrmg tvilppmpaf ynhpqslddv vnhivfrtld qfgihmpeae
      181 ekrwggmlpn
//
LOCUS       WP_007128966             200 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Paenibacillus].
ACCESSION   WP_007128966
VERSION     WP_007128966.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 200)
  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 200)
  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   3  (residues 1 to 200)
  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   4  (residues 1 to 200)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 200)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..200
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22485
     Region          32..200
                     /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"
ORIGIN      
        1 mrrllliheh vahaskpnqa saeasavaee nlseggyhvy tacsaadlpr cihevdaavv
       61 hlpiakiagw qrnleklrpv pmlwwcssys gtssadycqd dapidgiltp smspselhwa
      121 lhvgakqfld rqqwhterqq lrskleerkw idmakgilsd inriseaeay dmlrrkamne
      181 rkrivdvats ivkahqqlka
//
LOCUS       WP_007128973             276 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Paenibacillus lactis].
ACCESSION   WP_007128973
VERSION     WP_007128973.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus lactis
  ORGANISM  Paenibacillus lactis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Paenibacillus lactis"
                     /db_xref="taxon:228574"
     Protein         1..276
                     /product="formate/nitrite transporter family protein"
                     /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=29067
     Region          2..263
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msyvkpdqvv eamiqagtsk sqltveqmll rgflggallg fattlaftat aqtgigmaga
       61 llfpagfvii vllglelvtg nfaliplavm erkttalrml vswtwvfigh ligsvfygll
      121 yyaavtqfgh vqeggvidli rgaaeaktig yaslgwagmg tvfvkamlcn wmvclgavma
      181 nasrstggki aamwlpivif fgqgfehavv nlfviptgml mgagvslgdw wlwnqipvtl
      241 gniaggflft glalyltqkk paappvaeln sshkas
//
LOCUS       WP_007128887             684 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein/permease
            [Paenibacillus].
ACCESSION   WP_007128887
VERSION     WP_007128887.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 684)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 684)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 684)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..684
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=73181
     Region          1..670
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mgkdllgyrg akttfllvav ctlaqsmail lqakwlaqtv salfagaslq eqggtialfl
       61 laflmrhgvg avqqgiaqrs aeqtgtslrk ellgvlfrrg palirkegtg nvvtlvlegi
      121 gkfrkyaelt iprmmgagit palvwlyvfm tdrisgiill vtmpiliafl ilvglaarkq
      181 terqldsyrm lsnhfvdslr glmtlkflgq srkhsgsirq vsedyrkatm rtlrvaflss
      241 faldfftmls vasvavnlgl rlingsiell pallvlilap eyflpvrmvg adfhatldgk
      301 qageamqsii rasraeetgk peavetaryt gavgfgeaav ahsgvgeaag gagwihtada
      361 aadaegavpk ttdtaiarat naakvetint amgmtadaph aattdtarkv gtplsapilk
      421 ikdsstncgs spavfrwddc smlelsgvgl rheehgpasl edvsfripgk grigivgesg
      481 agksslidll ggftaptage irlngvtled gnreawrsgv tympqhpylf sstlednvrf
      541 yapdasdadv raaveaagli dlvralpngl hemigaggra lsggqaqrva larallggrq
      601 vllldeptah ldieteyelk etmlslfrdk wvflathrlh wmqdmdviiv lhrgrvaetg
      661 theelmqlkg vyyglitsqm egig
//
LOCUS       WP_007129821             200 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Paenibacillus].
ACCESSION   WP_007129821
VERSION     WP_007129821.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..200
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21725
     Region          6..200
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 meavrrkswv vgitgasgsi ygvrltesll slgydvhlvi tnagwrvlke emgfeaasre
       61 aavlerfggy egqivyhpia digatiasgs ylvegmiimp csmgtlssva hgasdnlmgr
      121 aadvmmkegr plvlvpretp lhaihlenml tlarlgvkii pampafyfgp qtlddivnfm
      181 vgkvldslri ehhlykrwgd
//
LOCUS       WP_007129868             402 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Paenibacillus].
ACCESSION   WP_007129868
VERSION     WP_007129868.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..402
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44096
     Region          1..398
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mnilvinags sslkyqlynm tdesvlakgl verigmdssi lthkptgkqe vtevseileh
       61 ttairrvlgm ltneehgvie sidsiqavgh rvvhggesfk esalvdsevk aeirrlfdla
      121 plhnpasmmg iraaetnmpg vpqvvvfdta fhqtmpeksy lyaiprvlyn kykvrrygah
      181 gtshayvsqa aaeflnrpie elkiitchig ngasltavdg gksvdtsmgm tpleglmmgt
      241 rsgdldpaiv pfvmnkeelt vnevnsmlnk hsgllaisgi ssdmreiteg mekgepnttl
      301 afnmyeyrlr kyigsyaaam ngvdvivfta gvgensivlr kkvleqltyl gveldeelns
      361 irsgeprris tanskvevlv iptneelvia rdthrivqal yr
//
LOCUS       WP_007130366             313 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Paenibacillus
            lactis].
ACCESSION   WP_007130366
VERSION     WP_007130366.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus lactis
  ORGANISM  Paenibacillus lactis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 313)
  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   2  (residues 1 to 313)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Paenibacillus lactis"
                     /db_xref="taxon:228574"
     Protein         1..313
                     /product="aminoglycoside 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=36807
     Region          19..269
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mqriqsimkn hygieisgvr pqqggwaala fkvsddrray flkqyeksra stpkwtaair
       61 eyipilawls eqesfrgkvp vpvqtldgqy rcedehgiyl lfeyiegeti seneltgeqv
      121 kqlseivsel hllgeeipys tqgiresfev pflrkledrm qeglpddmea aiaparshlv
      181 kgmrtvrtls erlagrnlrm alchmdlhhw nlmqsgdelv lldwegmkla pvesdlmfmt
      241 dtpyfeqfmh iyrsrhngyq mdedalrfyq irrrlediwe fmeqllydeq aeeerrntld
      301 slrkellefe aei
//
LOCUS       WP_007130522             347 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Paenibacillus lactis].
ACCESSION   WP_007130522
VERSION     WP_007130522.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus lactis
  ORGANISM  Paenibacillus lactis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 347)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Paenibacillus lactis"
                     /db_xref="taxon:228574"
     Protein         1..347
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=39510
     Region          <97..334
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 micdncstfe aiedrgrtvh mkparqelvr llaqngytvq ehnescavny kersdlisim
       61 eclqslprnl cdelsfcvtg geapktrhiw tpmqrfelqm ehydmvnvil hkeftsymqp
      121 ivdpsehiva yefllrplkg gipfkphelf etarktglqv fldqaartsa ietsaqwlpk
      181 gvkrfvnflp ssiydaqmcl nhtfhtierl gldpgdfvfe vvetekvddv ghlqsifeay
      241 rshgisvamd dvgagystle qmiklkpdyv kidrslidgc dqnptqqrql vtithmahef
      301 gamvlaegie rreefhfcre igielsqgyl fgkpsqrppc gpepqli
//
LOCUS       WP_007133606             498 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Segatella salivae].
ACCESSION   WP_007133606
VERSION     WP_007133606.1
KEYWORDS    RefSeq.
SOURCE      Segatella salivae
  ORGANISM  Segatella salivae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Segatella salivae"
                     /db_xref="taxon:228604"
     Protein         1..498
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54855
     Region          5..498
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mkqtaylqin kndnvvvclr amlvgeeikt shgiihvlre tpaghkillh dtnqnepiik
       61 ygypighake plkagewvne kniktnlsgt leyeyqprim pleiehedrh fkgflrrnge
      121 vgirneiwiv ptvgcvngia erlarqleke tqlkgidgih awhhnygcsq lgddhentrk
      181 vlrdicqhpn aggvlvislg cennqpedfm kllgdydter irllitqqve gdeveagmni
      241 lrklyhkaaq dqreevsvdk lriglkcggs dgfsgitanp lvgafsdwli aqggttvlte
      301 vpemfgaeti lmnrcltpql fqktvkmind fktyflehge pvgenpspgn kaggistled
      361 kalgctqkgg hapvcgvlsy gerievngln llsapgndlv aatalaasgc qmvlfttgrg
      421 tpfgtfvptm kistnsqlyq tkpnwidfna gelvegtemq tlrnkfidki lavangekvq
      481 nevngyqeia ifkngvtl
//
LOCUS       WP_007133863             309 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Segatella salivae].
ACCESSION   WP_007133863
VERSION     WP_007133863.1
KEYWORDS    RefSeq.
SOURCE      Segatella salivae
  ORGANISM  Segatella salivae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Segatella salivae"
                     /db_xref="taxon:228604"
     Protein         1..309
                     /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=36355
     Region          2..263
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mnkvkrnysi diargiailf vvswhcrvdn fgvtmwvmpl fffimgvfyh tpislklqir
       61 kktnqllipf viwsipyfiy ylftksflaf vkmwlnpyei mngpswfllc mfecyiiyyg
      121 ikkieveyrg llimllsiig fylgtyqlfg hhlklplfin ttltvipfay lgdllkdril
      181 peqktgreik lsvlllflfv mslynigmip idmywndyrq nyptflfnsl vgilliigis
      241 kfiptslavv grlsmlilvi hiyfyellkm ffshpivlfv avsalsifta wmidkyipyl
      301 sgkykylki
//
LOCUS       WP_007135344             107 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Segatella salivae].
ACCESSION   WP_007135344
VERSION     WP_007135344.1
KEYWORDS    RefSeq.
SOURCE      Segatella salivae
  ORGANISM  Segatella salivae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Segatella salivae"
                     /db_xref="taxon:228604"
     Protein         1..107
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12149
     Region          5..100
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(9..10,28..29,37,40,42..43,45,48..49,51,58,63,70)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(28,58..59,61,82)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mshfdsdtfr qevidivrqi prgrvltygl iarlagyplh arhvgkalhr vedkaipchr
       61 vvnsvgrttp dwpeqrllle kegvhfksng nvdlrhtlwe iashlea
//
LOCUS       WP_007136398             335 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Flavobacterium
            frigoris].
ACCESSION   WP_007136398
VERSION     WP_007136398.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium frigoris
  ORGANISM  Flavobacterium frigoris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 335)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Flavobacterium frigoris"
                     /db_xref="taxon:229204"
     Protein         1..335
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36452
     Region          3..335
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 myhskiaglg yyvpsnvvtn ddlskiidtn dewiqertgi qerrhiipge dtttsmgvka
       61 aeiaieragv akedidfvvf atlspdyyfp gpgvlvqrdl glktvgaldv rnqcsgfiya
      121 lsvadqyikt gmyknvlvig sevhsagldm tsrgrgvsvi fgdgagaavl sreedltkgi
      181 lsthlhsegq haeelivkap gmggrwvtdi ladndpndes yfpymngqfv fknavvrfae
      241 vineglqand lqvsdidmli phqanlrisq fiqkkfglnd dqvfnniqky gnttaasipi
      301 alteawelgk iktgdtvvla afgsgftwgs aiikw
//
LOCUS       WP_007136477             117 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Flavobacterium frigoris].
ACCESSION   WP_007136477
VERSION     WP_007136477.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium frigoris
  ORGANISM  Flavobacterium frigoris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 117)
  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 117)
  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   3  (residues 1 to 117)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Flavobacterium frigoris"
                     /db_xref="taxon:229204"
     Protein         1..117
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=13895
     Region          13..114
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mlrelffsna kklrenptqa eevmwlslsn nqldgykfrr qhpllnyvad fychqlklvi
       61 eidgeyhqtv eqkkldkert lniefqglyv irftnsevll didsvlskik efikiee
//
LOCUS       WP_007136605             352 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Flavobacterium
            frigoris].
ACCESSION   WP_007136605
VERSION     WP_007136605.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium frigoris
  ORGANISM  Flavobacterium frigoris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 352)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Flavobacterium frigoris"
                     /db_xref="taxon:229204"
     Protein         1..352
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38784
     Region          1..352
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mkikitgigs yvpekkvsnt dfgnhvflne dgtpfgkpnd iiinkfkgit giefrryaed
       61 nlnssdlafm aaqkaianag idpetidyii fahnfgdvky gttqsdmlps latrvknklq
      121 iknpksvayd ilfgcpgwie gvlqanayik sgmakrclvi gsetlsrvvd dhdrdsmiys
      181 dgagaaiiea sddeagmlsy esgtyamdea nylffgksyn tdldpdtryi kmhgrkiyef
      241 alttvpaamk scldksgiai ddvkkilihq anekmdeaii qrfyklhdrp vpqdimpmsi
      301 selgnssvat vptlfdllir geiknqsiqk gdvllfasvg agmnvnafvy ry
//
LOCUS       WP_007137121             109 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Flavobacterium frigoris].
ACCESSION   WP_007137121
VERSION     WP_007137121.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium frigoris
  ORGANISM  Flavobacterium frigoris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Flavobacterium frigoris"
                     /db_xref="taxon:229204"
     Protein         1..109
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12008
     Region          1..105
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(6..7,25..26,34,37,39..40,42,45..46,48,56,61,68)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(25,56..57,59,85)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mandnfferv ysiakqipyg kvtsygaiar algtarsarm vgwamnaahg lddvpahrvv
       61 nriglltgkf hfegtnlmqq llesegievv dnqivdfekh fwapdvmeg
//
LOCUS       WP_007137632             238 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Flavobacterium frigoris].
ACCESSION   WP_007137632
VERSION     WP_007137632.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium frigoris
  ORGANISM  Flavobacterium frigoris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 238)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Flavobacterium frigoris"
                     /db_xref="taxon:229204"
     Protein         1..238
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=26265
     Region          64..224
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 miykfcpavl llilsfspgn lffsetknvk eiakviktss etneeaiyns lnsnqfalpq
       61 lesfkealkg fyilkekgli skniltlidf smssnskrlw vidlttntil ynslvahgrn
      121 tgnefatsfs nspqsfkssl gfyatgeiys gkhgnslkld glekginsna reravvihga
      181 eyvsnsfiqn nkrlgrslgc palpleltdk iiqtikdksc lfiyfpsdsy kgasklis
//
LOCUS       WP_007137804             295 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Flavobacterium frigoris].
ACCESSION   WP_007137804
VERSION     WP_007137804.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium frigoris
  ORGANISM  Flavobacterium frigoris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 295)
  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   2  (residues 1 to 295)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Flavobacterium frigoris"
                     /db_xref="taxon:229204"
     Protein         1..295
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33972
     Region          166..224
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
     Region          227..292
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mdfkkaafyf kfsksqqtgi lflfaiivif qgvyffdnad svekdspekq kwlsmqaeid
       61 slnqsnskiv skiypynpnf itdykgyklg msveeidrll afrkenkyvn sanefqavtn
      121 vsdsllkvma vdfkfpdwvk nreaykknvn yekkdfvqkh vvvlsdinka tqedlikiyg
      181 igevislril rlkeslggfv smeqmkdvwg lsaevidnln shfkimavpk idkidinnas
      241 lkelakfpyf kygvaksivt yrsmngdfks fedlakindf pveklkiiel ylafn
//
LOCUS       WP_007138132             300 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Flavobacterium frigoris].
ACCESSION   WP_007138132
VERSION     WP_007138132.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium frigoris
  ORGANISM  Flavobacterium frigoris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Flavobacterium frigoris"
                     /db_xref="taxon:229204"
     Protein         1..300
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=33799
     Region          76..231
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkkyfyylif avaitscatn pykasekeyd tklktfkevi snkepeplpv vtktiisidn
       61 aytkqlytfk dtiskmgsta ldngiqtkwi stvnfnlrkp nfiiihhtaq dslqqtiktf
      121 tltrtqvssh yviaddgsvv qmlndymraw hagkgswgkd tdlnsssigi eldnngiepf
      181 seaqitslma llsklkkeyn iptqniighs diapsrktdp svlfpwktla engfglwade
      241 tlepapiafn ieqglriigy dtknlssaim afklhfiqte indildekti ntiysiykkq
//
LOCUS       WP_007138258             394 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Flavobacterium frigoris].
ACCESSION   WP_007138258
VERSION     WP_007138258.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium frigoris
  ORGANISM  Flavobacterium frigoris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Flavobacterium frigoris"
                     /db_xref="taxon:229204"
     Protein         1..394
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43573
     Region          14..392
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkiiiinsgs ssikyqlinm ptqevicsgm idrigldtsn ltyvtsntkl desllianhk
       61 iglekiaqll mddrigviks tqeidaighr vvhggatfsn tvvineevke kirqlfdlap
      121 lhnpanlegi dvaqeifata kqvavfdtaf hqtipviayk yaipskllte kkirvygfhg
      181 tshkyvseka ieyleksski isihlgngcs mtaiqdgksm dhtmgfspsn glimgtrsgd
      241 idhslifyli ntlgytptev nnlllkesgm lgltgysdlr diesnaekgn vdcqlalamn
      301 ayrirkyigs ytaamnglda iiftagigen ssyirklvct dmdyfgieid mekneirske
      361 ireintltsr tkimviptne eleisnqvyn llln
//
LOCUS       WP_007147135             413 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Scardovia wiggsiae].
ACCESSION   WP_007147135
VERSION     WP_007147135.1
KEYWORDS    RefSeq.
SOURCE      Scardovia wiggsiae
  ORGANISM  Scardovia wiggsiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Scardovia.
REFERENCE   1  (residues 1 to 413)
  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 413)
  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
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 413)
  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   5  (residues 1 to 413)
  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   6  (residues 1 to 413)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 413)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 413)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Scardovia wiggsiae"
                     /db_xref="taxon:230143"
     Protein         1..413
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43561
     Region          24..58
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          81..382
                     /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 mrnpftgsqs slreankall fdtiqkfgsl tqvelaentg lstatvsnlv rqlvddgvfe
       61 tsssirsgrr aslvsisrre gitagfcigv rsldlcitds antllaqhsl plgarhqads
      121 tlersavllk etltsidasa deligigvgl sapvdyklqr isvsgilpgw edvdihgyys
      181 sifhvkttid ndanlaalaq lrlsspeere adfvfinagd gigsgivvng qimrgatgma
      241 geighiqvdp lggvcscgnr gclntvvneq rlvsllavth gnittlddli eqansgdagc
      301 rrvisdaalr igtavadlci svdpeviilg gklaaardsf fdsfqesvqr llfpevltpi
      361 kiiladpslt rpergaallg lesassisri kldsiaaqdv dtgtarkegp hdr
//
LOCUS       WP_007147365             408 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Scardovia wiggsiae].
ACCESSION   WP_007147365
VERSION     WP_007147365.1
KEYWORDS    RefSeq.
SOURCE      Scardovia wiggsiae
  ORGANISM  Scardovia wiggsiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Scardovia.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Scardovia wiggsiae"
                     /db_xref="taxon:230143"
     Protein         1..408
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43749
     Region          3..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 maktvlvins gsssikyqlv dlengeglas glvekigept dgiythkfng ekhtftekie
       61 nheqglkkvl gffdefgpnl kdyelvavgh rvvqggyifp tpalvtpati qqvkdlavla
      121 plhngpeaig aevmtrllpd vpqgfvfdss fffelpeass tyalnkevae kyhirrygah
      181 gtsheyigsv vpetvgkpae glrqivlhig ngasasaqvs grpvetsmgl tpleglvmgg
      241 rtgdidpavv fhlirnahmd vdqldtlfnk esgmmgltgh gdmrdvddlr shgdkdaqla
      301 fdiyihrivs yigaytaqmg gcdvitftag vgendasvre avcdklapfg vkldkeknav
      361 rsgdprvisa pdssvtiavi ptneelaiar kvaklaeegd aygnvfgr
//
LOCUS       WP_007147374             234 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Scardovia wiggsiae].
ACCESSION   WP_007147374
VERSION     WP_007147374.1
KEYWORDS    RefSeq.
SOURCE      Scardovia wiggsiae
  ORGANISM  Scardovia wiggsiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Scardovia.
REFERENCE   1  (residues 1 to 234)
  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 234)
  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   3  (residues 1 to 234)
  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   4  (residues 1 to 234)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 234)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 234)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Scardovia wiggsiae"
                     /db_xref="taxon:230143"
     Protein         1..234
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=25824
     Region          14..234
                     /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"
ORIGIN      
        1 mvaeektdte glptvvvaed ealnrldiie slnengynvi geaangqeav drvrelkpdi
       61 vvmdvkmpek dgitaareln edflapvvml tafsqkdlva eavdagvmay vvkpfvperl
      121 fpalavaqer fkqmkalrdr isgipdsgas sadaseslaa adkeiqdlre qvdelknrle
      181 srkhvdkakg llmqhmglte qeafrwiqkt smdrrltmme vadavvqqie esrg
//
LOCUS       WP_007147814             242 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Scardovia wiggsiae].
ACCESSION   WP_007147814
VERSION     WP_007147814.1
KEYWORDS    RefSeq.
SOURCE      Scardovia wiggsiae
  ORGANISM  Scardovia wiggsiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Scardovia.
REFERENCE   1  (residues 1 to 242)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Scardovia wiggsiae"
                     /db_xref="taxon:230143"
     Protein         1..242
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=25574
     Region          120..242
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(188..189,192,215..218,220)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 migkphiraa dwrahkhdfa alvvgmiaaa ciilgaaigi irlfqssqqg rtpndagitt
       61 lsssatpgnt aqsarsakpa rssgsaakta epkapgrkid whgptggvqp nladygdlsi
      121 dvdlkkqrvy vksngqtiyt miastgmdnt tptgnfvagg yapnprgasf yntaermgaq
      181 nwicihdnil fhsvptding eyitseaekl gspashgcir lsiadskwly dqlptgtpih
      241 iy
//
LOCUS       WP_007148177             191 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Scardovia wiggsiae].
ACCESSION   WP_007148177
VERSION     WP_007148177.1
KEYWORDS    RefSeq.
SOURCE      Scardovia wiggsiae
  ORGANISM  Scardovia wiggsiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Scardovia.
REFERENCE   1  (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   2  (residues 1 to 191)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Scardovia wiggsiae"
                     /db_xref="taxon:230143"
     Protein         1..191
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19308
     Region          128..188
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mtpaqavcii lilvtglcas ltlliiqsss irslqqavgi aasdrsrgtg rhqdhqekdg
       61 dvaqhgtgds gntgsaagqa eeseqsrtlq qeaerkggaa gmsgqpsqga glsgnggnpg
      121 ssgkqdmrin insaseeqle tvkgigpsta kkiiayrtsh grftsvdell nvagigaktl
      181 akirgsisvs g
//
LOCUS       WP_007148593             115 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [unclassified
            Alcanivorax].
ACCESSION   WP_007148593
VERSION     WP_007148593.1
KEYWORDS    RefSeq.
SOURCE      unclassified Alcanivorax
  ORGANISM  unclassified Alcanivorax
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alcanivorax.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 115)
  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   3  (residues 1 to 115)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="unclassified Alcanivorax"
                     /db_xref="taxon:2638842"
     Protein         1..115
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12393
     Region          1..115
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mkmpggrsgi lslsikdkav lysaympfit ngglfiptek qyklgeeifl llnimdeadk
       61 ipvagkviwi tpkgaqgnrs agigvqfsdq ddtarvtien hlagslesdr pthtm
//
LOCUS       WP_007149487             343 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Alcanivorax sp. DG881].
ACCESSION   WP_007149487
VERSION     WP_007149487.1
KEYWORDS    RefSeq.
SOURCE      Alcanivorax sp. DG881
  ORGANISM  Alcanivorax sp. DG881
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alcanivorax.
REFERENCE   1  (residues 1 to 343)
  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 343)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 343)
  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   4  (residues 1 to 343)
  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 343)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Alcanivorax sp. DG881"
                     /db_xref="taxon:236097"
     Protein         1..343
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38714
     Region          32..199
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          268..340
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mttspspans qasnpshyar liarelglqa pdlgrllpnt glsveqllde dslltgqqqv
       61 qllnnalsis ddpafgfrlg rrltpathga vgflalssan lfealqaihl faptrmnfvr
      121 ielfdrgdwl ecyghfdmtl tdqmrrclte afimmffeta esilgrpahe vetlidypap
      181 pyapfyneyl pgpyefsaen fiakipkalc fypniaanhe nyqlalqqce tmlselrtnt
      241 qsfryrvekm mlsfppgtla eeeaaaalfm skrtlarklk nentgfrqiq kdilsqqaan
      301 ylrdskltvd aiaallnyhd ssnfrrafkr wfsvtpetfr qsl
//
LOCUS       WP_007149450             427 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Alcanivorax sp.
            DG881].
ACCESSION   WP_007149450
VERSION     WP_007149450.1
KEYWORDS    RefSeq.
SOURCE      Alcanivorax sp. DG881
  ORGANISM  Alcanivorax sp. DG881
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alcanivorax.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 427)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 427)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Alcanivorax sp. DG881"
                     /db_xref="taxon:236097"
     Protein         1..427
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=46710
     Region          21..418
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mtfkpvrklt vtrtlatgqa vtvgvlaqnr qgvffqydad ylgrygnlsp fglkattelq
       61 lapkrphsgl hglfgdslpd gwgsllqdrv frqhgilpaq itamdrlafv gasgmgalsf
      121 sptseyqvas agdidlatlg meaqaffdgq teevladlva agssggarpk aqlyispdep
      181 drchtvarpg neawlvkfts rnlplgheeg lceavylrla gklgleppew rlfeapeqsg
      241 arawlgvkrf dwishhqkag rlhmhsacgl ldadfrtpsl dyedlikasr hlcrspavgk
      301 lqfrramfnl lacnqddhsk nwaflqddag ewtpapfydv tfsphpyqeh atayagfgkn
      361 pplkaiqala aragyakweq aqhdideavd vladfsvvar dfgvdggiak lisrqldksr
      421 kvygvsr
//
LOCUS       WP_007149546             342 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Alcanivorax sp. DG881].
ACCESSION   WP_007149546
VERSION     WP_007149546.1
KEYWORDS    RefSeq.
SOURCE      Alcanivorax sp. DG881
  ORGANISM  Alcanivorax sp. DG881
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alcanivorax.
REFERENCE   1  (residues 1 to 342)
  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 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 342)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 342)
  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   5  (residues 1 to 342)
  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   6  (residues 1 to 342)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Alcanivorax sp. DG881"
                     /db_xref="taxon:236097"
     Protein         1..342
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38322
     Region          34..217
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          111..340
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mnrdrfiqld pgtgrspvpv nyvrnlveli sdvgvdtrrl lrqvglteee vynpepalrf
       61 eqfrrvmvga rdmtgnpalg lalgqqltlt ahgllgyaai ssadlgdalr lleryfrtrt
      121 rlcvpriept tegvrfclle svplgdiret ylevvvaavv ggiryllger frgavlelpy
      181 appahaeryr ellqmpvefg aevaalrlph sllsepftls dpasrhmaaq kceeelqrle
      241 adqdwasrvr arlmqaegml psleqlagnf hvtsrtlrry lnalgvsyrs lleevrmtka
      301 maylqanitv qqvaiklgya dpsnfarafr kwtghppshf qp
//
LOCUS       WP_007149584             690 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Alcanivorax sp. DG881].
ACCESSION   WP_007149584
VERSION     WP_007149584.1
KEYWORDS    RefSeq.
SOURCE      Alcanivorax sp. DG881
  ORGANISM  Alcanivorax sp. DG881
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alcanivorax.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Alcanivorax sp. DG881"
                     /db_xref="taxon:236097"
     Protein         1..690
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=75491
     Region          13..690
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mfltarqpfi aclgvflplv tfaedqdayv ldavtvqaqp gptaqgkvdl ereqaltpgg
       61 vtlleaedlt ernvvsigdm lryvpgmwtg tgstgddtfi ssrgsnldav aydgngiklm
      121 vdglpvtaad gnnhnsfidp laaryaviar ganaltygas tlggainfis ptarntdnqi
      181 ylsggshgtv qsritaggve gdldglvtve qrsydgfrdh qeqqrgsvya ntgwqindav
      241 enrfyftyvd ndqelpgslt qaqfdddpyq anpnnipgnf lknveswrva nrtqwqlsdt
      301 snlvvgfsfe dqhlyhpive npffsllidn dqttfgtnir ydkqlgnhdl lfglnygetr
      361 vkggnyshtg girgaldvrv dnkadnleif amdrwhfadr wtliygaqav tgtrevdnvt
      421 vasgaernpk ddyesinprv gviyqvadrs elfanvskly eaptlyeled dadasdetln
      481 amqgvvgeig trgaaplgqa sewnwevsvy yaqledeils mdnpsasgts lalnvedtih
      541 agvealvgas falgndgqri epllsmtynd ftfdndpeyg dnqlpvaptf fikgevmyrh
      601 gngffagptf divddrygdf annkdvdgye llglrtgvtr dswevylegr nltdevyvtn
      661 vsvsndetin pvgiqagepr svyagvrfdf
//
LOCUS       WP_007150073             302 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Alcanivorax sp. DG881].
ACCESSION   WP_007150073
VERSION     WP_007150073.1
KEYWORDS    RefSeq.
SOURCE      Alcanivorax sp. DG881
  ORGANISM  Alcanivorax sp. DG881
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alcanivorax.
REFERENCE   1  (residues 1 to 302)
  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 302)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 302)
  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   4  (residues 1 to 302)
  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 302)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Alcanivorax sp. DG881"
                     /db_xref="taxon:236097"
     Protein         1..302
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33808
     Region          49..302
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <185..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 mmseqrqtae tsrwplpasg qrtvippavl ssvsqhplca gcmphgvgfy pqahghrmar
       61 qqpaddlliy cvagagtvty egqsqpveag elllfpagla hhyqanpqqp wsiywvhlgg
      121 hevqayfdei agqpqsgirk vnvgvhsrla edfqtlmaaa tntqpehlmy aanllrslla
      181 yaalmrrqhq vrhatldvnr vnsylqtaia rrlsldalia atsdlsryhf ireykrqtgq
      241 tpmqafqrik vshacylldi sehsvaaial qlgyddpyyf srlfkkvmrv spqqyrqerg
      301 kn
//
LOCUS       WP_007150707             331 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Alcanivorax sp. DG881].
ACCESSION   WP_007150707
VERSION     WP_007150707.1
KEYWORDS    RefSeq.
SOURCE      Alcanivorax sp. DG881
  ORGANISM  Alcanivorax sp. DG881
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alcanivorax.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 331)
  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 331)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Alcanivorax sp. DG881"
                     /db_xref="taxon:236097"
     Protein         1..331
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36935
     Region          18..200
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          249..329
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtpdlamtyc rmiaqtlgld qagleklvad tgvdvdtlqh sdgfidwpga cqlisnarql
       61 sdrpdialqt glralpamhg pmgmaamasp tlrdamqlfa rfintrtqvf ttvfeeqqdt
      121 itlrqefayp lddnvqflve svmasafach vvlrgksidg gevhfnypap dyaecyaqtf
      181 pgtrlvfdaa ytaiklpary gdetlpshdr dllwiaieqc earqealrnr gtvsdqvlal
      241 lhqhhgkasl dtvadqlhms prtlirklkq entrfqqlrd qtlsrraaql lglphytvaa
      301 vaedlgytdv asfrrafqrw fgttpgsfrr e
//
LOCUS       WP_007151306              98 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Alcanivorax sp. DG881].
ACCESSION   WP_007151306
VERSION     WP_007151306.1
KEYWORDS    RefSeq.
SOURCE      Alcanivorax sp. DG881
  ORGANISM  Alcanivorax sp. DG881
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alcanivorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Alcanivorax sp. DG881"
                     /db_xref="taxon:236097"
     Protein         1..98
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10776
     Region          1..97
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(5..6,24..25,33,36,38..39,41,44..45,47,55,60,69)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(24,55..56,58,83)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mnpefrdavy qivaaippgh vssygavakq agfprharfv grlmsqlpkd trlpwhrvlr
       61 adgcialagt psgeiqtqrl ldenipvlgd rvprqyfi
//
LOCUS       WP_007151827             339 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Marinobacter algicola].
ACCESSION   WP_007151827
VERSION     WP_007151827.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter algicola
  ORGANISM  Marinobacter algicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 339)
  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 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 339)
  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   4  (residues 1 to 339)
  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 339)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Marinobacter algicola"
                     /db_xref="taxon:236100"
     Protein         1..339
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38879
     Region          22..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          252..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mseltvsrhf veaalvgaek agidthtllr eagispdllk iemarvsstq ysrlmqaawn
       61 amddefmglg prrcrtgtfa tmcalvidcp nleavyrqaf dfcrlfepmv tmklevedkt
      121 arlvtaiegd indpmhffre silviwhrlg swligqpvel lkaefsyprp phgdeyrhif
      181 hcplsfease taltfdkrfl qapvirdkpe mrqflktspa dllsrpdesn tftgrirali
      241 grdfarslpd fewiatelht spqtlrrrlk qentsfqeik dllrrdmaiy ylsrpdlpin
      301 diafrvgfte pstfhrafkk wtgvtpgayr egergqlqd
//
LOCUS       WP_007151858             352 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Marinobacter algicola].
ACCESSION   WP_007151858
VERSION     WP_007151858.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter algicola
  ORGANISM  Marinobacter algicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 352)
  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 352)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 352)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 352)
  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   5  (residues 1 to 352)
  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   6  (residues 1 to 352)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Marinobacter algicola"
                     /db_xref="taxon:236100"
     Protein         1..352
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38664
     Region          30..206
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          103..345
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkpntrhknp lgdisvlyva vmtralraeg raptdlldrf gldeqalgap aarisiprfm
       61 rmgqaaialt gnpafgltmg qlsrpvdagi aglaaqsaat ageaistliq yslltsrnsr
      121 gapwtvsqgr eahfysikpy nvfnffvvds vlaawvqflr ditghdrvve risieypsqg
      181 ydevfeqwfg cpvrfgaesn slrlapgive aaslqaqaam feslsgqcal elsriragws
      241 madrvkdqlp pllqggtptl mavahklgva pwtlqrqlae entgfrelvd dtrkelavey
      301 iretrvslse iswllgfanp aafhkawrrw fntspgehrk qylaeqaakg if
//
LOCUS       WP_007151914             344 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Marinobacter algicola].
ACCESSION   WP_007151914
VERSION     WP_007151914.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter algicola
  ORGANISM  Marinobacter algicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 344)
  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 344)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 344)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 344)
  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   5  (residues 1 to 344)
  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   6  (residues 1 to 344)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Marinobacter algicola"
                     /db_xref="taxon:236100"
     Protein         1..344
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38934
     Region          34..206
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <143..344
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          261..339
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mertvetssp malevplisa ryarqfirfm erkgvrrhai lgdtdissdm lddpdaslsm
       61 gqvrqllgka ewlmgderaa fqfgqqldlp ahgllgfavl gqenprrlis mivqylrvgl
      121 plmdmdlsst gstfriqlid nwglgdlrpc ltkiymgsih rissqvckhf cfefdfdssl
      181 epeqwrsiat dcefrfnapa nqvtmplsgr pirnddtgle filanarsre repseqadet
      241 vmqvremims qpgrpcamdn larrldmspr tlrqhlstag tsfrtlrnei rqnfatlylt
      301 dtaipldsia eklgfsdqag ftkayrswtg qtpgdvrrqa rdrk
//
LOCUS       WP_007154081             292 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Marinobacter algicola].
ACCESSION   WP_007154081
VERSION     WP_007154081.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter algicola
  ORGANISM  Marinobacter algicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Marinobacter algicola"
                     /db_xref="taxon:236100"
     Protein         1..292
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31673
     Region          11..282
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mtitqeadfc idlhchttas dgalppkelv arahargvth laitdhdtia gleeaseaar
       61 eagltliagt elsclwksht ihvvgldfdv dderlkqale rqnknrwsra rtitdklskl
      121 kienllekat dkavgdvpgr phfarvlvee gvvkdiaqaf krylgagkag dvkgfwpelp
      181 evvrwiteag gvavlahprk ykltatklra lvadfrqagg rsievstsgq ssgdlgflae
      241 lcrrenllas qgsdfhfpga pwcelgaimk mpdglepvwh hfkqpagvpa av
//
LOCUS       WP_007153954             720 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Marinobacter algicola].
ACCESSION   WP_007153954
VERSION     WP_007153954.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter algicola
  ORGANISM  Marinobacter algicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 720)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 720)
  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   3  (residues 1 to 720)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..720
                     /organism="Marinobacter algicola"
                     /db_xref="taxon:236100"
     Protein         1..720
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=77043
     Region          6..720
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 maldadeeil qdflveagei leklseqlvd leqnpddsdl lnaifrgfht vkggagflql
       61 dalvncchsa envfdilrnh krkvdselmd vvlealdhvn amfeqvrhhe eptpapeeli
      121 aaldalaqpa gepapanaav aseeqngsde agsgddggdi tddeferlld aleeekssap
      181 dssgdaness sgdggsgddi sddefealld qlhgkgqfsg ppesgkaapd sqdtsaakva
      241 gdeasdskgg ddlisddefe kllddlhgkg gsptaetaks tpppaakqpa aksvdaktdk
      301 spqpagkpek apaengkagv tpampardan apvaetsvrv dtkrlddimn mvgelvlvrn
      361 rlqrlgaqse dehmhkavsn ldvvttdlqs avmatrmqpi kkvfgrfprv vrdlarslkk
      421 einlemhgee tdldknlvea lsdplvhlvr nsvdhgieap dvrekagkpr qgrvtlsaeq
      481 egdhillsie ddgagmdpdv lrrkavekgi yeqdaadrlt ntecynlifa agfstkeqis
      541 dvsgrgvgmd vvktkisqln gqlsveselg kgsrivikvp ltlaimptlm imlgdqsfal
      601 plvnvveifh ldlskknivd grecivvrdk vfplfhikrw lvkgaagqpe penahvviva
      661 mgtrrvgfvv dqligqeevv ikplgralqg tpgmagatit gdgrialiid vpsllqnygk
//
LOCUS       WP_007154943             679 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Marinobacter algicola].
ACCESSION   WP_007154943
VERSION     WP_007154943.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter algicola
  ORGANISM  Marinobacter algicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 679)
  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 679)
  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 679)
  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 679)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..679
                     /organism="Marinobacter algicola"
                     /db_xref="taxon:236100"
     Protein         1..679
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=72126
     Region          1..665
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 msqetaiylk tngewqptrm sgprallwli aligiglslf qlysagiqpl glfyqrgihl
       61 alvmmlcfll fgprpgrprg vitalidtgf liasgasgfy lvwfldeitg ragfwnqtdi
      121 vmawvctitl leasrravgt gltvigviai lyamsgqrgp lselgewlpg ilnhrgysld
      181 rigaqlylgq egifglplgv aatfvfifvl fgamlevtga grffidlafa atgrqrggpa
      241 kaavlasasm gsisgsaian vvttgaftip lmkklgfrpa qaggieaaas tggqimpplm
      301 gagafliaey trvpyldivk vsvfpallyf atvyllvhic avkqgmkglp asdlpqlrev
      361 maygwyfllp iimlvyllvm gispmrvgfy avvgiigiag lnglylaykq gradnqlgka
      421 ltdalregvv kllqglelga rnavpvsiac aiagivvavv gltglglkfs smmiafadgn
      481 ilmalflvvi aslilglglp vtasyivliv lvgpaltnef gipllvahll vfwysqdsnv
      541 tppvalaafa gaaiagsktm etsvqawkfa kglyliplfm vfnpviiegg plplvlwngf
      601 iailalaafa aalegflfth mkpwmrlals gaviaifypd lqvevagvva mlallamnyw
      661 hrrrelhgag apeteeqsq
//
LOCUS       WP_007155701             302 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator, partial [Marinobacter
            algicola].
ACCESSION   WP_007155701
VERSION     WP_007155701.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter algicola
  ORGANISM  Marinobacter algicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 302)
  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 302)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 302)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 302)
  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   5  (residues 1 to 302)
  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   6  (residues 1 to 302)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Marinobacter algicola"
                     /db_xref="taxon:236100"
     Protein         1..>302
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [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          23..209
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <163..302
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mktlgtasva alrqyvrtad aqgldtsalf tkagldssvl qtdderinge qfqafirlvc
       61 eeshnpilgl etgdfvqpgs ysvlgyitms satlgeavar iapfeklvgd mgttqiagsg
      121 dhikliwscn ytdpvarpqm vdnvfaswin yarwladnnt aspvevhlkh pspgpelesa
      181 yterwgcsvr fesdedaivl hkdllstplr qpdpllrktl eahalsqlat letdtaltnr
      241 vkhsirkqlm hgitrqdmva dhlgmtsrtl qrklsqegvs yqqlldevrq vmaedfltns
      301 dl
//
LOCUS       WP_007156274             307 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Oribacterium sinus].
ACCESSION   WP_007156274
VERSION     WP_007156274.1
KEYWORDS    RefSeq.
SOURCE      Oribacterium sinus
  ORGANISM  Oribacterium sinus
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Oribacterium.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Oribacterium sinus"
                     /db_xref="taxon:237576"
     Protein         1..307
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34542
     Region          <37..72
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
     Region          <154..280
                     /region_name="PspC_relate_1"
                     /note="PspC-related protein choline-binding protein 1;
                     NF033840"
                     /db_xref="CDD:411409"
ORIGIN      
        1 mnayqrgqka lcgdyfkytp tgasqfkrag rwykeakagd ivffyspamg riahvgives
       61 vegnkittie gntsgtqgdr nggecrrktl nnfsvggknw ingfarpvyg ddtctaqdll
      121 dvargeigye ekasphgled khanrgnkny tkygqwynng kalseywcae fvswcfykac
      181 asvdvptgwt yrlnnwyyfk dgvpvsgkfe hingrwyvfd nsgfmikgwf kseegwyylg
      241 edggmlssqw lqdkgkwyyl tksglmatna kvrkakgdgy dfvgadgayd sfkslftgrm
      301 egveive
//
LOCUS       WP_007157703             564 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Oribacterium sinus].
ACCESSION   WP_007157703
VERSION     WP_007157703.1
KEYWORDS    RefSeq.
SOURCE      Oribacterium sinus
  ORGANISM  Oribacterium sinus
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Oribacterium.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 564)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Oribacterium sinus"
                     /db_xref="taxon:237576"
     Protein         1..564
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=66479
     Region          19..252
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mslrkpkdke lesyieshie eaiekewiqv ylqtnirgls krvcgaeals rwidpvygmi
       61 spgefipvle kkrkiqlldr yvmeticrel gerrrrgqfi vpismnfsrl dfdvptllqe
      121 meeimeknsl prnyvhieit esavmeneay mkdtvrelht lgykvwmddf gsgysslnll
      181 kefefdtfki dmrflsdmgk ksliiissil ymakeigiht vaegveteeq yrflkvagce
      241 rmqgyyfarp epmkewfaht kescemetee dcylydeigf vniispvpfd lersdsspsi
      301 hgfetgqpva vmsemdgvlk hlnftkpyrk nllelgyegt hqfqdllndr silftdkmrd
      361 imdlarksgr ieamdflsgg rhcqfqtrlv arkgnknifl vrldilsnir rfqknkefqe
      421 alsplytvyd mvfvfdlken llnpvyvnei yegvhessnl rgeiekfven kvypkdkeac
      481 wqflnpdtma ervesaekdf ilayfrsknr kneyvwkrfv lirsherskq drvifgihtl
      541 nmdkvsmmhk edqqifqegd ffer
//
LOCUS       WP_007156725             693 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Oribacterium sinus].
ACCESSION   WP_007156725
VERSION     WP_007156725.1
KEYWORDS    RefSeq.
SOURCE      Oribacterium sinus
  ORGANISM  Oribacterium sinus
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Oribacterium.
REFERENCE   1  (residues 1 to 693)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 693)
  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   3  (residues 1 to 693)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..693
                     /organism="Oribacterium sinus"
                     /db_xref="taxon:237576"
     Protein         1..693
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76403
     Region          1..689
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          172..250
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 mdstmegmld tylleteall dkldemliad ekvgdfstdd vneifrimht ikgssammef
       61 tplsniahhi edmfffirdk gidslsgdqk selfdlmfrs edflrsglek vkageeldnn
      121 veefagsina flakisgkap adsapvveaa dstkasgenr nlpkddkakk fihvfldegi
      181 gmenlrafmi vnaikefdle fryypadmds npetaqtiid egfflafdsd edcekgekil
      241 reqshilsye pveatkaeak aevksanaes ssapkaskep aaaqqtaqqk aaapvkqsli
      301 svnlqkldsl ndlvgeivit esmvtsspvl rmlpqesldn fmksarqlrk ltddlqdiam
      361 slrmvsisgv fqkmnrivrd mkqklgkdvk ltiigedtev dktivdsiqd plmhivrnsm
      421 dhgieetkee riaagkdsqg elilsashts seviitvqdd gygmdpekll dkaeekgily
      481 kprseyskke alglimlpgf stntavtefs grgvgmdvvk knlesvggti sisseigkgs
      541 tftmkipltl aimdgmkvnv gdtiftipiv nirqsfkvdd sevvfdengn emvkrmdvfy
      601 piirlnnfyg iegkytdlqd gvliwveagd kscclfvddl igeqqvvvkp lpayfnaydl
      661 kssgingcsi lgdgniciil dvlglysqai eni
//
LOCUS       WP_007158151             617 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Oribacterium sinus].
ACCESSION   WP_007158151
VERSION     WP_007158151.1
KEYWORDS    RefSeq.
SOURCE      Oribacterium sinus
  ORGANISM  Oribacterium sinus
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Oribacterium.
REFERENCE   1  (residues 1 to 617)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 617)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 617)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Oribacterium sinus"
                     /db_xref="taxon:237576"
     Protein         1..617
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=68617
     Region          2..557
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mikmrlirll egagkyivqq ivwqwislla qvvivyniah llenawqkkl stegialtmg
       61 ivllglgfrf lcdrlytkas fhasadvkri lrnkiygkml algpayresv nsaeivqmag
      121 egveqletyf grylsqffys llapitlffi lsrisvqtal llllavplip ivimlvmiva
      181 kkllsnyfai yyglgdsfle klqgmttlki yqadqaaaed mdreaelfrk itmkvlsmql
      241 nstsvmdiia yggaavgiis algqfskgai slsdvlmitl laaefflpmr llgsffhigm
      301 ngmkasdrif afldlpeaed gkavleekei rismeklcfs yeesreilrd veleipaysf
      361 vslvglsgsg kstiagilmg knkgykgsvk lngreltefs srsvldkmtm ighdswifkg
      421 tvrdnlllgn pgateeemke alkkvnllsf ieaqgglamp llsngtnisg gqkqrlslar
      481 allhdtpvyi fdeatsnida eseerimevi helaksrtil lishrlanvv gsdcifmlen
      541 grvaeagkhe ellkkggsys rlfkeqkele ifsetrkess tekqkdtgfe eqgimedlqd
      601 ktgeredtve eggekhe
//
LOCUS       WP_007158483             290 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Pseudomonadaceae].
ACCESSION   WP_007158483
VERSION     WP_007158483.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonadaceae
  ORGANISM  Pseudomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Pseudomonadaceae"
                     /db_xref="taxon:135621"
     Protein         1..290
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31389
     Region          3..278
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mridlhchtt asdgafapae vvrrahergv qllaitdhdt ldgyaealea adglglrllp
       61 giemsctwgg atlhvlgynf apeapelnaa lealhegrwe rareidrrla akgmpgtldg
      121 aravqlalgd srnaparphf aeylvqagfv edrgdafrkw lgggklgdvk qhwptlaetl
      181 atlkgakawi slahplaygf trtklrklig efvtggghai evvngvqpae qvgtlailar
      241 efglmvsags dfhapadwse lgmyrplped lpplwarfsq plypqnrepq
//
LOCUS       WP_007158649             303 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Pseudomonas
            oryzihabitans].
ACCESSION   WP_007158649
VERSION     WP_007158649.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas oryzihabitans
  ORGANISM  Pseudomonas oryzihabitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Pseudomonas oryzihabitans"
                     /db_xref="taxon:47885"
     Protein         1..303
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32671
     Region          14..259
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mappeclfdh sdelgegpvw dtrqqrllwv dilagrllra apqpaapvev lefgrplgca
       61 vphvdgstwl alsdgvwrla agaaqatpva qppravhgpq hrfndgkcda lgrfwlgttl
      121 ldeapgggrl ycldldgqlh qvldgitvsn glgwspdnrt fyyidsptrr vqafdfdlas
      181 gqlgrgrtli dfgeqpgvpd glavdsegal wiahwdgyrl srwsaegvll awvelpvarv
      241 tscafygarl eqllittarv glddsarqaq plagrsfrld pgvtglavsa crvrvpdhpq
      301 esa
//
LOCUS       WP_007158935             347 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas oryzihabitans].
ACCESSION   WP_007158935
VERSION     WP_007158935.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas oryzihabitans
  ORGANISM  Pseudomonas oryzihabitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 347)
  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 347)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 347)
  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   4  (residues 1 to 347)
  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 347)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Pseudomonas oryzihabitans"
                     /db_xref="taxon:47885"
     Protein         1..347
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37658
     Region          27..211
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          256..338
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mstpalrlgd lstgfvlala aavdqrgada agllarfgls aarlaepggr lsiphymrlg
       61 haaleltgdl alglamgram rpaflglagv tvgqapdvrh aaetllrlep lygrnyrgrs
      121 ryaaqgrdaw lhfysispyn aynrfvvdav lgawlallgt vagqalqprr vlieypapad
      181 lapyatafgc pvefgaaena llldaatlsr pgpehcpatw rqllalsdae hgrltrtrgl
      241 tervvevmgp llrhgeptle qiasrlrlps wtlrrklaee gtqyrallnl trrdlalayi
      301 rdteasfgei ayllgfaspa afqrafkrwt eqtpgdwrrl qrqgvag
//
LOCUS       WP_007158976             613 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Pseudomonadaceae].
ACCESSION   WP_007158976
VERSION     WP_007158976.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonadaceae
  ORGANISM  Pseudomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales.
REFERENCE   1  (residues 1 to 613)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 613)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 613)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 613)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 613)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 613)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Pseudomonadaceae"
                     /db_xref="taxon:135621"
     Protein         1..613
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=67325
     Region          1..613
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mivlatgvvy gdigtsplyt lkevfsphyg lplnhdsvlg ilslifwsli wvvtlkyitf
       61 vmradnqgeg gimaltalar raaqgsprla ttlvllglfg aalfygdsmi tpavsvlsav
      121 eglelafdgl eawvvpialv ilvgifaiqk rgtatigkff gpvmvlwftt lgalgvygiv
      181 qqpevlkafn pywavqffad npvkgfivlg aavlaltgae alyadmghfg rkpiarawll
      241 lvlpglvlny fgqgalllad paavrnpfyl lapewlllpm iglatlatvi asqavitgaf
      301 smtrqaiqlg yiprmqiqht ssqeqgqiyi plmnwalmlg vifliltfqs sanlaeaygv
      361 avtgtmlits clvsavilll wkwprwimvp lligfllvdv lyfsanapki fsggsfpvia
      421 givifilltt wkrgrqlvve rlddgalplp ifissiraqp pfrakgtavf ltartdvvph
      481 amlhnllhnq vlheqvvllt vryedrprvs rgermevedf gdgfyrvvlh ygfmdepdip
      541 lalshcpypg ldftpmrtty flsretvias krlgmapwre nlfvflmkna ngnlrffklp
      601 vnrvielgtq vei
//
LOCUS       WP_007159021             792 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pseudomonas oryzihabitans].
ACCESSION   WP_007159021
VERSION     WP_007159021.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas oryzihabitans
  ORGANISM  Pseudomonas oryzihabitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 792)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 792)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 792)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..792
                     /organism="Pseudomonas oryzihabitans"
                     /db_xref="taxon:47885"
     Protein         1..792
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=86661
     Region          37..792
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mvspllfrpr aplrlatlgl ltalagcqyl geeqptrsqs qlkgslplrg laqtasvrrn
       61 adgqpliett tfhdalfalg ydhaserlaq mvelrllaqg rlaeaygesr ldsdrfmrav
      121 dlrkaaqvay gnasprmktf fevyargvna ylyraservq ldghdyraey wkpedsallf
      181 ellnfaqavd lrketaalal atqvgperla wllptypdep lpdeetaklr glnlrgqlpg
      241 leallqvqrq laeqapfggp tgtawaatpg htrsgrslla vdrvsavgqs pftlvtlrap
      301 rfeavgttlp glpllldgyn gklawgaatl mgdsqdlyle rlqrqggrlq vqsggqwqpa
      361 gervetffvr gekprretly tssrgpllnl alapdangyg lalrssrlea dksldalfdl
      421 srakdveraf elardlrasd wnlvfadaeh igwqvtgryp nrrsglgllp spgwderytw
      481 dgyadpmlhp ydqdpvqgwl gaanqrvvpr gygmqlssnw sgperqerla qlagrsarld
      541 grdamalqqd qtttlaaklk tqldspgfaa plrqaiaals agqrpqaeea lrrlqgfdgr
      601 laagsadaal yeaflqalae qtfadelggt gspawqaftt lsdtgynaiv dhllarddsp
      661 ywddvstaah edkpaifara laaavatcea rlgsdraswq wgrlhrqdgn ayggdgstld
      721 ltashwggnd qvwlapalrl vvdfglaepl qasqvgtpgk gwtrgqyqsl plqpqnlerv
      781 ygrdrlllip qk
//
LOCUS       WP_007159023             190 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Pseudomonas
            oryzihabitans].
ACCESSION   WP_007159023
VERSION     WP_007159023.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas oryzihabitans
  ORGANISM  Pseudomonas oryzihabitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 190)
  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 190)
  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   3  (residues 1 to 190)
  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   4  (residues 1 to 190)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 190)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 190)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Pseudomonas oryzihabitans"
                     /db_xref="taxon:47885"
     Protein         1..190
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21426
     Region          1..190
                     /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"
ORIGIN      
        1 mrilliddtp kqvgrlkaal ieagfeviee sgltidlpar iealrpdvil fdtqspgrdv
       61 meqvclvtrd rprpivmftd ehdpavmrra iqsgvsayiv egiqtsrlqa iidvararfe
      121 tdqalraelq areqqllerr kvdqakgllm kmrgcredea ytlmrrqams kqqkliqvad
      181 qiiamsellg
//
LOCUS       WP_007159268             801 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [Pseudomonas].
ACCESSION   WP_007159268
VERSION     WP_007159268.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 801)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 801)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 801)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            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="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86716
     Region          48..97
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          75..800
                     /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 mqlfslrlia lsvslgvatl aqaapvalsq paqpladalq sfarasglqv nydpaalvgk
       61 rapalagrme pdvalqrlla gtglaasvsg svatvapvat qaaagsvtld tttisaddgs
      121 lagrtttegt rsyttgamst stglplsire tpqsvsvitr qrmedqgmtd lndvvryapg
      181 vtlnkfggdr qeflsrgfri dnimydglpt tagtftldtl ssadlsiydr vevvrgatgl
      241 mtgagdpsat lnlvrkrpta fpqvsvttsa gswdryrtev dasnklneag tlrgravaay
      301 edgnsfqdvr erkrqtfygv leadlsdttt wtigaskqre dktsdwgslp sgpngedlhl
      361 srstflsgdw aywdqdtytl fsdithtfdn gwkaklaaqk swaesdtfsn yvtafpytsv
      421 sdlgtasgay vtdvdqtnvd lslsgpitll grehqlmtgl srredkfyqr ggysgvtpvd
      481 iynfqpsniv kpdkgslspy asknttteea vyaaarfnpl dplhviiggr iswfdysgyi
      541 agsnyrtdtd ykatrevtpy agivydlndi ysvyasytgi fkpqseqgsg gsvlaptkgk
      601 syevgvkgay ldgalnasva lfetiqegra yqltpqpqec qeqsrtcydt agevrsrgid
      661 aeisgqlapn wqasaaytlv lseftkdvty edrrfapeqp khlfkaatsy qltgnlskwr
      721 igadllaqse tfkrvgngea kqdsysvvgl magyrfndhw dgrvnfnnvf derywqglsn
      781 gtgmgtygdp rnvmlslkwt l
//
LOCUS       WP_007160453             244 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Pseudomonas oryzihabitans].
ACCESSION   WP_007160453
VERSION     WP_007160453.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas oryzihabitans
  ORGANISM  Pseudomonas oryzihabitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  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   3  (residues 1 to 244)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Pseudomonas oryzihabitans"
                     /db_xref="taxon:47885"
     Protein         1..244
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27662
     Region          37..242
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mqgssasdna aqppqvyrsk geilaclrpa qqqhiplrit fnrqgqqfqs fvveideakg
       61 lialdefipr eaerlleqgq sfrvdsfheg irvtwqidrp vefseldgnr cywiglptel
      121 tyhqrrnayr vkllltrpat aelsqgnsqi qlrgqlidls atgcklrfpg nvthllqpgq
      181 qvqsftaelp igaintpvti rhvacpdrle ysdvgvcfdn lsgaaqrqve rfiyqlqren
      241 rrfe
//
LOCUS       WP_007160062             262 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas oryzihabitans].
ACCESSION   WP_007160062
VERSION     WP_007160062.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas oryzihabitans
  ORGANISM  Pseudomonas oryzihabitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 262)
  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 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   3  (residues 1 to 262)
  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   4  (residues 1 to 262)
  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 262)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Pseudomonas oryzihabitans"
                     /db_xref="taxon:47885"
     Protein         1..262
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28913
     Region          1..255
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <151..256
                     /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 mnaayldals rarpadlpal laslslvapl ldaipgvvff vkdlearyvl vnltlaqrcg
       61 fedvsellgr taeevfpapl ggayaeqdrr vlreglaldd qlelhlyagr tpgwcltrkl
      121 plhdtqgrlm gmagishdlq apaadhpaha kvaevdrylr ehyaqplsvg elsqrvglsv
      181 sqlerqckri lrltpqqllh karldaasrl lardlpvtev alacgytdhs afsrqfrrlt
      241 glsprqyrds lkprsrleet pa
//
LOCUS       WP_007160546             289 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Pseudomonas
            oryzihabitans].
ACCESSION   WP_007160546
VERSION     WP_007160546.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas oryzihabitans
  ORGANISM  Pseudomonas oryzihabitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Pseudomonas oryzihabitans"
                     /db_xref="taxon:47885"
     Protein         1..289
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31267
     Region          13..261
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mdwqpllpqr fklaegpfwd qetqalywvd iagfkacrls gehyqewqld rpcsafvptv
       61 rgdalvtlpd gvfrldldsp pdrpalelfc vadpdpgnrg nearcdaqgr lwlgtmqnnl
      121 daqggdvaid rhsgglfrid pdgsvsrhas dlgiantlvw seadnhvisa dtlkdtlyry
      181 pldangnlgt ptvwagpher gspdgsaids egcvwnarwd gncllrfspe gelleivelp
      241 vqrptscvfg gpdlrtlyvt saaadgaldg allkatapva gmpchrfag
//
LOCUS       WP_007160760             322 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Pseudomonas].
ACCESSION   WP_007160760
VERSION     WP_007160760.1
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 11438136
            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="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=36179
     Region          1..320
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msieiqgink rfgafqalkd inlhiesgel vallgpsgcg kttllriiag leapdtgnig
       61 fhgedvsgrd vrdrnvgfvf qhyalfrhmt vfdnvafglr mkprrerpse aqiaskvhel
      121 lnmvqldwla drypeqlsgg qrqrialara lavepkilll depfgaldak vrkelrrwla
      181 rlheeihlts vfvthdqeea mevadrivvm nkgqieqvgs pgevyeqpvs dfvyhflgds
      241 nrlalgeqev lfrphevele reprpgyhaa evrdirplga ttrvtlrvpe qsevievelv
      301 kdhpvlaglq rgaplhflpr tp
//
LOCUS       WP_007160782             814 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Pseudomonas oryzihabitans].
ACCESSION   WP_007160782
VERSION     WP_007160782.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas oryzihabitans
  ORGANISM  Pseudomonas oryzihabitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 814)
  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 814)
  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 814)
  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   4  (residues 1 to 814)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..814
                     /organism="Pseudomonas oryzihabitans"
                     /db_xref="taxon:47885"
     Protein         1..814
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89899
     Region          78..793
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mhdpvaaglr lapdeltrpf apeqfsfadt dqlepfrgil gqeravealq fgvamprpgy
       61 nvfvmgepgt grfsfvqryl kaeakrqptp ndwvylnhfe eprapgalel ppgegeafva
      121 dmahfidnll atfpavfehp afqqkksaie rafnqrydqa ldvveklale keialyrdan
      181 nvaftpmkeg kaldeadfaq lpeaererfh adisnleerl neelaslpqw rressnqlra
      241 lnedtiiqal qpllaplsek yndnpgvcay lqamqvdllk tvveqladda kpdmqrrkel
      301 reqyepnlii ghhvtggapv vfeshptydn lfgrieyqsd qgalytnyrq lrpgalhran
      361 ggfliveadk lltepfvwda lkralhsrql kmesplaelg rltamslapq qiplqlkvii
      421 igsrniyytl qeldsdfqem frvlvdfdee lplrdesleq faqllktrts eegmapltsa
      481 avarlatysa rlaehqgrls arigdlfqlv seadfirhla gdertdkghv eralkaketr
      541 tgrvcarvld dmltglilid tqgaavgkcn gltvlevads afgmparisa tvypgasgil
      601 dierevslgq pihskgvmil tgylgsryaq efplsisasi aleqsygyvd gdsaslgeac
      661 tlisalsrtp lkqcfaitgs inqfgevqpv ggvnekiegf frlcqarglt geqgviipra
      721 nvtnlmldet vleavraglf hvyavrqade alsllvgepa gapdakgrfp dgsvnarvvq
      781 rlkeiaelel edeladklsd nskakgknnq aaen
//
LOCUS       WP_007161708             287 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Pseudomonas].
ACCESSION   WP_007161708
VERSION     WP_007161708.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..287
                     /product="formate/nitrite transporter family protein"
                     /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=31114
     Region          38..286
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mkrdqeqaee prqsqestpe dpelsreeee dvgesqlpra vvlheiirtq gdhelertia
       61 alfwsalaag ltmglslmam gllnanlpeg gyskviasfg ysagflavil arqqlftent
      121 ltavlpvmse ptlhnfgrla rlwsivlvgn ligtilvayv vlhlplfdak tdakflqigt
      181 hvmendasam fakgivsgwm iatmvwmlpa aenariwiiv litylmalgd fthivvgsve
      241 vaylvfagea swsdflltfa gptlagnivg gslifalish aqvrsdt
//
LOCUS       WP_007161930             112 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Pseudomonadaceae].
ACCESSION   WP_007161930
VERSION     WP_007161930.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonadaceae
  ORGANISM  Pseudomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Pseudomonadaceae"
                     /db_xref="taxon:135621"
     Protein         1..112
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12302
     Region          8..108
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(11,29..30,38,41,43..44,46,49..50,52,60,65,74)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(29,60..61,63,89)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 msaspplepr rqavflalaa ipagrvvsyg qlaelaglgr garwvgwvlg rlpegsalpw
       61 hrviaadgrp sltrdspsgr eqrerlraeg vllhedrvdm rryrwnpaes ve
//
LOCUS       WP_007162234             162 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Pseudomonas oryzihabitans].
ACCESSION   WP_007162234
VERSION     WP_007162234.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas oryzihabitans
  ORGANISM  Pseudomonas oryzihabitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 162)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Pseudomonas oryzihabitans"
                     /db_xref="taxon:47885"
     Protein         1..162
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17013
     Region          15..161
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mtveltgvga glegyamlaa qveallager nlvanaaqls afiyqevpdl nwagfyfveg
       61 ddqlllgpfq gkvacmripf skgvcgaaar errtqrvedv hafpghiacd aasrselvvp
      121 lvqvgrligv ldldsphpar fsaadqagie alveaflaat dc
//
LOCUS       WP_007163040             241 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_007163040
VERSION     WP_007163040.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 241)
  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 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   3  (residues 1 to 241)
  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   4  (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   5  (residues 1 to 241)
  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 12820790
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26102
     Region          13..238
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <131..238
                     /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 mtprlaikry qgdhqphaha faqlvlpiqg gmelelagrs gtrlhtglaa lvapdcghaq
       61 qsepgsrflv idcaadwlpa pildralrqp glaiqpatrq liafaeltsp daldqhapel
      121 trlllaslda taagsafdrl laqveaqpag dwnnaamarl aglgltrlhl lfhqrfsqtp
      181 qawltdlrlr qaqrwlgdsr lpiadialrv gfsdqaaltr amtrrqgisp aawrrgqrlp
      241 g
//
LOCUS       WP_007163324             168 aa            linear   BCT 20-JAN-2025
DEFINITION  division/cell wall cluster transcriptional repressor MraZ
            [Erythrobacter sp. NAP1].
ACCESSION   WP_007163324
VERSION     WP_007163324.1
KEYWORDS    RefSeq.
SOURCE      Erythrobacter sp. NAP1
  ORGANISM  Erythrobacter sp. NAP1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Erythrobacter/Porphyrobacter
            group; Erythrobacter.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Chen,S., Jancrick,J., Yokota,H., Kim,R. and Kim,S.H.
  TITLE     Crystal structure of a protein associated with cell division from
            Mycoplasma pneumoniae (GI: 13508053): a novel fold with a conserved
            sequence motif
  JOURNAL   Proteins 55 (4), 785-791 (2004)
   PUBMED   15146477
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449500
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Erythrobacter sp. NAP1"
                     /db_xref="taxon:237727"
     Protein         1..168
                     /product="division/cell wall cluster transcriptional
                     repressor MraZ"
                     /GO_function="GO:0000976 - transcription cis-regulatory
                     region 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=18477
     Region          9..138
                     /region_name="MraZ"
                     /note="DNA-binding transcriptional regulator and inhibitor
                     of RsmH methyltransferase activity [Translation, ribosomal
                     structure and biogenesis]; COG2001"
                     /db_xref="CDD:441604"
ORIGIN      
        1 mpapgayngq ayspvgdkgr yvlppafrka vkessdgskt lclavhdkyd clvgfglsri
       61 delhaqleke eerairlgds dfdpderaqq lfgfeqvpfd dsgrfvmpeh lkelgmvedg
      121 lyfhgagkff fvwnpeelsr mgpafrgaqa scraqmakae akakgakk
//
LOCUS       WP_007163554              80 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Erythrobacter sp. NAP1].
ACCESSION   WP_007163554
VERSION     WP_007163554.1
KEYWORDS    RefSeq.
SOURCE      Erythrobacter sp. NAP1
  ORGANISM  Erythrobacter sp. NAP1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Erythrobacter/Porphyrobacter
            group; Erythrobacter.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 80)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 80)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 80)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Erythrobacter sp. NAP1"
                     /db_xref="taxon:237727"
     Protein         1..80
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8125
     Region          3..80
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mavtilflgp lrdlagaetl eveapldwsg llgsvgeeva dqlqqervnv acagrvladk
       61 talkakdgde vallppvsgg
//
LOCUS       WP_007163803             404 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Erythrobacter sp.
            NAP1].
ACCESSION   WP_007163803
VERSION     WP_007163803.1
KEYWORDS    RefSeq.
SOURCE      Erythrobacter sp. NAP1
  ORGANISM  Erythrobacter sp. NAP1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Erythrobacter/Porphyrobacter
            group; Erythrobacter.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 404)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Erythrobacter sp. NAP1"
                     /db_xref="taxon:237727"
     Protein         1..404
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44352
     Region          4..397
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 midaaaldif lgetrvgtia rldgdasift fdevyladld rptlslaykd angeiiaetr
       61 syrtkiepff snllpegtlr dylarragvk avreyhllaq lgrdlpgavr aiavdaeere
      121 adepnekaag kqaelalrfs lagvqlkfsa ikaqgknggl tipvtgsggd wivklpsarh
      181 pdvpeaefaa mklaakigid vpeidlvpld qidgipegit rygksafair rfdrgekgpv
      241 htedfaqvfg vfaddkyena syrqilsvla ietdeqsvve fvrrltysvl igngdmhlkn
      301 wsliypdrrn allapaydll stlayipgdd aalkfhssre wasytydele aiadkarlpa
      361 klitatakdv vaqfddawss esghlpfpdd vrsaierhrk tlai
//
LOCUS       WP_007165182             336 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Erythrobacter sp. NAP1].
ACCESSION   WP_007165182
VERSION     WP_007165182.1
KEYWORDS    RefSeq.
SOURCE      Erythrobacter sp. NAP1
  ORGANISM  Erythrobacter sp. NAP1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Erythrobacter/Porphyrobacter
            group; Erythrobacter.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Erythrobacter sp. NAP1"
                     /db_xref="taxon:237727"
     Protein         1..336
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37692
     Region          26..310
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mstkprplfl kdrrdtpnvp gggrkrealv eksriaireg shsfhaaarl fdkttreraw
       61 llyawcrrcd diadnqhmgg elgdqsnaed rlksirlltr raldglptad pafdafglva
      121 aevglteqma edviagfqld aadwrprtea dmmrycyhva gavgvmmavv mgvdpkdkdt
      181 ldrandlgla fqlsniardi veddaagrcy lpemwlveqd iepgqhtkph hreelaemaa
      241 rlvdlvekhe aaarvgaarl pfrsrwavls aariygaigr kvrkrgieaw nsrtyvprwe
      301 kawygvrgfv savinrphep dqpidwgiad yrpdpa
//
LOCUS       WP_007165540             207 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Erythrobacter sp. NAP1].
ACCESSION   WP_007165540
VERSION     WP_007165540.1
KEYWORDS    RefSeq.
SOURCE      Erythrobacter sp. NAP1
  ORGANISM  Erythrobacter sp. NAP1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Erythrobacter/Porphyrobacter
            group; Erythrobacter.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Erythrobacter sp. NAP1"
                     /db_xref="taxon:237727"
     Protein         1..207
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21883
     Region          4..154
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdkaahphav wwlaffcfie asffpipphp llglmclaep kkalrfsiia tlasvagglf
       61 gyaigyllyd svgvplltmi glidslpaak ctfdeygaya vtiaaatpvp fklltitagf
      121 lamdlvpfli aslagralif vtvgilfqif grpikriide ylgtvttvfv llvvggflai
      181 tqlgggddea gdedvcaaai eepaqqq
//
LOCUS       WP_007165713             165 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Erythrobacter sp. NAP1].
ACCESSION   WP_007165713
VERSION     WP_007165713.1
KEYWORDS    RefSeq.
SOURCE      Erythrobacter sp. NAP1
  ORGANISM  Erythrobacter sp. NAP1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Erythrobacter/Porphyrobacter
            group; Erythrobacter.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Erythrobacter sp. NAP1"
                     /db_xref="taxon:237727"
     Protein         1..165
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17488
     Region          13..165
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfdfkpdpsi dvaeryrqlv daadaltsde pdavanmanv aaliwefvdd lnwagfyrvg
       61 esksgaeelv lgpfvgrpac iripigrgvc gaaaekaqtq lvedvhafpg hiacdaasrs
      121 evvvpvvreg kvvavidlds psparfgkdd aaglerlael ladri
//
LOCUS       WP_007165767             308 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Erythrobacter sp.
            NAP1].
ACCESSION   WP_007165767
VERSION     WP_007165767.1
KEYWORDS    RefSeq.
SOURCE      Erythrobacter sp. NAP1
  ORGANISM  Erythrobacter sp. NAP1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Erythrobacter/Porphyrobacter
            group; Erythrobacter.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Erythrobacter sp. NAP1"
                     /db_xref="taxon:237727"
     Protein         1..308
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33798
     Region          209..288
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mekftdsmng dtefepdevs yeltsqslih vdyiappaai sdyvttlyhf rcdepkitdi
       61 qpasvghlsl fpygkgemhf raghsdpnpe vavmtplsta npivvdgpfh aigaaltplg
      121 waaltglhag enrdrlrdag eilgdratkl gadliaeyra gtktgqecal aigefigssv
      181 krvnsrhael ikvvnnwlgs slspdlgdll ekaayserqv qrlteryfgl spqalarkyr
      241 alraaallsf ptltpefeae lgeaffdqsh mireinrfvg rtparlknpd npylsemiap
      301 knlrelds
//
LOCUS       WP_007165768             292 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Erythrobacter sp. NAP1].
ACCESSION   WP_007165768
VERSION     WP_007165768.1
KEYWORDS    RefSeq.
SOURCE      Erythrobacter sp. NAP1
  ORGANISM  Erythrobacter sp. NAP1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Erythrobacter/Porphyrobacter
            group; Erythrobacter.
REFERENCE   1  (residues 1 to 292)
  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 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 292)
  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   4  (residues 1 to 292)
  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 292)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Erythrobacter sp. NAP1"
                     /db_xref="taxon:237727"
     Protein         1..292
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32457
     Region          7..261
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          188..261
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mlfetkhpve feliapppdl reqvnifyam rsgaeriedv mpaysgqvya ifegtfelhf
       61 esgtqkapap vflnapllqa trlsvlgpfr cvgaslthrg waelvgepvd avhhrmipph
      121 dalsheladr lvgigqadpd dpaqateals qvireaitpi kpahatfide tmswlskefn
      181 ppvealfdel aisrrqaqrl snrffgvppr qllkrvramr aatllsqpdl patvrdeisl
      241 ayfdqshlin dlrrytgrtp tileegdlvv rtfdpaahgp pgkyardale ke
//
LOCUS       WP_007171618             282 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Mycobacterium
            parascrofulaceum].
ACCESSION   WP_007171618
VERSION     WP_007171618.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium parascrofulaceum
  ORGANISM  Mycobacterium parascrofulaceum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            simiae complex.
REFERENCE   1  (residues 1 to 282)
  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 282)
  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   3  (residues 1 to 282)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Mycobacterium parascrofulaceum"
                     /db_xref="taxon:240125"
     Protein         1..282
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31476
     Region          173..277
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mddvfigsea vrqgrlspyq lrvgfraiyp dvylgeaatp slrtrcagaw lwsgrrgiva
       61 glaaaalhgs dwidddapie liwgnqhapt gvitrnqrve pdeitraagl pvttaartay
      121 dvarqfprde avarldallr arpfcleevp llakryprar glqrlraalp lvdpgaaspk
      181 etwlrlllid agfpapetqi pvndgwrlvg vldmgweryk vaaeydgdqh rtsrrqyard
      241 hwrlrkmeel gwivvrviae dkpqdvvarv gaaltrrgcr em
//
LOCUS       WP_007173684             210 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Hallella bergensis].
ACCESSION   WP_007173684
VERSION     WP_007173684.1
KEYWORDS    RefSeq.
SOURCE      Hallella bergensis (Prevotella bergensis)
  ORGANISM  Hallella bergensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hallella.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Hallella bergensis"
                     /db_xref="taxon:242750"
     Protein         1..210
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22977
     Region          36..208
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mkklslffla lmmstnmmsq eiiqlpesnk nvpttlfqal qdrhsvrnfe drsidmptls
       61 qllwaaigvn radgrmtapt avnaqeisvy vatkdgvcly lnkenalkvv skqdirkeia
      121 arqtgvanap vfliivsdlg kirakvgdra lmmtaedagy vsqniclgaa alglgtvprh
      181 gmnreviksv lelgdnheim lnhpigyprk
//
LOCUS       WP_007173693             159 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Hallella bergensis].
ACCESSION   WP_007173693
VERSION     WP_007173693.1
KEYWORDS    RefSeq.
SOURCE      Hallella bergensis (Prevotella bergensis)
  ORGANISM  Hallella bergensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hallella.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Hallella bergensis"
                     /db_xref="taxon:242750"
     Protein         1..159
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17406
     Region          4..158
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mimtdrmeek ykllvaqvva llegethvma vlsnvsaalh daflerffwv gfymvhgeel
       61 llgpfqgpva cyhigygkgv cglawqrget vivpdveqfp ghiacssrsr seivvpihgg
      121 dgsvkgvidi dstdldafgk vdrmyleqia vllsrqlnl
//
LOCUS       WP_007175074             156 aa            linear   BCT 20-JAN-2025
DEFINITION  division/cell wall cluster transcriptional repressor MraZ [Hallella
            bergensis].
ACCESSION   WP_007175074
VERSION     WP_007175074.1
KEYWORDS    RefSeq.
SOURCE      Hallella bergensis (Prevotella bergensis)
  ORGANISM  Hallella bergensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hallella.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Chen,S., Jancrick,J., Yokota,H., Kim,R. and Kim,S.H.
  TITLE     Crystal structure of a protein associated with cell division from
            Mycoplasma pneumoniae (GI: 13508053): a novel fold with a conserved
            sequence motif
  JOURNAL   Proteins 55 (4), 785-791 (2004)
   PUBMED   15146477
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449500
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Hallella bergensis"
                     /db_xref="taxon:242750"
     Protein         1..156
                     /product="division/cell wall cluster transcriptional
                     repressor MraZ"
                     /GO_function="GO:0000976 - transcription cis-regulatory
                     region 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=17622
     Region          2..122
                     /region_name="MraZ"
                     /note="DNA-binding transcriptional regulator and inhibitor
                     of RsmH methyltransferase activity [Translation, ribosomal
                     structure and biogenesis]; COG2001"
                     /db_xref="CDD:441604"
ORIGIN      
        1 mrflgnieak idskgraflp aqfrkmlmap gesglvlrqd ifedtliiyp esvwnslmde
       61 mrarlsrwdr qqqmvfrtfv sgvtsitmda ngriliprdf lqaagitqsl rfvgmgdtie
      121 iwpnkpqeal plmdkeefgs aleklmspnh danate
//
LOCUS       WP_007175289             126 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Hallella bergensis].
ACCESSION   WP_007175289
VERSION     WP_007175289.1
KEYWORDS    RefSeq.
SOURCE      Hallella bergensis (Prevotella bergensis)
  ORGANISM  Hallella bergensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hallella.
REFERENCE   1  (residues 1 to 126)
  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 126)
  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   3  (residues 1 to 126)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Hallella bergensis"
                     /db_xref="taxon:242750"
     Protein         1..126
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14846
     Region          25..124
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mesddyykta nplvygllkn nakrmrhgqt kaesflwsyi ranqlgvhfr rqhpigdfia
       61 dficidqrli ievdgnihnk peqqewdkqr taflesqdyr vvrfsneqvl hdidkvlahi
      121 ksyiik
//
LOCUS       WP_007175364             418 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Hallella
            bergensis].
ACCESSION   WP_007175364
VERSION     WP_007175364.1
KEYWORDS    RefSeq.
SOURCE      Hallella bergensis (Prevotella bergensis)
  ORGANISM  Hallella bergensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hallella.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 418)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Hallella bergensis"
                     /db_xref="taxon:242750"
     Protein         1..418
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47149
     Region          2..414
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mkrlyvyadf dwlkevelig elgyeslrgt dsysftfnne wlrkhgelfl sddlnnypgq
       61 qyslpekdif gcfsdalpdr wgrtlllrre qivaaeekrp vrrlssfdfl tgiddfsrmg
      121 gfrfkeipdg efinvseslk ippltdirgl iaasaeieks eeknilpdrk wiaqlvhpgt
      181 slggarpkan vidtdktlyv akfpsrkdey dvgiwehfsh qlaiksgisa aktgvmangg
      241 eyhtllsqrf drtqegrrih fasamtllgl sdgnnatsgh gyldivdfii qnctdveknl
      301 qelyrrvafn icignsddhf cnhgflltak gwilspaydm nptlneyqsl lisstsnkad
      361 lsilldacee ymlnrntaek ivsevveavk gwrdlavrsg lskremdifs gvldgrvl
//
LOCUS       WP_007176637             291 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Paraburkholderia].
ACCESSION   WP_007176637
VERSION     WP_007176637.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..291
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32331
     Region          14..253
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mtaaqrvtet tdilgecplw seaeqalywi dirrpgiqrw hpasdalryw pmpdlvgsia
       61 lcrdnrllva srslfyldtr tgemtrfapq raedpalrfn dgkcdrqgrf wvgtmndrtr
      121 epvgelfrvd ergavsieag irvpngtcfs pdgrtmyfad sdlqtiftya ldpgtgalge
      181 rrefakttlp avpdgatvde qghiwiaeyg gwcikryapd gsvdrvfdmp vqnptsctfg
      241 grnldtlyit tasqrltpde lakqpfagal lafqpgvrgl peplfrgnak s
//
LOCUS       WP_007176694             333 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Paraburkholderia].
ACCESSION   WP_007176694
VERSION     WP_007176694.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 333)
  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   6  (residues 1 to 333)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..333
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37123
     Region          21..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          85..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 metmlrsvam sgyfdvarrl glnpvelaqq vgidtaalan pddripaars crlleltank
       61 ascptfalqm aetrqkfgtg vvnvllahkr tlrevllata eyrhllneal alyvedaget
      121 vtireelvve pgtptnqaie lavgvlwrhs sallgdhwkp rsvhfvhqgp knltfhrrff
      181 gcplefgsdf ngfvcaaadl dypnpaadpe lvryaeslad slnmtgvdst alevrkaiyl
      241 llpleqasve lvarhlrlsv rtmqrqldva htsfshlvee vrrelavrym snprypigrv
      301 sallgysqqg sftnwfnsrf gvtprnwrns hlk
//
LOCUS       WP_007177658             373 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Paraburkholderia].
ACCESSION   WP_007177658
VERSION     WP_007177658.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 373)
  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 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   3  (residues 1 to 373)
  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   4  (residues 1 to 373)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 373)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 373)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..373
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38880
     Region          27..363
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(103..105,125..126,175,227,251)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mrrfamtaaa lmaacftlsa taqvvvtigh sapltgpqap ngkdnengar laidelnkag
       61 vtvagqkvtf kldseddqad pkigvqvaqk lvdsgvvavv gpynsgvaip asrvyntgnv
      121 pmlpvasnpa ltkqgfrnif rigasdeqlg gtmgqfaakt lkaktaavid drtaygqgva
      181 eqftkvakan giqiidqeft sssatdflgi ltniksknpd viffggyaaq gapmakqmrq
      241 rglrakllgg dgicsadmgk vagdaasivy caqggialek taagreflek ykaaynidtq
      301 vyavsyydgv klladamvka gtttdkaklt aqlakenykg vagtysfdey gdlkgapttv
      361 ytiknglpvp ygq
//
LOCUS       WP_007178477             277 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Paraburkholderia sp. USG1].
ACCESSION   WP_007178477
VERSION     WP_007178477.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. USG1
  ORGANISM  Paraburkholderia sp. USG1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 277)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 277)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Paraburkholderia sp. USG1"
                     /db_xref="taxon:2952268"
     Protein         1..277
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30763
     Region          18..101
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          127..276
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mnpvgkalwf ieshfarelt ldeiancgcv srfhlarafe aatgfsvmry vrgrrlseaa
       61 rrlasgapdi lavaidagyg sheaftrafr eqfgltpdal rarghldnla lvepikmdet
      121 lltrlepprf edgkaflvag lserytsetc aaipsqwqrf gdyfgkvpgq mgnvaygvcy
      181 naddngnldy lcgvevsdfs alpaelsrlr ispqryavfs hrehvstirr twntiwnqwl
      241 pasghipada pnferydgkf dpvsgmggle iwlplks
//
LOCUS       WP_007180017             382 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Paraburkholderia].
ACCESSION   WP_007180017
VERSION     WP_007180017.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 382)
  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 382)
  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   3  (residues 1 to 382)
  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   4  (residues 1 to 382)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 382)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 382)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..382
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40277
     Region          32..368
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(108..110,130..131,180,232,256)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mqhkmkqlag aalvaamsla gtanaqsted vkvgfagpmt gaqahygkdf qngitlaved
       61 mnatkpvigg kqvrfvldsa ddqadprtgt tvaqklvddg ikgmlghfns gttipasriy
      121 anagipeiam atapeytqqg fkttfrmmts dtqqgsvagt favktlgmkk ivivddrtay
      181 gqgladqfek aakaaggqiv dreytndkav dfksiltklk avqpdliyyg gadsqaapmv
      241 kqmkalgika plmggemvht ptfiqiagda angtvaslag lpleempggk dyvakykkrf
      301 nedvqtyspy aydgamamfd amkkanstdp akylpmlakt smpavtsanl aydskgdlkn
      361 ggitlykvvd gkwttlqsvg gk
//
LOCUS       WP_007185441             202 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Hydrocarboniphaga].
ACCESSION   WP_007185441
VERSION     WP_007185441.1
KEYWORDS    RefSeq.
SOURCE      Hydrocarboniphaga
  ORGANISM  Hydrocarboniphaga
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Nevskiales; Nevskiaceae.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Hydrocarboniphaga"
                     /db_xref="taxon:243627"
     Protein         1..202
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=22223
     Region          18..200
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mdepsksdri velagklgvl rpkdlaaegi qaeylrrvcd kglikkvgrg syvladkvvt
       61 phltlavagr avpngviclr salafhglae qltdevyiai erraarprld ypevkvarlg
      121 gpaftegvet hliegvevni yslektladl fkfrnkigph iavdalraaf lahkvhkdkl
      181 wyfaklcrve rvmkpyvdal as
//
LOCUS       WP_007186250             413 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Hydrocarboniphaga effusa].
ACCESSION   WP_007186250
VERSION     WP_007186250.1
KEYWORDS    RefSeq.
SOURCE      Hydrocarboniphaga effusa
  ORGANISM  Hydrocarboniphaga effusa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Nevskiales; Nevskiaceae; Hydrocarboniphaga.
REFERENCE   1  (residues 1 to 413)
  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 413)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 413)
  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   4  (residues 1 to 413)
  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 413)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Hydrocarboniphaga effusa"
                     /db_xref="taxon:243629"
     Protein         1..413
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45671
     Region          45..219
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          264..339
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mgtqknetvq dhtagtvsia fvreviasaa rrgqpaapll aaaqipskal endaarvspg
       61 qfgalwlavg ralddeffgl dsrrvkvgsf aliarsglqa rnlrevlvgi srffrilldd
      121 iridfetgae saelrlvdll prgpageidr vlahetlltl ihglacwlia rripvrralf
      181 ayprppwgee ykavyssdsq fdapvtrmif dallletpva qtertlgdfl rgapgnfilk
      241 yknenslssr vrrhlrsrpp sdwpsfevla defhigattl rrrleregts fsairdavrr
      301 dlaishlqrs dasiadialt lgfaepsafh rafkqwtgvr lsrrrkagqg aradlsedaa
      361 shcsfstyrq trpripgsdl arhgqskvaa trqadpvdrv pggrrvdrhr sgf
//
LOCUS       WP_007186419             388 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Hydrocarboniphaga effusa].
ACCESSION   WP_007186419
VERSION     WP_007186419.1
KEYWORDS    RefSeq.
SOURCE      Hydrocarboniphaga effusa
  ORGANISM  Hydrocarboniphaga effusa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Nevskiales; Nevskiaceae; Hydrocarboniphaga.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Hydrocarboniphaga effusa"
                     /db_xref="taxon:243629"
     Protein         1..388
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=42360
     Region          1..349
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mdiqirgihk gfgnfpalag vdldiasgel iallgpsgsg kttllrtiag lefadsgril
       61 fggqdtlglp vqqrrvgfvf qhyalfrhmt vldnisfglr vqkrserpsa eairkkalel
      121 ldlvqlggle krypsqlsgg qrqrvalara laieprvlll depfgaldak vrkdlrrwlr
      181 elhettgytt ifvthdqeea leladrvvvm nrgrieqvgt tdevyekpat pfvfeflgnt
      241 nvlpgqvrdg kvhvdglips iasartqade aveiyvrpsd lrlaepgdpg ieaivsstqr
      301 tgpivrseai asasgaklei elphlhrdvp allagahvrl rlnqfsvfpl asptespavl
      361 ragstprrtl edvvpnapae yrerarhg
//
LOCUS       WP_007186519             340 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Hydrocarboniphaga].
ACCESSION   WP_007186519
VERSION     WP_007186519.1
KEYWORDS    RefSeq.
SOURCE      Hydrocarboniphaga
  ORGANISM  Hydrocarboniphaga
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Nevskiales; Nevskiaceae.
REFERENCE   1  (residues 1 to 340)
  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 340)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 340)
  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   4  (residues 1 to 340)
  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 340)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Hydrocarboniphaga"
                     /db_xref="taxon:243627"
     Protein         1..340
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37622
     Region          25..212
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          256..337
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 makskdvrvp aryylrldev lrpqgvdils iassvglspe klqepdallp fstverlvsa
       61 alkesgrtdl glelgkllsv sahsivgfgm lscanvgqai rfvsryfrlv mptfqlrdtl
      121 tpehaelhft pttamghecl lfhleligsa alrnlhemfa garppcrlqi smlppphvar
      181 yselkdvrts fgsewgfgtr lrfaasltah plmmfdpnsf kvadercral vdqvvgvrqf
      241 gewiamtlre vgdglptlpe iagmlnmsar slnrylereg tsfreiagrv nhelacerla
      301 ttdmsvteia yslgfndtsn ftrafrsreg cspgvyrara
//
LOCUS       WP_007186592             377 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Hydrocarboniphaga effusa].
ACCESSION   WP_007186592
VERSION     WP_007186592.1
KEYWORDS    RefSeq.
SOURCE      Hydrocarboniphaga effusa
  ORGANISM  Hydrocarboniphaga effusa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Nevskiales; Nevskiaceae; Hydrocarboniphaga.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (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   3  (residues 1 to 377)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Hydrocarboniphaga effusa"
                     /db_xref="taxon:243629"
     Protein         1..377
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40701
     Region          <1..377
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdligelvlv rnrikrlgat pgvaigelrk tfseldvits glqaqvtrmr mqpirrlfak
       61 fpklardtar klgkqvever igedteldkt lvealgdplm hmvrnavdhg letpgariaa
      121 gkpacgrivl saeqaggqiv vtvsddgagm nadrlrakal ergligeaea armtreeclq
      181 lvflpgfstk eqisdlsgrg vgmdvvrsni valggvvaie sepgrgstir irlpltlaiq
      241 pvlmierasr lfalplqavq dvftldaslv gasddgwerv pyrdhslrll rlarwtgdeh
      301 dgerehvvvv nigserygli agsvrgreei vvkplgrllk glsgiaggtv tsegrvaliv
      361 elpgllaaye rdlsrtr
//
LOCUS       WP_007191422             125 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Thiocapsa marina].
ACCESSION   WP_007191422
VERSION     WP_007191422.1
KEYWORDS    RefSeq.
SOURCE      Thiocapsa marina
  ORGANISM  Thiocapsa marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiocapsa.
REFERENCE   1  (residues 1 to 125)
  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 125)
  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   3  (residues 1 to 125)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Thiocapsa marina"
                     /db_xref="taxon:244573"
     Protein         1..125
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14290
     Region          10..106
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mdqhpfaktl rqtmtdaeql lwrhlrarrl ngqkfrrqqp igpyivdcvh fgarlivead
       61 ggqhngsdrd svrdawleqq gfkvmrfwnn dilrnpegvl ssileapeqp applprplsr
      121 egrge
//
LOCUS       WP_007191465             355 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Thiocapsa marina].
ACCESSION   WP_007191465
VERSION     WP_007191465.1
KEYWORDS    RefSeq.
SOURCE      Thiocapsa marina
  ORGANISM  Thiocapsa marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiocapsa.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Thiocapsa marina"
                     /db_xref="taxon:244573"
     Protein         1..355
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38913
     Region          13..286
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mpqpmlktyy asaadlaacr qllrtgsrsf yaasfllpqr irdpaialya fcriaddaid
       61 cagdepgaqt ralaelhhrl driydgepid eytdraladv vrcfgipkal leallegfew
      121 daegrrfedi sgvydysarv agtvgammaa lmgarstqlv aracdlgvam qltniardvg
      181 edarngrlyl pmswmrevgi dpekwlekpv fnealasvie rllraaetly vrsdagiagl
      241 pmgcragina arylyaeigr qverqgldsi srravvpgsr kvqllapilg tavlspryvs
      301 appldetrfl vdavvysahr sseeetaapa gvggrviwvl elfeqleere raltn
//
LOCUS       WP_007192198             756 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Thiocapsa marina].
ACCESSION   WP_007192198
VERSION     WP_007192198.1
KEYWORDS    RefSeq.
SOURCE      Thiocapsa marina
  ORGANISM  Thiocapsa marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiocapsa.
REFERENCE   1  (residues 1 to 756)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..756
                     /organism="Thiocapsa marina"
                     /db_xref="taxon:244573"
     Protein         1..756
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=80126
     Region          35..754
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mtrpagptig rtvretgstl gglavvvaal qwgnafaqgl ptvesdaeti elaplvvtat
       61 rsgestfdlp vaidvldkai iqdqkpmvli sedlprvpgt vvtnrgtyaq eeqimirgfg
      121 graqfgtrgv kliadgipas tpdgqggpgl fdlgsarsie vmrggfsaly gnhsggvvqv
      181 ftedgppept lsvrlmggsd stwiagtklg gqtgrlnyvv dlsraqtdgy rdwsratkeq
      241 ansklgiald gggtlslivn alnlpeardp lgltaeevkr drrqaapaar tfqtgrtldn
      301 lqggvvldqp igaaddlrvm aytgtrgneq ylaiplanqn aitasggvsa fdrrfaggnl
      361 lwtrsttfad gpltlifgge ydrsaearkg ylndlgeraa lkrdadntvd swgtfvqgtw
      421 gfaprwsldl glrytevrfd sddgfictpd rvtapgtrpg tcsgstvpit atnlnpddsg
      481 srtygawtpa lgllynltps inlyanlgkt fetptfiela yrpdggagln lgldpavsrh
      541 yeigakvllg sdarlnlalf qidtddeltv atngggraty rnapasrrrg velllesplg
      601 rgfagslaat yleseftesf aacagipcrt vaptlnvttv eagnripgvp aftlfgelsy
      661 ayeplgfeaa islygqdkvy vndrnsetap aywlanlrgg ftqdlgglrl sqflridnll
      721 depyisavsv nasngrfyap gpgtnyligi tasysf
//
LOCUS       WP_007192957             363 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Thiocapsa marina].
ACCESSION   WP_007192957
VERSION     WP_007192957.1
KEYWORDS    RefSeq.
SOURCE      Thiocapsa marina
  ORGANISM  Thiocapsa marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiocapsa.
REFERENCE   1  (residues 1 to 363)
  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 363)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 363)
  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   4  (residues 1 to 363)
  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 363)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Thiocapsa marina"
                     /db_xref="taxon:244573"
     Protein         1..363
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39990
     Region          34..217
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          266..346
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mapvrahhgd sdlnipvvra qhlidyigvl rdlgvpvere lersrlpvai eetpndyvsl
       61 praldwlwrs rrefgvmelg flagraaslr slhpdvqrav trastglsri tvlsdrvhqe
      121 snavrigirr egidrrvvce iqgfrnsplv gfaewkaiag iigvmrsaag pdwcpteitf
      181 vsrerpsgaa leaygkpril tgqrycsvlv aaadlartci drrsssdgak dpttpsrpps
      241 glsdawdflt glralirpyl aqghpplsla aeivgmsers lqrrlaqrrt tysaivqear
      301 fliasdlmad sdlniadiaf aagyenashf crafkrltgm tprdyrcaaw nrvtdgvghk
      361 tar
//
LOCUS       WP_007192983             356 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Thiocapsa marina].
ACCESSION   WP_007192983
VERSION     WP_007192983.1
KEYWORDS    RefSeq.
SOURCE      Thiocapsa marina
  ORGANISM  Thiocapsa marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiocapsa.
REFERENCE   1  (residues 1 to 356)
  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 356)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 356)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 356)
  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   5  (residues 1 to 356)
  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   6  (residues 1 to 356)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Thiocapsa marina"
                     /db_xref="taxon:244573"
     Protein         1..356
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38902
     Region          39..222
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          119..353
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mqvdyaplsy mssdlplvme gslriapflq vpnllvefgl dpasitaeag ldiglfddpe
       61 qgiplaaagr llalaaersg cpsfghrlge qvgldalgri gqlaksapdv stalhqvvly
      121 lhlhdrgavp alwisadrvv mayvvyqaev pgiehiydga vaitfnivkl lcgagfepie
      181 vrlsrprpad vepyrrfyrs risfgaehsa vvfsadwlkr pldgadgvlh kqllqiiefa
      241 dvrgeenlva nlrrvircil vqgvapedts lahiarlfsl hrrtlnrrlq slgttfktli
      301 dearydvarq llrdtslpvv diaasldyad aaafsrafkr wsgvspgawr rslppp
//
LOCUS       WP_007193636             156 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Thiocapsa marina].
ACCESSION   WP_007193636
VERSION     WP_007193636.1
KEYWORDS    RefSeq.
SOURCE      Thiocapsa marina
  ORGANISM  Thiocapsa marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiocapsa.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Thiocapsa marina"
                     /db_xref="taxon:244573"
     Protein         1..156
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=17033
     Region          6..155
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mfvigrqpgf tlievmvvva ilgilaalav pqyrtfstra kiseglvllg pvklavseyy
       61 ashgrlptat nwltllrelg lnvdtvsgaa sgiyvkriww nntareirvr ygfapiddkl
      121 valradftsn gqaiwtcfap dtdgvpfryl pstcrg
//
LOCUS       WP_007193289             107 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Thiocapsa marina].
ACCESSION   WP_007193289
VERSION     WP_007193289.1
KEYWORDS    RefSeq.
SOURCE      Thiocapsa marina
  ORGANISM  Thiocapsa marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiocapsa.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Thiocapsa marina"
                     /db_xref="taxon:244573"
     Protein         1..107
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11938
     Region          14..107
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 msvptapeai pslfarevrk rlgahlkelr lfgsrargda rvnsdydmlv ivdarspeir
       61 atildievdl iarygvlvts lvrseaeweq rqgtplalni eregrrl
//
LOCUS       WP_007193644             135 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Thiocapsa marina].
ACCESSION   WP_007193644
VERSION     WP_007193644.1
KEYWORDS    RefSeq.
SOURCE      Thiocapsa marina
  ORGANISM  Thiocapsa marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiocapsa.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Thiocapsa marina"
                     /db_xref="taxon:244573"
     Protein         1..135
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14980
     Region          46..132
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mthphppasd rasrgqtvtp rrfdysalka rwdaqrnasa slsarlleqv eregaavfrr
       61 yhatratafg slvegrahar sdidlivfgt dpadywalrr dleetfgrpi dlhtesddar
      121 fvskaiargk viyaa
//
LOCUS       WP_007195047             811 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Thiocapsa marina].
ACCESSION   WP_007195047
VERSION     WP_007195047.1
KEYWORDS    RefSeq.
SOURCE      Thiocapsa marina
  ORGANISM  Thiocapsa marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiocapsa.
REFERENCE   1  (residues 1 to 811)
  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 811)
  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 811)
  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   4  (residues 1 to 811)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..811
                     /organism="Thiocapsa marina"
                     /db_xref="taxon:244573"
     Protein         1..811
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89631
     Region          1..804
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mpiasleata lyrrcdpeql qfettadldv rdgliaqdra iaavrfgigi hhegynlfal
       61 gpsgtgkyal lrsaveerah geavppdwcy vfnfedahrp ralrlppgkg aelkrdmdql
      121 vedlhraiqa lfesdeyrtr tqaleeelee rqeramgeir elakekdvil lqtptgftla
      181 plrdgkplgp nefhalsede rarieedins lqaemrkalh qmplwkkrsd eqiealnrem
      241 aaaaiqslme glcekyadlq avvdylnqvq ddvvenfrqf lpdhdkqpql lgiwipqntd
      301 gppwhqryrv nvllghdkng gapvvyadlp ahhqlvgrie hrahlgalet dftmiragal
      361 hqanggyliv dalkllmqpf awetlkrllq aaeiriesla qitslistls lepepipldv
      421 kivmlgerhi yyllceldpe fselfkvavd fedqlergpe shlvyarfia sevrraglhh
      481 fdraavarvi ehsarladdn erltshmrsi gdlvresdyw aktagretvg aedvqraida
      541 kiervdrisr rlreettrgt ilietrgskv gqvnglavms lggfafghps ritarvrlgk
      601 gelidierev klggpihskg vlilqgfiag ryaldyplsl saslvfeqsy ggvegdsass
      661 aelyallsal adlpisqsla vtgsvnqlge vqaiggvnek iegffdvcaa rgsvdgqgvl
      721 ipasnvkhlm lradvreava rgrfavypia nidegieilt gmpagtrasd gafpagsvna
      781 rvearlvgfs erlralhard gksrsgegae p
//
LOCUS       WP_007194674             123 aa            linear   BCT 20-JAN-2025
DEFINITION  PilZ domain-containing protein [Thiocapsa marina].
ACCESSION   WP_007194674
VERSION     WP_007194674.1
KEYWORDS    RefSeq.
SOURCE      Thiocapsa marina
  ORGANISM  Thiocapsa marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiocapsa.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 123)
  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   3  (residues 1 to 123)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 123)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Thiocapsa marina"
                     /db_xref="taxon:244573"
     Protein         1..123
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13212
     Region          8..123
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 matpgastgs lagqqrilsf aikdkaalya afmpfvkngg lfipttkryq lgdeiflllq
       61 lmeeteripv agkvvwvtpp gaegsraigv gvqfseqdkg marrkiedyl vgalnsdrpt
      121 htm
//
LOCUS       WP_007195082             671 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Thiocapsa marina].
ACCESSION   WP_007195082
VERSION     WP_007195082.1
KEYWORDS    RefSeq.
SOURCE      Thiocapsa marina
  ORGANISM  Thiocapsa marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiocapsa.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Thiocapsa marina"
                     /db_xref="taxon:244573"
     Protein         1..671
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=76532
     Region          64..586
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mdklkmhspd lsqeniakvr elfpgcvtea rddstgklrl svdfdqlkqe lsdhivdgpq
       61 eryrldwpsk keaiiianap iaktlrpsle essnfessrn lfiegdnleg lkllqeaylg
      121 vikliyidpp yntgrdfvyq ddfaqgstef lkrsmqhdnd gnrllalret egrfhsewls
      181 miysrllisr nllcqegiiv isvdekehan lkkvcdeifg aknfcgeivw knsskndqay
      241 isiqheyfvv yvkdketnpg dwterkagld eiykafggfl stygkewdai hkaalewyke
      301 fppsnpiyds khyswmddrg vyfpadisgp ndgqyvysid hpitkrpvke psrgwscpke
      361 hllslisedr vhfgkdettv pclktylkst etvsltsmrf ldgraaskrl rtlfgekvft
      421 npkdefllae lfkamkvrgn divldffggs gttahavfel nriqgsrcaf hmiqiaesle
      481 eslkvatgaa kkitknairf leardrpatv aeiskerirr agkkviegdc hpdwnrdvgf
      541 rvlkvdtsnm kdvyyrpdev kqadlldmvd nvkedrtaed llfqvlvdwg vdltlpirre
      601 tiqgkmvffv ddnalvacfe pgvtedlvke lagheplrii frdkgfvsda vkinveqifr
      661 qlspstevks i
//
LOCUS       WP_007195285             468 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Thiocapsa marina].
ACCESSION   WP_007195285
VERSION     WP_007195285.1
KEYWORDS    RefSeq.
SOURCE      Thiocapsa marina
  ORGANISM  Thiocapsa marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiocapsa.
REFERENCE   1  (residues 1 to 468)
  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 468)
  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 468)
  AUTHORS   ter Beek,J., 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 468)
  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 468)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Thiocapsa marina"
                     /db_xref="taxon:244573"
     Protein         1..468
                     /product="CmpA/NrtA family 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=51524
     Region          41..322
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mrnqdrpehq trgvlptrla aagiaalmls laarasaeal gppekedlkl gfikltdmap
       61 laiayekgff ededlfvtle aqanwkvlld rvidgqldga hmlagqplaa tigfgteapi
      121 vtplsmdlng naitvsnavw eqmkphvpkm adgrpehpik adalkpvves fkaagkpfkm
      181 gmvfpvsthn yelrywlaag glnpgyyaph kndtdgqida dvllsvtppp qmpatmesgt
      241 idgycvgepw nqqavfmgig vpvitdheiw pynpekvfgm taafveanpn tavrivkaml
      301 raakwldend nanraeavki lsrpnyvgad eaviaasmtg tfeyekgdsr dvpdfnvffr
      361 hnasypyysd avwyltqmrr wgqiaepksd dwymetakqv yrpdlyrlaa esliadglme
      421 asdfpdfdte tgfkptqtgf idgidydgtr pnayleqfsi glkgdkql
//
LOCUS       WP_007195969             408 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Hoeflea phototrophica].
ACCESSION   WP_007195969
VERSION     WP_007195969.1
KEYWORDS    RefSeq.
SOURCE      Hoeflea phototrophica
  ORGANISM  Hoeflea phototrophica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Hoeflea.
REFERENCE   1  (residues 1 to 408)
  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 408)
  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
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 408)
  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   5  (residues 1 to 408)
  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   6  (residues 1 to 408)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 408)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 408)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Hoeflea phototrophica"
                     /db_xref="taxon:244596"
     Protein         1..408
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44011
     Region          32..76
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          94..393
                     /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 mpfdksagwd ragtvipslr gsnqsglray nqrlvlslvy ahgslaktdi srmtglsaqt
       61 gsvlmrelea edlivkgepi rgkvgqpsvp lsinpdgaff vglkvgrrsa elilidflgq
      121 pkatlrksyp wptppliidf tldglgelld alpehlrtrv aglgiatpfe lwnwaeqaga
      181 prdemelwrs cdlraelaav cdmpvylqnd ataacaaelv fgkyeglsdy lylyigtflg
      241 ggvvlngsvy sgrtgnagal gplpvtgpeg tsvqlldras imvlermlrd rgidpsplwn
      301 npedwqgfed fleiwiaiva rslaqaivsa tavidfehai idgglpadvr ariveatrae
      361 verydlrgle lpkilpgtvg nlaralgaas lplfdkylid rntllgss
//
LOCUS       WP_007196064             250 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Hoeflea phototrophica].
ACCESSION   WP_007196064
VERSION     WP_007196064.1
KEYWORDS    RefSeq.
SOURCE      Hoeflea phototrophica
  ORGANISM  Hoeflea phototrophica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Hoeflea.
REFERENCE   1  (residues 1 to 250)
  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 250)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Hoeflea phototrophica"
                     /db_xref="taxon:244596"
     Protein         1..250
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26922
     Region          1..250
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mkfsanlgfl wtdrslpdai rtakaagfda vechwpyetp peqvkaalee tglpmlglnt
       61 vrgnpgengl calpgrqpea raaidqaidy ataigagaih vmagfadgpe aeaaflenlr
      121 yarrncpagi dllieplnrh dapgyflrtt dqaaailkql dmpgiklmfd cyhvgrtegd
      181 vvtrlkalaq vighiqfasv psrgapdqge ldyrfvfaki aemgwsqplg aeykpggatd
      241 dslgwlrslr
//
LOCUS       WP_007196317             696 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Hoeflea phototrophica].
ACCESSION   WP_007196317
VERSION     WP_007196317.1
KEYWORDS    RefSeq.
SOURCE      Hoeflea phototrophica
  ORGANISM  Hoeflea phototrophica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Hoeflea.
REFERENCE   1  (residues 1 to 696)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 696)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Hoeflea phototrophica"
                     /db_xref="taxon:244596"
     Protein         1..696
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72058
     Region          1..696
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 msgtltrllr pksvvyiggs qiagpiraar ragydgeiwv vnpvrdeieg iacyaaiadl
       61 psppdaavvg lspersikav gelrqagagg avvmssgfle lgtdagrdlq qrlvaaagem
      121 allgpncmgl inqfsgaavw gddnhierqh gpaaaiisqs galligitnv eqafplgfai
      181 slgnqavtgt pelihalled driraiglyv egindgeafg qacraalikg vpvialkggd
      241 gadgskisls htasmvverd lwesfctrfg ivevsspkal vetlklltvg glpkgnrlsi
      301 vsysgglngl aatrcgslgl klpmptqang afirdllpet vtlsnpldln ipfsasdgsi
      361 smrdtkgvad aiaafaedvs dqivffidvp rpgagnldrv wcdsmealie vrnrlgipvs
      421 vagilpegla tdfrkhmqtn gvaallgysd tmealavsar iaanrarilk qnrpepliag
      481 gepqgammhn eavskaalka fglttphhiv vpiedaanaa sslgfpvtvk vhsdtiahka
      541 riggvhlnlg dsamvtaavv smtetvsrae gghavthvlv esmiagaeae lilgikrhps
      601 mglalmigkg gvhaedlavf etvllpidgp eldralhrlg yrnheavlaa ahavanyals
      661 naaelvtldv npllittdgq aiaadalivl ggkvag
//
LOCUS       WP_007197807             820 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Hoeflea phototrophica].
ACCESSION   WP_007197807
VERSION     WP_007197807.1
KEYWORDS    RefSeq.
SOURCE      Hoeflea phototrophica
  ORGANISM  Hoeflea phototrophica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Hoeflea.
REFERENCE   1  (residues 1 to 820)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 820)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 820)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..820
                     /organism="Hoeflea phototrophica"
                     /db_xref="taxon:244596"
     Protein         1..820
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=90030
     Region          10..820
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mmrilkglik lilvvtpllv maigggmlwl srsqapvdge mqiaglsaev siardgngvp
       61 hikaatradv aaglgfvhaq erlwqmevsr magqgrlsem fgaatidtdi wlrtmgihea
      121 avaslavmde dtmamlegya rginawmtrn pqafssrlpp eyvilgyepe pwspehtlta
      181 ikmmsislaa nldeealrlg fyrmgfseae mldllpyvda dnpppmpdlr illgldsgei
      241 gadvttaavs rfgeveallg tgasnnwvls gertasgqpi vandphllls apsiwylahl
      301 evtkefdepr rligvslpgt pyvllgrgnd iawgftntat daqdvfveri npdnpdqyla
      361 ptgwvqfgqk eetikvkggd arvftrrwtr hgpvlpagfk hfdkllpent vaalqwtala
      421 nddttalvgp rlyamqtved fqngfdaflt pmqsmvvadr sgnigfvaag rvpqrdpanr
      481 lmgrapapgw naiydwrgya pyaalprqtn pesgviatan tkivgpdypl hltfdweeay
      541 rqqridslla epgelhsmaa shrmqadiys pafaglnprm lalldqsals aeeqglaaql
      601 adwdgmmare qaeplifmaw lraamiatfe ddlgitfknw mrargkvmer lvdgqtarnw
      661 cdvtdtsdee scseiftrsf ssaiadlktr ygddaskwrw gtahyakggh rpfgevgllr
      721 rffnvevess ggpftldrgy tqfyndddpy antnassyrg ifdlsdldrs tyiqttgqsg
      781 nvfsghysdf aglwanvqsi eipstgveep dglwtlspge
//
LOCUS       WP_007198081             342 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Hoeflea phototrophica].
ACCESSION   WP_007198081
VERSION     WP_007198081.1
KEYWORDS    RefSeq.
SOURCE      Hoeflea phototrophica
  ORGANISM  Hoeflea phototrophica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Hoeflea.
REFERENCE   1  (residues 1 to 342)
  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 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 342)
  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   4  (residues 1 to 342)
  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 342)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Hoeflea phototrophica"
                     /db_xref="taxon:244596"
     Protein         1..342
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37763
     Region          27..209
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          254..335
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtlrladrye aaaglasais tyaaslgida dpiarasgld pdrfdqiger vkldrlcrym
       61 ealalisgdd lfglksasmf tkgasgtfgy allnaptlrd vlvflgrnmr kisnlkictl
      121 eigakdaife wtyspliihr dqyvdmtlaq tlahfepflg qdikscrlel erkkpgninl
      181 hkqllgpktr fgatinrlii pasylsrtnp nadirlhkil vqqieaipfs pvdttdtvts
      241 irlhvierla sgipslkdea erlgmsartl qrrlteagts mqeiiddsrk emaqnlltet
      301 tlslseisfq lgfsapaaft rsairwfgkt psayrkqpss pd
//
LOCUS       WP_007203374             360 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Fictibacillus macauensis].
ACCESSION   WP_007203374
VERSION     WP_007203374.1
KEYWORDS    RefSeq.
SOURCE      Fictibacillus macauensis
  ORGANISM  Fictibacillus macauensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Fictibacillaceae; Fictibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Fictibacillus macauensis"
                     /db_xref="taxon:245160"
     Protein         1..360
                     /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=41517
     Region          1..286
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mrtvnskdlk isnmkgllif lvvfghliev ykstyynvfv fiysfhmplf ilisgylakn
       61 vkgkkilnll llyvvfqaff nflvyvigve ktlqwgyekp qfhlwyivsl cvwyalaygl
      121 krishallvv avvscvvlva vasryyahdv vsmlktvdpe mstytlsyqr tlsfapfflv
      181 gffitrerlq rlyvsfhrvg yitcgavivw lllyiqknph leqlfrgsyg ahrfmghgdg
      241 ylekmflhyg vafllswlll ksvtsrrswl ttwgdhslti flfhpifvfi lqanpswlqs
      301 vqkdtrlill gmgamlisal laskalnrlv sriiapyetl lvvyqvmrai fsrktegair
//
LOCUS       WP_007180116             161 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ribonuclease P protein component [Paraburkholderia].
ACCESSION   WP_007180116
VERSION     WP_007180116.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Reiter,N.J., Osterman,A., Torres-Larios,A., Swinger,K.K., Pan,T.
            and Mondragon,A.
  TITLE     Structure of a bacterial ribonuclease P holoenzyme in complex with
            tRNA
  JOURNAL   Nature 468 (7325), 784-789 (2010)
   PUBMED   21076397
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Harris,M.E. and Christian,E.L.
  TITLE     Recent insights into the structure and function of the
            ribonucleoprotein enzyme ribonuclease P
  JOURNAL   Curr Opin Struct Biol 13 (3), 325-333 (2003)
   PUBMED   12831883
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Pace,N.R. and Smith,D.
  TITLE     Ribonuclease P: function and variation
  JOURNAL   J Biol Chem 265 (7), 3587-3590 (1990)
   PUBMED   1689306
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..161
                     /product="ribonuclease P protein component"
                     /EC_number="3.1.26.5"
                     /GO_component="GO:0030677 - ribonuclease P complex
                     [Evidence IEA]"
                     /GO_function="GO:0000049 - tRNA binding [Evidence IEA]"
                     /GO_function="GO:0004526 - ribonuclease P activity
                     [Evidence IEA]"
                     /GO_function="GO:0042781 - 3'-tRNA processing
                     endoribonuclease activity [Evidence IEA]"
                     /GO_process="GO:0001682 - tRNA 5'-leader removal [Evidence
                     IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
                     /calculated_mol_wt=17767
     Region          35..118
                     /region_name="RnpA"
                     /note="RNase P protein component [Translation, ribosomal
                     structure and biogenesis]; COG0594"
                     /db_xref="CDD:440359"
ORIGIN      
        1 mpgseargna gtaeaqqlgs vplraqaafp kaarllktde fssvfrlrpw rrtahfvvyg
       61 rptgnearlg lvigkkyapr aatrnlvrri areafrlrra dfggwdvllr lhtrfdkkal
      121 psasspplra lcrseieall dkaarevtrr eappaeapkt e
//
LOCUS       WP_007203609             394 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Fictibacillus macauensis].
ACCESSION   WP_007203609
VERSION     WP_007203609.1
KEYWORDS    RefSeq.
SOURCE      Fictibacillus macauensis
  ORGANISM  Fictibacillus macauensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Fictibacillaceae; Fictibacillus.
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
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 394)
  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   5  (residues 1 to 394)
  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   6  (residues 1 to 394)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 394)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 394)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Fictibacillus macauensis"
                     /db_xref="taxon:245160"
     Protein         1..394
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41804
     Region          17..56
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          76..390
                     /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 mqrgtfqlmk slnrtiilnk vrlegpisra qiakdtsltp ptvssivkel isdglimese
       61 qgaskggrkp tmliinsnsf yvigvdagpt dittvltnle ghiltsfkrv lpfpltnddl
      121 lammieeiqk vfvqedklig igvgmhgvvd shngralyap nlnirdvnik dvleatfglt
      181 vmvendakal algevwfgea nrlshiaavn vgngigagmi angkivqghh fiageighmt
      241 idiggkpcsc gnygclqtla agpaiaeraq keiaigresv lkemmdgdlq gidgqlvyea
      301 akqgdelsih vlqttgnylg igltnlihil npehiiiggg vanagdflln avretvakma
      361 lteqakqtti tlstlgekgt vlgavalvlq dlfe
//
LOCUS       WP_007204225             384 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Yoonia vestfoldensis].
ACCESSION   WP_007204225
VERSION     WP_007204225.1
KEYWORDS    RefSeq.
SOURCE      Yoonia vestfoldensis
  ORGANISM  Yoonia vestfoldensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Yoonia.
REFERENCE   1  (residues 1 to 384)
  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 384)
  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 384)
  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 384)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Yoonia vestfoldensis"
                     /db_xref="taxon:245188"
     Protein         1..384
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=41093
     Region          20..371
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mtdaakdktm lnapstakam srrrallgcg aaltgaaala apaiaqgapr ilrlasswpa
       61 glggladsat rlaeqinivs dgryhielyw pgelvpafgv hdavgagevd lyhsaeyyfq
      121 nkhrgfnfft tvplglttpe qtawtkfggg qalwdelnar ynvkaiacgg tgiqmggwfn
      181 keilttddfe glimrlpglg aqvlaamgat avslpadgiv salfegsida tewvgpyndl
      241 qfgfqklltt yiypgfhepg tmasfgmnld lwnsldardr alfeticdae ltshtadfyg
      301 nngialvqll aesgvqptrl pddvwnelsr vsfdvtasva ndddlgrriv esyeayralv
      361 ngagaisqte yfarrgavdl fadl
//
LOCUS       WP_007204734             259 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Yoonia vestfoldensis].
ACCESSION   WP_007204734
VERSION     WP_007204734.1
KEYWORDS    RefSeq.
SOURCE      Yoonia vestfoldensis
  ORGANISM  Yoonia vestfoldensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Yoonia.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Yoonia vestfoldensis"
                     /db_xref="taxon:245188"
     Protein         1..259
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=29016
     Region          3..>55
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mlieastlkg fkisatdgsv gtvtdflfdd qswtlrwvvv etgswlsgrk vllpvsvlgh
       61 pdtsansfpv rlttksvkds pdidthnpvs rqheermyrh ynmspywgng fymggyggwt
      121 agmsethyad smlrqdalda krnqqrhqsd ephlrsinam tgynlhatdg aighvegfvi
      181 ddtdwtihfl tvntknwwpg khvvisprsa knvswadsvv nldvdrqtvm nsptydpsvp
      241 mdaafetrma rhyipdatk
//
LOCUS       WP_007204780             751 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Yoonia vestfoldensis].
ACCESSION   WP_007204780
VERSION     WP_007204780.1
KEYWORDS    RefSeq.
SOURCE      Yoonia vestfoldensis
  ORGANISM  Yoonia vestfoldensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Yoonia.
REFERENCE   1  (residues 1 to 751)
  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 751)
  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 751)
  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 751)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..751
                     /organism="Yoonia vestfoldensis"
                     /db_xref="taxon:245188"
     Protein         1..751
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=79255
     Region          163..735
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 makadiskfd ddtgplvaeg adeevieynr rlyegwvrwa maaalaiyaf fhiaalngls
       61 irdmtggvvn lpflprlpme swtyrtvhia gatalgflmf sgtsfsertg tgrdrlfsyl
      121 ayalmipalf slgvtfwfqs liaagtswng mdptiqfner wlfgipliga tfgaialswv
      181 hqrprtrvnp adlvlvvaal avasylvtiy ntpirattgt sfaplgisla giagtalile
      241 ltrrvtglal piiagifliy vwlghlapgv lnspqialqr ffsqvytdvg ilgqttsvss
      301 tyiilfiifa aflqaskvge yfinfafalt grqrggpakv aifasglmgm ingtsagnvv
      361 atgsltiplm hkvgydkkts gaieaaastg gqimppimga gafimaeitg ipyqeiaiaa
      421 iipsilyfas vyfmvdlsaa rigmtgmrae elpkvkammk qvflflpiii liaalfagys
      481 viragtyata aaavvswltp yrmgvrsvay afqiagsmsi qiiavcacag iivgvisltg
      541 vgarfsnlll glagvsqlla mffamviail lgmgmpttaa yavaasvvap glirlgidpl
      601 tahffvfyfa vvsaitppva lasyaaagis gadpmatsfa sfkiglaafi vpfmffynga
      661 llmnapwlei lqalttalvg vyflaaavqa wlwgkaagpl trvgllvasl fmisgglltd
      721 ilglgiavgl ilinrtfgpd sktplvqgra d
//
LOCUS       WP_007204878             192 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Yoonia vestfoldensis].
ACCESSION   WP_007204878
VERSION     WP_007204878.1
KEYWORDS    RefSeq.
SOURCE      Yoonia vestfoldensis
  ORGANISM  Yoonia vestfoldensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Yoonia.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Yoonia vestfoldensis"
                     /db_xref="taxon:245188"
     Protein         1..192
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=20900
     Region          1..163
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlrglydgtv alartryalw alglvafves sffpippdvl mipmiiarps rafviaavat
       61 lcsvlgglfg yyigfalyet igvqilqfys keayftefav tynsygawav lvagvtpfpy
      121 kvitiasgvt qlslpmfiaa sivaralrff lmaallwkyg apirdfierr lglmfalfcg
      181 lliggfavlg vm
//
LOCUS       WP_007204922             823 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Yoonia vestfoldensis].
ACCESSION   WP_007204922
VERSION     WP_007204922.1
KEYWORDS    RefSeq.
SOURCE      Yoonia vestfoldensis
  ORGANISM  Yoonia vestfoldensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Yoonia.
REFERENCE   1  (residues 1 to 823)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 823)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 823)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..823
                     /organism="Yoonia vestfoldensis"
                     /db_xref="taxon:245188"
     Protein         1..823
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=89893
     Region          9..818
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mftlfrwavr ltttlivlmv agvvlawyfa trslpdydat aqvagisapv eivrdnanvp
       61 hifgatdedv ffglgyahaq drlwqmtmlr rtvqgrlsel ygartfdidq vlrrydlyna
      121 atasvvaqda stlaaltaya dgvntwldev nkgalgrgap emwlfnhpia rwqpadsiai
      181 lklmalqlts slenevlrar vslivsparl sdvlpddpgs gvaalpsyaa lvpdvvpnqp
      241 strmaydplm pvppralaga snawaanatr satgstllan dphlgltaps iwflarlele
      301 gggviggtip gvpliltgrs anlgwgltta nvddqdvfle evnpnnseey rgldgwqsfv
      361 srdsiitikd apsvtirlrw tengpvipdd lfdlgtitpp ghvtaigwta lsqtdtsmsa
      421 amalmrarnv dqaiaagelh vapaqnltla drnrvamqti gaipmrdanh qsqgrypsfg
      481 ylpenrwqgv sayvdnprfv dpdggivgnt nnkmidrpfp rhvsfdwgdt qrvirwrrlm
      541 qarevhtrds fieaqldsvs ftartlltfm gadlwftgda apdgtperrr qialellaaw
      601 ngemnehlpe pliyaawara fqarvirdel gplaaefthl dpvflerifr dvdgasiwcd
      661 viqsapvetc adiarqalde aliwiaenhg taieavrwgd aheathdhpv lgatpilgwi
      721 vnirqstsgg dntlmrgrtr gtgpapfqnv haagyravyd fadpdssvfi sstgqsghpf
      781 sryydnlgem wrrgeyipms ldpdlaraaa vgvttlvpve sse
//
LOCUS       WP_007205062             314 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Yoonia vestfoldensis].
ACCESSION   WP_007205062
VERSION     WP_007205062.1
KEYWORDS    RefSeq.
SOURCE      Yoonia vestfoldensis
  ORGANISM  Yoonia vestfoldensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Yoonia.
REFERENCE   1  (residues 1 to 314)
  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 314)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 314)
  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   4  (residues 1 to 314)
  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   5  (residues 1 to 314)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Yoonia vestfoldensis"
                     /db_xref="taxon:245188"
     Protein         1..314
                     /product="TRAP transporter small permease subunit"
                     /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=35030
     Region          88..294
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mglveawggn afgwiaaqli aafynigfal lnpglwlswv pqingpmdpa akqalarfiy
       61 ygasvelffa vlvifavvti aglifnafmw rcvrvlegfa nsvgraaawa gllmvlqqiv
      121 iiflqgifav sdisiglgvt ferpvswwsd elklynaivi tlcatytfvq gghvrvdlly
      181 apmsfrakrc vdmfgalffm vpsaiviwiy gwffmwrhlv lpnasasdtl drlmtrsqaf
      241 qwnietists angfdayflf killlvftfm vllqavavfy rsllerkege aseakyldkd
      301 ktgdeiadls akih
//
LOCUS       WP_007205709             279 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Yoonia vestfoldensis].
ACCESSION   WP_007205709
VERSION     WP_007205709.1
KEYWORDS    RefSeq.
SOURCE      Yoonia vestfoldensis
  ORGANISM  Yoonia vestfoldensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Yoonia.
REFERENCE   1  (residues 1 to 279)
  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 279)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Yoonia vestfoldensis"
                     /db_xref="taxon:245188"
     Protein         1..279
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29354
     Region          3..279
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mtlktlaevl qpalrdnyav pglvclgwed mrayvmaaqe erapvilqag pscrahtplp
       61 vlgammrhla tsvdvpvvvh ldhgytfeec raaldagfts lmydgsrkpl aqnidetari
      121 aelahaagis cegeigfvgy sggensagtd paeaaifard sgvdamaisv gnvhlqtdhe
      181 ggldedrira ietltdvplv ihggsgvpya qrlalatgsr iakfnigtel rmafgaalrd
      241 avnadparfd rvsilkethd pvmsaaravi rglgasgra
//
LOCUS       WP_007209296             653 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Enterococcus
            italicus].
ACCESSION   WP_007209296
VERSION     WP_007209296.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus italicus
  ORGANISM  Enterococcus italicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 653)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 653)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..653
                     /organism="Enterococcus italicus"
                     /db_xref="taxon:246144"
     Protein         1..653
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=75558
     Region          35..636
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mekipkekiv fipevdteiv sdlapfnfti erdkllidds favpyvitky nnkprgnwfn
       61 rirkmsgdit ishyytkang nalndyynrt iknkqaeidr shdpltiirl eremkiaqtq
      121 leqavdents ylylytyvli ksksetklkk lcedfetrci asgvkalipy tmidkaywsa
      181 lplqsnevpe ytytiansis assifpfddn elsiftkhmm ieginkdten ivsidytdrk
      241 lvvnrnkfvf glsgggktty ltsdylkkya fsdnstelkh rivlfdpede qtervrslgg
      301 evislssmsd vrinpfqiys rntpdgtfke slsdfeedel idtleikpkd fqmtdreidk
      361 eiskrlnslt pyflmvdhsi tdsqlsivkl eakkcyttlc ekknlakmen tdfptfsdle
      421 krlkdlektd fkryqriedf iysledftvg srtifnghtn idlnnplicf slrdlqteeg
      481 irdlaylnsf sylfeevtnn phivtsvyad efhfllknki sadfffqayk rfrkynadct
      541 vstqqiddvl kasdnigkai ignsftkvff gldetdaqgi snelklkltk kelsfitskr
      601 qgeallfhgt krakirvdlt qeemrllnpd gyediygvsp kkeinwlvrs kiq
//
LOCUS       WP_007207063             169 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Enterococcus italicus].
ACCESSION   WP_007207063
VERSION     WP_007207063.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus italicus
  ORGANISM  Enterococcus italicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 169)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Enterococcus italicus"
                     /db_xref="taxon:246144"
     Protein         1..169
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18415
     Region          5..152
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 msqmattkqe qyelilaqla glleietnwi anlanssall ndafsdtvfa gyyvytdgel
       61 vlgpfqgkvs ctriklgkgv cgeaaetkrt livddvtthk nyiscdsaam seivvpmlva
      121 dkligvldld srkfssydai dqeylekfva lltasyqket vskafsseq
//
LOCUS       WP_007211265             585 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Bacteroides
            cellulosilyticus].
ACCESSION   WP_007211265
VERSION     WP_007211265.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 585)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..585
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=67029
     Region          40..>180
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Site            order(67..68,71..72,74,104,107..108,111..112,114..115,144,
                     147..148,151..152,155)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          67..91
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          102..132
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          109..>260
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          137..171
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          512..581
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mklscflaff llwvvnsfrt satvpdsllt ertirsiyvn ypdsalrlld eaekspasgi
       61 ipfridllra mcyeikhdlt akeicvrral qndsirlvpe rklssitmla nilerqnrye
      121 esigvchegi dlarnlackk eesdmysvma rvcigmtnde maqeyfqrav kllegtddvr
      181 emsrlstiyg eymsfyinrn rmaeaieigy rretviqrms glpgpppgyi dqqygflyak
      241 mavllhdegk keeateifrk yqstsfsktl igkqysvpyl lninqyaeaa alsdtcisaf
      301 tndtvsyeyl illnyraras rgmkrfdlad vftqrgwvvq dsiytresks kaqeyaskfe
      361 lkekelqlak shalserrml llagscvltv lliiilwttf vnlqktkmrn riaakqidel
      421 laqreelrkv ftqtrnthet tkeigtgspl peeetltaat ktdvaapgtn sdenyakfmk
      481 mesqlieqkl flkpgfgrdd lirvtdinkn dlspllrrya gsdnfndyln glkieysikl
      541 mkekpylsvd aiaeeanfns rstfyrafvk isgmtpaqym rtkie
//
LOCUS       WP_007211715             687 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Bacteroides cellulosilyticus].
ACCESSION   WP_007211715
VERSION     WP_007211715.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 687)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..687
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=74002
     Region          4..686
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mitnqllrpa sivvvgasnn vhkpggailr nlinggytge lravnpkete vqgvtayadv
       61 kdipdtelai laipaqmcpd avevlaaekq vrafiilsag fgeethegal ledriletvn
      121 kygasligpn ciglmntwhh svfsqpipql hpqgvdliss sgatavfile savtkglqfn
      181 svwsvgnakq igvedvlqym denfqadkds kikllyiesi gdpdrllfha sslikkgcki
      241 aaikagsses gsraasshtg aiassdsave alfrkagivr cysreelttv gciftlpelk
      301 gknfaiitha ggpgvmltda lskgglnvpk legpvvdelk sklfpgvavg npidilatgt
      361 pdhlrlcley ceekfdnida vlaifgtpgl vtmfemydvl hekmqtcskp ifpilpsint
      421 agaevaafla kghvnfadev tlgtalsrim nasrpaanei elfgvdvpri rriidsiped
      481 gyiqphyvqa llhaagipiv eefvsankde vlafvrrtgf pvvakvvgpv hksdvggvvl
      541 nikgeehlaf efermmqipe vtgiliqpml tgtelfvgak yeekfghvvl cglggifvev
      601 lkdvssglap lsyeeaysmi hslraykiik gtrgqkgvne dkfaeiivrl stllrfatei
      661 kemdinplla tekyviavda ririekk
//
LOCUS       WP_007212619              98 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [Bacteroides].
ACCESSION   WP_007212619
VERSION     WP_007212619.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..98
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11456
     Region          3..98
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mktteeilni lrefkhtagd kygieqialf gsaargelre dsdidvcvkp rkaidyftlq
       61 dvreeleklf qrkvdlltlh enmrqlfrqn ierdaiyv
//
LOCUS       WP_007213009             342 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Bacteroides].
ACCESSION   WP_007213009
VERSION     WP_007213009.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 342)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..342
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=39077
     Region          206..341
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkhfvlfacv avglifagcr nrqeppvpvv vqeaepkdta vlefphpkek qltaadislt
       61 kellydqhtl edtypykdtv rsfkwdvirn clayienmqr dttarwvvlq nyknlnkeap
      121 lvrkfvrnvy rrvsdtlgve ryqsvplylp adtlvperyg rdgtiaylkg eegsfyrilp
      181 atfeeewlap rsylkqlpds tvfnhvifvd rldqnittle hvsegewkir smnpattgmh
      241 appyaqetpl gmyllqqkkt rmvflkdgsa etggyapyas rftngayihg vpvnaprtsm
      301 ieyswslgtt prshmcvrna tshskfvfdw apterslvvv ie
//
LOCUS       WP_007213010             236 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Bacteroides].
ACCESSION   WP_007213010
VERSION     WP_007213010.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 236)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..236
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=25882
     Region          53..217
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mlrfivfilf lflpctlflg gkssdstpds aeraavsdve ayaslyrsmq lggvvnwkaf
       61 rqavagyyki dnrkrevltl idfsrpstak rlfvfdmrer kvlfssvvsh gknsgdnyat
      121 sfsneygsyk sslgfyltes tyqgkngysl ilnglekgin drareraivm hgaayadpsv
      181 vsrggrlgrs fgcpavpqkl srpiidaikg gsvmyiyaet peylahssvl kgadgl
//
LOCUS       WP_007213089             105 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Bacteroides cellulosilyticus].
ACCESSION   WP_007213089
VERSION     WP_007213089.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..105
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11635
     Region          1..98
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(6..7,25..26,34,37,39..40,42,45..46,48,56,61,68)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(25,56..57,59,80)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mdktsfgeev ysvvasippg rvltygqiay ligkpqcsrm vgqamhnape eqnlpchrvv
       61 nsqgrlapfw peqrelleke gtvfkkngcv dmktsgweil kevis
//
LOCUS       WP_007213660             186 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Bacteroides].
ACCESSION   WP_007213660
VERSION     WP_007213660.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..186
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20574
     Region          4..161
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mnevlkaiks rrsvrayteq qisqedlnai leaatyapsg mnyqtwhfta iqnaavleel
       61 nekikgafak seeprlqerg hsqtyccyyh aptlvivsne ptqwwaamdc acamqnifla
      121 akslgigscw inqlgqtydd pevrafltkl gipenhrvyg caalgyaaaa pvkerqlaeg
      181 tvtiik
//
LOCUS       WP_007214112              98 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [Bacteroides].
ACCESSION   WP_007214112
VERSION     WP_007214112.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..98
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11116
     Region          3..97
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mktkndyisl lkscgselkq qfgvrslhlf gsvarneqke tsdidiyvet etpnpflivr
       61 mkaylekllg csvdvirahk nmnaflkqqi ekdgihvf
//
LOCUS       WP_007214894             307 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Bacteroides
            cellulosilyticus].
ACCESSION   WP_007214894
VERSION     WP_007214894.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (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   2  (residues 1 to 307)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..307
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35408
     Region          219..297
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mkdtvldlsf qdylermnpq ssfqeqlvvi ylddsvtked kvgrypmqle asslilvvsg
       61 emqievdylp ytlkrstvmq lladniignv sytpgfrgyl llfspelkqe imsltssirl
      121 peagnlkrly peqsltddec aivlnrieri kkyiadsdhl yratviknev inlllditns
      181 rwkkygerei sfsrneiirq rfhelllgnc rkhrdvgfya qelcvtpdyl skiirecdgq
      241 salkwitnav vteaklllrr pdmnvsqvai elnfpdqstf gkffkrntgm aparyradal
      301 rkaihyt
//
LOCUS       WP_007215649             236 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Bacteroides].
ACCESSION   WP_007215649
VERSION     WP_007215649.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 236)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..236
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=25926
     Region          53..217
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mlrfivfilf lflpctlflg gkssdstpds aeraaasdve ayaslyrsmq legvvnwkaf
       61 rqavagyyki dnrkrevltl idfsrpstak rlfvfdmrer kvlfssvvsh gknsgdnyat
      121 sfsneygsyk sslgfyltes tyqgkngysl ilnglekgin drareraivm hgaayadpsv
      181 vsrggrlgrs fgcpavpqkl srpiidaikg gsvmyiyaet peylahssvl kgadgl
//
LOCUS       WP_007217174              97 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Bacteroides
            cellulosilyticus].
ACCESSION   WP_007217174
VERSION     WP_007217174.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..97
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11130
     Region          3..97
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mkskteyqki lchyfeevas qqgitrmalf gsvargeqne dsdvdvayeg tpnlflrvrm
       61 kmdleklfgc kvdlirlrkq fsgtlfgeel drdliyv
//
LOCUS       WP_007217968             350 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Bacteroides
            cellulosilyticus].
ACCESSION   WP_007217968
VERSION     WP_007217968.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 350)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..350
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38374
     Region          7..337
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mglyrfqntg ieaisatvpk kivktrsltg yyseeaiekf idatgveerr fsdenicasd
       61 lcyksaceif dnttirredi dmlifisqtp dykipgtsvs mqdrlglsrd tlvydvnmsc
      121 sgfihgllma ysflqmsdin hvmimvgdtl sklislqdkg tgmllgdagt aivvgkgdrf
      181 gesffsmste gsntnsvfip aggsrrpssa ktlamqefed gsirneeqii mvgpdvfsfa
      241 iselpkdikk llafankkie dvdkyafhqa nnfmtgyiak kakadvnkml ksihkygnta
      301 gtsiplcmve nrnkinvges ilmnaigagf aygtvllnia dckileltel
//
LOCUS       WP_007217969             333 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Bacteroides
            cellulosilyticus].
ACCESSION   WP_007217969
VERSION     WP_007217969.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 333)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..333
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36665
     Region          3..331
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 meayikaisy ylpeqiidnk tlakefpews eekiekklgi kirhiarede taadlaikaa
       61 ealfseyrid kdiidycilc tespdyilpt tacliqdklk lsnkigvldi nlgcsgfias
      121 lsvakglvfa gvaknilllt aetyskymhp rdkgnrtifg dgatasiist eglaqigefs
      181 fgtdgagaen livktggarn rtplndltfd dfgnprssdy iymngpeiln ytldripevt
      241 aevlerngli ledidlhvfh qankyiaglq rrklrvpeei yyccyensgn tvsstipial
      301 vhalkdgsik qgtkvlsvaq glgytwggvi lff
//
LOCUS       WP_007217983             352 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Bacteroides
            cellulosilyticus].
ACCESSION   WP_007217983
VERSION     WP_007217983.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 352)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..352
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39079
     Region          7..340
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 marwkiknvg mkgvsmavpe nvvktsdfdf fsqeeaevfd ntvgirrrhi gpdnmcasdm
       61 cqaaaeklle elgwerdsid vllfesvtgd yrtpptscil qdrlalsenc fcmdipmgcc
      121 gcmyaitvag nllttgnvkr allligdtal rmgsmkdksr vplfgdcgta ialeydeaan
      181 divvdfhtyg kgyealmtph ggfrypatpe sfeyedfgng ivrapihtli ngmnvfsfai
      241 srppksiesf ladynldrnv didyflihqa nkmivdrivk klklpqekvp ynleefgnlg
      301 gasipslmvt rlrgqllske ttllmssfgl gltwgtmwmk tkpmiipeiv im
//
LOCUS       WP_007219240             687 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate--CoA ligase family protein [Bacteroides].
ACCESSION   WP_007219240
VERSION     WP_007219240.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 687)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..687
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73974
     Region          4..686
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mitnqllrpa sivvvgasnn vhkpggailr nlinggytge lravnpkete vqgvtayadv
       61 kdipdtelai laipaqmcpd avevlaaekq vrafiilsag fgeethegal ledriletvn
      121 kygasligpn ciglmntwhh svfsqpipql hpqgvdliss sgatavfile savtkglqfn
      181 svwsvgnakq igvedvlqym denfqadkds kikllyiesi gdpdrllfha sslikkgcki
      241 aaikagsses gsraasshtg aiassdsave alfrkagivr cysreelttv gciftlpelk
      301 gknfaiitha ggpgvmltda lskgglnvpk legpvvdelk sklfpgaavg npidilatgt
      361 pdhlrlcley ceekfdnida vlaifgtpgl vtmfemydvl hekmqtcskp ifpilpsint
      421 agaevaafla kghvnfadev tlgtalsrim nasrpaanei elfgvdvpri rriidsiped
      481 gyiqphyvqa llhaagipiv eefvsankde vlafvrrtgf pvvakvvgpv hksdvggvvl
      541 nikgeehlaf efermmqipe vtgiliqpml tgtelfvgak yeekfghvvl cglggifvev
      601 lkdvssglap lsyeeaysmi hslraykiik gtrgqkgvne dkfaeiivrl stllrfatei
      661 kemdinplla tekyviavda ririekk
//
LOCUS       WP_007220520             209 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Candidatus Jettenia sp. AMX1].
ACCESSION   WP_007220520
VERSION     WP_007220520.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Jettenia sp. AMX1
  ORGANISM  Candidatus Jettenia sp. AMX1
            Bacteria; Pseudomonadati; Planctomycetota; Candidatus Brocadiia;
            Candidatus Brocadiales; Candidatus Brocadiaceae; Candidatus
            Jettenia.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Candidatus Jettenia sp. AMX1"
                     /db_xref="taxon:2293637"
     Protein         1..209
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=23390
     Region          17..179
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mkyeeamels qvkkaglhrr lyewtlhwah tpygafalfa lafcessffp ippdvllmal
       61 afsipkksfk yaaicsagsv lggcfgyfig yqffeylglp ilnfygitdk fdfvkeeyna
      121 nafiavaiag ftpipykvft iaagvckini wtfiiasavs rsgrffiiaa ltyvfgpkik
      181 dfidkyfnii siafvillvv gffiikllt
//
LOCUS       WP_007220549             299 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Candidatus Jettenia sp.
            AMX1].
ACCESSION   WP_007220549
VERSION     WP_007220549.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Jettenia sp. AMX1
  ORGANISM  Candidatus Jettenia sp. AMX1
            Bacteria; Pseudomonadati; Planctomycetota; Candidatus Brocadiia;
            Candidatus Brocadiales; Candidatus Brocadiaceae; Candidatus
            Jettenia.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Candidatus Jettenia sp. AMX1"
                     /db_xref="taxon:2293637"
     Protein         1..299
                     /product="formate/nitrite transporter family protein"
                     /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=31840
     Region          22..299
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msnaqnanpg sqeyaipvie idayapakma drvgmigvak sklstltlla lsilagvfia
       61 lgtqlamlvt htatsnygln qlvggaaftm aliliviaga elftgnclia msfmarkitg
      121 rdltrnliia fignfigalt lvlwiynsgq wminnhllga kivlaandkv nipfsaafar
      181 gvlcnalvcl giwlsysgrs nmdkilallw piscliasgf ehcvvnmwli pmalvlkgng
      241 svlaaaeniq ggkldlsnlt ffkgflidnm ipvvlgnlfg givlvagvyw fiylrpskr
//
LOCUS       WP_007220795             574 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Candidatus Jettenia sp.
            AMX1].
ACCESSION   WP_007220795
VERSION     WP_007220795.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Jettenia sp. AMX1
  ORGANISM  Candidatus Jettenia sp. AMX1
            Bacteria; Pseudomonadati; Planctomycetota; Candidatus Brocadiia;
            Candidatus Brocadiales; Candidatus Brocadiaceae; Candidatus
            Jettenia.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 574)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 574)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Candidatus Jettenia sp. AMX1"
                     /db_xref="taxon:2293637"
     Protein         1..574
                     /product="formate/nitrite transporter family protein"
                     /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=62392
     Region          21..238
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
     Region          284..557
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mpdtwdgtgk qkyiipvlei dtygsvemtn rvglvgvtks sldtlttlvl silagvfmal
       61 gaqlfilvth tatsnyginq lvggvaftla mvlivitgae lfagnclvam sfmarkisgk
      121 aftrnmvitf lgnfigalav vlclytsgqw mmnnhllgak ivltandkvn ipfgvvfarg
      181 mmgnallclg vwmcycgksn ldkilsllwp tsclmacgfe hcvvnmwlip mgiilkenra
      241 vlaaaekihg gipdlsnltp ckgkrkmaen nipestqtid rdvayspsqt asvvenkavi
      301 ragltvtqtl vlsilagiyv amgaqfatfv tsdsalhagf tsfitgivfs lglilvevag
      361 selftgnnln ivgylskkim trelfriwtl vyvgnfiggl mmvywmytah qweffhcmtg
      421 akalliahkk vnlsfeeala rgtlcnalvc lnvwlcyssr svadkvistl faiggfvasg
      481 fehcvanmyf ipmgvilrkh pdvvavaerm agktldlsql twkgffinnl lpvtlgnlig
      541 gviligavfw flylrphmry lsfssekefs tdse
//
LOCUS       WP_007222261             702 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Candidatus Jettenia
            sp. AMX1].
ACCESSION   WP_007222261
VERSION     WP_007222261.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Jettenia sp. AMX1
  ORGANISM  Candidatus Jettenia sp. AMX1
            Bacteria; Pseudomonadati; Planctomycetota; Candidatus Brocadiia;
            Candidatus Brocadiales; Candidatus Brocadiaceae; Candidatus
            Jettenia.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 702)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 702)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Candidatus Jettenia sp. AMX1"
                     /db_xref="taxon:2293637"
     Protein         1..702
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=77645
     Region          2..700
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 maiqwkksvc pycgigcglm vgieegkvvn ihgmkehpvn cgesctlvhn faplftdrdr
       61 ltqpmirrng tllpvtwdda imyvahefhr iireygpgai afyggaaafn eeyylinklm
      121 kgyigtnhve ctsrlcmast amgfistfga dapptcyadi eeadlfliag mnmavslpvi
      181 fnrvcaarka kgartividp rktettaiad vhlqirpgtd valnnalayi lleegfvhee
      241 evahyttgld dlklilkeys psrvaritgc tqeqifkaah lighakamlt fwlqgynqst
      301 qavfknntlh nlslltgnfc rpgagplsia gesnslgsrw mgvqshllpg mrfvtnpvhr
      361 qeiadfwgip aekiqstpgr siidiikglh tgevralwvm ssnpaaslpy tqwvteglek
      421 aeflvvqdil hptettvlad vilagaqwse ktvtlvsser rielaekile ppgmakpdye
      481 iicliagamg fskefsytsg eevfeelkei trgricdmng vsyerlrnti gpqlpcpktd
      541 hpgtarlfsd irfprpdgra allardyrkl aetadddypf ilitgrlasq fntgtrtrri
      601 kkltdiepnn fveihsadaq rlgiiegdev emasrrgsir civhikdhvl esnvymnlcc
      661 gnsplseddk qvnfvcntvy dahskqpelk ccavkitkva si
//
LOCUS       WP_007222581             814 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Candidatus Jettenia sp. AMX1].
ACCESSION   WP_007222581
VERSION     WP_007222581.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Jettenia sp. AMX1
  ORGANISM  Candidatus Jettenia sp. AMX1
            Bacteria; Pseudomonadati; Planctomycetota; Candidatus Brocadiia;
            Candidatus Brocadiales; Candidatus Brocadiaceae; Candidatus
            Jettenia.
REFERENCE   1  (residues 1 to 814)
  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 814)
  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 814)
  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   4  (residues 1 to 814)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..814
                     /organism="Candidatus Jettenia sp. AMX1"
                     /db_xref="taxon:2293637"
     Protein         1..814
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=91650
     Region          69..802
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mnyelsvhel rkrvdpvslg ikdtshirrl qgiigqkrav dalqfglkik dvgfnifvag
       61 qsgigkmcsv ksflediare ketppdwcyv nnfddpynpr viqlpagqgs klkedmntff
      121 nhiqkelpkv yeadeytahr eeilnklakq kekasqelsq kateegfaiq atpmgmvimp
      181 ikdggvlgdv eflalseskr eelqkrqdrl qseiksvmkn irklehctre kvkeldqkia
      241 lhvveevide lvekynnfpk ivnflhetqe dvlknietfk ilrqqkgaty ppsstpsdlq
      301 letmqqamlr kyevnvlvdn skqkglpviq ernptynnli griekevlfg alttdftmir
      361 agsllrangg flvisiedvl rnfnswdalk qalcscevqv eelgerlgym ttktirpqai
      421 pinvkvvlvg qpwfyhtlyf ydhefaelfk vkaefdirmd mteenindfl sfiatfcdke
      481 kmkhldneat agiieyasrl aedkeklstk fghladiire anfwtmqege sliksrhirk
      541 aldgkiyrsn lieeriremi drglilidtv gekigqvngl svinlgdyqf gkpnritvtv
      601 gpgdngiidi erevklagpi yskgvlivsg ylvnkymkgk mstltarvvf eqsyegiegd
      661 sasaaelysl lsalanipik qgiavtgsvn qlgqiqavgg inqkiegyyd vcrvkgltgd
      721 qgvvipksnv qnlmlredvi eavilkkfti wavntidegi elltgvtsgd mqndgtfppd
      781 tvnekvsrql adfekalkrs kdflgnvsgh rvts
//
LOCUS       WP_007222873             113 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Candidatus Jettenia sp. AMX1].
ACCESSION   WP_007222873
VERSION     WP_007222873.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Jettenia sp. AMX1
  ORGANISM  Candidatus Jettenia sp. AMX1
            Bacteria; Pseudomonadati; Planctomycetota; Candidatus Brocadiia;
            Candidatus Brocadiales; Candidatus Brocadiaceae; Candidatus
            Jettenia.
REFERENCE   1  (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   2  (residues 1 to 113)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Candidatus Jettenia sp. AMX1"
                     /db_xref="taxon:2293637"
     Protein         1..113
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12355
     Region          27..93
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mhilrkfcsv ivlvfaiafv cqticmsdeg vegkvninta tedqiallpg igpkiaievv
       61 nyrknngnfq tiedmkkvkg vgdkkfekik nfvavegdtt vkstkvvkvk epk
//
LOCUS       WP_007222910             202 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Candidatus Jettenia sp.
            AMX1].
ACCESSION   WP_007222910
VERSION     WP_007222910.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Jettenia sp. AMX1
  ORGANISM  Candidatus Jettenia sp. AMX1
            Bacteria; Pseudomonadati; Planctomycetota; Candidatus Brocadiia;
            Candidatus Brocadiales; Candidatus Brocadiaceae; Candidatus
            Jettenia.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Candidatus Jettenia sp. AMX1"
                     /db_xref="taxon:2293637"
     Protein         1..202
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21891
     Region          1..197
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 meniivgitg asgaiyaqrl lhilskkeyn ihlsisdaaa ivikhelgid lndnqpnlir
       61 llgcapdnvi yyrnsdisat iassrysika mvivpcsmnt lcsiacgisn nlvqraasit
      121 mkegrklvlv pretpfssih leamlklssa gacilpaapg fyynpktiad qidfvvakil
      181 dvlgighsli pqwhgeelmy re
//
LOCUS       WP_007223403              97 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Candidatus Jettenia sp.
            AMX1].
ACCESSION   WP_007223403
VERSION     WP_007223403.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Jettenia sp. AMX1
  ORGANISM  Candidatus Jettenia sp. AMX1
            Bacteria; Pseudomonadati; Planctomycetota; Candidatus Brocadiia;
            Candidatus Brocadiales; Candidatus Brocadiaceae; Candidatus
            Jettenia.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Candidatus Jettenia sp. AMX1"
                     /db_xref="taxon:2293637"
     Protein         1..97
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11439
     Region          3..97
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mksykkiedi lkkhkkelae kyrvkeigif gsyargeqkk rsdvdilvef eevpdlfkfl
       61 eleryleell gvrvdlvrke alreelkdtv lnevvni
//
LOCUS       WP_007219181             248 aa            linear   BCT 20-JAN-2025
DEFINITION  RHS repeat-associated core domain-containing protein [Bacteroides
            cellulosilyticus].
ACCESSION   WP_007219181
VERSION     WP_007219181.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 248)
  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 12859901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..248
                     /product="RHS repeat-associated core domain-containing
                     protein"
                     /calculated_mol_wt=27309
     Region          <3..127
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
     Region          <3..50
                     /region_name="Rhs_assc_core"
                     /note="RHS repeat-associated core domain; TIGR03696"
                     /db_xref="CDD:274730"
ORIGIN      
        1 mnwydygarq ydpalgrwna vdplaekyye mspyvycand pvknvdsdgr wfwaagtaid
       61 ygfqvynnys sgksgydawv gdvnfvsvgl sainpvgklk iaktlaveav kgtisytnnk
      121 gfavkndika itantlknta isigvgklte sssnkalenv nkemrttnqn vrtaqnrvnr
      181 hptseskraq ldnaksnaqq vrakqigtqm lnstigqins niveqtvtng tsklgliidw
      241 ndkkykke
//
LOCUS       WP_007230462             388 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Candidatus
            Seongchinamella marina].
ACCESSION   WP_007230462
VERSION     WP_007230462.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Seongchinamella marina
  ORGANISM  Candidatus Seongchinamella marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Halieaceae; Seongchinamella.
REFERENCE   1  (residues 1 to 388)
  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 388)
  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 388)
  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 388)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Candidatus Seongchinamella marina"
                     /db_xref="taxon:2518990"
     Protein         1..388
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=42319
     Region          18..378
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 maqgeterry spiiiltlva alvavlglwa adkagnqnsg gsagevvats neqfewklvt
       61 twpknfpglg saaenlatmv demsngrlki rvygggeivp algvfdavsq gvadaghgaa
      121 yywkgkvpss vfftavpfgl naqetfgwlh yggglelwee ayapynlvpm gggstgvqmg
      181 gwfnkeinsi edlqglkmri pglagevfta aggtsvtlpg selytslqtg vidalewvgp
      241 yndrifgfhq vakyyyypgw hepgsvlefi inkdslaalp ldlqaivrqa arassqdmld
      301 eytgrnnesl reliedhgve irrfpddvlk alwmgtqeam qklvaqdpma akvyasysaf
      361 ykgvrnyhhi seqayinmrd vvlededy
//
LOCUS       WP_007237187             321 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Gordonia otitidis].
ACCESSION   WP_007237187
VERSION     WP_007237187.1
KEYWORDS    RefSeq.
SOURCE      Gordonia otitidis
  ORGANISM  Gordonia otitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Gordonia otitidis"
                     /db_xref="taxon:249058"
     Protein         1..321
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33991
     Region          1..310
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mlldgaslwf rsfhalpekl taadgrpvna vrgfvdtias lvaahqptrl vvcldldwrp
       61 tfrtellpsy kahrvaqevp htgtddaedv dveevpdtlt pqvamildvl aaaglttsga
      121 tgceaddvig tlaaaesede vivvsgdrdl lqvvaddpvp vrvlyvgrgl akaelmgpte
      181 vadrygvpve ragtayaems mlrgdpsdgl pgvpgigekt aaklitaygd ldaleeaald
      241 tsstltprvr sslrdstgyl raartvvtvr tdaptvesrp ddhlpsapad pdrlanliee
      301 lrigasvgrl adalgwelrv r
//
LOCUS       WP_007237751             192 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Gordonia otitidis].
ACCESSION   WP_007237751
VERSION     WP_007237751.1
KEYWORDS    RefSeq.
SOURCE      Gordonia otitidis
  ORGANISM  Gordonia otitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Gordonia otitidis"
                     /db_xref="taxon:249058"
     Protein         1..192
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19989
     Region          76..167
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 mitalvvgvv agagaigvra vsghddpvsr lvaeagvgpa rqtfpttdts glspvrariv
       61 dvvhaeydrn apgtiysdgv eeswcadfvs tvmrkagvpf dnpnsgswri pgvatltdyl
      121 hssgrwraas hvpepgdivi ydapshfrqh tnivvamdgt tvttvggaea qgitvdhfdp
      181 rtvegvqgyg vp
//
LOCUS       WP_007238211             361 aa            linear   BCT 20-JAN-2025
DEFINITION  DNA polymerase domain-containing protein [Gordonia otitidis].
ACCESSION   WP_007238211
VERSION     WP_007238211.1
KEYWORDS    RefSeq.
SOURCE      Gordonia otitidis
  ORGANISM  Gordonia otitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Zhu,H., Nandakumar,J., Aniukwu,J., Wang,L.K., Glickman,M.S.,
            Lima,C.D. and Shuman,S.
  TITLE     Atomic structure and nonhomologous end-joining function of the
            polymerase component of bacterial DNA ligase D
  JOURNAL   Proc Natl Acad Sci U S A 103 (6), 1711-1716 (2006)
   PUBMED   16446439
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Zhu,H. and Shuman,S.
  TITLE     A primer-dependent polymerase function of pseudomonas aeruginosa
            ATP-dependent DNA ligase (LigD)
  JOURNAL   J Biol Chem 280 (1), 418-427 (2005)
   PUBMED   15520014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Gordonia otitidis"
                     /db_xref="taxon:249058"
     Protein         1..361
                     /product="DNA polymerase domain-containing protein"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=40160
     Region          4..314
                     /region_name="LigD"
                     /note="Eukaryotic-type DNA primase [Replication,
                     recombination and repair]; COG3285"
                     /db_xref="CDD:442515"
ORIGIN      
        1 masrspaeel dvdgvavrms npdkiyfpel genggrkrnl vgyyqrmaqs rddgsdgpvl
       61 talrdrptfl qrfpdgidgd eiyqkhlpkk rpdfvestri tfpsgrtgda lrptsaasiv
      121 waanlgtvtf hswptvaadn dhpdqlridl dpqpgtdfdd vrrvavella plldelgyag
      181 ypktsggrgi hvfvpieprw dfiatrrcgi alarelerrd pdavttswwk edrgerifid
      241 fnqnardrtm aapysvrrta iarvstpvtw aeladvepdd ctiatvpelv arrgdpmadi
      301 athrrglepl lemverddaq glgdmpypps ypkmpgeppr vqpskkvgah wdeegnrigp
      361 p
//
LOCUS       WP_007237879             384 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Gordonia otitidis].
ACCESSION   WP_007237879
VERSION     WP_007237879.1
KEYWORDS    RefSeq.
SOURCE      Gordonia otitidis
  ORGANISM  Gordonia otitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 384)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Gordonia otitidis"
                     /db_xref="taxon:249058"
     Protein         1..384
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=41291
     Region          37..247
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mstdhrpplv gqhtrptdad lecavdalid rggapslmfq piahlpqmnv agyevlsrfs
       61 chpgagpdrw faaaqrigre aelsalvltk alssrsqlpp rcflsinisp eallsdqver
      121 llgsgpldri vfeltehsvv ndyhtvasai anirslagfv avddagagya slrhilalrp
      181 dfvkldsslv qdlhrdqaks alvemfgefa sridawlvae giegqrdlhr lrqlgvplgq
      241 gyllgrpses mqalapetvd aaptalaapt etvaafvdvg htagfdtsda elratldsds
      301 dtpaitlldc ysrpvrlalr dgsrgvrrdh amcvlsssgh hevlrramtr plkrrfdplv
      361 ccdeagsytg lipidrliga laad
//
LOCUS       WP_007238663             206 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Gordonia otitidis].
ACCESSION   WP_007238663
VERSION     WP_007238663.1
KEYWORDS    RefSeq.
SOURCE      Gordonia otitidis
  ORGANISM  Gordonia otitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Gordonia otitidis"
                     /db_xref="taxon:249058"
     Protein         1..206
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22292
     Region          17..201
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mtdllpldpd elltttrsvr krldlerpvp ievvrealev aiqaptgsna qgwhwivitd
       61 tdlkrqvady yarsfaaysa qrtvstetar rvaasaqyla dvmgevpvlv lgaiktggel
      121 pegnqagvwg sllpgawslm lalrarglgs awttlhltye qevadllgip dgvhqgvllp
      181 iaytqgtdfs paqrkplddv lhvngw
//
LOCUS       WP_007240539             342 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Gordonia otitidis].
ACCESSION   WP_007240539
VERSION     WP_007240539.1
KEYWORDS    RefSeq.
SOURCE      Gordonia otitidis
  ORGANISM  Gordonia otitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 342)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Gordonia otitidis"
                     /db_xref="taxon:249058"
     Protein         1..342
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36032
     Region          12..338
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mthsptltla dvagylpdnr vpaaffseya esdaladnvm fsapayrhha aegetsadmm
       61 isaarilter hggdylddvt vvlthsqlpe vpvrgcggel adrlglrprt vldvhnggca
      121 afihmidlaa allsatgggk alvglaqnsa sqiftqdqvr gkaqaaipgd gaaaatvtld
      181 gengspvlgl ithsygeysa dmtsvaepdr ryweagpgqi higfteakit kvlargnrmv
      241 paaaievads igiapaaldw fitnqpnrif lrnwrealel pperhpdtfd ecgnlfgvgi
      301 pmtldaavtd griqsgdvvm msafahagdf agaaalrwsg rr
//
LOCUS       WP_007241358             190 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Haemophilus pittmaniae].
ACCESSION   WP_007241358
VERSION     WP_007241358.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus pittmaniae
  ORGANISM  Haemophilus pittmaniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 190)
  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   2  (residues 1 to 190)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Haemophilus pittmaniae"
                     /db_xref="taxon:249188"
     Protein         1..190
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=20035
     Region          120..189
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkslkslltl salalavsgs alatnnpltv vkdnamseak ttlqsnvdst kdsvaakska
       61 lkessvadkn altkkvdsvk ekvqsvkena katdgasvke tmqkkaddak akakekvndt
      121 qekikksakv nvnnadaatl qklsgigekk aqaiidyrnk vgkiknvael skidglgett
      181 iekitpyltf
//
LOCUS       WP_007243523             108 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Haemophilus pittmaniae].
ACCESSION   WP_007243523
VERSION     WP_007243523.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus pittmaniae
  ORGANISM  Haemophilus pittmaniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (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   2  (residues 1 to 108)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Haemophilus pittmaniae"
                     /db_xref="taxon:249188"
     Protein         1..108
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11413
     Region          39..107
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkllktlfga civasamlsn nalaedkvae staqtmqqsq advagklnin tagaaeiqra
       61 migigakkae aiiqyrekhg nftaveqlle vqgigkatle knrdritl
//
LOCUS       WP_007244067             833 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [Pseudomonas
            syringae group].
ACCESSION   WP_007244067
VERSION     WP_007244067.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 833)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 833)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 833)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..833
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..833
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90170
     Region          62..113
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          90..833
                     /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 mprparslhp lalavlmaca ampshavqps ppnadvstvr sfsisagdls qvlntfseqa
       61 glalafdpal trgkrspglq gqygtdeaia rllsgsglra talsanryri etapeavegs
      121 lelqattisg asrletatgp vtgyvatrgl satktdtali etpqsisvvt kdqmkaqgae
      181 nlsqmlrysa avvpetrgst asrldmlsir gfspalyldg lrmpdnrdaa pqkdvfdler
      241 vevlrgpasv lygqaspsgv vnmvsklpte tpfheiglty gtfnkkrttf dfggpiddqg
      301 vysyrlsgly ddadgqieht etrrqslasa ftwrpnedts ltllanlqsd pkgasygsmp
      361 aygsvvnspt grhidfdfyd geknfeksdr eyhavgylfe hhlndvwtlr qnarylrseg
      421 vyrsiyngwg tlqpdyrtse ratiatdvnl dsytidnqmq anfdtgplqh tlllgadyqn
      481 tstdtkagyg igptldifdp vygspvevpa ftesstqrdq qkglylqeql kwdkwvllmg
      541 grydwaessn sstnltsstk trssadseaf tgrlglvylf dnglapyisy sesfepqsgt
      601 glggalfdpt egtqyelgik yqppgsnsfi taaifdlrrs nvlsqdpngn lcngavcqvq
      661 tgevqsrgfe legkaslndn lditaayayl dnrvtkssnv vnvtsgiigd apgpdlttkg
      721 ttapaiprht asawvdytvh dgqlkgagvg ggaryvgasw gdeantlkvs gytlfdaavh
      781 ydipnisnam dnlrlalnvt nlankeyvas cytyswcwyg sqrtvqasat yrw
//
LOCUS       WP_007243104             283 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Haemophilus pittmaniae].
ACCESSION   WP_007243104
VERSION     WP_007243104.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus pittmaniae
  ORGANISM  Haemophilus pittmaniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Haemophilus pittmaniae"
                     /db_xref="taxon:249188"
     Protein         1..283
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30795
     Region          5..274
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mnkiydlhch stasdgvlsp tevvlrahaq gvqvlalcdh dtiagiseaa saatqcgmql
       61 ihgvevstew egkgihivgl nfdpqhpali dflnqqkqlr qqrafeigek lakagipday
      121 agaaalange vtrahyaryl lqigkvsnet qafkrylgag kscfvkahwa dipstieilh
      181 aaggvavvah plrynmsvrw irklladfkn wggegmevag cgqtgeqrkn larwarehgv
      241 agsvgsdfhf pcgwvelgkg lqlpddvtpi wkiwdknrfl nqt
//
LOCUS       WP_007240785             201 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Gordonia otitidis].
ACCESSION   WP_007240785
VERSION     WP_007240785.1
KEYWORDS    RefSeq.
SOURCE      Gordonia otitidis
  ORGANISM  Gordonia otitidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 201)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Gordonia otitidis"
                     /db_xref="taxon:249058"
     Protein         1..201
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=21133
     Region          81..200
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(149..150,153,173..176,178)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 misvakkqgr ghttrslvlg yawpalaava vlavtiatit gltqrssasa esaqhpkplp
       61 vvtapapplp scpanatgka ivvglasqhm alcedgrqis dvpvttgsvd rgagtplgtw
      121 qieshdvdrt lsgpgytvfv hywlhlfgdi gfhdspwqkf pygdttkyrt qgsegcihvp
      181 gdqikhlyew agdgtpvtit a
//
LOCUS       WP_007245650             407 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Pseudomonas
            syringae group].
ACCESSION   WP_007245650
VERSION     WP_007245650.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..407
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43338
     Region          8..404
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mtdqsqplll vlntgsssik fslysaaala asgpqclgng sfevrkdter lifqgadgca
       61 qkreewprng aslnkasans gtlanlmgwi erhadgqica aahrvvhggs rtqvaarvda
      121 vlmadmqalv plaplhqplc lapmtylsre hgglvqfacf dtafhhtldv letrfglpat
      181 ltaqglrryg fhglsyeyia svlphydqra aqgrtivahl gngaslcgmh nrvsrgttmg
      241 fstldgvlmg trpgrldpgv llyllrerrm svqalehlly hecgllgvsg gissdmrels
      301 asqapearda ialfvrnvvr eigslaailg gvdalvftgg igehaadvrd aildgcawlg
      361 lkrdravatq pgarlshpds avsawviatd enaiiarhal gllhert
//
LOCUS       WP_007245977             290 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Pseudomonas syringae group].
ACCESSION   WP_007245977
VERSION     WP_007245977.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..290
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30951
     Region          13..261
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mnwlpvsehr fklaegafwd aeaealywvd iagllacrlv ageyrqwrmp epvsafipte
       61 qgdalvtlas gvyrldltse rtslslfcva dptpgnrane arcdangrlw lgsmqnnida
      121 gggdvplvrr sgglfrvdad asvtrlldgq givntllwst dgsvlysadt ldeviyqypv
      181 ladgtlgprr vwaaeqsrgs pdgsamdaqg yvwnarwggs clirfapdgs vdrvvdlpvs
      241 hptscvfagp dlqtlyvtsa apgdahgqfd gavltahvgv sgkacqrfag
//
LOCUS       WP_007246132             143 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: pilin [Pseudomonas syringae group].
ACCESSION   WP_007246132
VERSION     WP_007246132.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..143
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14368
     Region          2..143
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkaqkgftli elmivvaiig ilaavalpay qdytirskvt egltqaasak lavaetaanv
       61 ggvanvtaan sgfvfnpvag tnsyvgavav gaggvitvtt ketgaavqpv fnlnpvqasp
      121 ndqitwtcvr taglakhlpa ncr
//
LOCUS       WP_007246140             700 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Pseudomonas syringae group].
ACCESSION   WP_007246140
VERSION     WP_007246140.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 700)
  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   3  (residues 1 to 700)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..700
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=75365
     Region          3..690
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msinldqaqq tfivearell qameesllql endpgdqdai gaifraahti kgsaglfglt
       61 pivsfthive dvldrlregs vavdagliav llksgdhmle lievvasrge alqpvalere
      121 aalrqalhiy qapssaated tacapgaaeg elaevvwhis lrfgvdvfrn gmdplsflry
      181 lntlgqmiqv ttvtdgipav eswdpeschl gfeidfrsaa gydainevfd fvredcvvli
      241 tpveqtpess eptgtdlvsq naqspvvang ellgdqravp rvpgqttave rpasggehks
      301 kdgsyvrvna dkldelinlv gelviasaga kllarscnnd plqeasstvs glveqildga
      361 lhlrmipigd tfnrfrrvvr dvsqelgkdi dliingaete ldktvvekig dplmhllrns
      421 mdhgiesaea rraagkpakg hlnlnafhds gsivieiadd gaglnreril dkaqqrglva
      481 agasltdqei ynlifepgfs taeavtnlsg rgvgmdvvkr nitllrgtvd ldsqpgqgti
      541 vrirlpltla iingflvgid qstyvipldm vqecieldeh drqssrdkgy ldlrgevlpl
      601 vylrdhfnhe gpparrqnvv vvryaehkag lvvddllgef qtvikplgkl fgalrgisgs
      661 tilgsgaval ildipallnq ivqlearlaq pphslspasr
//
LOCUS       WP_007246776             265 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phosphonate ABC transporter ATP-binding protein
            [Pseudomonas syringae group].
ACCESSION   WP_007246776
VERSION     WP_007246776.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
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   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..265
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=28601
     Region          3..247
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mtlhlsaidl rhsngtlalr gldlsierge rvaiigpsga gkttllnlla salppsagql
       61 evlgvnpwql ssrqrqqlrs rialihqapp lparqrvvta vsagklgqwg lgksllnllh
      121 pldvpgarav larldladkl fercqqlsgg qlqrvgiara lyqapellla depvsamdpr
      181 ladhtlallc qhaiehnvtl vaslhavela lahfpriigv rdgrihfdlp ageverqhld
      241 tlyaneqlsp qqvcevaetv waprc
//
LOCUS       WP_007246894             210 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Pseudomonas].
ACCESSION   WP_007246894
VERSION     WP_007246894.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 210)
  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 210)
  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   3  (residues 1 to 210)
  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   4  (residues 1 to 210)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 210)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 210)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            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="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=23256
     Region          22..206
                     /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"
ORIGIN      
        1 mtlraakkrl rndnaggikd lrdisvlvih pddedgrnli aqlqrigcqv rvqwpiperl
       61 hseadvivla vspeslstnt pwllhsatpp iipviayenp iivealvqln acsvipspvr
      121 sfglltalai tlsqarktre rekhvkrleg rmavmrtvqq akiilmetkg lseidaynal
      181 rdqamakrep vekiaealvk ahelfqqacs
//
LOCUS       WP_007247332             330 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_007247332
VERSION     WP_007247332.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 330)
  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 330)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..330
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36554
     Region          22..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          243..325
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpepsslasw tralrkqlda lgvdshalcr sagihmesld dpgaqfpada iarlwqlavh
       61 asldpalglr vsrfvsptaf halgytlvas gslrevferi vryramaeds leldfravge
      121 ryefrfgtpk scqlpahell dafaaiyvrt crsrlgrgya plsvhlqrpa pdnpqpwedl
      181 frspvmfsaq enllefggdd fdshlddgpm qvneqkangd plpsliweqr vrsaietllp
      241 dgeptaesia aalhlstrsl hrhladegcc ydlllnqcrq nlallhmndp qsslseiayl
      301 lgfsdtesls rafkrwtglt pgqyrsalgr
//
LOCUS       WP_007248126             330 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas
            syringae group].
ACCESSION   WP_007248126
VERSION     WP_007248126.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 330)
  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 330)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..330
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36634
     Region          22..202
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          243..325
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpepsslasw tralrkqlda lgadsnalcl sagidprqld dpdaqfpaat tallwelavq
       61 tsldptlglr vsrfvspttf halgytlvas gslrevferi vryhsvadds leldfraage
      121 ryefrfsapk scpspihell dafaaiylrt crnrlgrgya plavhlqrpa pdnpqpwhdl
      181 frsalnfsak enmlefgadd fdghlhdgpi qltehntngd plpsliweqr vrsaietllp
      241 dgeptaqsia ealhlsersl erhladegcc ydlllnqcrq nlallhmsep qtslsevayl
      301 lgfgdtdsls rafkrwtglt peqyrnglvr
//
LOCUS       WP_007249911             191 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Pseudomonas syringae group].
ACCESSION   WP_007249911
VERSION     WP_007249911.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 191)
  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 191)
  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   3  (residues 1 to 191)
  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   4  (residues 1 to 191)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 191)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..191
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21374
     Region          1..191
                     /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"
ORIGIN      
        1 mlrillindt arkvgrlksa lteagfdvid esgltidlpa rveavrpdvi lidtespgrd
       61 vmeqvvlvsr dqprpivmft dehdpgvmrq aiksgvsayi vegiqaqrlq pildvamarf
      121 esdqalraql hardqqlaer krielakgll mkmkdcneee aytlmrrqam srqqkliqva
      181 eqiiamsell g
//
LOCUS       WP_007250712             960 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: VirB4 family type IV secretion system protein
            [Pseudomonas syringae group].
ACCESSION   WP_007250712
VERSION     WP_007250712.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 960)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 960)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..960
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..960
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=108762
     Region          334..925
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 makksdlhly dselaglgrr nyqggmpiql lsdaflyeqq gryfhtldgr fakiwkisgv
       61 dasmynndml fdvtgsfadv lnkypagstg qflrhthrdi rqimglyqdq idpeagdfaa
      121 aiahsimdrq fsaatsangf fgdataatlk kmqedaladl emdevdedvr ataseaikre
      181 vregrfpfvn dfyivfmwqp eyifgkffdt tfkaalasvg ladankmter aynghakifg
      241 qycteieqal atygfqpevl tgqgyinlhy glmnpvrsfe ieppkyradi pildalenpd
      301 ivetrdnlaa tatfahvete pngwtihdrg vpyyirpvsv mgkpirsapg mlqvamagie
      361 seslitmnws iprpvvvtsr lairgrmiaa kesmrvgdke trerqradld avrnkvssen
      421 asnreqffdl svhinlmgfn keiiddqams lerrlwrigh kevlrgdavv rnsmpfnfrq
      481 tsmkllkrsi phltesvshm apmfvefqgv phpailmnnr agqpifldlw gnsvntahsl
      541 icgttgsgks ftfnnllmal rvkyrpkvwi idkgdsyesl clvlngnyvr ltterfvepv
      601 sgrtidpici npfalkrden drnvmpelde mffvarmlim mmeagdgsgs tksnltkvts
      661 sllyqaleef yrdwvetrpl deprfrdfip hliktnfheq kgevlaenlt lyygagpfaa
      721 ifdgfldvdw endftvletq rmskspalgi vtlalfrqid lyckfkldrs rkkvvavdea
      781 watlsdpnaa kalssfyrel rrygagclli sqtvkdfvnl ikaetsgggd sqdgilents
      841 hyfflacses dyrvakqela ftdeevdlwr slaslppmys evfyrmrtsq slyysgvfrl
      901 fsapmtlwia sshpddyrmr elrteeivne qriessvarq qaiidlskth pygarygqvv
//
LOCUS       WP_007251383             287 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Pseudomonas syringae
            group].
ACCESSION   WP_007251383
VERSION     WP_007251383.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..287
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30629
     Region          1..271
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mnvdlhchst asdgalspta lvarahengv rvlsltdhdt legleearaa ahslgmqlvn
       61 gvelsctwgg atihvlgygf dtqapaltaa iarlhegrwl raeeisrkla ikgmpgaleg
      121 araiqqelgd sgnaparphf adfmvragfv kdrgeafrkw lgagklgdvk qhwptledtv
      181 atlrasgawv slahpshydf trskrrklvg dfvqagghai evvngmqpad qvgtlsilar
      241 efgllvsags dfhgpgtwge igtyrpvped lpllscrfkh eqptaav
//
LOCUS       WP_007251404             160 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Pseudomonas syringae
            group].
ACCESSION   WP_007251404
VERSION     WP_007251404.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..160
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17201
     Region          27..159
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 midlqntgsg ldgygllaaq lealladerd fianaaqfsa flytqiedln wagfylnrne
       61 elvlgpfqgq iacvripfgr gvcgaaaqsr qtqrvqdvhe fpghiacdsa snselvvplv
      121 kdgrligvld ldspsvgrfk eedqvgierl aaiflastdc
//
LOCUS       WP_007251437             109 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Pseudomonas
            syringae group].
ACCESSION   WP_007251437
VERSION     WP_007251437.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (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   2  (residues 1 to 109)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..109
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11486
     Region          35..106
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mrttffsali fslltsasva vnaapasqpp veaaasavvq eqrndrvnln tadaltlqke
       61 lagigknkad aivayresng eftsvdelie vkgigkaile rnrdklaid
//
LOCUS       WP_007251742             290 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Pseudomonas syringae group].
ACCESSION   WP_007251742
VERSION     WP_007251742.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..290
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31269
     Region          13..261
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mnwlpvsehr fklaegsfwd aeaqalywvd iagflacrlv agqyrqwrmp epvsafiptt
       61 hgdalvtlas gvyrldltse ktslslfcva dptpgnrane arcdasgrlw lgsmqnnida
      121 eggdvplvrr sgglfrvdad arvtrlldgq givntllwna dgsvlysadt lddviyhypv
      181 rddgalgprq iwaaehsrgs pdgsamdaeg yvwnarwggn clirfapdgs vdrivelpvs
      241 hptscvfggp dldtlyitsa apadahgqfd gavlmahvgv tgtrcqrfag
//
LOCUS       WP_007252110             753 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Pseudomonas syringae group].
ACCESSION   WP_007252110
VERSION     WP_007252110.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 753)
  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   3  (residues 1 to 753)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..753
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79508
     Region          6..752
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msfgadeeil qdflveagei leqlseqlve lesrpddadl lnaifrgfht vkggagflql
       61 helvecchia envfdilrkg errvdselmd vvlealdavn smfgqvrert dvtpatpell
      121 aalarlaepq sadapvaaep epvveapapa vaqaaggddi tddefeqlld slhgsspvsa
      181 apaaapapaa saasgdeitd qefeslldql hgkgkfaadv vapaqapaaq sskaasgnde
      241 itddefeall dqlhgkgsfd gavaapvaaa pvaavakapa astaaasdei tdhefeslld
      301 elhgkgkfep qavvakapaa aaapapaakp apapaakaep akaapapapa raaaapaekp
      361 vateaettvr vdtarldeim nmvgelvlvr nrlvrlglns adeamskavs nldvvtadlq
      421 tavmktrmqp ikkvfgrfpr lvrdlarqlk keinlelvge etdldknlve aladplvhlv
      481 rnavdhgiet peereatgks rggrvilsae qegdhillsi sddgkgmdpn vlrsiavkrg
      541 vmdkdaadrl sdtdcynlif apgfstktei sdvsgrgvgm dvvktkisql ngsiniystk
      601 gqgskivikv pltlaimptl mvmlgnqafa fplvnvneif hlnlsttnvv dgqevvivrd
      661 kalplfylkr wlvssaahee qreghvvilt vgtqrigfvv dqlvgqeevv ikplgkmlqg
      721 tpgmsgatit gdgrialild vpsmlkryaa rri
//
LOCUS       WP_007252443             811 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: Lon protease family protein [Pseudomonas syringae
            group].
ACCESSION   WP_007252443
VERSION     WP_007252443.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 811)
  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 811)
  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 811)
  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   4  (residues 1 to 811)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..811
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..811
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89452
     Region          90..789
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mpdsvaanlr laphaltrpf saeqfsfstt ndlepfrgvl gqeravealq fgvamprpgy
       61 nvfvmgepgt grfsfvkryl kaeakrmqtp sdwvyvnnfd eprepkalel ppgsaqafma
      121 dinglidnll ltfpavfehp syqqkkssid rafnqrydra ldvierlsle kdialyrdss
      181 niaftpmadg kaldeaefsq lpeadrerfh ddisaleerl neelaslpqw kressnqlrq
      241 lneetitltl qpllaplsek yaenaavcay lqamqvyllk tvveqlvdda ktdaqarkll
      301 eeqyspslvv ghthdggapv vfeqhptydn lfgrieystd qgalyttyrq lrpgalhran
      361 ggflileaek mlgepfvwda lkrtlqsrkl kmesplgelg rvatvsltpq vipwsvkivi
      421 igsrslyytl qdldpdfqem frvlvdfdee ipmvdetleq faqllktrts eegmapltad
      481 avarlatysa rlaehqgrls arigdlfqlv seadfirqla ndhqtdaghi eralkakatr
      541 tgrvsarild dmmagvilid tdgaavgkcn gltvlevgds afgvparisa tvypggsgiv
      601 dierevnlgq pihskgvmil tgylgsryaq efplaisasi aleqsygyvd gdsaslgeac
      661 tlisalsrtp lkqcfaitgs inqfgevqav ggvnekiegf frlcearglt geqgaiipha
      721 nvttlmlder vvqavrdgqf hiyavrqade alsllvgepa gapdesgefp egsvnarvve
      781 rlrdiaemls dedlkeelek epaqlqpelk l
//
LOCUS       WP_007252662             833 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [Pseudomonas
            syringae group].
ACCESSION   WP_007252662
VERSION     WP_007252662.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 833)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 833)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 833)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..833
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..833
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90247
     Region          62..113
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          90..833
                     /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 mprpasslhp lalavlmaya alpshaaess lpeagvssar sfsipagdls qvlntfseqa
       61 glalafdpal tqgkrsngvq gryspdeaia rllsgsglra malsasryri eaapeavggs
      121 melqattisg asqfetatgp lsgyvatrgl satktdtali etpqsisvvt kdqmkaqgae
      181 nlsqmlrysa avvpetrgst asrldmlsir gfspalyldg lrmpdnrdaa pqkdafdler
      241 vevlrgpasv lygqaspsgv vnmvsklptd tpfheiglty gtfnkkrttf dfggpvddqg
      301 vysyrlsgly ddadgqieht etrrqsiasa ftwrpsddts ltllanyqsd pkgasygsmp
      361 aygsvvdspt grhidfdfyd gekdfeksdr eyhavgylfe hhlndvwtfr qnarymrseg
      421 vyrsiyngwg tlrpdyrtse ratiatdvnl dsytidnqmq anfdtgplqh tlllgadyqn
      481 tstdtqagyg lgptldifkp vygspvavpa ytesstqrdq qkglylqeql kwekwvllmg
      541 grydwaessn sstnltsrnk trssanseaf tgrlglvylf dnglapyisy sesfepqtgt
      601 gqggslfept egtqyelgik yqppgsnsfi taaifdlrra nvltqdpegn mcngsvcqvq
      661 tgevqsrgfe legkaslndn lditaayayl dnrvtksnnv vnvtsgiigd apgaevavkg
      721 ttapaiprht asawvdytfh dgqlkgagvg ggaryvgssw gdeantlkvp gytlidaavh
      781 ydipnisntm dnlrlalnvt nlankeyvas cytyswcwyg sqrtvqasat yrw
//
LOCUS       WP_007252729             795 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: penicillin acylase family protein [Pseudomonas
            syringae group].
ACCESSION   WP_007252729
VERSION     WP_007252729.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 795)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 795)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 795)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..795
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..795
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=88112
     Region          21..795
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkrslvilai ilailaggag wyinskqpvr dgeismsrlq apvtlryddr gvphiraene
       61 adlyralgya haqdrlfqme mlrrlargel aeilgpnlie tdtlfrslri rehadayvar
      121 qdknsptwka leayidginq yqdthakpie fdvlgiprrr ftaedtlsvg gylaysfaaa
      181 frteplltyv rdqlgpqylq vfdldwhpdg vldskpalvs adwkslnqla qlshkaleda
      241 glpqfegsna wvisgsrtqs gkpilagdph irfsvpsvwy eaqlsapgfe lyghfpalnp
      301 faflghnmdf gwsltmfqnd dvdliaektn penpnqvwyh gqwvdmtrte qqiavkgqap
      361 vsltllesph gpivnnvvgk nagkapiamw wsflmsanpv ldglyeanra dtldnmrsaa
      421 ekiqspgvni vwanangdig wwaaaqlpir pegvnpafil dgstaqadkl gfypfsanph
      481 eenpargyiv sanfqpespt gmpipgyynp aergqelnrq lsdstvkwdl nankalqlet
      541 rtdyapsilk plipvlrsvv sdpdeqalve rlanwkgdyp vdsvgatlft qflfdlteet
      601 fhdelgdaff etllssrvld salprlaada dspwwnnrns pheesrantv kvawrasvsh
      661 lkslygnnpd ewvwgrahtl tqshpmgsqp plgkifnvgp yaapgthevp nnlsssirpa
      721 pwpvgygpst rrlidfadpa hslginpvgq sgvafdkhys dqakafvkge ylpqrfsekd
      781 vadhtegvlr lvpge
//
LOCUS       WP_007253916             828 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Oceanicola granulosus].
ACCESSION   WP_007253916
VERSION     WP_007253916.1
KEYWORDS    RefSeq.
SOURCE      Oceanicola granulosus
  ORGANISM  Oceanicola granulosus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceanicola.
REFERENCE   1  (residues 1 to 828)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 828)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 828)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..828
                     /organism="Oceanicola granulosus"
                     /db_xref="taxon:252302"
     Protein         1..828
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=90647
     Region          9..819
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mallfhwllr iatalvvlgi aafalayyfa arslpdydrt yevagisapv eivrdnanvp
       61 hifgardddv ffalgyahaq drmwqmtmlr rtaqgrlsel fgartvgidk lmrrldlytl
      121 atrsvdaqdr qttaaleaya agvnswfgev nagargrgap emwlfnhaia pwqpadsiai
      181 vklmalemqs hldievlrar aslilederv ddllpsapgp gvaalpryga mmpgnlptya
      241 egtrlpddpl spinpaplag asnawaagia rsatgstlla ndphlglsap slfylarlel
      301 ssggviggti pgvpvvltgr sadlgwgvts ayaddidvfv eevnpddare yrtpdgwkrf
      361 etrdsivvvk ggaaqtlrlq wtdngpvlpp dlfelgtirp pghvtsvswt vlsdddtsls
      421 aamalmrahd veealeagar hvapamvltv adrnrialkl igalpardpd hrtrgrmpsl
      481 gyieenrwqg tfpasdnpvw vdpeggilgh tnnkivsspf prhvsyhwgd sqrvarwvrl
      541 mqsrevhtre sfieaqldtv sftarallpl igadlwftgd aapegtperq rqialtllae
      601 wngemnehlp epllyaawvr flqerlirde lgplarefth lqplfiervf rdlngasrwc
      661 dviqsaptet ctdiarqald dalvwigety gsdlqtlrwg dahearhdhs vlgevavlrw
      721 fvnirqstsg gdntlmrgmt lgtgpnpmln vhaavyrgvy dfadpdssvf itstgqsghp
      781 lsryydhlge rwrrgeyipm sldpslargg avgvtvlrpa vadavaad
//
LOCUS       WP_007254085             361 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Oceanicola granulosus].
ACCESSION   WP_007254085
VERSION     WP_007254085.1
KEYWORDS    RefSeq.
SOURCE      Oceanicola granulosus
  ORGANISM  Oceanicola granulosus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceanicola.
REFERENCE   1  (residues 1 to 361)
  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 361)
  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 361)
  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 361)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Oceanicola granulosus"
                     /db_xref="taxon:252302"
     Protein         1..361
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=38799
     Region          1..344
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mdrrsfltkg avgatagaaa salaapayaq gnrtltlvtt wgrglagvhd saqycadait
       61 amtdgqltvd lkaggelvgp fevfdavsag qadmyhgvdy yflsqhpals ffsqipfgmt
      121 fqeyanwhdh dggrelsdel ysifglksfp agntgpqsgg wfskemnspa dfqglrfrmp
      181 gqggevlgkl gasvqnlpga evyqalasgs idgtewigpw adekagfqei tkfyytagfh
      241 epgpnlnltm nldvyesltp aqqaivenas raanlwtmsl fmannsaalq rlqsggvqll
      301 efsdeiwdaf gqaaqevvea pmgdelydki ydsymaslds sanwisrsqg eftaqrdrvk
      361 g
//
LOCUS       WP_007256616             229 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Oceanicola granulosus].
ACCESSION   WP_007256616
VERSION     WP_007256616.1
KEYWORDS    RefSeq.
SOURCE      Oceanicola granulosus
  ORGANISM  Oceanicola granulosus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceanicola.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Oceanicola granulosus"
                     /db_xref="taxon:252302"
     Protein         1..229
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=24571
     Region          5..155
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mrhagalwqp spnfgarrgg avpdlvvlhy tamescaaal erlcaaehev sahyliaadg
       61 tlvqlvdetd rawhagagaw gavddvnsrs igieldnrgd dpfpepqlar lealladlla
      121 rhrippervi ghsdmapgrk hdpgprfpwr rlaraglsvw pdadpgpdra aapdrvrlaa
      181 alaafgyrge lapmldafhl rfrphagapd atdlamaeal aarwpvrpa
//
LOCUS       WP_007256688             208 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Oceanicola granulosus].
ACCESSION   WP_007256688
VERSION     WP_007256688.1
KEYWORDS    RefSeq.
SOURCE      Oceanicola granulosus
  ORGANISM  Oceanicola granulosus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceanicola.
REFERENCE   1  (residues 1 to 208)
  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 208)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Oceanicola granulosus"
                     /db_xref="taxon:252302"
     Protein         1..208
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22468
     Region          1..207
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 marelrrhkl tlalincppp nytdpdaprg faavpghaer frsdfrrslr yartlgaerv
       61 hvmagvaegp eagavfadnl awacaeapeq lltieplngh dvpgyflddy dlalsvlddv
      121 aapnlslqfd tyhaarltgn vvalweavgp rvghvqvgdh pgrhepgsge idfgtffaql
      181 rrdgyagwvs geyvpagrta aglgwrrg
//
LOCUS       WP_007256870             264 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Oceanicola granulosus].
ACCESSION   WP_007256870
VERSION     WP_007256870.1
KEYWORDS    RefSeq.
SOURCE      Oceanicola granulosus
  ORGANISM  Oceanicola granulosus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceanicola.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 264)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Oceanicola granulosus"
                     /db_xref="taxon:252302"
     Protein         1..264
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=28192
     Region          34..260
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mrqldttlha qqvrtpldya msardrdtpa mvaqalraga calalqpvvt apgrevafhe
       61 glirltdpgg rvlpaaafmg aveetatgrd ldaaslglal gllrarpgmr lsvnvsarsl
      121 gdsafravla elvaddgtlg erlileicer samllpeiva rfmeelqpqg vafalddfgg
      181 gflsfrhlrr fffdlvkidr gfisgidgda dnqvlvrall gvahqfdafv vapgveraee
      241 aawleaagvd clqgyffgap kvtr
//
LOCUS       WP_007263508             409 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Streptomyces sp. C].
ACCESSION   WP_007263508
VERSION     WP_007263508.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. C
  ORGANISM  Streptomyces sp. C
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 409)
  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 409)
  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   3  (residues 1 to 409)
  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   4  (residues 1 to 409)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 409)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 409)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 409)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Streptomyces sp. C"
                     /db_xref="taxon:253839"
     Protein         1..409
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42397
     Region          41..394
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(115..117,138..139,198,250,274)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mrsrqliavt aalaagaltl tacgsrddkg gaadaggttv viavdapltg dlsalglgik
       61 nsaelavkqa nekkyvkgvt fkfealddqa qatsgqqnat klvankdvlg vvgplnssvs
      121 esmqkvfdda kltqispant spsltqgpkw aegqkartyk syfrtattda iqgpfaaqyl
      181 fnkagkkkvf iiddkktyga glagtfkgef tklggqiage ghidpeskdf savvtqvkss
      241 gadvvyygge ypaagplskq ikaagtnipl vggdgikdkk yvelagpggq gdlctsvgap
      301 vetlpsakef idnykkagyk ddysayggys ydsawaiieg vkkvveanng klpsdarakv
      361 leavqgvsfe gvtgkvafde fgdatnkqlt vykvdgddfk svesgtlag
//
LOCUS       WP_007263940             692 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Streptomyces sp. C].
ACCESSION   WP_007263940
VERSION     WP_007263940.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. C
  ORGANISM  Streptomyces sp. C
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 692)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Streptomyces sp. C"
                     /db_xref="taxon:253839"
     Protein         1..692
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73434
     Region          8..692
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mhrspdatat hcpycalqcg mnlrpapagd avtveertgf pvnrgalcgk grtapavlss
       61 rvrlteplir thaggplvpa tweealdava aglartrrah gpdavavfgg ggltnekaya
      121 lgkfarvalg tsqidyngrf cmssaaaahq kafgldrglp fplediprtg cvvlvgsnpa
      181 etmppfvryl telkanggtl ivvdprrtrt aeladlhlap rpgtdlalal gllhlvvaeg
      241 rtdeefiaer ttgwedaraa amahwpelve ritgialpel rravelfctp aaamvltarg
      301 peqqskgtdt vgawinlcla tgragrphsg ygcltgqgng qggrehgqka dqlpgyrklt
      361 dpaarahvar vwgvdpqslp gpgrsayell dalggdvkal llmgsnpvvs apraahvedr
      421 irsldflava dvvlsetaal advvlpvtqw aeetgtttnl egrvllrrra ltpppgvrgd
      481 ldvlhglaar lgvekgfptd peqvfdelrr asaggpadys gisyarieae qgvfwpcpeg
      541 spgqprlfld rfatddgrar ftpvshrdaa evpdadypll lttgrvvaqy qsgaqtrrvp
      601 elnaaapgpf velhprlaar lgvtdgtpla vtsrrgrava parvtdavra dtvfmpfhwy
      661 gegrantltn paldpvsrmp efkvcavrve pa
//
LOCUS       WP_007264436             388 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Streptomyces sp.
            C].
ACCESSION   WP_007264436
VERSION     WP_007264436.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. C
  ORGANISM  Streptomyces sp. C
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 388)
  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 388)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Streptomyces sp. C"
                     /db_xref="taxon:253839"
     Protein         1..388
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=42700
     Region          1..370
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mttlslsade arrialraqg flgapdrrgg vrgvlrhlga vqldtisvla rshelipyar
       61 lgavgrdave kaywsdshaf eywshaacil pieewphfaf rrrarrargh rwhvledkdr
      121 stravldrlk adgpltssel ggaknggewf ewsetkiave wlldtgevvc cerrgwkrvy
      181 dlaeravpdv llhddlddge clrrlvalag qslgvgtrad iadyhrlkge qvdaviadsg
      241 lvpvevegwg kpawadpral dtaargrhrt tllspfdslv wdrprterif gfthrleayv
      301 pkpqrihgyf ampllaggrl rgrvdpgreg rtlvarqvsl ttpgaagama ralreaaewv
      361 gcdavrvera qspaeaaait aelaalga
//
LOCUS       WP_007264711             223 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Streptomyces].
ACCESSION   WP_007264711
VERSION     WP_007264711.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..223
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=23252
     Region          8..215
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mtdgkrtpwv vgvsgasgtp yaaavvrgll aagesvdlvv srasrltlld etgiafrdah
       61 wradleewlg rgadgkpgtf agfdldavry wgagdlaagp ssgsypvkgm livpastacv
      121 agvalglskd llqrvasvtl kerrrlvvav retplngqtl rhlvaldeag avvlpaspaf
      181 yagathiqdl vdfvagrvld aagvphglyr rwegelgsar pre
//
LOCUS       WP_007266042             288 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Streptomyces sp. C].
ACCESSION   WP_007266042
VERSION     WP_007266042.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. C
  ORGANISM  Streptomyces sp. C
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 288)
  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 12830887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces sp. C"
                     /db_xref="taxon:253839"
     Protein         1..288
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=30501
     Region          79..143
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          178..287
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mhrqkafirt lglaaavafa atacgpqgag aapaapsapa ggspsaspsk qddkpaspss
       61 apsapssssa pstsaapgak plmangdese qvrelqarlr qlklvstapt afygskttaa
      121 vktfqsqhgl patgsvdeat wqkvqgltkk ptddelrppt tnevdapdpr cmqgrvmcis
      181 kesrtlawmi dgkvvstmdv rfgsentptr eglfqvewka kewtstiyht smpysmffsq
      241 gqavhyssdf aargydgash gcvnvrdkkk lselfdqvkv gdkvvvyw
//
LOCUS       WP_007267117             421 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. C].
ACCESSION   WP_007267117
VERSION     WP_007267117.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. C
  ORGANISM  Streptomyces sp. C
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 421)
  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 421)
  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
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 421)
  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   5  (residues 1 to 421)
  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   6  (residues 1 to 421)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 421)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 421)
  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 15726307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Streptomyces sp. C"
                     /db_xref="taxon:253839"
     Protein         1..421
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42703
     Region          16..>72
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          84..378
                     /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 mtrmpgdgrg aanaaavlrt vldhgpvars gisalcglsp aavsrqatgl lragllrelp
       61 gpsahagsgr prvpldlhtg avggpvaagl higvpsstfs lvdlrgrtla rrslphhagr
      121 ndpariaaal rdflrdsdtg rpllglgaal ggwvrpdtgt vvrhpaldwh drpladelga
      181 alrlpvrvdn haravaaaev lfghpaarrs lvhlfignvv daafgiegav hqgpgsaagd
      241 vahlpvpgsg aacacgrtgc lqaaasdtal gaeavrrgiv pdpsvpllad aaaagdprad
      301 rllrerardv graaallldv fnpavmvvte lssvlhdayl deirtaaler srvcddpari
      361 vaphagpavl pqaaatvlla plfrdpagga pvpttgpapd ptppaphpdp tptppptpql
      421 i
//
LOCUS       WP_007267218             340 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Streptomyces sp. C].
ACCESSION   WP_007267218
VERSION     WP_007267218.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. C
  ORGANISM  Streptomyces sp. C
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 340)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Streptomyces sp. C"
                     /db_xref="taxon:253839"
     Protein         1..340
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35681
     Region          10..338
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mstqscdprp rvgitavgsl lpedvlssde lqrevarrsg lalparlltq atgivsrrva
       61 aagvyastla vgaarrales aglgpmdvdl lvfasasrdl vepatahivq aelgsrahav
      121 dvtnacnsfv ngidlarsav lagrarralv vtgetpsrav rmdpadfaef rsgfagytfg
      181 dagaavllee vgrggildvd sethsehwev ggipgggsrh prgdaytyfq gdghelrgvf
      241 ekvgtavidr tlhrtgmdwd gfakvlvhqv tvpylerfae ltgvpaqklv vtvpelgnva
      301 sasigvqler vfpelaager vlfvglgggi simtmvweks
//
LOCUS       WP_007268531             301 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptomyces sp. C].
ACCESSION   WP_007268531
VERSION     WP_007268531.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. C
  ORGANISM  Streptomyces sp. C
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 301)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 301)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Streptomyces sp. C"
                     /db_xref="taxon:253839"
     Protein         1..301
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32735
     Region          19..102
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          126..292
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mleqlnrald hlearldqev dvagaariaa vseyhfrrlf salagmplpv ylrrrrmtla
       61 gaevtagelt lldiavrygy gsaeafaraf rsvhgigpge arrtgavlta qprmsfrvvv
      121 egstamryrt vqkesfrfvg rkarvplvhe gvnaaaaahl edlderavvr mkelsgglep
      181 egilsaavyl tdsreegala dywigvltap gtaaaadfdf dgfdvldvpa gtwavfecrg
      241 plpgalqelw rdvftqwfps npytsrpgpe llrtapaatg eetrsqlwip vervgrraga
      301 p
//
LOCUS       WP_007268171             122 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Streptomyces sp. C].
ACCESSION   WP_007268171
VERSION     WP_007268171.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. C
  ORGANISM  Streptomyces sp. C
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Streptomyces sp. C"
                     /db_xref="taxon:253839"
     Protein         1..122
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=13369
     Region          19..86
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mtenawgyre tsgrlqgvdl sgfkveavdg gigkvdrhsd evgsaylvvd tgpwifgkev
       61 llpagtvsri dvdeekiyvd rtkeqiknap efhrekhlgd vgyhdelady yrsggafggr
      121 pl
//
LOCUS       WP_007268849             222 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Streptomyces sp. C].
ACCESSION   WP_007268849
VERSION     WP_007268849.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. C
  ORGANISM  Streptomyces sp. C
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Streptomyces sp. C"
                     /db_xref="taxon:253839"
     Protein         1..222
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=23975
     Region          <125..216
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mikhlwratv alslaaiava gpasaassav avsptvsiqm peppqaavav delqlltvep
       61 phpmtgysrt kfphwaaqfg kcdtrevvla rdgetvvqde ecrsvsgtwl slydnktfta
      121 sgqldidhmv planawrhga dnwttakrkq fandlehsql iavsaasnrs kgdqspefwv
      181 ppssaywcty grawthvkai yglsvtegek aalvklldtc ea
//
LOCUS       WP_007269134             343 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Streptomyces sp. C].
ACCESSION   WP_007269134
VERSION     WP_007269134.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. C
  ORGANISM  Streptomyces sp. C
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 343)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Streptomyces sp. C"
                     /db_xref="taxon:253839"
     Protein         1..343
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35881
     Region          4..329
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mtaigilgtg sylpadtvsn rvvgeragvt edwilqktgi rerryaaeye atsdlaveaa
       61 rsaldaagis aeqlswivva tstpdspqpa taclvqhrig avnaaafdvn svcsgfvfgl
      121 vaaarmlpgq dggvrghalv igadvysrii dredrrtavl fgdgagavvl gpvrsgygvl
      181 gsylasrgdq aelirveagg srlpasektv aeglhhfrmn grgvrdfvaa elpravgevl
      241 drhglersev dhfvphqang vmlgetvprl glprarthlt vaehgntsaa siplaldeay
      301 rsgafrdrdv vllagfgggm slgtvlvrwd eeaapaprkd saa
//
LOCUS       WP_007270086             404 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Paeniglutamicibacter
            gangotriensis].
ACCESSION   WP_007270086
VERSION     WP_007270086.1
KEYWORDS    RefSeq.
SOURCE      Paeniglutamicibacter gangotriensis
  ORGANISM  Paeniglutamicibacter gangotriensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Paeniglutamicibacter.
REFERENCE   1  (residues 1 to 404)
  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 404)
  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
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 404)
  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   5  (residues 1 to 404)
  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   6  (residues 1 to 404)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 404)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 404)
  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 20324439
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Paeniglutamicibacter gangotriensis"
                     /db_xref="taxon:254787"
     Protein         1..404
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40976
     Region          <19..>72
                     /region_name="COG3355"
                     /note="Predicted transcriptional regulator
                     [Transcription]"
                     /db_xref="CDD:442583"
     Region          80..382
                     /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 malttinpka pntgtgagdl fqylrngqpr trselatltg lsrstiatrv dalldtglvg
       61 avgaalssgg rppstfafap esrtvlaadl gaahailglt dlagniidhl radlditngp
      121 vpvldwvvar ftellqrngr dastlsgiai gvpgpvahst grptkppimp gwndfdipgt
      181 iqqtfdvpvl vdndvnimal geqslswpdt enlmfvkvat gigvglisgg alqrgaqgsa
      241 gdlghvqvpg gastpcrcgn tgclealagg gavaanlaaq gyavhtasdv gklaednnta
      301 aiqvlrqagr digsvlamcv nllnpsvivl ggrlasageh viagvreqvy frstplatqh
      361 lvivgsaaad magvrgasml vighvlapda vdhqvmnraa amat
//
LOCUS       WP_007271357             422 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paeniglutamicibacter
            gangotriensis].
ACCESSION   WP_007271357
VERSION     WP_007271357.1
KEYWORDS    RefSeq.
SOURCE      Paeniglutamicibacter gangotriensis
  ORGANISM  Paeniglutamicibacter gangotriensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Paeniglutamicibacter.
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   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   4  (residues 1 to 422)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Paeniglutamicibacter gangotriensis"
                     /db_xref="taxon:254787"
     Protein         1..422
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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]"
                     /note="Members of the family are the ATP-binding subunit
                     of ABC transporters for substrates such as betaine,
                     L-proline or other amino acids, choline, carnitine, etc.
                     The substrate specificity is best determined from the
                     substrate-binding subunit, rather than this subunit, as it
                     interacts with the permease subunit and not with substrate
                     directly.; Members of the family are the ATP-binding
                     subunit of ABC transporters for substrates such as
                     betaine, L-proline or other amino acids, choline,
                     carnitine, etc. The substrate specificity is best
                     determined from the substrate-binding subunit, rather than
                     this subunit, as it interacts with the permease subunit
                     and not with substrate directly."
                     /calculated_mol_wt=44933
     Region          13..306
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 msepsgaitg asilldevtk qypgqikpav ggltleipag sivmlvgpsg cgktttlkmi
       61 nrlieptdgk ividgedvtq mdgdtlrrri gyviqagglf phmtvaania ivpkmlgwdk
      121 akisarvdel lelvsldpav yrdrypkels ggqqqrvgva ralaadppvl lmdepfgavd
      181 pitrqrlqde llniqaevqk tivmvthdfd eavklgdwia vfdegaqlvq ydsperilan
      241 pandfvenfi gsgaglkqlt ltrvnevelv davtatpgel asavlsrlqg agqqlavvld
      301 srkrparrls rrqlsrmqvi ddtvddsmpv vsdqstlnda ldtmlvasse tavvtgrrdv
      361 frglinvqti meaiaqanss asadseapvg lnsgaipais venamagead gesaqhpvee
      421 pr
//
LOCUS       WP_007272216             398 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin
            [Paeniglutamicibacter gangotriensis].
ACCESSION   WP_007272216
VERSION     WP_007272216.1
KEYWORDS    RefSeq.
SOURCE      Paeniglutamicibacter gangotriensis
  ORGANISM  Paeniglutamicibacter gangotriensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Paeniglutamicibacter.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 398)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Paeniglutamicibacter gangotriensis"
                     /db_xref="taxon:254787"
     Protein         1..398
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42392
     Region          12..370
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mtpdlqrlrf ieradvykng vhagelsrta aggirfgyla nylaeghapv afslppdtaa
       61 vetsngalpa ffagllpegh rltvlknatk tsfddeltll lavgadvpgd vqvvpagdvp
      121 aepealadts npedldfavl ansvdlhalp gvqdkasasm lttplatrgq ryllkldpaq
      181 nphlvaneaa hlvgarnlnl pvarnrlihd kngltgllve rfdrrkgtdg hwhrmaledg
      241 tqvmglppaa kyavaaedva lalarlcvap vvasrnlylq yafawltgng dlhaknlsvl
      301 aredggfeis plydlpctll ygdetlalpv sgklknlkar hwaqfadslg lparaaasan
      361 rlalkaaasv dltalpfags plrgaqrelr frrhemqg
//
LOCUS       WP_007263132             157 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein, partial
            [Streptomyces sp. C].
ACCESSION   WP_007263132
VERSION     WP_007263132.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. C
  ORGANISM  Streptomyces sp. C
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 157)
  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 157)
  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 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   4  (residues 1 to 157)
  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   5  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10164212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Streptomyces sp. C"
                     /db_xref="taxon:253839"
     Protein         1..>157
                     /product="winged 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]"
     Region          9..66
                     /region_name="WHTH_GntR"
                     /note="Winged helix-turn-helix (WHTH) DNA-binding domain
                     of the GntR family of transcriptional regulators; cd07377"
                     /db_xref="CDD:153418"
     Region          10..>131
                     /region_name="ARO8"
                     /note="DNA-binding transcriptional regulator, MocR family,
                     contains an aminotransferase domain [Transcription, Amino
                     acid transport and metabolism]; COG1167"
                     /db_xref="CDD:440781"
     Site            order(28,30..31,39..43,45..46,49,59..60,62..65)
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:153418"
ORIGIN      
        1 myerssvael aeslrseldr ypiggklpss ramveryrvs pvtvsralaq laaeglvvtr
       61 pgagafrahp rtsgpapgdt swqevalsae gagdvvprsv dasgvansla vppagvieln
      121 ggylhpslqp eramaaalar agrrpgawgr ppmeglp
//
LOCUS       WP_007272648             228 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Paeniglutamicibacter
            gangotriensis].
ACCESSION   WP_007272648
VERSION     WP_007272648.1
KEYWORDS    RefSeq.
SOURCE      Paeniglutamicibacter gangotriensis
  ORGANISM  Paeniglutamicibacter gangotriensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Paeniglutamicibacter.
REFERENCE   1  (residues 1 to 228)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Paeniglutamicibacter gangotriensis"
                     /db_xref="taxon:254787"
     Protein         1..228
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=24606
     Region          101..186
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mardkdpkdw hghriitede laspefttda rlkrrrairh giiltlvvlv laaamvmayl
       61 intraivida lepqqtvess vafneacptt efsyiepgkm kvnvmnatqi sglagatatk
      121 lrkrgfkvvd vgnarlspve vvgavrsgpd gyaqamtvqr nikgltyvyd akrpgstvdv
      181 vigtkykdlv keksvntkag klgctapkpk deaketkapa ksapskdk
//
LOCUS       WP_007279641             240 aa            linear   BCT 20-JAN-2025
DEFINITION  16S rRNA (cytidine(1402)-2'-O)-methyltransferase [Lentisphaera
            araneosa].
ACCESSION   WP_007279641
VERSION     WP_007279641.1
KEYWORDS    RefSeq.
SOURCE      Lentisphaera araneosa
  ORGANISM  Lentisphaera araneosa
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Lentisphaerales; Lentisphaeraceae; Lentisphaera.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Zhao,M., Zhang,H., Liu,G., Wang,L., Wang,J., Gao,Z., Dong,Y.,
            Zhang,L. and Gong,Y.
  TITLE     Structural Insights into the Methylation of C1402 in 16S rRNA by
            Methyltransferase RsmI
  JOURNAL   PLoS One 11 (10), e0163816 (2016)
   PUBMED   27711192
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Kimura,S. and Suzuki,T.
  TITLE     Fine-tuning of the ribosomal decoding center by conserved
            methyl-modifications in the Escherichia coli 16S rRNA
  JOURNAL   Nucleic Acids Res 38 (4), 1341-1352 (2010)
   PUBMED   19965768
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Kozbial,P.Z. and Mushegian,A.R.
  TITLE     Natural history of S-adenosylmethionine-binding proteins
  JOURNAL   BMC Struct Biol 5, 19 (2005)
   PUBMED   16225687
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001055
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Lentisphaera araneosa"
                     /db_xref="taxon:256847"
     gene            1..240
                     /gene="rsmI"
                     /GO_function="GO:0070677 - rRNA
                     (cytosine-2'-O-)-methyltransferase activity [Evidence
                     IEA]"
     Protein         1..240
                     /product="16S rRNA
                     (cytidine(1402)-2'-O)-methyltransferase"
                     /EC_number="2.1.1.198"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0070677 - rRNA
                     (cytosine-2'-O-)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0000451 - rRNA 2'-O-methylation [Evidence
                     IEA]"
                     /calculated_mol_wt=26823
     Region          6..217
                     /region_name="RsmI"
                     /note="16S rRNA C1402 (ribose-2'-O) methylase RsmI
                     [Translation, ribosomal structure and biogenesis];
                     COG0313"
                     /db_xref="CDD:440082"
ORIGIN      
        1 masgaignsd dipkrtldav rdsdmlvfee drparavlka akvhreywky seqdevhtlr
       61 evekalkrge tvcymsdqgc ptledpgspv lksawsvkaq iqvipgpssv taaisacpft
      121 vkgivvagfl srdqelreke lrklsgsghp flimdtpyri khileslktv ldvqkkfvla
      181 idisgehecf fydnattila eaeklppkln fviivegkke kkqlkqavrg ngykqnrrrr
//
LOCUS       WP_007279694             454 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Lentisphaera araneosa].
ACCESSION   WP_007279694
VERSION     WP_007279694.1
KEYWORDS    RefSeq.
SOURCE      Lentisphaera araneosa
  ORGANISM  Lentisphaera araneosa
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Lentisphaerales; Lentisphaeraceae; Lentisphaera.
REFERENCE   1  (residues 1 to 454)
  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 454)
  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 454)
  AUTHORS   ter Beek,J., 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 454)
  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 454)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Lentisphaera araneosa"
                     /db_xref="taxon:256847"
     Protein         1..454
                     /product="CmpA/NrtA family 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=50748
     Region          35..312
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mknkikkall sfflfctvpt maesvdenti pldvekpnlh fgfikltdca slviakekgf
       61 feaeglnvkl taqknwvill dnvikgaldg ahmlagqpig atvgvsqkan vitafsmdln
      121 gngitmatdv weqmkehvpk daagkpihpi kadalkpvle ewdgpfnmgm vfpvsthnye
      181 lrywlaaagi hpgfytasds kghtdaevii spnapplmps ylnsrailgy cvgepwnqka
      241 vfaekdgkql gvpvvtnyei wknnpekvfg vtedwakkyp kthtavlkal iragkwldas
      301 menreeavqi lsrshyvgae akvlrnsmtg sfvyergdrr empdfnvffr ykatypfysd
      361 cvwfltqmrr wgqlkedksd ewytktakki ykpalymeaa kllveegnie aseipgddet
      421 gfkpvtsedi fidgkaydgt kpndyidsfe ikap
//
LOCUS       WP_007279944             490 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Lentisphaera araneosa].
ACCESSION   WP_007279944
VERSION     WP_007279944.1
KEYWORDS    RefSeq.
SOURCE      Lentisphaera araneosa
  ORGANISM  Lentisphaera araneosa
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Lentisphaerales; Lentisphaeraceae; Lentisphaera.
REFERENCE   1  (residues 1 to 490)
  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 490)
  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 490)
  AUTHORS   ter Beek,J., 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 490)
  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 490)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Lentisphaera araneosa"
                     /db_xref="taxon:256847"
     Protein         1..490
                     /product="CmpA/NrtA family 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=55006
     Region          131..370
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 msikslgdpy dkdaslthtv ncncksccae ksarqpltdk ertkilekqa esmetvsshd
       61 ikespqdsel ktsddyfdra iesafirgif ghndasrrsf lklvgtgtfa svlgtmfpln
      121 dlkaqakesi aklekkklki gfvpitcatp iimakpmgfy akygldvdvi ktagwavard
      181 kslngeydas hmltpmplam smgagsvaep yimptvenin gqaivlhtkh knkrnpkdwk
      241 gfkfgvpfdy smhnlllryy vaehgldpdk diqirvvppp emvanlragn ldgylspdpf
      301 nqravyekvg flhmltkdiw eghpccafac pakfakempn tfgalfrsiv datefsakae
      361 nraeiakais pknylnqpei vvnqvltgry vdglerkvfn epdridfdpf pwhsmavwil
      421 tqmkrwgyvk gdidykgiae qvyiatdtak imeelgypap kktyknhtim gkefdytkpd
      481 eyvksfaikr
//
LOCUS       WP_007280489             199 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Lentisphaera araneosa].
ACCESSION   WP_007280489
VERSION     WP_007280489.1
KEYWORDS    RefSeq.
SOURCE      Lentisphaera araneosa
  ORGANISM  Lentisphaera araneosa
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Lentisphaerales; Lentisphaeraceae; Lentisphaera.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Lentisphaera araneosa"
                     /db_xref="taxon:256847"
     Protein         1..199
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21659
     Region          4..197
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mthkryilai sgasgsyfak aclkalvntr akifvvasqt akqiwtdemn egtlddfihs
       61 lsteeqaliq veniknlsaa issgsfrhdg mlimpcsaks lasiangiss nlleraadvc
      121 ikegfplvig lretplsaih lenalklsrl gvqivpcipg fyhgdnsfeg mvnfvagkal
      181 dqlkidhkly krwkeddha
//
LOCUS       WP_007283789             784 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Gluconobacter thailandicus].
ACCESSION   WP_007283789
VERSION     WP_007283789.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter thailandicus
  ORGANISM  Gluconobacter thailandicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 784)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 784)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 784)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..784
                     /organism="Gluconobacter thailandicus"
                     /db_xref="taxon:257438"
     Protein         1..784
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=86096
     Region          23..784
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 masavlattt fvrsasgrti kglegltapl evwedkwgvp hvkaasvada yfangylvak
       61 drlwqmdfgh rqslgrlaev fgdafvpsdv anrlflfrgd adaelaryss vvqdsakayv
      121 aginayihtl kenpenlpae fallgyeple wtvqdlirvr aevtgntele irraclaarg
      181 alaydslitp lqpayiptll pgldvhsise kdlghlrvlq krlplgeiha atlqgdpshr
      241 ktnegsnswv iapsrtvtgr pilandphla fgapgprhvi hltapgldvi gagspgmpgv
      301 mqghnehiaf grtnfhidqe dlfvlrtran dssqywhagq wrkmeeetvs iavrnaeeqs
      361 vtlrfsaqgp visedmarnr avavsatwly pgangllani ginlahdwts fcdalhahts
      421 ptnftyadqq gnigwhaagg lperakdhdg mmpapgdgly dwkglqplen lpssfnpaag
      481 wfgtsnqmnl pvgysqkkyk vsyewsepfr ynrvaqvlda tqhtsvqdsa nlqhdtlsql
      541 alrviqllpe qnegtkfayq llkswngrvd rdspaaalye vwwthigaal yaatipselh
      601 dllpgplsps vqlallqtpd rtfgnngktv rdnmlteclq kavaelteri gplpaswkwg
      661 tlhtlnighv lekfgsthnp fpniggknyg sggdpytvma rwydpvhsck npyattggas
      721 flmvcdigew dnsvflnfpg qsanpatthy sdfldvwlkg dmqplyfssq nvtkhavrry
      781 mlsp
//
LOCUS       WP_007283825             192 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Gluconobacter thailandicus].
ACCESSION   WP_007283825
VERSION     WP_007283825.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter thailandicus
  ORGANISM  Gluconobacter thailandicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Gluconobacter thailandicus"
                     /db_xref="taxon:257438"
     Protein         1..192
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21055
     Region          1..163
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 minsvyrrit dlaaspkavw wliviamaea cvfpipvdlm lipmiltrqd rawflatvct
       61 aasvvggvig wilgaflmkh igmpiahfyh adgrilalee mfrrygvwii lgkgltplpy
      121 kfvtlaagaa hypllpfiaa sivtrgarff leaallkafg epvrdfiekr ltvillillv
      181 vivagvalve ll
//
LOCUS       WP_007287421             435 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Intestinibacter bartlettii].
ACCESSION   WP_007287421
VERSION     WP_007287421.1
KEYWORDS    RefSeq.
SOURCE      Intestinibacter bartlettii
  ORGANISM  Intestinibacter bartlettii
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Intestinibacter.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Intestinibacter bartlettii"
                     /db_xref="taxon:261299"
     Protein         1..435
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=48741
     Region          5..339
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 malynlgaeq silgailiep elvsvgnqfn lsvydffhpq hqiiykhmqk lyernekidp
       61 vtlsseltnh dqldkvggva yltslvtvvp svsnisyyir ivkdfsmkrs ghemlattsk
      121 niksmdqksl itfsedfksm vldnsnsedl vvnaskvsis vqrggiltgf agldallgdg
      181 lnfgtltvlt gspgagkstf lnqiianais ngfnsflysg eltyemcmdw ftrtvanpqh
      241 llnytsnmgk yakvsdegle mitqwvddkl ffyskeakad eanishaiey latkknvklf
      301 vldnlmtldc sgndkyekqi iavkslkrla kkykivivlv ahsnknsmmn kephvfeisg
      361 aseipnlady vlkasregre petelfvlkn ritgsirykt mltfdtarkr fftktgnelk
      421 kdfgympsye qesfd
//
LOCUS       WP_007287502             166 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Intestinibacter
            bartlettii].
ACCESSION   WP_007287502
VERSION     WP_007287502.1
KEYWORDS    RefSeq.
SOURCE      Intestinibacter bartlettii
  ORGANISM  Intestinibacter bartlettii
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Intestinibacter.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 166)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 166)
  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 166)
  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 166)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Intestinibacter bartlettii"
                     /db_xref="taxon:261299"
     Protein         1..166
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19067
     Region          73..162
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(92,111..112,130,133,141..142,154,159)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mkkkiefanl tsslaswlle klkaapldig nidefkegie glldgsnnsl mleidddtvy
       61 eeycfdviei gdltirpker rvlcntqeis ltpkeydill flvknrgevl tkeqiyqavw
      121 dseyllddsn imafirklrk kiepnpdapi yiltiwgigy kfndnl
//
LOCUS       WP_007288161             108 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Thermosinus
            carboxydivorans].
ACCESSION   WP_007288161
VERSION     WP_007288161.1
KEYWORDS    RefSeq.
SOURCE      Thermosinus carboxydivorans
  ORGANISM  Thermosinus carboxydivorans
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Sporomusaceae; Thermosinus.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Thermosinus carboxydivorans"
                     /db_xref="taxon:261685"
     Protein         1..108
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12174
     Region          17..102
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 metkkcfglt dadiayivsi iddfpeikka aifgsrakgn ykpgsdvdia vygedisltt
       61 larlhyrlee esplpyffdi vdythlkhqp lkehiervgk vifergqa
//
LOCUS       WP_007288414             677 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Thermosinus carboxydivorans].
ACCESSION   WP_007288414
VERSION     WP_007288414.1
KEYWORDS    RefSeq.
SOURCE      Thermosinus carboxydivorans
  ORGANISM  Thermosinus carboxydivorans
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Sporomusaceae; Thermosinus.
REFERENCE   1  (residues 1 to 677)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 677)
  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   3  (residues 1 to 677)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Thermosinus carboxydivorans"
                     /db_xref="taxon:261685"
     Protein         1..677
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=73838
     Region          1..677
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          167..245
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 mdisqylgif leetrehlqt lnrclleleh dpgnlavlde ifrsahtikg msatmgftai
       61 aelthemeni ldllrksvlk anseiidalf kcvdtleqsv eqvaangets ldikplvttl
      121 talakgemft dskapssvaa rpvsaidlnd tevkiiqaan sqglrayevq vrlregcllk
      181 saraymvmst ldtlgdviks ippaeeleke nfdlsfqtvv itdaepdkik qallsiaeie
      241 svnvilceat prlekaaava gqsdaesrri ggkhdeetek tvnpglntta dkkvkggqsv
      301 rvdiekldtl lnlvgelvin ktrleqigit hrlpdlveti eqmdrvttdl qavvmkvrmv
      361 pvgqvfnrfp rmirdlsrel nkevnliiqg eeteldrtvi deigdplvhl lrnaidhgie
      421 speereakgk npvgeirlia rhegnnviiv veddgrginp etvkqkavqk glitqaeadk
      481 mdvaeairli flpgfstadn itdvsgrgvg mdavktkies lggmvdvetk vnegskfkir
      541 lpltlaiiqa llvkvgeeiy aiplssidst ikvglpdikt iqnhevillr gqiipivrla
      601 kvlnvpetgq knqeelfvvi ihmgeqragv vvdtligqqe ivikslgkll agikviagat
      661 ilgngqvali ldvgslm
//
LOCUS       WP_007289883             387 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Thermosinus carboxydivorans].
ACCESSION   WP_007289883
VERSION     WP_007289883.1
KEYWORDS    RefSeq.
SOURCE      Thermosinus carboxydivorans
  ORGANISM  Thermosinus carboxydivorans
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Sporomusaceae; Thermosinus.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Thermosinus carboxydivorans"
                     /db_xref="taxon:261685"
     Protein         1..387
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=40652
     Region          <1..387
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mkfsgyrrpd gkvgirnhvl vipsvvcanr vargiaqqva gatwvehqhg ctqlgadael
       61 tfrvlvnhgt hpnvygvvvv glgcetiraq diaaairkqc pykpvhlvii qdeggsvkat
      121 aagvsaaram vseasclere lidaaelilg tecggsdacs gisgnpalgy asdllinagg
      181 tvvlaettei igaehiiasr avnpqvaakc fevikrcedm akqmgvdmrg gqptpgnieg
      241 glssieeksl gciykagskp lqdvigyadp itqkgliwmd tpgqdieqmt gmvaggchli
      301 vfttgrgtcc gspiaptikv stntqlferm ndnidldagt iivgretvqe vgqrifreil
      361 kvasgkltka evlgfndfai nrigptm
//
LOCUS       WP_007295716             385 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Rhodococcus].
ACCESSION   WP_007295716
VERSION     WP_007295716.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (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   2  (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
REFERENCE   3  (residues 1 to 385)
  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   4  (residues 1 to 385)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..385
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=40549
     Region          1..301
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mitfsgvtkr ypdgttavds ldleidaesf tvfvgpsgcg kttsmrminr mitptagtit
       61 vdgrdiaqtd avklrlgigy viqsagllph rtvvdnvatv pvlrgdsrrn arkaalavle
      121 rvgldpalas rypgqlsggq qqrvgvaral aadppillmd epfsavdpvv redlqaemqr
      181 lqaemrktiv fvthdideav klgdrvavfg pggrlqqyda pdtvlsapat dfvasfvgrd
      241 rgyrglsfrt adqvplhtir tatekelpal rlergewvlv vtdagvprgw idvtgvegar
      301 agrpvsecta aggslfspgs dlrqaldaai sspsgigvav dadgavtggi lgseviakla
      361 eqraaedrar gehfftaqpa tpdgp
//
LOCUS       WP_007295726             284 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Rhodococcus].
ACCESSION   WP_007295726
VERSION     WP_007295726.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 284)
  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 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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..284
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30354
     Region          15..266
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          188..267
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 msvadsdtav ssgafrrpaa plralvtgyd gyrlagfepg ihlglpspsl tvvvtidepl
       61 diaaqatpeq apgrfaalas giatapvtir hdgnehgvql alsplgaral lgvptaalgs
      121 wvvgleellg pdagelterl slepgwderf ailddlltrr aapaeidphl trawhllvag
      181 egtrvgdvah evgwsrrhlv nkfvaeygvt pkdvvrlsrf hrshrmlksa agatladvsa
      241 vcgyydqahm ardwrdlagv apsrwreidp fsfvqdpyhd dgae
//
LOCUS       WP_007296748             237 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease family protein [Rhodococcus].
ACCESSION   WP_007296748
VERSION     WP_007296748.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..237
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=25210
     Region          93..233
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mrhrpraafl alaavsvlgl sgcsaiadad pgtgslggap atpapvfdaa palakldtla
       61 vkgrapktgy treqfgpsws ddnsvegghn gcdtrndilr rdlvdltykt strdcvvatg
      121 tlhdtyagtt iafvrgqdts tavqidhvva lsdawqkgaq qlspeqrrdl andprnlqav
      181 dgptnsqksd sdaaswlppn kayrctyvsr qidvkalyrl wvtqaekdam sqvlhsc
//
LOCUS       WP_007298885             367 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-oxoacyl-ACP synthase III family protein
            [Rhodococcus].
ACCESSION   WP_007298885
VERSION     WP_007298885.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 367)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..367
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38921
     Region          21..355
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mvkrwlvmet engdlrmpfa trlagagrhl pvthltttdl msttrhsthi dlerltgire
       61 rrvsvgdeds ytlaisaald clersnrdag sidvvvscsi tkfhggltqw leptmssava
      121 qaigaqgamt fdlsnacagm ltgvtvmnnw irqgiveral vvsgeyisql gqnaaqhirn
      181 imskelaslt lgdagaalll erapagsagi glagfttvad ysrlclaypk ggdpgarmft
      241 nsrgiqraai adtplllhev ldaagislhd idhvithqts arairkgmae vtatlgdspr
      301 hdavitvdry gntastthtv alveeleagr iragenvali alasgleigv vlltldeelv
      361 aryghsh
//
LOCUS       WP_007299180             253 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease family protein [Rhodococcus].
ACCESSION   WP_007299180
VERSION     WP_007299180.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..253
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=27364
     Region          106..246
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mprsavpntg siittirtkw pwilagllvv vlvtmlspdp ddtlaagtgp vapsevtdaq
       61 qiqmafaqls tlevkgrapk tgydrelfga swtdnvsvdl grngcdtrnd ilrrdlvdit
      121 srdrtrncvv qsgtlrdlyt gtiiaftrgt ktsdavqidh vvalsdawqk gaqlldaqtr
      181 anlandprnl qavdgptnqr ksdadastwl pplaayrcty varqvevkva yrlwvtpper
      241 damaavltgc gar
//
LOCUS       WP_007299488             340 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-oxoacyl-ACP synthase III family protein
            [Rhodococcus].
ACCESSION   WP_007299488
VERSION     WP_007299488.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 340)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..340
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36244
     Region          4..333
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mdtvslidia gylpenrvga dyfaqfaasd rlaeiimfra pkfrhhiasd enavdmaera
       61 iaplverngs elvanvdili thtqlpdvpi lgtggelarr mgitpdwvvd lhnggcasfv
      121 ymiklarqim qtgnastali vsvqnsagqi ftqsdvrala qsavpgdgag acllvkseaa
      181 pvlglecrty pefagdmtaa vdpprkywea gtgqlhigft esriakvfar gnrlvpeval
      241 avckrigitp daidtlvtnq pnrlflrnwr dalelpaerh pdtfdecgnl fgaaipvtld
      301 ienragripn gslvmmsafa hagdfagaga irwgaapagv
//
LOCUS       WP_007301118             345 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Rhodococcus].
ACCESSION   WP_007301118
VERSION     WP_007301118.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 345)
  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   6  (residues 1 to 345)
  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 12117664
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37564
     Region          22..218
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          98..343
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtartipadf vrrslelsar sgvdlspals aagittasle dplarltptq vtaftqavwq
       61 itgdelfglg papvprgtfr lvclalihta dlsaalerma dilralpslp alhigpgvng
      121 gtrmtidirp aaaerstedv qssleatrvt tdfllillhr faawlvgkrv rllavelpyp
      181 aplphlaeny dhifgvpvtf dsdipavefd savmrapiiq teetledylr esptllmser
      241 dydstasaqv rrvlelgmkg rtstaediae mlsisvphlr rllrqegtsl nqlreevlrd
      301 aavaglrrge tvedlsarlg fsepsafrra fkrwtgstps syrga
//
LOCUS       WP_007301444             359 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Rhodococcus].
ACCESSION   WP_007301444
VERSION     WP_007301444.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..359
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37530
     Region          16..353
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mtglsvearv dargvdvgfd lgegevlavl gpngagksta lsvvaglvrp dvgrvelngr
       61 vltdttrgva vpphrrgval laqqallfph ltvaanvafa prsagrgrre araiaekwld
      121 avdatqfadr rphelsggqa qrvavarala aepqalllde pmaaldvaaa palrvllrrv
      181 lregnrtavv vthdildala ladrvivveg gqvvefgsvr dvltrprsaf aariaglnlv
      241 pvfgaqdgfe tetgvrlhgl pdadfvpgap avavfaphsv avhrrspegs prnvfrvsis
      301 eievrgptvr vraaeagsrf elsadvtaas vaeldlvpgl dvffvvkate valhavrtc
//
LOCUS       WP_007301461             690 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate--CoA ligase family protein [Rhodococcus].
ACCESSION   WP_007301461
VERSION     WP_007301461.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 690)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..690
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70393
     Region          7..685
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 msaivdrdlt alfdprsvav lgasndetky gnwisvqalr mtgsrsvhlv nrrgerilgh
       61 pslrslseld ervdlvvitv paqgfeeavd dalaagatai vgvtagfael gaagkavqdr
      121 vvervraaga vllgpnclgv ldsstaltla snplpagrva llsqsgnmal elsqflearg
      181 hgfsrfaslg nqadlgaadl irscvvhddt dliavycedf gdgrafvdaa aqasragkpv
      241 llltvggsea sirgaqshtg sltsdsavid aacraagvyr vssprqladv aatllgygpa
      301 evrrvgviad ggghagvasd vveaaglavp eftadissal rallppsagv tnpvdlagag
      361 eqditsfvsv ldtilqspav dsvlltgyfg gygsygekla raevdtaram aetarthgkp
      421 vvvhtmhpds aaarvladsg vpvfraveda agalgviaet aapqhpagge sepaepvtsd
      481 aywdarelfr gagvefpdaq lvrtcaeava aadsvgypvv lkamgllhks dsggvalgle
      541 taqqltdaft rmdgslaapa ycvesmadls agvelivgvq tdprfgpvam vglggiftev
      601 ladvafalap vdaetargll dnlrasallr gvrgrppinl daaadaiaav tavatahpei
      661 aeleinplfv tpkealglda rivldtsntn
//
LOCUS       WP_007301537             273 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: hydroxypyruvate isomerase family protein
            [Rhodococcus].
ACCESSION   WP_007301537
VERSION     WP_007301537.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 273)
  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 273)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..273
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29028
     Region          6..268
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mdtlaytlnc silltdvpll qrpqaardag fdavefwwpf dtavprdsdv dafvaaienv
       61 gvqltglnfa agnmpagdrg llsdpaqvsa frdniditvg igerlgtkaf nalygnridg
      121 tdpkiqddta aenlaqagka adrigavvlv epvsgtpayp lksaaeaiav idrvkaehgv
      181 dslrlladly hlevngddvg aaidayadri ghvqiadvpg rgepgtgtld idgylkrlag
      241 hgyrgyvgle ykstrpdtfd wlpreqrasr aah
//
LOCUS       WP_007302161             191 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Wolbachia].
ACCESSION   WP_007302161
VERSION     WP_007302161.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia
  ORGANISM  Wolbachia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Wolbachia"
                     /db_xref="taxon:953"
     Protein         1..191
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20916
     Region          4..186
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mnsrivigis gasgsiygvr ilealkntnh ethlvissag kitiaheike kledimslad
       61 fyyseekige kiasgsfkts gmviapcsmk tmseiasgvt snlltraadv tlkerrklvl
      121 mvresplhlg hlrnilklte mgaiiappmp afyikpksld divnhsvgkv lnlfdialpd
      181 feewqgnvny y
//
LOCUS       WP_007302240             491 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Wolbachia].
ACCESSION   WP_007302240
VERSION     WP_007302240.1
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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Wolbachia"
                     /db_xref="taxon:953"
     Protein         1..491
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=57350
     Region          53..211
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mklivkkcls vlfllllvap llygqqscls diendfqdlk tslknpifld papslnyddr
       61 egkkvlmvvv hhtesptlks tkyalnssgi svqlivdrdg sitlmvplek rawhagisya
      121 kvqvdnvvee lrklndysig ieivntglep fpeeqmksvk dlilylmkrf kirkdmifsh
      181 aeigtivyns aiegyamrkp dphklfdwel leksgiglhi gdrispqdae qkvnevlykv
      241 gdksenilkl kkrlngffyk ilpwndregn mifpdnnany snefdenfaw vinqfsmhhl
      301 pkeirkdlpl kleqedilpe flvkyrnlif seflslsdkt qlslkppfln eedykhllss
      361 laeyenniss dafamlmyki klyydsylry nirsslyipf rlnsfekldi lkneilsfks
      421 ispekaievs nlinefrski lsdfqnfekq wfqefkdtwk qkfipnmerq mswtalhetv
      481 leylekakke v
//
LOCUS       WP_007303411             112 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Crocosphaera watsonii].
ACCESSION   WP_007303411
VERSION     WP_007303411.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera watsonii
  ORGANISM  Crocosphaera watsonii
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae;
            Crocosphaera.
REFERENCE   1  (residues 1 to 112)
  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 112)
  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   3  (residues 1 to 112)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Crocosphaera watsonii"
                     /db_xref="taxon:263511"
     Protein         1..112
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=12967
     Region          33..110
                     /region_name="Endonuclease_DUF559"
                     /note="Putative endonuclease; cd01038"
                     /db_xref="CDD:411708"
ORIGIN      
        1 mkqgryflpy npkliekare mrknptfnrg gemkvwrqkp idnfivdfyc pklklvievn
       61 gdshftedgt lydaqrtlil egyglsvirf tndevincfe gvcakiedll pf
//
LOCUS       WP_007303449             230 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Crocosphaera].
ACCESSION   WP_007303449
VERSION     WP_007303449.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera
  ORGANISM  Crocosphaera
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Crocosphaera"
                     /db_xref="taxon:263510"
     Protein         1..230
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25314
     Region          30..225
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mivstttkps sqdtqalqev wlrltanscp yeynfhmhtk csdgqltpeq lieqatnigl
       61 kglaitdhhs vegykvaqnw lqrtsletpk dslphlwtgi eitsslldve vhilgyafds
      121 ehpaiqpylt gesrsgsqgl avnvieaihq aggmavlahp eryrhpatkv ipvavelgid
      181 gveafyaynn pkpwkpsprq tetvlslssf yglyhtcgtd thgpnllqri
//
LOCUS       WP_007304647             214 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Crocosphaera watsonii].
ACCESSION   WP_007304647
VERSION     WP_007304647.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera watsonii
  ORGANISM  Crocosphaera watsonii
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae;
            Crocosphaera.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Crocosphaera watsonii"
                     /db_xref="taxon:263511"
     Protein         1..214
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22727
     Region          <29..191
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mptynetngn drfnanrtak nrlrkwrmyg kdgndilsgg rkndslyggs gndrlygvsg
       61 ndslyggsgd drlyggwdhd tldggsgddr lyggwgrdtl vggsgndvln ggwghdalmg
      121 gtgddtligg fgsdtyifns ladgvdtirh fqghlshsfr dkiqvskagf gvgsldqfsf
      181 dtdsgslsfn gqkfanlelv sggsfsihnd ivlv
//
LOCUS       WP_007305448             184 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Crocosphaera watsonii].
ACCESSION   WP_007305448
VERSION     WP_007305448.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera watsonii
  ORGANISM  Crocosphaera watsonii
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae;
            Crocosphaera.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Crocosphaera watsonii"
                     /db_xref="taxon:263511"
     Protein         1..184
                     /product="TRAP transporter small permease subunit"
                     /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=21231
     Region          4..177
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mqkllniaki idtinewvgk ltywllllmi lvgvwnvigr ylgrligqnl tsnafievqw
       61 ylfdivfllg aaytlkhdeh vrvdlfykdw spkrkalanf igvfiflipf clmiiyyswg
      121 niinswkile mspdpgglpr ypiksmiivs yvllifqgia eaiknwaift gklnpqeehh
      181 dpsv
//
LOCUS       WP_007268960             274 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces sp. C].
ACCESSION   WP_007268960
VERSION     WP_007268960.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. C
  ORGANISM  Streptomyces sp. C
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Streptomyces sp. C"
                     /db_xref="taxon:253839"
     Protein         1..274
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=29700
     Region          12..254
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mrisdsgtrs vlevdgesim psagkprqil allalypgrv vpvptlmeei wgqdlpnsal
       61 ttlqtyilql rrrlgtamgp grpgaakevl ttrhggyllq vpqeavdvha yenlvargla
      121 afeggddega aarlraglaq wqgpalvdvr vgpvlaievm rleesrlvav erridvdlrl
      181 grhtellael teltarhaqh eglhsqlmva lyrsgrqgaa ldayrrlrgr ligelgveps
      241 pqlqrlhqam ltvdpaldvv agprrgstfd lyaa
//
LOCUS       WP_007305544             120 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Crocosphaera watsonii].
ACCESSION   WP_007305544
VERSION     WP_007305544.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera watsonii
  ORGANISM  Crocosphaera watsonii
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae;
            Crocosphaera.
REFERENCE   1  (residues 1 to 120)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Crocosphaera watsonii"
                     /db_xref="taxon:263511"
     Protein         1..120
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=12995
     Region          6..106
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mgnplyelrl yangrlmaty etvtgraesq nrnrhksgte aplpdgqyqv gsgvvagthp
       61 evggrflpie plfptgryal gihydpsfqk tngedgtegc ialtpdfsqi nlkaqsrdek
//
LOCUS       WP_007305987             739 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Crocosphaera
            watsonii].
ACCESSION   WP_007305987
VERSION     WP_007305987.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera watsonii
  ORGANISM  Crocosphaera watsonii
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae;
            Crocosphaera.
REFERENCE   1  (residues 1 to 739)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 739)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 739)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Crocosphaera watsonii"
                     /db_xref="taxon:263511"
     Protein         1..739
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=82887
     Region          1..719
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mtnstkticp ycgvgcglev lppaqpgkav nrdsegnpiw qvrgdrshps skgkicikgg
       61 tvseslvkdr lkypmmrdsl tdefrrvswd eameaivnrm qkvrltqgpd alcmygsgqf
      121 qtedyyiaqk lfkgflgsnn fdansrlcms savagyiqsf gsdgppccye dleltdcafl
      181 igtntaechp ivfnrlrlyh kknrkvkmvv vdprrtqtae aadlhlaikp gtdidlfngi
      241 ayllmrwgri dslfidectq nfpayaevir hyspelvark cgiriqdlek aakywgesqr
      301 vlslwsmgln qssegtakvr tlinlhlmtg digkpgagpf sltgqpnamg greagglcni
      361 lpgyrlvnnp qhraeveqfw gvrpgtiqpq rgrtawemiq gletgevgfl wiaatnpavs
      421 mpdlkrtqaa lkrspftvyq dayyptetat yahillpaaq wsektgvmtn servvnlcpq
      481 frdppgeara dweifaevgr rlgfekqfsf pnsaqvyaef vkitegrpcd ssglsyeklr
      541 rygplqwpya dtwpclegee ldrqnrtnkr lytdfcfntp dgrarfgayh srglaepsdq
      601 aypfvlttgr lyghwhtqtr tgripkinkk hpepfieihp rdaaklnike nsllevrsrr
      661 gkayfpakit keiapgtlfv pmhwgalwae naeanalthp tacpsslqpe lktcavqisi
      721 arvnevrnqr sevvfetri
//
LOCUS       WP_007306527             103 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [Crocosphaera].
ACCESSION   WP_007306527
VERSION     WP_007306527.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera
  ORGANISM  Crocosphaera
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Crocosphaera"
                     /db_xref="taxon:263510"
     Protein         1..103
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11970
     Region          1..99
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mnknlpitis rhtlsafckq yyikklslfg svlredftdk sdvdflvefe tgktpsfftl
       61 armerelsvi inlhkvdlrt pselsiyfrd rvmqeakvly els
//
LOCUS       WP_007308302             200 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Crocosphaera watsonii].
ACCESSION   WP_007308302
VERSION     WP_007308302.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera watsonii
  ORGANISM  Crocosphaera watsonii
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae;
            Crocosphaera.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Crocosphaera watsonii"
                     /db_xref="taxon:263511"
     Protein         1..200
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22782
     Region          8..98
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mnltlekrke kalkiaddci kilkeefgan eviifgslrg dspwheqsdl dlavkgmsdd
       61 diwnaygtle kvvpswlkfd lvpvekvpny vrdrilqtkp msnnkylalk trledemlaf
      121 eenintlksl meqsnnvpeg fvtptlasyi vdvytgcekm servavaldp rfrtskcsik
      181 kyivlkspki ipgqeyfsfh
//
LOCUS       WP_007310026              76 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein, partial [Crocosphaera watsonii].
ACCESSION   WP_007310026
VERSION     WP_007310026.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera watsonii
  ORGANISM  Crocosphaera watsonii
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae;
            Crocosphaera.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 76)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 76)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Crocosphaera watsonii"
                     /db_xref="taxon:263511"
     Protein         1..>76
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
     Region          <27..>76
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mptyngtngn drfnanrtak nrlrkwrmyg kdgndilsgg rkndslyggs gndrlygvsg
       61 ndslyggsgd drlygg
//
LOCUS       WP_007310664             125 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: endonuclease domain-containing protein
            [Crocosphaera].
ACCESSION   WP_007310664
VERSION     WP_007310664.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera
  ORGANISM  Crocosphaera
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae.
REFERENCE   1  (residues 1 to 125)
  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 125)
  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   3  (residues 1 to 125)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Crocosphaera"
                     /db_xref="taxon:263510"
     Protein         1..125
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14835
     Region          17..115
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mnylpynknl vsrakelrkn ltlaekkiwy kylinyqyrv yrqrpidnfv vdfycpklkl
       61 vieidgdshy renaqeydsq rteilqgygl kvirftneev lhnlegviav ieglippnpp
      121 wkrge
//
LOCUS       WP_007311191             164 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Crocosphaera watsonii].
ACCESSION   WP_007311191
VERSION     WP_007311191.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera watsonii
  ORGANISM  Crocosphaera watsonii
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae;
            Crocosphaera.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Crocosphaera watsonii"
                     /db_xref="taxon:263511"
     Protein         1..164
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16741
     Region          <19..142
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mfgsldsdil dagitpgfdg tdniafsgsg ddlidvvagt gdnrlygqsg ndtltlgggd
       61 rafggsgddq ffllggnnav tgglgadqfw ianaeipesr hiitdfnled dllniaglgv
      121 gsfsdltlsn edgnaliafd dnelatllrv dadsltadnf gvls
//
LOCUS       WP_007311250             198 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein, partial [Crocosphaera watsonii].
ACCESSION   WP_007311250
VERSION     WP_007311250.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera watsonii
  ORGANISM  Crocosphaera watsonii
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae;
            Crocosphaera.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Crocosphaera watsonii"
                     /db_xref="taxon:263511"
     Protein         1..>198
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
     Region          <5..178
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 msyigtngnd nefdnpnleq yglngddalg ksdgdfkpfg gegddtlfql gaflmdgfgg
       61 pgndwmtlvn tspgsslyge dgndiieagg gadtiyggea rdalygrggn dtlyggggnd
      121 drqnitagtq afgpnffntt lgglyggegd dlldggdgdd yldggdgndt leggtgddil
      181 egsagndnld gdigndsl
//
LOCUS       WP_007311460             329 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein, partial [Crocosphaera watsonii].
ACCESSION   WP_007311460
VERSION     WP_007311460.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera watsonii
  ORGANISM  Crocosphaera watsonii
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae;
            Crocosphaera.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Crocosphaera watsonii"
                     /db_xref="taxon:263511"
     Protein         <1..329
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
     Region          56..308
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 eftlledlvg sdyavdldan sgsltlvddd fdlptvsiev dntdliegdd itfsldalgg
       61 vdivpsddnp vtilvngdtv gglaefelfd ennnplfttv giesvsildd etnfsavlid
      121 pnasitfsvl ddgieegleq ftytladgqa dyvvdpnaes vtitiddpii ggpgadifda
      181 gltpgfdgvn dtvfaregdd lidtnggsgg ntlygeennd tfilrsndta fggegedsff
      241 llrgdniitg gpgadefwlv asdipesvni indfndidgd vlgiasldfd qltisdangd
      301 tliaaggnpf arligvdans lsednfiiv
//
LOCUS       WP_007312692             104 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Crocosphaera watsonii].
ACCESSION   WP_007312692
VERSION     WP_007312692.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera watsonii
  ORGANISM  Crocosphaera watsonii
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae;
            Crocosphaera.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Crocosphaera watsonii"
                     /db_xref="taxon:263511"
     Protein         1..104
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12111
     Region          4..99
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 msstitanin ipneeierfc eqyhieklaf fgsvlrddft lfsdidilve fnpehipgli
       61 rlslmenels rlfqrkvdlr tpedlsryfr qevldsaviq yvns
//
LOCUS       WP_007312748            1740 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein, partial [Crocosphaera watsonii].
ACCESSION   WP_007312748
VERSION     WP_007312748.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera watsonii
  ORGANISM  Crocosphaera watsonii
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae;
            Crocosphaera.
REFERENCE   1  (residues 1 to 1740)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 1740)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 1740)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..1740
                     /organism="Crocosphaera watsonii"
                     /db_xref="taxon:263511"
     Protein         <1..>1740
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
     Region          805..1053
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          <1319..1525
                     /region_name="COG1572"
                     /note="Serine protease, subtilase family
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:441180"
ORIGIN      
        1 glsslqntta iiteiqnsla nllqpglllt aqeiadqlst vpylnvevis etengvefal
       61 sldgttnlgq iniapdlgll ddfglnidak advnltynld glrfgvnqdq aylhkddsdl
      121 eilvevglpd asfhgdlgci pisfdlsdtf psslafdfnv dlsgfdysld fsqlgnislf
      181 dfdfalpdgt idlpgisgdf tlnlaelgni dfgdpsytdy nipfafdnie ldlgslygdf
      241 lepvldnina vfdpirpfie ifnieiplvs nlpgasfldf dsdgritfrd laelearrqg
      301 ininfelidt iiefsdfian iptvgnvini geinindlgn vsanptsfns pnldlpsgfn
      361 fpllddplnf vydfifgnpt elityrtpev dfsinpgifv piigplgvri egnlgfnaqf
      421 gfgfdtyglt ckdgthlafe dgfyisdtan ldgtgedipe avltaglgld ggvdlevvka
      481 fvggdingei finlndpngd gkirsneldl snpsnifdpi aldniyaqls awyqifpldk
      541 vsfplspqip llnkeqldsa sneitgfvdq iknaiedaqd flgnvwkeve kfagdvanav
      601 kkgvedlidf gsdigqaavt vlntttqavi dgkdavlgvl adfdeqfiqp fvegiglepf
      661 ftylderipl rkwlkevnna iddlgeyvsa atavingntt vkeiikdipk lytfsaeiid
      721 gqleinwdsn asnqylqdpk aelyvtieer wglkylqvfs apiksqekva rifkaecggf
      781 lgtdcswnek tpetkevehr nafefnlndi nkivingtny ddkiivdklv dtpvtikayd
      841 grdtiqggsn dddlqggrgd dtiiggeghd tiggdegndv lvggdtveed nitgndsitg
      901 gtgndtligg agedtlkgdd dndvlrggdd kdklyggdge dniygeggnd tasgggqndy
      961 ieggegddsl ngdggedyil gqggedtlng gidndqldgg ddddhlygds gndflqgged
     1021 ndhlygwddn dvlegglgnd evsggsgddd lygdnqdatg ngwdvlkggr gddylkgggg
     1081 ndnldgneda dllegddgdd ilrggknddt dandilrggd gedelyggns gegkgvfrgg
     1141 vtlegnnsaq ydfldgeagk dklfgeggtn ylrsevlsdy sveqvaggde lnyfiidlns
     1201 lanstyyrdf vislgnvqsq dflffnteei ndlmefynts vnfnsdgiev ngiridgigq
     1261 islnlpltay dsrviktgnp wlnfdanyqi ietetgfrll yepsdlpglk teslsisdtt
     1321 lkpdqtyeld fairnygnsn adpfkvdfyl sknsnpsdld pnvhlgtyeg fsnglvsrst
     1381 vndtqtielp efeynyssfs ffnpetelde qgfrdgsqrn slglnlvnny lisvvdfnne
     1441 vtefddsyts wdrkiipiti dahkpadlsf dyfrvrddin sdpnativtq pgqlldfnyt
     1501 iqntgdfave ddfvisyyls tsdkteyndq rrfsrnefeq ndiylgshev nlftpidpge
     1561 vydpgnilln agsivydgtg gvsikndeni irpttilsfi vdsygrfdda piaigldgyy
     1621 wqlagevnpe wnqefnqgtg iqhnkkyeip vgeilagtav shlnfinteg dfkevylgep
     1681 dininlpdwn hsiwdtvgeg tyylhtvidg nhdvgerngl nnweteeiei klpdlspsls
//
LOCUS       WP_007313210             251 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Crocosphaera watsonii].
ACCESSION   WP_007313210
VERSION     WP_007313210.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera watsonii
  ORGANISM  Crocosphaera watsonii
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae;
            Crocosphaera.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Crocosphaera watsonii"
                     /db_xref="taxon:263511"
     Protein         1..251
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28606
     Region          1..86
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mkiaddciki lkeefganev iifgslrgds pwheqsdldl avkgmsdddi wnaygtlekv
       61 vpswlkfdlv pvekvpnyvr drilqtkpms nnkylalktr ledemlafee nintlkslme
      121 qsnnvpegfv tptlasyivd vytgcekmse rvavaldesl pkgenwheql lrqmadiggy
      181 nrpplwqgsl lleldeyrkf rhlvrhnyqv klkayqvlil aqkiiissek vkeaittfnl
      241 wldskansvg a
//
LOCUS       WP_007316816             383 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Gordonia effusa].
ACCESSION   WP_007316816
VERSION     WP_007316816.1
KEYWORDS    RefSeq.
SOURCE      Gordonia effusa
  ORGANISM  Gordonia effusa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 383)
  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 383)
  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
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 383)
  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   5  (residues 1 to 383)
  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   6  (residues 1 to 383)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 383)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 383)
  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 15726307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Gordonia effusa"
                     /db_xref="taxon:263908"
     Protein         1..383
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39983
     Region          1..>75
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          82..354
                     /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 msrsgvvaae lhvgsvpaaa vlqavrtggp itrdqlvlat glsaatvnrq lhaltrvglt
       61 verpdlvdpg sigrpknplt tdrdklcvag mhigakrtll aiadiggrtl yshavatpdg
      121 dgddairqls aqlkeladrf sgrrlmwggl alggdvdeht gvvdhpvlgw hrvpvgrrlt
      181 dalgvpvsvc ehvqamaaae lllgyprdgg gtglfcyare tvgmaitfdg kvrvpargag
      241 tiaylpvdap llsaqaeqrs plsttlqdvi gsevlqaaal rrgqtpedhe llderarvlg
      301 qslammrdvl npdsivvagd afaghprgla piqaafdaas htpwplelcp srfglrvqeg
      361 aaivvalsvl yadpitsval sad
//
LOCUS       WP_007317180             296 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Gordonia effusa].
ACCESSION   WP_007317180
VERSION     WP_007317180.1
KEYWORDS    RefSeq.
SOURCE      Gordonia effusa
  ORGANISM  Gordonia effusa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 296)
  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 296)
  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   3  (residues 1 to 296)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Gordonia effusa"
                     /db_xref="taxon:263908"
     Protein         1..296
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32812
     Region          184..276
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mepfgrrprp tqmcdicgvh ttrdlkglgy sdsdirkadl therrgwyst saadpavlsa
       61 vraggvlscv salkfvqnhg ipalwvppgd tvhvrlskgg ksrvrsrcrv klcqgagrpl
      121 ptahavdeip valscaarcv aedcwiamcd svlhntplti pdlqaamgtv sqtvrtmmsr
      181 cdsrsetgte sivrvrlraa gyrvhvqpri grsqrsdlri grliiecdse ayhggearrg
      241 dlrrdrktvg rgwvtmrvdy fdvmhrwddv ladiadftss erhrirrpqd fpglid
//
LOCUS       WP_007317359              91 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Gordonia effusa].
ACCESSION   WP_007317359
VERSION     WP_007317359.1
KEYWORDS    RefSeq.
SOURCE      Gordonia effusa
  ORGANISM  Gordonia effusa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 91)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 91)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 91)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Gordonia effusa"
                     /db_xref="taxon:263908"
     Protein         1..91
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=9113
     Region          14..91
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 madestatpr pipinvryfa aiadatgcrt etldvasatv gglrtaigdr hgsragdlaq
       61 lcsvlsgdem lrdadaavgg evdllppfag g
//
LOCUS       WP_007317767             357 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Gordonia
            effusa].
ACCESSION   WP_007317767
VERSION     WP_007317767.1
KEYWORDS    RefSeq.
SOURCE      Gordonia effusa
  ORGANISM  Gordonia effusa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Gordonia effusa"
                     /db_xref="taxon:263908"
     Protein         1..357
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37597
     Region          15..354
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mtvtttdtad vvvrienrlp rlhlehtfag grttavvgpn gagkttllra lagllradva
       61 svavgddils gpglavpphr rnvallsqda rlfphlsvad nvafapraqr lsktqvndli
      121 aswlhaceva dladrkpsql sggqaqrvai aralaaqpri llldepfral dvdvagrlra
      181 llrdllaare qttimvthdv vdvvtladda lvfdngrvad rgpvpdvlhr pansfaasla
      241 glnlvsgvwd gaavvgpgvs vagfaaepvr vntsatavfg pdavvvatse ptdasfrnvy
      301 rttvsqvvpq gdrfllraef adqemsaelt realaqlrig vgshvwlavk asavrvy
//
LOCUS       WP_007317955             338 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Gordonia effusa].
ACCESSION   WP_007317955
VERSION     WP_007317955.1
KEYWORDS    RefSeq.
SOURCE      Gordonia effusa
  ORGANISM  Gordonia effusa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 338)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Gordonia effusa"
                     /db_xref="taxon:263908"
     Protein         1..338
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36283
     Region          4..333
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mtvvsltdva sylpenrvga eyfaqfaesd elansvmfka payrhhiged etvtdmiera
       61 vepllarhgs emlsqvdvli thtqlpelpi hgaggqvahr lgiapewvid lhnggcvafv
      121 ymmklakqil ettsarsali ctaqnsagqv ftqeqvrgla qaaipgdgcg vgyltksdes
      181 pilatvcrhl peyagdmigv adpprkywea gsgqlhvgft esriakvvgr gnrlvpevas
      241 evcerigvas sdldllvtnq pnrmflrnwr ealllpedrh pdtfdecgnl fgagipvtfd
      301 hvlttgsvkp gslvmfagfa hsgdfagaaa frwggagr
//
LOCUS       WP_007318365             201 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Gordonia effusa].
ACCESSION   WP_007318365
VERSION     WP_007318365.1
KEYWORDS    RefSeq.
SOURCE      Gordonia effusa
  ORGANISM  Gordonia effusa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 201)
  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 201)
  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   3  (residues 1 to 201)
  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   4  (residues 1 to 201)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 201)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 201)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Gordonia effusa"
                     /db_xref="taxon:263908"
     Protein         1..201
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21975
     Region          16..201
                     /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"
ORIGIN      
        1 mtdstqagev tptahrvlva eddslirmdl iemlreegyd vvgeapngqv avdltvklnp
       61 dlvimdikmp vrdgidaate iaakrlapvv mltafsqrdf iekardagam aylvkpftkt
      121 dlvpaievav sryqeltale kevatigdrl etrklvdrak gllmakqsms epeafswiqr
      181 aamdrrttmk avaqvvvetl g
//
LOCUS       WP_007318438             411 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Gordonia
            effusa].
ACCESSION   WP_007318438
VERSION     WP_007318438.1
KEYWORDS    RefSeq.
SOURCE      Gordonia effusa
  ORGANISM  Gordonia effusa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 411)
  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 411)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Gordonia effusa"
                     /db_xref="taxon:263908"
     Protein         1..411
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46307
     Region          6..409
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mvarsrelsa aqarrialaa qgftdswlst tpgrtdlkrv lrrtkliqmd svnilarahy
       61 mpmfsragay dtgvlqraaw nqsprpprll veywaheaal ipiddwplfg wrmnhfregr
      121 yrytrevlrr nksqvddvla vitdsgastp rqieealgie rqgalkgsww drgevkhlce
      181 amfaggtlsa vrndhfvrhy dlaprvlgpt advvvserea hrqlvsraan ahglatvadl
      241 adyyrlktad vravlgdlid agevtevrve gwsdpaylhr sakvpravdh sallspfdpl
      301 vfyrprterl fdfhyrieiy vpehkrvhgy yvlpyllgds ivarvdlkad rkagvlqvls
      361 shiepghdrt tvatslardl stmahwrgld tvevrsrgel apalraairq s
//
LOCUS       WP_007319273             249 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Gordonia
            effusa].
ACCESSION   WP_007319273
VERSION     WP_007319273.1
KEYWORDS    RefSeq.
SOURCE      Gordonia effusa
  ORGANISM  Gordonia effusa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
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   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 249)
  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 249)
  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 249)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Gordonia effusa"
                     /db_xref="taxon:263908"
     Protein         1..249
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26625
     Region          130..216
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(149,168..169,187,190,198..199,209,214)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mdlviltset sadavlpsls llahsarvap aevsslmatg saeavlvdar tdlaaarglc
       61 rllgstgsip vvavlteggl vavnadwdld dflltttgpa eldtrlrlla vrarggemve
      121 sgstialgel videdtytar lrgkpmdlty kefellkyla qnagrvftra qllqevwgyd
      181 ffggtrtvdv hvrrlraklg gdhesligtv rnvgykavrp ssrtrpsdde sdsaamdsdd
      241 felleeave
//
LOCUS       WP_007320274             830 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Gordonia araii].
ACCESSION   WP_007320274
VERSION     WP_007320274.1
KEYWORDS    RefSeq.
SOURCE      Gordonia araii
  ORGANISM  Gordonia araii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 830)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 830)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 830)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..830
                     /organism="Gordonia araii"
                     /db_xref="taxon:263909"
     Protein         1..830
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=89004
     Region          8..797
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mtvqyeheti rdewgiphvw gttaagvvyg qgracaqdra wqieflrlra egrtaeafgp
       61 iavewdrfar rsgmdrsara vyerstprtr elldayvagv nsalessrap eldeldhrps
      121 pwqpwtpiav flmhhilfgr fttklwrvqt arafgrdglt mfdfegdgpl sadapdlpde
      181 efvadllagl adrgldtglp gggldtpsrf aprhsttdna draqdpadra qdpadraqdp
      241 adraqdpadr aqnpadcahp gdaisgsnaw gvtsartstg galiagdphr flelpgiylq
      301 cqlgcpefdv vgfafagvpg vphfahaqev awaitnamgd yqdlyrekla rdgdgitalt
      361 pdgvqpaqsw tetiavrggd dvsveivvte ngpvilggad egyalslrsp mlagsegfsf
      421 davldllfar siadvedale swsepvnriv iadaegrvhr qvvgamprra senywlpvpg
      481 wderyrwagy haasvadesf dgevadsavi anqritdcpp lqpvtteava pgranritel
      541 laddenvsvd acteihrdvy lddasdlvdl ikpltglsag aeqirarlvd wdrsmaadsv
      601 eaylfaalrt rlvgpiaghd alaklrephg fspifdpwfa phprigaafa tvlsrsaglg
      661 vdtaglaats leslaettgg gadaptwgeh hrfapihgfd lmgaspahpe laarvrpdra
      721 plggdaecvf anasavgfdd qcrvgsaary vwdladrdrg rwivpmgvdg dpgaahfqdq
      781 lplwargeti pvvsdwavlr evrgasdgad psvsdvhase aaaatpggsr
//
LOCUS       WP_007320393             382 aa            linear   BCT 20-JAN-2025
DEFINITION  DNA polymerase domain-containing protein [Gordonia araii].
ACCESSION   WP_007320393
VERSION     WP_007320393.1
KEYWORDS    RefSeq.
SOURCE      Gordonia araii
  ORGANISM  Gordonia araii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Zhu,H., Nandakumar,J., Aniukwu,J., Wang,L.K., Glickman,M.S.,
            Lima,C.D. and Shuman,S.
  TITLE     Atomic structure and nonhomologous end-joining function of the
            polymerase component of bacterial DNA ligase D
  JOURNAL   Proc Natl Acad Sci U S A 103 (6), 1711-1716 (2006)
   PUBMED   16446439
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Zhu,H. and Shuman,S.
  TITLE     A primer-dependent polymerase function of pseudomonas aeruginosa
            ATP-dependent DNA ligase (LigD)
  JOURNAL   J Biol Chem 280 (1), 418-427 (2005)
   PUBMED   15520014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Gordonia araii"
                     /db_xref="taxon:263909"
     Protein         1..382
                     /product="DNA polymerase domain-containing protein"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=42125
     Region          2..335
                     /region_name="LigD"
                     /note="Eukaryotic-type DNA primase [Replication,
                     recombination and repair]; COG3285"
                     /db_xref="CDD:442515"
ORIGIN      
        1 maspatevdv dgvavrltsp dkivfpeasg ggrkrdvfdy yvsmagtadd pgpllravyr
       61 rptflqrfpd giegdevyqk hlprkrpdyl hgtviefpsk rtghalcpti padiawaaqm
      121 gtitfhcwpt vddtiplaga pggdesnpat degsartehp nnhpdqlrid ldpppgkdfd
      181 evravaldvv kpvldelglp gfvktsgsrg ihvfipvkpq wdfiatrrsv ialgremerr
      241 apdritmsww keergdrvfi dynqnardrs masaysvrrs akgkvstplt wtelvdadpd
      301 dltmstvaal vadrgdpwad maaaavgiep llemvardde qglgdlpypp sfpkmpgepp
      361 rvqpsrkvpe nwdqwgnrrt qt
//
LOCUS       WP_007322840             330 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Gordonia
            araii].
ACCESSION   WP_007322840
VERSION     WP_007322840.1
KEYWORDS    RefSeq.
SOURCE      Gordonia araii
  ORGANISM  Gordonia araii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Gordonia araii"
                     /db_xref="taxon:263909"
     Protein         1..330
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=35658
     Region          1..328
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msisvigank rygdfaaldd vsldipegsl tsllgpsgsg kstllraiag ldsldsgtvi
       61 ingtdvssas pqkrdigfvf qhyaafkhln vrdniafglk irkrpkeeid kkvdelldiv
      121 gltvfqkrfp aqlsggqrqr malaralavd pqvllldepf galdakvred lrkwlrrlhd
      181 evhvttvlvt hdqaealdvs driavlnqgr veqvgspddl ydrpvnpfva sflgstvrvn
      241 gelvrphdir igrnpeialp ggdadldtgv vkatvqrvvn lgfetrvell asatgdefaa
      301 qitrgdqnal hlqpgetvya ratkvaafdg
//
LOCUS       WP_007322865             262 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Gordonia araii].
ACCESSION   WP_007322865
VERSION     WP_007322865.1
KEYWORDS    RefSeq.
SOURCE      Gordonia araii
  ORGANISM  Gordonia araii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 262)
  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 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   3  (residues 1 to 262)
  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   4  (residues 1 to 262)
  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 262)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Gordonia araii"
                     /db_xref="taxon:263909"
     Protein         1..262
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28108
     Region          4..256
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          179..256
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mvdpsrgvly paklptltrl appplaaelv gwfwipewqi aagrssrqel vpfpasnlvv
       61 eldhvgftgp attishrdlt gtgwavgall rpagvaalid dpgayvdsyq pfeaadlhda
      121 vfaamtdgda atrhsraita fadwladrvp epsdearlan amadllmsdp tilrlddaaq
      181 alassprtlq rlarryvgls psamirrrrl qeaaqlirdd paadlasiaa dlgytdhahl
      241 sndfrsvlaf spsayrgtvh pn
//
LOCUS       WP_007323675             429 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Gordonia araii].
ACCESSION   WP_007323675
VERSION     WP_007323675.1
KEYWORDS    RefSeq.
SOURCE      Gordonia araii
  ORGANISM  Gordonia araii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 429)
  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 429)
  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
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 429)
  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   5  (residues 1 to 429)
  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   6  (residues 1 to 429)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 429)
  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 20324439
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Gordonia araii"
                     /db_xref="taxon:263909"
     Protein         1..429
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45078
     Region          <74..>125
                     /region_name="COG3355"
                     /note="Predicted transcriptional regulator
                     [Transcription]"
                     /db_xref="CDD:442583"
     Region          126..414
                     /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 mtsildrpvt ttriapprrv pharsprpvg apvparaprr padlhvttpd lalsdkpaaq
       61 vlravrlaap vfrdeiaest glsistvnrq vgallkagli rersdlapsg avgrprlpve
      121 isvaehltig vhigykvtsi tahdllhrvv gaisvptpad agaenaltal ahsvsgflar
      181 wrnreirwvg vavggrvhdg gvvdhprlgw sqaevgrifa qtlgypvsva shveamaaae
      241 lvanpeqras flyfyaremv gvafsvdgsv htpsagppvi ghfpigptrl ldphrtgqle
      301 aatsdtgiva aaraaglelt eiadlheaar dgneiardil teraevlgra valisdifnp
      361 dhvvlggqaf tdapqtlpvv artirdtsvt akrdvrvsra gvtvqqqaag aisldalytd
      421 plgaiaitd
//
LOCUS       WP_007323882             309 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Gordonia araii].
ACCESSION   WP_007323882
VERSION     WP_007323882.1
KEYWORDS    RefSeq.
SOURCE      Gordonia araii
  ORGANISM  Gordonia araii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Gordonia araii"
                     /db_xref="taxon:263909"
     Protein         1..309
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=34385
     Region          8..163
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mdhfpfdgeg ilriadakac gidprqiyqa erdqrlvrvm pgvyvlpver rpeqrhrlrv
       61 laaqlppatv vshssaavvh glgmlrpdld qlhltsvrga agyrrkmryl hpgrlgeddi
      121 vevdgvpvts kertafdvar ssrwgfagal svfdsalrak adravmeqfc lsrqagvgva
      181 rralaladar aenpgeswsr aqmiqagiss prlqtdvfdr hgtflarpdf dwideagaik
      241 lvgefdglgk yldylrpget aedvirreke regrlrdmei lvvrwtwkdl maravaalvs
      301 knlrlvglv
//
LOCUS       WP_007323933             298 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Gordonia araii].
ACCESSION   WP_007323933
VERSION     WP_007323933.1
KEYWORDS    RefSeq.
SOURCE      Gordonia araii
  ORGANISM  Gordonia araii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Gordonia araii"
                     /db_xref="taxon:263909"
     Protein         1..298
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32698
     Region          9..298
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 msadpergyr iaarlsarhg rtyhlaatll prrnrravha lygfarvadd ivdvrqvges
       61 spvarldelf agldaalrgm pvhssaettd llaavadsva ifdidpayft dfersmrmdl
      121 psapeftpry ldmahlreyt rgsaaviglm lvrvlgadpd dpvtatgaam lgeafqltnf
      181 lrdvaedldr driylpaddl aafgvdeahl racrargett pqlrralahl aavnrdwyhr
      241 aspaidalpg rtrpairaaa rsyadilrvl aenhyevfsd ravvgvrtrl rhaaaalf
//
LOCUS       WP_007326691             168 aa            linear   BCT 20-JAN-2025
DEFINITION  3-hydroxyacyl-ACP dehydratase FabZ family protein [Rhodopirellula
            baltica].
ACCESSION   WP_007326691
VERSION     WP_007326691.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula baltica
  ORGANISM  Rhodopirellula baltica
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
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 10101294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Rhodopirellula baltica"
                     /db_xref="taxon:265606"
     Protein         1..168
                     /product="3-hydroxyacyl-ACP dehydratase FabZ family
                     protein"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=18506
     Region          1..124
                     /region_name="FabZ"
                     /note="FabZ is a 17kD beta-hydroxyacyl-acyl carrier
                     protein (ACP) dehydratase that primarily catalyzes the
                     dehydration of beta-hydroxyacyl-ACP to trans-2-acyl-ACP,
                     the third step in the elongation phase of the bacterial/
                     plastid, type II, fatty-acid...; cd01288"
                     /db_xref="CDD:238615"
ORIGIN      
        1 mrwfwvdrft efvsgshasg vknvaldeev vddyclgytm lpptliiegl aqlggilvhe
       61 kfgftkrvvl akvgsakyya parpgdslqy hvklertqes gatvtgtshc dgelqaevdl
      121 mfafleeghl idgplfnpgd llammrmmnf fhvavtadge pipfhenl
//
LOCUS       WP_007329203             154 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Rhodopirellula
            baltica].
ACCESSION   WP_007329203
VERSION     WP_007329203.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula baltica
  ORGANISM  Rhodopirellula baltica
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 154)
  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 154)
  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   3  (residues 1 to 154)
  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   4  (residues 1 to 154)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 154)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 154)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Rhodopirellula baltica"
                     /db_xref="taxon:265606"
     Protein         1..154
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=17446
     Region          6..>142
                     /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"
ORIGIN      
        1 mkdsnlkiyl asgddgqrkv lqanlellth qvelstsspa vmirrcqenp pdiavvgtrf
       61 esddcfklln elselnvcpa vavlehqdid rshrlmadqv mgvlvqpvnd rdlrtaiyla
      121 rrrfdqsklm kqridelket leniddesee ashe
//
LOCUS       WP_007327462             184 aa            linear   BCT 20-JAN-2025
DEFINITION  transcription termination/antitermination protein NusG
            [Rhodopirellula baltica].
ACCESSION   WP_007327462
VERSION     WP_007327462.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula baltica
  ORGANISM  Rhodopirellula baltica
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Kang,J.Y., Mooney,R.A., Nedialkov,Y., Saba,J., Mishanina,T.V.,
            Artsimovitch,I., Landick,R. and Darst,S.A.
  TITLE     Structural Basis for Transcript Elongation Control by NusG Family
            Universal Regulators
  JOURNAL   Cell 173 (7), 1650-1662 (2018)
   PUBMED   29887376
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Liu,B. and Steitz,T.A.
  TITLE     Structural insights into NusG regulating transcription elongation
  JOURNAL   Nucleic Acids Res 45 (2), 968-974 (2017)
   PUBMED   27899640
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Steiner,T., Kaiser,J.T., Marinkovic,S., Huber,R. and Wahl,M.C.
  TITLE     Crystal structures of transcription factor NusG in light of its
            nucleic acid- and protein-binding activities
  JOURNAL   EMBO J 21 (17), 4641-4653 (2002)
   PUBMED   12198166
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415705
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Rhodopirellula baltica"
                     /db_xref="taxon:265606"
     gene            1..184
                     /gene="nusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
     Protein         1..184
                     /product="transcription termination/antitermination
                     protein NusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
                     /calculated_mol_wt=21045
     Region          26..183
                     /region_name="NusG"
                     /note="Transcription termination/antitermination protein
                     NusG [Transcription]; COG0250"
                     /db_xref="CDD:440020"
ORIGIN      
        1 mpilpfepdc ypddlidqee sldspwwlly tksrqekavi rklrdagvph yapmvkqrfr
       61 spagrmresf vplfstyvfl rgddqaryea ictgsvlkas eivqvpdlie dlqqirsliv
      121 mgvpltiesq lqpgehvrvk ngtfagyegt virrenetrl lvfvrfmeqg vsvkledcql
      181 ekid
//
LOCUS       WP_007332823             370 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Rhodopirellula baltica].
ACCESSION   WP_007332823
VERSION     WP_007332823.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula baltica
  ORGANISM  Rhodopirellula baltica
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Rhodopirellula baltica"
                     /db_xref="taxon:265606"
     Protein         1..370
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=39407
     Region          1..362
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mnvlvfnvgs ttlkyacida eteevissgl vdrigqpggd ainhivaaki aidevglnnv
       61 cvighrivqg gdlfleptvv tpdvlkrlrt ldtlaplhnp aarsvveglv gigtpqtlvf
      121 dtsyfatlsp aayryavped wyqkhavrry gfhgtshqyv tqkairfigg ndesriislh
      181 lgggasatas igghavdtsm gmtpleglvm atrsgdldpa ivlhmtehag fepsdvrnsl
      241 nrksgllglc gdqdmrtvln rrqagdpaat laidiyvrri iktvgsyiai lggldalvft
      301 agvgqhssei rglvcdslqh fgislseekn qsccddpadi sapdarvrtl vvdtneelai
      361 arlvrnrats
//
LOCUS       WP_007336079             184 aa            linear   BCT 20-JAN-2025
DEFINITION  transcription termination/antitermination protein NusG
            [Rhodopirellula baltica].
ACCESSION   WP_007336079
VERSION     WP_007336079.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula baltica
  ORGANISM  Rhodopirellula baltica
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Kang,J.Y., Mooney,R.A., Nedialkov,Y., Saba,J., Mishanina,T.V.,
            Artsimovitch,I., Landick,R. and Darst,S.A.
  TITLE     Structural Basis for Transcript Elongation Control by NusG Family
            Universal Regulators
  JOURNAL   Cell 173 (7), 1650-1662 (2018)
   PUBMED   29887376
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Liu,B. and Steitz,T.A.
  TITLE     Structural insights into NusG regulating transcription elongation
  JOURNAL   Nucleic Acids Res 45 (2), 968-974 (2017)
   PUBMED   27899640
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Steiner,T., Kaiser,J.T., Marinkovic,S., Huber,R. and Wahl,M.C.
  TITLE     Crystal structures of transcription factor NusG in light of its
            nucleic acid- and protein-binding activities
  JOURNAL   EMBO J 21 (17), 4641-4653 (2002)
   PUBMED   12198166
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415705
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Rhodopirellula baltica"
                     /db_xref="taxon:265606"
     gene            1..184
                     /gene="nusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
     Protein         1..184
                     /product="transcription termination/antitermination
                     protein NusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
                     /calculated_mol_wt=21031
     Region          26..183
                     /region_name="NusG"
                     /note="Transcription termination/antitermination protein
                     NusG [Transcription]; COG0250"
                     /db_xref="CDD:440020"
ORIGIN      
        1 mpilpfepdc ypddlidqee sldspwwlly tksrqekavv rklrdagvph yapmvkqrfr
       61 spagrmresf vplfstyvfl rgddqaryea ictgsvlkas eivqvpdlie dlqqirsliv
      121 mgvpltiesq lqpgehvrvk ngtfagyegt virrenetrl lvfvrfmeqg vsvkledcql
      181 ekid
//
LOCUS       WP_007337508              86 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Rhodopirellula baltica].
ACCESSION   WP_007337508
VERSION     WP_007337508.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula baltica
  ORGANISM  Rhodopirellula baltica
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 86)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 86)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 86)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Rhodopirellula baltica"
                     /db_xref="taxon:265606"
     Protein         1..86
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8944
     Region          6..86
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mneprsievl lfagaseaad gadrvivqsh enttaselik qladqysala plahrsrlai
       61 dqkyvspshv iqpgaevali ppvsgg
//
LOCUS       WP_007338896             753 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Rhodopirellula
            baltica].
ACCESSION   WP_007338896
VERSION     WP_007338896.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula baltica
  ORGANISM  Rhodopirellula baltica
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 753)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 753)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Rhodopirellula baltica"
                     /db_xref="taxon:265606"
     Protein         1..753
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=83749
     Region          59..747
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 msisikdnrn dagktfqlpt llqrrtgpmt relvlrpgdh glgmthdsma adttttatcg
       61 fcatgcglrl hlkdgeaigl tpetaypvnl gmacpkgwea lrvldspera tlpllrdetg
      121 klspiewdda fskfcdgmkk vqaehgpesv aflstgqiac eemaflgala rfgmdirhcd
      181 gntrqcmata vtaykesfgf dsppytyddf eqsdclvfig anpcighpim wervlrnphn
      241 peiividprr tetaaaatkh lqlrpkndla llyaitneli lrdfvehdfv qnhtqgfeel
      301 rqhvsqydla tvceeaglav edvsaaveai grgravslww tmgvnqsyqg trtaqaiini
      361 alitgnigrp gtgansitgq cnamgsrlws nttnlfghhs fteesdrrkv aealnipvek
      421 ipsttswkyd riiegirnge ikglwvvatn pahswidqgd vrelfdqldf lvvqdmyktt
      481 etcshadlil psagwgekeg tfinserryg llkkvrhapg qaladfqifr giahrwgvge
      541 mfaewtspea vfqimqrasr gqpsdisgie gyeqidrcgg iqwpwsadha sggfepeqqr
      601 rlfadgqffh edhrahlivd dvtpmpepad ddypivlltg rgtvsqwhtq trtrqspllr
      661 slypnqpyve mhprdadelg iehgdlvrvr srrghadata clthsvqpgq vfmpmhyect
      721 nqltlshfdp hsgqpsykdc avriepvlts dhd
//
LOCUS       WP_007339464             222 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Rhodopirellula baltica].
ACCESSION   WP_007339464
VERSION     WP_007339464.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula baltica
  ORGANISM  Rhodopirellula baltica
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Rhodopirellula baltica"
                     /db_xref="taxon:265606"
     Protein         1..222
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=24271
     Region          8..221
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 msdatkrrrr ivlamtgasg apiavrllqv mrrdpnvevh ltispsgaav lhqemglqln
       61 lrspdlnall acvpqwasep apefdeigpt gderlhyhqh ddymtpiasg sfltdamvlc
      121 pcsgstlsgi arsaasnlvq raaevhlkeh rklvvvpret pmsvlqienm hrlaaagvvl
      181 lpampgwyhd vkriedlvdf vvarildqig ldngliqrwk da
//
LOCUS       WP_007342505             164 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Neisseria bacilliformis].
ACCESSION   WP_007342505
VERSION     WP_007342505.1
KEYWORDS    RefSeq.
SOURCE      Neisseria bacilliformis
  ORGANISM  Neisseria bacilliformis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Neisseria bacilliformis"
                     /db_xref="taxon:267212"
     Protein         1..164
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=18237
     Region          1..141
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mktgnqhgft lielmmtimv iailaaiayp sydefirrsr lenvrgdlle narrlesfya
       61 rnrtfngfne lkndnkyfdi ffvynpldst lgnhlvgtsn aaadpdvghy lltakakast
      121 ngketrfmql nddgittict gqattqapvl ipdtgtppke cemy
//
LOCUS       WP_007342679             552 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Neisseria bacilliformis].
ACCESSION   WP_007342679
VERSION     WP_007342679.1
KEYWORDS    RefSeq.
SOURCE      Neisseria bacilliformis
  ORGANISM  Neisseria bacilliformis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Neisseria bacilliformis"
                     /db_xref="taxon:267212"
     Protein         1..552
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=62456
     Region          3..428
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mpqltwmgkd kvknhhhhvp fhlldklydf qaaegkpanr rdnllihgdn llalksllpe
       61 fggrinciyi dppyntgneg wvyndnvndp riqkwlgevv gregedlsrh dkwlcmmypr
      121 lkllkqllad dgvifisidd neqaalklvc deifgsanfi gnivratgtt aqdthglgka
      181 ydnilvfsks snyliggipl sesdekrynl edkkgkfsil qlrrtggedr redrpsmyfp
      241 ilapdgtevf pigptgyesr wrvgietvke meaenklyfk kdndgewkvy ykyyfenrtk
      301 rpsdlwtdld gnkkasielk eifaskvfet pkpvalleki ltiaaspnai ildsfigsgt
      361 tahavlnlnr kdggnrrfig iemmdyaenv taerirrvin gygtkaetqg gtgggfafyr
      421 vgdalfdaeh nlnsaapvas vrryiayteg lpvsarqpen gvmpsensnr qpenpvspyf
      481 lgakdgtayv fhyepdratd lslaflqtir aemlpepper wviyadrtll sdeqmqrlni
      541 rfkriprdis kl
//
LOCUS       WP_007348661             166 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Marinobacter sp. ELB17].
ACCESSION   WP_007348661
VERSION     WP_007348661.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter sp. ELB17
  ORGANISM  Marinobacter sp. ELB17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 166)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Marinobacter sp. ELB17"
                     /db_xref="taxon:270374"
     Protein         1..166
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=18343
     Region          11..165
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cl49639"
                     /db_xref="CDD:483979"
     Site            order(109,123,126,139..142,144)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mvigdsavsh llidiarqrl qlfddssvct gdysvstarn gtgerdgsgc tprgqhyirv
       61 migagqplns vfrgrrptge iyhpelaigy perdwilsri vwlcgrqwgv nrgpgvdtfr
      121 rfiyihgtpd tepmgtplsh gcvrmrnadl valfarlqpg mpvfif
//
LOCUS       WP_007348369             119 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Marinobacter sp.
            ELB17].
ACCESSION   WP_007348369
VERSION     WP_007348369.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter sp. ELB17
  ORGANISM  Marinobacter sp. ELB17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (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   2  (residues 1 to 119)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 119)
  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 119)
  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 119)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Marinobacter sp. ELB17"
                     /db_xref="taxon:270374"
     Protein         1..119
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13660
     Region          27..111
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(46,65..66,83,86,94..95,106,111)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mplllarlns lyrrdnpere ciqiadlriy pkeyrairse qelkltptsw killflarrs
       61 pvvvsrneie ahiwpnddvd egtvnvhlhq lrkvvdkpfn cplirthvgi glslsgetp
//
LOCUS       WP_007348911             155 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Marinobacter sp. ELB17].
ACCESSION   WP_007348911
VERSION     WP_007348911.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter sp. ELB17
  ORGANISM  Marinobacter sp. ELB17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Marinobacter sp. ELB17"
                     /db_xref="taxon:270374"
     Protein         1..155
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16990
     Region          18..144
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mvyltlfata faaatllpay seillgtlla kgygpfwlwf aattgntlgs vvngiigrqv
       61 drfkhkrwfp mtevqlhnar nrfnrfgqws llmgwlpigg daltlvggim rvpwlnfvil
      121 vgigkglrya ivmwlvlsay gpeiealvsg lvfsg
//
LOCUS       WP_007349019             354 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Marinobacter sp.
            ELB17].
ACCESSION   WP_007349019
VERSION     WP_007349019.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter sp. ELB17
  ORGANISM  Marinobacter sp. ELB17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 354)
  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 354)
  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 354)
  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 354)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Marinobacter sp. ELB17"
                     /db_xref="taxon:270374"
     Protein         1..354
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39422
     Region          23..349
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mrklivatla laatlatssa laeetynlrl aetwgpsspi lgdttkhmae maetmsggrl
       61 kiridssnkh kapfgifdlv rngqydmght asyyykgsip namyfttvpf gmiapeqyaw
      121 fyhgggmela qkvyqpfgll sfpggntgnq mggwfrdeit slddlkgikm rtpgfagevm
      181 selgvavtni ppgelysale rgtidavewv gpaldlqmgf hqiakyyysg wqepgaevqf
      241 linektwnkl pedlqeilrv amrtaaydmy iqsthesgva wsrmqqdypd vthkifppev
      301 isalrdvter llkeasaadp lakeiitsqq eylkqvrqwt nisdkaylns vvne
//
LOCUS       WP_007350042             173 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Marinobacter sp. ELB17].
ACCESSION   WP_007350042
VERSION     WP_007350042.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter sp. ELB17
  ORGANISM  Marinobacter sp. ELB17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 173)
  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 173)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 173)
  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   4  (residues 1 to 173)
  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   5  (residues 1 to 173)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Marinobacter sp. ELB17"
                     /db_xref="taxon:270374"
     Protein         1..173
                     /product="TRAP transporter small permease subunit"
                     /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=19347
     Region          1..156
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mtklamqgwd gllavlrwtm fvvlifmmlt icydvimryv fvaptswsle intfllvyla
       61 vvgageaqrh dahiritfft qrfpksgqal itmltsalgl vfctimvwrg slmahdawey
      121 gervssafgt pmvypyalip igfgvlglqf lidilrvgyd lchpksgedi tha
//
LOCUS       WP_007350071             254 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Marinobacter sp. ELB17].
ACCESSION   WP_007350071
VERSION     WP_007350071.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter sp. ELB17
  ORGANISM  Marinobacter sp. ELB17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 254)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Marinobacter sp. ELB17"
                     /db_xref="taxon:270374"
     Protein         1..254
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=27916
     Region          85..229
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mpmirlnqwl lgaalcsqii lgghnamaan sdkpltkats dsatfssats taqqtrlnnt
       61 laklapranp qvlrlaaral acaqpdakrl avidfslpst eqrlwvfdlk rqkllfkelv
      121 shgrgsgnae aksfsnipes yqssiglfrt lnsyhgrngy slrlkgleag vndlayqrai
      181 vihgadyvsk nfieqtgrlg rshgcpavrq evaiklidsl kenqylftyy pdpewlatse
      241 flsckrtdar lamn
//
LOCUS       WP_007350163             378 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Marinobacter
            sp. ELB17].
ACCESSION   WP_007350163
VERSION     WP_007350163.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter sp. ELB17
  ORGANISM  Marinobacter sp. ELB17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Marinobacter sp. ELB17"
                     /db_xref="taxon:270374"
     Protein         1..378
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=41837
     Region          1..353
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msitvdgikk rfgkfqalnn vsldipegkl tallgpsgsg kttllriiag lesadsgqis
       61 fsgrdvtglh vrdrnigfvf qhyalfrhmt vaqniafgld slprkqrpak agiqkrvsel
      121 lemiqlphla qrypaqlsgg qkqrvalars iatqpkilll depfgaldak vrkdlrrwlr
      181 nlhdefhfts ifvthdqeea lelsdqvvvm sqgrveqvne pielyarpes rfvfdflgqv
      241 nvisgqvkqg slnqgnawvt vpgvqhkgda qlylrphevr latapvahan lplrieavsl
      301 igsevrvelr pegwqsegsn niwevgisha efnsqrptrg dlryavpevg hlftgndaqp
      361 atvnwaeael aprvrlis
//
LOCUS       WP_007351581             176 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Marinobacter sp.
            ELB17].
ACCESSION   WP_007351581
VERSION     WP_007351581.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter sp. ELB17
  ORGANISM  Marinobacter sp. ELB17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 176)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 176)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 176)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Marinobacter sp. ELB17"
                     /db_xref="taxon:270374"
     Protein         1..176
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=19744
     Region          <1..>171
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 msellasaer veqgipltpe ldqalfhgss iggarpkalv edngikyiak fssttdlfsv
       61 vkaeyiamrl aslaglnvap vrltraagkd vllierfdre rrengwlrkp lvsaltilgl
      121 ddmmaryasy edlaevirhr ftkprqtlre lfsrlvfnvl cgntddharn heydrk
//
LOCUS       WP_007351778             303 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Marinobacter sp. ELB17].
ACCESSION   WP_007351778
VERSION     WP_007351778.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter sp. ELB17
  ORGANISM  Marinobacter sp. ELB17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Marinobacter sp. ELB17"
                     /db_xref="taxon:270374"
     Protein         1..303
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32986
     Region          23..297
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mlvtimqqqp tqqhdatipq qsplcidlhc hstasdgals padllarahe kgvshlaltd
       61 hdtlnglrsa rlaaqdynie lisgvelsca wrshtihivg ldfaeddpqf larlqqqnan
      121 rharagaive rlarlkvdnl lehatkhagg dvpgrphfaq alvdagvvkn iaqafkrhlg
      181 agkpgdvkay wpeleevvrw vndaggiavl ahprkydlsa tklralvadf rraagrgmel
      241 cspgqtasdv nflaqlcqse glwasqgsdf htpkapwael griqkmpegl spvwhhfkqp
      301 iaf
//
LOCUS       WP_007351794             257 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Marinobacter sp. ELB17].
ACCESSION   WP_007351794
VERSION     WP_007351794.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter sp. ELB17
  ORGANISM  Marinobacter sp. ELB17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 257)
  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 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
REFERENCE   3  (residues 1 to 257)
  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   4  (residues 1 to 257)
  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 257)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Marinobacter sp. ELB17"
                     /db_xref="taxon:270374"
     Protein         1..257
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28657
     Region          14..256
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <146..256
                     /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 mlnakllklp tashqhrheh hqvvvgvqge adlfvdgnas hidawraclv ptgarhdysg
       61 dqrnhvlvid vdpympsvgs rahshhqrlk plfrqsstls ldnrlqglvq faadefdrap
      121 ensslhqhfa gtilhclaqr laetprqpap lrnvvnpemv rrfllenlhr digvrdmaav
      181 sclsvsrfhd lfrqstgttp hqfllqtrle qaskllerts lsvseishrt gfssqsalan
      241 alkkyrgtta salrarc
//
LOCUS       WP_007351812             173 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Marinobacter sp. ELB17].
ACCESSION   WP_007351812
VERSION     WP_007351812.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter sp. ELB17
  ORGANISM  Marinobacter sp. ELB17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 173)
  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 173)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 173)
  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   4  (residues 1 to 173)
  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   5  (residues 1 to 173)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Marinobacter sp. ELB17"
                     /db_xref="taxon:270374"
     Protein         1..173
                     /product="TRAP transporter small permease subunit"
                     /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=18603
     Region          16..170
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 msqsvthsia srnsviagyi rvidtlaivt avfaaillal gvlvvvqmvf tryvlgestm
       61 wqtefttyai taamllatpy vlktgghvav tvlpdalhgl pkrimrltas lvglsfclal
      121 aygswyyvye aytmawttgt vwnpplwpav lpmavgasll slqyvaeilr gea
//
LOCUS       WP_007351937             395 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Marinobacter sp. ELB17].
ACCESSION   WP_007351937
VERSION     WP_007351937.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter sp. ELB17
  ORGANISM  Marinobacter sp. ELB17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Marinobacter sp. ELB17"
                     /db_xref="taxon:270374"
     Protein         1..395
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42980
     Region          6..393
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mentllvvnc gssslkialf dkdrqkiasm lagrlntpna rfrigkqrdv trlppntthk
       61 ealavlmdta qkkglmpkqp aaighrivhg getfreavli ddevlvaika cnllaplhnp
      121 vnvegimatr elfplvpqva vfdtafhqtl pehafhyalp qnyyrdwgvr rygfhgtsha
      181 ymlqqaalrl eqstaetsii sahlgngcsi tairdgksvd tsmgltpleg lvmgtrsgdv
      241 dpglfdylqs kgvsaeqlhn elnhssgllg lsgqtndmrt lsdladqgdp saqlaidvfc
      301 frlakyvaam mvslnrldal vftggigqns arvrqqtvnq lgllgfaidq qnnddnglnr
      361 dgridckesr fpilviatde erviageaar laeln
//
LOCUS       WP_007352059             425 aa            linear   BCT 20-JAN-2025
DEFINITION  TerD family protein [Marinobacter sp. ELB17].
ACCESSION   WP_007352059
VERSION     WP_007352059.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter sp. ELB17
  ORGANISM  Marinobacter sp. ELB17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Marinobacter sp. ELB17"
                     /db_xref="taxon:270374"
     Protein         1..425
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=45027
     Region          3..425
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mtvlgpgana pltsndltvl irhgtipgad idvsaflvta sgkvrsdadm cfygqpsvag
       61 gavalsgsen gearfavglg rvpagvekvv ftatihenra sfsrvpeitl daggvrgaip
      121 cagmtetali laelyqrnga wkfrvvgqgf ngglaalakh lgvevaepap paptpppapa
      181 ptpappptpa papiptptsn stptptpsps ptptpvppps trsvnlskvs ltkqnntvsl
      241 kkeggrfgkm qinlnwnqsq tqkktgffsr gsvaidldlg afvetrdgkr hvvqalgngf
      301 gdfqqapfvr llgddrtgst sdgewleing drwadirrvl vyafiyegvp nwketdgivr
      361 vlvpgqpeve irmnefeqdg smcavvgidn hdgqvrvsrq vtfhsghkal dkqydwgfrw
      421 tagrk
//
LOCUS       WP_007352348             409 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Marinobacter sp.
            ELB17].
ACCESSION   WP_007352348
VERSION     WP_007352348.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter sp. ELB17
  ORGANISM  Marinobacter sp. ELB17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 409)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 409)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Marinobacter sp. ELB17"
                     /db_xref="taxon:270374"
     Protein         1..409
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44628
     Region          18..387
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mtwtpiskay vfstllgdpv pvgvivkdeg ifsfayaksw lanpiayald plhipldtqt
       61 fqsnrlfgvl adslpdnwgq rvilathkqa paneiewlls argrgvgala fsasrskvqp
      121 sntppklsdl drvltamddi qasrpvddpe lihlieygss fggarpktii qhedtewlak
      181 lsrhddtfdq igaeaaslam akqlgldvpn fqvhmsgkrp vllvsrfdre sgqpsahyls
      241 gqsalatrki qesdfakdys yqglatvirk lssqpkqdlt elftrmafnv aigntddhlk
      301 nhgflfkpdq gwslapafdl lphpnqiaqh aigigvngrs stisnllsrs safglsdqqa
      361 nrivdqvlsi adeahhyfgq ygvpetdnrv lsgicqrfse ddagtgpsp
//
LOCUS       WP_007352737             178 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Marinobacter sp. ELB17].
ACCESSION   WP_007352737
VERSION     WP_007352737.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter sp. ELB17
  ORGANISM  Marinobacter sp. ELB17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Marinobacter sp. ELB17"
                     /db_xref="taxon:270374"
     Protein         1..178
                     /product="TRAP transporter small permease subunit"
                     /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=19892
     Region          4..166
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mskitrylrf qdglsewigr atswltlgii gvllyevaar yifnaptvwg helatmffga
       61 lsilagsytl lhrqhvcsdv iyrlfplrgq alcdvivytl gilvlavffk mavefayrsw
      121 ligeysnssi wrplvwpika tipvavglli lqsiaelvra lvrlagvpfd dpridtge
//
LOCUS       WP_007352919             109 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [Kamptonema].
ACCESSION   WP_007352919
VERSION     WP_007352919.1
KEYWORDS    RefSeq.
SOURCE      Kamptonema
  ORGANISM  Kamptonema
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Kamptonema"
                     /db_xref="taxon:1501433"
     Protein         1..109
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12551
     Region          10..105
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mqivsqekyq qlpikisedk iadfcqrnhi sklslfgsvl rsdfrpdsdv dvlvefmqek
       61 cpgffglagm eielteilgr kvdlrtaeel sryfrekvvn saeviyvyr
//
LOCUS       WP_007353065             612 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CHASE2 domain-containing protein [Kamptonema].
ACCESSION   WP_007353065
VERSION     WP_007353065.1
KEYWORDS    RefSeq.
SOURCE      Kamptonema
  ORGANISM  Kamptonema
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 612)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Kamptonema"
                     /db_xref="taxon:1501433"
     Protein         1..612
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=68320
     Region          27..607
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mnfkdwmvhl kktisvvqky lasnppwltg aiaavvsvgm lqlgawrple ylgyktlfql
       61 rdrsiipnpg wdrrivvigi ddrslqeygq fpwsrdryvq lleslkksap taigfdilfi
      121 dpspkdaela aaikasgnva lartgdeenl vpeikaaalf vgdilhesda dgisrranlw
      181 fngtpsfssa liqiynihnp gnpillpqpi vgveqqkvav nwpgktrflt tygfsdvvag
      241 kipqdaftnk lilvgfvaeg ldrvrtpldr ttagvylhaa midnllnsrl lrrvpkvwei
      301 illlgigpvt swilfhrdvk erttiaiglp tawftvaall fgfshwwipi aspigtiila
      361 gialqareqy ekqqlmrlfe khvdpetaqm iwkrkaeifq qgelepqevt atvlfmdirs
      421 fttisekmrp relltwlnty leamtdcimn rggvvdkyig daimavfgvp fchteekeie
      481 qdamnaiaac idmherlnel nkhlreegkp likfgiglht gqlvagsvgg arrlnysvig
      541 davnvaarle amnkevtsds pynllvtert fdcvrdryea qkvgsiqlrg kaettvvyai
      601 lgekqlltks et
//
LOCUS       WP_007353227             364 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Kamptonema].
ACCESSION   WP_007353227
VERSION     WP_007353227.1
KEYWORDS    RefSeq.
SOURCE      Kamptonema
  ORGANISM  Kamptonema
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 364)
  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 364)
  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 364)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Kamptonema"
                     /db_xref="taxon:1501433"
     Protein         1..364
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=38967
     Region          26..96
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          141..>251
                     /region_name="PHA03269"
                     /note="envelope glycoprotein C; Provisional"
                     /db_xref="CDD:165527"
     Region          278..341
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mtknlffllf kktkknlesa nteqaqslae igaqlrqfre qhsislervs vvtmirsrll
       61 qaieegelde lpepvytqgl ikryaeamgl dgeqfanfcp atpilerpkt swrdlplaql
      121 rpihlyllyl fvivasvngl sqaigrsdta dtaetgvtas kppakapips ksvtkqpgnq
      181 gtlvaerasl ptapvkqpsf pdaavrddya sspqplvtsa snqptpsisa qvtnasnqpt
      241 psisaqvtna sgqgspsvsv katnalaqpa ahqqvtisvt vkeetwvlie vdgktefegn
      301 lpvgtqrtwq akeqlffrag naggvllavn ngeakqlgqp gaieevvlka neppaatekr
      361 kdrg
//
LOCUS       WP_007354311             313 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Kamptonema].
ACCESSION   WP_007354311
VERSION     WP_007354311.1
KEYWORDS    RefSeq.
SOURCE      Kamptonema
  ORGANISM  Kamptonema
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Kamptonema"
                     /db_xref="taxon:1501433"
     Protein         1..313
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31964
     Region          68..309
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 matlfpnltn apgdntitqs qippnpnpqn ppqnqtppnp nppnppqnqt pptpptppan
       61 sisttsgndn itgdasdnfi lggtgsdtls ggestdtvsy lslnsaitlq aggivnkgaa
      121 gndildtieq iiaplgqint ldastgsgva sinvdlstns vavnnlpgig tlnltvenfv
      181 nvvgtpnvdv itgnrqnnnl vggagndtls glrgndtlig vdlssatpgs netdvliggq
      241 grdtfvlgda tntyyqgagv tfiqdfqqnr dviqlhgqls dytivgnsin lagtsdqiav
      301 iqgnfttdnf vfv
//
LOCUS       WP_007354324             237 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Kamptonema].
ACCESSION   WP_007354324
VERSION     WP_007354324.1
KEYWORDS    RefSeq.
SOURCE      Kamptonema
  ORGANISM  Kamptonema
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Kamptonema"
                     /db_xref="taxon:1501433"
     Protein         1..237
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25855
     Region          38..232
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mtvnlapgln lerprtptvl alkevfqgld adscpgsynf hlhtvcsdgq lrpdelmesa
       61 iaiglkglai tdhhstngyf qaqiwlerwi lndsesklit pnlwtgieis anllnievhi
      121 lgyafepghs slqpylhgkt aigdaylaen vidaihqagg lavlahpcry rlspnklipe
      181 aasfgidgve tfyaygnpip wcpspqqtml vkelakdwgl fntcgtdthg vnllqkl
//
LOCUS       WP_007354391             271 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Kamptonema sp. PCC 6506].
ACCESSION   WP_007354391
VERSION     WP_007354391.1
KEYWORDS    RefSeq.
SOURCE      Kamptonema sp. PCC 6506
  ORGANISM  Kamptonema sp. PCC 6506
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae; Kamptonema.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Kamptonema sp. PCC 6506"
                     /db_xref="taxon:272129"
     Protein         1..271
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28713
     Region          8..229
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mskqpsenin asqinpdtgf ldpanirlis tppidpaddp lfdpnffnlt ndedvvslap
       61 rilrstpggl ialagndfvk gsdepeling nagedtlvgs ggddtlrggi dfdqlyggsg
      121 ndilngnked dyiignegnd vlrggkgndn lvgeedndtl igdggidklw ggagedifvl
      181 skdsavpnqe vgslqprsnn dqfiidpvia dfildftpgs gdaigltggm tqddivvter
      241 fltigdrrdf dsrgpfsfgn pknfgfsirk y
//
LOCUS       WP_007355485             338 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Kamptonema].
ACCESSION   WP_007355485
VERSION     WP_007355485.1
KEYWORDS    RefSeq.
SOURCE      Kamptonema
  ORGANISM  Kamptonema
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Kamptonema"
                     /db_xref="taxon:1501433"
     Protein         1..338
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37744
     Region          1..333
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mgilvedvsk hfgsfqalsq vnleiktgsl vallgpsgsg kstllrliag leppdigkiw
       61 itgkdatyqs vqerqigfvf qhyalfkhlt irdnigfgmd irkspksrtr krveelldlv
      121 qlsglgdryp sqlsggqrqr valaralave pqvllldepf galdakvrke lrdwlrrlhh
      181 evnvttvfvt hdqeeameva deivvmnkgr veqvgtpaqi ydspatafvm sfigpvnvls
      241 stagifarqs leapspqiyl rphdvliqte peasfapaki nrivylgwei qielivdeqe
      301 iitayldrdr fkqlnvqvnq rvyvkprqak afpvelvv
//
LOCUS       WP_007355657             646 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Kamptonema].
ACCESSION   WP_007355657
VERSION     WP_007355657.1
KEYWORDS    RefSeq.
SOURCE      Kamptonema
  ORGANISM  Kamptonema
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 646)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Kamptonema"
                     /db_xref="taxon:1501433"
     Protein         1..646
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=65702
     Region          <21..625
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
     Region          321..575
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mttlddnpnq ldlnlpglgp dtifagagad firtatlggs lifgqgdndt lialgpndtl
       61 yggddedslr tqrtpayiyg dggndtiiae aratlyggda ddfiqgtaea nlmfgnqgad
      121 imlggaqrrd slyggkgnds igfftgvgdg snnlgltlsg gvagfvgneg nnflrgdlgd
      181 dliaginqrd tlyggkgndt lrvvgsnsya sgdddndtlr vfnsletnff stspvtigle
      241 risliggagd dslyggigdf ragknfydgg dgndtivsfa fqdtvlggdg ndfitsstat
      301 gissqganis tpgyagnsll dggrgndtir aafstdtmig gegsdslsgv ftqasgadgd
      361 dtidaslaan fgpitldggl gndrlignrs atnffnggeg ndfivfastg dsligsfagn
      421 dtisyatnvs fgnittptvi sdflgnnlit ggngrdsitt gagndiligg pqgdlstdtl
      481 dggdgddsly gdfgndnlig gngndtligg pgadtltggs gndvfvyfnp feggtltaqv
      541 dgivdfvvgq drialsstgl pggagfgfpi sgvanrrpld reflvledvl atgtqaeana
      601 paqflvyenl sgnlyfdtng vsagglvpla nfnnrprise sdiilf
//
LOCUS       WP_007355759             462 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Kamptonema].
ACCESSION   WP_007355759
VERSION     WP_007355759.1
KEYWORDS    RefSeq.
SOURCE      Kamptonema
  ORGANISM  Kamptonema
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae.
REFERENCE   1  (residues 1 to 462)
  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 462)
  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 462)
  AUTHORS   ter Beek,J., 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 462)
  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 462)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Kamptonema"
                     /db_xref="taxon:1501433"
     Protein         1..462
                     /product="CmpA/NrtA family 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=50451
     Region          64..326
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mtkfsdqfsp lsrrkfiata gasalgsill kgclgnppep vadtsagggt atsvlavane
       61 krvegiettk itlgyipive aaaliiaqek gffakygmte vtiakqanwg sardnveigs
      121 agggidggqw qmpmpylisq glitkssvqi pmyvlaqlnt qgngiavslk hegkglglkl
      181 dqsahdyikd lakagtpfka aytfpkvnqd fwirywlaag nidpdtdvsl ltvppaqtva
      241 nmktgsmdgf stgdpwplri vkekigfmsa ltsqiwkghp eeylairsdw vdkhpkatea
      301 ilaglieaqq wcdkpehrae lvsivssknf fdvppevlip pysgkymmgd nqpeiddfkm
      361 gplywhdgig nvsypykshd lwfltesvrw gflptttltd rktiidkvnr ediwkkaakl
      421 agvaeadipt stsrgvekff dgkefnpdkp edylkslaik kv
//
LOCUS       WP_007356025             296 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Kamptonema sp. PCC 6506].
ACCESSION   WP_007356025
VERSION     WP_007356025.1
KEYWORDS    RefSeq.
SOURCE      Kamptonema sp. PCC 6506
  ORGANISM  Kamptonema sp. PCC 6506
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae; Kamptonema.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Kamptonema sp. PCC 6506"
                     /db_xref="taxon:272129"
     Protein         1..296
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30484
     Region          9..255
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mrpdlnkpna vdniiysnnt snntnsiqfg tlendafhgr dsgnifhakl gndnlyggns
       61 kdilngnegs dfidgskgnd filggknndi llggegqdsi lgnrgqdsin ggekndling
      121 nqgddfidgg kgndslfggk nndvligsrg edslwgnlgd dtlcgsqand ylsgngnndi
      181 idgcggndti yggkgndtll gcggddilyg dlgndtligd sgndvfvlgv gqgldiiadf
      241 tkgedllgls ggltfnqlni tqvesatlis nsiggevlal lsgvqasqig sfdfkl
//
LOCUS       WP_007356814             263 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Kamptonema].
ACCESSION   WP_007356814
VERSION     WP_007356814.1
KEYWORDS    RefSeq.
SOURCE      Kamptonema
  ORGANISM  Kamptonema
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Kamptonema"
                     /db_xref="taxon:1501433"
     Protein         1..263
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25857
     Region          32..228
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mpgavpsqpi rptptpspgg ngsggntgtl pgggniirgt sepdslrgtg sgdqifglas
       61 fdtlyglggd dtlsgdtgdd svlgeggndi lfggsdrdsl fgddgddtif ggkgndsasg
      121 gvgnnqlfgn tgndtliggl dddslfggtd ddsliggagd dllsgdrgrd tltggegsdt
      181 fvigrltggl teadadvitd ftdgadrirl sagltfgdlt ivqgggtaps tviqlingnd
      241 vqflavlpgv arnsisssdf ttl
//
LOCUS       WP_007357563             159 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Kamptonema sp. PCC 6506].
ACCESSION   WP_007357563
VERSION     WP_007357563.1
KEYWORDS    RefSeq.
SOURCE      Kamptonema sp. PCC 6506
  ORGANISM  Kamptonema sp. PCC 6506
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae; Kamptonema.
REFERENCE   1  (residues 1 to 159)
  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 159)
  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   3  (residues 1 to 159)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Kamptonema sp. PCC 6506"
                     /db_xref="taxon:272129"
     Protein         1..159
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18218
     Region          17..120
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mtklynktse klkrqqlrre mtkaekllwe klksqqlenc kfrrqysvdk fvidfyspei
       61 klaievdgds hfqdgaieyd aerqtfiesv ginflrftnd evyhnlegvi eviagkiqll
      121 rrppnplgkg gvrrkgiaks rppnplgkgg vrrrgsnkg
//
LOCUS       WP_007364992             338 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Porphyromonas uenonis].
ACCESSION   WP_007364992
VERSION     WP_007364992.1
KEYWORDS    RefSeq.
SOURCE      Porphyromonas uenonis
  ORGANISM  Porphyromonas uenonis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Porphyromonadaceae; Porphyromonas.
REFERENCE   1  (residues 1 to 338)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Porphyromonas uenonis"
                     /db_xref="taxon:281920"
     Protein         1..338
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=38111
     Region          202..337
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mknimtflpl altlllacqp stdssaevtn mdsiiatdtv vadsqpeltv eqividrela
       61 fdkytledsy qyqketrtiq wnkireqllr ieqlqatphr wgvlqnyknl ngeapltkvw
      121 srdsyklvsd slgveryqav plyastdtlt pelygrdgtl iamtdtqgsn fwqgrtespe
      181 adwyvpkryv kllkpdvtfs hvvvvdrknq yiitlerqap ahylvrsinp attgrhkpph
      241 aketplgifl lqekkpkmfy tsdgssriag fapwasrftc gayihgvpvn npkgkiveys
      301 hslgttprsh mcvrnassha kfvydncptl atlivvie
//
LOCUS       WP_007367450             150 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Prevotella multiformis].
ACCESSION   WP_007367450
VERSION     WP_007367450.1
KEYWORDS    RefSeq.
SOURCE      Prevotella multiformis
  ORGANISM  Prevotella multiformis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Prevotella multiformis"
                     /db_xref="taxon:282402"
     Protein         1..150
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16432
     Region          2..150
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdflthflld ygywgmllsa flagsffpfs seavmlglla agldpvlllv ygsignvmgg
       61 mfnyglgrlg klewleryfh vkkasidray rfmgghgawm gffaflpilg saitivlglt
      121 ranlplsvls itigkvmrya vliwgadffl
//
LOCUS       WP_007370127             299 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Kosakonia].
ACCESSION   WP_007370127
VERSION     WP_007370127.1
KEYWORDS    RefSeq.
SOURCE      Kosakonia
  ORGANISM  Kosakonia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 299)
  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 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   3  (residues 1 to 299)
  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   4  (residues 1 to 299)
  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 299)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Kosakonia"
                     /db_xref="taxon:1330547"
     Protein         1..299
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33760
     Region          28..179
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          207..288
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkreeiclql tekikrlkin enrlaellpd irllygtqpg trtpvmyqpg ivflfsghki
       61 gyinervfry dtneyllltv plpfecetfa tpevplaglr lnvdilqlqe llmdigedey
      121 fhpgaaasgi nsavlseeil caaerlldvm ehpldarilg kqiiremlyh vltgprgeal
      181 lalvsrqthf slisrvlkri esqytenlsv dqlaaeanms vsafhhnfks vtstsplqyl
      241 ktfrlhkarm lmvhdgmkas aaairvgyes psqfsrefkr yfgltpgedv arirliqga
//
LOCUS       WP_007368741             224 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Prevotella multiformis].
ACCESSION   WP_007368741
VERSION     WP_007368741.1
KEYWORDS    RefSeq.
SOURCE      Prevotella multiformis
  ORGANISM  Prevotella multiformis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Prevotella multiformis"
                     /db_xref="taxon:282402"
     Protein         1..224
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25327
     Region          1..>27
                     /region_name="DUF2141"
                     /note="Uncharacterized protein conserved in bacteria
                     (DUF2141); cl01930"
                     /db_xref="CDD:470398"
     Region          136..211
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mrrlltiivf mltavaaada qgsvtvtqsa eidalvngkk pakktnkdrk kvesqrettr
       61 pavkpqetrq lavpklndhk peiarpdnst lqpreavrtk lvkrlvrrph vpapdemedt
      121 rlvtrrvrkg ikkvrgfrvq vfsggntria hqqadkagqk akelfpeqpv yvhfypprwm
      181 clvgnftsyd tarrvmrair kggyphanvi rtmvtiktsq fvdn
//
LOCUS       WP_007371200             315 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Kosakonia radicincitans].
ACCESSION   WP_007371200
VERSION     WP_007371200.1
KEYWORDS    RefSeq.
SOURCE      Kosakonia radicincitans
  ORGANISM  Kosakonia radicincitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Kosakonia.
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
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Kosakonia radicincitans"
                     /db_xref="taxon:283686"
     Protein         1..315
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=34876
     Region          1..309
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 miefknvskt fagqqavshl dlhvktgafs vligtsgsgk sttlkminrl iehdegaiyf
       61 agedirqlpv lelrrrmgya iqsiglfphw tvaqniatvl qlqkwsrgqr earvdelmal
      121 lgldvslrdr fphqlsggqq qrvgvarala adpevllmde pfgaldpvtr aalqqemvri
      181 hrllgrtivl vthdidealq ladhlvlmdk gkvvqqgtpl alltaphndf vreffgrsel
      241 gvrllslrqv kgylrrepvy egeplraemt lrealsafva qqceilpvhd dsgqpcgslh
      301 frdllrveas geasa
//
LOCUS       WP_007371356             202 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Kosakonia
            radicincitans].
ACCESSION   WP_007371356
VERSION     WP_007371356.1
KEYWORDS    RefSeq.
SOURCE      Kosakonia radicincitans
  ORGANISM  Kosakonia radicincitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Kosakonia.
REFERENCE   1  (residues 1 to 202)
  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 202)
  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   3  (residues 1 to 202)
  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   4  (residues 1 to 202)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 202)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 202)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Kosakonia radicincitans"
                     /db_xref="taxon:283686"
     Protein         1..202
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=23083
     Region          8..192
                     /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"
ORIGIN      
        1 msrknvqmrg lkvcvigcsd rdnhhlaqqf srigieglfc aafpdesqla eqqllvfdgd
       61 nstlfhptnl lpwpalpkia ltaietpsrl qwiaeqkids ymrkpvrfdg vmtaftlaln
      121 haahinqlea qlrrqeerlr arkflfsaql rvmhalrlee ddaysllrra smaqhmtien
      181 lscellndte swlnrlksll ae
//
LOCUS       WP_007373357             373 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Kosakonia].
ACCESSION   WP_007373357
VERSION     WP_007373357.1
KEYWORDS    RefSeq.
SOURCE      Kosakonia
  ORGANISM  Kosakonia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 373)
  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 373)
  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
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 373)
  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   5  (residues 1 to 373)
  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   6  (residues 1 to 373)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 373)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 373)
  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 20682457
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Kosakonia"
                     /db_xref="taxon:1330547"
     Protein         1..373
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39866
     Region          9..49
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          75..360
                     /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 miapnvtari lrlivenapi sqsdlkvrsg lsmstvsqat nrlltggivq elglrrvsmg
       61 rpktllglnp dhasvigiql naernlivlt dlggniigeq qmpsgamtpk qlgdalakfl
      121 rgvenrkvga iglalsglvd asngycvrsr vldwdnvpia rlleerfslp vfiendanal
      181 amaalvfgql ghaqsaiiat fgkgigagil ldrqlyrgrh gkageignal lgdgserlle
      241 dvassqailr rvaatlkdev pqalrdldmr ptqevlsala eaghqlgisl anlsvaydpd
      301 vvylamepqm asrilldnit qsfqtyrlkl tphmtplqfi tesnrmwaqg aagfavnkll
      361 dllaaqadee ias
//
LOCUS       WP_007373555             103 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Kosakonia].
ACCESSION   WP_007373555
VERSION     WP_007373555.1
KEYWORDS    RefSeq.
SOURCE      Kosakonia
  ORGANISM  Kosakonia
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Kosakonia"
                     /db_xref="taxon:1330547"
     Protein         1..103
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11296
     Region          4..101
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(7..8,26..27,35,38,40..41,43,46..47,49,57,62,69)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(26,57..58,60,84)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mdiqdsfpqr vwqivaaipe gyvttygdva klagspraar qvggvlkrlp egstlpwhrv
       61 vnrhgcislt gpdlqrqrqa llaegvvvsg sgqidlqryr wiy
//
LOCUS       WP_007374104             275 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Kosakonia radicincitans].
ACCESSION   WP_007374104
VERSION     WP_007374104.1
KEYWORDS    RefSeq.
SOURCE      Kosakonia radicincitans
  ORGANISM  Kosakonia radicincitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Kosakonia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Kosakonia radicincitans"
                     /db_xref="taxon:283686"
     Protein         1..275
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=30387
     Region          42..188
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkkyalamla lllagcasek giidkngyql dtrrqaqaay prikvlvihy taddfdvsla
       61 tltdkqvsah ylvparpply hgkpriwqlv peqdlawhag vsfwrgatri ndtsigiele
      121 nrgwqrsegg ktfapfapeq isaliplvkd iisryniapq nvvahadiap qrkddpgplf
      181 pwqalaaqgi gawpdaarva fylngrsphq pvetaslldl larygyevkp emtsaqqkrv
      241 ieafqmhfrp glwhgvadae sqaiaealle kygqg
//
LOCUS       WP_007374850             865 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [Kosakonia].
ACCESSION   WP_007374850
VERSION     WP_007374850.1
KEYWORDS    RefSeq.
SOURCE      Kosakonia
  ORGANISM  Kosakonia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 865)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 865)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 865)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..865
                     /organism="Kosakonia"
                     /db_xref="taxon:1330547"
     Protein         1..865
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=94246
     Region          66..115
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          93..864
                     /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 masknyhswl mlavlggnla gtsstlaqqs spagdnarqv qrynfsipgg gslaeallaf
       61 gqqsglqliv pseltnglss agfsgnysad dalrtllsgt plsfkyvntn tiqiystaqa
      121 stdgtevlgt vqvdgaldqg sdikgvngst ditategsgs lnggmltvgs kgatsvkdtp
      181 qsvsvitset mqqqgirtln damqkgtgit vqqgnnsrek nfysrgfqit rasidggspi
      241 ditggtnynn rfspsfdmsm ydhveilrga ddlfngfstt gpggtvnlvr krpldhfqlk
      301 ydgsagswdn yqnsldltsp lndagtlrar avltrkdshh fyrtakdent vaygtleadl
      361 tsstlltigg syqrirgvpl tnglelypdg rdphfsrkta wvfpweksds dtreifakla
      421 qkigdrwnfn lnytglyqrn stiysnvagn impdtglfsa episadgsns nnkqfsfdst
      481 ltgefdvfgl pqkltfggny skenywmtsp daasmvngwf gttgpimdpw hwdtsvpeps
      541 ipagyyayms sgssvnwgmy sqlvltpwkp lhfglglrln ayksnthtst asdqsdises
      601 trkwespyys vsydinddls wygsytkifi pqsnmiapsg qqidpetgsn letglkyaqp
      661 ggllnaslsl yqirlvnqgq ligadsvnlg ggrtgyyrna pdaniskgvd leitgtvqpw
      721 wqtslgytyn fnktsdlssd glndsittft pkhtikwwnd fqfnnagetl skfsfgvgvq
      781 aqsktkqigs wydddfnqhn ynantafyav ysarigyain rnwsvallgn nlfdktyyst
      841 vgnlhggywy gdprnfvlsi sgtfd
//
LOCUS       WP_007375721             152 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_007375721
VERSION     WP_007375721.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..152
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16025
     Region          1..152
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mqkydfyqsl vkqtesliag esnvianlan isallftsle dvnwagfyfm dsptelvlgp
       61 fqgnpaciri pvgkgvcgta aataetqlve dvhafdghia cdaasnseiv vpilkngkvf
      121 avldidspsv grfdtddkag lealvkclea sl
//
LOCUS       WP_007376340             103 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Pseudoalteromonas].
ACCESSION   WP_007376340
VERSION     WP_007376340.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..103
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11437
     Region          11..103
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(26,57..58,60,86)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(26..27,35,38,40..41,43,46..47,49,57,62,68)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mnadidketl iytviagipi gkvasygqva alagypqnsr lvgrllkmmp ndsvipwhrv
       61 vnsqgkisfp agsekyqeqr ekllsegvlf ksdkvnmrec rwe
//
LOCUS       WP_007376788             374 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Pseudoalteromonas].
ACCESSION   WP_007376788
VERSION     WP_007376788.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 374)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..374
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=42057
     Region          288..368
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mlftslpmqy lhaigtfqgi llaamllfsa gvnntgrimg vwclfqafyf csplivvhae
       61 dtvfanligw gyfvpasfga flylyfrsai ikksfhlkdg ihatplllcl llnidflfst
      121 ptekiniann afhkeniqll tqiimfvqaf fylalsvkli tksgrhardt lsnfnpkift
      181 llwivlnlya gmllteavst iiganstlai asdliaftli ysvsmaqwre pnlfvidnlg
      241 etpaealnst tkaqcfdsnt rakllenivq ymeeeqpyle seltldalar ytnlsshhls
      301 eilnqqankn fyqfvneyri ktvcsqissn pkerlidlal sagfsskstf navfkqfkgm
      361 tpsqyrkqlk ldse
//
LOCUS       WP_007376406             695 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Pseudoalteromonas].
ACCESSION   WP_007376406
VERSION     WP_007376406.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 695)
  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   3  (residues 1 to 695)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..695
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=77074
     Region          20..683
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msidlsqffe vffeesfegl dtmeaellnl vpgeedleti ntifraahsi kggsgtfgfs
       61 svadfthvle tlldqirqge relstehvnl llkavdclrg llaalqadqa sdlteanalr
      121 mqfehvlekk dnvleskpqn eavlstsnty qinfkphhhl fktgneplym iselaelgel
      181 kttvfydsvp ditelsydec flhwrfflnt shdekaikev fewveddaei tvelcvssfd
      241 deqpasisdh nhdlvlseqp eklekittlp akskpssnkd kkvasapest sirvgidkvd
      301 slinmvgelv itqamlnqls eqeitsttit slkeglaqla hntrdlqenv mrirmlpinf
      361 vfsrfprlvr diaqklnkkv elkligeqte ldktvmekis dpmvhllrns ldhgletvdq
      421 rvlagknpvg ivtlnafhqg gnivieimdd gqglntkkik ekaianelit adsnltdnei
      481 nelifmpgfs tmdevselsg rgvgmdvvkr niqslngsve vtsapgigst ftirlpltla
      541 ildgqlvkva qhtyiiplis iveslqidit kvsrvgkdld vlrlrdeyip ilrlyaifnh
      601 qnaiesldkt llvvvetdnq kvgllvddll sqqqvviksl eanyhkvdgv sgatilgdgr
      661 vslivdisgl iklsglkkpg sqeltietqa tleal
//
LOCUS       WP_007379058             646 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_007379058
VERSION     WP_007379058.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 646)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..646
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=72808
     Region          <220..643
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 magfkklifi qiiswllcva agsyfisvsf dnavseaqkn aqasvtnyin dlsfddnlvq
       61 nlkksladgk tfssftlrdy qgaevfnvns lidlplfadf iqsifnsarp qfavnkaadi
      121 kveftvniqh laeqlqislf iiifisavlv iipiilmqsi fnhlnksism tvsdvidvyi
      181 nqnqagelet vldssklksl gkdlvpsfnr lshflktkne yiqsealnik heaykdvita
      241 lgnrnmfvey yeknienseq stfgslamir cselqainqs rgyqkgdeyv kgvadiikhi
      301 sgtyagsqlf rlnssdfavv lphiplkeae rfgenlqsrf tqyqqnqels svantgivgy
      361 ekgkplgell svvdnamsma qskqinawhv qresdlvnnv sagfgnqnwr kvineviesk
      421 rvhlvmqnim plgksikaya eiqvrfkted nqvlptasfl amaeklgmav didkliidss
      481 lekvksrnls ekyfglnvta ssahndqfvi wlerrllkdt hiasklifev sefglqqnik
      541 askrfidmvh rvgarvtver fgvgltsfkf frdlkpdfik mdasytrgle ddknnqyfmr
      601 lmvdlahrig vnvfaegves qeekhiietl cldgvqgyyi ekpkdi
//
LOCUS       WP_007379857             651 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Streptomyces].
ACCESSION   WP_007379857
VERSION     WP_007379857.1
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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..651
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=69886
     Region          262..429
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mrgsatdpnr atrrvvgtla gtalllpllg avpssaedss aglqrafata aaeyhvpqsv
       61 llgvsylqsr wdthagvpsv tggygpmhlt dartalasap hhsegtedar gdsarvallp
      121 dtkvpepagl parletlpka aeltglstre lrtdpaantq taaprcrrpa gaggeplsqd
      181 padwygavar fsgaddtata aayandvfdv lrtgeerttd agqqvaltgr pnlapdttql
      241 artglrklga gntecpktvs cewipapyee fgdndygnhd lgdrpasqsi kyivihdteg
      301 swegvlnlvq dptyvswnyt lrstdghiaq hvkakdvawh agnwyinaks iglehegfla
      361 rpdawyteam yrssarlvky lsakygipld rqhilghenv pgpttstvag mhtdpgpywd
      421 wrhyfellgh pfratapkqg glvtirpdya tnqpqytgcv tkgepcashg ssevrlysap
      481 dessalitdi glggrapttd vndlssrvst gqqyavagrd gdwtaiwylg qkawfrnpas
      541 dptavnaagl vvtpkeglds vpvygraype asayptgvpa qavsplpykv lkgqtyvigd
      601 rvpgeyyyav tfttdshkvv vgkdlyyeiq yghrvafvra advdvkpsvr r
//
LOCUS       WP_007380472             385 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Streptomyces].
ACCESSION   WP_007380472
VERSION     WP_007380472.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 385)
  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 385)
  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
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 385)
  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   5  (residues 1 to 385)
  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   6  (residues 1 to 385)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 385)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 385)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..385
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40641
     Region          20..71
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          84..368
                     /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 mgrltggdps llrrinsavv lhalratdca tlteitrvtg lsrptvegvv egliegglvv
       61 ekaadesvar rqgrparrfr fraeaghllg ldigphrvaa llsdldgrvl gavakdveet
      121 asaeerlerl rtavaellrr agvardslwa vgvaspgive adgtirlcaa lpewtglrlg
      181 erlsrsfkcp vlvendanaa avaehwkgsa tesddvvfvl aglspgagsl iggrlhrgyg
      241 gaageigalh llgrevtpet llsttdeplh pldeqavaev faqaregdqr araavdrflq
      301 rlvhdvaalv laldpelvvv ggwaagldgv leplrrelar yclrppkval silgeaavat
      361 galrlaldhv eeqlfavegt vtarr
//
LOCUS       WP_007380487             387 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: exonuclease SbcCD subunit D [Streptomyces].
ACCESSION   WP_007380487
VERSION     WP_007380487.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..387
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41441
     Region          1..270
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          266..357
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrllhtsdwh lgrafhrvsm lgaqaefigh lvttvrehav davvvsgdvy dravpplaav
       61 elfddalhrl adlgvptvmi sgnhdsarrl gvgagligra gihlrtepaa cgtpvvlsda
      121 hgdvafyglp ylepalvkde fgvrkaghea vlaaamdrvr adlatrapgt rsvvlahafv
      181 tggeasdser ditvggvaav pagvfdgvdy aalghlhgsq titervrysg splpysfses
      241 dhrksmwlvd ldaggavtae rvdcpvpral arirgtleql ladprlvpqe eawveatltd
      301 pvrpaepmar lcerfphtls lvfdperapd dpdvsyarrl agrgdqeiae dfvahvrgag
      361 pdereqavlr dafdavrade avrevar
//
LOCUS       WP_007381326             408 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Streptomyces].
ACCESSION   WP_007381326
VERSION     WP_007381326.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 408)
  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 408)
  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   3  (residues 1 to 408)
  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   4  (residues 1 to 408)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 408)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 408)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 408)
  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 10156937
            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="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42495
     Region          37..392
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(111..113,134..135,193,245,269)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mviltsvmat galtltacgs rddkgsdsdn gggttltigv daplsgenst tglgiqygaq
       61 iavddanknk lvpgvtfklk afddkaqpat gqsnattitg dktavgavgp lnsgvaqtmq
      121 qvfasanmvq ispsntnpel tqgknwqtdk krpyktyfrt attdelqgsf aadyaynglk
      181 kkkvfvvddk qtygaglaki fneqfkklgg kvvgtdhint gdkdfgslvt kiknakadll
      241 yyggqydess litkqlkgag vkiplfggdg mfastyieta gassegdlat avgvpadtlp
      301 aaktfietyk skgykgdyga ygaysydatt aiikavkaav dansgkvpsd inalrssvvd
      361 gvqksdfegi sgkvafdqyg dttnkqltvy qvtkgawkav ktgtadlg
//
LOCUS       WP_007382667             944 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: penicillin acylase family protein [Streptomyces].
ACCESSION   WP_007382667
VERSION     WP_007382667.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 944)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 944)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 944)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..944
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..944
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=103269
     Region          42..944
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mpptttassg qqpgksgrkk grrarlivlv lvlalvgava yggywsvstv rasfpqtkgs
       61 ieleglsgpv dvkrdsygip qiyassdadl fmaqgyvqaq drfyemdvrr hmtsgrlsem
      121 fgkgqvddde flrtlgwdrv akkeydtkls astkkylqay akgvnaylqg ksgkaisley
      181 aalgfrndyk pekwtpvdsv awlkamawdl rgnmqdeidr almtsrlgpk qiadlypqyp
      241 ysrnqaivqe gqyneltqtf eqngssqeng lsgtgtgtst ggtgtstsgs gtstggtatg
      301 tsastsssta salqsqlsgl ynvlddvpta vgvngqgigs nswvvdgsht itgkplland
      361 phlsaslpsv wyqmglhcrt vsskcqydvs gytfagmpgv vighnakiaw gmtnsgvdvt
      421 dlyleklsgd gylydgrtkp fttreetikv aggtskkivv retnngplls drydelvkvg
      481 kkatvdnaap drgdgygval rwtaldpgts mdavfamdra snwsefraaa alfdvpsqnl
      541 vyadsenigy tlpgripira kghtgaipap gwdpkyawtg kyikqdelpy eynpergyiv
      601 tanqavvdkd kypytlttdw gygtrsqrit dlieqkikgg gkistddmrq mqldnsseia
      661 kllvpkllki dvedkdvrqa qellegwdyt qdadsaaaay fnavwrnilk lafgnklpke
      721 lrvkgqclwv dpvntvgpad eadkvrecgq rdadqaqpdg gdrwfevvrk lmddensdww
      781 ktpkgvgdrp aatnrdelfk ramidarwel taklgkdidt wswgrlhrlf lknqtlgieg
      841 pgflqymlnr gpwklsggea tvnatgwnaa ggygvvwvps mrmvvnlgdl dkskwinltg
      901 asghaysahy tdqtgkwvkg elldwsfsde avdknttdsl vlkp
//
LOCUS       WP_007382978             294 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Streptomyces].
ACCESSION   WP_007382978
VERSION     WP_007382978.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 294)
  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 294)
  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 294)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 294)
  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   5  (residues 1 to 294)
  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 10164212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..294
                     /product="winged 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=33140
     Region          11..71
                     /region_name="WHTH_GntR"
                     /note="Winged helix-turn-helix (WHTH) DNA-binding domain
                     of the GntR family of transcriptional regulators; cd07377"
                     /db_xref="CDD:153418"
     Site            order(31,33..34,42..46,48..49,52,62..63,65..68)
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:153418"
ORIGIN      
        1 mseergkgpt ilatlrsris dgeyrpgynl ppqralaeef evsrdtiqrv lmelktegwi
       61 esrrgsgskv rvtlpihvpt qtkvppgria lgpfvdrafa qpvveldvft ftsesldthl
      121 rlqaekirng qipapvritl rillpsdate lpypraraat ksaldvteld rilqartrei
      181 irrhtsslrn alrnlktdgl vpdvevlvre vplvpthkly lrrgveglig pykivertil
      241 mdddteidaw dvlglgstli rlandegdpn atgsvfmqtw qewfdscwrr ydls
//
LOCUS       WP_007382980             292 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Streptomyces].
ACCESSION   WP_007382980
VERSION     WP_007382980.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 292)
  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 292)
  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 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 292)
  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   5  (residues 1 to 292)
  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 10164212
            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="winged 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=32188
     Region          19..71
                     /region_name="WHTH_GntR"
                     /note="Winged helix-turn-helix (WHTH) DNA-binding domain
                     of the GntR family of transcriptional regulators; cd07377"
                     /db_xref="CDD:153418"
ORIGIN      
        1 mvvtqenvav ngsrrlspqe iadtlrerir tgdlkagdrl ptqaelaeef gvergavrqa
       61 lralqedgll snvskgsppr iaeripvtdk pqptmvalap rlaeaftaph vridaaclta
      121 etlmvalgep lrlihegsis pesievrill psreitlafp vpveepedgn pvherwltqr
      181 naqghvlrhn lqslrsshgi dvnvtfralp ftppvklyll ngtealiayy mvtrreelsd
      241 sgpldmydvl gsasllfsfd kdagqrdaaf veqsqkwfna lwetittdlt ls
//
LOCUS       WP_007385706             266 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Streptomyces].
ACCESSION   WP_007385706
VERSION     WP_007385706.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 266)
  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 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 11454538
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28464
     Region          13..257
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          175..249
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mtnsvsgwap rtpdelrpwi agikalavee adprkpfvql pdpttkvivr segrgrptll
       61 vsgprvraay hagkrqvsct evrlapgavr pllgvpavdl vgrivplgal pgqaarqlay
      121 elgrlepeev varladvlpg llptavggtr tellraavaa lsvrsghipg hvrevarela
      181 vserqlrnlf segvglspkh yaridrvrav lahatelasa elaavtgyyd qshmtsdfrt
      241 lmgvpprsyf tgrlpaprac qvidsq
//
LOCUS       WP_007386069             381 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Streptomyces].
ACCESSION   WP_007386069
VERSION     WP_007386069.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 381)
  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 381)
  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
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 381)
  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   5  (residues 1 to 381)
  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   6  (residues 1 to 381)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 381)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 381)
  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 15726307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..381
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40238
     Region          19..>141
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          81..367
                     /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 mltagmnqsa vrrvntsvil ralavssgpr kltelagqtg lsrrtielil dslveagwva
       61 eldrvpnngc agrparryel raehallaav rittvdasav vadvrghilg rahrplrayk
      121 dprttlddaa alvlqaleda ggsvdrlrag avagggaidd egvvrrlvht trwegvhlpe
      181 elarrvpvpw fadndtnlga laerwrgvaa dhdnvvwaml gnrtglgili rgavhrgldg
      241 aageivears mpagsvedrp vaaltsplpa qralalarfe aarhgdaasl aevdefveni
      301 asilttlswt vapslivlgg gledaadvll prvrdalrda rtpavelrat alghdaplig
      361 avklaldrmd telfgplvpv d
//
LOCUS       WP_007387271             399 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: exonuclease SbcCD subunit D [Streptomyces].
ACCESSION   WP_007387271
VERSION     WP_007387271.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..399
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43604
     Region          1..281
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          275..365
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrflhtsdwh lgrrfhtedl ipaqrafldh lvgtartedv dailvagdiy draipsldav
       61 rlfnralhql adldvpiimi sgnhdsahrl gvgsgllara gihlrtdpdt cdipvlleda
      121 dgpvavygip ylepsmvrdr leaeavshra vltaaldrih adltnnqpag trsvvlahaf
      181 vtsgtgqpee rdeseestse reiavggvah vgadvfagid yvalghlhgp qrvtdrihys
      241 gsplaysfse arhtksvtlv dltpnavpal arqpcpvplr lervsgfmed lltnpdhepl
      301 kdawlevtlt dtalpfeama rlrrrfphta slkhkpalip aqatntptys qrirgrgdld
      361 iagdfinsmr gtdptpdeqn llqqaveasr lneqqketv
//
LOCUS       WP_007388477              94 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Streptomyces coelicoflavus].
ACCESSION   WP_007388477
VERSION     WP_007388477.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coelicoflavus
  ORGANISM  Streptomyces coelicoflavus
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Streptomyces coelicoflavus"
                     /db_xref="taxon:285562"
     Protein         1..94
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10159
     Region          3..94
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(3..4,22..23,31,32,34..35,37,40..41,49,54,59)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(22,49..50,52,74)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mtfvddvrea vrsipagava sygdvgeqvg vgarqvgram slldenvpww rvvyadgtpp
       61 schggrapvl lrdeatpmrg trvdmtrarh rwtp
//
LOCUS       WP_007390837             399 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Megasphaera lornae].
ACCESSION   WP_007390837
VERSION     WP_007390837.1
KEYWORDS    RefSeq.
SOURCE      Megasphaera lornae
  ORGANISM  Megasphaera lornae
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Megasphaera.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Megasphaera lornae"
                     /db_xref="taxon:1000568"
     Protein         1..399
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43299
     Region          1..396
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mivlvvncgs sslkyqlvdm kneevmakgl verigleegi lthkwqgkkk elkqpipdhn
       61 vavklvlesl tdkecgvias mdeidavghr vvhggekfac stlitdavmd alnecvdmap
      121 lhnppniigi nackaimpqv pqvgvfdtaf hqtmpakafm yglpyelyte dgirrygfhg
      181 tshryvaget arvmgvplek lriinchlgn gsslaaikyg ksidttmgft plpgvlmgtr
      241 cgdidpaivl hemerrhlsa kemdtlmnkk sgvlgisgvs sdfrdlgeaa akgnerakla
      301 ldmfhyqvrk aigalaaame gvdvitftag vgengiedra aicrglaylg akldeernnv
      361 rgkdalistd dstvkmyvip tneeimiard trdivsqik
//
LOCUS       WP_007389378             429 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces coelicoflavus].
ACCESSION   WP_007389378
VERSION     WP_007389378.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coelicoflavus
  ORGANISM  Streptomyces coelicoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 429)
  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 429)
  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
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 429)
  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   5  (residues 1 to 429)
  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   6  (residues 1 to 429)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 429)
  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 20170230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Streptomyces coelicoflavus"
                     /db_xref="taxon:285562"
     Protein         1..429
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45205
     Region          <20..>60
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          80..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 magrngrtvr dlrranrtav lqrlyfdgpl srfelgpatg lssgsvsnvv adlvadglve
       61 eagsvdsdgg rprtllrvap asghmigvdv getrvrvelf dltltelara erplaqqryd
      121 vdvivghird giaevlaaag lpaerllgag igvpgiveht adrgavvhgq tigwdavple
      181 arlragsplp dtvpylidng aktlgqaemw fgagrgarna vvvlfgsgvg aslvtpdveq
      241 gravewghlt vrvrgrrcrc galgcleaya gaesllarwr eeggrvpegt deetaltall
      301 aaahpsgdes adpvalavle etaeylgagl sdlinlfqpe riliggwagl qlgtrflpav
      361 rrhavsyalr hparkvtvdl grlgpdavtv gaailpladf farggrrpep apeypvpawr
      421 taleeraph
//
LOCUS       WP_007393763             435 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Psychrobacter sanguinis].
ACCESSION   WP_007393763
VERSION     WP_007393763.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter sanguinis
  ORGANISM  Psychrobacter sanguinis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 435)
  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 11465564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Psychrobacter sanguinis"
                     /db_xref="taxon:861445"
     Protein         1..435
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=47080
     Region          <168..219
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          309..433
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mtmnakpitt qitakfapkl laatvaatlf afsstamaet apkkptksvd slqqlikdkn
       61 teseqqrvaa ekaqqadvsg elasddaqdv aiqtqvnkei aeqtnddvgt gqavamsnsa
      121 tdddsiksie nkdgkvyktt nlsnyaravn savwtpnmrk ntamtvkmqa lldwnhaspg
      181 pidggwgmns tkalsnfqtm kglpstgkmd tatwnaltkn idpnqpvlvq ytltkedvnt
      241 nfqdtpsgse akskmkglyy qnikemlger fhmdvrylek lnkgksfteg etltvinvge
      301 plkekinrvi adkatktlya yngdklvaty pttvgststp spsgtfkivn kvkmpwykst
      361 vkngdksqvf mlppgpnnpv gvvwmglskp sygihgspvp egisrqasag cvrltnwdvl
      421 evyanvenga svelk
//
LOCUS       WP_007393795             668 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Psychrobacter sanguinis].
ACCESSION   WP_007393795
VERSION     WP_007393795.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter sanguinis
  ORGANISM  Psychrobacter sanguinis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 668)
  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 668)
  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 668)
  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 668)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Psychrobacter sanguinis"
                     /db_xref="taxon:861445"
     Protein         1..668
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=71398
     Region          10..660
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mtthqeehss eqvnkqilek ydresitrhl tqgpakyfia aicilyslfh lyitfnpmpa
       61 llqravhvgv gfgliflifp atkstsrskv awydwiwlll sisgvaylfy ayqdivtsrg
      121 gmanqvdiif siitvicvle gsrritgwil pilasiflly pfishlnfmp drlltrpydm
      181 gdifgqlflk teglystaig asvtfiflfi lfgaflarsg mgqlfndlal alaghkqggp
      241 akvavlssgf mgsingsals nvvstgafti plmkkvgyhk dfagaveasa svggqilppi
      301 mgasafimae ttgvkygtia laallpavly ylgviaqvhf ragrrdlkgi akeslprike
      361 vmkvrghmll pivflisllm knvpvgysaa ytiaftvvis mlraetrmsi ndilgaledg
      421 arqslavmaa cavvgiiigv vsltsfgtvm tsaivtlgag slfltliltm lasmvlgmgl
      481 psipayiita tmaapalagf dipilsahmf vfyfgifani tppvclaafa gagiaggdpm
      541 ktgfqslkla lagfivpfmf iynptmlmid ptglavtake fplppmidii vvvltsvtgi
      601 iglsaavegy fkglmnpvmr illaigalll iypevitdvi gglivvgiav lnikanksnk
      661 kplqvtni
//
LOCUS       WP_007395045             629 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Psychrobacter sanguinis].
ACCESSION   WP_007395045
VERSION     WP_007395045.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter sanguinis
  ORGANISM  Psychrobacter sanguinis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Psychrobacter sanguinis"
                     /db_xref="taxon:861445"
     Protein         1..629
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=72081
     Region          66..604
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mfkqdnlemh spnivddntl kiaeifphcv tearddngnl ryvvdfdllr qelsqslveg
       61 gqeryrldwp gkrqailean tpiaktlrpv reesvnfdtt enlfiegdnl ealkllqesy
      121 lgqvkmiyid ppyntgndfi yeddfaedts dflqrseqvd eegnrlvtnt esngrfhsdw
      181 ltmmysrlkl arnllkddgl ifiscdaneq anlkkigdei fgyqnfesdi hwrrrhnqpn
      241 dkskiiarvs enilvyakns iilkergtyy glplsekrva dyknpdndpk gdwttnpwka
      301 atgrggttye iitptgqvhk ntwygnkvtf erlidegrvh wtdngnglpr ikiylkdane
      361 qgqaavnffn htefgsnqdg skelaslfgd aglfsnpkpt klisslikia tkeddlildf
      421 fagsgttads tlqmniedsm rrkfiliqld estdeksqaf ktgystisdl skerirragq
      481 kilednkdkk giedldigfr vlkidstnmk evyytpdeys qdqlenfesh ikedrtsedl
      541 lfqvmldwgv plslpievke ikdhlvyyvg fnsliacfdt ltpelvneia kyeplkfvts
      601 eraishdqdk tniksrfaql spntdvrfi
//
LOCUS       WP_007395707             172 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Psychrobacter sanguinis].
ACCESSION   WP_007395707
VERSION     WP_007395707.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter sanguinis
  ORGANISM  Psychrobacter sanguinis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Psychrobacter sanguinis"
                     /db_xref="taxon:861445"
     Protein         1..172
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=19611
     Region          19..>85
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mwkiitinlg qqlnlnlarh csrnhqgftl velmmvvtit gllmvialps ythyvqtnyq
       61 lmaqqralfi anqlhhwrak nltyaefslt ehssgkqelk hlivltdatg khlltderan
      121 tqgwrilvkp npdfkklals diyyldslgr rcvfddsvmv pdiasiefcp ks
//
LOCUS       WP_007403853             241 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Sphingomonas].
ACCESSION   WP_007403853
VERSION     WP_007403853.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 241)
  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 10614777
            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="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=25888
     Region          74..238
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mlenldaapg rrallknalv lagalavpga vnarqrltar dlrplhqppl pnhptmpnpt
       61 evatrpafas prvvrsplfr eamaalqkhg srvrqrdrma ivdfaagsse prlhlvdlis
      121 gksqsllvah gsgsdpshsg ylqrfsnafn snassegafl tdnyyvgkhg rsqrligldp
      181 tnnnalgrai vihsawyanr dmisshgmlg rsqgcfavge ndldrvfanl gpgrmiyaak
      241 v
//
LOCUS       WP_007404285             260 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein [Sphingomonas].
ACCESSION   WP_007404285
VERSION     WP_007404285.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..260
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=24450
     Region          193..>245
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mtrtlfttaa lalaiaatpa saqllggsgg lggtlggslg gtlgsagaga ngtlsrsgag
       61 elrterqvdt rsgrvraggs asgeggtlid srspigggga etrgsggvsg avdaqligtd
      121 avrstargva rdiagrgrea iggarnavgs tagnvagsga gsangsgtlg ngmlalagsa
      181 aaqgagsvdv rpgmnvvdak graigtvral kseadgrvrd vlvqvgnrva tlpaanfsge
      241 gnvlvsamar savsreataq
//
LOCUS       WP_007405763             392 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TerD family protein [Sphingomonas].
ACCESSION   WP_007405763
VERSION     WP_007405763.1
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 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..392
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=41993
     Region          24..391
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mtelqqggnt pvtgsrmsvg fswaipsgrd veadasayll taggkvrgda dmvfynqpdg
       61 aagavrfgdr tgprggftvd laqlpveler ivfcvtihea qakgqtlall adaeisvtpa
      121 gggdtiryrp mlagateaam vlgelyrrgs qwkfravgqg fngglaplar sfgievaeda
      181 apppappppp pappvrlskv tldkpgqtvs lekkgnhfge ivvnlnwsrg rkaffggsta
      241 idldlgclfe ltngrkgvvq algrafggfd qapyialsgd drtgdvsqge tmringahws
      301 dlrrivvfan iydgvpnwqq tdgvvtvtmp dqppievrmt egrndrrlcg ivliendggr
      361 lkatriveyv rdqqvlderf dwglrwvags kd
//
LOCUS       WP_007405065             438 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Sphingomonas].
ACCESSION   WP_007405065
VERSION     WP_007405065.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 438)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..438
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=47714
     Region          <102..415
                     /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 mnddlsrfas gtaapvahdp qgladepfwq flilvaignf amlrrhvgre qsamlaeava
       61 arvaglfpea tvratsttqi eimmlapqra aldvnlallg talarpftva gqecgiepvl
      121 gaatatnphe ddirlleeae qaladahiec rsvvrdlvvr tdrldritla reltqaierd
      181 alfveyqpkv hvrqqrvcsi eallrwrhpv hgmispvefi pvaeesriia pltlwtirrv
      241 iadqrrlaar gheqrifini sgvllgdrdf vrqacalvtd sgasvgfeit etsvirdpes
      301 aianlqtfvd igialaiddy gaglsslsyl kqlpacelki dklfitqlts snrdplivrs
      361 tidlahalem evvaegvetp aalalltvmg cdmvqgylis rpigfdalcq fldeqthqav
      421 iaqaaplslg rfvarara
//
LOCUS       WP_007408475             340 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Bacillus].
ACCESSION   WP_007408475
VERSION     WP_007408475.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..340
                     /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=39102
     Region          2..272
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mtksrdsyfd nakfiliflv vfghilrsfi ngnefmlhly kfiytfhmpa filvsgyfak
       61 nfkrkgyvkk lavkliipyl ifqgiysvfy yliqdesmas vnpidpqwsl wflvslffwn
      121 lllypftklp kmwalgascg lavmigyldf isstlslsrt fvflpmflvg fylkkqhfdl
      181 lrakrgrqia agvlgivfll cwcidfdysw lfgsepystf gtvsllsgls rigwyvlafa
      241 atfsflalvp qkryfftkwg trtfyvyllh gfiiktlrqi gledhlsdyq nlvmllilta
      301 altsilssna vktaaqpfie lritgwleav kgtrngaysk
//
LOCUS       WP_007408245             290 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Bacillus].
ACCESSION   WP_007408245
VERSION     WP_007408245.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 290)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 290)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..290
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32812
     Region          21..102
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..287
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mdslkrmnsa ltyieenltn didfkeaarl afcseyhfkr mfsfltgisl seyirrrrlt
       61 laafelkdss vkvidlaiky gyhspdsfar afqnlhgisp saakhnghsl kayprmtfql
      121 sikggnemny rieekkafri vgikkrvpil fkgvnpdias mwesldetai kqlkelsnva
      181 pvglisastn fsegrteeng eldhyigaat tkhcpnhlsq levpastwav feaagsfpda
      241 lqevwgriys ewfpsshyeq iegpeilwne hkdvtspsfk seiwipiskk
//
LOCUS       WP_007409515             295 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 5'-3' exonuclease [Bacillus].
ACCESSION   WP_007409515
VERSION     WP_007409515.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..295
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33041
     Region          1..289
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mnnklllvdg mallfrsffa tavhrnfmin engiptngvn gflkhlitav dtfqpthvvc
       61 cwdmgsktyr ndlfqdykan rsepplelip qfdlakeaar elgflnigik gyeaddcigt
      121 lsalfsgeae itivtgdkdl lqllnhqvqv allqkgigny kvytdeifre etgvppkali
      181 dikalmgdts dnypgvkgig ektayklire yqnidrlles lallpkgqqt kiqqslkele
      241 lsrqlaeihc evplactlee alfslkmeea almlrrhqik giermlekln areis
//
LOCUS       WP_007409672             521 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: M4 family metallopeptidase [Bacillus].
ACCESSION   WP_007409672
VERSION     WP_007409672.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 521)
  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 521)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..521
                     /product="M4 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=56672
     Region          48..520
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mglgkklsva vaasfmslti slpgvqaaen pqlkenltnf vpkhslvqse lpsvsdkaik
       61 qylkqngkvf kgnpserlkl idhttddlgy khfryvpvvn gvpvkdsqvi ihvdksnnvy
      121 aingelnnda saktanskkl sanqaldhaf kaigkspeav sngnvanknk aelkaaatkd
      181 gkyrlaydvt iryiepepan wevtvdaetg kvlkkqnkve haaatgtgtt lkgktvslni
      241 ssesgkyvmr dlskptgtqi itydlqnrqy nlpgtlvsst tnqfttssqr aavdahynlg
      301 kvydyfyqtf krnsydnkgg kivssvhygs kynnaawigd qmiygdgdgs ffsplsgsmd
      361 vtahemthgv tqetanlnye nqpgalnesf sdvfgyfndt edwdigedit vsqpalrsls
      421 tptkygqpdh yknyqnlpnt dagdyggvht nsgipnkaay ntitkigvkk aeqiyyralt
      481 vyltpssnfk dakaaliqsa rdlygsqdaa sveaawnavg l
//
LOCUS       WP_007413294             234 aa            linear   BCT 20-JAN-2025
DEFINITION  prolipoprotein diacylglyceryl transferase [Pedosphaera parvula].
ACCESSION   WP_007413294
VERSION     WP_007413294.1
KEYWORDS    RefSeq.
SOURCE      Pedosphaera parvula
  ORGANISM  Pedosphaera parvula
            Bacteria; Pseudomonadati; Verrucomicrobiota; Pedosphaerae;
            Pedosphaerales; Pedosphaeraceae; Pedosphaera.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002130
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Pedosphaera parvula"
                     /db_xref="taxon:1032527"
     Protein         1..234
                     /product="prolipoprotein diacylglyceryl transferase"
                     /EC_number="2.5.1.145"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008961 -
                     phosphatidylglycerol-prolipoprotein diacylglyceryl
                     transferase activity [Evidence IEA]"
                     /GO_process="GO:0009249 - protein lipoylation [Evidence
                     IEA]"
                     /GO_process="GO:0042158 - lipoprotein biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=25942
     Region          6..230
                     /region_name="Lgt"
                     /note="Prolipoprotein diacylglyceryltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0682"
                     /db_xref="CDD:440446"
ORIGIN      
        1 mrsspygwlm lagiivsicf wsrlakrddr llliyvsalv gaflgakivy vlaegwlhfg
       61 apdmwlqlat gktilgallg gylsveiakk lvgyhsatgd wfafiapigi ilgrigcffh
      121 gcctgvacka swctlkdahg vdrwpsvpme ilfnfaaivt ffllrrrqkl ngqhfhiylm
      181 aygifrfmhe fvreephilg pmsgyqiaal avfalgmmgf irrqhqpvpa vvss
//
LOCUS       WP_007415619             154 aa            linear   BCT 20-JAN-2025
DEFINITION  division/cell wall cluster transcriptional repressor MraZ
            [Pedosphaera parvula].
ACCESSION   WP_007415619
VERSION     WP_007415619.1
KEYWORDS    RefSeq.
SOURCE      Pedosphaera parvula
  ORGANISM  Pedosphaera parvula
            Bacteria; Pseudomonadati; Verrucomicrobiota; Pedosphaerae;
            Pedosphaerales; Pedosphaeraceae; Pedosphaera.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Chen,S., Jancrick,J., Yokota,H., Kim,R. and Kim,S.H.
  TITLE     Crystal structure of a protein associated with cell division from
            Mycoplasma pneumoniae (GI: 13508053): a novel fold with a conserved
            sequence motif
  JOURNAL   Proteins 55 (4), 785-791 (2004)
   PUBMED   15146477
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449500
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Pedosphaera parvula"
                     /db_xref="taxon:1032527"
     Protein         1..154
                     /product="division/cell wall cluster transcriptional
                     repressor MraZ"
                     /GO_function="GO:0000976 - transcription cis-regulatory
                     region 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=16910
     Region          16..152
                     /region_name="MraZ"
                     /note="DNA-binding transcriptional regulator and inhibitor
                     of RsmH methyltransferase activity [Translation, ribosomal
                     structure and biogenesis]; COG2001"
                     /db_xref="CDD:441604"
ORIGIN      
        1 mpgtetnevi yynslfhhgv dekrrvqipa kwrpsqpdve ftlilwpnga qpdaclmvlp
       61 paemaalaek irqmsfadpk asalrrllgs ksascsldkg gricipesma kavgidkeav
      121 mvglvdrfei wnperyetvs avdaallpea fkli
//
LOCUS       WP_007415834             295 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pedosphaera parvula].
ACCESSION   WP_007415834
VERSION     WP_007415834.1
KEYWORDS    RefSeq.
SOURCE      Pedosphaera parvula
  ORGANISM  Pedosphaera parvula
            Bacteria; Pseudomonadati; Verrucomicrobiota; Pedosphaerae;
            Pedosphaerales; Pedosphaeraceae; Pedosphaera.
REFERENCE   1  (residues 1 to 295)
  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 295)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 295)
  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   4  (residues 1 to 295)
  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 295)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Pedosphaera parvula"
                     /db_xref="taxon:1032527"
     Protein         1..295
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33297
     Region          58..295
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <191..295
                     /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 mktrekpegf vgqrlvvvpr pilaasiknp llqhllptda gyyptakghv cvrrkgcpev
       61 ifiycakgng wceiagrkhq isknqllvin aftphvygad knspwtihwf havgsnvsvy
      121 ldklgvteek pvvplggdvq lfslfeevle slehgftpth liyaahslth lmglilrhkd
      181 efgygetsvr ermansiefm kghlreplni vtlaalvnls rshystsfrr vtgyaplsyl
      241 nhlrmqravq llnatelsik eigdqlgfsd qfyfsrafrk vhnhspsehr rryas
//
LOCUS       WP_007417446             396 aa            linear   BCT 20-JAN-2025
DEFINITION  galactokinase [Pedosphaera parvula].
ACCESSION   WP_007417446
VERSION     WP_007417446.1
KEYWORDS    RefSeq.
SOURCE      Pedosphaera parvula
  ORGANISM  Pedosphaera parvula
            Bacteria; Pseudomonadati; Verrucomicrobiota; Pedosphaerae;
            Pedosphaerales; Pedosphaeraceae; Pedosphaera.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   McAuley,M., Kristiansson,H., Huang,M., Pey,A.L. and Timson,D.J.
  TITLE     Galactokinase promiscuity: a question of flexibility?
  JOURNAL   Biochem Soc Trans 44 (1), 116-122 (2016)
   PUBMED   26862196
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Holden,H.M., Thoden,J.B., Timson,D.J. and Reece,R.J.
  TITLE     Galactokinase: structure, function and role in type II galactosemia
  JOURNAL   Cell Mol Life Sci 61 (19-20), 2471-2484 (2004)
   PUBMED   15526155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Pedosphaera parvula"
                     /db_xref="taxon:1032527"
     Protein         1..396
                     /product="galactokinase"
                     /EC_number="2.7.1.6"
                     /GO_function="GO:0004335 - galactokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0005534 - galactose binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0046835 - carbohydrate phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=43235
     Region          3..395
                     /region_name="GalK"
                     /note="Galactokinase [Carbohydrate transport and
                     metabolism]; COG0153"
                     /db_xref="CDD:439923"
ORIGIN      
        1 mfevethfkr hfnappvhvv rapgrlellg nhtdyneglv mslavdkyie iaasprsdgk
       61 iqlvsssfpe keifsanefk knpavpwady vkgvlaqlyk rgvhftgfna vvhgtipmga
      121 gmsssaalsv ataliirklh pyalsetgla aapipdskgv vpvpthaekl hiakicraae
      181 hefvgvkvgl ldqisslfgk awhvmdidfr altvelspmp geaiivcnsg vkhslveggy
      241 nelrdncega arklgitslr sadakmldas kakltqreye cahhivteiq rvvfaeralr
      301 eddhqqfgqy mfqshessrd flknsvpeld llveiarkhp gclgarltgg gfggatinlv
      361 rhheaaafme ymareyekrg ghktqpilcq ivdgaa
//
LOCUS       WP_007415866             429 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Pedosphaera parvula].
ACCESSION   WP_007415866
VERSION     WP_007415866.1
KEYWORDS    RefSeq.
SOURCE      Pedosphaera parvula
  ORGANISM  Pedosphaera parvula
            Bacteria; Pseudomonadati; Verrucomicrobiota; Pedosphaerae;
            Pedosphaerales; Pedosphaeraceae; Pedosphaera.
REFERENCE   1  (residues 1 to 429)
  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 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   3  (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   4  (residues 1 to 429)
  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 429)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Pedosphaera parvula"
                     /db_xref="taxon:1032527"
     Protein         1..429
                     /product="CmpA/NrtA family 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=47303
     Region          49..302
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mktnpkqktt psprlsrrnf vgqtirglga vallgglprg wvgsvyadda pelksmkfgi
       61 ialtdcspiv iahekglfkk ygidsvvskg anwaairdsl stgdiqathm ltgmpiassm
      121 gllgspkkpm iipwimnrng qaitlkqewk gkvsddpkal lpfvekakkl geplsfamtf
      181 ppgthamwmr yylaagginp dkdvalitvp ppqmvanmki gkmdgfcvge pwnaravadk
      241 igftsiltqd iwkdhpekvc afaaefadkn pravkavlka lheasvwldk lenrpeqcei
      301 vskptyincn keiilgrlvg dvdygdgrkk kdanymiyss rncnypqpky avwwltqfrr
      361 wgmvsgapdy egvakqvmrh diyeeamkei gyahgglntd ketlfdgvtf dpakpeeyak
      421 gfsvcnlkg
//
LOCUS       WP_007417582             418 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Pedosphaera parvula].
ACCESSION   WP_007417582
VERSION     WP_007417582.1
KEYWORDS    RefSeq.
SOURCE      Pedosphaera parvula
  ORGANISM  Pedosphaera parvula
            Bacteria; Pseudomonadati; Verrucomicrobiota; Pedosphaerae;
            Pedosphaerales; Pedosphaeraceae; Pedosphaera.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Pedosphaera parvula"
                     /db_xref="taxon:1032527"
     Protein         1..418
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=46194
     Region          13..400
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mergkmtipr epdrvltina gssslkfalf egqdllarrl igkferigfs dalftatdlk
       61 tkrswekhma lkdhaaclpl lrevlgeadm lsvhvishri vhggmhlrep rvvteelire
      121 lrslrlfape hlpaeialls efsryypetp qvacfdtafh rdmprvsqll piprrydekg
      181 vrrygfhgls ysylmrelqr idreaargki ilahlgngas maavkegrgi dttmaftpaa
      241 glvmstrtgd ldpglmayfa raedmtatqf nemvnkqsgl lgvselssdi rdllaresnd
      301 vraaeaialf chqarkwiga lsaalggldt lifsggigen svvirkrice gleflgievd
      361 qranetnapi iskaearaiv rviptdeels laeaavevlg qrseagsfkp kikiegmv
//
LOCUS       WP_007420180             523 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Idiomarina sp. A28L].
ACCESSION   WP_007420180
VERSION     WP_007420180.1
KEYWORDS    RefSeq.
SOURCE      Idiomarina sp. A28L
  ORGANISM  Idiomarina sp. A28L
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Idiomarina.
REFERENCE   1  (residues 1 to 523)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Idiomarina sp. A28L"
                     /db_xref="taxon:1036674"
     Protein         1..523
                     /product="amidohydrolase family protein"
                     /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=57948
     Region          40..502
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mstsrimsvf amsfalvvva fsinstpvya eesvsegpfq riilrggtlv ngegappvgp
       61 vdiviegdri vrvdvvgypg vpilenrrpe arpgdreidi sghyvlpgfv dmhghtggsa
      121 pnippeyvyq lwlahgittv repgsfrgle wtveearkaa aheivaprvi pyagfgmgss
      181 epiisaeqat awveqaaekg aqgvkffgap prviaaaiqt anslglgtmm hhaqlnvvrt
      241 nvldsaamgl tsmehwyglp ealftdrviq dysadynyqn eqdrfseagr lwaqaakpgs
      301 erwnyvrdtl iemdftinpt ltiyeasrna saqrnaewha dytlptlerf ftpsryahgs
      361 ywfdwttdde iawrenyrlw maflndfknh ggrvttgsda gyiykiygfg yvqelellre
      421 agfnplevir aatlsgaeal gledeigsvi pgkkadlviv kenplrnfkv lygtghymln
      481 seneatrsqg vlytmrdgvl ydaqamlanv remvrqakae eqe
//
LOCUS       WP_007420334             453 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Idiomarina sp. A28L].
ACCESSION   WP_007420334
VERSION     WP_007420334.1
KEYWORDS    RefSeq.
SOURCE      Idiomarina sp. A28L
  ORGANISM  Idiomarina sp. A28L
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Idiomarina.
REFERENCE   1  (residues 1 to 453)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Idiomarina sp. A28L"
                     /db_xref="taxon:1036674"
     Protein         1..453
                     /product="amidohydrolase family protein"
                     /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=50507
     Region          16..445
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mvrsiifcvl iacawpvqae kialvggrli dgtvaepllr svvliengvi qqvgtvdtlq
       61 vpegyreinm gghdllpglw enhahlmlvg hadyphwnat ysdrfeseim paaalqllla
      121 gvtstrdlga plaasknvke airsgripgp hlyttgpflq hevaewqrdy rwevrtvaea
      181 qgrvrqlhea gmemvklidh ddmerevaqa ivdeahrlgm kvvghahkpd eirvgldigi
      241 dnfehtgltt apgypqdild aliertatgi fdgllfwtpt veglwnytnt vqnptrlddp
      301 cweqglstdi iadirssitq paqlgymqlt plrrstlrnk iaqlketgvv mligtdsgip
      361 mkfhcqstwq emawwvevme fdametiraa tywpavmmgv qdrfgsvqeg kvadiiavrg
      421 dvlryinllq rvdfvmkegv vykqegqvqe sal
//
LOCUS       WP_007420245             137 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Idiomarina sp. A28L].
ACCESSION   WP_007420245
VERSION     WP_007420245.1
KEYWORDS    RefSeq.
SOURCE      Idiomarina sp. A28L
  ORGANISM  Idiomarina sp. A28L
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Idiomarina.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Idiomarina sp. A28L"
                     /db_xref="taxon:1036674"
     Protein         1..137
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=15089
     Region          21..100
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mnyekrdtmg iykedlsgpg phlmgadtli gndvynqkde nlgdikeiml dvtngnvsya
       61 vlsfgsflgm geklfavpws altldtenkr fvlnvdkesl kdapgfdkkh wpnmadkaws
      121 kdvdtyyass ssrvspg
//
LOCUS       WP_007420448             255 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Idiomarina sp. A28L].
ACCESSION   WP_007420448
VERSION     WP_007420448.1
KEYWORDS    RefSeq.
SOURCE      Idiomarina sp. A28L
  ORGANISM  Idiomarina sp. A28L
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Idiomarina.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 255)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Idiomarina sp. A28L"
                     /db_xref="taxon:1036674"
     Protein         1..255
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=28801
     Region          26..242
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mrtnfpkdme pvigcnrcav dlpfkftfaf qpivnvktkt mfgyealvrg cdgssawsil
       61 sqvnddnrym fdqacrvtai rlaaklelds ilsinflpna vyepahcirs tllaakeynf
      121 pieklmfeit eseqvhdavh ltkifkhyae qgfvtaiddf gaghaglnll ssfqprvmki
      181 dmelvrdvhe itvkqiivds lltmcmrlgi tplaegiekl eevnyfksrg velmqgfffa
      241 kpgfetlpev dyksf
//
LOCUS       WP_007421378             112 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein, partial [Acidiphilium sp. PM].
ACCESSION   WP_007421378
VERSION     WP_007421378.1
KEYWORDS    RefSeq.
SOURCE      Acidiphilium sp. PM
  ORGANISM  Acidiphilium sp. PM
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidiphilium.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Acidiphilium sp. PM"
                     /db_xref="taxon:1043206"
     Protein         <1..112
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
     Region          30..109
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 ttpataaaaa pnpqvgkamp tiipptqaas agphdiqlga lvsmakanea wqillarvpd
       61 llagrtpvvv pgtvngqtfy rlrlggfasa aaaaafcdrl ktrhvacyvp pk
//
LOCUS       WP_007421499             211 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase, partial [Acidiphilium sp. PM].
ACCESSION   WP_007421499
VERSION     WP_007421499.1
KEYWORDS    RefSeq.
SOURCE      Acidiphilium sp. PM
  ORGANISM  Acidiphilium sp. PM
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidiphilium.
REFERENCE   1  (residues 1 to 211)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Acidiphilium sp. PM"
                     /db_xref="taxon:1043206"
     Protein         <1..211
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
     Region          28..184
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(127,141,144,157..160,162)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 rarwrrrafa adwrrlarry papgdrdfiv vdiarerldl frdgryragw rvstsrfgvg
       61 qrrgsdrtpv gvfrvvgelg rggpadqvln aagptgrfak pvlapghlaa srlivgrill
      121 leglqpgwnq ggdvdtlard ifihgtanvg mlgrpasrgc vqmapgavir larmilpgal
      181 vmitrggggl rripgpstgp gnldfseiak k
//
LOCUS       WP_007422440             630 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Acidiphilium].
ACCESSION   WP_007422440
VERSION     WP_007422440.1
KEYWORDS    RefSeq.
SOURCE      Acidiphilium
  ORGANISM  Acidiphilium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 630)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 630)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 630)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 630)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 630)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Acidiphilium"
                     /db_xref="taxon:522"
     Protein         1..630
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68314
     Region          1..630
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msesatphgs pgeklrlagl igvlgvvygd igtsplyavq aslsyfpgnk lqesdvlgll
       61 slifwaliit vtikyvllim radnegeggt lslmalaqrv tqsdrtkwii giigicgagl
      121 ffgdatitpa isvlsavegm evvspglkef vlpiaiavil vlffvqrfgt arvggafgpi
      181 mviwfvviga lglhqifihp nvlralvpvy gaafimrhdl lafialgsvv lavtgaealy
      241 admghfgakp irvswlffvl pclllnyfgq galvirdpha asnpfffllp halvvpmvil
      301 atiatviasq avisgaysva rqstqlgllp rmpirytnet eqgqiyvppv nsflfvvvvl
      361 lvlgfgsssa lasaygiavt gtflstnala afvycrhfnw plrrtvlvfg aiglvdfaff
      421 ssnvlkvfdg gwvplaigfs litvmttwrr grallhqrwq qdslplasfl grlpqsrivr
      481 vpgvavfmtg npeytpssll hnlkhnkvlh etvvfvtvrn pgvpfvgdar rakveelseg
      541 vyrvllsfgf mespnipral dllreqglpf npmqisyflg retivaatvp klgfirraif
      601 lfmlrnaisa teffkipsdr vvelgvriai
//
LOCUS       WP_007423573             353 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Acidiphilium sp. PM].
ACCESSION   WP_007423573
VERSION     WP_007423573.1
KEYWORDS    RefSeq.
SOURCE      Acidiphilium sp. PM
  ORGANISM  Acidiphilium sp. PM
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidiphilium.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Acidiphilium sp. PM"
                     /db_xref="taxon:1043206"
     Protein         1..353
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36864
     Region          5..269
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mrssdpdiaa caarlrrgsv sfhaasrllp aevraaatal yafcreadda vdlaadkpag
       61 vaaisarlea icrgarlddp vdrafaatia rhgiphalpe alieglawda agrryatlae
      121 lrayaarvag svgvmmamlm gardeaslaa acdlglamql tniardvged aaerrlylpl
      181 dwldeaglep erflarpaft palaqvigrl leeaerryaa agrgiaalpl acrpgiaaar
      241 riyreigrll aangldsvst rtrvsgrrkl glaalslada ataglwapla aspppcpevr
      301 flidaaaasg getvgaaarv illidrlere eraarmraag arrplvcgaa epa
//
LOCUS       WP_007425574             167 aa            linear   BCT 20-JAN-2025
DEFINITION  division/cell wall cluster transcriptional repressor MraZ
            [Oceaniovalibus guishaninsula].
ACCESSION   WP_007425574
VERSION     WP_007425574.1
KEYWORDS    RefSeq.
SOURCE      Oceaniovalibus guishaninsula
  ORGANISM  Oceaniovalibus guishaninsula
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceaniovalibus.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Chen,S., Jancrick,J., Yokota,H., Kim,R. and Kim,S.H.
  TITLE     Crystal structure of a protein associated with cell division from
            Mycoplasma pneumoniae (GI: 13508053): a novel fold with a conserved
            sequence motif
  JOURNAL   Proteins 55 (4), 785-791 (2004)
   PUBMED   15146477
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449500
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Oceaniovalibus guishaninsula"
                     /db_xref="taxon:1046117"
     Protein         1..167
                     /product="division/cell wall cluster transcriptional
                     repressor MraZ"
                     /GO_function="GO:0000976 - transcription cis-regulatory
                     region 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=18794
     Region          5..156
                     /region_name="MraZ"
                     /note="DNA-binding transcriptional regulator and inhibitor
                     of RsmH methyltransferase activity [Translation, ribosomal
                     structure and biogenesis]; COG2001"
                     /db_xref="CDD:441604"
ORIGIN      
        1 mfgvfigehe nkidakgrls ipadfrrele dgdpkwepgk nasmllvygd hrrshvevmk
       61 itdmrdvytk itrmprgsik rrdmerlyfq qaltatvdet grivlsarvr dklgldgtam
      121 vvgngstfei wkpetyaand lsnlrdedgy dpdldpsvyl pgddgdv
//
LOCUS       WP_007425986             283 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Oceaniovalibus
            guishaninsula].
ACCESSION   WP_007425986
VERSION     WP_007425986.1
KEYWORDS    RefSeq.
SOURCE      Oceaniovalibus guishaninsula
  ORGANISM  Oceaniovalibus guishaninsula
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceaniovalibus.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Oceaniovalibus guishaninsula"
                     /db_xref="taxon:1046117"
     Protein         1..283
                     /product="formate/nitrite transporter family protein"
                     /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=29968
     Region          28..280
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msasdeakkn gsateseeee asvneagrlt arliyevvrr dgldemsrpv msltfsalaa
       61 giliafsvlg eavfrthlpe haawsglvqs lgysfgfvlv ilgrmqlfte ntistvlplm
      121 agpsrhyfic tarlwaivls cnvagcfvaa lfiaysggvs ddlvaavrai sehatsisgw
      181 tafaraipag vliaalvwml palphnglll ivmftwlisv gdfahvvags vemaflmvtg
      241 hlgvaegfvg fwlpvlagnf aggtavftli twaqvksevr dda
//
LOCUS       WP_007426061             190 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Oceaniovalibus
            guishaninsula].
ACCESSION   WP_007426061
VERSION     WP_007426061.1
KEYWORDS    RefSeq.
SOURCE      Oceaniovalibus guishaninsula
  ORGANISM  Oceaniovalibus guishaninsula
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceaniovalibus.
REFERENCE   1  (residues 1 to 190)
  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 190)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 190)
  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   4  (residues 1 to 190)
  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   5  (residues 1 to 190)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Oceaniovalibus guishaninsula"
                     /db_xref="taxon:1046117"
     Protein         1..190
                     /product="TRAP transporter small permease subunit"
                     /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=20791
     Region          13..171
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mnaiaaairi isginiavgr vfawlslgiv vvcftvvvqr yvfsvsylwm qdlyiwlnga
       61 mftavagfal qrddhvrvdi fyrpaslrwk amidlvgvcv fllpfvivvf vyalpfvers
      121 wglregssnv ggmpglfvlk sfvlvfavlv glqgvamalr silvlggrqd llpvrlryeg
      181 aahvpgedpa
//
LOCUS       WP_007426075             362 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Oceaniovalibus
            guishaninsula].
ACCESSION   WP_007426075
VERSION     WP_007426075.1
KEYWORDS    RefSeq.
SOURCE      Oceaniovalibus guishaninsula
  ORGANISM  Oceaniovalibus guishaninsula
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceaniovalibus.
REFERENCE   1  (residues 1 to 362)
  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 362)
  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 362)
  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 362)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Oceaniovalibus guishaninsula"
                     /db_xref="taxon:1046117"
     Protein         1..362
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39182
     Region          1..355
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mdrrsflttt aaagtglaal sapaiaqgnm twrmvttwpk nfpglgvgaq rmadritaas
       61 ggrltiqvys agelvpplqa ldavidgtae lshsaayywq nksqalnfft gvpygmttge
      121 lsawvrylgg qeiwdeiydq fgvkgfmsgn tgvqaggwfr deltgldsis glrfrtpglg
      181 gqvweklgat vtnmaageif qalqsgtlda aefvgpyndl algfyqvakn yyfpsfvepg
      241 latelvvdka kyldlpddlq aiirdvsqae ydqvtadfia ndpralqtlv ndhgvtvrqf
      301 pdeiieagan askelllgvr dssddltqrt atsfldalrl lrsrtqdadg afiearrkyl
      361 ei
//
LOCUS       WP_007426205             693 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Oceaniovalibus guishaninsula].
ACCESSION   WP_007426205
VERSION     WP_007426205.1
KEYWORDS    RefSeq.
SOURCE      Oceaniovalibus guishaninsula
  ORGANISM  Oceaniovalibus guishaninsula
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceaniovalibus.
REFERENCE   1  (residues 1 to 693)
  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 693)
  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 693)
  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 693)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..693
                     /organism="Oceaniovalibus guishaninsula"
                     /db_xref="taxon:1046117"
     Protein         1..693
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=74059
     Region          12..679
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 msteteraea lteeqmkele erydpevrfr pllpalgwlt atalfvlscy hfytagygip
       61 qatthrgthl aftlglvfls fvafgqrkep hntvltplgl plydwilail givsalyvpw
      121 vfndlafrvg nplpidvtmg tilivvllea trramgwplp viallfiaya yfgqsmpgvl
      181 ihpgaswtni vnhlyltsqg iygtalgvis tyvfhfvlfg vlatriglgq lfidlasala
      241 grfaggpakv svissamlgs isgssiantv ttgsltipam irigyprhfa aaveaasstg
      301 gqitppvmga vaflmieylg vplttiltaa lvpafmhffg vlvqvhlear rrglrgmtkd
      361 elpvawavfk agwlttlplf vlvsvllsgk tpylaafygi lscllvlviq nivrhdlrta
      421 itesvretwd gfvvgakysl svtvaaalvg viigvvtltg vgfkiaymvt glaggwaqdv
      481 svwlsvlpfe lisvtsltll ftlimtavvc vlmgcgiptt anylimiava apilgllgve
      541 plvahffvfy ygvladitpp valaayaaag iadanafkag ntafrlgmgk vlvpfvfvfs
      601 pslllvvpgf twtefflatl gamagitvls aaianwlfap lrvyervlla laslllvapd
      661 lyativgavl ilpalirqlp llgrsvrare emt
//
LOCUS       WP_007426787             273 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Oceaniovalibus guishaninsula].
ACCESSION   WP_007426787
VERSION     WP_007426787.1
KEYWORDS    RefSeq.
SOURCE      Oceaniovalibus guishaninsula
  ORGANISM  Oceaniovalibus guishaninsula
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceaniovalibus.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 273)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Oceaniovalibus guishaninsula"
                     /db_xref="taxon:1046117"
     Protein         1..273
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=30376
     Region          31..258
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mkdvsedpgt tdpvpfvsgq rddavlamve ravadhnvml afqpvvpagr hdrpafyegl
       61 irildargri ipakdfilqv eclelgrrid clslecglrv lrenprlrla inmsarsidh
      121 pgwlavledg lrddptiger lileitessa iqmpdavqaf mtrlqargis faiddfgsgy
      181 tsmrylkdlr fdilkidgqf irgiarsadn qalvkaivsi grhfdmvtia efvetaedak
      241 ylgqigvdcl qgyyfgapti rprwepcree rag
//
LOCUS       WP_007426929             152 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Oceaniovalibus guishaninsula].
ACCESSION   WP_007426929
VERSION     WP_007426929.1
KEYWORDS    RefSeq.
SOURCE      Oceaniovalibus guishaninsula
  ORGANISM  Oceaniovalibus guishaninsula
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceaniovalibus.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Oceaniovalibus guishaninsula"
                     /db_xref="taxon:1046117"
     Protein         1..152
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=15951
     Region          10..145
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mtqshwpata ariasltege tdaialmatl acelhhsdpr fdwtgfyrvv gpellkigpy
       61 qgghgcltip fsrgvcgaaa rtgevqivdd vdafpghiac aastrseivl pvrdaagtli
      121 avldidsdrp aaftqadaea lgailhmtfa hr
//
LOCUS       WP_007427708             353 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Oceaniovalibus
            guishaninsula].
ACCESSION   WP_007427708
VERSION     WP_007427708.1
KEYWORDS    RefSeq.
SOURCE      Oceaniovalibus guishaninsula
  ORGANISM  Oceaniovalibus guishaninsula
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceaniovalibus.
REFERENCE   1  (residues 1 to 353)
  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 353)
  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 353)
  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 353)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Oceaniovalibus guishaninsula"
                     /db_xref="taxon:1046117"
     Protein         1..353
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=37803
     Region          1..349
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkrrdfiavg agaaalplaa paiaqgnmqw klptafpkna pgvgtnvtnf adkvaamsng
       61 rltftvygag elvppfaved avqqgnaeag hgptyyaagk npalhwftav pfgmtsnehv
      121 awlehgggqd lwnevyaerd lvpfysgnsn tqsggwfknr vegldslqgl nmriaglgae
      181 iyrklgvnav lmpppeifqa mqsgaidaae wvgpmldqaf glqkitnlcy lpafnepgag
      241 lavvfnkdaw dslpadlqai cknaahaaal enhaqfdyyn alamadlkre gveflafpdd
      301 vvaamrdawa evqdeltaqs ddvarvresy daylaqardy aaamtlpmla grd
//
LOCUS       WP_007428897             290 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Paenibacillus sp. Aloe-11].
ACCESSION   WP_007428897
VERSION     WP_007428897.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. Aloe-11
  ORGANISM  Paenibacillus sp. Aloe-11
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 290)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 290)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Paenibacillus sp. Aloe-11"
                     /db_xref="taxon:1050222"
     Protein         1..290
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32938
     Region          21..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..287
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mdllksmnea ikyieenltn didfkevarl aycsefhfkr mfsflagatl seyirrrrlt
       61 laafelkdsn vkvidiaiky gynspdsfar afqnlhgltp searingrsl kayprmtfql
      121 sikggsemny rieekgafri vgiqkrvpii fngvnpeiaa mwesldgeti nnlkrlsnae
      181 pmgmlsastn fsegrmkekg eldhyigvat tkecpdsltq levaastwav fevigsfpda
      241 lqdvwgriys ewfpssnyeq iegpeilwne nkditspnfk seiwipilkk
//
LOCUS       WP_007429964             278 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Paenibacillus].
ACCESSION   WP_007429964
VERSION     WP_007429964.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 278)
  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 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   3  (residues 1 to 278)
  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   4  (residues 1 to 278)
  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 278)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..278
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31517
     Region          44..274
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <161..270
                     /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 miltphhlrf flttrehslp lfiesigfns rqedvsrpeg ypcfhwiqtv sgegiftfkg
       61 gtfrlgeqsg vlllpgesha yrratkvwrt lyitfdgpia aavltalglk htrgyhwdkd
      121 selhtfgegi lhslvserdl sgldasanmy rfltllrkyg qhssmpslsh nverlapvla
      181 fmeqnyaspd vglsdmavmm nvsarhlntl fkqafgvtsy aylivirlrk akemmteyph
      241 ltvkevserv gfrdashfva tfrraegitp erfkllyt
//
LOCUS       WP_007430339             107 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Paenibacillus].
ACCESSION   WP_007430339
VERSION     WP_007430339.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..107
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11992
     Region          1..101
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(4..5,23..24,32,35,37..38,40,43..44,46,54,59,67)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(23,54..55,57,82)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mqpftarvlq iillipegkv mtygqiaaea gsprgarqvv rilhslsqkh rlpwhrvvnr
       61 lgeialqedg saslqrlyle eegicfnang ripldqylyd pqaeiee
//
LOCUS       WP_007431256             394 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Paenibacillus sp. Aloe-11].
ACCESSION   WP_007431256
VERSION     WP_007431256.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. Aloe-11
  ORGANISM  Paenibacillus sp. Aloe-11
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Paenibacillus sp. Aloe-11"
                     /db_xref="taxon:1050222"
     Protein         1..394
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43294
     Region          1..277
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          274..363
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrilhtgdwh lgrtlegrsr lkeqeaflee lakmaddqqa dlimmagdvy dsvnpsaaae
       61 qlfyeasarl taggrplvvi agnhdqperv ssvtplvsgr gitllglpsg kavrvhtprt
      121 gemaciaalp ypsesrlnel lsedgdetvl reaysrrvgl lmaqlgtafq pdtvnlsmsh
      181 iyvlgglesd serpiqvgga ytvdpsalsi gaqytalghl hrpqyvkgdg lmrysgspla
      241 ysfseagqak svtlidvvag kpaqveelyi tsgrplvrwr arggleevyr wldegldmda
      301 fidleitlde amsmgdiqrl rksregiihi rplypemaaa qlehqrselp vhelfrafyq
      361 rqtggaqpdd glvqlflelv eqdnardhae eenv
//
LOCUS       WP_007431295             183 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Paenibacillus sp. Aloe-11].
ACCESSION   WP_007431295
VERSION     WP_007431295.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. Aloe-11
  ORGANISM  Paenibacillus sp. Aloe-11
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (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   2  (residues 1 to 183)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Paenibacillus sp. Aloe-11"
                     /db_xref="taxon:1050222"
     Protein         1..183
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19184
     Region          113..182
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkrvwtgtai tlaligsgli lfaggqrpep qeewtllnrk veqvlavese pkelqgksdd
       61 asgkraakan sdqterspag qaagtmkhnp vkgaaavqva vsenlatgna nsattsvsge
      121 kkvnintata aelmelpgvg akkaeaildy rnqhgpfqrv ndldhvkgig akmlakmkpy
      181 vsl
//
LOCUS       WP_007431611             344 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Paenibacillus].
ACCESSION   WP_007431611
VERSION     WP_007431611.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..344
                     /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=38694
     Region          11..278
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mttshdiqge sfflnlrfml iicvfagnal eplansfhia qqwfswifmf hmplfvlvtg
       61 yfakssltgp agrkvllqig mqylifqsly svldvalfhv prihhsffap ylllwflash
      121 icwrllmlal rgvppvlqlg isvllgilvg ylpvegiwls vcrtfvylpy fiagyhlnya
      181 dvhrfftapv riiagavsll lmvlagtsyf gipagwlygs mtygelghte wyagiyrigm
      241 ygvqfiasma flglvpaitg ritemgrrtl yvfllhgliv rtvvakgvye yidtpveiil
      301 ivvcaaglcc lltmpwvrma trplvepqvd wmlkpapypf rrsa
//
LOCUS       WP_007432921             383 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Paenibacillus
            sp. Aloe-11].
ACCESSION   WP_007432921
VERSION     WP_007432921.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. Aloe-11
  ORGANISM  Paenibacillus sp. Aloe-11
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 383)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 383)
  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 383)
  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 383)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Paenibacillus sp. Aloe-11"
                     /db_xref="taxon:1050222"
     Protein         1..383
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44646
     Region          4..90
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(23,42..43,60,63,71..72,82,87)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mirlqfdaeg ysvicgteqv illakefall rflydnrnqv ftreqlldhv wpleypvert
       61 vddhiyrlrk klkswntlri htvrgygysl tltdvqrpih pslydqevqd avhglfrkyq
      121 llgqgnsiva laaqqeqmgf elspfyqmyt rfvqadilwf leredfapkd rlywmlllyt
      181 gtagvtdegl tlceralssr llssdqerel rilnileayv engqperaqe glpltlmvme
      241 rddldkfvmp valmemymhl vanhmekaae lsdrlkgmls kapylrelgr yrmmrglmll
      301 rtgdvdnaer lidegldtld mgkqellkik avcqirgflk lcgiypmlee kyaaryerld
      361 rnngltlhrs alrrwleqtl sgv
//
LOCUS       WP_007431876             593 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Paenibacillus sp. Aloe-11].
ACCESSION   WP_007431876
VERSION     WP_007431876.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. Aloe-11
  ORGANISM  Paenibacillus sp. Aloe-11
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 593)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 593)
  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 593)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Paenibacillus sp. Aloe-11"
                     /db_xref="taxon:1050222"
     Protein         1..593
                     /product="M4 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=63672
     Region          35..593
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mkkvwvsllg gamllgsvas gasaaessvs gpaqltptfh aeqwkapssv sgddivwsyl
       61 nrqkktllgt dstsvrdqfr ivdrtsdksg vshyrlkqyv ngipvygaeq tihvgksgev
      121 tsylgavite dqqeeatqgt tpkisaseav htayqeaatr vqalptsddt iskdaeepgs
      181 vskdtyseaa nngktssvek dklslekaad lkdskieave aepnsiakia nlqpevdpka
      241 elyfyakgda lqlvyvtevn ilepaplrtr yiidandgki vsqydiinea tgtgkgvlgd
      301 tktfnttasg ssyqlrdttr gngivtytas nrqsipgtil tdadnvwndp agvdahayaa
      361 ktydyykekf nrnsidgrgl qlrstvhygn rynnafwngs qmtygdgdgt tfiafsgdpd
      421 vvghelthgv teytsnleyy gesgalneaf sdiigndiqr knwlvgddiy tpriagdalr
      481 smsnptlydq pdhysnlyrg ssdnggvhtn sgiinkayyl laqggtfhgv tvngigrdaa
      541 vqiyysaftn yltsssdfsn ardavvqaak dlygassaqa taaaksfdav gvn
//
LOCUS       WP_007433183             311 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Paenibacillus sp.
            Aloe-11].
ACCESSION   WP_007433183
VERSION     WP_007433183.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. Aloe-11
  ORGANISM  Paenibacillus sp. Aloe-11
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 311)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Paenibacillus sp. Aloe-11"
                     /db_xref="taxon:1050222"
     Protein         1..311
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35230
     Region          28..140
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          <101..294
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mdpllhslfr plqvngsdps atyiekkpsa alrayvacyw esgpaarvve gnltasceda
       61 tslswldeaa vdrvlpdgct dilleynpvt krqeisycgt fthpfvsarq tgaetrifav
      121 rffpggahyf hgmpihlftg gnyrleeiwp enveiigeri leardfderv rimdeylsql
      181 llqqrtsdcd lmknllhrif vsggsvgike laereaiser qlnrkfgqwi gispkkfsev
      241 vrfqsvlhti qsggsldwte lalkhgffdq ahlsrdfrrf ygdspltaak dfrrlsdfyn
      301 traepsiilk t
//
LOCUS       WP_007433379              79 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Cutibacterium modestum].
ACCESSION   WP_007433379
VERSION     WP_007433379.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium modestum
  ORGANISM  Cutibacterium modestum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 79)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 79)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 79)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 79)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Cutibacterium modestum"
                     /db_xref="taxon:2559073"
     Protein         1..79
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8164
     Region          1..79
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mlvhyyggta eatgtteeti elpidltvdq vlehlgklhs dlgrvlgvct lfvngfaarg
       61 dqtvpdgaqv dvlppfagg
//
LOCUS       WP_007433480             603 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Cutibacterium modestum].
ACCESSION   WP_007433480
VERSION     WP_007433480.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium modestum
  ORGANISM  Cutibacterium modestum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Cutibacterium modestum"
                     /db_xref="taxon:2559073"
     Protein         1..603
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=66559
     Region          10..>400
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mpilsrktin llilgesgdv lealtrvpel aekyvgkvkl iyidppfnta qtfasyednl
       61 ehsvwltmmr drllhmkkll ssggsiwvhl dyaenhkmrv sldevfggen fvaeivwqka
      121 dsgrndatyf stdqdvllvy rksalfelnr lprpdamnsr fanpdhdprg pwamadpcap
      181 dapnnqpmvy aiqhpmtgel mypaqsscwr lapsvmfeem skwaryelrd tgdrvkraev
      241 sgvpveaahd mvpaimlaep ldsarehsra vlepglplle lvfprgglgr imrksripsr
      301 gmvprtlwpn sdvshsrgak kelvnlfpgv tafatpkper llqrvllist gagdlvldaf
      361 agsettaava qkmgrrwvtc elvedtferf tkarlakvvn dadpggvtrt kgeriaaedv
      421 elpegvsped aakftsvlnk liadepeakk dprvkalkaa akttrtkevm nwrggggfhv
      481 ahlspacfdy dpaldrvvst peatgqvlie svaanlgfpl lhpdddyife grrgntllkv
      541 iegvttvelv ddlvkelapg etlvlaatsv ldgvreylrk vrkgsrvvav pddvfgyqke
      601 tal
//
LOCUS       WP_007442198              94 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein
            [Brevundimonas].
ACCESSION   WP_007442198
VERSION     WP_007442198.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas
  ORGANISM  Brevundimonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae.
REFERENCE   1  (residues 1 to 94)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Brevundimonas"
                     /db_xref="taxon:41275"
     Protein         1..94
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10853
     Region          1..94
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mtraellekl relkpwleeq givnlrlfgs yardeagpds dvdllvdtsr pmgiefltte
       61 rllserletp vefcswevmr pyvrtkvekd lilv
//
LOCUS       WP_007442174             248 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Streptomyces
            coelicoflavus].
ACCESSION   WP_007442174
VERSION     WP_007442174.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coelicoflavus
  ORGANISM  Streptomyces coelicoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 248)
  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 248)
  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 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   4  (residues 1 to 248)
  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   5  (residues 1 to 248)
  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 10164212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Streptomyces coelicoflavus"
                     /db_xref="taxon:285562"
     Protein         1..248
                     /product="winged 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=26880
     Region          17..76
                     /region_name="WHTH_GntR"
                     /note="Winged helix-turn-helix (WHTH) DNA-binding domain
                     of the GntR family of transcriptional regulators; cd07377"
                     /db_xref="CDD:153418"
     Site            order(17,19,42,44..45,53..57,59..60,63,73..74,76)
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:153418"
ORIGIN      
        1 marttphvqs tpdtrpplyr rvadqllael rdgiappger lpgerrlaeh fgvsretvrq
       61 aldvlrrdgl lstdrrgshv alpgvpagsp aplvfpvgar aaeprtgdra tvvwappppe
      121 haaalglvpg ratlvhryts saaggngrrt avtsfsaval aeveelaryr dradgvacaq
      181 lrraydwmrr aglalhhrdt itlqpdtasv rvvrrvhdqy arpleitdll vdtrqdalvy
      241 eftlpaag
//
LOCUS       WP_007444795             237 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Streptomyces coelicoflavus].
ACCESSION   WP_007444795
VERSION     WP_007444795.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coelicoflavus
  ORGANISM  Streptomyces coelicoflavus
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Streptomyces coelicoflavus"
                     /db_xref="taxon:285562"
     Protein         1..237
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=25565
     Region          85..225
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mgakqgsagg sasggsgdgd rrigrraliv ggaaaavgtg vlardelsrl wwrmpgverp
       61 redgvvdyag arwvaasdan wrradrpddf gidmvivhvt qgsfdsavra fqdpghkaaa
      121 hyivgqdgri tqmireldva yhagnrdyne rsvgiehegf vdrprdftda myaasarlta
      181 gicarygipv drkhilghve vpgtdhtdpg phwdwdrylk lvrraatsap skpptka
//
LOCUS       WP_007445237             324 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Streptomyces
            coelicoflavus].
ACCESSION   WP_007445237
VERSION     WP_007445237.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coelicoflavus
  ORGANISM  Streptomyces coelicoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 324)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Streptomyces coelicoflavus"
                     /db_xref="taxon:285562"
     Protein         1..324
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34960
     Region          13..313
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mtapvttlea vesftpertv pisgladrlg lrrtklrlfe rvhglkeirf dpeldlfdvv
       61 lpaarritad ppvreriryv vyahttqava pahidpaqei karlgladae afalsqqnca
      121 ggmaavdtaa ellrsegwpg ehalvitgeq afspkiqlip dvaimgdaga aclvtldggg
      181 drvrsyatrt lgqfsaamll deekslevsk fyapvlaevv reavaragmt lpdidliiph
      241 nvnlqswrqt igelgidrsq vfldnverys hcfasdvfln yttlrdagrl tagrnylfat
      301 vglgatfaam vithqhtgqg ggpa
//
LOCUS       WP_007449076             243 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Streptomyces].
ACCESSION   WP_007449076
VERSION     WP_007449076.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            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="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26706
     Region          18..238
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mtmetvqadp sapggpalfd tmstmramrr lkpdavpdet veqliqaavw gpsggnmqcy
       61 eyvvvtdrev marlaplwkr cvdaylattg kyapegmdea aygrmvaaie yqrdhfadtp
      121 vlivpcyrfp eprldeegla asaralgpag tehmmntqtr fqalaegscv ypgvqnllla
      181 arglglaani tiwhlmleqe wkrelgiped matfaavpvg wpagnfgpvr rrpvadvihr
      241 drw
//
LOCUS       WP_007451695             261 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Streptomyces].
ACCESSION   WP_007451695
VERSION     WP_007451695.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..261
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26601
     Region          <108..259
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mnrhrltara avvallatgl aaspavaapt gtststgaka rvgadwakqs itftagagqv
       61 ndlhvvpmdr gdgvrrigfr dsvplqpgdh ctyltpgdet yvvcelptds srpdridvfl
      121 gdgddeiats dpgvatvsgg pgddmlhaht ahtvrgdagn dmvmgrvvld ggdgmdhlma
      181 vdgdqllwgg rgddmieaye gddvvyggpg ddhimggdgd dilfggsgdd mvhgeggddl
      241 vvggpgkdsv dggpgrnivl r
//
LOCUS       WP_007451930             681 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: M4 family metallopeptidase [Streptomyces].
ACCESSION   WP_007451930
VERSION     WP_007451930.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 681)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 681)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 681)
  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 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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..681
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..681
                     /product="M4 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=69983
     Region          82..667
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mrstpsrrat atgaliaaaa liavaipsga atatsapssa plggitagtk adpgalpakl
       61 spaqraells eanatkaata kelglgstek lvvrdvaqdr dgtthtryer tlgglpvlgg
      121 dlvvkaspag ategvskask atsaqlkavg ltadlapaaa ekqalgaaka egskakkase
      181 aprkvvwlgs gspqlayetv vgglqhdgtp nelhvvtdaa sgeklyewqa vhngtgntqy
      241 ngqvtlgtap sytltdttrg nhktynlnrg ssgtgtlfsg pddiwgdgtp qnaetagada
      301 hygaaetwdy yknvhgrsgi rgdgvgaysr vhygnnyvna fwqdscfcmt ygdgsgnvkp
      361 ltsldvaahe mthgltsvta klvysgesgg lneatsdifa agvefysnta qdpgdymvge
      421 kidingdgtp lrymdkpskd gaskdawysg ignvdvhyss gpanhwfyll segsgaktvn
      481 gvnydsptsd glpvtgigrd kalqiwfkal ttkftsttny aaartgtlav aselygatsp
      541 eyaavahawa ginvgarpgg gnpdpggkvf enttavtipd agaavtssvt vagvtgnaps
      601 tlkadvnith twrgdlvvdl vapdgtayrl knsssgdsad nvvetytvna ssevangvwk
      661 lkvqdiarqd tgrinsfklt f
//
LOCUS       WP_007452722             579 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Streptomyces sp.
            W007].
ACCESSION   WP_007452722
VERSION     WP_007452722.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. W007
  ORGANISM  Streptomyces sp. W007
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 579)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 579)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Streptomyces sp. W007"
                     /db_xref="taxon:1055352"
     Protein         1..579
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=60099
     Region          3..561
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mmlhpellra ahtarrplgl atallaavta thlaqavlla lvlariarge taalapllsa
       61 viavvlvrag lgraqrltav tagatvrirl rdtllerlgv lgptaitgar agavratlvd
      121 gvegvdayvs rylpqalitc avpplllvav alvepyaalv lgpalllall gprwwdrlla
      181 rrgkehwdsy ealaadylea lqgmptlrat gavgrvrerl eqrsaalhrt tvaklrvslv
      241 dtgltdlavq ggtaaavlva cssaatgrta atgtylllll asecfrpvrd lsrewhagyl
      301 gvsaadgitg lrtaeaavpd rgtvaadwas apeirfedvh fthpgsgrpa ldgvsftaaa
      361 grttavvgps gagkstllsl llrqrdpdrg sltvagtata aytlaslrrg iavvsqdtyl
      421 fhatiaenlr iarpaatdeq lraaartagi dqeiarlpdg yatlvgerga tlsggqrqrl
      481 alarallada pvlildeats avdergqari vrelaaagrg rtcvvvahrl davrhadhiv
      541 vldagrvaat gdhttllagg gvyaslvaag rtvqeeraa
//
LOCUS       WP_007453051             289 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: class II fructose-bisphosphate aldolase
            [Streptomyces].
ACCESSION   WP_007453051
VERSION     WP_007453051.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 289)
  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 289)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10097223
            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="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29995
     Region          44..281
                     /region_name="TBP_aldolase_IIB"
                     /note="Tagatose-1,6-bisphosphate (TBP) aldolase and
                     related Type B Class II aldolases. TBP aldolase is a
                     tetrameric class II aldolase that catalyzes the reversible
                     condensation of dihydroxyacetone phosphate with
                     glyceraldehyde 3-phsophate to produce tagatose 1; cd00947"
                     /db_xref="CDD:238477"
     Site            order(52,55..57,63,67,70..71,144,236..237,239..240,243,
                     247,250)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238477"
     Site            order(84..85,182..184,186,211..212,214,233,235..236)
                     /site_type="active"
                     /db_xref="CDD:238477"
     Site            order(85,183,211)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238477"
     Site            order(182,184,186,212,214)
                     /site_type="other"
                     /note="Na+ binding site [ion binding]"
                     /db_xref="CDD:238477"
ORIGIN      
        1 msiaatgdli aeaaaqhrav aafnvitleh aeaiaegaee agapvilqis enavayhrgr
       61 prplaraaae vaeqaavpvs lhldhvqste llhraadcgf ssamfdaarl pytenlaatr
      121 aavvwaherg lwleaelgqv ggkngepald ahapgartdp dearsfvaat gvdalavavg
      181 tshamtsrda vldhgllgrl reavpvplvl hgssgasdee laravmggir kvnigtalni
      241 amtgairerl arddrgvdpr ryladgrdam artvarmisv lpagrahaa
//
LOCUS       WP_007453757             389 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: exonuclease SbcCD subunit D [Streptomyces].
ACCESSION   WP_007453757
VERSION     WP_007453757.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..389
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42142
     Region          1..271
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          269..358
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrilhtsdwh lgrsfhrvsl ldaqaayldh lvatvrerev dvvlvagdvy dravppltav
       61 elfdralhrl aaagvptvmi sgnhdsarrl gvgaglfera gihlrtdpen catpvvladd
      121 hgdvafyglp ylepalvkdt lraagaghea vltaamdrvr adlatrpggt rsvvlahafv
      181 aggepsdser ditvggvaav pagvfdgvgy valghlhgsq rvtsrvrysg splaysfsea
      241 dhrktmwlid ldgdgdiaae eridcpverp larlrgrldt lledpalerh ehawaevtlt
      301 dpvrpaepma rlarrfphtl slvfdperpp ddpgasyaqr lqgrddhqia edfvahvrgg
      361 sgpsdlertv lraafddvrv detvrevsr
//
LOCUS       WP_007454934             224 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Streptomyces].
ACCESSION   WP_007454934
VERSION     WP_007454934.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 224)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 224)
  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 224)
  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 224)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            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="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23415
     Region          135..221
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(154,173..174,192,195,203..204,214,219)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mantrtfsaa saataaspap aaarpasrsl pahpnrhrlr avdsdevagp advtdflppg
       61 atwlpapqha lptlpgqppm igylvlvpad qqpalagava aasrlpsggs pfpqqpgpda
      121 apapasdsga sagpvridat rrtasvdgvv ldltylefel lshlvayphr vhtrdqlvtt
      181 vwgyghvgdg rtvdvhvarl rrklgaeyrr siqtvrrvgy kytp
//
LOCUS       WP_007454999             293 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Micromonospora lupini].
ACCESSION   WP_007454999
VERSION     WP_007454999.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora lupini
  ORGANISM  Micromonospora lupini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Micromonospora lupini"
                     /db_xref="taxon:285679"
     Protein         1..293
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /function="18.1 : Enzymes of unknown specificity"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30151
     Region          16..260
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 melteptvws tdrldlgegl rwvddrlvlv dllagrllet egdaptplre lrrldvplga
       61 vapvtgrpge wlaaagtgvt vlpatgdprp vadlvgdape ptrmndavad phgrfwagsm
      121 tyaavpgggt lfrltpgaep vaavtgltip ngpafdaagt tmyladtprg eidrftvdpa
      181 tgalhgrepf vrlspadggp dgmtldaagh lwialwggsa vrryrpdgtl dreirlpatq
      241 pagiclggpd rrrlfigtar vgldapgpqd gallavdvpv pglpaagaga pgs
//
LOCUS       WP_007455091             324 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Micromonospora lupini].
ACCESSION   WP_007455091
VERSION     WP_007455091.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora lupini
  ORGANISM  Micromonospora lupini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 324)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Micromonospora lupini"
                     /db_xref="taxon:285679"
     Protein         1..324
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /function="3.1 : Biosynthesis"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34325
     Region          1..323
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mpigvtglgs hvpetiidna tvgrwagvdp awvtertgii erryadaata tsdlaaaaar
       61 dalagderri eglivatctp dvpqpstaai lqhklglsgv pafdvnavcs gflfgltvae
      121 gmmlgrfgsg emlvvgadmf srimdrgdrk tvslfgdgag avvlgqvpeg ygivasrlqt
      181 hgehhdyvvv eaggtrqalt eetraagrhy frmdgrsvrd yavqtqrkli eqvladaalt
      241 ladvdrfvfh qantrllesl aremgigmdr valtapeygn tagasipvtl hashrvrplq
      301 rgerilmssv gggmtaaall ltwy
//
LOCUS       WP_007456722             409 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Micromonospora
            lupini].
ACCESSION   WP_007456722
VERSION     WP_007456722.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora lupini
  ORGANISM  Micromonospora lupini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 409)
  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 409)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Micromonospora lupini"
                     /db_xref="taxon:285679"
     Protein         1..409
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44933
     Region          3..403
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 maapeslsla qarrvalaaq gfadpppvgv ptrrhlrrvl drvgliqmds vnvlqrahyl
       61 plysrlgpyp tslldqaayr rprelfeywg heaslvpvgl hpllrwrmar ahseswggmr
      121 riaqeqpelv awvrdevaar gpltaaeieh dapretgnwg wnwsavkral eflfwagevt
      181 aaerstsfar rydlpervlp pavlaaptpt daeayralva laarslgvaa epelrdyfrl
      241 plagarqava elaeagelvp vtvagwrqpa wlhasarlpr wvrgntlvsp fdplvwerar
      301 terlfdfsyr ieiyvpapqr vygyyvlpfl qgdrftarvd lkadrkagvl lvpaawiepg
      361 adpgetaval aaelyrlagw lgldavvppa agdlagplta alagvsgvp
//
LOCUS       WP_007457043             382 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Micromonospora lupini].
ACCESSION   WP_007457043
VERSION     WP_007457043.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora lupini
  ORGANISM  Micromonospora lupini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Micromonospora lupini"
                     /db_xref="taxon:285679"
     Protein         1..382
                     /product="exonuclease SbcCD subunit D"
                     /function="8.3 : Degradation of DNA"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=40854
     Region          1..278
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          281..362
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkilhtsdwh vgkvlkgqsr aeehkavlag vidiaraeqp dlvivagdly dtaaptseat
       61 rlvtraltal rrtgadvvai ggnhdngpal dalrpwaeaa gitlrggvre npaehvidgt
      121 taggerwqla alpflsqrya iralemyelt aaeanqtyad hlgrvlgrlt egfaepdrvh
      181 lvtahltvtg aaagggerda htvlgyavpa tvfpatahyv alghlhraqq vagpcpvrys
      241 gsplavdfge qenvpsvtvv evtastaarv revpvtaasa lrtvrgtlaq laeieapdaw
      301 lrvfvreqpr aglreeiqel lpraleirid pellaapgsg ariaqrsgrs prelfgdyld
      361 srghadegvr dlfdelfeev eh
//
LOCUS       WP_007457469             238 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease family protein [Streptomyces].
ACCESSION   WP_007457469
VERSION     WP_007457469.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..238
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=25470
     Region          <117..223
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mprrlgflpa alltaitlta csaetvesdd pkppattnps gapggtpggs glplaeaigk
       61 ipvaeekrtg yerdsfkhwv dedddscttr aevllaeavt apeqgarcsl sggswlsyyd
      121 etevtdakkl didhmvplae awdsgahdwt perreayand lgsdrslvav taktnrskad
      181 rdpaqwmppa esatctylvd wtatklrwal tmddaektal lnlaepcads vveyesap
//
LOCUS       WP_007458786             266 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Streptomyces].
ACCESSION   WP_007458786
VERSION     WP_007458786.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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
REFERENCE   2  (residues 1 to 266)
  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 266)
  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 266)
  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 11444466
            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="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28329
     Region          9..79
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          <138..202
                     /region_name="PRK11901"
                     /note="hypothetical protein; Reviewed"
                     /db_xref="CDD:237015"
     Region          191..244
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 msignspedd rpsigralqq ariaaaltve evssstrvri pivhaieqdd fsrcggdvya
       61 rghirtlara vgldpeplve eydadhggrp aptpaaplfe aerirseprr pnwtaamvaa
      121 ivavigfvgf tlfsgedeps ntaqiaegsk pdktaakpta tkpsdpkpvp sesaiaaapr
      181 dkvtvklsad rgkswisakd hngrllfdgl llqgesktfq dkeridlvlg dagaielfvn
      241 gkqvedrfgp gqverlsytk gdpeag
//
LOCUS       WP_007459734             201 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Micromonospora
            lupini].
ACCESSION   WP_007459734
VERSION     WP_007459734.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora lupini
  ORGANISM  Micromonospora lupini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 201)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 201)
  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 201)
  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 201)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Micromonospora lupini"
                     /db_xref="taxon:285679"
     Protein         1..201
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /function="13.1 : Two-component systems"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21611
     Region          104..189
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(123,142..143,160,163,171..172,181,186)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 msvspassra gwhtsqpavp grppggqrrp antaapmltv tlsiplacee sltpparrll
       61 eaaremlerg egvitssapa erradgvpan raparaltpt ipalhilass rsvlrddepl
      121 pltrlefdll lhlvahprrv ftrlqllnav wgyehagvrt vdvhvrrlrg kvgvdvplvt
      181 tvygvgyrla ddarvtvdrt g
//
LOCUS       WP_007461696             811 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Micromonospora
            lupini].
ACCESSION   WP_007461696
VERSION     WP_007461696.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora lupini
  ORGANISM  Micromonospora lupini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 811)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 811)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 811)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..811
                     /organism="Micromonospora lupini"
                     /db_xref="taxon:285679"
     Protein         1..811
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /function="5.7 : Nitrogen metabolism"
                     /function="16.6 : Maintain"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88687
     Region          39..773
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mvdriaepwg ertpygpgde wpvrvdryla dgrtdvdvdr wvqsasvlhs ngdamdigva
       61 dgrivgvrgr avdrinrgrl dpkdlygwqa nnspdrltrp lvrdgdrlve sdwdtamgri
      121 varsrdlldg pggwgrfgfy tsgqlfleey yalgvigkag lgtphmdgnt rlctataaaa
      181 mkasfgtdgq pgsytdvdhc daialwghnv aetqtvlwmr mldrrrgpnp pamlavdpra
      241 tpvareadlh lavrngtnia lvngllreii rrgwydrdyv dahtmgfeel crivdgyppq
      301 rvadicdvpa adveraaell gtsqrllstv lqgfyqsnqa taaacavnnl hlvrgmigrp
      361 gagiyqmngq ptaqntretg adgdlpglrn wantshieel arlwnvevdt iphwapptha
      421 mqifryaeqg sikllwisat npavslpdla rirrilakpd lfvvvqdlfl tetaeladvv
      481 lpgatwgekt gtftsvdrtv hisdkavdpp geakpdldif ldyarrmdfr drdgqplirw
      541 tgpeevfeaw kecsrgrpcd ytgityarlr ggsgiqwpct eehpdgterl ytdgvfhtdp
      601 dycetygqdl atgaeftepe yrakepngra flhsvdyqps pevpdedhpm llttgrtvyq
      661 fhtrtktgra pqldraapdv wvelnpadae rlgiaegdlv gvssarggiq ararlcgirp
      721 gvvflpfhyg yfdqdpadrt praaneltit awdpvskqpl fkvaavavtk ladgrgvpsp
      781 aptiggsapp adagvpatvg gpaaeatsgk e
//
LOCUS       WP_007462540             265 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Photobacterium marinum].
ACCESSION   WP_007462540
VERSION     WP_007462540.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium marinum
  ORGANISM  Photobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 265)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Photobacterium marinum"
                     /db_xref="taxon:1056511"
     Protein         1..265
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=30172
     Region          32..253
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 makilrtrhe leqylnksea gyfyaryqgy amhsafqpiv sasgklfgye allrvydeag
       61 nklktepffn sefistaeri nfdrlarvih lrnfalflsk gtlflnlspi aaldsdkqea
      121 tqksfvrrid elglsidqiy fevlehtcsc dallvnslrn lqgygariai ddygveasse
      181 arardvrpdi ikvdrsllln yvegkrddll nviklarele arvllegved yrcyaagkhl
      241 qvdymqgyfi grpelvdslc qfepl
//
LOCUS       WP_007462621              74 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Micromonospora].
ACCESSION   WP_007462621
VERSION     WP_007462621.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora
  ORGANISM  Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae.
REFERENCE   1  (residues 1 to 74)
  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 74)
  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 74)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 74)
  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   5  (residues 1 to 74)
  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 10164212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Micromonospora"
                     /db_xref="taxon:1873"
     Protein         1..74
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /function="9.3 : Transcription factors"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=7822
     Region          10..73
                     /region_name="WHTH_GntR"
                     /note="Winged helix-turn-helix (WHTH) DNA-binding domain
                     of the GntR family of transcriptional regulators; cd07377"
                     /db_xref="CDD:153418"
     Site            order(10,33,35..36,44..48,50..51,54,64..65,67..70)
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:153418"
ORIGIN      
        1 mtsvpipyta reieddltrr iaagefrpgs rlptydalae eygsarrtva ravealksrg
       61 lvvgvpgsgt fvae
//
LOCUS       WP_007463856             786 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Micromonospora lupini].
ACCESSION   WP_007463856
VERSION     WP_007463856.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora lupini
  ORGANISM  Micromonospora lupini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 786)
  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 786)
  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 786)
  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 786)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..786
                     /organism="Micromonospora lupini"
                     /db_xref="taxon:285679"
     Protein         1..786
                     /product="TRAP transporter permease"
                     /function="7.1 : Amino acids, peptides and amines"
                     /GO_component="GO:0005886 - plasma 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=80137
     Region          109..775
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mspisspdgs sspprpansp adgpatnpad gpathpagep athpagepat spgggpprpr
       61 pgaepaepae pdgahspspt tlatkphqtg rdpdkpdpsg pdpsglgvae rasrdlaaqf
      121 edekpgrvls gpagllltta alavgalalw qvfrplsqgs kyyliiflag vlplvflayp
      181 adlrlpgrlr iwrgrastgp tvsdwvlval avaaclypvl pirigsgggg ynafldrqgl
      241 ltptdlvlgt illlllleac rrttgwilpa vcllflgygy yggflpqswp vahagldfsq
      301 lvdafynsds gfygtpldva asyivlftiy gaalefsgag rffvelsaaa frrsrtaagr
      361 tavasgfllg tvsgsgaatt vsigavtwpl lrragypper aggmlaaagv gailspptlg
      421 aaafiiaeyl gvsylqvlgw atvptvlyyl gilfaveida rrsgvrpavi dvgspwrlla
      481 rfgyhfasli aiivflavdv satravvfai lltvalsfld rahrltpgrl vtalvtgvrg
      541 vlavtavcaa agiitatttk tglgpqaaal liggaqavts dptfvlvlta llaavaltll
      601 glavpvtasf vigwvivgpa lldlgvtapa aamfvfyfav lsevspptal aavaaaavtg
      661 grlvptmwqt lryalpayli piafvitpag lgllgiggvq riafaavvta lsvavlavaa
      721 ggwlpgvgra gapervlgal agvtllwlep vpvtvgaala avaaagvflr rrsagrpstn
      781 plkerl
//
LOCUS       WP_007464386             412 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Micromonospora lupini].
ACCESSION   WP_007464386
VERSION     WP_007464386.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora lupini
  ORGANISM  Micromonospora lupini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 412)
  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 412)
  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
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 412)
  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   5  (residues 1 to 412)
  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   6  (residues 1 to 412)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 412)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 412)
  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 20021637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Micromonospora lupini"
                     /db_xref="taxon:285679"
     Protein         1..412
                     /product="ROK family transcriptional regulator"
                     /function="9.3 : Transcription factors"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41613
     Region          4..>93
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          89..399
                     /region_name="ASKHA_ATPase_ROK_BsXylR-like"
                     /note="ATPase-like domain of Bacillus subtilis xylose
                     repressor (XylR) and similar proteins; cd24076"
                     /db_xref="CDD:466926"
ORIGIN      
        1 mspthapaga arqgslreln lalvlgriaa adrppsradl atatgltrat vsavvedlla
       61 gqlvseadpa pragagrpar glvladrgpa glglevnvdy ltvcvvdlag qvrhrtvhra
      121 dlrpvapada larlvdlage aradaarqgl tlagaalavp glvddaglvr lapnlgwrdv
      181 pvpellsghp sltdevpgvp alvvdneanf aalgelhsrp pglasflhis gevgigagiv
      241 ldgalfrgvr gwsgeighlp vhpqgrpcrc ggrgcleqya gqeaivaaag llraelpadi
      301 atarlaelae agdpdalral hdagtalgva vasvvnlldl dtvvlgggya plapwlcppv
      361 laeiaarvlt aawspvtvrp stlgpeaaav gaaesvvrri varpagwlsr sg
//
LOCUS       WP_007464684             371 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Micromonospora lupini].
ACCESSION   WP_007464684
VERSION     WP_007464684.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora lupini
  ORGANISM  Micromonospora lupini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 371)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Micromonospora lupini"
                     /db_xref="taxon:285679"
     Protein         1..371
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /function="6.12 : TCA cycle"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=39048
     Region          2..369
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msrvlvlncg sssvkwrhyd gdrtldqgtv ervgepgggp adhasavrqi lagldltgla
       61 avghrvvhgg rtfsapalvd davlaaikdl vplaplhnpa nlagievara alpdvaqvav
      121 fdtafhhtlp eaaatyaidr dtaqrydirr ygfhgtshay vsrrtaellg rpydqlntit
      181 lhlgngasac avangrsvat smgmsplegl vmgtrsgdld ptvifhlrre gglsvddidd
      241 llnhrsgllg ltgandmrev lqrraagdpa aalafdvycr ritgyvgayy allghvdaia
      301 ftagvgehaa pvratalagl trlgitvdea rndgdgdrli spdgaevsvc virtdeerei
      361 arqtrdvvgt d
//
LOCUS       WP_007465191             790 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: Lon protease family protein [Photobacterium].
ACCESSION   WP_007465191
VERSION     WP_007465191.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium
  ORGANISM  Photobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 790)
  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 790)
  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 790)
  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   4  (residues 1 to 790)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Photobacterium"
                     /db_xref="taxon:657"
     Protein         1..790
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88888
     Region          87..790
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mpiqplssdq lyrvsdlkal pddckstknl tpldeivgqe raqqavefam sikekgyniy
       61 aigrnglgkr tmvlrylnrh epngngfkly dwcyvanfee prspkvlklp tgtghqfkkd
      121 ieklmtrlvk alplafdnem yysrseklkn qltqkqessl ltltneakek svslslttqg
      181 dyqlvalnge ephtedtfak lsekeqkqfe qtindlekkl rgivrqltel eeefsdkiek
      241 lndevaldvv vhfikelket yseqpevkay ldamqkdile nleifleese eqvalayaal
      301 dkkmprryqv nilvsqpehk fpivveesps yhnifgyven atfkgtvftd fslirpgslh
      361 ranggvllmd avkvlerpyv wdglkralrs rklnvssler evtlsgtisl epediplnvk
      421 iilfgdyqty qllqiydpef selfrvtadf edemprsdes eqqyaqfiss ivndsgmlhc
      481 drkaigriie yssrqaedqn klslhsadia nllretnyta kashatmira nhveqalqsq
      541 ekrvsrlrdh vmqtfangtt lidtegemig qinglsvvst tdhrfgapnr itattaygeg
      601 evfdierkvk lggsihskgv milssylasi fgkttkipls tnltfeqsyg gvdgdsasma
      661 elcaivsafa qaplrqdvai tgsmnqfgea qpiggvneki egffdvckik grhstqgvii
      721 pqsnvhnlml rkevveavek gefhiwaish vteaieiltg kpagvwmeet gypldsifgh
      781 aqvklnalrk
//
LOCUS       WP_007465746             178 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Micromonospora
            lupini].
ACCESSION   WP_007465746
VERSION     WP_007465746.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora lupini
  ORGANISM  Micromonospora lupini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 178)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 178)
  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 178)
  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 178)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Micromonospora lupini"
                     /db_xref="taxon:285679"
     Protein         1..178
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /function="13.1 : Two-component systems"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19178
     Region          83..171
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(102,121..122,140,143,151..152,163,168)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mrhyhrvvva ggaevpivvc vsadvsvrer vlrqldgigp vvtcadltql ramlfppsgg
       61 wmpavgpttp pvppqgrvsw gelvvdrvgh lvtwrgdplp ltrterella rlvgpplvvw
      121 syeqlfaavw agaylgdtai lhsavkrlrh klrglpggpr vhtvrgvgyr ldpppppa
//
LOCUS       WP_007466288             255 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora lupini].
ACCESSION   WP_007466288
VERSION     WP_007466288.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora lupini
  ORGANISM  Micromonospora lupini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 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
REFERENCE   4  (residues 1 to 255)
  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 18542080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Micromonospora lupini"
                     /db_xref="taxon:285679"
     Protein         1..255
                     /product="helix-turn-helix domain-containing protein"
                     /function="18 : Unknown function"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28117
     Region          1..63
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
     Region          72..249
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mndalrvaln dtghttesla etvgvdpktv arwltegrip hprhrfaaae alhkdvsdiw
       61 pdtsrrrdpi wfrpwqeier eavslrsyes tvlpgllqte ayaravlgga gliprgeier
      121 hlsvrlnrqg vlkrddppqf tavideailh rpvggratmr eqllavvaac aephirvhvv
      181 pravgayagl ngpfviahsh dhrvagyldn qlqgqvasdp ddiaammaaw envrgealsh
      241 rqsvdlmtev aetws
//
LOCUS       WP_007466591             381 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Photobacterium
            marinum].
ACCESSION   WP_007466591
VERSION     WP_007466591.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium marinum
  ORGANISM  Photobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 381)
  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 381)
  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 381)
  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 381)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Photobacterium marinum"
                     /db_xref="taxon:1056511"
     Protein         1..381
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=42072
     Region          54..379
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mvkrkvllwl aglcsaeghg mirlsrsivf wvlvlfglva cgqqgseadn kqvkpiewkl
       61 vtswpkgfpg lglaperlae kinklsqgrl virvygagel vpsfevfnav skgtaqmghs
      121 aayywqdrip aasffaavpf gmtslemsaw innggglelw qelydpygvl pvpggstgaq
      181 mggwfnrein tiedfqglki rlagyaahvl krigsipvsl sggelftale tgaidaaewv
      241 gpyndlafgl hnaakyyyyp gwnepgalme flinkdafqs lpddlqlivi taaqavnqdm
      301 ldeytvkniq alnvmlrehe vdlrpfppev laelkvltqq lleeksqtdp vferiyssyk
      361 lflsevrkyg kvtenadvnt d
//
LOCUS       WP_007468547             248 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Photobacterium marinum].
ACCESSION   WP_007468547
VERSION     WP_007468547.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium marinum
  ORGANISM  Photobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Photobacterium marinum"
                     /db_xref="taxon:1056511"
     Protein         1..248
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29188
     Region          25..200
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 miefdkisdf fsefydfkls dersyfdfhl httqakrrgs lpfyleflkd khhliaitdh
       61 neikgaisva eaginnvpai elackdgfei liyfrklqdl edfyirevec rkhfcrmert
      121 dkdieyyldv lvgrdcylsi phinglaghn ylqnkpyikk iltrvdaiet ynhslpknrn
      181 inaqiirrsy eldatfgsds ctnrdiesfy rllnqelrrq hkwmeslklp lgsdrlykps
      241 sshkgnsd
//
LOCUS       WP_007471533              99 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Segniliparus rugosus].
ACCESSION   WP_007471533
VERSION     WP_007471533.1
KEYWORDS    RefSeq.
SOURCE      Segniliparus rugosus
  ORGANISM  Segniliparus rugosus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Segniliparaceae; Segniliparus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Segniliparus rugosus"
                     /db_xref="taxon:286804"
     Protein         1..99
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10870
     Region          9..96
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(9,27..28,36,38,40..41,43,46..47,55,60,65)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(27,55..56,58,80)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mpqltdadfe rvrelvasip egrvatygdi akaagltnar hvgwimreds adlpwhrvig
       61 ssgrpaqhia aeqlarlrae gilsvdgkvp lrerrhvfh
//
LOCUS       WP_007472071             271 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Listeria
            fleischmannii].
ACCESSION   WP_007472071
VERSION     WP_007472071.1
KEYWORDS    RefSeq.
SOURCE      Listeria fleischmannii
  ORGANISM  Listeria fleischmannii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Listeria fleischmannii"
                     /db_xref="taxon:1069827"
     Protein         1..271
                     /product="formate/nitrite transporter family protein"
                     /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=29507
     Region          2..257
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msyyspkeit ettiekgiqk ahsntlslvi lgflggafis lgyllyirvv gtmphewgsf
       61 atfigasvfp vglvcillgg gelitgnmma vplaffdkki tftmllrnlg ivtlmnlvga
      121 lfvayffghf vgltegdfle ktvatagaki kdpfwvafvs gigcnwfvgm avwlsygakd
      181 fagkilgiwf pvmafvaigf qhvvanmfii paaifagsyt wtdfilnvip vylgntvgga
      241 ifvslfyfla ykkqavhpkk edirqpvten e
//
LOCUS       WP_007473009             174 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Caminibacter mediatlanticus].
ACCESSION   WP_007473009
VERSION     WP_007473009.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter mediatlanticus
  ORGANISM  Caminibacter mediatlanticus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF004685.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK06029
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Caminibacter mediatlanticus"
                     /db_xref="taxon:291048"
     Protein         1..174
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19306
     Region          1..171
                     /region_name="Flavoprotein"
                     /note="cl19190"
                     /db_xref="CDD:450266"
ORIGIN      
        1 mkkvlvcisg astvslgikl ynlipptyer ylvisenaki vlqkeenifl nddisappas
       61 gsfgiditfi vpcsmntlak ialgiadnli trsaavaike kkkliiapre mpfseihlnh
      121 mlnlsklsnv fiappifgyy skpktiedie mfligkwfdl agiennffkr wnsv
//
LOCUS       WP_007474239             647 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Caminibacter
            mediatlanticus].
ACCESSION   WP_007474239
VERSION     WP_007474239.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter mediatlanticus
  ORGANISM  Caminibacter mediatlanticus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 647)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Caminibacter mediatlanticus"
                     /db_xref="taxon:291048"
     Protein         1..647
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73334
     Region          2..646
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mtkticsycg vgcgfevegk vkgdkthpsn eglickkgsl edkvvnnril kplfrenked
       61 efreisyeea ikivankikn tspqkigfyl sgqllnedyy ianklakgfi ktnnvdtnsr
      121 tcmasavvgy kkvigsdyvp limedalncd lyilagsnia eahivffnrv kkakkkglkv
      181 vvidprftkt aeiadlyidi nvggdiylfl amqrkflddg midfeflrkk aefsedffen
      241 lkqinideyl kragvskdkf eklielwksn qnivgswtmg lnqssegvek niafinlfll
      301 tgkmfknlng plsltgqpna mggrevggla ttlavhldyt penvkkveef wgttaiptki
      361 gltademvkk gnleclivah tdpvyhlpnr hetekafrei dlvvelnayk wsetskfanl
      421 iipvapwgek egtqtnldrv itlqkpfrkk lakqdwevfa digkalgfsg fdfssskevf
      481 neykemtrls pdmniyecdy delenkpfrw gknldnaigg kakliwvdkq nrslmpneey
      541 lfllittrla nhwhsmtkta qvikdevefv emneedmrnl gindgeivkv kskfgettlk
      601 akkskikkgv vaipmhlriv nyltnnildp lskepdynht pvkvekc
//
LOCUS       WP_007475372             192 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Caminibacter
            mediatlanticus].
ACCESSION   WP_007475372
VERSION     WP_007475372.1
KEYWORDS    RefSeq.
SOURCE      Caminibacter mediatlanticus
  ORGANISM  Caminibacter mediatlanticus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Caminibacter.
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   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
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   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Caminibacter mediatlanticus"
                     /db_xref="taxon:291048"
     Protein         1..192
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23307
     Region          110..189
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(129,148..149,164,167,175,181,186)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 milvydytdi yefdkkivfs qdnffnevlk ekykiliinf dflkdfleik kffngyvifi
       61 yhiygfveyk kaleigdffy tydeiwkvnl rieylkkklk ikdiykikdf iidiknyiif
      121 kdnkpikisk aefeilktll lnqnkyiske filnsidein sydtikvlis klrnlgfnie
      181 tiknlgykik ee
//
LOCUS       WP_007476122             128 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Listeria fleischmannii].
ACCESSION   WP_007476122
VERSION     WP_007476122.1
KEYWORDS    RefSeq.
SOURCE      Listeria fleischmannii
  ORGANISM  Listeria fleischmannii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 128)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 128)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Listeria fleischmannii"
                     /db_xref="taxon:1069827"
     Protein         1..128
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=14080
     Region          3..125
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(6..9,39..41,44,68,107,121)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mdvfvdgass gspglsgagv viksdqiyeq halpigiltn heaefiacki glelalthnp
       61 dfvrlytdsk ividsvekry aknplfkphl dailqlseli plfyinyrnv sqnkkadela
      121 rqaiqsek
//
LOCUS       WP_007477533             286 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Bartonella melophagi].
ACCESSION   WP_007477533
VERSION     WP_007477533.1
KEYWORDS    RefSeq.
SOURCE      Bartonella melophagi
  ORGANISM  Bartonella melophagi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Bartonella melophagi"
                     /db_xref="taxon:291176"
     Protein         1..286
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32947
     Region          5..278
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mtnflpycld ilratdrdry isvlfapknk rralaalytf naeiarires vhnpligeir
       61 lrwwydsian aeiknnkhnp ilddllttia lfnlpktvfl rycdvrvfdl yndpiitihd
      121 leaycsktas tilqlacqil dfdvaqnftk ayehggiaqa lsgilrllsl mqsryqryfp
      181 sdmlkvmgie reelefnhin neqkheiika mvalskdhyl kfyehsitlp ktlkpaflpl
      241 aitpaslqrt mqlgaavfqe natlsqlhry wlitktamsg hfpkll
//
LOCUS       WP_007479645             393 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Acinetobacter].
ACCESSION   WP_007479645
VERSION     WP_007479645.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..393
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42318
     Region          5..388
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 maksvlvinc gsssikyali serredriyg laenlgsada rikgvtvgge plelsiphad
       61 hakaletlla rlanynpqai ghrvvhggnl tkaelltpei vkrieaatpl aplhnpahlv
      121 gieatmrlfp elpqvavfdt afhqtmpeha yryalpqnly tehhvrrygf hgtshayvte
      181 raselagakn qggwlsahlg ngsstcavwn gqsidtsmgm tplegvvmgt rsgdvdpslh
      241 lflasnlgwd iqkidnmlnk esgllglsgl sndmrtlvda sndghegatl aievfcyrla
      301 kslsalscgl prldglvftg gigensayvr ektlgylshf glqfskeknd alprgtegri
      361 dagqgpqiwv vptdeegria ketrqvveqt vla
//
LOCUS       WP_007484935             418 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Bacteroides nordii].
ACCESSION   WP_007484935
VERSION     WP_007484935.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides nordii
  ORGANISM  Bacteroides nordii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Bacteroides nordii"
                     /db_xref="taxon:291645"
     Protein         1..418
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=47284
     Region          2..288
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          283..398
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mirilhtadw hlgqtffgyd rveehvhflq wlarelkenk idvllvagdv fdvsnpsaas
       61 qrmfyhfirq vteenpklql vvvagnhdsa arleapvpll qemrteirgi vrkhegeidy
      121 dhlivelkns egevealcla vpflrqgdyp vvatdgnpya egvkelyvrl qeralqrrkd
      181 gqalvavghl qatgseiaer dfsertiigg lecvspdtft eqiaytalgh ihksqrvsgr
      241 envryagspl pmsfaereyh hgvvivtlae gwaveiekre yvplvgllsv prgkaatpee
      301 vleelahlpl aseeaegeqt erslhfpyle ikvlltepep mlrqrieevi adkavrlari
      361 vsvyrqaeen tleeevlaag lqemnplqiv katfentyqs empeelerlf qqamreae
//
LOCUS       WP_007482136             336 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Bacteroides salyersiae].
ACCESSION   WP_007482136
VERSION     WP_007482136.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides salyersiae
  ORGANISM  Bacteroides salyersiae
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Bacteroides salyersiae"
                     /db_xref="taxon:291644"
     Protein         1..336
                     /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=39018
     Region          4..281
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mndntnkrid fvdltkgici ilvvmahidg afakfdessm iscfrmplyf fisgiffksy
       61 egfagflirk inkllipftf fyitafllky vvwkiapgvf hlpvqwseml vifhghdlik
      121 fnppiwflia lfncnilfyl ihflrnkhln lmfastllig aagfymgkyr felpfymdva
      181 mtalpfyaag fwirrynffl fphrfdkwip lfmamaltim yftattpgmr tnsytgniaq
      241 fyiaalagif mimlfckrik hisvisylgr ysvitlgihg pilhfggqfv sryihnewvl
      301 aftllfvtla icivltpffl kvmpqvvaqk dlikir
//
LOCUS       WP_007485217             337 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Bacteroides nordii].
ACCESSION   WP_007485217
VERSION     WP_007485217.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides nordii
  ORGANISM  Bacteroides nordii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 337)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Bacteroides nordii"
                     /db_xref="taxon:291645"
     Protein         1..337
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37296
     Region          3..333
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 merkayikqi dyylpvhivk nedivadfpe wsvekiaqkv gvnkrhvase setatdlaik
       61 aakqlfakge vsrdeidyil fctqspdyfl ptsaciiqek lglrrnigal dfnlgcsgyv
      121 yglslakgli scgiansvll ltgetynkhl hpkdkgnrti fgdaasatvi sttgiseigd
      181 fslgtdgrga enlilktggm ripeklydls fddnnnpvss dylymngsei ftftldnvpp
      241 lidnvlqkng ltnedvdlyv fhqankymln flrkkirire erfyyclsev gntvsntipi
      301 alksaldegt innnmkvvia gfgvgyswga ttlyfnl
//
LOCUS       WP_007486955             336 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Bacteroides nordii].
ACCESSION   WP_007486955
VERSION     WP_007486955.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides nordii
  ORGANISM  Bacteroides nordii
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Bacteroides nordii"
                     /db_xref="taxon:291645"
     Protein         1..336
                     /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=39034
     Region          4..281
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mednkskrvd fvdltkgvci ilvvmahigg aftrfdedsm vscfrmplyf fisgiffksy
       61 egflgfflrk inkllipftf fyvgafllky vvwkiapgvf hlpvqwsell vvfhrhdlik
      121 fnppiwflia lfncnilfyl lhflrdrhlk lvfaltllig aigffmgkyr felplyvdva
      181 mtalpfyvag fwirrynffl fphrldklip lfiiaalaim yfvaftpgmr tnsyhgnifq
      241 fyiaafagif mimllckrvk hipvvsylgr ysvitlgiha pilhfsgqla sryihnewal
      301 aftllfitlg iciavtpffl kvmpqvvaqk dlirir
//
LOCUS       WP_007488469             398 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Flavonifractor].
ACCESSION   WP_007488469
VERSION     WP_007488469.1
KEYWORDS    RefSeq.
SOURCE      Flavonifractor
  ORGANISM  Flavonifractor
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Flavonifractor"
                     /db_xref="taxon:946234"
     Protein         1..398
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42289
     Region          1..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkvlvinags sslkyqlmdp atrevfakgl cerigidgrl thkvpakdak yefeipmpth
       61 seaiqavlda lldaghgvik saseidavgh rvvhggekfa ssvritdevm aaleecipla
      121 plhnpanitg ikacekvmpg vpmvgvfdta fhqtmpaksy iyalpyefye qdkvrrygfh
      181 gtshryvsar aaamlgkpie elkiitchlg ngssvaavdg gksvdtsmgf tplagvpmgt
      241 ragdldagil eylmgkhgyd mkemmtilnk ksgvlgisgv ssdfrdlena akegnqrael
      301 aleafqysvk klvgayaaam ggvdaivfta gvgendaatr mavasglefm gvkmdaeann
      361 vrgketviss adskvkvlli ptdeelmiam dtaeivgk
//
LOCUS       WP_007489658             258 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Flavonifractor plautii].
ACCESSION   WP_007489658
VERSION     WP_007489658.1
KEYWORDS    RefSeq.
SOURCE      Flavonifractor plautii
  ORGANISM  Flavonifractor plautii
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Flavonifractor.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Flavonifractor plautii"
                     /db_xref="taxon:292800"
     Protein         1..258
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28625
     Region          <84..143
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 mateqelrqs vvsimqgwig wseangkhkk iidlyntqkp lprgykvkyt dewcaatvta
       61 agmqaglsdi ilgecscsrm ialykakgrw meddayrpdi gdilmycwkd gdnyattdqt
      121 anpnhvgfvg avnsntmtiy egnkgeavat rtvpingryi rgyclpdyas kattikteae
      181 edddmdiskl tdadiealaa rldtvlskke psdwskeari waegqniisg dqagnkkykk
      241 patreelvqi lynienps
//
LOCUS       WP_007489760             138 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Flavonifractor].
ACCESSION   WP_007489760
VERSION     WP_007489760.1
KEYWORDS    RefSeq.
SOURCE      Flavonifractor
  ORGANISM  Flavonifractor
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae.
REFERENCE   1  (residues 1 to 138)
  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   2  (residues 1 to 138)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Flavonifractor"
                     /db_xref="taxon:946234"
     Protein         1..138
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14648
     Region          60..132
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkisrlefva lllaavfaaf aagwffrgqa apqpvrvete rtltqetpla lpaptpspsa
       61 qskedtlagg akinlntagv delmtlpgig ekraediiay rqangpfrip eeltevpgig
      121 egileglidy vttgeenr
//
LOCUS       WP_007490561             493 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Flavonifractor plautii].
ACCESSION   WP_007490561
VERSION     WP_007490561.1
KEYWORDS    RefSeq.
SOURCE      Flavonifractor plautii
  ORGANISM  Flavonifractor plautii
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Flavonifractor.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Flavonifractor plautii"
                     /db_xref="taxon:292800"
     Protein         1..493
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=52014
     Region          5..493
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 msrclriapt dnvavalepv aagirvaveg asvttredip qghklaltai pagadvikyg
       61 ypigrartei qpgqwvhthn latrldgaga pqaqvgggap aplrprsfqg yrradgrvgi
      121 rnelwivptv gcvngvarsm arrvedyarg rvdgvhvwsh pygcsqmged qehtrailcg
      181 lirhpnagav lvlglgcens siavlqerlg rwdsqrvafl ecqavedela egerllrela
      241 draaadrrep vgadelvvgl kcggsdglsg itanplagrv tdrviamggs allaevpemf
      301 gaegvlfrrc adegvtralp alveefkdyf trhgqvvyen pspgnkaggi ttleekslgc
      361 vqkggntpiv dvlhygetvr rrgltvlqtp gndlvsatgl aaagahlilf ttgrgtpfga
      421 pvptlklatn talasrkagw idydagglaq gdawephiqa llqlvldtas gaptraeaag
      481 yreiaiwkdg vtl
//
LOCUS       WP_007491240             196 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Streptomyces zinciresistens].
ACCESSION   WP_007491240
VERSION     WP_007491240.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces zinciresistens
  ORGANISM  Streptomyces zinciresistens
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Streptomyces zinciresistens"
                     /db_xref="taxon:1073330"
     Protein         1..196
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=21564
     Region          31..192
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 matpmsagrf ldrlraegtt vvevgdwenh nrnqvgpwgp vngvmihhta trgsaqtvel
       61 crkgyeglpg plchgvitkd grvhlvgygr anhaglgddd vlraviaeka lptdnesntd
      121 gnrhfygfec enlgdgkdpw perqldaiar vsaaicrhhg wsersvighl ewqpgkvdpr
      181 gfsmasmrer irerlk
//
LOCUS       WP_007494319             399 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces zinciresistens].
ACCESSION   WP_007494319
VERSION     WP_007494319.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces zinciresistens
  ORGANISM  Streptomyces zinciresistens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 399)
  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   5  (residues 1 to 399)
  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   6  (residues 1 to 399)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 399)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Streptomyces zinciresistens"
                     /db_xref="taxon:1073330"
     Protein         1..399
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40564
     Region          14..77
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          77..379
                     /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 metpgsqssl hranlervvr avrlagsltq aeiarttgls aatvsnivre lkdggtvevt
       61 ptsaggrrar svslsgdagi vigvdfghth lrvavgnlah qvlaeesepl dvdassaqgf
      121 draeelvnrl iaatgvdrak iagvglgvpg pidvesgtlg stailpgwtg tkpaeelrgr
      181 lgvpvhvdnd anlgalgelv wgsgrgvrdl ayikvasgvg aglviegkiy rgpggtagei
      241 ghitldesgp vcrcgnrgcl etfaaaryvl pllqsshgtd lsmegvvrla rdgdpgcrrv
      301 iadvgrhigs gvanlcnlln psrvvlggdl aeagelvlgp iresvgryai psaarqltvl
      361 pgalggraev lgalalalse mgdstlldgt lhaatpaft
//
LOCUS       WP_007494404              67 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Flavonifractor].
ACCESSION   WP_007494404
VERSION     WP_007494404.1
KEYWORDS    RefSeq.
SOURCE      Flavonifractor
  ORGANISM  Flavonifractor
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   3  (residues 1 to 67)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Flavonifractor"
                     /db_xref="taxon:946234"
     Protein         1..67
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7498
     Region          12..63
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msyfseiygd pelsarakqv lvylhdrank dgkswyaiat makdlsisrs tikralaeli
       61 hqgrvek
//
LOCUS       WP_007496044             501 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Streptomyces
            zinciresistens].
ACCESSION   WP_007496044
VERSION     WP_007496044.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces zinciresistens
  ORGANISM  Streptomyces zinciresistens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Streptomyces zinciresistens"
                     /db_xref="taxon:1073330"
     Protein         1..501
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=53127
     Region          <29..498
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mshrpvrras asplftphgt drasrkaarr qlaeatakar aetgthsaqa tspehemptp
       61 lhpaggrpgp asargnrlkl pahrmttava agaypflaeg glgaegiyig rdvhaeasfv
      121 fdpfalygkv egftnpnlll agvigqgksa laksfalrsi afgyrvyvpc dpkgewtpva
      181 qalggrsval gpglpgrlnp ldaaprpasv seadwageir krrllllgsl artvlgrdll
      241 pmehtgldva ldavvthada tgrtpllgdi asalnnpaal deaagmmsgr lgeaardlah
      301 amrrlvfgdl agmfdapstv dfdpnapmls idlsrlggsg ddtalvlamt casawmesal
      361 sdpdggrrwi vydeawrlmr hvgllqrmqa qwklsrglgi anlmvihrls dlltagdags
      421 qgralaegll adcstriiyr qetdqlhaaa tllgltsvem daiahlnrgr glwkvagrsf
      481 ivqhllhshe lalfdtdarm h
//
LOCUS       WP_007496643             118 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Streptomyces zinciresistens].
ACCESSION   WP_007496643
VERSION     WP_007496643.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces zinciresistens
  ORGANISM  Streptomyces zinciresistens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Streptomyces zinciresistens"
                     /db_xref="taxon:1073330"
     Protein         1..118
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=12831
     Region          7..74
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mfqagdirew rghdvvdveg rrigrlesiy vdtatdapsf atvtvglptr hrlvfvplag
       61 atvgpgylkv tyakhlvkda psidvdgvlp aedekavfah ydlahrpgaq gerrlarr
//
LOCUS       WP_007497243             214 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Streptomyces zinciresistens].
ACCESSION   WP_007497243
VERSION     WP_007497243.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces zinciresistens
  ORGANISM  Streptomyces zinciresistens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Streptomyces zinciresistens"
                     /db_xref="taxon:1073330"
     Protein         1..214
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=23000
     Region          <116..209
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mskfyarrrv slvaaltgvm asvavlaapt asaalptpvs gatargylaq ltvatedrtg
       61 ynrdlfptwi tqsgscntre avlkrdgtnv vtdsscaats gswyspydga twpaasdvdi
      121 dhlvplaeaw dsgadawtta rrqsfandmt rpqllavtdn vnqskgdqdp aqwmpsrtay
      181 rctyvrawvq vkyyyglsvd saeksaltny lasc
//
LOCUS       WP_007498918             282 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Streptomyces
            zinciresistens].
ACCESSION   WP_007498918
VERSION     WP_007498918.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces zinciresistens
  ORGANISM  Streptomyces zinciresistens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces zinciresistens"
                     /db_xref="taxon:1073330"
     Protein         1..282
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29470
     Region          15..252
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 msapyevavr aeaelgegpt wdaasgrllw idilgsrlht ydpvsgrrsv rtahqhlgav
       61 kpraggglvl nlrdgvglld pdgafrwlhh dpvpgrrand aavapdgslw agtmrydeap
      121 gggtlsrita dgtaevvldd vtvsngtgws pdgsllyyid tptrridvfd haegravdrr
      181 plvgiedgag fpdgltvdae gcvwvalwdg aavrrytpdg vldrvvtlpv prvtacafag
      241 pglgdlyitt artglasphp lagslfvvpg agrglaqpaf kg
//
LOCUS       WP_007501421             741 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Streptomyces zinciresistens].
ACCESSION   WP_007501421
VERSION     WP_007501421.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces zinciresistens
  ORGANISM  Streptomyces zinciresistens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 741)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Streptomyces zinciresistens"
                     /db_xref="taxon:1073330"
     Protein         1..741
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=78916
     Region          51..739
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mlgsthgtlt tdsrrarvia cgeqpapavh grpaepgdld vsgrplygev pdldrffrpe
       61 slavigasda egrpnagitr rlvdwaervg arvhpvhpsr psvfgvpcla svaelpeqvd
      121 lavllvadpl pvieelaeak vrfavvfasg faetgeegaa aqarladave rsgtrllgpn
      181 tnlnaferfr ddldgpaial itqsghqgrp vfalqelgvr lshwaptgne adletadfis
      241 yfaerpevga iacyveglkd grafllaadr aarrgvpvva vkvgrtetga rtaashtgkl
      301 tgadavvdaa mrqygvirvd gldelqdtaa llararppra dgvvvysisg gtgahfadla
      361 aeaglrlpel srakqdelhr wipaylgvan pvdngghpvg dhrgrkiida llddpsvgvl
      421 icpvtgpfpp lsdrlvrdlv daaertdklv cvvwgspvgt epayrevllg ssrvatfrtv
      481 ancitavray ldhhrfvsgy rspfdeaprt pspssrkara lmrqgrrlse haakqllray
      541 girvpreqlv tsaaaavraa glvgypvvmk asgariahkt elglvkvglt sasqvrdtyr
      601 eltdiarred ltldgvlvcq mvergvemvv gathdelfgp tvtvglggvl vevlrdtavr
      661 vppfgeeqar amcaelrgra lldgvrgrpp adldalvevv lrvqrmvlel gddlaeldin
      721 plvvlprgqg avaldalvvc r
//
LOCUS       WP_007501544             397 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Bacillus altitudinis].
ACCESSION   WP_007501544
VERSION     WP_007501544.1
KEYWORDS    RefSeq.
SOURCE      Bacillus altitudinis
  ORGANISM  Bacillus altitudinis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Bacillus altitudinis"
                     /db_xref="taxon:293387"
     Protein         1..397
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43223
     Region          68..393
                     /region_name="SpoIIB"
                     /note="Stage II sporulation protein SpoIIB (spatial and
                     temporal regulation of the dissolution of septal
                     peptidoglycan during engulfment) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5816"
                     /db_xref="CDD:444518"
ORIGIN      
        1 mvifldekig ehflnlptkv lfffllamlk ceterrtgyi raisldrkvf ltnnvrkrgm
       61 tvkkrqakkq glkvningke emlhgeehqp qkqqedqvtf snweekrqse qetaasgeep
      121 skpkeedfqw ddaadhiyhs dpkvvtpyqk kkgsfdqkfs knrgpfkrvm ttivfavvlg
      181 tglgvfalsl skdgsanpsg gdhisvsasg sgpsakaggd appadladts kdnegeksas
      241 ghfstfvvqa gkfssekgad dlvdslkeag yagkkvsmdd gyyviaglat eqgmtsavgk
      301 klidqhfeaw ggkelsfqvp deltglieka svlsskmiag ddvdqkevtq liselenakt
      361 tdapakssll kavqllndps aengwksqqa lldqlnt
//
LOCUS       WP_007503245             390 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Streptomyces
            zinciresistens].
ACCESSION   WP_007503245
VERSION     WP_007503245.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces zinciresistens
  ORGANISM  Streptomyces zinciresistens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 390)
  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 390)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Streptomyces zinciresistens"
                     /db_xref="taxon:1073330"
     Protein         1..390
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43316
     Region          1..386
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mttprpgtal sadearrial raqgflgspd rrggvrgvlr hlgavqldti svlarsheli
       61 pyarlgavgr rtveqaywtd thafeywsha acilpveewp hfafrrrayr drphwshdlp
      121 dgvyeqvikq lraegpltat elggakrtse wwdwsgakva veralmygev vcverrgwkr
      181 vydlaeraip qallhddldd teclrrlvrl agqslgvgtr adiadyhrlk geqvdaviad
      241 sglvpvsveg wgkpawadpa alatpprgrh rttllspfds liwerarter ifgfthrlea
      301 yvpkpkrvhg yfampvlagg rlvgrvdpar egrtlvarqv tldgpkavpa vaqalaeaas
      361 wvdcadvrve rvqapelrep lareaarlmg
//
LOCUS       WP_007504021             664 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Caldalkalibacillus thermarum].
ACCESSION   WP_007504021
VERSION     WP_007504021.1
KEYWORDS    RefSeq.
SOURCE      Caldalkalibacillus thermarum
  ORGANISM  Caldalkalibacillus thermarum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Caldalkalibacillus.
REFERENCE   1  (residues 1 to 664)
  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 664)
  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 664)
  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 664)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Caldalkalibacillus thermarum"
                     /db_xref="taxon:296745"
     Protein         1..664
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=71436
     Region          43..654
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mpqkkdkdla kdtagkidls leketlttni ekaiynpdqv svltrvarla tallaiglai
       61 yiiysaafgg lpswqhravf tsvllilcfs yvpykkgnqq whwlfdglpl vlsifilifv
      121 yfsypevslr qgnpslhdkf vatamvalvi egvrrtvgla mavlvlffwl yifigpwfpg
      181 llghqgfsyr rmtdtmfitt ngifsdpiyv astililfll faalllrtga gqffielafa
      241 ltgrfrggpa lasvlasgml atitgngaan atmtgpftip lmkkvgysrn fsgaveavas
      301 qggqimppim gasafimaey tgipyiqiag yalapavlyf lvagiviylq arkqrlegip
      361 reqlpslwav lysrgylilp lfiiiymmvk gyspmmaglw aiisvfvlsl lrketrlrvl
      421 ellaaleagv knsistvmac agagiiagsv imtglgtrfs rfaielsgge llpmlvmimv
      481 asiilgmgmp tvsayvilat vavgglvqig vpvvaahffv fyfgimsgit ppvaitsyit
      541 aglaggdplk tafqslhigm agfiipymlv ykpalllegs tadiaiglvt aalglvsfaa
      601 ciqgylvtgt slwqrvlllv salflvttsi vassigfmll fgiclvqwlg rikqnkaqqd
      661 lksi
//
LOCUS       WP_007504100             655 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Caldalkalibacillus thermarum].
ACCESSION   WP_007504100
VERSION     WP_007504100.1
KEYWORDS    RefSeq.
SOURCE      Caldalkalibacillus thermarum
  ORGANISM  Caldalkalibacillus thermarum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Caldalkalibacillus.
REFERENCE   1  (residues 1 to 655)
  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 655)
  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 655)
  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 655)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Caldalkalibacillus thermarum"
                     /db_xref="taxon:296745"
     Protein         1..655
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=70414
     Region          27..645
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mdtkkpqqel ldeqgkinta qvdsvdidgp aagrqltgwv rtlfliiavt galfhlyiln
       61 fhpidpwvfr sthlvfgavl gfmlfpgwrg akdkvhpvdw vliiatifvg yyifanlnqi
      121 lfrfgvaptt mdfivalvgv llvfeltrrt sgwmlpllag vfvlyvmlgp wlpgilnhsg
      181 yrfdrfvtyi ygldgvfgvt ldvsskyivl fiifgaflqm srvghyfmdv afavagglrg
      241 gpakvaifss glmgmmngts agnavatgsl tiplmkrvgy qpkfaaatea tasaggqllp
      301 pimgagaflm aeilgiryse vilaatipal lyfisvyfmv dfearkqgmt glprnqlpkv
      361 reiakkaylf apvliliyml vngysvilsg svgivscfvv swlhpetrmg lkkvlhalel
      421 gmknaiqlia vvacagiivg vialtgvglr fsslllsiad nnillalifa mgisillgmg
      481 mpttaayava asvvapglir mgidplfahl fvfyyavisa itppvalaay aaagisgtdp
      541 fktgvqafkl glaafivpfm ffyspqlllq gdswvkiifv altatvgvyl laaavqawff
      601 ggkvawygrl llfaasllli tanvtldlia valvaivili qrfthvsqkg kvsls
//
LOCUS       WP_007504207             289 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Streptomyces
            zinciresistens].
ACCESSION   WP_007504207
VERSION     WP_007504207.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces zinciresistens
  ORGANISM  Streptomyces zinciresistens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 289)
  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 289)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10097223
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces zinciresistens"
                     /db_xref="taxon:1073330"
     Protein         1..289
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29545
     Region          23..276
                     /region_name="TBP_aldolase_IIB"
                     /note="Tagatose-1,6-bisphosphate (TBP) aldolase and
                     related Type B Class II aldolases. TBP aldolase is a
                     tetrameric class II aldolase that catalyzes the reversible
                     condensation of dihydroxyacetone phosphate with
                     glyceraldehyde 3-phsophate to produce tagatose 1; cd00947"
                     /db_xref="CDD:238477"
     Site            order(27..29,32,52,55,58..59,63,67,70..71,144,236..237,
                     239..240,243,247,250)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238477"
     Site            order(84..85,182..184,186,211..212,214,233,235..236)
                     /site_type="active"
                     /db_xref="CDD:238477"
     Site            order(85,183,211)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238477"
     Site            order(182,184,186,212,214)
                     /site_type="other"
                     /note="Na+ binding site [ion binding]"
                     /db_xref="CDD:238477"
ORIGIN      
        1 mpltttgelv graaadrrav aafnvitleh veaviagaes tghpvvlqvs enavkfrygr
       61 llplaraava aaerarvpva lhldhvqsdd llrqapaagf ssvmydaarl pyadnlaatr
      121 aavdwahaqg lwieaelgrl ggkngeppld ahapgartdp dearafvaas gvdalavavg
      181 sshamttrta aldhdllkrl aaaldvplvl hgssgvpdge laaavtggia kvnvgtalni
      241 amtgairafl aahpeavdsr tylsvgream vravadlvrt vtgpapats
//
LOCUS       WP_007504331             376 aa            linear   BCT 20-JAN-2025
DEFINITION  GerAB/ArcD/ProY family transporter [Caldalkalibacillus thermarum].
ACCESSION   WP_007504331
VERSION     WP_007504331.1
KEYWORDS    RefSeq.
SOURCE      Caldalkalibacillus thermarum
  ORGANISM  Caldalkalibacillus thermarum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Caldalkalibacillus.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Caldalkalibacillus thermarum"
                     /db_xref="taxon:296745"
     Protein         1..376
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=41544
     Region          6..364
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 mnnqfnykis plemsisimt mligvsvlvm psrlaetmns pdgwisimis glavaglvtl
       61 ytrlqrrfpg qtlmgyfrqg ilgkwwallm gmgfvlyfvg vaaylvrtlv fvvqmyvldq
      121 tpseaiaslf lltttyavsk glqgiihlnl lflpvtlfig lgilsfnlpa melanllpvl
      181 geglspvlkg vkemivpflg veilfffmah mtanhlratp lnagilvvtl iyvmvtvmsy
      241 avfsleavkv iafptvelak evevpggffe rleslmitiw imtifnaaav sqyltvtiin
      301 dqflphtkla wlpslitfvi fiiafvpksi telftftewv gwlgaalffl gvgsgyvsvw
      361 vrnktatwnm tegsdk
//
LOCUS       WP_007505132             685 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Caldalkalibacillus thermarum].
ACCESSION   WP_007505132
VERSION     WP_007505132.1
KEYWORDS    RefSeq.
SOURCE      Caldalkalibacillus thermarum
  ORGANISM  Caldalkalibacillus thermarum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Caldalkalibacillus.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 685)
  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   3  (residues 1 to 685)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Caldalkalibacillus thermarum"
                     /db_xref="taxon:296745"
     Protein         1..685
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=75854
     Region          1..685
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdmnkyldaf ideatqhlqa vnenllllek epdnvalvqe ifrsahtlkg maatmgfedv
       61 adlthhlenv ldqvrngqlq vntpmldtlf savdtleqmi eaimkqeesg anpgqiisal
      121 srildrggak ddpvqlgnee kslplgssti lqavdeyvlt vltqseeagf hiyyiqvild
      181 qgcllkaara ymvfqllere geiiqshppv qeieeeafdf sfqllyvtkq pmeyiqqiil
      241 kvseieqvki fpisvdelkh sqgqkkmsat eevaagkeap aseaphpssr sntpstgagt
      301 krvlnktirv nidrldalmn lfselvidrg rlekiskelq hqelmetveh msrmssnlqd
      361 lilsmrmvpv eqvfnrfpkm vrslarelgk evelimsgte teldrtvide igdplvhllr
      421 naidhgletk eerrrlgkpe qgrielkayh sgnhvfievk ddgrgidrdk vlkraverei
      481 ltwergqeft dqdvyqllfa sgfstaetvs disgrgvgld vvknkieslg gsvsvqsepg
      541 agttftvqlp ltlsiisall vkvkhetyai pltsiievaa vkkgdvrtvq gqkvinfrgk
      601 vvplvsleev fevpgervde dvlsivivrk geklaglvvd aligqqevvl kslgaylnqv
      661 faisgatilg dgqvaliidc nalik
//
LOCUS       WP_007506102             334 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Streptomyces
            zinciresistens].
ACCESSION   WP_007506102
VERSION     WP_007506102.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces zinciresistens
  ORGANISM  Streptomyces zinciresistens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 334)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Streptomyces zinciresistens"
                     /db_xref="taxon:1073330"
     Protein         1..334
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35751
     Region          41..333
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 maygltafge algeetavkd vvadytedve rvlgygydhv hraapavsvs dlaveagrqa
       61 legvdprgvd llvlaltdla dhlywdaaar vqwalglsra eavlvdqgcv ggvtaldtva
      121 grfathpgyr talvvganrt veaywnrldt hsllfsdgaa aalavrdapt lrwrssyaet
      181 dgryadffrm dvggarrpfa pggetpavrd swdvvehfdh dserlaayae eiddrtarav
      241 hracrqagca eedlarllll ndnarvlaaq aelvgvpler tnarlaarhg hfgaadhlfs
      301 larthragel sagdlvalaa ngrgmhwaca vlqs
//
LOCUS       WP_007507284             163 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Rhodanobacter].
ACCESSION   WP_007507284
VERSION     WP_007507284.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter
  ORGANISM  Rhodanobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Rhodanobacter"
                     /db_xref="taxon:75309"
     Protein         1..163
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=17218
     Region          29..162
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mpvaihtgrr faslprsypr qaqgvphlrg ftlielmitv aviailaaia vpsyfqytlr
       61 snrsaaesvm qeiasaqery mvdarqfags lttlgysvpn tvdpnykidm vasaasasgg
      121 tgpdytitat pknsqvrdtg catltlkgdg sklastgatn cwk
//
LOCUS       WP_007507316             633 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Rhodanobacter denitrificans].
ACCESSION   WP_007507316
VERSION     WP_007507316.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter denitrificans
  ORGANISM  Rhodanobacter denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 633)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 633)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 633)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Rhodanobacter denitrificans"
                     /db_xref="taxon:666685"
     Protein         1..633
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68437
     Region          5..633
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mgrqnnpiet asdarrrlrt lalgaigvvf gdigtsplyt mketlgthgm tptepavlgv
       61 lslvfwslim vvslkyvtfv mradnkgegg imalmalaqr smsgsararw vlagfgifga
      121 alfygdgvit paisvlgave glqvaapglg kyvvwialai llgmfavqrh gthkvgkafa
      181 pvmtlwfvvl avlgvrqiia npqvlyainp lhavrfflsh gntsfialgg vvlaltgaea
      241 lyadmghfgk kpirlawfgf vlpalllnyf gqgallladp laisspfylm vpapllypmi
      301 vlsaaaavia sqavisgafs mtreamslgy sprlavvhts remsgqifvp wvnrmlmvlv
      361 ilavlgfrss dnlgaaygia vtgtmtmttl lalvvarkrw hwswltvvlv gvlfliidls
      421 ffganllkva hggwfplvlg vvlftvmttw rrgrelvvre ikqgglalap fieniaehpp
      481 lrvpgtaifl tanqhavpha llhnlkhnkv lhernvlltv etletpvaea deriaitpma
      541 gnffglelrf gfaedpnipl altqctregl gfdmmdttff lsretivada rrpgmalwrd
      601 klfaflsrna mpataffqip gnrlielgaq vei
//
LOCUS       WP_007507551              86 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Rhodanobacter].
ACCESSION   WP_007507551
VERSION     WP_007507551.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter
  ORGANISM  Rhodanobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 86)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 86)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 86)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Rhodanobacter"
                     /db_xref="taxon:75309"
     Protein         1..86
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8848
     Region          2..86
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mkvevslfga frdyqpaaav tlevpagarv adlrsalaay grahwpgfre glllrsafas
       61 qtcvlgeqev lpesgpvvvl ppvggg
//
LOCUS       WP_007509754             726 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate--CoA ligase family protein [Pseudofrankia].
ACCESSION   WP_007509754
VERSION     WP_007509754.1
KEYWORDS    RefSeq.
SOURCE      Pseudofrankia
  ORGANISM  Pseudofrankia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae.
REFERENCE   1  (residues 1 to 726)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 726)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..726
                     /organism="Pseudofrankia"
                     /db_xref="taxon:2994363"
     Protein         1..726
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76341
     Region          20..726
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mpeprhpelr hpelrhvdws rlfsprvvav vgasdtegsp qraqwtqvsq rlgalgaevi
       61 pvhpkkpdil gvkaypsvta lpadpdiviv lvrdplpvve eavsrnagfv vvfsagfsel
      121 gtaegdaaea rlrelasgat rvlgpntnln ifepwpdelp srkklaiitq sgyqgrpitq
      181 aqalgvgiei watigneadl ewadfagyla anrpnvgaia tyvegfqngg aflraadaca
      241 kagipivaik igrseegrvm aaahtghltg pdavhdavfd qygvirvddl devieisnmf
      301 cqtglvdgpg giavyamsgg tashvadlfg aagvripkfe qttvdaleky ipwylrrdnp
      361 vdsggvitar penrevlqlm lddpntdvlf apitgvfpgm sdalsrdlia lhqrflageg
      421 kpvvaawisp irddsyrslc eagvpvfhsf naavrglsel grysrfvray rspfdddqaa
      481 tgvpapaerp aaaaagrell agagatlnev dskkllagyg ipvagervvt saddavaaav
      541 elglpvvmki vspdiahksd lglvavgvgd edavratydr llataasaap eaaidgvlva
      601 qlvtdavaev ilglshqhpf gptitfglgg vftevfadva favppfdadr arkviestkg
      661 vkilrgtrgr pagdvdalvd vilrlqsval dlgdaiseld inpilvrpag qgvvavdalv
      721 ipakrp
//
LOCUS       WP_007510681             132 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein, partial
            [Pseudofrankia saprophytica].
ACCESSION   WP_007510681
VERSION     WP_007510681.1
KEYWORDS    RefSeq.
SOURCE      Pseudofrankia saprophytica
  ORGANISM  Pseudofrankia saprophytica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae; Pseudofrankia.
REFERENCE   1  (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   2  (residues 1 to 132)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 132)
  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 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   5  (residues 1 to 132)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Pseudofrankia saprophytica"
                     /db_xref="taxon:298655"
     Protein         <1..132
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          28..112
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(47,66..67,84,87,95..96,104,109)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 rpaagagagt apeaeaggvg dlvrhgglvv drrtrrield gqrlaitare fdllaflaad
       61 pgrvrtrrei fqavwgpwfg stkvldvhvg slrrklgrpe lietvygvgf rladpvaepg
      121 largqgragg lr
//
LOCUS       WP_007510996             964 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: molybdopterin oxidoreductase family protein
            [Pseudofrankia].
ACCESSION   WP_007510996
VERSION     WP_007510996.1
KEYWORDS    RefSeq.
SOURCE      Pseudofrankia
  ORGANISM  Pseudofrankia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae.
REFERENCE   1  (residues 1 to 964)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 964)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 964)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..964
                     /organism="Pseudofrankia"
                     /db_xref="taxon:2994363"
     Protein         1..964
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=101894
     Region          33..744
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mspdqaqaaa aatagaaasg tgdtvatasr aftpshcpyc alqcgielrp rpgvvdlipq
       61 ddfptnrggl cskgwtaagl ldhpdrlttp llrdrsagga rgelrpatwd ealerivtsw
      121 rdcqrrygrd svgvfggggl tnekayalgk fvrvalrsrs idyngrfcms saaaagnraf
      181 gidrglpfpv sdiaeadvvl lvgsnpadtm ppimqwfdag rakgarhivv dpratptarg
      241 ahlhlqptpg tdlalaagll hiairdglvd tdfvasrttg fdavrravta ywpgrverit
      301 gvpetnlrea vrllaeaera mvltargaeq hasgtdttqa finlalalgl pgrsfsgygt
      361 itgqgngqgg rehgqkadql pgyrkladpa drahiaaiwg vspdelpppg vsafemldal
      421 gteggvramw vlgsnpivsg pdanriadrl aaldllvvsd fflsetaala dvvlpvaqwa
      481 eeegtmtnle grvlrrrral apppgvrtdl eviselairl grsaeafpve pravfeelrr
      541 asaggladys gisyerieae kgvfwpcpap aaagedsana vgelgeagea vhpgtprlfa
      601 erfatpdgra rfvavhhrga aetpdrdypy ylttgrtmrq yqsgtqtrrv ralvaddpdp
      661 vvelhpvlat kyeitagdlv elssrrgrav frarvtdtir qdtlfapfhw ggystvnllt
      721 npaldptsrm pefkacaval rridhlpdgg aalpteatvp vatewsrprt tspstaantg
      781 tagtnvaggg gaggapsagl adladladla gpvatapasv rtfpgtgsar tgsdsaqdta
      841 pvshrkdrrm hstprflqgv fsfegqgltk pafldpslty tvppgataqp vyfrggnasd
      901 elvyvllvrd gapmryfpig aradvhvplr vvedllgdtr ielhlaapeg iegtvvidlg
      961 lief
//
LOCUS       WP_007511125             498 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Rhodanobacter denitrificans].
ACCESSION   WP_007511125
VERSION     WP_007511125.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter denitrificans
  ORGANISM  Rhodanobacter denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
REFERENCE   1  (residues 1 to 498)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Rhodanobacter denitrificans"
                     /db_xref="taxon:666685"
     Protein         1..498
                     /product="amidohydrolase family protein"
                     /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=53216
     Region          54..485
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mpvqarrpap vlapphprrn allaaalagl cavssawaqa pqlsartlqy vkyaqpliai
       61 thvrvidgtg tparenqtvl lrdglivavg rhvklpkdat vidasghtli pglvgmhdhm
      121 fypapkvnpe akeaiypeqa ssfpklylag gvtsirttgs tepytdlelk kaidagqipg
      181 pkmhttgpyl egkgsftpqm heltdaadat dtvnywigeg atsfkaymhi traelsaaia
      241 aahakhiqvt ghlcaigfte aaelgiddle hglpvdtefm agkqpdvcpd tklavaqlat
      301 msvddprirq lirtlvskrv avtstlpvfe tfvpgrapvd prvldamlpe trveylasre
      361 rvagmhdspw pkvfkleqdf erafvqqggi llagldptgy ggviagygdq revellveag
      421 ftplqairia tlngarfmge dqrigsievg kaadlvlldg npatnikdve hvalvfkdgv
      481 gydparlvka angtvglr
//
LOCUS       WP_007511219             203 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Rhodanobacter].
ACCESSION   WP_007511219
VERSION     WP_007511219.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter
  ORGANISM  Rhodanobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Rhodanobacter"
                     /db_xref="taxon:75309"
     Protein         1..203
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22839
     Region          3..172
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mrlfgalyar altwarepra lyylsglsfv esfifpippe vmlapmmlgk rhkafffanv
       61 sllfsllgal vgyvlghwaf halrpvldal hllapieqgv atlsrqmveh rwgmygvlil
      121 aalqpvvpmk fvtwacgiig vpilpflaci gvgrgkrvwl lallirlvge raerilhehi
      181 erigwaalvl lallllvwwf wlh
//
LOCUS       WP_007511352             448 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Pseudofrankia].
ACCESSION   WP_007511352
VERSION     WP_007511352.1
KEYWORDS    RefSeq.
SOURCE      Pseudofrankia
  ORGANISM  Pseudofrankia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 448)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Pseudofrankia"
                     /db_xref="taxon:2994363"
     Protein         1..448
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=46923
     Region          225..448
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mergsegddv adgctcrdag agraagagpd rpgqtvrrml svarqhldmq lsclsrsagd
       61 alvveategd aesfgiapgf vsadpeslcg klrdgrlppv lpdvrsnrrt agdpaagelg
      121 tgprigalvt aqvrcadgqi yglltcmshe pdprlqekdg hflslladal sysvaepsvs
      181 epgvaepgva epsvsergvg epgsgepgaa wqmrdrrfrr irgviddggp kmvfqpvfnl
      241 atmrmasaea larfppgfgs perwfadavs vglgtdlels aidaalrvlp rlphglaiav
      301 naspatvasg rlakllasep tdriivevte heriedypat raaldhlrar gvrtavddvg
      361 vgyaslhhlv qllpdvikmd rqltqridtd rnlhalasal aqfagdigac vlaegvetag
      421 elrslvsagv hqaqgfylgv prplpsaa
//
LOCUS       WP_007511972             100 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein
            [Pseudofrankia].
ACCESSION   WP_007511972
VERSION     WP_007511972.1
KEYWORDS    RefSeq.
SOURCE      Pseudofrankia
  ORGANISM  Pseudofrankia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Pseudofrankia"
                     /db_xref="taxon:2994363"
     Protein         1..100
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11210
     Region          4..100
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mhpliearra eiqglcrrlg irrldlfgsa tgeafdlgss dvdvlvefda dragfdyygt
       61 yfalkegler llgravdvvs vtsirnpyfr dqvmrtrqpl
//
LOCUS       WP_007511782             268 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Rhodanobacter
            denitrificans].
ACCESSION   WP_007511782
VERSION     WP_007511782.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter denitrificans
  ORGANISM  Rhodanobacter denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 268)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Rhodanobacter denitrificans"
                     /db_xref="taxon:666685"
     Protein         1..268
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29733
     Region          9..267
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          25..118
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
ORIGIN      
        1 mnegvgearg vlrhapvagv fhhariappp alagvvqhyw ivrwdlqggp pqlretlphp
       61 nvhlvceagg srihgihtdr fsttlegrgg vfgvkfrpgg frgflrqpvs alrnrsippq
      121 qvfgedaarl eailhaqphd ermvtlasdf laarlpppdt qalrvgevvd aiatdrsirt
      181 lddvasrwpl tprtlqrwfn qyvgigpkwv inryrmheal qrvdagdavd wsrlalelgy
      241 fdkahfirdf ralvgcppae yarrgrag
//
LOCUS       WP_007512597             399 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Pseudofrankia saprophytica].
ACCESSION   WP_007512597
VERSION     WP_007512597.1
KEYWORDS    RefSeq.
SOURCE      Pseudofrankia saprophytica
  ORGANISM  Pseudofrankia saprophytica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae; Pseudofrankia.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 399)
  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   5  (residues 1 to 399)
  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   6  (residues 1 to 399)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 399)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Pseudofrankia saprophytica"
                     /db_xref="taxon:298655"
     Protein         1..399
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41855
     Region          19..>53
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          73..385
                     /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 mhlsflrdyh ealvialart tptiergmva dvtgltpqav skvlarlvee gvivpagvrr
       61 palgkpatvy rlvpdsrwai gahvtrravr laltdlagtv rastttslpa dftpdqllth
      121 laagvegmtt ehhlfperkp aqppaaghsq prpgleatra satdqtgtst atrlgrrlvg
      181 vgigmigpld qasgmvrdah glrhwhdvpl adlaekrlgl pvlvdkdvta gvtaeawrcg
      241 agfrdaalvl vetgigaglw lsgaahrgth tnagefghtv vqldgppcvc grhgcleavh
      301 nratdpaaaa avlatgvinl lqtldlghvv lagsdllrhg avyhqtvera vrtqvpradw
      361 ltvnvtltsl gtdviaagaa mqvlnarygl pdptrlrvp
//
LOCUS       WP_007513901             143 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Rhodanobacter denitrificans].
ACCESSION   WP_007513901
VERSION     WP_007513901.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter denitrificans
  ORGANISM  Rhodanobacter denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Rhodanobacter denitrificans"
                     /db_xref="taxon:666685"
     Protein         1..143
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14786
     Region          1..143
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mknvqkgftl ielmivvaii ailaaiaipa yqdylirtqv segavltdga ktaisefysn
       61 tgsfpsknas aglaspasit gkyvakvdvs attgqivatf gkdankaikt stfvlsaits
      121 tgsiawsckk stvdpkylpt scr
//
LOCUS       WP_007513414             405 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Pseudofrankia sp.
            EUN1h].
ACCESSION   WP_007513414
VERSION     WP_007513414.1
KEYWORDS    RefSeq.
SOURCE      Pseudofrankia sp. EUN1h
  ORGANISM  Pseudofrankia sp. EUN1h
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae; Pseudofrankia.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 405)
  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 405)
  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 405)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Pseudofrankia sp. EUN1h"
                     /db_xref="taxon:1834515"
     Protein         1..405
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=40696
     Region          <3..133
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          142..209
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          316..379
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mvafdgprdq hrdlsadpve stgrvaqvap pagavpaepa epeapvrptr pevpagslag
       61 slldrpnpgs ppdrqgpgsp pnghgrpagr sadgsagtsa aeevrpeepv laasedaase
      121 dedvqsdeaa gvaspeaadd gatigarlar arsatgmsid evsartrira tlirqmeqdd
      181 fsgvggsvya rghirgiart lgidpeplva aydadherip spsspssass fdplrhgegr
      241 rggrhwgtam vvsaavlcll alvaflipgs srhdgptpta vtgapspsaa aspgaapgaa
      301 ppstapptev nlrleavsaq swlevsddsn hvvlrqilak gdtrtltaka lrvkmgnaga
      361 mdlscnghkl gtmgapgqvv tvlvalggsg dctvdgaapa agrsn
//
LOCUS       WP_007514045             489 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Pseudofrankia saprophytica].
ACCESSION   WP_007514045
VERSION     WP_007514045.1
KEYWORDS    RefSeq.
SOURCE      Pseudofrankia saprophytica
  ORGANISM  Pseudofrankia saprophytica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae; Pseudofrankia.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Pseudofrankia saprophytica"
                     /db_xref="taxon:298655"
     Protein         1..489
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=50990
     Region          1..373
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          371..455
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mlvlhtsdwh lgrglhgydl gaaqaafvdh lvdvaraerv glvvvagdvh draipplsal
       61 rlfdealsrl rdtgarvvvi sgnhdaparl gdkaglldpr vrirtdpael atpvvvedrf
      121 gpvrvypipy lepaavadll pevalpevda pgdgpagqga dadtaghgtg pdaglsalan
      181 erggyrastg daagvpagla plavaegpae ppfpgmvslf dddelapsli paparrpaaa
      241 grgraaplsh aatmrramaa vradlaghpg arsvvvahaw vtgaagsdse rdisvggiah
      301 vpaslfdgit ytalghlhrp qrvqdreqvr ysgsplaysf seagdakatl laelgpaglt
      361 rveaipvptr rrmtilrgrl adlltrleyg ehaddfiaav ltdqarpmda mtalrerfpr
      421 tlvlrheped adaadtgsfa rrtrgrddld vaadfvgfar gtsateaere llataltear
      481 laamaaeag
//
LOCUS       WP_007517011             197 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Pseudofrankia].
ACCESSION   WP_007517011
VERSION     WP_007517011.1
KEYWORDS    RefSeq.
SOURCE      Pseudofrankia
  ORGANISM  Pseudofrankia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 197)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 197)
  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 197)
  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 197)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Pseudofrankia"
                     /db_xref="taxon:2994363"
     Protein         1..197
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20759
     Region          97..187
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(116,135..136,158,161,169..170,180,185)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mppqpatvpa pptsprvpal atihtvrrpa gapdeptgag araragapgg paerfdlrql
       61 hrapvavrav tgaaaatsga ggspfgpaga sggrggltvd rsawaawldg elldltylef
      121 evldflvrhp grvysraall rhvwghhvdd dpgqagrtvd vlvtrlrrkl gtehrfriet
      181 vrrvgyryrp aaadrlg
//
LOCUS       WP_007516625             293 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Streptococcus
            oralis].
ACCESSION   WP_007516625
VERSION     WP_007516625.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus oralis
  ORGANISM  Streptococcus oralis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 293)
  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   2  (residues 1 to 293)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Streptococcus oralis"
                     /db_xref="taxon:1303"
     Protein         1..293
                     /product="aminoglycoside 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=34544
     Region          8..227
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mefiskiais kgwsddkryc vtdqnqqkyf lrisdnekld skkfefdmme kvaslgvrms
       61 kpikfelcgd evhsihewid gkdaidtilt ysenqqytyg ietgrllrki htipatevye
      121 dweiffnrki ddkiskykec svqyesgqvf idflnenrel lknrpqvfqh gdyhignfmi
      181 gedreiyvid fdrfdvgdpw eefnrivwta qvspafasgm idgyfddkvp dlfwkllavy
      241 ilsnligalp waipygeeev svmqnqakei lewyddmkqi ipswylidkk tee
//
LOCUS       WP_007515287             160 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA, partial [Rhodanobacter denitrificans].
ACCESSION   WP_007515287
VERSION     WP_007515287.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter denitrificans
  ORGANISM  Rhodanobacter denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 160)
  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   3  (residues 1 to 160)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Rhodanobacter denitrificans"
                     /db_xref="taxon:666685"
     Protein         <1..>160
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <1..>160
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 regllqlern trelqesvmr irmlpigsvf nrfprlvrdl erklgkqvrl elhgehteld
       61 ktvlekigdp lvhlvrnaid hglelpaqrk aagkpetgtl klnayheggn ivvqisddga
      121 glnraaivak aqqrgllgag qepsdievae lifqpgfsta
//
LOCUS       WP_007519146             621 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Streptococcus oralis].
ACCESSION   WP_007519146
VERSION     WP_007519146.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus oralis
  ORGANISM  Streptococcus oralis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 621)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Streptococcus oralis"
                     /db_xref="taxon:1303"
     Protein         1..621
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=71434
     Region          44..98
                     /region_name="TypeIII_RM_meth"
                     /note="Type III restriction/modification enzyme
                     methylation subunit; pfam12564"
                     /db_xref="CDD:432638"
     Region          175..545
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 msqafettiq qalrevvesf deqyvaegll kkdaiivdld nykpelvkki ltnailneaf
       61 tediagatil kindiiqmle vdeywsnsyt rytnkiglat nnhyldettd vvlnfpykdg
      121 ilkagmtkdd vsredaeesf lneivareei dvlldkkilk nakkydkngs spvseikdtd
      181 nliikgnnll alhslkkrfs gkiksiivdp pyyfkktkss dafnynsnfk lstwlvfmkn
      241 rldvakells deglciiivg eegcaqlkll adnifgedky igtiswrksd nqanigefak
      301 vtdyiliykk ssgklnklpl tdkarkeyry sdengyfrrq ilfhktrgky nyelttptgk
      361 klygpwmkek eeierldnlg kiywtrggqe qpygklylqd segqipndfw dnsfgtnqrg
      421 aeeirelfrg drlfdfpkpe rliynlmkis seegdivldf fmgsgttaav ahkmnrqyig
      481 ieqmdyietv averlkkvin geqggisqdv awsgggsfiy aelmdknatf idavlnskhs
      541 delkaifndm kttldfdfrv dlqevdqsiw dedfemqkki lvkiidknql yhnyseidde
      601 tiksqlsqsd ydfnksfyge k
//
LOCUS       WP_007519702             311 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phytoene/squalene synthase family protein
            [Pseudofrankia].
ACCESSION   WP_007519702
VERSION     WP_007519702.1
KEYWORDS    RefSeq.
SOURCE      Pseudofrankia
  ORGANISM  Pseudofrankia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Pseudofrankia"
                     /db_xref="taxon:2994363"
     Protein         1..311
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34383
     Region          18..300
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mtvtqeaela aiaaepvlrr syaaarrlna ehgrtyylat lmlpawkrpy vhalygfary
       61 addivdslds qlpaadraaw ladwggrlvd tlhrgadatd dsvlpaviht irrwdlpvgy
      121 fesfltsmam dltvtgydtf ddlmtyvygs gtviglqmlp vlgpsspaaa pyagdlgtaf
      181 qlinflrdvg edlrrgrvyl presmelfgv treklatgvv dgavrrllrh eigrarellr
      241 aatpgirllh ptsrdcmwta arlyggilde iekadyqvls rrvavgtprr lavaggvlvr
      301 srarrlvprq r
//
LOCUS       WP_007521978             278 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptococcus oralis].
ACCESSION   WP_007521978
VERSION     WP_007521978.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus oralis
  ORGANISM  Streptococcus oralis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 278)
  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 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   3  (residues 1 to 278)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 278)
  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   5  (residues 1 to 278)
  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   6  (residues 1 to 278)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Streptococcus oralis"
                     /db_xref="taxon:1303"
     Protein         1..278
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31184
     Region          27..102
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          125..275
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mmhqfnqtmd yleqqltgev dmkrfqqlsg ysyplfsrlf siladvtlae ylrnrrlsea
       61 vtdlressek vidialkygy dsadafsaaf kkfhgatpse vrngkpyrif prlqlslkit
      121 ggknmdikiq kkpaftvagv lleaidnskc psawehlyah hsfesleslg sgqsfgvcse
      181 vkegeiinym aaydvtdktk aeelglsikd vsaaeyaivp vkgpipasih nawkyvlevf
      241 fpetgyrhsg spdfevyseg dmsspdyqme lwipvikn
//
LOCUS       WP_007524970             207 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Haemophilus sputorum].
ACCESSION   WP_007524970
VERSION     WP_007524970.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus sputorum
  ORGANISM  Haemophilus sputorum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 207)
  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 207)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 207)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Haemophilus sputorum"
                     /db_xref="taxon:1078480"
     Protein         1..207
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23072
     Region          7..207
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Region          95..123
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(97..98,101..102,104,130,133..134,137..138,140..141,
                     164,167..168,170..171,174)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          128..158
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          163..190
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdteqyfnkt eeqqfeeaks wfkqngsail lamlvgasav fgwnfwknhn qqisqessaa
       61 ydnviesylq dpikneplve kfikesghns yatfaqftea qqlvnkgdfa kaktvleqav
      121 ntedatlqtv arfrlaqvdy qlqnydaala tlgqikekaw tlrkavltgd ilvakgdnag
      181 aksayqqala dapeqekali elrlnnl
//
LOCUS       WP_007526159             204 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Haemophilus sputorum].
ACCESSION   WP_007526159
VERSION     WP_007526159.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus sputorum
  ORGANISM  Haemophilus sputorum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 204)
  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   2  (residues 1 to 204)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Haemophilus sputorum"
                     /db_xref="taxon:1078480"
     Protein         1..204
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=20706
     Region          <22..143
                     /region_name="valS"
                     /note="valyl-tRNA synthetase; Provisional; PRK14900"
                     /db_xref="CDD:237855"
     Region          134..203
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mktfksllal gmavafsssa laqttdavga lkdsakttin nevasqkasa tsavnskvns
       61 vkenvsavkt agtekvaaaq anvtekasaa kaqvtdkvta tkaqatekva atkaqaaekv
      121 tatkataaqk tenaatkvka sskvninkad ektlqslsgi geakakaive yrnkvgkiks
      181 aeelskisgi gdatvekiap yltf
//
LOCUS       WP_007526304             165 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Haemophilus sputorum].
ACCESSION   WP_007526304
VERSION     WP_007526304.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus sputorum
  ORGANISM  Haemophilus sputorum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Haemophilus sputorum"
                     /db_xref="taxon:1078480"
     Protein         1..165
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=18328
     Region          20..157
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mtdyllaffg ffssnenqwl flflsaflsa tvlpgnseiv fsalasksiy ahesfwhael
       61 wllvlvatvg nslgsivtya mgmlapkpin sqkrlvkwal eksekygvyv lllswlpfvg
      121 dilcaiagwl rfpavasvif itigkfcryl illvslypll kyvvg
//
LOCUS       WP_007527488             205 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Rhizobium
            mesoamericanum].
ACCESSION   WP_007527488
VERSION     WP_007527488.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium mesoamericanum
  ORGANISM  Rhizobium mesoamericanum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 205)
  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 205)
  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   3  (residues 1 to 205)
  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   4  (residues 1 to 205)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 205)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Rhizobium mesoamericanum"
                     /db_xref="taxon:1079800"
     Protein         1..205
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22801
     Region          11..201
                     /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"
ORIGIN      
        1 mtnstskpgd lnvlvidens irasiieigl reagydnvti iddmnglarr imeinpdviv
       61 idienpnrdm lesifqisra vkrpiamfvd ksdeasieaa veagvsayiv dglkqervrp
      121 ilkmaisrfn afsrlnrele etrgelenrk lldrakgllm rsrgltedea yvlmrrtamn
      181 qnrkiveiaq slitaaslld pgtda
//
LOCUS       WP_007529743             500 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Rhizobium mesoamericanum].
ACCESSION   WP_007529743
VERSION     WP_007529743.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium mesoamericanum
  ORGANISM  Rhizobium mesoamericanum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Rhizobium mesoamericanum"
                     /db_xref="taxon:1079800"
     Protein         1..500
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=52084
     Region          7..500
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mtkdpwiils agdnvavata aipsgatvag iqtrekidpg hkialcdial gqpvvkygqa
       61 igrttadvka gdhvhshnlh fendrlaata nsapeeasaa drartfmgyr radgrsatrn
      121 yigiiasvnc sttvcraiad eanrtilphf dgidgfvpiv hdqgcgmsst gdgmavlhrt
      181 lagytrhvnf ggvlmiglgc evnqltlygq sgagnakrhf niqdaggsrr averamgmlr
      241 eiaqdvgrek rvalpigdii iglqcggsdg fsgitanpal gvaadllaaa ggtailsets
      301 eiygaehllr sravsdevat klddkiawwe kyvalhgasl dnnpspgnkr gglttileks
      361 lgavakggrs pltavygyae rvtatglvfm dtpgydpvsa tgqvagganm iafttgrgsc
      421 fgcrpapsik lssnsalyas meedmdidcg tiatgdatis akgreifdli idtasgkktk
      481 seefgygdne fvpwhlgatl
//
LOCUS       WP_007529725             314 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Rhizobium mesoamericanum].
ACCESSION   WP_007529725
VERSION     WP_007529725.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium mesoamericanum
  ORGANISM  Rhizobium mesoamericanum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (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   2  (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   3  (residues 1 to 314)
  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   4  (residues 1 to 314)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Rhizobium mesoamericanum"
                     /db_xref="taxon:1079800"
     Protein         1..314
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /function="7 : Transport and binding proteins"
                     /function="16.1 : Circulate"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33779
     Region          3..312
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 msmieirnvt krygptavvd nvsmdvekgs itvvvgtsgs gkstlmrmin rlvpitsgei
       61 fvggqnimdv pvtelrrkig yaiqghglfp hrtvaqniat vpqllgwdtt kikgrvaell
      121 glfnldpatf aekyphqlsg gqqqrvgvar alaaepelll mdepfgaldp virgkaqddl
      181 laiqkqfgtt vvlvthdmde afhlgnqivv msagkvlqcs tpekiltept dpfvqqltgt
      241 sdralklmsl lplkesmepa ksgltyalpq tlslrdalae miwqgvgeaa vqdasnvpvg
      301 sismtrllql grka
//
LOCUS       WP_007530528             146 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Rhizobium mesoamericanum].
ACCESSION   WP_007530528
VERSION     WP_007530528.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium mesoamericanum
  ORGANISM  Rhizobium mesoamericanum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Rhizobium mesoamericanum"
                     /db_xref="taxon:1079800"
     Protein         1..146
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15904
     Region          7..145
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mtdlavyagl flvafaaati fpmqseaglv alivtkqypi fvlvavattg nvlgstvnwl
       61 lgigieryrh krwfpasqpa ldkaqrwyrr hgkwslllsw mpvigdpiti vagvlrepfp
      121 tfllmvtiak aaryavlsaa tlgims
//
LOCUS       WP_007530612             396 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Rhizobium
            mesoamericanum].
ACCESSION   WP_007530612
VERSION     WP_007530612.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium mesoamericanum
  ORGANISM  Rhizobium mesoamericanum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 396)
  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 396)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Rhizobium mesoamericanum"
                     /db_xref="taxon:1079800"
     Protein         1..396
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46125
     Region          1..396
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mtnlisnsda rriflakqgl sappnkaltk agllelihel gfvqvdsiqt verahhqilf
       61 srnqtykreh ltallekegs lfehwthdas ilpsaffkyw khkfrheeda imerwrkwrg
      121 egfehafdet yervvrdgai mareikadgh vsggwwnwhp nktaleyfwh tgkfaiagrs
      181 nfqkiydlve rvipaqfrep qvsreefvdw acrsaltrlg fathgeiaaf wdllspdeak
      241 twvnehrdel ievfvkpalg dkpraswafp dllasvqdyp eapprvrvls pfdpmirdrn
      301 rterlfgffy rievfvpepk reygyyvfpl legdkligri dmkadrkrgt ldvkrlwlep
      361 gvkasagrld rldaelqrla rfsgvekvty ldgwra
//
LOCUS       WP_007530784             314 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Rhodococcus triatomae].
ACCESSION   WP_007530784
VERSION     WP_007530784.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus triatomae
  ORGANISM  Rhodococcus triatomae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Rhodococcus triatomae"
                     /db_xref="taxon:300028"
     Protein         1..314
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32729
     Region          1..307
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mtgpvllldg aslwfrayya lpesftakdg rpvnavrgft dmvaslitrh qparlvvcld
       61 ldwrpqfrvd lvpsykahrv aaeidagpdv eevpdtltpq vdmimdvlaa agiatagavg
      121 feaddvlgtl aarerddtvv vvsgdrdllq vasdhpvpvr vlyvgrglak aelfgpaeva
      181 ekygvpadrp gpgyaelall rgdpsdglpg vkgvgektas tlllqygsva alraavddpg
      241 sglakgvrak laassdylda alpvvrvavd apvvlsgpdh lpstprdpar ladlaeelni
      301 gtsisrltaa mgsr
//
LOCUS       WP_007531051             428 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Rhodococcus triatomae].
ACCESSION   WP_007531051
VERSION     WP_007531051.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus triatomae
  ORGANISM  Rhodococcus triatomae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
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   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   4  (residues 1 to 428)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Rhodococcus triatomae"
                     /db_xref="taxon:300028"
     Protein         1..428
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=46319
     Region          20..324
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mtatepdhvt sddhvhgvei vldevvkryp gqktaavggv smvipagetv vfvgpsgcgk
       61 tttmrminrl ieptsgriti agrdalsidp dklrrgigys iqqaglfphl tvaknvatvp
      121 gligwdrkri aarvdemldl vgldpdtyrd ryprqlsggq qqrvgvaral aadppvllmd
      181 epfgavdpit rgllqdellr lqselgktiv fvthdfneav klgdriavlg nqsrilqydt
      241 peailanpad dtvagfvggd aslkqltlsr vrdvrlmqcp ttqedgsvdd frralharkr
      301 qwglvldrrn rplrwvspah lthavslrgv gdpvselvsv qstlqdalea llaessastv
      361 vtgrrgeyvg litidtlvtw lhdlreehah drdeddedde dgedgedgea gdgnhhadgg
      421 pgnpepap
//
LOCUS       WP_007533646             374 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Rhizobium mesoamericanum].
ACCESSION   WP_007533646
VERSION     WP_007533646.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium mesoamericanum
  ORGANISM  Rhizobium mesoamericanum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
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   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   3  (residues 1 to 374)
  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   4  (residues 1 to 374)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 374)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 374)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 374)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Rhizobium mesoamericanum"
                     /db_xref="taxon:1079800"
     Protein         1..374
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /function="1.4 : Pyruvate family"
                     /function="7.1 : Amino acids, peptides and amines"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38623
     Region          27..358
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(99..101,122..123,172,224,248)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkksllsava ltamvafsgn awadiivgva gpltgpnaaf gaqlqkgaeq aaadinaagg
       61 ingeqvkivl gddvsdpkqg isvankfaad gvkfvighfn sgvsipasev yaengmleit
      121 paatnpkfte rglwntfrtc grddqqgaia gkyladhfkd akiavvhdkt pygqgladet
      181 kkalnaagvt evlyeginvg dkdfsaliak mkeagvsiiy wgglhteagl iirqaadqgl
      241 katlvsgdgi vsnelasiag davagtlntf gpdptlnpan kdlvakfkaa gfnpeaytly
      301 syaalqtiag gakaagstda eavaaalkak gpfptvlgdm sfdekgdpkl pgyimyewkk
      361 gpdgkysyfp qeak
//
LOCUS       WP_007533873             365 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Rhodococcus
            triatomae].
ACCESSION   WP_007533873
VERSION     WP_007533873.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus triatomae
  ORGANISM  Rhodococcus triatomae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Rhodococcus triatomae"
                     /db_xref="taxon:300028"
     Protein         1..365
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37806
     Region          6..356
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mralrvrarl ahrgaafdie lgdgevlavl gpngagkstl lgliagllrp degvvtlgdr
       61 tltdtatgvv vpphdrgval lsqqpllfph mtaranvafa prsrglsrte agsvaeywlr
      121 evdatalanr rpsqlsggqa qriaiarala aqprllllde pmaaldvava palrkllrri
      181 lrdegrtavi vthdlldala ladrvavvea ghvvesgtvr evlatprsaf aariagvnil
      241 sgirigndsl etpwgvtvsg vdgpgatpig ssavalfrpa avavhtepph gsprncvavt
      301 vgelelhgaa vrvraeenpd gsaglaadvt pasvaeldla pgrrvffvvk aqevtlhpal
      361 appvq
//
LOCUS       WP_007536905             461 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Rhizobium mesoamericanum].
ACCESSION   WP_007536905
VERSION     WP_007536905.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium mesoamericanum
  ORGANISM  Rhizobium mesoamericanum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 461)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Rhizobium mesoamericanum"
                     /db_xref="taxon:1079800"
     Protein         1..461
                     /product="amidohydrolase family protein"
                     /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=48524
     Region          1..442
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 masellvvng qivtgdgsti hdigyvrvrg hqivevaags pnaavdaivi naagctvipg
       61 vinahahgci igpsmpsgsk pvpatdveyf rnrhllcgtt tllnvcglal pdeidgdgls
      121 rhpldihvtt ahtpsniraa meidgeglgd rhlmatieam idagakalge agggqtlggg
      181 aqdyrfipea vlaatgvrls prwarrlket ilgraldgds aapaevleem iaecglasii
      241 epkllvqlir ktvmppvals leglaeiaas cerfglpsif hhalptartl ialadrhpsa
      301 rivaahanhp sfepeecisy arelkkrgvv idvstldcii trwrnapani dllvaeglvd
      361 tlstdfaggd fdsilaavhr mvqrrhltla ravalstgnv arvfpelagd rgllaagkra
      421 diavveshnl arvrhlivng rltlqngmak eaafqdvahq p
//
LOCUS       WP_007537194             415 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Rhizobium
            mesoamericanum].
ACCESSION   WP_007537194
VERSION     WP_007537194.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium mesoamericanum
  ORGANISM  Rhizobium mesoamericanum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 415)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 415)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Rhizobium mesoamericanum"
                     /db_xref="taxon:1079800"
     Protein         1..415
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=45551
     Region          15..406
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 madfevhidl hgsmrrigla rgnrvrgaet ilfeydvawl edpdrfslep alaltrgafa
       61 ppaglatfgs igdsapdtwg rrlmqraerr laeresralr tlaesdyllg vadatrlgal
      121 rfrwvgdetf qapigadvpa midlgrllqi terilrdeet dedlqlifap gsslggarpk
      181 asvidqhghl siakfpketd sysmetweei alrlagqagi atpqhelvev agkavmlsrr
      241 fdrdgvirvp flsamammaa kdgdrgsype ivdalarhga qgktdahaly rrvvfnvlis
      301 nvddhlrnhg flwlgkagws lspvydlnpv ptdlkarvlt tnidldegtc sldllehasq
      361 yfgltltrar aiikevatvt atwretakav garsaeitrm asafehddlt ralal
//
LOCUS       WP_007539233             269 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Rhizobium].
ACCESSION   WP_007539233
VERSION     WP_007539233.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..269
                     /product="calcium-binding protein"
                     /function="16.15 : Symbiosis"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27855
     Region          <4..157
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mektvlggpg snnffgsngd dvmvdptgnd widggpgnds isagegndrv fggagndhvf
       61 gdegndylyg dmgrdkpril gtallggdnd klyggagddv lfagdgrdsl aggagqdtfa
      121 fqfhnpmagf dpnfgsdhts ivdfdraqds fafdavgfgv dgiaanfinh eahghqvdtf
      181 ysgpasgang ehvvvitdrg ftdgsaaara isgeaagdii ayfnddsmta nlgyvtseny
      241 vddfahlsnv esllhltslg ltasdftff
//
LOCUS       WP_007545682             353 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Sulfurihydrogenibium yellowstonense].
ACCESSION   WP_007545682
VERSION     WP_007545682.1
KEYWORDS    RefSeq.
SOURCE      Sulfurihydrogenibium yellowstonense
  ORGANISM  Sulfurihydrogenibium yellowstonense
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Sulfurihydrogenibium.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  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   3  (residues 1 to 353)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Sulfurihydrogenibium yellowstonense"
                     /db_xref="taxon:304736"
     Protein         1..353
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41090
     Region          151..345
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mpekkpvveg yqkaieklsg vdinaivfll fliliiilav lflnnlskkl kakyqysefv
       61 kyakekelsd eqvsilwdys kkmgrdpfla lefkspfekv vdlyikdnpn fnenlikdmr
      121 eklgfdvvps fvpitvtkdi dlfqggrikl edgrsfnvvl ydkdelymyw aitdknipnl
      181 nvgdrvkisf trksdgayvv evqiedilke sgtvilkiph tfeilrtqrr eyprvdtdie
      241 avlgkkired dkeiikwyig rildispsga rfcvsieekn tlnlrigdei iltftleekd
      301 fqltgdvvni yekqkiicyg ikfkeikesv qrdifsyvrk eqqkmlslyk kqs
//
LOCUS       WP_007545888             139 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein, partial [Sulfurihydrogenibium
            yellowstonense].
ACCESSION   WP_007545888
VERSION     WP_007545888.1
KEYWORDS    RefSeq.
SOURCE      Sulfurihydrogenibium yellowstonense
  ORGANISM  Sulfurihydrogenibium yellowstonense
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Hydrogenothermaceae; Sulfurihydrogenibium.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 139)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Sulfurihydrogenibium yellowstonense"
                     /db_xref="taxon:304736"
     Protein         <1..139
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <2..111
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 kinitenlls vvknykgfgl niaiddfgte hsnfdrlvyi dfnflklasv likdadknek
       61 klkmlevmnf laykfdtyli aegiesfeea kilsdlgidy hqgffyckpm snpleainiv
      121 anilnnqled klakslimk
//
LOCUS       WP_007548768              99 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Listeria fleischmannii].
ACCESSION   WP_007548768
VERSION     WP_007548768.1
KEYWORDS    RefSeq.
SOURCE      Listeria fleischmannii
  ORGANISM  Listeria fleischmannii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Listeria fleischmannii"
                     /db_xref="taxon:1069827"
     Protein         1..99
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11046
     Region          1..99
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(6..7,25..26,34,37,39..40,42,45..46,48,56,61,68)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(25,56..57,59,80)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 maskafidsv ysvikripkg kvttygqiay miqhpknarl vgnvlkhtdr tlnlpchrvv
       61 nsagrtvpgw peqitllqqe qvpfkkngcv dlkqsfwqg
//
LOCUS       WP_007553482             146 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Bartonella sp. DB5-6].
ACCESSION   WP_007553482
VERSION     WP_007553482.1
KEYWORDS    RefSeq.
SOURCE      Bartonella sp. DB5-6
  ORGANISM  Bartonella sp. DB5-6
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Bartonella sp. DB5-6"
                     /db_xref="taxon:1094755"
     Protein         1..146
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=15814
     Region          58..132
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mkkiacttlm svlmasstya qsftvpskpe missmgivqv gsdmsvryvt platdfvass
       61 liganvynle denigevkdi ilrenniagf viaiggflgi gesyvvvspe tiqmtndygk
      121 wklitnatkd slkeaptfky egrwar
//
LOCUS       WP_007553694             624 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Bartonella sp. DB5-6].
ACCESSION   WP_007553694
VERSION     WP_007553694.1
KEYWORDS    RefSeq.
SOURCE      Bartonella sp. DB5-6
  ORGANISM  Bartonella sp. DB5-6
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 624)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..624
                     /organism="Bartonella sp. DB5-6"
                     /db_xref="taxon:1094755"
     Protein         1..624
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=71223
     Region          57..556
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mssmekldsk svdiveqniq qlkqlfpevf segkikfdhl qellgnyvik dedhynftwh
       61 gkraasrlaq tpstgtlrpc kqesvdwdtt qnlfiegdnl evlkllqkpy hrqvkmiyid
      121 ppyntgndfv ykddfkdsvq nylattgqld negkkiatns ssagryhtnw lnmmyprlkl
      181 arnllrddgv ifisiddnea anlkklcdev fgeenfiaql iwrrrvssgm seqnvsidhe
      241 yvlcyqrsai sefmgkkksf neyknpdndp rgpwiadnlt vgmnasmrpn qaydltdpkt
      301 gnvfpynpnr vwayapdsme rlikegkilf padtnkrpml krfqnelksn ynpfssimtd
      361 ivglnteatr miqkilhgni fdyskpmsll ttllgqivak ddlildffag sgttahavmq
      421 lnaedggkrr cisvqlpelt dakseafkag ykniaeiske rlrragkkik eeqnakldln
      481 tnssidigfk vfkldssnik rweadfdtlg tdlidavdyl kkdrsnedll yeillkygid
      541 ltvsiemrli aeknvyiigl gtlivcldtd idmnvinsig alkeelqpei mrvifkddsf
      601 kddvvktnal iylkrygifd vksl
//
LOCUS       WP_007554839             649 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Dialister micraerophilus].
ACCESSION   WP_007554839
VERSION     WP_007554839.1
KEYWORDS    RefSeq.
SOURCE      Dialister micraerophilus
  ORGANISM  Dialister micraerophilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 649)
  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 649)
  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 649)
  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 649)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Dialister micraerophilus"
                     /db_xref="taxon:309120"
     Protein         1..649
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=68040
     Region          25..649
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 madldtnakk inkkgkdlqe tlkeldkesn faeysgiwak lialicivfs lfqiytglfg
       61 vldamiqrci hlsfgialvf llnptkrswv kkgqihlldl glailsvvps cyilvqyksl
      121 ilragtvtpl davmgvlglv mvieaarriv gmpivcvvla fmaygflgpy mpgalahrgl
      181 tinqmvghlf fttegvfgip mgvsstfifl filfgaylek tglgkffidi anaiagwasg
      241 gpakvavlss alegtisgss vanvvgsgaf tipmmkklgy eknfagavea aastggqimp
      301 pimgaaaflm aefvgipyme vvkaaivpai lyfigvflgv hfeakrnnlk gtprsqlpsf
      361 gkimkeqghl aiplvviigl lssgytpmka alwgifisig tamlrantrm kmsdiigglv
      421 qgargclgvl iacaaagiii givtktgvgl kmastlvqla sgnfllllic tmltslilgm
      481 gvpttanyvi tstivapalv gagvpilaah mfvfyfgiia ditppvalaa yagsaiaggn
      541 pmktavnask lgiaafiipy vfvfspvllg inatitgmif stltaligma glsgamigqf
      601 adkckvweri vltigglcli dpklmtdvag iallaivgii qymrkkkaa
//
LOCUS       WP_007556161             380 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Dialister micraerophilus].
ACCESSION   WP_007556161
VERSION     WP_007556161.1
KEYWORDS    RefSeq.
SOURCE      Dialister micraerophilus
  ORGANISM  Dialister micraerophilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Dialister micraerophilus"
                     /db_xref="taxon:309120"
     Protein         1..380
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43132
     Region          1..270
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          267..>315
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkfihtadwh igklfygeyl teeqewilkn rflplvddek pdvvllagdv ydrsvppsea
       61 velldemiye ivgrrkipfi visgnhdssq rlsfggrlme sgglfmvgdi krsvkpivle
      121 dewgavafap ipyaepgtvr tvmkdetvkt heesvlslsn yllskidkni rkiaithefv
      181 aggstsdser plsiggtdli raeifkpyny talghlhspq ragfdnvrys gsllkysfse
      241 vtqkkgvivg elskdgevkt kfvplkprrd vriitglfed lmkneslftd dflqieltnd
      301 gpvidamarl rthfpyvmal qtkkrvqtge garnfdfkkr vnpidmmktf vdefrdepmn
      361 kteaeymqki feelkggefd
//
LOCUS       WP_007558569             423 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Phocaeicola
            plebeius].
ACCESSION   WP_007558569
VERSION     WP_007558569.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 423)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 423)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..423
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48250
     Region          2..415
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mkklyvfadf dwlkeprlvg elsyeslrgs dsygfcysne wlkdygslfl sddlnnypgq
       61 qytapdkdif gcfsdalpdr wgrtlinrre qilakdekrp vrrlssfdyl igiedfsrmg
      121 gfrfkesmdg dyinasetlr ippltdirel iaasseieks eeedqlpemr wiaqlvqpgs
      181 slggarpkas vldenknlci akfpsrkddy daglwehish llakkagina aetrvistnd
      241 kyhtllsrrf drledgrrih fasamtllgl ndganantgn gyldivdfii qnctnvednl
      301 kelyrrvafn icigntddhf rnhgflltvk gwtlspaydm nptvneyqsl linsytnksd
      361 lkelldscee ymlpketagq iigevlntvm ewrtlatklg iakseqerfa avfekqiily
      421 dcm
//
LOCUS       WP_007558617             338 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [Methylobacterium].
ACCESSION   WP_007558617
VERSION     WP_007558617.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium
  ORGANISM  Methylobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae.
REFERENCE   1  (residues 1 to 338)
  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 338)
  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 338)
  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 338)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Methylobacterium"
                     /db_xref="taxon:407"
     Protein         1..338
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=37212
     Region          8..336
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mrhtrfsrrs llagaaavpv fgiltrrgqa aefsyklatg qdpthpvnvr aqealdrire
       61 atggrleikl fpanqlgsdt dllaqvrngs veffnlatsi latfvpaasl pntgfafkdy
      121 davwaamdgg lgdyvraeia ktpiltvskv wdngfrqits streirtped lkgfkirvpp
      181 apmltslfka ldagaapinf nelysalqtk vvegqenpla itatarlyev qkscsltghv
      241 wdgywilgnk kawqrlpedl rrtvsseldr sgtdqradva klslslresl takgisfvdv
      301 drarfrealg rtsfyrdwka kygdaawshl edvsgklt
//
LOCUS       WP_007558701              98 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein
            [Methylobacterium].
ACCESSION   WP_007558701
VERSION     WP_007558701.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium
  ORGANISM  Methylobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Methylobacterium"
                     /db_xref="taxon:407"
     Protein         1..98
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10590
     Region          1..96
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mdshaalail raneaelrrr gvrhaalfgs vargearads dldvmieida pvvggvygyv
       61 glcrfigdlf pirvdvanra glkdrirera erdalvaf
//
LOCUS       WP_007558873             193 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Methylobacterium].
ACCESSION   WP_007558873
VERSION     WP_007558873.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium
  ORGANISM  Methylobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Methylobacterium"
                     /db_xref="taxon:407"
     Protein         1..193
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=20966
     Region          1..163
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlrrlyawil alsgrpsapy vlgavafaes sffpvppdam lvpmavsrpd rvwlyatiat
       61 vasvlgglvg yaigallfds vgewlirlyg lqnsaatfqd syaryghwvi llkgltpipy
      121 klvtitsgfa hyslfwftvl svitrgarff ilagllgryg vqirgvldrh lnavaaisva
      181 vvvlgfllfk vil
//
LOCUS       WP_007558885             440 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Phocaeicola plebeius].
ACCESSION   WP_007558885
VERSION     WP_007558885.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..440
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=49408
     Region          22..428
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mketlmnder ncfglnllha eeledavvga amletnslne iigfvrpemf ykkdnryiwe
       61 aiealvkagl qpdllmvahk laemgrleea ggpygvtrkt snlassahlw ehvhvvyefy
      121 lrrsvvesla krlgaaadrt qdiyevldgm mhdlmalreg spledhltnm kgmmektcar
      181 ivdrvsrsvn gvtgiptgip eldrmtggwq pgnliftagr prlgktqlgl kfamhaaekg
      241 yrvllytlem mteevgervl mmrvpdlykk vksgyvtsqe venlvdvakg medcrlmvdd
      301 tpyvsidqlc agartvksrw gldmvivdyl qlvgtnvrag rnreqevaec srrlkalara
      361 lecpvivacq lnrqveqtfd hrpelkhlre sgsieqdadl vlmlhrtdrn gdakrcgliv
      421 aknrhgevsk pnscmevelf
//
LOCUS       WP_007560155             154 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Phocaeicola].
ACCESSION   WP_007560155
VERSION     WP_007560155.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola
  ORGANISM  Phocaeicola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Phocaeicola"
                     /db_xref="taxon:909656"
     Protein         1..154
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17023
     Region          7..153
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdafiqflid wgywgmflsa flagtilpfs sevvllacig lgldpvwstl fttagnalgg
       61 ftcywigrig ktewiekyfk vdkkqmdkai rfihgrgswm affsflpvig dallialgfm
      121 rgnvwittia mtigklarya iivatalgvf rfig
//
LOCUS       WP_007560175             402 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Phocaeicola plebeius].
ACCESSION   WP_007560175
VERSION     WP_007560175.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 402)
  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 402)
  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
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 402)
  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   5  (residues 1 to 402)
  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   6  (residues 1 to 402)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 402)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 402)
  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 11973053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..402
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44290
     Region          <18..83
                     /region_name="COG3398"
                     /note="Predicted transcriptional regulator, contains two
                     HTH domains [Transcription]"
                     /db_xref="CDD:442625"
     Region          81..394
                     /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 mvqrlieglg sgtknmltqk riitylmhnh sstipdlakd idlsiptvtk fimelveegy
       61 imnygkqets egrppnlygl npdsaymvgv dikasclnig lmnftgdmvd vqmgvecrly
      121 ntlesleelt lhirnfidkh etvkerilqv gvnisgrvnp eegysfsmfn feerplaeil
      181 gekigipvsi dndtramayg ellkgavkge kdivfinisw glgsafiidg kiytgrsgfs
      241 gefghfsvfd neiicrcgkk gcletevsgs alhrilcekv ksgqssilsk riltgetslt
      301 leeivdatnk edilcielve eigrklgryl aglinlfnpe lvviggtlal tedyilqpik
      361 tairkyslnl vskdsavvls klqakagvvg acllsrsklf ew
//
LOCUS       WP_007560628             215 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Phocaeicola plebeius].
ACCESSION   WP_007560628
VERSION     WP_007560628.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..215
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23736
     Region          40..206
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mkkviysmlg agllclsscg gqtqteqtpa vdessaknqv ietimtrrsv rkylpqpvnr
       61 dtmqmildcg ihapngqnkq swavrvvdnp efingitevy kklnpkmaed pgfknmfrna
      121 ptvvfiandt sydmsqidcg llgenmilsa wsmgigsccl gspirfmkte pqaadylkrl
      181 nipegyelly ciafgypdes paakprdask vmfve
//
LOCUS       WP_007560372             672 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Methylobacterium].
ACCESSION   WP_007560372
VERSION     WP_007560372.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium
  ORGANISM  Methylobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae.
REFERENCE   1  (residues 1 to 672)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 672)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 672)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 672)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 672)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 672)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Methylobacterium"
                     /db_xref="taxon:407"
     Protein         1..672
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=71827
     Region          52..672
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msqtfapgva aqpvpaasda ppdsapaage tggtgpaqgp apggaldape kaetrhghag
       61 fwtllvgsvg vvygdigtsp lyafrealvp artdgillpe evigtvslil walflivtvk
      121 yvlillrmdn ngeggilslm alarkalggs rivfmlgllg aslfygdavi tpaisvlsav
      181 eglklvtpal ddyvlpitvt iivalflvqn rgtakvaaff gpmtivwfla malaalphig
      241 lhpevfraan pwyavhyllg hgtgalvalg avflavtgae alfadlghfg rkpiqvawvc
      301 lvfpalalny lgqaalvlek pdtadpffql vpawgllpmv vlatlatvva sqavitgafs
      361 lsrqaiqlgl lprleirhts eshagqiylp qinallmigv vllavlfkts sslasaygia
      421 vtgtmlltas mtflviwrmw gwspvaaalv mlpfivvefl fllsnlikvv eggyvplila
      481 gglvilmwtw vrgvtilfnk trktdvplve lvgmlekspp hhvrgtavfl tsdpeiapaa
      541 llhnlkhnkv lheknviltv etvdtprsne adkvriepvg phffrvvmkf gymetpnipk
      601 tlvllrrqgf kfdimatsff lsrrsirpat hsgmplwqdr ifitlaknan datdffqipt
      661 grvvevgtqv tv
//
LOCUS       WP_007561700             259 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Methylobacterium sp. GXF4].
ACCESSION   WP_007561700
VERSION     WP_007561700.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium sp. GXF4
  ORGANISM  Methylobacterium sp. GXF4
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Methylobacterium sp. GXF4"
                     /db_xref="taxon:1096546"
     Protein         1..259
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=28363
     Region          19..240
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mtkdkgcrac rdgaaldfdf tmafqpivdv gsghvwayea lvrgpngepa gtildrvtda
       61 tryqfdqaar vkaielagrl lprdsdtrls infmpnavye pnacirasle aarrvdfsyr
      121 rimfefteqe rfqdiehvkr ivaayrqqgf ltalddfgag faglnllanf rpdlikidme
      181 lvrgidtdsg rhaivagiia iaralgvtvl aegietaser dalrglgitl mqgyhfakpq
      241 lealpevegf tpraaaraa
//
LOCUS       WP_007562445             337 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Methylobacterium sp. GXF4].
ACCESSION   WP_007562445
VERSION     WP_007562445.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium sp. GXF4
  ORGANISM  Methylobacterium sp. GXF4
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 337)
  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 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   3  (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   4  (residues 1 to 337)
  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 337)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Methylobacterium sp. GXF4"
                     /db_xref="taxon:1096546"
     Protein         1..337
                     /product="CmpA/NrtA family 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=35555
     Region          3..250
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mrlqlgyvpl cdaapliaah efgfarsegl eldlsaepsw atlrdrlalg hldgahmlap
       61 lalasrlals gppsdlivpl qlsangnait vsrdlwaama pasegladva rafarvaaer
      121 rdagrpltlg tvhpfschsy qlrlfaeagg ldpaafrtvv vppqhsveal arglvdgyca
      181 gapwnavava aghgriaalg cdlapdapek vlavsarldg atlplvrava raghwcanpd
      241 nradlvhrla hrtylnldvd lidrafrsva vldaagatrp mpgpldvgar vqeprveavr
      301 wlvaqmrasr qipqdgrpev eaaavfrpdl yraamav
//
LOCUS       WP_007564003             492 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Methylobacterium].
ACCESSION   WP_007564003
VERSION     WP_007564003.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium
  ORGANISM  Methylobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Methylobacterium"
                     /db_xref="taxon:407"
     Protein         1..492
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50038
     Region          <5..190
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          198..417
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mthqsttqsa aqdqasqlsl gddqlfigsh gqdafpgtgq mdiafgrdgn dylagqgqnd
       61 dllggngrdv ltggagmdhl dggngadvli gnggddelrg aqgndylneg vghgdleggp
      121 gndiltggpg gdafdispgs gndvitdfsa gpgildhiav qgltpedltf qdtklgalis
      181 wdvaagagsv llegvqkadl aqddfmftdd rqviqptdpn athvsteisn ittepgdvtp
      241 ptsgadtgsg eairfdefnv ragteqadtf qgtdardyyv ggggndklfg aagdddlrgg
      301 ngndvlvgga gqdhlmgeag ndklyggpdn dnlmggagqd qlyagaghdm ldggqgndil
      361 nggdgadayi vrpgsgndiv tagfdagpga fdhiafeggi tpndvtiadq tsthgddhsg
      421 tlvswetsqg dgslflegvt ksqmaqddfm fgadtareaq ftndptitse gseyifrgae
      481 tsaagdpnht ya
//
LOCUS       WP_007564491             588 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Methylobacterium sp. GXF4].
ACCESSION   WP_007564491
VERSION     WP_007564491.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium sp. GXF4
  ORGANISM  Methylobacterium sp. GXF4
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 588)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Methylobacterium sp. GXF4"
                     /db_xref="taxon:1096546"
     Protein         1..588
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=61290
     Region          2..586
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mhlvgratpl drlesaltdl rlrlagprtp padlavvaid detvrreggf pvsrstmarl
       61 ietiadanpr viavdvlfld vgrqpeadra laaalgktna vlasaavfdg sasedgipva
      121 aavhrptpei gervasglvn vtedaagvpr hlplivrtse gasaafvlra aalaarsdpv
      181 ltkgrvqigt aaipldlgyh lplrpygprr tiatvsaasl ldgtapaaal adrivvigat
      241 algggdtfvt afdpvmpgve llatgiahlt tghglvrdaa vrrldaaaal vlsvgaalli
      301 allppgpgmm lvllltagwl vagavafahg lwlsaalpla aaglptllca agrqtlerrq
      361 sakvarseev lrrlqpaala drlaldpayl aepvardipv lfvdltgftr rsehlgpvrt
      421 rgmlkafhdl vdetvtghrg lvvnfmgdga milfgaldpd pdqasnavea aedlisrtrl
      481 wiarnpalse agpaldvrig ahygpvilsr lgsdtnqhit atgdtvnvas rllavaaqan
      541 arlalsaelt eaaglalseg tferrrtsir grtqtlevwl rhrreths
//
LOCUS       WP_007564830             400 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Phocaeicola coprocola].
ACCESSION   WP_007564830
VERSION     WP_007564830.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola coprocola
  ORGANISM  Phocaeicola coprocola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 400)
  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 400)
  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
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   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   5  (residues 1 to 400)
  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   6  (residues 1 to 400)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 400)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 400)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Phocaeicola coprocola"
                     /db_xref="taxon:310298"
     Protein         1..400
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44625
     Region          22..62
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          81..392
                     /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 mkerlleeiq kgskgavmkk hiityliyne nstitdlakd mdlsiptvtk iidemheqgy
       61 ideygkletn ggrhpilygl ntdsgyfvgv dvtwnsinig iinfkgevlk lqmgipferr
      121 dtlecidelc nhiehfiagl tidekkilhi nvtlcgrvnp elgyihsffn fgerplaeil
      181 terlkietsi dndsrtmlyg enikgvvkgv knvlfinigw glgmgimidg klykgksgfs
      241 geightygyd nqiichcgkk gcvetevscs alyrkfiehl qagetsiils ekdieeitld
      301 difsainred llaielveqi gqqlgfhigs lintfnpdmv iiggemsrag dfllqpvisa
      361 irkytlslms rdseivlskl kdqacvigsc llsrsklfea
//
LOCUS       WP_007566178             163 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein
            [Methylobacterium].
ACCESSION   WP_007566178
VERSION     WP_007566178.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium
  ORGANISM  Methylobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Methylobacterium"
                     /db_xref="taxon:407"
     Protein         1..163
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=15852
     Region          76..137
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mrksllllpl allslaglpa raqdasvign ktvlpgtgpg tstggagggp ltiaasaeaa
       61 vkrqgvkpat vlashligvt vrnaagdkvg tvddlliadg galkavvldv ggplglgskr
      121 iavepgalvl rpggerfsav lhmstdtvaa aqpfdpvkam aae
//
LOCUS       WP_007567609             127 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein
            [Methylobacterium].
ACCESSION   WP_007567609
VERSION     WP_007567609.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium
  ORGANISM  Methylobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Methylobacterium"
                     /db_xref="taxon:407"
     Protein         1..127
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=14064
     Region          16..92
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 maanpqpaar qprsliasdr vigtdvrrpd gskvgrierl mldkisgrva yavmsfggfl
       61 glgeefytlp wsvlhfepeq dayvlditee qlraapartp egtdpaedga weeqihryyd
      121 aapywgi
//
LOCUS       WP_007567993             144 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein
            [Methylobacterium].
ACCESSION   WP_007567993
VERSION     WP_007567993.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium
  ORGANISM  Methylobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Methylobacterium"
                     /db_xref="taxon:407"
     Protein         1..144
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=15277
     Region          35..111
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mptdlptert vrktgtleld ptgegiaide tarliasnkv egtavydreg khlgavynfm
       61 vdkvtgqvay avlafggflg lgenhhplpw kaltystelg gyvvdidpgn lagapshgpg
      121 edafadpnyr gkiedyygvr aptl
//
LOCUS       WP_007569937             281 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase, partial [Phocaeicola
            coprocola].
ACCESSION   WP_007569937
VERSION     WP_007569937.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola coprocola
  ORGANISM  Phocaeicola coprocola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Phocaeicola coprocola"
                     /db_xref="taxon:310298"
     Protein         1..>281
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
     Region          66..>281
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mkpnklelns vdgtqlnlea lyqiapscft evkddktgel rhvvnfktlr qllgdnaved
       61 ademyqftwp gkqearreaa rpttktlrpv vedsvdwdnt qnlyiegdnl evlkllqksy
      121 mgkvkmiyid ppyntgndfv ydddfavsqd dydlfsgnvd elgnryrknt esngrfhsdw
      181 csmmyprlmv aksllsdsgs ifltlddhei vngrklmdei fgeksfistv iwenfygrsn
      241 aaaislahny iliyskagee wknirnllpr dlkssekykn p
//
LOCUS       WP_007570355             151 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Phocaeicola].
ACCESSION   WP_007570355
VERSION     WP_007570355.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola
  ORGANISM  Phocaeicola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 151)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Phocaeicola"
                     /db_xref="taxon:909656"
     Protein         1..151
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17528
     Region          72..151
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mhlisesleq frfyksgiis hlcnflllqi tdilcqnnqe vsicikrtde ifrnfkklss
       61 hnyrkhhdil fyannlnist tylsrivkni tghtvhfhis ellcteakrl ldttdmgike
      121 iadeldfsdq svfgkffvka tgvsplkyrk r
//
LOCUS       WP_007571351              99 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Patulibacter medicamentivorans].
ACCESSION   WP_007571351
VERSION     WP_007571351.1
KEYWORDS    RefSeq.
SOURCE      Patulibacter medicamentivorans
  ORGANISM  Patulibacter medicamentivorans
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia;
            Solirubrobacterales; Patulibacteraceae; Patulibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Patulibacter medicamentivorans"
                     /db_xref="taxon:1097667"
     Protein         1..99
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10895
     Region          1..87
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(25,49..50,52,72)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 madeqrtrri ldgvraipeg yvrtygdldp laprlvgril retdedvpwh rvvradgsla
       61 mggeqrarlr aegvpirggr vdladarlpl ppgehlelp
//
LOCUS       WP_007571868             402 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Phocaeicola coprocola].
ACCESSION   WP_007571868
VERSION     WP_007571868.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola coprocola
  ORGANISM  Phocaeicola coprocola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 402)
  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 402)
  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
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 402)
  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   5  (residues 1 to 402)
  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   6  (residues 1 to 402)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 402)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 402)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Phocaeicola coprocola"
                     /db_xref="taxon:310298"
     Protein         1..402
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44429
     Region          18..61
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          83..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 mtrklleeie rgsknaltkk riityymynr sstipdlske ldlsvptvtk fimemcdegy
       61 imsygkqets egrpptlygl tsdsgyfigv dikkfslnig lmnfvgdfvd lkmgipyete
      121 nspeglnklc gyitdfinha nidkekilni gvnisgrvnp elgysfslfn feerplaeim
      181 tekigykvti dndtramtyg emvkglvkge kniifinlsw glgaglving diftgksgfs
      241 gefghfnvfd neilchcgkr gcletevsga alhrklvqcv qdgkqsilsk rilhgdtslt
      301 ldeiisatnk edllcielve eigqklgryl aglinllnpe lviiggvlaq tgdyilqpik
      361 savrkyslnl vnkdsvials klldkagvig acmlsrrsmf es
//
LOCUS       WP_007572103             501 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Patulibacter medicamentivorans].
ACCESSION   WP_007572103
VERSION     WP_007572103.1
KEYWORDS    RefSeq.
SOURCE      Patulibacter medicamentivorans
  ORGANISM  Patulibacter medicamentivorans
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia;
            Solirubrobacterales; Patulibacteraceae; Patulibacter.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Patulibacter medicamentivorans"
                     /db_xref="taxon:1097667"
     Protein         1..501
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50656
     Region          56..238
                     /region_name="choice_anch_P"
                     /note="choice-of-anchor P family protein; NF040603"
                     /db_xref="CDD:468576"
     Region          <320..>434
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mtgtllllla llavprgafa atdttaawqc rasgiyasia nmpapveplv angikgstpg
       61 ltfdkplcss deqgagntgg avpivdgllf asaaqaktti tpqtgapkaq svtasttlaq
      121 vnlkpaglae llsvgaikat atatckagkp efngtsiltd lkvlgapvsl dglvsalkga
      181 vdglglgalv aidtpnkivk tangivvqpl rirvaptags pngglldivi getkigasgd
      241 vcnsdgppkp pnpedqicpt gsvpqgrepi vcvipgtdry gvivigvpns tdtprggtvi
      301 plvearrlag lgqlpkskcl ygpgndyvvv gtakgdkiyg trgpdrilgl ggsdklygvd
      361 gndcldgnag adriyggegn driygaaggd rlyggngndr iygdagndsi hgdpgndrls
      421 ggagndfftt gtstkagger vftgpatskg rnivsisiyt kpvvvncgss rdvvrankne
      481 arnnrlrnck hvevttptkk r
//
LOCUS       WP_007572342             345 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Patulibacter medicamentivorans].
ACCESSION   WP_007572342
VERSION     WP_007572342.1
KEYWORDS    RefSeq.
SOURCE      Patulibacter medicamentivorans
  ORGANISM  Patulibacter medicamentivorans
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia;
            Solirubrobacterales; Patulibacteraceae; Patulibacter.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Magnet,S., Arbeloa,A., Mainardi,J.L., Hugonnet,J.E., Fourgeaud,M.,
            Dubost,L., Marie,A., Delfosse,V., Mayer,C., Rice,L.B. and Arthur,M.
  TITLE     Specificity of L,D-transpeptidases from gram-positive bacteria
            producing different peptidoglycan chemotypes
  JOURNAL   J Biol Chem 282 (18), 13151-13159 (2007)
   PUBMED   17311917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19799648
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Patulibacter medicamentivorans"
                     /db_xref="taxon:1097667"
     Protein         1..345
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=36811
     Region          21..>286
                     /region_name="YoaR"
                     /note="Vancomycin resistance protein YoaR (function
                     unknown), contains peptidoglycan-binding and VanW domains
                     [Defense mechanisms]; COG2720"
                     /db_xref="CDD:442033"
     Region          219..344
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mrqrtviala svllvlllac ggvlvadaat gkkipagvki ggvdvgglsa gdarakvqae
       61 ivdklrqpir vvhsdkewtl taktakvrvd idgaireamr tadegnafsr vyrritggtv
      121 dreiettssy srasisrlmd rvarglerdp qeasvtldag kldvhpgrvg lrldrsrvss
      181 lvrkavldps aphqvsaytr krqpktttad vrkkystalv anrstfkltl yknlrpvtty
      241 gisvgsvghd tpagqytign kaenpawhvp nsawagklag tvvppgpsnp ikarwlgiyd
      301 gvgihgtsdd asigtnashg clrmhvpdvi alyprvpvgt piwii
//
LOCUS       WP_007573337             404 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Hallella multisaccharivorax].
ACCESSION   WP_007573337
VERSION     WP_007573337.1
KEYWORDS    RefSeq.
SOURCE      Hallella multisaccharivorax
  ORGANISM  Hallella multisaccharivorax
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hallella.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Hallella multisaccharivorax"
                     /db_xref="taxon:310514"
     Protein         1..404
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44455
     Region          1..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkilvlncgs ssikyklydm tnesvlaqgg verigiedaf ikvklpngek rqimadlpth
       61 kegvalvfkc lldpeigaik sldeigavgh rivqggdlfe kscivtpeve kgieslidla
      121 pvhnkghlag ikavdelmpd vpqvtvfdna fhstmpdyay lyaipyewyt kyhvrrygfh
      181 gtshryvshr vceflgvdik kqkiitchig ngasvaaiky gkvidtsmgl tplaglmmgs
      241 rsgdidpsav cymmeksgmt phdmseylnk qsgvlgvagi ssdmrdnena dnegnkmahl
      301 alqmynyrik kyigayaaam ngvdiivwta gvgenqegvr wdscqgleyl gvkmdkernh
      361 vrskeqilsa ddskvkvvmi ptdeeiviar dtlalingre psdf
//
LOCUS       WP_007573143             340 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Patulibacter
            medicamentivorans].
ACCESSION   WP_007573143
VERSION     WP_007573143.1
KEYWORDS    RefSeq.
SOURCE      Patulibacter medicamentivorans
  ORGANISM  Patulibacter medicamentivorans
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia;
            Solirubrobacterales; Patulibacteraceae; Patulibacter.
REFERENCE   1  (residues 1 to 340)
  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 340)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 340)
  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   4  (residues 1 to 340)
  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 340)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Patulibacter medicamentivorans"
                     /db_xref="taxon:1097667"
     Protein         1..340
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36733
     Region          19..201
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          244..327
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mvppsviagl lqqagerrid papwfrglgi saahcevatt risyrqaaei irralaslpg
       61 eplglhvgtr dplvsfgvlg fammscrtvg ealaiglehh qaagslvdvs tdvrdgrvvv
      121 rvherfpdps llpflceeaf asmilvtrai vgrslsplsv elaypapsya aayrrifnce
      181 vrfdsdanrl tidagvlaap vrrhdpanla valaacreql igtaatndlv atverllrea
      241 hgerpsaaev aerlhisvrg lrrqlaasde tftsirnrvl eqraramlsd prrppvaava
      301 ddlgfsdsre frrafrrwtg iapsdarsga rrtadggera
//
LOCUS       WP_007575038             389 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Patulibacter
            medicamentivorans].
ACCESSION   WP_007575038
VERSION     WP_007575038.1
KEYWORDS    RefSeq.
SOURCE      Patulibacter medicamentivorans
  ORGANISM  Patulibacter medicamentivorans
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia;
            Solirubrobacterales; Patulibacteraceae; Patulibacter.
REFERENCE   1  (residues 1 to 389)
  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 389)
  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
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 389)
  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   5  (residues 1 to 389)
  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   6  (residues 1 to 389)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 389)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 389)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Patulibacter medicamentivorans"
                     /db_xref="taxon:1097667"
     Protein         1..389
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39182
     Region          <2..55
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          65..364
                     /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 midalrqspe itradvadrt glsratvsal vrdlerdglv evvagtangt rtgrrpevlr
       61 ltrragavlg vdfghehvrv avgdlagrtl sthqepvdvd hgmdaalaaa rrladraiae
      121 sgirptdvia cgagvpgpvd rlsgrigstm mlpgwsgttl avaleaqlgv pvvvdndanl
      181 galgeqtaga avgiddviyv kvssgvgagl isggnvlhgg tgiageighv avvpngvpcr
      241 cggrgcletv asapavrrql hatagdeipa ddlvaalatg dprvarllad agralgrvla
      301 sachlldpsa ivlggdpafa tdpvlagvre eldrhrlpgs gsgvqlvpar lgdlgqvvga
      361 lrlaaalpdr ripivphdqq pvppgggat
//
LOCUS       WP_007575616             152 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Hallella multisaccharivorax].
ACCESSION   WP_007575616
VERSION     WP_007575616.1
KEYWORDS    RefSeq.
SOURCE      Hallella multisaccharivorax
  ORGANISM  Hallella multisaccharivorax
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hallella.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Hallella multisaccharivorax"
                     /db_xref="taxon:310514"
     Protein         1..152
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16260
     Region          8..150
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 msqaltdfll dygywgmlla aflagsvfpf sseavmlgll aaglkpepli vygtvgnvlg
       61 slfnygvgrl grldwieryl hvkkanldka qrfmaghgaw igffaflpli gsaitvclgl
      121 mranivittv sitigkllry ivlvygagll as
//
LOCUS       WP_007576014             264 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Hallella multisaccharivorax].
ACCESSION   WP_007576014
VERSION     WP_007576014.1
KEYWORDS    RefSeq.
SOURCE      Hallella multisaccharivorax
  ORGANISM  Hallella multisaccharivorax
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hallella.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Hallella multisaccharivorax"
                     /db_xref="taxon:310514"
     Protein         1..264
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29337
     Region          <41..184
                     /region_name="valS"
                     /note="valyl-tRNA synthetase; Provisional; PRK14900"
                     /db_xref="CDD:237855"
     Region          181..257
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mkrivillls lmgvaltssa qtftqhlrqq qtgkgkitit qtkeidnlvn gnvsetvspq
       61 qktpaqpvkt apqtvkttpq sdrtaksdsl qklrdrqkae eekkkqaeka nedrraieea
      121 iamqkratek aadekaaeek rqaaersaae kraaeeaaed elhiptvdmr kkvmrgahkv
      181 tgyrvqafag gntradkika qqagnaikmr fpdqpiyvhf ysprwicrvg nyrtlgeaeq
      241 mlhsvkalgy ksaiivkgki tvfn
//
LOCUS       WP_007578777             424 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Paraburkholderia hospita].
ACCESSION   WP_007578777
VERSION     WP_007578777.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia hospita
  ORGANISM  Paraburkholderia hospita
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 424)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Paraburkholderia hospita"
                     /db_xref="taxon:169430"
     Protein         1..424
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=46399
     Region          35..254
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 msmieldppg fqpprpvagd egsrrtvryg gytvfsvfqp vfsvshrrai gyhaslrahd
       61 enerqvpsae vftqaarrgd llelgrlaes lhlgnfnafd shdewlflsl hpaalmdtsy
      121 gdallaglks lglppqrvvl evseqagget trfaeiidal rksgfliald gfgakhsnid
      181 rvwnlrpdiv tldrcilaqa sehshiervl pgivsmlhes gqlvlmgglt terdaliale
      241 cnvdfvqgtf faapsvepva rqatvslmdr llaalrerva areraqaerl apfvtaleaa
      301 stqlvegkpm aeatapllel retarcflld gsgrqigdnv lpqgrasqra krfrpllhse
      361 gaswerrpyf iqavrapgqv hltppylsin eahlcvtasi aaetargmqv lcvdinweva
      421 ahrn
//
LOCUS       WP_007579399             365 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Paraburkholderia hospita].
ACCESSION   WP_007579399
VERSION     WP_007579399.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia hospita
  ORGANISM  Paraburkholderia hospita
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 365)
  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 365)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 365)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 365)
  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   5  (residues 1 to 365)
  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   6  (residues 1 to 365)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Paraburkholderia hospita"
                     /db_xref="taxon:169430"
     Protein         1..365
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40041
     Region          43..230
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          123..363
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mqqrapahaa athqhapsvi gwrekrfaps klvalldvts eagidanavl agteldagav
       61 anpftltssl qfltaagnav rlcerpdlgv rvgcrlhass ygmygyallc sealaqtfdt
      121 avkyhqlang mldirwfehd daaswvfpnr devrmpdige plyrflidlq favhvtvikd
      181 vmgawcvpar alftqaqpph aamlsdvlec plafdqpqnl lsypaawlsr apqlanpita
      241 aqvstqcarl veqfrwqagv trrvyqeltr tpgkfpdieq iaeslcmtsr tlrrkleaeg
      301 asyselltgv rkalavdyls tttlsiedia vtlgfsdavs frhafkrwtg ktpndvrrdr
      361 gaalp
//
LOCUS       WP_007580414             361 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Paraburkholderia].
ACCESSION   WP_007580414
VERSION     WP_007580414.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 361)
  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 361)
  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 361)
  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 12807598
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..361
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=36129
     Region          38..102
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          39..361
                     /region_name="PRK10856"
                     /note="cytoskeleton protein RodZ"
                     /db_xref="CDD:236776"
     Region          286..348
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 msepqhpqph dmdthsdrpl paavpaavpt gfdslgavga rlaqlreskg wsvedvsarl
       61 kvspgklrgl eagdltqlpd ttfalgvlrs yakmvgadpa pmtqalrrek gvpepaltmp
      121 asagtdlprg kvslslggga prrrswmwgv alavvvlial amwhtnngds tawlarlkgi
      181 agsaasteta sssaaqaasg savtgeisas dsaaqtdtqa aaegasatpm ptplpmagva
      241 pastvasast paaaapkaas aapavaaaas asespvapeg sstvalsvkq dswfsvrqkd
      301 gkevfsglvh ageskevsgv pplkvtlgnk agldsitldg qpvdpakyvs akgnvarfal
      361 p
//
LOCUS       WP_007580508             144 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [unclassified Pseudoalteromonas].
ACCESSION   WP_007580508
VERSION     WP_007580508.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..144
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15895
     Region          3..140
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlyltlfisa fisatllpss sevimvgmia qgkvnlwlmw cvatlgnvlg scvnywlgtq
       61 vlrfkdkkwf pvsqkgldsa qkqfnkygvy sllfawlpvv gdpltviggi fkvrfsmfll
      121 lvtlgkgary lavialtvgf eklf
//
LOCUS       WP_007580710             199 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase
            [Paraburkholderia].
ACCESSION   WP_007580710
VERSION     WP_007580710.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..199
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21325
     Region          8..195
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 metraaaprr livaitgatg aiygvrllqt lrklggvesh llissagwln iqhelqlsre
       61 dvhpladvvh svrdvgasia sgsfstdgmi iapcsmktla svahglsdnl itraadvtlk
      121 errrlvlmvr etpfnlahlr nmtavtemgg vifpplpafy nrpetidqmv ddtvarvldl
      181 falgpalapa wqglnspsq
//
LOCUS       WP_007580729             101 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Pseudoalteromonas sp. BSi20429].
ACCESSION   WP_007580729
VERSION     WP_007580729.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. BSi20429
  ORGANISM  Pseudoalteromonas sp. BSi20429
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Pseudoalteromonas sp. BSi20429"
                     /db_xref="taxon:1097676"
     Protein         1..101
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11132
     Region          9..99
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(24,55..56,58,84)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(24..25,33,36,38..39,41,44..45,47,55,60,66)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mdidketliy tviagipvgk vasygqvaal agypqnsrlv grllkmmpnd svipwhrvvn
       61 sqgkisfpag sekyqeqhek llsegvlfks dkvnmrdcrl e
//
LOCUS       WP_007579939             718 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Pseudoalteromonas sp.
            BSi20429].
ACCESSION   WP_007579939
VERSION     WP_007579939.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. BSi20429
  ORGANISM  Pseudoalteromonas sp. BSi20429
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 718)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..718
                     /organism="Pseudoalteromonas sp. BSi20429"
                     /db_xref="taxon:1097676"
     Protein         1..718
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=79238
     Region          8..718
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mnpkflvstl atavalsfsa taiakdtsnk eqrfeqitvi gseqaindip gsatfisdee
       61 lqkfkftdis rvlasvpgvy vqeedgyglr pnigmrgtgt grndkisvme dgvlvapapy
      121 sapsayyfpt tgrmesievl kgaasvkygp rttggvlnll srslptepns skgmvdaalg
      181 gdgyykghay fgkeknntag lievftygad gfkelpvgnd ntgfektdll lkfghtfgqn
      241 dahnlelkik ysdetsdety mgltdedyqe spyrryaasq ndemntrhna yqlnyayrfg
      301 dgyeflatay lndfhrnwyk askvsesyle qysefeanpt segiegigik annrdyqakg
      361 iqselhipag dhyvtvgvry hedemdrfqw edkytlnqdl sltlteqgvp gsdsnrvdsa
      421 eastlfiqde wtidalvvsa glryeditit reewsksdpt rsngltkdvs ndteilvpsl
      481 gatytlnenv tllagiqkgy apaapgnadq eeeesvnief gsrfnmdgfs geviafysdy
      541 nnmhgnctaa vgcsddnigd qynygeveva gfefsaartf atdtamfpvk ltytytdsef
      601 kndfdseiwg tvekgdampy vpenqvalsl gaefsafvvn sqiryvsdah anltqsglna
      661 idsrvvwdla akylidenqk vylsvdnlfd ktyvanrsng giqpgkprtv qmgytysf
//
LOCUS       WP_007581257             255 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_007581257
VERSION     WP_007581257.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 255)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..255
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=28929
     Region          25..242
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 msekskdcek vtcsncadan dlefdfsmaf qpiincktnl iygyealvrg lngesaysii
       61 skvnednrya fdqlcrikai qlasklgits mlsinflpna iykpercirt tleaakkynf
      121 piqnimfeft evekiedtah ikrivdyyqs lgfktatddf gagysglnll adfqtdiikl
      181 dmalirdisn dkkrqlivth clnmfrdlni ialaegietv eeytwlknag velmqgylfa
      241 kpsfenlpev tyvfn
//
LOCUS       WP_007583128             211 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Pseudoalteromonas sp. BSi20429].
ACCESSION   WP_007583128
VERSION     WP_007583128.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. BSi20429
  ORGANISM  Pseudoalteromonas sp. BSi20429
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Pseudoalteromonas sp. BSi20429"
                     /db_xref="taxon:1097676"
     Protein         1..211
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23913
     Region          125..201
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mllfgtacsv speiktideq pqsnspdyvs italelaqlk daamqwqqar egierilrle
       61 keitylvnhi diinskaiaq snqgyssksv rsprntrnvk srqqvkqnys nkkqtvklnk
      121 pkhvfalqva svdseqgvak awqelntkaa plfrdkiltn vetakindkm fyrlklgsyq
      181 nfknakadcd vfklykldci vsnytdkpvr l
//
LOCUS       WP_007583909             210 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Paraburkholderia hospita].
ACCESSION   WP_007583909
VERSION     WP_007583909.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia hospita
  ORGANISM  Paraburkholderia hospita
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Paraburkholderia hospita"
                     /db_xref="taxon:169430"
     Protein         1..210
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=22452
     Region          8..195
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mteranrkpr ivvgisgasg amigvrllaa lrrigtheth livsasgait aaqelgltrs
       61 dldgladith nvrdigatia sgsfvtegmv iapcsmktla gvangfadnl ltraadvmlk
      121 errrlvlvar etplnlahlr nmtlatemga ivmppvpafy ahpktiedvv dhtvgrildl
      181 faiehreiak rwsgladefa srrdddgadr
//
LOCUS       WP_007585345             361 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudoalteromonas sp.
            BSi20429].
ACCESSION   WP_007585345
VERSION     WP_007585345.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. BSi20429
  ORGANISM  Pseudoalteromonas sp. BSi20429
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 361)
  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 361)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 361)
  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   4  (residues 1 to 361)
  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 361)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Pseudoalteromonas sp. BSi20429"
                     /db_xref="taxon:1097676"
     Protein         1..361
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40738
     Region          102..356
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          275..355
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mnlllvnlnt vvavlcvlma lhlflqkssn llavrllgac fmvlgihall lgfnltyssn
       61 vliaalqptm pvlfgplayl mfqsafqinw rlkrssllhl vpaalvlvlm lseqgrsvad
      121 fsillslmgy alllshlswc kkatfqtepe ntesvtqgfn ktiylwllif tayswlvlif
      181 dvlivleiit gkttfqsial mmtilfkvii isfaiflalq ksplfdwlyt sfstsigkni
      241 esknlqvfqt iicafeqlie datiytkevv slkamadklg vsdrlfsnai nhhygesytk
      301 rinrlrvnfa rrllveqpql simavmfdsg fqtkssfnke fkaltslsps eyrekqiker
      361 q
//
LOCUS       WP_007586096             296 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Paraburkholderia
            hospita].
ACCESSION   WP_007586096
VERSION     WP_007586096.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia hospita
  ORGANISM  Paraburkholderia hospita
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Paraburkholderia hospita"
                     /db_xref="taxon:169430"
     Protein         1..296
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32599
     Region          14..258
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mqtlecvlpa aaalgecprw derraklwwv dinapalncf dpktgentai pmpenigcfs
       61 lteddgfiag mrtgifllda kgqvvrklca naenpatsrf ndgrcdargr fwlgtldepk
      121 agdaaalyry angaltkidt glltsngmgf spdyrwcyhs dtprftiyrh pydidsgevg
      181 predwvkfqp tptdrgrpdg asvdsegyyw salyeggrvv rispegkvve ehplparcpt
      241 mctfggddlr tlyvttargg rpaeelekfp qsgsvfamrv svpgliekrs alrvte
//
LOCUS       WP_007586136             139 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Pseudoalteromonas sp. BSi20429].
ACCESSION   WP_007586136
VERSION     WP_007586136.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. BSi20429
  ORGANISM  Pseudoalteromonas sp. BSi20429
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Pseudoalteromonas sp. BSi20429"
                     /db_xref="taxon:1097676"
     Protein         1..139
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14250
     Region          4..139
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mktmtqkqqg ftlielmivv aiigilaaia lpqyqgytak sqatacyqei apgktqfeil
       61 tldgtgvtpn aasgseiglg dakscslhav tattivgtlq gsapidgetl tltrnansga
      121 wtctasgtid dsllpeecr
//
LOCUS       WP_007586917             152 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_007586917
VERSION     WP_007586917.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..152
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16024
     Region          1..152
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mqkhdfyqsl vkqtesliag esnvianlan isallftsle dvnwagfyfm dsptelvlgp
       61 fqgnpaciri pvgkgvcgta aataetqlie dvhafdghia cdaasnsevv vpimkhgkvf
      121 avldidspsi grfdaddkag lealvkclea sl
//
LOCUS       WP_007588810             270 aa            linear   BCT 20-JAN-2025
DEFINITION  YaaA family protein [Actinomyces sp. ICM39].
ACCESSION   WP_007588810
VERSION     WP_007588810.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces sp. ICM39
  ORGANISM  Actinomyces sp. ICM39
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Prahlad,J., Yuan,Y., Lin,J., Chang,C.W., Iwata-Reuyl,D., Liu,Y., de
            Crecy-Lagard,V. and Wilson,M.A.
  TITLE     The DUF328 family member YaaA is a DNA-binding protein with a novel
            fold
  JOURNAL   J Biol Chem 295 (41), 14236-14247 (2020)
   PUBMED   32796037
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Liu,Y., Bauer,S.C. and Imlay,J.A.
  TITLE     The YaaA protein of the Escherichia coli OxyR regulon lessens
            hydrogen peroxide toxicity by diminishing the amount of
            intracellular unincorporated iron
  JOURNAL   J Bacteriol 193 (9), 2186-2196 (2011)
   PUBMED   21378183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006857
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Actinomyces sp. ICM39"
                     /db_xref="taxon:1105029"
     Protein         1..270
                     /product="YaaA family protein"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=28340
     Region          2..209
                     /region_name="YaaA"
                     /note="DNA-binding protein YaaA associated with the
                     oxidative stress response [Replication, recombination and
                     repair]; COG3022"
                     /db_xref="CDD:442258"
ORIGIN      
        1 mliwlppseg knapaqgpsl dvnalsrasl atsrrtvcna laalgdgpea aavlkvgari
       61 dlsvntalds apcapasslf tgvlyeaiee capnawtsag aanvsifsgl fgvlspsdvi
      121 pdhrlamgvs lpdlgvlstw waprldetls aeaseriiid grsgpyraac kapwarvwel
      181 rvereadgkr svishdakrw rgaitgllla cdgyraeeta aaekaleeaa yslslgdakg
      241 hehrvtgvey gpekqtkkgg strtvtlvth
//
LOCUS       WP_007589343             338 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: endonuclease domain-containing protein
            [Actinomycetaceae].
ACCESSION   WP_007589343
VERSION     WP_007589343.1
KEYWORDS    RefSeq.
SOURCE      Actinomycetaceae
  ORGANISM  Actinomycetaceae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales.
REFERENCE   1  (residues 1 to 338)
  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 338)
  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   3  (residues 1 to 338)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Actinomycetaceae"
                     /db_xref="taxon:2049"
     Protein         1..338
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37424
     Region          226..336
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 msqevrgnda pfilnavera iirvprsshh gltkiptavn iagktyldla rltdidthql
       61 pqvvlaarly hlahthqtli atgqcalwah gygsdpalpp itvatssair pivlpaitig
      121 trtfapmkvt prhvrhlpai sdtrgllien lesaqitaar tssnrraaft qmcmnahayt
      181 hfdnfhmkas rnneeswkff lerelkqlgn rargrsqaqw iithadagca spgearvlye
      241 lcaaglagml tqvevhtrgr ryfidcafta ekvgiefdgr akygddarsi hsslarerer
      301 qrhlegegwh iirvgwhdld hpdeliaqvr aalaarlg
//
LOCUS       WP_007590306             399 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Actinomyces sp. ICM39].
ACCESSION   WP_007590306
VERSION     WP_007590306.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces sp. ICM39
  ORGANISM  Actinomyces sp. ICM39
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Actinomyces sp. ICM39"
                     /db_xref="taxon:1105029"
     Protein         1..399
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43028
     Region          6..396
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mssssvlvin sgsssikyql vdpetgdaia kgiverigdt tglikhehgd avtkeelpvp
       61 dhtvgmrevl rlfdtegpsl aeanilavgh rvvqggryfd gpalitdevr nlieelcpla
      121 plhnpahlkg idvarelmpd iphvavfdta ffqqlpdkaa lyaletetae kysvrrygah
      181 gtshqfvsqe iskmlgrddl kqivlhlgng asasavkngk pidtsmgltp leglmmgtrt
      241 gdidpavvfh lqrvagmtvd evdtlfnkks gmkgmtgesd mrsvwevinn tsdpeasrra
      301 rtamdvyinr llkyvgsyaa elggldvitf tagigenddd vrrelaeala pfgvkidvea
      361 nkgrvkepri vsapdsavtl vvyptneela iarqaltfa
//
LOCUS       WP_007591100             339 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Bradyrhizobium sp.
            WSM1253].
ACCESSION   WP_007591100
VERSION     WP_007591100.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. WSM1253
  ORGANISM  Bradyrhizobium sp. WSM1253
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 339)
  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 339)
  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 339)
  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 339)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Bradyrhizobium sp. WSM1253"
                     /db_xref="taxon:319003"
     Protein         1..339
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=36889
     Region          5..337
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 msfsrrtllk asaatavlgg lsaphvaraq saeftykyan nlpdthplnv ramemaaaik
       61 aetsgkfdlq ifannqlgsd tdmlsqirsg gvefftlsgl ilstlvpaas ingigfafpd
      121 ygtvwkamdg dlgafvrgei kkaglevmdk iwdngfrqtt ssskpitgpd dlkgfkirvp
      181 vsplwtsmfk afdaapasin faevysalqt rivegqenpl aiistaklye vqkycsltnh
      241 mwdgfwflan rkawsalped irtvvaknin aaavkeredt aklnanlqqe lagkgltfnl
      301 pavapfrdkl rsagfyaewk gkygdqawdl lekavgkls
//
LOCUS       WP_007591341             342 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Bradyrhizobium].
ACCESSION   WP_007591341
VERSION     WP_007591341.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 342)
  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 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 342)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 342)
  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   5  (residues 1 to 342)
  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   6  (residues 1 to 342)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..342
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38600
     Region          31..213
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          132..342
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mpfqvataip rravtpaafv rgvvaayery grdptealsr gqvtpdlvns pggrvtagqf
       61 ealaghamre lddealgwfs rrlpfgtygm lcrasitapt levalkrwcr hhrlltedvl
      121 ldlavgketa vvsirelrdl gslrefclvt llryvlgfsc wavdsrialr aaefpyaepg
      181 hvsvyptifc rnirfdadra sitfdkhyls lpltrsaadl dnmlkgalrl tvlpyrrdrl
      241 lvervrrvlr nargrslgae dvaselalst rtmhrrlree atslrdlkee akfelakqel
      301 mrgrspikri aeiagfsnek sfsrafrswt gtsprefrgr yr
//
LOCUS       WP_007591680             369 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [unclassified
            Lachnoanaerobaculum].
ACCESSION   WP_007591680
VERSION     WP_007591680.1
KEYWORDS    RefSeq.
SOURCE      unclassified Lachnoanaerobaculum
  ORGANISM  unclassified Lachnoanaerobaculum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Lachnoanaerobaculum.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="unclassified Lachnoanaerobaculum"
                     /db_xref="taxon:2625085"
     Protein         1..369
                     /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=43716
     Region          9..317
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mssdtgnhrk rnysldifkg vliflvvfgh fllpvkkrey tifnklfffi ysfhmpafif
       61 lsgylyydsw krrgtklksv iplimlflmm killhisdml fygdrniipd flhesstpwy
      121 isaliffrls lyplelflkl nkkktsqvkr eqfnsdavti yvtvliifft ffsmlnmnwq
      181 vkiddflsld rvvsfapyfy igvlykkyss vsktsifeei nirlfamgaf cvlvffvffk
      241 yvrfytlify ghwgyriaeg nilpifkgvl nplriiympy alstsyfifv ltslkknflt
      301 nifkrfgvys lpifafhrii rdafshlvld nfiwpvfgkt tiliilltis fltclilgnd
      361 kanrfcrfk
//
LOCUS       WP_007591967             276 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Lachnoanaerobaculum sp.
            OBRC5-5].
ACCESSION   WP_007591967
VERSION     WP_007591967.1
KEYWORDS    RefSeq.
SOURCE      Lachnoanaerobaculum sp. OBRC5-5
  ORGANISM  Lachnoanaerobaculum sp. OBRC5-5
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Lachnoanaerobaculum.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Lachnoanaerobaculum sp. OBRC5-5"
                     /db_xref="taxon:936595"
     Protein         1..276
                     /product="formate/nitrite transporter family protein"
                     /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=29106
     Region          6..276
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mnfsnttaev tqnlieageg kvkrplhkmi llgilagmli gagamassva ihdisntgia
       61 rlvaglvfpi gfvmmvlfgg elftgaclmi igvlkgkykv sdmiralivv fisnliggll
      121 failvafsgq fkysdglmga ftiklalska nipfgsalis gilcnffvcl gvvmaglskd
      181 isgkvlasfl pimtfvtggf ehcvanmfyi pagifaagns kyaevamtky gitakklatl
      241 nwknflltne lpvtigniig gmlfigvvmy ivyske
//
LOCUS       WP_007592021             197 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Lachnoanaerobaculum sp. OBRC5-5].
ACCESSION   WP_007592021
VERSION     WP_007592021.1
KEYWORDS    RefSeq.
SOURCE      Lachnoanaerobaculum sp. OBRC5-5
  ORGANISM  Lachnoanaerobaculum sp. OBRC5-5
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Lachnoanaerobaculum.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Lachnoanaerobaculum sp. OBRC5-5"
                     /db_xref="taxon:936595"
     Protein         1..197
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=23351
     Region          12..195
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mdyinkikek lknnggvits keftrsnipt iyltrmvktg eliridrgiy inssgdydey
       61 sffqnrytva ifsyvsalyl qgftdiiple ieatvykgyn khrinsnvri hyvkkeiydm
      121 gitdcqtmfg ntvkvynler ticdliknrn evetellskt lnryikysyk dlnrlyeysk
      181 kmkiyekvkk imeilye
//
LOCUS       WP_007592175             565 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Lachnoanaerobaculum sp.
            OBRC5-5].
ACCESSION   WP_007592175
VERSION     WP_007592175.1
KEYWORDS    RefSeq.
SOURCE      Lachnoanaerobaculum sp. OBRC5-5
  ORGANISM  Lachnoanaerobaculum sp. OBRC5-5
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Lachnoanaerobaculum.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Lachnoanaerobaculum sp. OBRC5-5"
                     /db_xref="taxon:936595"
     Protein         1..565
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=64706
     Region          8..505
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mqktgrlelt wvgkydekii eprilledke ksygdpasen mlirgdnlia lqalqqeyse
       61 rvkciyidpp yntgsafdyy ddnlehsiwl slmkqrlill rellsedgti wiqiddeeqa
      121 ylkvlcdevf grgnfinmis vnmkniagvs gggedkrlkk nceyilvyak eysllplfng
      181 pysytemsel vqqyidegks wkyttvllnp gekeyygstv dgdgneikvy lrknpemlsi
      241 kqvanrdgit ekeaykkygv sifqttnaqs sirtrvmdyr ieegikedli sieyvpktgk
      301 nrgkvyeqfy kgdkcrlfvw lrdtskvidg elykkdlqgt ywdmnawmkn ltkegsvefg
      361 sgkkpeqlvr qiiemttseg ewvldsflgs gttaavatkl krkwigvelg eqayshckpr
      421 ldrvidgadm ggvtklvnwq ggggyhfyel apsllvkndk lpiyqinpey nfdmiceaic
      481 kiegfkykpk dvfhgyssek ryihvtmelv naayitslsa hlaegeslli ygtkvqsdmv
      541 lpdnievkki pkdllekcvf esevr
//
LOCUS       WP_007594753             124 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein
            [Bradyrhizobium].
ACCESSION   WP_007594753
VERSION     WP_007594753.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium
  ORGANISM  Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Bradyrhizobium"
                     /db_xref="taxon:374"
     Protein         1..124
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=13414
     Region          16..79
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mlnqgeldqn emgrligsdk vegtsvygad rnkigsierv midkisgkvs yavlgfggfl
       61 glgndhyplp wqslkydtel ggyvtgittk elegapkyge rsdwnwgdda avrginsyyg
      121 vpfa
//
LOCUS       WP_007596455             348 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Rhizobium sp. PDO1-076].
ACCESSION   WP_007596455
VERSION     WP_007596455.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. PDO1-076
  ORGANISM  Rhizobium sp. PDO1-076
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 348)
  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   6  (residues 1 to 348)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Rhizobium sp. PDO1-076"
                     /db_xref="taxon:1125979"
     Protein         1..348
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38911
     Region          25..201
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          91..331
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mvefdrrmis psfveealdc lkragkptap vltslglppv idqpisaery galwlaiaae
       61 vddeffgmaa ramphgsftl lchcvlhakt leqalrralr fltivledpi gelvirdgla
      121 eiiltdkgea rsafayrtyw illhgiacwl vgrriairsv dfrcaepkqg adyrlffgap
      181 vlfsrpvsrl afdrtvlklp iarteqalkq flrgapanil lryrydagla aamrrhlrht
      241 ppadwgsfen iaaqmrksps tlrhrlhaeg qsfaaikeei rrdmaiells trtmrvsdva
      301 tglgfaepsa fhrafktwtg qtptqyrrah atlqeiddst smpdragn
//
LOCUS       WP_007596611             432 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Rhizobium sp. PDO1-076].
ACCESSION   WP_007596611
VERSION     WP_007596611.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. PDO1-076
  ORGANISM  Rhizobium sp. PDO1-076
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 432)
  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 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   3  (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   4  (residues 1 to 432)
  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 432)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Rhizobium sp. PDO1-076"
                     /db_xref="taxon:1125979"
     Protein         1..432
                     /product="CmpA/NrtA family 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=46350
     Region          40..301
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mtkttgtgis rrnilkttaa aalvsavrsa fpsgafaasa gpevtglklg yialtdaapl
       61 iiakekglfa khgmadvevl kqaswgatrd nlvlggeang idgahiltpm pylmetgkvt
      121 qnnvpvpmsi varlnldsqg isvaqeyaat gvqldasklk eafaakkaag neikvamtfp
      181 ggthdlwiry wlaaggidpd kdvstivvpp pqmvanmkvg nmdafcvgep wneqlvnqgi
      241 gftacttgel wkghpekalg lrtewieknp naakalmmav meaqiwadsm dnkeemsail
      301 gkrqwfnvpp kdvagrlkgt inygngrlve ntglemkfwk dhasypfksh dawfltenvr
      361 wgkfaadtdi kalvdkvnre diwreaakdl gvaaadipas ssrgvetffd gkvfdpenpq
      421 ayldslsika ga
//
LOCUS       WP_007596973             370 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Rhizobium sp.
            PDO1-076].
ACCESSION   WP_007596973
VERSION     WP_007596973.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. PDO1-076
  ORGANISM  Rhizobium sp. PDO1-076
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 370)
  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 370)
  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 370)
  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 370)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Rhizobium sp. PDO1-076"
                     /db_xref="taxon:1125979"
     Protein         1..370
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40105
     Region          1..360
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mnrrqfitqa gvagmgaaal atpalttpai aqenptitwr mtssfpksld iifgaatdia
       61 esvskatdgk fqiqvfaage ivpplqaada vtagtvemah tccyyyigkd pafalgtaip
      121 fglnarmtna wftagggnql lneflaghkl yalpagntga qmggwyrkei ktiddlkglk
      181 mriaglagdv mskvgvtpqq iagsdvypal ekgtidatef vgpyddlklg fykvapyyyy
      241 pawweggptv haffnldkfn elpesyqsil tdacaaanar mlarydasna talrelvang
      301 tqlrafssei ldvchkaake tyaelsakne nfkklfdsqq afkqdaylwa qiadysfdty
      361 qmiqqrqgnl
//
LOCUS       WP_007597646             633 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Rhizobium sp. PDO1-076].
ACCESSION   WP_007597646
VERSION     WP_007597646.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. PDO1-076
  ORGANISM  Rhizobium sp. PDO1-076
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 633)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 633)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 633)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Rhizobium sp. PDO1-076"
                     /db_xref="taxon:1125979"
     Protein         1..633
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68739
     Region          6..633
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 meqdkthsse ghkgargmff lalgsvgvvy gdigtsplya frealkpise ggvtrleiig
       61 lislmiwalt iivtlkyvlf llradndgeg gtlsllalls ktanghgpil mvlgligaal
      121 flgdsmitpa lsvlsavegl klvapdlsdy ivpisvaili gvfavqshgt aavarffgpi
      181 talwflvmaa ggvnhifddl gilsafnpwh aanfmlregf lgivvlgavf ltvtgaealy
      241 adlghfgrkp iqwawfvlvf pslvlnylgq galvlhnpda menpfylmfp qwallpvvil
      301 atfatiiasq avitgafslv rqaihlgflp rmqilftset htgqiylpsv nalllvgvla
      361 lvllfessea lataygisvt gamvvttima fefvrkrwnw svttavaall pllalelvfl
      421 ganllkihdg gyipvlfaav ftvimwtwrr gngilfaktr htdvplapfi asierksdha
      481 panvpgtaif ltsdaetapa allhnlkhnh vlherniilt iktigrprat aderfvieql
      541 serfsrveir fgfmenqnvs kalanlrrcg lkfdimstsf ylgrrklvpd aksgmpywqd
      601 rlyislanaa adpsdyfrlp anrvvelgsh vii
//
LOCUS       WP_007598062             739 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Bradyrhizobium sp. WSM1253].
ACCESSION   WP_007598062
VERSION     WP_007598062.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. WSM1253
  ORGANISM  Bradyrhizobium sp. WSM1253
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 739)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 739)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Bradyrhizobium sp. WSM1253"
                     /db_xref="taxon:319003"
     Protein         1..739
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=77470
     Region          28..737
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mearvsaasa ssrpwspapd asdivkgiha mlhprnivlv gatdkpgnya eriwnnlvky
       61 syegglypvn akrdaiwgvp cykdfaslpe kpdhvlvlvp arfavqvird aaaagarsat
      121 ivtsgfselq deesqklaae lqaavretgl avtgpnclgn lsageklftn iddrivtmeq
      181 gavaiagqsg aivmairqal edrgvgvgym vttgneagle tpdlmryfae dpsikvivvy
      241 legvrntkaf rdackaaraa skpvialklg aseggraaam ahtgalagsi etfdaiatre
      301 gvirvgglde liettecfvh aavprgdrla avtlsggkrg mlidafdaeg lnfaplsshv
      361 rselakmlgp gsivgnplda gfaavvdpsv ymksiglmid dpeidiviid aelpkaphel
      421 rernlrivde masragkpvi yisamsigft eftktlrksl phlavmqgmd ravtaiksll
      481 dyaklrkevp divssskpaa ravlekalks atgaaldeva skkllkaygi piskeaiaqt
      541 aaeavkiakq igfpvvakvv saeilhksdi ggvvlnltnp aevkkafadi tarvsrlkgk
      601 pkldgiliaq qvkadlelvv gasldaemgp vvlfgtggid ielmkdvala gapldeaear
      661 lligrtkagi kmrgyrgkpa lhetsavkal vglsnliada gdriasidvn pflinagtgv
      721 avdalivlnn aaakraagh
//
LOCUS       WP_007598802             297 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Bradyrhizobium sp. WSM1253].
ACCESSION   WP_007598802
VERSION     WP_007598802.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. WSM1253
  ORGANISM  Bradyrhizobium sp. WSM1253
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 297)
  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 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   3  (residues 1 to 297)
  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   4  (residues 1 to 297)
  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 297)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Bradyrhizobium sp. WSM1253"
                     /db_xref="taxon:319003"
     Protein         1..297
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32071
     Region          26..175
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          203..283
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtetllqias rysaahaddr gvastpfagv siiretapsa llyaisrplv alvlqgakrv
       61 atgrtsfdfg agaslliasd vptvsqitra taatpylslv veldptiieg lvvemgslpf
      121 ipsqplrvep teqeladaal rllrlidrps alpilrghlm relhywllag rhdgairalg
      181 iadshaqrig ravaliragy akplrvdrla kaaamspsaf hahfrsvtsl tplqfqkqlr
      241 liearramla dgaqiataah qvgyesitqf treysrlfgm ppgrdmreak rriesaa
//
LOCUS       WP_007600886             256 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Bradyrhizobium].
ACCESSION   WP_007600886
VERSION     WP_007600886.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium
  ORGANISM  Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 256)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Bradyrhizobium"
                     /db_xref="taxon:374"
     Protein         1..256
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=28346
     Region          25..137
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mrsffiafts lmllsagaaq akveitvdkd nqqmtvavdg iaryhwpvst gipsretpng
       61 afrafrmeed hyskefddap mphsifftki ghaihgtdsv grlgtpashg cvrlsrqnas
      121 tlyalvqqqg vlnttvtltg ssqvalarnp rgrnptavar apqpteeqya tsgdpvnlap
      181 taqparrymp qddnyiypad gsdtgtrypa prgsrplyda qvyqqqpqqy ynqgngtyyq
      241 pqprqvyqpr gyyyqn
//
LOCUS       WP_007600120             615 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Rhizobium sp. PDO1-076].
ACCESSION   WP_007600120
VERSION     WP_007600120.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. PDO1-076
  ORGANISM  Rhizobium sp. PDO1-076
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 615)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 615)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Rhizobium sp. PDO1-076"
                     /db_xref="taxon:1125979"
     Protein         1..615
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=65687
     Region          18..582
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mtsslplrfm llafaagflw agllglqhia grqsvidrie tflldarinl vgmrkasdav
       61 aivviddatv advgryplgr rqlahiidki trsgarglai dmllvsesds eadaalaaal
      121 ssspaiiasa aqfsnevghf rhipapkgal nplstlsdva ktglvnvvtd aggtprqipm
      181 lslfshgpep sivlgatgly ygempsmtae glrfrerelr ldlgwhlsln yygasgtikt
      241 isardlltde vsskilkdrl vvlgvtaigv gdrfttpfdq ilpgvevlat aisniidgsa
      301 lirdrtirri dataalvitl sgvaalsflp laagsivfma lnlgwffval lafthsywls
      361 galpivaslp piagvaflrq ilerneirhl aaaraalgqf qasiiakrlg edpvfllepq
      421 eqsaailfvd lvgftglser lgarharnll ksfhtivvde terqnglvmd fmgdgvmigf
      481 gipdpseqaa snavsaafrl ktavedwlvs erldvnvsav rvgahcgqvv lsrlghqnhq
      541 qiaatgdcvn vasrlldvar tcgaslvlss dliraaglek elltdncplq einirgreqp
      601 ikvaiwqkae efvsq
//
LOCUS       WP_007602251             459 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [unclassified Bradyrhizobium].
ACCESSION   WP_007602251
VERSION     WP_007602251.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 459)
  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 459)
  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 459)
  AUTHORS   ter Beek,J., 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 459)
  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 459)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..459
                     /product="CmpA/NrtA family 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=50097
     Region          99..338
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mstfdnpfdp nrnlragcac gqhqsaaehe qatalrcdpv eseekryegv vasavmramf
       61 pqdvarrafl ksvgastala alsqffplqt atevfaqagt pekkdlkvgf ipitcatpii
      121 maaplgfyak hglnvdvvkt agwavirdkt inkeydaahm lapmplaisl glganaipfa
      181 vpaieningq givlaskhkd krdpkdwkgm kfaipfdysm hnyllryyla ehgidpdtdv
      241 qlrsvpppem vanlradnid gflapdnicq raiydgvgfm hllskeiwdg hpccsfaasr
      301 efittapnsf aaltraivda tayaskaenr kqiaeaiapa nyinapvtvl eqvltgtyad
      361 glggvktdek rvdfdpfpwq sfavwmltqm krwgqikgdv dykaiaeqvy latdtrklmt
      421 emglappags yksfavmgks fdpakpedyl agfkirkas
//
LOCUS       WP_007603599             735 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor family protein
            [Bradyrhizobium].
ACCESSION   WP_007603599
VERSION     WP_007603599.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium
  ORGANISM  Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 735)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..735
                     /organism="Bradyrhizobium"
                     /db_xref="taxon:374"
     Protein         1..735
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=79723
     Region          64..735
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mlrcharrgv svvaiqaall assngafaqs ssavlppitv eapqqkrasa vrsprnsars
       61 arvtrslrtt pspqqtaseq sagapgaltv ltaqqalaei nqtpggvalv sadayrnstp
      121 sntikdvldy vpgvyaqpkw gddtrlsirg sglsrnfhlr gvqlymdgip intadgygdf
      181 qeidpsayky vevfkggnal qfganslgga infvtptgrd sfpngvsfdv ggfgykrlqa
      241 naggvngrwd gfvtasaqaa dgfrdhsfgs snrlsgnigy qfspdvetrf ylnanevrqr
      301 ipgtvtktsa ltdpeaaapa nvamdqqrni dtvrlanktt vrfddtkvef gafgvdrhlm
      361 hpifqwldyr ykdyggfaki tddrtiggfr nrlvagvyvl ngsidnqqfa niggqkgall
      421 sssidrsent sayvedsfyv ipnlaviggt qflyatrnrq drflsdgdqs gatrfnvwsp
      481 kggllwqidp awqafanvsr saevpsfges aigpgiptip ftsirpqiat tyeigsrmkr
      541 pdyaweltay ranirdelqc lysafgncnv tnadhtihqg ieagagaaif rdifvngpap
      601 dkiwlnvays fndfrfdkdp tfgnnrlpga pshylraell ykhptgfyvg pnvewvpqay
      661 fvdsmntltt epyallglka gfdnggpmsa yiegrnltnk tyiasasiid ratatsalfe
      721 pgtgravyag mryrw
//
LOCUS       WP_007603872             353 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Bradyrhizobium sp. WSM471].
ACCESSION   WP_007603872
VERSION     WP_007603872.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. WSM471
  ORGANISM  Bradyrhizobium sp. WSM471
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 353)
  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 353)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 353)
  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   4  (residues 1 to 353)
  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 353)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Bradyrhizobium sp. WSM471"
                     /db_xref="taxon:319017"
     Protein         1..353
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37612
     Region          <150..347
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          265..347
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mtlaatelaf raasvalllv laasllsdfr nvlaarlgaa falgsaahaa sysvgvsslv
       61 pawhapliav stgnivvfwl ftralfddef rlhrwhgltw glvtafsfvs clwiapgghv
      121 rsavtavnmi vlgfialaim qtiaswsadl verrrrvrvf ivcaaalygg lnavlqilvv
      181 gsdvgdvant vnagvlasiv aaiayammrv dgadlfpaaa eaapaiaasq pvgedaadqk
      241 lidalmrlma deriyrqeni sigvlagrlk ipeyrlrrli nqglgyrnfn vflnnhriee
      301 akaaladpaq aevpvitiam dsgfqslgpf nrafkavtgv tpteyrrlkv nav
//
LOCUS       WP_007605759             370 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Bradyrhizobium sp. WSM471].
ACCESSION   WP_007605759
VERSION     WP_007605759.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. WSM471
  ORGANISM  Bradyrhizobium sp. WSM471
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 370)
  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 370)
  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   3  (residues 1 to 370)
  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   4  (residues 1 to 370)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 370)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 370)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 370)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Bradyrhizobium sp. WSM471"
                     /db_xref="taxon:319017"
     Protein         1..370
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38662
     Region          30..359
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(102..104,125..126,175,226,250)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 msvlrvhrla aaalvslals ssarskdvyi aiagpmtgst aalgaqirdg aaaavdsina
       61 sgllpdtrli lriaddacdp kqavavanrl tsdgiklvvg hfcssssipa sdiyaeaevi
      121 qispgstnpr lterglttlf ricgrddqqg rvaaeyiarh hqgaklavld dkstagkgia
      181 divesrlraa gehpvrqsyv agekdytalv srlkregiql vyiggyynei glivrqaaea
      241 gsrltviand plmttdflai ageaangtlf tfmpdptkna agaaavaklk gssltaagyt
      301 lyayaavqaw adsvkragtl datrvaaalr sepidtaigt vafdskgdna apgfivyrwr
      361 dntveeveqn
//
LOCUS       WP_007605964             407 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Bradyrhizobium
            sp. WSM471].
ACCESSION   WP_007605964
VERSION     WP_007605964.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. WSM471
  ORGANISM  Bradyrhizobium sp. WSM471
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 407)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Bradyrhizobium sp. WSM471"
                     /db_xref="taxon:319017"
     Protein         1..407
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=45171
     Region          6..391
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mpdvsvldvh lygkpiatlt lvqgdrtlfa fnqsyiddpd rptlslsfkd qfgnlltafr
       61 pyrmvlppff snllpegplr rylaeragvk ekreffllwm lgqdlpgals vhpaegealp
      121 pqveedltpd erhnmlrfsl agvqlkfsal ksnskrgglt ipvegvggsw ivklpsnqya
      181 gvpeneysmm tiakamgmdv pdlqlldvna idglpegige fkgqalavkr fdrtadgpvh
      241 medfaqvfgv apdekyehvn ykgiagvlgi etgdadvaef irrlvfstli gntdmhlknw
      301 sliypdrrtp alspaydlls tipyiaddkm alnysrtkkm tefskdelkh laakakisek
      361 lvldtatetv qrfkqvwsdq kktlpldkkv vgsvdahavs ipiysel
//
LOCUS       WP_007607425             250 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Bradyrhizobium sp. WSM471].
ACCESSION   WP_007607425
VERSION     WP_007607425.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. WSM471
  ORGANISM  Bradyrhizobium sp. WSM471
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Bradyrhizobium sp. WSM471"
                     /db_xref="taxon:319017"
     Protein         1..250
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=25874
     Region          163..238
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mkatsflaaa alvgassvam aqgapqatgp vdhsavqsss rnqsadqrae nsmtnkggnk
       61 adavqsdpgq astrqqmvnd lqqagftdvk vrpqsflvea rdrsgnpvtm fvgpntfaev
      121 ktvganaqks stnsnsssns anatsdrlgg aftsvppkdg lssqlmglqv ynnakqdigt
      181 ikdvalneng idgyvlsvgg flglgdhyva vrpsainlkf dhaankwtat mdttadqlks
      241 apefkypsng
//
LOCUS       WP_007607856             682 aa            linear   BCT 20-JAN-2025
DEFINITION  sensor histidine kinase [Bradyrhizobium sp. WSM471].
ACCESSION   WP_007607856
VERSION     WP_007607856.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. WSM471
  ORGANISM  Bradyrhizobium sp. WSM471
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 682)
  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 682)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20493667
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Bradyrhizobium sp. WSM471"
                     /db_xref="taxon:319017"
     Protein         1..682
                     /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=74135
     Region          86..297
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          283..670
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mslslhpdtp qsstlpsaap vavasgttpg qgirsrlftk yvalfvavva iallanglfe
       61 vffyyrehka alirvqheqa eaaaakigqf vkeiesqlgw ttqlpwsags ieqrrfdalr
      121 llrqvpavte laqvdatgre rlrvsrlamd aidsgidlsd dpkfteavah kvfygpvyfr
      181 resepymtla qagsrkdagv siaevnlkli wdvvsqikvg ehghayvvgp egrliahpdi
      241 slvlrntdms gltqvraala ggsatldals earnlqgqkv ltasapiapl hwtmfvelpv
      301 eeayaalyaa lerlafvlla asifavlagi flarrmvgpi qalrsgaeri gsgdfsqris
      361 irtgdelegl adqfnhmger lqesyadlen kveqrtaelr qslndlrtaq drliqtekla
      421 slgqltagia heiknplnfv nnfsavstel idelnealqg asldgktkee vdeltgmlks
      481 nlekvvqhgk radsivrnml lhsregsgeh rpsdinaile eslnlayhga rverpgfnvt
      541 iergfdpaag mvdvypqeit rvflnlisng fyatakrkes aadafeptlr aatktlgdkl
      601 eirirdngtg ipsevrekmf npffttkpag egtglglsms hdivvkqhgg tidvntepgv
      661 ftefiitlpr mmaagdtsgg kt
//
LOCUS       WP_007607954             270 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Rhizobium sp.
            PDO1-076].
ACCESSION   WP_007607954
VERSION     WP_007607954.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. PDO1-076
  ORGANISM  Rhizobium sp. PDO1-076
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (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   2  (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   3  (residues 1 to 270)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Rhizobium sp. PDO1-076"
                     /db_xref="taxon:1125979"
     Protein         1..270
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30272
     Region          22..77
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msgtrpfrdv klqwlqqlsc dkdltdnars vaiyivtthl nghtekawps yqtiadatgk
       61 svktiqravr elevsgwfev ergngvghnt eyrpsasstl rasqarektd kivtlypdkg
      121 gqnrpgrrsd lsseggqicp pnlekeiink pnaredappr vetrravplv fvaetkadqv
      181 eqwrnwlqrs glpsmqalgv qtvkagrrgy slpgywppde tsrhaqewia ffndrrdhla
      241 getvwhlnpn fqttqlrpfw agaigelaas
//
LOCUS       WP_007607755             279 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [unclassified Bradyrhizobium].
ACCESSION   WP_007607755
VERSION     WP_007607755.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..279
                     /product="formate/nitrite transporter family protein"
                     /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=29826
     Region          2..260
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msylapsefv tkmvdagesk ifmstrdtii raymagaila laawfavtin vntgqpliga
       61 llfpvgfsml yllgfdlltg vfvlaplali dkrpgvtfgg vlrnwslvfv gnfagaltva
      121 fmmafvttfg ftqdpdkvgt aignigegrt lgyaahgaag matlfirgml cnwmvstgvv
      181 gamistsvpg kviamwmpil vffymvfehs vvnmflfpsg lmlhakfsim dyliwneipt
      241 vlgnlvggla ftgmtlyath vltqpkrqas kasspriaa
//
LOCUS       WP_007608278             284 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Rhizobium sp. PDO1-076].
ACCESSION   WP_007608278
VERSION     WP_007608278.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. PDO1-076
  ORGANISM  Rhizobium sp. PDO1-076
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Rhizobium sp. PDO1-076"
                     /db_xref="taxon:1125979"
     Protein         1..284
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30387
     Region          6..280
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 msetkpanea lclaalrdhd rdrylaallt padrragvaa lyaynaelar vrelvreplp
       61 gevrlqywrd llqgaghgan eanpvaaell qatrtyqlpv gplaamadar ifdlyddpme
      121 tvvmfegyag etaatliqlt slvldpaaaa saadtaghag vaqavagcll llpihrargq
      181 vylpleilra vglegpdllk gadkarlsaa ieafaglgld hlekarrsgt psrsilpayl
      241 patlarrvll sarsrgaail dhdirppqwr rqlrmmatlv sgri
//
LOCUS       WP_007608439             292 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Bradyrhizobium sp.
            WSM471].
ACCESSION   WP_007608439
VERSION     WP_007608439.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. WSM471
  ORGANISM  Bradyrhizobium sp. WSM471
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Bradyrhizobium sp. WSM471"
                     /db_xref="taxon:319017"
     Protein         1..292
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31113
     Region          16..256
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 meqvptsvls ddpchlgegp tydvttdtaw wfdiregrlf eaqlgrgsvr vhalgrmasa
       61 lgridaerql ivaedglyvr ktadgamtll cpleadnpat rsndarvhps gtfwigtmgr
      121 kaeagagaiy afhhgeisml fprisipnsi cfspdgatgy fadtaravly avplnpttgl
      181 prgepevllr htgiggldgs vcdadgqiwn acwgasrvdv yspqgerlrs lsvpvkqasc
      241 pafvgpdlsr llvtsawqdm daaaraadpq agytflleas argraepdvk la
//
LOCUS       WP_007608753             363 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [unclassified Bradyrhizobium].
ACCESSION   WP_007608753
VERSION     WP_007608753.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 363)
  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 363)
  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 363)
  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 363)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..363
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39953
     Region          1..355
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkrrdflkvs aagaaataav aspaiaqssp eikwrltssf pksldtiygg aeqmakyvae
       61 mtdnkfqiqv fqageivpgl qaldatqkgt vemchtvsyy yvgkdptfai fasvpfglna
      121 rqqnswlyqg ggnelaneff kkssvvgfpc gntgtqmggw frkeiktvad lsglkmrigg
      181 iagqvlqkvg vvpqqlaggd iypslekgti daaewvgpyd deklgfakva kyyyypgfwe
      241 ggptvhafan idkwnelpkn yqailtnatv ntntwmaary dmvnpgalkr lvaggtqlrp
      301 ftnevleacl katnelwgei saknpdfkks idamqayrsd eylwwqvaey tydsfmirsr
      361 trg
//
LOCUS       WP_007608769             193 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit [unclassified
            Bradyrhizobium].
ACCESSION   WP_007608769
VERSION     WP_007608769.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 193)
  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 193)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 193)
  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   4  (residues 1 to 193)
  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   5  (residues 1 to 193)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..193
                     /product="TRAP transporter small permease subunit"
                     /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=21544
     Region          3..172
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mqallklsng idaftrwtgk rlawlilvav visavnaiir ktldtssnsw lelqwvlfsi
       61 vfllcaswtl ldnehiridi fnsmmpkrar niidiighif flipltvvmi vtgvpfflrs
      121 lqineqsgna gglpqwpaks limigfafll vqgvselikr iavmrgmipd phesqisale
      181 aevehlveai eqk
//
LOCUS       WP_007610497             387 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Bradyrhizobium sp. WSM471].
ACCESSION   WP_007610497
VERSION     WP_007610497.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. WSM471
  ORGANISM  Bradyrhizobium sp. WSM471
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 387)
  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 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   3  (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   4  (residues 1 to 387)
  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 387)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Bradyrhizobium sp. WSM471"
                     /db_xref="taxon:319017"
     Protein         1..387
                     /product="CmpA/NrtA family 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=41446
     Region          2..262
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mtvplrigfi plvdaaaliv avdkgfaaae glqvelvrev swsnvrdkln iglfdaahll
       61 apvaiasslg lghvkvpiaa pfnlgingna itvspalhaa lmeeidgdrf dplatakala
      121 rvvakrrkag adplnfgmtf pfsthnyqlr fwmaaagvdp dedvrlvvlp ppymvdslan
      181 ghvdafcvga pwnsiavdlg ighilhfvsd ilahaaekvl alrqvwadkn pdvvarlvra
      241 avkaaefieh penrteaari laqperigvd aeviqrtltg rlkvspdgtf resgsyllvg
      301 reeagrpdpv qaawlyaqmv rwgqttltpd gvktamavfr pdlydgalgr rppaqapaaf
      361 gafagpafdp anirghleaf evgrwkv
//
LOCUS       WP_007614047             299 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Bradyrhizobium sp.
            WSM471].
ACCESSION   WP_007614047
VERSION     WP_007614047.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. WSM471
  ORGANISM  Bradyrhizobium sp. WSM471
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Bradyrhizobium sp. WSM471"
                     /db_xref="taxon:319017"
     Protein         1..299
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32923
     Region          21..263
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mtpdmipahq vetavaagdi lgetplwcdr srklwwvdid rrlhqsfdpa tgvhqvfpya
       61 cnslgsqalt adgshllaqd lglyrhspsd gppsqlceve tgrdnrlndg rvdargrlwi
      121 gtmdnqlhrp ngalyrvdad grtthmfgdv ivtngiafsl dnrtlyftdt rryctwqfdf
      181 dlddgvirnr rlfadysasg grpdgacidv agglwtaffs ggrvvryrpd gridtvipvp
      241 atnptcvcfg gadlktlfvt tarkfldreq lgrepqsghv laidgiaqgl pehrfgnss
//
LOCUS       WP_007614314             197 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit [unclassified
            Bradyrhizobium].
ACCESSION   WP_007614314
VERSION     WP_007614314.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 197)
  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 197)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 197)
  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   4  (residues 1 to 197)
  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   5  (residues 1 to 197)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..197
                     /product="TRAP transporter small permease subunit"
                     /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=21046
     Region          20..184
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 masvspaapq slnaaapapl rilldgidrl grldgwiggg cllmltllml cevatrflsn
       61 flsffpptis iaweyssylm aasftfgaam tlrvgghirv vlllknvpal fqraieilsa
      121 aagfafmafl tssmakfafg ayvrgqvsts sdtplwfpqg vvtfgmlllt lqflaraiqa
      181 vlglpledhr mkaspve
//
LOCUS       WP_007615421             345 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Paraglaciecola arctica].
ACCESSION   WP_007615421
VERSION     WP_007615421.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola arctica
  ORGANISM  Paraglaciecola arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 345)
  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   6  (residues 1 to 345)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Paraglaciecola arctica"
                     /db_xref="taxon:1128911"
     Protein         1..345
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39658
     Region          18..198
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <238..338
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mptkwlrasl lsgidkille qfslsislle neinfdfnll kdpdyklplt talkvlddca
       61 kytgcqyfga llaneqnndh lslmyslaks cnsfddalsv vfeqrlkrtn gfewqpskde
      121 fnayikshid disgidttqa tlfgiirlfk ffknitknkw cpsqiyftfp apnnikylkk
      181 ilgadiyfnm kfngfifpik qlslemsgqn sklntalkdf ltltgkssnt nkltqiklsi
      241 rsllilnqrc tltdiaesqh qttraiqyyl kkhqltyqnl ldgvryniar dmlietensi
      301 ykissligft dstvftrsfk khvglsptky rqeyqdlklg nnyml
//
LOCUS       WP_007615427             114 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Paraglaciecola arctica].
ACCESSION   WP_007615427
VERSION     WP_007615427.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola arctica
  ORGANISM  Paraglaciecola arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Paraglaciecola arctica"
                     /db_xref="taxon:1128911"
     Protein         1..114
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12789
     Region          1..104
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(7,25..26,34,37,39..40,42,45..46,48,56,61,68)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(25,56..57,59,85)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 msehpqyaki wrtvqliplg kvasygqiad laglpgrarl vgkslgfvpk dmevpwhrvl
       61 rsngqiafpt gseqsqkqsg llqqedvavf nnrvklsifq wqpdlaemlw kley
//
LOCUS       WP_007616813             287 aa            linear   BCT 20-JAN-2025
DEFINITION  formate dehydrogenase accessory sulfurtransferase FdhD
            [Paraglaciecola arctica].
ACCESSION   WP_007616813
VERSION     WP_007616813.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola arctica
  ORGANISM  Paraglaciecola arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Paraglaciecola arctica"
                     /db_xref="taxon:1128911"
     Protein         1..287
                     /product="formate dehydrogenase accessory
                     sulfurtransferase FdhD"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0097163 - sulfur carrier activity
                     [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30952
     Region          12..284
                     /region_name="FdhD"
                     /note="Formate dehydrogenase assembly factor FdhD, a
                     sulfurtransferase [Energy production and conversion];
                     COG1526"
                     /db_xref="CDD:441135"
ORIGIN      
        1 mshsseqgai periecndlv vieepleiwl saysssqska tpellfttmr tpgddlnlvr
       61 gwlyssgaiq dfskiesith tgtgrlksqs tnrvqinlaa ganvdltayq rvevmnaacg
      121 vcgqqsieni ldklphalsg dvqtpllain aihlltqqlr skqmmfeqtg gchgvalfdr
      181 svqlvdvred vgrhnafdkv iganidrlva dnhgvesilg vvlssrasfe lvqkaamvnl
      241 ryiialgaps slaidlakdc dicllgfvkt sgeaskfnvy ssphmla
//
LOCUS       WP_007618307             159 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Paraglaciecola arctica].
ACCESSION   WP_007618307
VERSION     WP_007618307.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola arctica
  ORGANISM  Paraglaciecola arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Paraglaciecola arctica"
                     /db_xref="taxon:1128911"
     Protein         1..159
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=17150
     Region          7..157
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mrivtytlrk qqkgfsliel misvaiigii atiaypsyqg fvvntnrgaa qadlmslaaa
       61 merhkaasfs ykgaadsaad tgkpaifhqh spsaelyanr kydlyisess gsaylieakp
      121 vtgtpqaddg nvafysdgrr awdinnngty satefcwsc
//
LOCUS       WP_007618329             138 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Paraglaciecola arctica].
ACCESSION   WP_007618329
VERSION     WP_007618329.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola arctica
  ORGANISM  Paraglaciecola arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Paraglaciecola arctica"
                     /db_xref="taxon:1128911"
     Protein         1..138
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15285
     Region          12..134
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mplqnkenns qnhfefctql gmtllelmvv viiigvlatl ifpsfeqqil aarrgdgitq
       61 llrlkiqqea frienssyae taqlglpvse yyafivtnvs attytitaka kgsqlddvkc
      121 ltmqinqsln ktpahcfl
//
LOCUS       WP_007619414             366 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Paraglaciecola
            arctica].
ACCESSION   WP_007619414
VERSION     WP_007619414.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola arctica
  ORGANISM  Paraglaciecola arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 366)
  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 366)
  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 366)
  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 366)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Paraglaciecola arctica"
                     /db_xref="taxon:1128911"
     Protein         1..366
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40515
     Region          27..358
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkllqlcvlv tvgmfllscg eqsstvpsvq veqqtyewkl vtswpknfpg lgkapetfak
       61 hvermsngrl kikvfgagqm vpgfevfdtv ssgaaemghs gsyywkgkap asqiftaipf
      121 gmnatemnaw lhygggmelw reiyapfnli pfaggnsgvq magwfkkevn svedlkglkm
      181 ripglggevl kklggipval tggelftslq sgaidatewv gpyndlafgl ykaakyyyys
      241 gwhepsatle fmvnkqafea lpddlqaiie vatravnqdm wdeytaanna amqalvethg
      301 vdmrplpadv mlalkkasie vmqeqsdadp mfkkvyksys dfqtnvmkyh qisefeyykn
      361 raidiq
//
LOCUS       WP_007622259             369 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Paraglaciecola arctica].
ACCESSION   WP_007622259
VERSION     WP_007622259.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola arctica
  ORGANISM  Paraglaciecola arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 369)
  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 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   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 369)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Paraglaciecola arctica"
                     /db_xref="taxon:1128911"
     Protein         1..369
                     /product="CmpA/NrtA family 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=40575
     Region          4..265
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 miepeqtdlt lgfipltdsa plivakelgf fsqwglnvsl qkqnswatlr dklhagllda
       61 tqmlapmpia stlglgcpkv kvitplvlsl ngnaitlsek lhqeilqenn iahvtlplaa
      121 yllqkvisvr kmqnrpklkf atvfpyschy yqvrdwlasa niseedldiv vvppvnmvaf
      181 lqsgeidgcc vggpwnakav ragigltalt sfdiwqdspe kvlgllasfq qanpntvlal
      241 taalkqaciw lenipnrfea arllssdqyl dasvdviaps ligsclthis lppraipsyn
      301 qfsksnngsi nvpeyirgew lisqmakagq lknidvpadi vrevfrpdiy qqmrlkledq
      361 avqffrrsg
//
LOCUS       WP_007623871             223 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Paraglaciecola arctica].
ACCESSION   WP_007623871
VERSION     WP_007623871.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola arctica
  ORGANISM  Paraglaciecola arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Paraglaciecola arctica"
                     /db_xref="taxon:1128911"
     Protein         1..223
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=25135
     Region          61..213
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mqkvilclll lslkvisteq vdadfniiqk piifdaqrka ltldymqshy gieqteptit
       61 ptmvvvhwte iptfeetfaa fnpavlpstr tkissagsvn vssqfvidrd gtvyqllpet
      121 tmarhvigln ytaigienva nghslpmtqa qleannkliq ylakkypiqy vlghseyqvf
      181 kgtplwkekd dnyltdktdp diafmdrlrg rlshldlrpl pqk
//
LOCUS       WP_007625092             442 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Paraglaciecola
            arctica].
ACCESSION   WP_007625092
VERSION     WP_007625092.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola arctica
  ORGANISM  Paraglaciecola arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 442)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 442)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Paraglaciecola arctica"
                     /db_xref="taxon:1128911"
     Protein         1..442
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=49780
     Region          27..428
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 malsiqlfvn gqwhdaanie fsssalngtv tltynnefim avpsfgqrdq wactlnaevs
       61 lvptdyphwp allddilpag ksrqwwldyl dlarqsefqq nigllthaci apighlrvkq
      121 afesrpqqnd mrfpieqait mqydfleytn qqgaaiggat gaggvapkll lmvedeqvyi
      181 dadfagkpla atpylvkfar nnkskrdnnv lraegiyyrv laelladtsl qtidveelri
      241 eeyqgqvslw lprfdvvsen dlakrigles vysiieagpg saqehfdvid rlwqrlklvs
      301 kmspadfvke yvardllniv fgnsdnhgrn taflkldndv rfapiydfap mkadpemvtr
      361 lfkwgrdcet ggevnfaqva qylgeycppe emmaflnnla nklinvpkyl eeqgcpeeil
      421 dfpaigfnfi eqklqrmgvi na
//
LOCUS       WP_007628994             707 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Rhizobium sp. CCGE 510].
ACCESSION   WP_007628994
VERSION     WP_007628994.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CCGE 510
  ORGANISM  Rhizobium sp. CCGE 510
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 707)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Rhizobium sp. CCGE 510"
                     /db_xref="taxon:1132836"
     Protein         1..707
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72729
     Region          <107..281
                     /region_name="COG3934"
                     /note="Endo-1,4-beta-mannosidase [Carbohydrate transport
                     and metabolism]"
                     /db_xref="CDD:443135"
     Region          430..673
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          <507..>627
                     /region_name="Peptidase_M10_C"
                     /note="Peptidase M10 serralysin C terminal; cl23859"
                     /db_xref="CDD:451582"
ORIGIN      
        1 maqavrindi irsfgidthi dytdgkysnv gevvkaldyl gldtvrdhap nsasdpngqt
       61 hlgdaaeagv qfvfsaqrev dpttvaqrlh tfvqahpgsv vgiegpnevn nwpvsyhgls
      121 gqaaaiayqk dlsaavnads llknipvlgf tgytvasasd yttihtyakd gdqpfswlsr
      181 eagvqraadp gkplvitetg yhtsltadtn ggwegvseat qaklvlntlm dgaalgskqt
      241 fiyelldays dpqganqekh fglfhldysa kpaattihnl ttileddgat kasfnagaln
      301 ysidgmpssa hsllteksdg syqiiiwnep diwnqstdta iqaattgvkv nlgasfgsvk
      361 vfdpvsgtta ikslsnvssl tvdvldhpii idigggsast ppptghtygg tgndiftvss
      421 ptqivdesrg ggtdtvmssi sfslkdtaht ignvenltlt gtanlngtgn glanalvgns
      481 gnnildgstg adhmsghagn dsyvvdnagd fadetgasgk dtvkasisfs ladvkhaagt
      541 ienlaltgta nlsatgnnta nvltgndgnn tinggkgadq ltgglgndkl igkagadtlt
      601 gggggdsfvf dvkpdnvsvd kitdfssaag dkllldhsif aalslsgfsd enlvlgtkal
      661 eaddrliydq asgslaydad gsaagtaihv adldnsaalh fkdfglv
//
LOCUS       WP_007629613             142 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Rhizobium sp. CCGE 510].
ACCESSION   WP_007629613
VERSION     WP_007629613.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CCGE 510
  ORGANISM  Rhizobium sp. CCGE 510
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 142)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Rhizobium sp. CCGE 510"
                     /db_xref="taxon:1132836"
     Protein         1..142
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=15428
     Region          30..141
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(93..94,97,110..113,115)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mktilaaaaa slllqfspia aeaatlvanv sigkqtmtvt engfikyrwk vstarngyvt
       61 ptgswsakwl srdhrsrkyd napmpyavff nggyavhatf dlkrlgrpas hgcvrlhpdn
      121 aaeffslarq aglantrvvi tr
//
LOCUS       WP_007629850             633 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Rhizobium sp. CCGE 510].
ACCESSION   WP_007629850
VERSION     WP_007629850.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CCGE 510
  ORGANISM  Rhizobium sp. CCGE 510
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 633)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 633)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 633)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Rhizobium sp. CCGE 510"
                     /db_xref="taxon:1132836"
     Protein         1..633
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68853
     Region          1..633
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mtsthadktg egtgrkgfvg lvvgaigvvy gdigtsplya lrealrpfaa dgvheaevig
       61 lislmvwtlt iivtfkyvlf llradndgeg gtlsllallm kkmgrnvpvl ffagligaal
      121 figdamitpa lsvmsalegl klvtpafaey vplasaaimi vlfgvqsrgt aavstffgpi
      181 tvlwflamaa gglihigddw tilealnpin aflflthagt vglivlgavf ltvtgcealy
      241 adlghfgrrp iqtawfvlvf palllnylgq galvlahpet aanpfflmyp dwallpvvll
      301 atmatiiasq avitgafsla rsavhlgflp rlrikftset ntgqiyvpsv nllllvgvlm
      361 lifsfrdses lataygisvt gtmvistmlv fqflravwgy slvlaavvll plflievlfl
      421 aanllkiydg gwvpvalala imilmwtwtr gqaylkrlra nneipldsfi rsierksdhs
      481 pvtvpgtavf ltsvpdrtpn vllhnlkhnh vlhqqnvils vwtedepyvp dsrrikisql
      541 sprfvrldlt fgfmddpdvt ralalcregg fkfeimktsf ylgrrnlvrt pntglpgwqe
      601 rifmalegla idpsdyfnlp snrvvelgeq vai
//
LOCUS       WP_007630707             373 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Rhizobium sp. CCGE 510].
ACCESSION   WP_007630707
VERSION     WP_007630707.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CCGE 510
  ORGANISM  Rhizobium sp. CCGE 510
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 373)
  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 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   3  (residues 1 to 373)
  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   4  (residues 1 to 373)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 373)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 373)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Rhizobium sp. CCGE 510"
                     /db_xref="taxon:1132836"
     Protein         1..373
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38752
     Region          27..358
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(99..101,122..123,172,224,248)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkksllsava ltamvafsgn awadvliava gpltgpnaaf gaqlqkgaeq aaadinaagg
       61 ingeqiklel gddvsdpkqg isvankfvad gvkfvighfn sgvsipasev yaengileit
      121 paatnpkfte rglwntfrtc grddqqgaia gkyladhfkd akiavvhdkt pygqgladet
      181 kkamnaaglt evmyeginvg dkdfsaliak mkeagvsiiy wgglhteagl iirqaadqgl
      241 katlvsgdgi vsnelasiag davagtlntf gpdptlnpan kelvekfkaa gfnpeaytly
      301 syaamqaivg aakaagsvdp eavatamkek gpfptvlgdi sfdakgdpki pgyimyewkk
      361 gadgkytyvp qdk
//
LOCUS       WP_007631751             723 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Rhizobium sp. CCGE 510].
ACCESSION   WP_007631751
VERSION     WP_007631751.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CCGE 510
  ORGANISM  Rhizobium sp. CCGE 510
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 723)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 723)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..723
                     /organism="Rhizobium sp. CCGE 510"
                     /db_xref="taxon:1132836"
     Protein         1..723
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=77131
     Region          11..670
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mtrvqqigva iglaivamlt ilraddpgif klirgvtfde yqrlvprtfe pmpvrvidid
       61 easlrefgqw pwprdrmall vdrlsamgas aiafdilfae pdrlsprnvv sevagvdpsl
      121 aeklpdndei farsiaekpv vlgfglsneg hyrppvkagf aftgespvsa ppylgastpl
      181 rpqleanaag lghislnpgn pspvvravpl fltdgeqlyp nlaiealrva qgastyvlsg
      241 apdragimts akigdfvvpl tavgelwlyv spdraeryis arqvlaaega spevaaavng
      301 sivfvgtsaa glqdirvtal genvpgvslh aqaveqilsg hflsrpdwad gleilviavl
      361 gcllvvvttf vspavalicg llatamalla swlsflyagl lfdplapivs gsiihfaats
      421 fkilvidrer ravrrafghy lspsllhrie htrdalrlgg ddreltvmfv dvrnfteise
      481 rlaptdvvaf lntlldalsr hvvanegtld kfigdsimaf wnapidvadh qtkavraala
      541 mretlaelna gdafgfgpgq evgigigiht glacvgnmga ktrfnysavg davnvaarle
      601 scckevgfdi lisdstarsv rgmalieaga iplkgkssrt qilavvgder vagsaefsal
      661 vvthqqlmqa lfahskntrk ligaaklraa gvidglaefy qrlsgrtdhf repndrfens
      721 aad
//
LOCUS       WP_007631852             279 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Rhizobium sp. CCGE 510].
ACCESSION   WP_007631852
VERSION     WP_007631852.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CCGE 510
  ORGANISM  Rhizobium sp. CCGE 510
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 279)
  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 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   3  (residues 1 to 279)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 279)
  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   5  (residues 1 to 279)
  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   6  (residues 1 to 279)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Rhizobium sp. CCGE 510"
                     /db_xref="taxon:1132836"
     Protein         1..279
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30785
     Region          18..101
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          127..278
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 msavgraiwf ieshfendls levisetagl shyhlsrvfg lvtghsissy irgrrlsrav
       61 paliggssti levalcagyg sheaftrafr dqfgvtpdav rrqgharnlv llepirmdpt
      121 hlndlepprf etlqpmlfag lqetypyggn aaipslwqkf nahfghisgq kgnvaygicn
      181 hidgeaekfr ymaaaevada gdlpadfatl klpgqryvvf ahrghvsgip ltmnrifgtw
      241 wptsglehga apdmferyde rfdpytgmgv teiwlpira
//
LOCUS       WP_007633554             109 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [Dietzia].
ACCESSION   WP_007633554
VERSION     WP_007633554.1
KEYWORDS    RefSeq.
SOURCE      Dietzia
  ORGANISM  Dietzia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Dietzia"
                     /db_xref="taxon:37914"
     Protein         1..109
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11841
     Region          13..109
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mtstaptpes rvlreliear sdefrallak ysatrprlfg svargtahge sdidivvdmd
       61 padgnllmra sglmeevrtl fgrenidifp aqllkrpisd aairdsvai
//
LOCUS       WP_007633594             500 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Rhizobium sp. CCGE 510].
ACCESSION   WP_007633594
VERSION     WP_007633594.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CCGE 510
  ORGANISM  Rhizobium sp. CCGE 510
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Rhizobium sp. CCGE 510"
                     /db_xref="taxon:1132836"
     Protein         1..500
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=52101
     Region          7..500
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mdklpwiils agdnvavata aiapgstvag ietrekidpg hkvaisdipl gaavvkygqa
       61 igrttaevka gdhvhshnlh fendrlaata nsapematse drartfmgyr radgraatrn
      121 yigiiasvnc sttvcraiad eanrtilphy egidgfvpiv hdqgcgmsst gdgmnvlhrt
      181 lagytrhvnf ggvlmiglgc evnqltlygq sgagaskrhf niqdaggsrr averamgmlr
      241 eiaadvgkek rvpmsigeii iglqcggsdg fsgitanpal giaadllaaa ggtailsets
      301 eiygaehllr sravsdevan kldekiawwe dyvalhgasl dnnpspgnkr gglttileks
      361 lgavakggrs pltavygyae rvtapglvfm dtpgydpvsa tgqvagganm iafttgrgsc
      421 fgcrpapslk lssnsalyas meedmdidcg tiatgdatis gkgreifeli vdtasgkktk
      481 selfgygdne fvpwhlgatl
//
LOCUS       WP_007633612             314 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Rhizobium sp. CCGE 510].
ACCESSION   WP_007633612
VERSION     WP_007633612.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CCGE 510
  ORGANISM  Rhizobium sp. CCGE 510
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (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   2  (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   3  (residues 1 to 314)
  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   4  (residues 1 to 314)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Rhizobium sp. CCGE 510"
                     /db_xref="taxon:1132836"
     Protein         1..314
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=34164
     Region          3..312
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 msmieirnvt krygaatvvd nvsmrvekge itvivgtsgs gkstlmrmin rlvpitegei
       61 fvggqnvidv evtelrrkig yaiqghglfp hrtvaqniat vpqlldwdsa riarrveell
      121 glfnldpatf adkyphqlsg gqqqrvgvar alaaepelll mdepfgaldp virgkaqddl
      181 laiqkqfgtt vilvthdmde afhlgnqiav msegrllqcs tpekiltepa dpfvqqltgt
      241 sdralklmsl lplresmepa ksglayalpq slslrdalae miwqgvdeat vqdgekapvg
      301 sismtrllel grka
//
LOCUS       WP_007633624             130 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Rhizobium sp. CCGE 510].
ACCESSION   WP_007633624
VERSION     WP_007633624.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CCGE 510
  ORGANISM  Rhizobium sp. CCGE 510
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Rhizobium sp. CCGE 510"
                     /db_xref="taxon:1132836"
     Protein         1..130
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=14659
     Region          22..98
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mlnqetdanr rdpnaksths liasdrvegt rvygadgkhi gsierliigk ldgrvayavl
       61 sfggflgigh dhyplpwekl nydtqldgyr idltkeqieg apsyadddds wyndngrrvy
      121 dyygvppywm
//
LOCUS       WP_007633649             415 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Rhizobium sp. CCGE 510].
ACCESSION   WP_007633649
VERSION     WP_007633649.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CCGE 510
  ORGANISM  Rhizobium sp. CCGE 510
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 415)
  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 415)
  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
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 415)
  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   5  (residues 1 to 415)
  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   6  (residues 1 to 415)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 415)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 415)
  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 20283677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Rhizobium sp. CCGE 510"
                     /db_xref="taxon:1132836"
     Protein         1..415
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44696
     Region          34..86
                     /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(47..49,58)
                     /site_type="other"
                     /note="non-specific DNA interactions [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            58..64
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            order(59..60,64)
                     /site_type="other"
                     /note="sequence specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238044"
     Site            59..60
                     /site_type="other"
                     /note="putative cAMP binding site [chemical binding]"
                     /db_xref="CDD:238044"
     Region          95..394
                     /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 msplggpeha svappilnpa gganqvrvra ynerlvlslv rlygalskad iarrsglsaq
       61 tvsvimrvle kegllsrgpp vrgrvgqpsi pmhlnadavy sfglkmgrrs adlvlmdfvg
      121 rirmqlhrty ayplpdeila fvtsgiqele drldekqrgr iaglgiaapf elwnwaeevg
      181 apagamevwr dvdlqadiaa hvphpvflqn datsacgael vfgvgpsypd fvyffigsfi
      241 gggivlnsai fsgrtgtaga igplpvrdrn getkqlleia sifvlenmlr ergidpeplw
      301 ysaddwvdfg epmetwiqds akalaqaiva aasivdfsaa vidggfpewv rsrvvqatid
      361 eaakldlqgv vmpeiiegav gaqaraigga slpifarylt dqnvlfkevd haert
//
LOCUS       WP_007634935             100 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Paraglaciecola psychrophila].
ACCESSION   WP_007634935
VERSION     WP_007634935.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola psychrophila
  ORGANISM  Paraglaciecola psychrophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 100)
  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   2  (residues 1 to 100)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Paraglaciecola psychrophila"
                     /db_xref="taxon:326544"
     Protein         1..100
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10788
     Region          38..97
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkklicilll sgvclttsvn lamadptkse isqkhmsrvn lntasleqlv slpglgkkka
       61 aaiieyrakh gkfksvndlv nvkgvgkkml qklknqietn
//
LOCUS       WP_007637725             207 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Paraglaciecola psychrophila].
ACCESSION   WP_007637725
VERSION     WP_007637725.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola psychrophila
  ORGANISM  Paraglaciecola psychrophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 207)
  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 207)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 207)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Paraglaciecola psychrophila"
                     /db_xref="taxon:326544"
     Protein         1..207
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22849
     Region          1..201
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 meqyeteeqq veaikrfwke nglslvigal lglggllgwr yyndsqieak eqasfafeka
       61 seelikgeag fgqaktfies hsdtgyailm afemtqqaie rkdldeavkq lefvvsnakl
      121 savqsiaqlr lariqieqge felalasank vsdkafiaqs qeikgdvyla qqlfdkaraa
      181 ysaaletner dqvlkmkldn lavaang
//
LOCUS       WP_007638720             506 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [unclassified Cellvibrio].
ACCESSION   WP_007638720
VERSION     WP_007638720.1
KEYWORDS    RefSeq.
SOURCE      unclassified Cellvibrio
  ORGANISM  unclassified Cellvibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Cellvibrionaceae; Cellvibrio.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="unclassified Cellvibrio"
                     /db_xref="taxon:2624793"
     Protein         1..506
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54220
     Region          1..505
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mnsiivlhds dnvgickval pagvlfvekd vtlrsdipam hkvairaisk gepilkygqt
       61 igfasqdiaa gehvhvhnca mgdwekdygf skeakttefv pvdqratfeg ykringkvgt
      121 rnyvgilttv ncsatvakai aqhftfsgel nnfpnidgvv amthdsgcgm rsdgegyetl
      181 rrtfngyarh pnfggvmmvg lgcetmqiqr vmeecglads ktftaftiqd vggtrlaiek
      241 gietlramlp lvnecqretv paselviglq cggsdalsgv tanpalgiag dilvrhggtv
      301 ilsetpeifg aehlltrraq spaiaqklld riewwkdyta rndfelnnnp spgnkagglt
      361 tiiekslgaq aksgstnltd vflygeditt kgfvfmdspg ydpvsatgqv asgaqilcft
      421 tgrgsafgck papsiklatn skiyehmned mdlncgkvvd geltleqsgq eifeeilava
      481 sgkktksell gygdnefipw kigavv
//
LOCUS       WP_007638951             302 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Cellvibrio sp. BR].
ACCESSION   WP_007638951
VERSION     WP_007638951.1
KEYWORDS    RefSeq.
SOURCE      Cellvibrio sp. BR
  ORGANISM  Cellvibrio sp. BR
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Cellvibrionaceae; Cellvibrio.
REFERENCE   1  (residues 1 to 302)
  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 302)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Cellvibrio sp. BR"
                     /db_xref="taxon:1134474"
     Protein         1..302
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33551
     Region          51..302
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mshsedrral lrgavagalg lsslaalgae stspkpssst tgstalkgni rhsvarwtfd
       61 fltleelclv vkrlgfsaid ligpkewhil kqhgvdssmc ngaelnledg wgdsrfhqpl
      121 ieryrehidl vadagyknli cfsgnkrgrd peeglkhatk glkkilaqae krgvvlqmel
      181 fnskvnhpdy fadnsawgie lckrldspnf kllydiyhmq isegdiirti qnhhqyfghy
      241 htagvpgrne iddtqelyyp aivraiqatg fkgyvaqefm pnrattaeki eslqaairic
      301 dv
//
LOCUS       WP_007640052             295 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Paraglaciecola
            psychrophila].
ACCESSION   WP_007640052
VERSION     WP_007640052.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola psychrophila
  ORGANISM  Paraglaciecola psychrophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 295)
  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 295)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Paraglaciecola psychrophila"
                     /db_xref="taxon:326544"
     Protein         1..295
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32804
     Region          44..295
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mnnprrnflk smaltgvalg tnvalsivas aseskllplk grinhsvarw tyadltieel
       61 cqtvksigfs aidlvgpkdw pvlkrygids smcngaeinl vdgwihpqfh delverytqh
      121 idlvanagyt nlvcfsgnar gmtkdtglkn avkalqrilp haekkgvvlq melfnskidh
      181 pdymadtsew gvalcqelds pnfkllydiy hmqvnegdii rtiknhhqyf ghyhtagvpg
      241 rneidesqel yypaiakair dsgfsgflaq efipkadnra gkieslrnai qicdv
//
LOCUS       WP_007639126             701 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Paraglaciecola psychrophila].
ACCESSION   WP_007639126
VERSION     WP_007639126.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola psychrophila
  ORGANISM  Paraglaciecola psychrophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 701)
  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   3  (residues 1 to 701)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Paraglaciecola psychrophila"
                     /db_xref="taxon:326544"
     Protein         1..701
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=75721
     Region          6..701
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mafdvdeeil adflveagei lellqvqlve lennpedtnl lnaifrgyht vkggagflsl
       61 telvdichga envfdvmrng qrtlthelmd vilqatdevv qmfdlvkage plvaaeksli
      121 dtltrlskpe lfdkvaaase pksavnitta nesaassdfs eeefeallde lhgndapgak
      181 edkapeetsl ndqdisddef ealldqlhgk gqfkgedkad teqlkespva pepspsgddi
      241 sddefealld qlhgkgkgpa evvseksfsv kesqpaiepp evkkaitppd kvevaqpiia
      301 kkeekksaap pqgettvrvd tkrldqimnm vgelvlvrnr llslstnvnd esmakaianl
      361 dvvtgdlqga vmktrmqpik kvfgrfprvv rdlartlkke itlvlegeet dldknlveal
      421 adplvhlvrn svdhgiempe krkaagkptm gtvkltasqe gdhillsiid dgkgmdpekl
      481 keiavsrgvm dadaasrmtd vdafnlifap gfstkteise vsgrgvgmdv vktkinqlng
      541 tvsidskmgi gttleikvpl tlailptlmi vigkqtfalp lgsvneiinl dmrktntvdg
      601 qltmivrska iplfylgewl argevnidkt kghvvvvqig tkqlgfvvda ligqeevvik
      661 pldellqgtp gmagatitsd ggialildvp gllkryaakk s
//
LOCUS       WP_007640425             272 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [unclassified Cellvibrio].
ACCESSION   WP_007640425
VERSION     WP_007640425.1
KEYWORDS    RefSeq.
SOURCE      unclassified Cellvibrio
  ORGANISM  unclassified Cellvibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Cellvibrionaceae; Cellvibrio.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 272)
  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   3  (residues 1 to 272)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="unclassified Cellvibrio"
                     /db_xref="taxon:2624793"
     Protein         1..272
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30687
     Region          47..245
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 msfldklfkk gqlkgaadsv qseaatstpv pdeyqalwel kkqrqllevk itgtsrsyqs
       61 mimaidlerg llwlddlfpq qlildagdel cirhhrntee lvirapival gssygtsgia
      121 ielpnfayyq prrrfpryti ghqsplsvki rpigqepsfg tlqdisvggm rlmvagnllp
      181 ylrhgavmpl cevnlseelq ircraricaf rmgrspyrht qisiefidle edkrtalgrf
      241 lreqqfntsl elgalqqhrp qtsrangray aa
//
LOCUS       WP_007642259             437 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Cellvibrio sp.
            BR].
ACCESSION   WP_007642259
VERSION     WP_007642259.1
KEYWORDS    RefSeq.
SOURCE      Cellvibrio sp. BR
  ORGANISM  Cellvibrio sp. BR
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Cellvibrionaceae; Cellvibrio.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 437)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 437)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 437)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Cellvibrio sp. BR"
                     /db_xref="taxon:1134474"
     Protein         1..437
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48962
     Region          5..434
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mlnlaevwlw dklvgalawa pdtatatfey tpewiktgvq iaplhmpsha dgthifhfpq
       61 lnrdtykglp acfadtlpdd fgnavinawl arngrdaqsf nplerllysg nrgmgaleya
      121 palrqtqqtn skleleslia maqqvldqrv glngslqhrg nddltailqv gtsaggarak
      181 alvalnktrt eirsgqvdap egfkhyllkf dgvieqgnsr etfgdpqgfg rmeyayylma
      241 kaagirmapc ellmdgerah fltqrfdrig nhkvhyqslc amdhadfkkp gyysyeqlfa
      301 varqlrltra eaveiyrrmv fnivarnhdd hsknigfilp gprmqwqlap afdiaysykp
      361 gspwvnshql nlngkrdnft rrdllsaatl isnftkeakl iieevldvvg qwptyastag
      421 vspeftrein nnlrlsl
//
LOCUS       WP_007643342             733 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [unclassified Cellvibrio].
ACCESSION   WP_007643342
VERSION     WP_007643342.1
KEYWORDS    RefSeq.
SOURCE      unclassified Cellvibrio
  ORGANISM  unclassified Cellvibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Cellvibrionaceae; Cellvibrio.
REFERENCE   1  (residues 1 to 733)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 733)
  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   3  (residues 1 to 733)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..733
                     /organism="unclassified Cellvibrio"
                     /db_xref="taxon:2624793"
     Protein         1..733
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=80430
     Region          1..723
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          <268..>327
                     /region_name="nfrB"
                     /note="glycosyl transferase family protein; PRK15489"
                     /db_xref="CDD:237974"
ORIGIN      
        1 mnldaalqtf faeaedllns meaallrlde gdtdpetine ifraahtikg saglfglndi
       61 vafthivenv ldrardnkil vtgdllsill pcrdhiavli ehamhdhsnd eeclakgqal
      121 lsslqpwled etavkgvala dptpamqady ikslvseser ecwhisvrfg pdllrngmdp
      181 lsimrflasl gdithittit dhlpdyehyd peqlylgfei almssasqqq iedafmfvrd
      241 dseltiippr snidayvnli kslpedskrl geilvkshai syqeldaalt mqkqqaksqs
      301 avsmlgdili egeavapeiv saaldkqkkn serktnpenr firvdaerld tlinligelv
      361 inrqridlla skmgnptlve avtsmgnfte airdaaltlr mvpvgdtfqk fkrvvrdtak
      421 slnkeielei egaeteldrs mveklndplm hivrnamdhg iesiavrear gkpaqgtikl
      481 tachdaghiv igihddgggl dvekirkkai angildesvh lsrqelfqli fhpglstaeq
      541 vtnlsgrgvg mdvvkrniee lqggveiese mgvgtslnir lpltlaiidg fhvvagtidf
      601 ivpqnailec vdlnslnhsh gqncvnlrge qvpyirlrei fslqgsgaer ekivvvqfge
      661 kragivvdel hgeiqtvvkp mgpifqalkg iggssllgtg avalildiqq lisyainreh
      721 lrtsalplta qeq
//
LOCUS       WP_007643470             374 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Cellvibrio].
ACCESSION   WP_007643470
VERSION     WP_007643470.1
KEYWORDS    RefSeq.
SOURCE      unclassified Cellvibrio
  ORGANISM  unclassified Cellvibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Cellvibrionaceae; Cellvibrio.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 374)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="unclassified Cellvibrio"
                     /db_xref="taxon:2624793"
     Protein         1..374
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=42066
     Region          292..373
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mktnflnihd vvllltalec cvlaallnll pakhlqprri lsaffvlial vltttlivwn
       61 gdlkgaainq splvvtilav clllqgpvly fylrslsqkm qllrwwnflh lvpalvaall
      121 lvlfdinsle wwpttelvga entavafiwa lvkisplgyi vacviaeykl renlkalysa
      181 ismselklad avlagfcihw lwsllayvle gqvsagvsds lgiidnyltv ilvnalfvfg
      241 lintrqllsv nampvakpiq ptkmdhkvav iekamnedkl ylesninler faeqtglkpr
      301 disailkmhy qsnffefinr yrveeakrll lspdyknetv leiiyksgfn spsafhrffk
      361 rmvgvtptef rqqg
//
LOCUS       WP_007643536             141 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein [unclassified
            Cellvibrio].
ACCESSION   WP_007643536
VERSION     WP_007643536.1
KEYWORDS    RefSeq.
SOURCE      unclassified Cellvibrio
  ORGANISM  unclassified Cellvibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Cellvibrionaceae; Cellvibrio.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="unclassified Cellvibrio"
                     /db_xref="taxon:2624793"
     Protein         1..141
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=15818
     Region          25..101
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mnyesrdtyg myktgngngp gpslmgaetl vgndvyncqd edigdikeim ldmssgkvcy
       61 avlsfgsflg mgeklfavpw talkldtehk rfildvtkdr lkdapgfdks dwpdmadnsw
      121 sndihtyyrt kpfdkaqrsy e
//
LOCUS       WP_007643770             702 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Cellvibrio sp. BR].
ACCESSION   WP_007643770
VERSION     WP_007643770.1
KEYWORDS    RefSeq.
SOURCE      Cellvibrio sp. BR
  ORGANISM  Cellvibrio sp. BR
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Cellvibrionaceae; Cellvibrio.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Cellvibrio sp. BR"
                     /db_xref="taxon:1134474"
     Protein         1..702
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=76380
     Region          21..702
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mrhsalpaah avkflpkpla mgialalsgg afmslpaiae tkalpkvvvv gtelgdaerq
       61 pgsvgivtee dlelrqprst eealrsvpgv aikpeeesai vanigirgls sadyktlile
      121 dgvpiapglf vgngryynpr iqrmetievl kgaaslrygp stiggvinyi tkqpedgvql
      181 earagsfnsr eatlevggss psqeaqfgaf ithassdgfm dkgydmtdvm iktgmaigdn
      241 qwlgvkisdy dseanisyrg vflqqykdgv denpapddyf isgrrgvdin hewdinattk
      301 lttlvfgset yrdywryntd ntasaaagqw vyldtlngnn rsferfgvds rlklqhqlfg
      361 ianeaefgvr lmnesmddvt vaatratprt gtinkdqves adslalyaqn rfvvterlav
      421 taglrvesye qttknkraat nneadtsnte vlpglgatyq insalqgfas vyeafspaln
      481 gdalngledq kldaersvnv eaglrgardk vnyeltffrm dfdnqiipan snsqfqrtng
      541 getlhqglea algwdlgagf slnssatyip daefvgarrd angnittpdg nrvtyvpewv
      601 tnlsleyktg klrtaisfhh tgeqytdvqn tkpitestsg fftgqidsyt lvdlnaiyef
      661 skdlsisasa knltdenyia slrqgiyvgt ertidvgvkf kf
//
LOCUS       WP_007643851             159 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Paraglaciecola psychrophila].
ACCESSION   WP_007643851
VERSION     WP_007643851.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola psychrophila
  ORGANISM  Paraglaciecola psychrophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Paraglaciecola psychrophila"
                     /db_xref="taxon:326544"
     Protein         1..159
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=17003
     Region          6..157
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkitlntlsk kqkgfslvel mivvaiigii tsiaypsyqg fvvstnrgaa qadlmslaaa
       61 merhkaasfs ykaaaasaad tgkpaifhkh spsaelydnr kydlyiseas gsaylieakp
      121 vtgtsqagng kiafysdgrr awdennngtf staefcwkc
//
LOCUS       WP_007643862             138 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Paraglaciecola psychrophila].
ACCESSION   WP_007643862
VERSION     WP_007643862.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola psychrophila
  ORGANISM  Paraglaciecola psychrophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Paraglaciecola psychrophila"
                     /db_xref="taxon:326544"
     Protein         1..138
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15591
     Region          17..134
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mpiqkkeesl knrvecsnql gvtlielmvv viiigllatl ifpsfeqhil tvrrgdgitq
       61 llrlklqqes frientryae teqlslptse yytfsvtdis aktytmtaka kgsqmddkkc
      121 lamqidqsln ktpahcff
//
LOCUS       WP_007643947             114 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [unclassified Cellvibrio].
ACCESSION   WP_007643947
VERSION     WP_007643947.1
KEYWORDS    RefSeq.
SOURCE      unclassified Cellvibrio
  ORGANISM  unclassified Cellvibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Cellvibrionaceae; Cellvibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="unclassified Cellvibrio"
                     /db_xref="taxon:2624793"
     Protein         1..114
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12356
     Region          9..100
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(26,57..58,60,86)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(26..27,35,38,40..41,43,46..47,49,57,62,69)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 msnssqhkea iylalmtipa gkvvtygela rlaglpgaar lagtlmagls entalpwhrv
       61 inaqgrislp ensparnmqq trleaegvif ergkinlriy synaeptrsn thkk
//
LOCUS       WP_007647193             121 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Shewanella sp. HN-41].
ACCESSION   WP_007647193
VERSION     WP_007647193.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. HN-41
  ORGANISM  Shewanella sp. HN-41
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 121)
  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   2  (residues 1 to 121)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Shewanella sp. HN-41"
                     /db_xref="taxon:327275"
     Protein         1..121
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12677
     Region          51..118
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mktklnitai vsaialtalv aapamaadpv keatkvqtqa kmdvkdaase akkampdtaq
       61 vnintasfeq lqmlkgigaa kaqaiidyrt qngkfkavdd lanvsgigak lieqnrhlmk
      121 i
//
LOCUS       WP_007647407             803 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Xanthomarina gelatinilytica].
ACCESSION   WP_007647407
VERSION     WP_007647407.1
KEYWORDS    RefSeq.
SOURCE      Xanthomarina gelatinilytica
  ORGANISM  Xanthomarina gelatinilytica
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Xanthomarina.
REFERENCE   1  (residues 1 to 803)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 803)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 803)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="Xanthomarina gelatinilytica"
                     /db_xref="taxon:1137281"
     Protein         1..803
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=92032
     Region          2..803
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkylkfivsl vlligiffil ntkfgsvpai geflnpaqgi wqneqdesit gtikieglkd
       61 kvtvhydehl vphifaqnnt dlykaqgyit akhrlwqmef qthasagrls eilgekaldy
      121 drmqrrkgmg fgaenalkkm qkedpeiidf ieaysegvns yiaslnpkdy pveykllgyk
      181 pepwsidkts yllmymidml cgresdleyt nalrllgkdr fdllypdffd vndpiipkkt
      241 dwsyidtait eiplselpqd siaetmdkph pnngsnnwav sgnksysgnp ilandphlgl
      301 nlpsiwfvmq latpehnayg atlpgalgvv sgfntdiawg etnatrdvrd wykiefkdnr
      361 rtqykydntw knttvrveei kikgketyld sviythhgpv sydrtfkgng qkegyamkwi
      421 ghiggnnqrt lidlnaakny ddylkalqhw vapaqnfvfa stsgdialwi qgafankwkg
      481 qgkflmdgsn pehdwqsfip snnnaftknp ergfvssanq hpvdasypfy vfndgyetyr
      541 nrvindffns ketftiqdfk dlqnnnynlk asellpymfk tmdtssltqe eleilntika
      601 wdfnsdidkt gpsiwdlwwk klypltwdef dldntafidp ytyqtiymlk nhpeddfmdi
      661 vetpeketak dlflitfket akeltewkke hgdynwqayk atfvghllqg lpafsrfnlp
      721 iggdrntvna adknhgpswr mivemtsppt algiypggqs gnpgskyydn fidrwaigey
      781 fqalfiqdqn nsediiatqt ltp
//
LOCUS       WP_007647887             278 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Xanthomarina
            gelatinilytica].
ACCESSION   WP_007647887
VERSION     WP_007647887.1
KEYWORDS    RefSeq.
SOURCE      Xanthomarina gelatinilytica
  ORGANISM  Xanthomarina gelatinilytica
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Xanthomarina.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Xanthomarina gelatinilytica"
                     /db_xref="taxon:1137281"
     Protein         1..278
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32262
     Region          6..272
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mkqlfdsssl kcskivtnay stsfslgikl fapsirphiy aiygfvryad eivdsfegyn
       61 qkelfhdfve dykksldrki slnpiinafq evvhnynlht yaddflkrme adlyvtdytt
      121 keayenyiyg sadvvglmcl rvfvnndeak fnalkdsarh lgsafqkinf lrdikddmeq
      181 lgrsyfpnls nnilnnatke eiiddinidl keaykgivql plesrfgvyi ayryylkllk
      241 klkkadseki lsgririsng lkvfiltksy iryklnff
//
LOCUS       WP_007648034             685 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Shewanella sp. HN-41].
ACCESSION   WP_007648034
VERSION     WP_007648034.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. HN-41
  ORGANISM  Shewanella sp. HN-41
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 685)
  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   3  (residues 1 to 685)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Shewanella sp. HN-41"
                     /db_xref="taxon:327275"
     Protein         1..685
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=74594
     Region          1..680
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 meqlllaldl ntpdpeelnt ifraahsikg gsgifgftal tsvthvmenl ldrtrkgtfe
       61 lssaiidlll rtvdtlshil slyreeepid wqevefaknq liaalngepf etnakakdkt
      121 tvatpkvetp itegansrsa spahdedlgf gffeddaela fttegehfgf fdeaytaaei
      181 raddidpkap aiavptgeta sdnladgldd elgfgffetl tsaqldqdii ttgtidpdlv
      241 ssakadklgq qpnehqaaai qtaskrdesh kltqavsrqp rvnsepvaks atkkstipaq
      301 datlrvetsk idtlvnlage lvitqsmltl ignelggelg erlktalnel erntremqea
      361 vmsvrmlpvs fvfnrfhrlv rdlseqlgkn vnlvieggnt eidkgmiekl vdplthlvrn
      421 sldhgienpe krraagksei gelslkasqr ggsiviavhd dgaglnreri lqkarengiq
      481 vadnasdkqv wqlifaagfs talevtdvsg rgvgmdvvrk niealggrid idsvagqgas
      541 feiqlpltla ivdgmsvsvg hqiyilplvh iiesiqpqie qlkflskerl ikvreeylpl
      601 lnlyqlmeie phahtpeqgi vvllesnnkr fglcvdalvg qqqvviksle khyrripgvs
      661 gatimgdgsv alildvesla lhikn
//
LOCUS       WP_007648587             152 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Shewanella sp. HN-41].
ACCESSION   WP_007648587
VERSION     WP_007648587.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. HN-41
  ORGANISM  Shewanella sp. HN-41
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Shewanella sp. HN-41"
                     /db_xref="taxon:327275"
     Protein         1..152
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16637
     Region          2..150
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mkskfyesln rqtlallege ddfvaamanf sallndnlte lnwvgfyvmr geqlvlgpfq
       61 gkvactripm gkgvcgtaaq tnqtqrvadv hqfdghiacd sasnseivvp vrsqgkviav
      121 ldidspvfnr fdeedqkgle llvksfescl fd
//
LOCUS       WP_007649526             290 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Xanthomarina gelatinilytica].
ACCESSION   WP_007649526
VERSION     WP_007649526.1
KEYWORDS    RefSeq.
SOURCE      Xanthomarina gelatinilytica
  ORGANISM  Xanthomarina gelatinilytica
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Xanthomarina.
REFERENCE   1  (residues 1 to 290)
  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   2  (residues 1 to 290)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Xanthomarina gelatinilytica"
                     /db_xref="taxon:1137281"
     Protein         1..290
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33933
     Region          157..218
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
     Region          220..287
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkshftftrk qrngifllil iivslqalyf fvsfskdvdt vdkdglnkfl feidslrlve
       61 ienrkpkvyp fnpnyitdyk gytlgmsnee idrllqfraq dkwvnsakef qqvtkvsdsl
      121 latmspyfkf pewitnpkik kdyinsnath qpknfdqkqd lntatatqlq ringigeays
      181 kriikyreky ggfiadvqlq evyglspevi erlleqftvk tpkqvekidl nqatieqlvt
      241 vqyidyevah hiieqrtlre gyksldellk vksfptnkfe iiklylklnq
//
LOCUS       WP_007650284             376 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Shewanella
            sp. HN-41].
ACCESSION   WP_007650284
VERSION     WP_007650284.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. HN-41
  ORGANISM  Shewanella sp. HN-41
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Shewanella sp. HN-41"
                     /db_xref="taxon:327275"
     Protein         1..376
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=42106
     Region          1..353
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msirltnisk kfgqfqalsp lnldiqegem igllgpsgsg kttllriiag legadsgqiq
       61 fgnrdvtqvh vrerrvgfvf qnyalfrhmt vadnvafgle vipkkqrpsa aeiqkrvnhl
      121 lemvqlghla qrypeqlsgg qkqrialara latqpevlll depfgaldak vrkelrrwlr
      181 slhdelkfts vfvthdqdea lelsdrvvvm snghieqint paelyshpns rfvfdflgnv
      241 nvfeaswqqk rwengeaflt ppeqqvlqqd galyvrshel alsdkpnsqa nlpfnivamt
      301 pigaevrvel aplgwhseel weakfthhnl qelglqkgnv vyatprtgyf fgaqgesspt
      361 rlswpflppg slafdi
//
LOCUS       WP_007651596             388 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Shewanella sp.
            HN-41].
ACCESSION   WP_007651596
VERSION     WP_007651596.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. HN-41
  ORGANISM  Shewanella sp. HN-41
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 388)
  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 388)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Shewanella sp. HN-41"
                     /db_xref="taxon:327275"
     Protein         1..388
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45306
     Region          1..373
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 msspfsprew lqlnmqqqgl lqpqesvpal isrlgyvqid sinvverahh hvlhsrmpqy
       61 qsgmldiala qgdifeywsh aaaylpmady rfslqrkqql qnggkhwfep ddkvmlevra
      121 riraegplka sdfehaegkn gawwdwkpak kaleqlfmrg elmvvrrekf qkcydlterv
      181 lpsyidtqap seaefarhli eryldahafg saaqmaylrk gikahvseql avmqsqgela
      241 sfkaegqwyf yrpelqltsv mpnrvwllnp fdnlliqrqr lkqwfdfdyq ievyvpaekr
      301 qygyyslail wrdcfvgrvd vkaerqsgll llqqltleeg fdgmdedfca afevavteya
      361 rfngcsrwkl mkanhkafkq kyarqqkl
//
LOCUS       WP_007652511             314 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-oxoacyl-ACP synthase III family protein
            [Parabacteroides].
ACCESSION   WP_007652511
VERSION     WP_007652511.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 314)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..314
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34526
     Region          3..313
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mfinatgfyv peervhnqhf lelngltsew ieqrtgiktr skakpeetic tmgmdavrna
       61 lpklpydite vdliisasys pydtvataah ytqrefnitn akalylssac ssflnalevv
      121 egyfamgkat kalilsadkn sayynetdpk aghlwgdaaa affiskervt ekdphiievf
      181 tqglghlgkg pegvqlrprd ggiqmpegrd vfiqactymp knavyllekn gfalddltyf
      241 ighqanmrim sniakqlnlp eekflhniee lgntgsvssa lvyaqndhtf kkgdlvcltv
      301 fgggysagac liqc
//
LOCUS       WP_007653875             548 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Pontibacter sp. BAB1700].
ACCESSION   WP_007653875
VERSION     WP_007653875.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter sp. BAB1700
  ORGANISM  Pontibacter sp. BAB1700
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Pontibacter sp. BAB1700"
                     /db_xref="taxon:1144253"
     Protein         1..548
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=58532
     Region          6..548
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 manntlkihp ednvlvaltd lqagdvvefn grqigivani pakhkfaeqq lnpgqeiimy
       61 gslvgkavea ipaggilttg nvkhqvsgft gktktiswqa pdvskwvdkt flgyhredgq
      121 vgtgnywlvi plvfcenrnv etikqafmen lgfgqqdlyk syvqqmvely qagkteeiaq
      181 lplnsvtsng qqrifenidg ikfltheggc ggirqdsdml callagyihn pnvagatils
      241 lgcqnaqvpi leerikalnp nfskpliile qqkegteqel ltlairrtfl glveankqkr
      301 epaplsklvi glecggsdgf sgisanpavg hvsdlvvalg gksmlsefpe lcgveqelin
      361 rcvsdetadr fvhlmrayar aaeavgsgfd mnpspgnikd glitdaiksa gaakkggtsp
      421 vvdvldygey atrpglnllc tpgndvestt amagsganii lfttglgtpt gnpiapvikv
      481 ssntklaqrm pdiidvdtgp viagektiee mgeamldyii evasgniqsk aqvlgqddfi
      541 pwkrgvsl
//
LOCUS       WP_007653923             304 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Pontibacter sp. BAB1700].
ACCESSION   WP_007653923
VERSION     WP_007653923.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter sp. BAB1700
  ORGANISM  Pontibacter sp. BAB1700
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Pontibacter sp. BAB1700"
                     /db_xref="taxon:1144253"
     Protein         1..304
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=33896
     Region          59..205
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkriltqals lilgcgllas catnpyaatn ksykkqakay akslraipaa pagehtypqg
       61 dywvgttnfn lrkpnfviih htaqnsteht lktftmpstk vsshyvigrd gkvyqmlhdh
      121 mrawhggnsr wgsntdlnss sigieldnng sepfpeemin sliavlgklk kehsipaenf
      181 ighadiapvr kvdpsplfpw ktladngfgl wfdedvleke qvlrevpvgg egdqspllvm
      241 etvpkytlpe hfnpldalri igydvrnpea avrafkihfi qndvnsplte deklilynly
      301 qkyl
//
LOCUS       WP_007654217             160 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Pontibacter sp. BAB1700].
ACCESSION   WP_007654217
VERSION     WP_007654217.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter sp. BAB1700
  ORGANISM  Pontibacter sp. BAB1700
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Pontibacter sp. BAB1700"
                     /db_xref="taxon:1144253"
     Protein         1..160
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17736
     Region          9..157
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 maeslivdqn ltkeekykal mpqiealvtg etdlianlsn mmaalrqgmg ffwvgvyfnk
       61 egqlvlgpfq gpvactripy hkgvcgacft rqetilvpdv eafpghiacs sdskseivip
      121 vikdgevklv ldvdsdkldd fdevdqkyle qlmklveswy
//
LOCUS       WP_007653932             417 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Pontibacter sp. BAB1700].
ACCESSION   WP_007653932
VERSION     WP_007653932.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter sp. BAB1700
  ORGANISM  Pontibacter sp. BAB1700
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 417)
  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 417)
  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
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 417)
  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   5  (residues 1 to 417)
  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   6  (residues 1 to 417)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 417)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 417)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Pontibacter sp. BAB1700"
                     /db_xref="taxon:1144253"
     Protein         1..417
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45545
     Region          29..71
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          93..406
                     /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 msaflaleeg yleklnhver kkhlqkikiv rhlyvkgars nadicnrfni ssptsmalln
       61 elmaeglvek qgrgesvggr kpelyglrnn slfvlsieme kfstrmaifd gnnnnitgih
      121 tfplnlskdl saieelyqha nslvlsagid tdrlmgigls mpglvssreg dsytylltgq
      181 nktplqdlla lkfskpvyiq ndvksitlae yrfgaaqskr dvlvltldwg iglgiimdgk
      241 lrvgtsgfag efghipfidn gvlchcgkrg cletvasgsa larmareglq agqdtllkal
      301 sdhepgkiep qaiiqaaheg dqyainilae tgrnlgkgia mliqlfnpel iiiggkmaea
      361 rqylttpiqq sintycmtql rerteialsk lgaqagilgp vatvmerifd hriestk
//
LOCUS       WP_007654707             475 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Parabacteroides goldsteinii].
ACCESSION   WP_007654707
VERSION     WP_007654707.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides goldsteinii
  ORGANISM  Parabacteroides goldsteinii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Parabacteroides goldsteinii"
                     /db_xref="taxon:328812"
     Protein         1..475
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=53344
     Region          32..468
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mkneqpknag qpktvsvaag nymstdngmp sseemeqavv lailtqstai cevgnrlrpe
       61 mftnpayclv yramlalyqh eadidmlsve remrridpeh atqlnglafi adgmlkvrna
      121 rfiktyaawv ircwvlrqai agmtarmvea repgvdvmaw lnasrkdlek ledefavhst
      181 trtaaevgdr vlaeiydeqe rrrageqlqi ttgidefdhy lgglyrgell vlagrpsmgk
      241 talalhmala aaqqgkkvcf fslemterql isrllctlsg vepdklrfkl mdaddqqrld
      301 kaaaelrklp lflnycsgcg laeirarcmv lnrkhkldlm ivdylnlvnv sadrgevkdt
      361 mdlalgevag glktvsmeqn vaclvlaqln rncetrtdhi pmmsdlrnsg eieqiadsia
      421 mvyrpeqyge lsdpvtresf yhvgrffvik nrnggtgevr fryndsltqi ypykk
//
LOCUS       WP_007656962             343 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Parabacteroides
            goldsteinii].
ACCESSION   WP_007656962
VERSION     WP_007656962.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides goldsteinii
  ORGANISM  Parabacteroides goldsteinii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 343)
  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 343)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 343)
  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   4  (residues 1 to 343)
  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 343)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Parabacteroides goldsteinii"
                     /db_xref="taxon:328812"
     Protein         1..343
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39701
     Region          32..206
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          255..329
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mfitagllnm llkhfgttqa eiseiltglk ydyailqnpt slidanilgv ylehivkktg
       61 ntrigletgf llpfvltgsf fniynqsktv reifenenpf dpainniyaf etkedennfs
      121 leisldsqfk qsypvasqqw iemqcgfflq yaysftgrfl hpirvysmye kegtkdklee
      181 ylgcpvifnh dklilifnks vldlpivtgn kemlaifedy mneiqmhesg qnnslsrtvr
      241 rylmhslsns slslkdvaek fnmserniqr klkaegtsyq kllndlrmel skkylkerip
      301 lpeigfllgf esqsafnkff kkhfrnrpsm fnsnnqsvkt kmk
//
LOCUS       WP_007657249             448 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: replicative DNA helicase [Bacteroidales].
ACCESSION   WP_007657249
VERSION     WP_007657249.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidales
  ORGANISM  Bacteroidales
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Bacteroidales"
                     /db_xref="taxon:171549"
     Protein         1..448
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=50432
     Region          7..439
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 meknvieral lcslfldqva ilevvgllrp emfsdpdhgf iyeaftdlfn rnkrpdlilv
       61 eeemkkkdpe ryvkmggmay lsdgmetvrl ehnaveyare ilhhyllgcm hklfvqkase
      121 clqygmdylk viedcerdll rlrmdnsesd sllplsevmk lsiddhldrm srkddsvrml
      181 tgingldglt gglyrkevlv lgglpsdgkt alamfmamnm arqgkhvlhf sfemtgeqta
      241 arffagyagv eaarlriggl regdidrmrr yaagmektpy yftnvssmsl dalraeimlr
      301 srkgecdvvv idylhtlapl tkrgetqesv irhtitvlkr iaveancaml vvsqlnrevl
      361 krsengfvpi msdlrdsgai efvadcvvii gcperfgknt aqcgsnasrl iklyvlknrn
      421 gstgiaevyr ndtytsfvnp ggnlhfed
//
LOCUS       WP_007657505              97 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Parabacteroides
            goldsteinii].
ACCESSION   WP_007657505
VERSION     WP_007657505.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides goldsteinii
  ORGANISM  Parabacteroides goldsteinii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Parabacteroides goldsteinii"
                     /db_xref="taxon:328812"
     Protein         1..97
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11043
     Region          3..97
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mkstneyltl lrqymdshag kygivrmgif gsvargeqte nsdvdicfea papnlltlar
       61 ikfdleallg swvdlvrlrd rmdeylkrni ekealyv
//
LOCUS       WP_007657899             347 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Parabacteroides
            goldsteinii].
ACCESSION   WP_007657899
VERSION     WP_007657899.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides goldsteinii
  ORGANISM  Parabacteroides goldsteinii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 347)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Parabacteroides goldsteinii"
                     /db_xref="taxon:328812"
     Protein         1..347
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38310
     Region          7..336
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mkvlinnici raissylpee nfemsslans ygekevvsii ratgvervri akcgetssdm
       61 cykaaeyllh keginreeid glifvsqttd yilpatsiil qdrlnlsket vcldihygcs
      121 gfiyglyqaa lwinsdsckn vlilagdtts rmihpldrsl kmvfgdagta tlvsigtkqm
      181 gvsicsdgsg ydrlivpagg fripvsgltn kiefdvdnng rtlenlymdg maifnfaisn
      241 vhkniqglld yidwekseid mfalhqanrf iinyirkklk vdeskvpinv qnfgntgpat
      301 ipllfsdlap eaenvqrvim sgfgvglswg siaiemsdth fykpinv
//
LOCUS       WP_007658471             448 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: replicative DNA helicase [Parabacteroides].
ACCESSION   WP_007658471
VERSION     WP_007658471.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..448
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=50078
     Region          7..443
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mkafekaeaa vissvlsves aiievypvlk pemfshpdla fvysaacsly ekgkradlvt
       61 vdtemhrlde khwkdingva vlndwmiqlr htanlkqyae evkrrymlri lsglfgglkg
      121 kaddfgtsya dligeaeqkl lslretctvg kplrqigava qevlqmhrer letgtdsmri
      181 ltgieafdyv tgglyngelt veagrpgdgk tavamhiamn vamagkhvcf fslemtalqt
      241 lnrlfagyag idanrlrisg anqadlgrme rlaedfkklp lyfdhtsgns vaniraqvkl
      301 qrrkkkcdlv vidylhliqk ersknetvdq aigrivealk qlaqeenipv lllsqmnrns
      361 vnrdgklhlp elhdlrdsgv ieqvadcvyf vyiplkngve ndpvtgeslv dvgelwikkv
      421 rngsvgvary rfnesytlis nysnrkkp
//
LOCUS       WP_007658659             456 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Pontibacter sp. BAB1700].
ACCESSION   WP_007658659
VERSION     WP_007658659.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter sp. BAB1700
  ORGANISM  Pontibacter sp. BAB1700
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 456)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Pontibacter sp. BAB1700"
                     /db_xref="taxon:1144253"
     Protein         1..456
                     /product="amidohydrolase family protein"
                     /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=50258
     Region          23..436
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mkayflllfl ivslyptlaq qpvssrdrev vfrgvslipm dkervienqt vvvkdgkita
       61 igsaskvehs knalivdgkg kylmpglaem hahvppvddl epmkevlqlf tlhgittirg
      121 mlghprhlel rsklqsgell gprfytsgps lngnsvktpg agaemvrqqk qagydflklh
      181 pglnnetfga iastanqigm pfaghvsydv gvwraveagy asidhmdgfv eslvpgleai
      241 peqeaglfam yiadqadttr ipklmtalre kniwvvptqa laerwmspae spetlgnkpe
      301 mkymnpktvq nwvatkqklm adprydaeai nryvdlrrkl ikacndnqvg lllgcdapqv
      361 fnvpgisthq eleylvaagl spyealrtgt vnvgryfdrd digvlkvgat admlllhgnp
      421 lndisqtqri agivightyl petyikqelk kmektr
//
LOCUS       WP_007659727             151 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SPOR domain-containing protein [Bacteroides].
ACCESSION   WP_007659727
VERSION     WP_007659727.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..151
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16813
     Region          65..133
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mkklglllia cfafaafasa qnnivksler nvpgqgkvti hqdarieali gqeyipngte
       61 nrvlksqgyr vqvyagnnts rakneahsvg srikeyfpel svytsfhspr wlcrvgdfrs
      121 ieeadammrq lratgvfkev sivkeqinip l
//
LOCUS       WP_007660995              80 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Pontibacter].
ACCESSION   WP_007660995
VERSION     WP_007660995.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter
  ORGANISM  Pontibacter
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 80)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 80)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 80)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Pontibacter"
                     /db_xref="taxon:323449"
     Protein         1..80
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8357
     Region          2..80
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mkvkvlafgi akdifgssst avelsgeatv ealrtalemq yprlkqlssf miavndeyae
       61 agqelapede vaiippvsgg
//
LOCUS       WP_007662480              96 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Caulobacter sp. AP07].
ACCESSION   WP_007662480
VERSION     WP_007662480.1
KEYWORDS    RefSeq.
SOURCE      Caulobacter sp. AP07
  ORGANISM  Caulobacter sp. AP07
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Caulobacter.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Caulobacter sp. AP07"
                     /db_xref="taxon:1144304"
     Protein         1..96
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10267
     Region          1..94
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mtldealakl raakplldry gvqrvgvfgs targeagpds dvdvlveflp ttlpgfgffr
       61 lerdlaalfg rpvdlvtpdg lhdliqervl geavfa
//
LOCUS       WP_007666010              90 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: zinc ribbon domain-containing protein [Bacteroides].
ACCESSION   WP_007666010
VERSION     WP_007666010.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 90)
  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 10577258
            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="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10275
     Region          5..89
                     /region_name="Zn_ribbon_2"
                     /note="Putative zinc ribbon domain; pfam12674"
                     /db_xref="CDD:463667"
ORIGIN      
        1 memkfcqscg mpltsnevcg tnadgslsad yctycyqngk ftqdctmdem iehcaqfvee
       61 fnkdseqkvt keeaiammkq efpklkrwqn
//
LOCUS       WP_007666914             355 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Caulobacter sp. AP07].
ACCESSION   WP_007666914
VERSION     WP_007666914.1
KEYWORDS    RefSeq.
SOURCE      Caulobacter sp. AP07
  ORGANISM  Caulobacter sp. AP07
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Caulobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Caulobacter sp. AP07"
                     /db_xref="taxon:1144304"
     Protein         1..355
                     /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=39529
     Region          41..299
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mlivevppeg llmsdvqdps rnatptprep raklldierg kglgillvvy ghlvmagslg
       61 epywynltkg siylfhmpff mylsgfvyfh tgshlgrrfg kffqarvdrl lvpflaisll
      121 vvvakilggl lahvddgvsn llsglwavis ngpnnpsisv wylltlfvya vstpflwrlt
      181 hgrwllllai algvqfipap eafylarilr yfiffvlgma acryaptvlk ayrwtlplti
      241 aafavalyvg ramphallic gvlsipvlhg llnlpvfard rvlvwfgens mviylfntla
      301 igvakvlyvr lfpyegawfg llvlvlmisg vfapialkai lrrieaakpv yqyiq
//
LOCUS       WP_007669599             417 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Caulobacter sp. AP07].
ACCESSION   WP_007669599
VERSION     WP_007669599.1
KEYWORDS    RefSeq.
SOURCE      Caulobacter sp. AP07
  ORGANISM  Caulobacter sp. AP07
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Caulobacter.
REFERENCE   1  (residues 1 to 417)
  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 417)
  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
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 417)
  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   5  (residues 1 to 417)
  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   6  (residues 1 to 417)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 417)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 417)
  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 15726307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Caulobacter sp. AP07"
                     /db_xref="taxon:1144304"
     Protein         1..417
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44287
     Region          1..>133
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          79..382
                     /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 matrgatqqs sapynrrivl dvirrrgevs rkeiidlval spqtvanitq dleeiglvvs
       61 krlkgekarg qppmaftldp rggdsigvsl eprrasaalv nlvgevlhrr eveidardqa
      121 atlatmvqlv relqacsada kriwgvgval pgpfdvpgls ftgptafegw tdlsiledlq
      181 katglhvfyn idsaagalge slfgvaqglt gffylhfgvg lggalvvdka aykgangnat
      241 eighipivph gkacycgnhg cleryvslhs lsesvsgdpd veltagqila lldaederlm
      301 dwcrqaaghl rnaiciienm ldpstivigg sapralverl valamplrhs vrggagdgga
      361 ritlserqed ssilgaavlp ihemlspsfd vllqerqgrl evetflggrp sgrantl
//
LOCUS       WP_007673500             658 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Caulobacter sp. AP07].
ACCESSION   WP_007673500
VERSION     WP_007673500.1
KEYWORDS    RefSeq.
SOURCE      Caulobacter sp. AP07
  ORGANISM  Caulobacter sp. AP07
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Caulobacter.
REFERENCE   1  (residues 1 to 658)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 658)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 658)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 658)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 658)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 658)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Caulobacter sp. AP07"
                     /db_xref="taxon:1144304"
     Protein         1..658
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=71022
     Region          21..658
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 maseasgapa ptsaascdvp pqaghdlkgh sflalavgsv gvvfgdigts plyafkealh
       61 atardgvtrp eilgvvslal walilvvtik yvlfimradn kgeggvlslm alaqhaigkr
      121 ttlvfvlgvt gaalfygdav itpaisvlsa veglrtipmf etrvttqmvl liatvmllgl
      181 ffiqsrgtav vgrlfgpvca vwfavmfalg ayhladnpgv faainpyyav sfllhhgmag
      241 fivlgavflt vtgaealsad mghfgrwpiq aawlffvlpc lavnylgqga falqtletan
      301 aaglpmpeln wffemapefl rlplvflaga atviasqavi tgafsltqqa iqlgllprqd
      361 ikrtsetqsg qifvpqlntm llvgvlaimf tfqtssalah ayglavtgtm cvttcmafiv
      421 mrrlwnwktp aalaflipfm tldltflsan alrfftggwl pvligavlft imatwvrgsq
      481 iltektrrds vplvdlmeil raraphrapg taifltsdpd mtpvalmhnl khnkvlhern
      541 vvltvrtadt prvaeedrir tqainadfkk veifygfmes pnvpkalall rkqqglkfdi
      601 matsfflgrr sivpsansgm plwqdriyif lmknaanptd ffkippgrvv elgaqvtv
//
LOCUS       WP_007673725             103 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Cronobacter condimenti].
ACCESSION   WP_007673725
VERSION     WP_007673725.1
KEYWORDS    RefSeq.
SOURCE      Cronobacter condimenti
  ORGANISM  Cronobacter condimenti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Cronobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Cronobacter condimenti"
                     /db_xref="taxon:1163710"
     Protein         1..103
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11307
     Region          5..103
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(7..8,26..27,35,38,40..41,43,46..47,49,57,62,69)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(26,57..58,60,84)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mdnhdtfpqr vyqivaaipq gcvttygeva rlagspraar qvggvlkrlp egsllpwhrv
       61 vnrrgeislt gpdlqrqrqa llaegiqvsg kgeidlaryg wry
//
LOCUS       WP_007674730             192 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Caulobacter sp. AP07].
ACCESSION   WP_007674730
VERSION     WP_007674730.1
KEYWORDS    RefSeq.
SOURCE      Caulobacter sp. AP07
  ORGANISM  Caulobacter sp. AP07
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Caulobacter.
REFERENCE   1  (residues 1 to 192)
  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 192)
  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   3  (residues 1 to 192)
  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   4  (residues 1 to 192)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 192)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Caulobacter sp. AP07"
                     /db_xref="taxon:1144304"
     Protein         1..192
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=20549
     Region          1..189
                     /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"
ORIGIN      
        1 mrvlvidpds araalvaegl agvdplqvrq attfderevl efapdvvvia sdspdrdtle
       61 slressvsnp rpvvmfvdrs epglaeqavr agvaayivdg lsparvrpil dvamsrfalt
      121 qqlrgdlaka kadlesrktv erakgllmke rgldedgayr llrklamdkg rpigavaadl
      181 lafanilkgd as
//
LOCUS       WP_007675000             203 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Caulobacter sp. AP07].
ACCESSION   WP_007675000
VERSION     WP_007675000.1
KEYWORDS    RefSeq.
SOURCE      Caulobacter sp. AP07
  ORGANISM  Caulobacter sp. AP07
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Caulobacter.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Caulobacter sp. AP07"
                     /db_xref="taxon:1144304"
     Protein         1..203
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21300
     Region          10..195
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 msdsqatpdk prlvvgisga sgvvyglrtl dacremgves hlvlsksaal tlaqetglgv
       61 aevnlkadiv hrvgdvgaai asgsyrtlgm ivapcsvrtm sevatgvtss lltraadvtl
      121 kerrplvlmv retplhlghl rtltklaemg aviapplpaf yakpatiaem vdqsvgrald
      181 lfglswrpvk rwgedlvtit gdt
//
LOCUS       WP_007674733             385 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Caulobacter sp. AP07].
ACCESSION   WP_007674733
VERSION     WP_007674733.1
KEYWORDS    RefSeq.
SOURCE      Caulobacter sp. AP07
  ORGANISM  Caulobacter sp. AP07
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Caulobacter.
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
REFERENCE   4  (residues 1 to 385)
  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 385)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Caulobacter sp. AP07"
                     /db_xref="taxon:1144304"
     Protein         1..385
                     /product="CmpA/NrtA family 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=40321
     Region          5..265
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 msgladltlg fipltdcapl vvakslgffa eeglevtlsr easwatirdk vavgaldgah
       61 mlapmalaag lgddgvvaap mlaplalnln gsaitvstal adalravdpe gmaaetvtar
      121 plarlieqrr gqgapplifa vvfphsmhsy alrywlaqag vdpdhdvrlv vtppprvvah
      181 lqsggidgfc vgapwnavav segvgeilik astfwpggpd kvfgvtqawa arrpddlraa
      241 lraliraaaw adepgnhael vallsrpdhv gaepevlara lrqeivfhrd aaglprreha
      301 lwflsqmvrw gqvgpdldle avadqvyrpd lfreaalsvg pvvepamafa dasppppaal
      361 fdgapfdpad argyaagfai srvgg
//
LOCUS       WP_007675085             336 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Caulobacter sp. AP07].
ACCESSION   WP_007675085
VERSION     WP_007675085.1
KEYWORDS    RefSeq.
SOURCE      Caulobacter sp. AP07
  ORGANISM  Caulobacter sp. AP07
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Caulobacter.
REFERENCE   1  (residues 1 to 336)
  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 11482063
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Caulobacter sp. AP07"
                     /db_xref="taxon:1144304"
     Protein         1..336
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=35280
     Region          1..330
                     /region_name="PRK06132"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:235709"
ORIGIN      
        1 mtvtlsrrlm iatavaaglc astahaqgak assaaefarm adqlkpgqwv wapqiapkgp
       61 llvyvdlsrq latvyrngvr iavstissgr agyetptgvf tilqkdadhk snkynsapmp
      121 yqqrltwdgv alhagglpgy peshgcvhlp mgfsqalfki ttlgatvvva gdaakpmqas
      181 dapllapida tgaarppegl daeeyrwtpe rsptgpltiv vskrdqaivv lrngveigrs
      241 raqiadddpg thvinlttgp ggaerwlyvg vpghdadagq pldeaalnrv rmprgfyeav
      301 kgqlkpgati lvtqssvgeg epgrpltild svtptp
//
LOCUS       WP_007675664             753 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Caulobacter sp. AP07].
ACCESSION   WP_007675664
VERSION     WP_007675664.1
KEYWORDS    RefSeq.
SOURCE      Caulobacter sp. AP07
  ORGANISM  Caulobacter sp. AP07
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Caulobacter.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 753)
  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   3  (residues 1 to 753)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Caulobacter sp. AP07"
                     /db_xref="taxon:1144304"
     Protein         1..753
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79514
     Region          1..745
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdeleaikvt ffqeceella dleggllamq dgnddgdtvn avfravhsik ggagafglep
       61 lvrfahvfet lldalrsnei pgtadltavl lrasdvladh vsaarglgmv dmdasaamaa
      121 elkawtdpsa apiaaaaapa eaepefegft pivigaddgm dddddlgfdf qpmtisldaq
      181 aadvavldnv wtvsirpksd lyrkanetgl llrelarlgp iqatlddsal ptlefldaea
      241 ayvtwsvrle teqgeeaire vfefvdgdce leitrgaapv advlaslmdv alpepatpve
      301 apiavapvae apppapvavs apvpatppva anapaaapaa kpaqievpgp gqsvirvdpe
      361 ridrlidlvg elvinqamla qrvgeygiap ssnlamglde leqltreiqd svmairaqpv
      421 ksvfqrmprl vrevanmtgk qarlvmdgen tevdktvier ladpithmlr naidhglesp
      481 eerkaagknp egvvrlaalh rsgrivievq ddgkginrer vlsiavkkgl ispdltltde
      541 eidnliflpg fstadkisdv sgrgvgmdvv krsvqalggr isiasrpglg stftlslplt
      601 lavldgmvvd vagetlvipl aciveslrpk aeeirplgpt gsvlavrdsf vplidvgltl
      661 nyrdrspppt egvvllvege dgsraalvad aihgqrqvvi ksleqnyqqv egvaaatilg
      721 dgrvalildv davinlrrrg ppppadptli aae
//
LOCUS       WP_007676699             217 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein, partial [Caulobacter sp. AP07].
ACCESSION   WP_007676699
VERSION     WP_007676699.1
KEYWORDS    RefSeq.
SOURCE      Caulobacter sp. AP07
  ORGANISM  Caulobacter sp. AP07
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Caulobacter.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Caulobacter sp. AP07"
                     /db_xref="taxon:1144304"
     Protein         <1..217
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
     Region          1..202
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 vggagddvlt grggddildg gagndiligg agadtltgga gsdvaiytdv tsgvtidlav
       61 ttaqntggag tdtlsgiehv fagnafgntl sgdgqlnalv ggagvdving rggddildgg
      121 aggdvlfgwt gadtltggpg ndtfafnygs gadritdfda hgegdvldls gyagtgvtwt
      181 vtqvgadavf tfsmgdtitl tgvtasahhm idtshwa
//
LOCUS       WP_007678120             652 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Novosphingobium sp. AP12].
ACCESSION   WP_007678120
VERSION     WP_007678120.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. AP12
  ORGANISM  Novosphingobium sp. AP12
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 652)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 652)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 652)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 652)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 652)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 652)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..652
                     /organism="Novosphingobium sp. AP12"
                     /db_xref="taxon:1144305"
     Protein         1..652
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=70044
     Region          21..652
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msdgtadasd vpavidpaas tapasghggg sgnitklamg avgvvfgdig tspiyafret
       61 fvgphplaid elhilgvvsl ifwsmtlvvs vqyvgvlmra dnkgqggsla lvalisgvir
      121 krhygglvvl lgvfatslfy gdsmitpavs vlsavegltv vqsdmapfvl pialvllvgl
      181 fviqksgtak vgalfapvmv tyfivlavlg iyhlvqmpev lkalnpwfav qffltdkmlg
      241 flalgsvvla vtgaealysd mghfgrgplr lswfgfvmpc llinyfgqaa milrlddaqa
      301 avamenpffn lapeslrlpl vilasgaafi asqavisgaf sithqamqlg fiprlstrht
      361 sehevgqiyi pfvnwalmtg vivlvlvfqn ssnlasaygi avtgamlidt clmavllial
      421 wkwklwlavp vivtffvvdg ayfaanatkv pdggwfplli ggvaftlltt wnkgrrlmrd
      481 rmteaalpln vfaksahgsa arvpgtaifm astnmgvpsa llhnikhnkv lhervvvltv
      541 evqdgpyvep aerfsvvelg qgfyrmtlry gfmeetdipa alahapmcgg pfemmktsff
      601 lsrqtlvpse kpgmmiwrek lfawmmrnaa sameffrlpt nrvvelgsql ei
//
LOCUS       WP_007678517             289 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Novosphingobium sp.
            AP12].
ACCESSION   WP_007678517
VERSION     WP_007678517.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. AP12
  ORGANISM  Novosphingobium sp. AP12
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Novosphingobium sp. AP12"
                     /db_xref="taxon:1144305"
     Protein         1..289
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31188
     Region          14..256
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mqitkldapr cvggenpvwd ertqtlyyid ntgmrvhsld tltgqsrtle ipsvittlvl
       61 resggaavtl rtgihfldle tgaledihpl patptyvynd gkvdargrfv lgastttfet
      121 pgpdgglfrl dpylrltqld agihfsngpc wspdfktlyf sdswlkttya ydydidtgai
      181 anrrtfiktd elgglpdgat vdvdglvwia iygsskvvaf rpdgsvermi empvrlvssv
      241 afggpdldrl yvttiahgid gapaeegags lyvidglgvs grlesrfag
//
LOCUS       WP_007681693             142 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Cronobacter condimenti].
ACCESSION   WP_007681693
VERSION     WP_007681693.1
KEYWORDS    RefSeq.
SOURCE      Cronobacter condimenti
  ORGANISM  Cronobacter condimenti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Cronobacter.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Cronobacter condimenti"
                     /db_xref="taxon:1163710"
     Protein         1..142
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15306
     Region          5..140
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 msdalslfsl ftssflsatl lpgsseavlv allisakstp wllvitatig nslggltnvi
       61 lgrlfplres srwqaraqgl lqrfgapall lswlplvgdl lcllagwlrl pwgrvifflc
      121 lgkalryivi aaatlqgmtw wh
//
LOCUS       WP_007681716             333 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Novosphingobium sp. AP12].
ACCESSION   WP_007681716
VERSION     WP_007681716.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. AP12
  ORGANISM  Novosphingobium sp. AP12
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 333)
  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 11482063
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Novosphingobium sp. AP12"
                     /db_xref="taxon:1144305"
     Protein         1..333
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=35464
     Region          1..316
                     /region_name="PRK06132"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:235709"
ORIGIN      
        1 mtrtglvlsg almlcalwan paaaqgstas spaefartae rlkpgqwvwa paiapsgpvl
       61 vyvdlsrqla tvyrngvrig vtsvssgkag hetptgvfti lqkdadhhss vynnapmpyq
      121 qrltwdgval hagglpgype shgcvhlpyg fsrslfqits igatvvidgd aidhvrstea
      181 sllapydakg rklasdtlgs qqftwtpers skgqmtiivs kreqrvvvlr sgieigrsva
      241 evadddpgth vvtltrtaag krrwiyvglp ghaeeqgrvv deavmnrihl prrfyesvla
      301 alqpgttili tdsavgtapd epmtvldava ptp
//
LOCUS       WP_007684120             644 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Novosphingobium sp. AP12].
ACCESSION   WP_007684120
VERSION     WP_007684120.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. AP12
  ORGANISM  Novosphingobium sp. AP12
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 644)
  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   3  (residues 1 to 644)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Novosphingobium sp. AP12"
                     /db_xref="taxon:1144305"
     Protein         1..644
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=67523
     Region          1..644
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdelleqfli egrelvaeas kdlsalardp qaaealdgaf raihtlkgsf avfalapaek
       61 llhaaedvld rarrqaslld aaavaglvac ldqtdrwidd versgalpta aeemadraia
      121 llaasahava agmmtgtaah tdwlaaltar etgaiaqaaa pltafrytpd adcffrgedp
      181 lgvvervpal ialavlptgg awpaiadmep facfsiiegl sgaseaevra afrlqpsqit
      241 latveprpvp qdsgeavrdk ailrvdaari daladglgdl ivainglapl adevgsvnra
      301 laarlraaqa dieratgtls rnltrvrlvp lettlrrlpr varqiaqglg keiaftlvge
      361 tievdkqvad glfepllhiv rnaidhgvep pevrrqkgkd akgqvtltfq rqgdaitstv
      421 sddgagidpa rlrasaverg llsqegadal ddaaalrlif ragfstassv teisgrgvgm
      481 davqaaiarl rgsveiesrp gagtrfrirl pvtalttrll vievageryg vsleqvaetv
      541 rideaalmpv grglacvlrd rtipvldlav llnappargr haklvvtyvd gnpvalrvdg
      601 fgeridtvlr pprgilaaap gvigsavlgd ggvllvldlp elaa
//
LOCUS       WP_007684219             293 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Sphingobium indicum].
ACCESSION   WP_007684219
VERSION     WP_007684219.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium indicum
  ORGANISM  Sphingobium indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 293)
  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 293)
  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 293)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Sphingobium indicum"
                     /db_xref="taxon:332055"
     Protein         1..293
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30199
     Region          19..85
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          178..244
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 maeepelesg aaperqpdtp garlraarea qglsiqdvat rtriaqrqle aierddyaal
       61 pgipyavgfa rayaraidvd evaiaadvrs avhnsdlgsn ryeafepadp arvpsralaw
      121 taaaivvllv agfavwrtqv mtpptgeeia aqqaapapaa tkpaagarpa apvvqtvvft
      181 anddvwlriy detgerlkdg lmkkgesftl panarnpmil tgrpqalavt vggkpiaplg
      241 ppdrtiadvp vnaeallara apaagqvqgr sapaapepva pasasgpapa aad
//
LOCUS       WP_007684906             434 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Sphingobium indicum].
ACCESSION   WP_007684906
VERSION     WP_007684906.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium indicum
  ORGANISM  Sphingobium indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Sphingobium indicum"
                     /db_xref="taxon:332055"
     Protein         1..434
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44976
     Region          26..>151
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          55..264
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          71..101
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          106..129
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          290..406
                     /region_name="DedD"
                     /note="Cell division protein DedD (periplasmic protein
                     involved in septation) [Cell cycle control, cell division,
                     chromosome partitioning]; COG3147"
                     /db_xref="CDD:442381"
ORIGIN      
        1 mkrkafakaa vasmligttm vgctgaafrt aavapqkpdr laagiekala drdgaravdl
       61 aeaavqaapq dagyrqllgr ayvadgrfas aetaladamt lgnrdartiv tlalvkvglg
      121 kdraardlla shadivpaad yglamamagd apegvrilse mihdpaatar trqnlayaya
      181 lagrwkdarm magfdldpla anqritqwaq naapglsqqr vaalmgvtid gadagqpaal
      241 alaapsspvr taeaapaeqa veaapvevaa vdpapapspa iadapapmiq aiaapvriaa
      301 prqaaplrav tpprlreapr lqpaafqasg rasghwvvql gaydnaaiak ekwfamarrn
      361 svlanlpvvt sqitvngatf arlavggfde rgeavalcra iqarrgqcfv renaidalpq
      421 rwalatkgrq yasr
//
LOCUS       WP_007685768             642 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Sphingobium].
ACCESSION   WP_007685768
VERSION     WP_007685768.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 642)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 642)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 642)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 642)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 642)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..642
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=69894
     Region          18..642
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 madeitggaa raddegvhdh ghagqkatvk lvvgaigivf gdigtsplya fretfaghhh
       61 leldpdhilg vislmfwsmm lvvtlkyvtv imradnkgeg gslallalin gqtktqrwsr
      121 givllgvfat slfygdsmit pavsvlsave glavynssla plilpaavli llglfwiqgl
      181 gtnrvaslfg pimlfyflti avlgiisivk tpgilhafnp ywavmffvtd plpaflalga
      241 vvlavtgaea lyadmghfgr spirvswlaf vlpalmmnym gqgallfreg aaalhspfyy
      301 lapqwaqlpl vglatlaaii asqavisgaf svtqqaiqlg fmprlriaht sastagqiyi
      361 plinwglmvm villvlvfqt ssnltaaygi avtgamfidn vlltvllyrl wkwrwyysap
      421 llsvlflvdg aylaanftkv pdggwfplli gfviftlltt wsrgrrlvqd rlreaampip
      481 vfvasaansa vrvpgtavfm tstpdgvpha llhnlkhnkv lhervilltv kikdvpvved
      541 dgrckledlg rgffrlvlqy gfmqepdvpa alknvtgcgq afrmmdtsff larqtllpsa
      601 kpgmplwrek ifawmlrnae sameffrlpt nrvvelgsqv ei
//
LOCUS       WP_007686126             265 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Sphingobium indicum].
ACCESSION   WP_007686126
VERSION     WP_007686126.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium indicum
  ORGANISM  Sphingobium indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 265)
  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 265)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Sphingobium indicum"
                     /db_xref="taxon:332055"
     Protein         1..265
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27779
     Region          1..260
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mkisasvsmm frelpllerf aaaaragfdg veiqvidegd paemaqaara agmpvvlmnl
       61 plgdlfaggp glsgvpgrea efasaaergl raaremdarf vhvgpsripp ghdreaclet
      121 yrrnagqala lagrlapdav llvepmnrve mpdalfasid eaadmvrlig sagfgllfdl
      181 yhvamngddi arawaahghi aphvqfsdap grnepgtgsi dfaaafaglr asgyggwhga
      241 eyrpagptta glgwlaemrr lhpsa
//
LOCUS       WP_007686143              77 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein, partial
            [Novosphingobium sp. AP12].
ACCESSION   WP_007686143
VERSION     WP_007686143.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. AP12
  ORGANISM  Novosphingobium sp. AP12
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 77)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 77)
  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 77)
  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 77)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Novosphingobium sp. AP12"
                     /db_xref="taxon:1144305"
     Protein         <1..77
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          3..72
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(7,26..27,45,48,56..57,64,69)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 alpvrltafe wrvlstlmlr ketvvdrrel ldrvyeydad vdsnsleviv grlrrkigae
       61 mirtirgrgy llsaapg
//
LOCUS       WP_007687108             793 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Sphingobium].
ACCESSION   WP_007687108
VERSION     WP_007687108.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 793)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 793)
  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   3  (residues 1 to 793)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..793
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=85065
     Region          1..539
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdellqefis etqetleala gevvaweadp adrdrldaif rffhtvkgsc gflnlprfer
       61 lshaaedvls eiragkriad patvsavlgi mdriaelaea vaigaalpqe nddyliaalt
      121 grlvaaevag pdenesltaa vavarasggq aaprtirlpl slidqlmngv sdmvlarnel
      181 srklrersgd pelesaferl stcvadmrda isktrmqrvd rlftaiprmv rdlgrdlgkr
      241 idlsleggdv emdremvemv vdplthivrn sidhgietpe krralgkpea grlrlearqs
      301 gnqivieisd dghgidtgrl vdkaiaagrl tpeaaarmse aekldlifhp glstanqvta
      361 isgrgvgmdv vranverigg vialdnrpgc gltitlrvpl tltiipgliv ragdlhfaip
      421 raavveilhd nnetlniaqv ggakiatirs vrhsmidled vlgmervaqp gpravmvvrs
      481 atgvpfamgv savenheelv irpasplvma sgvyagmtlp dngkpmllld aaglanaarl
      541 pnivddhaar ragegeeaqg vvemvpalrf eeysgerrll klslierved idarlfgrsg
      601 gcgfvrldgr lvpvanghha fseekvaalr lrdgareacy pvaavldive mpavpdmvam
      661 hgllsgvavi dgehlevinp falfaalpde piaerssgrc lladsedgwt reilapllrq
      721 aghevvmglp adeavdpqdv vlftgsdasq agellgcriv hlratprpag pqdssiyryd
      781 qdalmaalsg sqr
//
LOCUS       WP_007687445             171 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Novosphingobium sp. AP12].
ACCESSION   WP_007687445
VERSION     WP_007687445.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. AP12
  ORGANISM  Novosphingobium sp. AP12
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Novosphingobium sp. AP12"
                     /db_xref="taxon:1144305"
     Protein         1..171
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17813
     Region          23..103
                     /region_name="COG3942"
                     /note="Surface antigen [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443142"
ORIGIN      
        1 mvaaiaisla asvaspamak plqcvpyara hsgidlhgna atwwdqaegt yargqsprag
       61 svlvfkasga mrvghvavvd kivderhvvl nhanwsrpgm ietsamaedv sengdwssvr
      121 vwysptqslg lraspafgfi yapgtqdaap aaptpsrarf eaafadlvpa g
//
LOCUS       WP_007687203             285 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Novosphingobium sp. AP12].
ACCESSION   WP_007687203
VERSION     WP_007687203.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. AP12
  ORGANISM  Novosphingobium sp. AP12
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 285)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Novosphingobium sp. AP12"
                     /db_xref="taxon:1144305"
     Protein         1..285
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=30373
     Region          16..236
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mqagcqgcrs egaafdlama fqpivdcetg rpfafealvr gsngegaaev lskvtaenry
       61 afdqqcrvva itgaveagil atgaklsinf lpnavyspaa ciqltlktar evgfptdrli
      121 fefteneqmi dtdhvrniva syrkmgftta iddfgaghag lgllakfqtd likldmdlir
      181 nvdqseprri ivsgvvaiar algiaviaeg vetvgeydal reigirymqg yllarpgfki
      241 lpipllssdv flfkgarqdg eaaigvhria ppscgsslsh mpasc
//
LOCUS       WP_007687749             176 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Sphingobium indicum].
ACCESSION   WP_007687749
VERSION     WP_007687749.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium indicum
  ORGANISM  Sphingobium indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Sphingobium indicum"
                     /db_xref="taxon:332055"
     Protein         1..176
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18569
     Region          30..121
                     /region_name="COG3942"
                     /note="Surface antigen [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443142"
ORIGIN      
        1 miggfraiva aatlalgali ttpaaagvlq cvpfarqvsg ielygnansw wsqaegryer
       61 gheprvgavl afsasrsmpv ghvamvskvv serevlltha nwsyrggier nvraidvspn
      121 ndwtdvrvwy gpigdlglrp npakgfiyah kageapvqia madratagae aargaf
//
LOCUS       WP_007687947             164 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Novosphingobium sp. AP12].
ACCESSION   WP_007687947
VERSION     WP_007687947.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. AP12
  ORGANISM  Novosphingobium sp. AP12
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 164)
  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 164)
  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   3  (residues 1 to 164)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Novosphingobium sp. AP12"
                     /db_xref="taxon:1144305"
     Protein         1..164
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=17762
     Region          43..134
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mtaarktlgi sraesgpkad vkatfavtga rletlkerak eqrrnpteaq kalwaqlggs
       61 rlggvkfirq sivgsaivdf acpsrwiviq lsaedsnpdv telqdrklte vgirvlrfse
      121 devvanvdav ireinvelav pfdkrsarrk saapapgnym sdeg
//
LOCUS       WP_007688143             316 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Novosphingobium sp. AP12].
ACCESSION   WP_007688143
VERSION     WP_007688143.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. AP12
  ORGANISM  Novosphingobium sp. AP12
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Novosphingobium sp. AP12"
                     /db_xref="taxon:1144305"
     Protein         1..316
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=34816
     Region          2..314
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mirvqnvtkt fgdfaalhgi dleikpgefv allgpsgsgk ttllriiagl efqdggevlf
       61 dgedvssrsv gerqvgfvfq qyalfkhmtv aenvafglsv rrkgrpakad iraraeellr
      121 lvqleglgkr ypgqlsggqr qrvalarala ieprllllde pfgaldakvr kdlrrwlrdl
      181 hesmgltsif vthdqeeale ladrvvvmdh grieqvgtpe qvymepaspf vsnfvgetnq
      241 lpggvharph dielvgeggt pvlvdnvfrr ggswrvegri eghdkvvefd vdasqpapkl
      301 getvqirprr vrefss
//
LOCUS       WP_007688976             281 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Rhizobium].
ACCESSION   WP_007688976
VERSION     WP_007688976.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..281
                     /product="formate/nitrite transporter family protein"
                     /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=29547
     Region          4..250
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 myeetidkls eigkaksvav rrsplafivg samagayigf gdiimftaga hadpawahlv
       61 mgavfasalt ivtfagself tgtaiympla llsrrtsitd tlsvwitcwf gnlvgalala
      121 llfklggggv llgdgnatfi tavaakmnvp sgelfvrgli cnwlvclaiw msyrtqndaa
      181 kailifwpim ifvaagfehs vanmfafala llsdhpatit fygavhnltf vtlgnlaggg
      241 lmialgywvq ssasgqkeaa spemshpstp atknrmpanr g
//
LOCUS       WP_007691042             314 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: aminoglycoside phosphotransferase family protein
            [Rhizobium].
ACCESSION   WP_007691042
VERSION     WP_007691042.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 314)
  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   2  (residues 1 to 314)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..314
                     /product="aminoglycoside 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=35810
     Region          35..237
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mdtvinwaes wltahnyqvf ngpeliravp wskiyrfats rgniylkwsa sayareaalm
       61 ehlaerfpaa ilpvlawnqa idaflmpdgg eplrvklkes ydqqlvgivi gqyariqsat
      121 asnvdallal giddwrmvvf ptlydelvhd egllgregle taeikqlqrs gddvrrlcra
      181 laefkipetl ehcdfhdnnv lvdaegflin dwgdavishp ffslvgflds atrnhgmdvg
      241 spvytglkrt yfdvwldles lerqehvfei arvlrpiefa fnfrrvvrmt takefepcrg
      301 yigealrrfl lkir
//
LOCUS       WP_007692814             423 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Rhizobium].
ACCESSION   WP_007692814
VERSION     WP_007692814.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 423)
  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 423)
  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 423)
  AUTHORS   ter Beek,J., 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 423)
  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 423)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..423
                     /product="CmpA/NrtA family 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=45515
     Region          18..282
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mnssssgsnl aspsrltgeg pkvlragfip lvdasvliaa aefgfarkeg itldlvkdvs
       61 wanvrdrlaf rqfdiahmls pmpvasmlgl gsnpsptitp fslgsggnai tlstrlfdrm
      121 reetglsdla salenarala tvtkqmkarg eqpptlgmty pfsshnyefr ywlaaggidp
      181 dqdvklvvvp ppltsdalaa gaidgfcvga pwnmvaserg vgrivaakqd iwpsapekvi
      241 gmrpdwaesh petvsrllva ldaaarwcdr penhdalaea ladqryiaap vgiirnvlag
      301 efgldakgnr rvidryfsfh agfanyprps qalwilsqmv rwgqsalseh nirmaasayr
      361 pdlyrlalgn daapadadir iegdsdddrf mdgfifdpsd masyvagfav kaktqiassg
      421 eei
//
LOCUS       WP_007692815             432 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Rhizobium sp. AP16].
ACCESSION   WP_007692815
VERSION     WP_007692815.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. AP16
  ORGANISM  Rhizobium sp. AP16
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 432)
  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 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   3  (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   4  (residues 1 to 432)
  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 432)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Rhizobium sp. AP16"
                     /db_xref="taxon:1144306"
     Protein         1..432
                     /product="CmpA/NrtA family 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=46511
     Region          40..301
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mkkilsgsvt rrsllktsgt aalicavkta fpsgalaats gpevsgaklg fialtdsapl
       61 viakekglfa khglpdvdve kqaswgatrd nlvlggaang idgahilspl pylmhtgkvt
      121 qnnqpvpmal larlnydsqa isvakeyadt gvqldasklk vafdakraag keikaamtfp
      181 ggthdlwiry wlaaggidpd kdvstivvpp pqmvanmkvg nmdvfcvgep wneqlvnqgi
      241 gftacttgei wkghpekalg mraewieknp naakallmav meaqqwcdsm dnkdematil
      301 gkrqwfnvpp kdilgrlkgd inygngrvan gtdlymkfwk ggvsypfqsh dawfitenmr
      361 wgkfapntdv kklvgevnrq diwrdaakdl gvaaadipas tsrgketffd gkvfdpenps
      421 ayleslsikv as
//
LOCUS       WP_007694355             377 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Rhizobium sp. AP16].
ACCESSION   WP_007694355
VERSION     WP_007694355.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. AP16
  ORGANISM  Rhizobium sp. AP16
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
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
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 377)
  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   5  (residues 1 to 377)
  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   6  (residues 1 to 377)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 377)
  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 20170283
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Rhizobium sp. AP16"
                     /db_xref="taxon:1144306"
     Protein         1..377
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39459
     Region          <2..>46
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          71..371
                     /region_name="ASKHA_ATPase_ROK_CYANR"
                     /note="ATPase-like domain of
                     cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and
                     similar proteins; cd24073"
                     /db_xref="CDD:466923"
ORIGIN      
        1 mltssqrqll rvisesgpls rtvlaasmgl skaamsgiar dlislgvlhe tetvygqgrp
       61 silldlypeg affvgislle dpapmvlsdl ngkiiaretm plsrdpeiia slvadalpkl
      121 lagqpdaagk lsglgvalsg fvdekqancv qstllgwqdv plariirekt gietfienda
      181 kavavseklf gsardilnfs vvsfgdgigc ahfiggklyr gnhggageia hctielegsp
      241 crcgkrgcld tvasmkaike mskaaglact slteleeeas vgnaaairil hraggalgla
      301 iahliqfndp gmilvthveg nfdgqlgtvm qqaieanvlp ryagqtpirt qrvdsdvwar
      361 gaasiaahnf ligpnpn
//
LOCUS       WP_007694378             399 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Rhizobium sp. AP16].
ACCESSION   WP_007694378
VERSION     WP_007694378.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. AP16
  ORGANISM  Rhizobium sp. AP16
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 399)
  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   5  (residues 1 to 399)
  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   6  (residues 1 to 399)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 399)
  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 15726307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Rhizobium sp. AP16"
                     /db_xref="taxon:1144306"
     Protein         1..399
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41894
     Region          1..>126
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          78..348
                     /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 mdistsipht rqatsravlr tifetapvsr aelarltgls kqsmseivrd letegwlrvt
       61 grtqgsvgrs avtyeleprk afvfgadvgg tkihaalagl tgdiieeaie gtdarggehv
      121 ieqiarmhqa llqksgiaak svamgaigip gaihpktrrl amvpnipglt eltledslrn
      181 rlgldilidn dvnlaalgeq wrgdgrsidn fvfvalgtgi gmgiinegrl irgargaage
      241 istlpigadp fdsrsfaaga lessigsvai rgryealggt pglsvrdmfe reddpvaaiv
      301 idevarlvat slvaiaavvd pervifggsv garpelveri ifylsrcvpv plsctisplg
      361 skagligaia aaldrfratl feipgrgehg kgsitektp
//
LOCUS       WP_007695511             415 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Rhizobium].
ACCESSION   WP_007695511
VERSION     WP_007695511.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 415)
  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 415)
  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
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 415)
  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   5  (residues 1 to 415)
  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   6  (residues 1 to 415)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 415)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 415)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..415
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45008
     Region          31..75
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          95..394
                     /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 msppqdpeet ptsplildps gganqvrvra hnerlvlslv rrhgalskad iarrsglsaq
       61 tvsvimrale kdgllsrgep vrgrvgqpsi pmrlnpdavl sfgvkigrrs adlvlmdfvg
      121 qirmqlhqiy pyplpqdils fvtsgiqele srlnteergr laglgiaapf elwnwaeevg
      181 apdgamevwr gvdlqaeiaa rvpypvylqn datsacgael vfgvgphypd fvyffigsfl
      241 gggivlnssi fvgrtgtaga lgplpvrgrn getlqlleia sifvlenllr dhgfdpqplw
      301 ysadnwidfg epleiwiqet akalaqaiva aasvidfsaa vidggfpnwv rervvratik
      361 eaaeldlqgv vmpeiiegmv gpqaraigga slpifaryli dqnilfkeie haegh
//
LOCUS       WP_007695529             315 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Rhizobium].
ACCESSION   WP_007695529
VERSION     WP_007695529.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium 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   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   4  (residues 1 to 315)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..315
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=33991
     Region          4..313
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mtamielkgv tkrygnatvv dnvsmsmekg titvivgtsg sgkstlmrmi nrlvpisdgh
       61 isvggqdvmd vpatelrrri gyaiqghglf phrtvaqnia tvpellgwdr aringrveel
      121 lnlfhldpgi faakypsqls ggqqqrvgva ralaaepell lmdepfgald pvirgkaqdd
      181 llaiqkqfgt tvilvthdmd eafhlgdqia vmsngkllqc sepekiltep adpfvqqltg
      241 tsdralklms llplkgsmqp prpglgyslp qtlnlrdala emiwqgadea aveddskvlv
      301 gsismqhlie lgrka
//
LOCUS       WP_007698165             583 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Cronobacter universalis].
ACCESSION   WP_007698165
VERSION     WP_007698165.1
KEYWORDS    RefSeq.
SOURCE      Cronobacter universalis
  ORGANISM  Cronobacter universalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Cronobacter.
REFERENCE   1  (residues 1 to 583)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 583)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 583)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Cronobacter universalis"
                     /db_xref="taxon:535744"
     Protein         1..583
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=64956
     Region          29..583
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mfshidrkda rrmaaldmlr gnhghqdpvl lqfarlaslg lgipgcfiav vdkaglpvhl
       61 ahpeplqvda avltqtlced dapvwccdtt lddqarqhpl aasssdvrfy alaplrtrdg
      121 sltgtigmtd tvaqpfnder artlsliagl tgawletlna vgfldpvtrl pnrqklladm
      181 erlsasgsie rytlmifdci dmptayelar slgmpaletl lndlgpllrm klrlksdtvl
      241 ynvatgryal llktrnqkai rrnaavlplv narmlqgini rlnifagevg wqpekttpne
      301 alrraisavh eaiwlnkrhm vfdperdekr nvdfqllhdl sesiaknrgl ylmyqpkikl
      361 stnravgaea lligrhptrg dippgvfipl aqntslmeei tqwvidaalq qlqqwrkqgi
      421 tlplsvnisv sdlsragfad alearvlrag lstndiriec letekalese talcemdmlk
      481 lrgfkilldd fgagysniny lrripidiik ldrsltssia qerssqiivr nviqmlkeld
      541 yvvlaegved aetarlllef gcdeaqgyff srpvepeyia qwi
//
LOCUS       WP_007699729             295 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Rhizobium].
ACCESSION   WP_007699729
VERSION     WP_007699729.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..295
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31889
     Region          19..260
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mtaihdfqgt ilsdtasvlg egptydpdtd tvwwfnilgk elhelhlatg kkqvhelpmm
       61 asvlaridag rqliateegl flrdvatgel tfyaaieadk penrsndgrt hisgslwigt
      121 mgkraemqag aiyhvaggkv tkifdqisip nsicfspdgt mgyftdtrvs qlmrvmvdpl
      181 tglptgepiv lvdsmedpgg idgsvcdadg yiwnarwgsg fvdryspdgl rieryrvpaa
      241 qpscpafvgk dadrlavtta wegldedars tqpqagalle lgpvvkgvfd ppyki
//
LOCUS       WP_007699734             201 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein [Rhizobium].
ACCESSION   WP_007699734
VERSION     WP_007699734.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..201
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=20126
     Region          82..163
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mtgklftsva vgavfatasv lspmafaqaq qpstgndapl tqtapatpdt tkmpqndaqa
       61 patapattta qaggylteqs adqisaktyi gqsvyngqne sigsindlvl lkqggvvaav
      121 vgvggflgmg qknvavpfdk itatqnvedg svklttteta dalkaapefk tlaaqaseka
      181 armpaavpgt dstttssttn k
//
LOCUS       WP_007702545             191 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit [Rhizobium].
ACCESSION   WP_007702545
VERSION     WP_007702545.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 191)
  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 191)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 191)
  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   4  (residues 1 to 191)
  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   5  (residues 1 to 191)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..191
                     /product="TRAP transporter small permease subunit"
                     /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=21143
     Region          3..171
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mkallgfsrl idhvteiigk svswlilvav lvssgnaivr kvfnvssnaw leaqwylfga
       61 afmlaaaytl rqnehiridi lygslsrrvq hwidllghcl flmpfvllmi ydlipyvrms
      121 fmsgevsssa ggliiwpgka lllagfflla lqgvseiikk iaimrgdmdd ptpyvpthap
      181 ldiethagev r
//
LOCUS       WP_007705342             114 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein, partial
            [Enterocloster asparagiformis].
ACCESSION   WP_007705342
VERSION     WP_007705342.1
KEYWORDS    RefSeq.
SOURCE      Enterocloster asparagiformis
  ORGANISM  Enterocloster asparagiformis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Enterocloster.
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   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
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   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Enterocloster asparagiformis"
                     /db_xref="taxon:333367"
     Protein         <1..114
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          23..110
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(42,61..62,80,83,91..92,102,107)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 qvapapapsa seqqgeyvey pdlivnltny sviyrghsve mppkelelly flaaspnqvf
       61 treqlldhiw gyeyigdtrt vdvhikrlre kikdhanwai ttvwgigykf evkr
//
LOCUS       WP_007705469             306 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Sphingobium sp. AP49].
ACCESSION   WP_007705469
VERSION     WP_007705469.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium sp. AP49
  ORGANISM  Sphingobium sp. AP49
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 306)
  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 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   3  (residues 1 to 306)
  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   4  (residues 1 to 306)
  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 306)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Sphingobium sp. AP49"
                     /db_xref="taxon:1144307"
     Protein         1..306
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33731
     Region          56..305
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <207..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 maeymwvrsa npegksysll hlqagqsael eavrvcssti saslvaqerd eqvagqwysg
       61 dsyffnlslt grplsargrf egmeggyhpv gelffipagq rylaqggpgs qrtlfvelav
      121 dqqlrdelki gtdaapvwrt cmnmpfdrvr dilhrmarev repgfaselm veglgvtlla
      181 etlrilrqme anaarkggls pwrlrtiear iqdgatlptl gelaelcgls rrqlmrafre
      241 etgrtvgafv qdltldraka llqhtdlpig evaaqvgftt atafstafrr sigesprsfr
      301 atrskt
//
LOCUS       WP_007706392             330 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Enterocloster asparagiformis].
ACCESSION   WP_007706392
VERSION     WP_007706392.1
KEYWORDS    RefSeq.
SOURCE      Enterocloster asparagiformis
  ORGANISM  Enterocloster asparagiformis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Enterocloster.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Enterocloster asparagiformis"
                     /db_xref="taxon:333367"
     Protein         1..330
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36965
     Region          13..213
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mrkdggfkee gnwykgnlhs htvdsdgclt pgeavelfae hgysflgisd hdvysdyreq
       61 lnrenfiiip aveasavlwk detltqrlkv hhvhgilgpe svrkqavlpl mrhgeavqpr
      121 mfygewdgaa vaqemsdylr srgcltiynh piwsrvreed fadtdgllgl eifnyntvne
      181 sgtgfdttyw dailrkgrql ygfaaddnhn sgefddacgg fimvkapalt hemivsalme
      241 gefyassgpl ihdwgvcgrr vwvkcspvyr vnfiaggpvn agltvmcntr edgleyaeve
      301 lkgnetyvri ecadvygrta wsnalflnwp
//
LOCUS       WP_007706472             456 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: replicative DNA helicase [Cronobacter].
ACCESSION   WP_007706472
VERSION     WP_007706472.1
KEYWORDS    RefSeq.
SOURCE      Cronobacter
  ORGANISM  Cronobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Cronobacter"
                     /db_xref="taxon:413496"
     Protein         1..456
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=49872
     Region          4..427
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mrqdieasvi gglmiggltp masevlatle pesftiplyq kafrviqkqa rnrnlidmlm
       61 vaeecgdehf gdiietaksc psaanlkgya gmvadnhhrr lvlqlmdemr gpiqsgtida
      121 sgqamdelvk rlsairkprd evrpvhlaev ineyadvlek rqcngeesdt lktgiyelda
      181 itggmnaqdl viiaarpgcg ktelalkiae gvashampgg errgvlifsm emsnlqiaer
      241 siagagmlpv nalrnparld degwarisng isaligldvw lvdassltie qirsiaerhk
      301 qehpnlslil adylglikkp kaerndlaig hisgslkama kdlrtpvicl sqlsrdvekr
      361 pnkrpnnsdl rdsgsieqda dsiimlyrea vydenspaap faeiivtknr fgslgtvyqr
      421 fvhghftscd qdearqkctq aaapkqkgqr yalpdv
//
LOCUS       WP_007706580             276 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Sphingobium sp. AP49].
ACCESSION   WP_007706580
VERSION     WP_007706580.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium sp. AP49
  ORGANISM  Sphingobium sp. AP49
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 276)
  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 276)
  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   3  (residues 1 to 276)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Sphingobium sp. AP49"
                     /db_xref="taxon:1144307"
     Protein         1..276
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31405
     Region          2..100
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 maqtpierkf akacrsagle ieaeqqvgry rpdfivrahk laieldghdt hssvedrird
       61 grrqrylqrl gwtvlrftgr eihldvdacv aevmdfvqal gvpapvyaiy idwlffqrai
      121 vdferrnaah laqrgaisrd tflqvlplvi dmpetvavhl fgtastfsds arkleasrvm
      181 thegrsfvie ehqaefmaie lldhlkahrp tyqnrvvlva ddgayppefm dadphlaali
      241 rkdadrsrmm tiraakwqdi dylfaqiagv plhemv
//
LOCUS       WP_007706639             202 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Sphingobium sp. AP49].
ACCESSION   WP_007706639
VERSION     WP_007706639.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium sp. AP49
  ORGANISM  Sphingobium sp. AP49
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Sphingobium sp. AP49"
                     /db_xref="taxon:1144307"
     Protein         1..202
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=22238
     Region          17..202
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 meptthrera levvrhrgia rgrdfdaagv tratlqrlrd egvlqqvgrg lykladanvd
       61 sstslaeavr iqprgvicll salqfheltt qtphavwmml gqkdwapvnp svalkivras
      121 gealtagvet hvidgvpvpi tvpaktvadc fkhrnkigid vavealrdfm ksrprpdlna
      181 iyryaeldrv qsvirpylea mt
//
LOCUS       WP_007707252             632 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Enterocloster asparagiformis].
ACCESSION   WP_007707252
VERSION     WP_007707252.1
KEYWORDS    RefSeq.
SOURCE      Enterocloster asparagiformis
  ORGANISM  Enterocloster asparagiformis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Enterocloster.
REFERENCE   1  (residues 1 to 632)
  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 632)
  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 632)
  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 632)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Enterocloster asparagiformis"
                     /db_xref="taxon:333367"
     Protein         1..632
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=67015
     Region          9..627
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mdkkltyqkv vtavcmlvsl faviihvgny ttftmpsilf yawhlliglv liflykplgg
       61 skelspgmrt lcravdwili altavvsfyv ifnfetyttt mqnnmmtkel yvfgiiitll
      121 vleagrrmlg nvlpiiaiva iiyaltgdki pglfghrgys mqrvvlaifs drgvygtpig
      181 tsatnvylfl lfaaflsvsg adiifqniai aaagrkrggp akmaviasaf fgtisgscva
      241 nvvstgafti plmkrngypk kfagaveava stggqimppi mgaaafvlsd vagvpyaevc
      301 iaailpalmy yiclvkmvdl eavkhnlagl sedevpnlke slargmklfi pvgvllfmml
      361 glkttpmkaa ifataailvt gvldskdrmt lkgvvngava agkslcsvva acstagivva
      421 vfsltglglk fsnfivqlgs nslipslila mlvcailgmg lpttaayivc ataiapaltg
      481 lglpilaahl flmyfasisa itppvavasy aaagiaeenp mkvglqavkl gitgfilpfa
      541 falnpdyitf gwnlqtlltw isgmvvcysl aimlqgyves ritvlerlay lavivlaitp
      601 ymlnsligfv lfaalygfrk wqakraplla ss
//
LOCUS       WP_007707689             223 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Sphingobium sp. AP49].
ACCESSION   WP_007707689
VERSION     WP_007707689.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium sp. AP49
  ORGANISM  Sphingobium sp. AP49
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 223)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Sphingobium sp. AP49"
                     /db_xref="taxon:1144307"
     Protein         1..223
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=23076
     Region          55..218
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mnqdrrrfll sasvlvagav gtarasapgp mralkpmlpa qsiaptltpt ppalvkpalf
       61 aqaraamerh pqiinrqrma lvdfaapssd prlhivnlld gtatsylvah gsgsdpdhsg
      121 wlehfsnapg snascagafl tadpyvgkhg asqrligldp tnsnalsrai vlhgawyaep
      181 avasvrgklg rsqgcfavgd svkaqvmaql gqgsliyaak lva
//
LOCUS       WP_007708011             486 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Sphingobium sp. AP49].
ACCESSION   WP_007708011
VERSION     WP_007708011.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium sp. AP49
  ORGANISM  Sphingobium sp. AP49
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 486)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Sphingobium sp. AP49"
                     /db_xref="taxon:1144307"
     Protein         1..486
                     /product="amidohydrolase family protein"
                     /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=51748
     Region          29..463
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mktllaalla atallplpaa aktapahadl lirhatlvdv ehgrlvpdqa vatkgdriva
       61 vgddgtiaaa wragksveak grylipglwd mhvhfgggpd lveenkallp lyiangittv
      121 rdasgdlpyd vlrwrgeiad grlfgptlls sgpkiegikp vwkgtletgs eadvdqaiak
      181 lkeldvnfvk itdstlkpel flyavhqarg aglrasghip maltvgqaid agissiehid
      241 yahkagvkde aritadfaag kidraqasaq ldagfdeata maayrdmaar gvfvtptlsi
      301 srtvayldqn dhstdpelay igprlrktyd wrieraakat pdqiaqrhai yehnaailpl
      361 lqqagvtima gtdagflnsf dypgfalhqe lalyvdrglt pvqalasatr agpawfglld
      421 rygavaegkq admvlltanp ledihatkai davilrgtlq drarldalla etkakvaawn
      481 aaatrp
//
LOCUS       WP_007708194             615 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Enterocloster asparagiformis].
ACCESSION   WP_007708194
VERSION     WP_007708194.1
KEYWORDS    RefSeq.
SOURCE      Enterocloster asparagiformis
  ORGANISM  Enterocloster asparagiformis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Enterocloster.
REFERENCE   1  (residues 1 to 615)
  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 615)
  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 615)
  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 615)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Enterocloster asparagiformis"
                     /db_xref="taxon:333367"
     Protein         1..615
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=65764
     Region          2..602
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mlkrlsfala vlfcifhcwt amfgaaagig qkaihlglvl iiffldylaq edrkwycrvm
       61 daffilasag sliyimsidk tidlrsgmiy tydilfgvll iitlieatrr avgkslaivv
      121 icfivygfmg qhmpgflahv gmditritsv vylgtdgiyg taiyasasyi vlfvilgavf
      181 netgvgdyft klasrafgkf rggpakiavv asglfgsisg saianvigtg tftipmmkkc
      241 gfedeyaaav easastggqi mppvmgataf liaeylgipy fdlvkaalip avlfyvailm
      301 tvdlyarknn ikgvpeselp twkelvknvy lilpliyliv smsvfkmsvt ksgitsiiat
      361 ivctlfsarn ritpaklkki vkasingakp vaiacgvvgi iigivmgsgl gfrmssvliq
      421 vsnghlgill vltmvvslil gmgvpttaay lmlallvvpa lkqmnvlpla ahlfifyfgi
      481 isnvtppval aayaaagvar cnptktgvfa fklslsgfil pfmfvynpvl lmqggaleil
      541 qslitallgi yslsaalekf vfkwninqae rlvllasall liipgtitdl igfavllgif
      601 liktaeekkg nyaka
//
LOCUS       WP_007708267             387 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Enterocloster asparagiformis].
ACCESSION   WP_007708267
VERSION     WP_007708267.1
KEYWORDS    RefSeq.
SOURCE      Enterocloster asparagiformis
  ORGANISM  Enterocloster asparagiformis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Enterocloster.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Enterocloster asparagiformis"
                     /db_xref="taxon:333367"
     Protein         1..387
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=40935
     Region          <1..386
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mifqgyvrpd gtvgsrnlva vipsvvcand vaqaivaqvq gtvglyhhqg ccqlppdldr
       61 vtetliglgc gpnvgaalvv slgcegtdhe rlveeiartg kpveiiriqq lggvskaiaa
      121 gidaasrlvr aiapqqrrea diskvvlaik cgasdttsgm asncalgyva dklvdlggtv
      181 vfgetteflg aehilkrrav naqvadkide ivarmesrak slgcdmrkgq ptpgnieggl
      241 ssieekslga ivksgtrpiq gvmeytdrvg drkglwikdt pgrepeiltg mactgaqlmm
      301 fstgrgapqg fptmpvvkvc gnpityrnme ndmdinagli iegkksieqv geevfekive
      361 vlnggmskne slhyyssidi ytlgpvi
//
LOCUS       WP_007708569             117 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein, partial
            [Enterocloster asparagiformis].
ACCESSION   WP_007708569
VERSION     WP_007708569.1
KEYWORDS    RefSeq.
SOURCE      Enterocloster asparagiformis
  ORGANISM  Enterocloster asparagiformis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Enterocloster.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 117)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 117)
  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 117)
  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 117)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Enterocloster asparagiformis"
                     /db_xref="taxon:333367"
     Protein         <1..117
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          26..112
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(45,64..65,83,86,94..95,105,110)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 emilrikall rraqivnehr itlgpvvldy daltvsrgge vqtlprkefy llykllsypg
       61 kiftrvqlmd eiwgmesesd dntinvhvnr lrrrfegype fsietirglg ykavknl
//
LOCUS       WP_007708825             626 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Enterocloster asparagiformis].
ACCESSION   WP_007708825
VERSION     WP_007708825.1
KEYWORDS    RefSeq.
SOURCE      Enterocloster asparagiformis
  ORGANISM  Enterocloster asparagiformis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Enterocloster.
REFERENCE   1  (residues 1 to 626)
  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 626)
  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 626)
  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 626)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Enterocloster asparagiformis"
                     /db_xref="taxon:333367"
     Protein         1..626
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=66570
     Region          1..613
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mrkltgfwdy vvkalsvcli lfqlyttgvr lfsdmiqrsi hlafvltlvf ilkparkghd
       61 ldhvpwydvi faavscagcl yvvsiyktvv ynplqwlsav dkvfavllvi lvleasrrsv
      121 gwtfpvlgia fliyafwgea fpgmwahqnf sfnkvfqsfy hgttgiwgtm lglsatmlam
      181 fgifgailsg tggaetfiki gqrvagratg gsgkisvias slfgmisgsa ignvvatgvf
      241 tipsmqragy skewsaaiea isstggqilp pimgaaafim aqligvnylt iakaalvpav
      301 lyylscflsi hlvskrdqic gepdkptirv geylvilipl gifmfyllrg ytvmmgafwa
      361 tigavvtyav wflvseksvg kcagamgrvc fttaikgtns ivemcgilag sqitislvsl
      421 tgfgvklsdl ivslgegnlf lclicsmlvc ivlgmglptt aayvlgasvl apalialgis
      481 plpahlfvmy yaclsaitpp vcvavfmasg lakaawvrva liscmvslpa fvvpftfiyn
      541 palmldgsaf qvvfgiatal agvclidmcv tgywkrpval pmrllllacg illlipdvwi
      601 slvglaagsv sffavqrggg dgvtik
//
LOCUS       WP_007709591             121 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Sphingobium sp. AP49].
ACCESSION   WP_007709591
VERSION     WP_007709591.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium sp. AP49
  ORGANISM  Sphingobium sp. AP49
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Sphingobium sp. AP49"
                     /db_xref="taxon:1144307"
     Protein         1..121
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=13869
     Region          11..89
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mvemmtehrg dliasdrveg tvvynrqgek lgkishfmvd krsgqvryal lsfggflgmg
       61 nehyplpwsm lhydtdkggy vielakevle qaphylvedr pafddaygrn vyqyygliyp
      121 w
//
LOCUS       WP_007710404             103 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Cronobacter dublinensis].
ACCESSION   WP_007710404
VERSION     WP_007710404.1
KEYWORDS    RefSeq.
SOURCE      Cronobacter dublinensis
  ORGANISM  Cronobacter dublinensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Cronobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Cronobacter dublinensis"
                     /db_xref="taxon:413497"
     Protein         1..103
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11318
     Region          5..103
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(7..8,26..27,35,38,40..41,43,46..47,49,57,62,69)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(26,57..58,60,84)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mhnhdtfpqr vyqivaaipe gcvttygeva rlagspraar qvggvlkrlp egsvlpwhrv
       61 vnrrgeislt gpdlqrqrqa liaegvqvsg kgeidlsryg wry
//
LOCUS       WP_007710493             193 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Sphingobium sp. AP49].
ACCESSION   WP_007710493
VERSION     WP_007710493.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium sp. AP49
  ORGANISM  Sphingobium sp. AP49
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 193)
  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 193)
  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   3  (residues 1 to 193)
  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   4  (residues 1 to 193)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 193)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Sphingobium sp. AP49"
                     /db_xref="taxon:1144307"
     Protein         1..193
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=20934
     Region          1..191
                     /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"
ORIGIN      
        1 mriviiddsg lratvleegl reagyddihi vpprgafvar lermapdvvl mdlgspsrdt
       61 leemltvsra larpiamfvd qsdeamigaa idagisayvv dglrkervkp vlelavrrfn
      121 afakiqaele eartalsdrk vidraksilm nqrglteqda yallrssamn qgkkivdmaq
      181 alitasdllg gal
//
LOCUS       WP_007711367             177 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Sphingobium sp. AP49].
ACCESSION   WP_007711367
VERSION     WP_007711367.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium sp. AP49
  ORGANISM  Sphingobium sp. AP49
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Sphingobium sp. AP49"
                     /db_xref="taxon:1144307"
     Protein         1..177
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18567
     Region          30..121
                     /region_name="COG3942"
                     /note="Surface antigen [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443142"
ORIGIN      
        1 miggfralfa aamlalgafs avpatagvlq capfarevsg iqlfgnantw wnqaagqydr
       61 gheprvgavl sfaasrampv ghvamvskvv serevlltha nwsyrggver nvraidvspn
      121 ndwtdvrvwy gplgnvglrs npangfiyag kpgidqpvqi aladrataga dsargaf
//
LOCUS       WP_007711673             165 aa            linear   BCT 20-JAN-2025
DEFINITION  division/cell wall cluster transcriptional repressor MraZ
            [Sphingobium sp. AP49].
ACCESSION   WP_007711673
VERSION     WP_007711673.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium sp. AP49
  ORGANISM  Sphingobium sp. AP49
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Chen,S., Jancrick,J., Yokota,H., Kim,R. and Kim,S.H.
  TITLE     Crystal structure of a protein associated with cell division from
            Mycoplasma pneumoniae (GI: 13508053): a novel fold with a conserved
            sequence motif
  JOURNAL   Proteins 55 (4), 785-791 (2004)
   PUBMED   15146477
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449500
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Sphingobium sp. AP49"
                     /db_xref="taxon:1144307"
     Protein         1..165
                     /product="division/cell wall cluster transcriptional
                     repressor MraZ"
                     /GO_function="GO:0000976 - transcription cis-regulatory
                     region 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=18548
     Region          7..138
                     /region_name="MraZ"
                     /note="DNA-binding transcriptional regulator and inhibitor
                     of RsmH methyltransferase activity [Translation, ribosomal
                     structure and biogenesis]; COG2001"
                     /db_xref="CDD:441604"
ORIGIN      
        1 msdvilysgn afsvadgkgr fvlplemrrq vklasggenr lclsvhmdng catgfglshk
       61 lflfeeveel erlarvadrp fngdlerenr lgtiedvnfd eggrfflhpd ikeeagitda
      121 vffygvgryf qiwkpealve spdrpalirn kvrrwldqra aeggk
//
LOCUS       WP_007711774             314 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Sphingobium sp. AP49].
ACCESSION   WP_007711774
VERSION     WP_007711774.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium sp. AP49
  ORGANISM  Sphingobium sp. AP49
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 314)
  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 314)
  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 314)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Sphingobium sp. AP49"
                     /db_xref="taxon:1144307"
     Protein         1..314
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32215
     Region          17..87
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          180..246
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 madepeletg aesapeaqps tpgaklraar eaqglsvqdi atrtriaqrq leaierddya
       61 alpgipyavg farayaravd ldevaiaadv rsavhntdmg atryeafepa dparvpsrtl
      121 awtaaviaiv viagftiwrt qlltpptgee iaeqqeqrpa qsqqpaagap vaapvtgpvv
      181 ftavddvwlr iydeagerlk dgtmkkgesf tlpadakgpm iltgrpqalt vtvggkaiap
      241 lgaadrtiad vpvnaealla raapaaagqv paavpartpa rtsapvgtps iqapvpasat
      301 papapetpap sagn
//
LOCUS       WP_007711786             118 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Enterocloster asparagiformis].
ACCESSION   WP_007711786
VERSION     WP_007711786.1
KEYWORDS    RefSeq.
SOURCE      Enterocloster asparagiformis
  ORGANISM  Enterocloster asparagiformis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Enterocloster.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Enterocloster asparagiformis"
                     /db_xref="taxon:333367"
     Protein         1..118
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12830
     Region          2..100
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(3..4,22..23,31,34,36..37,39,42..43,45,53,58,65)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(22,53..54,56)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mdfyqrvgiv craipagkva tygqiallcg kprnarqvgy alnrgragad vpafrvvngq
       61 gvlsgaqafs rpntqkklla gdsirvsadn rvdlkrfgwh ntldealflr qeferlgi
//
LOCUS       WP_007712381             673 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Enterocloster asparagiformis].
ACCESSION   WP_007712381
VERSION     WP_007712381.1
KEYWORDS    RefSeq.
SOURCE      Enterocloster asparagiformis
  ORGANISM  Enterocloster asparagiformis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Enterocloster.
REFERENCE   1  (residues 1 to 673)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Enterocloster asparagiformis"
                     /db_xref="taxon:333367"
     Protein         1..673
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=71136
     Region          299..378
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          410..528
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(479..480,483,501..504,506)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
     Region          <539..>610
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
ORIGIN      
        1 msedqkklqd sgpehekkpv rrsrsreaaa arraekeras sepaagapag eqgksdsgfp
       61 kkpaggsrek srtawlpala gfvgvllcag iafyvyaaqa yktvffpntv ingadvsdrt
      121 vdevkaafsa gadryrltvv ardgsgeeit gqdiglhtvf dgglekilea qnpyrwvfhl
      181 rtprvyqigt mlkwdeeala revnglecmd esamvrprda ylsdyiegrg yevvpeeegt
      241 alkaeavqta asaavrsldp eisleelgcy ekpsvrsddp glaaerdarn ryvnvtvtyt
      301 fgdrtevlng srthewltgt gtdialdeaq iaeyvselak tyntaykpra fktsygptvn
      361 vsgsygwrin qkeeaaqlkg ileagesvtr epvysqtaaa hgdadygnty aevnltaqhl
      421 lfykdgnkil esdfvsgnvs rghttpagly sltykqrdav lkgegyaspv kywmpfnggi
      481 gfhdaswrss fggsiyktgg shgcvnmpya aakelyenvy agmpvicynl pgteskaptk
      541 asgkppaggq atqptkpaap ggqtaqpnvp atqpnvpatq pnvqptqpnv qppaggqeaq
      601 pgdqatqpgg qeaqpggqpp qpeptqasgt pggpeitpve ngttaagggg sgggygpafg
      661 saqstegggp gvs
//
LOCUS       WP_007712985             579 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Sphingobium sp. AP49].
ACCESSION   WP_007712985
VERSION     WP_007712985.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium sp. AP49
  ORGANISM  Sphingobium sp. AP49
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Sphingobium sp. AP49"
                     /db_xref="taxon:1144307"
     Protein         1..579
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=63670
     Region          10..>397
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 masgngtvdr lyygdnldil rahitdesvd lvyldppfns nasynilfrs pagtgadasi
       61 eafddtwswg paaagalmdi tnsgnhrlyv lmqamrtaig enammaylvm mavrlqelhr
      121 vlkssgslyl hcdptashyl klvldavfgv enfrseiiwr rtsshnklst qfgpvhdtif
      181 fysrsrdiif hpgrtphlrk yisgafrysd drgayrlnel tgagiragas glpwmgydpt
      241 arsrhwaipa slkallpldq qdappqqmld llhqagevvl sasgrptykq rlgqgtvyqd
      301 iwayqpgtdg clidteegid advkwldsed eklgyptqkp iglleriiaa ssnpgdvild
      361 pfcgcgtavd aaqklgrrwi gidithlaig liekrlregy gnaarfetig sprdlasaqr
      421 lavddphqfq hwitlklggw pwmggkkggd kgvdgyfyyv geggqtrtgv isvkaghnvn
      481 pamvrdlgrv mqrdghrigl fvcaaaptrg meqeadshgl vqtefgrfpa lqiftlaelf
      541 vdrhprlppl vspnrkapri etrvshqpga qagldfgdl
//
LOCUS       WP_007714466             197 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase, partial [Enterocloster
            asparagiformis].
ACCESSION   WP_007714466
VERSION     WP_007714466.1
KEYWORDS    RefSeq.
SOURCE      Enterocloster asparagiformis
  ORGANISM  Enterocloster asparagiformis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Enterocloster.
REFERENCE   1  (residues 1 to 197)
  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 197)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Enterocloster asparagiformis"
                     /db_xref="taxon:333367"
     Protein         <1..197
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
     Region          <1..195
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 hckdqgvvyr alkagfgsvm ydgsslpfee nlqntldvcr vahacgasve aelgslaage
       61 rshegsagdv eaytdpeaak qfvdgtgvda lavsvgtvhg lykgkpniri dilnainekl
      121 nmplvlhggs giperdilec irhgiakinv nteisvyavd qtklylesaa phfselslrq
      181 vgyvkeivkk yisffre
//
LOCUS       WP_007713898             232 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Sphingobium sp. AP49].
ACCESSION   WP_007713898
VERSION     WP_007713898.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium sp. AP49
  ORGANISM  Sphingobium sp. AP49
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Sphingobium sp. AP49"
                     /db_xref="taxon:1144307"
     Protein         1..232
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=25844
     Region          3..157
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mtdipmietp spnfderslp vtmlvlhytg mpdaasainw lanpeskvsa hyvvtedgqi
       61 irmvgedkra whagrshwrg iddvnsasig ieivnpghew gyrpfpeaqm gsliplihdi
      121 vqrhritrgn ivghsdiapa rkqdpgelfp wgqlarlrla lprptknlmd phwtdsgfml
      181 alerfgydia epqpavvafq rrfrpelidg ivdgecrail lalllpkptg dd
//
LOCUS       WP_007715094             308 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Enterocloster
            asparagiformis].
ACCESSION   WP_007715094
VERSION     WP_007715094.1
KEYWORDS    RefSeq.
SOURCE      Enterocloster asparagiformis
  ORGANISM  Enterocloster asparagiformis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Enterocloster.
REFERENCE   1  (residues 1 to 308)
  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 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   3  (residues 1 to 308)
  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   4  (residues 1 to 308)
  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 308)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Enterocloster asparagiformis"
                     /db_xref="taxon:333367"
     Protein         1..308
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35049
     Region          42..302
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <195..302
                     /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 mrkkvhhiey rneskeellp dfspdfpyis scaeldqcle gfipwhwhke velfymesgs
       61 leyytpggvl vfpagsggli nsnvlhmtki hekgrpvaql lhifdpslvg grqgsrieqk
      121 yvapivtssq leaiplspdv pehgpvleal rrsfqisdse yayeirlrga lsaiwsdllp
      181 laepmlreka ghdkandqik ammiyihehf seklpvaria asayiserec yrvfhdclht
      241 tpaeylrsyr lqtachllae sqesltfiah acglgnssnf gkifkeqmdc tpseyrrkwq
      301 drdmhgqe
//
LOCUS       WP_007715715             380 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Enterocloster asparagiformis].
ACCESSION   WP_007715715
VERSION     WP_007715715.1
KEYWORDS    RefSeq.
SOURCE      Enterocloster asparagiformis
  ORGANISM  Enterocloster asparagiformis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Enterocloster.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Enterocloster asparagiformis"
                     /db_xref="taxon:333367"
     Protein         1..380
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42785
     Region          1..269
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          265..356
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mklihlsdlh igkrvnefsm ledqeyilke iigmigreep dgviiagdvy dkpvppaeav
       61 rlfdwfltql admdrpvfvi sgnhdsperl sfggkllssr kvfvapvydg kvnpvelrdr
      121 hgsvfvyllp flkpaavrrc fpeaeidsyd gavrfaleqi rsgeefcpea rnvlvahqfv
      181 agatscesee lsvggldqva adafdgfdyv alghihgpqk agpnlrycgt plkysfseag
      241 hkksmtivrl eekgnvevet lpltplrdlr eirgsyeelt srafyqgtav gdylhitltd
      301 eedileaigr lraiypnvmr ldydnkrtrs gqtvetaaqr rkspeelfae lyelqnnqpm
      361 sreqqelagk mieelweetr
//
LOCUS       WP_007715878             381 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Brevibacillus sp. BC25].
ACCESSION   WP_007715878
VERSION     WP_007715878.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus sp. BC25
  ORGANISM  Brevibacillus sp. BC25
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 381)
  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 381)
  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   3  (residues 1 to 381)
  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   4  (residues 1 to 381)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 381)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 381)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Brevibacillus sp. BC25"
                     /db_xref="taxon:1144308"
     Protein         1..381
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39455
     Region          39..372
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(111..113,134..135,183,235,259)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkkwgsviva ttltfslava gcanqgastg gadaseilvg vilpvtgnna tdgkdmqnai
       61 emavkkinds ggvvgkklki evaddgcdpq mattaanklv sqnvvavvgg ycsgatlpss
      121 gvfknanipm ivpaansakl paqgydtlfl ingltpdqaq taadymaanq akkvvlihdn
      181 sayakdladf akasveksgg tviayeainp eekdfsalvt kikglqpdat yftgyyaagg
      241 lmvkqfkqkg vsglffagdg sfsedvikia gadnaeglli tatptsefie gaeaftseyk
      301 qtynnmapgp fsalsynavn lladaigran stdrdaikka iketkdfkal gqtisfnsqn
      361 tldtsnfavl kvtggkftla k
//
LOCUS       WP_007716893             208 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase, partial [Enterocloster
            asparagiformis].
ACCESSION   WP_007716893
VERSION     WP_007716893.1
KEYWORDS    RefSeq.
SOURCE      Enterocloster asparagiformis
  ORGANISM  Enterocloster asparagiformis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Enterocloster.
REFERENCE   1  (residues 1 to 208)
  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 208)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Enterocloster asparagiformis"
                     /db_xref="taxon:333367"
     Protein         1..>208
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
     Region          1..>208
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mlvnmneilr yaeekgccvg afdtpnleil mavlraaekr nepviiqhaq lhepempiri
       61 igpimvrmak easvpvcaml dhgedmdyvr talelgfsav midgsskpyd envsltreav
      121 alakeygasv eaeigivtgh egrefhieep gaaytdpela arfvrdtgid alaasvgtvh
      181 gfyatqpkld fdriekikel tglplvmh
//
LOCUS       WP_007718038             341 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Brevibacillus sp. BC25].
ACCESSION   WP_007718038
VERSION     WP_007718038.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus sp. BC25
  ORGANISM  Brevibacillus sp. BC25
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 341)
  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 341)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Brevibacillus sp. BC25"
                     /db_xref="taxon:1144308"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38946
     Region          20..198
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          244..326
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mksdrikfpa gfwaglqrlg iaphdlvrka rlpttiltep avvttaqyfr iwqaytdlig
       61 dtaigiikls ttfetaqypp tvlatyhard yrdalnrmvr ykqlcpperl riteegehct
      121 ielewmhseq pgppvlvgtt lafllelgrr gtgkrltaqs vefsqsmgdv taleayfgcp
      181 irigasvnrl tlyrrdldsl flsynkelle iltpvldrsl deecshsiae mvkwilkrsl
      241 tggrldirav aselgmsdrt lqrrltdect tfkqlltqar heqareylad pkldikevaf
      301 llgyedqnsf yrafrlwegd tpsnwrseyf rvnpsvkefp s
//
LOCUS       WP_007718234              74 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein, partial
            [Enterocloster asparagiformis].
ACCESSION   WP_007718234
VERSION     WP_007718234.1
KEYWORDS    RefSeq.
SOURCE      Enterocloster asparagiformis
  ORGANISM  Enterocloster asparagiformis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Enterocloster.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 74)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 74)
  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 74)
  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 74)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Enterocloster asparagiformis"
                     /db_xref="taxon:333367"
     Protein         <1..74
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          <1..66
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(17..18,36,39,47..48,59,64)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 efdlflflmg npgriisate lyqkvwctgk pdaansvavy iarlrhklee sqfvgrietv
       61 rgegyryvpt sktr
//
LOCUS       WP_007718509             237 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Brevibacillus sp. BC25].
ACCESSION   WP_007718509
VERSION     WP_007718509.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus sp. BC25
  ORGANISM  Brevibacillus sp. BC25
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 237)
  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 18524722
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Brevibacillus sp. BC25"
                     /db_xref="taxon:1144308"
     Protein         1..237
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=26155
     Region          51..157
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
     Region          168..234
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mvnrtitrll icfaailllt vsfpveieig qkivyaehsl piisdqgiit ievyprkhkl
       61 ivkkhgktvk tyqvavgnps tptpvgeyki iskgkdwgps fgprwlglnv pwgiygihgt
      121 nkphsigqhl shgcirmrnn dvielfkmip lgtkvtiygh ilgdpshdpr dlaegdvggd
      181 vqliqsrlks agyyhgvcdg kfrssttaal kkfqrdrkli pngvvskkvy eelglle
//
LOCUS       WP_007718542             372 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Brevibacillus sp. BC25].
ACCESSION   WP_007718542
VERSION     WP_007718542.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus sp. BC25
  ORGANISM  Brevibacillus sp. BC25
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Brevibacillus sp. BC25"
                     /db_xref="taxon:1144308"
     Protein         1..372
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=41136
     Region          5..369
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mvekknvlvl ncgsssvkyk lyempsktli ahdyleqiqr dqyedairgv feslkqysid
       61 ivshrvvhgg eafkqsviin dqvkdeirnl srfaplhnpi nltgievaqs lfpdlihvav
      121 fdtafhqtmp pssylyalpy eyyeeygirk ygfhgtshry vmgraaemmg rpkeqlrlis
      181 chigsgvsit airngesydt smgmtplagl smgtrsgnid pgiipyieei ektdtagaik
      241 ilnnnsglmg vsgvsndlrd vmkkaeeghh rsklalelft tilhkhvgly larlngvdgi
      301 iftagvgens savrelvcag leyagvnldr evnrtskgea fistkyspvk vmviptneel
      361 vmamdafelg hk
//
LOCUS       WP_007719779             189 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Enterocloster asparagiformis].
ACCESSION   WP_007719779
VERSION     WP_007719779.1
KEYWORDS    RefSeq.
SOURCE      Enterocloster asparagiformis
  ORGANISM  Enterocloster asparagiformis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Enterocloster.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Enterocloster asparagiformis"
                     /db_xref="taxon:333367"
     Protein         1..189
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20600
     Region          2..156
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mlkdlllncr syrrfhqevs ipagdledmv dntrltasas naqalkfkiv ntpaecakvf
       61 stvkwagalt dwdgpaeger psayiiiacd lslgrnkqwd dgiaaqtiml savekgyggc
      121 migsfnrsel aqaldldpqt ysldlvlalg kpaetvvlap lnadgsttyy rdkdqvhyvp
      181 krcledili
//
LOCUS       WP_007721012             377 aa            linear   BCT 20-JAN-2025
DEFINITION  GerAB/ArcD/ProY family transporter [Brevibacillus sp. BC25].
ACCESSION   WP_007721012
VERSION     WP_007721012.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus sp. BC25
  ORGANISM  Brevibacillus sp. BC25
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Brevibacillus sp. BC25"
                     /db_xref="taxon:1144308"
     Protein         1..377
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=42532
     Region          11..365
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 mstsiresam vspffvfflv hanivgvgil gfqrtivaha gydawislll agasihlivw
       61 mlysmlnags hdlfsihelc fgkwlgklms lvvliyvwma aflilrsyvs ivkqfifplm
      121 htwsttliil llilyivagg frtvtgvcff gvvipailml plflfpfeya hpnnlfpmfs
      181 hnlpslfasa kdavinymgf eilffyypfi kraahsqkwa hagvlfstll yvavaivtfl
      241 mfshgeldki iwptltmlki veipilqrle fivislwlfv ilpniclnlw gvtrgmkqif
      301 gisqiralll llvslamgsy liegttplll aldfygkvsi vfiyvyipll fllfllwgkk
      361 rsttgyqtpg aetekar
//
LOCUS       WP_007721211             687 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Carnobacterium sp. AT7].
ACCESSION   WP_007721211
VERSION     WP_007721211.1
KEYWORDS    RefSeq.
SOURCE      Carnobacterium sp. AT7
  ORGANISM  Carnobacterium sp. AT7
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Carnobacteriaceae; Carnobacterium.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 687)
  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   3  (residues 1 to 687)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Carnobacterium sp. AT7"
                     /db_xref="taxon:333990"
     Protein         1..687
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76175
     Region          1..676
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          171..249
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 mdenskyldl ffeetdehlq slneqvlele nnpedssivd vmfrsahtik gmaatmgydt
       61 maklthkmen vfdllkqkii padatsiali fdcldtlsdl vedlreenda erditnlvqr
      121 ldhvssgesa lveavtveqe tgsllnlsle kvedsdlmii eaakedgyna yvlairidee
      181 ssmknarvyl vmskleqhgd vlysepgtea lenddfgtif kliyvsklde etvlnlaldn
      241 seiaevliqt iqqaddllvq qaeksqtepq eklveeqeiv elveatqata kapgkakaqn
      301 hamnqsirvd igkldsfmnl vselviyrtr ledlsdqllv semkeplehv arisselqel
      361 vlkirmqpvs tvmtrfprmi rdlgndlgke fnlviegedt eldrtvvsel seplvhllrn
      421 sadhgvempe erlrlgknpk glikitayqe gnrvvltltd dgkgvnpvvi kasaerkgis
      481 tegmsdkeiq qlifhpgfst aqevtsisgr gvgmdavkqk itelggtvel esivgkgtvf
      541 kinlpltlsi iqsllvkvgq atfaiplgii ktivkvkeed iirvhnrevy kyeglavpvv
      601 rlhkaldvav teesnlhlvl vkqgdnynal avddlvrqqe ivikklgqel nmlknylgat
      661 ilgdgsivli ldasaicnes igeysei
//
LOCUS       WP_007721621             326 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Carnobacterium].
ACCESSION   WP_007721621
VERSION     WP_007721621.1
KEYWORDS    RefSeq.
SOURCE      Carnobacterium
  ORGANISM  Carnobacterium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Carnobacteriaceae.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 326)
  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   4  (residues 1 to 326)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Carnobacterium"
                     /db_xref="taxon:2747"
     Protein         1..326
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=36754
     Region          1..314
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 milfenvske yekgkpvvsn idleikdgef fvfigpsgsg ktttlkminr lipltsgfir
       61 idgkpisdyn lqelrwnigy vlqqialfpn mtveenitiv pemkkwsked mqnrvtelld
      121 svglepeayr krktaelsgg eqqrigvira laanpdiilm depfsaldpi skhnlqqdva
      181 klqkklnktv vfvthdmqea lalgdriclm nngkieqigt pddirrhpkn dfvrnflqtg
      241 indfkespti qqiiatgkle vreavegmgp ylaledtvdt lvvalareef vnikenegnl
      301 igkitkqqll dylaqeiqve kesmvr
//
LOCUS       WP_007722206             285 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Carnobacterium sp.
            AT7].
ACCESSION   WP_007722206
VERSION     WP_007722206.1
KEYWORDS    RefSeq.
SOURCE      Carnobacterium sp. AT7
  ORGANISM  Carnobacterium sp. AT7
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Carnobacteriaceae; Carnobacterium.
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   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 285)
  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 285)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Carnobacterium sp. AT7"
                     /db_xref="taxon:333990"
     Protein         1..285
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30940
     Region          1..69
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          <95..>127
                     /region_name="PutP"
                     /note="Na+/proline symporter [Amino acid transport and
                     metabolism]; COG0591"
                     /db_xref="CDD:440356"
     Region          207..274
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mneigeklke arkakgytld dlqqmtkiqk ryliaieegn ydvmpgkfya rafikqyadt
       61 vglngdqlle eytdavphth deeyvekvst dqtrsgknte nvfltkvqey lptiliglla
      121 vaivaaiyfa viktnnqgne dmitkesdei tvssadsise eesvkesses avseeseeaq
      181 giellssngs tttysvtgif egssliltas ggdswvsveg dgttidaqli tdgsnletei
      241 pdgtsslvvi ignapatkvn fngkdvpyap eaensvrqei efkfe
//
LOCUS       WP_007722812             297 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Cronobacter dublinensis].
ACCESSION   WP_007722812
VERSION     WP_007722812.1
KEYWORDS    RefSeq.
SOURCE      Cronobacter dublinensis
  ORGANISM  Cronobacter dublinensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Cronobacter.
REFERENCE   1  (residues 1 to 297)
  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 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   3  (residues 1 to 297)
  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   4  (residues 1 to 297)
  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 297)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Cronobacter dublinensis"
                     /db_xref="taxon:413497"
     Protein         1..297
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33267
     Region          29..179
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          208..288
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mnrdsvcrki adeirrlkek ekmlaflppe vrllygttpg artpviyqpg iiflfsghkt
       61 gylndkvfry dpreyllltv plpfecetfa tpqeplaglr inidllqlqa lvmeigeddh
      121 frpapcscgi nsgvltdeil caverllevl etpldarilg kqvvreilyh vlkgpgggal
      181 lalvsrqthf slisralrri etryaetltv eqlaaeanms vsafhhnfka vtstsplqyl
      241 ktwrlqqarl lmlhngmkas aaamqvgyes asqfsrefkr yfgvtpgeda armrama
//
LOCUS       WP_007722633             400 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Brevibacillus sp. BC25].
ACCESSION   WP_007722633
VERSION     WP_007722633.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus sp. BC25
  ORGANISM  Brevibacillus sp. BC25
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 400)
  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 400)
  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
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   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   5  (residues 1 to 400)
  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   6  (residues 1 to 400)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 400)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 400)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Brevibacillus sp. BC25"
                     /db_xref="taxon:1144308"
     Protein         1..400
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43709
     Region          18..>84
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          77..393
                     /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 mrrtgdlkli qelnrsiild tirhygpisr seiakrnkls pttvtsavse lirdsfvcev
       61 gtgesnggrk pilvqfspds rfligisisg skitiaemnl eavvkrkevh sikpyqgesv
      121 laylmdiieq flrgaaslet cmgisivtqg ivdsvhgvir ynpklrlqna avkemieqrf
      181 qmktwldndt nayllaekti gdfshyqnml yvtigdglga silmngaiyr gfkggagefg
      241 httidragvr cdcgnvgcle nyvswptiys klvsslakgk tsrisdlveq dvgritpavf
      301 rqalaeqdsl avsileetas ylasglvnli hlfnpeviil ggeiafenel liakvkdyvg
      361 eyahgiltee leirpnslge nvevagaaav llqdtfqfsl
//
LOCUS       WP_007724713              76 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyl carrier protein [Carnobacterium].
ACCESSION   WP_007724713
VERSION     WP_007724713.1
KEYWORDS    RefSeq.
SOURCE      Carnobacterium
  ORGANISM  Carnobacterium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Carnobacteriaceae.
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   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 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   4  (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 10011594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Carnobacterium"
                     /db_xref="taxon:2747"
     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=8689
     Region          1..74
                     /region_name="acpP"
                     /note="acyl carrier protein; Provisional; PRK00982"
                     /db_xref="CDD:179197"
ORIGIN      
        1 mtfekiqaii vdqldkeese vqletnfred leadsldlfq iindiedefd ikieseegli
       61 tvqnivtfve aelakk
//
LOCUS       WP_007724789             266 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Carnobacterium].
ACCESSION   WP_007724789
VERSION     WP_007724789.1
KEYWORDS    RefSeq.
SOURCE      Carnobacterium
  ORGANISM  Carnobacterium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Carnobacteriaceae.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Carnobacterium"
                     /db_xref="taxon:2747"
     Protein         1..266
                     /product="formate/nitrite transporter family protein"
                     /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=29260
     Region          12..263
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 metqntglmy nieksimkkq nlydnsksry fvramlaclf ltlgtavavm igqageeiap
       61 glgkmlyafm fswslvmiiy mnaelgtsnm mymtvaiqrk lmkpkkalai lfycilfnli
      121 ggiiaslvis ftykfhalps dhylftavag klaktplqif segifaniiv ntavfctirm
      181 kddagkiiam ifiififayl gfehvianfs sfalaffasg gsvpgmtlga vltnwgmall
      241 gnyvggalii gvlyswlnkn qteyvd
//
LOCUS       WP_007725814             395 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator
            [Carnobacterium].
ACCESSION   WP_007725814
VERSION     WP_007725814.1
KEYWORDS    RefSeq.
SOURCE      Carnobacterium
  ORGANISM  Carnobacterium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Carnobacteriaceae.
REFERENCE   1  (residues 1 to 395)
  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 395)
  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
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 395)
  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   5  (residues 1 to 395)
  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   6  (residues 1 to 395)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 395)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 395)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Carnobacterium"
                     /db_xref="taxon:2747"
     Protein         1..395
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44265
     Region          23..60
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          76..388
                     /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 mkitkrqkel qtkildiiyt kgplsridis qatgitpatv sdivgnlive qlihetgeiv
       61 sdtnksgrkk isldispnhs fyigvelsek ffayclidnk qnlfekkilt ndpstpernl
      121 taslfvtelh sfllhcsnyh pqsigialpg hfdeenqsil tnnsfwtnfn fkqllstinl
      181 pvyfknnvhc mtlserlfgh dstdnnftfv hvgrgmfcss iyqsnlygdn nnlvgeighi
      241 vvhpdgelce cgkrgclqty aseswiikks qilfdksdst ylrqlatdra hltievilqa
      301 yklgdegvin ilhnaikyls itlnnlsmmi dadkmiihge lfsekqlldl ikdyleknia
      361 llatkkktli eiknysaing alsaaglcva kqlls
//
LOCUS       WP_007729272             240 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Brevibacillus sp. BC25].
ACCESSION   WP_007729272
VERSION     WP_007729272.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus sp. BC25
  ORGANISM  Brevibacillus sp. BC25
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 240)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Brevibacillus sp. BC25"
                     /db_xref="taxon:1144308"
     Protein         1..240
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=27056
     Region          <11..235
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mnvvlakepp ypvfqplvhl ttgqffgyea llrssthhsp eflfrkarae ghlyeldtls
       61 mkkamesyft svpfhdhvpl lfinvfpstl lnpaflsfit eglfgawnsr ivleineane
      121 edkmweisll gqkirelrqh gflialddvg sgaaslkkiv eyepdivkld ryfgkqlssm
      181 pkkqklvslf vqycqdqtql vlegieeped lsvalalgvp vgqgfllghp eplqatqkrr
//
LOCUS       WP_007730072             314 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phytoene/squalene synthase family protein
            [Rhodococcus].
ACCESSION   WP_007730072
VERSION     WP_007730072.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..314
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34814
     Region          4..303
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mnalpasyef cedvtrehgr tyflatrllp vprrravhal yafarvvddi vdepsgpher
       61 gtvladvera avnaldnpta tggfpstvpl dltrvlpafa davktfdipr ayfdaffesm
      121 rmdapdtakf rpvyntmdel seymygsavv iglqmlpilg vsvpqqeavv pasnlgeafq
      181 ltnfirdvge dldrgrlylp agefaafgvd iemlehgrrt gtvdvrvkra lahfiavtrg
      241 ryrsaesgip mldrrvqpsi rtafvlygai ldqveradfr ilhrrvsvpg rtrlrvaapg
      301 lvrsatyaak nrmr
//
LOCUS       WP_007732756             345 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Paraburkholderia
            hospita].
ACCESSION   WP_007732756
VERSION     WP_007732756.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia hospita
  ORGANISM  Paraburkholderia hospita
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 345)
  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 345)
  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 345)
  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 345)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Paraburkholderia hospita"
                     /db_xref="taxon:169430"
     Protein         1..345
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=37352
     Region          27..343
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 msgfnsgrrl alkqgfamaa asaasglltg tparaagqvy syklgialda thpttvnlta
       61 aaaeiarasn grlnirvfpn sqlgndtdmi sqvragaidf vstagliwgt lvpvasisgi
      121 gfafpgydqv wkamdgelga hirgefakvn lmplpkiwdh gfrqvtsssr qintpqdlng
      181 fkirvplspa lttmfkafga apaginmaet ytalqtrvvd gqenpltilq tqklyevqky
      241 csltshvwdg fwlvanlrtw nalpedlrql aattfdayav kqrqavaaln srlrdelkgr
      301 gmvfnqpdvq vfrdylskag fyagwqqkfp agswalleky agrla
//
LOCUS       WP_007733546             361 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Rhodococcus].
ACCESSION   WP_007733546
VERSION     WP_007733546.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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 11438136
            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="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37128
     Region          18..354
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msglhvdiei perdvvatfd vaagevtavl gpngagkstv laavaglhhp rrglielnsr
       61 vltdtgrgva laphrrgtal laqeallfph lsaaanvafa prsagrsrrd sadsarhwld
      121 avdaaeladr kpsqlsggqa qrvavarala aepellllde pmsaldvasa palrsllrrv
      181 lrtgdrtavl vthdaldala ladtvvvldg grvvergdvr tvltrprsaf aariaginlr
      241 sgtmagdgml rspvgvdiag qtetdlpags aavavfepra vsvyldpphg sprnafavti
      301 aeienrgdvv rvraedeagq pglsaditas aaaeldlvpg saatfvvkat etliyaqgag
      361 s
//
LOCUS       WP_007734244             401 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Rhodococcus].
ACCESSION   WP_007734244
VERSION     WP_007734244.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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   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 401)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..401
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45772
     Region          18..399
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 msevvslaaa rrialaaqgf gkshpttvtr rnlvgvmdrl qvlqidsvnv fershylpvy
       61 arlgaydksr ldqlaftpgs gyleywghea tflpvdmwpl frwrmdqfra kalsdkdgwa
      121 sdrrvfldwl rqelrdngpm aaseiehean trrgpwwgws dvkvgletlf rwgevvsagr
      181 agferrygla eqmlapeild ahverseair elvlrgvkah glgtlddiad yfrlpsaear
      241 talqeledag svrrvsvdgw errgkarevw idprakrprs iradallspf dpvvwardra
      301 lrlfdfhyri eiytpahkrv hgyyvlpvli ddkicarvdl kndrqnrrll vraawaepta
      361 dadtaprlae llrrtarwqg cdtvevenkg tlsqqlaaam t
//
LOCUS       WP_007737638             826 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Paraburkholderia hospita].
ACCESSION   WP_007737638
VERSION     WP_007737638.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia hospita
  ORGANISM  Paraburkholderia hospita
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 826)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 826)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 826)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..826
                     /organism="Paraburkholderia hospita"
                     /db_xref="taxon:169430"
     Protein         1..826
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89475
     Region          80..129
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          107..820
                     /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 mglsaracan taalesrrra fpgwhiigia tatifatias pavfaadate saqtsprksf
       61 diaagplesa lnqygqqari mlsypsalta nrhsaglhge ydtqqglmrl lrgtglssiq
      121 qtngsytlve dasnveldds avlptvkvas tgirpgsyrp ppeanvtrsd ipvidtpeai
      181 nivpaqvlrd qrprnlddal anvsgivqgn tlagtqdtll krgfggnrdg simhngmplv
      241 qgrglnaaad svevlkgpss llygimdpgg vvdvvskqpl ltpyhaisal gstyghgrng
      301 adgtldltgp igdsglayrl vvdqvneqyw rnfgehretl vapslawygr dtqvvlsyey
      361 rkflypfdrg taldpktnkp laiparerld epfnemdges nlaqltidhq idanwkahfg
      421 ysynretyda gqlrvqgvns ttgvlsrsnd athgalstds yaiayidghf tvaglrndlq
      481 vgvddeyrri yrkdllrqat kytfnylhpv yglespsatv sasdsdqtdt lhdasvffqd
      541 slhltdkwil vggarflsyn qvagrgrpfq vntdlngtkw lprtgvvykw tdtvslygsy
      601 tqslkptsti aplstgvvid ssvlpeeats wevgakvamp agvtgtlaff nidksnvlvs
      661 qyndttkqtd wrtsgkarsr gieldvagqi gqrwsviasy ayidaktted plyagnrlwn
      721 vaqhtaslaa vydfgaifgg dqlrvgagah yvgerpgdsa nsftlpaytv adafanyntk
      781 wgghnvsfql nvknlfnkty ypssanryfv avgdarqvsl lstlef
//
LOCUS       WP_007739433             162 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Paraburkholderia hospita].
ACCESSION   WP_007739433
VERSION     WP_007739433.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia hospita
  ORGANISM  Paraburkholderia hospita
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Paraburkholderia hospita"
                     /db_xref="taxon:169430"
     Protein         1..162
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=17169
     Region          36..115
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mtpldpntqs qsqsqsqsad qgagivgigv gdgpgpdvma astldgtkvv tadgehvgki
       61 sdimldvrdg riayavlseg gflgmgttlh aipwsaltln vdekvflvnl madeiknapg
      121 fdkdhwpsma dpqwgssvhq yyrqqpywda trdavdgrps nl
//
LOCUS       WP_007740563             155 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein
            [Paraburkholderia].
ACCESSION   WP_007740563
VERSION     WP_007740563.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..155
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=16523
     Region          31..104
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mtildpkmnp vhggagivgg gvgegpgpev maaatldgnk vvssdgehvg kisdimldvr
       61 sgrvayavls eggflgmgsn lhaipwgalt ldtdekvfrv ditaqrikde pgfdkdhwps
      121 madetwgtqm hqyynrdpyw tttsvdpvav rdrgl
//
LOCUS       WP_007743372             380 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Paraburkholderia hospita].
ACCESSION   WP_007743372
VERSION     WP_007743372.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia hospita
  ORGANISM  Paraburkholderia hospita
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  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 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   3  (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   4  (residues 1 to 380)
  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 380)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia hospita"
                     /db_xref="taxon:169430"
     Protein         1..380
                     /product="CmpA/NrtA family 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=41317
     Region          14..262
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mnspaytsss desgklekth lrlgfvalsd aaplvaakll efghahglti ellkqpswaa
       61 irdkllsgdl daahslyglv ygvqlgiggp qtdmavlmvl nrngqaitvs nrlaaaldeh
      121 ktlpaalstl grkpvfaqtf ptgthamwly ywlasqgvhp lrdiegvvip ppqmvdalaq
      181 drldglcvge pwnavaqerg vgrtiaytse vwpdhpekvl asrrdfvtry pntaralvqt
      241 mleacrwldd dvhrveisar laadefvgvp agliaprlia agsdekrrav kffadgavnf
      301 phpaegvwff aqyarwgmae wrddfariag evnqvdlycq aaanvgvsvy adtpsavlid
      361 grvwdgkadq vymqgfsira
//
LOCUS       WP_007744562             302 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Paraburkholderia].
ACCESSION   WP_007744562
VERSION     WP_007744562.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..302
                     /product="formate/nitrite transporter family protein"
                     /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=32480
     Region          53..300
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mtkdtiqher hpdttdratp pdhpekagae sphldagekd qaaqhtapha lmlheivree
       61 geaalertvi alvwsslaag lsmgfsfltt avlqaglpdt swrhlvssfg yttgfvlvim
      121 grqqlfsest ltvvlpvltr rdldcllkal rlwivvlfcn llsswafaam lrlpgvfead
      181 vvdaldetar savgpantfp tfiravlggw lialmvwllp sarsarlltv vlitwvvava
      241 klshiiagst evayavlagd asmadyfgrf llptlagnvv ggmtlvalln haaiapeise
      301 rr
//
LOCUS       WP_007747448             333 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Paraburkholderia].
ACCESSION   WP_007747448
VERSION     WP_007747448.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 333)
  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   6  (residues 1 to 333)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..333
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36795
     Region          21..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          84..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 metmlrsvam ggyfdvtrrl glnpfelvqq fgidaaalan pddrvpatac crlieltadm
       61 ascptfalqm aetrqkfgtg vvnillahkr tlrevllaaa eyrhllneal avyvenagdt
      121 vtireelvve pgtptkqaie lavavlarha sallgdhwkp rtvhfthagp adltfhrrff
      181 gcalqfgsdf ngfvcaaadl dypnpaadpe lvryaeslat pmnaasadsa alevrkaiyl
      241 llpleqatve lvsrqlglsv rtmqrqlesa etsfstlvee vrrelavrym snprypigrv
      301 sallgysqqg sftkwftsqf rmtprdwrns rlk
//
LOCUS       WP_007747727             341 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Paraburkholderia].
ACCESSION   WP_007747727
VERSION     WP_007747727.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 341)
  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   6  (residues 1 to 341)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37605
     Region          29..213
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          92..341
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mastrpline riyapykiaa lvevlaeqgi apedslkgsg lsvdqlndas vmtsvrqyai
       61 varnavllst dpatpfktga rlhlsaygmy gyalmsclsl rdyfrlgvky hrlatptvti
      121 dwteypdrav wsfpdafvss psrelrefii eqqftqhvth lqdvaghscp pvmacfsypa
      181 pahadlypqy lgcpcffdap qcelvydsai lnqkpqlahk ltatllqdtc drligqakts
      241 vgtsgevyqv lmstpgvfpg meevatrlnm tsrtlrrhle aegtsfvaiv ddvrcslale
      301 ylqstkmstd dvamllgfsd aanfrralkr wtgkgpgelr k
//
LOCUS       WP_007748278             337 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Paraburkholderia].
ACCESSION   WP_007748278
VERSION     WP_007748278.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 337)
  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 337)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..337
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37831
     Region          31..206
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          250..331
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqapsatvpi slvngflaaa daqpdvmqry leqagitpel rsaagarvte eqfsmlyrtl
       61 aielddempg ifsrpfrsgt lkflclslld apnletalhr fgqffhivld dfhiesrrdd
      121 lmaqvelrpn paygsigplg qelmlklahg vsswligqki pllqvdfacp qpphafdhry
      181 ffsgpvrfgc natlmrcsaa fldmpirqsk rnlrkflars pgewifetfs eqrvshrvrq
      241 ylagelpdlp tidqaakslh csvrtlcrrl sseettfqll kdelrrdiai qrltdtqdti
      301 aviagdigfd dpsafhrafr hwtgstpgty rrplqag
//
LOCUS       WP_007749147             372 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Paraburkholderia hospita].
ACCESSION   WP_007749147
VERSION     WP_007749147.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia hospita
  ORGANISM  Paraburkholderia hospita
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 372)
  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 372)
  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   3  (residues 1 to 372)
  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   4  (residues 1 to 372)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 372)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Paraburkholderia hospita"
                     /db_xref="taxon:169430"
     Protein         1..372
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39201
     Region          32..362
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(105..107,128,177,229,253)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mnglkhsmnv vagiglggla ltwsvaacan lvvgvagpmt geyasggeqf rkgaeqavkd
       61 inaaggllgq kvdlvvgddv cdpkqavsva nsfvnkkvaf vdghwcssst lpasdvynda
      121 qipqvtvstn pkitergiqg ifritgrddq qgqvagdyia enfkgkkiav vddktayggg
      181 ladeiakels akqtpvvlrq sitagekdys glvsklkang vevlayggyy qevalilrqa
      241 aqaglklali ggdtltnnel vnaagpeink viftfppdpr knaaaakvve alraqkiepe
      301 gymlysyaam qvfadaakra nstdyaavvk qlhnasfstv vgpvdfdakg dlkspgyvvy
      361 rwkgnnyeyv nk
//
LOCUS       WP_007749378             149 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SPOR domain-containing protein [Bacteroides].
ACCESSION   WP_007749378
VERSION     WP_007749378.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..149
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16601
     Region          63..136
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mrklvlfvll lllvgagaqa qgiirslert vpgqgkvtih qdpriealig merpatgeqk
       61 viktsgfriq ayagnntrqa kndadrvasr vkeyfpelsv ytsfisprwl crvgdfrsie
      121 eadammrrlk atgmfkevsi vrdqinipl
//
LOCUS       WP_007752802             345 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Rhizobium
            sp. CF080].
ACCESSION   WP_007752802
VERSION     WP_007752802.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF080
  ORGANISM  Rhizobium sp. CF080
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Rhizobium sp. CF080"
                     /db_xref="taxon:1144310"
     Protein         1..345
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38159
     Region          1..343
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mevtisnirk eferfpalnd vslkiasgel iallgpsgsg kttllrliag ldfptsgkif
       61 fgdqdashhs vqdrnvgfvf qhyalfrhmt vaenigfglk vrpagsrppk aeirrrvsdl
      121 lemvqlggld krypnqlsgg qrqrvalara maieprilll depfgaldak vrkelrrwlr
      181 efhdrtghtt vfvthdqeea leladrvvvm sqgkieqvgs addvydrpgs pfvfsfiges
      241 sqlpvevkdg tmlfqgqpig isepgdgage lffrpedvtl vdapdalfgk vtacrrlagt
      301 riaeidiand ghapyhveve vplhapielg searfrptrw kvfrn
//
LOCUS       WP_007753161             293 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Rhizobium sp. CF080].
ACCESSION   WP_007753161
VERSION     WP_007753161.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF080
  ORGANISM  Rhizobium sp. CF080
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Rhizobium sp. CF080"
                     /db_xref="taxon:1144310"
     Protein         1..293
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31620
     Region          21..262
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mskpeiitpe vrrvidfplk vgesptwddr tgdlwlvdil apaaiclrad grvdrfempf
       61 kigclalceg ddiavaleng vhllnpktga mkllcdpdgg rpdsrlndgk vgpdgcfwvg
      121 trdeaipqtg narlyrvmpd gsfttivdgg lltsnglaws pdgrtmyhsd ssglfaqafd
      181 fdlrkgvtsp prrlhdftpe egrpdgaamd akgfywiagi lsggvnrlsp egevveiykm
      241 paksptmpcf gspdlatiyv ttlstdnngt fehgtlfafe agvrgtpihr fgi
//
LOCUS       WP_007754864             312 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Rhizobium sp. CF080].
ACCESSION   WP_007754864
VERSION     WP_007754864.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF080
  ORGANISM  Rhizobium sp. CF080
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
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
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Rhizobium sp. CF080"
                     /db_xref="taxon:1144310"
     Protein         1..312
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=33791
     Region          1..309
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mieidaitkr ydgvtvvdnv smvieprtvt vvvgtsgsgk ttlirminrl veasegairl
       61 dgednrsipg yelrrrigya iqghglfphr tvaqniatvp gllgwtkari dakveelltl
      121 fqlepktfgp ryphelsggq qqrvgvaral aaepyvllmd epfgaldpii rakaqedlla
      181 iqkhfgttiv lvthdmneaf hladkiavmd kgrvvqygpp aelvrapatp fvetligdae
      241 rpfrllsiat tgaaaepgea egvpigedrs qqealadliw sgrdalpvis rsgapmgrvt
      301 leailkraar qr
//
LOCUS       WP_007755541             784 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Rhizobium sp. CF080].
ACCESSION   WP_007755541
VERSION     WP_007755541.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF080
  ORGANISM  Rhizobium sp. CF080
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 784)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 784)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 784)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..784
                     /organism="Rhizobium sp. CF080"
                     /db_xref="taxon:1144310"
     Protein         1..784
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=86195
     Region          5..784
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 msdvqahetl rlsgleaqae iridrwgiph ikatsekdlf fvqgfnaard rlwqldlwrk
       61 rglgllaadf gpgylaqdha arhflyrgdm apewtsyapd tqaictafva ginayvtlce
      121 leparlspef dlfgtrpsrw epsdvvrirs haltrngise ilranimala daetdllrfe
      181 ldppvspkpe tgilladipl vatrlfklat aavtfdkarl tatladvwkw vdvtdlgdiv
      241 qaiaeegsnn wavhgsrtet grpilasdph rahavpslry lvhldapgfn aigtgeptap
      301 gislghndri afgltifgad qedvyvyetk dgdpdhyryg dgwetitrie esfpvkgypd
      361 qvltlsftrh gpilhenpki rqaiamrsvw lspgsaaylg slsymrsgsv rafsqtlgsw
      421 gtpsvnqvsa dvegnigwft agftpvrrnw egllpvpghg shewdgflpa eqlpracnpa
      481 dgfvasanem nlpadrdpnd psighewaev sraqriksvl radpkhtlka smalqtdvys
      541 rpaaamcavl qkvaghqsld nrqeraaklf ngwdyrleaa sapaalfevw wmkhlrpall
      601 akfapnptvr qlllpgdvdr mlvllsepgm lwdaaerdam llstlsagfa dcesrlgadp
      661 aawrwgdlhr alfehatsri ksegatdwni gplplggsrs tplhagyrmg dfgvnagasv
      721 rlvmdvgdwd nsvcintpgq sgdprsphyr dladtwskge yvpllysdar iiqetvhrit
      781 llpa
//
LOCUS       WP_007757225             283 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Rhizobium sp. CF080].
ACCESSION   WP_007757225
VERSION     WP_007757225.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF080
  ORGANISM  Rhizobium sp. CF080
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Rhizobium sp. CF080"
                     /db_xref="taxon:1144310"
     Protein         1..283
                     /product="formate/nitrite transporter family protein"
                     /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=29846
     Region          2..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msyvtpaefv tkmidageak ifmstrdtli rafmagaila lsaafavtit vqtgnalaga
       61 ilfpvgfcll ylmgfdlltg vftlaplali dkrpgatagg vlrnwtlvfi gnfagaflva
      121 vmmaiiftfg fseapnevgq righigegrt lgyaahgaag mltlfirgvl cnwmvstgvv
      181 aammstsvsg kvigmwmpim lffymgfehs ivnmflfpsg lllggkfsim dyliwneipt
      241 vignlvgglt fvgltlysth grksgkqsap agrignpavv pae
//
LOCUS       WP_007757482             397 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Rhizobium sp.
            CF080].
ACCESSION   WP_007757482
VERSION     WP_007757482.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF080
  ORGANISM  Rhizobium sp. CF080
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 397)
  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 397)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Rhizobium sp. CF080"
                     /db_xref="taxon:1144310"
     Protein         1..397
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46273
     Region          1..390
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mailipndqa rkiflerqrl ceppgraltk sgllqliddl gfvqvdsiat verahhmilf
       61 srnqtyrreh ltallekdge lfehwthdas iipasffryw khrfrrrepv laerwrkwhg
      121 egfdaafeet fqhiaengsi msrdmkaedh ksggwwnwhp nktaleyywh tgklaiagrv
      181 nfqkiydlme rvipphhhep evsheafidw acrgamtrlg fatsgelaaf fdlvtpdeak
      241 dwvksrrdel tevlietadg srprpsfafl gfpenlgeip epparvrvls pfdpllrnrd
      301 raerlfnffy rievfvpepk rqygyyvfpl legdrmigri dmkadrksgv ldvkrlwlek
      361 gvrasagrle kleaellrvg rfagvdkvty qmgwrge
//
LOCUS       WP_007757980             621 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Rhizobium sp. CF080].
ACCESSION   WP_007757980
VERSION     WP_007757980.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF080
  ORGANISM  Rhizobium sp. CF080
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 621)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Rhizobium sp. CF080"
                     /db_xref="taxon:1144310"
     Protein         1..621
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=70353
     Region          64..593
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 meklkmhspd lsqenidkir nlfpgcvtea rdeatgqlrl avdfdqlrqe lsdsivegaq
       61 eryrldwpgk qeavlaanlp iaktlrpvrd qsidfdasnn lliegdnlea lkvlqesflg
      121 rvkliyidpp yntgrdfiyd ddysqgtady lnlsgqaden girlvantea ngrfhsdwls
      181 mlyprlrlak nlladdgvvf vsiddnevds lrkmgseifg dsnfvativw qkvyapknsa
      241 kwfsedhdfi lvfaknkevw fpnplprtde mearyknldn dsrgpwkaen mtarnpydag
      301 vyslttpsgr visgpptgty wriskekfle ldadnriwwg kdgtnspavk kflsevssgr
      361 tpqtlwfynd vghtqdakkt llkyvpfeht envlnsvkpv ellqrivqla tkpeegaivl
      421 dffsgsapta havmlqnrmd ggnrrfigvq iaeplpipet kmetifdmgr lrltnvieef
      481 kaegdevtgf rvlkldtsnm kdvyyrpdel kqsdlldmvd nvkedrtaed llfqvlvdwg
      541 vdltlpihre avqgktvffv denalvacfd kgvsedlvke lakreplrvv frdsgfisda
      601 vkinveqifr qlspttevks i
//
LOCUS       WP_007757992             130 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Rhizobium sp. CF080].
ACCESSION   WP_007757992
VERSION     WP_007757992.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF080
  ORGANISM  Rhizobium sp. CF080
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Rhizobium sp. CF080"
                     /db_xref="taxon:1144310"
     Protein         1..130
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=14727
     Region          21..97
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mlhhepragq dpyvkdtpsl iasdkvegtk vygadgkhig siarvllekr ggrvgyavls
       61 fggflgigdd yyplpweklr ydeqldgyri dltkdqitga pryrdldddt wyndkgrtiy
      121 dyygvapywm
//
LOCUS       WP_007758015             112 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Bacteroides].
ACCESSION   WP_007758015
VERSION     WP_007758015.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..112
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12292
     Region          12..109
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(15..16,34..35,43,46,48..49,51,54..55,57,65,70,77)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(34,65..66,68,89)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mkdykvdkak fsasfcqevh qvvcdipvgk vstygeiatl lgmpqcsrmv gralkqvpeg
       61 isvpchrvvn asgrlvpgwt eqkqlllkeg isfkqngcvd lkkhlwnysa se
//
LOCUS       WP_007758103             317 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Rhizobium sp. CF080].
ACCESSION   WP_007758103
VERSION     WP_007758103.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF080
  ORGANISM  Rhizobium sp. CF080
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 317)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Rhizobium sp. CF080"
                     /db_xref="taxon:1144310"
     Protein         1..317
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=34805
     Region          27..252
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mtprsifanl vrsdngsfst vygpfllqsa lqpifrsgpe tgldieafeg llrasrdnep
       61 vspaeffplv spvdmadvds ilrtihilnt grlnraragi fvkfhpglfr tpqemrqevd
      121 rikvasheag lapdrivcei sersgaaddi vvaftehmqa igfriaiddy gardsdldrl
      181 krirpdyvkf eaawvrdfld nsagyallrv ivrqmlddgi epifegleel wqvdlceelg
      241 vplmqgyala rpelapttfn esfpesladl applqaggnd itlglsraam aapppvpakp
      301 vfarparafg rrqssge
//
LOCUS       WP_007758952             170 aa            linear   BCT 20-JAN-2025
DEFINITION  transcription termination/antitermination protein NusG [Rhizobium
            sp. CF080].
ACCESSION   WP_007758952
VERSION     WP_007758952.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF080
  ORGANISM  Rhizobium sp. CF080
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Kang,J.Y., Mooney,R.A., Nedialkov,Y., Saba,J., Mishanina,T.V.,
            Artsimovitch,I., Landick,R. and Darst,S.A.
  TITLE     Structural Basis for Transcript Elongation Control by NusG Family
            Universal Regulators
  JOURNAL   Cell 173 (7), 1650-1662 (2018)
   PUBMED   29887376
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Liu,B. and Steitz,T.A.
  TITLE     Structural insights into NusG regulating transcription elongation
  JOURNAL   Nucleic Acids Res 45 (2), 968-974 (2017)
   PUBMED   27899640
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Steiner,T., Kaiser,J.T., Marinkovic,S., Huber,R. and Wahl,M.C.
  TITLE     Crystal structures of transcription factor NusG in light of its
            nucleic acid- and protein-binding activities
  JOURNAL   EMBO J 21 (17), 4641-4653 (2002)
   PUBMED   12198166
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415705
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Rhizobium sp. CF080"
                     /db_xref="taxon:1144310"
     gene            1..170
                     /gene="nusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
     Protein         1..170
                     /product="transcription termination/antitermination
                     protein NusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
                     /calculated_mol_wt=18572
     Region          2..149
                     /region_name="NusG"
                     /note="Transcription termination/antitermination protein
                     NusG [Transcription]; COG0250"
                     /db_xref="CDD:440020"
ORIGIN      
        1 mwyvlrtapg rqslaldele aigidaiapv irrevmhyqt kswsmrrfpl fsgyvfgslh
       61 geadfdalrk mdhvqavlgg sdgpipiptk avielceaqn rgdydilrpp paasfapdvr
      121 vriesgplag ayarvtrakg kgkravmaiv esvenmreie lsianlrlaa
//
LOCUS       WP_007760107             368 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Rhizobium sp. CF080].
ACCESSION   WP_007760107
VERSION     WP_007760107.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF080
  ORGANISM  Rhizobium sp. CF080
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 368)
  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 368)
  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   3  (residues 1 to 368)
  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   4  (residues 1 to 368)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 368)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Rhizobium sp. CF080"
                     /db_xref="taxon:1144310"
     Protein         1..368
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37493
     Region          26..359
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(99..101,122..123,172,224,248)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mnlktllgat alaslvfapl ahadivigli apltgpvaay gdqvkngaet aiaeinkkgg
       61 ilgekvvlkt addaaepkqg vsaanqlvge girfvvgpvt sgvampasda laengvlmvt
      121 ptattpaltt rgltnvfrtc grddqqavva anyvlkafkd kkvaiindkg aygkgladaf
      181 kaalnaggvk evfddavtpg dkdfsalttr lksqnvdviy fggyhpeggl larqladlgv
      241 kativggdgl snsefwnigt kaaagtvftn asdatkspds kaaaealaar kipaeaftln
      301 ayaavevika giekaksaed teavaaaiks gepiataigk ltygetgdlt sqsfslfkwq
      361 dgkivpae
//
LOCUS       WP_007760211             329 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Rhizobium sp. CF080].
ACCESSION   WP_007760211
VERSION     WP_007760211.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF080
  ORGANISM  Rhizobium sp. CF080
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 329)
  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 329)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 329)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 329)
  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   5  (residues 1 to 329)
  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   6  (residues 1 to 329)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Rhizobium sp. CF080"
                     /db_xref="taxon:1144310"
     Protein         1..329
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37019
     Region          23..200
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <176..329
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mqtltyaldt twrtlladlv vvpanvlrra glpddllhqp svrlepedyy rlwesaeqek
       61 gdplfpirvc eavraesfsp plfaalcspn llvaaqrvak ykkligpmqm evrddrdmlt
      121 iefawldgpr rppvslvame llfcvtlvri gtreaispid vtttdlpspl apyenflgar
      181 lrrgprhmvr faksdavrpf ltsneplwaa fepdlrqrla dldasvtvak rvraalheai
      241 psglttmeai aqklavskrt lqrrieaegt sfqqilketr ealarhylek talpaseisf
      301 llgfdepnsf yrafrswtgk tpdsirqha
//
LOCUS       WP_007762185             686 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Bacteroides finegoldii].
ACCESSION   WP_007762185
VERSION     WP_007762185.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides finegoldii
  ORGANISM  Bacteroides finegoldii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Bacteroides finegoldii"
                     /db_xref="taxon:338188"
     Protein         1..686
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73695
     Region          4..686
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mittqllrpe sivvvgasnn vhkpggailk nlinggyqge lravnpkeke vqgvpafadv
       61 qdvpdtdlav lavpasmcpg ivetlagrkh trafiilsag fgeethegal leeriletvn
      121 kygasligpn ciglmntwhh svfsqpipnl npkgvdliss sgatavfile savtkglqfn
      181 svwsvgnakq igvedvlqfm denfdsekds rikllyiesi qnpdrllfha sslirkgcki
      241 aaikagsses gsraasshtg aiassdsave alfrkagivr cfsreelttv gcvftlpelk
      301 gknfaiitha ggpgvmltda lskgglnvpk legnlaeelk aqlfpgaavg npidilatgt
      361 pehlrlcidy ceekfenida vmaifgtpgl vtmfemydvl hekmqvcskp ifpilpsint
      421 agaevaafla kghvnfsdev tlgtalsriv napkpavpei elfgvdvpri rriidsipdd
      481 gyiaphhvqa llhaagiplv defvsdnkee vvafarrcgf pvvakvvgpv hksdvggvvl
      541 nikseqhlsl efdrmmqiad akaimvqpml kgtelfigak yeekfghvvl cglggifvev
      601 lkdvssglap lsyeeaysmi hslraykiiq gtrgqkgvne dkfaetivrl stllrfatei
      661 kemdinplla tekavvavda ririek
//
LOCUS       WP_007764196             414 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Rhizobium sp. CF080].
ACCESSION   WP_007764196
VERSION     WP_007764196.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF080
  ORGANISM  Rhizobium sp. CF080
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 414)
  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 414)
  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
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 414)
  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   5  (residues 1 to 414)
  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   6  (residues 1 to 414)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 414)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 414)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Rhizobium sp. CF080"
                     /db_xref="taxon:1144310"
     Protein         1..414
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44507
     Region          30..73
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          93..392
                     /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 msvsdsmaqg hallgnftgg snqvrvrayn erlvlslvrl ngsmskadit rrsglsaqtv
       61 svimralekd glllrgepvr grvgqpsvpm rlnpdavysf gvkigrrsad lvlmdfvgdi
      121 rlqyhetyay plpaniieii tsgitrlegq lnevqrgria gigiaapfel wnwaeevgap
      181 qgameiwrgi dlqaeiasrv phavylqnda tsacgaelvf gvgpsypdfv yffigsfigg
      241 givlnsaifs grtgtagavg plpvrgkdge trqlldiasi fvlenllker nidpqplwys
      301 andwidfgep ldlwirqtan alaqaivaaa siidfgaavi dggfpawvrr rivastieav
      361 arldlqgvii pdiiegmvgs qaraiggasl pifakyltdq svlfkdlrem pags
//
LOCUS       WP_007767582              97 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Bacteroides finegoldii].
ACCESSION   WP_007767582
VERSION     WP_007767582.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides finegoldii
  ORGANISM  Bacteroides finegoldii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Bacteroides finegoldii"
                     /db_xref="taxon:338188"
     Protein         1..97
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11333
     Region          3..97
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mktkdeiiai lrnfkeefge rygieklglf gsvvrgeqke dsdidicikl qepdyftrme
       61 ikeflekrfn akvdvvslta imrslfrnhi ekdaiyi
//
LOCUS       WP_007767934             815 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Mycobacterium
            colombiense].
ACCESSION   WP_007767934
VERSION     WP_007767934.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium colombiense
  ORGANISM  Mycobacterium colombiense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 815)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 815)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 815)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..815
                     /organism="Mycobacterium colombiense"
                     /db_xref="taxon:339268"
     Protein         1..815
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89177
     Region          38..771
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 maidriadpw gtrtpyepgt rwpervdtyl adgispesvd rwvqsaavlh sngdgldiav
       61 kdgrivgvrg ravdrvnhgr ldpkdlfgwq anasadrltt pmirvhgklk pcdwdtamqr
      121 ivdrtkglld sygpssigfy tsgqlfaeay ytqgaiahga igtnhvdgnt rlctataaea
      181 lkesfgcdgq pgsytdvdha dvialfghnv aetqtvlwar mldrlagesp paivcvdprl
      241 tpvarhatvh laplpgtnva lmngllheii ghgwidrdyi dsntvgfdel rgrveefgpe
      301 rvadicgvaa ddirraarll gtakrlmstv lqgfyqshqa taaavqvnni hlvrgmlgkp
      361 gcgvlqmngq ptaentrecg adgdlagfrn wsndshvael arlwnldllq iphygpptha
      421 mqifryaeeg tlrmlwvtat npavslpelr rirdilsqer lflivqdifm tetaaladvv
      481 lpaaawaekt gtftnadrtv hlsekavepp glarsdldif ldyarrmdfr dsdgqpfppw
      541 tdaesafeaw kkctagrpcd ytgltydklr ggsgiqwpcn aehpdgterl yadakfwaap
      601 dyceaygkdm itgaplqpde yrsmnpfgka iikaaeyvpp herpspdfpf alitgrtvyh
      661 fhtrtktara qqlqqaapev wvevserdaq rlgigegdlv evrtprgcvv caaricgird
      721 gvlfvpfhyg ywdtdgkthh ragnemtltd wdpvskqpiy ktaaarlrkl kvrppdrngh
      781 apttaastpv ngsvpatvgg epagvtevva tggrp
//
LOCUS       WP_007767945             171 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Mycobacterium colombiense].
ACCESSION   WP_007767945
VERSION     WP_007767945.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium colombiense
  ORGANISM  Mycobacterium colombiense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Mycobacterium colombiense"
                     /db_xref="taxon:339268"
     Protein         1..171
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18678
     Region          5..166
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 meawdalrar rnvreyqskp vppedldria eagwrapsak nrqpwdfviv tdreqlaels
       61 tvwrgaghia gaaaaiaivv pvppderrvi tdnydvgqat mammiaatdl glgtghssvg
      121 dqdkarailg vpdeylvafl lgvgypadrp lapirkpnrr pfaevvhhgr w
//
LOCUS       WP_007768409             158 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Mycobacterium
            colombiense].
ACCESSION   WP_007768409
VERSION     WP_007768409.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium colombiense
  ORGANISM  Mycobacterium colombiense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 158)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Mycobacterium colombiense"
                     /db_xref="taxon:339268"
     Protein         1..158
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=15875
     Region          73..156
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mkervpdstg lplramvmvl lflgviflll gwqalgssgs sdddsasags sasatssasp
       61 sptakpastq aevqiyniss kegvaarakd qltsagfkvt kvdnmtvpdv sattvyytda
      121 gdehatanav gknlgapvep ripalsgepp gvivlvag
//
LOCUS       WP_007771188             219 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Rhizobium sp. CF080].
ACCESSION   WP_007771188
VERSION     WP_007771188.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF080
  ORGANISM  Rhizobium sp. CF080
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Rhizobium sp. CF080"
                     /db_xref="taxon:1144310"
     Protein         1..219
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21972
     Region          <1..195
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 matleggayd dalfgsrfnd firahggddf vsggnghdlv fggdgddllf ggkghdslfg
       61 gdgsdllnge dgndnlvggw gddllygdkg sdtllggqgs dllsggkgad ilyggdgadi
      121 idggagndll vggaghdvfv fdggggndvi ldfnagedll qiskgingld vsspedlasr
      181 vtqvggnvvv dlghgdtltl vnvdaddiha npenyftvh
//
LOCUS       WP_007773509             339 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Mycobacterium
            colombiense].
ACCESSION   WP_007773509
VERSION     WP_007773509.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium colombiense
  ORGANISM  Mycobacterium colombiense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 339)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Mycobacterium colombiense"
                     /db_xref="taxon:339268"
     Protein         1..339
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36206
     Region          4..335
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mdnprvslid vatylpgepi padyyaqfae sddlrdnvmf rapkfrhhva adessidmie
       61 raaqglierh ghdvvegadv lithtqvpdm afygqgggia hrlgmrpswv ldlnnggcaa
      121 fvlalnvark llaagegrta iiaiaqnaag qffdqptirr kaqsavpgdg aavglvavgd
      181 qssildvecr tygeyagemt lsydpprkww qagagegsig fteskitkvl argnrqvpev
      241 alavcdrigl aakdidllvt nqpnraflrn wrdalelpks rhldtfdecg nlfgagipin
      301 ldraisdgrl gagqvvmmaa fahagdfaga aavrwggrg
//
LOCUS       WP_007775441             237 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Mycobacterium colombiense].
ACCESSION   WP_007775441
VERSION     WP_007775441.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium colombiense
  ORGANISM  Mycobacterium colombiense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Mycobacterium colombiense"
                     /db_xref="taxon:339268"
     Protein         1..237
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=25369
     Region          89..230
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mnrkvllwla aaaalallva yqtvgsstar hsaeyaarad vptvqpgtdv lagvavvplr
       61 qhrydylrsa fgdawdddnd apmghngcdt rddilnrdlv dktyvsvkrc pdavatgtlh
      121 dpytnktiaf qrgpkvgesv qidhivplay awdmgasgwp aaerlrfand panllavdgq
      181 anqdkgdspp aqwmppnaaf acqyamqfia vlrgyslpvd qastgvlrqa attcptg
//
LOCUS       WP_007775867             164 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Cronobacter malonaticus].
ACCESSION   WP_007775867
VERSION     WP_007775867.1
KEYWORDS    RefSeq.
SOURCE      Cronobacter malonaticus
  ORGANISM  Cronobacter malonaticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Cronobacter.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Cronobacter malonaticus"
                     /db_xref="taxon:413503"
     Protein         1..164
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17731
     Region          1..153
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mnktqfyael nrdfhslmag etsflatlan tsallferld gvnwagfyll edktlvlgpf
       61 qgkiacvrip ygrgvcgtav atgevqrvdd vhafdghiac dassnaeivl plradgqiig
      121 vldidstvfn rfdaddeqgl rtlveqleav iaatdfkkff apva
//
LOCUS       WP_007777638             142 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Cronobacter].
ACCESSION   WP_007777638
VERSION     WP_007777638.1
KEYWORDS    RefSeq.
SOURCE      Cronobacter
  ORGANISM  Cronobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Cronobacter"
                     /db_xref="taxon:413496"
     Protein         1..142
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15356
     Region          18..140
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 msdalsllsl ftssflsatl lpgsseavlv allvsvktap wllvltatig nslggltnvi
       61 lgrlfplres srwqeraqgw lqrfgapall lswlplvgdl lcllagwlrl pwgpvifflc
      121 lgkalryiii aaatlqgmtw wh
//
LOCUS       WP_007778729             386 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Desulfosporosinus youngiae].
ACCESSION   WP_007778729
VERSION     WP_007778729.1
KEYWORDS    RefSeq.
SOURCE      Desulfosporosinus youngiae
  ORGANISM  Desulfosporosinus youngiae
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfitobacteriaceae; Desulfosporosinus.
REFERENCE   1  (residues 1 to 386)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Desulfosporosinus youngiae"
                     /db_xref="taxon:339862"
     Protein         1..386
                     /product="amidohydrolase family protein"
                     /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=39930
     Region          1..372
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 msvialtnig klvtgniqkp lgeettivlq dgliakmgns dilqdytvek vidvngmtvt
       61 pglidshvht tlgdysprqk tqdyldgsvh ggvttfisag echtpgrpkd pagtkalail
      121 ahkayanlrs tglkvhggav ilekgltegd faemakegvw lvgeiglgsv kkpedaipmv
      181 kwakengmki amhtggtsip gsstvsaadv aavqptvvsh inggptaiap seveklinet
      241 dlaleivqcg npkiadftvr kltekdqlnr viigndspsg tgiiplgilr tvcsissmsd
      301 vapekaiama sgntastfgl ntgiiaegke adlvvmdapm gsvgedalea laagdlpavv
      361 mvlvdgtirv nksrntppss rsckik
//
LOCUS       WP_007781655             169 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Cronobacter malonaticus].
ACCESSION   WP_007781655
VERSION     WP_007781655.1
KEYWORDS    RefSeq.
SOURCE      Cronobacter malonaticus
  ORGANISM  Cronobacter malonaticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Cronobacter.
REFERENCE   1  (residues 1 to 169)
  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 169)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 169)
  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   4  (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   5  (residues 1 to 169)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Cronobacter malonaticus"
                     /db_xref="taxon:413503"
     Protein         1..169
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18534
     Region          <9..167
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          92..168
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 myiaaaacda lpddpciltl sgllreavtr aatwkenhlt asqqrlagvi ldeiaslpqv
       61 nlglpmpqda rliriarals arpddarrle ewaawaglss rtltrrfsae tgfsftqwrq
      121 rvrllkalel laagkpvtav aldlgydnvs tfialfrrvf gttpgryqi
//
LOCUS       WP_007781173             385 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Desulfosporosinus youngiae].
ACCESSION   WP_007781173
VERSION     WP_007781173.1
KEYWORDS    RefSeq.
SOURCE      Desulfosporosinus youngiae
  ORGANISM  Desulfosporosinus youngiae
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfitobacteriaceae; Desulfosporosinus.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Desulfosporosinus youngiae"
                     /db_xref="taxon:339862"
     Protein         1..385
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=40458
     Region          <1..384
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 meilgyrrpd gnvgirnhil ivptsvcsst vamnlanqip eavalpnqhg ccqigadhlq
       61 tvrtligfgk npnvaavlvv glgcegipir etaaeiaasg kpveviviqe aggtlkaeae
      121 glrklselvr qvahlhpekv pvselslgie cggsdftsgl asnpaagiaa dllvaaggnv
      181 mlsettefig aehvlarrak sqevaeklfk ivhdceerak fsnvnlregq ptpgniaggi
      241 stieekslgc iykaghapiq dvlsygeipq gkglyimdtp gqdiesitgm laggatvvif
      301 ttgrgtptgs piapvikita nnrtykmmed nidldaspii tgeetieqag qrifeeiiav
      361 angrrtkaes lgykefgiyr igsty
//
LOCUS       WP_007782528             419 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Cronobacter
            malonaticus].
ACCESSION   WP_007782528
VERSION     WP_007782528.1
KEYWORDS    RefSeq.
SOURCE      Cronobacter malonaticus
  ORGANISM  Cronobacter malonaticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Cronobacter.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 419)
  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 419)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Cronobacter malonaticus"
                     /db_xref="taxon:413503"
     Protein         1..419
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47582
     Region          1..405
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 msgvhlslra arhlhlaaqg llkkptrrar padilatitr msllqidtin ivarspylvl
       61 fsrlgsypgr wldealarge lmeywaheac flprsdfplf rhrmlkpenm gwkyraawme
      121 ehaqeigelm afierngpvr sadfehprkg asgwwewkph kkhleglfta gqvmvverrn
      181 fqrvydlttr vlpewddslh lidqaqaeaq mlansarslg ifrsawlady yrlrnvaigp
      241 llqawqeegv vvpvevetlg pmwlhhallp lleravagkl tathsavlsp fdpvvwdrrr
      301 aedffnfsyr lecytpapkr kygyfvlpll hkgalvgrmd akmhrlqgsl evialyaeeg
      361 vsftagviag lrqaiadfaa wqgatrvifr qlpaplaqaw gegweidpap ethvisskd
//
LOCUS       WP_007784306             275 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Desulfosporosinus youngiae].
ACCESSION   WP_007784306
VERSION     WP_007784306.1
KEYWORDS    RefSeq.
SOURCE      Desulfosporosinus youngiae
  ORGANISM  Desulfosporosinus youngiae
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfitobacteriaceae; Desulfosporosinus.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Desulfosporosinus youngiae"
                     /db_xref="taxon:339862"
     Protein         1..275
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30449
     Region          1..254
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mrsdlhihth esdgllsvke viklayannv qtiaitdhes tqgvseaesl akelnikvip
       61 gvelltsyqg hevhllgyfn hvnhpvlqnr lqeiraqrte lahdmvecln sggislgwed
      121 vekevganga vtkghimrai yhqssdnsrk nwpeiaahfr pggvahlpyl nhtfedavdl
      181 ifscgglpvv ahpgllrdpe mvfpllayrp iglevyygyw erqaeliryy tevanksall
      241 atggsdyhgp sgyiklgqmg vpdkcvfelr sylgi
//
LOCUS       WP_007785279             220 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Brevibacillus].
ACCESSION   WP_007785279
VERSION     WP_007785279.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus
  ORGANISM  Brevibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Brevibacillus"
                     /db_xref="taxon:55080"
     Protein         1..220
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=24270
     Region          2..>207
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mlevdiqkrl pdfvldvsfs teqeivvlfg psgsgkttil nsiaglvhpd gghislngrt
       61 fysagqkpla vqkrnvgylf qdyalfphmt vsqniryglr kghelhlepl lttvgidhll
      121 dkyphqlsgg qkqrvalvra latepdilll deplsaldta trkqcqdell rlhemwgipf
      181 llvthdrdea eklgdtillm engriveasa qkshtatsss
//
LOCUS       WP_007785750             575 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Desulfosporosinus
            youngiae].
ACCESSION   WP_007785750
VERSION     WP_007785750.1
KEYWORDS    RefSeq.
SOURCE      Desulfosporosinus youngiae
  ORGANISM  Desulfosporosinus youngiae
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfitobacteriaceae; Desulfosporosinus.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 575)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Desulfosporosinus youngiae"
                     /db_xref="taxon:339862"
     Protein         1..575
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=63218
     Region          3..564
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mlisrrlfai trgmrgsvvl kvligvlvtg tyiiqgvlta tvlskvfage awdkfvtnfv
       61 vilgmilirs alnwfnevqs kilagqakek lryimfekll slgpgflqnn rsgsiqsvfv
      121 dgveaigpyi ayyiphcfvt lisslgilay vfylntmvga imllgmiivm vvpslwlkvm
      181 rstgmtswek rnhfnaqfld alqgmmtlka fnasaakgke letnsrdwyk simhnlavsl
      241 ldscliglga aigsafsvgv aaylfavgql nitsiflilf lsvecfrpmt dlvkywhvgf
      301 rgltaadklf afldtqpqva epidapplek gdfhseivfd nvtfgynegv rqalqkvift
      361 igqgekvavv gksgagkstl vnlllrffdp qdgsvrisgr dlktvpsvsf hslisvvwqd
      421 tylfhgtiee nlriakpgas neeiekaakl anihefivsl pegyhtqvge rgvrfsgger
      481 qriavarafl kdapililde atssldaene aaiqkglqhl mqnrtvliia hrfstiread
      541 riivlddhki vqtgthdelm afgggayaql lraql
//
LOCUS       WP_007786812             545 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA, partial [Brevibacillus sp. CF112].
ACCESSION   WP_007786812
VERSION     WP_007786812.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus sp. CF112
  ORGANISM  Brevibacillus sp. CF112
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 545)
  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   3  (residues 1 to 545)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Brevibacillus sp. CF112"
                     /db_xref="taxon:1144311"
     Protein         <1..545
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          46..124
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
     Region          <115..545
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 aapavaeeea veaaqaegtp aedhdlddya lmvlkqskel gnnvmwikvt lnencllkaa
       61 raymvfdqle smgeviktkp svedienecf eqsfeiayvt mqsaekvrst ilniseiqdv
      121 aidpiqlkke appapvvtea aapvekkapd naqaaaakka taggktirvd idrldilmnl
      181 fselvidrgr leqlareigk selqetvehm srisgdlqni iltmrmvpve qvfnrfprmi
      241 rdlqkelhkk vnleiigaet eldrtvidei gdplnhllrn sldhgiespa drkmagkpee
      301 gtivlrafhs gnhvfievkd dgaginkekv lkkaiergiv npanadsmsd kqihellfaa
      361 gfstaevvsd isgrgvgldv vkskieslgg svgvesvrgq gttfliqlpl tlsiisamlv
      421 qvkdekyavp lssiietavf kkdqimmahr qkvidfrgrv vplvslqdif qvpdngadkd
      481 devavvivrk gekmaglvvd sfigqqeivl kslgkylvnv faisgatilg dgqvaliidc
      541 nalik
//
LOCUS       WP_007787771             440 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Rhizobium sp.
            CF122].
ACCESSION   WP_007787771
VERSION     WP_007787771.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF122
  ORGANISM  Rhizobium sp. CF122
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 440)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 440)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Rhizobium sp. CF122"
                     /db_xref="taxon:1144312"
     Protein         1..440
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48633
     Region          57..423
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mrltlqthfn cewhpaatle ikddaagfqg asivdydlny fvtvasaefa agktvhdnra
       61 lsvgypvdle nrysrswppf lldlmpqgha rrklaehlgl aegqrtsdlp lllrsatggi
      121 gnirikeaad aeierlhgvq rkgvteaeil ersdrfmeva drfgmlasgs salqgewpkv
      181 smtqagdgqy ypdsfvtdde alrhvivklv rstepvdrli legealysri ahdiglnvse
      241 psiyaegvli iprfdrkkge rgeairlgqe slvsaigvad fghvgtheay idilrqfsad
      301 pfadiveylk rdianlalgn pdnhgrnsal skhqdgtirl splfdfapmr lakegivrst
      361 rwsmmrdagr dhfpdwkqic gelfpepdmq kslagklsaf aerlrqapqi aedmsaprei
      421 iergmgrcae iaegvlaslt
//
LOCUS       WP_007788900             987 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Rhizobium sp. CF122].
ACCESSION   WP_007788900
VERSION     WP_007788900.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF122
  ORGANISM  Rhizobium sp. CF122
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 987)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 987)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..987
                     /organism="Rhizobium sp. CF122"
                     /db_xref="taxon:1144312"
     Protein         1..987
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=103509
     Region          <78..257
                     /region_name="rne"
                     /note="ribonuclease E; Reviewed; PRK10811"
                     /db_xref="CDD:236766"
     Region          <196..355
                     /region_name="rne"
                     /note="ribonuclease E; Reviewed; PRK10811"
                     /db_xref="CDD:236766"
     Region          <306..530
                     /region_name="rne"
                     /note="ribonuclease E; Reviewed; PRK10811"
                     /db_xref="CDD:236766"
     Region          906..982
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 madkqraydt rkntdlfadd dplaelariv gfeprvaant vedaprqepa fnledellre
       61 ferydepqsa asfdrlrepv leqpaayeap ieadtlpaae aepefvpefv vepevasetv
      121 arqplevasn ltpvawasna vregepvagg ardlieelem sigatpapva ptkapqwsaa
      181 sirlpianfh parrdeassa pivpiaapep avvasesvaa fdvpvaagfp aeidrheepe
      241 tvpdasemrq eapvvealid hsafdlaaaa kddgavqada alteaaptev ddiafdidel
      301 ladvshypvp erqimaaadv aemprspepv rvaapvvapl pkpveppvsa ptakaepegd
      361 dpfaghdfel dlegielela dfdfaepvkv qpqavesqrv qaqhveavrp qpvapvpafq
      421 pppapapvvv sapisripee vppvakapat pafsadagde lpfdpsmisd aeyhpeavee
      481 mhvpvlppve qpepvvatsd fdfdvdaeia nllapakpae tpakpaveew rtrapisiap
      541 taapvakqvp lqsldefera leedfrrsvn epvqrrenvs qvqiqsasea edmsrarsmk
      601 rmlaaaaaiv vfggvayagy tflardgglg iasgeprvit adkdpvkvvp enpggktvpn
      661 qdkavydsvg gaaaeapkqk alvssdeqpv dvvqrtltpe tlpedndsdi appmatpvgd
      721 tqdprllpsq dtaaadegdn anqapsvsar kvrtmivrpd gtlvardepa peaastlpka
      781 ttvqtqkita gskpaggtaa nfpasrqvat adirstpvee tkptaaqaps enalakaaaa
      841 tsanvdppvr avksstvsdt apapatrpaa tdaakapeap tapaaqkpkd vaavspaatq
      901 tqptaaaggy gvqiaslpse eeakksyasl skkfasvlsg rsyeirkaei agkgtfyrvr
      961 ipagskdeaa aicekyraag gsclisk
//
LOCUS       WP_007790146             399 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Peptostreptococcus stomatis].
ACCESSION   WP_007790146
VERSION     WP_007790146.1
KEYWORDS    RefSeq.
SOURCE      Peptostreptococcus stomatis
  ORGANISM  Peptostreptococcus stomatis
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Peptostreptococcus.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Peptostreptococcus stomatis"
                     /db_xref="taxon:341694"
     Protein         1..399
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42904
     Region          1..398
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkvlvlncgs sslkyqlidm eneavlckgl verigiegsi lkhekegldg khiveqpmkd
       61 hkdaighvls avadpavgav kemkeidavg hrivhggekf assavltdev iaaikdcsdl
      121 aplhnpanlm gveackailp dvpmvgvfdt afhqtmpeks fmyglphely kkhgvrrygf
      181 hgtshlyvsq kaaemlgkkp edlkiitchl gngasitavd ggksvdtsmg ltpleglimg
      241 trcgdidpai ipfvmkkegl dadgvdklmn kesgvygmtg issdfrdied aaaegnqlai
      301 naldayaqrv kkyigayaae mngvdaivft aglgengigm reticadmdf mgikldpekn
      361 dvrgkdriis addsrvkvll iptneelmia rdtlrlsnr
//
LOCUS       WP_007790501             186 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Peptostreptococcus stomatis].
ACCESSION   WP_007790501
VERSION     WP_007790501.1
KEYWORDS    RefSeq.
SOURCE      Peptostreptococcus stomatis
  ORGANISM  Peptostreptococcus stomatis
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Peptostreptococcus.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Peptostreptococcus stomatis"
                     /db_xref="taxon:341694"
     Protein         1..186
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21566
     Region          3..179
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdilecirsr rsvrsftdqe ltydeimeli dlgmcaptgq yrqpwgfvii qdpeeikrws
       61 digkedilsr iddlpayqky inwfkdpdfn lfygaknlli vfgentspwy iedccclaqn
      121 milagfskgi gscwigfgqe ifnredfkke ynipesyvsi aplilgymes kpkppkrkea
      181 lifskk
//
LOCUS       WP_007790716             198 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [unclassified Rhizobium].
ACCESSION   WP_007790716
VERSION     WP_007790716.1
KEYWORDS    RefSeq.
SOURCE      unclassified Rhizobium
  ORGANISM  unclassified Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="unclassified Rhizobium"
                     /db_xref="taxon:2613769"
     Protein         1..198
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21962
     Region          1..167
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlrrlydwtm slaarksaev wlaviafves svflvpadvl ylpmalakpe rayryalvat
       61 aasvlggiag wmlgyyayda iarpvlefyg kldafeqlrl yihdeweill lllvtsglah
      121 lppikvvtil agvihmnlgf fiisaivarg arffflawll rrygepirhf iekrlgqvag
      181 vvaavaialg iaykllah
//
LOCUS       WP_007790631             735 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Rhizobium sp. CF122].
ACCESSION   WP_007790631
VERSION     WP_007790631.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF122
  ORGANISM  Rhizobium sp. CF122
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 735)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 735)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..735
                     /organism="Rhizobium sp. CF122"
                     /db_xref="taxon:1144312"
     Protein         1..735
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=78879
     Region          11..636
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mtraqqigvi iglaivaalt vlrasdppll rqirditfde yqrisprafe ptpvriidid
       61 easlkefgqw pwprdrlavl verlsdlgaa aiafdvlfae pdrlsprtvm rdvagvdptl
      121 lnrlpdndel faeaiagrpv vlgfgltteg syrppvkagf aftgespvna pprldaatpi
      181 rpqlqinatg lghislnpgn psavvrkvpl fltdgeqlyp nlaiealrva qgastyvlaa
      241 apeapdtlts akigefivpv tasgelwlyt spdvaeryis agkilapqgv dpqiaaaieg
      301 sivfvgtssa glqdirttal gqnvpgvsmh aqtveqiltg hflsrpdwad gmeilaiavl
      361 gtilvvlttf vspavalvcg lcitalalaa swfafsawgl lldplapiia gsiihfaats
      421 frilvidrer revrrafgqy lspsllyrie htrdamrlgg ddreltvmfv dvrgftelse
      481 rlqpaevvrf lntlldalsr hvtanegtld kfigdsimaf wnapvdvlnh pakavraala
      541 mretlaslna sdafgfgkey qvgigigiht glacvgnmga etrfnysavg davnvaarie
      601 sackevgfdi lvsentagel lhfalldagl lglkgkssra hlyaviggeq vrssgafadm
      661 qhihtelvta lrahsaesrk mlsvaklkaa eltatlpqfy srlgrraehf rdspgnddds
      721 traglprepk vhlep
//
LOCUS       WP_007791945             453 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Salipiger bermudensis].
ACCESSION   WP_007791945
VERSION     WP_007791945.1
KEYWORDS    RefSeq.
SOURCE      Salipiger bermudensis
  ORGANISM  Salipiger bermudensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
REFERENCE   1  (residues 1 to 453)
  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 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   3  (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   4  (residues 1 to 453)
  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 453)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Salipiger bermudensis"
                     /db_xref="taxon:344736"
     Protein         1..453
                     /product="CmpA/NrtA family 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=49602
     Region          24..300
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mknlllalta ttalssplla qdlekdeltf gfikltdmap lavayeqgyf ldeglfvtle
       61 aqanwkvlld gviggqldga hmlagqplaa tigygteahi itpfsmdlng ngitvsnavw
      121 eemkpniptn edglpqhpis aealapvvek yrsegkpfnm gmvfpvsthn yelrywlaag
      181 glepgyyspe nvtgqigadv llsvtpppqm patleagtiy gycvgepwnq aavfkgigvp
      241 vitdyelwkn npekvfgita dfaeenpntt kavvkalira amwldendna nrmeavemls
      301 qpeyvgadae viansmtgtf eyekgdkrev pdfnvffryn atypfysdav wyltqmrrwg
      361 qiaeakpdsw ydevaksvyk peiyleaara lvdeglanea dfpwdsdgyk datpaadiid
      421 gipydgrtpn gyleslpigl kgeqkvvgne iqg
//
LOCUS       WP_007793920             149 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Salipiger].
ACCESSION   WP_007793920
VERSION     WP_007793920.1
KEYWORDS    RefSeq.
SOURCE      Salipiger
  ORGANISM  Salipiger
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Salipiger"
                     /db_xref="taxon:263377"
     Protein         1..149
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15864
     Region          7..143
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlteaaalgg lflaafgaat ilpfqsevvf vgmqlgnaap lvlivlvasv gnilgavvny
       61 vlgiwlehfr hrrwfpvsea qlaraqraya rwgvwtllls waplgdaftv iagvmrthwa
      121 vflalvtiak tgryivlawa taatmgtga
//
LOCUS       WP_007795149             218 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Rhizobium sp. CF122].
ACCESSION   WP_007795149
VERSION     WP_007795149.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF122
  ORGANISM  Rhizobium sp. CF122
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Rhizobium sp. CF122"
                     /db_xref="taxon:1144312"
     Protein         1..218
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=23111
     Region          10..195
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mtssdkrlnv vlavtgasga algvtvldql adsgvqvhlv vsdggkrtla hevgteahgk
       61 mlikahrhyd nrnigaaias gsfpvagmiv apcsmkslaa istglsdslv araadvqlke
      121 rrrlvlitre tplhlghlrn mtsvtemgai vmppvpafyn rpqsvediid hlarravdll
      181 alpiprlapa wqgeskvqsa ddsqrvrsek htvaatkq
//
LOCUS       WP_007795904             996 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Salipiger bermudensis].
ACCESSION   WP_007795904
VERSION     WP_007795904.1
KEYWORDS    RefSeq.
SOURCE      Salipiger bermudensis
  ORGANISM  Salipiger bermudensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
REFERENCE   1  (residues 1 to 996)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 996)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 996)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..996
                     /organism="Salipiger bermudensis"
                     /db_xref="taxon:344736"
     Protein         1..996
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=109070
     Region          <896..>945
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mirriihaac lalltplaal aqeqrdaakv yvfgnslvhh lneegtanvp ywmgvlarad
       61 gralaldgqw gflrdfassl pprpnwsvpd vsghwdagrg tfgdagfdav witptnfiqy
      121 qapdapydyd naanespmga ilkvvdwvdn rvpgipiyly egwaemaals rsfppsaral
      181 rryhamnqgd yhdwyetlrd dlrserpead irlipvapil svllgedgpl edvpaealyv
      241 dldphgtpsl yflaamitya atfqapppad ftppetlhpe ivanypelaa lvwdeisasg
      301 vlesagltpe apatrtaeaa aesepeaapa asaepmpvrg qvalpdpgar pegapalamg
      361 lngiadwstq apfldhmkta rqwvghlpgq wggveaeelr aegaldeagw pvsiperver
      421 leallltdis sdaeyligty rvfwegkgtl ditgrasrvr lgegegqfwy apgegavgvs
      481 itatdpddpi rnirivredq lalfeagalf nplwierird lrnlrfmdwm htngspvqsw
      541 ddrprmsdfs wtsrgvpaev mlrlanrvga dpwfniphma dddyvrqfae lvkarldpdl
      601 kvyveysnev wnhifeqarw adaqadalwg rseagwmqyy glrsaqvmqi wtdiygdeae
      661 drlvrvvsth tgwpgleesv lmaplaylql ghppqdlfda yavagyfgye mggeemapqv
      721 ddwlarseaa avaageaegl rrvalreyvr ehrfdaavap valalldgsl kelieeifpy
      781 hasaaeaagl elvmyeggth vsaqmvrvqd eelaeffkyf nytpemakly eelltgwvas
      841 ggtlfnafvd vapasqwgsw galrhladdn prwnmlmsyn atapadwepr apgsfddgll
      901 legdagsetl egsakpdill ggdgddtlig qggddilhgg egrdvavlpg aqadyaftre
      961 egrlvangpq givrmvqvea lsfsdapgve lptagl
//
LOCUS       WP_007797332             437 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Rhizobium sp. CF122].
ACCESSION   WP_007797332
VERSION     WP_007797332.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF122
  ORGANISM  Rhizobium sp. CF122
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 437)
  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 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   3  (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   4  (residues 1 to 437)
  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 437)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Rhizobium sp. CF122"
                     /db_xref="taxon:1144312"
     Protein         1..437
                     /product="CmpA/NrtA family 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=47192
     Region          45..306
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mtkisttgis ttsmtrrsml kmtataalig avktafpsga faagagpevk glklgfialt
       61 dsapliiake kgffdkhglp etdvakqasw gatrdnlvlg gaangidgah ilsplpylmh
      121 tgkvtqnnkp vpmailarln ldsqgisvak eyaetgvqld asklkaafek kkaegkevka
      181 amtfpggthd lwirywlaag gidpnkdvst ivvpppqmva nmkvgnmdvf cvgepwneql
      241 vnqgigftaa ttgelwkghp ekalglradw ieknpnaaka llmavmeaqq wcesmdnkae
      301 madilgkrqw fnvptkdvlg rlkgdinygn grevkatdly mkfwkdgasy pfkshdtwfm
      361 tenirwgnlp antdikalvn qvnrediwre aakdlgvaaa dipasssrgk etffdgkvfd
      421 penpfaylds lsikaas
//
LOCUS       WP_007798670             706 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Salipiger bermudensis].
ACCESSION   WP_007798670
VERSION     WP_007798670.1
KEYWORDS    RefSeq.
SOURCE      Salipiger bermudensis
  ORGANISM  Salipiger bermudensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Salipiger bermudensis"
                     /db_xref="taxon:344736"
     Protein         1..706
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72231
     Region          1..705
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mtdlslidgl iapksvaiig asedpgrigg rpiaamlkag yegrilpvnp krdtvqglpc
       61 yasvgdlpea peaaliavpa klvpqtieal grkgckaatl fsagfaetga egeaaqrelv
      121 alagkhgmrl lgpntlgvyn vdigyygtfs ssldtgfprp gnigiasqsg afgahlgala
      181 rdqglgcsvl ittgneadit vadairwmae sdsidvicty meavndapal laaldvaraa
      241 gkpvlalksg rsavgaraaa shtasltgda vvadavltdh gaiilrdpes mmdiayaask
      301 kvlpsqhslg vvtvsggagi vasdeaerig lpmpsmpdea qakllevlpy asavnpldct
      361 aqalnepall eqftraglee ggygavlcfl tyvagserls kvileamapl raafpdriia
      421 fcalgdpevl rrydeagilv fndpcravra ldavlrlgsa qassvkaalp epkpvllpat
      481 spdeaeakal laeaginaap eqavqsaeea vaaaegfgyp vvmkilspdi lhksdigavk
      541 lnirdadgvr aahadilsaa athasharvs gvlvarqlsg gveclmginr dptfgpvavf
      601 glggifvell ndvalracpf gpetaremil sirsaailqg argaapadid alaemlskls
      661 vfaagagerl vsidlnpvla mpegqgayal davieldaqe vaadgh
//
LOCUS       WP_007799847             333 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Salipiger bermudensis].
ACCESSION   WP_007799847
VERSION     WP_007799847.1
KEYWORDS    RefSeq.
SOURCE      Salipiger bermudensis
  ORGANISM  Salipiger bermudensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
REFERENCE   1  (residues 1 to 333)
  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 333)
  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 333)
  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 333)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Salipiger bermudensis"
                     /db_xref="taxon:344736"
     Protein         1..333
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=36807
     Region          1..328
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mktktllsma tglamilgga ahaettwkma tkmpvdspeg qvfekfaelt eeytdgelki
       61 tvypneqlgk enavleqlqa nivqiyaegf gymkkwepal gwlagpyafd dfahwqrfmn
      121 sdtvkgwfdn aaaesgvrpl gdptlvlrgp frvtvsnvpv esaadyeglk mrmhenkvai
      181 dtwdnlgaev itlpwtevyq siskgivqav nspialvesm rfnevapyit rmdeywqsvg
      241 fmvnesalea ldedtrdgll kayaeagels qeimfsvade siermvadga tyteidispl
      301 vekmatfyad maesgelpeg fleaveaart ptq
//
LOCUS       WP_007798878             390 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Salipiger bermudensis].
ACCESSION   WP_007798878
VERSION     WP_007798878.1
KEYWORDS    RefSeq.
SOURCE      Salipiger bermudensis
  ORGANISM  Salipiger bermudensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
REFERENCE   1  (residues 1 to 390)
  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 390)
  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
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 390)
  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   5  (residues 1 to 390)
  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   6  (residues 1 to 390)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 390)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 390)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Salipiger bermudensis"
                     /db_xref="taxon:344736"
     Protein         1..390
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42078
     Region          21..65
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          85..378
                     /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 mdgseihrls nganltgvra hnerlilsmi qrngalpgsd lakhtglsaq tvsnilrkle
       61 aegfllrgep qrgrvgkpsv pmaldpdaal tfglkigrrs adlvvmnimg evldasqity
      121 rypmpdlifg yldremqrlg agltpyqrer lcgigiaaps eiwswtevlg apqdftvwrd
      181 idfveevgrv splplfvend gtaacraehi fgrgreftdy ahvfigsfig ggvvlnsgva
      241 agahhnagaf gslrvpgpeg gelqlidaas lylleaaive aggdaaamwe mpqdwrdyep
      301 mlsewigatg kalahatrsi gsvmdfeail idgafpadvr hrlvertree lekldtrgmv
      361 pprpeaalvg anaralgagc apiyaqyffq
//
LOCUS       WP_007800661             265 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Salipiger bermudensis].
ACCESSION   WP_007800661
VERSION     WP_007800661.1
KEYWORDS    RefSeq.
SOURCE      Salipiger bermudensis
  ORGANISM  Salipiger bermudensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
REFERENCE   1  (residues 1 to 265)
  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 265)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 265)
  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   4  (residues 1 to 265)
  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   5  (residues 1 to 265)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Salipiger bermudensis"
                     /db_xref="taxon:344736"
     Protein         1..265
                     /product="TRAP transporter small permease subunit"
                     /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=30136
     Region          26..182
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mteqtevvaa isdpgeigra dhnrgdrfvi qvsnlaawlf pilmiaicaq vvlrqmghnq
       61 awlddlqwwl ygaavlmgig yavttnshvr vdifydnfek rkrirtdilg lawlflpfii
      121 lcwdvtldya ltsiradegs dspnglhnlw imksfmnvaf ifiaiavwst yvrllskltr
      181 palwkqllfa fpsvayainl icyyaifgva yatrdpemsa rdvgrlpifg ewefgqhemr
      241 wtilialilt vvaivvarlf drkda
//
LOCUS       WP_007801781             701 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Salipiger bermudensis].
ACCESSION   WP_007801781
VERSION     WP_007801781.1
KEYWORDS    RefSeq.
SOURCE      Salipiger bermudensis
  ORGANISM  Salipiger bermudensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Salipiger bermudensis"
                     /db_xref="taxon:344736"
     Protein         1..701
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72936
     Region          4..701
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mpasfpdlkp ffspksaalv gasadlrkfg grclkqlvdf gyegriypvn pkadtilgmp
       61 cypdiaslpe apdhvgivvp gkaipgvlkq cgdrgvrhvt ifssgfsegg sadgaafqae
      121 ivalarehgi rlmgpncngl inyvdgfalt statingpra pkgdvavlgh sgglaqvnvm
      181 yraqqaglgi syqvscgnda dldildyaaf mvddpetrvi lmlaetirdg gklralsdra
      241 raadkpivmm klgrseegmq aavshtgala ssdsvaddvl rqlgilrvdd chemidvamm
      301 lrtgrrlggr glaavsisgg nlvhladqgp mhglafpdfg satktrmael ipnygqasnp
      361 advtsaaigs peifagvlet iaqdpavdvi lpvltlhsae lirgtaqall aspkpcaviw
      421 sgnctdddtl thaelvrmgl pvfrdiapam qvidaaarya elaqaarpvv apvppvqgld
      481 tlpgqpdead akaflaangf dvprgmvaet aadagpladr lggavvvkil saeighktel
      541 ggvqlnlnga tasaaaeemg arirevapdl elrgflieem aapgvemilg lsrdpvfgmv
      601 ltvglggima elledvahrl lpvsedeals mlrqlrgwpl ldghrgrapa dvsalvrtit
      661 tlsdlgmgsd grietldlnp vivgeagqga tvcdalvvls r
//
LOCUS       WP_007801294             231 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Salipiger bermudensis].
ACCESSION   WP_007801294
VERSION     WP_007801294.1
KEYWORDS    RefSeq.
SOURCE      Salipiger bermudensis
  ORGANISM  Salipiger bermudensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Salipiger bermudensis"
                     /db_xref="taxon:344736"
     Protein         1..231
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=25193
     Region          17..164
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mgpravprga wrltplwhps dnfgprrdga vpdivvlhyt amasaegard wlchpdagvs
       61 ahyvigrqgt vwqlvreemr awhaglgawg svtevnsrsi gieiantgae pfpepqmaal
      121 ekllagilqr wrippervig hsdmtpgrki dpgprfdwar larrglaica apaapgdfha
      181 nahrvgyrve anrhdallsa frdrfrpgar gpldetdrsl maglaakypa t
//
LOCUS       WP_007801526             173 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Salipiger bermudensis].
ACCESSION   WP_007801526
VERSION     WP_007801526.1
KEYWORDS    RefSeq.
SOURCE      Salipiger bermudensis
  ORGANISM  Salipiger bermudensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
REFERENCE   1  (residues 1 to 173)
  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 173)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 173)
  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   4  (residues 1 to 173)
  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   5  (residues 1 to 173)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Salipiger bermudensis"
                     /db_xref="taxon:344736"
     Protein         1..173
                     /product="TRAP transporter small permease subunit"
                     /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=19212
     Region          4..173
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 msrllaryad gmdrvsvfvg qacsvlfftc iaisalevvl rygfdrptvw stelamtlca
       61 tawvlavgfv ternrhisit mlelvvspkl wrlfrllqmm iafgsilvlt ialwkpamkv
      121 lsrteyagta lnsiqptifk vlivigclly laqlaaniir wvqrtegdls sgh
//
LOCUS       WP_007801824             681 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Salipiger bermudensis].
ACCESSION   WP_007801824
VERSION     WP_007801824.1
KEYWORDS    RefSeq.
SOURCE      Salipiger bermudensis
  ORGANISM  Salipiger bermudensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
REFERENCE   1  (residues 1 to 681)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 681)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..681
                     /organism="Salipiger bermudensis"
                     /db_xref="taxon:344736"
     Protein         1..681
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=69564
     Region          1..681
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 msplsrffsp kaitviggga wceavvrqcr atgftgpiwp vhpkksevgg epaypdlasl
       61 pgvpdaafig vnreltvkma gdlsrmgcgg avcfaagfse avseladgdd lqaelveaag
      121 emrvlgpncy givnaldgva lwpdrhgmsp vesgvavigq ssnvlinltm qrrglplaav
      181 vaagnqaqts msdlgialle npritalglh iegisdlpaf ealaaraael gkpivalrvg
      241 sseqaqaaav shtasltgsd agarallrrl giaqvetpte lvetlkilhv tgglrsaria
      301 sascsggeas lmadmgeiag vaypaltdtq ktglraalgp kvalanpldy ntyiwgdeda
      361 ltatftalcd agaalglgcv vvdyprddrf dapdydqvlr avaktrdatg tpmamvslla
      421 eglpepvarr alemgvvplc gmgdalkair aavavppggn arpdpvtlpl ngsgaarvfs
      481 eaeakallsg vgvrvpgsgr aadaataaet aarigfpvvl kgegiahkte agavvlnlas
      541 aqevsdaaag mpaesflvee mitgtvaeli lgvtrdpahg fvltlglggi ltelirdtas
      601 vlipasrddi aaalqslrta plltgyrgrp gadmdaiidt amalqtlvqd nasalheiei
      661 nplicratda vaadalirme e
//
LOCUS       WP_007802940             282 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Salipiger bermudensis].
ACCESSION   WP_007802940
VERSION     WP_007802940.1
KEYWORDS    RefSeq.
SOURCE      Salipiger bermudensis
  ORGANISM  Salipiger bermudensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Salipiger bermudensis"
                     /db_xref="taxon:344736"
     Protein         1..282
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31119
     Region          13..252
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mtaticdtrp celgegafwh perqqlfwfd ilsarllsfd atgplawqfd emhsaagwid
       61 rdtlllaset glwrfdigsg qrerlaeiea eddrtrsndg radpqggfwi gtmgkhaepg
      121 agaiyryldg kvtrlydsis ipnaicfspd grtahfadtr rqiiwrveld adgwpcgere
      181 vfldlraqgl fpdgavidae gglwnaqwga grvarylpdg qfdreilvgg rhsscpafgg
      241 pdlrrlyitt aregiehpda aqgllyqadg pvaglaeprv ra
//
LOCUS       WP_007803805             187 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Salipiger bermudensis].
ACCESSION   WP_007803805
VERSION     WP_007803805.1
KEYWORDS    RefSeq.
SOURCE      Salipiger bermudensis
  ORGANISM  Salipiger bermudensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
REFERENCE   1  (residues 1 to 187)
  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 187)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 187)
  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   4  (residues 1 to 187)
  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   5  (residues 1 to 187)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Salipiger bermudensis"
                     /db_xref="taxon:344736"
     Protein         1..187
                     /product="TRAP transporter small permease subunit"
                     /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=19651
     Region          25..164
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 msedtsatpe dqfvpafsda pvgavlgsla aamsaigtaa igalmlliva dvigrnlldl
       61 pitgvseiag rtvvaivflq vpaailqlrl tradflvrri arsspraval memcfclvga
      121 ivfalivwss wpkftsawas geffgvqgvw tiptwpfrgi tvlgaatatl aalyrvtref
      181 qtlkaap
//
LOCUS       WP_007804448             146 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Flavobacterium sp. CF136].
ACCESSION   WP_007804448
VERSION     WP_007804448.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. CF136
  ORGANISM  Flavobacterium sp. CF136
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Flavobacterium sp. CF136"
                     /db_xref="taxon:1144313"
     Protein         1..146
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16251
     Region          33..119
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 mneiiriaek eigqtekpan snktkyskwf gldgvawcgi fvswcyaqag fmlpkigfsk
       61 gyagcqtava yfkkmnqits tpvegdivff dwnsdgrydh tgifvrwlts dtfetiegnt
      121 avgndsnggs vmrrnrnkkt aifvhp
//
LOCUS       WP_007805166             109 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Flavobacterium sp. CF136].
ACCESSION   WP_007805166
VERSION     WP_007805166.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. CF136
  ORGANISM  Flavobacterium sp. CF136
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Flavobacterium sp. CF136"
                     /db_xref="taxon:1144313"
     Protein         1..109
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12191
     Region          1..105
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(6..7,25..26,34,37,39..40,42,45..46,48,56,61,68)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(25,56..57,59,85)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 maednffekv yaiarqipyg kvtsygaiak algtarsarm vgwamnashn tedipahrvv
       61 nrkgllsgkh hfdgtnlmqq llesegikvv nnqivdfekh fwqpeinhe
//
LOCUS       WP_007805418             250 aa            linear   BCT 20-JAN-2025
DEFINITION  prolipoprotein diacylglyceryl transferase [Rhodanobacter
            spathiphylli].
ACCESSION   WP_007805418
VERSION     WP_007805418.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter spathiphylli
  ORGANISM  Rhodanobacter spathiphylli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002130
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Rhodanobacter spathiphylli"
                     /db_xref="taxon:347483"
     Protein         1..250
                     /product="prolipoprotein diacylglyceryl transferase"
                     /EC_number="2.5.1.145"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008961 -
                     phosphatidylglycerol-prolipoprotein diacylglyceryl
                     transferase activity [Evidence IEA]"
                     /GO_process="GO:0009249 - protein lipoylation [Evidence
                     IEA]"
                     /GO_process="GO:0042158 - lipoprotein biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=27383
     Region          3..229
                     /region_name="Lgt"
                     /note="Prolipoprotein diacylglyceryltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0682"
                     /db_xref="CDD:440446"
ORIGIN      
        1 mspvalhtaf ealayaigfr tflwtrrrla paafrhedhl vwvavgaivg aalgaklsfw
       61 lddpltafae fpdlhhlleg ksiigallgg lagvelakkv agvdnstgda fvlpltlgmc
      121 igrigcflag lgdhtygvpt tlpwgvdfgd glprhptqly eigfllaqyv llhrrrealt
      181 rpgdrfrafm igyllfrlmv efikpvfyty pgglsglqwl cvaglvyyar diprilralf
      241 argsgawepr
//
LOCUS       WP_007805580             296 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Flavobacterium
            sp. CF136].
ACCESSION   WP_007805580
VERSION     WP_007805580.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. CF136
  ORGANISM  Flavobacterium sp. CF136
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 296)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 296)
  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 296)
  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 296)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Flavobacterium sp. CF136"
                     /db_xref="taxon:1144313"
     Protein         1..296
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33340
     Region          205..292
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(224,243..244,262,265,273..274,284,289)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mhlirnhlsg krkylfgllv lsfisvicaa fsmddsddfd isrrevllrr ighelllqsg
       61 dstsrvlpvk kiaeneyqir fendltfqpd slvnttrrll akdplardyv vnvlncgnss
      121 vaygyaiskn kkddivacig rrqpkacymi nvkfksavii taknayllgs lsflafvgli
      181 flrsakprra lpdskhtnmf plgsvlfdak nrkliingnt idltgtetrv llifalspne
      241 tiersrlqke iwedegvivg rsldmfiskl rkklefdpni kivvirgkgy kleisa
//
LOCUS       WP_007805934             271 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Rhodanobacter].
ACCESSION   WP_007805934
VERSION     WP_007805934.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter
  ORGANISM  Rhodanobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Rhodanobacter"
                     /db_xref="taxon:75309"
     Protein         1..271
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29536
     Region          23..270
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          28..120
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
ORIGIN      
        1 mnggvgkarg vlrpapgaps tglfhharia pppalagvvq hywivrwdlq ggppqlretl
       61 phpnvhlacd aagnrihgih tgrfstvleg cggvfgvkfr pggfhgflrq pvsvlrnrsi
      121 apeqvfgtva aelatiiqas pddehmvsla sdflvtrlpp pdaqalrvge mvdaiaidrs
      181 lrtlddlatr wsitprtlqr lfnqyvgigp kwvinryrmh ealervdagk pmdwtqlald
      241 lgyfdqahfi rdfkalvgcs pvgyarrvqa g
//
LOCUS       WP_007806251             490 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Rhodanobacter spathiphylli].
ACCESSION   WP_007806251
VERSION     WP_007806251.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter spathiphylli
  ORGANISM  Rhodanobacter spathiphylli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
REFERENCE   1  (residues 1 to 490)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Rhodanobacter spathiphylli"
                     /db_xref="taxon:347483"
     Protein         1..490
                     /product="amidohydrolase family protein"
                     /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=51823
     Region          43..477
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mhglsmdrsr tvlavallla glalatpsra avptlappvr ayvahaqpll aithvrvvdg
       61 hgtgarenqt vllrdgriaa vgrhvdvpge atvidgsgqt lmpglvgmhd hmfypaprvn
      121 paskellape qassfpklyl aggvttirtt gsvepytdla lkkaidagli pgpkmhttgp
      181 ylegkgslmp qmhelvdadd arntvnywmd egatsfkaym hitraelsaa iaaahargik
      241 vtghlcsigf teaadlgidn lehglfadte fsagkqpdvc pdtkaaithl atlkvdgpei
      301 rqlirhlvak hvavtstlpv fetfvpgrap ldarvldaml pqareeylkt rehvaamkds
      361 pwpklfqlem afehafvkag gtllagldpt gyggviagyg dqrevellve agftpvqaiq
      421 iatlngarfm gvdkqigsid vgkaadlvlv kgnpasnikd ienvvlvfkd gvgydpaklv
      481 eaangtvglr
//
LOCUS       WP_007806276             418 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Rhodanobacter].
ACCESSION   WP_007806276
VERSION     WP_007806276.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter
  ORGANISM  Rhodanobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 418)
  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 418)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Rhodanobacter"
                     /db_xref="taxon:75309"
     Protein         1..418
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47156
     Region          2..408
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mlklaqaram qlaaqgllqp pkrqprradl vtaiermrml qidtihvvar spylvlhsrl
       61 gnypmawlde alaqgqlaec waheacfvsa adiawhrggq dhrshhwahr haqrvhrehr
      121 kdmdallagi rdsgpvraad ferrdggass gwwewkpekr wleawfalge lmvarrdrfq
      181 rvydlaervl agldppfdvt lafspaqqrr hfiletvral gvtpaawigd yfrlkprvsd
      241 relapllesg ellavpvegw gtpgyvhreh aewldkalag klratlttll spfdplvwdr
      301 srvlamfgfe ytlecytpaa krrygyfvlp ilhrgrlvgr ldakahrdtg vfevkalfle
      361 pdarpepalv savaraiaat atwhgtekir lgstqpaslg rllraqwraa rvklagpg
//
LOCUS       WP_007806350             186 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Rhodanobacter spathiphylli].
ACCESSION   WP_007806350
VERSION     WP_007806350.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter spathiphylli
  ORGANISM  Rhodanobacter spathiphylli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Rhodanobacter spathiphylli"
                     /db_xref="taxon:347483"
     Protein         1..186
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=20785
     Region          18..177
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 msltihdqpl pyvellperp aaavelvvih ctelpdlata reygervlhp sgagnsghyy
       61 idrdgavyry vpgtrvanhv rghnpnsigi elvnlgryph wwdsrqqrmt epytdaqiia
      121 lhtllaelrr dfpnlrriag heqldtdlmp asddpaiqih rkldpgplfp waevleacgl
      181 srpavp
//
LOCUS       WP_007806600             262 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Flavobacterium sp. CF136].
ACCESSION   WP_007806600
VERSION     WP_007806600.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. CF136
  ORGANISM  Flavobacterium sp. CF136
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Flavobacterium sp. CF136"
                     /db_xref="taxon:1144313"
     Protein         1..262
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30229
     Region          176..244
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mftntgtisf ylylvfilis iistviiyrf lkkgtlesek ldklidffkt vvfttaigtv
       61 aliitdlfke reqdvkeley fdkyvqevkd vngqgrlqls kylsivapsg emkdswtnyy
      121 kevqkdyney lkaqqalknd tlpnitkeql ikrvenqekv qlfenpltni nnndewyiva
      181 ggdpkinean felekaikin anstiikkgn sfrtvlvgys skteaekylq evkqkinkta
      241 yivnknswcr qlengdecli ck
//
LOCUS       WP_007806746             361 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Rhodanobacter].
ACCESSION   WP_007806746
VERSION     WP_007806746.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter
  ORGANISM  Rhodanobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae.
REFERENCE   1  (residues 1 to 361)
  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 361)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 361)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 361)
  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   5  (residues 1 to 361)
  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   6  (residues 1 to 361)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Rhodanobacter"
                     /db_xref="taxon:75309"
     Protein         1..361
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39631
     Region          46..230
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <179..361
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 marpagmigp spvtspaias ddprytaaef ppnkllylvq ladaagvdsr pwfaglalsr
       61 eqiadpalrv syrqantfvr ralqaldvpd aglrigregt iggfgllgla mmtsrtlgea
      121 mfagiahhki cgcllevave paserevall awprfgdtel mpffceelfa sclmiarelv
      181 gaelcpvrad fayprpayaa ryealfgcev rfgaprnqll idtqwlarpl pgynpltaqq
      241 alalcaqqrt pdggephqei vaaverllrs qlaqqprlnd vartlnlser slrrklaesg
      301 rifreihdrv raeralqllq agtlsvaqig sevgfndpre frrafkrwtg mppqdarrna
      361 s
//
LOCUS       WP_007806964             738 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Flavobacterium sp.
            CF136].
ACCESSION   WP_007806964
VERSION     WP_007806964.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. CF136
  ORGANISM  Flavobacterium sp. CF136
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 738)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 738)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Flavobacterium sp. CF136"
                     /db_xref="taxon:1144313"
     Protein         1..738
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=82263
     Region          32..724
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 maklpvsaen iikhfgphkn yspkegfegr depdelvkth ccfcgmqcgi qlsvkdnkvv
       61 gfepwmefpf negrlcpkgv qrylqnnhpd rllsplkrve gqgfvptswd damsktvsei
      121 kriqekygnd afsvlsgvsl tneksylmgk farvalktkn ldyngrlcmv sagagnkkaf
      181 gldrgsnnys dleyaeviiv aganisetfp tlthwiwkar drgaklivid prmiplarta
      241 dlyldvrpgt dsalygamlk ylvdhdmldh dfidnhtsgf qetldavkdn tlewaeeitg
      301 ikkekiqqaa elwgkantsf llhargiehh skgvdnvlgc inlvlatgri gkpycgyati
      361 tgqgngqggr ehghkcdqlp gnrdienpeh rkyisevwgi nekdlpgkgl sayeiieaih
      421 rgeikgllsi cfnplvslpn snyvrealek lefyvcidff lnetarhadi ilagslqeee
      481 egtttsaegr virirqavtp pgdartdtsi ileiakrlgv kdkftyense aifnelrias
      541 kggtadyygi tyqriedemg vfwpcpeigh pgtprlwedr kfktpdgkah fnpapyklpg
      601 evtdaeypvi lttgrvvsqy lsgtqtrrig klvdqypepl leihpnlakq ygikqrelic
      661 vstrrgegif panivetire dtvfipyhws gkksanqltp gtldpiskip efkvcachle
      721 plneiappss esmayasv
//
LOCUS       WP_007807343             255 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Rhodanobacter].
ACCESSION   WP_007807343
VERSION     WP_007807343.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter
  ORGANISM  Rhodanobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Rhodanobacter"
                     /db_xref="taxon:75309"
     Protein         1..255
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=27666
     Region          33..180
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 msrplrlsrs vavlalvall aacahapprn platwvpspn hdirrpvliv vhftnqhsaq
       61 esldtlrtkn sggpvsshyl vgsdghiyql vsdqlrawhg ggghwgtitd insasigiel
      121 dndghspfaq aqidsllrll tdlttrlhip rtqvighqdf aptrkddpgp lfpwpqlaaa
      181 gfglwpqgel idppsgfdpw malglvgypl edraaavraf hnhyrgiggd eldaqdlril
      241 ynlaqiverg tplsd
//
LOCUS       WP_007808404             643 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Rhodanobacter].
ACCESSION   WP_007808404
VERSION     WP_007808404.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter
  ORGANISM  Rhodanobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 643)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 643)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 643)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Rhodanobacter"
                     /db_xref="taxon:75309"
     Protein         1..643
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=69381
     Region          12..643
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mntqadnpaq psahgdtahv rgakstlilg aigvvfgdig tsplytmhet flpehglhpr
       61 pstvlgilsl vtwslimvva vkyvslvmra dnkgeggima lmtlaqrasg ksvatrravm
      121 lmallgaalf fgdgvitpsi tvlsaieglq vaapslshyv vpvtvavlvg lfwlqrhgta
      181 kvgaifgpvm vvwflalgvi gvwniiqape vlralnpwha vqffmthgkt silalgsvvl
      241 cvtgaealyt dmghfgrvpi raawfffvmp alllnyygqg glllvhpeti anpfyhsvpe
      301 walypmiala tmaaviasqa visgaftvcr qaiqlgflpr mqvvhtsrea igqvflpwin
      361 ralmvaviat vvgfgssnal agaygiavtg tmaidtvlvm ivarrmwqws rllviglgvi
      421 llaidlsyfg antlkilqgg wfplvlgllm favmttwrrg relvvreikq gglalapfie
      481 nmaahpplrv pgtavfltan lsavphallh nlkhnkvlhe rnvlltvgil etpvaeader
      541 iqltalssgs ddfyalelrf gfaedpnipq alsqcsregl afdmmdttff lsresivade
      601 rrpgmalwrd klfafmsrna lpataffqip gnrlielgaq vei
//
LOCUS       WP_007807489              78 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Flavobacterium sp. CF136].
ACCESSION   WP_007807489
VERSION     WP_007807489.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. CF136
  ORGANISM  Flavobacterium sp. CF136
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 78)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 78)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 78)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Flavobacterium sp. CF136"
                     /db_xref="taxon:1144313"
     Protein         1..78
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8549
     Region          1..78
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mieikyfgav aektkcsfen visteislqd llqdldekyq feslsfsvav nqkivskatd
       61 yslktrdvva llppfagg
//
LOCUS       WP_007808955             129 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Flavobacterium sp. CF136].
ACCESSION   WP_007808955
VERSION     WP_007808955.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. CF136
  ORGANISM  Flavobacterium sp. CF136
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Flavobacterium sp. CF136"
                     /db_xref="taxon:1144313"
     Protein         1..129
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14694
     Region          57..126
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mriltpskti llslsmfalt cninaqeqni slnqdpkfeq llndkrkint sistndtyki
       61 qifsgksdea kktlsgfkre fntidgtiif ntpnykvivg nfktrieaer nleeikkkyk
      121 svflvkpsk
//
LOCUS       WP_007812007             782 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Rhizobium sp. CF142].
ACCESSION   WP_007812007
VERSION     WP_007812007.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF142
  ORGANISM  Rhizobium sp. CF142
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 782)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 782)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 782)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..782
                     /organism="Rhizobium sp. CF142"
                     /db_xref="taxon:1144314"
     Protein         1..782
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=81335
     Region          40..284
                     /region_name="COG3934"
                     /note="Endo-1,4-beta-mannosidase [Carbohydrate transport
                     and metabolism]"
                     /db_xref="CDD:443135"
     Region          422..684
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          603..>710
                     /region_name="Peptidase_M10_C"
                     /note="Peptidase M10 serralysin C terminal; cl23859"
                     /db_xref="CDD:451582"
ORIGIN      
        1 maqairitdv idsfgidthi dytdgkysni aevvkalgyl gldtvrdhap tpasdpygqg
       61 hlgdaadagv kfvfvsgrdd tpatvvqrlh afveahpgsi vgiegpnevn nwpvaykgls
      121 geaaalayqk dlfnavnadp llkdipvlgf tgytvasand yttihtyake gdqpfswlsr
      181 esgdqmqadp gkplaiteig yhtsltadtn ggwegvdett qaklllntlm dgaflgsegt
      241 fiyqlldays dpqgsdqekh fglfrldytp kpaataihnl teiladdgat qasfnpgaln
      301 ysinglpsta rsylteksdg syqiiiwnep diwnqttdka iqasttsvnv nlggafgtvq
      361 vydplagdtp vksfsnissl nvdvvdhpii iniaagggaa lepghiyggt gddtftvtsp
      421 tdivdesrgg gtdtvmssis fsladtahai gaienltltg naninatgnq lanilvgnyg
      481 anvldggaga dsmkggggdd tyivdnindv vieaggsgkd tiksyvslsl mdkdhvtgtv
      541 enltllgtdn inatgnvmnn vltgnsgdny fdggrgedrm igglgndtyk vdsagdivde
      601 tggagndtvn asvsfslenv lgtvenltlt gssainatgn gennvltgni agnmlsggag
      661 ndqliggngn dilnggagad hfvfdfkpsa ynnidkiedf sesagdkivl dheiftaidp
      721 anfsagnfvl gtkaldsndr liydqttgkl fydadgsggg aavqiatlsn laalhhddfl
      781 fi
//
LOCUS       WP_007813075             338 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Roseobacter sp. AzwK-3b].
ACCESSION   WP_007813075
VERSION     WP_007813075.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. AzwK-3b
  ORGANISM  Roseobacter sp. AzwK-3b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 338)
  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   5  (residues 1 to 338)
  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   6  (residues 1 to 338)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Roseobacter sp. AzwK-3b"
                     /db_xref="taxon:351016"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37153
     Region          21..>164
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <151..334
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mdhlqtyslf matevacril gvdpqvmlen aglggltpgr searvtaqqy fdcwntmgal
       61 ssrpdyvpyl gvaisrgpvi pvfftlscap dmetglrrla qfksllgptv mrvfrdgdll
      121 rleyesvdar vpmppslgal qlvvavenir gatahlvcpv aagfdgseee rhmiaghlgi
      181 mpersqvtyv afapedakrr fisenaalwa dveadlrlkl aaqndhlpva yrvrgalvdl
      241 mpagrtgaed vglslgvsrs tlqrrlreeg tsyqqvldat rrglairylk ktalrvdeia
      301 nvlayrdans fsrsfrrwtg qapvafretl rrqageae
//
LOCUS       WP_007813457             142 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Roseobacter sp. AzwK-3b].
ACCESSION   WP_007813457
VERSION     WP_007813457.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. AzwK-3b
  ORGANISM  Roseobacter sp. AzwK-3b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Roseobacter sp. AzwK-3b"
                     /db_xref="taxon:351016"
     Protein         1..142
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15150
     Region          16..132
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mialsglfla afaaatifpf qseavlagll vaathpatll iavatlgnvl gsvvnwvlgr
       61 yllafrdrrw fpasasqldr aqawygrygr wsllgswlpv igdpltvvag lmreplpsfl
      121 llvtiakgar yillaaatla wl
//
LOCUS       WP_007815439            1051 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Roseobacter sp. AzwK-3b].
ACCESSION   WP_007815439
VERSION     WP_007815439.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. AzwK-3b
  ORGANISM  Roseobacter sp. AzwK-3b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Roseobacter sp. AzwK-3b"
                     /db_xref="taxon:351016"
     Protein         1..1051
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=111888
     Region          <551..709
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          678..919
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mrytmaintt ektyvnpdev ipasafgaef lgwepfsnfv arnqelnlph irwpggipve
       61 eginvdgsad gsrehvfdlk fdnlvewdrn ngdpregike mfayanetsa tfamvtptar
      121 yvekmfkqgd eaglaearad arifaeklva geygavpagf tievgseyya tgiwkemtsd
      181 esgrpyqkdp gplaekfgkv faavvdemge vfadptlnvn gtevklavql arhqadpsqn
      241 ggdfsdnidf ieafidtgai dkvdtllfhk ytptfdnisr gmdedangyr lddafalweq
      301 asggkefefl ggylspsags eerleygapg ltnllqvnaq flaagmdvgt vyaighsngg
      361 slgwreellv ggklfdlmge sipgkflydg fqdnisnvad lgrsyiggnh vnsyvygndt
      421 evtvflaasd ftgeqldyrl kfdesflnae ithlwatgeq lfhpgdgeli gsfgdslsyt
      481 idlmasdsps sldvtfehdy evvrivleks epvtfetlvl dapvelapve mllasaaaav
      541 stpasasdap gddlllgtda adringklgn dtvwgvagdd tvkggwgddi vdggagddkv
      601 tgdwgndqlf ggdgndvifg gtgdnvlfgg agndrlvatg rldildggag ndtliagaet
      661 tilkfttgqt igarqevdtv hdfvlgqdvi eidglnfsdr ddgfssadfl rehasirgnn
      721 leialseght vvlknlvsql pstsdsvdfq qifggsnaas tasieevpqa phgwihageg
      781 ndvmtgsatf dqlngelgdd tisggagndt vkggwgndrv dggsgddrvt gdwgddilfg
      841 gsgddtifgg dgsdslfggn gndrlvasgq kdfladgagn dtleagaett ilsftkndap
      901 fgpvetdivh gftlgqdfle idgldfdden gpqsreefml dnvsirgknl eirlsedhtv
      961 ilknvtaqip gdpsvadfqq ifgfgasssp edepdslssl liqepaetga aslelffmem
     1021 tggqletaaq eqmdkeaegt tandpwaflf a
//
LOCUS       WP_007815346             407 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Rhizobium sp. CF142].
ACCESSION   WP_007815346
VERSION     WP_007815346.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF142
  ORGANISM  Rhizobium sp. CF142
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 407)
  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 407)
  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
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 407)
  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   5  (residues 1 to 407)
  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   6  (residues 1 to 407)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 407)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Rhizobium sp. CF142"
                     /db_xref="taxon:1144314"
     Protein         1..407
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44194
     Region          13..60
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          78..374
                     /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 mltksstelv rqrnsvlvla tlrrhgplah teisdftrls satvsaitad lekaqvieks
       61 eqqaasgrgr prvllrqrrd cgylvvviis sdavqyslvd ysgklidrfs eershdpdga
      121 grfvngvrag lerilsrsri erekvllisi sskglvnsse pvlvwspifg sdqidfelal
      181 kpewkakvil dnetllvaaa lgareenvkg adfrslaals lghsiglgii rrtshgghev
      241 sapnfghmlh mangglcrcg trgcieayag fyailrtafe vpldtipakf vpvaeldkia
      301 ararqghris gfafrqagla lgnglsrmls ltermpiait gpgtryydll rqgieeglgq
      361 shmvrmegmp elrvvadeqi lvfeghlnra lavidedivv aglqggd
//
LOCUS       WP_007815596             308 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Roseobacter sp. AzwK-3b].
ACCESSION   WP_007815596
VERSION     WP_007815596.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. AzwK-3b
  ORGANISM  Roseobacter sp. AzwK-3b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 308)
  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 308)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 308)
  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   4  (residues 1 to 308)
  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   5  (residues 1 to 308)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Roseobacter sp. AzwK-3b"
                     /db_xref="taxon:351016"
     Protein         1..308
                     /product="TRAP transporter small permease subunit"
                     /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=35220
     Region          83..288
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mndtattggl davldgilwl vqniamafyn lgyaishphl wldwsdkeai mrfvyyggsv
       61 efffvvftvf lvctgiglwr ngfmwgcvrv legfantvgr ffawaglimv iqqiiivflq
      121 rifarpeivi gfgiplemdi swwseelkly nalvvslcat ytfvqgghvr vdliysavsf
      181 rtkrvidmvg sllfmmpmav iiwlygwffm wrhlivpnps asesldrllm ksralrwnve
      241 tigfspngfn ayflfkillv afagmvfiha vaffyrsfle wregpesenk yldkdslgeg
      301 qeafegth
//
LOCUS       WP_007815599             361 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Roseobacter sp.
            AzwK-3b].
ACCESSION   WP_007815599
VERSION     WP_007815599.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. AzwK-3b
  ORGANISM  Roseobacter sp. AzwK-3b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 361)
  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 361)
  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 361)
  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 361)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Roseobacter sp. AzwK-3b"
                     /db_xref="taxon:351016"
     Protein         1..361
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=38657
     Region          1..331
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mdrrsflkns alggtaaaaa glaapayaqg krtltlvttw grglagvhds aqycadaita
       61 msdgqltvdl kaagelvgaf evfdavtagq adlfhgvdyy flsqhpalsf fsqvpfgmtf
      121 qefnnwfdhd ggreladely sifglksfpa gntgpqsggw yakemnaved fqglrfrmpg
      181 qggqvmgklg asvqnlpgae vyqalasgai dgtewigpwa dekagfqeit kfyytggfhe
      241 pgpnlnlnvn levyesltpa qqsiienaar asnlwtmslf mannsaaltr lqssgvklls
      301 fsdaiwdafg aaskevvees lsdeiyktcy dsymaslass aswasrsege faaqrnrvmg
      361 l
//
LOCUS       WP_007815858             189 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Roseobacter sp.
            AzwK-3b].
ACCESSION   WP_007815858
VERSION     WP_007815858.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. AzwK-3b
  ORGANISM  Roseobacter sp. AzwK-3b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (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   2  (residues 1 to 189)
  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 189)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Roseobacter sp. AzwK-3b"
                     /db_xref="taxon:351016"
     Protein         1..189
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=20482
     Region          18..71
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msitalqnaf dairqhkmsn saklvllcla nrhnqetgrc dpsiptiatd mkiseraard
       61 glrelerlgl vktirrtvrt glgkrnmsnr ynlrggakya ggmgqnlpgk qeykrtsvfd
      121 dlamllesqp kadfgeagri nskpwpsasa gfaekgsegc hvapflsprg nlgdgtapdq
      181 eqpnspeee
//
LOCUS       WP_007816138             422 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA, partial [Rhizobium sp. CF142].
ACCESSION   WP_007816138
VERSION     WP_007816138.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF142
  ORGANISM  Rhizobium sp. CF142
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 422)
  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   3  (residues 1 to 422)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Rhizobium sp. CF142"
                     /db_xref="taxon:1144314"
     Protein         <1..422
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <24..411
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 aaaaaaaaas aaaqnnaaag agqtirvdld rvdrlinlvg elvinqamls qsviendttg
       61 tssinmglee lqqltreiqd svmairaqpv kpvfqrmsri vreiadmtgk sirlitegen
      121 tevdktvidk laeplthmir navdhgietp ekraaagknt egtvrltakh rsgriliela
      181 ddgaginrek vrqkaianel ispdanlsde eidnliflpg fstadkisdi sgrgvgmdvv
      241 krsiqalggr initsrpgqg svftmslplt lavldgmvvt vagqtlvvpl taivetlqpe
      301 aaaihsfgan hrlisirnsf cplvdvgril nfratqanpv egvallvese gggqralmvd
      361 aiqgqrqvvi ksleanythv pgiaaatilg dgrvalildv davvgasrgq slkaemslaa
      421 vg
//
LOCUS       WP_007816261             145 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Rhizobium sp. CF142].
ACCESSION   WP_007816261
VERSION     WP_007816261.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF142
  ORGANISM  Rhizobium sp. CF142
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Rhizobium sp. CF142"
                     /db_xref="taxon:1144314"
     Protein         1..145
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15766
     Region          2..141
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 madllaylgl fvsalgaati lpmqseavlv gllltekyst fwlvataggg nvlgallnwf
       61 lgrgierfrt hrwfpigpqa leraqhwyqr ygkwsllasw lpivgdpitv vagvlreplp
      121 mflllvtiak vgrylvltaa ttglt
//
LOCUS       WP_007817262             271 aa            linear   BCT 20-JAN-2025
DEFINITION  phosphonate ABC transporter ATP-binding protein [Roseobacter sp.
            AzwK-3b].
ACCESSION   WP_007817262
VERSION     WP_007817262.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. AzwK-3b
  ORGANISM  Roseobacter sp. AzwK-3b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
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   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Roseobacter sp. AzwK-3b"
                     /db_xref="taxon:351016"
     Protein         1..271
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=29221
     Region          25..271
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mmldlvtdrp sgaaakaqal aqngpliaah glcksydrrr tildgvdlei aagervalig
       61 sngsgkstll ksliglhpis ggtlqcfgep vdargsrkqr lamrrqtgfv fqkhclvrrr
      121 tvlsnvihgl fgdagswraf shslappewr dramqalaev dladkalera dalsggqqqr
      181 vaiaralvrr prlliadepa asldpvsgrn vmelftqlcr dhgitllyts hdmahavdya
      241 drvvalkggk vlfdrpaaqv tradlkdtfd g
//
LOCUS       WP_007817029             310 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Rhizobium sp. CF142].
ACCESSION   WP_007817029
VERSION     WP_007817029.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF142
  ORGANISM  Rhizobium sp. CF142
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
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
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Rhizobium sp. CF142"
                     /db_xref="taxon:1144314"
     Protein         1..310
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=33579
     Region          1..307
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mirmenvtkr ygesvapsvd nltldvpegs tvaligpsgc gktttmrmin rlieptegri
       61 fvngedvtka dpvklrrhig yviqnvglfp hmtiaeniaa vpnllgwdqp rivkrtdell
      121 dlvgldpkem lkryprqlsg gqrqrigvar alaadpsvll mdepfgaidp iartrlqdef
      181 kqilkrvrkt vvlvthdlde airlgdriai mragkivqyd apdailshpa ddfvanfvgi
      241 draikrlslf svadamrsda psspaasvaa nanlrdalsl mvaansdvls vvdgggivtg
      301 qltrdaifsi
//
LOCUS       WP_007818307             328 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Roseobacter sp.
            AzwK-3b].
ACCESSION   WP_007818307
VERSION     WP_007818307.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. AzwK-3b
  ORGANISM  Roseobacter sp. AzwK-3b
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 328)
  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 328)
  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 328)
  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 328)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Roseobacter sp. AzwK-3b"
                     /db_xref="taxon:351016"
     Protein         1..328
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=36302
     Region          1..326
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mqaawgggif lenaqsfanr vnemsggslv ievlsvdsvv ktsqmqdavh rgvldaahyv
       61 saywygksks aslfgtgpcf gwssqemlgw vhagggqelf delmdnlqln ivsffnspmp
      121 aqplgwfqqe itdasqmngl kyrtvglaad vllemgmsvv qlpggeiqpa mksglidaae
      181 fnnptsdrdf gmqdvskhyh lasyhqsqec fevtfnkdkf nalsaehqai irnasmaens
      241 gfywgntkry sddliklqea dgvnvyrtpd svlaaqleaw dvvanriaee dpffakvmes
      301 qkayakdvmn ylnlnqpdyk laynhyfg
//
LOCUS       WP_007819276             237 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phosphonate ABC transporter ATP-binding protein
            [Streptomyces].
ACCESSION   WP_007819276
VERSION     WP_007819276.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
REFERENCE   2  (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   3  (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   4  (residues 1 to 237)
  AUTHORS   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 237)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..237
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=24876
     Region          1..234
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mlrmsgitvs ygprtvlhgv dvsaapgemv avlgangsgk stllravigl qpmtagsvtl
       61 dsrpcgpldi amifqhihlv rrrtalenvc agalgrlspr hslhpalfph dvreeamacl
      121 drvgladrah dragglsggq qqrvavaral cqrprvllad epvsaldpaa seqvlgllad
      181 lahreklpvl avlhqpalad rhadriiglr dgrvlldgap gldvdtlyqs savepvs
//
LOCUS       WP_007819601             639 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Streptomyces sp. Tu6071].
ACCESSION   WP_007819601
VERSION     WP_007819601.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. Tu6071
  ORGANISM  Streptomyces sp. Tu6071
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Streptomyces sp. Tu6071"
                     /db_xref="taxon:355249"
     Protein         1..639
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=66871
     Region          260..410
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mherkskrwl tqavaagava agtlaflpap aqaqgapphd gglqadfaaa aasygvptsv
       61 lmavtheesg wrwhkgyses ggygladltd vtadmlvdgd agaggradla amvdkpelht
      121 lrkaakltgi paarlrtdrr anldgaaall asyqkslrae askdpadwtg avaeysglkd
      181 ekaargyvdn vfrtirsgas lrqadgntvr laadpsarpa vgrpaglklr ttaaapdaec
      241 paslscafdp vpiaangqvs drpangiaid rivlhtaegs fasakqslsa pgavsgahyl
      301 mdtdgtttql mankdlafav gnyhynlhsv sieqagftar gadwytdavy qrtaelvkyl
      361 aerydvpldr qhvlghdnvp gsldsnlaaq hwdkgtawdw nrfmrllgap tdagtrgvgk
      421 agsvvtiapq fgtsaeqtyt vcpaddpsga tpacakvpqp snslfvrtap aadaplfldp
      481 vvhpgdqagt daisdwsdrv qagqqfvvag regdwtaiwy ggqkgwihnp ggrntipakg
      541 vkvikargtt aapvygqayp easeypagls pstqkpltaa nygipvgqay vadqpptpad
      601 dyftsggevv tgsrtyyqvq fnhrtiyvns advtatpac
//
LOCUS       WP_007820883             399 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Streptomyces].
ACCESSION   WP_007820883
VERSION     WP_007820883.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 399)
  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   5  (residues 1 to 399)
  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   6  (residues 1 to 399)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 399)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..399
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40672
     Region          14..>59
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          77..379
                     /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 metpgsqssl hranlervvr avrlagsltq aeiarttgls aatvsnivre lreigtvevt
       61 ptsaggrrar svslsgnagi vigvdfghth lrvalgnlah qvlaeesepl dvdasaaqgl
      121 draeevvarl isatgvdeak iagvglgvpg pidvesgtlg stsilpgwsg trpaqelsgr
      181 lgvpvhvdnd anlgalgelv wgagrgvrdl ayikvasgvg aglvidgriy rgpggtagei
      241 ghitldeagp vcrcgnrgcl etftaaryvl pllhsshgad ltlermvrla regdpgcrrv
      301 vgdvgrhigs gvanlcnlln psrvvlggdl aeagelilgp iresvgryai psaarqlsvl
      361 pgalggraev lgalalalse mgdstllegp vpaarhaft
//
LOCUS       WP_007821239             265 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces sp.
            Tu6071].
ACCESSION   WP_007821239
VERSION     WP_007821239.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. Tu6071
  ORGANISM  Streptomyces sp. Tu6071
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptomyces sp. Tu6071"
                     /db_xref="taxon:355249"
     Protein         1..265
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=29920
     Region          1..252
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mryemlgplr vrdentyftl haqkvemvlt vlliradhlv fpeqlmreiw genlprraaa
       61 glhvyvsrlr kflklagasg npvetrtpgy vlhkgddqid aqifpelvdv grsllreqrt
      121 deaascfsqa lalwrgpipg hrcdgtgakg piiggfstwl teirrecqem lvecqlqlgr
      181 hreavsmlya ltaenpmcea fyrqlmlaly rserqadalk ayqsvrktln delglepgrp
      241 lqdlqrails gdmhlmsspl amsdr
//
LOCUS       WP_007822506             377 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: threonine synthase [unclassified Streptomyces].
ACCESSION   WP_007822506
VERSION     WP_007822506.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 377)
  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 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
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Parsot,C.
  TITLE     Evolution of biosynthetic pathways: a common ancestor for threonine
            synthase, threonine dehydratase and D-serine dehydratase
  JOURNAL   EMBO J 5 (11), 3013-3019 (1986)
   PUBMED   3098560
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10107605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..377
                     /product="threonine synthase"
                     /EC_number="4.2.3.1"
                     /GO_function="GO:0004795 - threonine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009088 - threonine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38552
     Region          57..367
                     /region_name="Thr-synth_1"
                     /note="Threonine synthase is a pyridoxal phosphate (PLP)
                     dependent enzyme that catalyses the last reaction in the
                     synthesis of threonine from aspartate. It proceeds by
                     converting O-phospho-L-homoserine (OPH) into threonine and
                     inorganic phosphate. In plants; cd01563"
                     /db_xref="CDD:107206"
     Site            order(74,79..80,95,118,134,137..138,144,160..166,168..170,
                     182..183,214,329..331,332..333,363)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:107206"
     Site            order(101,127,228..232,361)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:107206"
     Site            101
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107206"
ORIGIN      
        1 mtsaapssaa lpdrlcprdg trvpladpaw ccpacagpld ldfhpvpepp agpatslwry
       61 adilppaapg islgeggspl vpltervsak ldflmptlsf kdrgavllvg laqrlgarev
      121 ladssgnagt svaaycarag lrctvyvpes tspkkteqia ahgarvvrvp gdreataraa
      181 raaadepgvf yashvfhpyf tqgtktyahe lwdqlggrlp ealvvpvgng tlllgaalav
      241 eelygaglip hrpalhavqa eavsplaraw reglddlggd tpaaptlaeg iaiprpprar
      301 qilaavratg gafhtvpesa iapaqadlak rglyveatgv acwaavrega lgdteavvpl
      361 cgaglktgma pagttgp
//
LOCUS       WP_007821414             415 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Rhizobium sp. CF142].
ACCESSION   WP_007821414
VERSION     WP_007821414.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF142
  ORGANISM  Rhizobium sp. CF142
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 415)
  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 415)
  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
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 415)
  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   5  (residues 1 to 415)
  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   6  (residues 1 to 415)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 415)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 415)
  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 20283677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Rhizobium sp. CF142"
                     /db_xref="taxon:1144314"
     Protein         1..415
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45095
     Region          34..86
                     /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(47..49,58)
                     /site_type="other"
                     /note="non-specific DNA interactions [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            58..64
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            order(59..60,64)
                     /site_type="other"
                     /note="sequence specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238044"
     Site            59..60
                     /site_type="other"
                     /note="putative cAMP binding site [chemical binding]"
                     /db_xref="CDD:238044"
     Region          95..394
                     /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 mssldgpdsm papppilnps gganqirvra ynerlvlslv rlygalskad iarrsglsaq
       61 tvsvimrvle kegllsrgep irgrvgqpsi pmrlnpdavy sfgvkigrrs adlvlmdfvg
      121 rirlqlhriy ayplpdeils fvihgikele gklderersr iaglgiaapf elwnwadevg
      181 apegamevwr dfdlqseiat qvsyqvflqn datsacgael vfgigpsypd fvyffigsfi
      241 gggivlnssi fsgktgtaga igplpvrgkn getlqlleia sifvlenmlr ergidpqplw
      301 ysaddwvdfg epmeawiqdt akalaqaiva aasiidfsaa vidggfpdwv rrrivqatih
      361 eaekldlqgv vmpdiveglv gaqaraigga slpifarylt dqnvlfkeid naera
//
LOCUS       WP_007823717             212 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Rhizobium sp. CF142].
ACCESSION   WP_007823717
VERSION     WP_007823717.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF142
  ORGANISM  Rhizobium sp. CF142
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Rhizobium sp. CF142"
                     /db_xref="taxon:1144314"
     Protein         1..212
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=22265
     Region          10..183
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mtsfheqrdv vlavtgasga alglavldll cglgvrvhlv vsqggkrtll heagadahdg
       61 mlpkayrsyd ngdigatias gsfpvagmiv apcsmktlaa istglstslv araadvqlke
      121 rrrlvlmtre tplhlghlrn mtsvtemgai vmppvpafyn rpqsvqeivd hlarravdll
      181 glpvapqasa wpgeadfdqp ktetgsapkr ra
//
LOCUS       WP_007823928             416 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Rhizobium sp. CF142].
ACCESSION   WP_007823928
VERSION     WP_007823928.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF142
  ORGANISM  Rhizobium sp. CF142
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 416)
  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 11482064
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Rhizobium sp. CF142"
                     /db_xref="taxon:1144314"
     Protein         1..416
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=44517
     Region          1..414
                     /region_name="PRK06132"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:235709"
     Region          214..>271
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 msvrvsvlig llsatalvhp afaadartlq ifvskdkqsl avydgaeiva tskissgkdg
       61 httpsgifsv iekqkyhesn iysnapmpfm qrltwsgial hesnsvpryp ashgcvrmpg
      121 dfakslykmt emgvpviitd selapepidh ptlfrpdrpe papllsdvel rpaigdaktq
      181 vlvamnetta alpmpqfqlq aptadiapis mlitrrtlre nvidiqalln qlgfaagepd
      241 glagpatvqa inafkalrpt efardkglit dtllrevyaa agkgeppngv imvrqdfkpl
      301 feapitiadp glalgthffs lhsvddatgt adwlgvtlen nlsretvkrl gianqessii
      361 sgrptarals rismseetrh ridalispgs tltisdtglg setgegtgfi titres
//
LOCUS       WP_007824629              96 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Rhizobium sp. CF142].
ACCESSION   WP_007824629
VERSION     WP_007824629.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF142
  ORGANISM  Rhizobium sp. CF142
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Rhizobium sp. CF142"
                     /db_xref="taxon:1144314"
     Protein         1..96
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10309
     Region          1..93
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mrpsevlekn rqaireatkr fnaanprvfg svargedrsd sdldilvdal pgttlfdlgg
       61 lleelqdilg vkvdlvtagg lperikhrvl seasai
//
LOCUS       WP_007825909             412 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Rhizobium sp. CF142].
ACCESSION   WP_007825909
VERSION     WP_007825909.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CF142
  ORGANISM  Rhizobium sp. CF142
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 412)
  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 412)
  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
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 412)
  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   5  (residues 1 to 412)
  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   6  (residues 1 to 412)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 412)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 412)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Rhizobium sp. CF142"
                     /db_xref="taxon:1144314"
     Protein         1..412
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44962
     Region          29..>75
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          88..375
                     /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 mnqmngarls pdltganved agehnravvl rcvhrqapis raeiarqtgf tkpaiarivd
       61 rlldegliie arrrhglrgq paieleinpd affaiginid rdhltivavd avgnvrarvh
      121 hekryvrpae fmqltadais hfqrsrlidd ahlagiglam pdwlgeipfl gmpddysewm
      181 efdvraaien ltqhpvfien etnaaalael dyglgaesrs ffyiainacl ggglvldgng
      241 hrgamalsge igwlpiaddr dktapkvdll gemvtmffly kflgehglha svpqdlltld
      301 argkalvskw lkemsahlav avkhigmivd pdaiiiggrl pirmidellr yvhehlsagd
      361 ntlpslhras igedasalga aampmaaalm lasadavqrt rsplkfmdrl nn
//
LOCUS       WP_007828055             407 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Variovorax sp. CF313].
ACCESSION   WP_007828055
VERSION     WP_007828055.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. CF313
  ORGANISM  Variovorax sp. CF313
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 407)
  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 407)
  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
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 407)
  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   5  (residues 1 to 407)
  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   6  (residues 1 to 407)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 407)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Variovorax sp. CF313"
                     /db_xref="taxon:1144315"
     Protein         1..407
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43057
     Region          28..>73
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          91..393
                     /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 mpdadvpart pdllrprgsn qvgmrqfner tvlqalrvhg slpkadlarl tglsaqtigl
       61 itarleedgl ivkqsrvrgr igqpsvplal npdgafaigi kvgrrgaewl lidfaaqvre
      121 rhaisydfpd adellpaiaq hihrlrdglg plaarnvgag laapfqlggw hrtlglskaq
      181 sdlwnqmdla aevrartdvp vsfardtvaa cvaelvggrg hdlksflyif vdtfvggglv
      241 inshlhtgah gnagalaslp mqppgsrgal ppqlvaqasl weleqrlage gldamaaydd
      301 ralqppyaat tqawlesasq alahaivsgt amldltdvvv dgsmsrallq alldqtraal
      361 dgcnweglwq prlhggkaga qacalggaml plhanfapdh dvflkaa
//
LOCUS       WP_007829362             108 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Variovorax sp. CF313].
ACCESSION   WP_007829362
VERSION     WP_007829362.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. CF313
  ORGANISM  Variovorax sp. CF313
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (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   2  (residues 1 to 108)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Variovorax sp. CF313"
                     /db_xref="taxon:1144315"
     Protein         1..108
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11127
     Region          14..75
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mfkkilaata mlfaavsfaa vdvnkgtaad ldgvkgvgps mskrildark egefkdwpdf
       61 mqrvkgvkek kaaklsaegl tvngqgfggt atapkaakte kaakapks
//
LOCUS       WP_007826724             403 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. Tu6071].
ACCESSION   WP_007826724
VERSION     WP_007826724.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. Tu6071
  ORGANISM  Streptomyces sp. Tu6071
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  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 403)
  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
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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   5  (residues 1 to 403)
  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   6  (residues 1 to 403)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 403)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces sp. Tu6071"
                     /db_xref="taxon:355249"
     Protein         1..403
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41787
     Region          30..69
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          91..390
                     /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 mttkrasatk tsirrgtnlp rmgdfnesvv ldairrhkag lsrvelaeat glsaqtvsni
       61 trrlldqgva resgkqstgs gkprtllqvt pgaryaigvh ldpavityvl ldllgtvvar
      121 rseptprgvh teallagmaa svgaliedsg vdqervlglg iaapgpvdpv aglvidppel
      181 pgwgsvplre rleadtgfpa lldkdvvaaa vaerwsgaat dsrnflffyl gtgsgmglvv
      241 ddtvlrgssg nvgevgglga acssralvee aielgalghe ftptdpqdaq rslehlaria
      301 aegepraagi idrwgvrigr gvtaaatlld sdtivfggpl wpllaprllp liepmvaesp
      361 fvkpvhattv tttaigedva avgaaclvld rtlsaqprsl lla
//
LOCUS       WP_007830543             387 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Variovorax sp. CF313].
ACCESSION   WP_007830543
VERSION     WP_007830543.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. CF313
  ORGANISM  Variovorax sp. CF313
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
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
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 387)
  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   5  (residues 1 to 387)
  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   6  (residues 1 to 387)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 387)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 387)
  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 20682457
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Variovorax sp. CF313"
                     /db_xref="taxon:1144315"
     Protein         1..387
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40335
     Region          18..57
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          83..350
                     /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 mttigdqqll krmnrsvllr llraqpglsr arlasesglt kstvsllvre lldegwlsea
       61 gatvadgmgr pstplqinvg vralmgveia vetvrlvcvs lqgevlhadt raltdgspag
      121 acaqvarmaa aahvvlerlg lrlssigvcv pgavddctgv vrfapnfgwr nvsllpalek
      181 afaavglpgv tvqlqndada aalgeyefaa segqdgedpl ifvncdvgvg agvvlndrlf
      241 tgaqgmagei ghtileldgp lcscgrrgca eaffgsrvle regadmqraa affgvllqnl
      301 wvtfnpraiv lggkacadhr gfaqaafesv krhadgagmp ppdlrtaryg alapavgaaa
      361 lalheylrpl qpdakarrar alaraaa
//
LOCUS       WP_007832055             136 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Variovorax sp. CF313].
ACCESSION   WP_007832055
VERSION     WP_007832055.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. CF313
  ORGANISM  Variovorax sp. CF313
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Variovorax sp. CF313"
                     /db_xref="taxon:1144315"
     Protein         1..136
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14378
     Region          8..133
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mnepsharkt ggftlielmi tvaivailaa ialpsyqqyv irskrsaaqa qmmdianrqq
       61 qfllanrsya dnaalaasgy vlpaevssny synitlsttg vpgytltltp tplgsqsgdg
      121 altlnsegvk tppekw
//
LOCUS       WP_007832869             694 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Variovorax sp. CF313].
ACCESSION   WP_007832869
VERSION     WP_007832869.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. CF313
  ORGANISM  Variovorax sp. CF313
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Variovorax sp. CF313"
                     /db_xref="taxon:1144315"
     Protein         1..694
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=71571
     Region          1..694
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mnaisrllkp rsvavigasg datktagrpi sylvkhgfsg eiypvnpkad rigelacyad
       61 vaslpavpdv givllgaera hlavrdlaar gtaaaivlas gytetgeega rrqrqlmdaa
      121 gsmrilgpnt iglvnltdni vlsatgalem ahfpvggvgv vsqsggilgs llsraavrgi
      181 glsklistsn evdleladfi dhlaeddatk vialyvetvr npekfraaal kaaragkpvv
      241 afkigrseag akaavshtga lagadrmyda lfrqvgvira rtfndlldip aalatgrklr
      301 gnrvavltst ggagtlvsdd lglsgfdtpa pdaataealr alqtgdhavl drnpidvtla
      361 glrpdllrga idvllkspsy daltiivgss slampelmag aiqdclptsd kpviayvsph
      421 apeigalltq rgvpafaaae sctaalgaml rasqwkdpge ptaamqpvav gdlpsgslde
      481 aqakqlfsrf gvpcarelvv tepaqaeaaa relggrvvlk ilsaqvthks dvggvavnlt
      541 pdtvgarllq masdveanag srpqrflvqe mvaggtelil gmhrdalgta illgmggvta
      601 elfkdtamrl lpaqgglsrd ealgmaqelk twplldgfrg rpkadveall aaivafshma
      661 aqlgdrlvea einpvfvlpq gqgvraadgv vvla
//
LOCUS       WP_007833142             152 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SPOR domain-containing protein [Phocaeicola].
ACCESSION   WP_007833142
VERSION     WP_007833142.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola
  ORGANISM  Phocaeicola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Phocaeicola"
                     /db_xref="taxon:909656"
     Protein         1..152
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16959
     Region          65..133
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mryifillfl slglsavaqq niveslqrnr agegtvtiyq dpkitgligs iytgnvtgge
       61 qkmlkargyr vqvyagnnsr varneannva tkvkeefpdm pvyayfqppr wlcrvgdfrs
      121 ieeadaamrr lkatgvfkev sivreqinip ld
//
LOCUS       WP_007835027             793 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Variovorax sp. CF313].
ACCESSION   WP_007835027
VERSION     WP_007835027.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. CF313
  ORGANISM  Variovorax sp. CF313
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 793)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (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
REFERENCE   3  (residues 1 to 793)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Variovorax sp. CF313"
                     /db_xref="taxon:1144315"
     Protein         1..793
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86561
     Region          64..115
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          91..793
                     /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 mrplprqhll naalaaafgs vltvwapvas aqasgqaaaq vfevkvpsqa lgaalnefsr
       61 qtgvqvfaag evvagtssha vegkltvdqa lrqmlagtsl eatrtasggl airraadaps
      121 sqgtlpavqv vanaeespig pvsgyaarrs statktdtpl ievpqsisvi greemdargv
      181 qdvmeairyt pgvttntygp dnrgweyill rgfstssngv yrdglaqpaf gptyyltepy
      241 alervevlrg pssmvfgqgd aggivnrvsk qptgerirei elqygsyqrk qlafdlgdri
      301 gntdlsyrvv gvgldsndqd kypdghklnh trsyiapsvr wqpnsttslt vfgeflknnt
      361 aedpyyltqd yvlypvkvgd ysfgqlkqsq saigyrfeta lndtwtlrqn frysqialdr
      421 ravwagslrn dghtltrvar twndpvdlat ldtsvqgklq ygsvqhtvll gvdysdqkgk
      481 qrrfrgaapt ldiwapvygq avamptipmt dvaqstrqtg fyaqdqikfg dnwivtlggr
      541 hdevrqltdn ylarshtrrs dsafsgragi sylfgngwap ymsyttsflp nsgvdannqp
      601 fkpssgkqve vgvkfqpags rtsytaavfd lrktnvvtyd pttsegrqig kqrsrglele
      661 akgelapgln isaaytwldm kvlnsadage igkipplvpk qtasvwldyt mgnglgfggg
      721 vryigkrqnd ehnttyergv tlldaaahye rgpwrfalni snlankqyns icyhgqcyqg
      781 tlrtatltar ykf
//
LOCUS       WP_007836072             346 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Variovorax sp. CF313].
ACCESSION   WP_007836072
VERSION     WP_007836072.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. CF313
  ORGANISM  Variovorax sp. CF313
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 346)
  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 346)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 346)
  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   4  (residues 1 to 346)
  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 346)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Variovorax sp. CF313"
                     /db_xref="taxon:1144315"
     Protein         1..346
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38601
     Region          24..206
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          249..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkhlgrlmrs aslsgyvdlv rslgrdphaf lrtvglkaql lehpemlipg davrelleit
       61 aratrtedfa lrlaaqrkls algpigvvlr eeptprdald tlgrylklvn aslsfrledt
      121 gdmvilredl lpspglpmrq smelavgimf rvltelidpq wrpqqvcfth rppadvsahr
      181 affgrhvkfn qdfnglvcla adlrkpresg dqgaarfare yleaalkdrg estreacrel
      241 ilalmpgggc taqevarhlr vdrrtlhrrl eaegftfssl ldhvrsdlvk rhlrdsdlpl
      301 sevaellgfs gpssfshwfr hhfgcsasqw skqtasavaq gtvraf
//
LOCUS       WP_007836426             296 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Variovorax sp. CF313].
ACCESSION   WP_007836426
VERSION     WP_007836426.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. CF313
  ORGANISM  Variovorax sp. CF313
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Variovorax sp. CF313"
                     /db_xref="taxon:1144315"
     Protein         1..296
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31624
     Region          14..264
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mqaelvldar ngtgespvwh ggqqalywvd ipartlnrwh aseghtqwta nemiaciapr
       61 advpgewiag mesglfslkp qtdgtlaasp lapvahaapa mrfndgrcdr qgrfwagtml
      121 ldmaagarig rlyrygkgsd naaerlgdli vpnglafspd grtmylsdsh pgvqavwafd
      181 ydtdtgtptn rrlfidmkpl pgrpdgaamd tdgcywicgn daglvhrftp dgrldrslev
      241 pvkkpamcaf ggpdldtlfv tsirpggtdl sdqplaggvf alrpgakgla epafgi
//
LOCUS       WP_007836919             154 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Variovorax sp. CF313].
ACCESSION   WP_007836919
VERSION     WP_007836919.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. CF313
  ORGANISM  Variovorax sp. CF313
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Variovorax sp. CF313"
                     /db_xref="taxon:1144315"
     Protein         1..154
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=16310
     Region          9..152
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mnkypeaqth kgrlrsrgft lvelmivtav iailaaiayp sygryvlrak radakqqllq
       61 aaqwterylt angqyppatv alpagldqap ssgtanyaig yaartattyt lqavphgast
      121 adecgtltvn hqgvklaagq tsasnaqvqa cwnr
//
LOCUS       WP_007837843             430 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Variovorax sp.
            CF313].
ACCESSION   WP_007837843
VERSION     WP_007837843.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. CF313
  ORGANISM  Variovorax sp. CF313
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 430)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 430)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Variovorax sp. CF313"
                     /db_xref="taxon:1144315"
     Protein         1..430
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=46594
     Region          2..418
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mnvkileisl gtrrfgklfq yadlcrfvae pelvanppae vlslsmvasd paaqsalwsd
       61 vknplfnaqg gqlpgffqnl lpegvlrshi aqlrgcrend hfellaacgg dlpgavsarp
      121 vsvdrgtlqr litqdqdale msvvelpmpq gisvsgvqpk lglrrqggry vartragast
      181 rviaklpvag rphmpqleml slqmagaagv evchaelapl saiaaehsya lpdepeflav
      241 trfdrdgarr ihfedfaqvl aidpmrkygg syldmalamr afpslgdeav lellrrlavn
      301 dllgnpdahl knfgvlypdg vaprfapayd ivayaalqgv dghalpllpe pavparrtal
      361 ftpasvrafc fstglheplv rrvvadtarl ardrwpamid asalpapwkk rlqqrlqahp
      421 llqamakrgr
//
LOCUS       WP_007839065             710 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Variovorax sp. CF313].
ACCESSION   WP_007839065
VERSION     WP_007839065.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. CF313
  ORGANISM  Variovorax sp. CF313
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Variovorax sp. CF313"
                     /db_xref="taxon:1144315"
     Protein         1..710
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73018
     Region          12..710
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 matvevevgk glealfkprs iaifgasddv tkiggrplqf lqkygyrgai ypvnrkggtv
       61 qslpayanva elpsvpdlav mavppdavle avkdcaargv raavilssgf semgeegsrl
      121 qaaigevara sgmrvvgpnc lgsigvadrs iatfsvales sfptagpvgi vsqsgnlgsy
      181 tmrlavergi gisrllttgn ecdvdiadgi aslatdpats vilccmetcr naaklvrala
      241 mareagkpvv vlkvgvssag seaaashtga lagsdavfdv vlrnagairv psieqllevg
      301 havsvvgtar apkgprvalv tasggfgvlm adaasaqgle lpklsaatqe rivaalpyas
      361 pgnpvdmtaq vssrpellvq vlsavaedas cdavilqsay afqmprlrdv ylaaleqvrr
      421 ahpsrlvllc ckappdtmaq lnemgfptve tidaacatla alvrlgtrge qaevavasrs
      481 aealpaeafa neasakavla qagipvlkev taggrdeala aardigfpvv lkivspdiph
      541 ktevggvvtn vrseaqlrde ydsllarvaq kapqariagv lvaqmaqggt elilgtmkdp
      601 vfgpvvivgl ggiyaevlrd valqvapvte aqamqmlrsl kafalfdgar grpkadvaaa
      661 aravaalsrf avrharsvae idinplvvld hghgafalda llvpetkdkp
//
LOCUS       WP_007840163             138 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Chryseobacterium populi].
ACCESSION   WP_007840163
VERSION     WP_007840163.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium populi
  ORGANISM  Chryseobacterium populi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 138)
  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 138)
  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   3  (residues 1 to 138)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Chryseobacterium populi"
                     /db_xref="taxon:1144316"
     Protein         1..138
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=16357
     Region          42..132
                     /region_name="Endonuclease_DUF559"
                     /note="Putative endonuclease; cd01038"
                     /db_xref="CDD:411708"
     Site            order(42,71,88,95)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:411708"
ORIGIN      
        1 mnetlthing ipihrnfiek lpynphlknl lrdkrkagil sevlfwkqvr sgsfynidfd
       61 rqriignyiv dfyvkklglv ieingwshgk kqiydeerqk ylesltlkvf iitdfdiknn
      121 lavvmkdler fiiehygf
//
LOCUS       WP_007841707             340 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Chryseobacterium
            populi].
ACCESSION   WP_007841707
VERSION     WP_007841707.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium populi
  ORGANISM  Chryseobacterium populi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 340)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Chryseobacterium populi"
                     /db_xref="taxon:1144316"
     Protein         1..340
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37391
     Region          2..340
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mikstirgig fyvpdhvvtn ddlaklmttn dewitertgi kerrhrknrn dseettaylg
       61 fkasekalkq agltaknidy ivfatlssdy yfpgcgvllq dmlgcdtiga ldvrnqcsgf
      121 vyamsvanaf iksgtyknil vvgaevhsfg ldfsdegrgv svifgdgaga illsateden
      181 agdilavnmh segkyadelc tqfpgskfgw sdrmrkepen vtnkevypim ngnfvfkhav
      241 trfpetmqea lnkagktved ldmfiphqan lriaqfvqqk fglpdekihn niqkygntta
      301 asipialsea ielgkvkrgd lvllsafgsg ftwgsvlfey
//
LOCUS       WP_007842624             268 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Chryseobacterium
            populi].
ACCESSION   WP_007842624
VERSION     WP_007842624.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium populi
  ORGANISM  Chryseobacterium populi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 268)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Chryseobacterium populi"
                     /db_xref="taxon:1144316"
     Protein         1..268
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31487
     Region          195..268
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mdfhikyitp diklstyddk lfktetvfey hmlvwfisge tkiiqadrsy tfqagdifli
       61 prnhlatiin ypkdglphka vvmhltterl kkfysnidte pknlrkktgi hifnnhplle
      121 scmaslipyf dmkepfpehi aslkimeais iireidkntd avladfeepg kidlisfmek
      181 nymfnmpler fgyltgrsls tfnrdfrkaf qrtpqrwltk krlelayyql teknkkptdv
      241 fmevgfedls hfsyafkkqy gyapsgvr
//
LOCUS       WP_007843047              98 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Chryseobacterium populi].
ACCESSION   WP_007843047
VERSION     WP_007843047.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium populi
  ORGANISM  Chryseobacterium populi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Chryseobacterium populi"
                     /db_xref="taxon:1144316"
     Protein         1..98
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10913
     Region          1..94
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(5..6,24..25,33,36,38..39,41,44..45,47,53,58)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(24,53..54,56,75)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mdeifkqqvy eitrlipkgr vstygaiaka vgypnhsrhv gkamsgcpkd vpahrvvsss
       61 gtlsvkeflp kleaegviie nfrirnfkkl fwdpltel
//
LOCUS       WP_007844544             411 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Chryseobacterium populi].
ACCESSION   WP_007844544
VERSION     WP_007844544.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium populi
  ORGANISM  Chryseobacterium populi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Chryseobacterium populi"
                     /db_xref="taxon:1144316"
     Protein         1..411
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46311
     Region          1..286
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          283..387
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkflhtadwh igqlfheydr syehqqflnw lvetlvteki evllisgdif dssnpsaasv
       61 rmfyrflnqa ttvlpglqii itagnhdsaa rleapkplle ssnvhiiglv ekdaegniny
      121 ekllvkindt lgdikawcla ipflrmgdyp aiadcanpyt egvavlyqea fnyaeqhkse
      181 gqpiiamghl haqqaevtdl dkterlimgg vegisamafh qdikyvalgh ihkaqkiggk
      241 ehirysgspl pmsfseihyk hqvivfdleq eisnlktvei plfvplqrtp lqyrplhevi
      301 slleqlpsad snpenlpylq vrvllegpep alrhkveial agksvrlaki dvqypsstke
      361 tpvlirpekl nelqpldvfg kvyqsrynse vpdhllqlfq qvvqevnhka e
//
LOCUS       WP_007845292             605 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Phocaeicola dorei].
ACCESSION   WP_007845292
VERSION     WP_007845292.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola dorei
  ORGANISM  Phocaeicola dorei
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 605)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Phocaeicola dorei"
                     /db_xref="taxon:357276"
     Protein         1..605
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=70428
     Region          25..314
                     /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          213..241
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          247..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(248,251..252,255..256,258,287,290..291,294..295,
                     297..298,321,324..325,334..335,338)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          285..315
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          320..350
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          <490..599
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtgmrmlklw vvvmllgllp vvseaqeein nainvqleyl kkypkdkeal rkvsflylnk
       61 adydqaifyg rqlfemgyne rdyngaviys hiclgqahmm kgnvkeaysh lgqarliges
      121 nkndsalcsv ynglglyasn vqkdyyrslt yffkgveaar rchydrlysi llsniagiyy
      181 lkndstglky alecyelghe rkdpyliysg stntaymyyl ksdyntalky iqeaeftmvq
      241 ndfydqsnvy nlygyilhkl nkddealgff rkaldlkeqg nissvmnsyl gyaeilmehh
      301 qydravwmlk agielsyqqa naiyrsdllq alsrcyeedg mlvealkyhk lyqletdsly
      361 naekeravge irakydmerq eneikqnrle llekenkmql liagficifi aasllyylyy
      421 rknklyltiv kqnqdairre qqlqnkideq fveigrqsal lqeyltestk tslpqsekya
      481 sssltdekkq dlflrletll reekvftdnl ltkekvaeml gtnrtylsqi ineqtkqtft
      541 qfvngfrtke avrllsdpdn qtplkaisae lgfnsmttfy sqfqaatgmt paqyrnkvqe
      601 lhknr
//
LOCUS       WP_007846219             352 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Chryseobacterium
            populi].
ACCESSION   WP_007846219
VERSION     WP_007846219.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium populi
  ORGANISM  Chryseobacterium populi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 352)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Chryseobacterium populi"
                     /db_xref="taxon:1144316"
     Protein         1..352
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38648
     Region          1..352
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mtskiigvgn yippetitnl ffdkhnfink sgesltesna iiasklkeit gieerryasn
       61 dqvtsdlgli aaqaaiddag idpetldyii fahnfgdvrf gtvqsdtvps lasrvkhllk
      121 iknnfcvayd vlfgcpgwie gviqanafik sgiagrclvi gaetlsrvvd ihdrdsmiya
      181 dgagaailev sndesgiqsh vsasftlkek dylffgksyn nekcpdtkyi kmegrkiyef
      241 alsnvpdamk kcldesgyei nqldkiiihq anekmdeaiv krfyqlydtp mpenimpmvi
      301 nklgnssvat ipslltmiln gelpshqidk gdvvlfasvg agmnvnafvy kf
//
LOCUS       WP_007846357             149 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Chryseobacterium populi].
ACCESSION   WP_007846357
VERSION     WP_007846357.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium populi
  ORGANISM  Chryseobacterium populi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 149)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Chryseobacterium populi"
                     /db_xref="taxon:1144316"
     Protein         1..149
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16770
     Region          1..149
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mselkkrlss ilespkhnte eklqkvchll dqeisyfnwt gfyfkngdke elilgpyvga
       61 ptdhtiipyg kgicgqvavs netfvvpdvh qesnylscsi dtkaeivvpi fkdgknvgqi
      121 didshkidpf ttedrellew lcnevskil
//
LOCUS       WP_007848981             419 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Cronobacter
            sakazakii].
ACCESSION   WP_007848981
VERSION     WP_007848981.1
KEYWORDS    RefSeq.
SOURCE      Cronobacter sakazakii
  ORGANISM  Cronobacter sakazakii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Cronobacter.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 419)
  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 419)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Cronobacter sakazakii"
                     /db_xref="taxon:28141"
     Protein         1..419
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47591
     Region          1..405
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 msgvhlslra arhlhlaaqg llkkpvrrar padilaaitr msllqidtin ivarspylvl
       61 fsrlgnypgr wldealarge lmeywaheac flprsdfplf rhrmlspekm gwkyraawme
      121 ehaqeigelm afierngpvr sadfehprkg asgwwewkph kkhleglfta gqvmvverrn
      181 fqrvydlttr vlpdwddslh lidkaqaeaq mlansarslg ifrsawlady yrlrhvaagp
      241 llqawqdegf vvpvdvetlg pmwlhhellp lleravagkl tathsavlsp fdpvvwdrrr
      301 aeeffnfsyr lecytpapkr kygyfvlpll hkgalvgrmd akmhrqqgsl evialygeeg
      361 vsftagiiag lrqaigdfaa wqgatrvvfr qlpgplahaw gegweidpap ethvisskd
//
LOCUS       WP_007849115             144 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acidovorax sp. CF316].
ACCESSION   WP_007849115
VERSION     WP_007849115.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. CF316
  ORGANISM  Acidovorax sp. CF316
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Acidovorax sp. CF316"
                     /db_xref="taxon:1144317"
     Protein         1..144
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15118
     Region          1..142
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mrhksnrgft lielmtvvai vgvltaialp syneyirrgh radaragllq aaqymeraat
       61 angvyptsva aftlptqlsw tgdtskrygi avagtastft ltatrktgtp qatdkcgelt
      121 ltqagvrgas plsagatipe cwnk
//
LOCUS       WP_007849760             706 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Acidovorax sp. CF316].
ACCESSION   WP_007849760
VERSION     WP_007849760.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. CF316
  ORGANISM  Acidovorax sp. CF316
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Acidovorax sp. CF316"
                     /db_xref="taxon:1144317"
     Protein         1..706
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=76381
     Region          31..706
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mttrhtkapa ltpkltrcaa avalawlgap lalhaqdasp agdsaspale tiqitgswlg
       61 tglqnsvknf agartvvdke kidgtgaani gevlrripgv qatensgtag saislnigvr
      121 gltgrysprs tilldgvpla vapygqpqls fapvslnnie sidvvrggga vrygpqnvgg
      181 iinftsraip skpgltgdvt vrhnhysegg qdntqystfl gsqldnglgl allysgmtgs
      241 swrqgsdekv ndlafkfrye ltgssevygk vsyydvnsrt pggltvaqfn anpfqntrpt
      301 dywngerkgl dlgyintisd nqefevrayy ndstrkstli natstqlahq prdyevlgie
      361 prytqrvqlg atthdvtagy rflrergndr aynqtiatga nsvttrfdna tdahavyidd
      421 riafgawrvt pgvrfehiet nredrastqr fdttnnkalp slnvaylvnp altlfanygt
      481 sfgpvqniql nsqtatnplk pelaktaevg arwqtpqira eltafkirfd nqilqvpgit
      541 patfqnigat shegieaaid ysfdkasala glnvyanysy tkaiqksgtt agldvpfysr
      601 ntdtlgaryq lgdwafnlas thqsaqyada antfaepada rlgripgfrl wniqadwkvp
      661 gykgssiavg mnnladkryy trnvdgnpgr mvgaprmlyv qgrlaf
//
LOCUS       WP_007849466             421 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Acidovorax sp.
            CF316].
ACCESSION   WP_007849466
VERSION     WP_007849466.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. CF316
  ORGANISM  Acidovorax sp. CF316
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 421)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 421)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 421)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Acidovorax sp. CF316"
                     /db_xref="taxon:1144317"
     Protein         1..421
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=46423
     Region          2..409
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 maseifvway lpgdveptlc grfehgtsst ghmgvfayyk sylqnpsaia vdpialplra
       61 lqfsttlskg vfgalldamp eswgrhvidt vqwrqdfpar ymlntagdai gnlafsqsst
      121 eipvrrlpig vediglaqav lydldkhpel vfpemvewvw antamggarp kltvekdgrl
      181 wlakfpsrnd danlpmakle aamldlarrc ginsaisqvv egdgrhgdvl lverfdrgpv
      241 dgrgmarrda flsartlfec tgfrsdysgs yvrlaseler yscqsesdra elfrrmvfna
      301 lisntddhdr nhglvaddmp gtyrlspayd llpqwrstrq rgqamavgsn gamatkenll
      361 seceafgltr rnaeevhgqv aervaanwre clvaqgvadk gialvegcfs vvpdlmpgrk
      421 h
//
LOCUS       WP_007850618             377 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acidovorax sp. CF316].
ACCESSION   WP_007850618
VERSION     WP_007850618.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. CF316
  ORGANISM  Acidovorax sp. CF316
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 377)
  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 377)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 377)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 377)
  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   5  (residues 1 to 377)
  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   6  (residues 1 to 377)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Acidovorax sp. CF316"
                     /db_xref="taxon:1144317"
     Protein         1..377
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41149
     Region          55..242
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          157..372
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mysdiaegtr radpaqaama avqlpwsqas saaagekrfa psklsvlvev aqelgwpvda
       61 vlagtgldaa airdpftlts psqflhaarn avrlprgyea garvgarlha scygmygyal
      121 lcsesmrqmf dtgvrfhqla ngmlqikwve qqglatwllp shdtllvrdv dealyrllid
      181 lqfavhvtlf kdtmgpwclp qgasftcpep phaallaqll acplafgqaq ntlsypaawl
      241 drapqlanpi taahvssqcl rlledfrwha gitrrvyqel trtpgqfpdi evvaealsmt
      301 srtlrrklea egtsftdlla svrkalaidy lsttrlgadd iaaaigfsda vsfrhafkrw
      361 tgkspseyrr eagflqg
//
LOCUS       WP_007852605             144 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Acidovorax sp. CF316].
ACCESSION   WP_007852605
VERSION     WP_007852605.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. CF316
  ORGANISM  Acidovorax sp. CF316
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 144)
  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   2  (residues 1 to 144)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Acidovorax sp. CF316"
                     /db_xref="taxon:1144317"
     Protein         1..144
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14791
     Region          11..76
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 msifkkflli aallfagtvs aavdvnkasa aeldgikgig pamsekiine rknsefkdwn
       61 dfigrvggvg ektaakfsae gltvngkrfs aaaqakadkk kkeaeakask taakgedkpa
      121 rqkkdkaaep aaaapqaaas gakq
//
LOCUS       WP_007851693             359 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Phocaeicola dorei].
ACCESSION   WP_007851693
VERSION     WP_007851693.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola dorei
  ORGANISM  Phocaeicola dorei
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 359)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Phocaeicola dorei"
                     /db_xref="taxon:357276"
     Protein         1..359
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39825
     Region          10..343
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mvtsfnnkti savysvlpsq evdfldearn ysfseaqmlk lkkvmgfgtr rvakegetva
       61 dyaiygiqqm lndgvfkeee igaiivttts pdhfippvsn iiqgkfnfde dtvcidisqg
      121 ccgytvglty sfmtlnsign kkvllvagdm lsfkvstrdr asrpivgdgv sisvventty
      181 dnkvycslkn dgkdafavyi paggarmpit sentveepde fgnwrgkqhl vmqgdlvfni
      241 iinmtpvmie elldkangki edidyfichq sssftlkkla qrlgvsqerl prdivpkygn
      301 sssasipvtl cehydemfad kdkqmimfas fgtgmslgav ymevprfkdc kfidyphsi
//
LOCUS       WP_007853405             360 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Acidovorax sp. CF316].
ACCESSION   WP_007853405
VERSION     WP_007853405.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. CF316
  ORGANISM  Acidovorax sp. CF316
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 360)
  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 360)
  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 360)
  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 360)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Acidovorax sp. CF316"
                     /db_xref="taxon:1144317"
     Protein         1..360
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39844
     Region          1..354
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mhrrslikht glagvlasgv apavhaqatl rwriassfpr tsdnifggaq vfakavrtls
       61 ngkfeisvhp ggelmppfdv vdgvqsgtve mchavpyyfy sknpafalgc avpfgfnarq
      121 msawmlhgng rrlmnefyag fnmvsfacgn tgtqmggwfl revktpadfk glkirvgggl
      181 vaevmqrlga ipqslpggei yqalqkgsid aaewigpydd qklgfnkvap fyyypgwweg
      241 gpevdlfvnk kaydaltpdy rfiieaaasy ahadmlaryd alnpnalkql vaaktkvlpy
      301 sqvildaafr asmeafahnd arspewkkiy admrnfqrdq ilwfrfaear ydtfmsaqki
//
LOCUS       WP_007853446             570 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Acidovorax sp. CF316].
ACCESSION   WP_007853446
VERSION     WP_007853446.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. CF316
  ORGANISM  Acidovorax sp. CF316
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 570)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 570)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 570)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Acidovorax sp. CF316"
                     /db_xref="taxon:1144317"
     Protein         1..570
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=61510
     Region          293..520
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mfsighdatq vfavgfppll hsllfwifas lvvhvcqrlv ehtafaidps srrisashaa
       61 lcigcvvwal dvvgmlmyae laghmlglvp altglvimal sarltvptls tstskarill
      121 agtglslgml aahftisedy vssyarvngl avvlalatai giaaytsirh raakmkaltr
      181 iyipqkwqdk llagaailvl hwllvntfpl ewpdsaaptd gvallvivll fgmaiateql
      241 snmrfdqarq qllrrglslm rtssyevqap egdiqlslia dqlpqlllpe qlvlhfqpia
      301 dldsgevqfe allrvrsell gpihpeafll vcelqgktpl vdrliltnam awacqwrsag
      361 maaakfsvnv apatlleedf ahwlqaelar ralpgsalkl eltehalias gprmlesirr
      421 lqaigvgvlm ddfgagyssl gmladlpiag ikcdrlfmrq laqdprrqsl lrhvgalase
      481 fglsvvvegv etpaelqtla acglptiqgy vfcrpmpaad vpcwnqaqwp qhlatlraqa
      541 gttdspespe phaspaaaaa wmqqpqgarr
//
LOCUS       WP_007854783             199 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease P protein component [Acidovorax sp. CF316].
ACCESSION   WP_007854783
VERSION     WP_007854783.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. CF316
  ORGANISM  Acidovorax sp. CF316
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Reiter,N.J., Osterman,A., Torres-Larios,A., Swinger,K.K., Pan,T.
            and Mondragon,A.
  TITLE     Structure of a bacterial ribonuclease P holoenzyme in complex with
            tRNA
  JOURNAL   Nature 468 (7325), 784-789 (2010)
   PUBMED   21076397
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Harris,M.E. and Christian,E.L.
  TITLE     Recent insights into the structure and function of the
            ribonucleoprotein enzyme ribonuclease P
  JOURNAL   Curr Opin Struct Biol 13 (3), 325-333 (2003)
   PUBMED   12831883
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Pace,N.R. and Smith,D.
  TITLE     Ribonuclease P: function and variation
  JOURNAL   J Biol Chem 265 (7), 3587-3590 (1990)
   PUBMED   1689306
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Acidovorax sp. CF316"
                     /db_xref="taxon:1144317"
     Protein         1..199
                     /product="ribonuclease P protein component"
                     /EC_number="3.1.26.5"
                     /GO_component="GO:0030677 - ribonuclease P complex
                     [Evidence IEA]"
                     /GO_function="GO:0000049 - tRNA binding [Evidence IEA]"
                     /GO_function="GO:0004526 - ribonuclease P activity
                     [Evidence IEA]"
                     /GO_function="GO:0042781 - 3'-tRNA processing
                     endoribonuclease activity [Evidence IEA]"
                     /GO_process="GO:0001682 - tRNA 5'-leader removal [Evidence
                     IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
                     /calculated_mol_wt=20328
     Region          4..155
                     /region_name="RnpA"
                     /note="RNase P protein component [Translation, ribosomal
                     structure and biogenesis]; COG0594"
                     /db_xref="CDD:440359"
ORIGIN      
        1 mqrlktrpqf qaamaggtvs rtahfalhrl vlgadgtatt ggavvvapge patataaqpa
       61 atvsspgpgt spqalfgvsd dvwlgamvpk rwarravtrn tikrqiytvg atfearlpqa
      121 ahvvrlrstf drkqfisats dqlkaavrae llqlfgyaak rsgqapgagg eagkgggkgq
      181 ggsrsdksps aprvsavap
//
LOCUS       WP_007855124             374 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Acidovorax sp. CF316].
ACCESSION   WP_007855124
VERSION     WP_007855124.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. CF316
  ORGANISM  Acidovorax sp. CF316
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Acidovorax sp. CF316"
                     /db_xref="taxon:1144317"
     Protein         1..374
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=39321
     Region          15..371
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mtqplvpvll vlnvgsssik fqvferesls vlmagkvtgi gtsaqlsarl agaeapvrta
       61 lpaadhdsam aavialidqh ddgwrlaavv hrvvhggaaf hapvvvtpei laqlgalspl
      121 aplhqphnla giaasqrlas haldiacfdt afharmdplf qafalpqalr dqgvrrygfh
      181 glsyewlahe iartrpdlrg arvvaahlgn gaslcamhag rsvdttmgmt aldglpmgtr
      241 sgaidagavi ylqrelgmda dqvehllyqe sglkglsgis sdmqallasa epqaafavdy
      301 falkvaqyta mlavslsgld alvftggige naepvraavl arlqmlgrfd tlvieaneek
      361 mmalhakqll qaqa
//
LOCUS       WP_007856366             400 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Phocaeicola dorei].
ACCESSION   WP_007856366
VERSION     WP_007856366.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola dorei
  ORGANISM  Phocaeicola dorei
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Phocaeicola dorei"
                     /db_xref="taxon:357276"
     Protein         1..400
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44788
     Region          1..265
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          287..378
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkilhtadwh lgqtfyeydr reehfhflew lkqqikqhei dvlliagdvf dspnpsaesq
       61 rvyyrflrev tsenpslqiv iiagnhdsaa rleapnplle dmniivrgtv rrnaegdidl
      121 qhlivplyte gkvtayclav pylrqgdyps aetyskgvqq lyeqlfnevk ekgkpvlamg
      181 hlqatgseis eddrsertvi gglecvspda fdeaitytal ghlhrsqrvs rrdnvrysgt
      241 pmpmsfaern ntsgvvmiti daegtdinkl afeplaglvs ippqarplee vlqaigelpd
      301 gdatlrspyl eikilmtepe psykykieea lkgkavrlar iaamlpqkka sgisatsyee
      361 lqtirpldma ldvfkrkygg tempdtmkll lesvikeagv
//
LOCUS       WP_007857690             833 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Acidovorax sp. CF316].
ACCESSION   WP_007857690
VERSION     WP_007857690.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. CF316
  ORGANISM  Acidovorax sp. CF316
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 833)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 833)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 833)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..833
                     /organism="Acidovorax sp. CF316"
                     /db_xref="taxon:1144317"
     Protein         1..833
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89610
     Region          80..131
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          107..833
                     /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 mptaprhpaa rptacptlft lrptavlaat lasallasva lpapaqaqqq aaqanrstsy
       61 gipagplepa ltafakasgv llaytpdlvl grsspglqgs htpaqalaal lvgtglqavv
      121 adngtytlrr apiptpspgt agaaapagsv tlsevrvtae aprsdatteg tgsytargps
      181 gtatglalsl retpqsvsvm trqrmddfql etltdvmeqt pgistyrqgn atdfqargss
      241 vnlqtdgvrq ltsgwyyfts tmfalddmae idrvevlkgs sglvngygsa gatvnmvrkr
      301 ptaefqahvg asagswntlr sdvdvsgpln asgslrgriv asasdadsfr dheksnsqml
      361 fgaleadigp qttvnggftl rrrelrgmgs tqpiqrttst geavawlprs fnpgapwagy
      421 eqeslnvfgs vehrfaadws aklqfshqsv qmddmllgyl ydrnsiatap yqdidnrnwt
      481 vnldvkgpie lfgrkhellm gagtaryrge mqtsnsvrvp ltslglayad ggaqiptpdw
      541 srytyganlf srkqhyayaa grfhladplk litgvrvtdy aqrdttpfww nydlkehgvv
      601 tpyaglvfdv qpnvslygst tnifeaqsgq deqgralppe kgvtyevgak geffdkrlna
      661 sishfwmktd ntaeetgnlt psgdmayrav tgatrrgwev elsgeiakgw qaqgsyvtqs
      721 ssltsarqhp khqfklgtty rlggsalqgl tvgaatrwqs etstrndaaa lsqksywlvd
      781 lmaryqvnrh lsvganinnl fdkkylsgvt nfgslhytwg aprsfnlnmr ytf
//
LOCUS       WP_007858628             662 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter permease [Clostridia].
ACCESSION   WP_007858628
VERSION     WP_007858628.1
KEYWORDS    RefSeq.
SOURCE      Clostridia
  ORGANISM  Clostridia
            Bacteria; Bacillati; Bacillota.
REFERENCE   1  (residues 1 to 662)
  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 662)
  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 662)
  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 662)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..662
                     /organism="Clostridia"
                     /db_xref="taxon:186801"
     Protein         1..662
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=70579
     Region          47..660
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 madagnktlg qdtvslssve tvdadtqqel ldkydrdsav ekeskdwryk vsdimggilc
       61 lyvyitcavg apealmhrai fmcfcltmif llyalrkqdt grlprwydfi miatvlvvcg
      121 yvisnhrsit tgsgiaskle iflcillvlt vmeairrsgg tsiviiiaif layayfgkya
      181 pgalkhsgls ikriasqlll tseglfgsnv gtvagvlslf lifatfmekt gtgqfindfa
      241 lsiagksagg pakvsvvtsa lfgtisgnav snvvttgaft iplmkktgye pefagaveav
      301 sstagqlmpp imgasafima ditgiayski claaivpvll yytgcfamvh lracklglrg
      361 lakedcpkll lvlkedgylf lpfifvvvml cvgytvtwvg vraiplcvli aackkktrlg
      421 lkdiwqclql sgkrlvsvaa mccginmita vcnltgitqt lsnvilklag gnftiscili
      481 avicivmgmg lptisvymll stvaapalis gfnvpvlaah mfvfyfglla nvtppvaipa
      541 yaaaglanad pgktgwqafk lalggflvpm ifinspdllf cdglvtiwvi ekivtavigv
      601 mllstavegw mltkmqrwqr avvavaailm vipttltdvi gvtvmvvtgl sqnrllirqk
      661 qg
//
LOCUS       WP_007859013             418 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Clostridia].
ACCESSION   WP_007859013
VERSION     WP_007859013.1
KEYWORDS    RefSeq.
SOURCE      Clostridia
  ORGANISM  Clostridia
            Bacteria; Bacillati; Bacillota.
REFERENCE   1  (residues 1 to 418)
  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 418)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 418)
  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   4  (residues 1 to 418)
  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 418)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Clostridia"
                     /db_xref="taxon:186801"
     Protein         1..418
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=48162
     Region          <208..302
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          333..411
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 makivpmqsl ycsmqdenki csfdievlte pttplihpms rfwlinsgeg tlmlnnrpyh
       61 lkpgtvvsvl pwqisdivev aapiqffvma yyfdnineii ktfynpssdp lsimqslsrq
      121 pvlylegdal esmqklflqi keeigmestm dsgrdshass srdlgnlyit nklieiiicf
      181 lrakretgap aspqtiepse ifqylyshln ekitlamlsk ifymsessis ayitkttgls
      241 ffdllgemri gktinyllyt dftleelsei lgfvdsahis kvfsarvgmk andfrstyqn
      301 ignmcrikdr kdfysvvsyi yrhysedlhp ktvaeqfnms prelnrilly qvemnftdyl
      361 nfirvnrase lllkttksil eialetgynn ektlnrnflk frsmtpgwfr qtielqen
//
LOCUS       WP_007859672             281 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Acidovorax sp. CF316].
ACCESSION   WP_007859672
VERSION     WP_007859672.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. CF316
  ORGANISM  Acidovorax sp. CF316
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Acidovorax sp. CF316"
                     /db_xref="taxon:1144317"
     Protein         1..281
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31158
     Region          <74..120
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          178..261
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mphaglsacv rgtivrstlg halsdaqrin rfpatplcsl swwftgrsec lvpgragsmp
       61 dlhsprepfa grwvlagpqt rpstswcaep thammvmfmp dalhlltgla pedltdrtvd
      121 aatllprdwl amceavqhqa ddasrmdcle rfllprwqac rpgpasatqr ygdwathlaq
      181 raahsapgrs lrqlerrikr waglplrelr gfgkaeqaff dtlaadaaes pvrwaevaag
      241 agfsdqshlc rvtrritgya pqalydgiqr deafwvyriw v
//
LOCUS       WP_007860214             258 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acidovorax sp. CF316].
ACCESSION   WP_007860214
VERSION     WP_007860214.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. CF316
  ORGANISM  Acidovorax sp. CF316
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 258)
  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 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
REFERENCE   3  (residues 1 to 258)
  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   4  (residues 1 to 258)
  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 258)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Acidovorax sp. CF316"
                     /db_xref="taxon:1144317"
     Protein         1..258
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27555
     Region          <51..223
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          155..223
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mavdspaelq gsqfpamvgs mlvvrlegev lrdgtvlpaa awisastvat ayvhqgrvra
       61 vglmlrpeav psllaagrgv vnavrpmatm aaaswalaeq airaapddeg rigalwqfvr
      121 qerasqarce erlvqarall ehagasaqgt apfsgvgprq ferrfvaewg mtpkqfqvia
      181 rfsatlqham avptepgahl aadqgyydqs hmardmrrla gqplqglvqe aarsspsahw
      241 plqvgaqahq aadsprrr
//
LOCUS       WP_007860808             379 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Acidovorax sp. CF316].
ACCESSION   WP_007860808
VERSION     WP_007860808.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. CF316
  ORGANISM  Acidovorax sp. CF316
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 379)
  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 379)
  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   3  (residues 1 to 379)
  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   4  (residues 1 to 379)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 379)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 379)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 379)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Acidovorax sp. CF316"
                     /db_xref="taxon:1144317"
     Protein         1..379
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39177
     Region          27..367
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(103..105,126..127,176,228,252)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mpysqhwmig atlallgaga caqdvvrigh vgptsgpiah lgkdnelgar maidelnakg
       61 vviggkkvrl elqgeddagd prqgtaaaqk lvdakvhavv ghlnsgttip askiysdagi
      121 aqispsatnp kytrqgyktt frvvaddvhl ggtlgkyavn vlkgksiavi ddrtaygqgv
      181 aaefekgaks aggaivghef ttdkaadfma iltslkakkp dviffggmds vagpmlrqmk
      241 qlgiqarfvg gdgvctaelp klaagdmadg qvvcaeaggv egaqkkgmdd frarfkattr
      301 sevqvyapys ydavgvivaa mvkagssepa kylpvlaqtk gyqgvtgsis fdakgdlqgg
      361 altlytykag qreaigvvr
//
LOCUS       WP_007860861             186 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Clostridia].
ACCESSION   WP_007860861
VERSION     WP_007860861.1
KEYWORDS    RefSeq.
SOURCE      Clostridia
  ORGANISM  Clostridia
            Bacteria; Bacillati; Bacillota.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Clostridia"
                     /db_xref="taxon:186801"
     Protein         1..186
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20178
     Region          4..186
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 maeklvigis gasgapiaia llkelrrsgi gthlvisrgg eltidqetgy gleevkrlag
       61 tvydnqdlga slasgsfktl gmavvpcsmk tlagihsgys dslllraadv tikerrrlvl
      121 vtrecplspi hlrnmyelsq mgavilppvm syyqrpetie emtvhvvgki mdqfglecqs
      181 frrweg
//
LOCUS       WP_007860883             416 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Enterocloster citroniae].
ACCESSION   WP_007860883
VERSION     WP_007860883.1
KEYWORDS    RefSeq.
SOURCE      Enterocloster citroniae
  ORGANISM  Enterocloster citroniae
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Enterocloster.
REFERENCE   1  (residues 1 to 416)
  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 416)
  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
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 416)
  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   5  (residues 1 to 416)
  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   6  (residues 1 to 416)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 416)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 416)
  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 20170230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Enterocloster citroniae"
                     /db_xref="taxon:358743"
     Protein         1..416
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45904
     Region          <17..>57
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          76..394
                     /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 mqkgdnnlin ftnkvnvlnl lwsepsiyra eiarctslsi ptvmkiiddl sarglvkevg
       61 kgvssggkpp vmlefnksay yvigvdines wtevvlvnll lgieekriqd iritdtvdsv
      121 iqrvikeiht ilehnsqkad rilgigigip glidpkrgyi syspemnwrd vnmkelfckn
      181 fdgeivieer tramasaemr igraqnvknf lyvnnssgig saivmngkly ygnskssgrl
      241 ghmvvekdgl pcncgnhgcl elyasgnaia riarqrvken hnsliydlvf gdldkvdvyi
      301 vfeaarngdr taldvlrdaa eylamavssv inlmdpqlii fegkvcrigd ifmgmfeqal
      361 neryakyies eieivsgkgs snmasigaat filerflatg gelgrtlelv engmge
//
LOCUS       WP_007861010             467 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Acidovorax sp. CF316].
ACCESSION   WP_007861010
VERSION     WP_007861010.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. CF316
  ORGANISM  Acidovorax sp. CF316
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 467)
  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 467)
  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 467)
  AUTHORS   ter Beek,J., 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 467)
  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 467)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Acidovorax sp. CF316"
                     /db_xref="taxon:1144317"
     Protein         1..467
                     /product="CmpA/NrtA family 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=51550
     Region          107..346
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mseffspfda drplmlkcsc grdhtaadhh aevsadaaaa tlrqrslsse feaysnefie
       61 atlvkalfpq davrrrfika vgkgtamaai asvlpvasmq amaqekgale ktnlkigfip
      121 itcatplima hplgfyskqg lnvevtktag walirdkmin keydathfls pmplaismgl
      181 gsnatpmnva tiqnvngqai tlslkhkdnr dpknwkgfkf aipfeysmhn fllryylaea
      241 glnpdtdvql rvvppaemva nlragnidgf lgpdpfnqra vfeevgfihl ltkelwnghp
      301 ccafgtstef iqknpntfaa lyravltsaa mardpanrel iakviapqay lnqpeavltq
      361 vltgkfadgl gkiqnvpdra dfdpmpwqsm avwmltqmqr wgyvkgdvdy kqiaekvfli
      421 tdakkqmkal dqkvpegayp kfkimgrefd aakaaeyaks fpirkva
//
LOCUS       WP_007862581             369 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Polaromonas sp. CF318].
ACCESSION   WP_007862581
VERSION     WP_007862581.1
KEYWORDS    RefSeq.
SOURCE      Polaromonas sp. CF318
  ORGANISM  Polaromonas sp. CF318
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Polaromonas.
REFERENCE   1  (residues 1 to 369)
  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 369)
  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 369)
  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 369)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Polaromonas sp. CF318"
                     /db_xref="taxon:1144318"
     Protein         1..369
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40338
     Region          8..362
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mtesksprrr gllkgaaiaa galsapmvam aqttsfrfqs twpakdifhe yandfakkvn
       61 dmaggrlkie vlpsgavvpa fqlleavnkg tldgghgvva yhygknnala lwgsgpafgm
      121 dpnmvlswhn ygggkallee iykaigmdvv sylygpmptq plgwfkkpia kvadmkglkf
      181 rtvglsvdif tamgtsvnpl pgseivpald rglidaaefn nassdrvlgf pdvvkncmlq
      241 sfhqsgeqfe ilfnkskyna lpaelkaiid ygvqaasadm swkaidrnst dyaemkkqgi
      301 kfyktpdavl kaqleawdki iedkaqanpl fkkvidsqka yaartipwqn dymvdfkmay
      361 nhsfakkka
//
LOCUS       WP_007864535             511 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Polaromonas sp. CF318].
ACCESSION   WP_007864535
VERSION     WP_007864535.1
KEYWORDS    RefSeq.
SOURCE      Polaromonas sp. CF318
  ORGANISM  Polaromonas sp. CF318
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Polaromonas.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Polaromonas sp. CF318"
                     /db_xref="taxon:1144318"
     Protein         1..511
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=53816
     Region          5..511
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mttptpfirl hpaddvliar aqlvggtqve nitvrglipa ghkiatrala agepvrrynq
       61 iigfaskpia pgehvhthnl dmgpdkgdfa rdyafgadvk papakreatf kgirrpdgrv
      121 atrnyigils svncsataar aiadhfsrqn npsalkdfpn vdgvvalthg tgcgmdsdgl
      181 glqilqrtlt gyathpnfag vlvvglgces nqinawlahg slregetlrv fsiqdtggta
      241 ktvakgiami kemlpqanav krepcsaahi tiglqcggsd gysgisanpa lgaavdllva
      301 hggtailset peiygaehll trravrpeia eklisrikww ehyteinege mnnnpspgnk
      361 agglttilek slgavakggt snleavyeya epvgahgfvy mdtpgydpvs atgqvaggan
      421 iicfttgrgs aygcapspsl klatnsalwq rqeedmdinc geiidggvsv qemgqrifem
      481 vlatasgeps ksekhgygqn efvpwqvgav m
//
LOCUS       WP_007864576             519 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Polaromonas sp. CF318].
ACCESSION   WP_007864576
VERSION     WP_007864576.1
KEYWORDS    RefSeq.
SOURCE      Polaromonas sp. CF318
  ORGANISM  Polaromonas sp. CF318
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Polaromonas.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Polaromonas sp. CF318"
                     /db_xref="taxon:1144318"
     Protein         1..519
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54890
     Region          14..518
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mtatttasvp gspaasplir lhandnvlva ktalslgqel peagararaq vpaghkvaar
       61 riargervlk ydtvigvaar dieagdyvhs hnmalvdfer dpafgqdvrp vdyvpqgera
      121 sfmgfvrpdg rvgtrnfigi lssvncsatv ikniaahftp erlaafphvd gvaafaqtsg
      181 cgmsspsehf dvlrrtlagy arhpnlagvl ivglgcernq vsslmesqgl etsklmrtmv
      241 mqevggtrat ieagiaavle mlpeanaarr qpvpashlki glecggsdgf sgitanpalg
      301 aamdilvrhg gtailsetpe ihgveymltr ravtpevgqk lldrlawwek ytaghnaqfn
      361 gvvghgnqag glanifeksl gsamkggttp lqavyeyaep itqngfvfmd spgydpvast
      421 gqiasganli cfttgrgsmf gskpaptikl asntamfkrl eedmdincga ildgeldvaq
      481 mgrrifeeil rhasgeptks ealglgdhef vpwhlgivs
//
LOCUS       WP_007865031             316 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Polaromonas sp. CF318].
ACCESSION   WP_007865031
VERSION     WP_007865031.1
KEYWORDS    RefSeq.
SOURCE      Polaromonas sp. CF318
  ORGANISM  Polaromonas sp. CF318
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Polaromonas.
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   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   4  (residues 1 to 316)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Polaromonas sp. CF318"
                     /db_xref="taxon:1144318"
     Protein         1..316
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=33885
     Region          1..312
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mitldrltks fggsaqsavd glsltvntge icvligpsgc gktttmrmin rmvepdsgri
       61 evggrdvtki davelrrsig yviqqvglfp hmtlaenvat vprmlgwdsa riakrvdell
      121 alvhmdpsvy rnrfprelsg gqkqrvgvar alaadppvml mdepfgaidp itrarlqdef
      181 lrilrelgkt ivfvthdide airmgsriai lrsgkvvqyd tperilshpa dafveafvgg
      241 drslkrlall tagpyvesgt paagaprlpa atplrdalsa mldaganeaa ivdeqgqplg
      301 rvtlqsiqqa aavart
//
LOCUS       WP_007865077             359 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Polaromonas sp. CF318].
ACCESSION   WP_007865077
VERSION     WP_007865077.1
KEYWORDS    RefSeq.
SOURCE      Polaromonas sp. CF318
  ORGANISM  Polaromonas sp. CF318
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Polaromonas.
REFERENCE   1  (residues 1 to 359)
  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 359)
  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 359)
  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 359)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Polaromonas sp. CF318"
                     /db_xref="taxon:1144318"
     Protein         1..359
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39547
     Region          1..353
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkrrtliqna giagvlaagv apavhaqqvi rwrlassfpk sldtifgsae ifskavrams
       61 ggkfeistha agelmpafgv vdgvqqgsie vahtapyyff gkdetfalgc aipfglnsrq
      121 msawmyegng lklmrefyat yniinfpggn tgaqmggwfr kevksmadik glkfriggfa
      181 gkviqrmggv aqnipageiy qalekgtida aewigpyddl klglnkvapy yvypgwwegg
      241 pqldffinqk awdglsaenk aiveaaaaqs hvvmqaryde rnpaalkqlv gsgtklrpfp
      301 admmnaafkt smelysevsa knenwrkvya dfakfradqn lwfrfteatf drfmqsqkl
//
LOCUS       WP_007866039             795 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Polaromonas sp. CF318].
ACCESSION   WP_007866039
VERSION     WP_007866039.1
KEYWORDS    RefSeq.
SOURCE      Polaromonas sp. CF318
  ORGANISM  Polaromonas sp. CF318
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Polaromonas.
REFERENCE   1  (residues 1 to 795)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 795)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 795)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..795
                     /organism="Polaromonas sp. CF318"
                     /db_xref="taxon:1144318"
     Protein         1..795
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86403
     Region          60..108
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          87..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 mprsrfhlpp lalalalgsp vvysqgaasa raatpmqisl aaqplaqaln nlaqqaglel
       61 mvqpalvagk tapavsgqmt pqqaldrlla gsglaasidg nvfvvkaasa tpgaqtlpvv
      121 tvtagaetat sggngyvakr saagsktdtp iletpqsisv itkqqledqk prsvpealny
      181 spgvftglvg ssnrydyval rgfkdssvds tlldglrmls dqgsytsmqv dpyfleridv
      241 vrgpasvlyg raspgglval tsmtpqyqpy revqltlgnr nrreaavdls gpidkdgvma
      301 frltalsrsl dsqfntvkee rqalaaslai npskdtrlll qaylqddpdg syhsgvpada
      361 slnaghngrl isryffdgdp svekyqrnqr flgyqfehaf ndswkfrqnf rhvradttlr
      421 qiygfgwasa neltrfysga nestrgntid nqleghyqtg tlkhtvlagl dyqkrrvsgs
      481 wesgsalpin vftpsygapg ltgvtsdpid rkleqtglyl qnqteldrwr ftlggrmdwa
      541 kasnqygtgn paqwsgsrft kragvvylfd ngvapyagys dgfnpslrnd rlgnnlqpae
      601 tkqlevgvry qpkdsntlls aavyelsqkn vatrpvgvfy yeptgkvrsr glelearsql
      661 srsvsviasy sytdmkftes sdgftgntpy qaprhmaalw gdwnfspgyt agagvryvgs
      721 swadnanslk vppytlvdlm lrvdlaqlnp sfkganlrla vnnlfdksyv asclsqqycy
      781 wgdarsmtat vtyqw
//
LOCUS       WP_007867055              83 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Polaromonas sp. CF318].
ACCESSION   WP_007867055
VERSION     WP_007867055.1
KEYWORDS    RefSeq.
SOURCE      Polaromonas sp. CF318
  ORGANISM  Polaromonas sp. CF318
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Polaromonas.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Polaromonas sp. CF318"
                     /db_xref="taxon:1144318"
     Protein         1..83
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8579
     Region          2..83
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mkvtvkyfas ireaigqgie lrdtsattla alrdellaat pahaaslarg ravrmalnqv
       61 mcdetaalse gcevaffppv tgg
//
LOCUS       WP_007867290             182 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Clostridia].
ACCESSION   WP_007867290
VERSION     WP_007867290.1
KEYWORDS    RefSeq.
SOURCE      Clostridia
  ORGANISM  Clostridia
            Bacteria; Bacillati; Bacillota.
REFERENCE   1  (residues 1 to 182)
  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 182)
  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   3  (residues 1 to 182)
  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   4  (residues 1 to 182)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 182)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 182)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Clostridia"
                     /db_xref="taxon:186801"
     Protein         1..182
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=20294
     Region          1..178
                     /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"
ORIGIN      
        1 mtniivafsk pedgknikgi lvrngfqvva vctsgaqtls aaeglssgiv vsgyrfedml
       61 ydelrqylpg tfdmllissp srwsgqapgn viclpmplkv hdllntlemm vqaqmrfrrk
      121 mrgkpkerse eeqnliarak qllmernnmt eseahryiqk csmdsgtnlv etaqmvisli
      181 hv
//
LOCUS       WP_007867512             299 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Enterocloster citroniae].
ACCESSION   WP_007867512
VERSION     WP_007867512.1
KEYWORDS    RefSeq.
SOURCE      Enterocloster citroniae
  ORGANISM  Enterocloster citroniae
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Enterocloster.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Enterocloster citroniae"
                     /db_xref="taxon:358743"
     Protein         1..299
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33159
     Region          5..275
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mqtnridlhm hsfysddgec sprelvgkcl esgikvmaia dhnsvraneq gkeaagdagi
       61 tyipaveidc tyegvnfhvl gygidytspd fagiednisr qgaaasvkml hatralgfev
      121 tgeemaalag nnywkdrwtg emfaeilldk teykehpmlm pyrqggergd npyvnfywdy
      181 ysqgkpcyve mrypglgqiv etihgnggya vlahpgvnlk gheellrpli etgldgieaf
      241 ssyhsreqal dfynqarnhn lfytcgsdyh gktkpsiyvg qhgcvipyee vlgqlgglc
//
LOCUS       WP_007867463             344 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Polaromonas sp. CF318].
ACCESSION   WP_007867463
VERSION     WP_007867463.1
KEYWORDS    RefSeq.
SOURCE      Polaromonas sp. CF318
  ORGANISM  Polaromonas sp. CF318
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Polaromonas.
REFERENCE   1  (residues 1 to 344)
  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 344)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 344)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 344)
  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   5  (residues 1 to 344)
  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   6  (residues 1 to 344)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Polaromonas sp. CF318"
                     /db_xref="taxon:1144318"
     Protein         1..344
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37961
     Region          30..212
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          109..344
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mparspanpp vaatpmafar sitaaykryg qspdqalkla qitpnqlkqa nahitarqme
       61 vlsgaamqel gdeglgafsr klpwgsygml arasisspnl gialkrwcrh haliadditl
      121 rlttsgdtaa itveektpgr vgefgivhvl rnihglacwy vdsriplqga rfpfeapaha
      181 eaytlmfpgp glqfkaaqae irfdarylal plrrdekalq qmlqralplt vlqyrrdrll
      241 veqvrqalan pavlshnaet laaalnmspr slhrqlqeeg aslqqlkdev rfekakdlll
      301 rtskpikqva easgfrneks ftrafrewsg qspaefrqgn qpla
//
LOCUS       WP_007869640             359 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Polaromonas sp. CF318].
ACCESSION   WP_007869640
VERSION     WP_007869640.1
KEYWORDS    RefSeq.
SOURCE      Polaromonas sp. CF318
  ORGANISM  Polaromonas sp. CF318
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Polaromonas.
REFERENCE   1  (residues 1 to 359)
  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 359)
  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 359)
  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 359)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Polaromonas sp. CF318"
                     /db_xref="taxon:1144318"
     Protein         1..359
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39455
     Region          1..353
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mdrrslikna giagvlaagv apavhaqatv rwrlassfpk sldtifgaae vfakavknms
       61 ggkfeisvha agelmpafgv vdgvqqgsie aahtapyyff gkdecfalgc aipfglnsrq
      121 msawmyegng lklmrefytk ynivnfpggn tgaqmggwyr keiksvkdik glkmriggfa
      181 gkvleriggv pqnipggeiy qalekgtida aewvgpyddq klgfnkvapf yyypgwwegg
      241 peldffinnk afealspeyk aiveaaaaqa hgemqakyda knpaalkqlv gagtklrpfp
      301 tdvmnaafke amalyeelsa knenwkkiya dyskfradqn lwfrfteatf drfmqaqkl
//
LOCUS       WP_007869709             653 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Cronobacter sakazakii].
ACCESSION   WP_007869709
VERSION     WP_007869709.1
KEYWORDS    RefSeq.
SOURCE      Cronobacter sakazakii
  ORGANISM  Cronobacter sakazakii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Cronobacter.
REFERENCE   1  (residues 1 to 653)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..653
                     /organism="Cronobacter sakazakii"
                     /db_xref="taxon:28141"
     Protein         1..653
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=73906
     Region          63..535
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 meklkmhspn ltqgnitrir dlfpgcvtea kgedgsvkla vdfdqlrqel aesivegpqe
       61 ryhlnwpgkr eslltanapi aktlrpcrde svdfdttenl fiegdnldal kllqetylgk
      121 vkmiyidppy ntgkdfiykd dfstdvsdyl qqsnqvdser erlvantean grfhsdwlsm
      181 iyprlklarn llrddgtili siddnesdnl rkvcdevfge enfvgqivwq rskkgdskli
      241 akvheyvlcy ardkgsvlan gpwrrpkega dqvlakyael kanlgtnhea irremqawyk
      301 qlpnndprks hkhynwsddr glyfaadfag pddgresrpr hdilhpvtgk sckkpstgwr
      361 wdeektkwal tqtpprihfg pdettiptrk sylfeidsep yssvfyrdgr satlevedlv
      421 gkgwfpfpkn tdvlteliel vtkpddiild ffagsgstgh avmkvnqvhg skrrfiliqi
      481 peetgrtgya tiaeitkkrl leagkkaski ggstdidigf rvlkidtsnm aevyyspdal
      541 dnakfdlfvd nikpdrtped llfqvmldwg vdlalpiskq siqgkdvffv dgnvlaacfd
      601 asgsideafv kelakqqplr vvfrdagykn savkinveqi fkllspvtev kci
//
LOCUS       WP_007870800             398 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Clostridia].
ACCESSION   WP_007870800
VERSION     WP_007870800.1
KEYWORDS    RefSeq.
SOURCE      Clostridia
  ORGANISM  Clostridia
            Bacteria; Bacillati; Bacillota.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Clostridia"
                     /db_xref="taxon:186801"
     Protein         1..398
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42871
     Region          1..398
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkilvincgs sslkyqlidm enesvvakgl cerigiegsk lthqpsgkdk fviekpmpth
       61 ktaiemvmea lqdadhgvik dtseisaigh rvlhggtvys dsivvnedvk rvirecfdlg
      121 plhnpanlmg ieaceaampg tpnvavfdta fgmsmpekay myaipheyfe kygirrygfh
      181 gtshkfvsae aikfggldpk takvivchlg ngssvsasig gkcvdtsmgl tpleglimgt
      241 rsgdvdpavl qfimnkegld inemlnilnk ksgvygmtng issdfrdien akaegnhlae
      301 valdafiyrv tkyvgayaaa mngvdaiaft agvgendkag rkaicenlay mgvkiddeln
      361 nirgeervis sadskvkvml iptneelaia retldlvq
//
LOCUS       WP_007872543             270 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Polaromonas sp. CF318].
ACCESSION   WP_007872543
VERSION     WP_007872543.1
KEYWORDS    RefSeq.
SOURCE      Polaromonas sp. CF318
  ORGANISM  Polaromonas sp. CF318
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Polaromonas.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Polaromonas sp. CF318"
                     /db_xref="taxon:1144318"
     Protein         1..270
                     /product="formate/nitrite transporter family protein"
                     /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=29125
     Region          2..265
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 maylvpsefv tkmvdagesk ifmstrdtvi raymagaila laawfavtin vqtgqpllga
       61 vlfpvgfvml ylfgfdlltg vfvlcplali dkrpgvtvkg vlrnwglvft gnflgaftva
      121 vmmaiyvtng fstepsavgk aigvvgenrt lgyqkygang mltlfvrgml cnwmvsagvv
      181 gamistqvsg kviamwmpim lffymvfehs ivnmflfpsg lllgahftim dyliwneipt
      241 vlgnlvggla ftgltlyath vktgpsrsfk
//
LOCUS       WP_007873701             420 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Polaromonas sp.
            CF318].
ACCESSION   WP_007873701
VERSION     WP_007873701.1
KEYWORDS    RefSeq.
SOURCE      Polaromonas sp. CF318
  ORGANISM  Polaromonas sp. CF318
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Polaromonas.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 420)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 420)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Polaromonas sp. CF318"
                     /db_xref="taxon:1144318"
     Protein         1..420
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=45873
     Region          6..389
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 msvapvwvwl pgqaepvlag eltvmpaggr fryvetylgl eqpvsldpve lrltrrvrgi
       61 alrgadglpg vvrdarpagy gadrlnaqag relsalellq rgvpdgvgai evcqdleskl
      121 rwrpqslesl eallkeldql eapsralrrl ngdldtsagg erpkatlvhe gklwlakmqa
      181 rgdrpalpar efvtmrlage agieparvll rtlgehqvll verfdragdp vrpqrrlyas
      241 ahtvlqlqps atrgdparsy lnladrlrvw mhgredlqrq lellwrrmvf nalvgnvddh
      301 plnhgllhdg kgwalapafd itpaltqatk eeapmllmat gadgsavasa grlldasvyf
      361 glrredaqdw lnqaarlvag rwegmlreav gpvvedaark dalvadaraa fsyaeslarg
//
LOCUS       WP_007875134             156 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding
            protein, partial [Herbaspirillum sp. CF444].
ACCESSION   WP_007875134
VERSION     WP_007875134.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. CF444
  ORGANISM  Herbaspirillum sp. CF444
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 156)
  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 156)
  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   3  (residues 1 to 156)
  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   4  (residues 1 to 156)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 156)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 156)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 156)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Herbaspirillum sp. CF444"
                     /db_xref="taxon:1144319"
     Protein         <1..156
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          <1..145
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
ORIGIN      
        1 pkavfiggya pqggpikrqm kqlgidallm ggdgicspem grlggdaige svyctqggtm
       61 lekakegkaf addyqkkfgr paevyavsfy dgmmviaqam kaansvepkl ygpalakiky
      121 kgvagqyefd dkhdlkqspv tifrfkdgvp valtsy
//
LOCUS       WP_007875382             380 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Herbaspirillum sp. CF444].
ACCESSION   WP_007875382
VERSION     WP_007875382.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. CF444
  ORGANISM  Herbaspirillum sp. CF444
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 380)
  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 380)
  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   3  (residues 1 to 380)
  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   4  (residues 1 to 380)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 380)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 380)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Herbaspirillum sp. CF444"
                     /db_xref="taxon:1144319"
     Protein         1..380
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40055
     Region          29..369
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(105..107,128..129,181,233,257)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mliirnvsaw llllvasaas aapamlvvkl gfsgplsgsq asigkdalng vqlaidrlnq
       61 qgtlidgkvl rfellakdde adpdvgaira kelvdagvra vlgpfnsgvt lsaapiynea
      121 givsltvasn pkatlspanh aasqvfriaa sdsdigskma lyaarnlkik vvaiiddgsa
      181 yaqglieefq ktgkqnglqi alrevvsdra sdfrgvlnki rearvdaiff ggyapqasam
      241 lkqmqqlgms mpllggdalc sftiltqags gvgegtycvq ggvwltrvad gavfaaayqa
      301 rygtmpgvfa ptyydgvlll eramksansi dsrvfmpvla rirykgvtat yefdakhnmk
      361 dstvtilrvk dgklvplssf
//
LOCUS       WP_007876396             390 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Herbaspirillum sp. CF444].
ACCESSION   WP_007876396
VERSION     WP_007876396.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. CF444
  ORGANISM  Herbaspirillum sp. CF444
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 390)
  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 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   3  (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
REFERENCE   4  (residues 1 to 390)
  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 390)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Herbaspirillum sp. CF444"
                     /db_xref="taxon:1144319"
     Protein         1..390
                     /product="CmpA/NrtA family 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=42742
     Region          15..265
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mlglatggaw aagsdkpeke evkigfiplt dcasvvmasv lgfdkkygik ivpskeaswa
       61 gvrdkltnge ldaahvlygl iygvqmgigg qkkdmavlmn lnnngqaitl skkvadkggv
      121 dgpslarlmq tdkreytfaq tfptgthamw lyywlaangv npmkdakvit vpppqmvanm
      181 rvgnmdgfcv gepwghraiv dgvgitattt qdiwkdhpek vlgtsldfvk knpntcramm
      241 aaildagkwi daslanknkm aeviadksyv ntskdvidqr imgryqnglg ktwddpnymk
      301 fyndgavnfp ylsdgmwfmt qhrrwgllkd dpdylavars vnqidlykea aamtktsipk
      361 dpmrtsklmd gtvwdgknpk ayaasfkikt
//
LOCUS       WP_007876398             207 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Herbaspirillum sp.
            CF444].
ACCESSION   WP_007876398
VERSION     WP_007876398.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. CF444
  ORGANISM  Herbaspirillum sp. CF444
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
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   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   3  (residues 1 to 207)
  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   4  (residues 1 to 207)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 207)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 207)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Herbaspirillum sp. CF444"
                     /db_xref="taxon:1144319"
     Protein         1..207
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=23227
     Region          1..207
                     /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"
ORIGIN      
        1 mrnlrivvvn tiidhadetd talheqaerg kalrigllea gyniiaslpa dlylperiaq
       61 lqpdmiiida esdardvleh ivittrderr pivmfteddt tstmeaamea gvtayivagl
      121 qserikpvld valarfrqeq klltelsdtk lklaerklve rakgvlmarh klseeqayqk
      181 lrsmamnknl klseiaqrll dvedllg
//
LOCUS       WP_007878022             511 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Herbaspirillum sp. CF444].
ACCESSION   WP_007878022
VERSION     WP_007878022.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. CF444
  ORGANISM  Herbaspirillum sp. CF444
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Herbaspirillum sp. CF444"
                     /db_xref="taxon:1144319"
     Protein         1..511
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54272
     Region          6..511
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mkpispvirl npvddvviar rqlitgtvle eenglrvaal ipaghkmatr aiaagqpikr
       61 ygqiigtasq aiepgqhvht hnlamaefsr ehsfgadfkp vdyvdtpatf mgikrpdgrv
      121 atrnyigvlt svncsataar aiadyfrrdi hpealadfpn vdgivalthg lgcavdsege
      181 plamlrrtla gyakhpnfaa vlivglgcet nqisglleah nlkeneyfht ftiqstggta
      241 ktvalgieki kkmlpkandi krepvpashl tlglqcggsd gysgitanpa lgaavdllvk
      301 hggtailset peiygaehll trravspevg ekllariaww eeycakngae mnnnpsagnk
      361 agglttilek slgavakggt snlvdvykya etvtakgfvf mdtpgydpis atgqvaggan
      421 micfttgrgs aygcapspsl klatntalwq rqeedmdinc geiadgmatp qeigakffqm
      481 ildtasgkkt kselhgygqd efvpwhigvy t
//
LOCUS       WP_007878164             204 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Rhizobium/Agrobacterium group].
ACCESSION   WP_007878164
VERSION     WP_007878164.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium/Agrobacterium group
  ORGANISM  Rhizobium/Agrobacterium group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Rhizobium/Agrobacterium group"
                     /db_xref="taxon:227290"
     Protein         1..204
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=22131
     Region          17..204
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mapetsqqer lltflashpi arayelraag itpstisrav esgelvrisr glyqhvlgdm
       61 dssqalaeaa klaprgvval vsalafhglt dqipreiwva vsqrdwavap adsliriief
      121 rdtymtngie hhrisgvsvp ifsvtktiad vfrskvvdrs vaiealratl qqrkaspaai
      181 tetamvngaw rkmkpyleal tsng
//
LOCUS       WP_007879617             514 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [Brucella].
ACCESSION   WP_007879617
VERSION     WP_007879617.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..514
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=55294
     Region          11..514
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mndkavsavt pvillhpsdd vavarisvra gdpiglgdii ardligrghk valrdiaagk
       61 evhkygqvig vaiqdiavge hvhlhnlaml psehehqfsv dieergmlpe aerrqfmgyd
      121 rgfggvgtrn yigvissvnc satvsryiad yfnrmggldg fenvdgvval thgsgcalnt
      181 ksegyrlltr tiqgyakhpn fggilliglg cetnqiapim ehyrmeegsr lrtmtiqqhg
      241 gtrktidhai aeikemlplv nsakrtpqpl sklkvalecg gsdgysgisa npalgyasdl
      301 ivrnggttvl setpeiygae hlltrraitp avaekllqri dwwrdytarn gdelnnnpsh
      361 gnklggltti lekslgavak ggsmplkavy efaetvteqg ftfmdtpgyd pvavtgqvag
      421 gcnvicfttg rgsvsgfkpa pcikiatnse myehmkedmd fncggivtgd etieesgtri
      481 fehiiavasg eqtlseiydy gdnefvpwqv gavt
//
LOCUS       WP_007879689             276 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Herbaspirillum sp. CF444].
ACCESSION   WP_007879689
VERSION     WP_007879689.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. CF444
  ORGANISM  Herbaspirillum sp. CF444
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Herbaspirillum sp. CF444"
                     /db_xref="taxon:1144319"
     Protein         1..276
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=30627
     Region          18..187
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkfifltlil lisgcavtpf pidrgdykad qthpavaqne rirflvfhyt alddqksidv
       61 ltgpnvsahy laptvpaidn gkpvalqmva eekrawhagv snwgnrsnln dtsigieivn
      121 pgytdegaer rwydyapgqm dligklaldi isryqiapen vlahsdiapq rkydpgprfp
      181 wqalsrqgig awpdelvvek ylagrlllep asvaniqaal eeygytvpqt gvldeetrkv
      241 isafqmhfrp qnirgdadaq teaialalve kykkkn
//
LOCUS       WP_007880401             131 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein [Brucella].
ACCESSION   WP_007880401
VERSION     WP_007880401.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..131
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=14100
     Region          42..>88
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mrrlilataa tlalgsmafa qtatnvetev fvtakptdvi ssnilnldit nskdesigki
       61 qdliisegal tgyivsvggf lgigekyviv apqsveilya endkkwsakm dttkealeka
      121 pefkyegrwa k
//
LOCUS       WP_007880632             334 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Herbaspirillum sp. CF444].
ACCESSION   WP_007880632
VERSION     WP_007880632.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. CF444
  ORGANISM  Herbaspirillum sp. CF444
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  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   4  (residues 1 to 334)
  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 334)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Herbaspirillum sp. CF444"
                     /db_xref="taxon:1144319"
     Protein         1..334
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37032
     Region          61..212
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          240..319
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mdlndastdl dyasgapapl ssatvtpdge aderlraaqr elvtlisrlt egvegsletg
       61 iegfflhrit npqgpkhavq kpvfaviaqg akrlfvgddv ydydpmhylv ssvdlpmvgk
      121 vtisspetpy lglridldtk eigsligdeh lpqgipsdas rglfvnrlda tlldavlrll
      181 rlldtprdip ilapmvkrei lyrllmngqg allrqtvlqd sqmnriakai rmmkesfaqp
      241 lrvddiardv hmsvsslhhh fkvvtamspl qyqknlrlqe arrliladdv svalasqavg
      301 yespsqfsre ysrmfgsppl rdkrrwleee apil
//
LOCUS       WP_007880654             292 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Herbaspirillum sp.
            CF444].
ACCESSION   WP_007880654
VERSION     WP_007880654.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. CF444
  ORGANISM  Herbaspirillum sp. CF444
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Herbaspirillum sp. CF444"
                     /db_xref="taxon:1144319"
     Protein         1..292
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31617
     Region          13..261
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mqalplndhr ydvgespfwh aaqsawywvd iarklicrqt aegvykqwql pemvaciapd
       61 gaggmiagmh tgifgvtled dgnvlldkla qpsglqadqr fndgrcdrqg rfwsgvmcld
      121 mslaradgkl yrydaaglsa pvvdglivqn glawspdgkt mylsdshpas rliwafdydi
      181 asgtpsrrrv fadlnrhrgr pdgaamdvdg cywscandag cllrftpdgr ldrtielpak
      241 kpsmcafggd dlktmivtsi slgapqgdag aglvwtlnpg vagmpetpfv kn
//
LOCUS       WP_007880757             163 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Herbaspirillum sp. CF444].
ACCESSION   WP_007880757
VERSION     WP_007880757.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. CF444
  ORGANISM  Herbaspirillum sp. CF444
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Herbaspirillum sp. CF444"
                     /db_xref="taxon:1144319"
     Protein         1..163
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=18173
     Region          13..154
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 miesailwll ktlavptvgl tsvfiisfvs atllpmgsep avfavikanp emfwpvilva
       61 tvgntlggvv dywmgygakq tfakertsrw fhwlerfgak tmllgwlpgi gdpictlagw
      121 lklpfwpsvf ymavgkflry ilmtwlllnv pdgfwravad wla
//
LOCUS       WP_007881032             771 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Herbaspirillum sp. CF444].
ACCESSION   WP_007881032
VERSION     WP_007881032.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. CF444
  ORGANISM  Herbaspirillum sp. CF444
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 771)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 771)
  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   3  (residues 1 to 771)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..771
                     /organism="Herbaspirillum sp. CF444"
                     /db_xref="taxon:1144319"
     Protein         1..771
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=84064
     Region          1..759
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mkkdaardal vqegrellva meaallqies egpskdaina ifraahtikg saglfafdsi
       61 vsfthvlesv ldkvrngilk lddammslll ncgdymgdlv daieklqedq epdlarrtel
      121 eaalnahleq vavaeeanar dvpvvdatgl tetvaavtaa aaalagnaqy advdgdgdae
      181 ddhpavanpn whlslrfsqd vlrdgldpls flrylltmgr svyahtveht mptademdpe
      241 lcyigfeigf dsnadrqaie svfefvregs dinifsphcs leqyrcwlar mperdrmmrm
      301 llqsgaltda ecqflngegp lpcrtvtdsd aatlfaktaa ktvaktgsfe laphavadng
      361 avtrqksgdd kkgqeqkfik ievskldqli dlvgelviag agaslvakrk kdqrfeeatq
      421 lisglveqir daaltlrmvq inevfqrfpr vvrnisrelg keielivtga dteldksmve
      481 kisdplmhiv rnamdhgiea adirrdmgkp eagvlrlnat hesgsvviev fddgrgldke
      541 kivrkatqqg liavdanlse kdifrlifep gfstaeqvta lsgrgvgmdv vkrnidslhg
      601 evdifsnpgk gtmvrirlpl tlaiiagfqv vvggavfvip ldlvvecinl tahqvhdnvv
      661 tlrgeplpfi plrelfdlps resprkslvi vqygqmragl lvdnllgecq avikplgklf
      721 skvkglsgst ilgdgrvali ldvphliaht gqmeqvsirr seikvefger m
//
LOCUS       WP_007881596             358 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Herbaspirillum sp.
            CF444].
ACCESSION   WP_007881596
VERSION     WP_007881596.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. CF444
  ORGANISM  Herbaspirillum sp. CF444
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 358)
  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 358)
  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 358)
  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 358)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Herbaspirillum sp. CF444"
                     /db_xref="taxon:1144319"
     Protein         1..358
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39341
     Region          28..356
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mtpikpprgd fssnsspeps skrpsakrrt lltaaaslpl ftvwsgpara aefnyklatg
       61 qsldqpinar lkqatdrire asagrldirf fpasqlgsdt dlltqvrsgg veflniagsv
      121 istvvplaai tnvgftysdy qqvwssvdgd lgkliraqid ksgfvsvaka gdnsfrqiss
      181 askpiktpad lqgyrirvpv spmftslfks lganptsinf nelytalqtk lvdgqenglv
      241 aidsgklyev qkyitqtnhi wdpfwmlgnr rafanlpddl kkivqrefdr aymeqrgdve
      301 qlnttlkdql akkgiifeta nrdsfrkala dagfykewrd kfgaapwaal eavvgkms
//
LOCUS       WP_007883163             197 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Roseburia inulinivorans].
ACCESSION   WP_007883163
VERSION     WP_007883163.1
KEYWORDS    RefSeq.
SOURCE      Roseburia inulinivorans
  ORGANISM  Roseburia inulinivorans
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Roseburia.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Roseburia inulinivorans"
                     /db_xref="taxon:360807"
     Protein         1..197
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=22477
     Region          13..197
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mtaydrldll fqqnngivkt aqvlengiak stfyayakqr gveqaahgvy vspdawtdam
       61 yllhlrcaqa vfshesalff hdltdrepnp ysitvktgyn paslqadgik vytikkelhd
      121 vgivtmntpf gnpvpvydme rticdlirsr sgiemqtfqd alkqyakrkg kdlrklmrya
      181 qmfrvekllr qylevll
//
LOCUS       WP_007883297             346 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Herbaspirillum sp.
            CF444].
ACCESSION   WP_007883297
VERSION     WP_007883297.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. CF444
  ORGANISM  Herbaspirillum sp. CF444
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 346)
  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 346)
  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 346)
  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 346)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Herbaspirillum sp. CF444"
                     /db_xref="taxon:1144319"
     Protein         1..346
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=38222
     Region          13..346
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mtkdtltqsg itrrklltyg aagaalpmsa witkyahaae fnykfatgqd pthpvnkraq
       61 daitrikeat sgrvdiklfp anqlgsdtdl laqvrnggve ffniaasila tlvpaagivn
      121 tgfafssyde vwkamdgdlg kyifsqidkv gvmsmsrswn ngfrqitsgv kpirtpddlr
      181 gmklrvpaap iltslfqslg agptpinfne vysslqtklv egqenplpii atarlyevqk
      241 ycsmtshvwd aylvlgnkra fqklpadvqa ivlrefdkaa ldqradiarl ndslrqeltg
      301 kglqfidvdk nafrdalrkt tfykdwkakf geqgwhllqq ysgela
//
LOCUS       WP_007884420             633 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Herbaspirillum sp. CF444].
ACCESSION   WP_007884420
VERSION     WP_007884420.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. CF444
  ORGANISM  Herbaspirillum sp. CF444
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 633)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 633)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 633)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Herbaspirillum sp. CF444"
                     /db_xref="taxon:1144319"
     Protein         1..633
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=69648
     Region          13..633
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msssqvrpny sfrsqklhii tlaalgvvfg digtsplyal kecfspehgi afshdavlgi
       61 ismlfwsiti vvslkyvlfv mradnngegg vlalmalslr tavsgsrrak flmmlgvfga
      121 cmfygdvvit paisvlsave gmeiaapgts hyvipltlvi liglfliqrh gtnlvgklfg
      181 pimfiwfvsl galglfhilk apgilvainp yyavhfmieh slqafivlgs vvlvltgaea
      241 lyadmghfgi rpirfawlyt vmpclvinyf gqganllanp daiknpfylm vpdlllvpmv
      301 vlatfatvia sqavisgafs ltsqaillgf vprmriqhts edergqiyip linwmllvlv
      361 vavvlafkks dnlaaaygva vtttmvittm laavvmriew kwhpvlvtlv igaffivdfa
      421 ffaanllkia dggwfplllg gtaffllmtw ysgrmllrtr ikddgiplep fvegllahpp
      481 hrvggtavfm tgnintvpva llhnlkhnri lhervfflki siwdvpfvad aerltlkdlg
      541 gnvyllraaf gfkeapemhk vldltaaqfn mefdlmdtsf flardtvvps kllgmslwre
      601 qlfawmyqng akpsdffhip anrvvelgtk vei
//
LOCUS       WP_007888725             311 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Cronobacter sakazakii].
ACCESSION   WP_007888725
VERSION     WP_007888725.1
KEYWORDS    RefSeq.
SOURCE      Cronobacter sakazakii
  ORGANISM  Cronobacter sakazakii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Cronobacter.
REFERENCE   1  (residues 1 to 311)
  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 311)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 311)
  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   4  (residues 1 to 311)
  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 311)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Cronobacter sakazakii"
                     /db_xref="taxon:28141"
     Protein         1..311
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34221
     Region          28..178
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          206..287
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtmssvqret ielleqlapq egytrsqlda vrfmrsnral srtpvlyepc ivivcqgckr
       61 gyladkiyty naqhylvlsv plpfstetda tpqepllava vrlemtviae lvlaldderg
      121 adaappegil stplnaplad ttlrllrals hpqeahilgp aivkelyyrv lmgeqggair
      181 aalasfgkfs risrvlqrih adyagrldva tlaaeagmsa pafhahfkav tsnspvqyik
      241 avrlhqarll mirdnlsaat aasrvgyesp sqfnrefrrl fgrtpgaetr emkqsfallp
      301 ptqfeamttn h
//
LOCUS       WP_007889607             166 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Pantoea].
ACCESSION   WP_007889607
VERSION     WP_007889607.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 166)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..166
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17538
     Region          1..153
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mnkkafyedl nrdvrallag etsflaalgn csallferle gvnwagfyll tepntlvlgp
       61 fqgkiacvri pvgkgvcgta vaedkvqlve dvhafpghia cdaasnaeiv iplkvngtlv
      121 gvldidstvy srfdsedeag lvaltdglce vlagsdivkf iqlths
//
LOCUS       WP_007890167              66 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Roseburia
            inulinivorans].
ACCESSION   WP_007890167
VERSION     WP_007890167.1
KEYWORDS    RefSeq.
SOURCE      Roseburia inulinivorans
  ORGANISM  Roseburia inulinivorans
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Roseburia.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Roseburia inulinivorans"
                     /db_xref="taxon:360807"
     Protein         1..66
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7740
     Region          <1..61
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mgvtyfqyln eirlshiyrd ltstdlplkv llekhgftny klfrkmfyeq fattpgeyrk
       61 naavsd
//
LOCUS       WP_007890370             496 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Pantoea sp. GM01].
ACCESSION   WP_007890370
VERSION     WP_007890370.1
KEYWORDS    RefSeq.
SOURCE      Pantoea sp. GM01
  ORGANISM  Pantoea sp. GM01
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Pantoea sp. GM01"
                     /db_xref="taxon:1144320"
     Protein         1..496
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54027
     Region          1..496
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mqdairihsr dnvavalrdl pantqveinq qaitlqqevg rghkfalqpl aagelvikyg
       61 lpiahatqpi aageiihssn artnlsdvde ydyqpdflal ppqagdrdvq iyrrasgevg
      121 irnelwilpt vgcvngiarq iltrfmketh daegidgvhl fshpfgcsql gqdhentrtm
      181 lqnmvrhpna gavlviglgc ennqvdvfre tlggfdsdrv qfmecqkqdd eveaglerlh
      241 alyqamradk rqpgklselk fglecggsdg fsgitanpml gcfsdqmian ggttvltevp
      301 emfgaerilm srcrdeatfn ktvamindfk ryfidhqqpi yenpspgnka ggittleeks
      361 lgctqkagqs qvvdvlkyge rlhtpglnll sapgndavat salagagchm vlfttgrgtp
      421 yggfvptvki atnmqlaekk phwidfnagr liegmsmeam ladfvdmiva iangqparne
      481 tndfrelaif ksgvtl
//
LOCUS       WP_007890732             395 aa            linear   BCT 20-JAN-2025
DEFINITION  TerD family protein [Pantoea sp. GM01].
ACCESSION   WP_007890732
VERSION     WP_007890732.1
KEYWORDS    RefSeq.
SOURCE      Pantoea sp. GM01
  ORGANISM  Pantoea sp. GM01
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Pantoea sp. GM01"
                     /db_xref="taxon:1144320"
     Protein         1..395
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=42604
     Region          1..395
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mnmtpgsnap vpanlltvrv lsggavdasa frlfasgkvn gdadmvfygq pdnddrtisl
       61 kseghnsafa vdlnrlrpev qkvaftvtcd ggrnvsglqr laiqveqgge vllngsvelv
      121 grqeaalilg elyrrnndwk frfiaqgfng glqplaehfg vdvaepaptp apapqaapap
      181 apapaptpap akinlskvsl tkekpaislt krdnfgeiri nlnwhretns gggglrsffg
      241 gnkgvdldlg afvelqdgsr gviqalggnf gamhakpfvh lqgddrtgev tdgewlhing
      301 rewsqirevl ifafiyqgaa swdktdgvvt lhipdqppie trmtegenrr nmcaiarlvn
      361 engsirveri nqffnghsdm dkafgwgfnw ragsk
//
LOCUS       WP_007891396             242 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Streptococcus pseudoporcinus].
ACCESSION   WP_007891396
VERSION     WP_007891396.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus pseudoporcinus
  ORGANISM  Streptococcus pseudoporcinus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
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
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptococcus pseudoporcinus"
                     /db_xref="taxon:361101"
     Protein         1..242
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=27270
     Region          1..>239
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mirfnkvskq fgdtlvlqeq sfqvkdreff vlvgssgsgk ttllkmincl vkpssgqill
       61 nktpqneldl remrlsigyv lqqialfpnl tvaeniaiip emkkwtkekt lqrikdflnk
      121 vnlpaedymh rypkdlsgge qqrvgivral ishpkillmd epfsaldpis kkqlqdlmld
      181 lhrefdmtiv fvthdikeat klgdrvaild kgqiiqvdtp eaimanptnd fvaslfggdt
      241 nd
//
LOCUS       WP_007894216             745 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Pseudomonas sp. GM102].
ACCESSION   WP_007894216
VERSION     WP_007894216.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM102
  ORGANISM  Pseudomonas sp. GM102
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 745)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 745)
  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   3  (residues 1 to 745)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..745
                     /organism="Pseudomonas sp. GM102"
                     /db_xref="taxon:1144321"
     Protein         1..745
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79161
     Region          6..744
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msfgadeeil qdflveagei leqlseqlve lesrpddadl lnaifrgfht vkggagflql
       61 nelvecchia envfdilrkg errvdselmd vvlealdavn smfsevrers pitaatpell
      121 aalarlaepq tadesapvae vveepaaees gditdnefeq lldslnavka qaeapvaapv
      181 ptsdasasde itdaefesll dqlhgkgqfa vdavvaapaa paapkaagds sditddefea
      241 lldqlhgkgn favdalesai aavpapaapt akaaggdlis dhefesllde lhgkgkftev
      301 gtgsaasava tpvakapapv akapepkaea pkpaaaaapa parapsappp ekpaseaett
      361 vrvdtarlde imnmvgelvl vrnrlvrlgl nsgdeamska vsnldvvtad lqtavmktrm
      421 qpikkvfgrf prlvrdlarq lkkeinlelv geetdldknl vealadplvh lvrnsvdhgi
      481 eepaereamg kprsgkvils aeqegdhill sisddgkgmd advlrgiavk kglmdkdaad
      541 rlsesdcfnl ifapgfstkt eisdvsgrgv gmdvvktkia qlngtiniys tkgkgskivi
      601 kvpltlaimp tlmvmlgnqa fafplvnvne ifhldlsrtn vvdgqevviv rdkalplfyl
      661 krwlvssaah eeqreghvvi lsvgtqrigf vvdqlvgqee vvikplgkml qgtpgmsgat
      721 itgdgriali ldvpsmlkry aarri
//
LOCUS       WP_007894791             165 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Streptococcus pseudoporcinus].
ACCESSION   WP_007894791
VERSION     WP_007894791.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus pseudoporcinus
  ORGANISM  Streptococcus pseudoporcinus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Streptococcus pseudoporcinus"
                     /db_xref="taxon:361101"
     Protein         1..165
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17829
     Region          5..156
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mnirtkekny qlmiaqaqal fanednalan lanasallms slphsvfsgf ylfdgnelil
       61 gpfqggvscv rialgkgvcg qaaleektii vadvlqhdny iscdskamse ivvpiikngh
      121 llgvldldss vvgdydqldr lyleqlvail venssfnfem fgvkn
//
LOCUS       WP_007894822             253 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Streptococcus
            pseudoporcinus].
ACCESSION   WP_007894822
VERSION     WP_007894822.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus pseudoporcinus
  ORGANISM  Streptococcus pseudoporcinus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Streptococcus pseudoporcinus"
                     /db_xref="taxon:361101"
     Protein         1..253
                     /product="formate/nitrite transporter family protein"
                     /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=26965
     Region          1..253
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mknpeeiiqa tiaigqrkve kpflakailg figgamislg yllyvriaas gletfgafss
       61 ilgacafpig liiilmagge litgnmmavs asffakkipl tkllknwlvi tlfnvigaif
      121 vayvfghflg ltssgvfkee vihvaqakiv asplqafvsg igcnwfvgla lwlnygasda
      181 sgkllgiwfp vmtfvalgfq hsvanafiip aaifengatw lafvqnfalv yagnivggav
      241 fvslfyykaf yhd
//
LOCUS       WP_007896092             833 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas sp. GM102].
ACCESSION   WP_007896092
VERSION     WP_007896092.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM102
  ORGANISM  Pseudomonas sp. GM102
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 833)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 833)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 833)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..833
                     /organism="Pseudomonas sp. GM102"
                     /db_xref="taxon:1144321"
     Protein         1..833
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90822
     Region          75..125
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          102..833
                     /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 mtvraisknp lhfaaesgvl rhairaalfs talgvgllpt lgvaaqgsea sshpyniaag
       61 plsdvlnqfa rqagitlstt ptqtqglqsp glqgdysadq alshllngtg lvavsqdgss
      121 yvlrpvaete alalpatdik gfalgnalgs mdgynathsq iatktstall etsqsvsvvt
      181 reqmddqgsq tvsqamrytp gvltnpygat hrydyvamrg fndgsvdniy ldglksmgds
      241 gtystmqvdp yflervdilk gpssvlygrs spgglvalts kkplyepyhq vqatvgtqgq
      301 rgmgfdfsgp vdddkriayr ltgladqsdt qfdhnkekrf alaptvsidf tedtsltlqa
      361 ylqhdpdggy hggvpadgti hqrngnrisp nffegepgvd gfqrdqqsfg yqfehrfndv
      421 ftarqnfryl dskvkidqvy aygwttptsn elnryytggd eklhafivdn mlqaefftga
      481 tkhtvlmgad yqrrktvvdw tsgglapida fnpvygnsai dfysptsylr rleqtgvylq
      541 dliemdkwrf slglrqdwve tsdenrlaea arpvgteisd krtkltgrag alylfdngia
      601 pyisysesfn pnsyadsagn plaptdgtqw evglkyqppg tdnlftaslf ridqenlatk
      661 lpqenfyrav gavrsqglel eahmqltdnl kvlgsytftd ieysksmist lstatdvien
      721 kgnsptqapr hmasvwadyt fdsaaldglr lgggvryvgy swadaentlk vpsytlfdas
      781 vgydlgkvgl kgvdvrlnan nltnesyvas caslnfcymg eernvaatvs yqf
//
LOCUS       WP_007897291             153 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Pseudomonas sp. GM102].
ACCESSION   WP_007897291
VERSION     WP_007897291.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM102
  ORGANISM  Pseudomonas sp. GM102
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Pseudomonas sp. GM102"
                     /db_xref="taxon:1144321"
     Protein         1..153
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=17365
     Region          29..108
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mnyedrdtyg myktnllrda dseeqgpgpd lmgadtlign dvynhneedl gdikeimldv
       61 rngrvsyavl sfggflgmge klfavpwnal tldtvnkrfv lnvekerlen apgfdkdnwp
      121 nmadetwate ihsfygtkpf dydtvqrqni dqi
//
LOCUS       WP_007898142             510 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Pseudomonas sp. GM102].
ACCESSION   WP_007898142
VERSION     WP_007898142.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM102
  ORGANISM  Pseudomonas sp. GM102
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Pseudomonas sp. GM102"
                     /db_xref="taxon:1144321"
     Protein         1..510
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54622
     Region          6..508
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mttrevspvi rldpadnvvv arvaiaggtp ipgegittlq eiplghkiat rrigqghpvl
       61 kyntvigyas edlapgtwmh shniafgetd rdyrygldyv ptdllppeqr atfqgivrkd
      121 grvatrnylg vfvvgncgat varkianhfd eqhladypni ddvvpfvhei gcgmemtgep
      181 mdllrrtiag hirhantagg llialgcern nidgfiaqek leindllktl viqdvggvks
      241 avaqgiklie amlpeanrvk repvsaehlm igmqcggsdg fsglsanpal gaavdilvrh
      301 ggtailsets eifgvehtlt aravtpqvgr klieriewwl kynegrdtqi ngrvspgnna
      361 gglanvleks lggakkggna plmdvyeyay pvtthglvfm dtpgydpvsa tgqiagganm
      421 iafttgrgsc fgsvpaptfk lasnspmfnr msddmdincg qiidgdksik emgqeiferl
      481 lahasgektk selnglgede fcpwqigvla
//
LOCUS       WP_007898153             419 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Cronobacter
            sakazakii].
ACCESSION   WP_007898153
VERSION     WP_007898153.1
KEYWORDS    RefSeq.
SOURCE      Cronobacter sakazakii
  ORGANISM  Cronobacter sakazakii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Cronobacter.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 419)
  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 419)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Cronobacter sakazakii"
                     /db_xref="taxon:28141"
     Protein         1..419
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47607
     Region          1..405
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 msgvhlslra arhlhlaaqg llkkpvrrar padilaaitr msllqidtin ivarspylvl
       61 fsrlgnypgr wldealarge lmeywaheac flprsdfplf rhrmlspekm gwkyraawme
      121 ehaqeigelm afierngpvr sadfehprkg asgwwewkph kkhleglfta gqvmvverrn
      181 fqrvydlttr vlpdwddslh lidkaqaeaq mlansarslg ifrsawlady yrlrhvatgp
      241 llqawqdegf vvpvdvetlg pmwlhhellp lleravagkl tathsavlsp fdpvvwdrrr
      301 aeeffnfsyr lecytpapkr kygyfvlpll hkgalvgrmd akmhrqqgsl evialygeeg
      361 vsftagviag lrqaigdfaa wqgatrvvfr qlpgplahaw gegweidpap ethvisskd
//
LOCUS       WP_007899637             329 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Pseudomonas].
ACCESSION   WP_007899637
VERSION     WP_007899637.1
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 11438136
            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="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=36971
     Region          1..321
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msievrnvsk nfhafkaldn isldiqsgel vallgpsgcg kttllriiag letpdqgniv
       61 fhgedvsghd vrdrnvgfvf qhyalfrhmt vfdnvafglr mkpknqrpne sqiavkvhel
      121 lnmvqldwla drypeqlsgg qrqrialara lavepkvlll depfgaldak vrkelrrwla
      181 rlhedinlts vfvthdqeea mevadrivvm nkgvieqigs pgdvyenpas dfvyhflgds
      241 nrlhlgedrh vlfrphevsl srheledhha aevrdirplg attrvtlkve gqselieaev
      301 vkdhdslvgl akgetlffkp kvwqkvani
//
LOCUS       WP_007899648             334 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM102].
ACCESSION   WP_007899648
VERSION     WP_007899648.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM102
  ORGANISM  Pseudomonas sp. GM102
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  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   4  (residues 1 to 334)
  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 334)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Pseudomonas sp. GM102"
                     /db_xref="taxon:1144321"
     Protein         1..334
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37672
     Region          22..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          248..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mteptslasw tralrkqlda lgldstalcq qagldpqlmd dpnaryplsg ttrlwhiavq
       61 vsgdpaiglr vsrfvspttf halgyalvas gslrevferi vryhqvvsna ldleliraed
      121 ryrfhlkipq gnpapafeai dafaaiyvrt crnrlgrdya plavylrrpe padphqwhkv
      181 frspvyfnad edrlefalvd fdshlddanp elaehnetvl krtlaqlkpl twerkvrdai
      241 eeqlpegeps aeciaqalhl slrslqrhla degcrfdtll nesrenlall hlrdplcslg
      301 eisyllgfad tssfsrafkr wtgmtpgqfr dglq
//
LOCUS       WP_007900168             338 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM102].
ACCESSION   WP_007900168
VERSION     WP_007900168.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM102
  ORGANISM  Pseudomonas sp. GM102
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  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   4  (residues 1 to 338)
  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 338)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Pseudomonas sp. GM102"
                     /db_xref="taxon:1144321"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38174
     Region          23..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          252..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msekdtisiq lvreallqsc apgaateevl nkvgidpall qstdarvpat ayarlwrlla
       61 rrgddeffgm dprklksgsl eflcrcsmvq pslaagltsg lsflslmler mpaqlvrqqs
      121 laeivllede edprraftyf tywmivhgva cwlagrripi laielrcpap dfcddyrvmf
      181 senlrfdrlr trmifsadcl dlpikrssee lkrflahapa nilvkyrdpe slasrikhdl
      241 rqlpaehwpe tealaqqlcm sastlrrrla eegqtyqglk dsvrkelaiv wlaepaisfa
      301 eiatrlgfad assfykafrk wsgsnpghyr slilnead
//
LOCUS       WP_007900898             333 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM102].
ACCESSION   WP_007900898
VERSION     WP_007900898.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM102
  ORGANISM  Pseudomonas sp. GM102
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 333)
  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   6  (residues 1 to 333)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Pseudomonas sp. GM102"
                     /db_xref="taxon:1144321"
     Protein         1..333
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36881
     Region          20..199
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          114..332
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mhrmtcasfr vladvltdgg anveallkqf dsseevfanp kgvglelvyk vmeeavkrtg
       61 npdigllayt rahpanlevl gyavmssatl gtalqrlvdy hslisngfcm clerkpralr
      121 ligfdismep sltprpfida gaaqtlglvh wllpkhkpqp laasftypep adtswlerll
      181 gsnllfdapy nsltfslddc sialptadpa ldvlhveyar trlnlllnds mtarvrrvls
      241 erlaqgvpsd ldkiaqvvgv sarslqrrls nedmhfsalq dearlmlahn flrnsvrsvk
      301 yigallgfrd qssfhkacmr wfgmtpgryr ees
//
LOCUS       WP_007900932             126 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Leyella stercorea].
ACCESSION   WP_007900932
VERSION     WP_007900932.1
KEYWORDS    RefSeq.
SOURCE      Leyella stercorea
  ORGANISM  Leyella stercorea
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Leyella.
REFERENCE   1  (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   2  (residues 1 to 126)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Leyella stercorea"
                     /db_xref="taxon:363265"
     Protein         1..126
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14638
     Region          35..113
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mnpiseerrv fvqqkldewc anggykdsnv nmltlsrtlc isknelslff dqclhsnfri
       61 wlseirfnaa kkmmleypdy nndiisaecg fscrthlyri fktkegcspt ewrdfqstda
      121 aqndsn
//
LOCUS       WP_007903794             534 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Ktedonobacter racemifer].
ACCESSION   WP_007903794
VERSION     WP_007903794.1
KEYWORDS    RefSeq.
SOURCE      Ktedonobacter racemifer
  ORGANISM  Ktedonobacter racemifer
            Bacteria; Bacillati; Chloroflexota; Ktedonobacteria;
            Ktedonobacterales; Ktedonobacteraceae; Ktedonobacter.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Ktedonobacter racemifer"
                     /db_xref="taxon:363277"
     Protein         1..534
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=57403
     Region          35..534
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mdkpllprlq iqgsafphdk pidlqeaavl lqagddvaia rlplsrglvl rlpdgrllev
       61 gqriqaghkl alrgiaqgqp vlrygsiigf atqtiaagsh vhthnlavgt lhqqytygse
      121 lrlvdpvplh qrrtflgykr pdgrvgtrny laligtvncs astiraiqkr fgpeilrryp
      181 qidgiiglth kngcamgrqg iktlqrvlag mashpnvgay vlvglgcesn qiphlinemg
      241 lsagrqwkep lsltlqeheg vaqtveegvr lisellpqvn evrrepvpis eltlalqcgg
      301 sdgwsgvtan palgycadel irqggtavls etpeiygaeh vllrrarsqe vgekllarlr
      361 wweqyvaind memdnnpspg nklgglttiy ekslgaiakg gssplnavyq yaepiaergl
      421 vvmdtpgydp vsvtgqvagg anivvfttgr gscfgfkpap sikvatntpl yenmrndmdl
      481 nagvilegeg vgaeeigrqi leeviavasg kkskseaqdi geeefapwil gatm
//
LOCUS       WP_007903884             290 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Ktedonobacter
            racemifer].
ACCESSION   WP_007903884
VERSION     WP_007903884.1
KEYWORDS    RefSeq.
SOURCE      Ktedonobacter racemifer
  ORGANISM  Ktedonobacter racemifer
            Bacteria; Bacillati; Chloroflexota; Ktedonobacteria;
            Ktedonobacterales; Ktedonobacteraceae; Ktedonobacter.
REFERENCE   1  (residues 1 to 290)
  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   2  (residues 1 to 290)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Ktedonobacter racemifer"
                     /db_xref="taxon:363277"
     Protein         1..290
                     /product="aminoglycoside 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=32925
     Region          32..239
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mkpvellqrm nalhqttftf lekypdgeqg afavtdhlsr rwvlkwapga dnvewmqgak
       61 avtdllrslg ypapyyllig sipegiysiq salpgspvrq lpstllprll elnelqrgra
      121 ipgrkdwhqe vintvlwggd gyclheslqq hssgtaellq tlqalvmshq dephhttdiv
      181 hgdfqhanil ieekqisgvv dwdgfgagdc vfdiatllfy syesvevrer lwnyaleras
      241 lkllsiylah lilrqvdwsl ryhdqttser yitrghallq eiayrshsar
//
LOCUS       WP_007903986             118 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [unclassified
            Pseudomonas].
ACCESSION   WP_007903986
VERSION     WP_007903986.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (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   3  (residues 1 to 118)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 118)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..118
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12719
     Region          1..118
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mnepvspgpr ngilsltikd ravlyaaymp fikngglfip tnksyklgde vfmllhlmde
       61 pekipvagkv twitpkgaqg nraagvgvqf negddtarsr iethlagalk sdrpthtm
//
LOCUS       WP_007904284             439 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Ktedonobacter racemifer].
ACCESSION   WP_007904284
VERSION     WP_007904284.1
KEYWORDS    RefSeq.
SOURCE      Ktedonobacter racemifer
  ORGANISM  Ktedonobacter racemifer
            Bacteria; Bacillati; Chloroflexota; Ktedonobacteria;
            Ktedonobacterales; Ktedonobacteraceae; Ktedonobacter.
REFERENCE   1  (residues 1 to 439)
  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 439)
  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   3  (residues 1 to 439)
  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   4  (residues 1 to 439)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 439)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 439)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 439)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Ktedonobacter racemifer"
                     /db_xref="taxon:363277"
     Protein         1..439
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45449
     Region          45..421
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(122..124,145..146,214,266,293)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mqkrwtrmca lalgvpllla ilaacgpgta ttgsngggsg sttikvatdf pasgqdtang
       61 kpaqngaela vnesknlipg ytlqfvpkdd vgaqgvndpd tgkknvteli gdalvagivg
      121 pfnsavaqae mpvanqapiv lispsntnqc ltqeganvgc tgaqdkvptl rpsgkvtyfr
      181 lattddhqgs viadflfqkk glkkayvvdd ttvygvgian vfvqewqklg gtivgnresk
      241 qksndyggtv anvkaanpdv vfyggtdsqg gtqlrqqlln dsgtanlafa ggdgivttaf
      301 aqaigtkgga tygtvakvne tvlpaaksfi dnydkaygad qygaysaggy dcmkvllnai
      361 ksaidsgakt pkdsndsaga ktfrqavida mmktdyngit ghhtfdkngd ttnkvisiyq
      421 vadvnskpdf kfidqiaak
//
LOCUS       WP_007906983             340 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM102].
ACCESSION   WP_007906983
VERSION     WP_007906983.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM102
  ORGANISM  Pseudomonas sp. GM102
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 340)
  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 340)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 340)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 340)
  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   5  (residues 1 to 340)
  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   6  (residues 1 to 340)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Pseudomonas sp. GM102"
                     /db_xref="taxon:1144321"
     Protein         1..340
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39179
     Region          27..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <150..337
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mretdsvavy fmypmihalr eepqrlrsvl eqvgidpalm dqptarvpat afaalwlvqi
       61 relndeffql dshgmppgsf alicraliqe ptlekamrqc lanfalflrd frgtlsvrgk
      121 ravislqtrs qnsevsrlge etflvlmisl lcwlagrrip idradfrhqr lslrddallw
      181 gpnltfgter teiefashyl rlpvvqdlas lkvflrtapq wlvirfrnqh glasqvhqrl
      241 rhshysewpt lqafaleqhl spstfrrklg regcsyqeik devrravafe rlrqskasis
      301 diaeqlgfqe psafhrafkk wtgespgryr vryqaseaid
//
LOCUS       WP_007908286             291 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [unclassified Pseudomonas].
ACCESSION   WP_007908286
VERSION     WP_007908286.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..291
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31786
     Region          13..262
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mpwtaltqhr aqlgegpfwd aptqalywvd iagkqalrli gqnvqiwqmp ehvsafipca
       61 sgdalvtlss gvyrldldsp gleprltlfc vadpqpgnrp nearcdgqgr lwlgtmqnni
      121 gengedlpit rrsgglfrid pdkrvtpllr glgipntllw sddgttvlfg dslddtlyry
      181 fihadgnlda aqvwygpdqq ggpdgsamda egyiwnarwd gscllrltpd gkverkidlp
      241 vsrptscvfg gedlktlfit saqsphnhpl dgavlsmrvd vagklctrfa d
//
LOCUS       WP_007908608             408 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [unclassified Pseudomonas].
ACCESSION   WP_007908608
VERSION     WP_007908608.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 408)
  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 408)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..408
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46068
     Region          2..403
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mpatvsfslk qarrlalaaq gfngrqpptv kaahvhrlie rlgvlqidsv navvrshylp
       61 lfsrlgpyss dlldqaawss grrrslfeyw gheasllpls mypllgwrmq rarrgediyq
      121 qlarfgreqq dvvrrvlssv eeqgalgags lstredkagp wwdwsaekha lewlfaagev
      181 tvagrrgfer lydlpervip ssilqqalpd eaeaqrglll haaqalgvgt ekdlrdyfrl
      241 npadarprla elveagqlqm cevagwrqva yclpepkvpr kvvasallsp fdsliwersr
      301 terlfdfryr leiytpqdkr vygyyvlpfl hneriaarvd lraeraagql avhavheeep
      361 gldeegmlal avnlrqmadw lglervqlnc lresaarlrv alaqigcd
//
LOCUS       WP_007908634             160 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Pseudomonas].
ACCESSION   WP_007908634
VERSION     WP_007908634.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            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="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17168
     Region          14..159
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 midlqqsgqg legygmlaaq leslladerd fianaaqfsa flfnqlddln wagfylnrne
       61 elvlgpfqgq iacvripfgr gvcgaaaatr qtqrvedvha fpghiacdsa snselvvplv
      121 kdgrligvld ldspklarfg aqdqagieql aaiflrltdc
//
LOCUS       WP_007909980             173 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Ktedonobacter racemifer].
ACCESSION   WP_007909980
VERSION     WP_007909980.1
KEYWORDS    RefSeq.
SOURCE      Ktedonobacter racemifer
  ORGANISM  Ktedonobacter racemifer
            Bacteria; Bacillati; Chloroflexota; Ktedonobacteria;
            Ktedonobacterales; Ktedonobacteraceae; Ktedonobacter.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Ktedonobacter racemifer"
                     /db_xref="taxon:363277"
     Protein         1..173
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19249
     Region          60..126
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 mkvspwrqya lvmflcvlll nvipqagyas vaishrmtht llsqasaqrs ktsssrdavy
       61 cqcgtyvdry vngnigsfaq aselisllpq kgwhqepwgf lrvgdiavwd gsfappyght
      121 avvadisgyg nrinvtfkgt nqtgswfrel ncsnvsywnd sgsgwrrahy fyh
//
LOCUS       WP_007909798             812 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: Lon protease family protein [Pseudomonas].
ACCESSION   WP_007909798
VERSION     WP_007909798.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 812)
  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 812)
  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 812)
  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   4  (residues 1 to 812)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..812
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..812
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88876
     Region          65..800
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mpdpvaaslr lapealtrpf saeqfsfttt ndlepfrgvl gqeravealq fgvamprpgy
       61 nvfvmgepgt grfsfvkryl kaegkrlqtp adwvyvnnfd eprepralel psgtagvfig
      121 dinglidnll atfpavfehp syqqkksaid rafnqrydka ldiierlale kdvalyrdss
      181 nvaftpmldg kaldeaefaq lpeadrerfh edisgleerl neelaslpqw kresnnqlrs
      241 lneetitlal qpllsplsek yaenaavcgy lqamqvyllk tvveqlvdds ktdavarkll
      301 eeqyapslvv ghpvsggapv vfephptyen lfgrieyttd qgalyttyrq lrpgalhran
      361 ggflileaek mlsepfvwda lkralqsrkl kmesplgemg rfatvtlnpq hiplqvkvii
      421 igarslyytl qdldpdfqem frvlvdfded ipmvdesleq faqllktrts eegmapltad
      481 avarlatysa rlaehqgrls arigdlfqlv seadfirhla gdemtdaghi eralkakatr
      541 tgrvsarild dmlagiilid tdgaavgkcn gltvlevgds afgvparisa tvypggsgiv
      601 dierevnlgq pihskgvmil tgylgsryaq efplaisasi aleqsygyvd gdsaslgeac
      661 tlisalsktp lkqcfaitgs inqfgevqav ggvnekiegf frlcearglt geqgaiipqa
      721 nvatlmldek vlaavragqf hvyavrqade alsllvgepa gepnadgefp egsinarvve
      781 rlrdiaemis eedlkeaeke laqealaeak pa
//
LOCUS       WP_007909986             292 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Ktedonobacter racemifer].
ACCESSION   WP_007909986
VERSION     WP_007909986.1
KEYWORDS    RefSeq.
SOURCE      Ktedonobacter racemifer
  ORGANISM  Ktedonobacter racemifer
            Bacteria; Bacillati; Chloroflexota; Ktedonobacteria;
            Ktedonobacterales; Ktedonobacteraceae; Ktedonobacter.
REFERENCE   1  (residues 1 to 292)
  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 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 292)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 292)
  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   5  (residues 1 to 292)
  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   6  (residues 1 to 292)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Ktedonobacter racemifer"
                     /db_xref="taxon:363277"
     Protein         1..292
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33219
     Region          22..103
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          131..289
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mdyrmciqks idyieehlra citvdelaqi agfstyhyyr ifnayvgvpv veyirrrrla
       61 yaatelirgk rildiamdyg fdtyngfaka frktygcspe qyrshvsgql pqkvnlllfq
      121 eynilggivv epkiiskpaa kvagyelktt clegknlqei pafwsamtpe kfatlhktfp
      181 vvhhnelglc yppdsvtgdf syviaveven ydgvpadmfr gevpeatyav ftvppvenig
      241 pefsnaiqgt wkyimttwfp esgyefaegk vdyelyydat kveiyipikk ka
//
LOCUS       WP_007910986             172 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Ktedonobacter racemifer].
ACCESSION   WP_007910986
VERSION     WP_007910986.1
KEYWORDS    RefSeq.
SOURCE      Ktedonobacter racemifer
  ORGANISM  Ktedonobacter racemifer
            Bacteria; Bacillati; Chloroflexota; Ktedonobacteria;
            Ktedonobacterales; Ktedonobacteraceae; Ktedonobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Ktedonobacter racemifer"
                     /db_xref="taxon:363277"
     Protein         1..172
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=19479
     Region          3..172
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mdepgvlwlp snnyfpgrek hnvrwliihg tagfnsaqev geffqrtdvs thytigrdgv
       61 ivqsvrehda awgngyvseg hdpwwskgln pnyvtisieh vkpsrdnsda lttiqtevsf
      121 rlvknicerh eiprrradat ggitghysmd pvgrhfcpgp ypweelfsyl ar
//
LOCUS       WP_007911894             811 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [unclassified
            Pseudomonas].
ACCESSION   WP_007911894
VERSION     WP_007911894.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 811)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 811)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 811)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..811
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..811
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89217
     Region          63..113
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          91..811
                     /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 mrlstfrqrf syhciaysll mtsaasclvi shnaiaatva qryaiaagpl dnalsqfasa
       61 anvilsfspq qtsrlrsagl ngdftvdqgf aqllqgsglq avpqapgsyi lqalpngdal
      121 elaptningq lanpmnldya advgykaqns rigtktstpl setprsvsvv taqrmkdqks
      181 qtltevlgyv pgifappfaa gdslagdlfy irgfnatdyg ygllrdglrv qgnrydtste
      241 pyglerveif rgpssllyge napgglvnlv skrptaapqg evqlgygsnn rrqigvdvsg
      301 plndsgnvlg rvvmlgrksd tqtdhvpddr iyiapsltln fddfntltll anyqkdhtnm
      361 elglpaagtl ltnsngklsk gtllgdpdwn tferetwstg yefshsfndd wqfrqnsrym
      421 qsritrhetw pgnlnnagfg trlnmtaydr fnksmvysld nqlegkfqvg glentvlfga
      481 sydrtsfnqd wnagivgpid vynpvylrdp ttpiavqntl leqqmkgvya qiqskydhwl
      541 fllggrqdwv dsdfrdkvaq ssdissedkk ftyqggvmyq fdngmtpyvs ystsfvpvqq
      601 isnagapldp itssqyevgl kyepigwdta ftasvydlrk kddtyfdstt atyrqvgesr
      661 skgvelelns nltqnlnvta aytytdarit kdaatslvkg hqmtgvprnq asvwtkyrfl
      721 dgdlkglyvg ggvryfdsaf aytspslygk ldagdvtlvd aaigyqidtn wsvdlnaknl
      781 fdkeyvsgcn dagrcywged rtllgtvsyn w
//
LOCUS       WP_007912099             330 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_007912099
VERSION     WP_007912099.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 330)
  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   6  (residues 1 to 330)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..330
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36744
     Region          23..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          95..330
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mlhshlttln avslilntfk aeglsseall agsgisaadl sradtrittn qemqvcanav
       61 alkrdiglel grrmhvscyg ilgyalltca tfgdalrlai rypallgtlf elsleddger
      121 vwfvaadyre spamavfnae fclvslkvic ddllghplpl latrfehaap dyrdsyaehf
      181 nsplhfaakd nafafdrhwl dqplpladai thqamaercr kqnleftgrq awlgrirqll
      241 saqlnaapgl eglaqqmkcs prtlrrhlkd mgssyqelld elrferakqm lcedqlpiyr
      301 iaetlgfset asfrhafvrw sgvapsqfra
//
LOCUS       WP_007912810            1048 aa            linear   BCT 20-JAN-2025
DEFINITION  AAA family ATPase [Ktedonobacter racemifer].
ACCESSION   WP_007912810
VERSION     WP_007912810.1
KEYWORDS    RefSeq.
SOURCE      Ktedonobacter racemifer
  ORGANISM  Ktedonobacter racemifer
            Bacteria; Bacillati; Chloroflexota; Ktedonobacteria;
            Ktedonobacterales; Ktedonobacteraceae; Ktedonobacter.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Liu,Y., Sung,S., Kim,Y., Li,F., Gwon,G., Jo,A., Kim,A.K., Kim,T.,
            Song,O.K., Lee,S.E. and Cho,Y.
  TITLE     ATP-dependent DNA binding, unwinding, and resection by the
            Mre11/Rad50 complex
  JOURNAL   EMBO J 35 (7), 743-758 (2016)
   PUBMED   26717941
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Chen,Z., Luong,T.T. and Lee,C.Y.
  TITLE     The sbcDC locus mediates repression of type 5 capsule production as
            part of the SOS response in Staphylococcus aureus
  JOURNAL   J Bacteriol 189 (20), 7343-7350 (2007)
   PUBMED   17704228
REFERENCE   3  (residues 1 to 1048)
  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   4  (residues 1 to 1048)
  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
REFERENCE   5  (residues 1 to 1048)
  AUTHORS   Hopfner,K.P., Karcher,A., Craig,L., Woo,T.T., Carney,J.P. and
            Tainer,J.A.
  TITLE     Structural biochemistry and interaction architecture of the DNA
            double-strand break repair Mre11 nuclease and Rad50-ATPase
  JOURNAL   Cell 105 (4), 473-485 (2001)
   PUBMED   11371344
REFERENCE   6  (residues 1 to 1048)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Ktedonobacter racemifer"
                     /db_xref="taxon:363277"
     Protein         1..1048
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=122100
     Region          1..1025
                     /region_name="PRK03918"
                     /note="DNA double-strand break repair ATPase Rad50"
                     /db_xref="CDD:235175"
ORIGIN      
        1 mlitrielen iksyrhfsvd frrgttaisg engagkttlv eaigfalfds lpysqarfvr
       61 egekwgrvlv hllggderpy vverrcgsgs rwlihdeean mrieqgadvl dklhelfgid
      121 rerpldslfr dalgvpqgtf tsifleaask rkqtfdallq iedykaaaey lldsqkdyre
      181 qmqqrqsrid qleyetrele qwreqlkqsr qedaqqkvrn aeltttlaql ekreqelnaq
      241 ynqlqdlrrs searasqyds arsilanyqq alaqaqaaeq iacetetgyq qylqaegale
      301 qlrqqeqqrn rllkeqarlg nkhasiemka kglhtrlqev eqarqrietl qpdvqrqqel
      361 eerrdellqn vklyksicee gknqrerles trktggvleq ritaieplvd laqrlpeldl
      421 arsrlqvqsv erknkfqqln ekrralqerr dqhvplltkl qkaernvqli denraeaeem
      481 pklqellnei narlhrldgn ieaysdslkq saggqcpllr epclniknrg mvslesyfen
      541 llveeraqrq qvlterkdve arieqikkya dalgkyslyv ekrddlkrqm qqlesemeql
      601 eeacaeleaq lemlkehdsr vreneeqyke sklasekvat lpglrdqlqq neqlitqyet
      661 diqtmreran qlrdseprlq qvneqlitln dpraqlreqr nivaqaaqfq kevaeaeqel
      721 aelntqlaal heqlavyhel desikgqeel rqrsqgahqn ylkhieqara lperervfrq
      781 qeqeteqahq rmreaeqayi qaratfneqe ldevrrqrrd lhgeisslae kmqqiqrain
      841 eaeqriqnae qqlrelegtr qeyreledlh tmmeyfrkvi keaapyvlka mlndisaean
      901 rifgeimgdr saqlswqndy evvlrrqgvs rtfaqlsgge qmsaalavrl allkklstln
      961 laffdeptqn mdelrrmnla eqirrvrgfe qlivishddt feqgldslir lrkasgetql
     1021 qqeglsessf sdealypngs nepsmehv
//
LOCUS       WP_007913725             295 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Pseudomonas].
ACCESSION   WP_007913725
VERSION     WP_007913725.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            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="formate/nitrite transporter family protein"
                     /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=32300
     Region          24..274
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mttptdgktp dlsakeqhev eknqppraav lheiirsqgd qelersiaal wwsalaaglt
       61 mglslmgmgl lnsrlpdgde fkviasfgyc agflavilar qqlftentlt avlpvmtkpt
      121 lqnfgrlirl wtvvlvgnlc gtilvayvml elpifdtktd hafleigrkv menhasqmfa
      181 kgivsgwmia tmvwmipsme sakmwiiili tylmalgdft hivvgsaevs ylvfagelpw
      241 sdfwmvfagp tlagniiggs fifalishaq irsesgapke sadqaekpdp reikk
//
LOCUS       WP_007913864             803 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: penicillin acylase family protein [unclassified
            Pseudomonas].
ACCESSION   WP_007913864
VERSION     WP_007913864.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 803)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 803)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 803)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..803
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=88503
     Region          22..800
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkrvftvlal livvllvgvg gyvyskqptr qgqvelrnlq gsvtvryder gvphiraene
       61 tdlyralgyv haqdrlfqme amrrlargel aevlgpklld tdklfrslri reraasyvas
      121 ldkqspawkg lqayldginq yqdshaapie fdvlgipkrp ftaedsisva gymaysfaaa
      181 frteplltyv rdqlgadyln vfdldwqpkg vlvnghakpa palaagdwkd lnalarlseq
      241 alidnglpqf egsnawviag srsqsgkpll agdphirfsv psvwyeaqls apgfelyghh
      301 qalvpfaflg hnldfgwslt mfqnddldli aekvnpdnpn qvwyrgqwtd mvvtqqqinv
      361 kgqspvtltl rqsphgpivn dalgtaagkt piamwwafle tpnpilegfy qlnradtlak
      421 araaaakvqa pglnlvyana kgdiawwasa llpkrpagvr pefmldgssn qadkdgfypf
      481 sanpqeenpa rgyivsanfq pvsptgmeip gyynladrgq qlnrqlsdks vkwtneanqk
      541 lqlgtttgyg prllapllpv lrevvsdpaq lklveqlaqw pgdypldsvs atlfnqflyd
      601 ladaamrdel gndffetlls trvidaalpk laananspww dnrstpnket radivraawq
      661 asmqhlkltl gdnsaewkwg aahtlthghp lgqqkpleri fnvgpfaapg shevpnnlsa
      721 rigpapwpvt ygpstrrlvd fadpahglti npvgqsgvpf dshyddqaea yvdgmyvqah
      781 fndeevtant rstlkllpar aaq
//
LOCUS       WP_007914029             371 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Ktedonobacter racemifer].
ACCESSION   WP_007914029
VERSION     WP_007914029.1
KEYWORDS    RefSeq.
SOURCE      Ktedonobacter racemifer
  ORGANISM  Ktedonobacter racemifer
            Bacteria; Bacillati; Chloroflexota; Ktedonobacteria;
            Ktedonobacterales; Ktedonobacteraceae; Ktedonobacter.
REFERENCE   1  (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   2  (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   3  (residues 1 to 371)
  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   4  (residues 1 to 371)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Ktedonobacter racemifer"
                     /db_xref="taxon:363277"
     Protein         1..371
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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]"
                     /note="Members of the family are the ATP-binding subunit
                     of ABC transporters for substrates such as betaine,
                     L-proline or other amino acids, choline, carnitine, etc.
                     The substrate specificity is best determined from the
                     substrate-binding subunit, rather than this subunit, as it
                     interacts with the permease subunit and not with substrate
                     directly.; Members of the family are the ATP-binding
                     subunit of ABC transporters for substrates such as
                     betaine, L-proline or other amino acids, choline,
                     carnitine, etc. The substrate specificity is best
                     determined from the substrate-binding subunit, rather than
                     this subunit, as it interacts with the permease subunit
                     and not with substrate directly."
                     /calculated_mol_wt=41513
     Region          7..363
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mftvgvkfen vtkmyqngrp avqglslevq sgellvligp sgcgktttlr minrleepts
       61 gtiyvdghdv rsynpiqlrr gigytiqqtg llphmtveqn ielvprllrw dkkrrqervr
      121 ellelvgmdy rafahryprq lsggqqqrvg vlralatdpp vilmdepfga ldpisrevlq
      181 telkrlqakl hktiifvthd ideamrlgdr vailrdgqll qvgtptellh apqdefvakf
      241 lgrflslpqs pvdevrqliq tgesrilkel psgervvqmg sfpwcflidd qgvlkgatcq
      301 vpedleqwks iiwqeaasik etdtpdialk rliegeaeal pvvdeerhlv giishrsaik
      361 alssgvgrvs v
//
LOCUS       WP_007914373             232 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Ktedonobacter racemifer].
ACCESSION   WP_007914373
VERSION     WP_007914373.1
KEYWORDS    RefSeq.
SOURCE      Ktedonobacter racemifer
  ORGANISM  Ktedonobacter racemifer
            Bacteria; Bacillati; Chloroflexota; Ktedonobacteria;
            Ktedonobacterales; Ktedonobacteraceae; Ktedonobacter.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Ktedonobacter racemifer"
                     /db_xref="taxon:363277"
     Protein         1..232
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25201
     Region          114..194
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 mlkvllvsgs lfmvlmmfat smtvtmdaqa qgpplmmspg tqtidtsgtg rrtevvqwal
       61 kmaahlhctp arlvtdcqgs gadhyydagf ppeiiqwant rcpgcaawqa dtfqcvvfvi
      121 aayayvqplp vqgqnanqyw ehfvsqpgwq rlpvhgnvpq pgdimawngg ayghvsivlg
      181 vdprhtaitf aqangefpvq tlplnhdgsi ntqngywnaf evvgylhpli ls
//
LOCUS       WP_007914730             255 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Ktedonobacter racemifer].
ACCESSION   WP_007914730
VERSION     WP_007914730.1
KEYWORDS    RefSeq.
SOURCE      Ktedonobacter racemifer
  ORGANISM  Ktedonobacter racemifer
            Bacteria; Bacillati; Chloroflexota; Ktedonobacteria;
            Ktedonobacterales; Ktedonobacteraceae; Ktedonobacter.
REFERENCE   1  (residues 1 to 255)
  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 255)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Ktedonobacter racemifer"
                     /db_xref="taxon:363277"
     Protein         1..255
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28574
     Region          5..246
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mssikqavsw wcfanrgmtp rellqasadi gyqaveliep eywplvkefg ltiastnggl
       61 sieqglnrre hhaqlerdir atieqaekwg ipnvivfsgn rqglddrtga eitaeglsrv
      121 araaedagvt lvmellnski dhsdyqcdks awgievcrmv nsprvkllyd iyhmqimegd
      181 iirtiqdhha yfahyhtagn pgrheidetq eiyyppivrt ilatgyegyl gqefvplgdp
      241 ltalkqayal cnvki
//
LOCUS       WP_007915225             322 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Ktedonobacter racemifer].
ACCESSION   WP_007915225
VERSION     WP_007915225.1
KEYWORDS    RefSeq.
SOURCE      Ktedonobacter racemifer
  ORGANISM  Ktedonobacter racemifer
            Bacteria; Bacillati; Chloroflexota; Ktedonobacteria;
            Ktedonobacterales; Ktedonobacteraceae; Ktedonobacter.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Ktedonobacter racemifer"
                     /db_xref="taxon:363277"
     Protein         1..322
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33431
     Region          208..318
                     /region_name="COG3942"
                     /note="Surface antigen [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443142"
ORIGIN      
        1 msamdrestd resiygpgpy ggtsvftgdq qapynaqgga ptpmtpapgy aqtgplvspn
       61 ttrallapns tssllddtqa rtlgrsktta lrepllikge gkretsirpp qgrrvviqis
      121 vavlmlfimv gsllavntlg gptggnaatn ptnlglnnsn nlsdsqdpnq ssilsqaata
      181 tavsiygnnd vsysdngsgg svaggssnhg aygqctywaa mrfhavtgvw vpwygnawew
      241 asgalqygyh vsskpsvgai ivlqpgvqga ggvghvayve sinadgsvyt snynwynngg
      301 gfarlsywtf ypgsgvsfit lp
//
LOCUS       WP_007916865             213 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Pseudomonas].
ACCESSION   WP_007916865
VERSION     WP_007916865.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 213)
  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 213)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 213)
  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 11459477
            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="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22502
     Region          3..208
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 msstedeqla dlkdwwtrng kplvtgglla lvivfgwqay hkyqsnqsqg asvlyqqlle
       61 ttltpdgkpd aarvadlagk lnsefggsay aqygslfvak vavdsgkldd aatelkaivd
      121 kpanpalgei arqrlaqvlg aqnkaedglk lldgdadkaf latreelkgd llvqlgrtdd
      181 ankayqkaka alsdeaavgg lqiklddlak gda
//
LOCUS       WP_007916478             912 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Ktedonobacter
            racemifer].
ACCESSION   WP_007916478
VERSION     WP_007916478.1
KEYWORDS    RefSeq.
SOURCE      Ktedonobacter racemifer
  ORGANISM  Ktedonobacter racemifer
            Bacteria; Bacillati; Chloroflexota; Ktedonobacteria;
            Ktedonobacterales; Ktedonobacteraceae; Ktedonobacter.
REFERENCE   1  (residues 1 to 912)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 912)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..912
                     /organism="Ktedonobacter racemifer"
                     /db_xref="taxon:363277"
     Protein         1..912
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=103799
     Region          336..909
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mivkdeqian epvlltahqe hsqtekirse rarrqrpprf rrqhrrsrkh gsvqhqfvfl
       61 dhivqdvqvn raplaeepqe rdylaaleir atnytlksqe erstmmlafr allrslrfpi
      121 qmlirskpmd lssyvehlht htdqwqgeaf eiavsheram rllgaqrtli drrfylllta
      181 dqegvqgtwn sslrrllsrr artrarqahl deaqqilatr vqaiqhqlaa mgllshrlag
      241 keladlthga lqgeqalrfp lpesifalsd kplarpaldv lspssqeeet sfdpytaqme
      301 etlllpsard hllapadlma lkdllapesv rvtprylqvg eeyvrglaiv gfpreivegc
      361 lspllacdei fdlcfhfspq ntaefvkrll frkeqyastq rmnlhrgrqq dptlqvaead
      421 vtaligplas geesmlemgf yllvrapdla tlnartdrlr qilhqhlfva hpttlehaea
      481 frtcqptcmd tlgrtfttts tvaactfpfm sesfamqdgt fvgvttsgep vllnpwvles
      541 phefwggvtg sgksyavklw llherfrhpd tqvlildpsr eyerlvdvfg gtilrlspgs
      601 ehainpfdvl phgidmdwyv ttqrrgdrla ekmtqlhafl dlllaeyiph pttlsareka
      661 fldrafyecy rrvgittepr thdrqapflr dlydvlksgv vgqddyglad rleryvhgsl
      721 sglfnrqtsv tletslisfd vselrgsrel rpigmfliae liwsqalfhp rprrcyidea
      781 wsliaheegg rflerlarea rkhylslvti tqnpeqfiln pygniiaqna likvlkrlds
      841 vgaqaareaf gltqeeeqll lsiqqnrall svgskrmlve mnaspeehal ittdpqelav
      901 qrqqtqkegk tv
//
LOCUS       WP_007917523             332 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Pseudomonas].
ACCESSION   WP_007917523
VERSION     WP_007917523.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 332)
  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 332)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 332)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 332)
  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   5  (residues 1 to 332)
  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   6  (residues 1 to 332)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..332
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37940
     Region          22..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          92..332
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mrertiashf araalggarr vgfdysglll qlgispelld eprariapeq ftrliqglwl
       61 alddeylgfg napskpgsfa mmchasihcr nlekalqrgl lfyslfpeap rlslaredew
      121 vrlslddsqm wdpdhfltes llviwhrlgs wligqrirle qasfsyprpe hgaeydllfp
      181 cpltfgteqs sllfhsryls mpllqdertl khflerspad llsrpddgds lssrlrrlls
      241 rdtanwpdle avaahlhisp qtlrrhlree gtsfqelkdq lrrdiaiyhl gradlslqqi
      301 aeqlgfseps afhrafkkwt gltpgayraq eq
//
LOCUS       WP_007917573              65 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein, partial [Pseudomonas sp. GM16].
ACCESSION   WP_007917573
VERSION     WP_007917573.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM16
  ORGANISM  Pseudomonas sp. GM16
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 65)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 65)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 65)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Pseudomonas sp. GM16"
                     /db_xref="taxon:1144322"
     Protein         1..>65
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
     Region          <3..>62
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 maiingtaga dnllgtagdd qirglagndv lnggagndll iggdgadqli ggagfdivsy
       61 edvpn
//
LOCUS       WP_007918517             345 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Ktedonobacter racemifer].
ACCESSION   WP_007918517
VERSION     WP_007918517.1
KEYWORDS    RefSeq.
SOURCE      Ktedonobacter racemifer
  ORGANISM  Ktedonobacter racemifer
            Bacteria; Bacillati; Chloroflexota; Ktedonobacteria;
            Ktedonobacterales; Ktedonobacteraceae; Ktedonobacter.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Ktedonobacter racemifer"
                     /db_xref="taxon:363277"
     Protein         1..345
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36207
     Region          214..342
                     /region_name="COG3942"
                     /note="Surface antigen [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443142"
ORIGIN      
        1 msflerrskr nsksywepkv asnpviqeap nqeeayeikq lpfpditttd gisqlpptpt
       61 ttsqpntgpi yttgtlkail dttktpgttq pfatsayrsn ttalripvvi kgsgkqstgm
      121 lppqpkgrrl mlhvtvtall lfimagslma vaavgdvgah tgtgssspst ngmynssgdn
      181 sallaqqaat atavtqdgye pprqtpktss apapaptyag vtpgptlggs gnhffqgqct
      241 ywaayrfhql tnvwvpwlgd awqwsgqaaa ygwhvsssps vgaiivlqpg vqgaggyghv
      301 aivehinsng svyvstynwy aggggfgils ywtfspgsgv sfvtl
//
LOCUS       WP_007918188             365 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM16].
ACCESSION   WP_007918188
VERSION     WP_007918188.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM16
  ORGANISM  Pseudomonas sp. GM16
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 365)
  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 365)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 365)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 365)
  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   5  (residues 1 to 365)
  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   6  (residues 1 to 365)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Pseudomonas sp. GM16"
                     /db_xref="taxon:1144322"
     Protein         1..365
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40042
     Region          31..211
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          111..340
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mnvkvqdptf elalvspfll qtlaevvqsr gidsqslcrg lgftledlqd paqrisyrqa
       61 vamiqralkv lpnqglglwv gaqnvlgtlg llghvlslck tlrdafalgi rhqhtsggiv
      121 vssvdvvggq vhldaecrlp fadvqvfave effasllvyg ralagaefka iavefvhaap
      181 dylseyhrll gpdvrfgclh nrmlidgqwl dvnlpnhhsl alrqavalle leaaqvhqkl
      241 dliqaverai ardlssgshi ekiagdlnms srtlrrrlte haltfealle qvrqartlsl
      301 lanpdmpier iteevgysdv rsfrrafkrw tglspsawrn danphpsplp egeganrgvl
      361 shast
//
LOCUS       WP_007918946              83 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Pseudomonas].
ACCESSION   WP_007918946
VERSION     WP_007918946.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..83
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=9193
     Region          1..83
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 milinyfasy rdrlnlggek ipltdtlgcv edvrqmlmqr gdlwrevlga gnlmcavnqe
       61 lcqpsqvied fdeiaffppv tgg
//
LOCUS       WP_007918971             834 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [unclassified
            Pseudomonas].
ACCESSION   WP_007918971
VERSION     WP_007918971.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 834)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 834)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 834)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..834
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=91387
     Region          76..126
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          103..834
                     /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 mtvratcknt lnltaesgll rhavraalfs tvlgvgvmpg lsmadnpaas elshryniaa
       61 gplgealnqf arqagitlst tpqqtqgrqs pgvqgeystd qalshllggs gleavsqdgs
      121 syvlrplaet ealalpttdi kgfalgnalg smdgynaths qiatktstal letsqsvsvv
      181 treqmddqgs qtvsqamryt pgvltnpyga thrydyvamr gfndgsvdni yldglksmgd
      241 sgtystmqvd pyflervdil kgpssvlygr sspgglvalt skkplyeayh qvqatfgtqg
      301 qrgvgfdfsg pvdddkriay rltgltdqsd tqfdhnkekr falaptlsid fsedtsltlq
      361 aylqhdpdgg yhggvpadgt ihqrngnris phffegepgv dgysrdqqsf gyqfehrfnd
      421 vftarqnfry ldskvnmdqv yaygwtspss nelnryytgg derlhafivd nmlqaefftg
      481 atkhtvlmga dyqrrktvvd wtsgglapin afnpvygnst vdmygetsyl rrleqtgvyl
      541 qdliemdkwr fslglrqdwv etsdenriae agrpvdtein drrtkltgra galylfdngl
      601 apyisysesf npnsyadsag nplaptdgtq wevgmkyqpp gtdnlftasl fridqenlat
      661 klpqenfyra vgavrsqgle leahmqltdn lkvlgsytft dieysksmvs tlstptdvie
      721 nkgnsptqap rhmaslwady kfdnaaldgl rlgggvryvg yswadaentl kvpsytlfda
      781 sigydlgkvg lkavdvrlna nnltnesyva scaslnfcym geernvaatv syqf
//
LOCUS       WP_007919101             265 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phosphonate ABC transporter ATP-binding protein
            [unclassified Pseudomonas].
ACCESSION   WP_007919101
VERSION     WP_007919101.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
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   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..265
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=28236
     Region          3..246
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mtlslnqgrl rhangvdalr gvdlqigvge qvaiigpsga gkssllnlla talrpssgei
       61 evlgerawhl sarqrqrlra riglvhqapp lpprqrvvta vlagklgqws lgksllnllh
      121 pldvagaraa larldlgdkl fahcqqlsgg qlqrvgiarv lyqapeilla depvsamdpv
      181 maghtlsils rharehnvtl vaslhavdla lshfpriigl rdgqilfdsa sdqvshemld
      241 alyaneklqs ptaavapltv qiprc
//
LOCUS       WP_007919314             205 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein, partial [Pseudomonas sp. GM16].
ACCESSION   WP_007919314
VERSION     WP_007919314.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM16
  ORGANISM  Pseudomonas sp. GM16
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Pseudomonas sp. GM16"
                     /db_xref="taxon:1144322"
     Protein         <1..>205
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
     Region          1..205
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 dwtlganlen lvltgnavng tgnalnntlt gnaaantldg glgadtmigg dgvdtyyvdn
       61 vgdvvieada sltaldrvfa sidytlganv enlilignav ngtgnerdnr itgnalantl
      121 nggagadtmi ggdgvdtyyv dnvgdvviet dasltaldrv fasidytlga nvenliltgt
      181 anlngtgsav snritgndgd nildg
//
LOCUS       WP_007919459             218 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Ktedonobacter racemifer].
ACCESSION   WP_007919459
VERSION     WP_007919459.1
KEYWORDS    RefSeq.
SOURCE      Ktedonobacter racemifer
  ORGANISM  Ktedonobacter racemifer
            Bacteria; Bacillati; Chloroflexota; Ktedonobacteria;
            Ktedonobacterales; Ktedonobacteraceae; Ktedonobacter.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Ktedonobacter racemifer"
                     /db_xref="taxon:363277"
     Protein         1..218
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24341
     Region          16..213
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mslldlssdq lltttrsvrk rldfsrpiep eilqecleia lqaptgsnmq swhfvvvdda
       61 qkkaalaely rrsykdyrqa taatsgtafa knpergrvqe rvgnsadyla ehmhevpvml
      121 ipcfrgrten lpsgiqasiw gsilpaawsf mlaararglg sswttlhlty ekeaadildi
      181 pynkitqaal lpvaytlgtd fkpaprepls kilhwnqw
//
LOCUS       WP_007921226             277 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM17].
ACCESSION   WP_007921226
VERSION     WP_007921226.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM17
  ORGANISM  Pseudomonas sp. GM17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 277)
  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 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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Pseudomonas sp. GM17"
                     /db_xref="taxon:1144323"
     Protein         1..277
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30741
     Region          21..277
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <150..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 mnggqgesir fwqtaplagv ellaaryieh rfvphvhdgy vigmimdgaq ryryrgaehl
       61 agrgtlvlin pdelhtghkg tedgwlyraf ypdnaqilam lgelelptds lpafgatlyr
      121 dpdlvsgfcq lhqllespat alqqqtlwre mmllllrrha gikapgkpgr ehraivqake
      181 llqaqlaapp sleelaaavn lspfhfarvf rratgmppht wlmqqriaqa rallrdgclp
      241 levatqlgfa dqshlsrqfk qvygvgpaay rsarqsl
//
LOCUS       WP_007921622             248 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Pseudomonas sp. GM17].
ACCESSION   WP_007921622
VERSION     WP_007921622.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM17
  ORGANISM  Pseudomonas sp. GM17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  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   3  (residues 1 to 248)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Pseudomonas sp. GM17"
                     /db_xref="taxon:1144323"
     Protein         1..248
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28212
     Region          37..242
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mfnavnaeda pqppkvlttp leinstlrll qdshdpliit fhersqrfqs ylveidrdsn
       61 mialdemipr dgerfmlage pfrvegfheg vriawesngi ptidesnggr cyrgtlpdev
      121 vyhqrrnafr aalklaqlvn ielggeklka pivgklldis atgcklrfeg dissrlqlgq
      181 vyerfiaalp fgsmtapvel rylhheekid ttfagvrfhn msglvqrqve rfvyqlqrea
      241 rrfdkddl
//
LOCUS       WP_007923416             486 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Ktedonobacter racemifer].
ACCESSION   WP_007923416
VERSION     WP_007923416.1
KEYWORDS    RefSeq.
SOURCE      Ktedonobacter racemifer
  ORGANISM  Ktedonobacter racemifer
            Bacteria; Bacillati; Chloroflexota; Ktedonobacteria;
            Ktedonobacterales; Ktedonobacteraceae; Ktedonobacter.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Ktedonobacter racemifer"
                     /db_xref="taxon:363277"
     Protein         1..486
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51621
     Region          6..>485
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mnkelhslee vlqprsvail gasrspqkwg hvaarqlieg gfagevylin ptvseilgrp
       61 typslrdvpg qvdlaviats fphvpgsied ciakgvkgiv litagfsetg pegraleqdl
      121 varcrehgir iigsncmgly vrrsklnalg mvfplpegpi glvsqsgnlg myfyaqahld
      181 gcgfttflsv gnsvdvsfpe cmqyladdpe tsviagyves ieeetlrqvt rdmharghyk
      241 pavillsgat evgvraslah tgsqarvrpd sdtglfasgv vrvlrsdelf pvaqalalqp
      301 ttpqggrria iigdgggssv asgdavirag levpvlkaet qaalrelmps ratstnpvdv
      361 agaadedpls fahlaevcvk dpdvdgviit glfggyrwll sedfgpreea aaralgdlvr
      421 qygkpilvqt iyarhdipal rilrgegvpy yesveitcra maalsevgqf lakqestapa
      481 sqasir
//
LOCUS       WP_007923635             525 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Ktedonobacter
            racemifer].
ACCESSION   WP_007923635
VERSION     WP_007923635.1
KEYWORDS    RefSeq.
SOURCE      Ktedonobacter racemifer
  ORGANISM  Ktedonobacter racemifer
            Bacteria; Bacillati; Chloroflexota; Ktedonobacteria;
            Ktedonobacterales; Ktedonobacteraceae; Ktedonobacter.
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   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 525)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Ktedonobacter racemifer"
                     /db_xref="taxon:363277"
     Protein         1..525
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=58817
     Region          84..134
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
     Region          105..>193
                     /region_name="ARO8"
                     /note="DNA-binding transcriptional regulator, MocR family,
                     contains an aminotransferase domain [Transcription, Amino
                     acid transport and metabolism]; COG1167"
                     /db_xref="CDD:440781"
ORIGIN      
        1 mssiaalpst mqggrlfsva efpiatentt hsheqqpald eqsddqraya eftealrrel
       61 sanwiggycq mpdavrndpd lgnsaklvye qllsymwlkt drcwpsqtti aealgisrrt
      121 viraceelyq rghiekwrrg lcrtnvyfvn pisfarsfrr threepsvav laadnqarrv
      181 disqlppapd palehmlqsm cqndtsgsdt mshqevsech pkhtksnhiq gkhtldssrs
      241 argaepkkee fytrpetirr dedittetgt repepatqep kpenrntvas qerpaappcp
      301 iyvetylarl serfndlqpk asrtraakly hraraagcld eyefvgstds pepywiaaae
      361 aatvaklqrp geagitkvvk grkvampyff scleglvgka eqeraaydav iqdlqsqaqa
      421 eqlapepeaq eptyqpeqec prqddteaqe pepttapaps qepeaqeaeq eaphqepeaq
      481 eqpyqggytv eyqpsqesqr vdlreinpva advlarirar rrgsa
//
LOCUS       WP_007923665             937 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Ktedonobacter
            racemifer].
ACCESSION   WP_007923665
VERSION     WP_007923665.1
KEYWORDS    RefSeq.
SOURCE      Ktedonobacter racemifer
  ORGANISM  Ktedonobacter racemifer
            Bacteria; Bacillati; Chloroflexota; Ktedonobacteria;
            Ktedonobacterales; Ktedonobacteraceae; Ktedonobacter.
REFERENCE   1  (residues 1 to 937)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 937)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..937
                     /organism="Ktedonobacter racemifer"
                     /db_xref="taxon:363277"
     Protein         1..937
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=103864
     Region          329..874
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mvvdlrkhkh vspklgkvld ligvreiehg clclktagpa ydreykavva vdplnftlls
       61 dkekeavles frvllnrltf aisihirier ydidpylsrl dlaaqnartp aigemavdhk
      121 efvltlaath tllqrrfyii vpsdhekaks akkqpdacsq arsqlslrcn diiadldrag
      181 ltshrldnve lahyyqscvh agqardfpla gsnlaavarp ikptaaaval aglpaagdld
      241 inldatisar pdenilqqdv nntaethtia aatvtnegnk gkparartta tattdtpeka
      301 pdrfvnaael vaptglhvap dcltvrhnvg neflraftli gypaeveagw fdrlvqieep
      361 dvdlivyiap qeagpfvshl srrlttlrgt qlaeqhhgkt pdpyieaart diedlrkklv
      421 nrseqafevs tyilvrgtnk lqlaeksarl lsllkslelt avdltyehhr awqcglpdgr
      481 dilkrkkild tsslmmgfpf sstnlstptg iltgimpngs lvildplsdl lenghevkfa
      541 rsgagksfde kvrvgryila gfdalvidpe neykalceqy dgvnirmstg nyqlnpfdlp
      601 gadaddrnvl eekfqsllal fdlliadktp gvlsqrekay ltrclhltyh kagitadrst
      661 hvnrppnmtd fynvlrsgec gedsyeladr lqrfvpsfpd qtrldtnrpl tvfnirdlds
      721 esrpaallli tdyvwtlvrr srkyhprllv ideawsllqf eeggrflasm arrarkynlc
      781 lriisqdved clsseagrti lvnasmkflm kqdsstidav tqafhlsdee rkyllscakg
      841 sglffarssh vplrvvaspv eyklattnpn eseedtehdk dstavalpvi nvatrtteyd
      901 vvmpnffaaa pgadtgatpp sgyrklrler pgratdh
//
LOCUS       WP_007923923             633 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Pseudomonas sp. GM17].
ACCESSION   WP_007923923
VERSION     WP_007923923.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM17
  ORGANISM  Pseudomonas sp. GM17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 633)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 633)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 633)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Pseudomonas sp. GM17"
                     /db_xref="taxon:1144323"
     Protein         1..633
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68746
     Region          5..633
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mgqassqavg gehsrarplg mlvaavgvvy gdigtsplyt lkevfaghyg vpvnhdgvfg
       61 ilalifwslv wvvsikyvlf ilradnqgeg gimaltalar rastpyprlr vvlvilglig
      121 aalfygdsmi tpaisvlsav egleiafdgl ehwvvpmali vlvalfliqk hgtdrigklf
      181 gpvmvlwfvt lgglgiygia qhpevlqaln pvwgvrffiv hpgmgvailg avvlaltgae
      241 alyadmghfg rkpiarawfa lvlpalvlny fgqgallles peaarnpfyl lapswalipl
      301 vvlatlatvi asqavisgaf sltrqaiqlg yiprmyiqht ssaeqgqiyi gavnwalmvg
      361 villvlgfes sgalasaygv avtgtmlits ilvsavmlll wkwspvltvp illgfllvdg
      421 lffaanvpki fqggafpvla givlfalmtt wkrgkellmd rlgegalplp ifinsirvqp
      481 phrvqgtavf ltarsdavph allhnllhnq vlheqvvllt vvyediprvp tqrrfevdsy
      541 gegffrvilh fgftdepdvp ealklchlde ldfspmrtty flsretvits kivgmarwre
      601 tlfafmlkna ngnlrffklp vnrvielgtq iem
//
LOCUS       WP_007925489             636 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Janibacter hoylei].
ACCESSION   WP_007925489
VERSION     WP_007925489.1
KEYWORDS    RefSeq.
SOURCE      Janibacter hoylei
  ORGANISM  Janibacter hoylei
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Intrasporangiaceae; Janibacter.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 636)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Janibacter hoylei"
                     /db_xref="taxon:364298"
     Protein         1..636
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=67957
     Region          2..628
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 melaviavpa ervtqvvlec aavgvktlli issgfaevde agaarqqevl rlarthgmrv
       61 lgpnsfglin ndpavslnat ltpviprpgh lglfsqsgal aianldsaar rnlgisvfas
      121 agnrvdvsgn dlmqywvdde rthavglyle smgnprkfsr varhlasnkp vivvkpasat
      181 ygappghkvr kpkvkphvfg smlqqagvih cenvhqmfdv aqllvhqplp agrrvaivgn
      241 ssqlaalcad naterglevv hgpvaiptea sarefqravd aafgdpdvds vivcfippvg
      301 aldqevvdal rhaasrsdkp cvatllglrg vdeggdaafl hetgevaddt prqavplypm
      361 peeairalal atdygqwrdk dkgetvvrdg idrwaarall drvleedpeg raltsdesre
      421 llaaygidvw prfevadade avaiaeeigy pvvvkslspl vrgqallegi rvdlhdahav
      481 rsafetldrr lapmdanyfv vqrmarpgvs tvlstledpl fgpvvsfsia gapttllddi
      541 ayrippltdv dvrelvedlk lapllmghdg aapvdraale dilgrlsims ddflelssve
      601 lnpvvahpeg atvlgadvmi apvtrrridt garslt
//
LOCUS       WP_007925982              81 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Janibacter].
ACCESSION   WP_007925982
VERSION     WP_007925982.1
KEYWORDS    RefSeq.
SOURCE      Janibacter
  ORGANISM  Janibacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Intrasporangiaceae.
REFERENCE   1  (residues 1 to 81)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 81)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 81)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 81)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Janibacter"
                     /db_xref="taxon:53457"
     Protein         1..81
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8204
     Region          5..81
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mssttiryfa gaaeaagtde eqldgatvge vlaaarrahg drlsevlerc svlhagryvd
       61 ddstpvtaga tidvlppfag g
//
LOCUS       WP_007926035             809 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas sp. GM17].
ACCESSION   WP_007926035
VERSION     WP_007926035.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM17
  ORGANISM  Pseudomonas sp. GM17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 809)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 809)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 809)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..809
                     /organism="Pseudomonas sp. GM17"
                     /db_xref="taxon:1144323"
     Protein         1..809
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88035
     Region          61..111
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          92..809
                     /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 msrsldtllr psllavaial caplasppli aaeqassvra ynlpaaplas tlnqiasqag
       61 lalslnpsla agktsapvkg qfdaagalre alrgtglqle qssagtyslv aipdgvvalp
      121 etsitgqqay esawgpvdgy latrtaagtk tdtslveapr sisvatrqqm edrnvqnldd
      181 avrympgivs asygsdtryd wmrvrgfept qfldglplpr gvyanpkaet wnldrlallr
      241 gpassvygqt ppgglldmvs rrpsaessha iqlqygsdny rqinfastgk iddegqflyg
      301 lsgvvrdagt qvdhidnkry niapsltwni dtdtkltlls qftrddtgat sqfmpiqgtk
      361 iksplgdvsh hknlgdpdye fydrtyyalg yafehrfndv wqfrqnlryt kselsfqqlt
      421 vgsyayspad aagnisrtst nvdedisqfa vdnnfqadfa tgdithtvli gldhqrtdts
      481 ylsiygdggt tnifnpiygq pivrperssa yydynqktvq tglyvqdqma ldkwrltlgg
      541 redwvhqgtt yfnkndvtnt drsknfsgna alsyvfdsgl vpylsyaesf qpasnasvsp
      601 tesykptegk qwelgikyqp pgsntllsaa vydltqknvl vtsigagges vtnqtgevkv
      661 kgleleavsd vtdnlkviaa ytlaksevqk giykgnrlql mpnqqaslwt dytwhsgvld
      721 gfgigagary tgntygdqan twlgkanayt vfdasvhydl grldsslkga slklnatnlf
      781 dkdylstcdg sycyfgdqrs vvasatyqw
//
LOCUS       WP_007926771             145 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Pseudomonas sp. GM17].
ACCESSION   WP_007926771
VERSION     WP_007926771.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM17
  ORGANISM  Pseudomonas sp. GM17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Pseudomonas sp. GM17"
                     /db_xref="taxon:1144323"
     Protein         1..145
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16011
     Region          3..143
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 miptaclglf laafgaatll plqseavlvg lllngqhpvw lllavatlgn vlgslvnwwl
       61 gqrlehykdr rwfpvgprhl qrarshyqry ghwslllswl piigdpltlv agimgeplkr
      121 fllivtlakg arygvlawmt lgwvg
//
LOCUS       WP_007927097             324 aa            linear   BCT 20-JAN-2025
DEFINITION  prolipoprotein diacylglyceryl transferase [Janibacter hoylei].
ACCESSION   WP_007927097
VERSION     WP_007927097.1
KEYWORDS    RefSeq.
SOURCE      Janibacter hoylei
  ORGANISM  Janibacter hoylei
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Intrasporangiaceae; Janibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002130
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Janibacter hoylei"
                     /db_xref="taxon:364298"
     Protein         1..324
                     /product="prolipoprotein diacylglyceryl transferase"
                     /EC_number="2.5.1.145"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008961 -
                     phosphatidylglycerol-prolipoprotein diacylglyceryl
                     transferase activity [Evidence IEA]"
                     /GO_process="GO:0009249 - protein lipoylation [Evidence
                     IEA]"
                     /GO_process="GO:0042158 - lipoprotein biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34234
     Region          14..230
                     /region_name="Lgt"
                     /note="Prolipoprotein diacylglyceryltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0682"
                     /db_xref="CDD:440446"
ORIGIN      
        1 mdpslptswt psmthdlwvg igvltaggvl alekwrrgvs deriwalval avgfgavgar
       61 lgtwlqhlqp sandplavhw lygnrsilgg lafayvavlv gkrllrmqwr tgalfapava
      121 agmavgrvgc llteppgtat dvpwavtvts tadaaawgvp lgtrlhpsfa yeiafhllal
      181 laiwicrdrl adaadlftly itgyalfrfg veavrgneva wlgltrpqlf laatlppphl
      241 aqrrrgapst prsrawsspr hrvaptplph apgsawarap asarssassd psssrcspgv
      301 saascpgppg tepgwwssvs sppr
//
LOCUS       WP_007927578             424 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Pseudomonas sp.
            GM17].
ACCESSION   WP_007927578
VERSION     WP_007927578.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM17
  ORGANISM  Pseudomonas sp. GM17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 424)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 424)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Pseudomonas sp. GM17"
                     /db_xref="taxon:1144323"
     Protein         1..424
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47340
     Region          2..413
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mtltfdrpee gfaspcrfgy vqqylvdnle avasplarsv saqiplgwes wreerapafl
       61 ydlapaaatg rfllrqighe rpdgmgvelf llsrstaapi gnlrikesla glrrrpalgf
      121 srdqvivldn rfleyaheqg aafggtasig geapkllltq nregllypda llddasaarh
      181 wwvkfprnpa tqndgdilrs efhyyralqq lgidtlpaeg laleegprps lwmqrfdrrv
      241 tpmgverlav esiyslaglv ghgqgmrhte vlgilaelwr atgqesaipe lvadylrrdl
      301 lnkilgnsdn hgrnlsiirt dsrvqlapiy dlaptvmdde gitrtikwpg rmevagdvdw
      361 rlvcaslkpl ldpeaaltrl redaerlral pdllhasglp datlnhprih lrhldrrlqe
      421 wglr
//
LOCUS       WP_007929322              83 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Pseudomonas].
ACCESSION   WP_007929322
VERSION     WP_007929322.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..83
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=9052
     Region          1..83
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 milvnyfary reqlgiggek ialddslrsv gdvrtllmar getwqavlge tslmcalnqd
       61 lcnldapied fdeiaffpqv tgg
//
LOCUS       WP_007931045             248 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein [Pelosinus].
ACCESSION   WP_007931045
VERSION     WP_007931045.1
KEYWORDS    RefSeq.
SOURCE      Pelosinus
  ORGANISM  Pelosinus
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Sporomusaceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Pelosinus"
                     /db_xref="taxon:365348"
     Protein         1..248
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=28888
     Region          5..77
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
     Region          144..>191
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mlnkaktlsg ytlhssdgdi gkvkefyfdd hhwairylva ntgnwitgrq vlispyalaa
       61 vnkeeqyiti dltkkqiees pslnndkvvs rqfeksysmy ygmpmywngp dvwgaypniv
      121 rdpkmwnest psekswnpnl rntstvtgys iqasdgeigh vedfviddet weirylvidt
      181 qnwwpgkkvl vapqwiervs wdlstvfinl srdaikqspe ysaeallnrd yedamykhyh
      241 rqgywmmk
//
LOCUS       WP_007931755             807 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: Lon protease family protein [Pelosinus].
ACCESSION   WP_007931755
VERSION     WP_007931755.1
KEYWORDS    RefSeq.
SOURCE      Pelosinus
  ORGANISM  Pelosinus
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Sporomusaceae.
REFERENCE   1  (residues 1 to 807)
  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 807)
  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 807)
  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   4  (residues 1 to 807)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..807
                     /organism="Pelosinus"
                     /db_xref="taxon:365348"
     Protein         1..807
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=90183
     Region          2..793
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mmtkypelpv nklrftcden lfhfettasi spldvmigqk ravkavefgl faknhgynif
       61 isglvgtgki tyakaavakv akeqerpgdw cyvnnfknss qpialllpag mghvfckdie
      121 gliediktev gkvfssddye naknntiksf qerrtliids fnekasengi lpqwsttgfv
      181 gmpmkdgktl tpeefqslek eereatekki lavhekamev vrrmqelere mreeirkldg
      241 kvglfaagsm idevrqkyqd hsavveylea vkddvvknin dfknssgddd hsnplaflkk
      301 ntqdsirdky kvnllvdnre lkgapvivea nptyynlvgr veyetrmgmv stdftmikag
      361 alhkanggyl ilnvrdvltn igawealkri lktqklyven lseqygmmam aslkpqpvpi
      421 nvkvilignp ylyylmynyd edfgklfkih adfdtqmdsn mnnvqkmaef issaieskkl
      481 khfdrsavar vveyscrlag sqkklttrfs eivkilcead iwatmnqndm vtgehvkqai
      541 eekryrsnky eehlqemvad gklmidtkdk kigqvnglav mavgehmfgk psritantym
      601 gksgivnier etkmsgtsht kgvlilsgyi gqkyaqkypl altasltfeq lyggidgdsa
      661 sstelyalls slasvpikqs iavtgsvnqk gevqpiggvt ekiegffsic kmrgltgeqg
      721 vmiphqnvde lvlndeviea vkqgqfhiya vktidegiel ltdvpagecr vdgtyppgsi
      781 hylvtqklke ytdsfitlsk aaadakh
//
LOCUS       WP_007932093             469 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AAA family ATPase [Pelosinus].
ACCESSION   WP_007932093
VERSION     WP_007932093.1
KEYWORDS    RefSeq.
SOURCE      Pelosinus
  ORGANISM  Pelosinus
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Sporomusaceae.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Liu,Y., Sung,S., Kim,Y., Li,F., Gwon,G., Jo,A., Kim,A.K., Kim,T.,
            Song,O.K., Lee,S.E. and Cho,Y.
  TITLE     ATP-dependent DNA binding, unwinding, and resection by the
            Mre11/Rad50 complex
  JOURNAL   EMBO J 35 (7), 743-758 (2016)
   PUBMED   26717941
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Chen,Z., Luong,T.T. and Lee,C.Y.
  TITLE     The sbcDC locus mediates repression of type 5 capsule production as
            part of the SOS response in Staphylococcus aureus
  JOURNAL   J Bacteriol 189 (20), 7343-7350 (2007)
   PUBMED   17704228
REFERENCE   3  (residues 1 to 469)
  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   4  (residues 1 to 469)
  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
REFERENCE   5  (residues 1 to 469)
  AUTHORS   Hopfner,K.P., Karcher,A., Craig,L., Woo,T.T., Carney,J.P. and
            Tainer,J.A.
  TITLE     Structural biochemistry and interaction architecture of the DNA
            double-strand break repair Mre11 nuclease and Rad50-ATPase
  JOURNAL   Cell 105 (4), 473-485 (2001)
   PUBMED   11371344
REFERENCE   6  (residues 1 to 469)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Pelosinus"
                     /db_xref="taxon:365348"
     Protein         1..469
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51382
     Region          4..>201
                     /region_name="SbcC"
                     /note="DNA repair exonuclease SbcCD ATPase subunit
                     [Replication, recombination and repair]; COG0419"
                     /db_xref="CDD:440188"
ORIGIN      
        1 mssiiqavhl rgwqshvdss fhlgpglnvi tgpsdggkts iiravrwvaf ndpageafin
       61 eavgeakvai tltngiiiek rrrsgktayt lqapgdepki feksevpedv ktvlgiikhs
      121 fgdfaatlnf sfqldapfli seppsagakv lgriagtevi dlaiksvakd nyranqerlq
      181 ttkdierigk elkdfedlet lksqleacey lieqvdaaai rndtlakyed tyiqvttkit
      241 glaqeldrla ivdnleidil nmekaqqryd tllglysrlg klensiadlt hkldtytgvd
      301 alleevstld kdciklslls nlsivykkyt eevkkiknvl dstadldias ellggvkate
      361 lklsklqkla ityqentaci tryqnavnvt agvadagell aalaasrerl qrlaglkaty
      421 dvkrrtftqa stdersavim vdscqqelkt vwaslkvcpl ceqpvkgan
//
LOCUS       WP_007932734             188 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Pelosinus].
ACCESSION   WP_007932734
VERSION     WP_007932734.1
KEYWORDS    RefSeq.
SOURCE      Pelosinus
  ORGANISM  Pelosinus
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Sporomusaceae.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Pelosinus"
                     /db_xref="taxon:365348"
     Protein         1..188
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21352
     Region          2..154
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mfydlivsnr syrrfyeehs iseerlrelv nygrlspsga nkqplkyiis gdktknelif
       61 phllwagylk ewagpekger psgyivilqd tnigpsgvdh giaaqsillg arsmdlggcm
      121 iqsikrdelk atlqisdqye illvialgkp ketvildeie dgddikywrd tnlehhvpkr
      181 klkdiile
//
LOCUS       WP_007933474             339 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Pseudomonas sp. GM18].
ACCESSION   WP_007933474
VERSION     WP_007933474.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM18
  ORGANISM  Pseudomonas sp. GM18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 339)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Pseudomonas sp. GM18"
                     /db_xref="taxon:1144324"
     Protein         1..339
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35625
     Region          7..319
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mnasidgvsi ralsaaipqd vmtladfatl fgekevqria kstgihqvrv anrlstvdlc
       61 aaaaralfda adidpasidg lvvvtqtpds lmpassaila drlglkkala afdlnfgcsg
      121 yiyglfqaam likaggcrrv lvctgdvisk llspedrhvr lvfgdaatct lleggdqalg
      181 fafntdgaga qylntaldyt psatsrvqaa glhmdggqvm nfalekvpsa inafirdqgi
      241 dpervpffll hqankfmldy lakklgvapa kvpievadvg ntgpssiplm ickrhgredl
      301 rqdnliacgf gvglsigiah lslrdahiia pvevpalpn
//
LOCUS       WP_007933623             191 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Pelosinus].
ACCESSION   WP_007933623
VERSION     WP_007933623.1
KEYWORDS    RefSeq.
SOURCE      Pelosinus
  ORGANISM  Pelosinus
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Sporomusaceae.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Pelosinus"
                     /db_xref="taxon:365348"
     Protein         1..191
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21131
     Region          7..153
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 meqlivffqn fgvlglfiis fiesifspil pdlllvpmal svpekaiyys iiatvgsvlg
       61 givgyfignk ygiiavkkyv pnkyveking wleqyggwai flaalapipy kfvsissgvf
      121 rinmvvflia svfgrgkrfl legilifyyg pqaielikty sntfmigvii fivllavaia
      181 vmrkvpqrkl s
//
LOCUS       WP_007935507             333 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM18].
ACCESSION   WP_007935507
VERSION     WP_007935507.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM18
  ORGANISM  Pseudomonas sp. GM18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 333)
  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 333)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Pseudomonas sp. GM18"
                     /db_xref="taxon:1144324"
     Protein         1..333
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36759
     Region          20..196
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          248..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mhrmtsasfr vladvltdgg anveallkqf dsseevfanp kgvglelvyk vmeeavkrtg
       61 npdigllays rahpsnlevl gyammscatl gtalqrlvdy hslisngfcm clerkpralr
      121 ligfdismep sltprpfida gaaqtlglvh wllpkhkphp laatftypep adttrleqll
      181 gsnllfgapy nslsfsiddc sialptadpa ldvlhveyar arlnvllnds mtarvrrvls
      241 erlaqgvpsd ldkiaqvvgv sarslqrrls nedmhfsalq dearlmlahn flrnsvrsvk
      301 yigallgfrd qssfhkaclr wfgmtpgryr ees
//
LOCUS       WP_007935812             384 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: exonuclease SbcCD subunit D [Pelosinus].
ACCESSION   WP_007935812
VERSION     WP_007935812.1
KEYWORDS    RefSeq.
SOURCE      Pelosinus
  ORGANISM  Pelosinus
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Sporomusaceae.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Pelosinus"
                     /db_xref="taxon:365348"
     Protein         1..384
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43057
     Region          1..269
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          266..356
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrflhtsdwh lgrlfhgihl tsdqahvldq flalvreskp dgiiiagdiy dravppieav
       61 ellnqlisqi lvdykvptim iagnhdsaer lgfgsrllaa qglyvagalr reiepiilyd
      121 ehgpvyfapl tygepafvre rlscpdvsnh eqaieamvqh virkipnkar svaiahafia
      181 gsleseserp lsiggssmvk gavfqpfcyt alghlhnsqq agnpsihysg sllkysfaea
      241 fqrkgihlie mdkvggitve rislsprrdv rcikgyfkdi lnhsidqgnq qdyvsvtlld
      301 empildamgk lrekypnvlq iesprflkkg vlsglprdhr klsekelfaa fyhqmtgenm
      361 tqeqqmhlvd vietvyreer eail
//
LOCUS       WP_007935945             816 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pseudomonas sp. GM18].
ACCESSION   WP_007935945
VERSION     WP_007935945.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM18
  ORGANISM  Pseudomonas sp. GM18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 816)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 816)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 816)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..816
                     /organism="Pseudomonas sp. GM18"
                     /db_xref="taxon:1144324"
     Protein         1..816
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=88979
     Region          12..816
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 maspalthfl prfgvaaava gvlsltgcqt wnaqdtlppt sgvqalkgla qnvsvrrnam
       61 gmpliesnsf hdalftlgyv hasdrisqmv tlrllaqgrl aemsgadlld adrymravnl
      121 kksadelyka ssprlkrffe vyargvnayl fryrdklpad laatgykpey wkpedsalmf
      181 cllnfsqsan lpeeisslml aqtvstdkla wltpsapdek lpmaeaeklq gikltgqipg
      241 lseiskaagq lsdlnllgat ssnnwaiapq rsrsgkslla sdshgplgvp slfsyvqira
      301 pkyqasgvti aglpmvltgf ngkvawsmtt vmgdnqdvfl ekikrqgngl syevggkwqp
      361 aivrnetyfv kgqrpireav yetrhgplln saqgtalang fglalqapdf tddktldaff
      421 dlsraqster asdasreira ialnlvfada snigwqvtgr ypnrregegl lpspgwegry
      481 dwdgyadpml hpydqdpaqg wlgtanqrvi phgygmqlsn swsaperger maelagvgkh
      541 dtrsliamqy dqtttfaakl kkmfeapgms qplkqaieal pvadrgkare aytrlmafdg
      601 klsptsadaa iyelflqest kqifldelgp esspawkafi angklsyaaq adhllgreds
      661 pfwddvrtaq kedkpailar slaaaisagd sqlggdhkaw qwgklhryew knasgqtvrg
      721 plaaggdhtt lntasfawgq dfnttqapam rfivdfgqae plmgqnatgq sgnpasphyl
      781 dsvdpwlkgq ymslpmqpqn fdkvygktrl tltpgk
//
LOCUS       WP_007936449             809 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas sp. GM18].
ACCESSION   WP_007936449
VERSION     WP_007936449.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM18
  ORGANISM  Pseudomonas sp. GM18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 809)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 809)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 809)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..809
                     /organism="Pseudomonas sp. GM18"
                     /db_xref="taxon:1144324"
     Protein         1..809
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88497
     Region          61..111
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          92..809
                     /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 msrsldtvlr phllavaial caplassqlm aaeqassvra ynlpaaplan tlnqiasqag
       61 lalslnpsla agktsapvkg qfdatgalre alrgtglqle qssagtyslv avpegvmalp
      121 etavigvena etawspvegy vatrtaagtk tdtalveapr sisvatrqqm edrgvqnldd
      181 avrympgiva ssygsdtrdd wlrvrgfept qfldglplpr gvyanpkqet wnldrlallr
      241 gpassvygqt ppgglldmvs rrpsaesshe iqlqygsdny rqisfastgk iddegrflyg
      301 lsgvlrdsgt qvdhidnkry niapsltwni dpdtrftllt qftrddtgit sqflpvqgtk
      361 irsplgdish hknlgdpdwe yydrtyyalg yafehrlndv wqfkqnlryt ktdlsfqalt
      421 pgaypftqvd aqgnvgrtst svdedisqfa vdnnfqgdfa tgdirhtlli gldhqrtnsn
      481 ytsifgdglt tnvnnpiygq pivrpsrsta fydydqktyq tglyvqdqma ldqwrltlgg
      541 redwvhtgtr ffnkgdatnt erdkkfsgna aisyvfdsgl vpylsyaesf qptskatasp
      601 tesfkptegk qwelgikyqp pgsntlltaa vydltqknvs vtttnsdnvs itsqtgevkv
      661 kgleleavsd vtdnlkviaa ytlaksevqk gdfkgnrlql mpdqqaslwa dytwhngvld
      721 gfgigagary tgntygdqan twlgkadayt vfdaavhydl grldnslkga slalnatnlf
      781 dkdyistcds fycyygdqrs vvasatykw
//
LOCUS       WP_007937163             282 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: class II fructose-bisphosphate aldolase [Pelosinus].
ACCESSION   WP_007937163
VERSION     WP_007937163.1
KEYWORDS    RefSeq.
SOURCE      Pelosinus
  ORGANISM  Pelosinus
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Sporomusaceae.
REFERENCE   1  (residues 1 to 282)
  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 282)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Pelosinus"
                     /db_xref="taxon:365348"
     Protein         1..282
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=30179
     Region          2..273
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mslvtleeim kvhdgavgaf stydlftaqg iisaaeetnl pviamigapi lnkpgneyig
       61 eimvslakrs sanvcvfldh akdygtclka mklgfsavmi dgshlsiekn ieitnkvaev
      121 ahslgvsvea evgalagled geevkiakma stedvaqfls gakvealavs ignahglykg
      181 epkldfdllq rineiatvpl vlhggtgltq eqfalgvklg ikkinigtev rrtfveaaqk
      241 theknidawd laemsqaskn avtgmvrenl kffaynwkel ck
//
LOCUS       WP_007937866             148 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Pseudomonas sp. GM18].
ACCESSION   WP_007937866
VERSION     WP_007937866.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM18
  ORGANISM  Pseudomonas sp. GM18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Pseudomonas sp. GM18"
                     /db_xref="taxon:1144324"
     Protein         1..148
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16318
     Region          4..144
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlgayfglfl aafgaasllp lqseavlvgl llsdrywlws llavatlgnv lgsllnwwlg
       61 rgierfrerr wfpvsprhlq qaqkhyqryg hwslllswvp iigdpltlva gvmreplgrf
      121 liivtlakga rygvlavatl gwmgcsag
//
LOCUS       WP_007938113             121 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SPOR domain-containing protein [Pseudomonas].
ACCESSION   WP_007938113
VERSION     WP_007938113.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            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="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12720
     Region          <66..101
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mrkmvlviav ltlagcgedk gvdaqkpqpa vasvpaavtg pqwdvevrge tpqavsdlsg
       61 wliehsfvpn vvkengkvri lvgpfgsqae aqarqaeita altrakkmni eslivehpta
      121 q
//
LOCUS       WP_007938987             139 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Pseudomonas sp. GM18].
ACCESSION   WP_007938987
VERSION     WP_007938987.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM18
  ORGANISM  Pseudomonas sp. GM18
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Pseudomonas sp. GM18"
                     /db_xref="taxon:1144324"
     Protein         1..139
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=13800
     Region          2..135
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mknqngftli ellivvaiig ilatfalpqy skyqsrakvt aavaeisalk vpfedvinqg
       61 tdiaapagig attptgncti tatgtastgv gsigctilna pgpvlgktvt lsrtlaggwt
      121 cattvapeys pkgctasgt
//
LOCUS       WP_007939266             800 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pseudomonas sp. GM18].
ACCESSION   WP_007939266
VERSION     WP_007939266.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM18
  ORGANISM  Pseudomonas sp. GM18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 800)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 800)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 800)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..800
                     /organism="Pseudomonas sp. GM18"
                     /db_xref="taxon:1144324"
     Protein         1..800
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=88098
     Region          2..800
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkrvltvlal livilvaggg wyvyskqptr qgqvalqhlq gsvtvryder gvphiraene
       61 tdlyralgyv haqdrlfqme amrrlargel aevlgpklld tdklfrglri reraesyvaa
      121 ldrqspawka lqayldginq yqdshaapve fdvlgipkrp ftaedsisia gymaysfaaa
      181 frteplltyv rdqlgadyln ifdldwqpkg vlvkghaspa ptlaasdwkd lnalarlseq
      241 alvdhglpqf egsnawvisg nrsksgkpll agdphirfsv psvwyeahls apgfelygyh
      301 qalvpfaflg hnldfgwslt mfqnddldli aekvnpdnpn qvwyrgkwvd ivnteqqiav
      361 kgqspvtltl rqsphgpivn dalgtaagkt pvamwwafle tpnpildgfy qlnradtlak
      421 araaaakvqa pglnivyana kgdigwwasa llpkrpagvk pgfildgstp qadkegfypf
      481 sanpqeenpa rgyivsanfq pvsptgmeip gyynladrgq qlnrqlsdkn vkwdntanqk
      541 lqlgtttayg prllapllpv lrevvsdpae lklveqlaqw cgdypldsis atlfnqflfn
      601 ladaalrdel gndffetllp trvidaalpr laasadspww dnrntpgket radtvkvawq
      661 asmahlkttl gadsaqwqwg kahtlthghp lgmqkpldqi fnvgpfaapg thevpnnlsa
      721 kigpapwpvt ygpstrrlid fadpahslti npvgqsgvpf dshyadqaea yiegvyyqan
      781 fndeevtant rstlkllpar
//
LOCUS       WP_007940023             160 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Pseudomonas].
ACCESSION   WP_007940023
VERSION     WP_007940023.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            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="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17271
     Region          14..159
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 midlqksgqg legygmlwaq leslladerd fianaaqfsa flfnqlddln wagfylnrne
       61 elvlgpfqgq iacvripfgr gvcgaaaatl qtqrvedvha fpghiacdsa snselvvplv
      121 kdgrligvld ldspklarft addqagieql aaiflrltdc
//
LOCUS       WP_007940702             259 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Pseudomonas sp. GM18].
ACCESSION   WP_007940702
VERSION     WP_007940702.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM18
  ORGANISM  Pseudomonas sp. GM18
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Pseudomonas sp. GM18"
                     /db_xref="taxon:1144324"
     Protein         1..259
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=28734
     Region          18..175
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkflaliasl lvlagcasgp ridtshpsvn hdsriqfvvm hytsasleds lqllthgevs
       61 shyligddeh atiyklmden lrawhagesq wqgrtwlnss sigieivnpg fqdtptgrlw
      121 ypyseaqiqs mifllkdisk rqgisprhii ghsdiapmrk ldpgplfpwk rlaaeglgiw
      181 pneqavarqq aqfavqlpsi swfqaqlarl gyatpqtgel dvatrnvlaa fqlhfrpsrf
      241 dgtpdaqtaa llqvlnqtk
//
LOCUS       WP_007941926             338 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM18].
ACCESSION   WP_007941926
VERSION     WP_007941926.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM18
  ORGANISM  Pseudomonas sp. GM18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 338)
  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   5  (residues 1 to 338)
  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   6  (residues 1 to 338)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Pseudomonas sp. GM18"
                     /db_xref="taxon:1144324"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38988
     Region          27..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <150..336
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mretdsvavy fmypmihalr ekpqrlrsll eqvgidpalm dqptarvpat afaalwlaqi
       61 relndeffql dshgmppgsf alicraliqe ptlekamrqc lanfalflrd frgtlsvrgk
      121 ravislqtrs qnsevsrlge etflvlmisl lcwlggrrip idradfrhqr lslrddallw
      181 gpnltfgteh teiefashyl rlpvvqdlas lkvflrtapq wlvirfrnqh glasqvhqrl
      241 rhshysewpt lqdfaleqhl spstfrrklg regcsyqeik devrrgvafe rlrqskasis
      301 diaeqlgfqe psafhrafkk wtgespgqyr lrfqgrdd
//
LOCUS       WP_007942010             118 aa            linear   BCT 20-JAN-2025
DEFINITION  PilZ domain-containing protein [Pseudomonas sp. GM18].
ACCESSION   WP_007942010
VERSION     WP_007942010.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM18
  ORGANISM  Pseudomonas sp. GM18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (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   3  (residues 1 to 118)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 118)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Pseudomonas sp. GM18"
                     /db_xref="taxon:1144324"
     Protein         1..118
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12735
     Region          1..118
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mnepispgpr ngilsltikd rsvlyaaymp fikngglfip tnksyklgde vfmllhlmde
       61 pekipvagkv twitpkgaqg nraagvgvqf ndgddtarsr iethlagalk sdrpthtm
//
LOCUS       WP_007943688             234 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Pseudomonas].
ACCESSION   WP_007943688
VERSION     WP_007943688.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 234)
  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 10614777
            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="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=25333
     Region          37..204
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mallrfglpi aallltamsv psayadslaa alvkaaptad akvidlavra skcsiaqgka
       61 pvqrlavidy slpsteqrlw vfdlkkrkll fhelvahgrn tgenmavnfs nknesfatsl
      121 glyrtqssyv gqngyslrme glepgfndna fdraivihga pyvspmlarv ngrigrslgc
      181 pavrpaiahr lidsmkdgql lfsyypdqrw lktssyincg setvasaskp tirk
//
LOCUS       WP_007943973             812 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Pseudomonas sp. GM21].
ACCESSION   WP_007943973
VERSION     WP_007943973.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM21
  ORGANISM  Pseudomonas sp. GM21
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 812)
  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 812)
  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 812)
  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   4  (residues 1 to 812)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..812
                     /organism="Pseudomonas sp. GM21"
                     /db_xref="taxon:1144325"
     Protein         1..812
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88641
     Region          65..793
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mpdpvaaslr lapealtrpf saeqfsfstt ndlepfrgvl gqeravealq fgvamprpgy
       61 nvfvmgepgt grfsfvkryl kaegkrlqtp adwvyvnnfd eprepralel psgtagafig
      121 dinglidnll atfpavfehp syqqkksaid rafnqrydka ldvierlale kevalyrdas
      181 niaftpmseg kaldeaefaq lpeadrerfh edisgleerl neelaslpqw kressnqlrh
      241 lnegtitlal qpllsplsek yaenaavcgy lqamqvyllk tvveqlvdds ktdaiarkll
      301 eeqyapslvv ghsasggapv vfephptyen lfgrieystd qgamyttyrq lrpgalhran
      361 ggflileaek mlsepfvwda lkralqsrkl kmesplgelg rlatvtltpq hiplavkvvi
      421 igarqlyytl qdldpdfqem frvlvdfded ipmvdesleq faqllktrts eegmapltad
      481 avarlatysa rlaehqgrls arigdlfqlv seadfirhla gdemtdaghi eralkakatr
      541 tgrvsarild dmlagiilid tdgaavgkcn gltvlevgds afgvparisa tvypggsgiv
      601 dierevnlgq pihskgvmil tgylgsryaq efplaisasi aleqsygyvd gdsaslgeac
      661 tlisalsktp lkqcfaitgs inqfgevqav ggvnekiegf frlcearglt gqqgaiipqa
      721 nvatlmldek vlaavragqf hvyavrqade alsllvgepa gapdengefp egsvnarvve
      781 rlrviaemis eedlkeaeke aaqealvetk pa
//
LOCUS       WP_007945269             410 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Pseudomonas sp.
            GM21].
ACCESSION   WP_007945269
VERSION     WP_007945269.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM21
  ORGANISM  Pseudomonas sp. GM21
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Pseudomonas sp. GM21"
                     /db_xref="taxon:1144325"
     Protein         1..410
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44938
     Region          7..380
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mnepqekdrl hisvsatavg tlgrgqsrsd svftyvenag eqnsvsltmp arlesyaweq
       61 gvppifemnl pegvlreelv rrfskavrgf ddfamlsivg phqlgrvgia naqdandlpp
      121 etslsdllih dgaqglfedl lhtygqysgv sgvqpkvlvr dsattvdrlt hrgathlvks
      181 fraeeypela aneyfcmraa lhsglevpkf elsehgkflv verfdlneqg ylgfedfcvl
      241 nawpskakyd gsyegaarqi kafvspplln qalesffkiv alssalkngd ahlknfgvly
      301 ehcgmdaqis lapaydivtt svyiksdsma lllggskawp khkvlmrfgr sacnltegrc
      361 nellqqvahg mevamtemaa yikdssvfta vgeammeqwa sgiarslvks
//
LOCUS       WP_007945447             294 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Pseudomonas].
ACCESSION   WP_007945447
VERSION     WP_007945447.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            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="formate/nitrite transporter family protein"
                     /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=32192
     Region          24..274
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mdtpkdgktp nlsaeerhev dknqppraav lheiirtqgd kelersvaal wwsalaaglt
       61 mglslmamgl lnarlpdgeg fkviasfgyc agflavilar qqlftentlt avlpimskpt
      121 lgnfgrllrl wsvvlvgnlc gtllvayvml hlpifdtktd lafldigrkv mendaskmfa
      181 kgiisgwmia tmvwmipsme sakmwiiili tyfmalgdft hivvgsvevs ylvfagelpw
      241 kdfwlvfagp tlvgnivggs fifalishaq irsesgppkk sadqapdphk rkee
//
LOCUS       WP_007946771             748 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [unclassified Pseudomonas].
ACCESSION   WP_007946771
VERSION     WP_007946771.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 748)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 748)
  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   3  (residues 1 to 748)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..748
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..748
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79489
     Region          6..747
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msfgadeeil qdflveagei leqlseqlve lesrpddadl lnaifrgfht vkggagflql
       61 nelvecchia envfdilrkg errvdselmd vvlealdavn smfsevrers pitaatpell
      121 aalarlaepq sadeqapvae aaqapaaete sdditdnefe qlldslnavk aqaeapvatp
      181 tpvndaaasd eitdaefesl ldqlhgkgqf avdavtaapa apvapkaagd ssditddefe
      241 alldqlhgkg nfavdalesa iasvsvpaap taaaaggdli sdhefealld elhgkgkfse
      301 vatgsaasfv aapvakavap apvaktpepk aetpkpvaaa apaparapaa ppaekpasea
      361 ettvrvdtar ldeimnmvge lvlvrnrlvr lgansadeam skavsnldvv tadlqtavmk
      421 trmqpikkvf grfprlvrdl arqlkkeinl elvgeetdld knlvealadp lvhlvrnavd
      481 hgiespeere asgksrggkv ilaaeqegdh illsisddgk gmdpqvlrsi avkrgvmdkd
      541 aadrlsdtec ynlifapgfs tkteisdvsg rgvgmdvvkt kisqlngsin iystkgqgsk
      601 ivikvpltla imptlmvmlg nqafafplvn vneifhldls ttnvvdgqev vivrdkalpl
      661 fylkrwlvss aaheeqregh vvilsvgtqr igfvvdqlvg qeevvikplg kmlqgtpgms
      721 gatitgdgri alildvpsml kryatrri
//
LOCUS       WP_007946897             346 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_007946897
VERSION     WP_007946897.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 346)
  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 346)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 346)
  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   4  (residues 1 to 346)
  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 346)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..346
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38781
     Region          27..212
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          257..339
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkplpmrlgd lsvgfvhsla eavhshgvdp qplldqygld aarlaepgar lsiprymrlg
       61 hgaiqltddp alglrmgqls rlsqaglagv taaqaptvre aarclirfea lygsnyrgqs
      121 sfhedaqgaw lrfysispyn aynrfvvdsi iagwlqqlss lspaplraer ieiefdapdy
      181 reayailgdc piqfgaehnq lrlnlaslaq rnpvhcpstw rhllqlcere leqltrtrsl
      241 reritqllgp llnggrepdl eevaarlklp twtlrrklae egtqfrailn dtrrdlamty
      301 irdtelafge iayllgfasa eafqrafkrw ngqtpgefrr shrhsa
//
LOCUS       WP_007947467             321 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_007947467
VERSION     WP_007947467.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 321)
  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 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 11454538
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36138
     Region          53..316
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          232..312
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 msipdevfrv tstpadnlnr tigrwemnlv psereasirq hkliqtpklq csrlefdsai
       61 tiisavphgy vtfaisqasv grpiinnhel rpneiivlts depvhytcep netlltlttt
      121 lehykqcqes hstidllanr kdyrfqvanf ksmqsaiqai nthfnnannl pleqrdctea
      181 saiesallts llrvltpagr aslkvptrrk vamaaieyih gnlkkalsmk alvkqlqttt
      241 rtlhhgfvet fgispiayvr nlrlanvrrd lvrntwptvt etamywnfqh lsrfskayqd
      301 aygvtpsett rrnaaklsap n
//
LOCUS       WP_007947536             377 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Pseudomonas].
ACCESSION   WP_007947536
VERSION     WP_007947536.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 377)
  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 377)
  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   3  (residues 1 to 377)
  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   4  (residues 1 to 377)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 377)
  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 10156937
            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="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39670
     Region          30..364
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(103..105,126..127,176,228,253)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 msqtfykkgf lalavaaalg vsafaqadvk igvagpmtga naafgeqymk gaqaaadavn
       61 asggvngeki vlvkgddace pkqavtvakd ltnqkvagvv ghfcssstip aseiydeagi
      121 iaitpgstnp avterglsam frmcgrddqq givagdyivd vlkgkkvvvl hdkdtygqgl
      181 adatkaqlvk rgvtpvlyeg ltrgekdfst ivtkirgaga dvvyfgglhp eagplvrqlr
      241 eqglkdvkfm sddgivtdel vttaggpqfv dgvlmtfgad prllpeskav vdafrkagte
      301 pegytlyaya svqalaaafn gaksnsgeka aewlkknpvk tvmgektwda kgdlkvsdyv
      361 vyqwdkdgky hqlekqk
//
LOCUS       WP_007948272             262 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Pseudomonas sp. GM21].
ACCESSION   WP_007948272
VERSION     WP_007948272.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM21
  ORGANISM  Pseudomonas sp. GM21
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 262)
  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 262)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Pseudomonas sp. GM21"
                     /db_xref="taxon:1144325"
     Protein         1..262
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29438
     Region          1..250
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mtrlnahigf qftelpfler fsaaanagfr avefpspyey eapqiaellc ehelqmvqfa
       61 apsgptkgtt gicsskeafr sdlikaveya naldcrmvhl msgvsqaalg viadssiyrr
      121 nlkyavefls gegiepliev issnevpgyl msrydfaeem lqtlpglgli ldtyhtellg
      181 edclrklnqw wsrvshiqva dfpgrnepgt gnidfpklls mledrayqgw vgceyrprts
      241 tldgleelrr imkphphedd rw
//
LOCUS       WP_007950801             118 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Pseudomonas].
ACCESSION   WP_007950801
VERSION     WP_007950801.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (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   3  (residues 1 to 118)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 118)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            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=12613
     Region          1..118
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mnepvspgpr ngilsltikd ksvlyaaymp fikngglfip tnksyklgde vfmllnlmde
       61 aekipvagkv awitpkgaqg nraagvgvqf ndgdntarsr iethlagalk sdrpthtm
//
LOCUS       WP_007950815             291 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Pseudomonas sp. GM25].
ACCESSION   WP_007950815
VERSION     WP_007950815.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM25
  ORGANISM  Pseudomonas sp. GM25
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Pseudomonas sp. GM25"
                     /db_xref="taxon:1144327"
     Protein         1..291
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31741
     Region          13..262
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mtwtavtehr aqlgegpfwd aptqalywvd iagkqalrli aqnvqiwqmp ehvsafipca
       61 sgdalvtlss gvyrldldsp gleprltlfc vadpqpgnra nearcdgqgr lwlgtmqnni
      121 geqgedlpit rrsgglfrvd pdkrvtpllr glgipntllw sddgttllfg dsldstlyry
      181 fihtdgnldt aqpwyradqh ggpdgsamda eghvwnarwd gscllrltpd gqidrkidlp
      241 isrptscvfg gadlktlyit saksplnhpl dgavlsmrvd vagklctrfa g
//
LOCUS       WP_007950970             812 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: Lon protease family protein [Pseudomonas].
ACCESSION   WP_007950970
VERSION     WP_007950970.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 812)
  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 812)
  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 812)
  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   4  (residues 1 to 812)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..812
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..812
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88972
     Region          65..800
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mpdpvaaslr lapealtrpf saeqfsfttt ndlepfrgvl gqeravealq fgvamprpgy
       61 nvfvmgepgt grfsfvkryl kaegkrlqtp adwvyvnnfd eprepralel psgsaaafig
      121 dinglidnll stfpavfehp syqqkksaid rafnqrydka ldvierlale kdvalyrdss
      181 niaftpmleg kaldeaefaq lpeaererfh edisgleerl neelaslpqw kressnqlrq
      241 lneetitlal qpllaplsek yaenaavcgy lqamqvyllk tvveqlvdds ktdavarkll
      301 eeqyapslvv ghpasggapv vfephptyen lfgrieyttd qgalyttyrq lrpgalhran
      361 ggflileaek mlgepfvwda lkralqsrkl kmesplgemg rfatvtlnpq hiplqvkvii
      421 igarqlyytl qdldpdfqem frvlvdfded ipmvdesleq faqllktrts eegmapltad
      481 avarlatysa rlaehqgrls arigdlfqlv seadfirhla ndemtdaghi eralkakatr
      541 tgrvsarild dmlagiilid tdgaavgkcn gltvlevgds afgvparisa tvypggsgiv
      601 dierevnlgq pihskgvmil tgylgsryaq efplaisasi aleqsygyvd gdsaslgeac
      661 tlisalsktp lkqcfaitgs inqfgevqav ggvnekiegf frlcearglt geqgaiipqa
      721 nvatlmldek vlaavragqf hvyavrqade alsllvgepa gepneegefp egsvnarvve
      781 rlrviaemis eedlkeaeke laqealaeak pa
//
LOCUS       WP_007951909             325 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pelosinus fermentans].
ACCESSION   WP_007951909
VERSION     WP_007951909.1
KEYWORDS    RefSeq.
SOURCE      Pelosinus fermentans
  ORGANISM  Pelosinus fermentans
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Sporomusaceae; Pelosinus.
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   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   4  (residues 1 to 325)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Pelosinus fermentans"
                     /db_xref="taxon:365349"
     Protein         1..325
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=36493
     Region          6..313
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 martaiefrn vskqyantsq yavagvnmri segsfitilg tsgsgkttll kmvnriyeat
       61 sgeilyfges iknlkleeyr rkigyviqqv glfphmtvee nigtipqilr wdtdaiakrv
      121 dallelvcls prefkkrypr qlsggqqqrv glaramaadp dimlmdepfg aidaitrqnl
      181 qeeliriqrk lnktilfvth dvseafklgd kvvimhegei qqfdtpygii skpaneyvar
      241 liatqdivqr lkvlkaqsvm lpvdaqvsdr afrvgteesl hniltyfleh dqnhvlvedg
      301 grgvvgkitw eqlkvstrqg kilsa
//
LOCUS       WP_007952461              99 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Pelosinus fermentans].
ACCESSION   WP_007952461
VERSION     WP_007952461.1
KEYWORDS    RefSeq.
SOURCE      Pelosinus fermentans
  ORGANISM  Pelosinus fermentans
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Sporomusaceae; Pelosinus.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Pelosinus fermentans"
                     /db_xref="taxon:365349"
     Protein         1..99
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11119
     Region          7..95
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mdcalndtli hsiqaigrey aikrivlfgs rargdnksts didlavyplp efkskgyfss
       61 eiddlatlfk idvifidnht dikllenikk egvviyerl
//
LOCUS       WP_007952803             334 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM25].
ACCESSION   WP_007952803
VERSION     WP_007952803.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM25
  ORGANISM  Pseudomonas sp. GM25
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  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   4  (residues 1 to 334)
  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 334)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Pseudomonas sp. GM25"
                     /db_xref="taxon:1144327"
     Protein         1..334
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37878
     Region          22..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          248..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkeptslasw tralrkqlda lgldstalcq qagldpqlmd dpnaryplsa ttrlweiavq
       61 vsgdpaiglr vsrfvspttf halgyalvas gslrevferi vryhqvvsda leleltrted
      121 ryrfrlkipt dnpapafeai dafaaiyvrt crnrlgrdya plavylrrpe padahqwhkv
      181 frspvhfsae edriefaltd fdshlddanp elaehneavl krtlaqlkpl twerkvrdai
      241 eeqlpegeps aeriaqalhl slrslqrhla degcrfdtll nesrenlall hlrdpqcsls
      301 evsyllgfad tssfsrafkr wtgmtpgqfr dqlr
//
LOCUS       WP_007953344             399 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Pelosinus fermentans].
ACCESSION   WP_007953344
VERSION     WP_007953344.1
KEYWORDS    RefSeq.
SOURCE      Pelosinus fermentans
  ORGANISM  Pelosinus fermentans
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Sporomusaceae; Pelosinus.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 399)
  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   5  (residues 1 to 399)
  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   6  (residues 1 to 399)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 399)
  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 20170230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Pelosinus fermentans"
                     /db_xref="taxon:365349"
     Protein         1..399
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42945
     Region          <9..>58
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          <150..387
                     /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 mansfklgss ndaltlnvir rqgpvsrvei skmtgltppt vtnittklle lgliaedrig
       61 essggrrpll lkinsllatv iivyirserm igyvidpefq iqledsrsik gkkedeilkm
      121 lldiisdcrk gagvpvlavg vvvrgpvrrk dgiavfvpni gwrntplkgi ieehiglpaf
      181 iendvkalsn geyyygsvkd aksmillkvs hgigggiifn gslyrgvnds agevghttid
      241 iagpicscgn ygclealase nalvdavaka ikegqssiiy dmvkgelkdl tpeviykaad
      301 agdelairml gqvarylgig ianlvntfnp eiliigggia rgrqyiediv rqivedrsfe
      361 sssnvleisf lttttentlk gaadivfaei tesiwlgqr
//
LOCUS       WP_007954995             384 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Pelosinus fermentans].
ACCESSION   WP_007954995
VERSION     WP_007954995.1
KEYWORDS    RefSeq.
SOURCE      Pelosinus fermentans
  ORGANISM  Pelosinus fermentans
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Sporomusaceae; Pelosinus.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Pelosinus fermentans"
                     /db_xref="taxon:365349"
     Protein         1..384
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42911
     Region          1..269
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          266..356
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrflhtsdwh lgrlfhgihl tndqahvldq flalvreskp dgiiiagdiy dravppieav
       61 ellnqlisqi lvdykvptim iagnhdsaer lgfgsrllaa qglyvagals reiepiilyd
      121 ehgpvyfapl tygepafvre rlscpdvsnh eqaieamvqh virkipnkar svaiahafia
      181 ggmeseserp lsiggssmvn gavfqpfcyt alghlhnsqq agnpsihysg sllkysfaea
      241 sqrkgihlie mdkvggitve riplsprrdv rcikgyfkdi ldhsidegnq qdyvsvtlld
      301 empildamgk lrekypnvlq iesprflkkg vlsglpkdhr klsekelfaa fyhqmtgenm
      361 tqeqqmhlvn vietvyreer eail
//
LOCUS       WP_007935075             521 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type I restriction-modification system subunit M
            [Pelosinus].
ACCESSION   WP_007935075
VERSION     WP_007935075.1
KEYWORDS    RefSeq.
SOURCE      Pelosinus
  ORGANISM  Pelosinus
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Sporomusaceae.
REFERENCE   1  (residues 1 to 521)
  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   2  (residues 1 to 521)
  AUTHORS   Youell,J. and Firman,K.
  TITLE     Mechanistic insight into Type I restriction endonucleases
  JOURNAL   Front Biosci (Landmark Ed) 17 (6), 2122-2139 (2012)
   PUBMED   22652768
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Sistla,S. and Rao,D.N.
  TITLE     S-Adenosyl-L-methionine-dependent restriction enzymes
  JOURNAL   Crit Rev Biochem Mol Biol 39 (1), 1-19 (2004)
   PUBMED   15121719
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Murray,N.E.
  TITLE     Type I restriction systems: sophisticated molecular machines (a
            legacy of Bertani and Weigle)
  JOURNAL   Microbiol Mol Biol Rev 64 (2), 412-434 (2000)
   PUBMED   10839821
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114514
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Pelosinus"
                     /db_xref="taxon:365348"
     Protein         1..521
                     /product="type I restriction-modification system subunit
                     M"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=58542
     Region          8..142
                     /region_name="HsdM_N"
                     /note="HsdM N-terminal domain; pfam12161"
                     /db_xref="CDD:463478"
     Region          162..420
                     /region_name="HsdM"
                     /note="Type I restriction-modification system, DNA
                     methylase subunit [Defense mechanisms]; COG0286"
                     /db_xref="CDD:440055"
ORIGIN      
        1 mlqnnaalks kinqlwdkfw sggisnplta ieqityllfm kqlddldlkr iadadftgek
       61 ytskfdgkik lsgteqkvdk qtlrwshfkq mpaeemlshv qmkvfpflkm lngdespfth
      121 hmqnavfiip kpallveais tieeifaeie kdaneggqaf qdlqgdvyem llseiasagk
      181 ngqfrtprhi ikliaelvep klgnliadpa cgtggfllga yqymvtqldk nkkniqpded
      241 gfirnsvsgl lnkkvsdiln dslygydidv tmvrlglmnl mmhgvdtphi dykdtlskgf
      301 tesnkyqiim anppftgsid kgdineafkl gttktellfv eniynllkmg gtagvivpqg
      361 vlfgsgkafv earkilvekc elkaviamps gvfkpyagvs tailiftkgg etekvwfydm
      421 qsdgyslddk rtkqegygdl qdivaqfkkr dqrkesdrke kfffvlkgei vtenydlsms
      481 kykedvfeev vyekpdvila klktmegein qelaelegml e
//
LOCUS       WP_007953403             276 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM25].
ACCESSION   WP_007953403
VERSION     WP_007953403.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM25
  ORGANISM  Pseudomonas sp. GM25
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 276)
  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 276)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 276)
  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   4  (residues 1 to 276)
  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 276)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Pseudomonas sp. GM25"
                     /db_xref="taxon:1144327"
     Protein         1..276
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30492
     Region          20..276
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <170..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 msdqgesirf wqaaplagve lltaryiehr faphvhdgyv igmimagaqr yryrgaehla
       61 gsgtlvlinp devhnghkgt ddgwlyrafy pdtgqivall nelelptapm pafgatlyrd
      121 pdlvngfcql hrllespata lqqqtvwrem mmlllqrhaa vqingnpgke hravamakel
      181 lhaqlaapps leelaaavnl spfhfarvfr ratgmpphsw lmqqriacar gllqsgclpv
      241 evatqlgfad qshlsrqfkq vygvgpaayr sarldr
//
LOCUS       WP_007955008             816 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pseudomonas sp. GM25].
ACCESSION   WP_007955008
VERSION     WP_007955008.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM25
  ORGANISM  Pseudomonas sp. GM25
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 816)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 816)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 816)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..816
                     /organism="Pseudomonas sp. GM25"
                     /db_xref="taxon:1144327"
     Protein         1..816
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=88854
     Region          12..816
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 maspalshfl prfgvaaava gvlsltgcqt wnaqdtlppt sgvqplkgla qnvsvrrnam
       61 gmpliesnsf hdalfalgyv hasdrinqmv tlrllaqgrl aemsgssmld adrymravnl
      121 kksagelyka ssprlkrffe vyargvnayl fryadklpgd lassgykpey wkpedsalif
      181 cllnfsqsan lpeeiaslvl aqtvtndkla wltpsapden lplaeadklq giklngqipg
      241 ltelsnasek laainllgtq ssnnwaiapq rsrsgkslla sdshgplaap slwsfvqira
      301 pkyqaagvtv aglpmvlggf ngkvawslts vlgdnqdlfl ekirrqgstl syevngkwqp
      361 vavrnetyfv kgqrpireav yetrhgalln stqaaaqgag fglalqtpsf tddksldaff
      421 dlsraqnver asdasreira ialnlvfada snigwqvtgr fpnrregegl lpspgwegry
      481 dwdgyadpml hpydqdpsqg wlgtanqrvi phgygmqlsn swaaperger laelagsgkh
      541 dgrsviamqy dqtttfaakl kkmfeapgma qplkqaidal peaerskare aytrlmafdg
      601 klsptsadaa iyelflqesm kqifldelgp qgspawkafi angdlsyaaq adhllgreds
      661 pfwddartpq kedkpailar slaaaisagd sqlggdrrtw qwgklhryew knasgqtvrg
      721 piaaggdhtt lntaafawgq dfntmrapsm rfivdfgqne plmgqngtgq sgnpvspnyl
      781 ngidpwlkgq yiglpmqpqn fdrvygktrl tltpgk
//
LOCUS       WP_007956220             369 aa            linear   BCT 20-JAN-2025
DEFINITION  GerAB/ArcD/ProY family transporter [Pelosinus fermentans].
ACCESSION   WP_007956220
VERSION     WP_007956220.1
KEYWORDS    RefSeq.
SOURCE      Pelosinus fermentans
  ORGANISM  Pelosinus fermentans
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Sporomusaceae; Pelosinus.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Pelosinus fermentans"
                     /db_xref="taxon:365349"
     Protein         1..369
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=40582
     Region          5..362
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 mndlhpgklg vadgialvfg ivmprvflst isnliqqdgp ilwlamviyt iipliilymm
       61 ayvhkgitgd ifivcqklig tigawgills ysimflsnga lilrlyseyt lltalprvef
      121 qvvivwyavs agilcylgie altrtsyivm pfsiaaigmi llllipfyiv ynltpwqgng
      181 vmqavqtgik gagynvgvla lvflapafqn trtikkaaly alsyagmlrv sfilvytmvf
      241 gnavgaektm plfelarlvy lnqylqriea lfivvwvvfg llavagslyv glyllavllk
      301 lptlrpivpl gailianlam mppdigyvle vdqklitlfd vgiyvfptll fimawwkkrr
      361 gklctsass
//
LOCUS       WP_007957899             295 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Pelosinus fermentans].
ACCESSION   WP_007957899
VERSION     WP_007957899.1
KEYWORDS    RefSeq.
SOURCE      Pelosinus fermentans
  ORGANISM  Pelosinus fermentans
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Sporomusaceae; Pelosinus.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Pelosinus fermentans"
                     /db_xref="taxon:365349"
     Protein         1..295
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33329
     Region          3..269
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mnkidlhihs nhsadgelev qeildiskrq glntiaitdh nsvkgieaai hygnqlnidv
       61 ipgieidcsy hsvnlhllgy fidwkrkefi dleenlynqe maafpkmirk lraagivade
      121 deilkeaagk vpcgeligev llhkenakkn pmlrpylegg ersdmpylnf yrdffaqgki
      181 ahvplqylql keaielvkns ngipiiahpg dnlkdkmdml ddiiqegvmg ievfsnyhtp
      241 gqieffykka teeslfitcg sdfhgknkpg itigacncqf eieplrrpkd klenr
//
LOCUS       WP_007958788             211 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase family protein [Pelosinus].
ACCESSION   WP_007958788
VERSION     WP_007958788.1
KEYWORDS    RefSeq.
SOURCE      Pelosinus
  ORGANISM  Pelosinus
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Sporomusaceae.
REFERENCE   1  (residues 1 to 211)
  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 11465564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Pelosinus"
                     /db_xref="taxon:365348"
     Protein         1..211
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=23448
     Region          21..80
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          105..209
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mnvrtlylsh rlasiafeee sehpligeiq qlllhknlyq gpihqkydtq tirgitlfqe
       61 kenlpatgiv dpltycrlhq attttittls paakradfsl pranilitts srqltlfngn
      121 tpmhqypvgi gklttptplg nyaialkvmn pggvlgtrwl glnydsygih gtnrpwligt
      181 mvsngcirmh nqnveqiypl vkvgtpvyir n
//
LOCUS       WP_007959372             255 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Pelosinus].
ACCESSION   WP_007959372
VERSION     WP_007959372.1
KEYWORDS    RefSeq.
SOURCE      Pelosinus
  ORGANISM  Pelosinus
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Sporomusaceae.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Pelosinus"
                     /db_xref="taxon:365348"
     Protein         1..255
                     /product="formate/nitrite transporter family protein"
                     /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=27459
     Region          2..253
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 myyeeikkvs saaqakgall kgspikylls svlagmyvgl gilliftigg llsqadspav
       61 kiimgtsfgi alslvimags elftgnniim tigrmekkvt isevftihil sfignllgsf
      121 llaslfilsg lgqgstamlm vkiahskvsl pwmellargi lcnilvclai wcsfkmkeea
      181 gklimifwcl fafittgfeh svanmtllsa vlimpgadav slldfiynis wvtlgnmigg
      241 iffvalpywy iskqs
//
LOCUS       WP_007960772             811 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas sp. GM30].
ACCESSION   WP_007960772
VERSION     WP_007960772.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM30
  ORGANISM  Pseudomonas sp. GM30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 811)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 811)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 811)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..811
                     /organism="Pseudomonas sp. GM30"
                     /db_xref="taxon:1144328"
     Protein         1..811
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89553
     Region          63..113
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          91..811
                     /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 mrlptfrqrf shhciaysll mtsaasclam thnafaatva qrytiaagpl dnalsqfast
       61 anvilsfspq qtnrlrstgl ngnftveqgf aqllqgsglq avpqapgsyi lqalptgdsl
      121 elaptningq lanpmdldya advgykaqns rigtktstpl setprsvsvv taqrmkdqks
      181 qtltevlgyv pgifappfaa gdslagdlff irgfnatdyg ygllrdglrv qgnrydtste
      241 pyglerveif rgpssllyge napgglvnlv skrptaaprg evqlgygsnn rrqigidvsg
      301 plndsgnvlg rvvmlgrksd tqtdhvpddr iyiapsltln fddfntltll anyqkdhtnm
      361 elglpaagtl lsnpngklsk gtmlgdsdwn tferetwstg yefshsfndd wqfrqnsrym
      421 qsritrhetw pgnlnnagfg trlnmtaydr fnksmvysld nqlegrfqvg elentvlfga
      481 sydrtsfnqd wnagivgpid iynpvylrdp ttpiavqntl leqqmkgvya qlqskydhwl
      541 fllggrqdwv dsdfrdkvak gsnissedkk ftyqggvmyq fdngmtpyvs ystsfvpvqq
      601 isnagapldp itssqyevgl kyepigwdta ftasvydlrk kddtyfdstt styrqvgesr
      661 skgvelelns nltqnlnvta aytytdarit kdaatslvkg hqmtgvprnq asvwtkyrfl
      721 dgdlkglyvg ggvryfdsaf aytspslygk ldagdvtlvd aaigyqidth wsvdlnaknl
      781 fdreyvsgcn dagrcywged rtllgtvsyn w
//
LOCUS       WP_007961128             386 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Pelosinus fermentans].
ACCESSION   WP_007961128
VERSION     WP_007961128.1
KEYWORDS    RefSeq.
SOURCE      Pelosinus fermentans
  ORGANISM  Pelosinus fermentans
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Sporomusaceae; Pelosinus.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Pelosinus fermentans"
                     /db_xref="taxon:365349"
     Protein         1..386
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=40512
     Region          <1..385
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mnfmgyrrkn gtvgtrnyvg ilsavvcvne vvenivrqvq gtarfthhqg ccqtmldigi
       61 vnrtltalgk npnlhsvili slgcestnlt eviegirtsg krvehlvvqe tggatrttae
      121 aillaqamvr easlqerepf piselvlgmk cgssdttsgl vpnpaigvas dllvaaggts
      181 ilgevtefig aehilanhav netvaqgife lvdrmekram avgedirggq ptggnikggl
      241 ttieekslga iakagtapiq avyeyggrpt vkglvvmdsp grepeiltgl aaagcnvivf
      301 atgrgapqgf pfvpvlkitg srtavekmsd hidmdlsavi dggdtipdag erilkelvri
      361 gsgtmtkaei fgyvnsmdiy mqgpvi
//
LOCUS       WP_007961277             495 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Pelosinus fermentans].
ACCESSION   WP_007961277
VERSION     WP_007961277.1
KEYWORDS    RefSeq.
SOURCE      Pelosinus fermentans
  ORGANISM  Pelosinus fermentans
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Sporomusaceae; Pelosinus.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Pelosinus fermentans"
                     /db_xref="taxon:365349"
     Protein         1..495
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=53166
     Region          1..495
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mllnrinshd nvavaieelt agetylvgsm avtatatipk ghkialenip vganiikygf
       61 pighaiqeva mgdwvhshnv ktnlgdiley qyrpvgeesk seslprtfkg yprangkvgv
      121 rneiwvvptv gcvnrtaqli argasekfqa vkhidgiyef thpygcsqlg edhtstqril
      181 adlvnhpnaa gvlvlglgce nnyieefkkv lgpydanrvk flvaqdvede vesgikaiye
      241 lieqtakdqr vdcsiselvv glkcggsdgf sgitgnplvg efsdklgasg gtsvltevpe
      301 mfgaetilmd raineevfgk ivhlvndfkk yyedhnqpiy enpspgnkkg gittleeksl
      361 gctqkggrsq vvdvlgygdv vknkgltlls apgndivaat alaasgcqii lfttgrgtpl
      421 gtavptmkia tnsdiftrks nwmdfdagvl legqsmedta ekllqqvidv asgsltksek
      481 mgfrdiaifk ngvtl
//
LOCUS       WP_007961891             301 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Pseudomonas sp. GM30].
ACCESSION   WP_007961891
VERSION     WP_007961891.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM30
  ORGANISM  Pseudomonas sp. GM30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Pseudomonas sp. GM30"
                     /db_xref="taxon:1144328"
     Protein         1..301
                     /product="formate/nitrite transporter family protein"
                     /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=32919
     Region          24..274
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mttptdgktp nlstdeqhev eknqppraav lheiirtqgd qelersiaal wwsalaaglt
       61 mglslmgmgl lnsrlpegde fkviasfgyc agflavilar qqlftentlt avlpvmtkpt
      121 lknfgrlirl wgvvlfgnlc gtilvayvml elpifdtktd hafleigrkv menhasqmfa
      181 kgivsgwmia tmvwmipsme sakmwiiili tylmalgdft hivvgsaevs ylvfagelpw
      241 sdfwmvfagp tlagniiggs fifalishaq irsesgapke tgkgkqsadq aekpdpqqik
      301 k
//
LOCUS       WP_007961920             117 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Pseudomonas sp. GM30].
ACCESSION   WP_007961920
VERSION     WP_007961920.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM30
  ORGANISM  Pseudomonas sp. GM30
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Pseudomonas sp. GM30"
                     /db_xref="taxon:1144328"
     Protein         1..117
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12708
     Region          10..112
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(16,34..35,43,46,48..49,51,54..55,57,65,70,81)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(34,65..66,68,94)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mkepnhpdes eaqirrtaly stlaqvpegk vvsygqlael aglgraarwv grtlsqlpgd
       61 tklpwhrvlg aggrislplg spsgdeqrar lrsesvtvln nrvdiqrhgw rpvehsg
//
LOCUS       WP_007962002             833 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas sp. GM30].
ACCESSION   WP_007962002
VERSION     WP_007962002.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM30
  ORGANISM  Pseudomonas sp. GM30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 833)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 833)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 833)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..833
                     /organism="Pseudomonas sp. GM30"
                     /db_xref="taxon:1144328"
     Protein         1..833
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=91099
     Region          75..123
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          102..833
                     /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 mtvrltcknp lnftaesgll rhairaalls tvlgagalpg islaantsea sshryniaag
       61 plgealnqfa rqagitlsmt pqqtqgrqsp gvqgeystdq alshllsgsg lealsqdgss
      121 yilhsvsdsa alalpttdik gfalgnalgs megynathsq iatktstall etsqsvsvvt
      181 reqmddqgsq tvsqamrytp gvltnpygat hrydyvamrg fndgsvdniy ldglksmgds
      241 gtystmqvdp yflervdilk gpssvlygrs spgglvalts kkplyeayhq vqatvgtqgq
      301 rgvgfdfsgp vdddkriayr ltgltdqsdt qfdhnkekrf alaptlsidf tedtsltlqa
      361 ylqhdpdggy hggvpadgti hqrngnrisp hffegepgid gysrdqqsfg yqfehrfndv
      421 ftarqnfryl dskvnmdqvy aygwttptsn elnryytggd erlhafivdn mlqaefftga
      481 tkhtvlmgad yqrrktvvdw tsgglapina fnpvygnsai dmygetsylr rleqtgvylq
      541 dliemdqwrf slglrqdwve tsdenriaea grpvgteind rrtkltgrag alylfdngla
      601 pyisysesfn pnsyadsagn plpptdgtqw evglkyqppg tdnlftaslf ridqenlatk
      661 lpqenfyrav gavrsqglel eahmqvtdnl kvlgsytftd ieysksmvst lstptdvien
      721 kgnsptqapr hmaslwadyk fdsaaldglr lgggvryvgy swadaentlk vpsytlfdas
      781 igydlgkigl kgvdvrlnan nltnesyvas caslnfcymg eernvaatvs yqf
//
LOCUS       WP_007962269             331 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM30].
ACCESSION   WP_007962269
VERSION     WP_007962269.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM30
  ORGANISM  Pseudomonas sp. GM30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 331)
  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   6  (residues 1 to 331)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Pseudomonas sp. GM30"
                     /db_xref="taxon:1144328"
     Protein         1..331
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36903
     Region          23..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          95..329
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mlhshlttln avslvlntfk aeglssdall agsgisaadl aradtrittn qemqvcanav
       61 alkhdiglel grrmhvscyg ilgyalltsa tlgdalrlai rypallgtlf elrleddgeq
      121 vwfvaadyre spsmavfnae fclvslkvic ddllghplpl latrfehtap dyrdsyaehf
      181 dsplhfaakd nafafdrrwl dqplpladsi thqamadrcr kqnieftgrq awlgrirqll
      241 saqlnaapgl eglaqqmkcs prtlrrhlkd mgssyqelld elrferakqm lcedqlpiyr
      301 iaetlgfset asfrhafvrw sgvapsqfrp h
//
LOCUS       WP_007962467             142 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: pilin [Xanthomonas].
ACCESSION   WP_007962467
VERSION     WP_007962467.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..142
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14397
     Region          2..141
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkkqqgftli elmivvaiia ilaaialpay qdytirsrvs elavmassfk ttvaeniann
       61 ggtlpadacv gvgataattn masiactpat gnivvtgdat rtkgtvltya ptvgaansav
      121 gttwtctgsg sqskyypaec rr
//
LOCUS       WP_007962735             259 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Pseudomonas sp. GM30].
ACCESSION   WP_007962735
VERSION     WP_007962735.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM30
  ORGANISM  Pseudomonas sp. GM30
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Pseudomonas sp. GM30"
                     /db_xref="taxon:1144328"
     Protein         1..259
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=28731
     Region          26..175
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkffallasl lvlagcaggp rydtshpsan hdsrvqfviv hytsaslars lqllthgevs
       61 shyligddks atiyklmden qrawhagesq wqgrtwlnss sigieivnpg fkdtptgrlw
      121 fpyseaqiqs livllkdisq rqgisprhii ghsdiaplrk ldpgplfpwk rlaaeglgvw
      181 pneqavarqq vqfnaelpsi swfqeqlarv gydtpqtgel dvatrhvlaa fqmhfrpsrf
      241 dglpdaqtaa lllvlnqtk
//
LOCUS       WP_007963436             338 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM30].
ACCESSION   WP_007963436
VERSION     WP_007963436.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM30
  ORGANISM  Pseudomonas sp. GM30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  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   4  (residues 1 to 338)
  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 338)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Pseudomonas sp. GM30"
                     /db_xref="taxon:1144328"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38137
     Region          23..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          252..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msekdtiavq lvreallqsc apgvatdevl nkvgiapall hseqgrvpas qyaklwrlla
       61 rrgddeffgm dprrlksgsl eflcrsamtq ptlaaglgmg lnflslmlek mpaqlahqqs
      121 laeivlledd peprraftyf tywmivhgva cwlagrripi laielrcaep dfcddyrvmf
      181 senlrfdrpr trmifaadcl dlpikrtaee lkrflahapa nilvkyrdpe slasrikqdl
      241 rqlpaeqwpe tealaqqlcm sastlrrrls eegqtyqglk dsvrkelait wlaepsisfv
      301 eiatrlgfad assfykafrk wsgsnpghyr tlilneav
//
LOCUS       WP_007963855             669 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Xanthomonas].
ACCESSION   WP_007963855
VERSION     WP_007963855.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 669)
  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   3  (residues 1 to 669)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..669
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=71327
     Region          1..669
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdmnqlmqtf laesrdlled merhlleaer gepspdavna ifraahtikg sgglfdlpql
       61 vgfthvvesv ldlvrdeals lsseliglll vccdhihalv etaadpshad pvalaaeaep
      121 llaqlqtylq rsacgvtata vaqgapekqs gywritlklf adalrfgnsp lklirnlrsl
      181 gsvesintdi sqlpafddld peanylgfqi llrsdadraa ieevfefvre dcdleivsvp
      241 apsdaaellt aeaaaspvpn kplaavpsaa sapgraapda aarnadarsi rvdadkldrm
      301 idlvgeliia vsstnanaqr tgdaqllesa silaglvedv resalqlrmv kiggtfsrfq
      361 rvvhdvarel gkdialvvag edteldksvv ekigdplthl vrnamdhgie padvrvargk
      421 pargtvglna yhdsgsiviq itddggglnr drilakaler gliepgrqls drdvfamife
      481 pgfstaekvt nlsgrgvgmd vvkrnitalr gtveidsaag vgttisvrlp ltlaiingfq
      541 vgvgksvfvv pldvveecve ftpdyasdyi dlrgsvlpyv rlrelfalgg ktpsresivv
      601 irqgaqrfgl vvdtllgewq tvikplskvf aqvkgisgss ilgsgdvali ldvpsliqql
      661 hpnqdalaa
//
LOCUS       WP_007964813             408 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Pseudomonas sp.
            GM30].
ACCESSION   WP_007964813
VERSION     WP_007964813.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM30
  ORGANISM  Pseudomonas sp. GM30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 408)
  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 408)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Pseudomonas sp. GM30"
                     /db_xref="taxon:1144328"
     Protein         1..408
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45952
     Region          2..403
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mpatlafslk qarrlalaaq gfngrqpptv kapqlnrlie rlgllqidsv navvrshylp
       61 lfsrlgsyss dlldqaawss grrrtlfeyw gheasllpla myplmgwrmq rarngrdihq
      121 qlakfgleqq dvvrrvlsav eargalgags lstredkagq wwdwsaekha lewlfaagev
      181 tvagrrgfer lydlpervip ssilqqalpn eaeaqrglll haaqalgvgt ekdlrdyfrl
      241 npgdarprla elvedgqlqt cevagwrqia yclqqpkvpr kvvasallsp fdsliwersr
      301 terlfdfryr leiytpqdkr vfgyyvlpfl hneriaarvd lraeraagrl avhavheeap
      361 gldeegmlal alnlrqmadw lglarvqlnc qresagrlrv alaeicsd
//
LOCUS       WP_007964914             713 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Xanthomonas citri].
ACCESSION   WP_007964914
VERSION     WP_007964914.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas citri
  ORGANISM  Xanthomonas citri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Xanthomonas citri"
                     /db_xref="taxon:346"
     Protein         1..713
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=79126
     Region          46..713
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mstfrfhala iaiaastltl pqltrasdtp ttdvldasgg gtpiraldai qvqgsllgrs
       61 kpddvqryag srqvidreql rnggnrsldd alqrvpgiki fdetgtgalp qlmlrglyes
      121 rsgrvqvled giplalapyg qtslslfpvg lnqidridiv rggaavqygp nnvggvinlv
      181 skeipsawst tlahkvtagg hgqflqdsal ssggyltdnf gmqvdanrty geywrahsdt
      241 disnlrvrae wwlddtkllk asvqrylvdm dlagalspdd yrrdprqstr pldsfngrtt
      301 raslnyeqll gdwgpmqdvr ldwsnfsars srnfivgmrq astetwrsdl ppqlrqtapr
      361 dfrvvgsepr lswsmgdagg vrqqwtagvr avredidflv gnlrlsdglf ttvrdwrfed
      421 ralaayvsna itlpgervti tpglryerld sryfnratgv stlnqtrdvl pgltvgfqat
      481 eqwffyadgq rsmrapqvtq iifgnnldae lawnyeagar yqpnertrvq lggylidfdq
      541 qiqldnttrv frnlgktrhq ggelelqwsp eqlraltlna syayldasqe sgafrglrvp
      601 ytsrnqitlg gtyalghttv alsgyyfska fsdaantvqe naiasvgqlp aymvwntqvs
      661 htlferdgqk fsaslainnl fdrhywfrgv dtspwgrqaa partvtagle ytf
//
LOCUS       WP_007965506             248 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Xanthomonas citri].
ACCESSION   WP_007965506
VERSION     WP_007965506.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas citri
  ORGANISM  Xanthomonas citri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 248)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Xanthomonas citri"
                     /db_xref="taxon:346"
     Protein         1..248
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=27123
     Region          20..237
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mttlpvcnac rdgqdfptai tmafqpivdv strsiyagea lvrgingesa gsilaavder
       61 nryafdqacr ikaiecaaqi alpallsinf mpnavynpeh clratlaata qygwplnaii
      121 fevseqehla dpahllgilr tyqargmkta iddfgagyag lgllaefqpd llkldialvr
      181 gidtdrsrqa ivrhvtrmce elgiaviaeg iehpdqyrtl rdlgihlqqg ylfarpqige
      241 lpkvhwpe
//
LOCUS       WP_007965868             309 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Pseudomonas].
ACCESSION   WP_007965868
VERSION     WP_007965868.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 309)
  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 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   3  (residues 1 to 309)
  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   4  (residues 1 to 309)
  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 309)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..309
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34541
     Region          39..191
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          219..298
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtsfdrfqsp pdadmekqra elaaiirrnt tddgsyqtai gslfmsrhtk shdfapvlaq
       61 palcimaqgr kevrladeff nydplnylvv svsmplsgrv vnvspedpil avrldidpae
      121 italiadagp mgvptrptgr glyvekidsa mldavlrlar lldapkdiam laplirreil
      181 yrllrspqgh rlyeiaians qshrisqaik wlngnfeqpl riddlakevn lsvstlhhrf
      241 kamtamsplq yqkqlrlqea rrlmlaegle asaagyrvgy espsqfsrey srlfgapplr
      301 dlarlrqsv
//
LOCUS       WP_007965962             332 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM30].
ACCESSION   WP_007965962
VERSION     WP_007965962.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM30
  ORGANISM  Pseudomonas sp. GM30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 332)
  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 332)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 332)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 332)
  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   5  (residues 1 to 332)
  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   6  (residues 1 to 332)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Pseudomonas sp. GM30"
                     /db_xref="taxon:1144328"
     Protein         1..332
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37901
     Region          22..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          79..332
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mrertiashf araalggarr sgfdyapllq qlgispelld eprariapeq ftqliqnlwl
       61 alddeylgfg napskpgsfa mmchalihcr slekalqrgl lfyslfpdap rlslsredew
      121 vrlslddaql wdpdhflses llviwhrlgs wligqrirle qatfsypkpa hgaeydllfp
      181 cplvfsaqqs sllfhsrylh mpllqdertl khflerspad llsrpddgds lssrlrrlls
      241 rdsaqwpdle avaaqlhisp qtlrrhlree gssfqelkdq lrrdiaiyhl gradlslqqi
      301 aeqlgfseps afhrafkkwt gltpgayraq eq
//
LOCUS       WP_007967206             634 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Xanthomonas citri].
ACCESSION   WP_007967206
VERSION     WP_007967206.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas citri
  ORGANISM  Xanthomonas citri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 634)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 634)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 634)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 634)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 634)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 634)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Xanthomonas citri"
                     /db_xref="taxon:346"
     Protein         1..634
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68847
     Region          1..634
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mshtpksags shapansqta lvigaigvvf gdigtsplyt lkeafsphyg ltpdhdtvlg
       61 ilslvfwalm lvvtlkyvtv imradndgeg gimaltalaq rtlpggsrsm yvvgilgifg
      121 aslffgdgvi tpaisvlsav eglevaapkl epfvvpitlv vlsmlflaqr fgtervgkaf
      181 gpitllwffa lgaigvynma rapevlhaln pwwgvrffaq hnwhavfvlg avvlavtgge
      241 alyadmghfg akairrswqf vvlpmltlty lgqgalvlrn paavsnpfye avpewalypm
      301 ivlataatvi asqalitgay svasqamqlg yiprmhirht shstigqiyv pavnwcllal
      361 vavavigfgd saslataygv svtgtmlitt vlmiiyaran prvpapllwl falvflavdc
      421 affyaniikf ldgawfplll glilftlmrt wrrgrkllhd eirkdgikld tflpglmlap
      481 pvrvpgtavf ltadpmvvph almhnlkhnk vlhernvflt vetlqvpyav agkrlkidai
      541 gdefyrvhvr fgfmetpdvp lalmrscdqg giyfdpmdtt yfasretiva sanrgmpiwr
      601 dklfalmhrn aapatgffri pgnrlvelga qvei
//
LOCUS       WP_007967607             118 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Pseudomonas].
ACCESSION   WP_007967607
VERSION     WP_007967607.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (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   3  (residues 1 to 118)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 118)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            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=12601
     Region          4..118
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mneaispgpr ngilsltikd ksvlyaaymp fikngglfip tnksyklgde vfmllnlmde
       61 aekipvagkv awitpkgaqg nraagvgvqf ndgdntarsr iethlagalk sdrpthtm
//
LOCUS       WP_007967878             658 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Xanthomonas citri].
ACCESSION   WP_007967878
VERSION     WP_007967878.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas citri
  ORGANISM  Xanthomonas citri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 658)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 658)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 658)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Xanthomonas citri"
                     /db_xref="taxon:346"
     Protein         1..658
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=70597
     Region          109..643
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 maardpvsst trddtatrnr plraetppad hwrrwadeva spadtavpvs aaiipapaaa
       61 aaaspavavv vpravaasgs arvaaasapt asptsaapta phdgednvaa dapyrvlive
      121 ddrsqalfaq svlhgagmha qvemtaasvp qaiqdyhpdl ilmdlhmpel dgirlttlir
      181 qqpgqqllpi vfltgdpdpe rqfevldsga ddfltkpirp rhliaavsnr irrarqqalq
      241 qageqvsvrs npetglptrg hvmdlladal erkqsgglff ieiasalglr erygyaayer
      301 lmtqaghrla saaqpyplar lndnsfllla vdmpeasleq qaleirqrls anafpvreee
      361 svhvrcaigv aplglgfddt gsaleavert alqarlrsdg vqtylapsqa eqqeqlrlve
      421 gqlelayqpi vavaggdtaq yqvllrlrqa dgtllsagqv ipaaeaagri adldqqvmdh
      481 algllhlyqh aspplrlfvs qsprtlarda fadwllkalv ergvagqsli vdlrlddali
      541 havtvqqfca klmpagvqfc lsqfepgdea nallgqlpls fvrmanrfad ahgnaavrde
      601 lrgvidiahq rglliigqri edpqaaaamw msgvdfiqgn lvqtvgkeld fdftsavl
//
LOCUS       WP_007968234             348 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Pseudomonas sp. GM30].
ACCESSION   WP_007968234
VERSION     WP_007968234.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM30
  ORGANISM  Pseudomonas sp. GM30
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Pseudomonas sp. GM30"
                     /db_xref="taxon:1144328"
     Protein         1..348
                     /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=38420
     Region          2..276
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 msskkkslei etlrglacll lvlyhvigpl ggglkidigs pfrviadsmv yvrmplftfi
       61 sgyiysiyki rgndfsaffs gkvrrllvpl fcvgvpfsvl qavgpgvnkd vgvidallsf
      121 wvpvnhfwfl qavfiifmfv gllewrgmlr smtrlyllfa faaavfllpp fkldafging
      181 aiyllpffva gmigqenvea lkqrfkvigp lvfvlisltl lyvaaidrel ivdrrsligl
      241 tvgcvscial lssdmrskwl twlggysyai flfhvlfaat srfvmgrlgv kdesilvlsg
      301 llfgllgpvv lsmifsrfnv tsvlflgera akkkpaasvt pvvqtqri
//
LOCUS       WP_007969972             140 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Xanthomonas citri].
ACCESSION   WP_007969972
VERSION     WP_007969972.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas citri
  ORGANISM  Xanthomonas citri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Xanthomonas citri"
                     /db_xref="taxon:346"
     Protein         1..140
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15115
     Region          3..139
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mtyfslfvvs liaatllpaq seavlvalll dggsavglva vaslgnvlgs linwwigrea
       61 vrfqgrrwfp ikpnallraq awyrrygkws lllswmpvig dpltlaagvm replravvpl
      121 lvvakttrya vvawatlava
//
LOCUS       WP_007970067             360 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Xanthomonas citri].
ACCESSION   WP_007970067
VERSION     WP_007970067.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas citri
  ORGANISM  Xanthomonas citri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 360)
  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 360)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 360)
  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   4  (residues 1 to 360)
  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 360)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Xanthomonas citri"
                     /db_xref="taxon:346"
     Protein         1..360
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40418
     Region          49..232
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          280..357
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpraraavir rqptsevgka rrapadtrri adivpntvrs llglvedrgh aperlckglg
       61 ftgrdlhdrd lllsyqqvra lilrarrlle epamglaagm rqrpvswglt glamltcetf
      121 geaiayglgh qheagammqh lfaqqgpeas ielvphvfdl eiepylieea fagalnvsrc
      181 mlgpdirpra velafarsap leiytrffrc pvrfgagrnr mtleakwlaa rlpgydrttc
      241 gllrqqletl iqrppwrnel vesialrlrs daeraprqpe larqancser tlrrrlgaqq
      301 vgyralrdaa ryeraqdllr nsqmtvaeva qavgyadara frrafqrwsg rspgqaresh
//
LOCUS       WP_007970320             256 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Pseudomonas sp. GM33].
ACCESSION   WP_007970320
VERSION     WP_007970320.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM33
  ORGANISM  Pseudomonas sp. GM33
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Pseudomonas sp. GM33"
                     /db_xref="taxon:1144329"
     Protein         1..256
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=28444
     Region          5..172
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkpinynhyr strsfnsrir flilhytaan fsgsvstltg pnvsahylvp ditdpsylka
       61 gysgqevfnl vdeshrawha gvsqwgnrsn lndtsigiev vnlatdnkgq ftfppyhpeq
      121 iaaieqlaln ilkrypditp tqvlghsdis igrksdpgpm fpwqalylkg vgawfdeatr
      181 dqylsqytts gvpgrsellg lfksygydvs gasteggfqq lvrafqmhfr pekfdgkmda
      241 qtaanlkalv fkyfsg
//
LOCUS       WP_007970781             552 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Xanthomonas].
ACCESSION   WP_007970781
VERSION     WP_007970781.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 552)
  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   3  (residues 1 to 552)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..552
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=59283
     Region          6..547
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msavpddiaa dfiveaqeil drlgeqlvsl eqapeeadql navfrgfhtl kggagflaik
       61 pmvelchaae etlgmarsgq avlqahhfda aqqsldylqa mldamgsgea vphapatlia
      121 qfdaksappv lkaapqaaaa kpvaaahgdd ahapapkagg kgaaktgaea eqtvrvdtkr
      181 ldaivnlige lvlsrnrlkt lrtrlrdeel dravstldia tarlqtavmr trmqpvskvf
      241 arfpkvardv artlskevel eligaeteld rnlvealadp lvhlvrnaid hgiespalre
      301 atgkprsghv rlsaqqegdy vsieiqddga gidperlrei arnkglidae aaarlstdec
      361 lhlifmpgfs tkvevtdisg rgvgmdvvqs rirelsgqiq iqselgrgsr fmirvpltla
      421 ilptllvqag eavyalplar vvevlhapqt slgwfdgrav ldrrshtlpl idlrrwlgvp
      481 aeqpplltvv llqagetrfg lvvdqvrgre evvikplpra lrglpgyaga tligdgrmal
      541 ildvdglrss dh
//
LOCUS       WP_007970894             248 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Xanthomonas].
ACCESSION   WP_007970894
VERSION     WP_007970894.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 248)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..248
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=27169
     Region          20..237
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mttlpvcnac rdgqdfptai tmafqpivdv strsiyagea lvrgingesa gsilaavder
       61 nryafdqacr ikaiecaaqi alpallsinf mpnavynpeh clratlsata qygwplnaii
      121 fevseqehlt dpahllgilr tyqargmkta iddfgagyag lgllaefqpd llkldialvr
      181 gidtdrsrqa ivrhvtrmce elgiaviaeg iehpdqyrtl rdlgihlqqg ylfarpqige
      241 lpkvhwpe
//
LOCUS       WP_007970901             812 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: Lon protease family protein [Pseudomonas].
ACCESSION   WP_007970901
VERSION     WP_007970901.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 812)
  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 812)
  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 812)
  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   4  (residues 1 to 812)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..812
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..812
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88748
     Region          65..800
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mpdpvaaslr lapealtrpf saeqfsfstt ndlepfrgvl gqeravealq fgvamprpgy
       61 nvfvmgepgt grfsfvkryl kaegkrlqtp adwvyvnnfd eprepralel psgtagafig
      121 dinglidnll atfpavfehp syqqkksgid rafnqrydka ldvierlale kdvalyrdas
      181 niaftpmgdg kaldeaefaq lpeaererfh edisaleerl neelaslpqw kressnqlrh
      241 lneetitlal qpllsplsek yaenaavcgy lqamqvyllk tvveqlvdds ktdavarkll
      301 eeqyapslvv ghsasggapv vfephptyen lfgrieystd qgalyttyrq lrpgalhran
      361 ggflileadk mlsepfvwda lkralqsrkl kmesplgelg rlatvtltpq hiplqvkvvi
      421 igarqlyytl qdldpdfqem frvlvdfded ipmvdesleq faqllktrts eegmapltad
      481 avarlatysa rlaehqgrls arigdlfqlv seadfirhla gdemtdaghi eralkakatr
      541 tgrvsarild dmlagiilid tdgaavgkcn gltvlevgds afgvparisa tvypggsgiv
      601 dierevnlgq pihskgvmil tgylgsryaq efplaisasi aleqsygyvd gdsaslgeac
      661 tlisalsktp lkqcfaitgs inqfgevqav ggvnekiegf frlcearglt geqgaiipha
      721 nvatlmldek vlaavragqf hvyavrqade alsllvgepa gepdengefp egsvnarvve
      781 rlrviaemis eddlkeaeke laqealaetk pa
//
LOCUS       WP_007971495             191 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Pseudomonas].
ACCESSION   WP_007971495
VERSION     WP_007971495.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 191)
  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 191)
  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   3  (residues 1 to 191)
  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   4  (residues 1 to 191)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 191)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            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="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21534
     Region          1..191
                     /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"
ORIGIN      
        1 mlrillindt akkvgrlkaa lteagfevid esgltidlpe rvemvrpdvi lidtespgrd
       61 vmeqvvlvtr dqprpivmft dehdpdvmrq aiksgvsayi vegihaqrlq pildvamarf
      121 esdqalraql qardqqlaer krielakgll mkmkdcneee aytlmrrqam srqqkliqva
      181 eqiiamsell g
//
LOCUS       WP_007971640             816 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pseudomonas sp. GM33].
ACCESSION   WP_007971640
VERSION     WP_007971640.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM33
  ORGANISM  Pseudomonas sp. GM33
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 816)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 816)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 816)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..816
                     /organism="Pseudomonas sp. GM33"
                     /db_xref="taxon:1144329"
     Protein         1..816
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=89036
     Region          12..816
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 maspalthfl prfgvaaava gvlsltgcqn fnaqdtlppt sgvqplkgla qnvsvrrnam
       61 gmpliesnsf hdalftlgyv hasdritqmv tlrllaqgrl aemhgadlld adrymravnl
      121 kksagelyka ssprlkrffe vyargvnayl fryrdklpad laatgyqpey wqpedsalif
      181 cllnfsqstn lpeeisslvl aqtvttdkla wltpsapdek lpvaeseklq glklngqvpg
      241 laelskateq lsdlnllgat ssnnwaiaaq rsrsgkslla sdshgplgvp slfsyvqira
      301 pkyqasgvti pglpmvlggf ngkvawsmas vmgdnqdlfl ekikrqgngl tyenagkwqp
      361 aivrnetyfv kgqrpireav yetrhgplln saqgttlang fglalqmpnf tddksldaff
      421 dlsraqsaer asdasreira ialnlvfada nhigwqvtgr ypnrregegl lpspgwegry
      481 dwdgyadpml hpydqdpaqg wlgtanqrvi phgygmqlsn swaaperger laelagagkh
      541 dsrsliamqy dqtttfaakl kkmfeapgma qplkqaidal paadrakahe aysrlmafdg
      601 klsptstdaa iyelflqest rqifldelgp esspawkafv adgklsyaaq adhllgreds
      661 pfwddvrtaq kedkpailar slaaaisagd sqlggdhrvw qwgklhryew knssgqtvrg
      721 plpaggdhtt lntaafawgq dfnttlapam rfivdfgqse plmaqngtgq sgnpasanyl
      781 nsiepwlkgq ymslpmqpqn fdnaygknrl tltpgk
//
LOCUS       WP_007971652             117 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Pseudomonas].
ACCESSION   WP_007971652
VERSION     WP_007971652.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..117
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12687
     Region          16..112
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(16,34..35,43,46,48..49,51,54..55,57,65,70,81)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(34,65..66,68,94)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mtdptdepes aaqirrtaly ltlaqvpegk vvsygqlael aglgraarwv grtlsqlpsd
       61 sklpwhrvlg angrislpvg spsgdeqrar lrmegisvln nrvdiqrhgw rpvehsg
//
LOCUS       WP_007971747             634 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Xanthomonas citri].
ACCESSION   WP_007971747
VERSION     WP_007971747.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas citri
  ORGANISM  Xanthomonas citri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 634)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 634)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 634)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 634)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 634)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 634)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Xanthomonas citri"
                     /db_xref="taxon:346"
     Protein         1..634
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68817
     Region          7..634
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mshtpksags shapansqta lvigaigvvf gdigtsplyt lkeafsphyg ltpdhdtvlg
       61 ilslvfwalm lvvtlkyvtv imradndgeg gimaltalaq rtlpggsrsm yvvgilgifg
      121 aslffgdgvi tpaisvlsav eglevaapkl epfvvpitlv vlsmlflaqr fgtervgkaf
      181 gpitllwffa lgaigvynma rapevlhaln pwwgvrffaq hnwhavfvlg avvlavtgge
      241 alyadmghfg akairrswqf vvlpmltlty lgqgalvlrn paavsnpfye avpewalypm
      301 ivlataatvi asqalitgay svasqamqlg yiprmhirht shstigqiyv pavnwcllal
      361 vavavigfgd saslataygv svtgtmlitt vlmiiyaran prvpapllwl falvflavdc
      421 affyaniikf ldgawfplll glilftlmrt wrrgrkllha eirkdgikld tfllglmlap
      481 pvrvpgtpvf ltadpmvvph almhnlkhnk vlhernvflt vetlqvpyaa agkrlkidai
      541 gdefyrvhvr fgfmetpdvp lalmrscdqg giyfdpmdtt yfasretiva sanrgmpiwr
      601 dklfalmhrn aapatgffri pgnrlvelga qvei
//
LOCUS       WP_007973901             144 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: pilin [Xanthomonas].
ACCESSION   WP_007973901
VERSION     WP_007973901.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..144
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14864
     Region          1..144
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkargftlie lmivvaiiai laaialpayq dylvraqvae glslasgakv aveefhwaqs
       61 vsptsnaqag lgnadtikgr yvssvtvgad gvitvafatl ganesirgsq lqlvpdwsva
      121 gstvwrcdga gttlqakylp kacr
//
LOCUS       WP_007973383             337 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_007973383
VERSION     WP_007973383.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 337)
  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   6  (residues 1 to 337)
  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 11677366
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38051
     Region          25..207
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          85..337
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msnptpvtfa svfvssllaa ardrgyeieg flrdagidpq qpqdldhhvt vdqyvallrk
       61 tikglddegi alfsrklrrg sfmlmmrsal tgdtlfgalr efthtlrllq ddldpvlldd
      121 grhvrvelhf lttqvesrdf ahvlflrliw rvmawleggs lrpagidvaf tqpesvgdyr
      181 klfptelrfg tafstiwfds qalqapvrrd sshlheylak alldllvpai parvsdrvrv
      241 ylreerarhs gwpdleqtsa alhcsasslq rhlaqegasf qnirdslrrd waiyrlktsk
      301 lptpvlaeel gfadsasfqr afkrwtgqtp gqvrkgn
//
LOCUS       WP_007974287             338 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM33].
ACCESSION   WP_007974287
VERSION     WP_007974287.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM33
  ORGANISM  Pseudomonas sp. GM33
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  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   4  (residues 1 to 338)
  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 338)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Pseudomonas sp. GM33"
                     /db_xref="taxon:1144329"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38224
     Region          23..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          252..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msekdtisiq lvreallqsc apgidkdevl ikvgidpqll gnadarvpat ayarlwrlla
       61 rrgddeffgm dprklksgsf aflcrsamlq pnvaaglagg laflslileh lpaqlvrqqs
      121 laeivlledd reprraftyf tywmivhgva cwlagrripi laielrcskp dfcddyqvmf
      181 senlrfdrpr trmifsadcl dlpikrspee lkrflalapa nilvkyrdsq slasrikhdl
      241 rhlpaehwpe tetlaqrlcm sastlrrrla eegqtyqglk dsvrkelaiv wlaepaisfs
      301 eiatrlgfad tssfykafrk wagsnpghyr slilndvq
//
LOCUS       WP_007974350             699 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Pseudomonas sp. GM33].
ACCESSION   WP_007974350
VERSION     WP_007974350.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM33
  ORGANISM  Pseudomonas sp. GM33
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 699)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Pseudomonas sp. GM33"
                     /db_xref="taxon:1144329"
     Protein         1..699
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73200
     Region          6..699
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 msqtirdnlk rmlapqhvaf vggrsmaral krsaeggypg qmwlvnpqhd nlegvpcvrs
       61 vaelpcgpda vfiatnrelt ltcvaelaai gaggaicyas gfaetgaegq alqqqlleaa
      121 gdmallgpnc yglldylhss alwpvahggk avekgvavlt qsgnfaynls msdrslpvay
      181 masvgnqaql gvaelmdvll deprvtaigl hleglknvpg faraahkale kgipiialkt
      241 gvsqigaela lshtsslsgs dalydalfdr lgvirvsgpv sfvetlkaaa cgnlpagnsl
      301 ialacsggda gliadyaern dlglpkldqg qvgelahvlp tyanlvnpld fttaiwgdge
      361 alnrmldsal rteadaamlv ldypseftge rkecdlllel ycaalqrhgk tgfvtsafpe
      421 llpaharerl haqgvaalqg vedglaawgr iagyqrnrqa llalgesalv plcphalede
      481 grllnewdsk qalkafglpt pngvlstpeq alkdaeslgy plvlkavsaq lphkteagav
      541 alnlkdgaal saalekmras iaayapgvaf dqlllepmar pplaelivgi krendfglal
      601 vigaggilve llkdsrslll pttdgairna llslrsapll qgfrgrepad ldalvtaira
      661 vadyacenaa qlleldvnpl lvgaqgttav dalirlghe
//
LOCUS       WP_007975374             279 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Pseudomonas].
ACCESSION   WP_007975374
VERSION     WP_007975374.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 279)
  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 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   3  (residues 1 to 279)
  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   4  (residues 1 to 279)
  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 279)
  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 12820790
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30738
     Region          21..275
                     /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 mdadqgesih fwqtpplagv ellsaryidh rfaphvhdgy vigmimagaq ryryrgaehl
       61 agsgtlvlin pdelhtghkg tedgwlyraf ypdsgqitsl laelelpthh lpafgatlyr
      121 dqdlvngfcq lhrllespat alqqqtvwre lvlsllqrha avpdagkpgk ehravslake
      181 llhaqlaapp sletlaaavn lspfhfarvf rratgmppht wlmqqriara rallqsgclp
      241 levamqlgfa dqshlsrqfk qvygvgpgay rsakrglea
//
LOCUS       WP_007976182              66 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Pseudomonas sp. GM33].
ACCESSION   WP_007976182
VERSION     WP_007976182.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM33
  ORGANISM  Pseudomonas sp. GM33
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Pseudomonas sp. GM33"
                     /db_xref="taxon:1144329"
     Protein         1..66
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7097
     Region          <3..50
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 msvsmlnkmh mngydvlsvn ngpwrvctqg drlgsfnsre ealafaaslp gyraradkpa
       61 gshqtk
//
LOCUS       WP_007977002             296 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM33].
ACCESSION   WP_007977002
VERSION     WP_007977002.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM33
  ORGANISM  Pseudomonas sp. GM33
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 296)
  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 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 296)
  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   4  (residues 1 to 296)
  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 296)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Pseudomonas sp. GM33"
                     /db_xref="taxon:1144329"
     Protein         1..296
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32356
     Region          31..183
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          211..294
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mlltrhldan atlvsliepl strdgfvptt lpgvqvlras cdvargpqiy epslviiaqg
       61 sklaylgprt leygaghyli qalpvpfece tfaapdgpml gvsvaidrvm lgelvlamgl
      121 apgrhipaqt pesmtsavld damrgcverl lrclhdplec qimgqarlre llfvalrgpq
      181 advlralveq qgqfariaas lshlhvhfae plnvetlasc anmsastfhe hfkrstllsp
      241 vqylkrlrll raqqlllgeg lgvaqvahrv gyqstsqfsr eykryfernp gderaa
//
LOCUS       WP_007977029             291 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Pseudomonas sp. GM33].
ACCESSION   WP_007977029
VERSION     WP_007977029.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM33
  ORGANISM  Pseudomonas sp. GM33
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Pseudomonas sp. GM33"
                     /db_xref="taxon:1144329"
     Protein         1..291
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31369
     Region          13..263
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mtltavtghr aklgegpfwd aptqalywvd iagkqalrli ganvqiwqmp ehvsafipce
       61 sgdalvtlss gvyrldldsp glaprltlfc vadpqpgnrp nearcdaqgq lwlgtmqnni
      121 geqgedlpiv rrsgglfrid rtgrvvpllr nlgipntllw sddgtrvyfg dsldgtlyrh
      181 firsdgalda sqvwfgphgr ggpdgsamda egfiwnarwd ghcllrlspd gkidrtielp
      241 isrptscvfg gadlktlyit saasplghpl dgavlsipvd vpgkrctrfa g
//
LOCUS       WP_007977277             349 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM33].
ACCESSION   WP_007977277
VERSION     WP_007977277.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM33
  ORGANISM  Pseudomonas sp. GM33
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 349)
  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 349)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 349)
  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   4  (residues 1 to 349)
  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 349)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Pseudomonas sp. GM33"
                     /db_xref="taxon:1144329"
     Protein         1..349
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38617
     Region          40..215
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          264..346
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msgsktqapg deislfeeal qpttissytv aiaqaleasg vdskrifaam giplgvatdp
       61 mtrlpaatmt rlyqacvdvt hnpyfgltva rhihlthlha lgyslaasgt lmdfcrrler
      121 yfrlvsqvak aslsqddshv lmrfdhllel sgetedaffg flirtmrlly kqdfkpvrve
      181 lcrpmphega apyetlfrsp vlfgqasgll vfdkaevmqv lsgscpelaq vndniiisyl
      241 arldksdvit gvtqkiiefl pdgdctrdkv asalcmsptk lqlklsqrgt hfqqllddtr
      301 kelacsylsq asrpvteitf llgfsdtsnf trafkrwtgl sptdfrqqg
//
LOCUS       WP_007977822             265 aa            linear   BCT 20-JAN-2025
DEFINITION  phosphonate ABC transporter ATP-binding protein [Pseudomonas sp.
            GM33].
ACCESSION   WP_007977822
VERSION     WP_007977822.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM33
  ORGANISM  Pseudomonas sp. GM33
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
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   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Pseudomonas sp. GM33"
                     /db_xref="taxon:1144329"
     Protein         1..265
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=28267
     Region          3..247
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mtlhlnrvsl thdtgvralh eidlhigage qvaiigpsga gkssllnlla talrpgsgtv
       61 evlgehawql garqrqrlra riglvhqapp lpprqrvvta vlagklgqwg faksllsllh
      121 pvdvpgaraa lvkldlgdkl faqcqqlsgg qlqrvgiarv lyqapdvlla depvsamdpv
      181 laghtlsilc rharqhkvtl vaslhavdla lsnfsriigl rdgqilfdlp aadvdrdlld
      241 rlyaneqlqs ppapvaplsl qiprc
//
LOCUS       WP_007981572             117 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Pseudomonas sp. GM48].
ACCESSION   WP_007981572
VERSION     WP_007981572.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM48
  ORGANISM  Pseudomonas sp. GM48
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Pseudomonas sp. GM48"
                     /db_xref="taxon:1144330"
     Protein         1..117
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12731
     Region          16..112
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(16,34..35,43,46,48..49,51,54..55,57,65,70,77)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(34,65..66,68,94)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mtdptdepes aaqirrtaly ltlaqipegk vvsygqlael aglgraarwv grtlsqlpsd
       61 sklpwhrvlg angrislpvg slsgdeqrar lrmegisiln nrvdiqrhgw rpvehsg
//
LOCUS       WP_007982218             346 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM48].
ACCESSION   WP_007982218
VERSION     WP_007982218.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM48
  ORGANISM  Pseudomonas sp. GM48
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 346)
  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 346)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 346)
  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   4  (residues 1 to 346)
  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 346)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Pseudomonas sp. GM48"
                     /db_xref="taxon:1144330"
     Protein         1..346
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38889
     Region          27..212
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          257..339
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkplpmrlgd lsvgfvhsla davrshgvdp qplleqygld tarlseagar lsiprymrlg
       61 hsaiqltdnp alglrmaqfs rlsqaglagi taaqaptvre aarclirfea lygsnyrgqs
      121 sfhedaqgaw lrfysispyn aynrfvvdsi iagwlhqlss vspaplraer ieiefeqpdy
      181 raaydvlgdc pivfggehnq lrlslsslaq rntehcpstw rhllqlcere leqltrtrsl
      241 reriiallgp llnggrepdl eevaarlklp twtlrrklae egtqfrailn dtrrdlamty
      301 irdtelafge iayllgfasa eafqrafkrw ngqtpgefrr shrkta
//
LOCUS       WP_007982473             347 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM48].
ACCESSION   WP_007982473
VERSION     WP_007982473.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM48
  ORGANISM  Pseudomonas sp. GM48
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 347)
  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 347)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 347)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 347)
  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   5  (residues 1 to 347)
  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   6  (residues 1 to 347)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Pseudomonas sp. GM48"
                     /db_xref="taxon:1144330"
     Protein         1..347
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39447
     Region          28..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <150..334
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mrekdsvaay fvqamihglr ddpqrvtavl eqagidpavm qqptarvpan afaalwliqi
       61 relddeffgl dshgmppgsf alicraliqe pdlhkamrqc lanfglflrd frgslavrgk
      121 ravisletrs tdndasrfge etflvlmisl lcwlggrrip idradfrhar lslgddrllw
      181 gpnltfgaer teiefashyl rlpvvqdlas lkvflrtapq wlvirfrnqh glasqvhqrl
      241 rgshysewpt lqafaleqhl spstfrrkle regcsyqeik devrrgvafe qlrqsdasis
      301 diaeqlgfqe psafhrafkk wtgespgryr aryqgeqiat lqepcdp
//
LOCUS       WP_007982579             799 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pseudomonas sp. GM48].
ACCESSION   WP_007982579
VERSION     WP_007982579.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM48
  ORGANISM  Pseudomonas sp. GM48
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 799)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 799)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 799)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..799
                     /organism="Pseudomonas sp. GM48"
                     /db_xref="taxon:1144330"
     Protein         1..799
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=88323
     Region          2..796
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkrsltalal livvlavgag gylyskqpsr qgmvelqhqq gsvtvryder giphiradne
       61 tdlyralgyv haqdrlfqme vlrrlargel aevlgpklld tdklmrslri reraetyfan
      121 ldkqsasfia mqayldginq yqdshakpve fdvlgipkrp ftaqdtisia gymaysfaaa
      181 frteplltfv rdqlgpeyln ifdldwqpkg vlngtaptla svdwkdlnal arlseqalad
      241 nglpqfegsn awvvagsrtq sgkpllagdp hirfsapsvw yeaqlsapgf elyghyqalm
      301 pfaslgmnrd fgwsitmfqn ddldliaekv npdnpnqvwy rgkwvdmvts eqkiavkgqe
      361 pvtlvlrqsp hgpivndals nsvgktpiam wwaflesqnp ilegfyqlnr adtlakarga
      421 aakiqapgln vvwanakgdi gwwaaaqlpk rpagvrpwfi ldgstaeadk dgfypfsanp
      481 qeenpargyi vsanfqpvsp tgmeipgyyn ladrgqqlnr qlsdkavkwd lensqklqlg
      541 tttaygprll apllpvlrev vsdpaelklv eqlaqwkgdy pldstnatvf nqflfnlada
      601 tmhdelgndf fetllstrvi daalprlaas adspwwdnrd tlgketradt vkaawqasia
      661 hlkttlgadf tqwqwgraht lthghplgqq kpldlvfnvg pfaapgshev pnnlsakigp
      721 apwpvtygps trrlidfadp ahsltvnpvg qsgvlfdshy ddqaeayieg myfqahlnde
      781 evtantrstl kllparaap
//
LOCUS       WP_007984377             233 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Pseudomonas sp. GM48].
ACCESSION   WP_007984377
VERSION     WP_007984377.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM48
  ORGANISM  Pseudomonas sp. GM48
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 233)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Pseudomonas sp. GM48"
                     /db_xref="taxon:1144330"
     Protein         1..233
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=25491
     Region          36..203
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 malnrfgllf ailltclsvt sayadslena lvkaapgada kvialavrat qcsraqgiap
       61 aqrlavidys lpsteqrlwv fdlkrrkllf helvahgrns genmatlfsn qnesyatslg
      121 lfrtqesyrg qngyslrmeg lepgfndnay draivihgap yvspvlaran grigrslgcp
      181 avrpaiahrl idsmkdgqll fsyypdqrwl ksssyincgs dtvasrekst srq
//
LOCUS       WP_007986092             288 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Paraglaciecola chathamensis].
ACCESSION   WP_007986092
VERSION     WP_007986092.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola chathamensis
  ORGANISM  Paraglaciecola chathamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Paraglaciecola chathamensis"
                     /db_xref="taxon:368405"
     Protein         1..288
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32571
     Region          1..275
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mkidlhchty ysdgqlspve lvdrannmqv dvlaitdhdt vqaldearah qakqkrlmhi
       61 vdgielstsw hnfdihilgl nvnkddelfq qrlveqkner geraqkmadk lakagvenvl
      121 ddakllageg qltrahfarv lverkevrdf esafkkylgk gkrahvkprw isieeavqwi
      181 hdaggkavia hpghydmtak wlrrlvaqfk eaggdgiett harinpekrk livelateyn
      241 lqasagsdfh fvsrwtelgr nlgvpehltp iwhdwsfidp svdatsna
//
LOCUS       WP_007986414             176 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Paraglaciecola
            chathamensis].
ACCESSION   WP_007986414
VERSION     WP_007986414.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola chathamensis
  ORGANISM  Paraglaciecola chathamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 176)
  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 176)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 176)
  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   4  (residues 1 to 176)
  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   5  (residues 1 to 176)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Paraglaciecola chathamensis"
                     /db_xref="taxon:368405"
     Protein         1..176
                     /product="TRAP transporter small permease subunit"
                     /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=19861
     Region          1..168
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mnsvvkllgk fidgvghlcs vlmmlmilnv fydvimryff nevsigmqel ewhlfaamfm
       61 fgigytlkad ghvrvdvfyd nfsprvkayi nlfgalffvl pvtflilyys wdytleayem
      121 gegsadpggl phrfiirgvi pvssvflivc alyvvleqlq rltgstpsst ehkdai
//
LOCUS       WP_007986873             307 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Paraglaciecola].
ACCESSION   WP_007986873
VERSION     WP_007986873.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola
  ORGANISM  Paraglaciecola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Paraglaciecola"
                     /db_xref="taxon:1621534"
     Protein         1..307
                     /product="formate/nitrite transporter family protein"
                     /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=33478
     Region          54..304
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msddlehgeh dheakivsps gellfnestk erskertres qeyasvivkr vdetfrhpdd
       61 ilekaidegv eqlarpsmsl fmsalaagmi icftvlavgv mttivgdmst gfnrvlvalv
      121 yplgfvmcil srtqlfteht atafypildr risvfrmfrl wgiviagnii ggifsaglla
      181 lsdevihase gyfiiaehil syspltllis atlagwlmal gawtilsths ttsqilciyi
      241 vtfiiglggl hhsiagsvel lvgyftsdql sliemlkala vvllgnaigg svfvallnys
      301 hirklnk
//
LOCUS       WP_007987472             346 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM48].
ACCESSION   WP_007987472
VERSION     WP_007987472.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM48
  ORGANISM  Pseudomonas sp. GM48
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 346)
  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 346)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 346)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 346)
  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   5  (residues 1 to 346)
  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   6  (residues 1 to 346)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Pseudomonas sp. GM48"
                     /db_xref="taxon:1144330"
     Protein         1..346
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38473
     Region          31..211
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          111..341
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mqmkvidptf elalvspfll qtlaevveqk ginpeslcrg lgfsvedlqd paqrisyrqa
       61 vamiqralkv lpnqglglwv gaqnvlgtlg llghvlslck tlrdafelgi rhqhtsggiv
      121 vssveeagdr vfvdvecrlp ftdvqlfave effasllvyg ralvgadfkp vavefmhaap
      181 dylgeysrll gpdvrfgglq nrmvidaywl dvhlpnhhsl alrqavklle leaaqvhqkm
      241 dliqaverai ardltegshi ekiasdlnms srtlrrrlte haltfealle qvrqartmsl
      301 lanpdmsier itevvgysdv rsfrrafkrw tgmspsafrn espgvv
//
LOCUS       WP_007987059             265 aa            linear   BCT 20-JAN-2025
DEFINITION  phosphonate ABC transporter ATP-binding protein [Pseudomonas sp.
            GM48].
ACCESSION   WP_007987059
VERSION     WP_007987059.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM48
  ORGANISM  Pseudomonas sp. GM48
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
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   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Pseudomonas sp. GM48"
                     /db_xref="taxon:1144330"
     Protein         1..265
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=28318
     Region          3..247
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mtlhlnrvsl thgndvralh eidlhigage qvaiigpsga gkssllnvla talrpdngav
       61 evlgehawql gahrrqqlra riglvhqapp lpprqrvvta vlagklgqwg faksllsllh
      121 pvdvpgaraa llkldlgdkl faqcqqlsgg qlqrvgiarv lyqapevlla depvsamdpv
      181 laghtlsvlc rharehnvtl vaslhavela lahfsriigl rdgqilfdlp asdvdhelld
      241 klyaneqlls ppapvaplil qiprc
//
LOCUS       WP_007987868             212 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Paraglaciecola
            chathamensis].
ACCESSION   WP_007987868
VERSION     WP_007987868.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola chathamensis
  ORGANISM  Paraglaciecola chathamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
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   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   3  (residues 1 to 212)
  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   4  (residues 1 to 212)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 212)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 212)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Paraglaciecola chathamensis"
                     /db_xref="taxon:368405"
     Protein         1..212
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=23700
     Region          16..206
                     /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"
ORIGIN      
        1 mistakkttq lasheqlnil lidenvqrae sivtalgnsr ykvshlactq agllkqvdei
       61 qpdiividie spnrdmlesl htishynpkp vvmfssqqdt etinlsvqsg vsayvvgdid
      121 pervkpilda avarfkafhk lkdelddtkh qlesrksidl akrllmktnk mseeqafhsm
      181 rktamdtgqk ledvaktivs mlrsleqghe hd
//
LOCUS       WP_007987870             370 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Paraglaciecola chathamensis].
ACCESSION   WP_007987870
VERSION     WP_007987870.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola chathamensis
  ORGANISM  Paraglaciecola chathamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 370)
  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 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   3  (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   4  (residues 1 to 370)
  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 370)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Paraglaciecola chathamensis"
                     /db_xref="taxon:368405"
     Protein         1..370
                     /product="CmpA/NrtA family 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=40781
     Region          3..264
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mikpeqpnis lgfipltdsa pliiakelgf feqwglnvtl qkqnswatlr dklhagvlda
       61 aqmlapmpla salglgappa nvitplvlsl ngnaitlseg llqevlkene insvtlpmaa
      121 yllqkvvekr krngeaklkf atvfpyschy yqlrdwlkav kvdlddveml vvppvsmvec
      181 lkngdidgfc vggpwnakav ragigmtalt sfdiwqdspe kvlglleefh kkypntvlal
      241 caalkqacaw lesvpnrfea arllcnekyl naeldviaps llgsclthqs lpprsipsyn
      301 qfsvsnngci nqpelvrgew likhmvsagq ipphvtipld lvakvfrpdi yqqmrllied
      361 qgvqfyrrsg
//
LOCUS       WP_007987914             466 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Paraglaciecola chathamensis].
ACCESSION   WP_007987914
VERSION     WP_007987914.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola chathamensis
  ORGANISM  Paraglaciecola chathamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 466)
  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 466)
  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 466)
  AUTHORS   ter Beek,J., 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 466)
  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 466)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Paraglaciecola chathamensis"
                     /db_xref="taxon:368405"
     Protein         1..466
                     /product="CmpA/NrtA family 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=51831
     Region          43..320
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mvknsvfnsl altvkslrla viatvctttl vghnvaaqtv gwpekeelkf gfikltdmap
       61 laiayekgyf edeglyvtle aqanwkvlld rvidgeldga hmlagqplga tigygtkadi
      121 itafsmdlng naitvsndiw qqmkpnipqe ngkpvhpika dalkpvvesy kkqgkpfkmg
      181 mvfpvsthny elrywlaagg ihpgyygpnn dvkglinaea qlsvtpppqm pstmeagtiy
      241 gycvgepwnq qavfkgigvp vvtdyeiwkd npekvfgvnk awaeenpnth irvvkamira
      301 aiwldeknna nrpeavqila ksqyvgadae vignsmtgtf eyekgdkrsv pdfnvffrhn
      361 atypyysdai wyltqmrrwg qiseqksddw ykdiakkvyr pdiyaqaals liaegkanae
      421 dfpefssesg fkqpqthfid nivydgtqpn aylekfdigl kgdnki
//
LOCUS       WP_007988011             371 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM48].
ACCESSION   WP_007988011
VERSION     WP_007988011.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM48
  ORGANISM  Pseudomonas sp. GM48
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 371)
  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 371)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 371)
  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   4  (residues 1 to 371)
  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 371)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Pseudomonas sp. GM48"
                     /db_xref="taxon:1144330"
     Protein         1..371
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41281
     Region          20..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          252..334
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 myrmssgyas mlantflaqg ldlaglcqea gldvefvgrp gafcersviy rlwdlaaqas
       61 ddlniglkay gefhpssfqi vgytmmsssn lkralerlvr fspligtgfs lflvqeqqhy
      121 rlasldhqqh gsvkprqytd aalasllgfc rwlaggkspq plsveftype pedtsehqrl
      181 fgcplsfgaa ydsilfdgqe llsplsmane alatlhdsfa vaqldllsgy fmvgrirali
      241 terlsqgqgq gqcdmesiaa alniskrtlq rglekdgtqf kdvlndvrrq madfylrhsh
      301 fnmkhvtsll gfhdhssfhk acirwfgmtp gqyrtdelsp vvekvagvrs mnpiglyrdq
      361 kiagsaermh r
//
LOCUS       WP_007988743             332 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM48].
ACCESSION   WP_007988743
VERSION     WP_007988743.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM48
  ORGANISM  Pseudomonas sp. GM48
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 332)
  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 332)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 332)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 332)
  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   5  (residues 1 to 332)
  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   6  (residues 1 to 332)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Pseudomonas sp. GM48"
                     /db_xref="taxon:1144330"
     Protein         1..332
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38068
     Region          22..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          94..330
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mrertiashf araalggarr hgydysgllq qlgispelld eprariapeq ftqliqalwl
       61 alddeylgfg qapskpgsfa mmchavihcr nldkalnrgl lfyslfpgap rltlsredew
      121 vrlslddaql wdpdhflsea llviwhrfgs wligqrirle qatfsyprpe hgaeydllfs
      181 cplefsrtqs sllfhsryla mpllqdertl khflerspad llsrpdegds lssrlrrlls
      241 rdsarwpdle avathlhisp qtlrrhlree gssfqelkdq lrrdiaiyhl sradlslqqi
      301 aeqlgfseps afhrafkkwt gltpgayraq en
//
LOCUS       WP_007988951             191 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Pseudomonas].
ACCESSION   WP_007988951
VERSION     WP_007988951.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 191)
  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 191)
  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   3  (residues 1 to 191)
  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   4  (residues 1 to 191)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 191)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            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="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21454
     Region          1..191
                     /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"
ORIGIN      
        1 mlrillindt akkvgrlkaa lteagfevid esgltidlpe rvetvrpdvi lidtespgrd
       61 vmeqvvlvtr dqprpivmft dehdpgvmrq aiqsgvsayi vegihaqrlq pildvamarf
      121 esdqalraql hardqqlaer krielakgll mkmkncneee aytlmrrqam srqqkliqva
      181 eqiiamsell g
//
LOCUS       WP_007990088             738 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Paraglaciecola
            chathamensis].
ACCESSION   WP_007990088
VERSION     WP_007990088.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola chathamensis
  ORGANISM  Paraglaciecola chathamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Paraglaciecola chathamensis"
                     /db_xref="taxon:368405"
     Protein         1..738
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=80990
     Region          1..738
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mkrsllatsi altmfsaiaq etpnnkaiet vtiygnqlka qeatgaaqyi geqdlekfay
       61 tdiqriirqa pgvslqvedg yglrpnisir gvatersgri tllednvlia papysapsay
      121 yfptagrmsa fevvkgpaai tqgpytigga inmlstpipn tqsgqvtlea gqdatyraha
      181 tiggkndngf gylleahqwq sdgfqdidrs sndtgldvtd ltmklayapk nsrhsvelkl
      241 qytdqdseqs ylgltdadfa ndaqrrygls aldnisteht qvmlnyafqi nkelnftava
      301 ynntherdwf ktegidldgs dnaqdysrts wsnvisainn neaigetsva mlqgildgti
      361 dteagsiqlr snsreyysrg iqfglnwnkq fgdakhhief gvrlhedeed rlqrnstyqq
      421 vdgqlllsdl gelgnagnrv qdadalavhv ydrielgdwv ftpglrfedi sqsrtrytng
      481 adrvfrddre ndttvllpgl gvlykidsnl nliagahkgf tapsnspgak eeeavnyelg
      541 frynndafna elvyflsdyd nivgvctass gsdceigdaf ngdaatvqgi efllktelgq
      601 fngiripfnl tysyidsefd tdisgtdffg dvsagdsipy ipesqgqvtl glegdkwaty
      661 lnavfvdsvc trascdafea tdssfildls gsynvnadlr vfarienltd eedivsrqpy
      721 garpnksrta svgitysf
//
LOCUS       WP_007990427             133 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Pseudomonas sp. GM48].
ACCESSION   WP_007990427
VERSION     WP_007990427.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM48
  ORGANISM  Pseudomonas sp. GM48
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Pseudomonas sp. GM48"
                     /db_xref="taxon:1144330"
     Protein         1..133
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14286
     Region          1..131
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mrssnrgftl ieimiviaii glvmtfaaps fteylnkgrr aevagllseq aqllerfysq
       61 knaytdatgl sagndyytit ptladqtfll mavrkagtsm atdkcgdlti tntgvlgmvn
      121 aktgltskdc wgr
//
LOCUS       WP_007990468             812 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Pseudomonas sp. GM48].
ACCESSION   WP_007990468
VERSION     WP_007990468.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM48
  ORGANISM  Pseudomonas sp. GM48
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 812)
  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 812)
  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 812)
  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   4  (residues 1 to 812)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..812
                     /organism="Pseudomonas sp. GM48"
                     /db_xref="taxon:1144330"
     Protein         1..812
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88688
     Region          65..800
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mpdpvaaslr lapealtrpf saeqfsfstt ndlepfrgvl gqeravealq fgvamprpgy
       61 nvfvmgepgt grfsfvkryl kaegkrlqtp adwvyvnnfd eprepralel psgsagafig
      121 dinglidnll atfpavfehp syqqkksaid rafnqrydka ldvierlale kdvalyrdas
      181 niaftpmgdg kaldeaefaq lpeaererfh edisaleerl neelaslpqw kressnqlrh
      241 lneetitlal qpllsplsek yaenaavcgy lqamqvyllk tvveqlvdds ktdavarkll
      301 eeqyapslvv ghsasggapv vfephptyen lfgrieystd qgalyttyrq lrpgalhran
      361 ggflileadk mlsepfvwda lkralqsrkl kmesplgelg rlatvtltpq hiplqvkvvi
      421 igarqlyytl qdldpdfqem frvlvdfded ipmvdesleq faqllktrts eegmapltad
      481 avarlatysa rlaehqgrls arigdlfqlv seadfirhla gdvmtdaghi eralkakatr
      541 tgrvsarild dmlagiilid tagaavgkcn gltvlevgds afgiparisa tvypggsgiv
      601 dierevnlgq pihskgvmil tgylgsryaq efplaisasi aleqsygyvd gdsaslgeac
      661 tlisalsktp lkqcfaitgs inqfgevqav ggvnekiegf frlcearglt geqgaiipha
      721 nvatlmldek vlaavragqf hvyavrqade alsllvgepa gepdengefp egsvnarvve
      781 rlrviaemis eddlkeaeke laqealaetk pa
//
LOCUS       WP_007993114             799 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pseudomonas sp. GM49].
ACCESSION   WP_007993114
VERSION     WP_007993114.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM49
  ORGANISM  Pseudomonas sp. GM49
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 799)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 799)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 799)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..799
                     /organism="Pseudomonas sp. GM49"
                     /db_xref="taxon:1144331"
     Protein         1..799
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=88200
     Region          2..796
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkrsltalal livvlaagag gylyskqpsr qgmvelqhlq gsvtvryder giphiradne
       61 tdlyralgyv haqdrlfqme vlrrlargel aevlgpklld tdklmrslri reraetyfan
      121 ldklspsyia mqayldginq yqdshakpve fdvlgipkrp ftaqdtisia gymaysfaaa
      181 frteplltfv rdqlgpeyln ifdldwqpkg vlngtapsla sadwkdlnal arlseqalad
      241 nglpqfegsn awvvagnrtq sgkpllagdp hirfsapsvw yeahlsapgf elyghyqalm
      301 pfaslgmnrd fgwsitmfqn ddldliaekv npdnpnqvwy rgkwvdmvts eqkiavkgqe
      361 pvtlvlrqsp hgpivndalg navgktpiam wwaflesqnp ilegfyqlnr adtlakarga
      421 aakiqapgln vvwanakgdi gwwaaaqlpk rpagvrpwfi ldgstteadk dgfypftanp
      481 qeenpargyi vsanfqpvsp tgmeipgyyn ladrgqqlnr qlgdkavkwd lensqtlqlg
      541 tttaygprll apllpvlrev vsdpaelklv eqlaqwkgdy pldstsatlf nqflfnlaea
      601 tmhdelgndf fetllstrvi daalprlaas adspwwdnrd tlgnetradt vkaawqasia
      661 hlkttlgadf tqwqwgnaht lthghplgqq kpldlifnvg pfaapgshev pnnlsakigp
      721 apwpvtygps trrlidfadp ahsltvnpvg qsgipfdshy ddqaeayieg myfqahlnde
      781 evaantrstl kllparaaq
//
LOCUS       WP_007994071             220 aa            linear   BCT 20-JAN-2025
DEFINITION  formate dehydrogenase accessory sulfurtransferase FdhD, partial
            [Pseudomonas sp. GM49].
ACCESSION   WP_007994071
VERSION     WP_007994071.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM49
  ORGANISM  Pseudomonas sp. GM49
            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 10003943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Pseudomonas sp. GM49"
                     /db_xref="taxon:1144331"
     Protein         1..>220
                     /product="formate dehydrogenase accessory
                     sulfurtransferase FdhD"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0097163 - sulfur carrier activity
                     [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
     Region          49..>220
                     /region_name="FdhD"
                     /note="Formate dehydrogenase assembly factor FdhD, a
                     sulfurtransferase [Energy production and conversion];
                     COG1526"
                     /db_xref="CDD:441135"
ORIGIN      
        1 mlcqveqady rsdtnapapk plsvnfreyd saasvcqaal aaeialaity nglsqavmmv
       61 spgnledfir gfsvsndivr dpreiydlrl trfdqavqad vqissrafwa lknhrrqmag
      121 tsgcglcgvq aleqalpkld ildpvplppa ehfidirsri eqaqqmarss galhaalyfd
      181 sqgnalicre digrhnaldk ligalqhagi dsrsgftvvt
//
LOCUS       WP_007996409             133 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Pseudomonas sp. GM49].
ACCESSION   WP_007996409
VERSION     WP_007996409.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM49
  ORGANISM  Pseudomonas sp. GM49
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Pseudomonas sp. GM49"
                     /db_xref="taxon:1144331"
     Protein         1..133
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14232
     Region          1..131
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mrssnrgftl ieimiviaii givmtiaaps lteylnkgrr aevagllseq aqllerfysq
       61 knvytdatgl sagndyysit ptltdqtfll tavrkadsgm atdkcgdlti tntgvlgmvn
      121 aksgltskdc wgr
//
LOCUS       WP_007996734             191 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Pseudomonas sp. GM49].
ACCESSION   WP_007996734
VERSION     WP_007996734.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM49
  ORGANISM  Pseudomonas sp. GM49
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 191)
  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 191)
  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   3  (residues 1 to 191)
  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   4  (residues 1 to 191)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 191)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Pseudomonas sp. GM49"
                     /db_xref="taxon:1144331"
     Protein         1..191
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21485
     Region          1..191
                     /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"
ORIGIN      
        1 mlrillindt akkvgrlkaa lteagfevid esgltidlpe rvetvrpdvi lidtespgrd
       61 vmeqvvlvtr dqprpivmft dehdpdvmrq aiksgvsayi vegihaqrlq pildvamarf
      121 esdqalraql hardqqlaer krielakgll mkmkscneee aytlmrrqam srqqkliqva
      181 eqiiamsell g
//
LOCUS       WP_007997172             116 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein, partial
            [Pseudomonas sp. GM49].
ACCESSION   WP_007997172
VERSION     WP_007997172.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM49
  ORGANISM  Pseudomonas sp. GM49
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 116)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 116)
  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 116)
  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 116)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Pseudomonas sp. GM49"
                     /db_xref="taxon:1144331"
     Protein         <1..116
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          21..110
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(40,59..60,78,81,89..90,102,107)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 rrvaldrrpv ptvpvpsmds lrfddesfev fygeqagglt rseyrlletl hrsadevlsk
       61 aflyqqvlqr gyaahdrsld mhisqirrkl kaigyterev rtvwgkgyil saadem
//
LOCUS       WP_007998171             699 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Pseudomonas sp. GM49].
ACCESSION   WP_007998171
VERSION     WP_007998171.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM49
  ORGANISM  Pseudomonas sp. GM49
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 699)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Pseudomonas sp. GM49"
                     /db_xref="taxon:1144331"
     Protein         1..699
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73136
     Region          6..699
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 msqkirdnlk rmlapqhvaf vggrsmaral krcaeggyqg qmwlvnpqhd slegvpcvrs
       61 vaelpcgpda vfiatnrelt ltcvgelaai gaggaicyas gfaetgaegq alqqqllqaa
      121 gdmallgpnc yglldylhss alwpvahggk avekgvavlt qsgnfaynls msdrslpvay
      181 masvgnqaql gvaelmdvll deprvtaigl hleglknvpg faraahkale kgipiialkt
      241 gvsqigaela lshtsslsgs dalydalfdr lgvirvsgpv sfvetlkaaa cgnlpagisl
      301 ialacsggda gliadyaern dlglpkldqg qvgelaqvlp syanlvnpld fttaiwgdge
      361 alnrmldsal rteadaamlv ldypseftge rkecdlllel ycaalqrhgk tgfvtsafpe
      421 llpaharerl haqgvaalqg vedglaawgr iagyqrnrqa llalgesalv plcphalege
      481 grllnewdsk qalkafglpt pngvlstpeq alkeakslgy plvlkavsaq lphkteagav
      541 alnlkdgaal saalekmhss iaayapgvaf dqlllepmak pplaelivgi krendfglal
      601 vigaggilve llkdsrslll pttdgairka llslrsapll qgfrgresad ldalvtaira
      661 vadyacenaa qlleldvnpl lvgaqgttav dalirlghe
//
LOCUS       WP_007998612             271 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM49].
ACCESSION   WP_007998612
VERSION     WP_007998612.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM49
  ORGANISM  Pseudomonas sp. GM49
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 271)
  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 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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Pseudomonas sp. GM49"
                     /db_xref="taxon:1144331"
     Protein         1..271
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29543
     Region          28..269
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <158..268
                     /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 mdrlstllth fgvnagtfhs gtfcgtaayd gqqasghlhl lqagelllkm gdqpdlqlte
       61 psliffprpy rhrlfaaega gtqlvcatld fdggagnala aalpdylvlq ldeipalagt
      121 lewlfkeafd gtcgreavmd rlfellvill lrhilsttgq qpgmmaglad arlsrplslm
      181 hqtpakawtv velsvaanms rasfaehfrr vvgqtpvdyl vswrislaqk rlregrpial
      241 iaeevgyesp salarafrrk tglsprewkd s
//
LOCUS       WP_007999780             334 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM49].
ACCESSION   WP_007999780
VERSION     WP_007999780.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM49
  ORGANISM  Pseudomonas sp. GM49
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  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   4  (residues 1 to 334)
  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 334)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Pseudomonas sp. GM49"
                     /db_xref="taxon:1144331"
     Protein         1..334
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37741
     Region          22..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          248..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mteptslasw tralrkqlda lgidstalch qagldpllmd dpnaryplsg tthlwhlavq
       61 vsgdpaiglr vsrfvspttf halgyalvas gslrevferi vryhqvvsda leleltraed
      121 ryhfrlkipa gnpapafeai dafmaiyvrt crnrlgreya pmatylrrpe padahqwhkv
      181 frspvhfgad edrlefalvd fdshlddanp elaehnetvl krtlaqlkpl twerkvrdai
      241 eeqlpegeps aehiakalhl slrslqrhla degyrfdtll nesrenlall hlrdpqvsls
      301 eisyllgfad tssfsrafkr wtgmtpgqfr dglr
//
LOCUS       WP_008000618             256 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Pseudomonas sp. GM49].
ACCESSION   WP_008000618
VERSION     WP_008000618.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM49
  ORGANISM  Pseudomonas sp. GM49
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Pseudomonas sp. GM49"
                     /db_xref="taxon:1144331"
     Protein         1..256
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=28439
     Region          5..172
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkpinynqyr sirsvnsrvr flifhytaan fsssvsaltg pnvsahylip ditdpgylka
       61 gytgqetfnl vnethrawha gvsqwgnrsn lndtsigiei vnlatdnkge ftfppyhpeq
      121 iaaieqlaln ilkrypditp tqvlghsdvs igrksdpgpm fpwqalylkg vgawfdattr
      181 deylcqynts gvpvrsellg lfksygydvs gasteggfqq lvrafqmhfr pekfdgkmda
      241 qtaanlkalv vkyfpg
//
LOCUS       WP_008000670             809 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas sp. GM49].
ACCESSION   WP_008000670
VERSION     WP_008000670.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM49
  ORGANISM  Pseudomonas sp. GM49
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 809)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 809)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 809)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..809
                     /organism="Pseudomonas sp. GM49"
                     /db_xref="taxon:1144331"
     Protein         1..809
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88066
     Region          68..119
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          95..809
                     /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 mksraksgsv kqwlsvsals fsvlallpls valaaetggs qsreqfsfsl aakplpqals
       61 dfsrvtgisv vytdeapygl napaingqms aeqalqrllt gsgltfrrtd ghtialeprp
      121 tegalnlgat titsvmddsm syqppptssv mrssapvqei pqtinvvpaq virdqaprnl
      181 ddalanvsgi tqantlgstq dsvmvrgfgd nrngsimrdg mpivqgrgln asvdrvevlk
      241 gpasllygiq dpggvvnmvs kkpeleqyna lnlrgssygd gkngsgggld stgalgdsgl
      301 ayrmvldhed edywrnfgvh resliapsla wygestkllf ayehrefltp fdrgtlidpr
      361 tnhpldisrn erldepfnnm qgrsdlyhfe adhqlndnwk ghfgyswnre tydasqvrvt
      421 aidtqkgtlt rsmdgtrnai stdrfttasl egnvnvlgmq hdllfgidde yrkifredli
      481 rqkslttfsy vnpvygreva gttvsapdsa qtdelrsdsv flqdsihltd qwilvagarf
      541 qvydqyagkg vpfhantdsn gqkwvpragl vykytdalsf ygsytesfkp nstiaplsgs
      601 stvldggiap eeakswelga kldlpgrvtg nialfdikkr nvlvanaegp ttiysaagev
      661 rsrglevdls gqlsdrwsmi gsyaytdaev tedpvykgnq lqnvaknsgs lsavydfgtv
      721 iggdqlrvga garyvgerag navndfdlpg ytvadafaty dtkverqkvk fqlnvknlfd
      781 rtyytsaasr ffvsmgdsrq islsstlef
//
LOCUS       WP_008001580             346 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM49].
ACCESSION   WP_008001580
VERSION     WP_008001580.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM49
  ORGANISM  Pseudomonas sp. GM49
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 346)
  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 346)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 346)
  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   4  (residues 1 to 346)
  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 346)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Pseudomonas sp. GM49"
                     /db_xref="taxon:1144331"
     Protein         1..346
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38816
     Region          27..212
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          257..339
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkpqpmrlgd lsvgfvhsla davrshgidp qplldqygld aarlseagar lsiprymrlg
       61 hsaiqltdnp alglrmgqls rlsqiglagv taaqaptvre aarclirfea lygsnyrgqs
      121 sfhedaqgaw lrfysispyn aynrfvvdsi iagwlqqlss vspaplraer ieiefeepgy
      181 raaydvlgdc piqfggernq lrlsqaslaq rnpehcpstw rhllqlcere leqltrtrsl
      241 reriiallgp llnggrepdl qevaarlklp twtlrrklad egtqfrailn dtrrdlamty
      301 irdtelafge iayllgfasa eafqrafkrw ngqtpgefrr shrkta
//
LOCUS       WP_008001638             347 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Pseudomonas sp. GM49].
ACCESSION   WP_008001638
VERSION     WP_008001638.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM49
  ORGANISM  Pseudomonas sp. GM49
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 347)
  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 347)
  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 347)
  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 347)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Pseudomonas sp. GM49"
                     /db_xref="taxon:1144331"
     Protein         1..347
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=37567
     Region          21..345
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 msriltesvs rrsflvsagv tvggafaasl lpsgafaatk pivlrytssl pdthplnkqm
       61 kaasqaikve tngavdlqvy angamggdtd mlsqvragai dfiplpgail stlvpamsie
      121 smpfafkdyd svwaaldgkl gehvraktek vglipmekvw nngfrqitss trpintpqdl
      181 agfklrvlvs plwtsmfsal gasptgisin etysalqtkv vdgqenplvv vesarfyevq
      241 kycsmtdhiw ggfwivasgk tfpklpadvq eivsrqinaa alvqrqqvid lnsslepslt
      301 ahgitfnkvd ralfradlqs kgfysqwkek ygpeawslle qyagqls
//
LOCUS       WP_008002180             259 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Pseudomonas sp. GM49].
ACCESSION   WP_008002180
VERSION     WP_008002180.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM49
  ORGANISM  Pseudomonas sp. GM49
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Pseudomonas sp. GM49"
                     /db_xref="taxon:1144331"
     Protein         1..259
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=28923
     Region          26..175
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkyfalivsl illagctsgp rydtshpsan ydsrvqfvvv hytnaslers lqllthgevs
       61 shyligddkg atiyklmden vrawhagese wngrtwlnss sigieivnpg fkdtptgrvw
      121 ypytedqvqs livllkdisk rhgirprdiv ghsdiapfrk ldpgplfpwk rlaaeglgiw
      181 pneqsvarqq mqfaeqlpsi swfqaqlahl gyaspqtgel dvatrhviaa fqmhfrparf
      241 dgtpdaqtaa illvlnqtk
//
LOCUS       WP_008003094             339 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM49].
ACCESSION   WP_008003094
VERSION     WP_008003094.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM49
  ORGANISM  Pseudomonas sp. GM49
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 339)
  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 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 339)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 339)
  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   5  (residues 1 to 339)
  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   6  (residues 1 to 339)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Pseudomonas sp. GM49"
                     /db_xref="taxon:1144331"
     Protein         1..339
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38569
     Region          28..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <150..334
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mrekdsvaay fvqamihglr ddpqrvkavl eqagidpavm qqptarvpan afaalwliqi
       61 relddeffgl dshgmppgsf alicraliqe pdlhkamrqc lanfglflrd frgslavrgk
      121 ravisletcs tdndasrfge etflvlmisl lcwlggrrip idradfrhsr lslgddrllw
      181 gpnltfgaer teiefashyl rlpvvqdlas lkvflrtapq wlvirfrnqh glasqvhqrl
      241 rgshysewpt lqafaleqhl spstfrrkle regcsyqeik devrrgvafe qlrqseasis
      301 diaeqlgfqe psafhrafkk wtgespgryr aryqgeqge
//
LOCUS       WP_008003827              83 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Pseudomonas sp. GM49].
ACCESSION   WP_008003827
VERSION     WP_008003827.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM49
  ORGANISM  Pseudomonas sp. GM49
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Pseudomonas sp. GM49"
                     /db_xref="taxon:1144331"
     Protein         1..83
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=9361
     Region          1..83
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 milinyfary reqlnlggek lpltddlkti edvrrllmar gevwshvlge nnlmcalnqa
       61 lchpdqvied ydeiaffppv tgg
//
LOCUS       WP_008004443             309 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein, partial [Pseudomonas sp. GM49].
ACCESSION   WP_008004443
VERSION     WP_008004443.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM49
  ORGANISM  Pseudomonas sp. GM49
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Pseudomonas sp. GM49"
                     /db_xref="taxon:1144331"
     Protein         <1..>309
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
     Region          5..240
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 lasytlganv enlyfggsgn fagtgntlan tivggagndv lvggagndvl iggagadtmv
       61 ggvdndtyev dnlgdvltel agsgsdtvwt slasytlgan venlffggsg nfagsgnvld
      121 ntlvggagnd lliggagadt maggggndvy evtelgdvvs elagagidtv wtslasytlg
      181 advenlffgg sgnfagsgnt ldntlgggag ndflggsgga dtilggggad tmfggvgddv
      241 yevadlgdvv aelagsgsdt vwtslasytl ganvenlffg gsgnfagign elantiggga
      301 gndflngng
//
LOCUS       WP_008004472             140 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Pseudomonas sp. GM49].
ACCESSION   WP_008004472
VERSION     WP_008004472.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM49
  ORGANISM  Pseudomonas sp. GM49
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Pseudomonas sp. GM49"
                     /db_xref="taxon:1144331"
     Protein         1..140
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14294
     Region          2..136
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mnnqkgftli ellvvvaiig ilatlglpmy skyqarakvt aalaeltamk vpfedvinqg
       61 dtptianvap agatstthca lsvtastpeg egsivctlqn apgvvvgktv tltrnetkgw
      121 sckgtvsqdy lpkgcsgpat
//
LOCUS       WP_008007767             330 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM50].
ACCESSION   WP_008007767
VERSION     WP_008007767.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM50
  ORGANISM  Pseudomonas sp. GM50
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 330)
  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 330)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Pseudomonas sp. GM50"
                     /db_xref="taxon:1144332"
     Protein         1..330
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36632
     Region          23..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          250..329
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mlhshlttln avslvlntfk aeglsseall agsgisaadl sradtrittn qemlvcanav
       61 alrrdiglel grrmhvssyg mlgyalltsa tlgdalrlal hypallgtlf elsleeeder
      121 iwltagdyre npalapfnve fclvsmkvtc edllghplpl lgarfehpap dyqaryaerf
      181 dcplqfdavs nafafdkrwl eqplpladai thqamaercr kqnteftgrq awlgrirqll
      241 aaqlsaapgl dglakqlncs artlrrhlkd lgcsyqelld elrfeqakrl lcedqlpiyr
      301 iaealgfset asfrhafvrw sgvapsqfrp
//
LOCUS       WP_008008172             809 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas sp. GM50].
ACCESSION   WP_008008172
VERSION     WP_008008172.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM50
  ORGANISM  Pseudomonas sp. GM50
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 809)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 809)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 809)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..809
                     /organism="Pseudomonas sp. GM50"
                     /db_xref="taxon:1144332"
     Protein         1..809
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88341
     Region          61..111
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          92..809
                     /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 msrsldtvlr prllavaial caplassqli aaeqassvra ynlpaaplas tlnqiasqag
       61 lalslnpsla agktsapvkg qfdatgalre alrgtglqle qssagtyslv avpegvmalp
      121 etaviglena etawspvegy vatrtaagtk tdtalveapr sisvatrqqm edrgvqnldd
      181 avrympgiva ssygsdtrad wllvrgfept qfldglplpk gvyanpkqet wnldrlallr
      241 gpassvygqt ppgglldmvs rrpsaesshe iqlqygsdnh rqinfastgk iddegrftyg
      301 lsgvlrdsgt qvdhidnkry niapsltwni dpdtkftllt qftrddtgit sqflpvqgtk
      361 ihsplgnish hknlgdpdwe yydrtyyalg yafehrlndv wqfkqnlryt ksdlsfqalt
      421 pgaypftqvd aqgnvgrsst svdedisqfa vdnnfqgdfa tgdirhtlli gldhqrtntn
      481 ytsifgdglt tnvnnpiygq pivrpsrsta fydydqktyq tglyvqdqma ldqwrltlgg
      541 redwihtgtr ffnkgdatnt erdkkfsgna aisyvfdsgl vpylsyaesf qptskatssp
      601 tesfkptegk qwelgikyqp pgsntlltaa vydltqknvs vtttnsdnvs itsqtgevkv
      661 kgleleavsd vtdnlkviaa ytlaksevqk gdfkgnrlql mpnqqaslwa dytwhngvld
      721 gfgigagary tgntygdqgn twlgkadayt vfdaavhydl srldnslkga slalnatnlf
      781 dkdyistcds fycyygdqrs vvasatykw
//
LOCUS       WP_008009595             334 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM50].
ACCESSION   WP_008009595
VERSION     WP_008009595.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM50
  ORGANISM  Pseudomonas sp. GM50
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  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   4  (residues 1 to 334)
  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 334)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Pseudomonas sp. GM50"
                     /db_xref="taxon:1144332"
     Protein         1..334
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37716
     Region          22..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          248..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mteptslasw tralrkqlda lgldstalcq qagldpqlmd dpnaryplsg ttrlwhiavq
       61 vsgdpaiglr vsrfvspttf halgyalvas gslrevferi vryhqvvsna ldleliraed
      121 ryrfhlkipq gnpapafeai dafaaiyvrt crnrlgrdya plavylrrpe padphqwhkv
      181 frspvyfnad edrlefslvd fdshlddanp elaehnetvl krtlaqlkpl twerkvrdai
      241 eeqlpegeps aeciaqalhl slrslqrhla degcrfdtll nesrenlall hlrdplcslg
      301 eisyllgfad tssfsrafkr wtgmtpgqfr dglr
//
LOCUS       WP_008011431             346 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM50].
ACCESSION   WP_008011431
VERSION     WP_008011431.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM50
  ORGANISM  Pseudomonas sp. GM50
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 346)
  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 346)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 346)
  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   4  (residues 1 to 346)
  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 346)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Pseudomonas sp. GM50"
                     /db_xref="taxon:1144332"
     Protein         1..346
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38892
     Region          27..212
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          257..339
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkpqpmrlgd lsvgfvhsla davrshgldp qplleqygld aarlaeagar lsiprymrlg
       61 hgaiqltddp tlglrmgqls rlsqaglagv taaqaptvre aarclirfea lygsnyrgqs
      121 sfhedaqgaw lrfysispyn aynrfvvdsi itgwlqqlss vspaplraer ieiefeapdy
      181 reayavlgdc piqfgaeqnq lrlsleslaq rnpehcpstw rhllqlcere leqltrtrsl
      241 reritqllgp llnggrepdl eevaarlklp twtlrrklae egtqfrailn dtrrdlamty
      301 irdtelafge iayllgfasa eafqrafkrw ngqtpgefrr shrqsa
//
LOCUS       WP_008011605             248 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Pseudomonas sp. GM50].
ACCESSION   WP_008011605
VERSION     WP_008011605.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM50
  ORGANISM  Pseudomonas sp. GM50
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  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   3  (residues 1 to 248)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Pseudomonas sp. GM50"
                     /db_xref="taxon:1144332"
     Protein         1..248
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28069
     Region          37..242
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mfnalnaeda pqppkvlttp leisgnlrql qdshdpliit fhersqrfqs ylvdvdrdsn
       61 mialdemipr dgerfllage pfkvegfhdg vriawesngp ltidesgdgr cyrgalpdev
      121 vyhqrrnafr aalklaqlvn velggdklks pvsgklldis atgcklrfeg ditarlqlgq
      181 vydrfiaalp fgsmtapvel rylhfeekin ttfagvrfhn msglvqrqve rfvyqlqrea
      241 rrfdkddf
//
LOCUS       WP_008015152             425 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Pseudomonas sp.
            GM50].
ACCESSION   WP_008015152
VERSION     WP_008015152.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM50
  ORGANISM  Pseudomonas sp. GM50
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 425)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Pseudomonas sp. GM50"
                     /db_xref="taxon:1144332"
     Protein         1..425
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47043
     Region          11..417
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 msspiprfkp tesltvtang vmvgelsrie gkgiyfvydk ewlakgfdls pltmtfddkp
       61 qlaresrlfk glhgpfadsl pdgwglllmd rffdatfgag tsltlspldr layigdramg
      121 ifeyhpkaek iaaesvnlar lfeasvevqq gdtpgvlkgl rlaggspgga rpkaiaalsh
      181 dletatsafg qlppgyahwl vkfralsepl etggieqaya vmarragvnm ahtellevqm
      241 rqggferffa akrfdrdgdr kihmitlcal vyadfraptm dysqllklts altksaaeve
      301 kmtrlmifna vfhnyddhtk nfaflyhepq dksgqggwrl spaydltfsd gmgehstafs
      361 ghgkptrkvi rdlckdykyl kpdeyldqtl aalddwdrvl ralkipksag aaihrvlsds
      421 rvrfa
//
LOCUS       WP_008019108             329 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Pseudomonas].
ACCESSION   WP_008019108
VERSION     WP_008019108.1
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 11438136
            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="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=36934
     Region          1..321
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msievrnvsk nfhafkaldn isldiqsgel vallgpsgcg kttllriiag letpdqgniv
       61 fhgedvsghd vrdrnvgfvf qhyalfrhmt vfdnvafglr mkpknqrpse sqiatkvhel
      121 lnmvqldwls drypeqlsgg qrqrialara lavepkvlll depfgaldak vrkelrrwla
      181 rlhedinlts vfvthdqeea mevadrivvm nkgvieqigs pgdvyenpas dfvyhflgds
      241 nrlhlgednh vlfrphevsl srheledhha aevrdirplg attrvtlkve gqsdlieaev
      301 vkdhdsligl akgetlffkp kvwqklani
//
LOCUS       WP_008019828             346 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM55].
ACCESSION   WP_008019828
VERSION     WP_008019828.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM55
  ORGANISM  Pseudomonas sp. GM55
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 346)
  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 346)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 346)
  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   4  (residues 1 to 346)
  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 346)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Pseudomonas sp. GM55"
                     /db_xref="taxon:1144333"
     Protein         1..346
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38816
     Region          27..212
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          257..339
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkpqpmrlgd lsvgfvhsla davrshgvdp qplldqygld aarlseagar lsiprymrlg
       61 hsaiqltdnp alglrmgqls rlsqiglagv taaqaptvre aarclirfea lygsnyrgqs
      121 sfhedaqgaw lrfysispyn aynrfvvdsi iagwlqqlss vspaplraer ieiefeepgy
      181 raaydvlgdc piqfggernq lrlslaslaq rnpehcpstw rhllqlcere leqltrtrsl
      241 reriiallgp llnggrepdl eevaarlklp twtlrrklae egtqfrailn etrrdlamty
      301 irdtelafge iayllgfasa eafqrafkrw ngqtpgefrr shrkta
//
LOCUS       WP_008020099             350 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM55].
ACCESSION   WP_008020099
VERSION     WP_008020099.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM55
  ORGANISM  Pseudomonas sp. GM55
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 350)
  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 350)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 350)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 350)
  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   5  (residues 1 to 350)
  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   6  (residues 1 to 350)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Pseudomonas sp. GM55"
                     /db_xref="taxon:1144333"
     Protein         1..350
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39772
     Region          28..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <150..337
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mrekdsvaay fvqamihglr ndpqrvtavl eqagidpsvm neptarvpan afaalwliqi
       61 relddeffgl dshgmppgsf alicraliqe pdlhkamrqc lanfglflrd frgslavrgk
      121 ravisletcs tnndasrfge etflvlmisl lcwlggrrip idradfrhsr lslgddrllw
      181 gpnltfgaer teiefashyl rlpvvqdlas lkvflrtapq wlvirfrnqh glasqvhqrl
      241 rgshysewpt lqafaleqhl spstfrrkle regcsyqeik devrrgvafe qlrqsdasis
      301 diaerlgfqe psafhrafkk wtgespgryr aryqgergae vanrqefcap
//
LOCUS       WP_008020218             344 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM55].
ACCESSION   WP_008020218
VERSION     WP_008020218.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM55
  ORGANISM  Pseudomonas sp. GM55
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 344)
  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 344)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 344)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 344)
  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   5  (residues 1 to 344)
  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   6  (residues 1 to 344)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Pseudomonas sp. GM55"
                     /db_xref="taxon:1144333"
     Protein         1..344
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38383
     Region          21..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <153..335
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mpklvraavm tnylevtqyl gfnprdvmag vglsraqlqa petripidaa vrlledsaaa
       61 sgcqtfglsm aesrqlsdfg vvslllshqr tlrdalqvvv nyrhlmndsl aifieeagkm
      121 viireevvte tpmpsrqate laigvmfrlc sallgshwhp ysvnfmhqpp enlhlhrrlf
      181 gcnlefgsef ngivcpdisl dmtnpnadpa maryaqsyld slqnhegasm lfevrkaiyl
      241 llpmgratie qvaqsqgmnv rtlqrrlkdd gcafndvind vrrdlvlryl dnpnyslsri
      301 admlgysmas sftrwfisqf gmppatwraq rqssakpvag pkep
//
LOCUS       WP_008020641             345 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Pseudomonas sp. GM55].
ACCESSION   WP_008020641
VERSION     WP_008020641.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM55
  ORGANISM  Pseudomonas sp. GM55
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Pseudomonas sp. GM55"
                     /db_xref="taxon:1144333"
     Protein         1..345
                     /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=37794
     Region          2..276
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 msskkkslei etlrglacll lvlyhvigpl ggglkidigs pfrviadsmv yvrmplftfi
       61 sgyiyaiyki rgndfsaffs gkvrrlivpl fcvgvpfsvl qavgpgvnkd vgvidallsf
      121 yvpvnhfwfl qavfiifmfv gllewrgllr tatrlyllfa faalvfllpp fkfdafging
      181 aiyllpffva gmigrakvgv fkqrfkvigp lvfvlisltl lyvaavdrel ivdrrsligl
      241 tvgcvscial lssdmrskwl twlggysyai flfhvlfaat srfvlgrlgv kdesllvlgg
      301 vacgllgpvv lsivfsrfnf tsvlflgera atrkpaania pvaqs
//
LOCUS       WP_008021707              99 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [Bacteroides].
ACCESSION   WP_008021707
VERSION     WP_008021707.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..99
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11481
     Region          2..97
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mklienniqk iidlckkhkv hklfvfgsvl tsrfndnsdv dlvvdfnkae vsdyfdnffd
       61 fkyalenlfg rkvdlleeqt iknpylkknv datktliyg
//
LOCUS       WP_008022124             336 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Bacteroides xylanisolvens].
ACCESSION   WP_008022124
VERSION     WP_008022124.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides xylanisolvens
  ORGANISM  Bacteroides xylanisolvens
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Bacteroides xylanisolvens"
                     /db_xref="taxon:371601"
     Protein         1..336
                     /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=38866
     Region          1..278
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mtsaksvryn widwsksiai flviwghvpm qsethtiiys fhmplfflis gylynpkgti
       61 keelykdlkt lllpyliyqf ifypywfvre livphqvini hnsiihpliq slssdpingp
      121 twfiyclfmi kiysytiqkk qsiywltagi sslvsilicy wlnqhsiygt yathsffalq
      181 iffftgqalk rtkitnians lhqsiiwlil stvsfatffs mgytsnyttl peivnfhllg
      241 ftgscmilgi gfilnqitst inynvsigtm vilgihwmfi gvfnfaikky lhidnityst
      301 fiafiislli tainypliif ckkhiplllg kiripk
//
LOCUS       WP_008022915             397 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Bacteroidaceae].
ACCESSION   WP_008022915
VERSION     WP_008022915.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidaceae
  ORGANISM  Bacteroidaceae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales.
REFERENCE   1  (residues 1 to 397)
  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 397)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 397)
  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   4  (residues 1 to 397)
  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 397)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Bacteroidaceae"
                     /db_xref="taxon:815"
     Protein         1..397
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45274
     Region          176..395
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          311..393
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mdipalhtlt ngiiigicls isfglvcfkq mahainpkyr rachffiaas liiaaghlae
       61 llvdgfgvyr sldlfsilvl vlassqalmf tfmlillfds ryvtfanvmk haapslvfil
      121 lyvvscciea dvcvyslaew racvvhnlpl avrtlfgvty tvqlfvyvrl ffrkkhryit
      181 hlkeltgeci sklelrwtmr aflyalsigi gawvllvcpg pipefsfsfl ivvfypafaw
      241 lytnyhytye mlrrfiveqd gklsqpplea dmgdlicylq sgdsnhlfee leaylqkeqp
      301 yldynfkrdd likalgtner nlsaavgrat gltlqnyllr lrirhamdll llpdyanhti
      361 ediagasgfk amrtfnrnfr elvkmtptef rqqksvl
//
LOCUS       WP_008022926             496 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [Bacteroidaceae].
ACCESSION   WP_008022926
VERSION     WP_008022926.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidaceae
  ORGANISM  Bacteroidaceae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Bacteroidaceae"
                     /db_xref="taxon:815"
     Protein         1..496
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54223
     Region          4..496
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 metkylrinp adnvavaivn lpagehlsvd dieitlnedi paghkfalkn faegenviky
       61 gypigharma kkqgdwmnet niktnlagll dytynpiqvs ldiphkdltf kgyrrkngdv
      121 gvrneiwiip tvgcvngiig qlaeglrhet egkgvdaiva fphnygcsql gddhentkki
      181 lrdmvlhpna gavlvvglgc ennqpdvfre flgefdedrv kfmvtqkvgd eyeegmeilr
      241 dlyakaskde rtdvplselr vglkcggsdg fsgitanpll gmfsdfliaq ggtsvltevp
      301 emfgaetilm nrckneelfe qtvhlindfk eyflshgepv genpspgnka ggistleeka
      361 lgctqkcgks yvsgvmpyge rlqkkglnll sapgndlvaa ttlaasgchm vlfttgrgtp
      421 fgtfvptmki stnstlaknk pgwidfnagv ivenepmekt cerfidyiik vasgefvnne
      481 kkgyreiaif ktgvtl
//
LOCUS       WP_008023580             326 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM55].
ACCESSION   WP_008023580
VERSION     WP_008023580.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM55
  ORGANISM  Pseudomonas sp. GM55
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 326)
  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 326)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Pseudomonas sp. GM55"
                     /db_xref="taxon:1144333"
     Protein         1..326
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36555
     Region          74..305
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          220..300
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 msiappdeif hlssalpsql nrtigkwems lipteheahi rqhklfhsae lqcsrlefds
       61 svtlvsavpa gcvtfaisha pigrpvvnsh klrpneiivl rsdesvhytc epnetlftlt
      121 ttlehydrcr qrrsvidvla nrtehsfqae nfqfirsaiq aigdacddin dadavlasll
      181 qaltpaggfs rkvptrrkva ieaieyihen tkktltiksl vrqletttrt lhfgfietfg
      241 mspiayirnl rlasarqdli nktwptvtet amfwnfhhlg rfskayqiay getpsetarr
      301 nsakprntts svynqivggl lskpck
//
LOCUS       WP_008024108             762 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor, partial [Pseudomonas sp.
            GM60].
ACCESSION   WP_008024108
VERSION     WP_008024108.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM60
  ORGANISM  Pseudomonas sp. GM60
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 762)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 762)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 762)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..762
                     /organism="Pseudomonas sp. GM60"
                     /db_xref="taxon:1144334"
     Protein         <1..762
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          5..54
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          31..762
                     /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 agaaisfdar qleglkspgl ngafgisegf arilggsglq aepqangtyv lrpapaagsa
       61 lelgatning qmlgattens gsyttgavti gkgehslret pqsvtvmtrk mlddqnlnti
      121 dqvmektpgi tvydstmggk yfysrgfrms gqyqydgvpl dmgslyvqad sfsgdmayyd
      181 rveilrgaag mmkgsggtag gvnfvrkrgq taphtditls ggswdnyrgq vdtggplnes
      241 gtlrgravva eqsrhysvdd asrkdqvyyg aldadlspdt tlglgvayed vdanpcwggl
      301 pryrdrsdlk lsrstcldps wntwrsqrtt vfsdlnhrfn ddwslkvasv ytkntqdiky
      361 afasgavtpg tnttgmlgsm ydydqvdygl dayvdgkfna fgqqhelivg anasrskkdd
      421 fysvaflkqr qnvfnpdkhi pepddsyfid nssrggpvns vtkqkgiyst lrlkladplt
      481 fvvgsrvswy ysetdsdfin tgtsehssat etgqvtpfag vlldlnenlt ayasysdift
      541 pqgnfrsedg salkplvgqs yelgikgawf dgrlnssfnl frtiqkdqaq tdynsscpss
      601 dgycyvnagk vraqgfeaev sgevierlqv lagytytqtk tlddidtsln gaafnsyvpr
      661 hvlrmwgdya lsgplerfti gagvnaqsdn frvspssgek isqsgyavwn grigyriddt
      721 wsvalngnnl fdkryyttig tetfgnyygd prnfmvsvka sf
//
LOCUS       WP_008024649             249 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM60].
ACCESSION   WP_008024649
VERSION     WP_008024649.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM60
  ORGANISM  Pseudomonas sp. GM60
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 249)
  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 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   3  (residues 1 to 249)
  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   4  (residues 1 to 249)
  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 249)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Pseudomonas sp. GM60"
                     /db_xref="taxon:1144334"
     Protein         1..249
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28104
     Region          27..249
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <147..249
                     /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 mfpslnqfkp cdlptllssl qpiatlldtl advvffikds earyvfvnqt larrcgfkhs
       61 gqllgltadq vfparfgply teqdrrvlst greladqlel hlyfgnqpvw clthklalhd
      121 eqgrivglag isrdlqlpqs nhpafqklaa vdahirrhfa rpislaelta iagfsvaqle
      181 rhckrvfqlt prqmihksrl eegsrllldt dlpiteialr cgytdhsafs rqfraltsls
      241 psqyrdsrr
//
LOCUS       WP_008024996             350 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Bacteroides].
ACCESSION   WP_008024996
VERSION     WP_008024996.1
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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..350
                     /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=40250
     Region          3..282
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 megnqsrrid fvdltkgvci ilvvmahvgg afeqldtnsm lscfrmplyf fisgvffksy
       61 egllgfilrk inkliipflf fylsaflmky ivwkiapgvf qlpvswnell vvfhghdlik
      121 fnppiwflla lfncnilfyl ihflrekhlp vmfavtilig cagfylgklq ielplyidvs
      181 mtalpfyvag fwirrynffl ypshrfdkli pvfvvlalvv myftattlgm rtnnytgnif
      241 qvyiaafagi fmimllckkv kkikvvsylg rysiitlsih gpilhflgpl vsryihnswa
      301 qasalllitl sicllltpvf lkvipqmvaq kdllkvkqdh tkktvyedkq
//
LOCUS       WP_008025757             279 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Bacteroides].
ACCESSION   WP_008025757
VERSION     WP_008025757.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 279)
  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 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   3  (residues 1 to 279)
  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   4  (residues 1 to 279)
  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 279)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..279
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32542
     Region          46..279
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          195..273
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mlqqyhtklk gtlaltdsyl tekalqkekg lykfiwvrng sitveidhqe mtltkdevis
       61 lthlqhlefk sidgeyltll fnsnfyciyg ndhevscsgf lfngsshlir ftlnekerke
      121 ldtitealen eftvsdslqe emlrillkrf iiqctriarh rmnitrekes gfeivrqyyn
      181 lvdehyrtkk qvqdyadmlh kspktlsnif stcklpsplr viherveaea krlllysnks
      241 akeiadilgf edqasfsrff knmtgqsavq frntqegkn
//
LOCUS       WP_008027389             403 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [unclassified Pseudomonas].
ACCESSION   WP_008027389
VERSION     WP_008027389.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 403)
  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 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   3  (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   4  (residues 1 to 403)
  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 403)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..403
                     /product="CmpA/NrtA family 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=44048
     Region          16..267
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mnettagpla wvngsdapek tdinlgfmal sdcasvvvaa tqgfaqpygl tlnlkrqssw
       61 anlrdklvsg eldaahslyg liyavhlgig gvaptemavl mglnqngqsi nlshglqalg
      121 vtgpealdrh vhqtrpkltf aqtfptgtha mwlyywlasq gihplhdvds vvvpppqmva
      181 hlqagridgf cvgepwsasa vkhnlgftma ttqtiwpdhp ekvlgctraf veqypntara
      241 lvkaileasr fieesvenrr staqllsapq yldapldcie prllgdyadg lgnrwqdlha
      301 lrfhgagevn qpylsdgmwf mtqfrrwgll rddpdylava rqvqqldlyr eaasavdvds
      361 saremrssql idgkiwdgsd pagyarsfkl hamsdsspll asr
//
LOCUS       WP_008028060             194 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Rhodobacter ferrooxidans].
ACCESSION   WP_008028060
VERSION     WP_008028060.1
KEYWORDS    RefSeq.
SOURCE      Rhodobacter ferrooxidans
  ORGANISM  Rhodobacter ferrooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Rhodobacter group; Rhodobacter.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Rhodobacter ferrooxidans"
                     /db_xref="taxon:371731"
     Protein         1..194
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21134
     Region          1..165
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mfralyhwtl rwagsrqapv alaavsfves svfpipadvl fvpmclsrpe kamryaliat
       61 vtsvlggilg wvigfyffdm iarpilefyg klaafdalrq gtgaeailll lvtsglshlp
      121 pmkvvtilsg vvafdlklfi lsaivargar fyllawllrr ygqaivgfie rrfplvvagv
      181 agalalvwaa vkyl
//
LOCUS       WP_008028349             234 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Pseudomonas sp. GM60].
ACCESSION   WP_008028349
VERSION     WP_008028349.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM60
  ORGANISM  Pseudomonas sp. GM60
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 234)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Pseudomonas sp. GM60"
                     /db_xref="taxon:1144334"
     Protein         1..234
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=25216
     Region          37..204
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 maldrfgfli talllssmsv taayadslea alvkaapdan akvialavra sqcslaqgaa
       61 pvqrlavidy slpsteqrlw vfdlkqrkll fhelvahgrn sgenmavkfs nqnesfatsl
      121 glyrtqssyv gqngyslrme glepgfndna fdraivihga pyvspvlara ngrigrslgc
      181 pavrpaiahk lidsmkdgql lfsyypdqrw lkkssyincg sgtvastakp stnr
//
LOCUS       WP_008030040             633 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Pseudomonas].
ACCESSION   WP_008030040
VERSION     WP_008030040.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 633)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 633)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 633)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..633
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68092
     Region          5..633
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mgqassqaag aehsaakpig mlvaavgvvy gdigtsplyt lkevfsggyg vpvnhdgvlg
       61 ilalifwsli wvvsikymmf vlradnqgeg gimaltalar raaaghkklr tllvvcglig
      121 aalfygdsmi tpaisvlsai eglglafegi dhwvvplsli vlvalfliqs hgtarigilf
      181 gpimvtwflv lgalgvygim qhpevlqamn pvwgvrffiv hpgmgvailg avvlaltgae
      241 alyadmghfg rkpiarawfi lvlpalvlny fgqgalllgd peaarnpfyl lapswalipl
      301 vglstlatvi asqavisgaf sltrqaiqlg yiprmhiqht ssaeqgqiyi gavnwalmvg
      361 vvllvlgfes sgalasaygv avtgtmlmts ilvsavilll wkwppvlavp vllgfllvdg
      421 vyfaanvpki vqggafpvia gialfvlmtt wkrgkqllve rmdegglplp ifissiavqp
      481 phrvqgtavf ltarpdavph allhnllhnq vlheqvvllt vvyediprvp ttrrfevesh
      541 gegffrvilh fgfidepdvp qalklchldd ldfspmrtty flsretvias klegmarwre
      601 alfafmlkna ngnlrffnlp lnrvielgtq vem
//
LOCUS       WP_008030136             425 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Rhodobacter ferrooxidans].
ACCESSION   WP_008030136
VERSION     WP_008030136.1
KEYWORDS    RefSeq.
SOURCE      Rhodobacter ferrooxidans
  ORGANISM  Rhodobacter ferrooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Rhodobacter group; Rhodobacter.
REFERENCE   1  (residues 1 to 425)
  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 425)
  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
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 425)
  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   5  (residues 1 to 425)
  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   6  (residues 1 to 425)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 425)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 425)
  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 20021635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Rhodobacter ferrooxidans"
                     /db_xref="taxon:371731"
     Protein         1..425
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45055
     Region          22..>91
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          101..396
                     /region_name="ASKHA_ATPase_ROK_CYANR"
                     /note="ATPase-like domain of
                     cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and
                     similar proteins; cd24073"
                     /db_xref="CDD:466923"
ORIGIN      
        1 mmpqlrkaar nkasqgcgpl ipplsettrp lrqqvfervr aagliprvql akelgvspas
       61 vttitselie aglieevaap rdgdqgrgrp avalgvrasa hrvagmklsd rehtavivdf
      121 agnliaddvi prrpgamalp elldamatll vrvcakagma padlsalglg vpgfvdceag
      181 vvhwssvltd rlvplaqaat arlglpvhvd ndanlvtlae lwfgagrals dfavvtiehg
      241 vgmgyvlnhr iyrggqglgm elghtkvqld galcrcgqrg cleayvadya lareatialn
      301 wshkegqsin vlleslydha kagnsaarsi frragrylav glsnvvnlfd paliilsger
      361 mrydylyaae tlaemenlsi atgrprapie ihawgdllwa hgaaalalsa vseglvapyr
      421 eiaaq
//
LOCUS       WP_008030351             160 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [unclassified
            Pseudomonas].
ACCESSION   WP_008030351
VERSION     WP_008030351.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..160
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17305
     Region          14..159
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 midlqqsgqg legygmlhaq leslladerd fianaaqfsa flynqlddln wagfylnrne
       61 elvlgpfqgq iacvripfgr gvcgtaaatl qtqlvedvha fpghiacdsa snselvvplv
      121 kdgrligvld ldspklarft ehdqagiekl aaiflrltdc
//
LOCUS       WP_008030590             143 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Rhodobacter ferrooxidans].
ACCESSION   WP_008030590
VERSION     WP_008030590.1
KEYWORDS    RefSeq.
SOURCE      Rhodobacter ferrooxidans
  ORGANISM  Rhodobacter ferrooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Rhodobacter group; Rhodobacter.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Rhodobacter ferrooxidans"
                     /db_xref="taxon:371731"
     Protein         1..143
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15292
     Region          16..141
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mielgglfla afaaatlipa qseavlvali lsanqpvwll llvatvgnvl gsavnwamgr
       61 flirfagrrw fpasvtqidk atgwyarwgh wsllaswvpv igdpltlvag vlrepfgrfl
      121 livtlakggr ylalawithg las
//
LOCUS       WP_008030697             780 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Rhodobacter
            ferrooxidans].
ACCESSION   WP_008030697
VERSION     WP_008030697.1
KEYWORDS    RefSeq.
SOURCE      Rhodobacter ferrooxidans
  ORGANISM  Rhodobacter ferrooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Rhodobacter group; Rhodobacter.
REFERENCE   1  (residues 1 to 780)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 780)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..780
                     /organism="Rhodobacter ferrooxidans"
                     /db_xref="taxon:371731"
     Protein         1..780
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=85436
     Region          236..747
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mflereglrg raralipadp kiyahlpyvi elddevvrtr dnglmislev tgidgitsgs
       61 saitalragf ahlldtlder fsfylhrmmr panaqlkpih gqsfaadidr awsgelqrrn
      121 lqesvliltv vrrqvaplav plfgkaaakv wgedtdrrle elrevvsile tglgvkshrl
      181 kiregsligf yaslltgelr nkprsafgii aedasdaair fgkgqftlee gadtprvgav
      241 lyvksyatst wpgmldalga srdtiithsy tpiergsite rvkrrvaqmr asediaatie
      301 aqlfeaadks esgelgfgih qmtitvfagd qaaldtevar irgiahqngm rlvrevtale
      361 aaffamhpgn mdyrardmtv sslnfadmaa lhaadtgtea srlpwqtplt lfqtlqgslh
      421 rfsfhepgdp laeptnghtl vlgksgggkt ttvaflaaqa qraggrtiif dkeaglkmav
      481 ralggryaei ragrptglnp latesgerge awfldwlval leqrsgpmtp lqsealksai
      541 sqngkaregl rnfrafqelf gdvgdgldla qrisewgpeg rygwvfgeas epvvdftshd
      601 vtavdlteil dlgtertail gylfrrieml ieekrptlil ideawkvldd eyfakklaew
      661 lvtarkknvv vvmmtqfpsq irgskarsil ealpnqllfp ngeaasadyd gfrltdgeld
      721 fvlspipgqr mvlsrtprss tvlnvdlkal gplltalggg qagqnafgad yanrpkfwke
//
LOCUS       WP_008031662             252 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein, partial [Rhodobacter ferrooxidans].
ACCESSION   WP_008031662
VERSION     WP_008031662.1
KEYWORDS    RefSeq.
SOURCE      Rhodobacter ferrooxidans
  ORGANISM  Rhodobacter ferrooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Rhodobacter group; Rhodobacter.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Rhodobacter ferrooxidans"
                     /db_xref="taxon:371731"
     Protein         <1..252
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
     Region          2..203
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 agndaitggt gvdtalylgt gavtvslalt vaqvtgqgsd rlleienlqs gsgndrlqgn
       61 tganllvsga gndtlrgdag ndtltgedga dqllgdagdd vlfggagnds lwgglgndrl
      121 eggmgydslm geagadtllg gvandtldgg tdsdlldggg ggdrltgglg adrfvfsiga
      181 dvitdfrltd gdrlviddav llavrgmtaa qvvtsfahdm gtyvsfdfga gntvrldgla
      241 ntidlahsll li
//
LOCUS       WP_008031995             316 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Rhodobacter
            ferrooxidans].
ACCESSION   WP_008031995
VERSION     WP_008031995.1
KEYWORDS    RefSeq.
SOURCE      Rhodobacter ferrooxidans
  ORGANISM  Rhodobacter ferrooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Rhodobacter group; Rhodobacter.
REFERENCE   1  (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   2  (residues 1 to 316)
  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 316)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Rhodobacter ferrooxidans"
                     /db_xref="taxon:371731"
     Protein         1..316
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34779
     Region          14..67
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mshkatvwai qqrglkpatk ivlwflcdrh npdfgcfptq arladdaems isalnehlar
       61 leesrlihrv rvhdprthkr qatryilgfe dgfppeptpe tgdgfegtdg erggdptpes
      121 ghgaisgfsv kpspdfaqsh lrnpetnlvr eplskpvkee egaqacaais dqffgevlaa
      181 lgldpaalpg wwqgwpprlh vqrwrdelgl teaeivtvae asrqehpapp dgpkaldram
      241 qraaqrkvea agqkrrkrks epapaakpit dlpafyakiv nadgylpvsa inntmrdaml
      301 grglvtaerl rergvr
//
LOCUS       WP_008033000             199 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Rhodobacter
            ferrooxidans].
ACCESSION   WP_008033000
VERSION     WP_008033000.1
KEYWORDS    RefSeq.
SOURCE      Rhodobacter ferrooxidans
  ORGANISM  Rhodobacter ferrooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Rhodobacter group; Rhodobacter.
REFERENCE   1  (residues 1 to 199)
  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 199)
  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   3  (residues 1 to 199)
  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   4  (residues 1 to 199)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 199)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 199)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Rhodobacter ferrooxidans"
                     /db_xref="taxon:371731"
     Protein         1..199
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21250
     Region          17..194
                     /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"
ORIGIN      
        1 mkrrvrsqnl agaqawllhr phptvqalqr qlaaiglmve qcwpdlpaaa lgadfiffda
       61 dqgddaqfpw apgaapmpmi aligseapgr iewalnagad aqllkpvgdg gafsalltar
      121 atfdlrqals aqiadlqqrl dqrqtvvrav tmlmglgrte deayaqlrqm amawrisfea
      181 aalriveagr gpaagkvgp
//
LOCUS       WP_008034389             334 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Pseudomonas].
ACCESSION   WP_008034389
VERSION     WP_008034389.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  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   4  (residues 1 to 334)
  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 334)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..334
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37724
     Region          22..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          248..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mteptslasw tralrkqlda lgldstalch qagldpqlmd dpnaryplsg ttrlweiavq
       61 vsgdpaiglr vsrfvspttf halgyalvas gslrevferi vryhqvvsda ldlelsrted
      121 ryrfrlkipp gnpapafeai daftaiyvrt crnrlgrdya plavylrrpe padahqwhkv
      181 frspvhfsad edrlefalvd fdshlddanp elaehnetvl krtlaqlkpl twerkvrdai
      241 eeqlpegeps aehiakalhl slrslqrhla degcrfdtll nesrenlall hlrdpqcsls
      301 eisyllgfad tssfsrafkr wtgmtpgqfr dglr
//
LOCUS       WP_008034797             816 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pseudomonas sp. GM60].
ACCESSION   WP_008034797
VERSION     WP_008034797.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM60
  ORGANISM  Pseudomonas sp. GM60
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 816)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 816)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 816)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..816
                     /organism="Pseudomonas sp. GM60"
                     /db_xref="taxon:1144334"
     Protein         1..816
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=88548
     Region          12..816
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 maspalthfl prfgvaaava gvlslsgcqt wnaqdtlppt tgvqplkgla qnvsvrrnam
       61 gvpliesssf hdalftlgyv hasdritqmv tlrllaegrl semsgsdlld adrymravnl
      121 kksagelyka ssprlkrffe vyargvnayl fryrdklpad ltatgykpey wkpedsalif
      181 cllnfsqsan lpeevsslvl aqsvttdklp wltpsapdek lpvaeaeklh glklngaipg
      241 laeiskatgq lsdlnllgat ssnnwaiapq rsrsgkslla sdshgplgap slfsyvqira
      301 pkyqasgvti aglpmvlggf ngkvawsmts vmgdnqdlfl ekiqrqgngl syevggkwqp
      361 vivrnetyfv kgqrpireav yetrhgplln sakgtalgng lglalqtpnf tddksldaff
      421 dlsraqtvek asdasreira itlnlvfada snigwqvtgr ypnrregegl lpspgwegry
      481 dwdgyadaml hpydqdpaqg wlgtanqrvi phgygmqlsn swsaperger maelagvgkh
      541 dtrsvitmqy dqtttfvakl kkmfaapgma qplkqaieal pvadrgkahe aftrlmafdg
      601 klaatsadaa iyelflqesa kqtfldelgp esspawkafi angklsyaaq adhllgreds
      661 pfwddartpq kedkpailar slaaaitagd sqlggdhkaw qwgklhryew knasgqtvrg
      721 plaaggdhtt lntaafawgq dfnttlapam rfivdfgqae plmgqngtgq sgnpaspnyl
      781 dsvdpwlkgq yvslpmqpqn fdkvygtkrl tltpgk
//
LOCUS       WP_008037670             234 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [unclassified Pseudomonas].
ACCESSION   WP_008037670
VERSION     WP_008037670.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 234)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..234
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=25284
     Region          37..204
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 maldrfgfli talllsstsv taayadslea alvkaapnan akvialavra sqcslaqgaa
       61 pvqrlavidy slpsteqrlw vfdlkqrkll fhelvahgrn sgenmavkfs nqnesfatsl
      121 glyrtqssyv gqngyslrme glepgfndna fdraivihga pyvspvlara ngrigrslgc
      181 pavrpaiahk lidsmkdgql lfsyypdqrw lkkssyincg srtvastakp stnr
//
LOCUS       WP_008038926             332 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Pseudomonas].
ACCESSION   WP_008038926
VERSION     WP_008038926.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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   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   4  (residues 1 to 332)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..332
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=36412
     Region          1..323
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 miqienlnkk fgsitavedv sfnveegqic vllgpsgcgk tttlkminrl itptsgtiri
       61 ggrdtaelds vtlkrsigyv iqqvglfpnm tveenicvvp nllgwdktks rkraaellev
      121 valdpskflk rypcelsggq qqrvgvaral aadppvmlmd epfgaidpin rdviqdefmr
      181 iqrqvgktvl fvshdideav kmadcvalfh ngkieqfgss ddllarpnse fvanfmggdr
      241 imkrlrllra advaskippr eqmqivggns aistrsqlvv kpgddlrqvl sqllgrgqdw
      301 alcndsdgrf igyvhqtdil arlvdnitpa vh
//
LOCUS       WP_008039689             329 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [unclassified Pseudomonas].
ACCESSION   WP_008039689
VERSION     WP_008039689.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..329
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=36895
     Region          1..321
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msievrnvsk nfnafkalnd isldiqsgel vallgpsgcg kttllriiag letpdqgniv
       61 fhgedvsghd vrdrnvgfvf qhyalfrhmt vfdnvafglr mkpknqrpte sqiaakvhel
      121 lnmvqldwls drypeqlsgg qrqrialara lavepkvlll depfgaldak vrkelrrwla
      181 rlhedinlts vfvthdqeea mevadrivvm nkgvieqigs pgdvyenpas dfvyhflgds
      241 nrlhlgedkh vlfrphevsl srheledhha aevrdirplg attrvtlkve gqsdlieaev
      301 vkdhdsligl akgetlffkp kvwqkvani
//
LOCUS       WP_008039818             757 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [unclassified Pseudomonas].
ACCESSION   WP_008039818
VERSION     WP_008039818.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 757)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 757)
  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   3  (residues 1 to 757)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..757
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..757
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79856
     Region          6..756
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msfgadeeil qdflveagei leqlseqlve lesrpddadl lnaifrgfht vkggagflql
       61 nelvecchia envfdilrkg errvdselmd vvlealdavn gmfsevrerg pitaatpell
      121 aalarlaepq tadqaapvae vveepaaeae sgditdnefe qlldslnavk aqaeapaava
      181 lpagdaatsd eitdaefesl ldqlhgkgqf avdavatpaa paapaapkap gdssditdde
      241 fealldqlhg kgnfavdale saiasvptpa aptaaaaggd lisdhefesl ldelhgkgkf
      301 tevgtgsaas svatpvakap apvakapepk aeaakpaaaa apkpaaaaaa paparaaaap
      361 paekpaseae ttvrvdtarl deimnmvgel vlvrnrlvrl gansadeams kavsnldvvt
      421 adlqtavmkt rmqpikkvfg rfprlvrdla rqlkkeinle lvgeetdldk nlvealadpl
      481 vhlvrnsvdh gieepadrea mgkprsgkvi lsaeqegdhi llsisddgkg mdadvlrgia
      541 vkkglmdkda adrlsesdcf nlifapgfst kteisdvsgr gvgmdvvktk iaqlngtini
      601 ystkgkgski vikvpltlai mptlmvmlgn qafafplvnv neifhldlst tnvvdgqevv
      661 ivrdkalplf ylkrwlvssa aheeqreghv vilsvgtqri gfvvdqlvgq eevvikplgk
      721 mlqgtpgmsg atitgdgria lildvpsmlk ryaarri
//
LOCUS       WP_008040365             147 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Bartonella tamiae].
ACCESSION   WP_008040365
VERSION     WP_008040365.1
KEYWORDS    RefSeq.
SOURCE      Bartonella tamiae
  ORGANISM  Bartonella tamiae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Bartonella tamiae"
                     /db_xref="taxon:373638"
     Protein         1..147
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=15601
     Region          59..133
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mkkialiamm ttacagvafa qaptapttps taystaqtdh atndmaalyv tptktdfvas
       61 slintkvlnl qdetigeikd vviqkneieg ivigvggflg vgeryvvvdp stirmtndng
      121 swkvitnatk aslesapefk yegrwdl
//
LOCUS       WP_008040533             409 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [unclassified Pseudomonas].
ACCESSION   WP_008040533
VERSION     WP_008040533.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 409)
  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 409)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..409
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46236
     Region          2..404
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mpamlsfsik qarrlalaaq gfngrqppaa ikavqlnrli erlgilqids vnalvrshyl
       61 plfsrlgnys sdlldqaaws sgrrrtlfey wgheasllpl smyplmrwrm qragrgediy
      121 qqlarfgreq qdtvrrvlas veelgalgag slstrqerag pwwdwsaekh alewlfaage
      181 vtvagrrgfe rlydlpervi psailqqpll aedeaqrgll lhaanalgva tekdlrdyfr
      241 lspgdarprl aelvevgell tcevqgwrqp gfclpepkvp rkveasalls pfdsliwers
      301 rterlfdfry rleiytppdk rvygyyvlpf lyneriaarv dlraeralgr lavhavheee
      361 pgldeegmla lavnlrrmad wlglervqln cpresagrlr valagiggd
//
LOCUS       WP_008040758             803 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: penicillin acylase family protein [unclassified
            Pseudomonas].
ACCESSION   WP_008040758
VERSION     WP_008040758.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 803)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 803)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 803)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..803
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=88694
     Region          18..800
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkrsltvlal livalaagag gyiyskqptr qgmvelqhlq gsvtvryder giphiraene
       61 tdlyralgyv haqdrlfqme vlrrlargel aevlgpklld tdklmrslri reraetylan
      121 mdkqspafia mqayldginq yqdshakpae fdvlgipkrp ftaqdtisia gymaysfaaa
      181 frteplltyv rdqlgaeyln vfdldwqskg vlannhsstp pplasadwkd lnalarlseq
      241 aladnglpqf egsnawvvag nrtksgkpll agdphirfsa psvwyeaqls apgfelyghy
      301 qalmpfaslg mnrdfgwsit mfqnddldli aekvnpdnan qvwyrgkwvd mvtseqqiav
      361 kgqppvklll rqsphgpivn dalgnsvgkt piamwwgfle sqnpilegfy qlnradtlak
      421 arsaaakvqa pglnivwana kgdigwwaaa qlpkrpagvr pwfildgssa eadkdgfypf
      481 sanpqeenpa rgyivsanfq pvsptgmeip gyynladrgq qlnrqlsdka vkwdleasqk
      541 lqlgtttayg prllapllpv lrevvsdpae lklveqlaqw tgdypldsts atlfnqflfn
      601 ladatmhdel gndffetlls trvidaalpr laanadspww dnrntlgket radtvkvawq
      661 aslahlkstl gadftqwqwg kahtlthghp lgqqkpldri fnvgpfaapg thevpnnlsa
      721 kigpapwpvt ygpstrrlid fadpahsltv npvgqsgvpf drhfddqaea yvegvyfqah
      781 lndeevtant rstlkllpar saq
//
LOCUS       WP_008041399             232 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Reinekea blandensis].
ACCESSION   WP_008041399
VERSION     WP_008041399.1
KEYWORDS    RefSeq.
SOURCE      Reinekea blandensis
  ORGANISM  Reinekea blandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Saccharospirillaceae; Reinekea.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 232)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Reinekea blandensis"
                     /db_xref="taxon:374838"
     Protein         1..232
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=25899
     Region          5..220
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 maiamafqpi vncrdhsifa yealvrgpkg esagsilnqv tegnkysfdq acrveaiktm
       61 agldrsarls inflpnaiyn pntciqrtls aakqyqydts klifevvehe episqhklse
      121 iftayramgf ttaiddfgag ysglnqlldl kpdlikldra lvdgidqnpd kkivvkhlva
      181 mlkdmriqvl aegverreey ellhqlgidl mqgyyfarpl lgalpvvpes cw
//
LOCUS       WP_008041671             161 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Reinekea blandensis].
ACCESSION   WP_008041671
VERSION     WP_008041671.1
KEYWORDS    RefSeq.
SOURCE      Reinekea blandensis
  ORGANISM  Reinekea blandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Saccharospirillaceae; Reinekea.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 161)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Reinekea blandensis"
                     /db_xref="taxon:374838"
     Protein         1..161
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17405
     Region          9..157
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 maeqlttsts ddrltqyrdl llqlkgltdg epnrvanlan vaaalrqtfg ffwvgfycve
       61 geelvlgpfq gdiactriay grgvcgtawq eatpqwvpdv dafpghiacs sesrsevvvp
      121 ilkddevvav ldvdsdrlnd fteadvagls eisawlgtsq f
//
LOCUS       WP_008041905             269 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Reinekea
            blandensis].
ACCESSION   WP_008041905
VERSION     WP_008041905.1
KEYWORDS    RefSeq.
SOURCE      Reinekea blandensis
  ORGANISM  Reinekea blandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Saccharospirillaceae; Reinekea.
REFERENCE   1  (residues 1 to 269)
  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   2  (residues 1 to 269)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Reinekea blandensis"
                     /db_xref="taxon:374838"
     Protein         1..269
                     /product="aminoglycoside 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=29581
     Region          2..225
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mklkkiaegn taevfslepg kviklyhvgy padeaikeae kcevafkqgl ptprvidltt
       61 mdgrqgivfd ecsgptmear lrdhptdidl maktfaqlhh qihdcsgmgl pttqertgmk
      121 ishaqildek trsalqaels qqpgethfch gdfhpgnvll tekgpvlidw vdatmgspva
      181 dvartlmlir yseipaepte alafnrmkda fldaylahyt slrafpeqam drwlplisaa
      241 rlsenatgpd qtkailslve tsidrslng
//
LOCUS       WP_008043521             117 aa            linear   BCT 20-JAN-2025
DEFINITION  PilZ domain-containing protein [Reinekea blandensis].
ACCESSION   WP_008043521
VERSION     WP_008043521.1
KEYWORDS    RefSeq.
SOURCE      Reinekea blandensis
  ORGANISM  Reinekea blandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Saccharospirillaceae; Reinekea.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (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   3  (residues 1 to 117)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 117)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Reinekea blandensis"
                     /db_xref="taxon:374838"
     Protein         1..117
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12615
     Region          1..117
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mnpklggars gilsitmkdk avlyaaympf vkngglfiat nkrfnigddv fllltlmdep
       61 ekipvagkvi wmtprgaqgn ratgigvqfs kknelakdki etylagslns dkpthtm
//
LOCUS       WP_008044057             180 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Reinekea blandensis].
ACCESSION   WP_008044057
VERSION     WP_008044057.1
KEYWORDS    RefSeq.
SOURCE      Reinekea blandensis
  ORGANISM  Reinekea blandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Saccharospirillaceae; Reinekea.
REFERENCE   1  (residues 1 to 180)
  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 180)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 180)
  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   4  (residues 1 to 180)
  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   5  (residues 1 to 180)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Reinekea blandensis"
                     /db_xref="taxon:374838"
     Protein         1..180
                     /product="TRAP transporter small permease subunit"
                     /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=20525
     Region          17..180
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mstqdndqqe htpknpldra lkwlgdvasl lfvltvlisf yevmmryvfn sptiwvheta
       61 sflggmlfvl ggsyalatnr hvrvvllyds vsehtrkiln lfhhvmgmvf aalmiyasyh
      121 mvqaswfspl ggihlessgs awdpdfpayt klfiliifiv mfvqfllhli qeiielrsdr
//
LOCUS       WP_008044709             260 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [unclassified
            Pseudomonas].
ACCESSION   WP_008044709
VERSION     WP_008044709.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..260
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=28973
     Region          26..176
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkfltlfvsl illagcasgp rfdtshpsan hdsrvqfvvv hytsaslers lqllthgevs
       61 shyligddkn atiyklmden qrawhagese wqgrtwlnss sigieivnpg fkelptggry
      121 wypyseaqvq slivllkdis krhainphsi ighsdiapfr kldpgplfpw krlaaeglgv
      181 wpdeqavarq qvqfdsklps vswfqaqlar lgyatpqtge ldvatrhvig afqmhfrpsr
      241 fdgmpdaqta allqvlnqtk
//
LOCUS       WP_008046058             354 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Reinekea blandensis].
ACCESSION   WP_008046058
VERSION     WP_008046058.1
KEYWORDS    RefSeq.
SOURCE      Reinekea blandensis
  ORGANISM  Reinekea blandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Saccharospirillaceae; Reinekea.
REFERENCE   1  (residues 1 to 354)
  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 354)
  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 354)
  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 354)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Reinekea blandensis"
                     /db_xref="taxon:374838"
     Protein         1..354
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39961
     Region          19..350
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mksllqnlar wlvpvcfiaf sfseepyqlk lamswgsdfp vfsespkrma ervakmsngr
       61 ltidvigsee hgrpldvfdm vrngeydlgh sasyywkgkv pntlffttmp fgmlpleqya
      121 wlehgggqal mdevyqplgl lslpggnsgs qmggwfqkri knteslnglk mrvpgfagev
      181 lselgvvptn ipatdlyeam srnviqaaef vgpstdfnlk lhlaaqfyyt gwhepgaelq
      241 flindevyqs lpadlqailk aamrasaydt yvhsvdvsaq awadmrrqfp tirvkdfpde
      301 vmselrrvne rklvefaddn dqarriiesq lgyqammrnw tllsdysyle sigr
//
LOCUS       WP_008045555             332 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM74].
ACCESSION   WP_008045555
VERSION     WP_008045555.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM74
  ORGANISM  Pseudomonas sp. GM74
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 332)
  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 332)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 332)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 332)
  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   5  (residues 1 to 332)
  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   6  (residues 1 to 332)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Pseudomonas sp. GM74"
                     /db_xref="taxon:1144336"
     Protein         1..332
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36689
     Region          23..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          95..329
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mlhshlttln avslvldafk aqglsseall agsgisaadl nradtrittn qemqvcanav
       61 alkrdiglel grrmhvscyg mlgyalltsa tfgdalrlai rypallgtlf elsleddger
      121 iwfaaadyre spamavfnae fclvslkvtc ddllghplpl lgarfehaap dyeatyaehf
      181 ncplhfgarn nafafdkrwl dqplpladvi thqamaercr kqnleftgrq awlgrirqll
      241 saqlnaapgl eglagqmncs artlrrhlkd mgcsyqelld elrfeqakqm lcedqlpiyq
      301 iaealgfset asfrhafvrw sgvapsqfrp hg
//
LOCUS       WP_008046059             358 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Reinekea blandensis].
ACCESSION   WP_008046059
VERSION     WP_008046059.1
KEYWORDS    RefSeq.
SOURCE      Reinekea blandensis
  ORGANISM  Reinekea blandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Saccharospirillaceae; Reinekea.
REFERENCE   1  (residues 1 to 358)
  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 358)
  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 358)
  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 358)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Reinekea blandensis"
                     /db_xref="taxon:374838"
     Protein         1..358
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40368
     Region          3..346
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mimkrmtlil scllisrltl aadvitlkla etwgpdypif gdatknfaal aaelsggrln
       61 iqidsadvhq qplgvfdlvk sgdydmghsa syywtdkvpn tqyfstmpfg miaseqyswf
      121 yfddgmalmd evyaphnlys fpggntgqqm ggwfkqeirt pddldglrmr ipgfageima
      181 elgvqpvnlp sgelyqalin reidalewvg psldlamgfp naaeyyytgw hepatelqfl
      241 inrevfnglp tdlqeilkva mrlsaydmwv qsqhesaknw atmleqnpni kvrqfsdeim
      301 kqlreanrrl laqkaeqdpl aariiasqqa ylekarawid iseraytgnm dargnrsq
//
LOCUS       WP_008046097              93 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Reinekea blandensis].
ACCESSION   WP_008046097
VERSION     WP_008046097.1
KEYWORDS    RefSeq.
SOURCE      Reinekea blandensis
  ORGANISM  Reinekea blandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Saccharospirillaceae; Reinekea.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 93)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Reinekea blandensis"
                     /db_xref="taxon:374838"
     Protein         1..93
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10604
     Region          1..82
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 manafdygtk efstlinrhf gknfyefvns yriqeatdrl idpahqtesi tevylasgfn
       61 sksvfntlfk kthdmtpsqy rrlsipvtvt kta
//
LOCUS       WP_008046932             350 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM74].
ACCESSION   WP_008046932
VERSION     WP_008046932.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM74
  ORGANISM  Pseudomonas sp. GM74
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 350)
  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 350)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 350)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 350)
  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   5  (residues 1 to 350)
  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   6  (residues 1 to 350)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Pseudomonas sp. GM74"
                     /db_xref="taxon:1144336"
     Protein         1..350
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39715
     Region          28..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <150..334
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mrekdsvaay fvqamihglr ddpqrvtavl eqagidpavm hqptarvpan afaalwliqi
       61 relddeffgl dshgmppgsf alicraliqe pdlhkamrqc lanfglflrd frgslavrgk
      121 ravisletrs tdndasrfge etflvlmisl lcwlggrrip idradfrhsr lslgddrllw
      181 gpnltfgaer teiefashyl rlpvaqdlas lkvflrtapq wlvirfrnqh glasqvhqrl
      241 rgshysewpt lqafaleqhl spstfrrkle regcsyqeik devrrgvafe qlrqseasis
      301 diaeqlgfqe psafhrafkk wtgespgryr aryqgeqgae vatlqepcep
//
LOCUS       WP_008048305             110 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Reinekea blandensis].
ACCESSION   WP_008048305
VERSION     WP_008048305.1
KEYWORDS    RefSeq.
SOURCE      Reinekea blandensis
  ORGANISM  Reinekea blandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Saccharospirillaceae; Reinekea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Reinekea blandensis"
                     /db_xref="taxon:374838"
     Protein         1..110
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12658
     Region          7..92
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(22,51..52,54,77)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(22..23,31,32,34..35,37,40..41,43,51,56)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mtdrtvfyqt lagipqgyyt sygrladlcg vhvrqvqawl rtlprdtelp wfriinsqrk
       61 itehpgaprq yqrlaeegli pddrgrfpld rywptsapag qniketqvrs
//
LOCUS       WP_008048624             191 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Pseudomonas].
ACCESSION   WP_008048624
VERSION     WP_008048624.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 191)
  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 191)
  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   3  (residues 1 to 191)
  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   4  (residues 1 to 191)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 191)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            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="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21513
     Region          1..191
                     /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"
ORIGIN      
        1 mlrillindt akkvgrlkaa lteagfevid esgltidlpe rvetvrpdvi lidtespgrd
       61 vmeqvvlvtr dqprpivmft dehdpdvmrq aiksgvsayi vegihaqrlq pildvamarf
      121 esdqalraql hardqqlaer krielakgll mkmkdcneee aytlmrrqam srqqkliqva
      181 eqiiamsell g
//
LOCUS       WP_008048854             346 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM74].
ACCESSION   WP_008048854
VERSION     WP_008048854.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM74
  ORGANISM  Pseudomonas sp. GM74
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 346)
  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 346)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 346)
  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   4  (residues 1 to 346)
  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 346)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Pseudomonas sp. GM74"
                     /db_xref="taxon:1144336"
     Protein         1..346
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38758
     Region          27..212
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          257..339
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mnpqpmrlgd lsvgfvhsla davrshgvdp qplldqygld aarlseagar lsiprymrlg
       61 hsaiqltdnp alglrmgqls rlsqaglagv taaqaptvre aarclirfea lygsnyrgqs
      121 sfhedaqgaw lrfysispyn aynrfvvdsi iagwlqqlss vspaplhaer ieiefeepgy
      181 raaydvlgdc piqfggernq lrlsltslaq rnpehcpstw rhllqlcere leqltrtrsl
      241 reriiallgp llnggrepdl qevaarlklp twtlrrklad egtqfrailn dtrrdlamty
      301 irdtelafge iayllgfasa eafqrafkrw ngqtpgefrr shrqst
//
LOCUS       WP_008051459             745 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Limnospira indica].
ACCESSION   WP_008051459
VERSION     WP_008051459.1
KEYWORDS    RefSeq.
SOURCE      Limnospira indica
  ORGANISM  Limnospira indica
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Sirenicapillariaceae;
            Limnospira.
REFERENCE   1  (residues 1 to 745)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 745)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..745
                     /organism="Limnospira indica"
                     /db_xref="taxon:147322"
     Protein         1..745
                     /product="CHASE2 domain-containing protein"
                     /EC_number="4.6.1.-"
                     /function="13 : Signal transduction"
                     /function="16.12 : Sense"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016849 - phosphorus-oxygen lyase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=83344
     Region          16..649
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mpktirerfw nwrvvlvttp svtlavillr ltgilqtlel aaydqymrwr ppetrdsriv
       61 ivgidendlq figqgyvpdg vyfeliqrln amnprvigld iyrdlpfepg hsqlvrlfet
      121 tdnligiekv igdhffsrvg pppalaargq vgandlivdq dnrvrrally fprengetvh
      181 sfavhlalry lsaepdfsve ivegtdnwwk fgdvvfvpfe gndggyvrad dggyqvllny
      241 rgpsqhfeiv smrdifenrv asdwgsdrii ligsvgesmk dlfsipytla pdqrmtgvei
      301 hanivskiis aalenrplir tlpevvewll imfwsglgat ltwrlrdptr vgqflfkrvv
      361 ilvlaggill gftwvaflgs wwlpvvpssi alvgsvavit ayiarsasdi rktfgrylsd
      421 eivanllehp eglkmggerr kitiltsdlr gftalserlp peevvqvlnf ylsymadvit
      481 hyqgtidefm gdgilvlfga ptlreddper avacavamql amaqvneqme kwelpalemg
      541 igintgevvv gnlgsekrtk ygvvgshvnl tyriesyttg gqiiiseetl ncttpnwvki
      601 ddkklvqpkg vknpiaiyev sgiagkynlf lpketeifys lsqpislqyt vlegkhvgen
      661 lfsgrllqls drsaligaed gtdslplvlt niklnlkssn lelrediyak vlekpaepgk
      721 fyirftskpp vieaklndiy qmikg
//
LOCUS       WP_008052106             139 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Pseudomonas sp. GM74].
ACCESSION   WP_008052106
VERSION     WP_008052106.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM74
  ORGANISM  Pseudomonas sp. GM74
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Pseudomonas sp. GM74"
                     /db_xref="taxon:1144336"
     Protein         1..139
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14179
     Region          2..135
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mnnqkgftli ellvvvaiig ilatlglpmy skyqarakvt aalaeltamk vpfedvisqg
       61 etptianvap agktstnhct lsvtattpga gsvvctlhna pgvvqgktvt ltrdeakgws
      121 ckssvsedyl pkgcsgsaa
//
LOCUS       WP_008052152             117 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Pseudomonas sp. GM74].
ACCESSION   WP_008052152
VERSION     WP_008052152.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM74
  ORGANISM  Pseudomonas sp. GM74
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Pseudomonas sp. GM74"
                     /db_xref="taxon:1144336"
     Protein         1..117
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12666
     Region          6..112
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(34,65..66,68,94)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(34..35,43,46,48..49,51,54..55,57,65,70,77)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mtdptdepes aaqirrtvly ltlaqvpegk vvsygqlael aglgraarwv grtlsqlpgd
       61 sklpwhrvla angrislpag spsgdeqrar lrmegisiln nhvdiqrhgw rpvehsg
//
LOCUS       WP_008051503             332 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM74].
ACCESSION   WP_008051503
VERSION     WP_008051503.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM74
  ORGANISM  Pseudomonas sp. GM74
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 332)
  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 332)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 332)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 332)
  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   5  (residues 1 to 332)
  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   6  (residues 1 to 332)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Pseudomonas sp. GM74"
                     /db_xref="taxon:1144336"
     Protein         1..332
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38142
     Region          22..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          92..330
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mrertiashf araalggarr hgydysgllq qlgispelld eprariapeq ftqliqalwl
       61 alddeylgfg qapsrpgsfa mmchavihcr nlekalhrgl lfyslfpgap rltlsredew
      121 vrlslddsrl wdpdhflses llviwhrfgs wligqrirle qatfsyprpe hgaeydllfs
      181 cplefsrpqs sllfhsryla mpllqdertl khflerspad llsrpddgds lssrlrrlls
      241 rdsshwpdle avaahlhisp qtlrrhlree gssfqelkdq lrrdiaiyhl sradlslqqi
      301 aeqlgfseps afhrafkkwt gltpgayraq en
//
LOCUS       WP_008052229             699 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Pseudomonas sp. GM74].
ACCESSION   WP_008052229
VERSION     WP_008052229.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM74
  ORGANISM  Pseudomonas sp. GM74
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 699)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Pseudomonas sp. GM74"
                     /db_xref="taxon:1144336"
     Protein         1..699
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73206
     Region          6..696
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 msqtirdnlk rmlapqhvaf vggrsmaral krcaeggypg qmwlvnpqhd slegvpcvrs
       61 vcelpcgpda vfiatnrelt ltcvaelaai gaggaicyas gfaetgaegq alqqqllkaa
      121 gdmallgpnc yglldylhsc alwpvahggk avekgvavlt qsgnfaynls msdrslpvay
      181 masvgnqaql gvaelmdvll deprvtaigl hleglknvpg faraahkale kgipiialkt
      241 gvsqigaela lshtsslsgs dalydalfdr lgvirvsgpv sfvetlkaaa cgnlpagnsl
      301 ialacsggda gliadyaers dlslpkldqg qvgelaqvlp tyanlvnpld fttaiwgdge
      361 alnrmldsal rteadaamlv ldypseftge rkecdlllel ycaalqrhgk tgfvtsafpe
      421 llpalarerl haqgvaalqg vedglaawgr iagyqrnrqa llalgesalv plcphaldae
      481 grllnewdsk qalkafglpt pngvlstpdk alkdaetlgy plvlkavsaq lphkteagav
      541 alnlkdgaal saalekmrts iaayapgvpf dqlllepmak pplaelivgi krendfclal
      601 vigaggilve llkdsrslll pttdgairna llslrsapll qgfrgreaad ldalvtaira
      661 vadyacenaa hlleldvnpl lvgahgttav dalirlgqe
//
LOCUS       WP_008053734              96 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [Limnospira].
ACCESSION   WP_008053734
VERSION     WP_008053734.1
KEYWORDS    RefSeq.
SOURCE      Limnospira
  ORGANISM  Limnospira
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Sirenicapillariaceae.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Limnospira"
                     /db_xref="taxon:2596745"
     Protein         1..96
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /function="17 : Mobile and extrachromosomal element
                     functions"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10916
     Region          1..94
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mrkqealtll anhqntlknf gvkslmifgs vardeahins dvdllvefdr pvglftfvrl
       61 kryleeiler svdlgtpdsl kldlrepvfq eairaf
//
LOCUS       WP_008054455             808 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas sp. GM78].
ACCESSION   WP_008054455
VERSION     WP_008054455.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM78
  ORGANISM  Pseudomonas sp. GM78
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 808)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 808)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 808)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..808
                     /organism="Pseudomonas sp. GM78"
                     /db_xref="taxon:1144337"
     Protein         1..808
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88000
     Region          67..117
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          94..808
                     /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 mksraisgsi kqwlgvsals faaltllpln gamaaqagta qstlfsfsma akplpqalsd
       61 fshvtgisvv ytdeapyglt apalngqlra eqalqrllsg sgltsrridg htmvleplpt
      121 egalnlgatt itsvmdqyts yqppptssvm rsstplqeip qtvnvvpaqv irdqaprnld
      181 dalanvsgit qgntlgstqd svmtrgfgdn rngsimrdgm pvvqgrgmna tvdrvevlkg
      241 pasllygiqd pggvvnmvsk qpeldpynal tlrgstygeg kngsggtfds tgalgdsgfa
      301 yrmvldhede eywrnygvhr etlvapsltw fgestqltfa yehrefltpf drgtvidprd
      361 nhpldiprdr rldepfnnme grsdlyhfqa dhdlndnwka hfgyswnret ydasqvrvta
      421 idtskgtltr smdgtqnais tdrfttasle gkvdvagmqh dlvlgiddey rkiyradlir
      481 qkslttfsyl dpvygrevpg ttvspadsaq tdilrsdsvf lqdsihltdq wilvaggrfq
      541 eydqyagkgv pfkantdgng qkwvpraglv yrytnelsfy gsytesfkpn stiaplsgss
      601 tvldgsiape eakswevgar lempgrvtgn ialfdikkrn vlvanaegpv tlysaagevr
      661 srglevdlsg qltdrwsmig syaytdaevt edpvykgkql qnvaknsgsl savydfgsvi
      721 ggdqlrvgag aryvgeragn avndfdlssy tvadafatyd tqldgqrlkf qlnvknlfdr
      781 tyytsaasrf fvsmgdsrqv tlsstlef
//
LOCUS       WP_008055026             541 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Limnospira].
ACCESSION   WP_008055026
VERSION     WP_008055026.1
KEYWORDS    RefSeq.
SOURCE      Limnospira
  ORGANISM  Limnospira
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Sirenicapillariaceae.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Limnospira"
                     /db_xref="taxon:2596745"
     Protein         1..541
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55726
     Region          217..451
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 msafgfgtma qdinisplsd ltdiidqesi reeeedpeig lldnsdndtl pvdngdngdn
       61 gdngdngdnd tlpvdngdng dngdngdngd ngdngdngee eeeeipfipe pappipqptp
      121 apfeptpppv aqptppppvp iptppptptp tpaptptptp tptptptptp tptptpsqpt
      181 ptptpsqptp tptpseptpt pseptpsept ptptlpsadh vfeggdgnsl ilgtegndll
      241 yggggnntly gftgndtlig gggndllygg qnndfldggn gnntlyggln ddtllggigr
      301 dllfgeagnd fldggdgndt lyggedndtl lggngndllf gnqgndsldg gpgddtlygg
      361 kgddtllgsq gddillgnqg ndilyggngd dtlyggqgdd tlyggrgrdy lsgdrgndfl
      421 vgvdtsadfp glttidtlvg gegfdtfvlg nekgpfydng nddingvady alilnfnsat
      481 dvillsnddy lfstdipqpl pqgtaifrrt pgeneliail egvvdlqfdg tnlddgpirf
      541 i
//
LOCUS       WP_008055085             732 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Pseudomonas sp. GM78].
ACCESSION   WP_008055085
VERSION     WP_008055085.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM78
  ORGANISM  Pseudomonas sp. GM78
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 732)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 732)
  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   3  (residues 1 to 732)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="Pseudomonas sp. GM78"
                     /db_xref="taxon:1144337"
     Protein         1..732
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=80224
     Region          1..708
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          <259..>323
                     /region_name="nfrB"
                     /note="phage adsorption protein NrfB; PRK11234"
                     /db_xref="CDD:236884"
ORIGIN      
        1 mnldsargal vqegrellaa meeallaied qgfteerina ifraahtikg saglfglesl
       61 vsfthvaesl ldqvrtgelf vegamlslll tcgdyigsll taveegsemh epnavlrahl
      121 lvqlqeyldr thsdpgpege vsgssesald etsgeplnsh fwhlslrlsa dvlrngmdpl
      181 sflrylsklg rivhlhtvte qlpigdsfdp escylgfele lessaskqqi edvfefvrdd
      241 cqlsilaphs rveeyldlik vlpespqrlg eillqsgalt pteldrvldr qrleappapl
      301 lgsllleeql vpppvmtaal nkqkhnedkr vheqvfikve vgkldqlinl vgelviagaa
      361 tnlhalrrdm dmleeaaqsm svlvesirda slslrmvaig evfqrfprvv rdiskelgkd
      421 iqllvtgadt eldksmverl adplmhivrn amdhgietaq erlgngkvas gslrlnayhe
      481 sgsivievsd dgrgldrqri lakaiqrglv psdqplsdae vyrlifepgf staehvtnls
      541 grgvgmdvvr rniellrgev evlsefgrgt tvrirlpltl aiidgfqvrv geehfvlple
      601 qviecvdlpp qegrhhlisl rgeplpflrl rdlfgitgga tgreslvvlq hgahraglvv
      661 dqlvgefqav ikplgmlfqk srglsgstil gdgrvalild vanllqrana lsvetpgrpm
      721 dvapdvnrsv mn
//
LOCUS       WP_008055350             753 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Pseudomonas sp. GM78].
ACCESSION   WP_008055350
VERSION     WP_008055350.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM78
  ORGANISM  Pseudomonas sp. GM78
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 753)
  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   3  (residues 1 to 753)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Pseudomonas sp. GM78"
                     /db_xref="taxon:1144337"
     Protein         1..753
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79719
     Region          6..752
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msfgadeeil qdflveagei leqlseqlve lesrpddadl lnaifrgfht vkggagflql
       61 nelvecchia envfdilrkg errvdselmd vvlealdavn gmfsevrerc pitaatpell
      121 aalarlaepq aadevaavpv aavveadsgd itdnefeqll dslnavkaqa eapavvpapa
      181 sevaasdtag sdeitdaefe slldqlhgkg kfavdavapa paappepkaa gdssditdee
      241 fealldqlhg kgnfaveale saiasvpapa aptaaaagsd lisdhefeal ldelhgkgkf
      301 sevgtataas gsnsvaasta kvvapkpvak apepkaeapa pvaavvpaaa rapaappaek
      361 paseaettvr vdtarldeim nmvgelvlvr nrlvrlgans adeamskavs nldvvtadlq
      421 tavmktrmqp ikkvfgrfpr lvrdlarqlk keinlelvge dtdldknlve aladplvhlv
      481 rnavdhgies peereasgka rggkvilaae qegdhillsi sddgkgmdpn vlrsiavkrg
      541 vmdkdaadrl sdtecynlif apgfstktei sdvsgrgvgm dvvktkisql ngsiniysak
      601 gqgskivikv pltlaimptl mvmlgnqafa fplvnvneif hldlsrtnvv dgqevvivrd
      661 kalplfylkr wlvssaahee qreghvvils vgtqrigfvv dqlvgqeevv ikplgkmlqg
      721 tpgmsgatit gdgrialild vpsmlkryat rri
//
LOCUS       WP_008055394             334 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Pseudomonas].
ACCESSION   WP_008055394
VERSION     WP_008055394.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  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   4  (residues 1 to 334)
  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 334)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..334
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37621
     Region          22..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          248..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mteptslasw tralrkqlda lgldstalcq qagldpqlmd dpnaryplsg ttrlweiavq
       61 vsgdpaiglr vsrfvspttf halgyalvas gslrevferi vryhqvvsda leleltradd
      121 rycfhlkipp gnpapafeai dafvaiyvrt crnrlgrdya plavylrrpe padphqwhkv
      181 frspvyfatg edrlefaltd fdshlddanp elaehnetvl nrtlaqlkpl twerkvrdai
      241 eeqlpegeps aehiakalhl slrslqrhla degcrfdtll nesrenlall hlrdpqcsls
      301 eisyllgfad tssfsrafkr wtgmtpgqfr dglr
//
LOCUS       WP_008055395             410 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Pseudomonas sp.
            GM78].
ACCESSION   WP_008055395
VERSION     WP_008055395.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM78
  ORGANISM  Pseudomonas sp. GM78
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Pseudomonas sp. GM78"
                     /db_xref="taxon:1144337"
     Protein         1..410
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=45110
     Region          8..405
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mdeaqeqdrl fisvsgalag tlgrgqsrsd svftyvestq eensvsltmp arlesytwen
       61 gvppifemnl pegalldelv rrfskavrgf ddftmlaivg pyqlgrvgia naqdsndrpp
      121 etrladllvh dgaqglfedl lhtygrysgv sgvqpkvlir dsattidrlt hrgathlvks
      181 fraeeypela aneyfcmraa lhsglevpkf elsehgkflv verfdlndrg ylgfedfcvl
      241 nawpskakyd gsyegaarqi kafvspplln salesffkiv alssglkngd ahlknfgvly
      301 edcatdaqis lapaydivtt svyikndsma lllggskawp kykmlmrfgr sacnltegrc
      361 kellqqvahg mdvamsemaa hikgnsdfan vgealveqwk sgmarslvsr
//
LOCUS       WP_008055520             287 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [unclassified
            Pseudomonas].
ACCESSION   WP_008055520
VERSION     WP_008055520.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..287
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31091
     Region          1..278
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mnvdlhchst asdgalapav lvarafekgv qvlaltdhdt legldearha analgmqlvn
       61 gvelsctwgg atihvlgygf dvnaaplvea iaklrdgrwl rseeisrkla lkgmpgaleg
      121 areiqqtlgd sgnaparphf adwmvregfv kdraeafrkw lgagklgdvk qhwptledtv
      181 etlraakawv slahpchyef trskrrrlia dyiqagghai evvnghqpae qvgslailar
      241 efgllvsags dfhgpggwse igeyrplped lpplwcrfkh dpiiaav
//
LOCUS       WP_008055659             334 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM78].
ACCESSION   WP_008055659
VERSION     WP_008055659.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM78
  ORGANISM  Pseudomonas sp. GM78
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 334)
  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   5  (residues 1 to 334)
  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   6  (residues 1 to 334)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Pseudomonas sp. GM78"
                     /db_xref="taxon:1144337"
     Protein         1..334
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37162
     Region          21..202
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <160..334
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mpsllrsssl tnfidvalsv gldpyrqlrk agitdaalmd psimipaksv mhlledsaya
       61 akiedfglrm gqtrqldnlg plaialreeq tlrkawqslt rrlgltnesm dlsieeangv
      121 aifkqeltdn mggsvrqate lvtcvifrtl kqllgpawkp rsvcfthqap anlamhrqvf
      181 gasvrfnhef dgivlatsdl daaiqsydpl iarharefld aklaqsdvtm pdkvrklvfa
      241 llpagecvae kvaqqlgvdr ktmyrhlahh dqsyssivdd vrvdlvnryv vnrerslsev
      301 aillgfssls afsrwfsgrf gcsvtawrre kqra
//
LOCUS       WP_008056185             827 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas sp. GM78].
ACCESSION   WP_008056185
VERSION     WP_008056185.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM78
  ORGANISM  Pseudomonas sp. GM78
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 827)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 827)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 827)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..827
                     /organism="Pseudomonas sp. GM78"
                     /db_xref="taxon:1144337"
     Protein         1..827
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89297
     Region          66..114
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          96..827
                     /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 mrslprrtpl alavqrpslh ktlltsvllt atllgstman aapvkvsiav qplssaltql
       61 gmqtnlqily spdqvagiks ravsgsleps aalaemlkgt gisfqingns vtlvsggsss
      121 lqlgattisg qalglttedt gsyttgattt atklpltire tpqsvtvvtr qqmddrgvqs
      181 vgdalkntpg itsqkydsdr tefsargfai tnfqydgvni pydgvygenp nntddaanld
      241 rvevikgatg lmtgagdpsa tvnlvrkkpt kefkasvsat agywdsyrte gdisgsltes
      301 gnvrgrfvga mqdkdsyidh ysqkrdlyyg vleadltddt lltlgvdkss atprgsswtg
      361 ntvyyadggk tnfsrsfnpg adwsrrdfds ttyfasleqa landwkfkas fdqkttdhdt
      421 qlasasggyp drntgegmff yqghweghrv qntadvnvsg pftlggrehe lvagfmaahs
      481 rqtgstfgap tdsdglvpgs ifdwtghiak pdfpkdgkye rtlsqngayl atrlrptddl
      541 sfilggrvst ykynedytyy pgagladtha sykehgvvtp yagvvydldd tysvyasyts
      601 iyqpqinkda dgktldpveg dsyetglkaa yfegklnasl affrieqdnv aesigtneit
      661 gdgiykavdg attngvelel agelapdwnv sagytyartr dkdhqrifgf platskpehv
      721 vrtfttyrlp galdqftvgg gvswqsafyg qsyspnvggg eggstmlkqg gytlvdlmtr
      781 yqyddhlsft vnaynvfdkr yltglgnfgt tfygeprnmq itakydf
//
LOCUS       WP_008056398             403 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Pseudomonas sp. GM78].
ACCESSION   WP_008056398
VERSION     WP_008056398.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM78
  ORGANISM  Pseudomonas sp. GM78
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 403)
  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 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   3  (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   4  (residues 1 to 403)
  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 403)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Pseudomonas sp. GM78"
                     /db_xref="taxon:1144337"
     Protein         1..403
                     /product="CmpA/NrtA family 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=43770
     Region          16..267
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mnepstnpla wvngsdapek teinlgfmal sdcasvvvaa tqgfaqpygl tlnlkrqssw
       61 anlrdklvsg eldaahslyg liyavhlgig gvaptdmavl mglnqngqsi nlshglqaag
      121 vtspealdrh vhqtrpkltf aqtfptgtha mwlyywlasq gihplhdvds vvvpppqmva
      181 hlqagridgf cvgepwadsa vkqnlgfsla tsqaiwpdhp ekvlgctraf veqypntara
      241 lvmaileasr fiddsvenrr staqllsapq yldaplscie prllgdyadg lgnewqdpha
      301 lrfhgqgavn lpylsdgmwf mtqfrrwgll rddpdylava rqvqqldlyr eaasavgvaa
      361 pgnemrssql idgkvwdgad pagyarsfrl hamsdsspll asr
//
LOCUS       WP_008057043             292 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Pseudomonas sp. GM78].
ACCESSION   WP_008057043
VERSION     WP_008057043.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM78
  ORGANISM  Pseudomonas sp. GM78
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Pseudomonas sp. GM78"
                     /db_xref="taxon:1144337"
     Protein         1..292
                     /product="formate/nitrite transporter family protein"
                     /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=31795
     Region          24..274
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mdtkkdgktp dlsakeqhev eknqppraav lheiirtqgd qelersvaal wwsalaaglt
       61 mglslmgmgl lnsrlpdgeg fkviasfgyc agflavilar qqlftentlt avlpimskpt
      121 lgnfgrllrl wgvvlvgnlc gtilvayvml elpifdsktd vafldigrkv mendasqmfa
      181 kgiisgwmia tmvwmipsme sakmwiiili tylmalgdft hivvgslevs ylvfagqlpw
      241 kdfwlvfagp tlvgnivggs fifalishaq irsesgapkd kgseakstpe er
//
LOCUS       WP_008058367             139 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Pseudomonas sp. GM78].
ACCESSION   WP_008058367
VERSION     WP_008058367.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM78
  ORGANISM  Pseudomonas sp. GM78
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Pseudomonas sp. GM78"
                     /db_xref="taxon:1144337"
     Protein         1..139
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14090
     Region          2..133
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mnnqkgftli ellivvaiig ilatfalpay skyqarakvt aglaeisalk vpfedlmnqg
       61 tdpdlaqvgg sastsnctmt aagnaaegtg tigctilnap aqvlnktitl trsltgwact
      121 tgvdqqyapk gctgvapqa
//
LOCUS       WP_008058783             626 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Methyloversatilis universalis].
ACCESSION   WP_008058783
VERSION     WP_008058783.1
KEYWORDS    RefSeq.
SOURCE      Methyloversatilis universalis
  ORGANISM  Methyloversatilis universalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Sterolibacteriaceae; Methyloversatilis.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 626)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 626)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 626)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 626)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Methyloversatilis universalis"
                     /db_xref="taxon:378211"
     Protein         1..626
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=67882
     Region          2..626
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mtqakheska laplmiaalg vvfgdigtsp lyafkeafag thglplsean vlatlsalfw
       61 avtliisfky vfivlrfdne geggslalas laqrsarvgv qrrvaavtaa gvfaaamfyg
      121 davitpaisv lsavegiavv aptlehwiep itifilvilf cvqrsgtavv grffgpvtvi
      181 wfavlallga wsiaqtpevl ralnpmyaas fvaekpgqsf lllgaiflal tggealyadm
      241 ghfgarpvrm awyfivspal linyfgqgal vlrsseavsn pffmlapedw rlplvalatm
      301 atviasqati sgafsitaqa trlgylprlr qlhtsdterg qvyipavnwm mlvavvvlvl
      361 efdtsselaa aygiavsgdm iittllmlfi ttmsqrrlkt vllvvlggfl vvevlffasn
      421 ltkfmaggwl pmllggalft mlttwkrgss litrerrrin ipmkdfvggp pldvprvpgt
      481 aiyltsdtet vpsalfhnlk hfkvlhervf flhvsiedvp rvpdidhiev helgggnytv
      541 evrygfreep nipealaala dlglvlepms ttyfvaratv vegqgndlqa wrralfgwmm
      601 rqsegpanyf hlppnqvvel gtqisl
//
LOCUS       WP_008058971             224 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Methyloversatilis universalis].
ACCESSION   WP_008058971
VERSION     WP_008058971.1
KEYWORDS    RefSeq.
SOURCE      Methyloversatilis universalis
  ORGANISM  Methyloversatilis universalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Sterolibacteriaceae; Methyloversatilis.
REFERENCE   1  (residues 1 to 224)
  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 224)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 224)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Methyloversatilis universalis"
                     /db_xref="taxon:378211"
     Protein         1..224
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=24629
     Region          3..219
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 maaldleeqe qlsaikswwn qwgnaitwlv iavsaviigq qgwnwyqrdq svkasgiydv
       61 lqeaalggdl kktreaaael tehfpgtqya algallsakv haenndtqta raqlewvkdk
      121 asedvvrdla rlrlayvlie eqkfddaakl ldgkaeasle arfleargdl hlmrdqrdea
      181 rtayqaaltr idesikaggd aariaqqgir svveikldav ggkq
//
LOCUS       WP_008059124             160 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [unclassified
            Pseudomonas].
ACCESSION   WP_008059124
VERSION     WP_008059124.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..160
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17223
     Region          14..159
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 midlqksgqg legygmlhaq leslladerd fianaaqfsa flfnqlegln wagfylnrne
       61 elvlgpfqgq iacvripfgr gvcgtaaatl qtqrvedvha faghiacdsa snselvvplv
      121 kdgrligvld ldspqlarft vqdqagieql aaiflrltdc
//
LOCUS       WP_008059254             119 aa            linear   BCT 20-JAN-2025
DEFINITION  PilZ domain-containing protein [Methyloversatilis universalis].
ACCESSION   WP_008059254
VERSION     WP_008059254.1
KEYWORDS    RefSeq.
SOURCE      Methyloversatilis universalis
  ORGANISM  Methyloversatilis universalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Sterolibacteriaceae; Methyloversatilis.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 119)
  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   3  (residues 1 to 119)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 119)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Methyloversatilis universalis"
                     /db_xref="taxon:378211"
     Protein         1..119
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12787
     Region          1..119
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 msdaqmqnrr svlslavnsk svlyaafmpf lkgggiflpt nrsyrlgdev flllqlmddp
       61 aklpiqgtva wvtpadaqgg kqqgiglrfg ddessksara kieqvigsyl gssrqthtl
//
LOCUS       WP_008059337             295 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Pseudomonas sp. GM78].
ACCESSION   WP_008059337
VERSION     WP_008059337.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM78
  ORGANISM  Pseudomonas sp. GM78
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Pseudomonas sp. GM78"
                     /db_xref="taxon:1144337"
     Protein         1..295
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32069
     Region          13..264
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mpaelivdar navgespiwa peenalywvd ipagrlqrws vqtghvhawk tpqmlaciar
       61 hpdggwvagm etgffhlhah edgrldsapl ahvdharpgm rlndgrcdrq grfwagsmvl
      121 dmnanaavgt lyrydagqqg plqaqmngli vpnglafspd gktmylsdsh plvqqvwafd
      181 ydvdsgipsn rrvfidmnqy ggrpdgaavd aegsywicgn daglvhrftp dgrldrslav
      241 pvkkpsmcaf ggsrldtlfv tsirpgddqd eqslaggvfa ldpgvkglpe phfkq
//
LOCUS       WP_008059771             159 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Methyloversatilis universalis].
ACCESSION   WP_008059771
VERSION     WP_008059771.1
KEYWORDS    RefSeq.
SOURCE      Methyloversatilis universalis
  ORGANISM  Methyloversatilis universalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Sterolibacteriaceae; Methyloversatilis.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Methyloversatilis universalis"
                     /db_xref="taxon:378211"
     Protein         1..159
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=16680
     Region          1..144
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkrtraglqa gvtlielmiv vviigilsai aypnytqyvi dsrrataaac ltqqaqvler
       61 ffttnltyvg gdgdanangt rdlnelqcvt dltnfytfgv tisnasprqf sitaaprnaq
      121 qsndskcgcs laldqagtkg asgtpsrcst gagvtacwk
//
LOCUS       WP_008060379             651 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Methyloversatilis universalis].
ACCESSION   WP_008060379
VERSION     WP_008060379.1
KEYWORDS    RefSeq.
SOURCE      Methyloversatilis universalis
  ORGANISM  Methyloversatilis universalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Sterolibacteriaceae; Methyloversatilis.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 651)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Methyloversatilis universalis"
                     /db_xref="taxon:378211"
     Protein         1..651
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=69093
     Region          78..632
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mnslrmrlla allgvgvlaf aaalatalwv srdrveaqma sqaqaialsl tvaltaggep
       61 alqnaeslve pvfdqsylrr ievrdakgav iasrqaparl pggapqwfid llplaagpqt
      121 sdimhgwria gsvqvephph waqlqlwsia etlmlwmggg laaasvlglm alrwglrplr
      181 rvqrsavaaa srkfmpidea rmpvelqplv gafnrmltam agaleseagr aqqfrdqalv
      241 deltglpnrr afraaleari eagersgwla llrvegledl nhlygrdtvd dllaesagfm
      301 qaldhvvlsg rvegacfaml fdddeagtrd alaallvrld slasaagsgq ayawragaad
      361 gagtdidagg wlaaadralh qwrietgttp vmahareaet gagslriqvr elirgghiaf
      421 atqathgltp tglasplhve lraaldagdr liraaeyisy agearvaaal dsaclmrale
      481 qarsrrdgla tvvnvgaatl tdadilrwvr gyrhddrvgt lilefpesal lgdvdaaeaf
      541 aqlaqsrgla lgikhfglha nalqllrrlr pahvkfsvtl treallnpds gayvqslagi
      601 aatlaitpva vavehveafe glyglgirav qgaavaveql plpdrngspp r
//
LOCUS       WP_008060575             453 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Methyloversatilis universalis].
ACCESSION   WP_008060575
VERSION     WP_008060575.1
KEYWORDS    RefSeq.
SOURCE      Methyloversatilis universalis
  ORGANISM  Methyloversatilis universalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Sterolibacteriaceae; Methyloversatilis.
REFERENCE   1  (residues 1 to 453)
  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 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   3  (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   4  (residues 1 to 453)
  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 453)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Methyloversatilis universalis"
                     /db_xref="taxon:378211"
     Protein         1..453
                     /product="CmpA/NrtA family 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=49655
     Region          92..331
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mstfrnpfdp nvklngcscg rhhsqaehdh aetlseeaml dravegavmr alfphdetrr
       61 nfiravgast amaaistflp lgtvkdafas pgplektrlk vgfipitcat piimahplgy
      121 yskqgldvev vktagwavir dkslakeyda ahmlspmpla isigagsnpi pwtmpaveni
      181 ngqaitlsvk hkdkrdpksw kgfkfavpfd ysmhnyllry ylaehgidpd tdvqiravpp
      241 pemvanlrag nidgflapdp vnqravydgv gfihtltrdi weghpccafa askefvttmp
      301 ntykallrai isatgtasnp anrkqiaeai apanylnqpv tvveqvltgt yadglggvqk
      361 vpgrigfepf pwesfavwil tqmkrwgqik gdidyqkiar evflatdaaa lmkevglpvp
      421 ttttkkfsvm kkefdpakpe eylnsfkirk vaa
//
LOCUS       WP_008060993             247 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SPOR domain-containing protein [unclassified
            Pseudomonas].
ACCESSION   WP_008060993
VERSION     WP_008060993.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..247
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26890
     Region          178..242
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mrklglgflv tgvvgqlsal lwtytaigpl cennvdnsyi qknvtklkql iddtanevvt
       61 nlttkysdgl tplaenespi pdsteahaaq flienpdesp vfslpslptq arnwtiilsg
      121 liastglllv lfarkktsdp qwhvfrsvpg slitlespcl tcgsyilhak keasttpssg
      181 lwvieialnt psrhratnai kqlelpvark ennfvvigpy rqkqdaarvv kelseshgvr
      241 gwmmagn
//
LOCUS       WP_008061531             168 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Methyloversatilis
            universalis].
ACCESSION   WP_008061531
VERSION     WP_008061531.1
KEYWORDS    RefSeq.
SOURCE      Methyloversatilis universalis
  ORGANISM  Methyloversatilis universalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Sterolibacteriaceae; Methyloversatilis.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Methyloversatilis universalis"
                     /db_xref="taxon:378211"
     Protein         1..168
                     /product="TRAP transporter small permease subunit"
                     /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=18017
     Region          3..168
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mralltlaal idrlneacgr llpwtilaav llavgnalar kfdagsnall eaqwylvsaa
       61 fllgagrvlr ldehvridll tarlsprgrl kadiaalalt vlpvcllmlw lswpwflssw
      121 lshevsasag glplwparil vpagfalltl qalalivrra aalreada
//
LOCUS       WP_008061926             313 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM78].
ACCESSION   WP_008061926
VERSION     WP_008061926.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM78
  ORGANISM  Pseudomonas sp. GM78
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 313)
  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 313)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Pseudomonas sp. GM78"
                     /db_xref="taxon:1144337"
     Protein         1..313
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34883
     Region          43..195
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          223..302
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mssldhfsqp pqapldadme kqraelaaii rrntaedgty atavgslfms rhsqnhdfap
       61 vlaqpalcim aqgrkevrla deyfnydpln ylvvsvsmpl sgrvvnvsve epilavrldi
      121 dpaeitalia dagplglptr ptgrglyveq ldsamldavl rlarlldtpk diamlaplvr
      181 reilyrllrs kqghrlyeia iansqshris qaikwlngnf eqplriddla kevnlsvstl
      241 hhrfkamtam splqyqkqlr lqearrlmla egleasaagy rvgyespsqf sreysrlfga
      301 pplrdlarlr lsv
//
LOCUS       WP_008062748             296 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM78].
ACCESSION   WP_008062748
VERSION     WP_008062748.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM78
  ORGANISM  Pseudomonas sp. GM78
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 296)
  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 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 296)
  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   4  (residues 1 to 296)
  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 296)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Pseudomonas sp. GM78"
                     /db_xref="taxon:1144337"
     Protein         1..296
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33385
     Region          49..290
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          206..286
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mslapanhea rfrqqkliag crrpcsrlqf dsavtligsv phgcitlais rttvgrptvn
       61 nhqlrpneii vlssgesvhy tcepnetlft ltttlehyaq cvknhslidv lahrqvhqfq
      121 vanfklvqsa idvfkahlid inepdlnqrd hheqsaadge llvallralt pigrcalkpp
      181 trrkiateai eyihqntnrp lnmkvlvkql ktttrslhhg fvetfgtspi ayirnlrlah
      241 vrrdlirntw ptvtetamyw nfhhlsrfsk ayqkaygetp setarrnstk laaank
//
LOCUS       WP_008064964             803 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pseudomonas sp. GM78].
ACCESSION   WP_008064964
VERSION     WP_008064964.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM78
  ORGANISM  Pseudomonas sp. GM78
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 803)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 803)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 803)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="Pseudomonas sp. GM78"
                     /db_xref="taxon:1144337"
     Protein         1..803
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=88620
     Region          2..800
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkrsltalgl livalaagag wyvyskqpsr qgmvelqqlq gsvtvryder giphiradne
       61 tdlyralgyv haqdrlfqme vlrrlargel aevlgpklld tdklmrslri reraetylan
      121 mdkqspafla lqayldginq yqdshakpve fdvlgiakrp ftaqdtisia gymaysfaaa
      181 frteplltyv rdqlgadyls vfdldwqakg vlatrhsaap aplasadwkd lnalarlseq
      241 aladnglpqf egsnawavag nrtksgkpll agdphirfsa psvwyeaqls apgfelyghy
      301 qalmpfaslg mnrdfgwsit mfqnddldli aekvnpdnpn qvwyrgkwvd mvsseqqiav
      361 kgqapvtltl rqsphgpivn dalgnsvgkt piamwwgfle sqnpiidgfy qlnradtlak
      421 arsaaakvqa pglnivwana kgdigwwaaa qlpkrpagvr pwfildgsts dadkdgfypf
      481 sanpqeenpa rgyivsanfq plsptgmeip gyynladrgq qlnrqlsdkn vkwdlensqq
      541 lqlgtttayg prllapllpt lrevvsdpae lklveqlaqw kgdypldsts atlfnqflfn
      601 ladaamrddl gndffetlls trvidaalpr laatpdspww dnrntlgket radtvkvawl
      661 asiahlkatl gadfsqwqwg kahtlthghp lgqqkpldri fnigpfaapg thevpnnlsa
      721 kigpapwpvt ygpstrrlid fadpahsltv npvgqsgvpf drhfddqaea yiegiyfqah
      781 lndeevtant kstlkllpar saq
//
LOCUS       WP_008065693             223 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Novosphingobium nitrogenifigens].
ACCESSION   WP_008065693
VERSION     WP_008065693.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium nitrogenifigens
  ORGANISM  Novosphingobium nitrogenifigens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 223)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Novosphingobium nitrogenifigens"
                     /db_xref="taxon:378548"
     Protein         1..223
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=23362
     Region          54..221
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mnsgrrrflg aiagtaatvl lprsaqaatv rgadtwlpws mlppeslavg nvqgdvapsl
       61 lsralsaldt hsaritdrsv igvvdfsaps rtqrmhivdl aggrilsshl vahgrgsdpa
      121 nsgwvehlsn rvgseascsg sfvigdtyhg khglsrrilg ldpendqaev rgivihaasy
      181 vgsdflseyg rigrsqgcfa vsgseidtvl qqlgpgrllf aar
//
LOCUS       WP_008065840             296 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM78].
ACCESSION   WP_008065840
VERSION     WP_008065840.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM78
  ORGANISM  Pseudomonas sp. GM78
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 296)
  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 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 296)
  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   4  (residues 1 to 296)
  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 296)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Pseudomonas sp. GM78"
                     /db_xref="taxon:1144337"
     Protein         1..296
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32348
     Region          30..183
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          211..294
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mlltrhldan atlvsliepl strdgfvpta lpgvqvlras cdmargpqiy epslviiaqg
       61 sklaylgprt leygaghyli qalpvpfece tfaapdgpml gvsvaidrvm lgelvlamgl
      121 apgrhipaqt pesmtsavld damrgcverl lrclhdplec qimgqarlre llfvalrgpq
      181 advlqalveq qgqfariaas lshlhahyte plnvetlasc anmsastfhe hfkrstllsp
      241 vqylkrlrll raqqlllgeg lgvaqvahrv gyqstsqfsr eykryfernp gderaa
//
LOCUS       WP_008066744             265 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phosphonate ABC transporter ATP-binding protein
            [unclassified Pseudomonas].
ACCESSION   WP_008066744
VERSION     WP_008066744.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
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   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..265
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=28368
     Region          3..247
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mtlhltrvsl thangvqalr sldlhieage qvaiigpsga gkssllnvla tglrpgigel
       61 qvlgeqpwql sarqrqrlra riglvhqapp lpprqrvita vlagkigqwg lgksllnlvh
      121 pldvpgaraa larldlhdkl faqcqqlsgg qlqrvgiarv lyqapevlla depvsamdpv
      181 laghtlkvlc eharehavtl vaslhavela lahfsriigl rdgqilfdlp asavdrerld
      241 tlyaneqlqp spapvpplsv qiprc
//
LOCUS       WP_008067789             118 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Pseudomonas].
ACCESSION   WP_008067789
VERSION     WP_008067789.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (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   3  (residues 1 to 118)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 118)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            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=12733
     Region          1..118
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mnepispgpr ngilsltikd ravlyaaymp fikngglfip tnksyklgde vfmllhlmde
       61 pekipvagkv twitpkgaqg nraagvgvqf negddtarsr iethlagalk sdrpthtm
//
LOCUS       WP_008068743             249 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Pseudomonas sp. GM79].
ACCESSION   WP_008068743
VERSION     WP_008068743.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM79
  ORGANISM  Pseudomonas sp. GM79
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 249)
  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 249)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Pseudomonas sp. GM79"
                     /db_xref="taxon:1144338"
     Protein         1..249
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27186
     Region          1..245
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mlkfnahlgf qfnelpflqr ieaaaaagfr avefpspyef daslladhla qyslpliqfa
       61 apagvtkgia alqgkeeefr hgllqaarya kalacsdvhi msgvttqdda gpifggnley
      121 avkyfedqgl rplievictq empgyymsdf skaqqvletf psvglildly haqlltgdav
      181 dvlarfydrt vhvqiadcpg rhepgtgnin favlfaaleq rgytgwigce yrpsgstvas
      241 ldwikqlsa
//
LOCUS       WP_008069307             372 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Novosphingobium
            nitrogenifigens].
ACCESSION   WP_008069307
VERSION     WP_008069307.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium nitrogenifigens
  ORGANISM  Novosphingobium nitrogenifigens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 372)
  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 372)
  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 372)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Novosphingobium nitrogenifigens"
                     /db_xref="taxon:378548"
     Protein         1..372
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=38216
     Region          48..109
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          208..276
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mdeardavpq dgahddkaas avmaevarsa tprstpaasg spmtatgrlr aarealgltt
       61 aeisertrit lrhveamdrg dlaalpgrpy vlgfvrsyar vvglddtelg eqvrremdis
      121 vprpeprpln qydvndpakt pspliswlav glvvvilvag tvfwrsyysp agalpalaps
      181 eapapapsaa pvqaapaqta pvpsgpvvft atadgvwvkf tdgqghqllq knlargesyt
      241 vpadavspql wtgrpdalti tiggtpvppl adkqtvmkdv pvsaqallar ansappvqps
      301 paqsplaqtv pagvqggvaq aaplpastgn lshsprrhvr prhvetpavt ndgaapatpa
      361 avpavaaagt pq
//
LOCUS       WP_008070876             361 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Novosphingobium nitrogenifigens].
ACCESSION   WP_008070876
VERSION     WP_008070876.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium nitrogenifigens
  ORGANISM  Novosphingobium nitrogenifigens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Novosphingobium nitrogenifigens"
                     /db_xref="taxon:378548"
     Protein         1..361
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36404
     Region          74..316
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mvktvkfgsl dalvglsfds aslaysaptk ingtvtntta sttevltyyg lsatvgspfi
       61 tlpnisfkvv svsdatnelt idayygssmv aelgftvtgf saaglalssi pidamvltgt
      121 nlpslmgsaf vlgyniaqaa sqsiqfkesd lysftpsakv vfgtakadti tgttgpqtll
      181 gmdgndriva gsgadmlygg ngadvliaga gndtlyggag ndllygstgt svlkggagnd
      241 tlrawtghta mtggdgadtf vfalgntggs spstadvind fshtagdhin lslfdshlpa
      301 ggpthltfig taafdghage vryetvgqnl aiygdidgdg tadfcivaks istlvasdfl
      361 l
//
LOCUS       WP_008071244             826 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas sp. GM79].
ACCESSION   WP_008071244
VERSION     WP_008071244.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM79
  ORGANISM  Pseudomonas sp. GM79
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 826)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 826)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 826)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..826
                     /organism="Pseudomonas sp. GM79"
                     /db_xref="taxon:1144338"
     Protein         1..826
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90423
     Region          69..120
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          98..826
                     /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 msasrfmlrp ltrallmsst trsrmtstgl glamtlamtp yvqaqewtln ipaqplaqal
       61 qtlgqqtnlq iiyspesiqn lrssalngry qeddslnaml kgtgirhqrd gntvtllapa
      121 tgsamelapt singqrlgat tegsnsyttg avtigkgehs lretpqsitv itrkmlddqn
      181 lntieqvmek tpgitvydsp mggkyfysrg frmtgqyqyd gvpldigssy vqadafnsdm
      241 aiydrvevlr gaagmmkgag gtaggvnfvr krgqdtphtq lslsagtwdn yrgqvdtggp
      301 lndagtirgr avvtqqtrqy fydvaerrdq iyytaldfdl sdyttlglgm ayedvdatpc
      361 wgglpryadg sdlklsrstc lntawnnqrs kratyfgdlk hefndnwalk vagvyskntq
      421 dmeyafpsgs vplgatstst amigsifdyd qvdygldayv dgkfdafgqe helivganas
      481 rshkddfyav allpqsqnvl npnhhlpqpd esfylanatr ggpvdmrikq ygaystarlk
      541 ladpltfvlg srvswykset dsvsfwrgeg tptsseaket gqvtpfaall fdindnltvy
      601 tsyadiftpq gnyktingst lkpligqsye lgikgewfdg rlnsavnlfr tvqkdaaqdd
      661 pacpdsscsl nsgkvraqgf eaevsgevid rlqllagyty tqtkiledad vsqdgvsynt
      721 yvprhllrvw gdyalsgple rvtvgagvna qssnyrtsas sgknitqagy avwngrigyr
      781 iddtwsvaln gnnlfdkryy atigsegwgn fygeprnfvm svkadf
//
LOCUS       WP_008071862             234 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Novosphingobium nitrogenifigens].
ACCESSION   WP_008071862
VERSION     WP_008071862.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium nitrogenifigens
  ORGANISM  Novosphingobium nitrogenifigens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Novosphingobium nitrogenifigens"
                     /db_xref="taxon:378548"
     Protein         1..234
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23544
     Region          <19..184
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 msapvktdkp iytlkakqad lvftsdtthi gngnglantm tgaggndtly gmggtdtlyg
       61 gigndrlygg tgvdtlyggn gadllyggkg advlsggngn drlfggfgnd tldggsgrnv
      121 lyggagadkf vfsaapgngn fntiadfrha dgdhivldsk vfaaltagtl pdadfasgrg
      181 vtsaktadqh vlydthtgyl yydadgaggn aavkigqigt alhpdltasd fliv
//
LOCUS       WP_008072213             334 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM79].
ACCESSION   WP_008072213
VERSION     WP_008072213.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM79
  ORGANISM  Pseudomonas sp. GM79
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  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   4  (residues 1 to 334)
  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 334)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Pseudomonas sp. GM79"
                     /db_xref="taxon:1144338"
     Protein         1..334
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37721
     Region          28..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          247..328
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msglvrsasl tnyaeiarsl hvdhleqlrl vgldhrcllq pdlkipneav arllensare
       61 agvddfglrm aetrklsnlg plallwrdeq tirsameafr dflflhnqgl vlnieesggv
      121 vvlrmeqvtv gnlpvrqame lsvgvthrll ktllgnhwhp sivcfrhaap mddsrhrrif
      181 atsvqfnslm dgivcrstdl dkalpsadpd maryvhqylh sireesktal lekvrqmiwi
      241 vlptghcsve qvaanlgwdr rtlhrklaqe getfsslldq vraelamrhl ahsnqrlsei
      301 agvlgfsels afsrwfsrhf dcspstwrar qsnl
//
LOCUS       WP_008072725             633 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Pseudomonas].
ACCESSION   WP_008072725
VERSION     WP_008072725.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 633)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 633)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 633)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..633
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68332
     Region          5..633
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mgqassqvaa sehsaakpig mlvaavgvvy gdigtsplyt lkevfsggyg vpvnhdgvlg
       61 ilalifwsli wvvsikymmf vlradnqgeg gimaltalar raaaghaklr tllvvcglig
      121 aalfygdsmi tpaisvlsai eglglafegi dhwvvplsli vlvalfliqr hgtarigilf
      181 gpimvtwflv lgalgvygis qhpevlqamn pvwgvrffmv hpgmgiailg avvlaltgae
      241 alyadmghfg rkpiarawfi lvlpalvlny fgqgalllgd peaarnpfyl lapswalipl
      301 vglstlatvi asqavisgaf sltrqaiqlg yiprmhiqht ssaeqgqiyi gavnwalmvg
      361 villvlgfes sgalasaygv avtgtmlmtt ilvsavmlll wkwppilavp vllgfllvdg
      421 lyfaanvpki iqggafpvia givlfvlmtt wkrgkqllve rmdegglplp ifissirvqp
      481 phrvqgtavf lsarpdavph allhnllhnq vlheqvvllt vvyediprvp pqrrfavdsy
      541 gegffrvilh fgftdepdvp ealklchldd lnfspmrtty flsretvias klegmarwre
      601 tlfafmlkna ngnlrffnlp lnrvielgtq vem
//
LOCUS       WP_008072754             816 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pseudomonas sp. GM79].
ACCESSION   WP_008072754
VERSION     WP_008072754.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM79
  ORGANISM  Pseudomonas sp. GM79
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 816)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 816)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 816)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..816
                     /organism="Pseudomonas sp. GM79"
                     /db_xref="taxon:1144338"
     Protein         1..816
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=88933
     Region          12..816
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 maspalthfl prfgvaaava svlsltgcqt wntqdtlppt sgvqplkgla qnvsirrnam
       61 gmpliesnsf hdalftlgyv hasdrisqmv tlrllaqgrl aemsgadlld adrymravnl
      121 kksagelyka ssprlkrffe vyargvnayl fryrdklpad laatgykpey wkpedsalif
      181 cllnfsqsan lpeeisslml aqtvstdkla wlapsapdek lpvaeaeklq giklngqipg
      241 lseiskatgq lsdlnllgat ssnnwaiapq rsrsgkslla sdshgplgvp slfsyvqira
      301 pkyqasgati aglpmvlggf ngkvawsmtt vmgdnqdlfl ekikrqgngl syevsgkwqp
      361 aivrnetyfv kgqkpireav yetrhgplln saqgaalang fglalqtpnf tddktldaff
      421 dlsraqsvek asdasreira ialnlvfada snigwqvtgr fpnrregegl lpspgwegry
      481 dwdgyadpml hpydqdpaqg wlgtanqrvi phgygmqlsn swsaperger maelagvgkh
      541 dtrsliamqy dqtttfaakl kkmfeapgms qplkhaieal pvadrgkare aytrlmafdg
      601 klsptsadaa iyelflqest kqifldelgp esspawkafi angklsyaaq adhllsreds
      661 pfwddlrtsq kedkpailar slasaisagd sqlggdhkaw qwgklhryew knasgqtvrg
      721 plpaggdhtt lntaaftwgq dfnttlapam rfivdfgqae plmgqngsgq sgnpasahyl
      781 dsvepwlkgq yislpmqpqn fdkvygktrl tltpgk
//
LOCUS       WP_008072871             185 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Vibrio sinaloensis].
ACCESSION   WP_008072871
VERSION     WP_008072871.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sinaloensis
  ORGANISM  Vibrio sinaloensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Vibrio sinaloensis"
                     /db_xref="taxon:379097"
     Protein         1..185
                     /product="TRAP transporter small permease subunit"
                     /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=20656
     Region          17..179
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 msdknlhqph eqeeqprnml dkavikisnl lswlfiftvf isfyevvmry vfnapttwvh
       61 etasfiggsl fivggiyafa ankhvrvvli ydsvsaqgrk ylnlihhvvg lafaamlaya
      121 afamaeeawf tpwgelrlet sgsvlnapyp allkglifvv lcvlvvqfvl hliqeiiglg
      181 kkddv
//
LOCUS       WP_008072985             359 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Vibrio sinaloensis].
ACCESSION   WP_008072985
VERSION     WP_008072985.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sinaloensis
  ORGANISM  Vibrio sinaloensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 359)
  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 359)
  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 359)
  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 359)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Vibrio sinaloensis"
                     /db_xref="taxon:379097"
     Protein         1..359
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39982
     Region          6..357
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mlpklkilrs llvgavtlsl tttsfttlaa dkvyrlklae twgpntpilg datknmakla
       61 eemsngrlki ridsankhka plgifdmvks gqydlghsss yywkgkvpnt lyfssmpfgm
      121 isteqyawfy rgggmelmek vyaphnllsf pggnsdiqmg gwfkkeinsv edlkglkiri
      181 pgfagevmak vgakptniap gelytslerg tidalewvgp afdlrmgfqk iapyyytawh
      241 epgsetqflv nkkkwdslpk dlqtiletaf rvsafdmytq avdananswa tmsaeypdik
      301 vrdfppevlk amqtattell keqassdala keiinsqkqy ltkvrawtei sskayldtn
//
LOCUS       WP_008073187             265 aa            linear   BCT 20-JAN-2025
DEFINITION  phosphonate ABC transporter ATP-binding protein [Pseudomonas sp.
            GM79].
ACCESSION   WP_008073187
VERSION     WP_008073187.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM79
  ORGANISM  Pseudomonas sp. GM79
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
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   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Pseudomonas sp. GM79"
                     /db_xref="taxon:1144338"
     Protein         1..265
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=28388
     Region          3..247
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mtlrltqisl thangvqalr gvdlhigase qvaiigpsga gkssllnlla talrpgngel
       61 qvlgerawql sarqrqrlra riglihqspp lpprqrvvta vlagklgqwg lgksllnllh
      121 pldipgaraa larldlsdkl faqcqqlsgg qlqrvgiarv lyqapevlla depvsamdpv
      181 laqhtlsvlc sharqhnvtl vaslhavela lahfsriigl rdgqilfdlq asevdrelld
      241 qlyaneqlls ppiapaplsv qiprc
//
LOCUS       WP_008073854             515 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [unclassified Pseudomonas].
ACCESSION   WP_008073854
VERSION     WP_008073854.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..515
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54390
     Region          12..515
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 melimktgaa avlrlnpldd vliarrplla geilepegvt irqaivpghk vasrrieagq
       61 pvrrygqiig favvdieage hihvhnlamg eftrdyafsv dakpnvkpse apsfmgivrp
      121 dgrvatrnyi giltsvncsa tvaraiadhf rrdinpaalq afpnvdgvva lthsagcavd
      181 pagdglsmlr rtlagyatha nfaavlvigl gcetnqidsl lttqgltrsn tlrtfniqds
      241 ggtskaitsg ighvkellge anriqresvs arhlivglqc ggsdgysgit anpalgnavd
      301 rlvacggtai lsetpeiyga ehlltrravs revgekliar ihwwerycer mgaelnnnps
      361 agnkaggltt ilekslgava kagssnlmdv yeyaqtvtan glvfmdtpgy dpvsatgqva
      421 gganliaftt grgsaygcap apsiklatns alwarqredm dincgeiaed tltieacgaa
      481 ifetmlrias gersmseqhg ygqnefvpwq igavt
//
LOCUS       WP_008074084             403 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Pseudomonas sp. GM79].
ACCESSION   WP_008074084
VERSION     WP_008074084.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM79
  ORGANISM  Pseudomonas sp. GM79
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 403)
  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 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   3  (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   4  (residues 1 to 403)
  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 403)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Pseudomonas sp. GM79"
                     /db_xref="taxon:1144338"
     Protein         1..403
                     /product="CmpA/NrtA family 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=43834
     Region          16..267
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mnepsagpla wvngsdapek teinlgfmal sdcasvvvaa tqgfaqpygl tlnlkrqssw
       61 anlrdklvsg eldaahslyg liyavhlgig gvastdmavl mglnqngqsi nlshglqalg
      121 vtspealdrh vhqsrpkltf aqtfptgtha mwlyywlasq gihplqdvds vvvpppqmva
      181 hlqagridgf cvgepwaasa vqqnlgftma tsqtlwpdhp ekvlgctraf veqypntara
      241 lvmaileasr fieashenrh staqllsape yldapldcie prllgdyadg lgnrwqdpha
      301 mrfhgggevn lpylsdgmwf mtqfrrwgll rddpdylgva rqvqqldlyr eaatavgvpa
      361 rsqemrssql idgkvwdgsd pagyarsftl hamsdsapll asr
//
LOCUS       WP_008074108             682 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Vibrio sinaloensis].
ACCESSION   WP_008074108
VERSION     WP_008074108.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sinaloensis
  ORGANISM  Vibrio sinaloensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 682)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 682)
  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   3  (residues 1 to 682)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Vibrio sinaloensis"
                     /db_xref="taxon:379097"
     Protein         1..682
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=75055
     Region          4..677
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 maldmeqlrk mfyeecrenl evledvllnl dlaqfddesi ntifraahsi kggaatfnll
       61 disefthsve ayldlvrnge rqltadtvdi llksgdciqs mleqhesgsq vdqallddvs
      121 aqladllgne sviadtqstp ppgnsddvks gswhvsfvph reiffsgndp lrilrelqdl
      181 sdeciieant tqlpeiddie aelcylswqa qlpgeidksv ieeifewved ecdltierqv
      241 qsssvlesne pdtevqptqa eeasrpssds kpvkaakaes svssirvdid kvdslinlvg
      301 elvitqsmlt eigndftidk leklkagldq llqnskdlqe nvlnirmlpm sfafsrfprl
      361 vrdlstrldk qvdlqikgeq teldktvler ivdplvhlvr ngidhgiesr aqrlesgkpe
      421 lgvielnayh qggsivieis ddgaglncdk lwqkasekgv ldadarrdef sdkqimnlif
      481 apgfstadev sdisgrgvgm dvvrrnieel gghieveskl gegsrftisl pltlaildgq
      541 lvkvagevyv iplltivesi qidkscikla sggvelyrlr denipilrlq delemgasgn
      601 ldkrilcfve aagnrvglli delldqqqvv ikslesnysk vagisgatil gdgsvslild
      661 iqglitqfln rtsdsvqkgi aa
//
LOCUS       WP_008074209             253 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Vibrio sinaloensis].
ACCESSION   WP_008074209
VERSION     WP_008074209.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sinaloensis
  ORGANISM  Vibrio sinaloensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 253)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Vibrio sinaloensis"
                     /db_xref="taxon:379097"
     Protein         1..253
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=28347
     Region          <23..249
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mqtdtandqt kqcsqiknvp sdlnqlrsvi dqrttvtfaq piieltnlgs igfealargp
       61 ldsplhtadk lfgaanyhnc ladleiaclc ahleniqrys dttlfsvnls pnmlfdpqih
      121 qalsqfttph rikleltehl pvedwapvkq qmdryrqmgy qfwlddvgcg ffdlqlvdtv
      181 rpevvklcit lmdrlesgea fltelrsvia kvhsyggevl aegieteqql tkvramgvdl
      241 aqgyyfakps llk
//
LOCUS       WP_008074321             331 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio sinaloensis].
ACCESSION   WP_008074321
VERSION     WP_008074321.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sinaloensis
  ORGANISM  Vibrio sinaloensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 331)
  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 331)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Vibrio sinaloensis"
                     /db_xref="taxon:379097"
     Protein         1..331
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36834
     Region          22..201
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          247..327
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkranrfsvs piwkvllsdm qidpqavlty anlpadllnr enatltpqey fqlcngleha
       61 agdvevpllf aqhlsveafd aplfaaicsp dlnsalhrls qykpligpml sevsqgsdat
      121 tinircygyq gelpktlglm etvfftqlar latreaiqpl nvtlqvlpdn isayqdyfgc
      181 qiekgpevsi rfsavdaqrk fltsnlamwe ffeaklnqkl adldgdasns drvrsvlfei
      241 lpagqssiee vaaklaiskr tlqrklsheg esfqallqsv raeladhyle kshmslgeis
      301 fllgfqesns firaystwkg vspghyreqc h
//
LOCUS       WP_008075900             457 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein [Vibrio
            sinaloensis].
ACCESSION   WP_008075900
VERSION     WP_008075900.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sinaloensis
  ORGANISM  Vibrio sinaloensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 457)
  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 457)
  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 457)
  AUTHORS   ter Beek,J., 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 457)
  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 457)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Vibrio sinaloensis"
                     /db_xref="taxon:379097"
     Protein         1..457
                     /product="CmpA/NrtA family 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=50849
     Region          30..311
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mkwtsilkrs lvattltcsv yipnalaelg epeledlkfg fikltdmapl avayekgffe
       61 deglyvtlea qanwkvlldr vidgeldgah mlsgqplgat igigtkaevi tafsmdlngn
      121 aitvsnktwq qmkpnipvqa dgklvhpika dalkpvvesy ldegkpfnmg mvfpvsthny
      181 elrywlaagg ihpgfyapds gdnsgqvnad vllsvtpppq mpatmeagti egycvgepwn
      241 qqavfkgiga pvvtdyeiwk nnpekvfgvs kawaekypnt hirvvkalir aahwldennn
      301 anrveavkll akseyvgadf dviansmtgt feyekgdvre vpdfnvffrh natypyysda
      361 iwyltqmrrw gqisqekpds wymdvakqvy rpdiyqqaaq alvkdgvlns kdfpdfsted
      421 gfrapqthfi dnivydgrsp naylekfsig lkgkdkv
//
LOCUS       WP_008075981             234 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Pseudomonas].
ACCESSION   WP_008075981
VERSION     WP_008075981.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 234)
  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 10614777
            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="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=25453
     Region          37..204
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 maldrfgflm tallltaftl paayadslea alikaapnan akvialavra sqcsraqsaa
       61 paqrlavidy slpsteqrlw vfdlkkrkll fhelvahgrn sgenmarqfs nrnasfatsl
      121 glyrtqssyv gqngyslrme glepgfndna feraivihga pyvspdlara ngrigrslgc
      181 pavrpaiahq lidsmkdgql lfsyypdqrw lksssyincg natvadsskp nrsh
//
LOCUS       WP_008076156             398 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Pseudomonas sp.
            GM79].
ACCESSION   WP_008076156
VERSION     WP_008076156.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM79
  ORGANISM  Pseudomonas sp. GM79
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 398)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Pseudomonas sp. GM79"
                     /db_xref="taxon:1144338"
     Protein         1..398
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44095
     Region          25..389
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mkmtslkvst peggsgrilt saedfifryd edalpnmais ltmpvrpdef rrrdlhpifq
       61 mnlpegyvle qlrnrlaktv nvdpmlllal sgssspigrv hvrseavdal lgaqtfagek
      121 leeiltwdgt edifadlldr yilragisgv qpkvlvpeqq esrpritskt sdliiksgrd
      181 efpglainef lcmsiakeag ipvpefflsd nsklfvmrrf drddqldplg fedmaalmgl
      241 sadqkysksy aaivkairlf cpaqhlrssl dqlfdsvals civgngdahl knfgllysep
      301 tqrdahlapa ydivnttayi pedvlaldla gnksmfasre gllefaqtce vthpkeriqt
      361 llaalevvle rypqhreqap hvvraiqkaa apfvltfg
//
LOCUS       WP_008076432             812 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas sp. GM79].
ACCESSION   WP_008076432
VERSION     WP_008076432.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM79
  ORGANISM  Pseudomonas sp. GM79
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 812)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 812)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 812)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..812
                     /organism="Pseudomonas sp. GM79"
                     /db_xref="taxon:1144338"
     Protein         1..812
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88358
     Region          61..111
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          92..812
                     /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 msrsldtvlr phllavaial caplasgpli aaeqassvra ynlpaaplas tlnqiasqag
       61 lalslnpsla agktsapvkg qfdatgalre alrgtglqle qssagtyslv avpegvmalp
      121 etaiigagnt enawgptegy latrtaagtk tdaaiaelpr svsvvtreqm ddrsvlslnd
      181 alrytagvqs sgygsdsrsd wllvrgfipt qfldglplpk gnyatpkiep wnleriavlr
      241 gpassvygqt ppgglldmvs rrpeaqsshe velqagsneh kqinfdstgk iddegqflyr
      301 vsgvvrdsna pvdhipdkry nlapsltwni nddtrltlls qytrddtgit gqflplqgtk
      361 lstpagkish hknlgdpdwe fydrtyyalg yafehrfndt wqfrqnlryt kndlefqgit
      421 aggqiwpagp deavsddgti qrtagkvded isqfavdnnf qadfqtgals htlllgldhq
      481 rsnsnsrwlw gsagvpssni nrpvygqdfs nvtyftmydy nqktqqtgly aqdqialdnw
      541 rltlggredw vhtgtifhnq ndatntqrdk kfsgnaalsy vfdngvtpyl syaesfqpas
      601 gatvnstdsf kptegkqyea gikyqppgtk tlltaavfdl tqenlsvten nitrqvgevr
      661 vrgleleasg dvtdnlklvg sytyndseit kgasaekgkr maqvprqqat awadytwhng
      721 lldgfgvgag vryvgdtygn ttntdwghvg sytvydasah ydlgrlnssl kgvsvavdak
      781 nlfnkdylst cdgfycyygd ernvvasvny kw
//
LOCUS       WP_008077011             282 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Vibrio sinaloensis].
ACCESSION   WP_008077011
VERSION     WP_008077011.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sinaloensis
  ORGANISM  Vibrio sinaloensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Vibrio sinaloensis"
                     /db_xref="taxon:379097"
     Protein         1..282
                     /product="formate/nitrite transporter family protein"
                     /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=29995
     Region          5..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mstdfkpaef vqtminvgea ktktsardlv lrgtmagiil slavvvaitt ivqtgvgvvg
       61 alvfpvgfvi lsvmgydlvt gvfglaplak fegrpgitwn rvfrcwglvg lgnligsliv
      121 aylvaisltg nfslelnava kkfiavstar sagfeamgmd gwitcfvrgi fcnlmvclgv
      181 ignmtartva grvammwfpi fiffalvfeh tvvnmflfpl gmilgadfgi atwlnfnlip
      241 tilgnivggl imtciplylt haktapslnd eeevnakpal ak
//
LOCUS       WP_008077636             144 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Pseudomonas sp. GM80].
ACCESSION   WP_008077636
VERSION     WP_008077636.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM80
  ORGANISM  Pseudomonas sp. GM80
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Pseudomonas sp. GM80"
                     /db_xref="taxon:1144339"
     Protein         1..144
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15845
     Region          4..144
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mgaayfglfl aafgaatllp lqseallvgl ivsdgywlwg llavatlgnv lgslvnwwlg
       61 rgierfqdrr wfpvsprhma qarkhylryg hwslllswlp iigdpltlia gvmreplgrf
      121 llivtlakga rygvlamltl gwlg
//
LOCUS       WP_008078482             138 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: pilin [unclassified Pseudomonas].
ACCESSION   WP_008078482
VERSION     WP_008078482.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..138
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=13996
     Region          2..130
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkkqqgftli ellivvaiig ilatialpqy skyqarakvt agiaeasalk vnfedvinag
       61 stdpsltnvn agtaatqnct ltaagkvadg tgtitctlln apapvlgqtv tltrsattgw
      121 tckfsgskdy tttscpgv
//
LOCUS       WP_008078572             812 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: Lon protease family protein [unclassified
            Pseudomonas].
ACCESSION   WP_008078572
VERSION     WP_008078572.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 812)
  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 812)
  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 812)
  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   4  (residues 1 to 812)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..812
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..812
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88876
     Region          65..800
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mpdpvaaslr lapealtrpf saeqfsfttt ndlepfrgvl gqeravealq fgvamprpgy
       61 nvfvmgepgt grfsfvkryl kaegkrlqtp adwvyvnnfd eprepralel psgtaasfig
      121 dinglidnll atfpavfehp syqqkksaid rafnqrydka ldiierlale kdvalyrdss
      181 niaftpmldg kaldeaefaq lpeadrerfh edisgleerl neelaslpqw kresnnqlra
      241 lneetitlal qpllsplsek yaenaavcgy lqamqvyllk tvveqlvdds ktdavarkll
      301 eeqyapslvv ghpvsggapv vfephptyen lfgrieyttd qgalyttyrq lrpgalhran
      361 ggflileaek mlsepfvwda lkralqsrkl kmesplgemg rfatvtlnpq hiplqvkvii
      421 igarslyytl qdldpdfqem frvlvdfded ipmvdesleq faqllktrts eegmapltad
      481 avarlatysa rlaehqgrls arigdlfqlv seadfirhla gdemtdaghi eralkakatr
      541 tgrvsarild dmlagiilid tdgaavgkcn gltvlevgds afgvparisa tvypggsgiv
      601 dierevnlgq pihskgvmil tgylgsryaq efplaisasi aleqsygyvd gdsaslgeac
      661 tlisalsktp lkqcfaitgs inqfgevqav ggvnekiegf frlcearglt geqgaiipqa
      721 nvatlmldek vlaavragqf hvyavrqade alsllvgepa gepnadgefp egsinarvve
      781 rlrdiaemis eedlkeaeke laqealaeak pa
//
LOCUS       WP_008079377             274 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio sinaloensis].
ACCESSION   WP_008079377
VERSION     WP_008079377.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sinaloensis
  ORGANISM  Vibrio sinaloensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 274)
  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 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   3  (residues 1 to 274)
  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   4  (residues 1 to 274)
  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 274)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Vibrio sinaloensis"
                     /db_xref="taxon:379097"
     Protein         1..274
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31523
     Region          33..272
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <167..272
                     /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 mkkdqsasfk qstllpwiel rianqstacy dahshdefsf giiqqgkaqy rnrqqehrig
       61 agdivtinps dvhscnpeqg kwsysmlfvd alelgevqad ilqssrqpsh fdyqpfaadc
      121 srdktvkhry vqlfqslnqe snplraqscl ydfvetafsl ncdqsidrsp pslrrikeal
      181 lddirgdhql sqlatevems ryqflrafkh qfglpphayl mdekikrakv mlkkglaisd
      241 vaytlgfsdq ahfqrhfkkr lavtpkyyqs hfie
//
LOCUS       WP_008079449             345 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM80].
ACCESSION   WP_008079449
VERSION     WP_008079449.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM80
  ORGANISM  Pseudomonas sp. GM80
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 345)
  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   6  (residues 1 to 345)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Pseudomonas sp. GM80"
                     /db_xref="taxon:1144339"
     Protein         1..345
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38225
     Region          31..211
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          111..339
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mnvkvqdptf elalvspfll qtlaevaqnk gvdpeilcrg lgftledlqd paqrisyrqa
       61 vamiqralkv lpnqglglwv gaqnvlgtlg llghvlslck tlrdafalgi rhqhtsggiv
      121 vssvdvvgaq vhldaecrlp fadvqvfave effasllvyg ralagadfkp iavefvhaap
      181 dylseyhrll gpevrfgclh nrmlidvqwl dvnlpnhhsl alrqavalle leaaqvhqkl
      241 dliqaverai ardlsrgshi ekiagdlnms srtlrrrlte haltfealle qvrqartmsl
      301 lanpdmpier iteevgysdv rsfrrafkrw tglspsawrh estta
//
LOCUS       WP_008080487             421 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Pseudomonas sp.
            GM80].
ACCESSION   WP_008080487
VERSION     WP_008080487.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM80
  ORGANISM  Pseudomonas sp. GM80
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 421)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 421)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 421)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Pseudomonas sp. GM80"
                     /db_xref="taxon:1144339"
     Protein         1..421
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47429
     Region          15..419
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mtliavyadw eslkgarrlg flharktrnt nvfefeydpk aladpelsfi tldprigpfe
       61 grqfpgehqs rfgafadssp drwgqmlmkr rlerdvrdgl lpsnsklfes dyllgvhdlf
      121 rvgalrykln dagnflddrd gvaappfvel raleqaslal endrdntald grewlrmlia
      181 pggslggarp kasvvdefgr lwiakfpstr ddydvggwef vvnalalncg lrvatgmarr
      241 yasdhhcflv krfdrtergg rhhfasamtm tnrvdgddas tgasylelae vimehgsepn
      301 tdlrelwsri vfnilvsntd dhlrnhgfif dpgrgwrlsa aydmnpvaha dglklnitds
      361 dnaldlelar evagyfrvsr edsadiieri qdvirlwpei antlgmsrse qermapafrt
      421 f
//
LOCUS       WP_008080764             796 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas sp. GM80].
ACCESSION   WP_008080764
VERSION     WP_008080764.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM80
  ORGANISM  Pseudomonas sp. GM80
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 796)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Pseudomonas sp. GM80"
                     /db_xref="taxon:1144339"
     Protein         1..796
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86536
     Region          68..119
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          147..796
                     /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 mssspvsqrh plnralqgam lglivssyal pslaqtssad hsnpvkqwni aagplapald
       61 rfareagisl sfdassvanr ttagvngtle tsaalssllq gselqieqqg pnayllvpqv
      121 ktagplelda tdvedyrlap liinakvrvs adddansvva kelwvggkva tsilntpasv
      181 svvtnkemeq rsvstteeal qytpgvitdf ygtddrndyf qirgfqatty rdgltlssmr
      241 gvredpfaye rieilrgans tlfgpadpgg svnfvtkqpr feqfgqgyvt ygsfdhvetg
      301 idvgdalnde ktlagrftak gqnsdreydh sqddnqlfmg gltwaptdyt satmildylk
      361 tesspnsggy pldkeydrkk fygepsynfh dvertslsgn vthdfdngfv lrsnlryskl
      421 tddfgyvyls dsaarvgttv dryqfgtdte adqfngnlml qydarfenid ssslvgveyl
      481 dsttressvy apttsidian pvftgvsrsi apyavnkrda ttkavflqqn lsfyerfivt
      541 ggvrndsmdl tskglestek dtfsetsyrg altyivndev styvsmvesv sppqvgvtpq
      601 tgrqyeigvk yapmgmdalf saavydltqe nvtiavvlps giieqqtvge srargldlea
      661 kaqvtqnlsl iggysymese vqrgslydgs slkgnefata pkhsaslwsy ydvpatdvsv
      721 glgaryvgsy yfdaansgks dgttlfdaaf nykiakgtdl avnlsnllde qhvvgsgtan
      781 fynpgreita kvsykw
//
LOCUS       WP_008081134             192 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Vibrio sinaloensis].
ACCESSION   WP_008081134
VERSION     WP_008081134.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sinaloensis
  ORGANISM  Vibrio sinaloensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 192)
  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 192)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 192)
  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   4  (residues 1 to 192)
  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   5  (residues 1 to 192)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Vibrio sinaloensis"
                     /db_xref="taxon:379097"
     Protein         1..192
                     /product="TRAP transporter small permease subunit"
                     /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=21364
     Region          5..173
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mlskllatyc lginrlvywv gvsasvlmpi laatvafevf sryvlgkpti waydvslflf
       61 gyiaalggal aqqnkahinv dvlylsvsmr vrslfnlasy slaifflsvv ammalgkfee
      121 aiefnyrrqs ewapsmahfw vmmmvactaf ivqftsdmiq dlyyvvtgka liepeneqqe
      181 sadnfveqag da
//
LOCUS       WP_008081397             811 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas sp. GM80].
ACCESSION   WP_008081397
VERSION     WP_008081397.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM80
  ORGANISM  Pseudomonas sp. GM80
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 811)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 811)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 811)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..811
                     /organism="Pseudomonas sp. GM80"
                     /db_xref="taxon:1144339"
     Protein         1..811
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88380
     Region          51..100
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          80..808
                     /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 mfntwprnly agvalatlst salaqdltfn lpagplastl naiagqsgqi islepalvqg
       61 krapavvgqm paaqamqkal sgsglqlrvt gqgnfsvepa sdssaslqld atniversld
      121 attegsnsya aravsigkgt htlkeipqsi tvmtrkqldd qdlvdlkdav nkttglvglq
      181 gvgkgmiiss rgfqiddwqy dgvpiprnty algnwatqdl iffdrveilr gapgllqgtg
      241 spggainlvr krgqnaptvt itgkagswdh yglqldaggp lnstgsvrgr fvadedqsqs
      301 fvdyewskth slygaldfdl rddttlglai snsdgesrpm irglpryadg kplnvprsty
      361 ggarwnhldi dvttlyadle hrfnddwafk vgavrmdetn kgksqrlqts gdginpdgsg
      421 iqyadfvtdf datklgldmn vtgkfealsm ahevmlggny skytsddkia rtfnnnttdt
      481 ifdidhdrpe isyegilntp ggqatpskyd irqkglygsw rikpidpltl vlgsrvswyd
      541 ysykyatqra fnaaipqpes tvtetgvvtp yagivydlsr ewavyasytd vfepqtnrda
      601 ggstlkpvvg snyevglkge lldgrvntsl avfrydqenr aindlasgmv cdgwycsnaa
      661 gkvrsqgiea eisgevlnnl qlfagytynt tkylddpdne gkvfstwtpk hmlrvwgdyq
      721 fsgdwervst glgftaqsht lgyehtydva gstvwsarlg yqlskeigla vnannlfdkr
      781 yytsaynqln gnnnfgdprn vmfsvkytpe f
//
LOCUS       WP_008081679             179 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Vibrio sinaloensis].
ACCESSION   WP_008081679
VERSION     WP_008081679.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sinaloensis
  ORGANISM  Vibrio sinaloensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
REFERENCE   1  (residues 1 to 179)
  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 179)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 179)
  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   4  (residues 1 to 179)
  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   5  (residues 1 to 179)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Vibrio sinaloensis"
                     /db_xref="taxon:379097"
     Protein         1..179
                     /product="TRAP transporter small permease subunit"
                     /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=20221
     Region          4..169
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mrsliyverl fnrfgdflgw lssvlfilll anvvydvvmr yafndvsiaf qemewhlfsa
       61 vfllgvpyai kagghvrvdl fyerlsnkaq aiidmlgtlf flfpfcllva yygidfakes
      121 yalgetsgdp gglpyrwiik amiplsfffm avsgvglflh slnkivnphl lhnatnsqk
//
LOCUS       WP_008084394             811 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas sp. GM80].
ACCESSION   WP_008084394
VERSION     WP_008084394.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM80
  ORGANISM  Pseudomonas sp. GM80
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 811)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 811)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 811)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..811
                     /organism="Pseudomonas sp. GM80"
                     /db_xref="taxon:1144339"
     Protein         1..811
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89241
     Region          63..113
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          91..811
                     /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 mrlptfrqrf syhciaysll mtsaasclvv shnavaasaa qryaiaagpl dnalsqfasa
       61 anvilsfspq qtsrlrsagl ngnftvdqgf aqllqgsglq avpqapgsyi lqalpngdsl
      121 elaptningq lanpmnldya advgykaqns rigtktstpl setprsvsvv taqrmkdqks
      181 qtltevlgyv pgifappfaa gdslagdlfy irgfnatdyg ygllrdglrv qgnrydtste
      241 pyglerveif rgpssllyge napgglvnlv skrptaapqg evqlgygsnn rrqigvdvsg
      301 plndsgnvlg rvvmlgrksd tqtdhvpddr iyiapsltln fddyntltll anyqkdhtnm
      361 elglpaagtl ltnpngklsk gtmlgdpdwn tferetwstg yefshsfndd wqfrqnsrym
      421 qsritrhetw pgnlnnagfg trlnmtaydr fnksmvysld nqlegkfqvg glentvlfga
      481 sydrtsfnqd wnagivgpid mynpvylrdp ttpiavqntl leqqmkgvya qiqskydhwl
      541 fllggrqdwv dsdfrdkvaq ssdissedkk ftyqggvmyq fdngmtpyvs ystsfvpvqq
      601 isnagapldp itssqyevgl kyepigwdta ftasvydlrk kddtyfdatt ssyrqvgesr
      661 skgvelelns nltqnlnlta aytytdarit kdaatslvkg hqmtgvprnq asvwakyrfl
      721 dgdlkglyvg ggvryfdsaf aytspslygk ldagdvtlvd aaigyqidth wsvdlnaknl
      781 fdkeyvsgcn dagrcywged rtllgtvsyn w
//
LOCUS       WP_008085561             323 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM80].
ACCESSION   WP_008085561
VERSION     WP_008085561.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM80
  ORGANISM  Pseudomonas sp. GM80
            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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 323)
  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 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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Pseudomonas sp. GM80"
                     /db_xref="taxon:1144339"
     Protein         1..323
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35981
     Region          111..322
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          242..322
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mfpspvrqqi ilrsdnlrsd dfgalfsklf gnryadnppl paniiiggvy grhegvsfrr
       61 mhyrgdftva fpdpqdeitf viptagkivf nhatesigvc qvglaidkad irsmrffdvh
      121 ahhgmsinrh qlterlaall gkpilerivf epsvnldsaa fqgikalidl atgtefdlli
      181 nsgtlmpsrl remlidavle awphnfseal rrptatvapr hvklavefiq ahpeqlvsgv
      241 dlarlsnvsq ralqegfrrf vgmsivgyqr qvrlerayev lkqrdagsvt evalrfgfsn
      301 vgrfcqyfqg aygvspaefr arg
//
LOCUS       WP_008085626             357 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM80].
ACCESSION   WP_008085626
VERSION     WP_008085626.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM80
  ORGANISM  Pseudomonas sp. GM80
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 357)
  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 357)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 357)
  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   4  (residues 1 to 357)
  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 357)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Pseudomonas sp. GM80"
                     /db_xref="taxon:1144339"
     Protein         1..357
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39993
     Region          22..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          252..329
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpstdtiatw aqviartlea rgidaapllh eagisrchlh dpdqrialpa msafwraarr
       61 isadecfglq vaqysyptdf hglffaaqss stviealqrg vryapvitts aamslvrgph
      121 ttrmvygvad gaeveqiate asiacavrft rqtwvdlpiv dgvrlarpap edpqrwtrll
      181 gcpirfdage naieysnrwl daplntanha vaqgldgvln dylerqrrln lpervraaii
      241 rylplgevqq srvadelgms vrnlhrhllk hdssfktlld dcrrqlafsy lrqtdcsine
      301 vcyrlgfnep ssfnrafrrw tgaspgkwrr ddlplqpqry vprptvfaae ralsiav
//
LOCUS       WP_008087022             834 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas sp. GM80].
ACCESSION   WP_008087022
VERSION     WP_008087022.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM80
  ORGANISM  Pseudomonas sp. GM80
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 834)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 834)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 834)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Pseudomonas sp. GM80"
                     /db_xref="taxon:1144339"
     Protein         1..834
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=91168
     Region          76..126
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          103..834
                     /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 mtvratckns lnftvesavl rhavraalls talgvsvlpn lsvaaataas evshryniaa
       61 gplgealnqf arqagitlsm tpqqtqgqqs pgvqgeystd qalshllggs gleavsqdgn
      121 sytlrplaes aalalpttdi kgfalgnalg smdgynaths qiatktstal letsqsvsvv
      181 treqmddqgs qtvsqamryt pgvltnpyga thrydyvamr gfndgsvdni yldglksmgd
      241 sgtystmqvd pyflervdil kgpssvlygr sspgglvalt skkplyeayh qvqatvgtqg
      301 qrgvgfdfsg pvdddkrvay rltgltdqsd tqfdhnkekr falaptvsid fsedtsltlq
      361 aylqhdpdgg yhggvpadgt ihqrngnris phffegepgi dgysrdqqsf gyqfehrfnd
      421 vftarqnfry ldskvnmdqv yaygwttpts nelnryytgg derlhafivd nmlqaefftg
      481 atkhtmlmga dyqrrktvvd wtsgglapin afnpvygnsa idmygetsyl rrleqtgvyl
      541 qdliemdkwr fslglrqdwv etsdenriae agrplgtein drrtkltgra galylfdngl
      601 apyvsysesf npnsyadsag nplaptdgtq wemglkyqpp gtdnlftasl fridqenlat
      661 klpqenfyra vgavrsqgle leahmqltdn lkvlgsytft dieysksmvs tlstptdvie
      721 nkgnsptqap rhmaslwady kfdsaaldgl rlgggvryvg yswadaentl kvpsytlfda
      781 sigydlgkvg lkgvdvrlna nnltnesyva scaslnfcym geernvaatv syqf
//
LOCUS       WP_008087253             291 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Pseudomonas sp. GM80].
ACCESSION   WP_008087253
VERSION     WP_008087253.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM80
  ORGANISM  Pseudomonas sp. GM80
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Pseudomonas sp. GM80"
                     /db_xref="taxon:1144339"
     Protein         1..291
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32024
     Region          13..262
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mpwtaltqhr aqlgegpfwd aptqalywvd iagkqalrli gqnvqiwqmp ehisafipcn
       61 sgdalvtlss gvyrldldsp gleprltlfc vadpqpgnrp nearcdaqgr lwlgtmqnni
      121 geqgedlpii rrsgglfrvd pdkrvtpllr glgipntllw sndgttllfg dsldstlyry
      181 fihtdgnldt ayiwygpdqq ggpdgsamda egyvwnarwd gscllrltpd gyidrridlp
      241 vsrptscvfg gedlktlyit saksphnhpl dgvvlsmrvd vpgklctrfa g
//
LOCUS       WP_008087699             349 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Pseudomonas sp. GM80].
ACCESSION   WP_008087699
VERSION     WP_008087699.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM80
  ORGANISM  Pseudomonas sp. GM80
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Pseudomonas sp. GM80"
                     /db_xref="taxon:1144339"
     Protein         1..349
                     /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=38407
     Region          2..276
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 msskkkslei etlrglacll lvlyhvigpl ggglkidigs pfrviadsmv yvrmplftfi
       61 sgyiysiyki rgndfsaffs gkvrrlivpl fcvgvpfsvl qavgpgvnkd vgvidallsf
      121 wvpinhfwfl qavfiifmfv gllewrgmlr satrlyglfv faallfllpp fkfdafging
      181 aiyllpffva gmigqenvdr lkqtfkvigp lvfvlisltl lyvaaidrel ivdrrsligl
      241 tvgcvscial lssdmrskal twlggysyai flfhvlfaat srfvlgrlgv kdesllvlgg
      301 lsfgllgpvv lsmifsrfnf tsvlflgera akkkpvvpiv pvvqtqssl
//
LOCUS       WP_008088244             408 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Pseudomonas sp.
            GM80].
ACCESSION   WP_008088244
VERSION     WP_008088244.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM80
  ORGANISM  Pseudomonas sp. GM80
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 408)
  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 408)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Pseudomonas sp. GM80"
                     /db_xref="taxon:1144339"
     Protein         1..408
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46072
     Region          2..403
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mpatlafslk qarrlalaaq gfngrqpptv kaahlnrlie rlgllqidsv navvrshylp
       61 lfsrlgnyps dlldqaawss grrrslfeyw gheasllpls myplmgwrmq rarrgediyq
      121 qlakfgreqq dvvrrvlssv qeqgaigags lstredkagp wwdwsaekha lewlfaagev
      181 tvagrrgfer lydlpervip ssilqqalpd eaeaqrglll haaqalgvgt ekdlrdyfrl
      241 npadarprla elveagqlqi cevagwrqia yclpepkvpr kvvasallsp fdsliwersr
      301 terlfdfryr leiytpqdkr vygyyvlpfl hneriaarvd lraeraagrl avhavheeep
      361 gldeagmlal avnlrrmadw lglarvqlnc qresaarlrv afaqigcd
//
LOCUS       WP_008089219             202 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Pseudomonas sp. GM84].
ACCESSION   WP_008089219
VERSION     WP_008089219.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM84
  ORGANISM  Pseudomonas sp. GM84
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 202)
  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 202)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Pseudomonas sp. GM84"
                     /db_xref="taxon:1144340"
     Protein         1..202
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21519
     Region          2..>62
                     /region_name="kgd"
                     /note="multifunctional oxoglutarate
                     decarboxylase/oxoglutarate dehydrogenase thiamine
                     pyrophosphate-binding subunit/dihydrolipoyllysine-residue
                     succinyltransferase subunit; cl39092"
                     /db_xref="CDD:476867"
     Region          91..146
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 matasttass gspaapktka trkkpnaade vknaaasgtg spkaatpsak akktpkepae
       61 dksiaerwgk dltaagwtai pnavfehsqd lglktahivv ilhlagywwr kgndpfpska
      121 tlaqkmgvqp rtvqraiael eamgyiertq rfwksggnms nsysfnglik karvyakqmi
      181 aereakavas srkkparapk st
//
LOCUS       WP_008089574             378 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [unclassified Pseudomonas].
ACCESSION   WP_008089574
VERSION     WP_008089574.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 378)
  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 378)
  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   3  (residues 1 to 378)
  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   4  (residues 1 to 378)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 378)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 378)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..378
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40049
     Region          30..365
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(104..106,127..128,177,229,254)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 msqtfykkgf lalavatalg vssfvqadvk igvagpmtga naafgeqymk gaqaaadkvn
       61 aaggvngeki vlvkgddace pkqavsvanr lvdqdkvigv vghfcssnti pasevydeag
      121 viaitpgstn pqvterglsg mfrmcgrddq qgivagnyiv dvlkgkkvav lhdkdtygqg
      181 ladatkaqle krgvkpvlye gltrgekdfs avvtkiraag advvyfgglh peagplvrql
      241 reqglkdvkf msddgivtde lvataggaqy vdgvymtfga dprllpdska vveefrkagt
      301 epegytlyay asvqalaaaf ngaksnkged aakwlkanpv qtvmgekkwd skgdltvsdy
      361 vvyqwdkdgk yhqlekqk
//
LOCUS       WP_008090441             699 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Pseudomonas sp. GM84].
ACCESSION   WP_008090441
VERSION     WP_008090441.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM84
  ORGANISM  Pseudomonas sp. GM84
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 699)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Pseudomonas sp. GM84"
                     /db_xref="taxon:1144340"
     Protein         1..699
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72821
     Region          1..696
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 msqairdnlk rllaprhlaf vggrsmaral krcadggyqg qmwlvnpqqd sidgvpcvrs
       61 vaelpcapda vfiatnrelt ltcvaelaak gaggaicyas gfaesgaegq alqqqllaaa
      121 gdmallgpnc yglldylhss alwpvahggk avekgvavlt qsgnfaynls msdrslpvay
      181 masvgnqaql giaelmdvll deprvtaigl hleglknvpg faraahkale kgipiialkt
      241 gvsqigaela lshtsslsgs dalydslfer lgvirvsgpv sfvetlkaaa cgnlpkgdsl
      301 ialacsggda gliadysecn qlrlpaldag qveelaqvlp ayanlvnpld fttaiwgdgp
      361 akqrmldsal rsdadaamlv ldypaeftge rkecdlllel ycaalkrhgk tgfvtsafpe
      421 llpasarerl haagvpalqg vedglaawgr varyaqkrqa llalgesalv plcpqalagd
      481 sqllnewesk qalrgfglpi pngvlsspqn aladarkvgf plvlkavsaq lphkteagav
      541 alnlgdeaal graleqmrtr iaayapevpf nqvllepmag aplaelivgi krepdfglal
      601 vigaggilve llkdskslll pttdgairna vlglrsaall qgfrgkpaad ldalvaaira
      661 vadyacenas qlleldvnpl mvgatgttav dalirlgqv
//
LOCUS       WP_008090690             256 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Streptococcus
            ictaluri].
ACCESSION   WP_008090690
VERSION     WP_008090690.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus ictaluri
  ORGANISM  Streptococcus ictaluri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Streptococcus ictaluri"
                     /db_xref="taxon:380397"
     Protein         1..256
                     /product="formate/nitrite transporter family protein"
                     /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=27167
     Region          1..256
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mktpeqilea tihigehkia ktavtkailg figgamislg yllyvriaas gletfgafss
       61 ilgacafpig liiilmagge litgnmmavs aaffakkvta sellknwlvi tlfniigavf
      121 vafifghflg ltgtgifkqe vievahakla asplqaivsg igcnwfvgla lwlcyganda
      181 tgkllgtwfp vmtfvalgfq hsvanafvip aaifeggatw ldfltnfslv yigniiggai
      241 fvslfyykay yhpksh
//
LOCUS       WP_008091139             843 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas sp. GM84].
ACCESSION   WP_008091139
VERSION     WP_008091139.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM84
  ORGANISM  Pseudomonas sp. GM84
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 843)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 843)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 843)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..843
                     /organism="Pseudomonas sp. GM84"
                     /db_xref="taxon:1144340"
     Protein         1..843
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=91772
     Region          63..112
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          90..843
                     /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 mkskrmrnkg aalaagpakw slrasalvls lamahahakp vavdipaqpl dqalvalgkq
       61 tglqmvyspd lvsgkrapkv sgtmepdqal aqlldgaglt yriennsvml istdssdiga
      121 gamvigetti mgqgmgqate ntgsytpglt svgsksptsl ketpqsvsvv trqliedrqi
      181 tdindamkav pgvtvqsstf riqdfysrgf piqniqldga apmalgttag sfyssniydi
      241 aefdhvevlr gssalfggtg dpggiinlvr krpldfyqlk ftasagswdn yrseldvtgp
      301 lgfdgklrgr avvayqdrqy fvdnratdkp ffygvleadv tddtmltagm rfnkvhetgt
      361 asavprysdg adlglprhtg lsttwayadg fsreyfakvd hrlnddwkln lsytniydti
      421 dtnnattlgs vnpvtgsgvt rygtwvtqws eqnlydanis gdfsmfglnh rlvvggdyqe
      481 idsrwqgtgr fttaggpvnv fdpdstpwdd pgarpnisrd ykpnsqtqyg lysslrlqva
      541 eplhvilgar vqrykfeqty qtanaagvwt qqsrvdmhep tkvtpfggiv ydltdewaay
      601 asyaeifkpq qnllagpans gstldpmtgk tyetgikgel fggavntsia lyytkredqa
      661 vqdanfpptq vafggnccyv nggetiskgi dmeisgeilp ewmmmasytl nlnknrdtds
      721 alstvtpkhm akvfttyrlp gvlndfrvgg gvdiqsatkv sgtaatfdgq gnvvqanvpf
      781 eyeqsgyaiw namvdyride hwnvalngnn lfdkkyyqtv gtstygnyyg dprnfmltvr
      841 aty
//
LOCUS       WP_008091773             339 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM84].
ACCESSION   WP_008091773
VERSION     WP_008091773.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM84
  ORGANISM  Pseudomonas sp. GM84
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 339)
  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 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 339)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 339)
  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   5  (residues 1 to 339)
  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   6  (residues 1 to 339)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Pseudomonas sp. GM84"
                     /db_xref="taxon:1144340"
     Protein         1..339
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37618
     Region          27..202
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          92..332
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mpvqartavl tnyldvarhl klntisllge vglspallsd psqripatas iilleksarl
       61 sgcdtiglrm aelreladfg evslllshqn nlrdalqviv hygqqinesl aiyieevgnt
      121 viireelvtd rgtdnrqsie laiavmhrfc aallgshwqp ikvcfthdap adlsvhrrif
      181 ackvefgcef ngivcpaahl dtaiplanaa marhaqrymd sllgkrdhsv agevrkaiyl
      241 llpmgratla qiaqsqgmnv rtlqrrldee gvsfseliss vrrdlvvryl enpsyslgri
      301 admlgysmpn sftrwfisqf dmppaawrse rkivarkds
//
LOCUS       WP_008092005             812 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Pseudomonas sp. GM84].
ACCESSION   WP_008092005
VERSION     WP_008092005.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM84
  ORGANISM  Pseudomonas sp. GM84
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 812)
  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 812)
  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 812)
  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   4  (residues 1 to 812)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..812
                     /organism="Pseudomonas sp. GM84"
                     /db_xref="taxon:1144340"
     Protein         1..812
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89473
     Region          90..788
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mpdpvaarlr lapealtrrf speqfaftht ddlepfrgvl gqeravealq fgvamprpgy
       61 nvyvmgepgt grfsfvkryl kaegkrqqtp adwlyvnhyd darepralel psgsaaafis
      121 dmgglidnll atfpavfehp syqqkkgaid rafnqrydra ldvierasle kdvalyrdas
      181 nvaftpmadg kaldeaefgq lpeevreqfh edialleerl neelaslpqw kresnnqlrq
      241 lneetitlal qpllaplsek yaenaavcay lqsvqlnllr tvveqlvdds ktdaaarkll
      301 eeqyapslvv ghnadggapv vfephptydn lfgrieystd qgalytsyrq lrpgalhran
      361 ggflileaek mlgepfvwda lkralqsrkl kmesplgelg rvatvsltpq miplnvklvi
      421 igsrqlyyal qdhdsdfqem frvlvdfded mpmvdenleq faqllrtrtn eegmapltsd
      481 avarlatysa rlaenqsrls arigdlfqlv seadfirqla sdemtdaghi eralkakatr
      541 tgrvsqrvld dmlagiilid tegaaigkcn gltvlevgds afgmparisa tvypggsgiv
      601 dierevnlgq pihskgvmil tgylgsryaq efplaisasi aleqsygyvd gdsaslgeac
      661 tlisalsrtp lkqcfaitgs inqfgevqav ggvnekiegf frlcearglt geqgviipra
      721 nvatlmlder vlqavengqf hvyavsqade alsllvgeda gelddkgqft egsvnarvve
      781 rlreiaemis eeeieraeke rleeviaqak pa
//
LOCUS       WP_008092070             258 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Pseudomonas sp. GM84].
ACCESSION   WP_008092070
VERSION     WP_008092070.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM84
  ORGANISM  Pseudomonas sp. GM84
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Pseudomonas sp. GM84"
                     /db_xref="taxon:1144340"
     Protein         1..258
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=28947
     Region          18..174
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkalfsalll ivlagcstgl ridrshpsan qddriqfvvl hytnaslers lellthgevs
       61 ahyligdgpa tvyqlidenr rawhagesqw qgrtwlnsss igieivnpgf ddtpngrvwy
      121 pyteaqiqsl iallkdivkr nnieprhiig hsdiaplrkl dpgplfpwkr laeagigiwp
      181 danavarqqa yfnvnpptig wyqqelarfg yaieqtgqld vatrhviaaf qmrfrpqrfd
      241 gtpdaqtaam lqvlnrmr
//
LOCUS       WP_008093330              83 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Pseudomonas sp. GM84].
ACCESSION   WP_008093330
VERSION     WP_008093330.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM84
  ORGANISM  Pseudomonas sp. GM84
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Pseudomonas sp. GM84"
                     /db_xref="taxon:1144340"
     Protein         1..83
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8912
     Region          1..83
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mirvnyfary rellgsegea lpwaptlttl galraqlvgr gglwaqtlgq tnlmcarnee
       61 lctldeplcd gddiaffppv tgg
//
LOCUS       WP_008092684             406 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Pseudomonas sp.
            GM84].
ACCESSION   WP_008092684
VERSION     WP_008092684.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM84
  ORGANISM  Pseudomonas sp. GM84
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 406)
  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 406)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Pseudomonas sp. GM84"
                     /db_xref="taxon:1144340"
     Protein         1..406
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45657
     Region          1..400
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mplelstrqa rrlalsaqgf gkqppspptl palkrmlqrl gvlqidsvna lvrshylplf
       61 srlgdyapam ldqlawgrgr qrqlfeywgh easllplsly pmlrwrmaha adgrgiyrql
      121 aqfgrerqdv iarvlaavre qgalgagsls trqeragpww dwseekhale wlfaagevtv
      181 agrrgferly dvpdnvlpra ildqpqpgea eahqglmlha atalgvater dlrdyfrlep
      241 aqgraalael iadgrlqavq vqgwkqpays agtpriprri easallspfd slvwernrte
      301 rlfdfryrle iytpahkrvy gyyvlpflfd eriaarvdlr aeralgqlav havhaeadgl
      361 gevgyetlaa qllrlarwlg lervqlncpr eegsqlrral lsaala
//
LOCUS       WP_008096214             687 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Pseudomonas sp. GM84].
ACCESSION   WP_008096214
VERSION     WP_008096214.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM84
  ORGANISM  Pseudomonas sp. GM84
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Pseudomonas sp. GM84"
                     /db_xref="taxon:1144340"
     Protein         1..687
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=76016
     Region          1..686
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mrpvlplssc lglvaavtvg pqataapsve lgqlliteee qseleyarer lqsipgasnl
       61 vdmqrveqgr vasnqdvlay qpgvfaqsag ndgiklsirg sginrapgah gsgvytmfdg
      121 lpltgpggtp yelfeplwls raevlrgang fdqgalalgg ainyvthtgh daeplqvrye
      181 vgshgyqhrh vssgqvlgdl dyyvaltdse ydgyqehssg sgkgiaanlg yrfnpnletr
      241 fylryreten dlagrltkqq ikhdpraanp aylarddsrp qpgstwvgnk ttfyleddar
      301 leaglvyhdy pmdlregpmr lkvaytdvsg tlnylrrdtl fgheskttvg wrttkhlpns
      361 gasqfarssg enfgarsrdf syqgsdtvlh vgndlelipd lwlttglami ytrresdvty
      421 petggkvsqh dwdyaprlgl rydispqlqv ygnlsrsvep phpwaliwss tvatqpiemq
      481 nqtattlelg argesvlgrw dlawyysqvr hellaveivp galpkefnas ptvhqgveag
      541 ldstlwedsg igrlslrqay tfsdfhyrdd drfgdnrlpg ipmhyyqael rydwpsgfya
      601 gvntqmaskv qvdyansyha dayallgarl gwnspkqdwq twldlrnltn eryaatvtpg
      661 yddgqdiars tpgegfavya gvsysfr
//
LOCUS       WP_008103376             283 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Pantoea sp. YR343].
ACCESSION   WP_008103376
VERSION     WP_008103376.1
KEYWORDS    RefSeq.
SOURCE      Pantoea sp. YR343
  ORGANISM  Pantoea sp. YR343
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 283)
  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 283)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10097223
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Pantoea sp. YR343"
                     /db_xref="taxon:1144341"
     Protein         1..283
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29733
     Region          5..281
                     /region_name="TBP_aldolase_IIB"
                     /note="Tagatose-1,6-bisphosphate (TBP) aldolase and
                     related Type B Class II aldolases. TBP aldolase is a
                     tetrameric class II aldolase that catalyzes the reversible
                     condensation of dihydroxyacetone phosphate with
                     glyceraldehyde 3-phsophate to produce tagatose 1; cd00947"
                     /db_xref="CDD:238477"
     Site            order(26..28,31,51,54..56,60,64,67..68,141,233..234,
                     236..237,240,244,247)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238477"
     Site            order(81..82,177..179,181,208..209,211,230,232..233)
                     /site_type="active"
                     /db_xref="CDD:238477"
     Site            order(82,178,208)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238477"
     Site            order(177,179,181,209,211)
                     /site_type="other"
                     /note="Na+ binding site [ion binding]"
                     /db_xref="CDD:238477"
ORIGIN      
        1 mfammndliq aaaqqryavl aincfnleta raaiqaaeqq raplilnvyq ghsahfppav
       61 avplvrtlad aasvpvalal dhgkafplig qafragftgl midassepla enirqtaavv
      121 kmahtagvcv egelghiada ptyeladasv kmtqvadvlp fieqtnidll aisvgtahgl
      181 ypagvkpkid fqrlqelhav strplalhgg sgtpaedirr vsefgvakin vgaavfdagk
      241 mameqalkqh phaeladllg lmesacrevv aeylgwsgsa gkv
//
LOCUS       WP_008109008             762 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pseudoalteromonas sp. BSi20311].
ACCESSION   WP_008109008
VERSION     WP_008109008.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. BSi20311
  ORGANISM  Pseudoalteromonas sp. BSi20311
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 762)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 762)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 762)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..762
                     /organism="Pseudoalteromonas sp. BSi20311"
                     /db_xref="taxon:383911"
     Protein         1..762
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=84828
     Region          19..748
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mfkvikrlll vvvvlalagt aivygvltls lptldgkgrs davtqpvkva rdtlgqavit
       61 aatrheaayg lgyahgqdrf fqmdllrrna agelselfgk aalaldkkmr fhqlrkrsqa
      121 ilktlpeadk qllksyaqgv neglaqigyp sfeylltgae qqpwqsedsl lvifsmyldl
      181 qtatferdqa liqiqqqyga kmvefltqps qyqaaldgsv ltpytqtipq lptqslaaik
      241 titanlevgs nnwavtadlt ntqaamlsdd mhlsmavpvi wyraqlnyth dnqayqvtgv
      301 slpgapaivv gsnnkiawgf tngyidtadw valtdssktw qvnevialpn gnsetypltl
      361 seygpvkyin nqpyalswaa hqpyavdmql lqleqaetvd dalniasnvg ipvqnlmvvd
      421 sqgsaawkhm ggipartaps elaineneys atwqqnevir pfvknpqsgr lwtgnsrvvs
      481 aednarfgng gyalgaratq irdrlfekqr fnesdfyqlq ldnqarflmp whallleqlk
      541 kqparykdhi nalenwqqca cpqsigytlv ktyrdelini lfssiettln qqdgtlkyvk
      601 rdlepavwql ikaqptswvn pqftnweqql qgafeqtlaq lttkfgnniq nwqwgkvnel
      661 tiehpfakqi pmlskllnmp tasgfgdsym pavqkrgfga sqrfiaqpgh lesailtvpg
      721 gqsghplsef yragfdeyve gkhtpllpqt fmhqieivpm sd
//
LOCUS       WP_008111026             259 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Herbaspirillum sp. YR522].
ACCESSION   WP_008111026
VERSION     WP_008111026.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. YR522
  ORGANISM  Herbaspirillum sp. YR522
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Herbaspirillum sp. YR522"
                     /db_xref="taxon:1144342"
     Protein         1..259
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=28474
     Region          29..245
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mipihqdilp agkagcggcq apaqddiafe fayqpivdld trsvyafeal vrgpagesaa
       61 svlaqvnegn qyrfdqacrm kavegaarlg mtsllsinfl pnavyrpevc irstfeaart
      121 hgfpieniif evtegehiqd rphlvdifrq yrrfgfqtai ddfgagyagl nllaeyqpdi
      181 vkidmdlvrd ihlhkprqai vrgitgicre lgirvlaegi etreerdflc sagislmqgy
      241 wfakpgfmal pgiapaawa
//
LOCUS       WP_008111219             194 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [unclassified Pseudoalteromonas].
ACCESSION   WP_008111219
VERSION     WP_008111219.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..194
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21350
     Region          5..165
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mavqkklkqk trqfiesknm lggitiasfl estivpiple avlvplmqar reklwqialm
       61 atlgcivgal fgyalgyylf dvigdwvint fsspeqfenv kqkmqsqgfw fvlslgivpi
      121 pfqiamlaag atkyslalfl lasaiarsir yfglaivvyy agnqaeriis khktkamigl
      181 tilvaigwii stli
//
LOCUS       WP_008111649             365 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Herbaspirillum sp.
            YR522].
ACCESSION   WP_008111649
VERSION     WP_008111649.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. YR522
  ORGANISM  Herbaspirillum sp. YR522
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 365)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Herbaspirillum sp. YR522"
                     /db_xref="taxon:1144342"
     Protein         1..365
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39344
     Region          37..338
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mqatahditf agfrtavpaq rhsyarepgm ftqaeadklv estgiyerrv lpphlcasdm
       61 ctaaaidllk sldwdpasve vlifvsqdsd ynlpatacli qnrlglptsc aaldinlgcs
      121 gfvyacwias qmltgasgtr alvlcgdtst rhlmpedrst rplfgdagaa valekrpgag
      181 pmhvvmgtdg rgapnivvra ggrrnplipr aerftdeeht tlyrdarlsl ngpevftfsl
      241 ravpplvrnt lahagvtedk vdyyvlhqan klmleqirrk igvdaerfiv dlynfgntss
      301 asiplaicss mgerlsqgsa kvllagfgvg wswasmlldi gpipapavie iaddfeplsl
      361 tfkrp
//
LOCUS       WP_008111841             310 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Herbaspirillum sp. YR522].
ACCESSION   WP_008111841
VERSION     WP_008111841.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. YR522
  ORGANISM  Herbaspirillum sp. YR522
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Herbaspirillum sp. YR522"
                     /db_xref="taxon:1144342"
     Protein         1..310
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33003
     Region          <72..205
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 msnatppqll qpllqayrgd llvrlseggp gwyvrdhvvs hyfdadddpa eiaemiaain
       61 tdivlrhhpe pdgplwalgt tgndvvvsdd hdvsvsvddg kdvvitgagd dylsgdggdd
      121 wlyggagddn llggagndrl vgelgddmln ggsgddrlfg gdgndrlhgd ggndrlngga
      181 gddiyffgkt dgadrifnnd adgddrvqfr ngidpgqlwl rrlgsnlevm ltetgdtltl
      241 yhwfageqyr vdrfqlssdg mapncsylss dkvevlvaam salpppqvgt tvlpphyqva
      301 lnavlaaswt
//
LOCUS       WP_008112532             101 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [unclassified Pseudoalteromonas].
ACCESSION   WP_008112532
VERSION     WP_008112532.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..101
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11203
     Region          9..101
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(24,55..56,58,84)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(24..25,33,36,38..39,41,44..45,47,55,60,66)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mdvnketviy tiiasipkgc vvsygqvaal agypnnarlv grllkemakd stipwhrvvn
       61 sqgkiafvqg saqyqtqrek llsegvtfnn qrinmakhrw q
//
LOCUS       WP_008113434             359 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Herbaspirillum sp. YR522].
ACCESSION   WP_008113434
VERSION     WP_008113434.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. YR522
  ORGANISM  Herbaspirillum sp. YR522
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Herbaspirillum sp. YR522"
                     /db_xref="taxon:1144342"
     Protein         1..359
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39761
     Region          1..350
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msievkqink rfgsftaldd vslnfpagel tallgpsgcg kttllriiag lesldsgqvl
       61 ldgedasarn vrerqvgfvf qhyalfkhmt vfeniafglr vkprsqrpse svirdkvrkl
      121 lelvqldwla dryppqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 rlhdelhvts ifvthdqeea levadqvvlm nkgrveqlgs paevynhpat pfvygflgnv
      241 nlfhgrlheg vldtggarfe apnhgdardl agigfvrphe ldveryspga qgivvqlrrs
      301 haigplaqle lerddnaeli eavisnerfa qlglksgetl vvrprrlqvf anqdagaas
//
LOCUS       WP_008113303              97 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Pseudoalteromonas].
ACCESSION   WP_008113303
VERSION     WP_008113303.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 97)
  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   2  (residues 1 to 97)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..97
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10245
     Region          29..91
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mklikiisla aalcllpmgt tfaqsdmlsk qvqsavvnin tadlkqlikl pgvgkkkaqa
       61 iidyretngd fasledlakv kgvgkkmlak ldgkvaf
//
LOCUS       WP_008114756             443 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Herbaspirillum
            sp. YR522].
ACCESSION   WP_008114756
VERSION     WP_008114756.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. YR522
  ORGANISM  Herbaspirillum sp. YR522
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 443)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 443)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Herbaspirillum sp. YR522"
                     /db_xref="taxon:1144342"
     Protein         1..443
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48184
     Region          5..423
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 msmlrslrir lgtvelgslf alddgrcyfr fdddyamsga qhpvlsqlyc asseqrtraq
       61 lldptlaanr gdgrgglppf fqnllpegql rkhlvqragl spddefglla ycgrdlpgdv
      121 salaeqldep glgrllgqgh dsyemssgql pvpggeslsg vqpklalvrq aggryvmrsr
      181 drqgshfiak lpatdypnmp qvefssltla aaagvtvcgf aleplsviad hlpfglrnda
      241 srfllvqrfd rdaptatgrl hmedfaqvtg tapsakyagt yaaigailme rstrgvedvf
      301 ellrrikvne llgnfdahlk nfsllyhtpq qaalspaydi vayaayvggn ghalalvpgq
      361 garqllspav lrqlaniwgv aetrlrtvli dtveramsqw paliaelplt hdqrlrlwah
      421 idanpsvvaw rrraarptrk apa
//
LOCUS       WP_008114789             384 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Herbaspirillum sp. YR522].
ACCESSION   WP_008114789
VERSION     WP_008114789.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. YR522
  ORGANISM  Herbaspirillum sp. YR522
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 384)
  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 384)
  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   3  (residues 1 to 384)
  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   4  (residues 1 to 384)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 384)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 384)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Herbaspirillum sp. YR522"
                     /db_xref="taxon:1144342"
     Protein         1..384
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40459
     Region          33..369
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(109..111,132..133,182,234,258)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mqspfpvprv irhllaagll aaslgvhaer vvtiglavpl sgpsgstgas leqaaqlaid
       61 dlnaarpvid gepvrfalla qddradprtg elvadyfvks rvaavvghwn sgvgipasri
      121 yaaagivqva pavtspaytq qgyagafriv phdgegarhi aqyvvremka anvvviddrt
      181 pfgagyaaef agnvvalggk igarfalssk ssdfngilrt vrslkpdavl fagldaqaaq
      241 lvsemrrlqi gapligiggl vgptfvrlag sagegtvvle pgpasyrgpq wthfeaawka
      301 ryqepitlya pfaydavrvi aaamrqanat ggaplarelh riryrgvtgp iafdregnlr
      361 dpvftlygvk qgrwqvikti ders
//
LOCUS       WP_008117128             193 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Herbaspirillum sp. YR522].
ACCESSION   WP_008117128
VERSION     WP_008117128.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. YR522
  ORGANISM  Herbaspirillum sp. YR522
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Herbaspirillum sp. YR522"
                     /db_xref="taxon:1144342"
     Protein         1..193
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20795
     Region          3..190
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mprqrliiai tgatgaaygv rllqhlrqsd qvethlmisd agvlnihqel dlgrkdveal
       61 advvhhvrdi gasiasgsfa scgmvvapcs mktlaavahg lsdnlitraa dvvlkerrrl
      121 vlmvretpfn lahlrnmtav temggvifpp lpgfyqrpqs ieqmidhtlg rvldlfgvah
      181 altpewlglk pgg
//
LOCUS       WP_008117953             346 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Herbaspirillum sp.
            YR522].
ACCESSION   WP_008117953
VERSION     WP_008117953.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. YR522
  ORGANISM  Herbaspirillum sp. YR522
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 346)
  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 346)
  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 346)
  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 346)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Herbaspirillum sp. YR522"
                     /db_xref="taxon:1144342"
     Protein         1..346
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=38161
     Region          12..344
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 msklaedfrs srrgflktas vasaalatgl ygnsahaaef tlkygnnlpm thpmnvrake
       61 maekiaaesk grvelqvysn gqlgtdtdml sqvrsgaidf ftispevlgt lvsagqlsgv
      121 gfafkdygqv waamdgdlga lvrrelaakt slfafekcwd ngyrqvttst raitrpedfk
      181 gmklrvppsp latslfrgfd asptsinfae vysalqtkiv egqenplavi stvkfyevqk
      241 fcsmtnhvws gfwfmgnkks ferlpkdlqe ivsrnineag vkqrvdvkal neslvadmka
      301 kglqfnnidn dafraklrsa gfytewhkkf gdeawatlek ytgkla
//
LOCUS       WP_008119202             416 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Herbaspirillum sp. YR522].
ACCESSION   WP_008119202
VERSION     WP_008119202.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. YR522
  ORGANISM  Herbaspirillum sp. YR522
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 416)
  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 416)
  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   3  (residues 1 to 416)
  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   4  (residues 1 to 416)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 416)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 416)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 416)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Herbaspirillum sp. YR522"
                     /db_xref="taxon:1144342"
     Protein         1..416
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44818
     Region          64..400
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(140..142,163..164,213,265,289)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 meagshsrcc tqdqpgddrr rqllawlmal alplpamaan gkpaapdglr qpaatdedpa
       61 ttlrigfagp lsgpsagvgk smhdavllav eeanqrgvri ggkpwrirli aqddradsat
      121 aeyvarylvg qkvigvighw nsgaslaaap iyhaagviqi spatmsrrft aqaypavfrt
      181 ipnnesvgly sahyavrrmg iksvvtiddr tpfgqglaeq faraaherga evlgtysvse
      241 ktsdfngpll qirhrrpqli ffggldwqag llakaiarln iearlmvsag svglpflmsa
      301 gaagngavvl epgaapermp gwkafrqryg qrfdsdlhly asfaydavqa llmairqras
      361 sdptvvaqel hrlrftgvsg piafndegdl enpsftvyev qqqrwmpllq idglpr
//
LOCUS       WP_008119996             399 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Herbaspirillum sp. YR522].
ACCESSION   WP_008119996
VERSION     WP_008119996.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. YR522
  ORGANISM  Herbaspirillum sp. YR522
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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   3  (residues 1 to 399)
  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   4  (residues 1 to 399)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 399)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 399)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 399)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Herbaspirillum sp. YR522"
                     /db_xref="taxon:1144342"
     Protein         1..399
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42735
     Region          40..375
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(115..117,138..139,188,239,264)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mpkllsvdvl wrillslavi lypapgvsad vepvprivli gfsgalsgvs edlgkslana
       61 aemalaeanr lqlrvsgqrv afrllryddr ddpatameva rqmlqagvva vvgtansnts
      121 eavaklysda gvalispaas atalsergyt sffrlidhde hagqflghyv vrdmklrrla
      181 vidngsmygv gvassffsqv rangativmr drisyasnlp qlvrrlrlrg tealffggya
      241 aqaaqlaqtl rhegggmrll massgvvgas fliaarngan gtvaiesgvp aaemagwrrf
      301 eheyqqrfgl hlhgltpfay daaqvavaav rqadsldsrr ivqalrrisf rgltgvvafd
      361 akgnprnpll sisevrdqrw vplrtidvrh ggtlkpggs
//
LOCUS       WP_008121579             206 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein, partial [Phyllobacterium sp. YR531].
ACCESSION   WP_008121579
VERSION     WP_008121579.1
KEYWORDS    RefSeq.
SOURCE      Phyllobacterium sp. YR531
  ORGANISM  Phyllobacterium sp. YR531
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Phyllobacterium.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Phyllobacterium sp. YR531"
                     /db_xref="taxon:1144343"
     Protein         1..>206
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
     Region          <2..164
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 maiidgttgn dnlegtpnad iingfegddq lfgragndrl kggagldrly gfegddtlng
       61 eagsdwvfag egndvlngdi gddlllgeag sdtiyggege ddlrggdgdd llhggagddw
      121 llgdwnggap gndrlnggeg ndnlngqdgd dvldggvgad tfwggagsdk fyvdnvgdkv
      181 iednvagidv vsssvsfatg gqhien
//
LOCUS       WP_008121817             200 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding
            protein, partial [Phyllobacterium sp. YR531].
ACCESSION   WP_008121817
VERSION     WP_008121817.1
KEYWORDS    RefSeq.
SOURCE      Phyllobacterium sp. YR531
  ORGANISM  Phyllobacterium sp. YR531
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Phyllobacterium.
REFERENCE   1  (residues 1 to 200)
  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 200)
  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   3  (residues 1 to 200)
  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   4  (residues 1 to 200)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 200)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 200)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Phyllobacterium sp. YR531"
                     /db_xref="taxon:1144343"
     Protein         1..>200
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          27..>200
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkksllsgva faaclvfnsy asadillgvg apltgpnaaf gaqiqkgaea aiaeinaagg
       61 ingekieivl gddvsdpkqg isvankfvad gvkfvighfn sgisipasev yaenglleis
      121 paatnpvyte rglwntfrtc grddkqgtia gayiaekfkd akvavihdkt pygqgladet
      181 kkalnakgvt eamyegvnvg
//
LOCUS       WP_008121867             371 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Phyllobacterium sp. YR531].
ACCESSION   WP_008121867
VERSION     WP_008121867.1
KEYWORDS    RefSeq.
SOURCE      Phyllobacterium sp. YR531
  ORGANISM  Phyllobacterium sp. YR531
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Phyllobacterium.
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   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   3  (residues 1 to 371)
  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   4  (residues 1 to 371)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 371)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 371)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Phyllobacterium sp. YR531"
                     /db_xref="taxon:1144343"
     Protein         1..371
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38739
     Region          27..358
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(99..101,122..123,172,224,248)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkkslfsgva faamlalsgh ayadlligvg gpmtgpnaaf gaqlqkgaea avaeinaagg
       61 vngeqiklsl gddvsdpkqg isvankfvad gvkfvvghfn sgvsipasev yaengilevt
      121 paatnpvfte rglwntfrtc grddqqgvva ggyiaekfkd akvavvhdkt pygqgladet
      181 kktlnakgvt ealyegvnvg dkdfsaliak akqagvtvly wgglhteagl iirqladqgl
      241 kvtfisgdgi vsnelasiag davagtlntf gpdpskdpan kelvekfraq gfepeaytly
      301 syaatqviaa aataaksndp etvaktlkek gpfktvlgdi afdekgdpkl pgyvmyewkk
      361 gedgkytytq q
//
LOCUS       WP_008123627             641 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Phyllobacterium sp. YR531].
ACCESSION   WP_008123627
VERSION     WP_008123627.1
KEYWORDS    RefSeq.
SOURCE      Phyllobacterium sp. YR531
  ORGANISM  Phyllobacterium sp. YR531
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Phyllobacterium.
REFERENCE   1  (residues 1 to 641)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 641)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 641)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 641)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 641)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 641)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Phyllobacterium sp. YR531"
                     /db_xref="taxon:1144343"
     Protein         1..641
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=70292
     Region          19..641
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mndhqtvgdd cdngsvnyep ephhkeafpv lvlgalgvvy gdigtspiya frealhaasl
       61 dgslsrtdvl gvvsmifwal alivtikyvi fvlradndge ggilslmala rssfksrpql
      121 ilglgiigas lfygdavitp aisvlsaveg leivtptlkp fivpitivil ltlfsiqrfg
      181 tasvakifgp itliwflaig ffgllhiadd lsifaavnpy yafeyiinnp qtafptigtv
      241 flavtgaeal yadlghfgrk piatawmwvv fpclllnyfg qgafilaypd eaknpffemf
      301 phwallpmvl latmatvias qavisgaysl srqavqlnll prlniehtse kqsgqvylpk
      361 vnvllgivvv llvlgferss nlasaygiav tgnmlvttil lfivmtriwk wslwlaaslt
      421 gcfliidltf vsanlikvvd ggwaslvvaf lvvlimftwv rgsrklfekt rkgevplali
      481 skkmaenppt lvpgtavflt gdpkstptal mhslkhykvl hqnnviltvi tapsplvkks
      541 drvriepind lfmrvtltfg ymerpniprt laicrkqgwk fdimttsffl srrslkasar
      601 semprwqdrl fialarsasd ateyfqiptg rvveigtqvn i
//
LOCUS       WP_008124059             476 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Phyllobacterium sp. YR531].
ACCESSION   WP_008124059
VERSION     WP_008124059.1
KEYWORDS    RefSeq.
SOURCE      Phyllobacterium sp. YR531
  ORGANISM  Phyllobacterium sp. YR531
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Phyllobacterium.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Phyllobacterium sp. YR531"
                     /db_xref="taxon:1144343"
     Protein         1..476
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=52029
     Region          12..472
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mnmqapvqgf iieieqevlg tllgggdfrr iagvledhhf vedlhrilfg virsahdryn
       61 stampvvakl iseefaeavr rkldkpvnay lasmvastln gpdgleknar kiieqwarvs
      121 lsneaarlha aandpatnpv elvtnaglvf ddilsdvrrg pkrktqvtvg dastnafaat
      181 reaiergsgl tgvtwgltdv nrltggiqrr dltligarps mgkttvglsv slkaakagag
      241 vgfislemda dklaaraitd iaydrnvkvp yqdlitgrik sgdlqaleaa tkdmeqlplw
      301 iedqsglsit dirikteslm ikaekmgqkl dvlvidhlgl ikasnryagn rtneiaemtg
      361 alktmareyg iavvalsqln rgleqqadkr pqlsslrdsg aieqdadtii flyreayyld
      421 rekasspeke meriekladc qnklefhiak qrngpvtnvd lfvdiacstv rngsry
//
LOCUS       WP_008125548             424 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Hoylesella
            timonensis].
ACCESSION   WP_008125548
VERSION     WP_008125548.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella timonensis
  ORGANISM  Hoylesella timonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 424)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 424)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Hoylesella timonensis"
                     /db_xref="taxon:386414"
     Protein         1..424
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48232
     Region          2..412
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mekldviasf dwmdkeekvg slgheylrgs dvfsfefdkt wlkrypkidf gcdlrpytgv
       61 qysqgnhifg cfsdtlpdrw grrlidlras letegkasht lsdwdylkgv edemrmggfr
      121 fqdptdgsfi sstpsysvpp aihidellqa akeiekseyk hlepekkwvq rlfqpgssmg
      181 garpkacvqs ggqlylakfp sinddinvsr wehfahlmak ecgitvaetq vikagtgqdi
      241 llskrfdrte dnkrihmass ltvlgltdgd gqrnskgyld ivdfiissgg nhieanleel
      301 ykrvafnici gntddhfrnh afllgkdgwe lspaydmnpt nsmfqallid antnesslnh
      361 lynahelyml dettargiim dvtrnmkywe siaediglpr reityftdrf eqgmefqyga
      421 glrr
//
LOCUS       WP_008127844             101 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [unclassified Pseudoalteromonas].
ACCESSION   WP_008127844
VERSION     WP_008127844.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..101
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11200
     Region          9..101
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(24,55..56,58,84)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(24..25,33,36,38..39,41,44..45,47,55,60,66)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mdieketliy tviagipagk vasygqvatl agfpqnsrlv grllkimpsd svipwhrvvn
       61 sqgkiafpvg snkyqeqrqk llsegvlfin dkvnmrecrw q
//
LOCUS       WP_008128830             397 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Phyllobacterium sp. YR531].
ACCESSION   WP_008128830
VERSION     WP_008128830.1
KEYWORDS    RefSeq.
SOURCE      Phyllobacterium sp. YR531
  ORGANISM  Phyllobacterium sp. YR531
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Phyllobacterium.
REFERENCE   1  (residues 1 to 397)
  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 397)
  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
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 397)
  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   5  (residues 1 to 397)
  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   6  (residues 1 to 397)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 397)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 397)
  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 15726307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Phyllobacterium sp. YR531"
                     /db_xref="taxon:1144343"
     Protein         1..397
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42861
     Region          20..>73
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          106..379
                     /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 mfltidetay edahqrdcar vaallsgegp hsrasvadrl kmtstatshv vgdlterglv
       61 merpgtkvgr grppigialn lkrlgasiih issrtllgfl ldlggtvleh kaveipadsd
      121 naamaeamrq lvqwlinkcp vgmlhlgtsv avpgvvdvka rtwlitsrwp kvrnldigna
      181 lapvtpvvlv crhldaelda rttretayrs gntlllhwgw giglscsigg qpllqnggpf
      241 geighwrfna ldqrecdcgn hgcletgaal wallphlrkl wpnlseeeep lagqlaglpl
      301 ldipemaeai klmarsltnv crllfpsrvi itgpfvanad vweaftaafk tegligslel
      361 paliadkfsq eyvihgaclp llnaglesfi renkraa
//
LOCUS       WP_008129628             196 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Bradyrhizobium sp.
            YR681].
ACCESSION   WP_008129628
VERSION     WP_008129628.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. YR681
  ORGANISM  Bradyrhizobium sp. YR681
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 196)
  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 196)
  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   3  (residues 1 to 196)
  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   4  (residues 1 to 196)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 196)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Bradyrhizobium sp. YR681"
                     /db_xref="taxon:1144344"
     Protein         1..196
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21786
     Region          8..196
                     /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"
ORIGIN      
        1 msaeqspkiv ivdespiraa ileeglreag ftqivhisem qsllariyav dpdiilidle
       61 npsrdvleam fqvsravrrp iamfvdqsds ssiqasveag vsayivdglk kerikpildl
      121 cvsrfnafak lqeelertks qledrkiiek akgilmkvkg lnedeayvll rstamrekkk
      181 igeiaqsiit asemlk
//
LOCUS       WP_008129630             387 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Bradyrhizobium sp. YR681].
ACCESSION   WP_008129630
VERSION     WP_008129630.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. YR681
  ORGANISM  Bradyrhizobium sp. YR681
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 387)
  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 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   3  (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   4  (residues 1 to 387)
  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 387)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Bradyrhizobium sp. YR681"
                     /db_xref="taxon:1144344"
     Protein         1..387
                     /product="CmpA/NrtA family 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=41058
     Region          2..262
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mtaplrigfi plvdaaaliv avdkgftaae gldvelvrev swsnvrdkln iglfdaahll
       61 apvaiasslg lghvkvpiaa pfnlgvngna itvspalhaa lmeeidgdrf dplvtakala
      121 kvvakrrkag adpltfgmtf pfsthnyqlr fwmaaagvdp dedvrlvvlp ppymvdslan
      181 ghvdafcvga pwnsvavdlg ighilhfvsd ilvraaekvl avrqvwadkn pdvvaslvra
      241 avkgaafied pvnlaeaarv laqperigvd aeviqrtltg rlkispdgtf resgryllvg
      301 regagrpdpv qaawlyaqmv rwgqtaltpd gvktamavfr pdlydaalgr papaeapaaf
      361 vafagpafdp gnirghleaf evgrwka
//
LOCUS       WP_008130606             627 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_008130606
VERSION     WP_008130606.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 627)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 627)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 627)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..627
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=70509
     Region          80..615
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mlkgrvkvsw lvagfalflv slvvyiyyty httraeimes vdarllnaaa svkhilgddy
       61 lntmnqngqi nffdyevksr qlsefaqald vayvyamilk nnrvyftass ytqddmnngk
      121 itqyldiype atdlnisafy stepvfevsa dqwghfktif ipfvddktgk tyltgaditi
      181 ldlnqklses vskaaamasf fffiailvaa iyvyllkrsl atdsstgfen hialeyllkk
      241 snshhmqlav vwvneiedin sfygteigdk vmknllmhfk srcsanchly rlatnklvll
      301 spketpyeel sdlietynan tplltdpfiy itlcagiatg nkslllenah iaalqakqgr
      361 htvinyskal hdvktqyqyn vemakevhda fdnnrivpyf qpiidtktnq ivqyeclarm
      421 vtasgeilkp daflnvvtrs rmdglltrti fsqcisrfrk tnicwslnit aqdmldpsln
      481 efitnelkry phpsnitlel ietqaianys evkafismvk skgvkviidd fgsgysnisn
      541 vlklevdgik ldgglikqii hdndiylfie hiaafanqld llliaesven aaivnaleka
      601 nvtlmqgnhf aqpapqfatp enadlis
//
LOCUS       WP_008133524             741 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Bradyrhizobium sp. YR681].
ACCESSION   WP_008133524
VERSION     WP_008133524.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. YR681
  ORGANISM  Bradyrhizobium sp. YR681
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 741)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Bradyrhizobium sp. YR681"
                     /db_xref="taxon:1144344"
     Protein         1..741
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=82082
     Region          23..657
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mkrlkilrrw farkfgfarl mclallvvfa girlwdpppv qelrlrtfdm fqlidprhkt
       61 vrpvtivdid dkslaklgqw pwprtriadl iqnltsggav avgfdvvfse adrlnpdmva
      121 sqmrylddat raklrelpsn dqvladaikr srvvlgetgq raisseidks lpftgvatvg
      181 eenaerflfe fpgllrnvpv iekvaagrgl ftirperdgl irrvpmvmra qgnimpslsl
      241 eilrvvtgtp tllvrtdktg vrairlkgve iptdrngqlw vhyarqdpsi yvsaadvldn
      301 tappakiagk lvlvgtsavg lndikttpvs stmpgveiha qvlesvlsga visqpnyalg
      361 vellaalvig llviiltpnl gpvrlvlaga afaailvgvs wffysqyryl idftypllst
      421 taiyltlifa sfvreqrqrk eirgmfaqyl spvlveqltp eklvlggeer gmtvmfsdvr
      481 gftsisesyk hdpqglialm nrfltpltnv itdrkgyvdk ymgdaimafw naplddvehe
      541 vnaceaaiqm leridavnre reqeaadggh vyiplnvgig lntgigvvgn mgsdlrknyt
      601 algdcvnlas rlegqtkeyg fpiivgssta laakdkfail eldfimvkgk sepeviyaia
      661 gredvmhsga fqrlrnvtie mlgcyrsrdw qgaldaierg rrsedadtle klfrlyearv
      721 kdfqinppae dwngafallt k
//
LOCUS       WP_008134972             697 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease, partial [Bradyrhizobium sp. YR681].
ACCESSION   WP_008134972
VERSION     WP_008134972.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. YR681
  ORGANISM  Bradyrhizobium sp. YR681
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 697)
  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 697)
  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 697)
  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 697)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Bradyrhizobium sp. YR681"
                     /db_xref="taxon:1144344"
     Protein         1..>697
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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]"
     Region          28..697
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mlqaegsaep ikvefdnfeh gfpegfgpgw wghlaywigi afatfqlyva afnylpsqvv
       61 rgvhvgflvl ltfglianft arsdigrafg wvigaagffc glyqwifyad liardgdptn
      121 vdlavgtlla vlifegtrrl mgaalplmcg acllywffgq ylpsplnhrg ygfdqivthl
      181 sfgtegfygv piyvsatyif lfilfgsfle ragmiqlftd vslglfgrtr ggpakvavfa
      241 sgmmgtisgs gvanvvtvgq ftiplmirfg yrrafaagve atasmggqim ppvmgavafi
      301 maetlgvqys eivkaaaipa ilyfasafwm vhleagkhgl vgmkkaeips awkalvtrwy
      361 lvlplaalvy mlfegftply agsmglaltv alilgtaitt gasstvvrsi fwiglalvva
      421 alsrdglqiv pvasvvvgli vitafirggf kalrecrdal aesaksaitv gmacaivgvi
      481 igmmsqtgvg tifgswvigl gekslflali mtmllsillg tgiptiptyi itaalaapal
      541 aklgvplias hmfafyygim adlsppvala alaaapiake npdkigweam rialagyvip
      601 fifvyspalm lqagdpmaak lgfygavala sfkalvaial fgmvaigylf trltllervv
      661 glgaalcllg dfafsdtagf tlaaalvlwq wrqrppa
//
LOCUS       WP_008135014             324 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein, partial [Bradyrhizobium
            sp. YR681].
ACCESSION   WP_008135014
VERSION     WP_008135014.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. YR681
  ORGANISM  Bradyrhizobium sp. YR681
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 324)
  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 324)
  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 324)
  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 324)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Bradyrhizobium sp. YR681"
                     /db_xref="taxon:1144344"
     Protein         <1..324
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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]"
     Region          1..322
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 aaavplvalr trpaqaaefe yklatgqslt qpintrldqa vkriketsgg rleikffpas
       61 qlgsdtdllt qirsggvdfl niagsvlstv apvagianvg fafsdygqvw samdgelgkl
      121 iasqiektga lviakpadnt frqissftkp iktpadlagy rirvpvspif tslfkslgan
      181 ptsinfnely talqthlvdg qenglvtiea gkiyevqkyi setnhiwdpf filgnrrsvk
      241 alpdelqaiv rrefdqaame qradtaklnl tlkdqlvakg itfeasdkea frkelstagf
      301 ykewrgkfge dnwktleaaa gala
//
LOCUS       WP_008135438              99 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Pseudoalteromonas sp. BSi20495].
ACCESSION   WP_008135438
VERSION     WP_008135438.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. BSi20495
  ORGANISM  Pseudoalteromonas sp. BSi20495
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Pseudoalteromonas sp. BSi20495"
                     /db_xref="taxon:386429"
     Protein         1..99
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=10835
     Region          18..99
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mavgnainpn daipsaqnve llffgqlker lkcsklslei tqpltiselk lklvsqyphw
       61 qpwleerell aalnqtmsss deivkagdel affppvtgg
//
LOCUS       WP_008136806             145 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Pseudoalteromonas sp. BSi20495].
ACCESSION   WP_008136806
VERSION     WP_008136806.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. BSi20495
  ORGANISM  Pseudoalteromonas sp. BSi20495
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Pseudoalteromonas sp. BSi20495"
                     /db_xref="taxon:386429"
     Protein         1..145
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14837
     Region          4..140
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mktmtqkqqg ftlielmivv aiigilaaia ipqyqnyiar sqfseahsll sgsrvavqer
       61 vsqgaaftga slglktagty gaigapadya anaatyalty tfsgantnln tktvtytyta
      121 atsawacstt vaaefatnct vaagg
//
LOCUS       WP_008136743             734 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [unclassified
            Pseudoalteromonas].
ACCESSION   WP_008136743
VERSION     WP_008136743.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 734)
  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   3  (residues 1 to 734)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..734
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=78723
     Region          5..734
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mfevdedilq dflveageil ellseqlvel ennpedtell naifrgfhtv kggagflamt
       61 elvdachgae nvfdllrqgv rsvnselmdv ilqaldtine mfatiqnrdk pepadpqlle
      121 vlhklglppt edelsgtspe vvveqpqeea aeaqtpstdg adpfafdelf sgptssetds
      181 qideitedef enlldelhgt sqesavkapt nshdlngdit ddefdnllde lhgvgsfgsv
      241 aaqesnvtpd vqkpspstnn tdssnddisd defeslldel hgkgtapksl estpaiaekp
      301 aakqavpkpk aapvpkveas kpvpakpaek taakapaaap kkataptaet tvrvdtkrld
      361 qimnmvgelv lvrnrlvsla tnseseamgk aisnldvvta diqgavmqtr mqpikkvfgr
      421 fprvvrdlar slnkdinlll vgeetdldkn lvealadplv hlvrnsvdhg iempdfreaa
      481 gkprtgtvtl sasqqgdhil ltikddgagm daeklkkiai skgvldhdqa srlsdteayn
      541 lifapgfstk eeisdisgrg vgmdvvktki tqlngsvsiq selgvgttle ikvpltlail
      601 ptlmvvvgeq tfalplagvs eifhldltkt nvvdsqltii vrkkaiplfy lehwlvkgad
      661 rsqrkahghv vivqigtqqv gfvvdsligq eevvikplda llqgtpgmag atitsdggia
      721 lildvpnmlk hyag
//
LOCUS       WP_008137052             345 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Bradyrhizobium sp. YR681].
ACCESSION   WP_008137052
VERSION     WP_008137052.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. YR681
  ORGANISM  Bradyrhizobium sp. YR681
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Bradyrhizobium sp. YR681"
                     /db_xref="taxon:1144344"
     Protein         1..345
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37761
     Region          1..342
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mtievknlvk kfgsfaaldg vdlkvdngel lallgpsgsg kttllriiag ldwpdsgevs
       61 fngedalaqg arerhvgfvf qhyalfrhmt vfenvafglr vqpravrkde atirarvkel
      121 ldlvqldwla drypsqlsgg qrqrialara laieprilll depfgaldak vrkelrkwlr
      181 slhheinvts ifvthdqeea levanrvvvm dkgrieqigs pddvyetpat afvhgfiges
      241 ielpvqvegg virlgdhplr laadglapga sklfvrrhdm lvgppgsgaf egavqhvrnf
      301 gpvqraeval sggqtieida prgrelragd tigleprryr ifagt
//
LOCUS       WP_008139085             256 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Bradyrhizobium sp. YR681].
ACCESSION   WP_008139085
VERSION     WP_008139085.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. YR681
  ORGANISM  Bradyrhizobium sp. YR681
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 256)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Bradyrhizobium sp. YR681"
                     /db_xref="taxon:1144344"
     Protein         1..256
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=27838
     Region          17..236
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 magvckgcgg gaglpfefrm afqpivavne qrvwgyealv rgpqgesaqs vlsqltedql
       61 yrfdqaarvm aietagklfd dpqarlsinf mpnavyepqa ciqqslaaar rsnfppanlm
      121 feftenerms dpahvehivr tykklgflta lddfgagyag lsllarlqpd likvdmellr
      181 dihlsrpkqv ivagiasmar eldirllaeg veseaeltvl raagidlfqg yyfskpgfms
      241 lpdvsafsaa taarag
//
LOCUS       WP_008139561             206 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Pseudoalteromonas sp. BSi20495].
ACCESSION   WP_008139561
VERSION     WP_008139561.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. BSi20495
  ORGANISM  Pseudoalteromonas sp. BSi20495
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 206)
  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 206)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 206)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Pseudoalteromonas sp. BSi20495"
                     /db_xref="taxon:386429"
     Protein         1..206
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=21975
     Region          1..199
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 mdihsteeeq aeaikrffre ngvslalgiv vglgglygwk aynqnqitta ekasnsftkl
       61 vegddvlssa dtfisenkdt nyatlaafva akdavdaqkl dvaseklswi vsnvqntelk
      121 aiaitrlari qiaqtkydda lntlnaplpe afnanvaelk gdiyaqqgnk dhartayqaa
      181 vdaggltsnp llqvklddla vtspaa
//
LOCUS       WP_008139603             322 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Bradyrhizobium sp. YR681].
ACCESSION   WP_008139603
VERSION     WP_008139603.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. YR681
  ORGANISM  Bradyrhizobium sp. YR681
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 322)
  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 322)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 322)
  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   4  (residues 1 to 322)
  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 322)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Bradyrhizobium sp. YR681"
                     /db_xref="taxon:1144344"
     Protein         1..322
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35541
     Region          <110..313
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          230..311
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mpvrwlkpsr vlsvehysdf esfrpsevlg ggtstplepr qfslhrailp lrdglfvlqr
       61 tfarrlqanv gtdhgvglvi plachstang reidnsmigv vrgkvateav ehhpntylml
      121 rfnsdmrhrg wadyetglef trldddamar lratildmfc lasqcndprq feaidrpiqe
      181 rllatlddal apvdaqdlrr gsfdkhrklv aqldeaaals gssplysgdl analgvsvrt
      241 lqsatqavhg vslhhhlrlk rlwstrtqlm tggngmtvka aalangfwhm gefsklyktt
      301 fgempsgtla qardfadvsa hl
//
LOCUS       WP_008140746             468 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase, partial [Phocaeicola
            coprophilus].
ACCESSION   WP_008140746
VERSION     WP_008140746.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola coprophilus
  ORGANISM  Phocaeicola coprophilus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Phocaeicola coprophilus"
                     /db_xref="taxon:387090"
     Protein         1..>468
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
     Region          38..449
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mnsndranli krintleglt dkersallgl lrenktyglv wedkpedvee rlrnelpilt
       61 evperaivse dkdapnhili egdnlealat laythegkid viyidppynt gnkdfiynds
      121 yvdkedsyrh skwlsfmsrr lkiakkllse rgmifmsidd neqaqlkllc devfgqenfv
      181 asilwqkihs ikndakylsv nhdfilmyak dinfininll krtetmnsry knpdndprgp
      241 wqsgdlvane trtngnydvv gptgklfnvp egkhwvysee nmmqliqekr iwfgkngtsf
      301 prkkrylsev qqgrtpdtww tsdevghnqe garelkslld dkllfsypkp srlisrilqi
      361 ssleysiild ffagsgttlh atmqlnaedg ghrqcilvtn nenniceevt yernrrviqg
      421 ytnakgeevv gasknnlryy rtgfvgrnrs mqnmrklvnl atdmlcik
//
LOCUS       WP_008142004             221 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Bradyrhizobium sp.
            YR681].
ACCESSION   WP_008142004
VERSION     WP_008142004.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. YR681
  ORGANISM  Bradyrhizobium sp. YR681
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 221)
  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 221)
  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   3  (residues 1 to 221)
  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   4  (residues 1 to 221)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 221)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 221)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Bradyrhizobium sp. YR681"
                     /db_xref="taxon:1144344"
     Protein         1..221
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=24402
     Region          10..203
                     /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"
ORIGIN      
        1 mssrllqnfk ggraivvtrr gewestlett laklgvstey peivdgraqi daaslqadrd
       61 ilfvdgdleg avaieinpas rlppapvigl vgveapsrlk alvnlgatsf lrkpvhggav
      121 ytslfmginq fllraemfer lqdleerrrg rravvravil lmqqdgfdee gaysrlrres
      181 mrarqnmely ceeflnkrak ppdttgrttg imlqggdkqa i
//
LOCUS       WP_008142145             404 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Phocaeicola coprophilus].
ACCESSION   WP_008142145
VERSION     WP_008142145.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola coprophilus
  ORGANISM  Phocaeicola coprophilus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Phocaeicola coprophilus"
                     /db_xref="taxon:387090"
     Protein         1..404
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=45398
     Region          1..283
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          281..377
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkilhtsdwh lghalynydr seeqicflnq ltgivqeeqp dvmvvsgdiy hystpsaatq
       61 kmytdgllri hqacpsmtiv vtagnhdsss kleidsnlwd hfrvkvighi ercgsavnwe
      121 kqiiaipgqd gnpvgyvaam phvypqnfpi lsddtpreer qsrffqalld etgkqntqql
      181 pvvlmahlsv egsdrtgqdd saggmefisl stlgkgydyl alghihcpqt lkgsenhary
      241 cgtplpvsfd etyphsvtiv qirhqgeqpe ittrsirnpw plltlpatpv pfdealkale
      301 aypdheqtyi rlnvlirdyl apdcnekasa atrgkacrfc yikctreqqe qatpetalti
      361 qevkemspld iarryyreae geemdeelct lmqeviaqvh akdi
//
LOCUS       WP_008146628             404 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Parabacteroides johnsonii].
ACCESSION   WP_008146628
VERSION     WP_008146628.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides johnsonii
  ORGANISM  Parabacteroides johnsonii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 404)
  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 404)
  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
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 404)
  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   5  (residues 1 to 404)
  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   6  (residues 1 to 404)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 404)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 404)
  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 19786117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Parabacteroides johnsonii"
                     /db_xref="taxon:387661"
     Protein         1..404
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44435
     Region          20..>65
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
     Region          81..393
                     /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 mntnfllssd nnsrsellkk kiihyyiang datiadlgre mdlsiptvtk lvaelqedgy
       61 ildfgkqets ggrkpniygl npasgyfvgv dmlkdklnia aidfkgdkvq leenipyqle
      121 ntpasleqfc kiiddfivsl pvernkilai gvnitgrvnp asgysysify feekplaqil
      181 eerlqakvfi endsramtyg eymkgvvqge knilfvnmaw glglgiiidg nlyygksgfs
      241 gelghfcmfe nevlchcgkk gcleteasgs afhrilmery rkgsntilag kldsgeeisl
      301 gdlleavrke dvlcidilek mgvnlgkgia glmnifnpel vilggtlsla geyislpiks
      361 airkyslnlv nqdteikisk lgeragsfga cllsrskllg mihy
//
LOCUS       WP_008146767             675 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Parabacteroides johnsonii].
ACCESSION   WP_008146767
VERSION     WP_008146767.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides johnsonii
  ORGANISM  Parabacteroides johnsonii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 675)
  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   2  (residues 1 to 675)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..675
                     /organism="Parabacteroides johnsonii"
                     /db_xref="taxon:387661"
     Protein         1..675
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=79444
     Region          55..120
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkrmfinllv yllissyqlk sqtlysvdkw meyieemase tedeerieal ytdlsylveh
       61 pfelntvteg elkrlpflsd lqirelleyr srygkmltly elknveafdl etislfipfv
      121 yigeiivdkr pitvknllkr stnnlqiryd rcfqqkkgyr sypdsmlqqy pnrkylgepf
      181 yhsvrysyaf deriqfglva ekdagepfwn eyhkgydyys mhlflkdmnk wlkslaigdy
      241 kisfgqglvi sndfspsrna lvsqaerrtn gfrrhfstne ndffqgaaat vnwknldisl
      301 fysyrkldgs vdstivtsfk tdglhrlvrd rekmrkvamq tyggniryat pdlcigltal
      361 sysfgnysiq pdpkpynlfy frgnrnlnis vdyllknrwi kfygetamsr ngtvaslnal
      421 qltpasyfsl lllyryydkr yqaffgnafs qnsavqneqg vymgmqwtpf srwklsayad
      481 ifrfpwlkyg vdapstgkey mlqldytpsr nlsvyvryky kqkediepyf qqrlrmqvly
      541 aisssvslrt sadgicytet skkskgwmit qsvgwksvdi pvqtdfyvag fhtdnyrtri
      601 fsyeknilya fnmpsfygkg vrlalsfrwd ivkqlsfsak fgytyyadrd vigtdleeie
      661 ghmkadvyts lrwkf
//
LOCUS       WP_008147347             470 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein, partial
            [Parabacteroides johnsonii].
ACCESSION   WP_008147347
VERSION     WP_008147347.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides johnsonii
  ORGANISM  Parabacteroides johnsonii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 470)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Parabacteroides johnsonii"
                     /db_xref="taxon:387661"
     Protein         <1..470
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          386..465
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 clhdelkkad yvklllqkak acgnkemesi alfnmgkmiy yqedkkqgye lmneaielmk
       61 ntdykykydn lrynyntlli mqqrdnqyek alktldllee ivtkdmegtt digsltdkek
      121 ktmyaqrali lsrlgrmqea deayrawlai gdtyskddyl iipylmdrkl ydkviemnka
      181 hedflythnd tvtyhmrtik rslgdayekk keykeaakyf kdlailidsl kvreqkssal
      241 elakiyethe kdmqikeqka kleeqhiilv ailgvlflag lafylvirhl raikrknrfl
      301 arqidsqlay reelhkanee ikqllkqqhe pslpiasgkq tqsrekeedy gdirtsaedk
      361 klfeeldrlv eedklfldpn isrelllnql hiskntfaql iqaysgtnfs gyinnkrldy
      421 sihllkdykr ytieavatds gfsnvrsfyr ifrekygmtp seyrntfeke
//
LOCUS       WP_008147264             277 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Parabacteroides johnsonii].
ACCESSION   WP_008147264
VERSION     WP_008147264.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides johnsonii
  ORGANISM  Parabacteroides johnsonii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 277)
  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 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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Parabacteroides johnsonii"
                     /db_xref="taxon:387661"
     Protein         1..277
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32409
     Region          23..276
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          196..275
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mevlrttaed pffvgtincs dmphhlfkle daciffchsg earieidlle ydimpntqii
       61 flpnsiinys yaspdlsisy itfsnaffqe atvrldpsff hflkenpvvt lpvertrtin
      121 gliialedly kdkencfrlq ilrnyiqsfl ldiydkthri feqnrpegis rqeelfkrfi
      181 qlihkhclnq revsfyaqkm fitprylsai aqtvagetak niidkhvile ikvllestdl
      241 siqeianrlq fpdqsffgry fkkhtgispq yyrrklg
//
LOCUS       WP_008148493             157 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Parabacteroides johnsonii].
ACCESSION   WP_008148493
VERSION     WP_008148493.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides johnsonii
  ORGANISM  Parabacteroides johnsonii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Parabacteroides johnsonii"
                     /db_xref="taxon:387661"
     Protein         1..157
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17231
     Region          8..153
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 maenliingg nkrelyetll pqlqsltage tdiianmanv aaalkqtfdf fwvgfyivke
       61 emlvlapfqg plactriryg kgvcgtawke artiivpdve qfpghiacss asrseivvpv
      121 irdgkvvavl didsdklsef dkmdaeyleq lcaflpm
//
LOCUS       WP_008148755             111 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Pseudomonas sp. GM41(2012)].
ACCESSION   WP_008148755
VERSION     WP_008148755.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM41(2012)
  ORGANISM  Pseudomonas sp. GM41(2012)
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (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   2  (residues 1 to 111)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Pseudomonas sp. GM41(2012)"
                     /db_xref="taxon:1144708"
     Protein         1..111
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11482
     Region          41..108
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mrtgyfyslv falltsasig aiaaptakpe ggnaplvlev spkaqsgkvd lnqadaptlq
       61 relsgvgeak akaivayreg ngpfasvdel levkgigkai ldknreklev n
//
LOCUS       WP_008150226             414 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Parabacteroides johnsonii].
ACCESSION   WP_008150226
VERSION     WP_008150226.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides johnsonii
  ORGANISM  Parabacteroides johnsonii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Parabacteroides johnsonii"
                     /db_xref="taxon:387661"
     Protein         1..414
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46606
     Region          4..284
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          284..393
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mslkiihtad whlgqtffgy drddeheafl swltdllvqr qtdvlliagd vfdvanpsaa
       61 aqrrffrflr eanrrnphlq ivviagnhds aarleapipl leelntsivg ivprtdlcki
      121 dfdslliply nkegkrealc lavpylrqgd ypaseerkdt yvegvtrmyr glydyadsqr
      181 qpgevllamg hlhatgaels eddrsertim gglesisvea fnedlaytal ghihkaqrvg
      241 grehvryags plpmsfseqh yhhqvvaftl kngclsdlea vpiplrtalh ripaepalpa
      301 evllqlsdlp laeegadrsl wpylevqvll tepdpgfrhr veevladkav rltsiipsyp
      361 kkegeedsrp lsytdlqkia pldmlrhtft nrfggdlpee lekmfndvir evsl
//
LOCUS       WP_008150467             803 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pseudomonas sp. GM41(2012)].
ACCESSION   WP_008150467
VERSION     WP_008150467.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM41(2012)
  ORGANISM  Pseudomonas sp. GM41(2012)
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 803)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 803)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 803)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="Pseudomonas sp. GM41(2012)"
                     /db_xref="taxon:1144708"
     Protein         1..803
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=88713
     Region          18..800
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkrsltvlal livalaagag wyvyskqptr qgmvelqhlq gsvtvryder giphiraene
       61 tdlyralgyv haqdrlfqme alrrlargel aevlgpklld tdklmrslri reradtylan
      121 mdkqspafia mqayldginq yqdshpkpae fdvlgipkrp ftaqdtisit gymaysfaaa
      181 frteplltyv rdqlganyln vfdldwqpkg vlaknrsaam pplastdwkd lnalarlseq
      241 aladnglpqf egsnawavsg shtksgkpll agdphirfsa psvwyeaqls apgfelyghy
      301 qalmpfaslg mnrdfgwsit mfqnddldli aekvnpdnsn qvwyrgkwvd mvtseqqiav
      361 kgqapvtlvl rqsphgpivn dalgsgvgkt piamwwgfle sqnpilegfy qlnradtqak
      421 arsasakvqa pglnivwana kgdigwwaaa qlpkrpagvr pgfildgsta dadkegfypf
      481 sanpqeenpa rgyivsanfq pvtptgmeip gyynladrgq qlnrqlsdkt ikwdldasqk
      541 lqlgtttayg prllapllpv lrevvsdpae lklveqlaqw kgdypldsts atlfnqflfn
      601 ladatmhdel gndffetlls trvidsalpr laatadspww dnrntlgket radtvkvawq
      661 asiahlkttl ggdfaqwqwg kahtlthghp lgqqkpldri fnvgpfaapg thevpnnlsa
      721 rigpapwpvt ygpstrrlid fadpthsltv npvgqsgvpf dshyddqsea yiegiyyqah
      781 lndeevtant rstlkllpar sgq
//
LOCUS       WP_008151324             234 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Pseudomonas sp. GM41(2012)].
ACCESSION   WP_008151324
VERSION     WP_008151324.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM41(2012)
  ORGANISM  Pseudomonas sp. GM41(2012)
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 234)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Pseudomonas sp. GM41(2012)"
                     /db_xref="taxon:1144708"
     Protein         1..234
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=25127
     Region          37..204
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 maldrfgflf tallltsvsv paayadslea allkaapgan akviglavra tqcslaqgka
       61 pvqrlavidy slpsteqrlw vfdlkkrkll fhelvahgrn sgenmavkfs nqnesfatsl
      121 glyrtqssyv gqngyslrme glepgfndna yeraivihga pyvspvlara ngrigrslgc
      181 pavrpaiahk lidsmkdgql lfsyypdqrw lksssyincg ggtvaaastp gtrq
//
LOCUS       WP_008152152             208 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Parabacteroides johnsonii].
ACCESSION   WP_008152152
VERSION     WP_008152152.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides johnsonii
  ORGANISM  Parabacteroides johnsonii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Parabacteroides johnsonii"
                     /db_xref="taxon:387661"
     Protein         1..208
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23566
     Region          3..190
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdfyevlekr rtyrdfsdre vsdeilkrvi gaafkaptnd hlrqlefvvv rgreniakii
       61 aplaknmaaf kelvaevdes ddedkmamfa dalpkqqrml iqsgllvipf frqltwpllk
      121 pveqsslnyf asawcalenm llaataeglg tvfhipvade aekikqivna pedyeftcll
      181 tmgypaenaf lpkqkvidve srihtgiw
//
LOCUS       WP_008152242             825 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas sp. GM41(2012)].
ACCESSION   WP_008152242
VERSION     WP_008152242.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM41(2012)
  ORGANISM  Pseudomonas sp. GM41(2012)
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Pseudomonas sp. GM41(2012)"
                     /db_xref="taxon:1144708"
     Protein         1..825
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89310
     Region          66..114
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          93..825
                     /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 mrpqtrrtpl alavqrptlh rtlftsvllt atllgssman aapvkvniag qslsnaltel
       61 gmqtnlqily spdqvagiks ravsgsleps dalkallqgt gisfqingns vtlvsgggss
      121 lqlgattisg qalglttedt gsyttgattt atklpltlre tpqsvtvvtr qqmddrgats
      181 vgdvlrntpg vtaqkydsdr tefsargfai tnfqydginl pydgvygenp nnsddaasld
      241 rvevikgatg lmtgsgdpsa tvnlvrkkpt kefkasvsat agywdnyrte gdisgslnds
      301 gsvrgrfvga lqdkgsyidh ysqkkdlfyg ileadltddt lltlgvdkss atprgsswtg
      361 nspyftdggr tdfsrsfnpg adwsrrdfds vtyfssleqa landwkfkas fdqkttdhdt
      421 qlasasggya dratgegnyl ywgrweghrv qntadvnvsg pftlggrehe lvagfmashs
      481 rqtgstydts afelvpgsiy dwngslpkqd fpkngkyert qsqnglylat rlrptddlsf
      541 ilgsrlstfk ynedysyypg gtltdthasy kehgvvtpya gvvydlndty svygsytkiy
      601 qpqinkding stlapvegds yetglkaayf egklnaslaf frieqdnvaq svgtdlntgd
      661 gifkatdgat tngvelelag elaqdwnvsa gytyartrdk deqrifgfpl atskpehvir
      721 tfttyrlpga ldqftvgggi swqsafygqs yspnvgggeg gstmlkqggy tlvdlmtryq
      781 ydehlsftan annvfdkryl tglgnfgttf ygeprnlqit akydf
//
LOCUS       WP_008152819              98 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Parabacteroides johnsonii].
ACCESSION   WP_008152819
VERSION     WP_008152819.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides johnsonii
  ORGANISM  Parabacteroides johnsonii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Parabacteroides johnsonii"
                     /db_xref="taxon:387661"
     Protein         1..98
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11264
     Region          3..97
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mkttteyiel irscsqklvq dfgvrslkif gsvarnqqhk dsdidvciet etpnpflild
       61 lkeflerllg cpvdiirlhr nmnpflkeqi dkdgiyvl
//
LOCUS       WP_008153365             460 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase, partial [Parabacteroides johnsonii].
ACCESSION   WP_008153365
VERSION     WP_008153365.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides johnsonii
  ORGANISM  Parabacteroides johnsonii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Parabacteroides johnsonii"
                     /db_xref="taxon:387661"
     Protein         <1..460
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
     Region          36..449
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 geemnggisl ndmekalvcl lmtsmeapvq aesagltqem fadaslgfvy gvimkiyatg
       61 vrpdmvlver gmreadeeqa arlgglsfll pymlnvrhdg nvaayvegik kqyklrclvt
      121 lfgtmafkag kvssvpeela geaerllmqf rqetaegtpv rtigelaaea vtwhhrrlsg
      181 eleaeqvksg laefdyvtgg fhnteltiia grpsdgktav tlqmalnaar agksvcffsl
      241 emsslqmlnr vlagmtdvnp dhlrinkptg revehleeaa lrlkdlpfyl dytvgatveq
      301 irakvllqcr qgkcdlvvvd ylhllggdrr kgetqeqmvg rniralkqla ldsncpvltv
      361 sqmnracear adkaylpvms dlrdsgtieq vadcvafiyr perygftrdd ktghslvgvg
      421 kiyiaknrng stgiarfryn psftritdyi qpgtqtslgi
//
LOCUS       WP_008154912             131 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [unclassified Pseudomonas].
ACCESSION   WP_008154912
VERSION     WP_008154912.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..131
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14231
     Region          1..129
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mrrsnrgftl ieimiviaii givitigyps lteyvnkgrr tevagllseq aqilerfysk
       61 nnvytnatgl sagndfytit ptltdqtfll tavrkpgkam aadkcgdfti tntgvrsmvn
      121 ataatkdcwg r
//
LOCUS       WP_008155472             414 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Parabacteroides johnsonii].
ACCESSION   WP_008155472
VERSION     WP_008155472.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides johnsonii
  ORGANISM  Parabacteroides johnsonii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Parabacteroides johnsonii"
                     /db_xref="taxon:387661"
     Protein         1..414
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46580
     Region          4..284
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          284..393
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mslkiihtad whlgqtffgy drddeheafl swltdllvqr qtdvlliagd vfdvanpsaa
       61 aqrrffrflr eanrrnphlq ivviagnhds aarleapipl leelntsivg ivprtdlcki
      121 dfdsllvply nkegkrealc lavpylrqgd ypaseerkdt yvegvtrmyr glydyadsqr
      181 qlgeallamg hlhatgaels eddrsertim gglesisvea fnedlaytal ghihkaqrvg
      241 grehvryags plpmsfseqh yhhqvvaftl kngclsdlea vpiplrtalh ripaepalpa
      301 evllqlsdlp laeegadrsl wpylevqvll tepdpgfrhr veevladkav rltsiipsyp
      361 kkegeedsrp lsytdlqkia pldmlrhtft nrfggdlpee lekmfndvir evsl
//
LOCUS       WP_008155686             209 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Parabacteroides johnsonii].
ACCESSION   WP_008155686
VERSION     WP_008155686.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides johnsonii
  ORGANISM  Parabacteroides johnsonii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Parabacteroides johnsonii"
                     /db_xref="taxon:387661"
     Protein         1..209
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23877
     Region          3..191
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdfyqvlekr rtirdfsdke vteevlekvl stafkaptnd hlrqfefvvv rgqeniarli
       61 slvaentqki qqagleaaas tmdkdeytmf vdalpkqqrm lmqsnclvlp ffrqkdcplc
      121 ypadqsslny fasawcaven illaataegl scafripign epehvkhlvh apeeyeftcf
      181 laigyaaena hickqkeirv mdrihrnvw
//
LOCUS       WP_008155817             749 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Pseudomonas sp. GM41(2012)].
ACCESSION   WP_008155817
VERSION     WP_008155817.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM41(2012)
  ORGANISM  Pseudomonas sp. GM41(2012)
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 749)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 749)
  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   3  (residues 1 to 749)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Pseudomonas sp. GM41(2012)"
                     /db_xref="taxon:1144708"
     Protein         1..749
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79383
     Region          6..748
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msfgadeeil qdflveagei leqlseqlve lesrpddadl lnaifrgfht vkggagflql
       61 nelvecchia envfdilrkg errvdselmd vvlealdavn gmftevrers pitaatpell
      121 aalarlaepq tadetapvae aveepaaese sgditdnefe qlldslnavk aqaeapaavp
      181 apssnaagsd eitdaefesl ldqlhgkgqf avdavapapa apaapkaagd ssditddefe
      241 alldqlhgkg nfavdalesa iaavpapaap takaaggdli sdhefeslld elhgkgkfte
      301 vgtasgasap vaapvakava pkpvakapep kaeapkpapa aapaparaas apppekpase
      361 aettvrvdta rldeimnmvg elvlvrnrlv rlglnsgdea mskavsnldv vtadlqtavm
      421 ktrmqpikkv fgrfprlvrd larqlkkein lelvgeetdl dknlvealad plvhlvrnsv
      481 dhgieepaer eamgkprsgk vilsaeqegd hillsisddg kgmdadvlrg iavkkglmdk
      541 daadrlsesd cfnlifapgf stkteisdvs grgvgmdvvk tkiaqlngti niystkgkgs
      601 kivikvpltl aimptlmvml gnqafafplv nvneifhldl sttnvvdgqe vvivrdkalp
      661 lfylkrwlvs saaheeqreg hvvilsvgtq rigfvvdqlv gqeevvikpl gkmlqgtpgm
      721 sgatitgdgr ialildvpsm lkryaarri
//
LOCUS       WP_008156046             309 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. GM41(2012)].
ACCESSION   WP_008156046
VERSION     WP_008156046.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GM41(2012)
  ORGANISM  Pseudomonas sp. GM41(2012)
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 309)
  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 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   3  (residues 1 to 309)
  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   4  (residues 1 to 309)
  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 309)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Pseudomonas sp. GM41(2012)"
                     /db_xref="taxon:1144708"
     Protein         1..309
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34488
     Region          39..191
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          219..298
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mssldhfqap ldadmekqra elaaiirhnt aedgtyatav gslfmsrhsq shefapvlaq
       61 palcimaqgr kevrladeyf nydplnylvv svsmplsgrv vnvtseepil avrldidpae
      121 isaliadagp lgvptrptgr glyveridta mldavlrlar lldtpkdiam laplirreil
      181 yrllrsqqgh rlyeiaians qshrisqaik wlngnyeqpl riddlakevn lsvstlhhrf
      241 kamtamsplq yqkqlrlqea rrlmlaegle asaagyrvgy espsqfsrey srlfgapplr
      301 dlarlrlsv
//
LOCUS       WP_008155940             256 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Parabacteroides johnsonii].
ACCESSION   WP_008155940
VERSION     WP_008155940.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides johnsonii
  ORGANISM  Parabacteroides johnsonii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 256)
  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   2  (residues 1 to 256)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Parabacteroides johnsonii"
                     /db_xref="taxon:387661"
     Protein         1..256
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29472
     Region          118..181
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mnwrdllyfs kgerraltll lclvtiswil llwtdtkrmp iesqtdahrt enqqasgerr
       61 iitgkntsek etssirkesv phpnktknal tdknailidn apystskkrk gytpytqtek
      121 yapgtlveln tadttilkkv pgigstfarr iikyrellgg fydvsqlaev ygideeryqa
      181 lalwfiadtl hirrlevnal saatlrkhpy ldyrqakaie qlrkqksrls gwenlqliee
      241 ftdtdkkrlt pylsfk
//
LOCUS       WP_008156061             675 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Parabacteroides johnsonii].
ACCESSION   WP_008156061
VERSION     WP_008156061.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides johnsonii
  ORGANISM  Parabacteroides johnsonii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 675)
  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   2  (residues 1 to 675)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..675
                     /organism="Parabacteroides johnsonii"
                     /db_xref="taxon:387661"
     Protein         1..675
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=79322
     Region          55..120
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkrmfinllv yllissyqlk sqtlysvdkw meyieemase tedeerieal ytdlsylveh
       61 pfelntvteg elkrlpflsd lqirelleyr srygkmltly elknveafdl etislfipfv
      121 yigeiivdkr pitvknllkr stnnlqiryd rcfqqkkgyr sypdsmlqqy pnrkylgepf
      181 yhsvrysyaf deriqfglva ekdagepfwn eyhkgydyys ihlflkdmnk wlkslaigdy
      241 kisfgqglvi sndfspsrna lvsqaerrtn gfrrhfstne ndffqgaaat vnwknldisl
      301 fysyrkldgs vdstivtsfk tdglhrlvrd rekmckvamq tyggniryat pdlcigltal
      361 sysfgnysiq pdpkpynlfy frgnrnlnis vdyllknrwi kfygetamsr ngavaslnal
      421 qltpasyfsl lllyryydkr yqaffgnafs qnsavqneqg vymgmqwtpf srwklsayad
      481 ifrfpwlkyg vdvpstgkey mlqldytpsr nlsvyvryky kqkediepyf qqrlrmqaly
      541 aisssvslrt sadgicytet sekskgwmit qsvgwkpvdi pvqtdfyvag fhtdnyrtri
      601 fsyeknilya fntpsfygkg vrlalsfrwd ivkqlslsak fgytyyadrd migtdleeie
      661 ghmkadvyts lrwkf
//
LOCUS       WP_008156180             404 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Parabacteroides johnsonii].
ACCESSION   WP_008156180
VERSION     WP_008156180.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides johnsonii
  ORGANISM  Parabacteroides johnsonii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 404)
  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 404)
  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
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 404)
  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   5  (residues 1 to 404)
  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   6  (residues 1 to 404)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 404)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 404)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Parabacteroides johnsonii"
                     /db_xref="taxon:387661"
     Protein         1..404
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44463
     Region          18..61
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Site            order(33,36,85)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
     Region          81..393
                     /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 mntkfllssd nnnrsellkk kiihyyiang datiadlgre mdlsiptvtk lvaelqddgy
       61 ildfgkqets ggrkpniygl npasgyfvgv dmlkdklnia aidfkgdkvq leenipyqle
      121 ntpasleqfc kiiddfivsl pvernkilai gvnitgrvnp asgysysify feekplaqil
      181 eerlqakvfi endsramtyg eymkgvvqge knilfvnmaw glglgiiidg nlyygksgfs
      241 gelghfcmfe nevlchcgkk gcleteasgs afhrilmery regsntilag kldsgeeisl
      301 gdlleavrke dvlcidilek mgvnlgkgia glmnifnpel vilggtlsla geyislpiks
      361 airkyslnlv nqdteikisk lgeragsfga cllsrskllg mihy
//
LOCUS       WP_008156230             495 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Parabacteroides johnsonii].
ACCESSION   WP_008156230
VERSION     WP_008156230.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides johnsonii
  ORGANISM  Parabacteroides johnsonii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Parabacteroides johnsonii"
                     /db_xref="taxon:387661"
     Protein         1..495
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=53675
     Region          3..495
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mrtyiqinpa dnvivavkdl qagaslding ktivvlqdip aghkvalqdf kegdyiikyg
       61 apigharkai tagswvnekn iktnleglre yefnpqptpe qssgkplsfk gyrrkngevg
      121 irneiwvipt vgcvngithr ltdrlqqetq gagvdaivaf phnygcsqlg ddhentrkil
      181 rdmvlhpnag avlvvglgce nnqvgafrei lgdydterir fmetqkvdde letgmallre
      241 lyaiasqdqr tdiplnelrv glkcggsdgf sgitanpllg vfsdflvaqg gttvltevpe
      301 mfgaetilmn rseskavfek tvhlindfks yfienkqpiy enpspgnkag gistleeksl
      361 gctqkagtsa vrdvmlygeq lktkglnlls apgndlvast alassgchlv lfttgrgtpf
      421 gtfvptvkvs tnsnlnarkp nwidfnagsl legksmeelc ecfiqfiigi asgnptnnek
      481 ngyreiaifk sgvtl
//
LOCUS       WP_008162448             825 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Achromobacter arsenitoxydans].
ACCESSION   WP_008162448
VERSION     WP_008162448.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter arsenitoxydans
  ORGANISM  Achromobacter arsenitoxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Achromobacter arsenitoxydans"
                     /db_xref="taxon:1147684"
     Protein         1..825
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90028
     Region          74..125
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          101..825
                     /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 mtlartsrta rltpvptvls tvlsgllcga algfvapdvq aqgavaaqda eytfvieagp
       61 ldqalnqfar aagvnvsfda aqvsglrseg lqgrwtirrg lsallartgf eavrlssggy
      121 avrpqpggga tllepvtvtg qeyrlmtegt gsyttsavti gkgeqqlrdi pqsvsvvtrq
      181 rldeqnltsv ydalenttgv tlqqspqggk yiysrgfnns viqydgvple rsmygrasny
      241 sggtafydrv evlrgaagll qgsgspggav nlvrkrplqe drvmveatag swdrygmqvd
      301 gsallnedgs lrgralidrq ddrsfvdrvd mknttvyatl eydfsprtqv nlgysyedlr
      361 grpsisglpr ysngeevgfk rstsfganwn rqetsnqgfy adfthafndd wrfkmtgayv
      421 qesqylkyta ssravnpatq matvsvartv adidtsgvda nltgkfrafg rthdvvvgan
      481 yghskidtsy aylvnyatfn afnfnpdlpe pstaairagt devrigsnre lgfygttrlq
      541 ladplklvlg grfsrsnriw ttdtttagql vngqtkqant hftpyaglmf dlspqwttyv
      601 sytdifqpqs evnaageslk pivgesyelg lkgelldgri ntafalfrin qnnraqvdfn
      661 tsptcaagyf cytdagkvrs qgfdaeisge ltrgwnlyag ytfnttkylk dqdsegqafa
      721 wytpkhifrl wttyqlpgdw saftvgggvn aqsgqsrqig attvhasgra vwsayakyqi
      781 nrnwattvnv nnlfdktyys avgnlvngih ygdprnvmlt lrgtf
//
LOCUS       WP_008163427             429 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Achromobacter
            arsenitoxydans].
ACCESSION   WP_008163427
VERSION     WP_008163427.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter arsenitoxydans
  ORGANISM  Achromobacter arsenitoxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Achromobacter arsenitoxydans"
                     /db_xref="taxon:1147684"
     Protein         1..429
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47318
     Region          4..421
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 megelfvyvd iqgeavlagv ltlddtdedr fyaeftyvqs yvndprafsl dplnlpltda
       61 rttfrtesry qtlgaifdaa pdawgrnvmr vdnagarvte nevllkgrgm gvgalffsar
      121 pltpnmrkty rlpevsqves lgglladidq gikpkglyrd ilgsswdigg arpktivrdg
      181 ngemwiakfp rkgdsydrqr veyanlqmar aiglnvpais lantplgavl lthrfdrill
      241 paesgadpvi arrhflsgas lispsvqigk reldgprgka tysyarladv trrissrpvq
      301 dllelyarmi lnvavhntdd hlknvgflkd dgaetyrlsp lfdvvtqegs akhylhigsg
      361 gressfancl seyrrfglrs eaaatsildr vldvvrdrrr yyeaagmape eialvestlt
      421 alrqpsaqa
//
LOCUS       WP_008164458             642 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Achromobacter arsenitoxydans].
ACCESSION   WP_008164458
VERSION     WP_008164458.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter arsenitoxydans
  ORGANISM  Achromobacter arsenitoxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 642)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 642)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 642)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 642)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 642)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Achromobacter arsenitoxydans"
                     /db_xref="taxon:1147684"
     Protein         1..642
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=70122
     Region          12..642
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msqgtasvps sstspaggmh apssraalil galgvvygdi gtsplytlra cltglsvhtd
       61 lepahllgvl silfwmlmvv vslkyvtlvl radnrgeggt lallelavra regklrwvli
      121 vlgifgaalf ygdsmitpai svlsalegig ivshtldawv vpialvvlia lfaiqshgtg
      181 amgklfgpvm llwfstlaal gawqiwltpe vlaalnpmwg lrfivefpwi sfvllgavvl
      241 altgaealya dmghfgrpai rgawfsmvlp altlcyfgqg alllrdptai rnpfflmape
      301 wglaplvala tiativasqa visgaysvtr qavqlgfwpr mqilhtsave kgqiylpqvn
      361 alllcavlvl vlwfrnsdnl aaaygfavtg tmlttsvlaf avlprgstgi krvmwflvlg
      421 llllldvllf sanvfkiheg gwlplavaiv vftlmmtwrr grrllsdmqq rdrqplkefm
      481 eqleeyppsr vpgtaifmtm nsgnvppall hnlkhnkvlh dhvlfltilv advpyvspee
      541 rfqvdklsas swaatvnygf kedpdvpeal rlvaeaypel dlepmrtsff lsrqtvvaak
      601 kpalwrwrra lfsfmarnst rstkffkipa nrvvemgmqv el
//
LOCUS       WP_008165052             212 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Achromobacter arsenitoxydans].
ACCESSION   WP_008165052
VERSION     WP_008165052.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter arsenitoxydans
  ORGANISM  Achromobacter arsenitoxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 212)
  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 212)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 212)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Achromobacter arsenitoxydans"
                     /db_xref="taxon:1147684"
     Protein         1..212
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22731
     Region          1..209
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 maydleeqek ldaikawwar ygtlvftlvt vvllawggww gwkayeshra nqamgyfeal
       61 edaarlggad ssvriktaaa tlrekypatg yaargalvaa qalqaqkdda gareqlewla
      121 gqgknpsmqa varlrlagll ldqkqydaal aqltnppaaf aalfadrrgd vlaaqgkree
      181 araawqsaid glgtanpltq vvqlkldals ga
//
LOCUS       WP_008165313             298 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudoalteromonas sp.
            BSi20652].
ACCESSION   WP_008165313
VERSION     WP_008165313.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. BSi20652
  ORGANISM  Pseudoalteromonas sp. BSi20652
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 298)
  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 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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Pseudoalteromonas sp. BSi20652"
                     /db_xref="taxon:388384"
     Protein         1..298
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32684
     Region          28..181
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          210..291
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mptianmlqq yaehsqllsf egtmetiipg vyfhratkss prqpliynsg iiivgqghki
       61 ihfpehqiky gagdylvlgv pvpleceaft dnglpvmgia idinpamlhk lvnqmilhkp
      121 lctsssssqt ggvqsatldt amehvthrll tvlnnpleae vfgedivkel vyrvlcgpqg
      181 dtliglamhd ghyariartl stmhssyanq itveglaedv nmsvssfhra fkqvtfespl
      241 qylkkvrlak akelitasgs kaneaalkvg ytsasqfsre fkrhfnktps evltqlhs
//
LOCUS       WP_008165874             304 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Achromobacter arsenitoxydans].
ACCESSION   WP_008165874
VERSION     WP_008165874.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter arsenitoxydans
  ORGANISM  Achromobacter arsenitoxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Achromobacter arsenitoxydans"
                     /db_xref="taxon:1147684"
     Protein         1..304
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=32734
     Region          24..255
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mttsetcrnp vvsdaeiaam vtgrdglrvl lqpqvdlltg rivsaealar wqhprlgivm
       61 psefvpavnr lgldgilfer vcvrvidall tlrragvavp lainapattl seaksvdfll
      121 ervraaelpp slvrvelted qpirdldvlr asllrledag cevslddfgt ghaslkllsa
      181 iplsevkidq yfvarmrrsa vafevlrsaa elatrlgwrv vaegvenvad ipalraagcr
      241 ygqgfslgrp mpldeimirl rtqrdggepl aapaayassw ldafdggsqd gaepgrslrh
      301 tail
//
LOCUS       WP_008166373             157 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Pseudoalteromonas sp. BSi20652].
ACCESSION   WP_008166373
VERSION     WP_008166373.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. BSi20652
  ORGANISM  Pseudoalteromonas sp. BSi20652
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Pseudoalteromonas sp. BSi20652"
                     /db_xref="taxon:388384"
     Protein         1..157
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=16711
     Region          1..133
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mrtkgftlie lmvvvsiigi laavalpqys ryiqkaelvd plamaavire dvtvyylenr
       61 rfpasneqag vpaseflign rvtgitvdng aihislgnka sqplqntvlt frpavvtgsp
      121 tspiawlcgf dkpvtgmqav genkttvpke ilpsaci
//
LOCUS       WP_008166216             796 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Achromobacter arsenitoxydans].
ACCESSION   WP_008166216
VERSION     WP_008166216.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter arsenitoxydans
  ORGANISM  Achromobacter arsenitoxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 796)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Achromobacter arsenitoxydans"
                     /db_xref="taxon:1147684"
     Protein         1..796
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87819
     Region          57..108
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          85..796
                     /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 mpstirlstp rlfrllplca alalapaaya qparatfeqa aaplesalnq yagtarvtls
       61 fdpaltagrq apalrgdysv ldgfaallag sglvaeqtga rhfvirpaaa pvstlspvtv
      121 tgesaaeryn pptaigsktp ltqrqipqsi svvtqermrq qamqtlddam rntagvtver
      181 rdnsrsifhs rgfdmtsyqi dgiptqydwr mlsssdlaiy drvevlkgpa glyngagglg
      241 gainlvhkrp qkdfgfegsv sagswdnyrs qvdltgglne dgslrgrlvg vyqdrrffyd
      301 ktneqhsvly galaydftpn ttltvggsrq erdihasmws ipafmtvgpg gqpsfsladi
      361 krstfigadw nrdqftstea yadlehrlan gwtaklsgry aenkldreqa ygwgpantsn
      421 nliqllsakg ptrqaqssyd ayadgpfqlf grehnltlga nytdsrfdna wdyptpnwap
      481 liditnprsd fdrldyafnn snhartkqwg iysnlrlrla dpltlvaggr fswwdltstq
      541 rtlageksqd akfngkftpn vgliydlnqt yslytsysei fspqngysta dgnmlkpleg
      601 rqveagikge yldgalnasf avfeirdqnr atlapdsttv ytangktrnr gfelqvngei
      661 rpgwnvyagy twlqarvdqs asydsnvtav aprhllrvwt dyrlpgewnr ytigggvnvq
      721 sgtyvafpqy ngarleqggy atvdlkfgyd isrnldvaln itnlfdrkyy atissprsqn
      781 ifgepqafml tlraky
//
LOCUS       WP_008166395             761 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pseudoalteromonas sp. BSi20652].
ACCESSION   WP_008166395
VERSION     WP_008166395.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. BSi20652
  ORGANISM  Pseudoalteromonas sp. BSi20652
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 761)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 761)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Pseudoalteromonas sp. BSi20652"
                     /db_xref="taxon:388384"
     Protein         1..761
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=84503
     Region          18..748
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 myklikrlll livilglast avvygvlsls lpaldgngrs navaepvkis rdalgqavin
       61 ansrndaayg lgyahgqdrf fqmdllrrna agelselfge aalgldkkmr fhqlrkrsha
      121 ilqtlpktdk qllksyaqgv neglaqvgys sfeylltgai qkpwqsedsl lvifsmyldl
      181 qsatferdqa liqieqaytk qmvdfltqps kyqaaldgsk lapynggipt lpiqtqqtvk
      241 sieanqergs nnwavtgalt ktgagmvsdd mhlsmavpvi wyraqlnymh sgeqtqvtgv
      301 slpgapaivv gtnnnvawgf tngyldtadw ialnddsktw qvdepialpd geienyslil
      361 seygpvkyin ekpyalswaa hqpyavnmql lkleqaktvd daltvasdvg ipvqnlmvvd
      421 sqgsaawknm ggiparktps elgvnaddys vlwqqteler pfvknpqsgr lwtgnsrvvs
      481 aedntrfgng gyalgarssq irdrlfekqt faesdfyalq ldnqarflmp whalllkqlk
      541 antaknqqyi talenwqqca cptsigytlv kryrdevini lfsniesqln kqqgtlkyvk
      601 rdlepavwql innkpdtwin pqfknwdaql rgafnqtitk lteqfgnnvq gwqwgkvnel
      661 viehpfakqm pllakllnmp taagfgdsfm pavqrrsfga sqrfiaqpgh lehailaipg
      721 gqsghplsef yragfddyve gnhtpllpqt lmhqivikpi k
//
LOCUS       WP_008166575             138 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Pseudoalteromonas sp. BSi20652].
ACCESSION   WP_008166575
VERSION     WP_008166575.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. BSi20652
  ORGANISM  Pseudoalteromonas sp. BSi20652
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Pseudoalteromonas sp. BSi20652"
                     /db_xref="taxon:388384"
     Protein         1..138
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14835
     Region          1..136
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mknkhgftli elmiavaivg ilasialpny teyvkrasra eaaaalldaa nkeeqyfvdn
       61 reyteaftdl glqdktengh felditvvdg ntftitakpi agavrgdadc telsvtdtgl
      121 knakgskgns didycwgr
//
LOCUS       WP_008167564             826 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Achromobacter arsenitoxydans].
ACCESSION   WP_008167564
VERSION     WP_008167564.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter arsenitoxydans
  ORGANISM  Achromobacter arsenitoxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 826)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 826)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 826)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..826
                     /organism="Achromobacter arsenitoxydans"
                     /db_xref="taxon:1147684"
     Protein         1..826
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89153
     Region          74..126
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          101..826
                     /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 matrqsssps alsspwmrpa plrlavhlal aalaplaapa aswaqsasag diafaispsp
       61 ldvalgqfgv aakvtvaasp eltrgvmtqg lsgrytaeqg laqllagtgl qavanangeg
      121 yrlrrapqna pgvstlapvt vlgqadsavt egsgsytsrf vtigkglqtl keipqsvtvv
      181 trqrmddqna ntldevlana tgmtlyrspm ggsyvysrgf rvdsyqfdgv nrafyypqad
      241 sftsntvild rveiirgatg lmqgagspsa avnlvrkrpl aenqvqmlas ggswnnyrad
      301 idatgplnes gtlrargvas yndreyfydg adsrsgvlyg alsydlgpat tltggvsyee
      361 lrstpffhgl physngddig lkrstslgqd wnrwngkqts vfaelahrfn kdwslrltgt
      421 stqesndsky aftegavnpq tglgpmlyag lfdlsthnka lnldvdgafe algrkhsvsf
      481 gasineltsk ndfalnrlnr avnvwnpdhh vpepsddwmr enayrsaatv vkmkqtgvyg
      541 vgrfsladpl tlvagarvsw yentsryrds geqysdpykd ngvvtpyggl iyafnpqwsg
      601 yvsyaqifep qnsldasgkv ldpivgknye vgikgelldg rvntsvalfr idqknraqqd
      661 lvgnctvgdi cylssgkvrs qgldaeisge vapgwqlfag ytfntlkfld dttvtttnfg
      721 rtvtpkhilr lwsdyrlpgn lsawslgagv nyqtgsytet rgvkvsqgsy avwnarvgyq
      781 inkhwsaaln vnnifdktyy qtigapgwgs fygdprnatl tvrgtf
//
LOCUS       WP_008167780             423 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Achromobacter
            arsenitoxydans].
ACCESSION   WP_008167780
VERSION     WP_008167780.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter arsenitoxydans
  ORGANISM  Achromobacter arsenitoxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 423)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 423)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Achromobacter arsenitoxydans"
                     /db_xref="taxon:1147684"
     Protein         1..423
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47278
     Region          16..420
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mtmigvyadw dglprpqrvg vlnsrrtrah etfefqydpa aladpvighl vldpkiflfd
       61 gpqyptapqd rfgvfadssp drwgrllmdr rlardirtgm raagtrlyet dyllgvhdly
      121 rvgalrykre degefldntv glaappfaei raleqasral eedpndeaqq gqdwlrmlia
      181 pggslggarp kasvadeqgh lyiakfpsar ddydvggwem vvnalavgcg lnvaaaeark
      241 faseyhcfmv rrfdrtdegr rlhfasamtm tghvdgddas tgvsylelae vlirygsrtn
      301 adlrelwsri vfnilvsntd dhlrnhgfil vpgagwrlse aydmnpvpfa dglklnitev
      361 dnaldlelar evaayfrldl headeiieef qaivsqwrtv arelglpare qermgeafra
      421 ang
//
LOCUS       WP_008167813              99 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Pseudoalteromonas sp. BSi20652].
ACCESSION   WP_008167813
VERSION     WP_008167813.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. BSi20652
  ORGANISM  Pseudoalteromonas sp. BSi20652
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Pseudoalteromonas sp. BSi20652"
                     /db_xref="taxon:388384"
     Protein         1..99
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=10814
     Region          18..99
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mvvgsainpn dvlsstgkve llffgqlker lkcsklslei tqplsiselk lklvsqyphw
       61 qpwleerell aalnqtmsss deivkagdel affppvtgg
//
LOCUS       WP_008168051             189 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Pseudoalteromonas sp. BSi20652].
ACCESSION   WP_008168051
VERSION     WP_008168051.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. BSi20652
  ORGANISM  Pseudoalteromonas sp. BSi20652
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Pseudoalteromonas sp. BSi20652"
                     /db_xref="taxon:388384"
     Protein         1..189
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21021
     Region          100..180
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 maikkefisa lfltvtalyi tgcststnka epaplapntv sistadlqal kktadewksa
       61 esevnhllql enqlaqlksr lktlnestnq akvesilksd qaffaiqvaa fknksklqtt
      121 laklklkape ffyatlivni epkvinnsti yrlklgaykn kaeaenhcya lkkqqincfi
      181 syyteqqpq
//
LOCUS       WP_008168298             694 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Achromobacter arsenitoxydans].
ACCESSION   WP_008168298
VERSION     WP_008168298.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter arsenitoxydans
  ORGANISM  Achromobacter arsenitoxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Achromobacter arsenitoxydans"
                     /db_xref="taxon:1147684"
     Protein         1..694
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72949
     Region          1..694
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mtqhldplln prsiamigas snpgriggmp lelltrfgyk ggiypvnpky qevfglrcwp
       61 eieavpepvd lavlaiaaad vtpmlrrcha kgiraaivya agfaeaggdg vrlqdeleaf
      121 vaesgmavag pncmgfanln tqahtafasv fktapaqegt gsvslltqsg nvcaavyaia
      181 rrlglpfshf intgneacld fsqyleylaa dpqteivlgy ieqlrdgerf vracrelerq
      241 gkllialkag atdkgaqavq shtsalagdr rvyaaafrql nvieatdfaq mahlaslatl
      301 rhrtagkrva vltmsgalga iladkfigag ldlpdlppdl qsvlrggipd ygmvgnpvdv
      361 tgnvvndpaf vrtvlqalat sdaidavvvy apgymldrma dalaeasrqh rrlfvaidtg
      421 laqsraalre aevavfedlg qavgalapyl lwcdarasrr lapaprldaa sapalpcnet
      481 darayvaafg lpqavsaaar saddavrdar tagypvalki lspdiahkte aggvalnlad
      541 deavrhahaq vtqaaaraqp daridgvmvq kmergvaeli vgatrdpvfg pvltvglggv
      601 lteiyqdtsh rllpvdedia lqmlrelkaf alldgyrgkp rgdlaaacrs ivavgnalla
      661 apahvaeiev npllikeagq gvavldalil patp
//
LOCUS       WP_008170224             192 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Pseudoalteromonas sp. BSi20652].
ACCESSION   WP_008170224
VERSION     WP_008170224.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. BSi20652
  ORGANISM  Pseudoalteromonas sp. BSi20652
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Pseudoalteromonas sp. BSi20652"
                     /db_xref="taxon:388384"
     Protein         1..192
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21583
     Region          3..162
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mklftklydm alvwakhrha erylaamsfa esvffpippd vmlapmslaq pkkawrfasf
       61 atvasvvggv vgyllgfwlf epvvepliaq mhwqekfdia lnwfknygvw vvflagfspi
      121 pykvftigag vlqmaflpfl lasaigrgar fflvsalmkw ggvnmekklr qyieilgwgl
      181 vvliavayil lr
//
LOCUS       WP_008170229             157 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Marinobacter manganoxydans].
ACCESSION   WP_008170229
VERSION     WP_008170229.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter manganoxydans
  ORGANISM  Marinobacter manganoxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Marinobacter manganoxydans"
                     /db_xref="taxon:1150997"
     Protein         1..157
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=16249
     Region          7..154
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mknmqinhtq kgftlielmi vvaiigilaa iaipqyqdyt arsqvsrvvg evsavrtave
       61 elvnrggvtl sttasdagyi gynaaasdlv safgitgtpp nvvltatmgd agaavssaev
      121 iwerdnngaw scriegvtdg qggwknsyap ngcqpsn
//
LOCUS       WP_008170312             355 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Marinobacter].
ACCESSION   WP_008170312
VERSION     WP_008170312.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter
  ORGANISM  Marinobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae.
REFERENCE   1  (residues 1 to 355)
  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 355)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 355)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 355)
  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   5  (residues 1 to 355)
  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   6  (residues 1 to 355)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Marinobacter"
                     /db_xref="taxon:2742"
     Protein         1..355
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40161
     Region          38..217
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          111..349
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mmttqktgdl qkpgpgipsn ysrliareld ltakqlprll lgtglgvtqf lseeslltaa
       61 qqvrilrnal dlsgqpelgl wlgkrltpat hgamgfvays spdfltalqa ihtflptras
      121 fiqlhlrqvn erlecildyq esldddiqrc lsdamvkalf efgefiigrp lheaeicfah
      181 peppyqamya dflpgqirfd cdqlkltlpm slcrepnasa nhenyrlalq qcesmlaqlq
      241 sdkpsyqtql kmmmlsrppg tlsedeaaas lfmskrtlar klkqersgfr kvrdeilsqq
      301 aatylrdsql sieaiaalmn yhdsanfrra fkrwfdqspe qfrqnvrsqt vhphd
//
LOCUS       WP_008170518             349 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Marinobacter].
ACCESSION   WP_008170518
VERSION     WP_008170518.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter
  ORGANISM  Marinobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae.
REFERENCE   1  (residues 1 to 349)
  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 349)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 349)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 349)
  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   5  (residues 1 to 349)
  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   6  (residues 1 to 349)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Marinobacter"
                     /db_xref="taxon:2742"
     Protein         1..349
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38661
     Region          43..214
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          113..348
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mnahlsspsk nrnslgdisv lyvsallraa eaegassael asrfqldhqt ltspearisi
       61 prfmrlghaa inetgnpalg lrmgalsrpv dagiaglage tagtagaala tliryallts
      121 rnsrgvptvq petrqakfys irpyngfnyf vvdsvlaawt qflrtvtgry dvlekvtiey
      181 rsigqddlfe swfrcpvqfg assnsltvrq diwesasqqa qpamheklsd lcerelqqir
      241 rgwttgdrvk nlltplfrge tpsletiavk lgiapwtlqr qlaaegtgfr elvdetrkql
      301 ardyiretet slaeiawllg fanpaafhka yrrwfnlspg ehrkqirhg
//
LOCUS       WP_008171353             102 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Marinobacter].
ACCESSION   WP_008171353
VERSION     WP_008171353.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter
  ORGANISM  Marinobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Marinobacter"
                     /db_xref="taxon:2742"
     Protein         1..102
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11275
     Region          1..102
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(25,56..57,59,85)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(25..26,34,37,39..40,42,45..46,48,56,61,67)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mpeptkdqki wqvvlavpeg rvvsygqvae maglgrqary igkalgklpe ghavpwyrvi
       61 rsngqiafpa gsekyreqvs rleaegvevt dgrvsmsryc wq
//
LOCUS       WP_008172084             363 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Marinobacter].
ACCESSION   WP_008172084
VERSION     WP_008172084.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter
  ORGANISM  Marinobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Marinobacter"
                     /db_xref="taxon:2742"
     Protein         1..363
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=41261
     Region          1..352
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msieiqgink ffdkfqalhd inltipdgql tallgpsgsg kttllriiag letpeegrir
       61 fsgkdvtdlh vrdrrvgfvf qhyalfrhmt vaenvafgln vlprkerpgk peirkrvkdl
      121 lemvqlehla drypaqlsgg qkqrialara mamrpeilll depfgaldak vrkdlrrwlr
      181 slhdelhfts vfvthdqeea lelsdqvvvm sngrieqvdt plelygrpds rfvfeflgqv
      241 nvlsgkvrdg vmsqgdawir lpegcendda qlylrphevr ltqaasdqah lpfrieainl
      301 igaevrielk pdgweceelw evgishtefn arqpqrgdrc favpdvghlf cehavepktl
      361 ewr
//
LOCUS       WP_008172132             298 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Pseudoalteromonas sp.
            BSi20652].
ACCESSION   WP_008172132
VERSION     WP_008172132.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. BSi20652
  ORGANISM  Pseudoalteromonas sp. BSi20652
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Pseudoalteromonas sp. BSi20652"
                     /db_xref="taxon:388384"
     Protein         1..298
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion 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          16..266
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mfdfkvtvfn ntqnqlgesp lwhplldtlf wvdidkkily srkedsilkn dlndtsivkq
       61 vtmddtvtal awlnadylil gtntgiyrhh innetqeliv aiekdesntr sndgradpwg
      121 gfwlstmhvd akkgqgkiyr yykhklkciv nnltipnglc fdkarlrgyy cdsfasciym
      181 idldedtgap cseprvfyqf snanvdpdgc vtdtlgnlwv avwgmgcvmc lsskgklitt
      241 iklcaikptc tafggknael llvtsafdda innrvstqgv vfqisgikng qfeppvil
//
LOCUS       WP_008172180             175 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Pseudoalteromonas sp. BSi20652].
ACCESSION   WP_008172180
VERSION     WP_008172180.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. BSi20652
  ORGANISM  Pseudoalteromonas sp. BSi20652
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Pseudoalteromonas sp. BSi20652"
                     /db_xref="taxon:388384"
     Protein         1..175
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=19148
     Region          2..146
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlsgitvasf lestivpipl eavlvplmqa rreklwlial matlgcivga lfgyalgyyl
       61 fdavgdwiin tfssseqfes vkqqmqdqgf wfvitlgivp ipfqiamlaa gatkysvwlf
      121 llasgiarsi ryfglavivy yagneaerii skhktkamig itilvlglwg lstfi
//
LOCUS       WP_008173316             181 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Marinobacter].
ACCESSION   WP_008173316
VERSION     WP_008173316.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter
  ORGANISM  Marinobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae.
REFERENCE   1  (residues 1 to 181)
  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 181)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 181)
  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   4  (residues 1 to 181)
  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   5  (residues 1 to 181)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Marinobacter"
                     /db_xref="taxon:2742"
     Protein         1..181
                     /product="TRAP transporter small permease subunit"
                     /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=19877
     Region          3..170
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mrwiiklddg larlsifcgw vacvamilma anvfydvvar yafnnvsigm qemewhlysv
       61 vfllgipyal rtdghvrvdv fytkwsnkak awvnlvgafi fvipfaylig iygydfalds
      121 ysmgegsgdp gglphrwiik svipvsavfi giaglnmaty avrvmagdke yegehsgggl
      181 a
//
LOCUS       WP_008173482             200 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Marinobacter].
ACCESSION   WP_008173482
VERSION     WP_008173482.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter
  ORGANISM  Marinobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae.
REFERENCE   1  (residues 1 to 200)
  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 200)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 200)
  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   4  (residues 1 to 200)
  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   5  (residues 1 to 200)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Marinobacter"
                     /db_xref="taxon:2742"
     Protein         1..200
                     /product="TRAP transporter small permease subunit"
                     /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=21999
     Region          31..190
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mstanlssgp estpgqgdll petdedigft rldraivwlg kklslvfali vlvsfyeivr
       61 ryvfgsptlw vhetvtfaga tlfvlgglya latdrhvriv liydavspai qrwlrvvhhl
      121 fglafcsmll yaswfmarga vwapwggwrl etsgsawnpp fpaflkviil vaiavmtlqf
      181 vlhlirdlrg patagekgnv
//
LOCUS       WP_008174336             218 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Marinobacter manganoxydans].
ACCESSION   WP_008174336
VERSION     WP_008174336.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter manganoxydans
  ORGANISM  Marinobacter manganoxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 218)
  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 218)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 218)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Marinobacter manganoxydans"
                     /db_xref="taxon:1150997"
     Protein         1..218
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23696
     Region          1..212
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Region          129..160
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
ORIGIN      
        1 maelrteeeq vqaikdwwkk ngsslligig aalaivfgwq awqnhqaqqr teaanqfanl
       61 lnafsdqade tsgetvafva qtlredytds ayavygnlil vrqqlmqegn aeaaidslkw
      121 alektgehea lalvvrnrla raqfssgqye dalatidgag nadafdamys elrgdillaq
      181 gdregareay laareqsqqg rsgilelkla dlgvgeda
//
LOCUS       WP_008174355             238 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Marinobacter].
ACCESSION   WP_008174355
VERSION     WP_008174355.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter
  ORGANISM  Marinobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae.
REFERENCE   1  (residues 1 to 238)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Marinobacter"
                     /db_xref="taxon:2742"
     Protein         1..238
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=26187
     Region          42..209
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mkktrrllpa glllafwawl plssvgasld ddlfgrlsaa apkldtkvlr taisasrcav
       61 ssgvqmperl avidfslpss qerlwifdle kgelllrdlv ahgknsgnfk stafsnvegs
      121 yqssiglfqa resyygkhgy slrldglepg indlarqrai vihgadyvnd dwvskygrig
      181 rshgcpavdn qiikrvvdnl kggqlvfkyy pdqewlhssg flkcdnrtla gknlkksg
//
LOCUS       WP_008175104             327 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Lysinibacillus fusiformis].
ACCESSION   WP_008175104
VERSION     WP_008175104.1
KEYWORDS    RefSeq.
SOURCE      Lysinibacillus fusiformis
  ORGANISM  Lysinibacillus fusiformis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lysinibacillus.
REFERENCE   1  (residues 1 to 327)
  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 327)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 327)
  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   4  (residues 1 to 327)
  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 327)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Lysinibacillus fusiformis"
                     /db_xref="taxon:28031"
     Protein         1..327
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37453
     Region          13..193
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          237..319
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mplgfweglr qlgiaphdvi rkaqlpitlm teptvslaqy yaiwqayadh iddmakgiiq
       61 latsfdsnhy pptvlaayha rdfrdalkrm arykqlcppe slriteegen ctielqwsdr
      121 eqsgppmlvg itlafllelg rrgtdsplta kcvefshsmg diqmleayfg cciqigtkwn
      181 rltlhredld hpfssynlel lemltplldq slsehqqshs ltetvkwmmk rslmggrpdi
      241 qtvaselgms drtlqrrlsd ectsfknllt evrheqaqvy ladptldike vafligyedq
      301 nsfyrafrlw egdtpanwrt khiernv
//
LOCUS       WP_008176373             361 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Lysinibacillus].
ACCESSION   WP_008176373
VERSION     WP_008176373.1
KEYWORDS    RefSeq.
SOURCE      Lysinibacillus
  ORGANISM  Lysinibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Lysinibacillus"
                     /db_xref="taxon:400634"
     Protein         1..361
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=41616
     Region          <128..358
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 metgmtlfes nrksvlesie hkksftivyi tiiswhdldl skcidvvrrk ltlyqpkvew
       61 yrvfdkefll vchaqsqarl isqelsniey lkihylyvqd rklpalnyvr qvylqnitsd
      121 elkecnsqkg lvteefeivf qpilhhnrql sfealskwrw eemgsispgi cipilniesl
      181 ieltkniikk avdllsryne vvyvsinlsa plikditwli ehldeigitn nnriafeite
      241 etimgiease nlkiirdrgh iifidgfgsg sgnsnfqyms llpldgvkld rlfisgksnk
      301 kvmelltnii kaidleviie gvdnveqlnt lseaqydsiq gyyiskplti neltkfmndn
      361 c
//
LOCUS       WP_008176764             350 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Marinobacter
            manganoxydans].
ACCESSION   WP_008176764
VERSION     WP_008176764.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter manganoxydans
  ORGANISM  Marinobacter manganoxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 350)
  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 350)
  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 350)
  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 350)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Marinobacter manganoxydans"
                     /db_xref="taxon:1150997"
     Protein         1..350
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=38254
     Region          2..340
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkllkaltgv agaialttgs afaedlrwkm pvafatnlpg lgspaawvad nlttasdgsi
       61 qvrvyepgkl vppfdilqsv sdgkvsagyt wigydqgkvp aiplfaavpf gmkppayigw
      121 yyygggheml qetyankgfn vhaqlcgiig petagwysep ietledykgl kirfaglggk
      181 vleklgasvt mmpggelyqa lekgtidate fsmpaidqil gfnqvvkynl fpgwhqqfta
      241 qymlinkdew arateaqkal veasctaatt rglaegeykn gkvlaefqdk gvqadqiprd
      301 vllklrevte evleeeaskd adfkrvyesq qefmesykvw dtrayvpadl
//
LOCUS       WP_008179578             293 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Lysinibacillus fusiformis].
ACCESSION   WP_008179578
VERSION     WP_008179578.1
KEYWORDS    RefSeq.
SOURCE      Lysinibacillus fusiformis
  ORGANISM  Lysinibacillus fusiformis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lysinibacillus.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 293)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Lysinibacillus fusiformis"
                     /db_xref="taxon:28031"
     Protein         1..293
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=33964
     Region          <32..273
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mesaveqnik tnnvfsllky lygqhqqntl ymkrlkalkq iiqqgslhty fqpivdlqta
       61 qtigfealnr pisselftsv dqfyefvgqt dcvflfecfc rnlslqrfme rmhndlmdkn
      121 llvflnihpn vlldkkyhsg etlqllkelg ikpqqvvfel tersavidfv efervlshyr
      181 sqgyriavdd vgsgynslkt liylkpefik ldrsliqsid qiseqqqlvt llmkyaeqak
      241 tkiiaegier qeeleylhri gihyaqgyai gkpakeihlg kirvgdhedw gsh
//
LOCUS       WP_008180426             138 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ribonuclease HI family protein [Moorena].
ACCESSION   WP_008180426
VERSION     WP_008180426.1
KEYWORDS    RefSeq.
SOURCE      Moorena
  ORGANISM  Moorena
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Coleofasciculales; Coleofasciculaceae.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 138)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 138)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Moorena"
                     /db_xref="taxon:1155738"
     Protein         1..138
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=15520
     Region          10..134
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(14..17,47..49,52,76,116,130)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mtdksnnlai ihfdgvskrr tnqsacgaii qyqgevypvs qyvgfttqnq teymglilgl
       61 qktlklgakq akiygdcelv inqlhgdymv knnnlvsfht raktlldkld fyeliwinkt
      121 qnleadqlan dcidleks
//
LOCUS       WP_008180777             255 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phosphonate ABC transporter ATP-binding protein
            [Moorena].
ACCESSION   WP_008180777
VERSION     WP_008180777.1
KEYWORDS    RefSeq.
SOURCE      Moorena
  ORGANISM  Moorena
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Coleofasciculales; Coleofasciculaceae.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
REFERENCE   2  (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   3  (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   4  (residues 1 to 255)
  AUTHORS   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 255)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Moorena"
                     /db_xref="taxon:1155738"
     Protein         1..255
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=28136
     Region          5..251
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mtkipifelk qvsqqfgqfr altnlnlkiy pgervalvga sgagkstlir llngillpsk
       61 gevwvlgrnl arisprqlrq vqrrlgtvyq qfnlvnnlrv ihnvnaghlg rwslmkalvs
      121 llfpqevdta lkalaqvgip eklyapteel sggqqqrval arvlvqnpdv iladepisnl
      181 drqmsreimd llkeisetgg ktlvtslhsl efacshcdrl vglqrgqivf dvppgvlsqt
      241 midklyatet dlinv
//
LOCUS       WP_008181445             179 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit [Moorena].
ACCESSION   WP_008181445
VERSION     WP_008181445.1
KEYWORDS    RefSeq.
SOURCE      Moorena
  ORGANISM  Moorena
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Coleofasciculales; Coleofasciculaceae.
REFERENCE   1  (residues 1 to 179)
  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 179)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 179)
  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   4  (residues 1 to 179)
  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   5  (residues 1 to 179)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Moorena"
                     /db_xref="taxon:1155738"
     Protein         1..179
                     /product="TRAP transporter small permease subunit"
                     /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=20287
     Region          4..177
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mqqllrisrl idsfnerigr ltywilplmi ligvwnvvgr ylgrfigenl ssngfietqw
       61 ylfdlvfllg aaytlkhngh vrvdvfyksl kpkaqaianl igtllflipf cimviyfswg
      121 aivnswtiqe mspdpgglpr ypiksmiivs fgllilqgis eaiknwaifa gylapqeee
//
LOCUS       WP_008184017             397 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein, partial [Moorena producens].
ACCESSION   WP_008184017
VERSION     WP_008184017.1
KEYWORDS    RefSeq.
SOURCE      Moorena producens
  ORGANISM  Moorena producens
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Coleofasciculales; Coleofasciculaceae; Moorena.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Moorena producens"
                     /db_xref="taxon:1155739"
     Protein         <1..397
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
     Region          97..343
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 dtttdtdsdt ttdtdpdttt dtdpdtttdt dpdttpdpdp dttpdpdpdt ttdpapepii
       61 aaapaipaap dpdtdgidat vtftgnqlal fpdnkltlsd annttlvgat vkianllnpt
      121 eelltvdntd tliavnfdan ngilslsgvd tiqnyqqvln tleyentsgv tdasgriiqf
      181 vvddglafnn vsevatliti qdndstvigt fqndtllggn gndtlegnsg ndlldggagn
      241 dslvggdnsd tllggdgndv ldggtngdfl dggagndnls ggensdtlig aegndslfgg
      301 ngddileggl gndilsgagg idtyvlnpge gtdtvfsfed gidmfklggd ltfdqlaiad
      361 mgattitang evlaqvfgvs asqltaadfi veedivv
//
LOCUS       WP_008187879             367 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [unclassified Moorena].
ACCESSION   WP_008187879
VERSION     WP_008187879.1
KEYWORDS    RefSeq.
SOURCE      unclassified Moorena
  ORGANISM  unclassified Moorena
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Coleofasciculales; Coleofasciculaceae; Moorena.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="unclassified Moorena"
                     /db_xref="taxon:2683338"
     Protein         1..367
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38269
     Region          83..314
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mttifgfetg dfinwntigd asietaafgs ipsqgkfqal itndvgsvsd selenllgln
       61 pgtidgfgng dakegsalkl kpitvnagdv lsfdfnfltd eltpdstfkd fafvsitpnv
      121 lfnladtnss fllsptgfrq etdyntftyk fptsgtylvg mavvdvedel lesallvdnl
      181 kvvpkdeviv gtsndetlfg tadndtiygq ggndtifgse gvnilyggag ddlifggsns
      241 dniyggtgnd rifssggsns vyggigndfi dtgtgndfvv ggfgndtirl gggqdivvle
      301 arkgtdtiin feagkmflgl sgaltfsnlt fnqsggdvei sansevlavv nnaqvstias
      361 asnflti
//
LOCUS       WP_008188375             256 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phosphonate ABC transporter ATP-binding protein
            [Stappiaceae].
ACCESSION   WP_008188375
VERSION     WP_008188375.1
KEYWORDS    RefSeq.
SOURCE      Stappiaceae
  ORGANISM  Stappiaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
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   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Stappiaceae"
                     /db_xref="taxon:2821832"
     Protein         1..256
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=27678
     Region          7..249
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 msvaaalcdv thqfdehpal snvsltlkag esvaflgpsg agkstllall dgrlrnwrgt
       61 aevlettysa tarpprdars dvgfifqefa lvdrlsvyqn vmngrlgrmr twqslwsrfg
      121 erdhlvvsgv ledtgltdla arradklsgg qrqrtaiarc laqepklila depvsnldpa
      181 naekilglit aaarkrgitv vfsshqpels qrfadriigl rdgkllfdrp sgqvsasdis
      241 elyhgaspsa elrvvs
//
LOCUS       WP_008189061             753 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: molybdopterin oxidoreductase family protein
            [Moorena].
ACCESSION   WP_008189061
VERSION     WP_008189061.1
KEYWORDS    RefSeq.
SOURCE      Moorena
  ORGANISM  Moorena
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Coleofasciculales; Coleofasciculaceae.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 753)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 753)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Moorena"
                     /db_xref="taxon:1155738"
     Protein         1..753
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=83547
     Region          1..727
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mtdsaktlcp ycgvgcglev lppagsgrat yrdsqgnpiw kvrgdrshps nqgmvcvkga
       61 tvsesldkdr lkypmmrdsl dqpfqrvswd ealdrvvnri qtvrftqgpe aicmygsgqf
      121 qtedyyiaqk llkgclgtnn fdansrlcms savagyiqsf gsdgppccyd dleltdcafl
      181 igtntadchp ivfnrlrkhh kkhrhvkmiv vdprrtstak ladlhlaikp gtdidllngm
      241 ahlllrwgkl dtefieects dfsayaqvii nyppdivaer cgipvhelee aarywakskr
      301 vlslwsmgvn qssegtakvr tiinlhlmtg nigkpgtgpf sltgqpnamg greagglahi
      361 lpgyrvvknp qhrseveqlw klkpgtispn pgldawsmik gletgevgfl wiaatnpavs
      421 mpdiertkaa lrkssftvyq dayyptetaa yahvllpaaq wsektgamtn servvtlcpq
      481 frnppgearp dweifaevgr rlgftkefdf tdsaavygef vqlsrgrlcd mtglsherlr
      541 kdgpiqwpcp eelqnqessk slstekssln sgkrlytdfr fntpdskakf aafhskglae
      601 ppsdeyplvl tsgrlyghwh tqtrtgriek itkmypypll eihprdaqkl gikdgdwvev
      661 rsrrgtcrfp aqvtkaitpg tvfapmhwga lwanqaeana lthpescpis lepelkacav
      721 nlvpisetds mrsqnpdqep igtpileklk vlr
//
LOCUS       WP_008189189             283 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Roseibium alexandrii].
ACCESSION   WP_008189189
VERSION     WP_008189189.1
KEYWORDS    RefSeq.
SOURCE      Roseibium alexandrii
  ORGANISM  Roseibium alexandrii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 283)
  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 283)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Roseibium alexandrii"
                     /db_xref="taxon:388408"
     Protein         1..283
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29981
     Region          3..274
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mtlatlsqvl qpalkdgyav aglvtlgwed mrayvaaaee egvpvilqag pscrkhtplp
       61 vlgamfrhla egstvpvvah ldhgytfeec qqaldsgfts lmydgsrkpl sqnidetari
      121 aelahsagis cegeigfvgy ahgaasegtd pvdaekfaad sgvdamaisv gnvhlqenke
      181 ggldearisa iqarttvplv ihggsgvpve qrqklarttn ickfnigtel rkafgtvmrd
      241 avnsdpdrfd rvtilsethd pmvaatrtvl kafggpsrne pke
//
LOCUS       WP_008189435             270 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Moorena].
ACCESSION   WP_008189435
VERSION     WP_008189435.1
KEYWORDS    RefSeq.
SOURCE      Moorena
  ORGANISM  Moorena
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Coleofasciculales; Coleofasciculaceae.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Moorena"
                     /db_xref="taxon:1155738"
     Protein         1..270
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27950
     Region          5..255
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mktifgtpgd diisasggnt tifastgkdd ltvfqggnnt ifanegnqgd rvslgmgsnn
       61 tvytgvgddv itvfesnenl ifagegnnqi slvksdnnqi fvgagddtif tergdneifa
      121 gegdnvittl fgdniiymgt gddtittkfg dnvifagegd nlidaqsgnn tiyagsgndq
      181 ittgfgddli fagvgnnfis agigndtvfa gsgideflll egegavtihg fqsgqdvfqn
      241 nelsftvsgn ntlvfaqsgd ilatlmdvql
//
LOCUS       WP_008191890             187 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Moorena].
ACCESSION   WP_008191890
VERSION     WP_008191890.1
KEYWORDS    RefSeq.
SOURCE      Moorena
  ORGANISM  Moorena
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Coleofasciculales; Coleofasciculaceae.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Moorena"
                     /db_xref="taxon:1155738"
     Protein         1..187
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18977
     Region          <8..187
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 maailspgst gplfisdfeg amffdspqeg ggvfavgqed qtnififgdg ndvaaggdev
       61 dilmagagdd niqgaggtdf vfgglgddiv rgglgddvvv gnegsdvlis gggsdiyeff
      121 adqflegdld iildfevgsd aivvvgstdv sydaftgfls vdgsevavln rgldidvftr
      181 tnsavvf
//
LOCUS       WP_008192571             100 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [unclassified
            Thermotoga].
ACCESSION   WP_008192571
VERSION     WP_008192571.1
KEYWORDS    RefSeq.
SOURCE      unclassified Thermotoga
  ORGANISM  unclassified Thermotoga
            Bacteria; Thermotogati; Thermotogota; Thermotogae; Thermotogales;
            Thermotogaceae; Thermotoga.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="unclassified Thermotoga"
                     /db_xref="taxon:2631113"
     Protein         1..100
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11670
     Region          6..100
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mkllaqkvlk eakrvaevlr erysvrrvvl fdslakylrr tgkftkrsdi dlaveglpke
       61 eyfkvlsein rlsefeidli dlegcpeflk rlieregiei
//
LOCUS       WP_008192653             306 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Roseibium
            alexandrii].
ACCESSION   WP_008192653
VERSION     WP_008192653.1
KEYWORDS    RefSeq.
SOURCE      Roseibium alexandrii
  ORGANISM  Roseibium alexandrii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 306)
  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   2  (residues 1 to 306)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Roseibium alexandrii"
                     /db_xref="taxon:388408"
     Protein         1..306
                     /product="aminoglycoside 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=34423
     Region          28..223
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
     Region          <203..277
                     /region_name="CotS"
                     /note="Thiamine kinase or a related kinase [Coenzyme
                     transport and metabolism]; COG0510"
                     /db_xref="CDD:440276"
ORIGIN      
        1 mtdrmtdael ldflqgrypf gdlsgarlrp lpssythrfw rlrtrerdyv ikeyfpglen
       61 nplyptlpqe eataltller hrlaprlecf ldspagsplv iygyergsea eidvrdaaql
      121 lgrfaalela pedismvpsg yhqvlahada ilgkipnsrr aanlkrlrpq dsaikvsaap
      181 qctlihrslc lgtvqmtaag palidwqyag lgdpvediac flspglltly glkplvlyae
      241 dlflehypdr tivdrflaer sayhwrlaay clfrqetlth enapasraya raleeevdll
      301 lrlrgk
//
LOCUS       WP_008193417             181 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [unclassified
            Thermotoga].
ACCESSION   WP_008193417
VERSION     WP_008193417.1
KEYWORDS    RefSeq.
SOURCE      unclassified Thermotoga
  ORGANISM  unclassified Thermotoga
            Bacteria; Thermotogati; Thermotogota; Thermotogae; Thermotogales;
            Thermotogaceae; Thermotoga.
REFERENCE   1  (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   2  (residues 1 to 181)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="unclassified Thermotoga"
                     /db_xref="taxon:2631113"
     Protein         1..181
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=20168
     Region          37..106
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
     Region          119..180
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mrlrkqhqrt ilfvalvffi llgivmeret rteedttasq kvvafpveln tasledlmsi
       61 pgigpvkaqr iidyreshgg fssveelknv sgigektlek isryvtvegv eqhikrevtk
      121 lnvntasvee letlpyigev kakaiveyre kngpfrsped lldvpgigek tlekiggkit
      181 f
//
LOCUS       WP_008194300             382 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Roseibium alexandrii].
ACCESSION   WP_008194300
VERSION     WP_008194300.1
KEYWORDS    RefSeq.
SOURCE      Roseibium alexandrii
  ORGANISM  Roseibium alexandrii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Roseibium alexandrii"
                     /db_xref="taxon:388408"
     Protein         1..382
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=40181
     Region          4..382
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mggilvlnsg sssikfalfd esldetlsgs ateiggasdl kisskdlvtk easadlpdha
       61 aalrailnav qtegvdianl agaghrvvhg gsvlqaairv dgqviaeier csdlaplhnp
      121 hnlaaimalr dlapdlvqva cfdtafhasn pevarryalp dwpemetlrr ygfhgisyqg
      181 likkladvse tgvpnrllaf hlgngaslca iksgqsvatt mgyspleglt mgtrtgnidg
      241 nlvlrlaeen giedtkelln kksgllglgg lsdmrtlhaa etdasrfave hfcywavrha
      301 gsmiaamggl dgiaftggig endavvrqki isglrflgat cdpqsndsnr sridvsgstv
      361 piwivkaeee ktiaaetqkl ia
//
LOCUS       WP_008194332             379 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [unclassified
            Thermotoga].
ACCESSION   WP_008194332
VERSION     WP_008194332.1
KEYWORDS    RefSeq.
SOURCE      unclassified Thermotoga
  ORGANISM  unclassified Thermotoga
            Bacteria; Thermotogati; Thermotogota; Thermotogae; Thermotogales;
            Thermotogaceae; Thermotoga.
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
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 379)
  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   5  (residues 1 to 379)
  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   6  (residues 1 to 379)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 379)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 379)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="unclassified Thermotoga"
                     /db_xref="taxon:2631113"
     Protein         1..379
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42569
     Region          11..59
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          76..363
                     /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 meiyslkqar tinklrvlnt irfepgvtrn misektgldp stvtklvnem kkkkmiyerg
       61 ilpsklgrhs krlyvnkdfs kaivvdlgvt hsivgisffd gsvevvdefd tpdtpeecfr
      121 vltekvskfp gvfplivigv pgsvdkshkk lafapnlnrw rdidvdkyfk vfevylenda
      181 nlaalaemmr nkhfgdrkni vyilvregig ggiiiegkly kgsfnaagei ghmkmydrgp
      241 cfcgrvgcwe antsishcvh qyekkktlpg ntmyekfeml crmyeedpla kevldeftgi
      301 lidgivnlvn ilspeivivg gegvflpesv fevivsetrr qvhpmdkevs vekgslsnke
      361 vvlegtsils smmiserlv
//
LOCUS       WP_008194736             394 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Roseibium alexandrii].
ACCESSION   WP_008194736
VERSION     WP_008194736.1
KEYWORDS    RefSeq.
SOURCE      Roseibium alexandrii
  ORGANISM  Roseibium alexandrii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Roseibium alexandrii"
                     /db_xref="taxon:388408"
     Protein         1..394
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=41953
     Region          4..388
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mapvilvlns gsssikfsly dgpaeqvtgq isglgakphl nleallsgrk idraldstdg
       61 nshgaalgal lpilneelgg rsvaavghrv vhggtkhdlp vhitgavmqe lrvleplapl
      121 hqphnlagie aaraafpgae qvacfdtafh rkhpwvndtf alprsfydeg vrrygfhgls
      181 yeyicehlkk htpdayegkv ivahlgngas mcairagqsi gstmgftald glpmgtrcgq
      241 ldpgailylm ttkgmsadei sdllykksgl kglsglsqdm rtlsqsddpr aaeaieyyvf
      301 rvrrelgama avlsgvdtlv ftggigensa lirdrvcadq ewlgiqidpa lnnagdgtis
      361 tqcsqvavlv vptneeemir rhteallash qfpa
//
LOCUS       WP_008195248             140 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Roseibium alexandrii].
ACCESSION   WP_008195248
VERSION     WP_008195248.1
KEYWORDS    RefSeq.
SOURCE      Roseibium alexandrii
  ORGANISM  Roseibium alexandrii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Roseibium alexandrii"
                     /db_xref="taxon:388408"
     Protein         1..140
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15295
     Region          1..139
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mialflssfl aatffpaqse lglvylvtty pedlvaliav asvgntlgsv vnwaiglgli
       61 rfagpaehsg kaskwyvkaq hwyerygyws lliswaplvg dpvtlvagvf replwrffll
      121 vaiaktvryi vvaaialqft
//
LOCUS       WP_008195685             394 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Roseibium alexandrii].
ACCESSION   WP_008195685
VERSION     WP_008195685.1
KEYWORDS    RefSeq.
SOURCE      Roseibium alexandrii
  ORGANISM  Roseibium alexandrii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Roseibium alexandrii"
                     /db_xref="taxon:388408"
     Protein         1..394
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=43264
     Region          35..294
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 msditpdnle sfvpfattts kqraraaqas sslsrhadlr ecaaairkgs ksfhlaslil
       61 paetrkaals lyafcrhsdd liddpradrt aleqlkdrld lvyrgipapy acdrafartv
      121 qaygipkcvp dalldgfamd lgerhyktia qvkdyatcva atvglmmslv mragdkdala
      181 raadlgiamq ltniardvge darngrlylp edwmrdagld peaflaspkf spelrevvlr
      241 llaeaghhye lghagiaalp encrhairta alvyqeigte iavnnydsvt rrahtrkikk
      301 lslllkarlp qleqsnaahl nmrrpadpsa ahlvsacans fetharlqka anasvaddsn
      361 mewvlgvmik lqaesrahhr sqklamqrrs qdsf
//
LOCUS       WP_008196667             258 aa            linear   BCT 20-JAN-2025
DEFINITION  phosphonate ABC transporter ATP-binding protein [Roseibium
            alexandrii].
ACCESSION   WP_008196667
VERSION     WP_008196667.1
KEYWORDS    RefSeq.
SOURCE      Roseibium alexandrii
  ORGANISM  Roseibium alexandrii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
REFERENCE   2  (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   3  (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   4  (residues 1 to 258)
  AUTHORS   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 258)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Roseibium alexandrii"
                     /db_xref="taxon:388408"
     Protein         1..258
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=27571
     Region          13..255
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mlhtppadtk dvaiatsalk kqykngqvpv lkgvdltirh gervaligsn gsgkstllkc
       61 liglhavneg svqtlgetfg siptaaqraq lrkqtgfvfq khclvkrhsv lsnvvhgmlg
      121 lpgswraftq atapsswrak amsalddvnl adkarsrada lsggqqqrva iaraivrgpr
      181 liiadepaas ldpvagtevm rlfselaqvh gitllftshd mehaaaysdr tvalkdgqil
      241 fdkascevcd qdlrdtfq
//
LOCUS       WP_008196847             746 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Roseibium alexandrii].
ACCESSION   WP_008196847
VERSION     WP_008196847.1
KEYWORDS    RefSeq.
SOURCE      Roseibium alexandrii
  ORGANISM  Roseibium alexandrii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 746)
  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 746)
  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 746)
  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 746)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..746
                     /organism="Roseibium alexandrii"
                     /db_xref="taxon:388408"
     Protein         1..746
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=78557
     Region          175..735
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mtdkttpaed ddhliaqgvd eepvevnrrl yegkslmfit sfaalyaafh maalnglsis
       61 ewtgivipfl ptfpmetwnf rivhvagala lgfllfagri dfpekgqetp ilgyaayalm
      121 ipalfslgma fsfaaeissg kmwngidegi rfsetylfgl plivatagsi ilswfhqrer
      181 sglaapdvvl avcgaavaay litiygtlmr nstgtpfapi gisiaavagt alimeltrrv
      241 agmalvviaa iflcyvfigd klpgflnspp itwqrffsqv ytdagilgpt tavsstyiil
      301 fiifaaflqa skvgdyfvnf afaaagrarg gpakvaifas glmgmingts agnvvstgsl
      361 tiplmkkvgy hrktagavea aastggqimp pimgagafim aeitgipyte itiaalipav
      421 lyfvsvyfmv dfeaaklgmr gmkseelpkf sqmvrqvylf lpiiiliyal fmgysvirag
      481 alatmsaavv swltpyrmgp rsifrafeia gtmsvqiiav cacagiivgv isltgvgarf
      541 sslllsladt sqllalffam cisillgmgm pttaayavaa svvapglvql giplltahff
      601 vfyfavlsai tppvalasya aagisganpm etsvasfkig iaafivpfmf fynsallmdg
      661 svldigraal tavvgvflls savqgwflga vaawflrigl iaaallmieg glisdligvg
      721 iaaavfavqr ifhpkpdaai pvrgad
//
LOCUS       WP_008197368             295 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Roseibium alexandrii].
ACCESSION   WP_008197368
VERSION     WP_008197368.1
KEYWORDS    RefSeq.
SOURCE      Roseibium alexandrii
  ORGANISM  Roseibium alexandrii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Roseibium alexandrii"
                     /db_xref="taxon:388408"
     Protein         1..295
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32136
     Region          15..257
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mshtitrfld ttyqlaecpt wdertnrllw adiqgrsvqs mdwdtraitt wqfdnevgsf
       61 glcddgrlit svwdkvvlfd pqtgtqevla eveadkpqtr lndgkvgpdg afwvgtmdts
      121 sprepiagly rvdssgevae irdelqcsng lawtpdgdym yhsdtspgwi ecyafdaatg
      181 slgakmlfaq qtnatgrpdg atvdangnyw sggvssgvvn cfapngelle aikmpvqrpt
      241 mpcfcgpnld hlivtsikqp sdptsvepdt lsgglflieg hgqtglktyr fktaq
//
LOCUS       WP_008197786             160 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Algoriphagus machipongonensis].
ACCESSION   WP_008197786
VERSION     WP_008197786.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus machipongonensis
  ORGANISM  Algoriphagus machipongonensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Algoriphagus machipongonensis"
                     /db_xref="taxon:388413"
     Protein         1..160
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17185
     Region          9..160
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 msenlmipes ankaekyeal ipqiealisg epdlyanlan itaalkeafg ffwvgfylvk
       61 etqlvlgpfq gpiactrisi gkgvcgtawq daktqlvpdv dafpghiacs sasrseivvp
      121 vfkgeqvamv ldvdsdqvnd fdsadqlyle klmgilgktl
//
LOCUS       WP_008198500             292 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Algoriphagus
            machipongonensis].
ACCESSION   WP_008198500
VERSION     WP_008198500.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus machipongonensis
  ORGANISM  Algoriphagus machipongonensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Algoriphagus machipongonensis"
                     /db_xref="taxon:388413"
     Protein         1..292
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33338
     Region          15..257
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mktynytsip sqcflaegpy whsdrqsffw vdiengnlfe hspksgdtnt infphrltvv
       61 legkenelil gldcklakyh leskeltwia eveqefplhr fndgkvdpkg riwigtlstl
      121 ftesagslyr vgkdlkpvkq ldqltisngm awtednqtfy fidtptreik afsfdlesgy
      181 irferiavei peelgfpdgm cidqegmlwv ahyggfgvir wdpttgemid kielpvphvt
      241 sccfggenld tllittaqen lseqqlleyp msgdvfmvkt ntrgfeanky hy
//
LOCUS       WP_008198635             112 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Algoriphagus machipongonensis].
ACCESSION   WP_008198635
VERSION     WP_008198635.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus machipongonensis
  ORGANISM  Algoriphagus machipongonensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Algoriphagus machipongonensis"
                     /db_xref="taxon:388413"
     Protein         1..112
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12413
     Region          3..107
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(27,58..59,61,87)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(27..28,36,39,41..42,44,47..48,50,58,63,70)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mpkekpnyfd lvyqvvreip tgratsygai ahylglksga rmvgyamnaa halpdvpahr
       61 vvnrlgmltg rhhfstptam qealesegvk iendqikdfd kvfwdpetel si
//
LOCUS       WP_008198969             452 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Microcystis sp. T1-4].
ACCESSION   WP_008198969
VERSION     WP_008198969.1
KEYWORDS    RefSeq.
SOURCE      Microcystis sp. T1-4
  ORGANISM  Microcystis sp. T1-4
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Microcystaceae; Microcystis.
REFERENCE   1  (residues 1 to 452)
  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 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   3  (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   4  (residues 1 to 452)
  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 452)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Microcystis sp. T1-4"
                     /db_xref="taxon:1160279"
     Protein         1..452
                     /product="CmpA/NrtA family ABC transporter
                     substrate-binding protein"
                     /function="16.1 : Circulate"
                     /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=48620
     Region          56..317
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 msnfsrrkfl ttaavsaaga vvlkgcvgnp pdstggtttt apaspaaspv aiapeqapet
       61 tkiklgyipi veaapliiak ekgffakygm advevskqan wgsardnvei gadaggidgg
      121 qwqmpmpyli seglitknnv kvpmyvlaql ntqgngiaia gkhegknigl dlkpakdyil
      181 gmkttgtpfk aaytfpkanq dfwirywlaa gginpdtdin liavpaaqtv anmktgtmda
      241 fstgdpwpar ivadqigfms altaeiwpyh peeylairad wvdknpkatk allkgimeaq
      301 qwldqeanra eaaailakpa yfnlkeeiia gplkgmqkmg dgkpeitdkn kgvfywkdpa
      361 gsvsypyksh dlwfltesvr wgflpketlt tastlidkvn redlwkaaat elgvpaadip
      421 tstsrgvekf fdgktfdpan pqayldslai kk
//
LOCUS       WP_008199121             216 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Microcystis].
ACCESSION   WP_008199121
VERSION     WP_008199121.1
KEYWORDS    RefSeq.
SOURCE      Microcystis
  ORGANISM  Microcystis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Microcystaceae.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Microcystis"
                     /db_xref="taxon:1125"
     Protein         1..216
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23132
     Region          9..202
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mtlpldvpta inqrrsiknf ttdpiapell ktlveltvaa pssfniqdwr iilvqdeaqk
       61 aalaeaawgq kqiiqapvtf vfaadaaagg gdltpiyeqa lstgawsegt vkyfkqaipg
      121 fqkalgektr eyaikdaiia athlvlaaes lglsscflng wiedkvkavi gaadhphlai
      181 avvvpigyaa eprlnpgrlp ldynvfvdrl gnpyqv
//
LOCUS       WP_008199468             307 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Algoriphagus
            machipongonensis].
ACCESSION   WP_008199468
VERSION     WP_008199468.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus machipongonensis
  ORGANISM  Algoriphagus machipongonensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 307)
  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 307)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Algoriphagus machipongonensis"
                     /db_xref="taxon:388413"
     Protein         1..307
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35304
     Region          35..192
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          221..302
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtqnnfiagv pwrntrdlkt lvenrttytl encelnifet hqqaddvnlv fgdlvlttml
       61 kgkkvmhlfd kpgfeylpge svivppnevm kidfpeaqwd nptqcialsi skemieatfn
      121 llnekfpdkv itkdwgldls yfhlintqdl seiinrfvri gvkdgskekd liatlalkel
      181 lirlsqtqar dmlektykel asgnrmahvv eyikkniret islddlagea cmskahflrs
      241 fkqelgltpm efvlherlnl akqylllgnh qiqevcymag frnityfira fkqefgltpk
      301 vfqtksn
//
LOCUS       WP_008200009             804 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Algoriphagus machipongonensis].
ACCESSION   WP_008200009
VERSION     WP_008200009.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus machipongonensis
  ORGANISM  Algoriphagus machipongonensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 804)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 804)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 804)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..804
                     /organism="Algoriphagus machipongonensis"
                     /db_xref="taxon:388413"
     Protein         1..804
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=92112
     Region          51..804
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkyisfllal gititlaiyv skpigpvppi atlidpnhgf wqnmiseddl aetevllegl
       61 nspvqivydk nliphifaqn eedlykaqgy vtakhrlwqm efqtraaagr lseivgdval
      121 eldrmtrrkg lgygaelgmd flkesdpetl ryleayasgv nqyinsigpg qlpveykiln
      181 yrpeewtpyk sllllkymsd mlvgdrdley snlrkilgeq mlnklypdyp kdadpviesd
      241 kvwefeplei qkpdsleypd dllsmkpleq plpgtgsnnw avapsktkng hpilandphl
      301 slnlpslwya iqlttpdysv kgaslpgalg visgfnenia wgvtnatkda rdwykitfqd
      361 eqrkaykygd qwrptnfrie eikvkdqdaf ldtvvythyg pvvydksfrs erqdvnfalk
      421 wtvhmgsneq ktflllnkat nhedynvald nftapaqnfv faskngdiam riqgkfalkw
      481 peqgkffmdg adprmewqkf ipneqnpstl npnrgfvasa nqhpvassyp yyvfdnsyeh
      541 yrnrringkl remeditved mkklqfddfy fqasealptm lnllggdysk egntekyikq
      601 lkewdyyadp nqkaptlyyv wwgklynqiw qawddfgvsv vkpnsyqtiq llknepndsi
      661 fdlektqeie nakshvlksf emmvkeisdw eqnegdyawa nfkqtsiqhl vpqfksfset
      721 nvytgggagi vnatserhga swrmvvelgd kptafgiypg gqsgnpgsky yknfipvwae
      781 gnyldfnlrs qkdttnllyq ttlk
//
LOCUS       WP_008200683             132 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Algoriphagus
            machipongonensis].
ACCESSION   WP_008200683
VERSION     WP_008200683.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus machipongonensis
  ORGANISM  Algoriphagus machipongonensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 132)
  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 132)
  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   3  (residues 1 to 132)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Algoriphagus machipongonensis"
                     /db_xref="taxon:388413"
     Protein         1..132
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15502
     Region          17..120
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 myflpynrsl kefsrelrnh stlseillwn klkaknfrgy sfnrqkplgn yivdfyckkl
       61 glvievdgds hvhpeavlkd nvrqkvledl gleffripda eikrqmlevl dslnrlidkl
      121 eeekgldktn fv
//
LOCUS       WP_008200735             544 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Algoriphagus machipongonensis].
ACCESSION   WP_008200735
VERSION     WP_008200735.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus machipongonensis
  ORGANISM  Algoriphagus machipongonensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 544)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Algoriphagus machipongonensis"
                     /db_xref="taxon:388413"
     Protein         1..544
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=57900
     Region          3..544
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 minkalcldp adnvgvaltd lkpgdsyaln gakgqiisev sskhkfaled lsvgedilmy
       61 gtivgettqe ikageavtla nikhkirdfk esgatyewss ldvkrwsdkt fmgyeradgq
      121 vgtanywlvm pmvfcentnv kllqdafeka lgfavdnpye nqvrnlvaay qqekftesvs
      181 aplqdtnskv fenidgvrfl theggcggtr rdsdtlcall agyinhpnva gatilslgcq
      241 naqvsilkes lskiqkgask pvivcdqqee gttkvlleka vketfaglve ankiprtpap
      301 lsklviglec ggsdgfsgis anptlgqvsd mvislggaai lsefpelcga eqtlidrckt
      361 peisdkfirl mdeyaraaen vgsgfdmnps pgnikdgllt daikscgaak kggtapvsdv
      421 ldyteyikek glnllctpgn dvesttglag sganvilfst glgtptgnpv cpvikvstnd
      481 klaarmpdii dfntggiisg eetiesagdk llelivdvas grvktkaeqk knydfipwkr
      541 gvsl
//
LOCUS       WP_008203336             117 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [Microcystis].
ACCESSION   WP_008203336
VERSION     WP_008203336.1
KEYWORDS    RefSeq.
SOURCE      Microcystis
  ORGANISM  Microcystis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Microcystaceae.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Microcystis"
                     /db_xref="taxon:1125"
     Protein         1..117
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13480
     Region          24..113
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 msafptpeld kilkekdiqg eqqrqtllak tqqwlhenav kyginrayif gsvtrpykfh
       61 pgsdvdiave ninpelhfea isilsyylgr evdiillknc hfahrireeg ilwttdk
//
LOCUS       WP_008205245             176 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Microcystis].
ACCESSION   WP_008205245
VERSION     WP_008205245.1
KEYWORDS    RefSeq.
SOURCE      Microcystis
  ORGANISM  Microcystis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Microcystaceae.
REFERENCE   1  (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   2  (residues 1 to 176)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Microcystis"
                     /db_xref="taxon:1125"
     Protein         1..176
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19534
     Region          106..175
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mtpqnwlgrt fnplkakisn dpyyrfrsld eiamaaqlgi kinvsqagvd dwlrlpgisi
       61 hqarmlvels gmgvellcle dlaaalsvpv arlkawepil efayyspesh lappkinpnt
      121 asieqlttlp ligdnlaaai iksreeqglf knivdfkgrl sldaqeisql mhffqf
//
LOCUS       WP_008206687             402 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Roseobacter sp.
            SK209-2-6].
ACCESSION   WP_008206687
VERSION     WP_008206687.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. SK209-2-6
  ORGANISM  Roseobacter sp. SK209-2-6
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 402)
  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 402)
  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 402)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Roseobacter sp. SK209-2-6"
                     /db_xref="taxon:388739"
     Protein         1..402
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=42309
     Region          26..94
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          293..360
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mirrltlrka kehdaapapk sfddyelrlg dvmrgeratm gkslldvqre lrikasyiaa
       61 ienadptafd tpgfiagyvr syarylnmdp eaafdtfcre sgfevahgms aeassrrpep
      121 gpissggagl gsgafngsnv pfapaagsif sqidpraigs lavlaaliag igwggwsvlk
      181 evqqvqfapv eqtplvladv dplnsaqlge egaltanpal ealdrlyrpq aldvpvltar
      241 dapiatldps slgnfavpel psftlaeasi pdsgaslqaa vpqvveelak gvemlavrps
      301 wvqvtaadgs vifeaimnag qsftvpltee aprlrtgess aiyfavngah ygpvgdrgqv
      361 sknidlsvdg lkgrfqladl tdgrnqalat mvaelketpv se
//
LOCUS       WP_008207360             334 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Microcystis].
ACCESSION   WP_008207360
VERSION     WP_008207360.1
KEYWORDS    RefSeq.
SOURCE      Microcystis
  ORGANISM  Microcystis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Microcystaceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Microcystis"
                     /db_xref="taxon:1125"
     Protein         1..334
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=36964
     Region          1..333
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiiieqvsk qfgaftaldn inleiksnrl vallgpsgsg kttllraiag leppdtgkii
       61 ingkdtthln vrkrnigfvf qhyalfkhlt vrqniafglk irkaapdyiq krvdsllsli
      121 qlqglgdryp aqlsggqrqr valaralave pevllldepf galdakvrke lrvwlrqlhe
      181 evhvtsvfvt hdqeeameva deivifnegk ieqvgtpdqv ydhpasafvm sfigrvnvvp
      241 ptsaalfeql ggstngvkif irphdleils spngssiaak veriihlgwa idvelilpdr
      301 slliahlnre qldqlhlkvg eqvyvrprda rvfa
//
LOCUS       WP_008207735             198 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Roseobacter sp.
            SK209-2-6].
ACCESSION   WP_008207735
VERSION     WP_008207735.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. SK209-2-6
  ORGANISM  Roseobacter sp. SK209-2-6
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 198)
  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 198)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 198)
  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   4  (residues 1 to 198)
  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   5  (residues 1 to 198)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Roseobacter sp. SK209-2-6"
                     /db_xref="taxon:388739"
     Protein         1..198
                     /product="TRAP transporter small permease subunit"
                     /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=22624
     Region          5..197
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mprpilryir miealnrfig rfamylifal igvllwssvs ktffnpslwt letaqfimva
       61 yyilggpysm qmgsnvrmdl fyggwslrtk awvdaftvif lmfylgvlfy gavsstaysl
      121 gyfglepfaf fgelitilft egpttagekl gylersstvw rpylwpvkti lcfgvflmll
      181 qclaelfrdi grlrgvei
//
LOCUS       WP_008208410             146 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Rhodanobacter sp. FW021-MT20].
ACCESSION   WP_008208410
VERSION     WP_008208410.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter sp. FW021-MT20
  ORGANISM  Rhodanobacter sp. FW021-MT20
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Rhodanobacter sp. FW021-MT20"
                     /db_xref="taxon:1162282"
     Protein         1..146
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=15124
     Region          8..145
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 msntrssqgf tlielmivva iiailaaiai payqnylika qvsegmslad sakaavweyi
       61 sntgtfpasn ltaglpeeas isgsyvssvn vangritvaf anpkaniaiq nqvlvlspat
      121 tggsitwdcs thttlsgkyl psvcrk
//
LOCUS       WP_008209418             217 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Roseobacter sp.
            SK209-2-6].
ACCESSION   WP_008209418
VERSION     WP_008209418.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. SK209-2-6
  ORGANISM  Roseobacter sp. SK209-2-6
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 217)
  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 217)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 217)
  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   4  (residues 1 to 217)
  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   5  (residues 1 to 217)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Roseobacter sp. SK209-2-6"
                     /db_xref="taxon:388739"
     Protein         1..217
                     /product="TRAP transporter small permease subunit"
                     /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=23496
     Region          13..185
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 magsaavled gslisrldrk llqleqvfal lsglavfslm llavisvggr ntmnaplpgy
       61 vdwieqampl iafmgiayvq rdgghirmdi vigalrgrgl wlfelisvlm mlvlmlalvw
      121 gswahfersf dfsaplwsrd ssidiglpiw pakllapvaf svlvlrlflq vwgygralml
      181 gleapvavpl iqdaaeqaaa eaeqlsghdd daiggrr
//
LOCUS       WP_008209464             270 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Rhodanobacter sp. FW021-MT20].
ACCESSION   WP_008209464
VERSION     WP_008209464.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter sp. FW021-MT20
  ORGANISM  Rhodanobacter sp. FW021-MT20
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Rhodanobacter sp. FW021-MT20"
                     /db_xref="taxon:1162282"
     Protein         1..270
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=29161
     Region          41..188
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkptamrqil qipglvraat lllalallaa cthapprnpl atwvpspnhd irrpvlivlh
       61 ftnehsaqea ldtlrtrnsg gpvsahylig sdghiyqlva dqlrawhagp grwgtitdln
      121 sasigieldn dghtpfaqpq iasllrllad lttrlhippt qiighedlap grkddpgplf
      181 pwqqladagf grwpkgplcd ppagfdpwma lavvgypldd rpaavrsvhh hfrgmdgdtl
      241 daqdlrilyn laqqiepgpd tcaapapqsp
//
LOCUS       WP_008209527             404 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Roseobacter sp.
            SK209-2-6].
ACCESSION   WP_008209527
VERSION     WP_008209527.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. SK209-2-6
  ORGANISM  Roseobacter sp. SK209-2-6
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 404)
  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 404)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Roseobacter sp. SK209-2-6"
                     /db_xref="taxon:388739"
     Protein         1..404
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46307
     Region          1..397
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 malprlengl arrlfmdrha lleapsgpak gadlldlisr lgfvqldsin tvarahdvil
       61 yarrpsyrpk hltslydqgd tlfehwthda amipmefypr whlrfqrdea llrkrwrnwr
      121 rdgfeqqfet vlthvrdhgp vsssdvgkge kkgsggwwdw hpsktaleyl wrkgaltvvg
      181 rtgfqkrydl tervieevlr pphetldpaa tvdwlcnaal drlgfatsge laafwdtasa
      241 aeardwcrda lgrgelieie veaadgslrk hfarpdvveq aadlgtapgr mrvlspfdpm
      301 lrdrkraerl fgfhyrievf tpapkrkygy yvfpliegqr mvgridmkad rnadllrvta
      361 lwpergvkfs parikrleae lervarfagl aevdladewl repa
//
LOCUS       WP_008210645             219 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Rhodanobacter sp. FW021-MT20].
ACCESSION   WP_008210645
VERSION     WP_008210645.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter sp. FW021-MT20
  ORGANISM  Rhodanobacter sp. FW021-MT20
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Rhodanobacter sp. FW021-MT20"
                     /db_xref="taxon:1162282"
     Protein         1..219
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23694
     Region          110..175
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mflrllfvfl mtlniavgaw lllgqndalg rsatdpgvpe lqllseqapv apsatasvpa
       61 aapaapsesy acmtlgpfat pqdmrtarsa larqtvrera rqeqttelrg wwvhlptsgs
      121 raqalaeark leakhitdyf vvgsgdqqnt vslglfkdpa nahnrldqvv aagfpakltq
      181 rteqvpqywl dlvvadsahf nwrsrirdps vgshssgcf
//
LOCUS       WP_008211099             255 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein, partial [Rhodanobacter
            sp. FW021-MT20].
ACCESSION   WP_008211099
VERSION     WP_008211099.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter sp. FW021-MT20
  ORGANISM  Rhodanobacter sp. FW021-MT20
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Rhodanobacter sp. FW021-MT20"
                     /db_xref="taxon:1162282"
     Protein         1..>255
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          2..246
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mlgegivwcd raqalywtdi qagtlwrhap asgetqhwvl perlasfalc eadgwlllal
       61 asrlaffrla dgalhtvcev esglptrcnd gacdrqgrfv fgtlhepagr gpkqaiggfw
      121 rldadlslqr lplesvaisn slafspdggt lyycdsptri ircceygdtv gpsrnfvdlr
      181 gisgepdgsc vdadgglwna qwgmgrvvry hpdgredrvi pvparqptrp alggaaldtl
      241 yvtsardgld evala
//
LOCUS       WP_008211366             335 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Lentilactobacillus parafarraginis].
ACCESSION   WP_008211366
VERSION     WP_008211366.1
KEYWORDS    RefSeq.
SOURCE      Lentilactobacillus parafarraginis
  ORGANISM  Lentilactobacillus parafarraginis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lentilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Lentilactobacillus parafarraginis"
                     /db_xref="taxon:390842"
     Protein         1..335
                     /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=38296
     Region          2..289
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 makkriewid iakaygiiav vighalssgl tthviywwhm plffiiggff lkpinvqkls
       61 ewkkffnkri yrdlliyfma giglillysi lynkdwqylv nhwsrlivgg rtlnlytstf
      121 lfinvyllsi vavtglisvv khrwlqltiv sialflgtcy dkinwlhlyn fetmpwnadi
      181 vliaafftyi gylvfhtnyh wienpkvigm ivaamgalvv lylngqfdfq fsmkshlieg
      241 slpkvllvgt iplifsfgvm glsyltthfs ssfilatigq htmiimylhn alldmttmag
      301 idniatkvii avivpmlitl lkhpvirnrs lyldn
//
LOCUS       WP_008211898             414 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Rhodanobacter
            sp. FW021-MT20].
ACCESSION   WP_008211898
VERSION     WP_008211898.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter sp. FW021-MT20
  ORGANISM  Rhodanobacter sp. FW021-MT20
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 414)
  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 414)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Rhodanobacter sp. FW021-MT20"
                     /db_xref="taxon:1162282"
     Protein         1..414
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47116
     Region          2..397
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mlsvnqarcl qlaaqgllqp prrrakrtdv paivermrll qidtihvvar spylvlharl
       61 gdyppewlde alergrlaec waheacfvpa sdvalhrawr gqrdghwahr harrmrdeha
      121 admdallahi rangpvraad fersdrgasg wwewklekrw leawfasgel mvarrdrfqr
      181 vydmaervla rlnppldaad aglshedlrr rfildsvral gvararwiad yyrlkpgvtt
      241 relqpllasg ellavevagw tepgyvhadh aamlakacag rlrathtall spfdplvwdr
      301 arllamfdfd yriecyvpap krrygyyvlp ilhrgrlagr ldakahraeg vfevkslyle
      361 egvepdsrlv adfamaitrt arwhetpqvr lgrcrptala pllraalwda aetg
//
LOCUS       WP_008213685             408 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Rhodanobacter sp.
            FW021-MT20].
ACCESSION   WP_008213685
VERSION     WP_008213685.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter sp. FW021-MT20
  ORGANISM  Rhodanobacter sp. FW021-MT20
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 408)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 408)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Rhodanobacter sp. FW021-MT20"
                     /db_xref="taxon:1162282"
     Protein         1..408
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=46008
     Region          19..396
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mkikqlsvat pqgeagdiyr qsqyafnyst kdpsaavsll mplraasysg nqlppvfsms
       61 lpegflheri irrlakfeki ddmrllgitg qqtigrltyt ipgqtstgkp aeiglrrlls
      121 erasnemfeh lvdmyfdsgi sgaqpkvmlp dadkpmsdra tmlhsdlivk sggedyphls
      181 aneflcmdaa rragisvpef wltddsslfv mkrfdldgdk pmgfedmtvl mnlpreptgh
      241 ykytqsyeav trfirafcre naleslqrfy acfvlcvavr ngdahlknfg llyehpaaaa
      301 prlsplydvv ttaayddinv rtgqmqtdrt lalklnkstr ypnreqlvef gktfclvrsp
      361 ekvidrvcea mtdslsanrd rvddtffrrl qdewdrgres ispprapm
//
LOCUS       WP_008213725             184 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Lentilactobacillus parafarraginis].
ACCESSION   WP_008213725
VERSION     WP_008213725.1
KEYWORDS    RefSeq.
SOURCE      Lentilactobacillus parafarraginis
  ORGANISM  Lentilactobacillus parafarraginis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lentilactobacillus.
REFERENCE   1  (residues 1 to 184)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Lentilactobacillus parafarraginis"
                     /db_xref="taxon:390842"
     Protein         1..184
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=20821
     Region          1..>39
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
     Region          61..184
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(141..142,150,157..160,162)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mrkyiqlvvv fllavilsgc gndhadshhn gdkpktakvi nwkkssqnkp ypkittknar
       61 yilvslkkqr vyimspnnrv lytmyastgi hnstpkgtyh iqqehgnffy ngksregary
      121 wtswkdhgiy lfhtvptnak gqyikseaah lgkranshgc irlsipdakw inrtvpvgtk
      181 vkiv
//
LOCUS       WP_008214653             129 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Lentilactobacillus parafarraginis].
ACCESSION   WP_008214653
VERSION     WP_008214653.1
KEYWORDS    RefSeq.
SOURCE      Lentilactobacillus parafarraginis
  ORGANISM  Lentilactobacillus parafarraginis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lentilactobacillus.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 129)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Lentilactobacillus parafarraginis"
                     /db_xref="taxon:390842"
     Protein         1..129
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=14196
     Region          2..127
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(7..10,40..42,45,72,109,123)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 miklytdaav nqhsghaaig ilivkdgrqt qlkskissmn nhqaeffaai qgflalkkmg
       61 taanelifyy tdskivvdsl tksyakhfep qvtqllalqq aydtvvnqwi pdsqnhgahf
      121 lalqalhak
//
LOCUS       WP_008216105             725 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Vibrio chagasii].
ACCESSION   WP_008216105
VERSION     WP_008216105.1
KEYWORDS    RefSeq.
SOURCE      Vibrio chagasii
  ORGANISM  Vibrio chagasii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 725)
  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 725)
  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 725)
  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 725)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..725
                     /organism="Vibrio chagasii"
                     /db_xref="taxon:170679"
     Protein         1..725
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=77490
     Region          2..696
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 msdslqqelk kfelptrtdf pwvgkaittm gvilsllhiw fntlstlpel wisathftgf
       61 aiicalwypa hislkkskva lavdigiala alacliyipf aedalyergv kfiasdwffs
      121 ilaiaiviel irrtmgwfip vlilvclsyv vlwgqwtsgi fhfpglslet llyrsfysse
      181 gmfgsisris wtfvfmfilf gaflvrsgvg dyiidvsraa agkviggpgf iavigsglmg
      241 svsgssvant vstgvisipl mqkagfpsrf aagveaaast ggqlmppvmg agafimasyt
      301 qipyvdiiav sflpaliyfl svaffvriea krsgvqkvss gcepllkvll sgwhnlipla
      361 vlvtllvqgf tptyaagisi isvvvaswfs knhkmgpkai iealsqgakn mattavllvg
      421 iglvvnvist tgigntfslm inswangdll vmialialas lilgmglpvt aayivlgtls
      481 apalykliae sqlldllvsg qlpeqakaif mlaapeklel lnapmaleta kelialvpad
      541 fvetlleqsl gleaislall sahliifwls qdsnvtppvc ltafaaatia ktppmrtglm
      601 awkiakglyl vplliaytnl vswdvtsvlv tggfaiigty afiaaiegyl eseinlvlra
      661 vlialgvalv wpdvsivirl vgvalfvaif iysgrkydin qvkkpsdeeq eslpqtepdt
      721 vassl
//
LOCUS       WP_008216149             493 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Rhodanobacter sp. FW021-MT20].
ACCESSION   WP_008216149
VERSION     WP_008216149.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter sp. FW021-MT20
  ORGANISM  Rhodanobacter sp. FW021-MT20
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Rhodanobacter sp. FW021-MT20"
                     /db_xref="taxon:1162282"
     Protein         1..493
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=49865
     Region          <2..125
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          71..321
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mgsaskdlvk glagddqlfg lggddtlqgg dgddylaggg gsgtgsgadr leggagndtl
       61 sgedgndaml ggtgddsyvy gggqdtidnt gggydgvffn dgitasrlaf srdgddllit
      121 vdgdagstvr vakhflggdy aidyvqpasg smldtaaina laggssggdp dpgntgndgd
      181 ytnvvdgtaa geqllgtngr dlihglggnd tifgfggddk feggdgddyl sggngsfsgs
      241 gndiliggag vdtlvgedge dlliggtgnd kyvwqagsgs dvidntgggt dwlffngvar
      301 trlsfhrdgd dlvirvdgda aqqvrvqdhf kggdlaisyv qpsdgnaipa sqfgslltlm
      361 paasarqasa sgvssaivmd qpresgpvft qppaepwhad agghgnglda wndgthrrhp
      421 dlrrwhdawg ggvthgvqvn hevqqliqam arfgaaagge sslpdyaeqh hgfalgapgq
      481 lhgatmhrem sha
//
LOCUS       WP_008216314             943 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Rhodanobacter sp. FW021-MT20].
ACCESSION   WP_008216314
VERSION     WP_008216314.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter sp. FW021-MT20
  ORGANISM  Rhodanobacter sp. FW021-MT20
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
REFERENCE   1  (residues 1 to 943)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..943
                     /organism="Rhodanobacter sp. FW021-MT20"
                     /db_xref="taxon:1162282"
     Protein         1..943
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=106088
     Region          142..580
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 markptapkt iatlkhkeak rkniptaeyq svmqkedqtp vkvayartak glddekqsrn
       61 rdldpqlvwr gkdqqdwsdl vvnapplyiq ekvnpkvlid dlqresqaga qlqsgsmadl
      121 fgdfnglpeg adktdfyqyd gnwqnrmilg dslqvmasla ereglrgkvq ciyfdppygi
      181 kfnsnfqwst tsrdvkdgna ehitrepeqv kafrdtwrdg ihsyltylrd rltvardllt
      241 esgsifvqig denvhrvrav mdevfgdena iatipfkkts alggktldvv ydtilfyakd
      301 kekvkyrkql msvgydtyay pnvesvdgsw rrlssdergn fdpkfgrlfr tdnitsqsgg
      361 ektafpvtle gkllkpskgs fwktnergms vlakaerlka vgntltytry qddfparalt
      421 awwddtiqst faaknvyvvq tytkvvqrcl lmstdpgdlv ldptcgsgtt ayvaeqwgrr
      481 witldtsrva lalararimg arypyyllad spegqhkeae itrsvpssqp tygniahgfv
      541 yervphvtlk siannseidv iwdkfqqlle plreqlnkal gkhwqeweip readvkwpda
      601 tsklhadwwr ertarqreid asiaakadse ylydkpyedk kkvrvagpft veslsphrvl
      661 gvdendelid gvgddkpgyg derdfvqmil enlktagvqq ahkadkitft altpwpgdlv
      721 caearyvegn kekraaifig pefgtvsrpd lvaaareagd adfdvlitca fnydamssef
      781 dklgripvlk armnadlhma ddlkntgkgn lfvifgepdi aildagedge pgqirvkvng
      841 vdvfhpntge vrsdgaegia cwfidtdyne esffvrhayf lgandpyksl kttlkaeine
      901 eawatlnsdt srpfdkpksg riavkvinhl gdevmkvfrv sgt
//
LOCUS       WP_008222763             204 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Vibrio].
ACCESSION   WP_008222763
VERSION     WP_008222763.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 204)
  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 204)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 204)
  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 11459477
            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="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22019
     Region          1..202
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 melydseeqq veaikdwwke ngkavifgav iglgglfgwr yyqdsvvear eaasesyttv
       61 isaldakgvd aqsdiqafid ankdaeysvl aamqlakvqv qagelsaale qlewakaatk
      121 daalspllty rvarikaeqg efdaalsdla avtdeswkgr vaelrgdisl rkgdtdaays
      181 ayteaqqavd asqtlqikld dlak
//
LOCUS       WP_008225950             413 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Roseobacter sp.
            GAI101].
ACCESSION   WP_008225950
VERSION     WP_008225950.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. GAI101
  ORGANISM  Roseobacter sp. GAI101
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 413)
  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 413)
  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 413)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Roseobacter sp. GAI101"
                     /db_xref="taxon:391589"
     Protein         1..413
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44084
     Region          22..89
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          304..371
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 migrwssktv kneeaeaqgf dafelrlgdl mrgeratlgk slldvqrelr ikasyiaaie
       61 nsdpeafdtp gfiagyvrsy arylhmdpdk afdafcaesg fsvahgmsak asvikkptre
      121 ermnrspdsd mfnrpatpft pvgdsflsri epgalgsvlv lvglisaigf ggwsvlqevq
      181 rvqvtpvdet pvvlsdldpl qgalatspkt sgtdeifdnv atnpmtaprg dsldrlyrpa
      241 aldvpvliar dapiasidpr nsgtftagis avkvaavaqt gpvdvpsdvv avpqvvegma
      301 ptlrlvaayp swvriraadg kviyegimnk gdswdvpate epptlrtges galyfamdgq
      361 yfgpvgdrga vtsnlplhrq alaelyqpal ieensalatm vaelqnaaet pte
//
LOCUS       WP_008225786             257 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Roseobacter sp. GAI101].
ACCESSION   WP_008225786
VERSION     WP_008225786.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. GAI101
  ORGANISM  Roseobacter sp. GAI101
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 257)
  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 257)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Roseobacter sp. GAI101"
                     /db_xref="taxon:391589"
     Protein         1..257
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27510
     Region          1..256
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mkfsanlgfl ftdlslpdai raaksggfda vechfpydtp ppemkdalaq tglrmlgmnt
       61 wpgdraagdf glaalpdrvd earaeiarav dyaaaagvea vhvmagrtdg gpaaeecfra
      121 nlnhacdlaa ahglsvliep intrdvagyh lsgtahaeri vndlarpelk imfdcyhmqi
      181 mqgdlantle hllpkighiq iaavpdrgep dcgevdygwl lphltalgyq ghigaeyrpr
      241 agteaglgwm armrlaq
//
LOCUS       WP_008227227             224 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Roseobacter sp. GAI101].
ACCESSION   WP_008227227
VERSION     WP_008227227.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. GAI101
  ORGANISM  Roseobacter sp. GAI101
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Roseobacter sp. GAI101"
                     /db_xref="taxon:391589"
     Protein         1..224
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=24395
     Region          1..160
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mvtdviqhps pnfgprrdgl rpsfivvhyt amdnaaaald rlcdtqaevs ahylisakge
       61 vtqmvaedmr awhagqgewa glkdinsrsi gieldnrgth pfsepqmsal etllreimdr
      121 wdispagvig hsdmapgrkt dpgpkfdwar larqglaslg qtakgapear pdsymaaarq
      181 agftadadfd tllqatrlrf apwrtgplca adlnlchvlc skwk
//
LOCUS       WP_008227910             266 aa            linear   BCT 20-JAN-2025
DEFINITION  3-deoxy-manno-octulosonate cytidylyltransferase [Roseobacter sp.
            GAI101].
ACCESSION   WP_008227910
VERSION     WP_008227910.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. GAI101
  ORGANISM  Roseobacter sp. GAI101
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 266)
  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 266)
  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 10787365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Roseobacter sp. GAI101"
                     /db_xref="taxon:391589"
     Protein         1..266
                     /product="3-deoxy-manno-octulosonate cytidylyltransferase"
                     /EC_number="2.7.7.38"
                     /GO_function="GO:0008690 - 3-deoxy-manno-octulosonate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0033468 -
                     CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28764
     Region          1..259
                     /region_name="KdsB"
                     /note="CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell
                     wall/membrane/envelope biogenesis]; COG1212"
                     /db_xref="CDD:440825"
ORIGIN      
        1 msvlivipar yastrypakp lallkgsggt srslierswl aacevqgvdr vvvatdddri
       61 kdaaeafgae vvmtsvecan gtercaqahe vlgggydivv nlqgdapltp hwfveslvqg
      121 lksdpnagia tpvlrcdgai lnslladrka grvggttsvf atdhkalyfs kevipftskt
      181 yaedemtpvf hhvgvyayrp dalaaypawp vgpleqlegl eqlrfmengh tvlcvevdak
      241 drqfwelnnp edvlkieamm aqmgle
//
LOCUS       WP_008231065             410 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Roseobacter sp. CCS2].
ACCESSION   WP_008231065
VERSION     WP_008231065.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. CCS2
  ORGANISM  Roseobacter sp. CCS2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 410)
  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 410)
  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 410)
  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 410)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Roseobacter sp. CCS2"
                     /db_xref="taxon:391593"
     Protein         1..410
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=45483
     Region          24..391
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mmigdklsri srrdlfklag qygmsstlma agtfggamsl anlasaaest yerrfskeak
       61 ynlkfgasgf narnlliera galefardle artdgeirie figdnqicgq tscvektqqg
      121 itdifaastq nsaggapyln vldyaymfrn radqyhflys pasmrllrep yerrhglkfl
      181 fshaelrgiq mglnfddkpl vtsvedlagt knrvtgtqlg riamealnln pvpvaweetl
      241 dglkqglidg aetwasavay anmapvvsqs vhlnffcgte htamsasvfd slegylqdav
      301 mesaywaqth vqaanevali rtvgqsdpql pgtifaehgv rnaflspeei kkaeemcspe
      361 yqpalwedwr erlngwsggl dtyqeiydev rtisadtlpe nveprrwwkg
//
LOCUS       WP_008232155             183 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Roseobacter sp. CCS2].
ACCESSION   WP_008232155
VERSION     WP_008232155.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. CCS2
  ORGANISM  Roseobacter sp. CCS2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 183)
  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 183)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 183)
  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   4  (residues 1 to 183)
  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   5  (residues 1 to 183)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Roseobacter sp. CCS2"
                     /db_xref="taxon:391593"
     Protein         1..183
                     /product="TRAP transporter small permease subunit"
                     /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=20336
     Region          19..178
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mtekivdrlh ddpgadphsg vlgriinaig ivfaigills agilvieifl ryvvnaptiw
       61 ahetviflta safvygglyv varnthirvv liydylpkpi rryfdiaism tcflasgifa
      121 waawkgvera iwtpagdfrl etsgsawnpp tpgmlkvfll filivmtvqf liltiayfkk
      181 kdh
//
LOCUS       WP_008232904             398 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Roseobacter sp.
            CCS2].
ACCESSION   WP_008232904
VERSION     WP_008232904.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. CCS2
  ORGANISM  Roseobacter sp. CCS2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 398)
  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 398)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Roseobacter sp. CCS2"
                     /db_xref="taxon:391593"
     Protein         1..398
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45311
     Region          1..392
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 msvpvlynia arhvflakhg lasrpsgpgk gadlkgvidn lgfvqldsvn tfarahdlil
       61 wsrrqqfrpk alqhllhrdr qvfehwthda atipiesfah wrlrfardav rmeqrwkewr
      121 rgdfmakidd vlrqisddgc ctsgqvgtde srgsggwwdw hpsktaleyl wrsgqvsvvr
      181 rdgftkvydl tervipaehl nrhhheedti awccagaldr lgfatsgela afwdhvtpae
      241 akewcatala egriievdva cvhgklrrsf awpdlmdapi aapvpriril spfdpalrdr
      301 kraerlfgfs yrieifvpap krqygyyvfp vmegdrligr idmkredgvl avrafwpeag
      361 vrigsgrkaa lqkeltraaq fggcddlrfa pdwirpik
//
LOCUS       WP_008233131             574 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Roseobacter sp. CCS2].
ACCESSION   WP_008233131
VERSION     WP_008233131.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. CCS2
  ORGANISM  Roseobacter sp. CCS2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Roseobacter sp. CCS2"
                     /db_xref="taxon:391593"
     Protein         1..574
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=64606
     Region          9..513
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mmakkgklel twvgkddrpr lepriliedp eksyhaqerk segdifdnvl ikgdnllalk
       61 aleqdysglv kcvyidppfn tgnafehydd gvehsiwlnl mrerleilrr llrrdgflca
      121 hiddseghyl kvlldevfgr enyqttiylq vrypqktlkq dmsyhkqiem ihiyrnsfda
      181 kpwltpkssg ldkfnfyvst qgegkeielg gkktivfepg nykiekgeps vdgrkeiwat
      241 gsildgnssg rffrdyldgr vkedglgaly kvygigddkf dhrfftgpkk atatkgkyfq
      301 gvptsklena nsgnqpienf ldlagafgnc rheggvefrs gkkpevllqk ilthfsdend
      361 lildsfagsg ttaavahkmk rkwitveige hcethvmprl agiidgtdmt gasenldwkg
      421 gggfryytla pslietdrfg msiiskeyna amlaeamckh mgftyapstt dywnhgyste
      481 tdfiyvttqs lthdtlrkis advgkdrtll vcckaysgge nldnltihki psivldkcew
      541 grddyslnva nlpmaevdpd adlplftegg sdde
//
LOCUS       WP_008233329             351 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Roseobacter sp. CCS2].
ACCESSION   WP_008233329
VERSION     WP_008233329.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. CCS2
  ORGANISM  Roseobacter sp. CCS2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Roseobacter sp. CCS2"
                     /db_xref="taxon:391593"
     Protein         1..351
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36817
     Region          <35..187
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mdmtilllla asgvllipll seddddesdk nevrgtledd ipldgtdgdd lilgfdgndt
       61 inggagldfi naglgndtvn ggdgrdvieg ragddilngd dgndtilgga gdddinggfg
      121 sdiirggrga deifggfgar lldgelnnat drtdtlrgeg gedeiylwgg gglavggqns
      181 ddpgtgdekd vlvlvtgegr ledsegttdf falaniende etfaiitefd esehrmiltv
      241 didldgaaat pqvgfeatls tieegdetvn gflitaklln pddfpdaefe essaffrgea
      301 nttsddlqtf vqdnydievv ftdaadndyv dpettinain sqipdnppvp v
//
LOCUS       WP_008234068             697 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Roseobacter sp. CCS2].
ACCESSION   WP_008234068
VERSION     WP_008234068.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. CCS2
  ORGANISM  Roseobacter sp. CCS2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 697)
  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 697)
  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 697)
  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 697)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Roseobacter sp. CCS2"
                     /db_xref="taxon:391593"
     Protein         1..697
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=72009
     Region          8..695
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 msdetpveaa aqrdftgltn talsilcfli avghiyvafd pvisefqrna yhfagfafla
       61 avlnplikgq trskpilafd ltlgvlvaaa aiympfaeqg iydrgvkfsp ldwiaavici
      121 igaieltrrl tgwvipalii iaisyvgwwg qmiggvfsfp glswesiafr sifgddamfg
      181 tiarisstfv flfiifgafl lrsgagdfvi niaraiagrl vggpgivavi asgltgtisg
      241 savantastg vitiplmkka gfpskfaggv eaasstggql mppimgagaf vmasftqipy
      301 etivavaalp allyflsvvf fvriearrlr lqpmendget vgsafkkgga sfvipiggli
      361 amlvsgftpa yaavfgilav iasswltqnp mgpravfeal vmgtkgmimt avllcavglv
      421 vnviatagig ntfslmiadw aggnlliaiv mvaiaslvlg mglpvtaayi vlatlsapal
      481 agmisdrfvi ealaagtlgd agnavlmfgv pdpsvlvgpl ttedataiir alplevaapl
      541 rdlvvpqeva vaailsahmi ifwlsqdsnv tppvalaaft aaaiakapam atgfaswkla
      601 kglyivplmm aytpflsgdw gamlvifafg vigiyglaga lqgcmeapln pvtriiaglg
      661 gaaciwpapi mvhvggaavv illlavnarq lrqtaav
//
LOCUS       WP_008234541             397 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Roseobacter sp. CCS2].
ACCESSION   WP_008234541
VERSION     WP_008234541.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. CCS2
  ORGANISM  Roseobacter sp. CCS2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 397)
  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 397)
  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 397)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Roseobacter sp. CCS2"
                     /db_xref="taxon:391593"
     Protein         1..397
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=41428
     Region          26..92
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          291..356
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 migktfkrad asedvqaagf daydvrlgdl mrgeratmgk slldvqrelk ikaayiaaie
       61 nadpsafdtp gfiagyvrsy arylnmdpdd afeafcdesg fvtahgmsae asslkgksfd
      121 ptatplgkdi fsssatpfip ageavlssve praigsvvvl valicglgyg gwtvlqevqk
      181 vqfapveqtp vvlsdldpla gagnaiqpsd pladfnapsr qaldrlyrpq aldvpvlvar
      241 dapistlspg tigalvpdag vpvlpeltva dldlpappai qvvepdvpel qlvavrpawv
      301 rvrsadgtvi fegvmepgqn fvvpsteepa tlrvgesgam yfavngvhyg pvgpagvvts
      361 nvalttqslt etyavadlna dtdlaeivnv aevtage
//
LOCUS       WP_008235049             255 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Roseobacter sp. CCS2].
ACCESSION   WP_008235049
VERSION     WP_008235049.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. CCS2
  ORGANISM  Roseobacter sp. CCS2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 255)
  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 255)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Roseobacter sp. CCS2"
                     /db_xref="taxon:391593"
     Protein         1..255
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27231
     Region          1..255
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mkfsanlgfl wsdlslvdai haakaagfda vechwpydtp apdvaaalae tnlrmlglnt
       61 srgdvaagen glsalpgrea daraaidqal syadaigtpn vhvmagfaeg daalaafqan
      121 ltyaceqaaa ldvtiliepl nhydapgyfl tttdqarrii etvshtnlkl mfdcyhvqlm
      181 egcisrrlqa lapiighiqf asvpdrgppd dgelnysyif giisqlgwdv plgaeyrpkt
      241 gtnatlgwlh ragws
//
LOCUS       WP_008235062             338 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Richelia
            intracellularis].
ACCESSION   WP_008235062
VERSION     WP_008235062.1
KEYWORDS    RefSeq.
SOURCE      Richelia intracellularis
  ORGANISM  Richelia intracellularis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Richelia.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Richelia intracellularis"
                     /db_xref="taxon:1164990"
     Protein         1..338
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37716
     Region          1..333
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mgvivenlsk qfgnfqavkq vnleiksgsl vallgpsgsg kstllrliag levpdtgkiw
       61 ltgkdatyqs iqernigfvf qhyalfkhmt vkqniafgme irkapkakik lrveellnlv
      121 qlsglgdrfp sqlsggqrqr valaralave pkvllldepf galdakvrkd lrawlrrlhd
      181 evhvttvfvt hdqeeameis dkivvmnkgn veqigapaei ydhpatafvm sfigpvnilp
      241 stsrifqkhs fgsahtemfl rpqdviveks ptatsvparv krlihlgwei qaelylddgq
      301 evtahlsrek fdqlnlepkq rvyvkpkdak sfplyysi
//
LOCUS       WP_008235464             277 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Roseobacter sp. CCS2].
ACCESSION   WP_008235464
VERSION     WP_008235464.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. CCS2
  ORGANISM  Roseobacter sp. CCS2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Roseobacter sp. CCS2"
                     /db_xref="taxon:391593"
     Protein         1..277
                     /product="formate/nitrite transporter family protein"
                     /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=30189
     Region          26..272
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mthpnqtsne dedlikkteg laskhifeii rrdgeeeler pngslfwsgi aaglmislsv
       61 lgeaifrtyl pdaqwsylve nlgyslgflv vilgrmqlft entittvlpv mhnpvwsmfk
      121 rlvilwcivl lanvigafgv atafaygsfi pvelipaite lsehatgfga segfqraipa
      181 gilvaaivwm lpesdgfgff vilvftwlia agdfthivag svemaflmvq gmlpfsdalf
      241 gfflpvlagn ilggtvifal lafgqvrrel pegarkk
//
LOCUS       WP_008235853             820 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Roseobacter sp. CCS2].
ACCESSION   WP_008235853
VERSION     WP_008235853.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. CCS2
  ORGANISM  Roseobacter sp. CCS2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 820)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 820)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 820)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..820
                     /organism="Roseobacter sp. CCS2"
                     /db_xref="taxon:391593"
     Protein         1..820
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=90078
     Region          9..820
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 malifrwlvr lasalivlcv aaialvyyfa srslpdydan sdvagiaapv eivrdnanvp
       61 hifaqtdedv yfalgyahaq drlwqmtmlr rtaqgrlsel fgertvgide vlrrfdlytl
      121 svssvdaqtd eanayleays sgvnawlnev nngalgrgap emwlfnhaia pwqpadsial
      181 lklmaldlts sledevlrar tsllldndrl rdilpddptg giaalpeyas lvpgvapytp
      241 nmrlaydpls pikpgplrga snawaasasr attgstllan dphlgltaps iwylarlele
      301 tggviggtip gmplilsgrs dqlgwgvtta kvddvdivve evnpdnpeey rspngwvpfr
      361 trdsiinvkd ssavtlrlrw tangpvmprd tynlgtitpp ghvtaiswta lsdrdttmsa
      421 afalnhartv eeaitagdaf iapaqnltla drnriamktv gaipardanh qsqgrlpafg
      481 ylaenrwqgr fpysenpefl dppggilgnt nnktvdrpfp rhvthkwgdt qrinrwrrlm
      541 qarevhtrds fieaqldtvs ftartlstlm gadlwftgna apdgtperqr qialnllsaw
      601 ngemnehlpe pliysawvra fqqrlirdel gplaeefthi epvfiervfr didgasawcd
      661 viqsapietc tdiarqaldd allwiaenhg daveavrwgd ahvathdhpv lgntpilewv
      721 vnirqstsgg dhtlqrakts gvdphpfhnv hsgayrgvyd fadpdssvfi tstgqsghpl
      781 srhydnlgel wrrgeyipms ldpdlaraaa vgvtvltpae
//
LOCUS       WP_008236310             275 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Roseobacter sp. CCS2].
ACCESSION   WP_008236310
VERSION     WP_008236310.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. CCS2
  ORGANISM  Roseobacter sp. CCS2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 275)
  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 275)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Roseobacter sp. CCS2"
                     /db_xref="taxon:391593"
     Protein         1..275
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29138
     Region          3..274
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mtlvtlkdvl qpalrdgyav gglvclgwed mrayvaaaea encpvilqag pgcrahtplp
       61 vlgkmfrhla eeatvpvvah ldhgytydec sealdagfts lmfdgsrkpl vdniketlqi
      121 vemahrsgis cegeigfvgy sggeesagtd pgeaaqfaae tgvdamaisv gnvhlqqdke
      181 ggldepriaa iqamtsvplv ihggsgvpia qrnhlakntn ickfnigtel rmafgaamrd
      241 avnsdperfd rvsilkethd pvmaaartvl rnlkg
//
LOCUS       WP_008236337             740 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Roseobacter sp. CCS2].
ACCESSION   WP_008236337
VERSION     WP_008236337.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. CCS2
  ORGANISM  Roseobacter sp. CCS2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 740)
  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 740)
  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 740)
  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 740)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Roseobacter sp. CCS2"
                     /db_xref="taxon:391593"
     Protein         1..740
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=78468
     Region          164..736
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mttdktlddq tegpviaegv deepvehnrr iftgraylvi aamsafyalf hmaalngwsi
       61 rgwtgvdipf lpvfpmetwn friihiagal ilgftlysar afpdkdadkn svldylayaa
      121 llpaiyacyt afgfaaqird gvmwngmdag irnaeiyhyg ypliiatiag ivlgwmrprv
      181 rgtiapadlv lsvcgiavaa ylitifgtlm rnstgtqfap igmsiaavag salimeltrr
      241 vaglaliiia gvfltyvfvg dllpgflnap ditwqrffsq vytdagilgp ttavsstyii
      301 lfiifaaflq askvgdyfvn fafacagrar ggpakvaifa sglmgmingt sagnvvatgs
      361 ltiplmkkvg ykpttagave aaastggqim ppimgagafi maeitgipye diaiaaiipa
      421 vlyfvsiyfm vdfeaaklnm rgmredelpk fkdlvrrvfl flpiiiliaa lfmgysvira
      481 gtlatasaav vswftpyrmg irsvskafel agimsiqiia vcacagiivg visltgvgar
      541 fssvllniae anqllalffa mciaillgmg mpttaayava asvvapglvq lgipmltahf
      601 fvfyfavvsa itppvalasy aaagisgsnp matsvasfki gisafivpfm ffyngailmd
      661 gtwfevirag itavfgvfll ssgvqgwwvg draawpiria lllvalfmie ggwmsdligi
      721 agavglyvva qitkpkvaaq
//
LOCUS       WP_008237487             811 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pedobacter sp. BAL39].
ACCESSION   WP_008237487
VERSION     WP_008237487.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. BAL39
  ORGANISM  Pedobacter sp. BAL39
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 811)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 811)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 811)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..811
                     /organism="Pedobacter sp. BAL39"
                     /db_xref="taxon:391596"
     Protein         1..811
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=91463
     Region          54..811
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mnkikaficl lipillayag ntkfgdlppi vkflnpftgf wqnaerntik akkslvlkgt
       61 kekvsiafdd rmiphifakn dhdlyfaqgy vtamhrlwqm dfqtryaagr lsevvgkkai
      121 evdryqrrmg mvygaeqslk gmmadpksre milaytagin ayihrlspak lpveyklldf
      181 tpedwtpikc alllkqmsav lamgsdefym snirkkfgta vvkdlfpdyp fkedpiipig
      241 tswdfkplai peapvivekp giadvstkqk edgigsnnwa lsgaktrsgy pilandphld
      301 lslpsiwyqi qlhapgvnay gvslpgapgi iigfnndiaw gvtnvaadvl dfyqikfkdd
      361 shqnywynnk wnktrsrvek ikirgtstel dtvfythhgp vvylekpeky taanniptgs
      421 alrwiaheqs nelktfylln rshnyadyrk alisytapaq nfvfaskdnd iaitangkfp
      481 lkwkdqgkfv ldgadpkndw rgwipaeqnp tvknpsrnfv ssanqsstdp sypyyinwef
      541 saydrgkrin drlsvmtkat adsirlmqsd sysifaqnil ptissmidin glnatqkeaf
      601 ritsewnkfy eatalgatif elwakrltdn iwkdefdvag ipmrypsrdr tvqlilheqq
      661 skwidniktp vkeslsdlvn eafkytcdsl erkygaigks wawanvkntn irhlaripgl
      721 gsntlmiggg kmtinalgeh ngpswrmvve lgkkpkghgv ypggqsgnpg srfydnmidt
      781 wangqlydly fmqsaddasa kiisqltisk k
//
LOCUS       WP_008238298             158 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Pedobacter sp. BAL39].
ACCESSION   WP_008238298
VERSION     WP_008238298.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. BAL39
  ORGANISM  Pedobacter sp. BAL39
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 158)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Pedobacter sp. BAL39"
                     /db_xref="taxon:391596"
     Protein         1..158
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16878
     Region          9..156
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 maedlnivtd vskevqyqti ipqiealiag epdlianlan vaaalkqqfg wfwvgfylvk
       61 gdelvlgpfq gpvactrikk grgvcgsswe qaatlvvpdv dqfpghiaca sasrseivvp
      121 vvkdgivigv ldvdseylsh fdavddiyln eivalvhg
//
LOCUS       WP_008239765             542 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Imtechella halotolerans].
ACCESSION   WP_008239765
VERSION     WP_008239765.1
KEYWORDS    RefSeq.
SOURCE      Imtechella halotolerans
  ORGANISM  Imtechella halotolerans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Imtechella.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Imtechella halotolerans"
                     /db_xref="taxon:1165090"
     Protein         1..542
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=58632
     Region          5..542
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mtinkkilqi npkdnvvval dtlikgsvva fndisievme dipvkhkmal etitsgatiy
       61 mygvpvgial iaiekggllt vdnvkhsaap ykfggmnysy svdvatkwke atfdgyyrnd
      121 gqvgtanfwi fiplvfcqnr nllvlkeafe telgykkenh hkvklrnlmt gkdsesyese
      181 geltaqrwfp nidgikflth eggcggtrdd akslvrllag yiknpnvaga tvlslgcqha
      241 qvsmlqealk elqietvkpv yyfeqqhyes esimlnevve ttyeglkian knirkpapls
      301 kliiglecgg sdgfsgitan pliglisdri nalggksils efpelcgveq dlidrclskh
      361 eaerfislme synkkaesvg sgfdmnpspg nirdglitda iksagaatkg grstinavld
      421 ygeyvnntgl hllctpgndv esttglagsg anlilfstgl gtptgnpicp vlkissnsvl
      481 permkdiidf dagkiisagi smdtladqlm nliievssgr kqtkaaslgq ddfipwkrgv
      541 sl
//
LOCUS       WP_008240070             409 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Imtechella
            halotolerans].
ACCESSION   WP_008240070
VERSION     WP_008240070.1
KEYWORDS    RefSeq.
SOURCE      Imtechella halotolerans
  ORGANISM  Imtechella halotolerans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Imtechella.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 409)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 409)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Imtechella halotolerans"
                     /db_xref="taxon:1165090"
     Protein         1..409
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=45867
     Region          5..408
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mkyasinelk vglnfdgdii pvgrlalrdy riyfeydqnf igrgleispl klpleaglqv
       61 fdyrpfeglp gvfndslpdg wgrllfdryv rslhllpqef tpldrlthig stglgalvye
      121 pdhsevnkqi eeinldllsq qtqeildgda edvlkvlinl ngssagarpk aligfnkvmn
      181 riisgkhnlp enyehwivkf anssdgvdag aieyvyalma keagvemmpv nlfeaskgag
      241 yfatkrfdri gnqrfhmhta sgllhsdfra psldyvdlit ltgiltkdir evekmyrlav
      301 fnvlshnrdd hsknfsflmd aegiwklspa ydltfssgpr gqqstmvmge gqfptidhlv
      361 klgieahlkr dkidaviqqt knalnqweil atnhgvtkan ikliksric
//
LOCUS       WP_008240675             395 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Imtechella halotolerans].
ACCESSION   WP_008240675
VERSION     WP_008240675.1
KEYWORDS    RefSeq.
SOURCE      Imtechella halotolerans
  ORGANISM  Imtechella halotolerans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Imtechella.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Imtechella halotolerans"
                     /db_xref="taxon:1165090"
     Protein         1..395
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43350
     Region          3..393
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mtnilvinsg sssikfqlis mpkeevtasg lverigleda mlhyqsekhq isekriipdh
       61 siglqmiakl lmdkeygviq nvddipyvgh rvvhggstfs dtivideavk qkikdlfsla
      121 plhnppnyvg iqvaetifrn atqvavfdta fhqsipqkay tyaipksfld dfkirmygfh
      181 gtshkyvstk amqylnnpka kiisvhlgng csitavkdgk sidhslgfgp vnglimgtrs
      241 gdidqsvify lieklgytsa qvsellhkks gmlgltgfsd lrdieanaan gntdcqlale
      301 mnayrikkyi gsyaaamngv daivftagig ensstlramv csdmeylgve ldpdkntlrd
      361 kvvrsihkds akvqvlvipt neeleiaqqv fklcl
//
LOCUS       WP_008241445             418 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Imtechella halotolerans].
ACCESSION   WP_008241445
VERSION     WP_008241445.1
KEYWORDS    RefSeq.
SOURCE      Imtechella halotolerans
  ORGANISM  Imtechella halotolerans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Imtechella.
REFERENCE   1  (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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Imtechella halotolerans"
                     /db_xref="taxon:1165090"
     Protein         1..418
                     /product="amidohydrolase family protein"
                     /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=46260
     Region          24..418
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mnylsvigyv mmamlsfkgy sqsktpqeki rilkngyiiq ltsdnasvkk gslviegdki
       61 keilyeevse iadadiidit gkyvlpglvd ahvhlatvpk eernennqym eqqldkmlfa
      121 gittvrdmag naiilgdykr avslgqvkgp diyhaamfag pgyfemtrrf psgkrspkdt
      181 pweqtitdtt tislaiarak gagvsgikiy sdlskelvqk iteeaklqgl qawahaaifp
      241 aspmdiaqsk vhsmshafdi vygldkkgpi tredkvtpid tkkldlllqv mkenniilda
      301 tnyiaennkl yigtvitkra kefgvkvavg tdwpylmede ipfykelrll veksgftmae
      361 alwsatqigt esigltdrgs ikegkradfl itnenplegl sqlkdvhlvv kagvvykk
//
LOCUS       WP_008241916             108 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Pedobacter sp. BAL39].
ACCESSION   WP_008241916
VERSION     WP_008241916.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. BAL39
  ORGANISM  Pedobacter sp. BAL39
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Pedobacter sp. BAL39"
                     /db_xref="taxon:391596"
     Protein         1..108
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11833
     Region          1..104
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(5..6,24..25,33,36,38..39,41,44..45,47,56,61,68)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(24,56..57,59,85)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 meqsfydqvf elvrlipkgr vssygaiars lgaggsarmv gyamsnagla hpkvpahrvv
       61 nssglltgrf hfsdpndmer llaeegvrvk ndkvvdfkkl mwdplqel
//
LOCUS       WP_008242116             406 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Pedobacter sp. BAL39].
ACCESSION   WP_008242116
VERSION     WP_008242116.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. BAL39
  ORGANISM  Pedobacter sp. BAL39
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 406)
  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 406)
  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
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 406)
  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   5  (residues 1 to 406)
  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   6  (residues 1 to 406)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 406)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 406)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Pedobacter sp. BAL39"
                     /db_xref="taxon:391596"
     Protein         1..406
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44705
     Region          22..66
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          87..399
                     /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 mrttffddhd knitgvaykn ihikktiily fadkgnttit elckelnlsv pkvttlvldl
       61 iadglvkdfg ktgstggrrp niyglapdsv fflgvdvkyn hinigltdlr kkliriskgv
      121 pydlqnseas lkelcrliln fiketgvpke kilgiglnms grinyltgys ynffhfneep
      181 lnkvienelg lktylendsr amaygefnsg avedeknvlf lnldyglgmg mminkeiyyg
      241 ksgfsgelgh iplfnnelic rcgkkgclet easgmamvrm fkesisngss sslkkgpnde
      301 iqmeeiidaa nnddvlciel mekigynlgr giallinifn peliilggal attgeylhlp
      361 iksalnklsl slanndtqir isslgedagv igacllarkr lledtl
//
LOCUS       WP_008242729             322 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pedobacter sp. BAL39].
ACCESSION   WP_008242729
VERSION     WP_008242729.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. BAL39
  ORGANISM  Pedobacter sp. BAL39
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
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
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Pedobacter sp. BAL39"
                     /db_xref="taxon:391596"
     Protein         1..322
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=36009
     Region          1..252
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mielsnvsky fgsakavdgv sfsvnegenl vllgtsgcgk tttlkminrl inpdngaisi
       61 kgkdiqqenp etlrrsigyv mqniglfphy tiyeniatvp kllkwdtnkt rprvmelmkk
      121 lhlpeelldr fpaelsggqm qrvglaralv adpplllmde pfgaldnvtr ssiqaefkql
      181 dellrktiim vthdvqeafe ladriclmdk gkimqigtps allhqpandf srkfldgqrl
      241 alefrvstlk diwpymrakq tgiqrdqpda peeelhrtlg lpgntsvwta lelakanaqt
      301 nkvsftalmd gftqyqkavr he
//
LOCUS       WP_008243056             795 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Sulfurovum sp. AR].
ACCESSION   WP_008243056
VERSION     WP_008243056.1
KEYWORDS    RefSeq.
SOURCE      Sulfurovum sp. AR
  ORGANISM  Sulfurovum sp. AR
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurovaceae; Sulfurovum.
REFERENCE   1  (residues 1 to 795)
  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 795)
  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 795)
  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   4  (residues 1 to 795)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..795
                     /organism="Sulfurovum sp. AR"
                     /db_xref="taxon:1165841"
     Protein         1..795
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89497
     Region          1..794
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mikplatdkl ynhcdlalfd fntteelkdp neiigqdral kaisfgigik kegynlyamg
       61 rvgsgkhtvv ekfiqsqakd ekkpgdwcyv nnfedsrkpi ylklessmgv qlkkdmeeli
      121 eelqtvipsl feseeyriqk qaiidkltda kekslrevkr rakeenifin yttagytlap
      181 mshdgkvlak eeyqalstqd kdqiqekilk frnelenivq divieskiqq keirelerkm
      241 tkkavdtsin elkrkyqdye kvvaylesve ediidnsqdf lisaqnslam mganyakqsg
      301 ifnryhvnvi vahkdqegap iiyednptyt nlfgeiehia qmgtlltdfn likagalhka
      361 nggylildas kvlmqpfvwe glkrmlrsse irieplarsl slistlslep etieldikiv
      421 ligdrflyyl lynydpefre lfkinadfen etdrndeniq lyarmigmia kdngllpldk
      481 qavgkvieys srmaedsqkl tthlgglsdl lheadfiasq edmdhiskaq idqaimekie
      541 rsdrikdkmy eaiqrgtili etegsaigqi ngvavldlgn fsfghpskit altrlgkggv
      601 iniereakls gpthdkgimi lssylaatya kdfplsitat lvfeqsygki dgdsascael
      661 fallsslsev aldqsiavtg svnqngqvqa vgginekieg ffdvcnlvks kkhhgiiipa
      721 snvkhlmlke evleavkenr fkiyaiesvd egleiltgkk sgtkdanghf pkesinylve
      781 eklklfanks kqkki
//
LOCUS       WP_008243296             293 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Pedobacter sp. BAL39].
ACCESSION   WP_008243296
VERSION     WP_008243296.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. BAL39
  ORGANISM  Pedobacter sp. BAL39
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 293)
  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 293)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Pedobacter sp. BAL39"
                     /db_xref="taxon:391596"
     Protein         1..293
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32469
     Region          45..293
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mskelsrrta lknivagtaa lgvsatlpsf alesspstml kgnvnhsvcr wcfgdidldt
       61 lcieakkigi kaidlvgpad whilkkhgly ssmcngaein ledgwndpqf hptliknyse
      121 mipkvaaagy tqlicfsgsr rgkddetgwk ncvdglkqvi giaekhnvvl vmellnskvd
      181 hkdyqcdtta wgaelakrlg senfkllydi yhmqidegnv inninkyhqy ishyhtagvp
      241 grneiddtqe lfypaiirav latgfkgyla qefipkykdk ikslsdavki cdv
//
LOCUS       WP_008243343             303 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Sulfurovum sp. AR].
ACCESSION   WP_008243343
VERSION     WP_008243343.1
KEYWORDS    RefSeq.
SOURCE      Sulfurovum sp. AR
  ORGANISM  Sulfurovum sp. AR
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurovaceae; Sulfurovum.
REFERENCE   1  (residues 1 to 303)
  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 11465564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Sulfurovum sp. AR"
                     /db_xref="taxon:1165841"
     Protein         1..303
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=34682
     Region          <45..102
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          158..301
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mpfikilftl ftlismanak nyfkthddmc dgtqtiqctn dfntvrnlqi alnrdkhinv
       61 klkvdgrwge ktkeaviafq tyyglthtdg wvgketkskl dkisknikfp kdkqvkhvkl
      121 mkynnyadfr khtnlrksys iyedkkllsk angrntklkv diseqrirly vndkvalcap
      181 cttgakrkle pntgiirnqs tpkgtfcike kiadkrstif gkmyrgkklv ykgdrrkykg
      241 kkakyvgasl knwmrltsgg iglhaskyvk rypgsngcir lpykvsktif nkvrkgtpvs
      301 ivn
//
LOCUS       WP_008244866             242 aa            linear   BCT 20-JAN-2025
DEFINITION  3-deoxy-manno-octulosonate cytidylyltransferase [Pedobacter sp.
            BAL39].
ACCESSION   WP_008244866
VERSION     WP_008244866.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. BAL39
  ORGANISM  Pedobacter sp. BAL39
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
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   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 10118537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Pedobacter sp. BAL39"
                     /db_xref="taxon:391596"
     Protein         1..242
                     /product="3-deoxy-manno-octulosonate cytidylyltransferase"
                     /EC_number="2.7.7.38"
                     /GO_function="GO:0008690 - 3-deoxy-manno-octulosonate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0033468 -
                     CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=26962
     Region          2..237
                     /region_name="CMP-KDO-Synthetase"
                     /note="CMP-KDO synthetase catalyzes the activation of KDO
                     which is an essential component of the lipopolysaccharide;
                     cd02517"
                     /db_xref="CDD:133010"
     Site            order(8..10,49,76,96,98)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133010"
     Site            order(120,137,143..145,151..152,154..160,168,194..195,
                     198..200,207..210)
                     /site_type="active"
                     /note="oligomer interface [active]"
                     /db_xref="CDD:133010"
ORIGIN      
        1 msyivvipar ykstrfpgkp ltdingksml lrtyeqcmka vdpslvyvat edqrivdhce
       61 sfgiqvllts ddcltgtdri aevadlvkad yyinvqgdep lfnpediskv islldtysgd
      121 ilngycaidn dhqyrsvsvp kvvfrpdgrl lymsrsaipg nkavafvkaw rqvciyafpf
      181 ealkafaasn gktpleaeed ieilrflelg yevrmlelss esvavdnped lgevlarlne
      241 ve
//
LOCUS       WP_008245369             279 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Sulfurovum sp. AR].
ACCESSION   WP_008245369
VERSION     WP_008245369.1
KEYWORDS    RefSeq.
SOURCE      Sulfurovum sp. AR
  ORGANISM  Sulfurovum sp. AR
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurovaceae; Sulfurovum.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Sulfurovum sp. AR"
                     /db_xref="taxon:1165841"
     Protein         1..279
                     /product="formate/nitrite transporter family protein"
                     /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=29878
     Region          2..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msylaptefv kkmvdsgesk vymstkdtli raymagaila laavfaitva mktgsglvga
       61 affpvgfiml ylmsfdlltg vfvlvplawi dkrpgvtvgq ilrnwglvgl gnlggaltva
      121 vmmafiftyg fdtdggaiaq kvagigeart lgyqehgisg wftvfirgml cnwmvamgvv
      181 gamisttvsg kaiamwmpim lfffmgfehs ivnmflfpfs limggdftvv dyllwnevpv
      241 algnltggll ftgltlyath vktgakrelr ikskdasaa
//
LOCUS       WP_008248732             369 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Zhongshania
            aliphaticivorans].
ACCESSION   WP_008248732
VERSION     WP_008248732.1
KEYWORDS    RefSeq.
SOURCE      Zhongshania aliphaticivorans
  ORGANISM  Zhongshania aliphaticivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Spongiibacteraceae; Zhongshania.
REFERENCE   1  (residues 1 to 369)
  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 369)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 369)
  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   4  (residues 1 to 369)
  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 369)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Zhongshania aliphaticivorans"
                     /db_xref="taxon:1470434"
     Protein         1..369
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41237
     Region          26..227
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <171..357
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          273..354
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtdinrlhdi pvkkfqrlld ylehvgidsk tiaqqaglda kkllsapeqg tlpgykysal
       61 yenaaeamqe mdiavpwgag igsdvfrfmc ysiincqnle ealnraaryq kmlypitgyk
      121 itvntsadit elryefnsdf sksqftpksw drnehsdava kasglrvwfa figwltarel
      181 qltgltisap avseayttsm asllgitpkf naehtalffn ssalrartvh tptsleaflq
      241 havyslitqd srpastsaai rsllansgtg slpsfeamae dlhmspsslr rrlhsedtsy
      301 qelkdqyrcd iamrqlrnpm lkiheigeql gflesssfir sfrnwagltp kqfrdqlddi
      361 dqaksttsd
//
LOCUS       WP_008248919             225 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Zhongshania aliphaticivorans].
ACCESSION   WP_008248919
VERSION     WP_008248919.1
KEYWORDS    RefSeq.
SOURCE      Zhongshania aliphaticivorans
  ORGANISM  Zhongshania aliphaticivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Spongiibacteraceae; Zhongshania.
REFERENCE   1  (residues 1 to 225)
  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 225)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 225)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Zhongshania aliphaticivorans"
                     /db_xref="taxon:1470434"
     Protein         1..225
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=24332
     Region          1..214
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 metfrteeeq veaikrwwqe ngkstvfgia lalaivfgwk gwqghvkdqg aeasaifdnl
       61 miadaavqrd gtsrntaehl antlkdqygn lsygqfaaly kakyavqdge ydaaaselew
      121 vldqgpepvl maqtqlrlaq vrfalddyaa alalledvas sgyaaqaael rgdilfaqgd
      181 kpgalsayqq akvlareqev psnnalldlk isdlsvaatt ekgtn
//
LOCUS       WP_008248763             337 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Zhongshania
            aliphaticivorans].
ACCESSION   WP_008248763
VERSION     WP_008248763.1
KEYWORDS    RefSeq.
SOURCE      Zhongshania aliphaticivorans
  ORGANISM  Zhongshania aliphaticivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Spongiibacteraceae; Zhongshania.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 337)
  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   6  (residues 1 to 337)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Zhongshania aliphaticivorans"
                     /db_xref="taxon:1470434"
     Protein         1..337
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37567
     Region          22..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          88..336
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mrtptvckdy ldnllaylga qgvsarqlqs vlrldpldhl seqgrvplrl feltldagas
       61 llndpclgah agtdcsrtpw gmvdylgmsa ansreavdam qrysrllidh gdmvlseins
      121 etaclswllp arkqasrhvv efffanwyrv nkpmldkgat rrevhfahsg ggreqqmadl
      181 feapvkfgkk vnavhfgral ldqptlyphp aiyksleqaa riemsnlqye vrlikevrdc
      241 iidqladgvp rledisaqlg igtrtlqrrl nstatsyksl vdatrrersl rlmsqselal
      301 ldisaalgfs dqsafqkafk rwygqapgrf railqag
//
LOCUS       WP_008248941             341 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Zhongshania
            aliphaticivorans].
ACCESSION   WP_008248941
VERSION     WP_008248941.1
KEYWORDS    RefSeq.
SOURCE      Zhongshania aliphaticivorans
  ORGANISM  Zhongshania aliphaticivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Spongiibacteraceae; Zhongshania.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 341)
  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   6  (residues 1 to 341)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Zhongshania aliphaticivorans"
                     /db_xref="taxon:1470434"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38132
     Region          30..210
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <222..341
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mpvsdlpaas eravnssafk alfqaaealg aditalftem gvtlseleds drrypvsdlf
       61 rlyelvahkv aspdiglyig ridyvnrlnl qlyacsactt freylnvmps vlrivgdige
      121 vkvrregefi rldwqplape saaqrylsds slsvaaaivn svcvrpipir aahfsyaepa
      181 dldllkqqfg dclrfdqpts cvyldracld yalikldanw vqalaqpiry lfednsnnnd
      241 fvlavrktll rllpsgdmni draaealgis rrtlqrrlaa qgtqflqvlq elraelaiqy
      301 lgderlsitd iafllgymdq ssfsgafrsw hgqsprdyrk q
//
LOCUS       WP_008249374             351 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Zhongshania
            aliphaticivorans].
ACCESSION   WP_008249374
VERSION     WP_008249374.1
KEYWORDS    RefSeq.
SOURCE      Zhongshania aliphaticivorans
  ORGANISM  Zhongshania aliphaticivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Spongiibacteraceae; Zhongshania.
REFERENCE   1  (residues 1 to 351)
  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 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   3  (residues 1 to 351)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 351)
  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   5  (residues 1 to 351)
  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   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Zhongshania aliphaticivorans"
                     /db_xref="taxon:1470434"
     Protein         1..351
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39458
     Region          50..215
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <187..343
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mdleavptrf acsllnlaae rgyehhsiln iagiafnpln krspgyqtti samqysklyq
       61 qvvslvqdea fglmlgknlt pgafrmmcyc liscenlgna ikraceffrt fydadaqiyl
      121 dtrkdsaivg ygsvkkgfag lqvdvadiyg lsiwhrffcw lvgsnielke vrfagqapvg
      181 karvakyqql fgcpvyygql rdefvfdtry lsyplvhner tlkdflraap yplmvmsgsr
      241 ddgslvarvr amighdfsqg fpsferitaa lnmsaptlrr rlkkegttfq qlkdecrrda
      301 amaylgnsel sinavaalmg ftdpsafhrc fkkwtamtpg eyrvneresh s
//
LOCUS       WP_008249506             343 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Limnobacter].
ACCESSION   WP_008249506
VERSION     WP_008249506.1
KEYWORDS    RefSeq.
SOURCE      unclassified Limnobacter
  ORGANISM  unclassified Limnobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Limnobacter.
REFERENCE   1  (residues 1 to 343)
  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 343)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 343)
  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   4  (residues 1 to 343)
  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 343)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="unclassified Limnobacter"
                     /db_xref="taxon:2630203"
     Protein         1..343
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37296
     Region          31..206
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          260..341
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mnnkasnpts ntptalaswm rglarelehq gcdaralfne agldfallda pearypvpqt
       61 tllwqkavaa tgdetlgika irhitpatfh avglsvmase tleqafgrmr rfvdlvtdas
      121 eiellsthde fivelklreg ahpahqstdg flcllanagk glgdpslvpq rvelsrpapq
      181 annldffeks faaplefgcn tmrivyelsm vrtrlkganp liaehldqas qaaierlkpa
      241 ssvskkvrtw vvnhltqgap sieeaaaymn msarnlqrkl adegtnlasi vdeirqseat
      301 rrlkqsqdsl taialdlgfs dasafsrack rwfgkspsdi rgg
//
LOCUS       WP_008231412             371 aa            linear   BCT 20-JAN-2025
DEFINITION  ferrochelatase [Richelia intracellularis].
ACCESSION   WP_008231412
VERSION     WP_008231412.1
KEYWORDS    RefSeq.
SOURCE      Richelia intracellularis
  ORGANISM  Richelia intracellularis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Richelia.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ferreira,G.C.
  TITLE     Ferrochelatase
  JOURNAL   Int J Biochem Cell Biol 31 (10), 995-1000 (1999)
   PUBMED   10582332
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Ferreira,G.C., Franco,R., Lloyd,S.G., Moura,I., Moura,J.J. and
            Huynh,B.H.
  TITLE     Structure and function of ferrochelatase
  JOURNAL   J Bioenerg Biomembr 27 (2), 221-229 (1995)
   PUBMED   7592569
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Taketani,S.
  TITLE     Molecular and genetic characterization of ferrochelatase
  JOURNAL   Tohoku J Exp Med 171 (1), 1-20 (1993)
   PUBMED   8122254
REFERENCE   4  (residues 1 to 371)
  AUTHORS   Cole,S.P. and Marks,G.S.
  TITLE     Ferrochelatase and N-alkylated porphyrins
  JOURNAL   Mol Cell Biochem 64 (2), 127-137 (1984)
   PUBMED   6390167
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Richelia intracellularis"
                     /db_xref="taxon:1164990"
     Protein         1..371
                     /product="ferrochelatase"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0004325 - ferrochelatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42025
     Region          21..349
                     /region_name="HemH"
                     /note="Protoheme ferro-lyase (ferrochelatase) [Coenzyme
                     transport and metabolism]; COG0276"
                     /db_xref="CDD:440045"
ORIGIN      
        1 mvaisktvek gsehlsnqdn vavllmgyge vesyndfasy neqalnllta kfapvpawvy
       61 pplakllalf drhewghthh dfisphnaif erqragieen lqakwgnkvk vfkafnfcap
      121 flpsqvlaei kaqgfeklli ypllvvdsif tsgiaieqvn qalvnindge chwvkslryi
      181 psffnepdyi nliaqlveek insslvnnyi pseigiilmn hgcphkakgf tsgitesqvl
      241 ydsvreklin ryplisigwl nhdtpliewt qpnvtqaarn liqlgakvii fmpigfaten
      301 hetlldvdhi ihylekqyte vnyiqmscvn dnskflamat rwtenhieal fstkgitvna
      361 snnnhyhkhd h
//
LOCUS       WP_008249820             275 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Zhongshania aliphaticivorans].
ACCESSION   WP_008249820
VERSION     WP_008249820.1
KEYWORDS    RefSeq.
SOURCE      Zhongshania aliphaticivorans
  ORGANISM  Zhongshania aliphaticivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Spongiibacteraceae; Zhongshania.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Zhongshania aliphaticivorans"
                     /db_xref="taxon:1470434"
     Protein         1..275
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29406
     Region          1..272
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mivdlhthtt asdgglsple lvqrarergv qllaitdhdt vagfaalkde agagmqllag
       61 ielsctwsgv nihvlglgid tmapafvsel egqrsardsr aqligqrldk lgfvgsyeaa
      121 aelaagraig rpdfarflva eghvssmaaa fdkylgsgkl gdikavwpdl gevvswirda
      181 ggvavmahpl qykmtnaklr rmlaefkevg geglevcngk psnqdlaylr qlcqqfelea
      241 sagsdfhhps swselgcdak iiapckavwd rwctq
//
LOCUS       WP_008249846             729 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Limnobacter sp. MED105].
ACCESSION   WP_008249846
VERSION     WP_008249846.1
KEYWORDS    RefSeq.
SOURCE      Limnobacter sp. MED105
  ORGANISM  Limnobacter sp. MED105
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Limnobacter.
REFERENCE   1  (residues 1 to 729)
  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 729)
  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 729)
  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 729)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Limnobacter sp. MED105"
                     /db_xref="taxon:391597"
     Protein         1..729
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=77020
     Region          87..718
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mttpssaart aeedrliaqg vddeplannq rtftqkaalf vsiisaayaf whvfslnvap
       61 vetwafrilh vagalvigfi aysssttehp argnqnliki lagilalpil yslymvfems
      121 qiiangemis pelevnhfgi plavgtfiai vasmflrpag nkfnwldatl vlaviastay
      181 lmvhldgtam rmragtpfas pgnawaalvg ialileltrr vagtalviis vifviysfvg
      241 pylpgflthd gftfsrffsy mytdagvlga ttavsstyii lfivfaaflq askvgdyfvn
      301 fafaaagrsr ggpakvavfa sglmgmingt sagnvvatgs ltiplmkkvg yngktagaie
      361 aaastggqim ppimgagafi maeitgipys eiaiaaiipa vlyflstylm vdfeaaklgm
      421 rgmrsdelpq fskmvkqvyl fipiiiliva lfmgysvira gtlataaaav vswlspfkmg
      481 pksifkafdl agvmsiqiit vcacagiivg vialtgvgar fssilldiae nsqlialffa
      541 mciaillgmg mpttaayava asvvapglie lgiqplvahf fvfyfavisa itppvalasy
      601 aaagisganp matsftsfki gltafivpfm ffynaallme gewfvilraf vtacigvffl
      661 aaaiqgwfwg ahsnwvvrgi lliaalcmie gglytdigga vlavvaivln kffkgkpape
      721 pmvqtkgmd
//
LOCUS       WP_008250009             629 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Limnobacter sp. MED105].
ACCESSION   WP_008250009
VERSION     WP_008250009.1
KEYWORDS    RefSeq.
SOURCE      Limnobacter sp. MED105
  ORGANISM  Limnobacter sp. MED105
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Limnobacter.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 629)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 629)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 629)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 629)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 629)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Limnobacter sp. MED105"
                     /db_xref="taxon:391597"
     Protein         1..629
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68045
     Region          1..629
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mnkpeskdkt kaglaaltlg aigvvygdig tsplytvkev fgensgvpln penltgaisv
       61 ifwalmlvvt lkyvililka dnhgegggla ltalaseavr knpklktlll ligvfgatlf
      121 ygdsvitpai svlgameglt litptltpyi iplsvlilig lfavqrygts vvgrffgpii
      181 vlwfatlgav gvanilsape ilyalnpvhg iqfildrgwg lfaafgaivl altgaealya
      241 dmghfgkkpi rmawtflvfp clalnylgqg alliadpgai enpfyrsfpd awvipvlcla
      301 tmaaiiasqa visgaysmsk qaiqlgflpr mkiqytsake sgqiympavn wlllagvlla
      361 vlmfqnssnl agaygiavtl tmlitttlty fvirhswglp awlsvgatif fvlidlllvi
      421 scafklfdgg wfpivlglal fvvmstwwrg rkllmksiqk dgidlndflp tlnvdqinra
      481 yrtavypvad pgkvpmallh nlkhnqvlha snviltvvfe svpwvseasr vevkslsrgf
      541 wqvtvrygfm ntpdipkale ltdevglkis lfettyflsr etvvptagsg mvkwreqlfa
      601 tmsrnaggvv dffrlpsnav velgtrvqi
//
LOCUS       WP_008250148             280 aa            linear   BCT 20-JAN-2025
DEFINITION  phosphonate ABC transporter ATP-binding protein [Limnobacter sp.
            MED105].
ACCESSION   WP_008250148
VERSION     WP_008250148.1
KEYWORDS    RefSeq.
SOURCE      Limnobacter sp. MED105
  ORGANISM  Limnobacter sp. MED105
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Limnobacter.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
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   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Limnobacter sp. MED105"
                     /db_xref="taxon:391597"
     Protein         1..280
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=30580
     Region          3..253
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mklqiqdida chpsaptggi paikrmslti qageqvalig psgagkttll qvlactlkpl
       61 ngefkvnnqs pwalskrklq klrgnlivap qvpplpprqr vitsvlagkl pamgllqsik
      121 slfypvdipa ahsalskldl pekifervdr lsggerqrvg larlfvspaq lwlvdeplsa
      181 ldptrarqam saltesaten gitlvctlhq vdmalaffkr ivglrngqie fdlpteqvtp
      241 amlktlysqy ehellgqvdr eliekqfekm tpavvvnncr
//
LOCUS       WP_008250569             207 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [unclassified Limnobacter].
ACCESSION   WP_008250569
VERSION     WP_008250569.1
KEYWORDS    RefSeq.
SOURCE      unclassified Limnobacter
  ORGANISM  unclassified Limnobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Limnobacter.
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   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   3  (residues 1 to 207)
  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   4  (residues 1 to 207)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 207)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 207)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="unclassified Limnobacter"
                     /db_xref="taxon:2630203"
     Protein         1..207
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22791
     Region          12..204
                     /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"
ORIGIN      
        1 mvnsktgkaa tpplkvllvd eepgraaile ralldagyvl vsrlssadrl vehvavsqpd
       61 ivivdidspd rdclenmavl srsnpkpvim fsdednedti asaikagvsa yvadgmnpdr
      121 vrpivqvava rfrefqalkn elqktrdqla drklidkakg llmkhrnfne deayhamrkl
      181 amernqrlvd tarnvievfe mlggggl
//
LOCUS       WP_008250941             339 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Haliea sp.].
ACCESSION   WP_008250941
VERSION     WP_008250941.1
KEYWORDS    RefSeq.
SOURCE      Haliea sp.
  ORGANISM  Haliea sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Halieaceae; Haliea.
REFERENCE   1  (residues 1 to 339)
  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 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 339)
  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   4  (residues 1 to 339)
  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 339)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Haliea sp."
                     /db_xref="taxon:1932666"
     Protein         1..339
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37650
     Region          25..207
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          256..332
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msdstsatti asytmaihma leanghdaaa vfkaaglsda psqdpldryt taqmaalfre
       61 avkstgnpaf glvaarflhp snvhalgyal lasatlrdac erlvyyfria snqgsyriee
      121 segrfclvle vvadgvafet idawnafiir vfrmiyrpdf kplsvrltrp lpegyvdlyt
      181 rsfhvpvtfd apdcticlds aivdlpllgg nreiasehdk ilqnyiaald aedivnrvkr
      241 vilrklpsen ctkqhvasel amspsalqqk laaketsfqd llnqvrksla ldymeqsris
      301 itemsfmlgf ndtssftraf rrwtgksprd yrrekgvep
//
LOCUS       WP_008251105             754 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Limnobacter sp. MED105].
ACCESSION   WP_008251105
VERSION     WP_008251105.1
KEYWORDS    RefSeq.
SOURCE      Limnobacter sp. MED105
  ORGANISM  Limnobacter sp. MED105
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Limnobacter.
REFERENCE   1  (residues 1 to 754)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 754)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="Limnobacter sp. MED105"
                     /db_xref="taxon:391597"
     Protein         1..754
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=82299
     Region          22..700
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 msklikswrk iagkafrigv gfsftavall hvlgfapsev vkrldylvyd vrlraeaqlp
       61 eldprivivd ideqslsevg rwpwsrdvva klvveltdrl gaaavgfdiv faepqqsdal
      121 laldtiienk palgsqlqem rsgiqaqfdr daqlaqvlad rpvvlgyyln qdatalsgal
      181 ppalfkksql gelsldstsw qgyggnipvl qknaeggyfn pivdedgtvr sipliaqfnd
      241 ayyqsfalgt lrralgnpqv ipvfpegvpd dygavelial rspeveldip verglltrvh
      301 frakggpnag gyryvsaadv lagalkpedi egrivligtt apglldlrst pvnpaypgve
      361 vhanvisgml dsiyklrpey sqgllfitvl avgfvlsvmm pilsatwsll valavlvasv
      421 ainsvlyfqa glvlpvavvl llvlaifmfd vaygylaesr skrqmvdlfg eyvapelvse
      481 masdptrysm egesreltvl fsdvrgftti seslqpnelr eyineyltvm seiirshrgt
      541 ldkyigdaim afwgapiada ehaelatkaa iamqeeavrl nerllarnwp tlaigvgvnt
      601 gqmrvgdmgs kirraytvmg davnlgsrle gitktygvgv ivgpqtkaav pgmvfqelda
      661 vkvkgknepv siyaplgert vltqasldql eqwnrflkaf raqqwlpare qlaglqgslv
      721 tnptlhalye nriayfelnp ppdnwdgvtq fdtk
//
LOCUS       WP_008251395             338 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Zhongshania
            aliphaticivorans].
ACCESSION   WP_008251395
VERSION     WP_008251395.1
KEYWORDS    RefSeq.
SOURCE      Zhongshania aliphaticivorans
  ORGANISM  Zhongshania aliphaticivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Spongiibacteraceae; Zhongshania.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 338)
  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   5  (residues 1 to 338)
  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   6  (residues 1 to 338)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Zhongshania aliphaticivorans"
                     /db_xref="taxon:1470434"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37893
     Region          22..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          101..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkpkyhsakt ilaplnklre egisvgqalt gtglslsiln kpeqhvslsq elmflrnlrk
       61 atanpaiglk vgacyplslf giygyalmsa atvrdalkla yeyvelsfaf fehshsfhgs
      121 hvvmnmssnd ygsddiamln eremlatlmi lrglmgddfr lhsatlrsaa sapvseyeky
      181 fqcpvsfnae dnalifpael ldipvlqcds dtaslcierc erlkarltee ynivdevrel
      241 illrpgyfps ieeisskfnm sgrtlrrklt mqgvgyqkil ddlrfelsre ylyttnisve
      301 qmsillgysd sahfshafrr wagtspsdfr safiaesr
//
LOCUS       WP_008251425             700 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Limnobacter sp. MED105].
ACCESSION   WP_008251425
VERSION     WP_008251425.1
KEYWORDS    RefSeq.
SOURCE      Limnobacter sp. MED105
  ORGANISM  Limnobacter sp. MED105
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Limnobacter.
REFERENCE   1  (residues 1 to 700)
  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 700)
  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 700)
  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 700)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Limnobacter sp. MED105"
                     /db_xref="taxon:391597"
     Protein         1..700
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=73836
     Region          27..691
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 msntpdsavt teansgfhdp tsagftrsfe grllfwiavl fstfqiataa hlfdlpsqvq
       61 rachvgflll ltfpliamkk hvalkaiawv lalaalgvag yqwveyepll iragdpteld
      121 iylgviaiat vfvatwllmg palpiicgtf fayclfgqyl papfdhrgyd fhqviehmay
      181 gtegiygipt yvsasyiflf ilfgafleka gmiklftdfa lglvghaqgg aakvavvssa
      241 lmgtisgsgv anvvttgqft iplmkkfgyr aafaggvest asmggqlmpp vmgavafima
      301 etlgvaysei vkaaiipail yffgafwmvh leagkhglkg ldkkdlpspl kavkeqwylv
      361 iplvalvwll vggytplfag tvglaftvvl ilgasiaigl pntvirvlfw iglgvvcaaf
      421 lqfgiwviag tiialiavna mkkggretla acrdsladga ksalpvgvac amvgiiigtm
      481 tltgaantfg qfvvsvgens lflslvltmi tcivlgmgip tipnyiitss iagpaleqlg
      541 vplivshmfv fyfgiladlt ppvalacfaa apiakerglt ismeavkiaa agfvipfmav
      601 ytpslmlqdg gplaesigyi paviyivvkt vlaislwgaa vigylgaklp vwlrvlgmig
      661 sftliaalpi tdeigfaiav vfgylawrnm ravkgklqpa
//
LOCUS       WP_008251466             145 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Zhongshania aliphaticivorans].
ACCESSION   WP_008251466
VERSION     WP_008251466.1
KEYWORDS    RefSeq.
SOURCE      Zhongshania aliphaticivorans
  ORGANISM  Zhongshania aliphaticivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Spongiibacteraceae; Zhongshania.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Zhongshania aliphaticivorans"
                     /db_xref="taxon:1470434"
     Protein         1..145
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15282
     Region          1..143
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkrnlgftlv elmitvaiig ilasiaypsy qeqiaksrrn eatnalfssa qaleryysan
       61 gryttasggt alpavfvsrv pdsgtafyti aataaanntf tlkatrsgpm vgdacgnftl
      121 netgqlalld kpsgssktva dcwrr
//
LOCUS       WP_008252185             245 aa            linear   BCT 20-JAN-2025
DEFINITION  phosphonate ABC transporter ATP-binding protein [Limnobacter sp.
            MED105].
ACCESSION   WP_008252185
VERSION     WP_008252185.1
KEYWORDS    RefSeq.
SOURCE      Limnobacter sp. MED105
  ORGANISM  Limnobacter sp. MED105
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Limnobacter.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
REFERENCE   2  (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   3  (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   4  (residues 1 to 245)
  AUTHORS   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Limnobacter sp. MED105"
                     /db_xref="taxon:391597"
     Protein         1..245
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=26671
     Region          5..244
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mssniidiqn lemviagrri lkveslqiar gekvailgrn gagkstllrc lngfvkptag
       61 hivvnqhtvf plrrerdlrp vraqvgqvlq glhlvarlsa menvlvggla rmprlrswar
      121 iftteetqra qaalkavgma hlsekradkl sggerqkvai armlmqqpel vladeptaal
      181 dptaadevce llvkatenst litvvhnvsl vpmlshrvig lkagevvldc asheltqaql
      241 dhlye
//
LOCUS       WP_008252870             172 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Limnobacter sp. MED105].
ACCESSION   WP_008252870
VERSION     WP_008252870.1
KEYWORDS    RefSeq.
SOURCE      Limnobacter sp. MED105
  ORGANISM  Limnobacter sp. MED105
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Limnobacter.
REFERENCE   1  (residues 1 to 172)
  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 172)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 172)
  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   4  (residues 1 to 172)
  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   5  (residues 1 to 172)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Limnobacter sp. MED105"
                     /db_xref="taxon:391597"
     Protein         1..172
                     /product="TRAP transporter small permease subunit"
                     /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=18899
     Region          4..170
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mkgllviscg idrlntwlgl tvgwfilltt lvsaynavvr kvfdtssngl leiqwylfga
       61 vfllgaaytl qqnahvridv lsnrfsestr awvdilghvl ftlpligfvl vsgwdfayes
      121 frineysadp gglirwpaka livvgfallg lqvcseiikk iavlqghptp cq
//
LOCUS       WP_008253236             232 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein, partial [Limnobacter sp. MED105].
ACCESSION   WP_008253236
VERSION     WP_008253236.1
KEYWORDS    RefSeq.
SOURCE      Limnobacter sp. MED105
  ORGANISM  Limnobacter sp. MED105
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Limnobacter.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Limnobacter sp. MED105"
                     /db_xref="taxon:391597"
     Protein         1..>232
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          21..>232
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mstaaplsan qldwsdphli nadlhchstv sdgtlepeel aaraaangvq iwsltdhdev
       61 sglaraaraa aehnlifipg veisvtwsav tlhivglnvq yensplekgl asvrngrter
      121 aiemsrqlek vgiegvyega lkyvgnpnli srthfarclv erkvcadire vferfltpgk
      181 pgyvphewas lkqavdwild snglpviahp grydlkpmqm delveqfvkm gg
//
LOCUS       WP_008253846              92 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Mycobacterium].
ACCESSION   WP_008253846
VERSION     WP_008253846.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium
  ORGANISM  Mycobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 92)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 92)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Mycobacterium"
                     /db_xref="taxon:1763"
     Protein         1..92
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=9319
     Region          12..92
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mgqspaqetg isvtvryfaa aqaaagveae tlvvrpgttv gelverlaah gsrlatvlsr
       61 csylcdgvav rdettalrsg dtidvlppfs gg
//
LOCUS       WP_008254433             215 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Mycobacterium].
ACCESSION   WP_008254433
VERSION     WP_008254433.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium
  ORGANISM  Mycobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Mycobacterium"
                     /db_xref="taxon:1763"
     Protein         1..215
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24001
     Region          19..205
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 meidylltat psarksldld advdlgdire clriglqaan gsnaqswrwl viadpalrak
       61 iaelyreayl rrvggqllad lmpagtpesr vmsstewlve nmarvpllvi pcyeayvpri
      121 dgdesfhlat lygsifppvw nfqlalhtrg ygtcittlhl hheeevrkll gipqtyvqgc
      181 llpvgrlrag rtfrpaprrp vedvvardrw dgpal
//
LOCUS       WP_008256332             318 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 5'-3' exonuclease [Mycobacterium].
ACCESSION   WP_008256332
VERSION     WP_008256332.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium
  ORGANISM  Mycobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Mycobacterium"
                     /db_xref="taxon:1763"
     Protein         1..318
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33487
     Region          1..309
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mpgplvlldg asmwfrsyfg vpssitapdg rpvnavrgfi dsvafvitqq rpsrlvvcld
       61 ldwrpqfrvd lvpsykahrv aepeppgepd ieevpddltp qidmiaelld afgiptagae
      121 gfeaddvlgt laarerddpv vvvsgdrdlm qvvsddpvpv rvlylgrgls katlfgpaev
      181 aehygvpver agpayaelal lrgdpsdglp gvpgvgekta asllaqhgsl eqilaaahdp
      241 kskmpkglra kllgaldyie aagdvvrvat dahvtfstas delplvaadp qrtaklatel
      301 gvgssvarlq kaldalpt
//
LOCUS       WP_008256532             231 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: aminoglycoside phosphotransferase family protein
            [Mycobacterium].
ACCESSION   WP_008256532
VERSION     WP_008256532.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium
  ORGANISM  Mycobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae.
REFERENCE   1  (residues 1 to 231)
  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   2  (residues 1 to 231)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Mycobacterium"
                     /db_xref="taxon:1763"
     Protein         1..231
                     /product="aminoglycoside 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=26042
     Region          4..200
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 milqrfvldw irdepwapan evlilgllad tsvpapkvia adphgqdtgv ptvlmtalpg
       61 avvwdppeld pwldavidvm mtihaipapq qlrrwepypp enapptwtry rwaweravtt
      121 yhdvrpssdr vflhrdfhpg nilwqqgkis glvdwvssca gpvqediahf rvnlamhhgq
      181 avadrflrhw mhasgqfeyh ptwdlltavs mggdepnhql defiaaaanr l
//
LOCUS       WP_008256807             209 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Mycobacterium].
ACCESSION   WP_008256807
VERSION     WP_008256807.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium
  ORGANISM  Mycobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Mycobacterium"
                     /db_xref="taxon:1763"
     Protein         1..209
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22776
     Region          6..201
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdiatvdell sttrsvrkrl dltrpvgrdv ileciqlamq aptasntqdw rwlvitdpdk
       61 raaiaeiyrs igaqylayaa dnatdpqtqr vyqsamslte tlgqvpvhvi pclnqridta
      121 epgiaaaawa siipagwsfl lalrsrglgs vwttmhlfke revaellgip ptvtqaalfp
      181 vaytigtdfr paarppaati tfwdgwgeg
//
LOCUS       WP_008256926             367 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Mycobacterium].
ACCESSION   WP_008256926
VERSION     WP_008256926.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium
  ORGANISM  Mycobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Mycobacterium"
                     /db_xref="taxon:1763"
     Protein         1..367
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38494
     Region          5..362
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mselqlravv adrqvdvefs vsagevlavl gpngagkstv lhviagllrp dhgtvrlgdr
       61 vltdtaagid vpthdrrvgl llqdallfph mtvaanvafg phnrraslrp gratqkataa
      121 rwlrevdaer ladrkprqls ggqaqrvaia ralaaepdvl lldeplagld vaaaaairav
      181 lravvtrsgc aailvthdll dvftladrvl vlesgkvaei gpvpdvltap rshfaariag
      241 vnlvngtvdr dgslvahggd rwyaaaperg elvspeqhai avfpptvvav yrdrphgspr
      301 navevtvaem dvrgsavlvr gaqqpdgapg laaeitadag aelrlapgdr vwfsvkahev
      361 tlypaah
//
LOCUS       WP_008257686             204 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Mycobacterium].
ACCESSION   WP_008257686
VERSION     WP_008257686.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium
  ORGANISM  Mycobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae.
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   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   3  (residues 1 to 204)
  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   4  (residues 1 to 204)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 204)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 204)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Mycobacterium"
                     /db_xref="taxon:1763"
     Protein         1..204
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22608
     Region          13..204
                     /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"
ORIGIN      
        1 mtgpttdtda avprrvliae dealirldla emlreegyei vgeagdgqea velaerhrpd
       61 lvimdvkmpr rdgidaasei askriapivv ltafsqrdlv erardagama ylvkpftisd
      121 lipaielavs rfgeiaeler evaslsdrle trklverakg llqteqgmte peafkwiqra
      181 amdrrttmkr vaevvletld ppke
//
LOCUS       WP_008259666             103 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Mycobacterium].
ACCESSION   WP_008259666
VERSION     WP_008259666.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium
  ORGANISM  Mycobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Mycobacterium"
                     /db_xref="taxon:1763"
     Protein         1..103
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11016
     Region          5..99
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(27,55..56,58,80)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(27..28,36,38,40..41,43,46..47,55,60,65)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mapvtddqve rvralvaaip sgrvatygdi asvaglsspr ivgwimrtds sdlpwhrvit
       61 asgrparhlt trqlellrae gvlardgria lgevryefpg gvl
//
LOCUS       WP_008260966             171 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Mycobacterium].
ACCESSION   WP_008260966
VERSION     WP_008260966.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium
  ORGANISM  Mycobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Mycobacterium"
                     /db_xref="taxon:1763"
     Protein         1..171
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18704
     Region          5..166
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdawdaicar rnvreyqpra isdedldria eagwrapsak nrqpwdfviv tdraqlqels
       61 tvwrgaghia aapaaiaiva pvppderrvv tdnydigqat mammiaatdl gigtghssvg
      121 dqekarailg vpddhlvafl lgvgypadrp lrpirtpnrr pfsevvhhgr w
//
LOCUS       WP_008261733             419 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: DNA polymerase domain-containing protein
            [Mycobacterium].
ACCESSION   WP_008261733
VERSION     WP_008261733.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium
  ORGANISM  Mycobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Zhu,H., Nandakumar,J., Aniukwu,J., Wang,L.K., Glickman,M.S.,
            Lima,C.D. and Shuman,S.
  TITLE     Atomic structure and nonhomologous end-joining function of the
            polymerase component of bacterial DNA ligase D
  JOURNAL   Proc Natl Acad Sci U S A 103 (6), 1711-1716 (2006)
   PUBMED   16446439
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Zhu,H. and Shuman,S.
  TITLE     A primer-dependent polymerase function of pseudomonas aeruginosa
            ATP-dependent DNA ligase (LigD)
  JOURNAL   J Biol Chem 280 (1), 418-427 (2005)
   PUBMED   15520014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Mycobacterium"
                     /db_xref="taxon:1763"
     Protein         1..419
                     /product="DNA polymerase domain-containing protein"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=46809
     Region          1..305
                     /region_name="LigD"
                     /note="Eukaryotic-type DNA primase [Replication,
                     recombination and repair]; COG3285"
                     /db_xref="CDD:442515"
ORIGIN      
        1 mtrpvlleva grevtvthpd kvvfpradgh ktsgpytkld lvryylsvad galrgvagrp
       61 milkrfvkgi teeavfqkra pakrpdwvdv aelryargts aaeavirdaa glawainlgc
      121 vdlnphpvla ddldhpdelr vdldpmpgvs wrrivdvalv arevledygl tpwpktsgsr
      181 gfhiyariar rwefrqvrla aqtvarever rvpeaatsrw wkeeregvfv dfnqnakdrt
      241 vasaysvrat pdarvstplh wdevagcrpe aftidtvpar faeigdpweg mddavgdldr
      301 llvlaeemgp perapkgsgk rdkgtggrrq ssmplieiar tktkdeamaa ldtwrdrhpa
      361 aaerlqpvdv lvdgmrgpss iwyririnlq hvpedqrppq eeliadyspw anyggkqqp
//
LOCUS       WP_008263133             364 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Mycobacterium].
ACCESSION   WP_008263133
VERSION     WP_008263133.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium
  ORGANISM  Mycobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae.
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   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   4  (residues 1 to 364)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Mycobacterium"
                     /db_xref="taxon:1763"
     Protein         1..364
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=38595
     Region          1..299
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mitfdevskv fgdgtaavdr lnldvpsgkl tvfvgssgsg kttalrminr mieptsgtia
       61 idgvdvatrd pvklrlgigy viqhaglmph qrvidnvatv pvlrgqsrra arkagyevle
      121 rvgldvklar rypaqlsgge qqrvgvaral aadppillmd epfsavdpvv rhelqneilr
      181 lqsdlhktiv fvthdideal rlgervavfk ggslqqydep arllsrpand fvsrfiglgr
      241 gyrwlqrlda aglplhdvar itpetlsgtg lsddwavvvd gggaplgwid aegarrhrdg
      301 aplsdcmsga gslfrprgnl sqaldaalss psgvgiavdd ggkviggvla advlaavesq
      361 rgsr
//
LOCUS       WP_008263543              82 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Brevundimonas].
ACCESSION   WP_008263543
VERSION     WP_008263543.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas
  ORGANISM  Brevundimonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae.
REFERENCE   1  (residues 1 to 82)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 82)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 82)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 82)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Brevundimonas"
                     /db_xref="taxon:41275"
     Protein         1..82
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8804
     Region          1..82
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mtrilyfgrv aeklgtegal elpaegltvr eirrrladqd evaadalirs dvrasvdqvi
       61 agedalarpd qeiaffsifs gg
//
LOCUS       WP_008264086             756 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Brevundimonas].
ACCESSION   WP_008264086
VERSION     WP_008264086.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas
  ORGANISM  Brevundimonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae.
REFERENCE   1  (residues 1 to 756)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 756)
  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   3  (residues 1 to 756)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..756
                     /organism="Brevundimonas"
                     /db_xref="taxon:41275"
     Protein         1..756
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=80027
     Region          1..750
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdafeaikat ffqecdella elesklmlle qgqtdletin avfravhsvk ggagafglea
       61 lvrfahvfet lmdelragrk pcdtvtiktl lrasdvladh iqaaqglapp vdeersaglv
      121 helellthgg eappvveede ddfgfvpmaf dvpldeplps lgepeavaae aqtgwrilfk
      181 phgrmygsan eaglllrelg rlgpitvsve dsalptldvl vaedgyltwt idltaaieek
      241 vvrevfdfve adcdltispl gggsepvlvf eeeppavlpa sdeldiaall akaagdapav
      301 eqptpdavap apaleavapa pvpapaapap apapvaaapa paapippaqv aapvapapvt
      361 irvdldrvdr linvvgelvi qqamlsqrvl esglarssgi algledlell treiqdsvma
      421 iraqpvksvf qrmprlvrev admvskqvrl vtagedtevd ktvverlaep ithmlrnaid
      481 hgletpderi aagktaegtv rlaalhrsgr ivieisddgr ginrervkki aidkglvapd
      541 aaltdeqidn liflpgfsta avvsdisgrg vgmdvvkrsi qalggrisis svpgkgstft
      601 lslpltlavl dgmvvsaadq iliaplpaiv esltpqegdl hyvggvdpvi rfrdrflpli
      661 dvamtmgfrd tpvvpsegva vvveteggqq aallfdaiqg qrqvviksle tnyqqvegia
      721 aatilgdgrv alildvdvlv tdmrrrssrp dfklas
//
LOCUS       WP_008265014             747 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor family protein
            [Stenotrophomonas].
ACCESSION   WP_008265014
VERSION     WP_008265014.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 747)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..747
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=81438
     Region          24..747
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mpshaplrrn llallvcasl pslaaaetap atdaqsattl dsisvigrge arqvqrvtae
       61 dmkvlppgan plkllatkpg vhfesadatg ayewsttisl rgfnqnrlgy tldgiplgnm
      121 aygnsnglhi sravisenlg gaevstgiga lgtpstsnlg gvfqfysidp steygvvlaq
      181 gfgsdsarrs yarletgehq gfaaylsgvy segdkwkgkg sqelkqfnsk atynfgtdsk
      241 italfnvsrr veadyqdlsl emidrlgwdw dnyapdwdra vaaargtfsg gvnspwdayy
      301 sghglrnddl ssiagdfgln esmrlkvnvy nhsnrgqghw fspsnpsnpg tsreipisir
      361 tteyaidrtg vtsaftwnvg gheleaglwy ednghsvqrn fyyidgpitd dfflrnpdqr
      421 vwhqryttit rqfyvqdrfr lfddrltidi gaksphtrts vrtplgsyan nssltakkgf
      481 lpqagfnfkl negneifgsf akniaayalg vgspfnvpqa afdasaqnlk peqsrtielg
      541 wrgygqgyea svavydvkfd nrllaiaqcv gilgcpalfs nvgsvtsrga eatlqlkpmq
      601 dlawsnalsw ndstydndyv nngvvptrgk ktvdtpewmf astlawtpgp wdmrlsanhv
      661 gkryvtytnd vsvpsywlvn asvaydfgtl gpaqnltval nltnltdkry lssintngty
      721 aadptrslat mqvgaprqvm atatvrf
//
LOCUS       WP_008266833             628 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Stenotrophomonas].
ACCESSION   WP_008266833
VERSION     WP_008266833.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 628)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 628)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 628)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..628
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..628
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=67049
     Region          83..613
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 maaiespaga rpgraetppa dhwqrwavea vthtpaapae vmaqggtada psinsapppl
       61 pgpsalaeag nndqappasd spyrvlived draqalfaqs vlhgagmqai vhsdadgalq
      121 aikdhrpdli lmdlhlpgld gmrltalirq qpglqllpiv flsgdpdper qfevldsgad
      181 dylskpirpr hliaavanri rraraqaatl pgasgapats npetglptrh hvlqqlnaal
      241 ahrdpggvlf vevssalglr erygyaafer lmvqagqrla eaghphllar lndnsfllla
      301 rntdedsleg iaaalreqls arafvirdde svhlrgvvgy aplssgfdda nsaleavert
      361 tlqarllsag vaghvhreai seqehlalle gqlelayqpi vavaggntaq yqlllrlrqa
      421 dgtvlaagqv ipaaeaagri adldqqvmdh alglldlyrh atqplnlfvs qslrtlqrda
      481 fadwlleslh qrdlpgsalv idvrlpdali htvpllqfcq rmasagvrfc lsqfepggea
      541 dallthlpls fvrmaarfss shanpatree lrraieqaha aglqiigqqi edpqaaaamw
      601 vggvdyiqgn mvqsagsdln fdfhnavl
//
LOCUS       WP_008266948             133 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: division/cell wall cluster transcriptional repressor
            MraZ [Stenotrophomonas].
ACCESSION   WP_008266948
VERSION     WP_008266948.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Chen,S., Jancrick,J., Yokota,H., Kim,R. and Kim,S.H.
  TITLE     Crystal structure of a protein associated with cell division from
            Mycoplasma pneumoniae (GI: 13508053): a novel fold with a conserved
            sequence motif
  JOURNAL   Proteins 55 (4), 785-791 (2004)
   PUBMED   15146477
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11478503
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..133
                     /product="division/cell wall cluster transcriptional
                     repressor MraZ"
                     /GO_function="GO:0000976 - transcription cis-regulatory
                     region 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=14697
     Region          1..120
                     /region_name="PRK00326"
                     /note="transcriptional regulator MraZ"
                     /db_xref="CDD:234728"
     Site            order(65,67,95,102,111..112,115)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293784"
     Region          73..77
                     /region_name="DXXXR"
                     /note="DXXXR [structural motif]"
                     /db_xref="CDD:293784"
ORIGIN      
        1 mavptayrdl varasnnrlv ltynpfeagc lwlyaesewe rvrddvmskp ntqrvvrllq
       61 qklvgsaahl eldgngrisi pashrgavgi ekkavllgmg dkfelwseqa hraliqqtls
      121 dedlgdglld lkl
//
LOCUS       WP_008267514             188 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase
            [Stenotrophomonas].
ACCESSION   WP_008267514
VERSION     WP_008267514.1
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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..188
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=21028
     Region          18..182
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mpnpllpglq lqplpyhdrl plrdpatlem vvihctelpd lamareyger vlydsgagns
       61 ghfyidrdgr vvqyvapdrv ahhvrgmnah tlgielvntg ryphwfdsrh qamdepytea
      121 qlvaleqlll alvahypslr riaghdqldl eqvvasddpt lrvarkrdpg plfpwarvla
      181 kvplqsvg
//
LOCUS       WP_008268779             165 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Enterococcus].
ACCESSION   WP_008268779
VERSION     WP_008268779.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            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="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18206
     Region          23..156
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mwtekqkkda yeilllqqqg lleaednwla nlvnssalln etlpetvfag yylfdgneli
       61 lgpfqgrvsc trikmgkgvc gesaekqetl ivddvkthan yiscdsaaqs eivvpmvkeg
      121 nligvldidc gvtkgydeid qaflekyvdl llanfdinaf sfinn
//
LOCUS       WP_008274402             114 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Crocosphaera chwakensis].
ACCESSION   WP_008274402
VERSION     WP_008274402.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera chwakensis
  ORGANISM  Crocosphaera chwakensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae;
            Crocosphaera.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Crocosphaera chwakensis"
                     /db_xref="taxon:2546361"
     Protein         1..114
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13339
     Region          22..110
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mniqkkssnf iqqrlklspi ditniceqwk ikkmslfgsi lredfnhnsd idiliqfapy
       61 arqglltlak lkhhledmtq rsvdivvqes vensenwirk eeilntaqii yeqr
//
LOCUS       WP_008274314             258 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Crocosphaera chwakensis].
ACCESSION   WP_008274314
VERSION     WP_008274314.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera chwakensis
  ORGANISM  Crocosphaera chwakensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae;
            Crocosphaera.
REFERENCE   1  (residues 1 to 258)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Crocosphaera chwakensis"
                     /db_xref="taxon:2546361"
     Protein         1..258
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=28837
     Region          134..244
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkykltlalf tclvmfayvs hgkqkqgqsi ealetdnvvl rqensfsheq peqltptlnp
       61 ettlesstap nfspysspre typqtittwe repyieppqn nddsgpytna rmsqgnymtl
      121 tptqtknalg npiyelrlya ngqligtyqt vtgransqnr nrhqsgteap lpdgqyqvas
      181 aevagthpev ggrflpiepl fptqryalgi hydpsyqknn gedgtegcia ltnkpdldqv
      241 leyvytyqpq yldvklqg
//
LOCUS       WP_008274475             449 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Crocosphaera chwakensis].
ACCESSION   WP_008274475
VERSION     WP_008274475.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera chwakensis
  ORGANISM  Crocosphaera chwakensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae;
            Crocosphaera.
REFERENCE   1  (residues 1 to 449)
  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 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   3  (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   4  (residues 1 to 449)
  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 449)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Crocosphaera chwakensis"
                     /db_xref="taxon:2546361"
     Protein         1..449
                     /product="CmpA/NrtA family 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=51131
     Region          40..297
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mkrrnfikys glglaslgia acsntdifpf nqeknnvdfg tleksnlilg yvangdaapl
       61 iiaqekgffe ryglsvtlkr letwegvkke llgwqmdagq lpyafpmlaq lgkdedplis
      121 lmtlnlnssa itinqkawda girpsvdyfn ftdfeenirr ywrnretpvt lavdsafstd
      181 ayltrywlsa iglmpkteve lvefpasqmi yklqagmidg ysasspwnqq tvlekagfvt
      241 yvsrdiwhgh pnkilatmdg warkhpnttr almaavieac qycdrldnqt evaailgqpn
      301 ylnldtslie stlignysys setdenyqrf ipdytifhhr kaeywgendh anypwrshav
      361 wmltqmirwh dleiydypkn adqlldkiyp itiyeevaea lniplpsdnm kketstafid
      421 grsfdpsnpv aylnqfpira ngpqifgfv
//
LOCUS       WP_008275555              96 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Crocosphaera chwakensis].
ACCESSION   WP_008275555
VERSION     WP_008275555.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera chwakensis
  ORGANISM  Crocosphaera chwakensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae;
            Crocosphaera.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Crocosphaera chwakensis"
                     /db_xref="taxon:2546361"
     Protein         1..96
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10932
     Region          1..96
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mklkqilqek renilkiaaq hgafnihifg svargeetqd sdidflveme sgrnlldria
       61 liqdledylg ykvdvatiks lrdyfkekii keaipl
//
LOCUS       WP_008276921              96 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Crocosphaera chwakensis].
ACCESSION   WP_008276921
VERSION     WP_008276921.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera chwakensis
  ORGANISM  Crocosphaera chwakensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae;
            Crocosphaera.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Crocosphaera chwakensis"
                     /db_xref="taxon:2546361"
     Protein         1..96
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10925
     Region          1..93
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mkrhevlkii aehreqlekl gvkslslfgs vardeagpds dvdflvelnr emglfefiki
       61 rlylqdilnc svdlgtedtl rehlrepvlk dvihal
//
LOCUS       WP_008276731             341 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Crocosphaera chwakensis].
ACCESSION   WP_008276731
VERSION     WP_008276731.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera chwakensis
  ORGANISM  Crocosphaera chwakensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae;
            Crocosphaera.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Crocosphaera chwakensis"
                     /db_xref="taxon:2546361"
     Protein         1..341
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36825
     Region          <3..232
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mrgivrylgn gndvfratig dddifaqggn dlvygnrgkd glyggqgeds llgegdgdyl
       61 dggedsdild ggegddwlyg gegngqdhlf ggngedflvg hdgddflygd dgsspfyfdy
      121 fdvgdtperv erlddndeli pgwdsddvlr ggrgndflfg eqgkdklygd dgndyldggv
      181 rgdtlyggtg ndtligndgw dtligvdwna sdpgkyeidi lqgdnpngsf gnepdvfvlg
      241 ktnklfyddd niystgihdy alirdfdkte diiqltklpe feigsqphyr lgssplsgvq
      301 gtaifyddgi snglpselia ivqfqggstn ldlsdsyfty v
//
LOCUS       WP_008277813             385 aa            linear   BCT 20-JAN-2025
DEFINITION  ferrochelatase [Crocosphaera chwakensis].
ACCESSION   WP_008277813
VERSION     WP_008277813.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera chwakensis
  ORGANISM  Crocosphaera chwakensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae;
            Crocosphaera.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ferreira,G.C.
  TITLE     Ferrochelatase
  JOURNAL   Int J Biochem Cell Biol 31 (10), 995-1000 (1999)
   PUBMED   10582332
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Ferreira,G.C., Franco,R., Lloyd,S.G., Moura,I., Moura,J.J. and
            Huynh,B.H.
  TITLE     Structure and function of ferrochelatase
  JOURNAL   J Bioenerg Biomembr 27 (2), 221-229 (1995)
   PUBMED   7592569
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Taketani,S.
  TITLE     Molecular and genetic characterization of ferrochelatase
  JOURNAL   Tohoku J Exp Med 171 (1), 1-20 (1993)
   PUBMED   8122254
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Cole,S.P. and Marks,G.S.
  TITLE     Ferrochelatase and N-alkylated porphyrins
  JOURNAL   Mol Cell Biochem 64 (2), 127-137 (1984)
   PUBMED   6390167
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Crocosphaera chwakensis"
                     /db_xref="taxon:2546361"
     Protein         1..385
                     /product="ferrochelatase"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0004325 - ferrochelatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=43657
     Region          19..350
                     /region_name="HemH"
                     /note="Protoheme ferro-lyase (ferrochelatase) [Coenzyme
                     transport and metabolism]; COG0276"
                     /db_xref="CDD:440045"
ORIGIN      
        1 mvatpekqki etaegknksd rvavllmgyg evesyedfan yneqalnllt akfapvptwi
       61 ypplakllai fdlhewqhqh dhfisphnhi fehqrksiek nlqekwgdrv qvfkafnfck
      121 pflpeqvlse ikaqgfdkil iypllvvdsi ftsgiaveqv nnalaslaeg eehwlkglry
      181 ipsfynepgy ldlmaklvdd kikddladky lpsqigiill nhgcpheakg ftsgidesqi
      241 lyelvrerli hryplisvgw lnhqtplikw tqpnaelaak nlmelgakai ifmpigfate
      301 nhetlldveh iihglhkkss dvtyvqmpcv ndepefcema aqwadshiae llstealtvn
      361 palatgildv nhhhhdhgng hhhhh
//
LOCUS       WP_008278803             602 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Crocosphaera chwakensis].
ACCESSION   WP_008278803
VERSION     WP_008278803.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera chwakensis
  ORGANISM  Crocosphaera chwakensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae;
            Crocosphaera.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 602)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Crocosphaera chwakensis"
                     /db_xref="taxon:2546361"
     Protein         1..602
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=69342
     Region          17..>458
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mpkkiksrin rlfclklllt iavtittigi rhlgglqwle wlavdllfkl qpsegmdrri
       61 vlvgeteedi qafksaqisd rtmaqlltri eqqepiavgv dffrdqpvge greqllelfe
      121 tnpnfygvgk qtgdrenplf apvapppinq sqitevavqp dsdgvlrrmf lfpqtkppal
      181 pnlglvlaye ylakqgiype paeqgwlqln qatfwpfrns sgpytqiddg syqiflnwrn
      241 vefefvsisd vlsghikpsi fkdklviigs yasskkdyff tpfsrtlsss pelmfgmevq
      301 aqlasviisn algerplikf weeleinigl vvfgiiicfc lnefflqwkl ltvfllttst
      361 iiailsyslf ilgiwipiip tlillwslgi imaifdyewq qkrqkdkila lnerlkkkid
      421 erqiyrdyav lltpfeeslt etlqyisnsk ylisteeeil tekinqfvsn pkhkikidqs
      481 vsqltiyyqq imekieyisq ktaiyfptld slasltykes nlpqglveiq slideiissi
      541 rrviyneygv dlldlitlkv tpastfiret hklliifnri fddiflshqi eekeyplmkf
      601 wf
//
LOCUS       WP_008279442             191 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Roseovarius].
ACCESSION   WP_008279442
VERSION     WP_008279442.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius
  ORGANISM  Roseovarius
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 191)
  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 191)
  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   3  (residues 1 to 191)
  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   4  (residues 1 to 191)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 191)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Roseovarius"
                     /db_xref="taxon:74030"
     Protein         1..191
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=20993
     Region          1..191
                     /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"
ORIGIN      
        1 mklhivivep detraklvid slqplghqvt viaepaglsr rvsdiapdiv lidmsnpsrd
       61 tleemalasg pmerpvaffv drtdrdltkq aieagvsayv vdglqperva svmdaaiarf
      121 qmfrrmrrel ettrraleer klidrakgil mkarglteee ayallrktam dqgrkvaeva
      181 salvtaagll s
//
LOCUS       WP_008279632             278 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Roseovarius].
ACCESSION   WP_008279632
VERSION     WP_008279632.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius
  ORGANISM  Roseovarius
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 278)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Roseovarius"
                     /db_xref="taxon:74030"
     Protein         1..278
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=30655
     Region          35..262
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mgqkhkwadi pagfdtplsy avsardrsvl dmvnqavhhk qvllayqavv parqqdrpaf
       61 yeglirvlda tgrvipakdf itqievtetg riidclalek glrtlinypd lrlainmsar
      121 sigysrwmrt lkkglsddpt igerlileit essamlvpel vtgfmkelqa kgisfalddf
      181 gagytsfrfl kefyfdilki dgqfvrgiat dpdnqvltaa lasigqqfdm vtvaesvekp
      241 edaaylaalg idclqgyyfg aptvrppwid saldrata
//
LOCUS       WP_008279748             376 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [Roseovarius].
ACCESSION   WP_008279748
VERSION     WP_008279748.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius
  ORGANISM  Roseovarius
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 376)
  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 376)
  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 376)
  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 376)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Roseovarius"
                     /db_xref="taxon:74030"
     Protein         1..376
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=41282
     Region          7..369
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mtnkskmdrr sflrraavga pavaagalaa pavlaqaplv lkmqtswpag diwqemaqdy
       61 atrveemsgg rlkidvlpag avvgafqvld avndgvldia hsvpvywygk nkaaslfgtg
      121 pvfggsattm lswfyegggk alydeltqdi mglevdgymg fpmfaqpfgw fkgevntvad
      181 lqgfkyrtvg laadllqsmg msvaqlpgge ivpamergvi dafefnnpss drnfgahdva
      241 knyylssyhq asesfeflfn kltmedldpd mrailkyave aastantaka mrrysadlkw
      301 lqeeagvtih rtstdilngq ieawdklipv leedpfmkkc ldsqrawveq vtyyelmnap
      361 dyalafdhyf pgklkm
//
LOCUS       WP_008279874             255 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Roseovarius sp. TM1035].
ACCESSION   WP_008279874
VERSION     WP_008279874.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius sp. TM1035
  ORGANISM  Roseovarius sp. TM1035
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseovarius.
REFERENCE   1  (residues 1 to 255)
  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 255)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Roseovarius sp. TM1035"
                     /db_xref="taxon:391613"
     Protein         1..255
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27153
     Region          1..254
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mrfsanlgfl ftdrplpeai haaaragfaa vechfpydfa adevraalee tglpmlglnt
       61 wpgdraagdf glaavagred earaairqav dyaqaigaga vhvmagctds gaeaeavfrs
      121 nlayacdlaa phgltiliep inqrdvpgyh lsstahaasv iaalrrdnlr mmfdcyhlqi
      181 mggdllrrfa ryqpiighvq fagvpdrgap dqgevdygwl lpqiaalgwp gpfgaeyrpg
      241 eagteaslgw ltrfa
//
LOCUS       WP_008282134             296 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Roseovarius sp. TM1035].
ACCESSION   WP_008282134
VERSION     WP_008282134.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius sp. TM1035
  ORGANISM  Roseovarius sp. TM1035
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseovarius.
REFERENCE   1  (residues 1 to 296)
  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 296)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 296)
  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   4  (residues 1 to 296)
  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   5  (residues 1 to 296)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Roseovarius sp. TM1035"
                     /db_xref="taxon:391613"
     Protein         1..296
                     /product="TRAP transporter small permease subunit"
                     /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=33712
     Region          71..275
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mldavlwifq nigmafynla yaishpaswl dwsdkeaimr vvyyggsvef ffvaftvflv
       61 itavglwkna flwgcvrgle gmantvgrfa awaglimviq qilivfiqri farpdmvfgi
      121 giplqldisw yseelklyna livtlcatyt fvqgghvrvd liyapvshat kkiidmvgsl
      181 ifmmpmavlt wmygwffmwr hlivpnpsas etldrllmks ralrwnveti gfspngfngy
      241 flfkvllvlf agmvflhama ffwrsylefk egpdslgkyl drdtlgqgee afegth
//
LOCUS       WP_008282238             192 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Roseovarius].
ACCESSION   WP_008282238
VERSION     WP_008282238.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius
  ORGANISM  Roseovarius
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Roseovarius"
                     /db_xref="taxon:74030"
     Protein         1..192
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21096
     Region          1..163
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 miralydwti rmadhrhalw vlaavsfves svfpippdvl mipmilarps rawlialval
       61 vssvlggllg yaigafafqe igqpilaalg kgdamtefst rfndfgfwav ltagitpfpy
      121 kvitimsgwt amplgvfias silargirff lvaallwkyg psvrdfierr lglvtivfvv
      181 llfggfyatr ff
//
LOCUS       WP_008282839             260 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phosphonate ABC transporter ATP-binding protein
            [Rhodobacterales].
ACCESSION   WP_008282839
VERSION     WP_008282839.1
KEYWORDS    RefSeq.
SOURCE      Rhodobacterales
  ORGANISM  Rhodobacterales
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
REFERENCE   2  (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   3  (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   4  (residues 1 to 260)
  AUTHORS   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 260)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Rhodobacterales"
                     /db_xref="taxon:204455"
     Protein         1..260
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=27554
     Region          4..250
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mniairiddl nfahpggsvp alervsltis tgesvallgp sgagkttlla lldgrlqgwr
       61 grvsvlgapl dpdqpppras rpdtgfvfqe falverstvl rnvlngrlgr maplrallgs
      121 ptphdldiar taltdcgiad laerrvdsls ggqrqrvaia rclaqeprli ladepvsnld
      181 ptragevlal ltgaaqarga talfsshqpd larrfaqrii gmrdgriafd vptselndda
      241 taelyrevep ipgiglravs
//
LOCUS       WP_008282846             170 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Rhodobacterales].
ACCESSION   WP_008282846
VERSION     WP_008282846.1
KEYWORDS    RefSeq.
SOURCE      Rhodobacterales
  ORGANISM  Rhodobacterales
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Rhodobacterales"
                     /db_xref="taxon:204455"
     Protein         1..170
                     /product="TRAP transporter small permease subunit"
                     /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=18739
     Region          2..156
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mdwidrgirg igvvtawltv vsiaaygalq mldrklqlgv ssylpdlsts llfilifltf
       61 gytylrdghv rvdvlrrhws arriawieli gglfvllpla ailtyygwdg lmrttkyaet
      121 qlwaqriagv igpillalag mivalrniaf ltgrraqgap eqasglhnge
//
LOCUS       WP_008286449             157 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Hydrogenivirga sp. 128-5-R1-1].
ACCESSION   WP_008286449
VERSION     WP_008286449.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenivirga sp. 128-5-R1-1
  ORGANISM  Hydrogenivirga sp. 128-5-R1-1
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Aquificaceae; Hydrogenivirga.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Hydrogenivirga sp. 128-5-R1-1"
                     /db_xref="taxon:392423"
     Protein         1..157
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16490
     Region          1..148
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlegleawar gvvesygyag iflisfsesi aqpvppdpfi agatalglsp llsalvatlg
       61 svlggltaht lglllgepva kkllgernfl kgealfnrfg vwavllaalt pipfkvicwl
      121 agifemprlp fliasfvgrl prfllvaylg dllggll
//
LOCUS       WP_008286732             116 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Hydrogenivirga sp.
            128-5-R1-1].
ACCESSION   WP_008286732
VERSION     WP_008286732.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenivirga sp. 128-5-R1-1
  ORGANISM  Hydrogenivirga sp. 128-5-R1-1
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Aquificaceae; Hydrogenivirga.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Hydrogenivirga sp. 128-5-R1-1"
                     /db_xref="taxon:392423"
     Protein         1..116
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13015
     Region          1..97
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 miseelksqi ieviskhlem dkcvvvlfgs ealgeatgrs didlgvdcve pisdsvflel
       61 eralneevnt lkkidlvels dldedfllfa lkgaiiwhvg rdylrswikr keplks
//
LOCUS       WP_008287514             386 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Hydrogenivirga
            sp. 128-5-R1-1].
ACCESSION   WP_008287514
VERSION     WP_008287514.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenivirga sp. 128-5-R1-1
  ORGANISM  Hydrogenivirga sp. 128-5-R1-1
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Aquificaceae; Hydrogenivirga.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 386)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 386)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Hydrogenivirga sp. 128-5-R1-1"
                     /db_xref="taxon:392423"
     Protein         1..386
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44905
     Region          3..372
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mdikayhggs ligtlfense reyafeysdk adthlclsmp ntrrvyisrf rlhpffdtfi
       61 pegylfellr nlinkgegra ddftmlyyla ggvegrirle gkerpeeeka isleevlend
      121 twdtfralln tflyknaigg vqpktlapve greyiiktfg eeypelarne yfcmraverv
      181 giripniyls rngrfivvek ftrgeypgfe emgsllgktr etkyegsyeq iakvverfst
      241 cpeedmktyy kltvmnfllr ngdahvknfg liytddfsei rlspaydvvc ttvyipddkp
      301 alfmhgtkrw hgrdglmefg mkhcglskee akelyekcen avreemeevk eymkeemgfr
      361 gvgermvrew ekailkwlkh gticss
//
LOCUS       WP_008289034             346 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Hydrogenivirga sp. 128-5-R1-1].
ACCESSION   WP_008289034
VERSION     WP_008289034.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenivirga sp. 128-5-R1-1
  ORGANISM  Hydrogenivirga sp. 128-5-R1-1
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Aquificaceae; Hydrogenivirga.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  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   3  (residues 1 to 346)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Hydrogenivirga sp. 128-5-R1-1"
                     /db_xref="taxon:392423"
     Protein         1..346
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40933
     Region          172..339
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mdervnvlvd afrrtteqgv tlegilivvf lfsfivlslv lsyklkiyfq ehrlkkiffe
       61 ysenigltrd eaeiiwetsk kidrdpylsl evkqtfekii dyyiktnpef denkirhmrk
      121 vlgfdyippf ipltstkdid lyqsatlisd kgsfnialvd kdelymywti ldnvpvrlnk
      181 gdsvkinflr tddayysfed kiediykekd ryivkiphtf hlvrtqkrke irikinvpve
      241 vhidkikina etenislggl kfciyksend ymkilrigky iylrlkigsn viiteakikn
      301 ilekedmicv gvefvdldke ykqilsdfit kkqmeimqqy kkqkgl
//
LOCUS       WP_008289523             286 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Hydrogenivirga sp. 128-5-R1-1].
ACCESSION   WP_008289523
VERSION     WP_008289523.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenivirga sp. 128-5-R1-1
  ORGANISM  Hydrogenivirga sp. 128-5-R1-1
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Aquificaceae; Hydrogenivirga.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Hydrogenivirga sp. 128-5-R1-1"
                     /db_xref="taxon:392423"
     Protein         1..286
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=32132
     Region          5..>219
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mikvnikkkl kgykgdfild vefqlekgqf lsifgksghg kttllriiag letpdegyie
       61 fngkvyfdse kkinlppqkr nvgfvfqdfa lfpnmtvyen ltfanrnekk iheilkklei
      121 yelkdrypst lsggqkqrva lgraiirnpe illldeplsa ldesirlklq deikkihney
      181 gltsiivshd kkevfkladr vfvlengkiv kqgtprdvfi ekdisgkfsf ygqvidvrpa
      241 givniatidi ndnlvevvvg ndvkigdsvl vgvkgfnpvv kvvslp
//
LOCUS       WP_008290229             309 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Methylophaga
            thiooxydans].
ACCESSION   WP_008290229
VERSION     WP_008290229.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thiooxydans
  ORGANISM  Methylophaga thiooxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
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   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 309)
  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 309)
  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 12807598
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Methylophaga thiooxydans"
                     /db_xref="taxon:392484"
     Protein         1..309
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33995
     Region          13..83
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          17..308
                     /region_name="PRK10856"
                     /note="cytoskeleton protein RodZ"
                     /db_xref="CDD:236776"
     Region          233..299
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 msdghsddat vattsptigs rlqqareakk ysvaevaaql rlnkdivtym enqqwdklhg
       61 rtyargyfas yvkflglpfd emlavfndey qtsepslnlf qhghdqldrq fpwfmlalia
      121 tvmvviwlaf qqwqqtqvvq qasmaesdnv eeadnfstsi vdpsdaiesp nqpmissaeq
      181 taeqlgisan nldeitatev asstsaaler nsqmtvtdqq anepvstees tlqlsfsgec
      241 wvevtnadsq vlvskvmrad qslllksdqp lsillgraka asvtfnnqtv dlsphmqgdl
      301 arltlgves
//
LOCUS       WP_008291579             274 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Methylophaga
            thiooxydans].
ACCESSION   WP_008291579
VERSION     WP_008291579.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thiooxydans
  ORGANISM  Methylophaga thiooxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Methylophaga thiooxydans"
                     /db_xref="taxon:392484"
     Protein         1..274
                     /product="formate/nitrite transporter family protein"
                     /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=28762
     Region          10..267
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 maeqqeavsd pyppvdiark veglgvtkah tdtltllvla vlagafislg alfysvvvtd
       61 sglgfgitrl lgglsfclgl ilvviagael ftgnnliama wasgligtre virnwiivyl
      121 gnvvgclgtv llvfwsnvaq lgdsavgqtl vniahtkadl slseaftrgv lcnvlvclai
      181 wlaigarsvs gkilailfpi tafvaigfeh sianwfflpl gavldvqngv sllpmvknii
      241 avtagnmvgg tllvagiywl aylraermrm pppk
//
LOCUS       WP_008291606             165 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Methylophaga thiooxydans].
ACCESSION   WP_008291606
VERSION     WP_008291606.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thiooxydans
  ORGANISM  Methylophaga thiooxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
REFERENCE   1  (residues 1 to 165)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Methylophaga thiooxydans"
                     /db_xref="taxon:392484"
     Protein         1..165
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=18420
     Region          12..165
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cl49639"
                     /db_xref="CDD:483979"
     Site            order(120..121,124,137..140,142)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 maktmpttwl disisaqhcq lwhhdklvfs aavstalngp gekegsggtp rgwhqiraci
       61 gqgqpvntvf vgrrptgery tpdlgktfpd rdwiltrilw lsglelgknr lgnvdtmrry
      121 iyihgcpdal pmgqalshgc irmhnrdllt lfeqvkpglk vwihe
//
LOCUS       WP_008291887             305 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Methylophaga
            thiooxydans].
ACCESSION   WP_008291887
VERSION     WP_008291887.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga thiooxydans
  ORGANISM  Methylophaga thiooxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
REFERENCE   1  (residues 1 to 305)
  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   2  (residues 1 to 305)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Methylophaga thiooxydans"
                     /db_xref="taxon:392484"
     Protein         1..305
                     /product="aminoglycoside 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=35257
     Region          29..278
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mvekrdsdka gsnlfqqlks dsalpelysa eripslfeds thqlwrceta dgdmilkrch
       61 rttveqspiw qmmhqlfdvs lpddlahfha iqamlekqgv lpipeliacg geaddsaafv
      121 lsrvvegeai qkkhltddlv iqfarqiatl hlkqqttwgk lfqadkvaed wpamllktll
      181 rhsrklrige pwlykvmtql eqvtpryfvp imldnrwdqy lindnkital vdldafvigp
      241 pelelvlley qldqkqadvf vqeyqkylaf pdiasyrlsy rlllflmnal gesnldrwmt
      301 sphrw
//
LOCUS       WP_008292873             337 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Congregibacter litoralis].
ACCESSION   WP_008292873
VERSION     WP_008292873.1
KEYWORDS    RefSeq.
SOURCE      Congregibacter litoralis
  ORGANISM  Congregibacter litoralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Halieaceae; Congregibacter.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 337)
  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   6  (residues 1 to 337)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Congregibacter litoralis"
                     /db_xref="taxon:393662"
     Protein         1..337
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36881
     Region          19..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <159..329
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msqitslyvh kilsqvsagv etadlledlg fiagaavdpk rmvastqfyd ffaslvardp
       61 hglslplrig atmrsdeyga fglawktapn lrgsygrsqr yghvlgsaei ytpeqsndgw
      121 ffsldkagdg rlgmllsnea smaavdvisr evttanfapl avyfkhaarg dvsvyethfg
      181 cpvhfesprd allvgedtld apnrlgdetv vsffdrhlee elasssndhg leqrvrrava
      241 rtlsegvptl ssiaselgig srtlqrrlsd sghsfqsvvd marrdlarrl lretdyslae
      301 igfltgfseq saftrafkrw agqtprsyrl gptsqen
//
LOCUS       WP_008295943             220 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Congregibacter litoralis].
ACCESSION   WP_008295943
VERSION     WP_008295943.1
KEYWORDS    RefSeq.
SOURCE      Congregibacter litoralis
  ORGANISM  Congregibacter litoralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Halieaceae; Congregibacter.
REFERENCE   1  (residues 1 to 220)
  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 220)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 220)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Congregibacter litoralis"
                     /db_xref="taxon:393662"
     Protein         1..220
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23826
     Region          1..179
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 mesyrteeeq vealkrwwke ngrstmvgvv lalglgfgwq awqknqetaa qnasnlyqqm
       61 lqalsaeetg tigrqiatel kdshrgtvya qfaalhlarl avndgqpqva eqelrwtlam
      121 adegddvhqv aqlrlarvla aqekeeeala llagantdfi asyaiargdi llaqgreada
      181 laayesaaaa leegapvpqt lqdkleylga rvdttvaeas
//
LOCUS       WP_008297115             298 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Bhargavaea
            cecembensis].
ACCESSION   WP_008297115
VERSION     WP_008297115.1
KEYWORDS    RefSeq.
SOURCE      Bhargavaea cecembensis
  ORGANISM  Bhargavaea cecembensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Bhargavaea.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 298)
  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 298)
  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 298)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Bhargavaea cecembensis"
                     /db_xref="taxon:394098"
     Protein         1..298
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32226
     Region          1..69
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          217..276
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mselgarlkq armekgysle dlqeitkiqk rylaaieegk fgimpgtfyv rafikqyaea
       61 vdldademla mykaeapepl itgdsagmsa ptmrrtsmrr agkaaeampk vilalfivva
      121 igivwflkan qaadtepaee inetestvqv eqvgpedaed aapaedadpa eeeaaeeaee
      181 paeteepaep eaalavdrte gentfynlsg tdkasitlng kgrswisvtd ntgkqylsks
      241 lengqtetie aqgvqwlrfr igyvpgveit vngspltyav pgtdrvtqni iiqlgaaq
//
LOCUS       WP_008294686             468 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Congregibacter litoralis].
ACCESSION   WP_008294686
VERSION     WP_008294686.1
KEYWORDS    RefSeq.
SOURCE      Congregibacter litoralis
  ORGANISM  Congregibacter litoralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Halieaceae; Congregibacter.
REFERENCE   1  (residues 1 to 468)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Congregibacter litoralis"
                     /db_xref="taxon:393662"
     Protein         1..468
                     /product="amidohydrolase family protein"
                     /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=50709
     Region          36..460
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mersqkvitn fstaavklsa aliasaliav sahagtalvg grlidgfgha piansvilve
       61 dgviqevgtv gtldvpedye vvstegmdvl pglwenhahl mlnghadysh whptykdrla
      121 seimpssavq lllagitsar dlgapleasi svktriesge ipgprlfvsg pfiqhgaypn
      181 tefyrwgvds vadgrrkvkk ladagvdiik lidqdnmtle eaqavvdeah khglkvvahs
      241 hrpnevrrgl eigvdnfeht glttapeypa dviemlrert atgriaggpl fwtptveglw
      301 nydqtvanpe kldsecwhrg lepstiadik asiqepgqla ytqltplrkp tlkrkfqqlr
      361 dagvvmlvgt dsgipmkfhc qstwnemdvw vnvmgvdpms tiraatywga vmmgvsdkvg
      421 tvsagkyadi iavkgdvlrh inllsrvdfv mkngvvykqd gvavesal
//
LOCUS       WP_008299808             290 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Bhargavaea
            cecembensis].
ACCESSION   WP_008299808
VERSION     WP_008299808.1
KEYWORDS    RefSeq.
SOURCE      Bhargavaea cecembensis
  ORGANISM  Bhargavaea cecembensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Bhargavaea.
REFERENCE   1  (residues 1 to 290)
  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   2  (residues 1 to 290)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Bhargavaea cecembensis"
                     /db_xref="taxon:394098"
     Protein         1..290
                     /product="aminoglycoside 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=33249
     Region          6..>191
                     /region_name="CotI"
                     /note="Spore coat protein CotI/CotS, protein kinase
                     superfamily [Cell cycle control, cell division, chromosome
                     partitioning]; COG5881"
                     /db_xref="CDD:444583"
ORIGIN      
        1 maaggnirqi kqnvwkwdvg gkryslkkyd saqqarkvrr ihdelenigf phvlpiigsa
       61 deraviqpwl drarpadyss ragrdrtlsv lrmlhatsdq vnwegtgvly rypliakwed
      121 rlskfrnqkk nlvplvgskh ydaivyhaee alsairktyd peedctllhg dvvhhnflkg
      181 pdgkyvmidf dlactgpsgt etalwihrvl shvdfdldyl cgeqpelgll sassfnllly
      241 pnellrewly lltldedkqr qmkakldrft dkalsawipl cyqvskrvnn
//
LOCUS       WP_008300943             669 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Bhargavaea cecembensis].
ACCESSION   WP_008300943
VERSION     WP_008300943.1
KEYWORDS    RefSeq.
SOURCE      Bhargavaea cecembensis
  ORGANISM  Bhargavaea cecembensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Bhargavaea.
REFERENCE   1  (residues 1 to 669)
  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 669)
  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 669)
  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 669)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Bhargavaea cecembensis"
                     /db_xref="taxon:394098"
     Protein         1..669
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=71589
     Region          16..661
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 madektkkde qnlqlseeeq qellkkydpe sntrdvrgim kkivffglla fsvfqlytai
       61 fgqytayiqr svhlgfalsl ifllfpfrrk sakkdrvpfy diilallsvg vglywplqyn
      121 elvlrvgrvt dldmtvaila vlltleasrr avglpitiia safliyaftg pywpgflahr
      181 gqdlsalaql mfyttdgvlg tpigvsatfi fvfllfgafl vktgvgqyfn dlavalagkl
      241 tggpakvaif ssalqgtisg ssvanvvtsg sytipmmkkl gyrkefagav easastggql
      301 mppimgaaaf lmvefiggit yweiakaaai pallyfsgiw imthfeakrv glsglsddql
      361 pnrkevlkki ylltpilgii iflligiptm qaalwgivlt ivvsafdkkt rlnfkdmina
      421 lvdgartala vaaatacagi ivgvvvktgl glslanglis asgghlfltl fftmlaaivl
      481 gmgspttany vitstiaapa viallmidep agaavpvvva lsahlfvfyf giiaditppv
      541 alaafaasgi sggdpirtgv naaklaiaaf iipymfvynp amlmidasvi eiiwvtataf
      601 agmlavgagf vgfwyrklnw lerilalaag gmlifpegmt dvfglvlfvi llaiqfmtrn
      661 krdretvaa
//
LOCUS       WP_008301697             425 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Paraglaciecola
            chathamensis].
ACCESSION   WP_008301697
VERSION     WP_008301697.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola chathamensis
  ORGANISM  Paraglaciecola chathamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 425)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Paraglaciecola chathamensis"
                     /db_xref="taxon:368405"
     Protein         1..425
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48331
     Region          10..412
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mstdannevn vlqisihdvl igylagfkng rnvlsiadtf knnperptfs lithpkfpls
       61 nklmaepwar nqrlhpvlsn llpegslrel iaqslkvhvd nefhilsylg adlpgaieai
      121 pmepedvpdh vlnthgkaka vkfdkvthen kfslagvqmk fsmkekegry nlskgdvlgd
      181 wiiktpstkh kfvplneyta mslaelvgvd ipqiklveln kldnlpqinl pdeklafaik
      241 rfdraddkri hmedfaqilv kyprdkytsa nyenlgkviy dfsgdalada qqfarrllvn
      301 illangdahl knwsflypdk vtprlspayd ivttsvyien etqfalnlsk tkewftvtma
      361 hfrtwadksg ipwraikphl ddtmskarel wpealkklpm deihkeglra hwsklqedfk
      421 ieatk
//
LOCUS       WP_008303564             269 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Moraxellaceae].
ACCESSION   WP_008303564
VERSION     WP_008303564.1
KEYWORDS    RefSeq.
SOURCE      Moraxellaceae
  ORGANISM  Moraxellaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Moraxellaceae"
                     /db_xref="taxon:468"
     Protein         1..269
                     /product="formate/nitrite transporter family protein"
                     /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=29030
     Region          2..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 maylapaefa kkvvdagesk lhmatrdvli rafmagaila laavfaitia vqtgspliga
       61 llfpvgfcml yllgydlltg vfvltplawl dkrpgvtwgr ilknwglvfv gnftgclvva
      121 vlmaavytmg faadpnpvgv kiahigeert lgyaeygfag wmtifirgml cnwmvslgvi
      181 gammsttvsg kfiamwmpim lffamgfehs vvnmflfpfa mmmggdfsia dyflwnelpv
      241 algnlvggla ltglalytth vrtgvkkef
//
LOCUS       WP_008303817             314 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Acinetobacter sp. HA].
ACCESSION   WP_008303817
VERSION     WP_008303817.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. HA
  ORGANISM  Acinetobacter sp. HA
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 314)
  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 314)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Acinetobacter sp. HA"
                     /db_xref="taxon:1173062"
     Protein         1..314
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35731
     Region          27..74
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msldattwaw kvrqkqkpgg stkplkrlvl lsladraged hcaypsiarl vedtemdrkt
       61 vlkiideliq dgliedtger kgrtkqvkvy rligvngret vptmesfdae nedlkgpnig
      121 tvptteqfqr svervptfrg kspnvgtrnl sknlsieskn kkswfcfnkl reeifltdds
      181 idfeiivdsk wierekrafe vynaeklmsd elmiyhfadw vinayrnkys ketsvkpaga
      241 shktdqlsek qiftfsqkls qhpefaskfs epgesyekla ariavklkdp aqakkwegyl
      301 kqvgfngdlp diaa
//
LOCUS       WP_008304183             295 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Paraglaciecola
            chathamensis].
ACCESSION   WP_008304183
VERSION     WP_008304183.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola chathamensis
  ORGANISM  Paraglaciecola chathamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 295)
  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 295)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 295)
  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   4  (residues 1 to 295)
  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 295)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Paraglaciecola chathamensis"
                     /db_xref="taxon:368405"
     Protein         1..295
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32285
     Region          24..179
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          205..286
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mnketikrli dnkvsksglv etgipgvqlf nitepvscap avyepsitai vggckeaild
       61 gnrhfydssa yiccpmsmpv eagtpeastd npligvyirf dtramtelaf elestngliq
      121 kakdaaypqg istanwddaf tealyrlill senptdiail grsrlrelyy ailkgdaggs
      181 vrrsfgvgnd iarsieflss nlsapvtien ladqigmsra vfhrkfkqat nmspiqfvks
      241 mrlnkaamki aegrnvnvaa mevgyvsssq fsrdfrrmyg qspkqwiqaq esnna
//
LOCUS       WP_008304340             130 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Paraglaciecola chathamensis].
ACCESSION   WP_008304340
VERSION     WP_008304340.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola chathamensis
  ORGANISM  Paraglaciecola chathamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Paraglaciecola chathamensis"
                     /db_xref="taxon:368405"
     Protein         1..130
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14369
     Region          10..128
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkqqlffdtn tgfsllelmi vlaivgilai ialptyqshi ihgrrvdaqn tllkwhlqqe
       61 ryrishtqya detalpppag tayqfsaadi sathftltae atsaqqtdvg cttltidqsm
      121 hktpqacwpr
//
LOCUS       WP_008305287             512 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Paraglaciecola chathamensis].
ACCESSION   WP_008305287
VERSION     WP_008305287.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola chathamensis
  ORGANISM  Paraglaciecola chathamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Paraglaciecola chathamensis"
                     /db_xref="taxon:368405"
     Protein         1..512
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=55400
     Region          20..512
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mqetiskell ektarqqrsv lqvhkqdnvl ialkdlakge qvnysettlt vqenikaghk
       61 iamrdfekge tvvkygygig sttqavnega hihshnlatd ldgsetyhya psqmtvetps
      121 rmptfkgykr qsghvgvrne vwiintvgcv nqaatriaql akrqfaarad dfianthpfg
      181 csqlgddlnn trnilaslmq npnaggvlvi glgcennqld alirssptid psrlrffnsq
      241 evedevevgl alveelldem atdqredlpv ssltlgmkcg gsdgfsglta naivgrvsdk
      301 ltgfggrvil tetpemfgae qvllnranse atfnnivklv ndfkqyfiaq nqpiyenpsp
      361 gnkagglttl eekslgaiqk ggkaiinevi dygqrastgq gmtllqspgn davsstalaa
      421 aganivlftt grgtplgfpv ptvkiasnsd lavrkkhwid fnagkilded ididqcadel
      481 fecilaiasg qktrneenen remaiwkngv tl
//
LOCUS       WP_008304990             479 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Paraglaciecola chathamensis].
ACCESSION   WP_008304990
VERSION     WP_008304990.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola chathamensis
  ORGANISM  Paraglaciecola chathamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 479)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Paraglaciecola chathamensis"
                     /db_xref="taxon:368405"
     Protein         1..479
                     /product="amidohydrolase family protein"
                     /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=52180
     Region          45..461
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mpysknplla lsrcttlltl lggifssvna ygvdeefiny dqneiaivnv tlidgtgapp
       61 ktnqavliks ghiaavdsak dikisqtttv idgtgktlip glvmmhehmf yptgnahyte
      121 mlysfprlyl aggattvrta gttapygdln lrdainsgkt mgpdidvtap ylngpglpil
      181 kikslrdaqd aknmmqywdq egvtsykaym hihqdelaqv lssahqrkrk vtghlcsity
      241 keaaelgidn lehgffaatd fvkdkkknqc paaelhqslv dldinapeve alisllvskn
      301 valtstltvf etftkgrpka yplalealip qvreqyetrw qkiaqqenat wpivfkkmmq
      361 lekrfveagg tlmagtdptg yggviagfsn qrqiellvea gfsiqqaiki atlngatfle
      421 rdtkigsiea gkqadlvlid gelindtsai rdmavvfkhg vgynvskivq qtksvvglh
//
LOCUS       WP_008305909             694 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Paraglaciecola chathamensis].
ACCESSION   WP_008305909
VERSION     WP_008305909.1
KEYWORDS    RefSeq.
SOURCE      Paraglaciecola chathamensis
  ORGANISM  Paraglaciecola chathamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Paraglaciecola.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 694)
  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   3  (residues 1 to 694)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Paraglaciecola chathamensis"
                     /db_xref="taxon:368405"
     Protein         1..694
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=75666
     Region          3..689
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msidmeqfhg vffdesqehl admeqqlmel dlsepdpeql nsifraahsi kggsgifgfd
       61 altglthime nlldrarnnt iemttpivdl llettdllkv tldnyrnqee ieqadidqgi
      121 sklnilmtsl edstaqnssn tgddgdnden ennegvsgdl dgfgffddep sdahtaqidd
      181 ddedgfgffe qppatasepe ndenqgfgff dttptetpat nagnsaiicd taptaaesid
      241 kgygffpene hpkddpsdnk kgygffeklp vpsakskkts avkepkknaa ksstakasve
      301 sssirvdtgk idslvnlige lvitqsmlsq vssdmpgepn eklqnaiael trntreiqes
      361 vmsmrmlpmh ftfnrfprvv rdlssklgkk vdlvieggnt eidkgmiekl vdplthlvrn
      421 sidhgiekte drlalgkvem gtvilkaeqk gssiiisiid dgaglnreri lakaqengms
      481 vdvdmpdsdv wklifeagfs taeavtdvsg rgvgmdvvrr nleaiggrie iessqgegss
      541 fnihlpltla ivdgicvsva sqtfvvplvn iiesvqpdps qmklisnekl lwirdqywpl
      601 vklhqkmqie gaitepseai vmliessnkr fgllvdglmg qqqvviksle qnyrrvegva
      661 gatimgdgqv alildvesla nsvkangmsk esil
//
LOCUS       WP_008308258             115 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Leptolyngbya sp. PCC 6406].
ACCESSION   WP_008308258
VERSION     WP_008308258.1
KEYWORDS    RefSeq.
SOURCE      Leptolyngbya sp. PCC 6406
  ORGANISM  Leptolyngbya sp. PCC 6406
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Leptolyngbyales; Leptolyngbyaceae; Leptolyngbya group;
            Leptolyngbya.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Leptolyngbya sp. PCC 6406"
                     /db_xref="taxon:1173264"
     Protein         1..115
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13282
     Region          5..99
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mavttkeqvi hlieehhqdl qrlgvhrcgl fgsfvrnamt eqsdvdilve fepqqktfnn
       61 fmdlcfflek ilgrnvdlvt reslspyigp rilkeveyis ilpekrfscr lgete
//
LOCUS       WP_008309059             114 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Leptolyngbya sp. PCC 6406].
ACCESSION   WP_008309059
VERSION     WP_008309059.1
KEYWORDS    RefSeq.
SOURCE      Leptolyngbya sp. PCC 6406
  ORGANISM  Leptolyngbya sp. PCC 6406
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Leptolyngbyales; Leptolyngbyaceae; Leptolyngbya group;
            Leptolyngbya.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Leptolyngbya sp. PCC 6406"
                     /db_xref="taxon:1173264"
     Protein         1..114
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12941
     Region          1..114
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mnpiekirei epidqqamse frsrletiip ildlrvfgsr argdaredsd ldvfiqvetl
       61 drtlreqihn laweigfeyd rvistfvvte dqlregavga splltkvlee gitv
//
LOCUS       WP_008313452             129 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Leptolyngbya sp. PCC 6406].
ACCESSION   WP_008313452
VERSION     WP_008313452.1
KEYWORDS    RefSeq.
SOURCE      Leptolyngbya sp. PCC 6406
  ORGANISM  Leptolyngbya sp. PCC 6406
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Leptolyngbyales; Leptolyngbyaceae; Leptolyngbya group;
            Leptolyngbya.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Leptolyngbya sp. PCC 6406"
                     /db_xref="taxon:1173264"
     Protein         1..129
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14318
     Region          36..125
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mssptvpgpv pidpqyvayw qhlraaqsva qgqaydlawr eareiaacly rdfgairvlv
       61 fgslvrdrft edsdidlaae gipperyfaa vaqanqlstr wvdlkpleal epyfrqrvla
      121 tgvdldath
//
LOCUS       WP_008313531             770 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Leptolyngbya sp. PCC
            6406].
ACCESSION   WP_008313531
VERSION     WP_008313531.1
KEYWORDS    RefSeq.
SOURCE      Leptolyngbya sp. PCC 6406
  ORGANISM  Leptolyngbya sp. PCC 6406
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Leptolyngbyales; Leptolyngbyaceae; Leptolyngbya group;
            Leptolyngbya.
REFERENCE   1  (residues 1 to 770)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 770)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 770)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..770
                     /organism="Leptolyngbya sp. PCC 6406"
                     /db_xref="taxon:1173264"
     Protein         1..770
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=84285
     Region          8..725
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mtpskfpsss fdpvstlcpy cgvgcglavq ppalpgrpvn rdkagnplwq vrgdrahpss
       61 qgmvcvkgat vaealdqdrl kypmirdsld apfqrvtwdd aldricdriq tlrrtlgsqs
      121 icmygsgqlq tedyyvaqkl lkgclgtnnf dsnsrlcmss avagytqsfg sdgppccyad
      181 leltdcafli gtnaaechpi aynrlrkyhk kqrgkvkliv vdprrtqtar dadlhlaiap
      241 gsdipllhgi ahlllrqgwi dpefitncte gftayteila hyppervail cgirqqdlet
      301 aaqwwgesqr vlslwsmgmn qssegtakvr slinlhlmtg qvgkpgagpf sltgqpnamg
      361 gretgglahi lpgyrsvtnp qhrqeleqaw glppnsispq pglaardmvl alerghlgll
      421 wivatnpavs lpdlvrtkaa lraspftvyq dayyptetaa yahillpaaq wgektgtmtn
      481 sermvtlcqq frlppgqarp dweifaevgr rlgftdqfdf pssaavhgef vhltqgrlcd
      541 msglshdrla tegaiqwpcp qgetvpatqq dkrlyedrif atangrahfa achekglaep
      601 pdpaypfvlt tgrlyghwht qtrtgrieki rtlhpipqle mspldaqrlh lqsgnwvevr
      661 srrgrarlqv lvtqyirqgt vfmpmhwgal waeeaecnal tvpnvcpesl qpelkacavq
      721 vipvstvaed satdrsthgt thgtangatd emiadsavap asaiaiahkt
//
LOCUS       WP_008314000             321 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Leptolyngbya sp. PCC 6406].
ACCESSION   WP_008314000
VERSION     WP_008314000.1
KEYWORDS    RefSeq.
SOURCE      Leptolyngbya sp. PCC 6406
  ORGANISM  Leptolyngbya sp. PCC 6406
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Leptolyngbyales; Leptolyngbyaceae; Leptolyngbya group;
            Leptolyngbya.
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
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Leptolyngbya sp. PCC 6406"
                     /db_xref="taxon:1173264"
     Protein         1..321
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=35289
     Region          4..315
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mgtiefhqvs lhfpqaprpa vkavsvqiqr gelvvllgps gcgkttllkm vnrlyepsag
       61 witlegqdic rlpptqlrqn igyviqqsgl fphmtvaqni avvprllgws rpriqsrvea
      121 lldlvklspg efrdrypaql sggqqqrvgi aralagdpey llmdepfgai daitrsalqg
      181 eilrlqhqlr ktilfvshdv eealrladri lvlrqgevvq fdtpfrlltq padpfvhdll
      241 gaddrvrqlg llriapamap lpnspirngq ptltpedslr dalslilktg fpeitvvhng
      301 rpvglltldh irtsamggtq n
//
LOCUS       WP_008316494             132 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Wohlfahrtiimonas chitiniclastica].
ACCESSION   WP_008316494
VERSION     WP_008316494.1
KEYWORDS    RefSeq.
SOURCE      Wohlfahrtiimonas chitiniclastica
  ORGANISM  Wohlfahrtiimonas chitiniclastica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cardiobacteriales; Ignatzschineriaceae; Wohlfahrtiimonas.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Wohlfahrtiimonas chitiniclastica"
                     /db_xref="taxon:400946"
     Protein         1..132
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14306
     Region          1..128
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mhkkgftlie lmivvaiigi iamfavpsyq naqrktkiae giaaltaaqs qiektrlekr
       61 ktyneitlae aniantvkhg sttiyqlayk hdagkqytlt ataqgdwlka adpcktielk
      121 ssgaitppec qk
//
LOCUS       WP_008316807             112 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Wohlfahrtiimonas].
ACCESSION   WP_008316807
VERSION     WP_008316807.1
KEYWORDS    RefSeq.
SOURCE      Wohlfahrtiimonas
  ORGANISM  Wohlfahrtiimonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cardiobacteriales; Ignatzschineriaceae.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 112)
  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   3  (residues 1 to 112)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 112)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Wohlfahrtiimonas"
                     /db_xref="taxon:582472"
     Protein         1..112
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12251
     Region          6..112
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 msvkqmqlef kdfeqvanvy mdfvvgggff ipmqtvnyql gdeifialil pddpgkrnpa
       61 atkvvwinte nsrkgkpgig vqltgmnagp lnerlkkcvg sakkkspftl tm
//
LOCUS       WP_008316949             107 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Leptolyngbya sp. PCC 6406].
ACCESSION   WP_008316949
VERSION     WP_008316949.1
KEYWORDS    RefSeq.
SOURCE      Leptolyngbya sp. PCC 6406
  ORGANISM  Leptolyngbya sp. PCC 6406
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Leptolyngbyales; Leptolyngbyaceae; Leptolyngbya group;
            Leptolyngbya.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Leptolyngbya sp. PCC 6406"
                     /db_xref="taxon:1173264"
     Protein         1..107
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12044
     Region          13..103
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 malqvsnfsl sdqavaefcq rwqvqtlalf gsvlrpdysp nsdidilitf spiakrgllt
       61 lakmkheled mtgrkvdlvv rqsvldsanw lrrqhilnsa qviyear
//
LOCUS       WP_008317265             550 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Leptolyngbya sp. PCC 6406].
ACCESSION   WP_008317265
VERSION     WP_008317265.1
KEYWORDS    RefSeq.
SOURCE      Leptolyngbya sp. PCC 6406
  ORGANISM  Leptolyngbya sp. PCC 6406
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Leptolyngbyales; Leptolyngbyaceae; Leptolyngbya group;
            Leptolyngbya.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 550)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Leptolyngbya sp. PCC 6406"
                     /db_xref="taxon:1173264"
     Protein         1..550
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59957
     Region          29..>419
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mlqrflinpv vrflsssvll tslvvsggll tvralgvlqe neltaydrfv rwqpdegpde
       61 rllvvginek diqsrqedpi qdgtiadvla alqeheprai gidigrdipq gpvegrerml
      121 aaiqsdpnii mvcllsspnf pgvpvppevs eaqvgfadlp idpngivrrg llfsvpeapp
      181 mmpvgrhlcn danldfdlps fslllavayl egegievgat eamelafgdr vipslsngfg
      241 gysteelppy qtmiryrsar navevvglse vlegqvppek irdrvvlvgy tslvakdlft
      301 tpylaaqeyv rempgvvvha qivsqllaat legralvwsl pspvewlliw lwglgggvia
      361 yrlrraslcw lilglavaat wgstyglflt gawlpvvpms lnlvlcgvaa ggvkqatrqg
      421 ytqalyemik gqlqedveae esqndyfgal vqraqtirsg eapkarskka mdlndpemqa
      481 iladiraqav adfareqqtl gpqattpsnr rqrqqqqrve allarsrqvr ttleqaapsl
      541 psekglesiq
//
LOCUS       WP_008318804             172 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Leptolyngbya sp. PCC 6406].
ACCESSION   WP_008318804
VERSION     WP_008318804.1
KEYWORDS    RefSeq.
SOURCE      Leptolyngbya sp. PCC 6406
  ORGANISM  Leptolyngbya sp. PCC 6406
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Leptolyngbyales; Leptolyngbyaceae; Leptolyngbya group;
            Leptolyngbya.
REFERENCE   1  (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   2  (residues 1 to 172)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Leptolyngbya sp. PCC 6406"
                     /db_xref="taxon:1173264"
     Protein         1..172
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19422
     Region          105..171
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mprsplqhfh plrqrlrqnp qtrlrsrgev eiaaamglgi danratiddw lrlpgisihq
       61 artlteltrs gviffaledv aaalglpvaa ldplapgiqf ryydtdslvp tpidlnqatv
      121 eqlcrvpelp rdwaewivrs rlagpyrsle dfqhrcqvpp aamsrwlhhl ri
//
LOCUS       WP_008325560             168 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: pilin [unclassified Herbaspirillum].
ACCESSION   WP_008325560
VERSION     WP_008325560.1
KEYWORDS    RefSeq.
SOURCE      unclassified Herbaspirillum
  ORGANISM  unclassified Herbaspirillum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="unclassified Herbaspirillum"
                     /db_xref="taxon:2624150"
     Protein         1..168
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=17525
     Region          7..167
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkpvvtrrpq qgftllelmv tlaiigilam lgasqyqdyi ararvsegfn laepyklavt
       61 eqissnngvf tvaqlglpaf tatdnvskie vspmekrgvg gvititygpr vgdggtltlt
      121 ptitsgtiqw qcaakdvkqa ptpegatpnt gfvagtlpak fapancrg
//
LOCUS       WP_008325969             703 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Herbaspirillum sp. GW103].
ACCESSION   WP_008325969
VERSION     WP_008325969.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. GW103
  ORGANISM  Herbaspirillum sp. GW103
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Herbaspirillum sp. GW103"
                     /db_xref="taxon:1175306"
     Protein         1..703
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=76460
     Region          29..703
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mktsqatllf ahdlriatst lvslamlgwp laslaqqpaa aqvqsglepi qvsgdwlgtg
       61 lessvrtypg arsvvkkqei dstgaisigd vmrripgvqs sdnagtagsa ialnigvrgl
      121 tgrfsprsti lldgipmava pygqpqlsfa plslnniesi divrgggavr fgpqnvggvi
      181 nfktrsipat tgisgdasvr ynsygqgggn tqttafaggq ndngigmafl ysgqdgrgwr
      241 dksdehlndf alkmrytlsp saelyakfny ydvmsrtpgg lttaqyaadp fqntrprdnw
      301 sgtrkgfdlg ylntisdhqe feirsyfnqa trqstlinaa rvqlshqprn yetlgiepry
      361 thrlawgsvt hdvtvgyrhv rergddnlyn esvrtgalsg faqfrnstda hagyiddkia
      421 fgqwritpgl rfehvrstrv dvnkkasyet gsnkplpsin vaylltgqlt lfsnyntsfg
      481 vvqnsqlntm ssanplspel drtmeagarw ksaqasaeat lfhldfdnqi vsvqgtnpsv
      541 frnigktrhd gielaadytf dqqgplqgws vfanytytra lqksgsnpgk dlpfyarttd
      601 tlgarfksgp wgvslstthq srqfadeant laestdgslg eipgfrlwha qaswkvpgrk
      661 gldvtaginn ltdhryftrt vdgnpgklvg aprtlyvqgr yaf
//
LOCUS       WP_008325990             381 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [unclassified Herbaspirillum].
ACCESSION   WP_008325990
VERSION     WP_008325990.1
KEYWORDS    RefSeq.
SOURCE      unclassified Herbaspirillum
  ORGANISM  unclassified Herbaspirillum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 381)
  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 381)
  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   3  (residues 1 to 381)
  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   4  (residues 1 to 381)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 381)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 381)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="unclassified Herbaspirillum"
                     /db_xref="taxon:2624150"
     Protein         1..381
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39899
     Region          30..369
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(106..108,129..130,179,231,255)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mqkikmipva talvaafafa gaaqaqevik ighvapltgp nahigkdnen garmavdeln
       61 akgfmiagkk vtfqlvaqdd asdpkqattv aqalvdakvk gvvghmnsgt tipaskiyyd
      121 agipqispsa tnpkytqqgf ntafrvvand gqlggvlgry avnelkgksv aviddrtayg
      181 qgvaeefrks amaagativa tqyttdkatd fnailtsvks kkpdlvffgg mdavagpmlr
      241 qmdqlgisak fmggdgictt elpalagagl kdsevvcaea ggvteagkkp ledfkaaykk
      301 kfnqdvviya pytydalmtl adamqqagss dpkvylpfla kihhkgvtge iafdskgdil
      361 ngtltlytyk ggkrtllsvv k
//
LOCUS       WP_008326537             332 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Herbaspirillum
            sp. GW103].
ACCESSION   WP_008326537
VERSION     WP_008326537.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. GW103
  ORGANISM  Herbaspirillum sp. GW103
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 332)
  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   2  (residues 1 to 332)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Herbaspirillum sp. GW103"
                     /db_xref="taxon:1175306"
     Protein         1..332
                     /product="aminoglycoside 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=36707
     Region          25..249
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mekaqliatv tallraesla rdevtlsamg gggnnrvfla tseagrfvvk ayfndpadsr
       61 drlgaeyafl ayardigldv vpqaiardta qhigvyefia gqkmtasqlr rehvlaaaqf
      121 iadlnadtrh ghalapasea cfeveqhlai vdrrlaalqk iptndvlgre vhtlvremaa
      181 wwrsqrprit ssaiapldsa drcispsdfg fhnalsasdg qlhfidfeya gwddpakmag
      241 dffcqpevpv pskyvddfma vafqyspraq ilrdrtasll paaqikwcci mlneflvsaa
      301 rrrqfadpss tpeqrkraql dkahqffhsr la
//
LOCUS       WP_008328199             251 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [unclassified
            Herbaspirillum].
ACCESSION   WP_008328199
VERSION     WP_008328199.1
KEYWORDS    RefSeq.
SOURCE      unclassified Herbaspirillum
  ORGANISM  unclassified Herbaspirillum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  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   3  (residues 1 to 251)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="unclassified Herbaspirillum"
                     /db_xref="taxon:2624150"
     Protein         1..251
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28016
     Region          35..247
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 manhdeiddd spyrvhsrre iialltsmme knqllsllik ggsesvitsi levdddddsl
       61 iidaapsaml nesivsskri nfealynsir itfavdgarq veyqsrpalr vdipeslvrl
      121 qrreyfript piakplrctf ritqpdgsfi tvvtllnnis aggvgitdek kllpttpgvt
      181 yedcqlelgd ntlvsvklqv rdckefkmtn gkvvnrfglq fidiprtvla aiqrfitkle
      241 reqnakasgm m
//
LOCUS       WP_008328477             415 aa            linear   BCT 20-JAN-2025
DEFINITION  AAA family ATPase [Maritimibacter alkaliphilus].
ACCESSION   WP_008328477
VERSION     WP_008328477.1
KEYWORDS    RefSeq.
SOURCE      Maritimibacter alkaliphilus
  ORGANISM  Maritimibacter alkaliphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Maritimibacter.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Liu,Y., Sung,S., Kim,Y., Li,F., Gwon,G., Jo,A., Kim,A.K., Kim,T.,
            Song,O.K., Lee,S.E. and Cho,Y.
  TITLE     ATP-dependent DNA binding, unwinding, and resection by the
            Mre11/Rad50 complex
  JOURNAL   EMBO J 35 (7), 743-758 (2016)
   PUBMED   26717941
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Chen,Z., Luong,T.T. and Lee,C.Y.
  TITLE     The sbcDC locus mediates repression of type 5 capsule production as
            part of the SOS response in Staphylococcus aureus
  JOURNAL   J Bacteriol 189 (20), 7343-7350 (2007)
   PUBMED   17704228
REFERENCE   3  (residues 1 to 415)
  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   4  (residues 1 to 415)
  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
REFERENCE   5  (residues 1 to 415)
  AUTHORS   Hopfner,K.P., Karcher,A., Craig,L., Woo,T.T., Carney,J.P. and
            Tainer,J.A.
  TITLE     Structural biochemistry and interaction architecture of the DNA
            double-strand break repair Mre11 nuclease and Rad50-ATPase
  JOURNAL   Cell 105 (4), 473-485 (2001)
   PUBMED   11371344
REFERENCE   6  (residues 1 to 415)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Maritimibacter alkaliphilus"
                     /db_xref="taxon:404236"
     Protein         1..415
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45403
     Region          3..236
                     /region_name="SbcC"
                     /note="DNA repair exonuclease SbcCD ATPase subunit
                     [Replication, recombination and repair]; COG0419"
                     /db_xref="CDD:440188"
ORIGIN      
        1 mtklrklsvs gfrgarfalp vdftnksrsl aifgenaagk stitdalewf ltdrvghlwr
       61 edckqealrh vliaeeddst vavefigdnl tgekrlssal ktntdlandn tralveglqh
      121 driilrhadi vafldqqkga krkaiadiig yeeinkfrda iqgtlnalkr epaytgaktn
      181 aetlagdmvr dvgqivpdrq aflaisqtia apfklgteit devtfagavk alnalgnsee
      241 kikkaqrldq lakactalat eistfvsdae afvasynala keresvnqlr lseflgkgha
      301 viesndyvdd acpfclseye lgtlqgevak rieamsaiqq rldtakaqkd evlkailaig
      361 mqaktigety tdltgfddlm vatttarkll waahqgitaa fdsltvydap rwlrr
//
LOCUS       WP_008328669             827 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Maritimibacter alkaliphilus].
ACCESSION   WP_008328669
VERSION     WP_008328669.1
KEYWORDS    RefSeq.
SOURCE      Maritimibacter alkaliphilus
  ORGANISM  Maritimibacter alkaliphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Maritimibacter.
REFERENCE   1  (residues 1 to 827)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 827)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 827)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..827
                     /organism="Maritimibacter alkaliphilus"
                     /db_xref="taxon:404236"
     Protein         1..827
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=91002
     Region          25..824
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 maslfkwmvr gvsavlvlav lalafvyyla srslpdyeae rsvigleapv eivrdnhdvp
       61 hifgktdndv yfalgyahaq drlwqmvtmr rtvqgrlsem fgertlktde lmrrldlyrl
      121 aqasveaqdd atkaaltaya rgvnawldrv ndealgrgap efflfdnais pwvpadsiai
      181 lklmgvqlag hieeevlrar vslsldedrv adilpdmpgs gvaalpdyas lfpdrpdatq
      241 faayddsped allypaadrg lggasnawaa apdrsaaggt llandphlgf saptiwylar
      301 lelasgavig gtlpgvpavl lgrsadfawg ltssylddqd vfiekvnpen paevmtplgy
      361 qpltqrssii rvkdaapvti nlqwsdngpi ipgkhynlas vtppghvasl gwtllagndr
      421 smtaamklmq aksvvqgiea grdfvapsqn vtmidrdtia lktigamprr dadhmtfgrl
      481 papgwreenr wvgreayaan pqfvspsggi vgntnnklle rpfplhvsyd wgdsqriqrw
      541 eflmqnrevh tresfieaql divsptarnl lplvgadlwf tgeaapegtp drkrqqaldl
      601 lanwngemne hlpepliyma wmralqnrli rdemgplatv fhhvepifie rvyrdvdgas
      661 vwcdvvqsap tetcteiare alddallwid ehygssyesl rwgdaheath dhqvlgdlpv
      721 lkwfvnirqs tsggdntllr gktsgrdpdp flnvhgagyr gvydfadpds slfitstgqs
      781 ghflsrhydd lgdlwrrgey vpmsldpdla raasvgttvl tpagpqn
//
LOCUS       WP_008329546             402 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [unclassified Herbaspirillum].
ACCESSION   WP_008329546
VERSION     WP_008329546.1
KEYWORDS    RefSeq.
SOURCE      unclassified Herbaspirillum
  ORGANISM  unclassified Herbaspirillum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 402)
  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 402)
  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   3  (residues 1 to 402)
  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   4  (residues 1 to 402)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 402)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 402)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 402)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="unclassified Herbaspirillum"
                     /db_xref="taxon:2624150"
     Protein         1..402
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42920
     Region          49..385
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(125..127,148..149,198,250,274)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mniktraist isgklmtraa rrhllalala gvwcsmagss awatprtvvi glaapmsgps
       61 gstgvslera aqlavddinh gkpviggepv lfrllpqddr adprtgelia dyfvkskvaa
      121 vvghwnsgvg vpaariyaaa giphvapavt apaytqqgda safrivphdg egarltadyv
      181 vrelkarnia viddstlfgs tyadefaksv kvlqgrvtgr ytvssktsdf nnvlrsirds
      241 epdvvlfagl daqaaqlvqd mrrlqirapl vgigglvgpt flrlagpsge gvsvvepglp
      301 sykgpqwrhf eqawkaawqd eiylyapfay davrviaaam qqadstdpgk vtaslhrigy
      361 kgitgniafd aqgnlrdpvf tlyrvngghw rvvrsmaqhd rn
//
LOCUS       WP_008329877             214 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [unclassified Herbaspirillum].
ACCESSION   WP_008329877
VERSION     WP_008329877.1
KEYWORDS    RefSeq.
SOURCE      unclassified Herbaspirillum
  ORGANISM  unclassified Herbaspirillum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 214)
  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 214)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 214)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="unclassified Herbaspirillum"
                     /db_xref="taxon:2624150"
     Protein         1..214
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23170
     Region          1..207
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 maydleeqeq ldsikawwak ygnlvtwali ivlaayaawt gwntyqgrqs aqasvlyeeq
       61 qkslaakdna kvqraaadiq dkfsgtayae msalvaaksa fdandmeaak kqlqwvidhg
      121 rgkeykaiaa vrlagvllda kaydealkvl sgdypaqfag aiadrkgdvl aaqgkrdear
      181 tayklaleks dakdparqli qikldaigge apka
//
LOCUS       WP_008330042             191 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Maritimibacter].
ACCESSION   WP_008330042
VERSION     WP_008330042.1
KEYWORDS    RefSeq.
SOURCE      Maritimibacter
  ORGANISM  Maritimibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 191)
  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 191)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 191)
  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   4  (residues 1 to 191)
  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   5  (residues 1 to 191)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Maritimibacter"
                     /db_xref="taxon:404235"
     Protein         1..191
                     /product="TRAP transporter small permease subunit"
                     /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=20353
     Region          <52..174
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mtdvnrpadp tgpgptdpal lrlvdglala laliagvalv llavnvlvdv tgraamnrpf
       61 pgtleytqnw wmptltlmaf aftewkqehi kvtilldtlp atmrrmvegv fgliatvlll
      121 vlayhafnea mdaaafgktt sssppvavwp tmfmapagvl alalqtaats fryfsgrypl
      181 pdtvhaegea v
//
LOCUS       WP_008330539             201 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Maritimibacter alkaliphilus].
ACCESSION   WP_008330539
VERSION     WP_008330539.1
KEYWORDS    RefSeq.
SOURCE      Maritimibacter alkaliphilus
  ORGANISM  Maritimibacter alkaliphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Maritimibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Maritimibacter alkaliphilus"
                     /db_xref="taxon:404236"
     Protein         1..201
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=22144
     Region          <1..123
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 masaeaaldr lcspehevsc hyliaqdgal wqmveedrra whagqgdwgg rgdvnsrsig
       61 ieldnsglvp ftepqmaalt tlisdirgrw siplhgvigh sdfaplrksd pgrrfdwrrl
      121 aregqavwpd pndegaqpre eaflgaarif gypvgegfga vldamrqrfr pwargpfdgr
      181 dmaiirdlad rfpvdrgapa a
//
LOCUS       WP_008330846             807 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Maritimibacter alkaliphilus].
ACCESSION   WP_008330846
VERSION     WP_008330846.1
KEYWORDS    RefSeq.
SOURCE      Maritimibacter alkaliphilus
  ORGANISM  Maritimibacter alkaliphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Maritimibacter.
REFERENCE   1  (residues 1 to 807)
  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 807)
  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 807)
  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 807)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..807
                     /organism="Maritimibacter alkaliphilus"
                     /db_xref="taxon:404236"
     Protein         1..807
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=84863
     Region          209..805
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 masapvkplt pfllddkraa tafawaafai lclvaetiis lkfnlyryaa lpvgwapegi
       61 twlrllalia tagfvwkvas derrtalwfg laalalltvd alvgfhfapp fdpemdlray
      121 eypilrvgdf girvvpilsm glvaaalflm qslrnlehgr araamiagll mgltglisvl
      181 paipfatigl aawrgeyipd mfgigpaspt ekynaimfll aalivvltlg rseedigrvq
      241 hrglaigdwi afaalgyavl qylvigtetf glgvsdahta vigclailyl cwrvfgaala
      301 lcgavalayy fassylpgif halalgytsa aenlwfntad avlgsklsil lnnvlpfiif
      361 gallsatgaa dslikisfyl mrnarggpah aavlasglfg svsgsavsnv vgtgvvtipm
      421 ikkrgfradf aggveatast ggqimppimg aaalvmadlt gtpylnimta alvpalayyl
      481 slfatvrfes rrldmsaqgs deldpvttqd yinvlllvfl plaviiwrli agaspagsal
      541 taiivvlals afspvvrrap iilltaiadg gktfgrllmv vgvvgiivgv mdatdlpsrl
      601 grsisdyaev allltlvita vvslllgmgm ptlpayltvi iilgpalnsl glslmtshmf
      661 vfyfgvasai tppvavaafa aaaiagakpi gtgiaavrig ivifavpfmf alnpdmmivp
      721 eafddgaafs migflsaifr tlamiylfas amsrfdrhrl hpvevllrvg lallliaplp
      781 avhlvafaga lgivgqhylr aqkeqta
//
LOCUS       WP_008332101             400 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Maritimibacter alkaliphilus].
ACCESSION   WP_008332101
VERSION     WP_008332101.1
KEYWORDS    RefSeq.
SOURCE      Maritimibacter alkaliphilus
  ORGANISM  Maritimibacter alkaliphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Maritimibacter.
REFERENCE   1  (residues 1 to 400)
  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 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   3  (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   4  (residues 1 to 400)
  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 400)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Maritimibacter alkaliphilus"
                     /db_xref="taxon:404236"
     Protein         1..400
                     /product="CmpA/NrtA family 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=42858
     Region          6..257
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mkgavlsvgf iplvdaapli vaqemgfaae egltldlvra pswsslrdml vfgrvdaahm
       61 lspvpvatam glggagadls alavlsvngt vigvsraleg rlrdnghgfd frdarsagea
      121 liaakvdrlr igvpfplsmh aellyywlss lglpapqgvd iktmppplma daieageida
      181 fcvgepwgsi avengvgall lpgksiwsfs pekvlavrsd wasaetglsa rliravyrsg
      241 rwiadpesrl ltaellsrpe yldlppevie ralsgnliis srgeqrtvdg fvgfhkgaan
      301 fpwrsqaqwi anqlaarmgl dreeslrqaa qvfrpdlyra alegialdlp gasskiegsi
      361 evetpvasey grltlppdlf fdrrtfdpda tirskithkn
//
LOCUS       WP_008332103             194 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Maritimibacter].
ACCESSION   WP_008332103
VERSION     WP_008332103.1
KEYWORDS    RefSeq.
SOURCE      Maritimibacter
  ORGANISM  Maritimibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 194)
  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 194)
  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   3  (residues 1 to 194)
  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   4  (residues 1 to 194)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 194)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 194)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Maritimibacter"
                     /db_xref="taxon:404235"
     Protein         1..194
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21291
     Region          3..194
                     /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"
ORIGIN      
        1 mkdklsvviv eknrergili eeslrvagdf evtvvaetnd lagkikdlkp dvvlvdienp
       61 srdtleelal asgplerpva mfvdtsdegl traaieagvs ayvvdglksd rlkpildaav
      121 trfnmfqrmr velettkral eerklidrak giimkarkvd edeayailrk aamdqnkrva
      181 dvaqalvtta glls
//
LOCUS       WP_008333052             356 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-oxoacyl-ACP synthase III family protein
            [unclassified Herbaspirillum].
ACCESSION   WP_008333052
VERSION     WP_008333052.1
KEYWORDS    RefSeq.
SOURCE      unclassified Herbaspirillum
  ORGANISM  unclassified Herbaspirillum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 356)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="unclassified Herbaspirillum"
                     /db_xref="taxon:2624150"
     Protein         1..356
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37353
     Region          14..336
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mpdttsalhs rlagihlrgl vaalpaqted adtltrqwgy enahkvaaat gihtrhlvpp
       61 gmtacdlgea aarklleglq wpadsvdlli vvtqtpdypl pgnapllqhr lglrkhcgsl
      121 ditsgcsgfv dglwvassll assngrrall vvgdtttqfv ppqdhntrpl fgdavcaial
      181 ergdqdsgfl avvpgvdgsg apyltvrdga arhpvddacf ghlfmdgaqv faftlrqvpk
      241 niaaamevag wnnadvdyll lhqanetmlr hlankvgfse qqmvlaldgf gntssasipl
      301 aiasalagpa vqataplnll msgfgvgwrw asaawrtapl qyceivevas paasss
//
LOCUS       WP_008333422             278 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Maritimibacter alkaliphilus].
ACCESSION   WP_008333422
VERSION     WP_008333422.1
KEYWORDS    RefSeq.
SOURCE      Maritimibacter alkaliphilus
  ORGANISM  Maritimibacter alkaliphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Maritimibacter.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 278)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Maritimibacter alkaliphilus"
                     /db_xref="taxon:404236"
     Protein         1..278
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=31329
     Region          32..261
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mrfeipdepd vvlsspltia iqqrdrdtma mvrravqtkq vmlafqpvmr aqaadtvafy
       61 eglirvldht griipakdfi dvveeqelgr iidalalelg laaleeepsl tlsinmsars
      121 igyprwktvl rqglerdptl gerlileite rtaivmpdlv qvfmsemqae gisfalddfg
      181 agytafrylr dlyfdilkid gefirgiadn pdnqviaqam lslarhfdmm tvaecvetle
      241 daqfmadngc dflqgyffga ptirpwwkge gleqrqra
//
LOCUS       WP_008334089             385 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Maritimibacter
            alkaliphilus].
ACCESSION   WP_008334089
VERSION     WP_008334089.1
KEYWORDS    RefSeq.
SOURCE      Maritimibacter alkaliphilus
  ORGANISM  Maritimibacter alkaliphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Maritimibacter.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 385)
  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 385)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Maritimibacter alkaliphilus"
                     /db_xref="taxon:404236"
     Protein         1..385
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43761
     Region          1..385
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 miatrltnrd arrlwlaahg lldaptrapd vmaiirdlgf lqidtirnvv rahdhilwsr
       61 ahtyregrvw rhlarrelfe hfthdaslip revlpdwhrq frrlgakaar gawyqsglar
      121 geidairari aeegalstha fdtkvesrem warpphkkal dqmwyagdla tchrenfvkf
      181 ydlgdrvlgg idhgrseaeq agalhdaama rlglanasel nrywdatgpa eardwterad
      241 lvpveveaad gtvarsfahp ehlarlpdla dpttririvn pfdpafrdra rterlfgfhy
      301 rnemfvpqak rvygyyvypl legdrfvgrt evkadkasgm ltvtgfwpep svrwgagrta
      361 rldaeldrfa rfggqagvtw tcprp
//
LOCUS       WP_008334230             378 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Herbaspirillum sp. GW103].
ACCESSION   WP_008334230
VERSION     WP_008334230.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. GW103
  ORGANISM  Herbaspirillum sp. GW103
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 378)
  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 378)
  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   3  (residues 1 to 378)
  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   4  (residues 1 to 378)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 378)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 378)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Herbaspirillum sp. GW103"
                     /db_xref="taxon:1175306"
     Protein         1..378
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39931
     Region          31..367
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(107..109,129..130,179,231,255)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mfkrvsglni iaaslalipa famaqdtqvv kigfsspltg pqasagkdnq gglmmaverl
       61 naqpitvggk kikfeviaed dqadpkqgva vaqkladegv kaivgpynsg vtipasrvyn
      121 dagivvatva snpkitqqgf atlfrvaasd sqlggkmaly aakelkfkrv aviddrtayg
      181 qglaeeftkv akangievis kdftndkatd ftailtsikg kkpdavflgg yapqggpikr
      241 qmkqlgidvp lmggdgicsp emgrlggdai gesvyctqgg tmldkakdgk vfaddyqkky
      301 nrpaetyavs fydgmmliaq amkqansvep kafgpalaki sykgvagqyd fdanhdlkqs
      361 pvtvyrfkdg lpvpltsy
//
LOCUS       WP_008334462             757 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Herbaspirillum sp. GW103].
ACCESSION   WP_008334462
VERSION     WP_008334462.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. GW103
  ORGANISM  Herbaspirillum sp. GW103
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 757)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 757)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..757
                     /organism="Herbaspirillum sp. GW103"
                     /db_xref="taxon:1175306"
     Protein         1..757
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=83288
     Region          29..705
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mlrrlrtala kywgrwllal lliglaeamv sgllpnpvve rmdlffydlr mrvakpaldp
       61 rivivdider sidelgrwpw srdlvaklvq qmtqtyqaqa vgfdvvfaep dttsgygrle
      121 dlahgplkdv pqlaqqlrml kpqmdydgrl aaalkgqpvv mgyafsnesg avvkgelppp
      181 aftvadlggr dvdvvrwray ganlpqlqsa araggffnpv pdddglirtv sllarhgdnf
      241 yeslalatar vavggkrikp vfltsadgll gsqkenydal aaiavearpq pliipverrl
      301 ttlvtyrghg gpqggayryv paidvirgty phdqldgrim lvgttvpgln dlratpvnpv
      361 ypgveihanl iasiidddfk trpdfaagyd gvqvalagll lglllpmlgp lasmllslgt
      421 agalawlnyw lydsagmvlp lasvlllval lfisnlgwgy lfeyrnrkai vnlfgeyvap
      481 elvaemaanp asynmegeir eltvmfsdvr gfttiseslq pnelreyinl yltamsedir
      541 gnrgtldkyi gdavmafwga pldvpdhaar avatalkmqq ttlllneeft rrnwpplkig
      601 igvnsgqmrv gdmgsrirka ytvmgdavnl ssrlesitkv ygvgvlvgea trqaapqfay
      661 reldrvrvkg knepvpifep laleseldad lraevqqwha alalvraqrw deaqhaierl
      721 qatqarglyt lyleriahfr qtppaahwdg vttfetk
//
LOCUS       WP_008334474             286 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Maritimibacter
            alkaliphilus].
ACCESSION   WP_008334474
VERSION     WP_008334474.1
KEYWORDS    RefSeq.
SOURCE      Maritimibacter alkaliphilus
  ORGANISM  Maritimibacter alkaliphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Maritimibacter.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Maritimibacter alkaliphilus"
                     /db_xref="taxon:404236"
     Protein         1..286
                     /product="formate/nitrite transporter family protein"
                     /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=30913
     Region          32..283
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mhdhspdrds papdpaleee eqqeeikeas klspttiyev irldgeeelr rnklslmwsg
       61 isagivisls vlgeaifrah lpdtparyli enlgyslgfl mvivgrmqlf tentmttvlp
      121 lldkpgwgvl grtavlwaiv lianvigafv valfyaygga lgddlmaamf elslhavgfe
      181 pgeafargip agvliaaivw mlpqvkdaav aiiviftwli aagdfthiva gsvemallmv
      241 vgdlsltdgv fdfflpvlag nviggtaift mliygqtrrd rerrlg
//
LOCUS       WP_008334538             150 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Maritimibacter alkaliphilus].
ACCESSION   WP_008334538
VERSION     WP_008334538.1
KEYWORDS    RefSeq.
SOURCE      Maritimibacter alkaliphilus
  ORGANISM  Maritimibacter alkaliphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Maritimibacter.
REFERENCE   1  (residues 1 to 150)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Maritimibacter alkaliphilus"
                     /db_xref="taxon:404236"
     Protein         1..150
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=16274
     Region          35..136
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(101..102,105,118..121,123)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mlapilaati fstttapasa eevfsssnra kqrivvrvdv seqrmtviqg gqrlydwdvs
       61 tarvgkytpr gtfqpqffsp nhrsskygga pmpwsvfydg dyaihgtdai srlgapasag
      121 cvrlhpdnak llyamifeag kaetfivvqd
//
LOCUS       WP_008335724             616 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter permease [Rhodobacterales].
ACCESSION   WP_008335724
VERSION     WP_008335724.1
KEYWORDS    RefSeq.
SOURCE      Rhodobacterales
  ORGANISM  Rhodobacterales
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria.
REFERENCE   1  (residues 1 to 616)
  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 616)
  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 616)
  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 616)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Rhodobacterales"
                     /db_xref="taxon:204455"
     Protein         1..616
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=64239
     Region          1..604
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mrtivmvlaa afaiwvihsn lfiisdpliq gilfvsgift ilflaigats rapdsipiyd
       61 wflsalslat gvyfyvtsga iadrisllde fttdqfffgs allfltieat rrttglgltg
      121 vvvlfliynl fgyllpppfg hrvsefsyll dilvfttdgl fgvplqvvas yvflfvmfgt
      181 flakagggdf ffnlaalvtg narggpakia iissglygtm sgsptsdvva tgsitipvmk
      241 rlgyrarfag avevaastgg samppimgsa afimaeysgi synaivlaal vpallyytgv
      301 faqvhfrsvk hnlrpsadei psaketfktg wvfllpiigi ivalilgysp tftagvgvlv
      361 tilaamilkd trlslwqlve glgattlqil pvagacaaag lvigglsmtg lgmksanvil
      421 tvsnmqpllt lviaalvtiv lglgmptpsa yilaavlvgp alaklgfptl psqmfllyya
      481 ilsaltppia vaaiaasaia dedpfkiafs avrlaivgfl lpfafvwnpg illelgplan
      541 tlavvgafag alavaasleg lvktqltaie rgvlpiaaig avspylavsa icilvivaml
      601 irqiafttes ahvdra
//
LOCUS       WP_008337783              83 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Sulfurimonas gotlandica].
ACCESSION   WP_008337783
VERSION     WP_008337783.1
KEYWORDS    RefSeq.
SOURCE      Sulfurimonas gotlandica
  ORGANISM  Sulfurimonas gotlandica
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurimonadaceae; Sulfurimonas.
REFERENCE   1  (residues 1 to 83)
  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   2  (residues 1 to 83)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Sulfurimonas gotlandica"
                     /db_xref="taxon:1176482"
     Protein         1..83
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8965
     Region          16..76
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkilamvilg fsilfgavdi ntadkeelms lkglgdkkaa avieyrakdc fesvegitkv
       61 kgigkkfiek nrdnliasec ktk
//
LOCUS       WP_008339648             159 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Sulfurimonas gotlandica].
ACCESSION   WP_008339648
VERSION     WP_008339648.1
KEYWORDS    RefSeq.
SOURCE      Sulfurimonas gotlandica
  ORGANISM  Sulfurimonas gotlandica
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurimonadaceae; Sulfurimonas.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Sulfurimonas gotlandica"
                     /db_xref="taxon:1176482"
     Protein         1..159
                     /product="TRAP transporter small permease subunit"
                     /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=17913
     Region          26..146
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 midngikylg yftalilall vllvvydata rylfstgsia lqelewhlfd viilfgiayt
       61 lkenahvrvd ifyatysekt kvivniissl ffilpfsfli iyigidfval sfsqneassn
      121 pggleyrflv kallplsfaf lalvafkdlk snyikwksl
//
LOCUS       WP_008340488             328 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Sulfurimonas gotlandica].
ACCESSION   WP_008340488
VERSION     WP_008340488.1
KEYWORDS    RefSeq.
SOURCE      Sulfurimonas gotlandica
  ORGANISM  Sulfurimonas gotlandica
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurimonadaceae; Sulfurimonas.
REFERENCE   1  (residues 1 to 328)
  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 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   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 328)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Sulfurimonas gotlandica"
                     /db_xref="taxon:1176482"
     Protein         1..328
                     /product="CmpA/NrtA family 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=36119
     Region          25..289
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mlkkiiglgl glslvaasll aaelekkklt igfialtdca piviaeekgf fkkygldvhv
       61 vkegggwpgi qqkvisgeyd fshalagmpi aatlgingna nlqavlsldf ngngitfgnn
      121 iikemkkygm detkrplgse slkkyidakh kaegssyqpl sfgmvhpvst hnyelrywma
      181 ssgivpdrdt tikpfppptm psnliagnie gycvgepwne rivlkkkgst lvtnydiwnn
      241 npekvlqtra dfieknpett kavmkailea qmwldaswen rkeaaiimsk pnyvkapvsv
      301 leksmtgtfq ysnyflstsf thlfslfi
//
LOCUS       WP_008342369             124 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Caballeronia].
ACCESSION   WP_008342369
VERSION     WP_008342369.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (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   2  (residues 1 to 124)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..124
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12188
     Region          20..81
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mfkqalssia afalifsigs afaavdvnta nsdalrgikg igpakakail derqahgpfk
       61 dasdlgtrvk gmggktvqrl eaegltigat tktaavaapp ggansavatp vsasasakpv
      121 ivkk
//
LOCUS       WP_008343079             166 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Bacillus].
ACCESSION   WP_008343079
VERSION     WP_008343079.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 166)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..166
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17549
     Region          7..161
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfhvekqsgd pskdyqllik qveaitdgep dlianlanaa allyhslpev nwagfylakd
       61 gelvlgpfng lpacvripsg kgvcgtafat gdvqriadvh afpghiacda asqseivipl
      121 kvngqiigvl didspvkdrf naidetylvq ftevvqnals astdvs
//
LOCUS       WP_008343775             367 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: threonine synthase [Bacillus].
ACCESSION   WP_008343775
VERSION     WP_008343775.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 367)
  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 367)
  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   3  (residues 1 to 367)
  AUTHORS   Parsot,C.
  TITLE     Evolution of biosynthetic pathways: a common ancestor for threonine
            synthase, threonine dehydratase and D-serine dehydratase
  JOURNAL   EMBO J 5 (11), 3013-3019 (1986)
   PUBMED   3098560
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10107605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..367
                     /product="threonine synthase"
                     /EC_number="4.2.3.1"
                     /GO_function="GO:0004795 - threonine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009088 - threonine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40052
     Region          49..365
                     /region_name="Thr-synth_1"
                     /note="Threonine synthase is a pyridoxal phosphate (PLP)
                     dependent enzyme that catalyses the last reaction in the
                     synthesis of threonine from aspartate. It proceeds by
                     converting O-phospho-L-homoserine (OPH) into threonine and
                     inorganic phosphate. In plants; cd01563"
                     /db_xref="CDD:107206"
     Site            order(71,76..77,95,118,134,137..138,144,160..166,168..170,
                     182..183,214,327..328,330..331,362)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:107206"
     Site            order(101,127,227..231,360)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:107206"
     Site            101
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107206"
ORIGIN      
        1 mnqlicnhcg ekyemtptlw kcdcggvfnl vkdtpkidvt awdhypnslw ryvetmpfpk
       61 gsktwetvtm gegqsplivl dpnepntyvk vdymmptlsf kdrgaavlmt kakelgvtkv
      121 iadssgnagt aiaayaarcg iacdiylsdq tspkkvaqik ahgatikeih gtrediaaaa
      181 qkavdeenvf yashvynpyf fegtktyaye iyeqlkgapd aliipvgngt lllgayygfk
      241 elfenglihk ipkiiavqak ncaplvkafq haeesatpmt nkgtvaegia iaaparskqi
      301 leavyktngt fidieeeeil harsklsekg fyvevtsain fagymkyqke saesviiplc
      361 gagikst
//
LOCUS       WP_008344367             513 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [Caballeronia].
ACCESSION   WP_008344367
VERSION     WP_008344367.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..513
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54290
     Region          10..513
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 msttstdhav irlhpnddvv iatrqllsga riasedlvva glippghkia trdiaagapv
       61 krynqiigva keaiargqhv hthnlsmadf arehefgvdl hptpfvdkpa tfmgirredg
      121 rvatrnfvgv ltsvncsatv araiadhfrr dvhpealady pnvdgvialt hglgcgidmq
      181 geglgilrrt lagyavhpnf hsvlfvglgc etnqisgvle ssglkdgshl ksftiqdsgg
      241 trktiergia lvkemladan rvqreplpas hlivglqcgg sdgysgisan palgaavdkl
      301 vahggtails etpevygaeh lltrravsre vgeklltrik wweeycarng aamdnnpsag
      361 nkvgglttil ekslgavakg gttnlvevye yaqridakgf vfmdspgydp msatgqvasg
      421 anlicfttgr gsaygcapsp slklatntal werqeedmdi ncggvidgsa tieqlgdeif
      481 qmmldcasgv askselhgyg qsefvpwqvg vvt
//
LOCUS       WP_008344390             200 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Caballeronia].
ACCESSION   WP_008344390
VERSION     WP_008344390.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..200
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21325
     Region          8..195
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 msapaaakrr livaitgatg aiygvrllet lrrlsgveth llvssagwln iqheleldka
       61 avhaladvvh svrdvgatia sgsfatdgmv vapcsmrtla siahglsdnl itraadvmlk
      121 errrlvllvr etpfnlahlr nmtavtemgg vifpplpafy qkpasidemv dhtvarvidl
      181 fgfaqpvapa wrglrgeasd
//
LOCUS       WP_008344512             215 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Bacillus].
ACCESSION   WP_008344512
VERSION     WP_008344512.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 215)
  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   3  (residues 1 to 215)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..215
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24636
     Region          13..208
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mlqigdaiti eyvnenkevk takskvlenn nddicinypa dketgrtiyl nqeteitvff
       61 fdenqipykc tskvigkrke dipmivvsip pkeemirlqr reylrvdtmv kasitqngee
      121 tfdtfivnms aggvaiavpe gvslkeygev vtefelslke pvkikaiaem nrvyqdeqtg
      181 ktraimefie itndhqqhim kycfqqqllt rvkkv
//
LOCUS       WP_008344967             161 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Caballeronia
            zhejiangensis].
ACCESSION   WP_008344967
VERSION     WP_008344967.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia zhejiangensis
  ORGANISM  Caballeronia zhejiangensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (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   2  (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   3  (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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Caballeronia zhejiangensis"
                     /db_xref="taxon:871203"
     Protein         1..161
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17771
     Region          49..104
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
     Region          76..>158
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 matattsakv vslhtvsadk asdkkwgkpv mklgfcvvps vllraqqrlg lnptqlavll
       61 qladywwdpd rkpypskqal serlglgprq iqryiaelee eglvrrverr atnggklsne
      121 ydlsglverl kkiapeieaa nemkravtrr ggirkavvpl a
//
LOCUS       WP_008346355             295 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 5'-3' exonuclease [Bacillus].
ACCESSION   WP_008346355
VERSION     WP_008346355.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..295
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32762
     Region          1..275
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mnkhvllvdg mallfrsfya tavhrnfmin drgvptngvn gylkhlltav qtfepthivc
       61 cwdmgsqtyr nelfqdykan rgeapvelvp qfdlakeate elgimnigvt gfeaddcigt
      121 lasiyqnear vtvltgdkdl lqilneqvtv almqkgigny khytkalfee emgispkali
      181 dmkalmgdts dnypgvkgig ektalkfiqt yetidrllen vhaltaaqqk kmqagledlk
      241 lsrilaeikc dvplscpidq tkmninperv aamlrlhqik giepmvnrls qlgis
//
LOCUS       WP_008346317             191 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Caballeronia].
ACCESSION   WP_008346317
VERSION     WP_008346317.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..191
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20672
     Region          3..187
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mstrriavgi sgasgftygv rllellreld iethvtisrs alltmqqete hkladvnpla
       61 sftyrcddma aaissgsfst lgmivapcsm ktlaeiaggl ssslisraad vtlkerrplv
      121 llaretpytl ahlrnmiavt emggivappv pafyarpasl demidhtlgr vldlfgldcn
      181 vvrrwkehka d
//
LOCUS       WP_008347107             497 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [Bacillus].
ACCESSION   WP_008347107
VERSION     WP_008347107.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..497
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54244
     Region          4..497
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mrdfvvihps dnvgialkvl eqgeelqhqg htiilketva kghkfalaei kekeniikyg
       61 ypighastai stgewvhthn iktnlsgkld yeyrpslten pyektnltfk gykrkngasg
      121 irnelwivpt vgcvngiadq iiqiftaemg gsihpfetal vlkhnygcsq lgddhentkt
      181 ilqnavkhpn aggvlvlglg cenndiedfk atlgeydqtr vkflrsqevg deietgvall
      241 keiydaaked qrediplsel kiglkcggsd gfsgitanpl lgrlsdfiva qggttvltev
      301 pemfgaetil meraeskatf dnivqmindf kqyfmdhrqp vyenpspgnk aggistledk
      361 slgctqkagt svikdvltyg ellkrkglnl lsapgndlva ssalaasgcq lvlfttgrgt
      421 pfgtfvptmk vstntalyet kkhwidfnag elledvpedv vlekfiatvi dvasgkllnh
      481 eknnfrelai fktgvtl
//
LOCUS       WP_008346742             263 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Caballeronia].
ACCESSION   WP_008346742
VERSION     WP_008346742.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..263
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=29043
     Region          30..247
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mkdkpaiqla hgdashkctg crvpdsdvid lafafqpivd trngvayahe alvrgpnges
       61 agsvlarvde anryhfdqrc rtvaieqaas lemsgflsin fmpnavyqpe acirstfeaa
      121 ekfkfatdri ifetvegesv isrshlveif rayrrfgfqt aiddfgagys gltllaefqp
      181 dfikldmelv rgidtdsvrq sivrgvlsmc gdlgirviae gietrgerdf ffaqgvtlmq
      241 gyffakpafr slpaptedwt vqs
//
LOCUS       WP_008347553             321 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Bacillus].
ACCESSION   WP_008347553
VERSION     WP_008347553.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
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
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..321
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=36445
     Region          1..310
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 miefknvsmq fsddryavqs vdleiqkgef fvligpsgsg ktttlkminr lisstegeiy
       61 ikgrtisdyd iyelrwdigy vlqqialfph mtieeniavv pelkqwkrte tnqrvdelmf
      121 mvglepstyr hrkpaelsgg qqqrvgvara laadpeivlm depfsaldpl treklqddll
      181 elqrriqkti vfvthdmqea mklgdricvm negkvvqvgr peeliqhpvn pfvrefvsga
      241 arhvdhqafe lttiyqpmpq ddllgdevvs ihatleevls rlaeheelvv ekdgerigli
      301 trqaviqyla gtsaergeth e
//
LOCUS       WP_008346682             280 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Caballeronia].
ACCESSION   WP_008346682
VERSION     WP_008346682.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..280
                     /product="formate/nitrite transporter family protein"
                     /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=29702
     Region          32..276
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msesqagaes phldhdqreq aadhstphal viheivreeg etamertasa liwsglaagl
       61 smgfsflvqa ilqselpask sqhliaslgy tigfvfvilg rqqlftestl tavlpvltrr
      121 dlrtvgktlr lwsivllsnl vgtavfaall qfkdvfdpdv naalaevara pfsagfgvtl
      181 vravfagwli almvwllpsa rsarlltill vtytvgvskl thviassaea ayavmthaas
      241 igdyfgvfll ptllgnmigg ismvaivnha aiapeigdtq
//
LOCUS       WP_008347768             289 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Caballeronia].
ACCESSION   WP_008347768
VERSION     WP_008347768.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 289)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..289
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=31369
     Region          23..258
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mkrtthgspv akaapesdha frhrileglk agefciayqg iyrvhggela qmealirwrh
       61 peygvllpga fseafkdadi mreltwfvld avaseigewr esggahysva vnvppsvaal
      121 pgfaermesi crahditpdc ielellesed larmpamrkv vrrlknkgvs vamddfgtgy
      181 sclaalgpid fgtvkiakel laeaprcpna clvfssvltl ltrlkvaivv egvetaaqaq
      241 wiaqwphvla qgfflarpaf gignvpgali grpgtrrkeq qtirladaa
//
LOCUS       WP_008348021             302 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Caballeronia].
ACCESSION   WP_008348021
VERSION     WP_008348021.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..302
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32806
     Region          18..268
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 msaavraeri daagratvge cplwraqega lywvdiparr ivrleiesar rtewafdeqv
       61 acfafdkagr vvagmesgmf gvtladenqa havklaapsf patgmrfndg rcdrqgrfwa
      121 gtmvmdmsla savgalyrfd eqgalsesvv dglitqngla wspdgrtmyl sdshpqrrmi
      181 wafdfdpdtg rphaqrafad lhhyagrpdg aavdadgcyw tcandagrll rftprgeldr
      241 eivlpaskps mcafggsdlk tlyvttirpa mnatdddghv falnpgvqgl pepeyaallp
      301 va
//
LOCUS       WP_008349023             252 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Caballeronia].
ACCESSION   WP_008349023
VERSION     WP_008349023.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  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   3  (residues 1 to 252)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..252
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28241
     Region          43..248
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mlaeplpqtt diekfaedhe rfarhtpsei sivlrtlvqr gdmltvtsgr gqivtqllkt
       61 dareacivfd wggveadnrv llearqlyfk gapdgvrvef ttlaaravty egrqafevpf
      121 peklyqfqrr eyfrvptpvl epfyakgafa dgeafrhevh dlslggialr mdtprlaete
      181 rgtlfrdvvl hlgpgaalpv dlelvsprsv ttprgdvryv vgfrfvrlsa aaenvlqrli
      241 trmeakrrsl sa
//
LOCUS       WP_008349135             164 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Caballeronia].
ACCESSION   WP_008349135
VERSION     WP_008349135.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..164
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17523
     Region          10..160
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfsiseatha tkaaqyddll qqarallade tdfianaanf sslvyhtlpd lnwagfylfd
       61 gtelvvgpfq gkpacvrial grgvcgtaar errtqvvpdv hafpghiacd sasrseivvp
      121 lvgsdgalig vwdvdspvpn rfddedalgm ealcaefial awkk
//
LOCUS       WP_008349313             194 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Caballeronia].
ACCESSION   WP_008349313
VERSION     WP_008349313.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 194)
  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   2  (residues 1 to 194)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..194
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18844
     Region          18..80
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mlkkllmlcf sfvvsmgaaf aavdvntadq aalesvkglg pvkskaiide rtkngpfkda
       61 ddlatrvkgl gaksvtnleq ngltiggssl pptgkpskpa tpstqggsaa pnstvkssta
      121 atgatspaat taqtpattpa apasgtkask kskkdsaasa aasasspsaa seakpakskr
      181 skkdkaasaa aasq
//
LOCUS       WP_008353144             300 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Caballeronia].
ACCESSION   WP_008353144
VERSION     WP_008353144.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 300)
  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   3  (residues 1 to 300)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..300
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32016
     Region          105..298
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mteetvadar qslarlepse iplgtplewp ivaadgamlf dagavvpdga alefmfrhfe
       61 pnraiqaaap sapeeefakd gpltledigl tigarvglrg tggtgsamya srvigfstpr
      121 rngerslfvt qplmagfdpl vltlgeqvdl valtgrgvfr factvdatcr epfnyavlsa
      181 pgairrlrtr kfarmptrla ahfaavgepq salqlgrvsd ispygmsltv anpvahmger
      241 lqlsfqfrtd gvevkietia ivrhvgatdp adgsaaygle fetlepsqri alksfmaehs
//
LOCUS       WP_008353393             327 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Caballeronia].
ACCESSION   WP_008353393
VERSION     WP_008353393.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..327
                     /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=36069
     Region          4..268
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mdlrnrtida argigivlvv lghaiglpew lfrviyschm plffflsgyl fngkrgplev
       61 mrrnsrrllm pyavaaaiai fpsilfgntt slsqffvqlg gtaysiprsn ltfyctplwf
      121 ltclfcteam yaaltryarh vvhvviaasl vvgctlmafv kgfspwniki afvalfyfhl
      181 gfvaaeskml dgrrfpawtl plcalgwiia slwnpkaanl agetignpal fllasicgiw
      241 alarlarlta tsralsflgk ntlpifafny plnlfaqwlf apttpwfvfa asemalavgf
      301 vfllrripai arvfsiesgq rasptav
//
LOCUS       WP_008353280             641 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Caballeronia].
ACCESSION   WP_008353280
VERSION     WP_008353280.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 641)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 641)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 641)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 641)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 641)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 641)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..641
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68721
     Region          12..641
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mgstapglpa ddnhapkphg hpalmglsla algvvygdig tsplytlktv fdpagglplq
       61 panvigivsl ifwsltiivs lkyvtlilra nnhgeggima llalaassve skkrlkhvll
      121 lvgvmgaalf ygdgvitpai svlsavegle vaapglqpyv vpltlvalva lfvmqkhgts
      181 gigavfgpvm vlwfivlavs glmnikdsph ilaalnpleg lefcmrhrwl afvalgavvl
      241 sltgaealya dmghfgsrpi rltwfaivfp alalnylgqg alliadpaal qnpfyrlfps
      301 wmlypmvvls tiatviasqa visgtysmtk qamqlgflpr msvvytsare igqiyvpgin
      361 wtlllavvaa vlgfgsstal gsaygiavtg tmlittlltf fviryawryn walcifataf
      421 ffvidamffs anclkiadgg wfpvaiglvm ftimatwgrg aqmmiqeara ragtmplkpf
      481 lanllerspa rvegtaifms ndpsgvphsl lnnlmhnrvl hehtvfltva tepvpwvdea
      541 rrvsietlgn gcfqvtvnyg fkdevdlpaa lekcrgaglk fdratisyfm sratvvptpg
      601 agmalwrerl faimlhnvgn vaaylrlpad rvielgarve i
//
LOCUS       WP_008353561             264 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Caballeronia].
ACCESSION   WP_008353561
VERSION     WP_008353561.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 264)
  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 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   3  (residues 1 to 264)
  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   4  (residues 1 to 264)
  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 264)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..264
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29219
     Region          1..248
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <145..252
                     /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 mtiapppast ladmlahfal lapvfdampd ivffvkdrea ryamvnrtla rrcghkddks
       61 allgktaedv fprrfgriyt aqdqaiiaqg hqlidqlelh lypgrepgwc mtckqplhdt
      121 qghivglagi srdlqaaegt hpaysrlaav vqhiqenyvq plnmrqlaqm anmsiaqler
      181 yfhkvfhltp rqvllktrld aatallvsqe kvtdvaalcg ytdhsaftrq fkatvgltps
      241 eyrallqagt ssasrpdsir etnv
//
LOCUS       WP_008354430             306 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Bacillus
            xiamenensis].
ACCESSION   WP_008354430
VERSION     WP_008354430.1
KEYWORDS    RefSeq.
SOURCE      Bacillus xiamenensis
  ORGANISM  Bacillus xiamenensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 306)
  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   2  (residues 1 to 306)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Bacillus xiamenensis"
                     /db_xref="taxon:1178537"
     Protein         1..306
                     /product="aminoglycoside 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=35217
     Region          18..240
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mkyeklkqls pllrqaisfq pitsgfsgdr tflvttssek lvlklsdirk yaslkrkasv
       61 lqklkdrgvl csevmeigms aeqsctfrif pfiegenara sihrltneeq yeigrragrd
      121 lslihtyhap aheapwdekv makheryiha yqssgvafsh dqfvldfiqs hadavkgrph
      181 qfqhddfhlg nillqgnqya gvidfdqsdf gdpihdfykl slfsreisip fsagqvdhyl
      241 skqgtndfwl lfsiytamsc fssivwtlsy dpghvkdmvn rvdrilkdhk rftqlqpvwy
      301 adwhhl
//
LOCUS       WP_008354116             384 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Caballeronia].
ACCESSION   WP_008354116
VERSION     WP_008354116.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 384)
  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 384)
  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   3  (residues 1 to 384)
  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   4  (residues 1 to 384)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 384)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 384)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..384
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40392
     Region          34..370
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(110..112,133..134,183,235,259)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mrfrtrplaw lvacaaatlg avpfaasade lpvkvgfaap ltganagygk dlqngvqlal
       61 deanakkiti ggktakfeir aeddqadprv gvqaaqklvd dgvvvvvghf nsgttlpasp
      121 iynnagipti dpaatnptit trglanmftv issdaqnagn agvyavtttk akriaiiddr
      181 tafgqgeade fekavkakgg tivtreysdn qtvdfsaqlt rikstnadli ffggldrqaa
      241 avvkrmkqlg mnaqfvgggg vmdadflkla gdaaegaqaw eygspldklp egkafsekfq
      301 krfgvailsy apfgydaawa ainamqkans idpnvyrpvl ktnkfdgitg piafddngal
      361 knasstlyqv kngqwesvvt khgm
//
LOCUS       WP_008354435             300 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Caballeronia].
ACCESSION   WP_008354435
VERSION     WP_008354435.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..300
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33202
     Region          14..264
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mpevrllvda nnhlgegplw dvkeerlywi dstaaeiysc radggdvkry fvprhigsma
       61 lreqggavva langlhfydf daqtvqfiad pesddpetrf ndgkvdrrgr fiagtmsydf
      121 drydadrgqr strsgglyrl dtngqvtrld sgiscsngpc wgpdnktfyf tdtyskemya
      181 ydydietgaa tnkrlfasah dmagtfdgat vdeegyvwsa lvfggrilrf apdgkldrvv
      241 pfpvrnltsv mfggpsldil yvstmgrpmw gipqkerdkg glfavtglgv rgipeprfag
//
LOCUS       WP_008354448             807 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: penicillin acylase family protein [Caballeronia].
ACCESSION   WP_008354448
VERSION     WP_008354448.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 807)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 807)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 807)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..807
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..807
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=89615
     Region          9..804
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mnrrkgqrli altigaslia pldariafad tpgdetiava glsqpsdili drwgvphifa
       61 vndsdaffvq gfnaardrmf qidlwrrrgl gelsevfgpa yveqdkatrl flyrgdmate
      121 wqrygpdakp aatryaagvn ayidwlaahp drmpyefrki gywpakwsad divrirshgl
      181 trnltsevar arvtckssld adtvrfglqp qwkaqmpagl dpclpddvlk vftlatqgvr
      241 vtkesmkstd asttmiaaae npeevtegsn nwviapsksa tgraimandp hrayaapslr
      301 yiqqistptl niigagepsa pgisighngs iaygltifni dqedlyvyel npansrqyry
      361 kgkwepmrvv reqiavrnga pvtadllytr hgpviyteer khrafavrta wlspgmspyf
      421 dsmrymrakn yaqfkaslat wgaptvnqly adkdgnigwv psglapkrpn wdglmpvpgd
      481 gryewagfwp rdampsvynp aqayfttsne mnlpagypya erklgfewtn gsrhqridev
      541 lkslprvsie dserlqnddv siparrlval laplssdded traalamlkd wdahmsassp
      601 qaaleevwfs rhlgrtfkea vlpkdaaasf gapdtsvmld slehpetrfg deapakrdav
      661 llsslrdaya emrhlqgada tqwrwgklqt nlnahpladv vdadmrakln vgpigkggsa
      721 ytpnqstyra sdfretngps frvvvdvgnw dnsravnlpg esgdpdsphy rdlaqmwldg
      781 qyfpllysrs aveaatekrv hlvpdah
//
LOCUS       WP_008354472             675 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Bacillus].
ACCESSION   WP_008354472
VERSION     WP_008354472.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 675)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 675)
  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   3  (residues 1 to 675)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..675
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..675
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=74728
     Region          1..675
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          166..245
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 mdvnqyldif ldesrehlqt cnekllelek nptdlqlvnd ifraahtlkg msatmgfddm
       61 aqlthhlenm fdairneqmi vtpesmdtmf ealdhleamv qsiaeggdgk rdvteiskkl
      121 dvtgshaeaa savetadepa aakdldynef ertvldeare qgfkcyeltv tlsdacllka
      181 vrvymiferl nevgevvkti pnaellesed fesefsisyl skqpmdevkk ivtsiseveh
      241 vdisevsafe etapaekqea kpeqkkekas vpapkapand apkangnnga aaggtktirv
      301 nidrldslmn lfeelvidrg rleqiakele nneltdtver mtrisgdlqs iilnmrmvpv
      361 etvfnrfprm irqltkelnk kieliiegae teldrtvide igdpllhllr nsldhgiesp
      421 eervkkgkpe kgtvllkayh sgnhvfieve ddggginrkk vlekalergv itereaetle
      481 dhqidslifa agfstadtis disgrgvgld vvknkleslg gsvsinsteg qgslfsiqlp
      541 ltlsiisvll vkleeetfai pissiietav ikksdilqth drevidfrgf ivpvvylkkq
      601 fnvpnanele eelhiivvrk gdkltafvvd sfigqqevvl kslgdylpnv faisgatilg
      661 dgqvalivdc nalik
//
LOCUS       WP_008354598             372 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Nocardioides].
ACCESSION   WP_008354598
VERSION     WP_008354598.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 372)
  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 372)
  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
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 372)
  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   5  (residues 1 to 372)
  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   6  (residues 1 to 372)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 372)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 372)
  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 20170230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..372
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38555
     Region          6..>68
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          89..365
                     /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 mskarrrtlr pigkllqeda rrhhrslvlq hlfavgpasr adlarasglt ratvsdlvgs
       61 lledglveel gapvesrvgk ppmlvglaad sthivavdvs gddqvagavl nltgdvirht
      121 trcregrtgs davrlvkelv teliastdrp ilgigigspg vvsadgtvia apnlgwtdva
      181 laeqvrretg rptyvandan tavlgeytfg qsgdgglmlv rvgtgvgagl vlegallhgf
      241 vdaagevghv tvdpdgplca cgrtgcletf lavprlrerl etahddalve agehlgkala
      301 pvvgtlnlhe lvlsgpadll dgtlretadr iirertmpvs geplefrtst lgedvvivga
      361 avlvlagelg vs
//
LOCUS       WP_008356592             497 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Bacillus xiamenensis].
ACCESSION   WP_008356592
VERSION     WP_008356592.1
KEYWORDS    RefSeq.
SOURCE      Bacillus xiamenensis
  ORGANISM  Bacillus xiamenensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Bacillus xiamenensis"
                     /db_xref="taxon:1178537"
     Protein         1..497
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54484
     Region          4..497
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mrdfivihps dnvgialkvl eqgeelqyqe htvvlketva kghkfaladi kqkeniikyg
       61 ypighattli skgewvhthn iktnlsgkld yeyqpslten pyektnltfk gykrkngasg
      121 irnelwivpt vgcvngiadq iiqiftaemg gnihpfetal vlkhnygcsq lgddhentkt
      181 ilqnavkhpn aggvlvlglg cenndiedfq atlgeydqtr vkflrsqevg deietgvall
      241 keiydaaked qreeiplsel kiglkcggsd gfsgitanpl lgrlsdfiva qggttvltev
      301 pemfgaetil meraeseetf dnivqmindf kqyfmdhqqp vyenpspgnk aggistledk
      361 slgctqkagt saikdvlkyg ellkrkglnv lsapgndlva ssalaasgcq lvlfttgrgt
      421 pfgtfvptmk vstntalyet kkhwidfnag elledvpeev vlekfistii dvasgkqlnh
      481 eknnfrelai fktgvtl
//
LOCUS       WP_008356636             364 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GerAB/ArcD/ProY family transporter [Bacillus].
ACCESSION   WP_008356636
VERSION     WP_008356636.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..364
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=40705
     Region          3..362
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 mvnhkesiss yqasaiisnt tlgasmlvlp rsmaqaastp dgwialllms viyivfifan
       61 vlmmkkvpfs syydytnegl gkwigtianl liiiyflgva syevrsmsem vkffllqntp
      121 iavtmlsfil vgfylviggi gdfarlcpff livtliilfv ayglsvqefe ldnlrpvlge
      181 gfspvfqsfn asaisfvgie mmlfmpaymk sqkhtfayga vgflipaiiy iftyilvvga
      241 ltvketatlt wptialfqsf diqgifieri esfllivwlv qlytsfvgyt ffaamgvskl
      301 tkfpkkvvlg lmavviylaa ifpkdvdtvr vylayvnnlf fllfgilpfl lfiivffkrr
      361 rkaa
//
LOCUS       WP_008358093             295 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 5'-3' exonuclease [Bacillus].
ACCESSION   WP_008358093
VERSION     WP_008358093.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..295
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32805
     Region          1..275
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mnkhvllvdg mallfrsfya tavhrnfmin drgvptngvs gylkhlltav qtfepthivc
       61 cwdmgsqtyr nelfqdykan rgeapvelip qfdlakeate elgimnvglk gfeaddcigt
      121 laalyqkear vtvltgdkdl lqilneqvtv almqkgigny kpftkalfee emgitpkali
      181 dmkalmgdas dnypgvkgig ektalkfiqt yqsidrllen ieeltaaqqk kmqagledlk
      241 lsrilaeikc dvplscpide tkmninpera aamlrlhqik giepmvhrvs qleis
//
LOCUS       WP_008360393             198 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Nocardioides luteus].
ACCESSION   WP_008360393
VERSION     WP_008360393.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides luteus
  ORGANISM  Nocardioides luteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Nocardioides luteus"
                     /db_xref="taxon:1844"
     Protein         1..198
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22068
     Region          3..193
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mefsevvrrr kmvrsytsdp vdpevidkil hnatrapsag fsqgwaflvl dtpedvrryw
       61 eatadvdnpd rwltgmmtap vivipcsska ayldryaepd kgwtdrdeah wpmpfwhmdt
      121 amatmlilqt vvdeglgaly fgippesdaa vrkafdipdd fdpigavtig hpasggakgs
      181 ptrrkraple evvhrgrw
//
LOCUS       WP_008363947             988 aa            linear   BCT 20-JAN-2025
DEFINITION  chromosome segregation protein SMC [Mycoplasma feriruminatoris].
ACCESSION   WP_008363947
VERSION     WP_008363947.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasma feriruminatoris
  ORGANISM  Mycoplasma feriruminatoris
            Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Mycoplasmataceae;
            Mycoplasma.
REFERENCE   1  (residues 1 to 988)
  AUTHORS   Cobbe,N. and Heck,M.M.
  TITLE     The evolution of SMC proteins: phylogenetic analysis and structural
            implications
  JOURNAL   Mol Biol Evol 21 (2), 332-347 (2004)
   PUBMED   14660695
REFERENCE   2  (residues 1 to 988)
  AUTHORS   Jessberger,R.
  TITLE     The many functions of SMC proteins in chromosome dynamics
  JOURNAL   Nat Rev Mol Cell Biol 3 (10), 767-778 (2002)
   PUBMED   12360193
REFERENCE   3  (residues 1 to 988)
  AUTHORS   Harvey,S.H., Krien,M.J. and O'Connell,M.J.
  TITLE     Structural maintenance of chromosomes (SMC) proteins, a family of
            conserved ATPases
  JOURNAL   Genome Biol 3 (2), REVIEWS3003 (2002)
   PUBMED   11864377
REFERENCE   4  (residues 1 to 988)
  AUTHORS   Strunnikov,A.V. and Jessberger,R.
  TITLE     Structural maintenance of chromosomes (SMC) proteins: conserved
            molecular properties for multiple biological functions
  JOURNAL   Eur J Biochem 263 (1), 6-13 (1999)
   PUBMED   10429180
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11493846
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..988
                     /organism="Mycoplasma feriruminatoris"
                     /db_xref="taxon:1179777"
     Protein         1..988
                     /product="chromosome segregation protein SMC"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003682 - chromatin binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0030261 - chromosome condensation
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=112603
     Region          3..981
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
ORIGIN      
        1 mlflkqiras gfksfadltv mdfnydmtgv vgpngsgksn itdairwtlg eqstktlrgs
       61 kmddivfsgn nekkaadvae vtlvfnnthe nfssiksdvv eitrrfdknt reseffinst
      121 kcklkdvqsi aleagltrss iaiisqgtva nfteskpetk reifddaagv skykkrkret
      181 llklekaten ltrlediake isrrlpnler qskkaleyqq kvnelkniel yiltkdlkvl
      241 vnrieelrve kieyetqikk ltneinmsqe evnliidkdv ednqklgeln akfntlveki
      301 anlkvrkqka elkeqenlnt kdqdeykatl ikkqfeekqi siktekdklt kaensllelk
      361 dkydyytsky neiyreieti ranvsriniq iesiehskki aaqsyqdgvs ailnnqkqig
      421 gvvdvlksli svkeeyqiai svtasghmns lvmktdqdvk raieflkknn nlgrvtflpl
      481 ntlspnlinp vqrqilekse gfvgfanelv eysetiskav eyalasiivv qtyddainla
      541 kntnfrfniv sldgqrilph gaivggsakn anifakqnaq nqdntleelk tkvelleqke
      601 itktkeltey ktandnlrdq indlngtirn aknnlnnwte nlkelseehk sltgkdlftg
      661 vfsrsdeses itlarqisel eiqrdevqie insisfkrnq tmekqremns anslkrdeld
      721 qlkshagsin teynvllqrr itiidrlsng yqiteetals mevediedeq vareriielt
      781 tyiqnignvn mdaieeykne kerfdyydqq ikdiydakek lesiildidi amesqfkqii
      841 edvnkalpev fskmfgggya eliytdpdni letgidikif ppgkkitnln llsggekslv
      901 alsvlfailk arplplvild eaeapldpvn verfaryvrh fshntqfiiv thregtmtqc
      961 dslfgvtmqt kgitkiinvk lieaknlh
//
LOCUS       WP_008364169             291 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Nocardioides luteus].
ACCESSION   WP_008364169
VERSION     WP_008364169.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides luteus
  ORGANISM  Nocardioides luteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Nocardioides luteus"
                     /db_xref="taxon:1844"
     Protein         1..291
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30504
     Region          1..253
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mridlhthsr vsdgtdspte liqaakaagl dvvaitdhdt aaswdeaaaa aaeagielvr
       61 gmeisanhag hgvhllaylp drtypplvee larvlagrdg rlplmldrla rlgievsled
      121 vaavsgdaaa sgrphladal vakgyvlsrd eafnrylgag kpayvnryaa plepmirtva
      181 aaggvtviah pwgrsgreqp deaalsalvd aglsglevdh qdhtpetrek lrviarnldl
      241 vvtgssdyhg tgkvghhlgv nttapaeyer lleraaaasa asgrttpevv r
//
LOCUS       WP_008366861             824 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas sp. M47T1].
ACCESSION   WP_008366861
VERSION     WP_008366861.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. M47T1
  ORGANISM  Pseudomonas sp. M47T1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 824)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 824)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 824)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..824
                     /organism="Pseudomonas sp. M47T1"
                     /db_xref="taxon:1179778"
     Protein         1..824
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90398
     Region          67..116
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          94..824
                     /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 mtgkapltrf pldlraalls aavgvaalpi avqaaepgat qsadrtysia agplgealnq
       61 farqaditla atptltqgkq saglqgnysv qqglsmllag sslqatradg arfvlqetqg
      121 eamtlpatdv rgfslgnalg stdgynaths qiatktstal letsqsvsvv trqqmddqga
      181 qtvaqtmryt pgvltnpyga thrydyiamr gfndgsvdni yidglksmgd sgtystmqid
      241 pyflervdil kgpssvlygr sspgglvalt tkkplyedyh eiqatvgtqg ehgvgfdfsg
      301 plddekhiay rvtglthqsd tqfdhneekr yaiaptlsid fdedtsltlq aylqhdpegg
      361 yhgglpadgl lhqrngqris ehffegepdi dhysrdqqsf gyqfehrfnd tftarqnfry
      421 ldskvdldqv ygygytsats nelnryysga serlhsfiid nmlqaeyftg aakhttllgv
      481 dyqrrktvvd wtsgslaaid afnpvygnst isyysptsyl rrlqqtgvyl qdlieldkwr
      541 fslgvrqdwv ktsdenriae tdrpvgttis ddrsklttra gvlylfdngi apylsysesf
      601 npnsysdasg nplpptdgtq weaglkyqpp gtenlytasv fridqenlat klpqenfyra
      661 vgavrsqgve leahlqltdn lkllssytft dlkytksmvs tlstadniie nkgnsptqap
      721 rqmasvwady kfssgaldgl rlgagvryvg yswadaentm kvpaytlyda svgydlgkig
      781 lqgldlrvna nnltdekyva tcaslnfcyv geernvtatl sykf
//
LOCUS       WP_008371527             258 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Pseudomonas sp. M47T1].
ACCESSION   WP_008371527
VERSION     WP_008371527.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. M47T1
  ORGANISM  Pseudomonas sp. M47T1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 258)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Pseudomonas sp. M47T1"
                     /db_xref="taxon:1179778"
     Protein         1..258
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=28139
     Region          22..249
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mtrtffptpf epascaqcrn lealdfdftm afqpivnvrt gllyayealv rgpngesaas
       61 vlgqvndgnr yrfdqacrvk aietaarlgi vaipdcklsi nflpnavyra etciratlea
      121 arasafpler lmfevtegek vedpehlksi fkayerqgft taiddfgsgy sglnllatfq
      181 pqvlkldmal trnidsdgvr eaivagivlv aqrlgitlla egvetdgerd allalgielm
      241 qgylfarpqv avlplkpl
//
LOCUS       WP_008371532             135 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Pseudomonas sp. M47T1].
ACCESSION   WP_008371532
VERSION     WP_008371532.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. M47T1
  ORGANISM  Pseudomonas sp. M47T1
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Pseudomonas sp. M47T1"
                     /db_xref="taxon:1179778"
     Protein         1..135
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=13415
     Region          1..135
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkgqkgftli elmvvvaiig ilaaiaipay tnyqakakvt aglaevsalk tpfedlinqg
       61 tdvtaanlga nasgncnytt ttgtastgag tltctlvnap pavsgvtvtl trasgtglwt
      121 cattaaatyk pknct
//
LOCUS       WP_008374008             292 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Pseudomonas sp. M47T1].
ACCESSION   WP_008374008
VERSION     WP_008374008.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. M47T1
  ORGANISM  Pseudomonas sp. M47T1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Pseudomonas sp. M47T1"
                     /db_xref="taxon:1179778"
     Protein         1..292
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31576
     Region          13..262
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mnwqalnplr yrlaegafwd aptqalywvd iagfkacrlq dgelrhwqls epvsafiptq
       61 agdalvtlas gvhrldldsp phapritlwc qadpvpgnra nearcdpqgr lwlgsmqnnl
      121 daegadlple rrsgglfrid eqarvealle gqgivntllw tadgttllsa dtldgviyhy
      181 pldaqglpgp rhvwaaqhpr gdpdgsamda qgfvwnarwg ghcllrfapd gsldrvvelp
      241 vehptscvfg gadlsrlyvt sscqagsdnp ldgavlwadv gvagqpcqrf ag
//
LOCUS       WP_008375054             335 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Allocoprococcus comes].
ACCESSION   WP_008375054
VERSION     WP_008375054.1
KEYWORDS    RefSeq.
SOURCE      Allocoprococcus comes
  ORGANISM  Allocoprococcus comes
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Allocoprococcus.
REFERENCE   1  (residues 1 to 335)
  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 335)
  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 335)
  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 335)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Allocoprococcus comes"
                     /db_xref="taxon:410072"
     Protein         1..335
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=37637
     Region          1..335
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mkkavrmava agmcaalals agcqkktvad devqryawpl ataspedtvt qiyaekfaee
       61 veelsdgkmk iqvypngtig gdrellesck dgdipfviqn tapqvtfmpd lavfdipcrf
      121 stidevrekv ddpefyglle dvyenggynl lgyadqgfrv mstnkmvesl adfkgqkirt
      181 mensyhmdfw kklkasptpm sfsevyiglq qgtidaqenp yevivsnkly eqqdyvvetn
      241 hlphlisliv sdeffqdlpe dkqailveaa eiakeearqa sddriadkik viedsgtqiv
      301 tlsdelraei reavqpvyde ieknvdkkly naymk
//
LOCUS       WP_008375483             346 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. M47T1].
ACCESSION   WP_008375483
VERSION     WP_008375483.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. M47T1
  ORGANISM  Pseudomonas sp. M47T1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 346)
  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 346)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 346)
  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   4  (residues 1 to 346)
  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 346)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Pseudomonas sp. M47T1"
                     /db_xref="taxon:1179778"
     Protein         1..346
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38287
     Region          27..199
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          257..339
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpttpiklgd lsvgyihsla davashgldp aplllqygld plrlgeagar lsiprymrlg
       61 haaiqltgda alglrmgras rmtqaglagv taaqaptvre aartlirftp lnqsnyrgqa
      121 slhedargaw lrfysispyn pynrfvvdsv lagwlqqltt lcqmpisaer idveyaapty
      181 aeqyqalssg pvtfgaehnq lrlslaslal rnpdhcpsty khllilceqe leqrtrtrsl
      241 reritqllgp llnggrepdl eevaarlklp twtlrrklad egtqfrailn dtrrdlamay
      301 irdtelafge iayllgfasa eafarafkrw kgqtpgdyrr dsvral
//
LOCUS       WP_008376201             283 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Gordonia malaquae].
ACCESSION   WP_008376201
VERSION     WP_008376201.1
KEYWORDS    RefSeq.
SOURCE      Gordonia malaquae
  ORGANISM  Gordonia malaquae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 283)
  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 283)
  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   3  (residues 1 to 283)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Gordonia malaquae"
                     /db_xref="taxon:410332"
     Protein         1..283
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31701
     Region          161..255
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mfsraqmgrl gftdatlrta irqgrvrrlr qgwfafddad ptvvsavkag gvlgcvsalt
       61 lnslwvppgy snvhvrrska lrgagkragc ttpvgrapat ltavdpveya lacaascmta
      121 edwiavcdsy lnstgtsvdd lrfrlepftg yrlagllekv dersqsgtes imrvrlratg
      181 fdvvvqpgia eyewadmrig rlllecdgrq yhetkkqyak drrrdrrslk dgwmsmrfiy
      241 ddvifgwadt ladirgvtdd drhrvrsvrs rravdrslrr nql
//
LOCUS       WP_008377623             153 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Enterococcus].
ACCESSION   WP_008377623
VERSION     WP_008377623.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..153
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16711
     Region          20..150
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mnkkieayel mllqlkglle aesnwianla nssallnetl edtvfagyyl feegelilgp
       61 fqgrvsctri tlgkgvcges aekkttlivp nvkehenyis cdsaamseiv vpmvvddqll
      121 gvldidsgkt nsydaidqky leefaallva srq
//
LOCUS       WP_008380127             653 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Gordonia malaquae].
ACCESSION   WP_008380127
VERSION     WP_008380127.1
KEYWORDS    RefSeq.
SOURCE      Gordonia malaquae
  ORGANISM  Gordonia malaquae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 653)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..653
                     /organism="Gordonia malaquae"
                     /db_xref="taxon:410332"
     Protein         1..653
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=73199
     Region          29..529
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mddlidlesl pveqliemir ektgagvnls fpgkvlarqi grrvrprnqr tvkslsagde
       61 hgrarnvlle gdnlqalasl yrergqvdmi ltdppyntgg dfryndkwdk dpndpdmgef
      121 vgsddparht kwmkfmyprl qmmkamlkpt gvlaicidsr elfhlgqmld elfhednrla
      181 iinwqkitsp knhdqgvsta teyvliyakd edkvrtgrlp rsektasgyv npdsdplgaw
      241 apsdstlmga sthpgqvygi qnpftgklhy pqegrcwrne rakmkaaaea wgaeyedrdl
      301 ddglrpalvi kgarnpltrd yskdpavraa kklalerrka gswpryfwrn drsrnpghge
      361 lryktylsdv evgvvpttyw asdeefevae idtvswphpq sgtsetgkse lnavvgrghg
      421 fdtvkplqlm ekiislwcpp gglvldpfag sgttghavld lnkatgsdrr filieqgrpd
      481 ngdsyartlt vdrlrrvidg dwskgahepl gggftfkkle kkvdaktlll merdemidtv
      541 iashsstgsr rravlipvvd adeepyaylv aknaanegif lvwsgadsnt dlteevyeei
      601 aeeaeaakls dvyhvysrrn livtddvvwy qipdrilsdf gldvrsepft eev
//
LOCUS       WP_008380664             108 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Enterococcus].
ACCESSION   WP_008380664
VERSION     WP_008380664.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..108
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11641
     Region          1..94
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(4..5,23..24,32,35,37..38,40,43..44,46,52,57,64)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(23,52..53,55)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mnpfyeevya larqipfgkv vsysqiawkl gqingaravg ramrlspqdv pahrvvradg
       61 vlvgptanvr kaalvdegvv fkasgridmk acswsmseia paqmkepl
//
LOCUS       WP_008382116             249 aa            linear   BCT 20-JAN-2025
DEFINITION  YaaA family protein [Gordonia malaquae].
ACCESSION   WP_008382116
VERSION     WP_008382116.1
KEYWORDS    RefSeq.
SOURCE      Gordonia malaquae
  ORGANISM  Gordonia malaquae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Prahlad,J., Yuan,Y., Lin,J., Chang,C.W., Iwata-Reuyl,D., Liu,Y., de
            Crecy-Lagard,V. and Wilson,M.A.
  TITLE     The DUF328 family member YaaA is a DNA-binding protein with a novel
            fold
  JOURNAL   J Biol Chem 295 (41), 14236-14247 (2020)
   PUBMED   32796037
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Liu,Y., Bauer,S.C. and Imlay,J.A.
  TITLE     The YaaA protein of the Escherichia coli OxyR regulon lessens
            hydrogen peroxide toxicity by diminishing the amount of
            intracellular unincorporated iron
  JOURNAL   J Bacteriol 193 (9), 2186-2196 (2011)
   PUBMED   21378183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006857
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Gordonia malaquae"
                     /db_xref="taxon:410332"
     Protein         1..249
                     /product="YaaA family protein"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=26074
     Region          2..246
                     /region_name="YaaA"
                     /note="DNA-binding protein YaaA associated with the
                     oxidative stress response [Replication, recombination and
                     repair]; COG3022"
                     /db_xref="CDD:442258"
ORIGIN      
        1 mlvilppset ksdggtsvpl dleslslpal tdvrrrlada vvtlssdlda srealglgas
       61 daaiaevarn aelftsptrp aitrytgvly daldypgmtr askakaadrl mvgsalfgvv
      121 satdeipayr lsggsklpgf gtlgsvwkpv lspaldaidd fvvdlrsgvy qklgpvagav
      181 tatvvteyan gtrkvvshfn khykglvahe lvrtrrnvrd inglaavlsd agqrveitsp
      241 ieitvvteg
//
LOCUS       WP_008383112             158 aa            linear   BCT 20-JAN-2025
DEFINITION  division/cell wall cluster transcriptional repressor MraZ
            [Rhodovulum sp. PH10].
ACCESSION   WP_008383112
VERSION     WP_008383112.1
KEYWORDS    RefSeq.
SOURCE      Rhodovulum sp. PH10
  ORGANISM  Rhodovulum sp. PH10
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Rhodovulum.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Chen,S., Jancrick,J., Yokota,H., Kim,R. and Kim,S.H.
  TITLE     Crystal structure of a protein associated with cell division from
            Mycoplasma pneumoniae (GI: 13508053): a novel fold with a conserved
            sequence motif
  JOURNAL   Proteins 55 (4), 785-791 (2004)
   PUBMED   15146477
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449500
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Rhodovulum sp. PH10"
                     /db_xref="taxon:1187851"
     Protein         1..158
                     /product="division/cell wall cluster transcriptional
                     repressor MraZ"
                     /GO_function="GO:0000976 - transcription cis-regulatory
                     region 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=17177
     Region          3..147
                     /region_name="MraZ"
                     /note="DNA-binding transcriptional regulator and inhibitor
                     of RsmH methyltransferase activity [Translation, ribosomal
                     structure and biogenesis]; COG2001"
                     /db_xref="CDD:441604"
ORIGIN      
        1 mdrfvgnfta rldskgrvsi papfravlar dgfeglycyp sldrpavdag ghallaeids
       61 liarfppysd ereeflvaly gtsetlridg egrvvltema rshagvrdav tfvglghkfq
      121 iwepeafrah lakatatvra ttkrlgserr aagdgare
//
LOCUS       WP_008382975             167 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Rhodovulum sp. PH10].
ACCESSION   WP_008382975
VERSION     WP_008382975.1
KEYWORDS    RefSeq.
SOURCE      Rhodovulum sp. PH10
  ORGANISM  Rhodovulum sp. PH10
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Rhodovulum.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Rhodovulum sp. PH10"
                     /db_xref="taxon:1187851"
     Protein         1..167
                     /product="TRAP transporter small permease subunit"
                     /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=17314
     Region          2..167
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mferlitpvv hlllafaall iflmgflvva dvigrgafss pvqgtpelvs mgiviicfll
       61 aghavqsggm lkadilvgaf grsgqsfael lsgilgavff glvvwggidp aiyawtssef
      121 egegalrvpa wparfivvgg aalvvviylg kafralqalv rgrtpaa
//
LOCUS       WP_008388331             713 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Rhodovulum sp. PH10].
ACCESSION   WP_008388331
VERSION     WP_008388331.1
KEYWORDS    RefSeq.
SOURCE      Rhodovulum sp. PH10
  ORGANISM  Rhodovulum sp. PH10
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Rhodovulum.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 713)
  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   3  (residues 1 to 713)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Rhodovulum sp. PH10"
                     /db_xref="taxon:1187851"
     Protein         1..713
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=75634
     Region          1..711
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mtspdpietf rqeaqelleq lehtlldlgh rptdadlida afralhtikg sgamfgferv
       61 agfthhveta fdlirkgrvr ataelialtl aakdqmrrli etpaeadeaa gdailgrlqa
      121 aidaatvgvp aaaavaagpa apapasataa aravrtwrvr frlpknamat gsnplllide
      181 lrelgeatvi adttkipple dldptdclvg weatvttahp rdaieqvflf llddmeliie
      241 avdaqgaeeg aaaptpasps sssssnsagq gspataaiap vnwaevgtka apkssapgps
      301 pspaaaaaep aaqaqkgaat akasgsvrvp aerldelmdq vgelviahsr lkqitaqthd
      361 pqvksvveei erlarelqdt tmgvrmmpig slfgrfrrlv ydlsrdlgkd ielitsgeet
      421 eldktvierl adplvhlirn aadhgiepre rridagkpaa grvmltarha gaavlisvad
      481 dgrgldreri qaraeenglv apgakvtdee lfklifaagf starevtnls grgvgmdvvk
      541 rtieelrgsi evrstagrgs evtlrlpltl aiidgllvrv gngryviplg aveecveltp
      601 eddlrstgrc flnirgdlvp firlreqfat rtppdpyqkv iivsaegmhv glvvdqvigd
      661 hqtvikslsr lhaevemfsg atilgdgsva lildvpqlva hgqaqeerlk aag
//
LOCUS       WP_008390663             374 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Rhodovulum sp. PH10].
ACCESSION   WP_008390663
VERSION     WP_008390663.1
KEYWORDS    RefSeq.
SOURCE      Rhodovulum sp. PH10
  ORGANISM  Rhodovulum sp. PH10
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Rhodovulum.
REFERENCE   1  (residues 1 to 374)
  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 374)
  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 374)
  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 374)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Rhodovulum sp. PH10"
                     /db_xref="taxon:1187851"
     Protein         1..374
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=38934
     Region          30..371
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mtditrrrla ggaalgglaa sglaagglat sglavlatpa varaetrrwr mvtswpkrlp
       61 gpgmsaerva sriaemsggr laitvhaage lvpafevlda vgggvaemgh taafywqgkq
      121 paaafyttvp fgltpaehva wveagggqal wdelyapfgv kpfmggntgv cmggwfrdpl
      181 nsladlkgkt vrslglggev yrrlgavpqt tapaeiltsl qsgvldgaef vgpgtdialg
      241 lyrvaslyyg pgfnkpngtg eclvslaawn gldaelkaiv shacaveatf alsemerlna
      301 ealaalvrqh hvrlsefpad ligaaraqat dvlaevaars dvarrvhdsy vafrdrvadw
      361 srvsiravle arga
//
LOCUS       WP_008391289             180 aa            linear   BCT 20-JAN-2025
DEFINITION  transcription termination/antitermination protein NusG [Rhodovulum
            sp. PH10].
ACCESSION   WP_008391289
VERSION     WP_008391289.1
KEYWORDS    RefSeq.
SOURCE      Rhodovulum sp. PH10
  ORGANISM  Rhodovulum sp. PH10
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Rhodovulum.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Kang,J.Y., Mooney,R.A., Nedialkov,Y., Saba,J., Mishanina,T.V.,
            Artsimovitch,I., Landick,R. and Darst,S.A.
  TITLE     Structural Basis for Transcript Elongation Control by NusG Family
            Universal Regulators
  JOURNAL   Cell 173 (7), 1650-1662 (2018)
   PUBMED   29887376
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Liu,B. and Steitz,T.A.
  TITLE     Structural insights into NusG regulating transcription elongation
  JOURNAL   Nucleic Acids Res 45 (2), 968-974 (2017)
   PUBMED   27899640
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Steiner,T., Kaiser,J.T., Marinkovic,S., Huber,R. and Wahl,M.C.
  TITLE     Crystal structures of transcription factor NusG in light of its
            nucleic acid- and protein-binding activities
  JOURNAL   EMBO J 21 (17), 4641-4653 (2002)
   PUBMED   12198166
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415705
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Rhodovulum sp. PH10"
                     /db_xref="taxon:1187851"
     gene            1..180
                     /gene="nusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
     Protein         1..180
                     /product="transcription termination/antitermination
                     protein NusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
                     /calculated_mol_wt=19887
     Region          15..180
                     /region_name="NusG"
                     /note="Transcription termination/antitermination protein
                     NusG [Transcription]; COG0250"
                     /db_xref="CDD:440020"
ORIGIN      
        1 mldrtagwda galpnaassw ivvnthahke rvaienlerq fygtycpmir tqvrharkts
       61 qvlrplfpgy lfvaldlerd rwrpilstlg vrsvvrdrdt psrldpaiie slkarevdga
      121 ivrpaspyqv gqdvkiagga ldglvvkiia lgekdrivvl ldllnrsiev rmgasqvrav
//
LOCUS       WP_008391806             245 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Rhodovulum sp. PH10].
ACCESSION   WP_008391806
VERSION     WP_008391806.1
KEYWORDS    RefSeq.
SOURCE      Rhodovulum sp. PH10
  ORGANISM  Rhodovulum sp. PH10
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Rhodovulum.
REFERENCE   1  (residues 1 to 245)
  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 245)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 245)
  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   4  (residues 1 to 245)
  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   5  (residues 1 to 245)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Rhodovulum sp. PH10"
                     /db_xref="taxon:1187851"
     Protein         1..245
                     /product="TRAP transporter small permease subunit"
                     /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=26656
     Region          3..208
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mnaliavsra idavnarlgk slswlivvav lisavnalvr kffgvsanaw lelqwvlfga
       61 vfllcspwtl lanehiridi vnahfprwlr ntielvghtl fliplcvlml vtswpfflas
      121 apsradfaga fsafpavfea pvsawlpnla dwwrlflglg eqsfnagglp qwpakflvfa
      181 gfavllvqai selikriavv lgrlpdphdg kaghaassfa adaeefmagr ptpeevsrra
      241 rsras
//
LOCUS       WP_008394324              74 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Anaerostipes hadrus].
ACCESSION   WP_008394324
VERSION     WP_008394324.1
KEYWORDS    RefSeq.
SOURCE      Anaerostipes hadrus
  ORGANISM  Anaerostipes hadrus
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Anaerostipes.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Anaerostipes hadrus"
                     /db_xref="taxon:649756"
     Protein         1..74
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=8104
     Region          1..>56
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mkadlhchtv lsdgamrvdq impyakrigl dyiaisdhes thsipeavrl gkelgvhags
       61 fhdgiywnsd rsit
//
LOCUS       WP_008394792            1018 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Clostridium sp.
            M62/1].
ACCESSION   WP_008394792
VERSION     WP_008394792.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. M62/1
  ORGANISM  Clostridium sp. M62/1
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 1018)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 1018)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1018
                     /organism="Clostridium sp. M62/1"
                     /db_xref="taxon:411486"
     Protein         1..1018
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=114797
     Region          423..1009
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mnhkidrdty iippnfiesg tffggmfkar nvieagilaf aigvpvfsll plsltariia
       61 lcltalpaal valigisges lssfllifik ylrnrriigg nsaedavpaa ehggkhikkk
      121 vhkpdkaprr srrsgredfp aefdevrgye irqklrpvkk qkpakekkaa kqkkkvsker
      181 kvkrpirtqe pkpaclnpva dylpiskien giiytkdhry vkvvevvpin fmlrsaqeqr
      241 niiysfvsyl kispiklqik vltrraeinr hldtvrkeme qetneqcllm qedylqfvqq
      301 igsreaitrr fflifeyepw sntkrsdeeg eainalqsav htatnylrqc gnevivpenw
      361 deftvdvlyn llcrnesavk plsvraqevv aeylakgrds eidhipatef capksidfth
      421 ghhicidgly yayllvpsdg yktqvpagwl slivnagdgi dmdmflsrqp ketiiqkvgq
      481 qlrinrskik dasdtntdfd didgairsgy flkeglanne dfyylnllit itasneedle
      541 wkvsemkkll lsqdmnactc hfreeqafls alplvamekk lyergkrnll tggaascypf
      601 tsyemcddng illgvnkyns sliivdifns avyknanmsi lgtsgagktf tmqlmalrmr
      661 rknipifiva plkghefhra csnvggsfiq ispasphcin vmeirrvdrs vneildgpgi
      721 qlselaakiq qlhiffslli pdmsheerql ldealvrtyn tkgithdnas ledpaqpgqy
      781 rempvlgdly eilktsketm rmahilnrlv ngsastfnkq tnvrldnkyt vldissltgd
      841 lltvgmfval dfvwdrakad rteekaifid ecwqllsgag aagvrlagdf lleiaktirg
      901 yggasifasq dladffdldg grfgkgiinn sktkiilnle ddeaqrvqea lhlsdaetme
      961 ithferghgl istnnnnimv efkasplekd littdrrelr eiverkrreq stsaeqqi
//
LOCUS       WP_008395640             395 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Clostridium sp. M62/1].
ACCESSION   WP_008395640
VERSION     WP_008395640.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. M62/1
  ORGANISM  Clostridium sp. M62/1
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Clostridium sp. M62/1"
                     /db_xref="taxon:411486"
     Protein         1..395
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=45234
     Region          1..285
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          284..367
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkffhlsdlh igkqlngwsl renqeavlgq ivryaeeyrp davlicgdiy dksvpsgeay
       61 sifggflerl agigipvlvi agnhdsperl sfagqileke rifissfpps ekgerlrrvt
      121 lsdrwgevdf ylfpfmrpgy vrrllaaesg eqedisvqsl tydqafrlml ereeidssrr
      181 nvilchqffv sasekpdtce setavlmagg ldqidisald cfdyaalghl hgsqrvgres
      241 arycgtpyky svseerhrka vvmvelgrkg eepllsflpl agvqdvrker gtlkqvlsra
      301 fepschdfvs ivltderepa nfreqlreky dhileiridn ertrrrlede kepipvlkpm
      361 eafrqffsmi lnsdlteeee rlmaqvieea keeed
//
LOCUS       WP_008397255             305 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Clostridium sp. M62/1].
ACCESSION   WP_008397255
VERSION     WP_008397255.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. M62/1
  ORGANISM  Clostridium sp. M62/1
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 305)
  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 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   3  (residues 1 to 305)
  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   4  (residues 1 to 305)
  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 305)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Clostridium sp. M62/1"
                     /db_xref="taxon:411486"
     Protein         1..305
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35258
     Region          71..301
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <189..300
                     /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 mritrnlefm tgskeeklpy rtldfpytas qaeldyyrer fvpwhwhrai elfyiesgei
       61 qyctphktav fpagtagmvn snvlhmtkir shrekniqli hifdpkllag gqgslieqky
      121 itplitapqi eilalypdqp eqsalidsir gafllaerdf gyeinireal skiwvqlcki
      181 sfallqdnpq renrtadkvk qmmvyvhehy tekisipela gcvflserec yrafqnclhm
      241 tpaeyiksyr lqmacqilad sqmpiteagy acglgnasyf gkvfrefagc tplqyrrrwq
      301 ncdkt
//
LOCUS       WP_008398168             460 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Clostridium sp. M62/1].
ACCESSION   WP_008398168
VERSION     WP_008398168.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. M62/1
  ORGANISM  Clostridium sp. M62/1
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 460)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Clostridium sp. M62/1"
                     /db_xref="taxon:411486"
     Protein         1..460
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=49589
     Region          <246..>292
                     /region_name="COG5263"
                     /note="Glucan-binding domain (YG repeat) [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:444077"
     Region          305..428
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(372..373,376,401..404,406)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkkrnlraaa lllaaamtvg ggstafaaee tatgpgleie qkeqqnqgap sgaeeggqna
       61 ggqgaetpad qgqtgtdgta psdtgqetqq qeqastapyv svsytqgvgt evtnlsmtln
      121 nyngiggvsy rpyvnnggfi wwnhdggpsg gteastyvea veivltgdae rdydiyycvt
      181 ssgqgkmgwa kngeiagtsn lgehlvsiev mlvpkgqpgp vsvagrylne ltnyiriape
      241 gstmtnqdgt pyngwvsydh ekfyfkdgks vsgwqyidgl kfyfepsgrl vqdvdsligk
      301 qssyvikvnk alncstiyak dgdngyiipv kamltsvgdd tplgtfktpe kyrwrlmvnd
      361 tytqwatrit qgflfhsity aepdiyklnt egynglgvsr slgcvrltce nakwvydnca
      421 lgttveiyed snvaspfdkp dlipisnsqn wdptdpsiqr
//
LOCUS       WP_008398706             736 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Clostridium sp. M62/1].
ACCESSION   WP_008398706
VERSION     WP_008398706.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. M62/1
  ORGANISM  Clostridium sp. M62/1
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 736)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Clostridium sp. M62/1"
                     /db_xref="taxon:411486"
     Protein         1..736
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=79599
     Region          <429..511
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          536..654
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(605..606,609,627..630,632)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
     Region          657..>716
                     /region_name="COG5373"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:444140"
ORIGIN      
        1 msdfsrkdep dqnmevrsag qtdeiedgle wieeteeapq tdgmpekfrs eveitedsra
       61 dmsgdtaldg meegvleela eeeepeeken rqgdimptee eilraagssf tepprkerra
      121 qtqtappead rireknrpse eragggdanr srgrsrrkgs vppeslrrag kdiqsdepsv
      181 rkvrgrrpgq gerrfgrrqa avaagaaaav lliggavyvg lgqkyrnvff pgteingldv
      241 sgktvaeaeq misdgisgyt ltieergdkt eqlsqadigl haefdgtmek iiasqnplaw
      301 geyvfspasy kiktmmayde eafqkavesl ecfdedapap edahlseyte gegysivpek
      361 kgakavyevv ekgisdailn lqpsvsleei ggyeepevts edetliklcd smnkaagvvi
      421 tyqfgdatet lsgdrihewl vpnadgtvgv dsgkvnayvk eladkyntnn kaknlktsyg
      481 ktvtirggty gwkinqsaea delaalirsg qsqsgrepvy sqkaashgan dygdtyvein
      541 ltaqhlffyk ngkllvesdf vsgnlskgwg tpagsyplty kqrdavlkge nyrtpvdywm
      601 pfnggigmhd akwrssfggt iyktggshgc inlphsvakk iyenisagmp vlcynlegte
      661 kasepekpke tqpstqapae stapvpteps tqppaestap aptepstqap tqpsaqepdg
      721 pasddggsgg asgpgm
//
LOCUS       WP_008398844             203 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [unclassified Clostridium].
ACCESSION   WP_008398844
VERSION     WP_008398844.1
KEYWORDS    RefSeq.
SOURCE      unclassified Clostridium
  ORGANISM  unclassified Clostridium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="unclassified Clostridium"
                     /db_xref="taxon:2614128"
     Protein         1..203
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=23322
     Region          22..203
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mkgsgtvgqf eqldhlletq dgmlrtaqvv sagiskpvfy dyvrsreler vahgiylsrd
       61 awvdamyllh lrvgqavfsh etalffhdlt drepmeytvt vktgynptkl kaegvqvfti
      121 kaelhevgli taqtpfghtv pvydmertic dllrsrnnme tqifqgalkm yarrkdkdlr
      181 nlmryagmfr vekilrqyle vll
//
LOCUS       WP_008399200             162 aa            linear   BCT 20-JAN-2025
DEFINITION  zinc ribbon domain-containing protein [Clostridium sp. M62/1].
ACCESSION   WP_008399200
VERSION     WP_008399200.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. M62/1
  ORGANISM  Clostridium sp. M62/1
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 162)
  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 12181465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Clostridium sp. M62/1"
                     /db_xref="taxon:411486"
     Protein         1..162
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18622
     Region          49..156
                     /region_name="zinc_ribbon_15"
                     /note="zinc-ribbon family; pfam17032"
                     /db_xref="CDD:465334"
ORIGIN      
        1 milytcirff rtgiqtsegl gmrqrgrrnm ifiggissav kqlnylktvi csrcggygry
       61 qvfmtytyfs fffipvfkwn rqfyvkmscc gsvyeldrev gmkilrgesv direedltli
      121 kaggrsfels dfeeertcpg cgasvsedys ycpycgepld rr
//
LOCUS       WP_008400892             395 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Clostridium sp. L2-50].
ACCESSION   WP_008400892
VERSION     WP_008400892.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. L2-50
  ORGANISM  Clostridium sp. L2-50
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Clostridium sp. L2-50"
                     /db_xref="taxon:411489"
     Protein         1..395
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42558
     Region          1..395
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkvlvincgs sslkyqlids dteellakgl ceriavdgrl thtttgkeky tkdlpmpdhn
       61 aavsyvleal tdketgaiad lseidavghr ivhggekfak svvitdevia aieecndlap
      121 lhnpanligi racrklmpgv pnvgvfdtaf hqtmpdkayi ygipyeyytd ykirrygfhg
      181 tshsfvskrt aellgknied tkiivchlgn gssitavkgg ksvdttmglt plagvimgtr
      241 sgdidpaiie flanktgkni eeintilnkk sgvyglsggf sdfrdlgkgm eegndrcrla
      301 ldvfaygvkk yigayaaamg gvdaiaftag igennpyvrn lamtdmeymg itidqeankv
      361 mgdeklistp dskvkvfvvp tneelaiare tvalv
//
LOCUS       WP_008399875             506 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Clostridium sp. L2-50].
ACCESSION   WP_008399875
VERSION     WP_008399875.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. L2-50
  ORGANISM  Clostridium sp. L2-50
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Clostridium sp. L2-50"
                     /db_xref="taxon:411489"
     Protein         1..506
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=57964
     Region          8..452
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mekkgklelt wvgkyeeekl epriliedks ksygdpdten mlihgdnlla lkalenkfrg
       61 rvkciyidpp yntgsafaqy ddnlehsiwl smirkrllil kellsedgti wisidddeqa
      121 ylkvlcdeif mrsnfvsnvi wekkfspqnd akwlsdshdf ilvyaknknl wkpnllprta
      181 gmnsryknpd ndprgpwtss dftartysgn tdypittpsg rvvtptksrs wisskeefdr
      241 lvsdnriwfg ingnnvprkk tflsevksgs vpmtiwkyed vgstqdakke vkqinpedpf
      301 atpkpeklie rileiatkpg diildsflgs gttiavahkm nrrwigveig eqaynqcklr
      361 ldkvidgndg ldiskklgwq ggggykfyel aepllvknkv lpvyqinpsy twdmvceaic
      421 kiegftyeps gefqghssen rfihiteefv ntkyvmsimk nlgdkqslli yckknqadmi
      481 lpenvevkki pkdlldkcnf esevqe
//
LOCUS       WP_008403316             497 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Solibacillus isronensis].
ACCESSION   WP_008403316
VERSION     WP_008403316.1
KEYWORDS    RefSeq.
SOURCE      Solibacillus isronensis
  ORGANISM  Solibacillus isronensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Solibacillus.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Solibacillus isronensis"
                     /db_xref="taxon:412383"
     Protein         1..497
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54609
     Region          1..497
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mketivihss dnvavalrsf eagepfsigq ekinleqevp rghkiatrni qkgehiikyg
       61 ypighatedi akgtvvhthn vktnlqdiin ynydkkdisl nypqrnltfk gyrrsngevg
      121 irnelwiips vgcvngiadm iirefeqrvg siapfestlv lkhnfgcsql gddhentrti
      181 lldavnhpna aavlvlglgc enntieqmkq elgdydtsrv kfvvsqqvdd eveasvealv
      241 alheavrndr redipiselr iglkcggsdg lsgitanpll grfsdflvsq ggttvltevp
      301 emfgaetilm nraqdeetfg kivslindfk qyfidynqpi yenpspgnka ggittledks
      361 lgctqkagsa eivdvlkyge rlkkrglnll sapgndlvac talasagcql vlfttgrgtp
      421 fgsfvptmki stnsaiyeqk khwidfnagq iledgvdeda vleefiqyii avasgkqlnh
      481 ermnfkemai fktgvtl
//
LOCUS       WP_008403702             288 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase family protein [Streptomyces].
ACCESSION   WP_008403702
VERSION     WP_008403702.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 288)
  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 12830887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..288
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=30373
     Region          79..147
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          177..288
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mataalgtla llavagcrvd aaagpglspa ppppatteda rppapspppp pptpspaptt
       61 atpkpppppp tpsatkpaap avlmrpgqts eqvrelqarl aslglfgrsp tgfygdvtse
      121 avsayqrkga lpvtgttdav twdrlragtp rptqddlhpp ttlplskpdk rcltgrvlci
      181 skqsrslawm vdgkvraamd vrfgsqytpt rdgafkvywk srdhhstlyd tpmpyalffs
      241 ggqavhyskd fatqgyagas hgcvnvrdkk kvaalfdqvr egdrvivy
//
LOCUS       WP_008404151             721 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Solibacillus isronensis].
ACCESSION   WP_008404151
VERSION     WP_008404151.1
KEYWORDS    RefSeq.
SOURCE      Solibacillus isronensis
  ORGANISM  Solibacillus isronensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Solibacillus.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 721)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Solibacillus isronensis"
                     /db_xref="taxon:412383"
     Protein         1..721
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=78902
     Region          7..712
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mtqnvesyes irpllypesv ailgasenky kigniqlqal idgkfqgeiy pihpkaeqia
       61 glksypsltd vpnsidlvif cvaydqikng liacaekkvk aaiifasgfs eageegkklq
      121 lelaeyakln nirllgpncv glvntsngli gtfsssvldv pmsgkrgvgy vsqsgafgvl
      181 tymaaaqygi nfnyfissgn emdttmedyi dymvhddeie visgyiegak npeklkqaah
      241 kalekkkpiv lmktgrsdag sraaashtga lagsdkiyda ffrqhgiirv edaedviafs
      301 klfnpnrlpk gkntaiitss ggrgineadr ceayglnivr lsdetmaemr ktlpdyasvt
      361 npidltaaas ftnpeffldt lkvlvnspev dnilltefph swdehneyfk efitvaknse
      421 kfigffpfpl geitypqttp ilieneiavv sgalnpvral sqlveysqfl ntvqtdgmee
      481 ryeheniddl ltpgavlses easevlaryg ipitkryvtl saeeaveral qigfpvvlki
      541 dsqqiphkte adairlnvss eeevkeafme imknarnynp tailngvsvq emlpqgtevi
      601 igakndevfg pvimaglggi fvevfkdiaf kiaplsrqda gtlldelqak aildgargqv
      661 avdkeaiidv llrvsqlmld yrdqikeldi nplivyengi kaadamlvvt eesikkelig
      721 g
//
LOCUS       WP_008404206             287 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Streptomyces].
ACCESSION   WP_008404206
VERSION     WP_008404206.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 287)
  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 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   3  (residues 1 to 287)
  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   4  (residues 1 to 287)
  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 287)
  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 12820790
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31096
     Region          33..287
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <172..287
                     /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 merqdapdtp eqrqaarewa rhwsweplpg ldllraryir htfprhsheg ytlgavthgv
       61 ervelpgttl hagpgtlvmv npevahaara gtpegwayat lypslglvre vadatghppg
      121 tpvfdrpiad darsgrlvra vhraveegda laadtllrvl iarllnlygt taphavpasa
      181 grgtaarard llaerltdpp sleelartlg sspfavlraf kaaygmppht wltdarvrra
      241 rallhsgatp aetatavgft dqphlnrhft rivgvtpgay rrarrae
//
LOCUS       WP_008405166             320 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phytoene/squalene synthase family protein
            [Streptomyces].
ACCESSION   WP_008405166
VERSION     WP_008405166.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..320
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34826
     Region          16..282
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 msareldaaq itdpalraay rtcrtlnarh grtyflatrl lpverrpavh slygfarhad
       61 divddlgtsa ttgeraaald rldrrlaagl rtgtsdepvv haladtvrry aidhrhfhdf
      121 masmrsdltv tdypdlaals rythgsaavi glqmlpvlgt vvpreeaapy aaglgvafql
      181 tnflrdvged ldrgriylpa dllaahgvdr allcwsratg hrdaritral reaaavtrei
      241 yhraapgial ldpvarpcir tahilygsil davaadgyaa vhrravvprr rravvaadgl
      301 arlaaarrrh rrapapkaea
//
LOCUS       WP_008404694             291 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Streptomyces].
ACCESSION   WP_008404694
VERSION     WP_008404694.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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   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 291)
  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 291)
  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 18542080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..291
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32150
     Region          27..82
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
     Region          108..286
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mvaqaggsgv ptggeadgtd evadlfralg rqikvarvra gmsqkelgdr lgygeetiss
       61 vergrrtpqp ellvavdell ecggllaaaa edverararr rvrhpewfrd yarleleave
      121 lhyygalslp gllqteghar avftarspll deetieqrlt arlarreilt rwppplvtft
      181 veesvlqrpi ggrdvhreql krllevaplr nvelqvmptd qpdhpslggp ftlltpkgkp
      241 qvgylevqnv srlvtdaeev rilaarygsi raqaltpres lalierllgd r
//
LOCUS       WP_008405541             641 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Streptomyces].
ACCESSION   WP_008405541
VERSION     WP_008405541.1
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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..641
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=68728
     Region          251..420
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mtalasaalv lpllgaapgp apaqadtglq gafaaaarey rvpesvllgv aylqsrwdth
       61 ggapsvtggy gpmhltdart alarstghhg ehgedargde srpartpepv lpsageelpe
      121 rlttlrqaar lsglpaerlr sdpaanirgg aallaeaqre rgaapggdaa dwygavaafs
      181 gaedratata yadevfsvlr sgearttdsg vrvvlapqps avadasqtag lglresgakg
      241 svecprtvsc ewlpapyeef gegdygnhdk adrprsarid sivihdteat wdttlelvqd
      301 peyvswhysl rstdghiaqh lrtkdvgwha gnwytnaksi glehegflad pdawyteamy
      361 rtsarlvshl akkygipldr qhilghdtvp gttpatipgm htdpgpywdw qhyfallgap
      421 lkasagknae lvtiapeyrk nrpeftgcek agepcaphgs savrvytepr edaplvqdig
      481 lrpdgspsti dvndlgsrvs agqsyavaer rgewtaiwyl gqkawfknpr kapvavpasg
      541 rvltprpgla evpvygrayp ekeaypagvt pqeivplpyr iaagqryatg gqvpgeyysa
      601 ptfdtsghtv vrgklryyei qyghrvgyvr addvvvrtak r
//
LOCUS       WP_008405982             292 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 5'-3' exonuclease [Solibacillus].
ACCESSION   WP_008405982
VERSION     WP_008405982.1
KEYWORDS    RefSeq.
SOURCE      Solibacillus
  ORGANISM  Solibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Solibacillus"
                     /db_xref="taxon:648800"
     Protein         1..292
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32440
     Region          1..270
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mtkphllivd gmallfrsff asaamnqfir lddgtpsngv qgfarhvlta qnlmqpthla
       61 vcwdmgavtf rndlydgyka nrpappeeml pqfdmakrvs emigwqnfgt qgleaddlig
      121 smikkwkdda qitvisgdkd llqllnpstk iaftkkgyte ydvytesrfv eeygiapkqf
      181 aevkafmgdt sdgypgvkgi gpktalqliq nhgsidgvle alptlkpgqr ikisenlaml
      241 rlshqlatih cdvpidveld hlalspyapd lfnhieqqgy rliakharsi yk
//
LOCUS       WP_008406033             661 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter permease [Solibacillus].
ACCESSION   WP_008406033
VERSION     WP_008406033.1
KEYWORDS    RefSeq.
SOURCE      Solibacillus
  ORGANISM  Solibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae.
REFERENCE   1  (residues 1 to 661)
  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 661)
  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 661)
  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 661)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..661
                     /organism="Solibacillus"
                     /db_xref="taxon:648800"
     Protein         1..661
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=70387
     Region          13..650
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mifkkkveef dvaetlendk eaggairtft gktgfiisal lfalaffsvy vnslmniqei
       61 yrnaifltfi lvltfllypa tkkssktkit vvdyiwaafg faggayilln ysnihnvkfs
      121 eptfidyvfa fitivvllev srrtiglfip ilsaialffa lfgpwfpgmf ghagfsferl
      181 lyrlymtteg ifgmtfsiat tyivifilfg aflnasgatr lfndlalsia gqrrggpaqv
      241 avlssaltgm lsgsavanva ttgtftiplm ksiglkprfa aaveatastg gmimppimga
      301 aafimagflg vgynvivlaa iipailyyas liiaidleak kqglkgiskd nipdvievik
      361 argvlilpiv ivivtlmtgf tallagfsgi facivaswlt kdkefrigik sivnaliega
      421 rgsiqvavac atvgiiiavi tmtglgstla yniiqisgnn laiililvmv tsivlsmglp
      481 stalyivvav aaapalieag vnpiaahffv fwfgalsnit ppvalasyta agiaradamq
      541 tswtavklcl pgfllpfmiv ynpalvmqtd atgidaifqi afafttsilg vfalstavfn
      601 ffttgmnmme rmlmgiasil liipelitsa iglaliiivl aihiprgkka naqvnnlsve
      661 r
//
LOCUS       WP_008406755             278 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AfsR/SARP family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_008406755
VERSION     WP_008406755.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            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="AfsR/SARP family transcriptional regulator"
                     /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=30259
     Region          1..259
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mdiallgtla vreqgysitp tapkarqvla llalhadqvv pvpdlieelw agtpprsart
       61 tlqtyvlqlr slisaaleqr qekgqegapg rrtakdvllt lpggyllhsg ggtsdvrgfd
      121 rlvvrgsqam dagdfpgaar llrealsrws gpafadvdsg vqletearrl eetrlcaldq
      181 rieadlrigr hrellaeltv lagryrthen lhgqfmlalh rsgrrgeald vyqrlhqtlv
      241 relglepsav lrrlqrsilm agpdaplgaa efhggrvg
//
LOCUS       WP_008406861             321 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Streptomyces].
ACCESSION   WP_008406861
VERSION     WP_008406861.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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   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 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   4  (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 18568702
            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="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=36897
     Region          17..74
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          96..271
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 msrrkaapgv ltaattadvf gevlryfree agltqealar qipcdrsqia hieagtrvpq
       61 dtfvktcdea lgtrdalmrl wvridwypqv ehpdwfkrra emdevavavr qyqaqtipgl
      121 lqteeyaqal faqvngpeet eervrarlsr qqrfldpdgp myialldesc lrtvvgdfdi
      181 mrrqymylle lgrrpniriq vvpagatgai rpntsmsiir lpegqewvys esldrghfsd
      241 apavlarhnq tydvlradal sasesaslis emteryrphg qvqpqrnpld qeqlqrqqrr
      301 rlprtrprvp rprprprqqd r
//
LOCUS       WP_008408645             237 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LytR C-terminal domain-containing protein
            [Streptomyces].
ACCESSION   WP_008408645
VERSION     WP_008408645.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 237)
  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 15441974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..237
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=23707
     Region          29..>125
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; cl16268"
                     /db_xref="CDD:472888"
     Region          92..169
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 msmltppgmg gkyritgdky prmrrtggrr klvlaatggv lalglvgwgt fqlvdvftgg
       61 stataaggrn cpapatsasp akatplpapg rikvnvlnat ersglakqta dalkkrgfai
      121 gevgnateey dkkvkgtvll lgaadavdga fpvlatqvgg akqkveapvk gepakadaae
      181 aegeadgaak gprkpnevdl iigdgfkkla peaaatgalk alnapkpsps ptaagrc
//
LOCUS       WP_008409893             244 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Desulforamulus
            hydrothermalis].
ACCESSION   WP_008409893
VERSION     WP_008409893.1
KEYWORDS    RefSeq.
SOURCE      Desulforamulus hydrothermalis
  ORGANISM  Desulforamulus hydrothermalis
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Peptococcaceae; Desulforamulus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 244)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 244)
  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 244)
  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 244)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Desulforamulus hydrothermalis"
                     /db_xref="taxon:412895"
     Protein         1..244
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27718
     Region          145..235
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(164,183..184,206,214..215,227,232)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 msikkfpdkq lrqgnlpgkh ewltvvpfll hpdpwqrrra amlfqagggl islqevllrl
       61 drfpedilvq aldwlqqwqw paaeapgsrl lllcinlanh pdarlaaagk gllsrlqkqr
      121 wpvqlhertv syaavsskqr eipfltvyln keeawlgdqy ldltpaqkrl vmrlagaagr
      181 flardalyta vqggdavygv pgdvkthikl lrhklgddgq rqhyieskrh ygyrlnltnv
      241 qiqk
//
LOCUS       WP_008411453             422 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp. SM8].
ACCESSION   WP_008411453
VERSION     WP_008411453.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. SM8
  ORGANISM  Streptomyces sp. SM8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 422)
  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 422)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces sp. SM8"
                     /db_xref="taxon:1195457"
     Protein         1..422
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45279
     Region          25..76
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msheavtwam ddapmlrtek grpdtttrgv lqvlaehadk dgqnarpsla rlryrtgydr
       61 rtvqralrrl eaaglikatg thgeitvyal alrtirpasd wtelledeqr qkdaardrqr
      121 ksrakraass aaaepstdpd vthlddvteq gvthsdderh asevrdvths ddarhalsaa
      181 ltvsepstep sttlgdgrrp ttgsegapeg gcaaaatasp aeeeteelrt aavgcviglm
      241 phrlrdqlpn pvpravtdai rtelarglta dqlvervgrr wwnhgyedaa esgdgpgilr
      301 pvgvaialvr rgqctsercd dgtdvdtgar crtcereaed rkrrreaaqa pvqgtilvgv
      361 psgatdaapa aprparrlpa qrteirdcer dcgsvhrtvp apapaglcpr ctaddaaqaa
      421 ng
//
LOCUS       WP_008411764             644 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Desulforamulus hydrothermalis].
ACCESSION   WP_008411764
VERSION     WP_008411764.1
KEYWORDS    RefSeq.
SOURCE      Desulforamulus hydrothermalis
  ORGANISM  Desulforamulus hydrothermalis
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Peptococcaceae; Desulforamulus.
REFERENCE   1  (residues 1 to 644)
  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 644)
  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 644)
  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 644)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Desulforamulus hydrothermalis"
                     /db_xref="taxon:412895"
     Protein         1..644
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=68009
     Region          22..644
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mtehnhqpqd rlnidrfmak ydresdfrrm sgwagiavav iavafslfql ytaifgvlda
       61 qiqravhlsf glalvyllyp arkswprhrl hwfdgllall avagplyiii yyqeiimrag
      121 ivtpadmllg glgilmvmea arrvvgwpiv ivatlflgya fagpylpgaf ahqgtnlsgl
      181 vghlfftteg vfgiplgvss tfiflfilfg aylektglgk ffidlanava gwarggpakv
      241 avlssglmgt vsgssvgnva gtgsltipmm kklgyrpefa gaveaaastg gqlmppimga
      301 aaflmaemvg tpyvnivkaa aipallyftg iwigvhleak kaglqgiprd qlprigsill
      361 erghlalpll aivyllvsgr spmnaalwai alaigasllr rstriswrdv lkgleegars
      421 algvviacat agiiigvvtk tglglklgsa lidlaggrll ptlfftmits iilgmgvptt
      481 anyvitstia aptliqlgvp vlaahmfvfy fgiiadvtpp valaafagsg iarsnpmktg
      541 veasklavaa flipyifvls pslllinttl pkvllmitts llgmtaiaaa lsgylaapar
      601 plerlvffgg gllmidpnll tdlvglgllv layllnlrqr arqa
//
LOCUS       WP_008412980             698 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Desulforamulus hydrothermalis].
ACCESSION   WP_008412980
VERSION     WP_008412980.1
KEYWORDS    RefSeq.
SOURCE      Desulforamulus hydrothermalis
  ORGANISM  Desulforamulus hydrothermalis
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Peptococcaceae; Desulforamulus.
REFERENCE   1  (residues 1 to 698)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 698)
  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   3  (residues 1 to 698)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..698
                     /organism="Desulforamulus hydrothermalis"
                     /db_xref="taxon:412895"
     Protein         1..698
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /function="11.2 : Protein modification and repair"
                     /function="12.3 : Protein interactions"
                     /function="13.1 : Two-component systems"
                     /function="15.2 : Chemotaxis and motility"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=75900
     Region          1..697
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mfsdleigvf ideleekiqv indgllaler degnpdiiqe ifraahtvkg ssgimgyqnm
       61 anlthemenl fdkirhgeiq vtsaminvlf ecldtlkalk eevtgegppv dtagvvakik
      121 qfvagagsdr parpasaaap peqaaavaaa paprrwldig eveenvirea elrgfqcykv
      181 avdidrdcqm knvraflvfe tlqqageiik seppaediqe gkydlgfqll lvtkedadri
      241 knlvitisev teaevqpvvl gnpepalaaa apdtagrlpa agpehngtkp eaadkkavkt
      301 vrvdvnkldn lmnlvgelvi drtrlnrfae ifesrfgsdd lveaineisn hlgqvtgdlq
      361 eqimkarmlp vaqlfnrfpr mvrdtaqklg keidfvvegk eteldrnvie vigdplihli
      421 rnaidhgiep aqerlaagkp atgtlllkas yaeshivitv kddgrgmdag kirhkavemg
      481 fvdretadrm sdrealqlif rpgfstknne vsdlsgrgvg mdvvntaieq ingtveldtk
      541 pgagttitir lpltlaiira lmvtlgnqvy afpltnvset iritdqdvrr ignnevivvr
      601 dkilplvrlg rlfncsecqe dskmfvvilg sgdkriavvv dkllgeqeiv ikslgdylgq
      661 vpglsgacil gdgkvalivd vrglvkelgt eevayaag
//
LOCUS       WP_008413185             404 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Streptomyces].
ACCESSION   WP_008413185
VERSION     WP_008413185.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 404)
  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 404)
  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 404)
  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 18568555
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..404
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43694
     Region          <8..64
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          <92..404
                     /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 mshtgnhrlr aariaagyps qqaladalgv gvrqvrrwes dappwpqgdv qqalprllgs
       61 nltelgftpp gsaphprptp rlttppttaa vptqatrhrq pasaaedyla vvrahrrlyw
      121 svaptilhpa avahaalgha lltetagrtr alvaaglges hllagrieff dlheadraaa
      181 twlralqaag eaddallgaa vlahtafvpg wagdreaame rmvaartyar rgpasaqlla
      241 wldaveaece trcghvrtal nlirhgeell argdehetpe wmdwfsagrl aafkgntqlk
      301 aghlpqardt llaaldalet geekqrsvll gdlaateaar grpeaacqya vraldqlelt
      361 wyavgmdrvr evrraltphq qeqcvrdldd rlygwsttvs alsr
//
LOCUS       WP_008414543             197 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Streptomyces].
ACCESSION   WP_008414543
VERSION     WP_008414543.1
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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..197
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=21283
     Region          29..194
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mappmsadrf lkalkeegvt vvevgswrsh nrnskgawgp vngvmihhtv tsgsartvdi
       61 crngysglpg plchgvitkd grvhlvgygr anhaglgddd vlaaviaera syppvneant
      121 dgnarfygfe cenlgdgkdp wtsaqldaie rvsaaicrvh gwnqqsvigh lewqpgkidp
      181 rgftmksmre rikgrlk
//
LOCUS       WP_008417552             123 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein [Streptomyces].
ACCESSION   WP_008417552
VERSION     WP_008417552.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..123
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=13490
     Region          8..68
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mqsdidprsl igrkafdrhg tkvgtvdevy lddatgvpew aavrtglfsr dafvplepse
       61 lvegglripf eralireapd fgvgrhlspe qelqlyhhyg ldigapeppp drdfgriagt
      121 dep
//
LOCUS       WP_008415465             279 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Streptomyces].
ACCESSION   WP_008415465
VERSION     WP_008415465.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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   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 279)
  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 279)
  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 18542080
            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="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30773
     Region          17..70
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
     Region          94..273
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mvnrkelnpe asphaafgak lrvvreaqgl tqdqlgsamg ytcghissve tgrkvptlrf
       61 srqvdqalgt antedsferq wreirqgsll egapeymgce arsaeirlye vgvvpgllqt
      121 peyaltlaeg avlrgsitee qaaervqmia drqealsrrs ppmvfvvlde sclrrpvgep
      181 timnaqleyl mefadrpntm vqvapfdlga rrpfdlpiyi ltmpdrqlms yaesaqrghl
      241 drestsvlpl ltayhqlqal alsqaasvam isqlrkgtp
//
LOCUS       WP_008419543             123 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: zinc ribbon domain-containing protein [unclassified
            Clostridium].
ACCESSION   WP_008419543
VERSION     WP_008419543.1
KEYWORDS    RefSeq.
SOURCE      unclassified Clostridium
  ORGANISM  unclassified Clostridium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
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 12181465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="unclassified Clostridium"
                     /db_xref="taxon:2614128"
     Protein         1..123
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14202
     Region          21..>63
                     /region_name="zinc_ribbon_15"
                     /note="zinc-ribbon family; pfam17032"
                     /db_xref="CDD:465334"
ORIGIN      
        1 miiwgwgrvt rkfiggvtqr tcnycnktsv wqlcivrtwf tlffipiipy kktyqiacps
       61 cgsyikltqe qfekiklels gassngatvn eienslkyeg ktetqinylk qmeeqkrmqa
      121 nnq
//
LOCUS       WP_008422528             198 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [unclassified
            Clostridium].
ACCESSION   WP_008422528
VERSION     WP_008422528.1
KEYWORDS    RefSeq.
SOURCE      unclassified Clostridium
  ORGANISM  unclassified Clostridium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="unclassified Clostridium"
                     /db_xref="taxon:2614128"
     Protein         1..198
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22027
     Region          4..194
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mnetlsviks rrsiknfqpe qikdteleai leagtyapsa snqqswhftv vqnkrligql
       61 seaikkiyam mpvsfleqmk ndkkahflqq ignnekvhlf hnaptivvis gdktemytve
      121 ncslaagnmm naaksldvgs cwvsglpqli daepdnqfik elnlpegykp vcvillgyka
      181 gadkkvaerk envvnyik
//
LOCUS       WP_008422707             281 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Clostridium].
ACCESSION   WP_008422707
VERSION     WP_008422707.1
KEYWORDS    RefSeq.
SOURCE      unclassified Clostridium
  ORGANISM  unclassified Clostridium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 281)
  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 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   3  (residues 1 to 281)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 281)
  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   5  (residues 1 to 281)
  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   6  (residues 1 to 281)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="unclassified Clostridium"
                     /db_xref="taxon:2614128"
     Protein         1..281
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32432
     Region          21..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..278
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mdwlermnka ldyiennldg kinytevaqt aycseyhfsr mfssiagisl seyirrrrlt
       61 naafeiqknn triidvavky gyesadsfsr afrkthginp sdarqkgvql kayprisfqi
      121 sikgdmemey rienidfelr ivgksksvkt srafktiptl wnnakkdgft qelidmswen
      181 pkcmlesilg vcgkeatimd eefdyfmgvr ydgkapsgme tliippstwa vfpnitdawk
      241 rlysewipts gyefanlpci ecfygpkhkp rhelwvpvip k
//
LOCUS       WP_008423855             205 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Clostridiaceae].
ACCESSION   WP_008423855
VERSION     WP_008423855.1
KEYWORDS    RefSeq.
SOURCE      Clostridiaceae
  ORGANISM  Clostridiaceae
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales.
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   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 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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Clostridiaceae"
                     /db_xref="taxon:31979"
     Protein         1..205
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=23451
     Region          14..67
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mkkgemldkv yksnlpsrak qimfyfinra naegtcfpsv ktiasdcgvs ertiqrnmni
       61 lveegfiike eryrdnggqs snlyrlqikp ennnikpnan enkldeeklk dievkeeisn
      121 ienievvnfe dyeeekdvie netkkektyi vdvsmgvpsn kanlvnkync hpsifyeigk
      181 krkpitimsa lsslchgesd nlypp
//
LOCUS       WP_008426153             187 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [unclassified
            Clostridium].
ACCESSION   WP_008426153
VERSION     WP_008426153.1
KEYWORDS    RefSeq.
SOURCE      unclassified Clostridium
  ORGANISM  unclassified Clostridium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="unclassified Clostridium"
                     /db_xref="taxon:2614128"
     Protein         1..187
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21472
     Region          3..184
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdviqaieer rsirkfqdkt ipkdiiekil elatkapsgk nrqpwrfvvf qnskknelvn
       61 imedalnkyk kqskstgsfe lsinsineas avilvfnafs nfeedynhhr lltdiqsiga
      121 avqtlilaaq nfelgtlwic difhcdkeic swlnrkdelv aavaigypnq kpysrprkll
      181 eeviewm
//
LOCUS       WP_008425615             279 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase family protein [unclassified
            Clostridium].
ACCESSION   WP_008425615
VERSION     WP_008425615.1
KEYWORDS    RefSeq.
SOURCE      unclassified Clostridium
  ORGANISM  unclassified Clostridium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 279)
  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 12830887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="unclassified Clostridium"
                     /db_xref="taxon:2614128"
     Protein         1..279
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=30420
     Region          50..114
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          160..278
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(228,231,251..254,256)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkktilslav aeviiscsmq skahavtisn tndtsngiat istlqgsgki isigskgsiv
       61 rsiqrllnsl egyniqedgi ygaetynait kfqaknglkq dgivgkqtad kllsintkpe
      121 inivnskign glekvkvtnv keiinsklnl keinsdtnyf iavsksqrev yiyhkeidsw
      181 vnikafscni gapgsptieg dfysglkgke lrinetyvky ftqisgnylf hsvpyneige
      241 aiddcfgeev shgcvrlsle dakyiydtip agtsikiie
//
LOCUS       WP_008426354             348 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [unclassified Clostridium].
ACCESSION   WP_008426354
VERSION     WP_008426354.1
KEYWORDS    RefSeq.
SOURCE      unclassified Clostridium
  ORGANISM  unclassified Clostridium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="unclassified Clostridium"
                     /db_xref="taxon:2614128"
     Protein         1..348
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39834
     Region          1..346
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mslyidienn lpsfdlkvnf ehkngilgfl gasgsgksmt lkclsglvtp skgkiilnnl
       61 vlfdsekkin lspqkrkvgy lfqnyalfpn mniiqnieig ishfnydkkk slckeyierl
      121 gltglekhyp wqlsggqqqr valaralits pdillldepf saldqhlrnn lekeltsilk
      181 dysgnvifvt hdiaeayrmc seiivydkgi slekrekndl fkrpknlsea tltgcknisk
      241 arktgehtiy aenwgheyti vdkipndvqy icirahniei aqdnkkentf pykigkiien
      301 pfeftvymkn stsseatlie ykvekknmnf tinetvyltf snehlfyf
//
LOCUS       WP_008427449             300 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Clostridium].
ACCESSION   WP_008427449
VERSION     WP_008427449.1
KEYWORDS    RefSeq.
SOURCE      unclassified Clostridium
  ORGANISM  unclassified Clostridium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 300)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   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
REFERENCE   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="unclassified Clostridium"
                     /db_xref="taxon:2614128"
     Protein         1..300
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34996
     Region          22..105
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          134..291
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mkdlketiie tidyiennly nkislddisl htgiskyylh rifksltges iieyvqarkl
       61 tssinelist nmrvidialn ygfdyeqsyi rafkksfgct plkvrseqts islilkekin
      121 vndilslgnt vtytphfvfk qkfnligikh kilsksgdks anaygrdffy nhkdsirsii
      181 npheyygftd wgsdefiyyv psvqvsdcny ipegmtsisi pshkyvvfrl vgffrpddln
      241 grhlgrllvq lyrkwifnsg yefadtfrfe yidssiskdn ycelyvyqpi kdierkmelv
//
LOCUS       WP_008428598             288 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Planococcus
            donghaensis].
ACCESSION   WP_008428598
VERSION     WP_008428598.1
KEYWORDS    RefSeq.
SOURCE      Planococcus donghaensis
  ORGANISM  Planococcus donghaensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Planococcus.
REFERENCE   1  (residues 1 to 288)
  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   2  (residues 1 to 288)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Planococcus donghaensis"
                     /db_xref="taxon:414778"
     Protein         1..288
                     /product="aminoglycoside 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=32741
     Region          19..241
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mikkvlekfa vqpvamhkve dsfsstvykc alhtgehiyv kiaytklkye reldayklla
       61 gkvpvpqmld ywsgdsecpg afllselkgk tlttdvssev afqvgilhaq mhavcppvgq
      121 ettsienefs nwlnfieskf ldfaedvkei vetalyeksm nkfselkqql papvgpsfih
      181 mdfrpaniiv dgekvsgvid fesvrfgsid idftklyrdf lsvndgfyqa yqdgyrtikp
      241 lldlkkvlpf yqfldafnsi gwcrrrgiek natfleenlv ilkkivne
//
LOCUS       WP_008428749             194 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [unclassified
            Clostridium].
ACCESSION   WP_008428749
VERSION     WP_008428749.1
KEYWORDS    RefSeq.
SOURCE      unclassified Clostridium
  ORGANISM  unclassified Clostridium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="unclassified Clostridium"
                     /db_xref="taxon:2614128"
     Protein         1..194
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22082
     Region          4..190
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 menvieviks rrsirkykse qindedlytv lecgkrapsg gnsqtwhftv iqnkeillkl
       61 nkyiklafek levdentyks kksgkvasqn dnysfyynap tliivsndmn ysnamadsac
      121 aienmlltan ylelgacwin qvtwfdrden vrkllsslgi penyrvcgsi sigyidgekp
      181 kekilkentv tiik
//
LOCUS       WP_008429616             263 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Planococcus donghaensis].
ACCESSION   WP_008429616
VERSION     WP_008429616.1
KEYWORDS    RefSeq.
SOURCE      Planococcus donghaensis
  ORGANISM  Planococcus donghaensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Planococcus.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 263)
  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 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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Planococcus donghaensis"
                     /db_xref="taxon:414778"
     Protein         1..263
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29839
     Region          24..259
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <160..259
                     /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 mplamdsilf hsiqsfsvpy gtsqhyqlhh hpdtielllv lsgtvhckid gqiyiapagt
       61 vlfiqagswh eqlytasdkh cgyrltfcpv dstnygdlpp iipikpidsl ktlfmqlqqe
      121 keylrtdskq mahhlinsil lhvyrsaskh escsysnlee tvqeikhyme enhakslsle
      181 dlaarfnltk yqlarlfkki tgmsplqyii scrittakyl lrtsdnsvsk iavkigyksd
      241 tqfqaafkti vgvtprqyrv nsk
//
LOCUS       WP_008429770             255 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [unclassified Clostridium].
ACCESSION   WP_008429770
VERSION     WP_008429770.1
KEYWORDS    RefSeq.
SOURCE      unclassified Clostridium
  ORGANISM  unclassified Clostridium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="unclassified Clostridium"
                     /db_xref="taxon:2614128"
     Protein         1..255
                     /product="formate/nitrite transporter family protein"
                     /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=27045
     Region          12..255
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mfceefnsvv maakakvnll rtnksgyfis smlaglyvgm gimlifsigg llggsaspat
       61 kivmgvsfgv alslvimags elftgnnfim taaslkgkvk wtdtiniwiv cfignlvgsi
      121 iagvmfyctg lsagpvgefi aktsatkmsi pfwpllmrgi fcnilvclat wcsfklkses
      181 aklimifwcl fafitsgfeh svanmtllti gllnpgaasv simgyaynig vvtlgnmigg
      241 avflalpyyi iskkk
//
LOCUS       WP_008429775             173 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [unclassified
            Clostridium].
ACCESSION   WP_008429775
VERSION     WP_008429775.1
KEYWORDS    RefSeq.
SOURCE      unclassified Clostridium
  ORGANISM  unclassified Clostridium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="unclassified Clostridium"
                     /db_xref="taxon:2614128"
     Protein         1..173
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19370
     Region          4..166
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mnevlqnils rrsvrqfkpe qikddelkli leagtyapsg mnkqswqftv vqnkekieql
       61 akvirealgr dagynfyapp tlimlsndkd ntngladcac aleniflman slgigscwin
      121 qlkticdeke vrevltsfei penhivwgia avgypestpk aherkdgvik fvk
//
LOCUS       WP_008430533             129 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Planococcus donghaensis].
ACCESSION   WP_008430533
VERSION     WP_008430533.1
KEYWORDS    RefSeq.
SOURCE      Planococcus donghaensis
  ORGANISM  Planococcus donghaensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Planococcus.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 129)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Planococcus donghaensis"
                     /db_xref="taxon:414778"
     Protein         1..129
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=14371
     Region          2..126
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(7..10,40..42,45,69,108,122)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mlevfvdaas agipqvsavg vfirgeghvi hwseyvgemd nhtaeftalv kglelakela
       61 pqmisiksds qvtvdaferr fiknpkfkpl leraleigdq feycfikwip dsqnraadal
      121 artelrahk
//
LOCUS       WP_008431273             388 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Planococcus donghaensis].
ACCESSION   WP_008431273
VERSION     WP_008431273.1
KEYWORDS    RefSeq.
SOURCE      Planococcus donghaensis
  ORGANISM  Planococcus donghaensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Planococcus.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Planococcus donghaensis"
                     /db_xref="taxon:414778"
     Protein         1..388
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43897
     Region          1..275
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          271..355
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkffhtadwh lgklvqgiym tedqqfvleq fldaikeekp daiiiagdly dravpptdav
       61 nlldellaei vlelktpvls vvgnhdspgr lnfgsrlmkg ngihiaghvh knhqavvlnd
      121 qfgevhfhli pyadpsmvry efdddtirth ndamkaiten iksaynphar hvfvghafvt
      181 phgeqeents dserplsigg aehvdahhfe gfhytalghl hkahfvlnet irysgsplky
      241 siseehhkkg fhiveldaqg evtvekrlft pkrnmrtveg tideilthei sddyvfvtll
      301 detpvlfpme kvrsvypnam hvgrqnfsgt mlqsetgsrr kmdslslfha fyeevkgeka
      361 tketvdtfkd vlgeflreep avkeevks
//
LOCUS       WP_008432847             133 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Pseudomonas sp. Ag1].
ACCESSION   WP_008432847
VERSION     WP_008432847.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. Ag1
  ORGANISM  Pseudomonas sp. Ag1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Pseudomonas sp. Ag1"
                     /db_xref="taxon:1197727"
     Protein         1..133
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14020
     Region          7..131
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mgkdctgftl ielliavaiv gllagvaypg ylshmkkvyr aeiagllseq aqyleryysr
       61 ngtfidatgv iagndryrit palnpqdfvl latpaidsvm agdpcaafsl sstgarsnpg
      121 aapdmtrkac wgq
//
LOCUS       WP_008433295              86 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Rhodanobacter thiooxydans].
ACCESSION   WP_008433295
VERSION     WP_008433295.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter thiooxydans
  ORGANISM  Rhodanobacter thiooxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 86)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 86)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 86)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Rhodanobacter thiooxydans"
                     /db_xref="taxon:416169"
     Protein         1..86
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8781
     Region          2..86
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mkvevslfga frdhepgaav tlevpagarv adlrsalaay grahwpgfre glllrsafas
       61 qtcvlgeqea lpesgpvvvl ppvggg
//
LOCUS       WP_008433413             808 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Rhodanobacter thiooxydans].
ACCESSION   WP_008433413
VERSION     WP_008433413.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter thiooxydans
  ORGANISM  Rhodanobacter thiooxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
REFERENCE   1  (residues 1 to 808)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 808)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 808)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..808
                     /organism="Rhodanobacter thiooxydans"
                     /db_xref="taxon:416169"
     Protein         1..808
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=87828
     Region          29..805
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mtatsrrksr wrllralslv llallavafi vlgwllagsr aqldgtrqaa gltapvsldr
       61 dalgtvtlvg ksrtdlsyal gyvhaqerff amdlmrrvsa gelsalvgpa aletdldhrr
      121 hrlravvaaa yaqltptkqh qldryrdgvn agladlrvrp weylllgsrp qpwrsedsml
      181 viaamyldln sggrnerelr maqmravlpg alvdfllapd pdweaplsgw lsrppvvpda
      241 dvfdlrrlpt aaastslaaa lvpaldtprp gsnnfavagt ltgngaamla ndmhlglrvp
      301 niwfrtrlry pdptapgsqr dingvslpgt paiivgsngq iawgftnsyg dwqdwvrvlr
      361 dpadasrykv angwasieth eehirvkgqp dtilkvedtr wgpimgsdid stplalawig
      421 grahgynldl mqlerapdva aaielaprlg ippqnllvad raghigwtia gnsiplragi
      481 drllpsdwsa pgsgwqgwaa paqyprienp adgrlwtann rtvdgdalal lgngghdvga
      541 raqqirddlr arasftpgal ldiqlddral flarwqrllq dtladnrdps lqqlrrltaa
      601 wggraavdsv dyrlvrafrn qvgeavlapl aarvqqryad fswpretsae aavwalvrqq
      661 pmawldpkyp dwhallidaa krvadelgqq sgglaarswg ehnragirhp lsaalpswla
      721 rfidmpdqpm pgdnnmphva apgfgasehl vvapgqeahg ilnmpggqsd hplspyfgag
      781 hadwvagrpt pllpglpqht lvlqpvar
//
LOCUS       WP_008433482             184 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Rhodanobacter thiooxydans].
ACCESSION   WP_008433482
VERSION     WP_008433482.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter thiooxydans
  ORGANISM  Rhodanobacter thiooxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Rhodanobacter thiooxydans"
                     /db_xref="taxon:416169"
     Protein         1..184
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=20718
     Region          18..172
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mpltihdqpl pyvdllperp avavelvvih ctelpdlama reygervlha sgtgnsghyy
       61 vdrdgavyry vpgtrvanhv rghnpdsigi elvnrgryph wwdshqqqmt epyaevqiaa
      121 llallaqlra efphlrriag heeldtdlmp asddparqir rkfdpgprfp wdaivpasgl
      181 erlr
//
LOCUS       WP_008434017             113 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Rhodanobacter thiooxydans].
ACCESSION   WP_008434017
VERSION     WP_008434017.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter thiooxydans
  ORGANISM  Rhodanobacter thiooxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Rhodanobacter thiooxydans"
                     /db_xref="taxon:416169"
     Protein         1..113
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12004
     Region          16..102
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(23,54..55,57,83)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(23..24,32,35,37..38,40,43..44,46,54,59,68)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mneaaariya aiaaiprgrv asygaiaara glpgrarlvg rllgevpdgm elpwyrvlrs
       61 sghiamapgs rgfreqsrrl raegvevkng rvplsrfgld gdldhalwgm pdg
//
LOCUS       WP_008434095             295 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [unclassified Pseudomonas].
ACCESSION   WP_008434095
VERSION     WP_008434095.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..295
                     /product="formate/nitrite transporter family protein"
                     /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=32331
     Region          24..276
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 matqedgktp nlsqeeqhdv dknqppraav lheiirtqgd qelernvaal wwsalaaglt
       61 mglslmgmgl lnsrlpdgee fkviasfgyc agflavilar qqlftentlt avlpvmskpt
      121 lknfarllrl wavvlvgnlc gtllvayvml hlpifdtktd lafleigrkv mendayqmfa
      181 kgivsgwmia tmvwmipsme sakiwiiili tylmalgdft hivvgsaevs ylvfagelpw
      241 kdfwlvfagp tlagniiggs fifalishaq irsesslpgk aaadprhpqq inkgq
//
LOCUS       WP_008434352             809 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [Pseudomonas].
ACCESSION   WP_008434352
VERSION     WP_008434352.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 809)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 809)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 809)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..809
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..809
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87921
     Region          66..111
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          92..809
                     /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 msrtldtllr psllavaial saplastqll aaeqassvra ynlpaaslat tlnqiasqag
       61 laltlnpgla agktsapvkg qfdaqgalre alrgtglqle qssagtfslv aipdgvvalp
      121 etsitgqada esawgpvdgy latrtaagtk tdtalveapr sisvatrqqm qdrnvqnldd
      181 avkympgivs asygsdtryd wmrvrgfept qfldglplpr gvyanpkaet wnldrlallr
      241 gpassvygqt ppgglldmvs rrpsaessna iqvqygsdny rqinfastgk iddegqflyg
      301 lsgvvrdagt qvdhidnkry niapsltwni dtdtkltfls qftrddtgat sqflpivgtk
      361 iksplgdish hknlgdpdye yydrtyyalg yafehrfndt wqfkqnlryt kselafqqlt
      421 vgsygystid aegntsrsst nvdenigqfa vdnnfqadfa tgdithtlll gldhqrtdts
      481 ylsifgdggt vnlynpvntk pvvrparsta yydynqktiq tglyaqdqma ldqwrltlgg
      541 redwvhqgtt yfnkndatnt drsknfsgna alsyvfdsgf vpylsyaesf qpasnasvsp
      601 tesykptegk qwelgvkyqp pgsntllsaa vydltqknvl vtsfgaggqs itdqtgevkv
      661 kgleleavsd vtenlkviaa ytlaksevqk gqykgnrlql mpnqqaslwt dytwhagvld
      721 gfgigagary tgntygdqgn twlgkanayt vfdasvhydl grldnslkga svklnatnlf
      781 dkdyistcda sycyygdqrs vvasatyqw
//
LOCUS       WP_008434507             821 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [unclassified
            Pseudomonas].
ACCESSION   WP_008434507
VERSION     WP_008434507.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 821)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 821)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 821)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..821
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90293
     Region          68..118
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          95..821
                     /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 msaiagiprf tkalfmrrml qpgfsatafs malalpfsaq vqaqeinfni paqslasalq
       61 algtqsnmqv lysaddvkgq hsqpvsgrls peqalsqmlv gtgavftvqa ntvtvrarat
      121 gdslelgatt isgqavesay gpvdgyvatr satgtktdtp lleipqtvnv vtakqietqg
      181 alnltqalry tpglntggft drnaiadeit srgfaptqly ldgaylpyag slggapqidp
      241 ytlerievlk gpssvlfgqn qpgglinmvs krptteqrse vkigagsynr vngafdtsgp
      301 lddqkefsyr ivgvakkgnq qvdhthserm llapsltwap nddtsltvla qiqrdrgled
      361 yqalpmigsl ergpngkrid rnffsgdsky ndykrdqfil gydlthsfse nlkgrstary
      421 tdvrddykgf ylrsfvtdav tgavdqtran rvkldwrqhn taytidnnle ykfntgaleh
      481 ttlvgldyrn fnrkytgyna ynvlpinlyg ennnydtssv tpekttkwdn tvrqtgvylq
      541 dqikldkwil tiggrqdwae venkdlians iteqrdnkft grvgltyvtd fglapyvsys
      601 esflptvgtt aperggkafa ptegeqyevg vkyqpfektl itasvyqikq knvlsqdney
      661 tqysvqqgqv rsrgvelevk ssianvdvla aasyldafyi knnygntgnr teqqapvsas
      721 lwvdyhftqa vlngltfgag arytgpkpgd aansfevpgf vvydttvsyd lskvspslrg
      781 vetslnvqnv fnreyvshcn ysfgcyygqe rvasvdvtyn f
//
LOCUS       WP_008434551             828 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [unclassified
            Pseudomonas].
ACCESSION   WP_008434551
VERSION     WP_008434551.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 828)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 828)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 828)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..828
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..828
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90010
     Region          67..118
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          94..828
                     /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 mqafpskrsp lkhavhaall gaclngsalp lavmaqtpvs dtqardwnia pgplatvldq
       61 farqasisls ydatsvagkt spglngalds qqalsqliqg qglqaqrqsn ntwlllpqva
      121 dtgalnlgat tvtgehlgvt tdgsgsyttg avtigkgahs lretpqsvsv mtrkliddqn
      181 ittidqlleh tpgittydsp mggkyfysrg fkmlgqyqfd gvpldigkdy vqadsftanm
      241 aiydrvevlk gaagmlkgag tasgavnfvr krpqdkptts lslsagtwdn yradvdtggp
      301 lndsgtvrgr avvsqqnrgs ymdvskrqdq avylaldvdl spdttlgiga syedvdatpc
      361 wggvprysdg ksiglsrstc lgqawndwqs qrttlfadlt hhfnddwqlk vtavnsrnlq
      421 dikyaasqgt vkygdpapta emyaalfdyd hrdfgldayl dgkfeafglq heliigangs
      481 rgtqddvyai rslpdrqsif lpnhhfpqpa ndtfwpnmyr ggtvketatq ygtyatlrlr
      541 laeplmvvlg srvswfenrr qsnnlawgew alqdartket gevtpfaavi ydlddnlsvy
      601 asyadifqpq ssnatvtgaa lkpkigenye lgikgewfeg rlnsslalfr aieknaaetd
      661 yttqcgtsad gycytdtgkv raqgveaels gellerlqva ggytytqtkn lnninsaaig
      721 avansyvprh mlrlwgdyql dgtlskwsvg tgvnaqssny riqgikleqa gyavwnarla
      781 yrvddtwtva lngnnlfdkn yyqtvgtadw gnfygeprnf tvslkgnf
//
LOCUS       WP_008434582             829 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas sp. Ag1].
ACCESSION   WP_008434582
VERSION     WP_008434582.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. Ag1
  ORGANISM  Pseudomonas sp. Ag1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 829)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 829)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 829)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..829
                     /organism="Pseudomonas sp. Ag1"
                     /db_xref="taxon:1197727"
     Protein         1..829
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90026
     Region          76..127
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          104..829
                     /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 mragqtsvan splrsfrkkp lqvalfgvsl mvqysllgpl lspgssavaa spqktfsiap
       61 gplgsvlsrf asdagvvlsf dsgltagkqs qgltgtysve qgfarllags alsvaangdg
      121 syglipqssg altlgatsin aeglsltten tgsyttgats tatklplslr etpqsvsvvt
      181 rqlmddqhls tlnevlaftp gissnhrdse rysfysrgfe iqnfqydgip sqvanesqqy
      241 tgaisdmaiy drvevvrgat glmsgagtps atinlvrkrp tkdfqayvsg eagawdryrs
      301 evdvsgplte tgnmrgrfva ayqkqnsfid wykqdkrvmy galdidlnen ttlrtsldyq
      361 nndangstyg hiplfynngt qthfsrsfnp asrssymdnt sytfttmldh kldddwslkt
      421 ayshqysyrk gqgasasggy pdpvtgqgag afiyrlnsyq tqdtvdvyat gpfqlggreh
      481 elvmgasssr thlnfpdyss gsadndygqv dniftwdgrq ysrrsytevg gtvttlqqtg
      541 vyaalrlkpi dpltiilgtr vswwnqenad rdyaagtkti dktrktgvvt pyagviydln
      601 dtysvyasyt niflpqtfyk tsskgslapq qgdnyeiglk geffngalna sialfdieqk
      661 ntpeqsgtds sgaavykaia gtstrgvete isgevaegwn vfggytyres hdkdgarvqa
      721 nqpinlfklg tsyrlpgnld rltiganvtw qseiyassqi nyegpyykak qdpygvvgll
      781 asyqvdehls vglnvnnlfd qkyydglgtf nsgsygeprn amvkakwqf
//
LOCUS       WP_008435383             124 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Rhodanobacter thiooxydans].
ACCESSION   WP_008435383
VERSION     WP_008435383.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter thiooxydans
  ORGANISM  Rhodanobacter thiooxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
REFERENCE   1  (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   2  (residues 1 to 124)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Rhodanobacter thiooxydans"
                     /db_xref="taxon:416169"
     Protein         1..124
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12353
     Region          23..87
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mfnklvtaal alafalavpg lllaatpvni nqadaaaiak sldgigpaka eaivawreah
       61 gpfkkaddlk hvkgigkati ernraailla ddgsaapata aadapakkah rskkaataea
      121 agee
//
LOCUS       WP_008436760             234 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Rhodanobacter thiooxydans].
ACCESSION   WP_008436760
VERSION     WP_008436760.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter thiooxydans
  ORGANISM  Rhodanobacter thiooxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
REFERENCE   1  (residues 1 to 234)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Rhodanobacter thiooxydans"
                     /db_xref="taxon:416169"
     Protein         1..234
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24926
     Region          64..206
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 msrlprhaaa ltlflaaagf saahaatpsl qdalsqlapq anpkviglal aatecaaaqg
       61 qppsdrlavi dyskpstepr lwvfdlakrk llyhelvahg rntgdnlatr fsntpeslqs
      121 slglfrtldt yagrngyslr meglepgtnd haleralvih gaayvnpala hqqgrigrsy
      181 gcpavrsaia rplidalkgg qyvfsyypds rwlnaspylk cssgramtas inap
//
LOCUS       WP_008437318             197 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Rhodanobacter thiooxydans].
ACCESSION   WP_008437318
VERSION     WP_008437318.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter thiooxydans
  ORGANISM  Rhodanobacter thiooxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Rhodanobacter thiooxydans"
                     /db_xref="taxon:416169"
     Protein         1..197
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=22024
     Region          15..197
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mlptpihrlf ahsstlrsse latqgvprmq lsrwvaegkl qrlgrglyal pdyapnqhas
       61 lvevaspapr vvfclltalr fhelttqapf evwiaignke hpprlpypkl rvhrfspasl
      121 hygveehrvd gaklrvtdva ktvadcfkfr nkigldvale alrdavqgrr tnmdeiwraa
      181 tvcrvaavmr pyleslg
//
LOCUS       WP_008437725             110 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [unclassified
            Pseudomonas].
ACCESSION   WP_008437725
VERSION     WP_008437725.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (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   2  (residues 1 to 110)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..110
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11793
     Region          45..107
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mrkayfssfv faflaslsla ttaapstkpe tptsistqmt kvdhttkvsl nsadaetlrr
       61 dlfgigaaka kaivayretn gpftaidell evkgigkall eknrdrlevn
//
LOCUS       WP_008437541             399 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Pseudomonas sp. Ag1].
ACCESSION   WP_008437541
VERSION     WP_008437541.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. Ag1
  ORGANISM  Pseudomonas sp. Ag1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 399)
  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 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   3  (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   4  (residues 1 to 399)
  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 399)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Pseudomonas sp. Ag1"
                     /db_xref="taxon:1197727"
     Protein         1..399
                     /product="CmpA/NrtA family 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=43638
     Region          12..263
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 msdplawvng sdapekssln lgfmalsdca svvvaatqgf aqpygltlnl rrqsswaslr
       61 dnlvsgelda ahslygliya vhlgiggvap tdmavlmgln qngqsinlsr glqqlgvtsp
      121 ealdrhvhqs rtkltfaqtf ptgthamwly ywlasqgihp lqdvdsvlvp ppqmvahlqa
      181 gridgfcvge pwcasavkqn qgftlattqa lwpdhpekvl gctqafveqy pntarvlvma
      241 ilqasrfieq stenrrstaq llsapqylda pldcieprll gdyddglgnh wqdphalrfy
      301 gdgevnlpyl sdgmwfmtqf rrwgllredp dylgvarrvq qldiyrqaas avgvpaggea
      361 mrssqlidgk iwdgsdpagy arsfrlhama dvasrqalr
//
LOCUS       WP_008437905             292 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Pseudomonas sp. Ag1].
ACCESSION   WP_008437905
VERSION     WP_008437905.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. Ag1
  ORGANISM  Pseudomonas sp. Ag1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Pseudomonas sp. Ag1"
                     /db_xref="taxon:1197727"
     Protein         1..292
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31637
     Region          13..255
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mrievlvdvk ttlgegpvwd veqqrlywid sadgrilrct edgrelrawd vgqkigsmal
       61 rhsgeqaiva lqngvhlldl nsgelalvid pepalpnnrl ndgkvdrqgr fvfgsmdtle
      121 dsasaklyrl dadlslhtld egiivsngpc wspagdtfyf cdtwsgeiwa ydydpasgav
      181 snrrtfakvd tsgggaadgc tvdaegclwq alvyagklvr ytpdgqvnri iqmpvkkvts
      241 ltfggpnldt lfvtsmakpp lprfpadgqq rgalfaitgl gvqgiaerrf as
//
LOCUS       WP_008438606             147 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: pilin [Rhodanobacter].
ACCESSION   WP_008438606
VERSION     WP_008438606.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter
  ORGANISM  Rhodanobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Rhodanobacter"
                     /db_xref="taxon:75309"
     Protein         1..147
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=15498
     Region          9..146
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mlhqrisagf tlielmivva iiailaaiai payqdylirt qvtegmslad gaksavwdfv
       61 sntgrfppnn qsaglaknrs iegsyvssvd vtggaikvly qgtkanthin ggsiylllsp
      121 ithagsiawt csastldpky lpsscrr
//
LOCUS       WP_008438998             484 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA, partial [Rhodanobacter thiooxydans].
ACCESSION   WP_008438998
VERSION     WP_008438998.1
KEYWORDS    RefSeq.
SOURCE      Rhodanobacter thiooxydans
  ORGANISM  Rhodanobacter thiooxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 484)
  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   3  (residues 1 to 484)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Rhodanobacter thiooxydans"
                     /db_xref="taxon:416169"
     Protein         <1..484
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <95..470
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 vhavqqrlel avvealldsm ygnaapgtva paplpaapaa sattidddef ealldalhgk
       61 pgqpaaplpt pvaaaapava aapaaapahh aapaensvrv dtarldllvn hagelvllrn
      121 rllslaarhg sealaaaane ldritdelqg avmgmrmqpv grlfqrfpri vrdlarqlgk
      181 dvelvlegeg tdldrslvea ladplihllr naldhgvemp dareragkpr kgrvclsasq
      241 rgeriviavr ddgrgmdpei lrrkavekgv idavqasrls dgecyelifr pgfstaaavs
      301 disgrgvgmd vvktrvaelg gtlqvrstlg qgseleltvp ltlavlrvlm vrvdtrlfal
      361 pmgnvaevfe ldagqdclld grliarhrgr alplldltgw agapaaagrh vvvlhighrr
      421 lgclvhevlg redvivkplg plfdgvpgia gatvtgdgrl alvmdlagla gdddqpstsl
      481 qstg
//
LOCUS       WP_008443517             493 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Janthinobacterium sp. HH01].
ACCESSION   WP_008443517
VERSION     WP_008443517.1
KEYWORDS    RefSeq.
SOURCE      Janthinobacterium sp. HH01
  ORGANISM  Janthinobacterium sp. HH01
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 493)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Janthinobacterium sp. HH01"
                     /db_xref="taxon:1198452"
     Protein         1..493
                     /product="amidohydrolase family protein"
                     /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=54019
     Region          20..487
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mktirrigct laslslllct qawagtqtwi tnvqlvspek ldrieagsvl iederivrvv
       61 rgaggkapag arrvdgkgqf ltpglidshv hlfsvpgmsf eqadqkktma aeyfaqmprs
      121 flyygyttvi dlaagsrefi drvkaaplhp dvydcgaplv fangypssya ppetrfemfs
      181 nfiydpaqad kiparfkped ytpakgvarv kadhgicvkt hfehgfgtmh nlpvmspavy
      241 gevraaasrd nlvlvthgns feaqtfavdg gadvlahgmw hwgemdkeke lppairqlld
      301 kiaarkigyq atmqvlhgln ayfepaylnh palpkllpps mlawlktpeg qwfkqeiaed
      361 etdaavlkgm eaplrrqrqv vaylaakdan fvfgtdtpss ptygnipgln gylemqdlhq
      421 aglslaqlfk aatinnartf kidaqvgtie agkvanlvlm kmspladira ydsvqtvwvr
      481 gretprdsla vap
//
LOCUS       WP_008443737             819 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Janthinobacterium sp. HH01].
ACCESSION   WP_008443737
VERSION     WP_008443737.1
KEYWORDS    RefSeq.
SOURCE      Janthinobacterium sp. HH01
  ORGANISM  Janthinobacterium sp. HH01
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 819)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 819)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 819)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Janthinobacterium sp. HH01"
                     /db_xref="taxon:1198452"
     Protein         1..819
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88193
     Region          62..112
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          91..818
                     /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 msnthatpsa rclsravria vlsmslaaas laaaaepapq tyqldagplg rtlstiavga
       61 gmplsfdpal taglnspalk gsytpraame rllagsglal vgrsdgtltl qkhaptpats
      121 stsataiaga ttlaqvevhg mgegsngtpg kirssgatgl elsvrdtpqa msvigsqrih
      181 dqgletlqdv vaqttgitld hssttretdq lfsrgfavdt ylfdgipttk lveptgfdan
      241 iyerieivrg aaglmggtgs paaainlvrk rpsrelraea elqagswdry raqadisapl
      301 sddksvrgrv vvaeqeqgsf idryrqdkdl fyaiveadlg hstllstgls yqherlngas
      361 rrfigfysdg sqtdfprsin sasqasfydr kqslsfvtle hffdndwsak lavnyaanqy
      421 daeqgyamrg qldkrtgagl slwqtkwdsk pqqlsidaya sgpfsafgrq hdlvfglsas
      481 ntkttgptfp awslpgydat vpnfytwngn sptpnyngti ngsnlekers lagygsvrlr
      541 ptdalslilg mrvtnwkrdt esvsfgsptv sdsfskngkl tpyvgavyal tpdwstyasy
      601 tsiyspqtyr drsnsllppl egnntelgik gdflngllst sasvfhmrqd nlaemdadef
      661 llpagggtya yhtvkgataq gfelevsgql rrgwqltagy arsrvedssg krlqtsqpln
      721 nlklwssyel pdvgngltvg gginwqgeiy tdnagpnrer ftqssyalvs lmaryrisqq
      781 lsatlnvnnl ldkhyyssgg ggfygdprnv mlslnyrfh
//
LOCUS       WP_008445199             209 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Oxalobacteraceae].
ACCESSION   WP_008445199
VERSION     WP_008445199.1
KEYWORDS    RefSeq.
SOURCE      Oxalobacteraceae
  ORGANISM  Oxalobacteraceae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales.
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   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   3  (residues 1 to 209)
  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   4  (residues 1 to 209)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 209)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 209)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Oxalobacteraceae"
                     /db_xref="taxon:75682"
     Protein         1..209
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22616
     Region          11..198
                     /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"
ORIGIN      
        1 mnvptspkrl ilivdddqll ldflgevlgs sgydilkass aeqalqliaq repdlalldi
       61 hmpgmnglel akqlhatssv pfmflsgrgd adagkqaasy gavgflvkpv dathlmpaft
      121 aglaradeir qlrrtelnln aalaagrets lavgllmckf qtdrntafev lrdharsnrr
      181 kvnevadqll aaeetlnslh vafnqrlkk
//
LOCUS       WP_008446950             233 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Janthinobacterium sp. HH01].
ACCESSION   WP_008446950
VERSION     WP_008446950.1
KEYWORDS    RefSeq.
SOURCE      Janthinobacterium sp. HH01
  ORGANISM  Janthinobacterium sp. HH01
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Janthinobacterium sp. HH01"
                     /db_xref="taxon:1198452"
     Protein         1..233
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=25934
     Region          1..>217
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mqiqiditkt lrsgartfal rarlasasqr ivvygpsgag ksmllkavag lmtpdhgrie
       61 vagrclydsv dgvnlspqrr rlaylfqdya lfphlnvrqn iafglrrgwr nplarvdgev
      121 vrywlqafel ehvaqqlphq lsggqrqrva laralapepa allldepfaa ldpalrqrmr
      181 aeldtlqrrl gipmilithd pddvsafgdh vlrmengsma dienlelver nea
//
LOCUS       WP_008448110             751 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Prevotella amnii].
ACCESSION   WP_008448110
VERSION     WP_008448110.1
KEYWORDS    RefSeq.
SOURCE      Prevotella amnii
  ORGANISM  Prevotella amnii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 751)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..751
                     /organism="Prevotella amnii"
                     /db_xref="taxon:419005"
     Protein         1..751
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=84661
     Region          41..751
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mhvsikmlsl lltltpfrgy aqqnesipkl pnksmtdslh qinevvvran qmlgsqfear
       61 nrtgsayyis pkelgkfdyt dinrmlksvp gvniyeedgf glrpnislrg tqaerserit
      121 lmedgilaap apyaapaayy fpnaarmyai evlkgssqvq ygpfttggai nlvstpipqd
      181 klircsmsag sfgslklqta igksfkytgf lieylryqar gfrhdtpder igfkrndvia
      241 kwmirtnred ginhrlelky gfanetsdet ylgltdqdfa vkpyfryaga qkdnlvtrhs
      301 qfsatyiikg mrswdittqa yynyffrnwy klnevrtgyt kaerrsigdv ladpitnkdy
      361 fdiltgkssy igealmlran hrvyhsrgvq ikgeyktmly ggyftgeigm ryhadsedry
      421 qqddgysmnn grmelflrgd pgsqanritt ahalsgyala kwakgmftft agvryedvkl
      481 lnrdytkadw rrtgmmriei pnsarafmpg iginckltpq lslfsgihkg fappsaslgq
      541 kaessinvea gvryankwlk gefigfnnny snmlgsdlaa qgglgtldqf nvgralvrgi
      601 emlvqcrplp atwkvqlpiq lsytftdtkm knsftsaswg hvlygdeipy ifrhalngqi
      661 gieskwadih fnmryngdmr tvpgqgkiaq rekipanfii datakihlik nidftmnivn
      721 ltnkvymvsr hpsgvraglp fgiyggvqwk l
//
LOCUS       WP_008447739             236 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Janthinobacterium sp. HH01].
ACCESSION   WP_008447739
VERSION     WP_008447739.1
KEYWORDS    RefSeq.
SOURCE      Janthinobacterium sp. HH01
  ORGANISM  Janthinobacterium sp. HH01
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Janthinobacterium sp. HH01"
                     /db_xref="taxon:1198452"
     Protein         1..236
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=25237
     Region          92..223
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(97..100,132,133,136,160,205,219)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mndiefevla taaykgerva arrlaarsnv seaaalhqvl vqvagaqglp qllaerdalr
       61 lrdeerrsar iaekarlleq raarmrpaad gwrgwfdgsa hpnpgqigig allcgpgger
      121 veisrragyg nsgeaeylal talleaagel gatglvvhgd sqvvvndvnl seqavaagrg
      181 akgleeyrqr vmalmvplga vslrwvprhr ngdadrlsqq aidrtlaehg fppsre
//
LOCUS       WP_008449392             141 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Janthinobacterium sp. HH01].
ACCESSION   WP_008449392
VERSION     WP_008449392.1
KEYWORDS    RefSeq.
SOURCE      Janthinobacterium sp. HH01
  ORGANISM  Janthinobacterium sp. HH01
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Janthinobacterium sp. HH01"
                     /db_xref="taxon:1198452"
     Protein         1..141
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14616
     Region          1..131
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mqraqkgftl ieimvsvaiv gilmavaipa ysdyvirgrl seaftglgga qpaaeqfwsn
       61 nrtyigfnga snfpsntanf tyalsaatas sytltatgig kmngfvytid qngthattgs
      121 ptgwgvsasc wvdhkggacs n
//
LOCUS       WP_008449970             416 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein
            [Janthinobacterium sp. HH01].
ACCESSION   WP_008449970
VERSION     WP_008449970.1
KEYWORDS    RefSeq.
SOURCE      Janthinobacterium sp. HH01
  ORGANISM  Janthinobacterium sp. HH01
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 416)
  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 416)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Janthinobacterium sp. HH01"
                     /db_xref="taxon:1198452"
     Protein         1..416
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47206
     Region          19..403
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mteliislaa aralhlaaqg llqprrrkar qadvvdairq mgvlqidtih vvarspylvl
       61 wsrlgdypqp wleqalaagq lfeywaheac fvpiedygly rhrmldpaam gwkysetwmr
      121 erraevdavl dhirlngptr ssdfertdgq sggwwswkpe krslevlfta galmiaerqn
      181 fqriydlaer vlpgwddsrm phmddtrrml vlkavkamgc aragwisdyf rtkpprldpe
      241 elvgqgallr awvddwddpv yvhpdhaall aaaaagtlap tlttilspfd pvvwdrrral
      301 elfgfdyrle cytpaekrry gyftlpilrr galvgrvdak ahrrggvfel kslvlepgar
      361 isdrfvrdia galqrlanwh ecpdiqivha apegfapllr aaldfntkda kemeaa
//
LOCUS       WP_008451024             168 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Janthinobacterium sp. HH01].
ACCESSION   WP_008451024
VERSION     WP_008451024.1
KEYWORDS    RefSeq.
SOURCE      Janthinobacterium sp. HH01
  ORGANISM  Janthinobacterium sp. HH01
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 168)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Janthinobacterium sp. HH01"
                     /db_xref="taxon:1198452"
     Protein         1..168
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17797
     Region          14..168
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mtftlsdtay gtdtpaakla mfddlrsqlt glvhgerdli antanfsslv fnsmpglnwa
       61 gfyflkgdel vlgpfqgkpa cirikkgrgv cgttvvegks ivvpdvhafp ghiacdvnsr
      121 selvvpvrga ageivgvfdl dsplpnrfdq tdadgiemlv kileatla
//
LOCUS       WP_008451574             379 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Oxalobacteraceae].
ACCESSION   WP_008451574
VERSION     WP_008451574.1
KEYWORDS    RefSeq.
SOURCE      Oxalobacteraceae
  ORGANISM  Oxalobacteraceae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales.
REFERENCE   1  (residues 1 to 379)
  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 379)
  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   3  (residues 1 to 379)
  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   4  (residues 1 to 379)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 379)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 379)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 379)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Oxalobacteraceae"
                     /db_xref="taxon:75682"
     Protein         1..379
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39905
     Region          27..365
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(103..105,126..127,176,230,254)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mlfktkfipl aialafagsa gaqevikigh vapvsgpsah lgkdnengak maveelnakg
       61 ikiggkpvkf vlvleddggd pkqgtavaqk lvdakvngvi ghlnsgttip askiyfdagi
      121 peispattqt kytqqgfnsa frvvandakl ggtlgayavn kmgvkkiavi ddrtsygqgv
      181 aeefvkgakk ampgvqivgk efttdkatdf nailttikak npdviffggm dsvggpllrq
      241 mkalgikaky mggdglctes lpklageaav pvvtcaeagg vppelqknmd dfharykkky
      301 nmdvqlyapy vydsvmtmaa amqqansaep akylpvlqki kyqgvtglie fdakgdikdg
      361 sltlynynng tktitsvik
//
LOCUS       WP_008452526             237 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Oxalobacteraceae].
ACCESSION   WP_008452526
VERSION     WP_008452526.1
KEYWORDS    RefSeq.
SOURCE      Oxalobacteraceae
  ORGANISM  Oxalobacteraceae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (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   3  (residues 1 to 237)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Oxalobacteraceae"
                     /db_xref="taxon:75682"
     Protein         1..237
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26183
     Region          44..235
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mssnppppse aktqeyefeq mnlqvggriq fithrtikpi qhfstligwv kdeymivkvp
       61 fengapialn dgdkltirvf sgvnvcsfsc vvqrvfprpl fyvhlsfpvs iqgtslraam
      121 rvkvdipaqv tspagttsvf lvnlsvsgal iesakklsed eaqvglsfyl iaqpgnrqvr
      181 inpnatirni nvvkpatsdk aevftygvqf idldpvhytm lqnltyeali adrqkiv
//
LOCUS       WP_008452528             155 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: pilin [Oxalobacteraceae].
ACCESSION   WP_008452528
VERSION     WP_008452528.1
KEYWORDS    RefSeq.
SOURCE      Oxalobacteraceae
  ORGANISM  Oxalobacteraceae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Oxalobacteraceae"
                     /db_xref="taxon:75682"
     Protein         1..155
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=15527
     Region          10..128
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mksmkmmkkq aqagftliel mivvaiigil aavaipaysd ytvkakmana qgaidsikta
       61 valcaqeggg dltgcnagak gvptftptke vsgatvtdgv ivetfatgvg kdidgktatf
      121 tptiaagaan vtwnvtttvt ntaasqaltk nnvtp
//
LOCUS       WP_008454000             162 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Enterobacteriaceae].
ACCESSION   WP_008454000
VERSION     WP_008454000.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 162)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..162
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17415
     Region          1..152
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mnkeqfyadl nrdfsalmag etsflatlan tsallferle gvnwagfyll eaqtlvlgpf
       61 qgkiacvrip vgkgvcgtav aagtiqrved vhafdghiac daasnseivl pltvdgqtig
      121 vldidsteyg rfseedemgl ktlisrlsdv lsgtdfkkff pr
//
LOCUS       WP_008454624             118 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein
            [Enterobacteriaceae].
ACCESSION   WP_008454624
VERSION     WP_008454624.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (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   2  (residues 1 to 118)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..118
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11848
     Region          45..117
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mtsgikafsl slvlagllgc apahaaaeka gsasvssaat qpkaasakta eqgeglvsin
       61 sapaeelaqk mngvglkkaq aivsyrdefg pfktldqlqe vpgigaslve rnlarikl
//
LOCUS       WP_008454130             365 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein
            [Enterobacteriaceae].
ACCESSION   WP_008454130
VERSION     WP_008454130.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
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   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   4  (residues 1 to 365)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..365
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=39503
     Region          1..294
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mitfnnvtkf yddgtvvvdg lnltapggki tvlvgpsgcg kttslrminr liepssgdil
       61 lngestsamd vvqlrrrigy viqnaglfph rniidniatt ailngmpkak araragelle
      121 vvglapqlak rypwqlsggq qqrvgvaral aadpefmlmd epfsavdpvv rdqlqeeflr
      181 iqkevsktii mvthdideam klgdlvavlk pggklgqmas pgellnapqs dfvadfigrd
      241 rgyrklsfyn sgpltsmqte ptaevgtpid marniavqrw llvtregkac gwfdthqqve
      301 avvpehinlg atffpqtgtl rqmldsalss pchravvige raevlgtlgl dhvldacksm
      361 areav
//
LOCUS       WP_008459121             309 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Enterobacteriaceae].
ACCESSION   WP_008459121
VERSION     WP_008459121.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 309)
  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 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   3  (residues 1 to 309)
  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   4  (residues 1 to 309)
  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 309)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..309
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33975
     Region          36..187
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          216..297
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqpterpsgr iidelhqrva rrypaggggv kelscalpwl sfirieqptl lnrgmlspsm
       61 cmvlqgskkm ligdnvteyg pgsyslaavd mpvsgqvtra seaepyygvr idldgkeiad
      121 limnmnvvlp dgngektgaw vaaaeeelqg aflrlvtlld spqhlhalap likqeilyrl
      181 viapagasfw kqalgwaqgk gvgeainwik qnyaeplvid elakrvgmsa sslhhrfkal
      241 timsplqyqk qlrllearrr llscegdvas vawkvgydsp sqfnreyrra fgasplqdid
      301 alrqqgtsf
//
LOCUS       WP_008460077             156 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Lactobacillus equicursoris].
ACCESSION   WP_008460077
VERSION     WP_008460077.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus equicursoris
  ORGANISM  Lactobacillus equicursoris
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 156)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Lactobacillus equicursoris"
                     /db_xref="taxon:420645"
     Protein         1..156
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16987
     Region          2..153
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 maaasqeeye lflkqaealv ygesdwiant anvsallyhq lknvnfagvy rfekgelilg
       61 pfqgqpacvh iqigkgvcgk aakdqatqiv envhdfpghi acdsasnsei vvpifnqqgd
      121 lwgvydfdst tfsnfdqldq eylekiagvv lgqaqn
//
LOCUS       WP_008463560             267 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Flavobacterium].
ACCESSION   WP_008463560
VERSION     WP_008463560.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium
  ORGANISM  Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 267)
  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 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   3  (residues 1 to 267)
  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   4  (residues 1 to 267)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Flavobacterium"
                     /db_xref="taxon:237"
     Protein         1..267
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31225
     Region          <115..265
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          194..266
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mdhisryltp eiklscyedk ffksdimfdd hmliwfisge tkiiqydasf lfkkgdifli
       61 prnqlatiin ypsngephkt vvmhlsverl kkfyqnielv kkpipenkiy sfnnhplles
      121 claslvpyfd lkshfsedla slkitealsi lraidknvdn vlanfdepgk idligfmern
      181 fmfnmplekl gyltgrslst fnrdfkkhfn ttpqkwlthk rlelayyqla ekkkkpidvy
      241 levgfenlsh fsyafkklyg ispkqli
//
LOCUS       WP_008463978             310 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Flavobacterium].
ACCESSION   WP_008463978
VERSION     WP_008463978.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium
  ORGANISM  Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 310)
  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 310)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Flavobacterium"
                     /db_xref="taxon:237"
     Protein         1..310
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36127
     Region          36..188
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          221..301
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mnnqrflvnp lqlsqekslk tlvenrtiyn lnncelnlfe tyestqkvpl kfndlvvtsm
       61 lrgkkimhlf ddpefvylpg etvivpsnve mkidfpeask nnptqclala idqdkiveil
      121 nflneqypke gtnmywqlny qnyffynnve maatinklik ecmstsvakd ifadltlkel
      181 liriiqtqtv ksidegkfld annpikevte yikqnlkenm slkslsekac msttsfyrff
      241 krelgmspie yilnekikca knllknptlq inevcylagf edanyfirlf kkyegitpkq
      301 yqllyinqrc
//
LOCUS       WP_008464216             352 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-oxoacyl-ACP synthase III family protein
            [Flavobacterium].
ACCESSION   WP_008464216
VERSION     WP_008464216.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium
  ORGANISM  Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 352)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Flavobacterium"
                     /db_xref="taxon:237"
     Protein         1..352
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38742
     Region          1..352
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mkikiigigs yipnlevknt dfdkhvflne dgtpfgypne vvikkfkgit gienrryaep
       61 qynasdlaff aaekaianaa idaetldyii iahnfgdvkp gttqsdilps latrvknklg
      121 iknpkcvayd iifgcpgwie gvlqanafik sgmakrvmvi gaetlsrvvd dhdrdsmiys
      181 dgagasilea stdeagllay esatyatdea nylffgksyn kdldpdtkyi kmygrkiyef
      241 alsnvpcamk scldksgiai devkkilihq anekmdeaii erfyklydkt apkdimpmsi
      301 hdlgnssvat vptlydlilq gkvegheink gdvlifasvg agmninafvy ry
//
LOCUS       WP_008464678             476 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Pseudoalteromonas sp. BSi20439].
ACCESSION   WP_008464678
VERSION     WP_008464678.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. BSi20439
  ORGANISM  Pseudoalteromonas sp. BSi20439
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 476)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Pseudoalteromonas sp. BSi20439"
                     /db_xref="taxon:420915"
     Protein         1..476
                     /product="amidohydrolase family protein"
                     /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=52356
     Region          26..459
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mkytlllpfs lllstlsfan ekqhvdllih hanvvdikna vvipnqtiai tdakiiargd
       61 daiklnyhat tqidaqgrfv mpglwdmhvh fgggdaliee nkqllplyla ygvttvrdaa
      121 adlspsvlsw reqitkgeli gptiytsgpk legkdsiwpg dlevettqem haaidkldam
      181 nvdfvkitds altpelylqa vkevkkrgyk isghipfsls vtdvssagld aiehmtyllk
      241 aaakneddis akvkagelsy rsalpivmdn idkdtamkky rllaknntav vptliggqvt
      301 ayidedshqq deflnylgkg lkdtyqwrvd rankdtpaqi karkqrfvqt aqllpwaqea
      361 gvpiiagtda gflnsyiypg lslhqelaif sdygltpqqi lhsatqagpt fldkaqqfgs
      421 levgkvadii ildsnplinv rntqslqgvi shnryydkaa lenlkaqakq fvssqq
//
LOCUS       WP_008466206             257 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Flavobacterium sp.
            F52].
ACCESSION   WP_008466206
VERSION     WP_008466206.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. F52
  ORGANISM  Flavobacterium sp. F52
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
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
REFERENCE   2  (residues 1 to 257)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Flavobacterium sp. F52"
                     /db_xref="taxon:1202532"
     Protein         1..257
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29522
     Region          6..109
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          <136..250
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mniidfipte qlrpfiktyr iiesedelvn rvlpstslai gfrckgyvny ikenqheklp
       61 vstisgirks vrlinyakdt atliiqfkea gakaffkepl helfeesvsl dnfipqqkta
      121 iieellveak tnnqkiavie qfllsrlhny kpdnlisaai tiiqskkgiv kikeladalf
      181 isqdafekrf rktigsspkq fcyvvriksi idhkqknqnl idlaidagyf dqphfnkdfk
      241 lftgqtpsef fnfpsfw
//
LOCUS       WP_008466835             129 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SPOR domain-containing protein [Flavobacterium].
ACCESSION   WP_008466835
VERSION     WP_008466835.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium
  ORGANISM  Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Flavobacterium"
                     /db_xref="taxon:237"
     Protein         1..129
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14614
     Region          57..117
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mrilspsksl lltittiala hninaqdqnl tlnqdpkfeq llnekrkint sintndtyri
       61 qifsgksdea kktlsdfkke nsdidgtiif stpnykvivg nfktrieaer nlaeikkryk
      121 svfllkpgk
//
LOCUS       WP_008467020             256 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Flavobacterium sp.
            F52].
ACCESSION   WP_008467020
VERSION     WP_008467020.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. F52
  ORGANISM  Flavobacterium sp. F52
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Flavobacterium sp. F52"
                     /db_xref="taxon:1202532"
     Protein         1..256
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30005
     Region          15..109
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          <142..254
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mnyqnivped sislfvkniw vfenedknih ttlpffadgc pglmfqqtdh glivkphdkk
       61 mpevflygqt ilpieleisg afliivfqly pyvlktffdi qpqsindncy yfddteedis
      121 wlkkqlelse svkdkieiis klllryfekk kenldfeirq gieyifqtkg qesirsiagk
      181 lkfnirtfer rfltetgltp kqfakiiqfq asldqltvkd yekhtdivyq ngfsdqshfi
      241 kvfkaftgkt pksfek
//
LOCUS       WP_008467433             401 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Pseudoalteromonas
            sp. BSi20439].
ACCESSION   WP_008467433
VERSION     WP_008467433.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. BSi20439
  ORGANISM  Pseudoalteromonas sp. BSi20439
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 401)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 401)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Pseudoalteromonas sp. BSi20439"
                     /db_xref="taxon:420915"
     Protein         1..401
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44336
     Region          2..397
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mtseayvfid gledspvicg ffklntqtgr gefnygksyl arsdafaldp lhlplqpgiv
       61 sysankgvfg vlsdagadsw grklilslhn tkpknelefl lagsgygvga lvfslsrsas
      121 khkankntla dlalldqakd dllankaisq eakkafefgq smggarpkts vkidqklyla
      181 kfnrqddlfn laraehgamc manelgirta ntriheteng dvllverfdv sddlpthhfl
      241 sansllqkpk vaindlatyy sygelaefir hhtgefaada telykrmvfn vfigntddhs
      301 rnhaflyhfa gqtwrmspay ditpinnskq hgiglgddgr yasidnllsq akrfglnkaq
      361 atkiiaeves ytrqwathfk rfanisdidi krlesvipsi s
//
LOCUS       WP_008470632             219 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Lactobacillus hominis].
ACCESSION   WP_008470632
VERSION     WP_008470632.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus hominis
  ORGANISM  Lactobacillus hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 219)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Lactobacillus hominis"
                     /db_xref="taxon:1203033"
     Protein         1..219
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24666
     Region          90..216
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(161..162,166,190..193,195)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mhknvkllgi ivviaiflcg favfqynsrs lnifeptktv kvksskkvpk kkekkfllyk
       61 dpsdiekegt wkkksekktq pnlatvkdlw irvslkgnrt yimsgnkpiy tmlstagrfn
      121 ksgksdtpvg tyhieaekgq affnqklgeg alnyvswhkh giylfhsvpt kkdksinvke
      181 anklgktaas hgcvrlsipd skwlmnnvpy gtkvvikky
//
LOCUS       WP_008470636             305 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Lactobacillus hominis].
ACCESSION   WP_008470636
VERSION     WP_008470636.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus hominis
  ORGANISM  Lactobacillus hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 305)
  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 305)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10097223
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Lactobacillus hominis"
                     /db_xref="taxon:1203033"
     Protein         1..305
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33079
     Region          7..286
                     /region_name="TBP_aldolase_IIB"
                     /note="Tagatose-1,6-bisphosphate (TBP) aldolase and
                     related Type B Class II aldolases. TBP aldolase is a
                     tetrameric class II aldolase that catalyzes the reversible
                     condensation of dihydroxyacetone phosphate with
                     glyceraldehyde 3-phsophate to produce tagatose 1; cd00947"
                     /db_xref="CDD:238477"
     Site            order(28..30,33,53,56..58,63,67,70..71,232..233,235..236,
                     239,243,252)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238477"
     Site            order(86..87,176..178,180,207..208,210,229,231..232)
                     /site_type="active"
                     /db_xref="CDD:238477"
     Site            order(87,177,207)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238477"
     Site            order(176,178,180,208,210)
                     /site_type="other"
                     /note="Na+ binding site [ion binding]"
                     /db_xref="CDD:238477"
ORIGIN      
        1 maylvngndi fkaarenhya vgayntnnle wtrallrgak etrtplliqv stgaakymgg
       61 yktvkdlvln emdnmdidvp vilnldhgdy esakecialg yssvmfdghn lptdenlakt
      121 keivklaher gisveaeigk igenqgadgg elasvedakt fvaagvdkla cgignihgvy
      181 pegwkglnfd rlkeiadavp geplvlhggs gipqdqieka iqlgiakini ntefqlafqa
      241 atrkyiedkm dldkgnkgyd prkllragtd aitdsmkemi swmgtapids kessvkfdea
      301 slnee
//
LOCUS       WP_008470974             240 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Lactobacillus hominis].
ACCESSION   WP_008470974
VERSION     WP_008470974.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus hominis
  ORGANISM  Lactobacillus hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
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   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 240)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Lactobacillus hominis"
                     /db_xref="taxon:1203033"
     Protein         1..240
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=27867
     Region          19..73
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mqeqpsyysv ltanvrydkk lkahekvlfs eitalankng yctatnsyfa nlydksktti
       61 snwinhlker gylkifiekd gkqiisrkly pvaepvkeke dtpikekfnr yskkakegik
      121 enfkppiken fkenitsnnn tsinreikgd qkiiinwsli vdnlldyyfe qaqqfrvdvs
      181 kvtnhertll tqavrgkplt alykavddti lrepdypigy likciknidp ittriyqnak
//
LOCUS       WP_008471582             397 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Lactobacillus hominis].
ACCESSION   WP_008471582
VERSION     WP_008471582.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus hominis
  ORGANISM  Lactobacillus hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 397)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Lactobacillus hominis"
                     /db_xref="taxon:1203033"
     Protein         1..397
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=45073
     Region          119..236
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          264..395
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(346..347,350,368..371,373)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mnqktnnryt nlliavaaiv viilggflif qhhnnaklaa qekfnkthfn qnvtiydvnv
       61 gkltknkayi kvnknaknra tlekdkisfs ktdkeiiskk eiqkyfdeqh tkydsnkkyn
      121 fenkdlitae nklnaiknrs vtyhidgksy vfkrdkllpk vsyyegqyhf enveplkaki
      181 esinkevttf hksypfklpd gktitvknes ygwaintkhl ipavekaiid gksevqgkny
      241 iyglgfstyg tgygmsnhgi gdtyivvslk qqkawfykng krvlvlddvv tgtaaknprt
      301 qtsdatptgv wyieykqsps vlrgsnddgs syaspvkywm pftisgcgfh daswrtdwsk
      361 taylkggshg cvnvkpseik kvwdvveeme pviiydk
//
LOCUS       WP_008475236             394 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Nitrolancea hollandica].
ACCESSION   WP_008475236
VERSION     WP_008475236.1
KEYWORDS    RefSeq.
SOURCE      Nitrolancea hollandica
  ORGANISM  Nitrolancea hollandica
            Bacteria; Pseudomonadati; Thermomicrobiota; Thermomicrobia;
            Sphaerobacterales; Sphaerobacterineae; Sphaerobacteraceae;
            Nitrolancea.
REFERENCE   1  (residues 1 to 394)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Nitrolancea hollandica"
                     /db_xref="taxon:1206749"
     Protein         1..394
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=43773
     Region          273..393
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(349..350,353,366..369,371)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 marrtllvlt lllafiamip gpaladeggn pasvyfpqtg hklslgfldf wrlnggvtvf
       61 gypitdemad pqtgqtvqyf eravfeyhae apedqriqlr aldpsdring litfnesqrr
      121 yqhlasfafa gvplsqpfar idtapdtndr iyfpetghtv amgfqdfwer hggadifgnp
      181 tteeymdpas gysvqyfera ifewhtegpg vphvelrnvg traaaragin tapvpqaeni
      241 ptydpnlwnd sgpanpadvt tplpgapsga akwievdlsq qyirawehkt lvfgqyvstg
      301 laqhptptgy frifaklpfd dmtngpaapa ddfydlkdvp nvmyfetggy aihgtywhtn
      361 fgrpqshgcv nmtrsgsawm fnwapnrttv wvhd
//
LOCUS       WP_008476354             880 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Nitrolancea hollandica].
ACCESSION   WP_008476354
VERSION     WP_008476354.1
KEYWORDS    RefSeq.
SOURCE      Nitrolancea hollandica
  ORGANISM  Nitrolancea hollandica
            Bacteria; Pseudomonadati; Thermomicrobiota; Thermomicrobia;
            Sphaerobacterales; Sphaerobacterineae; Sphaerobacteraceae;
            Nitrolancea.
REFERENCE   1  (residues 1 to 880)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..880
                     /organism="Nitrolancea hollandica"
                     /db_xref="taxon:1206749"
     Protein         1..880
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=98170
     Region          135..631
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mpkknpapak vesirhkdkr pnipteelrd fvaddeaapk tmlyprdpsl dpqlvwkgkd
       61 eqdredlsvp vvpiyiqeki hpqaiiddll dhaarpaggr iaeeavayqa elfadfnggp
      121 hdfadkidfy nheqnwtnrm ilgdsllvmt slaekeglkg kvqtiyidpp ygikfgsnwq
      181 vstrkrdvkd gkaedatrqp eqirafrdtw klgihsylay lrdrltvard lltetgsifv
      241 qigdenvhlv rcvldevfgs enfvsqitfk ktsgagspmv stlvlpgttd fiiwyakdfe
      301 rlkyrqlyap kpdatgqyvw adngvrrwrp saaehlaedv rwfrpsplts estgsggttv
      361 fpvtwksdvy tppkggwktn rsgmnrlisa drliavgktl syvryvddfp avpytslwed
      421 tqasgfgdpk lyvvqtnskv iercllmttd pgdlvldptc gsgttayvae qwgrrwitcd
      481 tsrvalalar trlmaakfpy ylladspegi kketeltgkt ppgyktggdi rkgfvykrvp
      541 hitlksiann pdiregmtre eidaaiarha dtetlfdqpy tdnkrvrvtg pfsveslsph
      601 rvlstaddnl dgtvseqeak keqdfatmil dnlkkagvqn trkaerlkfd rldpyagtwi
      661 qaageytgae gkirrvavsi gpehgtvgpd qvkeaakeav qgigfdlliv cgfafdphvg
      721 eevtrygrlt vlpakmnpdl amgdellkkt gagnlfmvfg epdieikkqh dgqivveing
      781 vdvydpttgq irgsstddia cwfidtdyng esffvrhayf tgadepydkl kralradide
      841 dawrglyatv srpfdppstg kiavkvinhy gdevltvypv
//
LOCUS       WP_008477403             139 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Nitrolancea hollandica].
ACCESSION   WP_008477403
VERSION     WP_008477403.1
KEYWORDS    RefSeq.
SOURCE      Nitrolancea hollandica
  ORGANISM  Nitrolancea hollandica
            Bacteria; Pseudomonadati; Thermomicrobiota; Thermomicrobia;
            Sphaerobacterales; Sphaerobacterineae; Sphaerobacteraceae;
            Nitrolancea.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 139)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Nitrolancea hollandica"
                     /db_xref="taxon:1206749"
     Protein         1..139
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=15186
     Region          10..130
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(15..18,50..52,55,87,127)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mgisegsadl elvfdggalg npgagygsfq lrdregfcei srldfgdnvt nnqaeyrtli
       61 agleaalgha gslgwhprtl rvrvrtdsql vveqvlgrwk vrhpnlqpls trarellarf
      121 gstdiawhpr vesvrilgh
//
LOCUS       WP_008477488             101 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Nitrolancea hollandica].
ACCESSION   WP_008477488
VERSION     WP_008477488.1
KEYWORDS    RefSeq.
SOURCE      Nitrolancea hollandica
  ORGANISM  Nitrolancea hollandica
            Bacteria; Pseudomonadati; Thermomicrobiota; Thermomicrobia;
            Sphaerobacterales; Sphaerobacterineae; Sphaerobacteraceae;
            Nitrolancea.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Nitrolancea hollandica"
                     /db_xref="taxon:1206749"
     Protein         1..101
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11581
     Region          7..98
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mtgtvlkseq lrsllrafke qhteayhlra lgyfgsyarn eatpdsdidv vfvtdrpdlf
       61 rtamlkqdle afldhpvdvv rlrdtmnprl kariereatf v
//
LOCUS       WP_008477810             250 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Nitrolancea
            hollandica].
ACCESSION   WP_008477810
VERSION     WP_008477810.1
KEYWORDS    RefSeq.
SOURCE      Nitrolancea hollandica
  ORGANISM  Nitrolancea hollandica
            Bacteria; Pseudomonadati; Thermomicrobiota; Thermomicrobia;
            Sphaerobacterales; Sphaerobacterineae; Sphaerobacteraceae;
            Nitrolancea.
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   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 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
REFERENCE   4  (residues 1 to 250)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Nitrolancea hollandica"
                     /db_xref="taxon:1206749"
     Protein         1..250
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26183
     Region          1..69
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          181..241
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 msefgellrh arayrgvtlg daeratrinr nhlaalekee fselppliya rgivrtyaey
       61 lgldpiavls lfeeihgqks ggfqvvpavk plhipshwap nfaiiafmva msavifiwmy
      121 safyapadav pvvptvaanp atpgsggpat ladgaiaqgg gvamapsgsp sdasgtvhtf
      181 siealssvwv easidgqsql attlddgetk sfkgrqlhvs tgnasnvrvl vdgvdqgplg
      241 pswnasrsfp
//
LOCUS       WP_008478529             128 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Nitrolancea hollandica].
ACCESSION   WP_008478529
VERSION     WP_008478529.1
KEYWORDS    RefSeq.
SOURCE      Nitrolancea hollandica
  ORGANISM  Nitrolancea hollandica
            Bacteria; Pseudomonadati; Thermomicrobiota; Thermomicrobia;
            Sphaerobacterales; Sphaerobacterineae; Sphaerobacteraceae;
            Nitrolancea.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Nitrolancea hollandica"
                     /db_xref="taxon:1206749"
     Protein         1..128
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=13874
     Region          33..>84
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mttsvgwgfg ssgvnpsevt haqqeetlgr ihrgmavynv eghrigsvgg vlrapgdraf
       61 avvvrtgwfg lgkelyiplq yvnvwgnqvs lsvdrhvihr mgwdkrpayl ekpvteptve
      121 ehgapaka
//
LOCUS       WP_008475660              92 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Nitrolancea hollandica].
ACCESSION   WP_008475660
VERSION     WP_008475660.1
KEYWORDS    RefSeq.
SOURCE      Nitrolancea hollandica
  ORGANISM  Nitrolancea hollandica
            Bacteria; Pseudomonadati; Thermomicrobiota; Thermomicrobia;
            Sphaerobacterales; Sphaerobacterineae; Sphaerobacteraceae;
            Nitrolancea.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Nitrolancea hollandica"
                     /db_xref="taxon:1206749"
     Protein         1..92
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=10223
     Region          9..82
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mswnpspdfd ydqlrnldvy gakgnkigsi dqvltdttth rhyllvkagp lglgtedyyi
       61 petaidmvgq drvvidkted qlkssgwtkp pr
//
LOCUS       WP_008479087             389 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Nitrolancea hollandica].
ACCESSION   WP_008479087
VERSION     WP_008479087.1
KEYWORDS    RefSeq.
SOURCE      Nitrolancea hollandica
  ORGANISM  Nitrolancea hollandica
            Bacteria; Pseudomonadati; Thermomicrobiota; Thermomicrobia;
            Sphaerobacterales; Sphaerobacterineae; Sphaerobacteraceae;
            Nitrolancea.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 389)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Nitrolancea hollandica"
                     /db_xref="taxon:1206749"
     Protein         1..389
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=41412
     Region          19..388
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mvarvddlgg ggviprryia alnagssslk lgvfdweteq qlaeesitwg ddggggirnh
       61 adaarqllsa wnpesigaig hrvvhggarf rqavridaev kqaiadlapl aplhnpaala
      121 vidaaehmlp lvpqvavfdt afhrtmppss ylypvpfqwy tewgiqrfgf hglshaycsl
      181 rasellkrpv dglklvtchl gsgcslaave sgrsvattmg ftpleglmmg trsgsvdpgm
      241 llylltqrhl ntgdlehtly ydsglkgvsg vspdirevia akraglrqag lafdlyttri
      301 regigamaaa msgldglvft agvgegsadv reavcrplew lgvaldaqan avaspdtdva
      361 tagsrvrilv vhtreelmva ketrraler
//
LOCUS       WP_008479471             439 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Nitrolancea hollandica].
ACCESSION   WP_008479471
VERSION     WP_008479471.1
KEYWORDS    RefSeq.
SOURCE      Nitrolancea hollandica
  ORGANISM  Nitrolancea hollandica
            Bacteria; Pseudomonadati; Thermomicrobiota; Thermomicrobia;
            Sphaerobacterales; Sphaerobacterineae; Sphaerobacteraceae;
            Nitrolancea.
REFERENCE   1  (residues 1 to 439)
  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 439)
  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   3  (residues 1 to 439)
  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   4  (residues 1 to 439)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 439)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 439)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 439)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Nitrolancea hollandica"
                     /db_xref="taxon:1206749"
     Protein         1..439
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46108
     Region          65..423
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(143..145,166..167,231,284,310)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mgtnrfkrfl afiaitivvv pflaacgggt stpapggtas prpsasspvs saasptgnts
       61 kgtikivssw pltgqaekvg tdsvkavqma iadhggaagg ykiefqpldd ataakgawds
      121 akesenanka iadpdvmiyl gtfnsgaaki sipilnqagl amiseantwp gltkkiegmt
      181 eanepdvyyp agkrnyvrvv ptddlqgsla aqwakdlgak kvyilddtel yghgialifa
      241 daakklglev iggpegidkk apdyralmtn irskspdliy fggitennag klvqdmraag
      301 mtdvkfmgpd giftegfida agaaaegaya tfgglpasql kgkgadwyqr fkqqynedpe
      361 ayavyayeaa svalnaidra gkkdrqaile avrntkdfng llgtwsftdt gdttlktmsg
      421 nqvkggkwqf vktlelagq
//
LOCUS       WP_008481869              96 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Nitrolancea hollandica].
ACCESSION   WP_008481869
VERSION     WP_008481869.1
KEYWORDS    RefSeq.
SOURCE      Nitrolancea hollandica
  ORGANISM  Nitrolancea hollandica
            Bacteria; Pseudomonadati; Thermomicrobiota; Thermomicrobia;
            Sphaerobacterales; Sphaerobacterineae; Sphaerobacteraceae;
            Nitrolancea.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Nitrolancea hollandica"
                     /db_xref="taxon:1206749"
     Protein         1..96
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10623
     Region          1..94
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mrrndvlrsl gehrdelahl gvgsialfgs vargearpes didllvdfnq pvglfelvdl
       61 knyleellgc svdlvtrdsl krqlrerilk dvipaa
//
LOCUS       WP_008482904             636 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Gallaecimonas xiamenensis].
ACCESSION   WP_008482904
VERSION     WP_008482904.1
KEYWORDS    RefSeq.
SOURCE      Gallaecimonas xiamenensis
  ORGANISM  Gallaecimonas xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Gallaecimonadaceae; Gallaecimonas.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Gallaecimonas xiamenensis"
                     /db_xref="taxon:1207039"
     Protein         1..636
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=69273
     Region          5..636
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mgfsrtlial allpvavqaa qsadehllvl grqtqavdsl paavtlisqa diensgatsl
       61 esllrgragi qvansgsgpv lslrgfapdq sganvlvlid grrlnsqsla gpalaslrlg
      121 niarievlqg sagvlygdqa vggviniitk ggsdggqvsa slgsfdhqal ganlskgfan
      181 glyvdsnlaw dkadnyrdhs qsrtasvqgr lgyrtqgrhl yaelgwdqdd rdqpgpltfs
      241 qtdrrfsrpe fakdfinqis qvarlgleqq lddnwqllvd gsasrrerdy nqsymdwavd
      301 npsetterln risprlkgql gelavlagid yehgnyddds lgahnsrdsq slyangqwqh
      361 qaltlsaglr ytdvdddliy astyaqgvsi srdattwsla gqyqldqagr lfaridrnvr
      421 fakldeqgyt pagilgldpq kglsvelgwa geqlslsafr ldlkdeivfd anapapeggl
      481 faganvnadq srrygvnlag hqdfgpltlg vdyqwldaqf tkgasdghkv pwvsrhsgll
      541 ygdlvlskal sarveyqyrg sqyllsdnln qgdkvgsygl wnlagiwqqg pwhfvlrvdn
      601 lfdkrfadya vynawgedsw ypgkgrelnl tarynf
//
LOCUS       WP_008485325             657 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Gallaecimonas xiamenensis].
ACCESSION   WP_008485325
VERSION     WP_008485325.1
KEYWORDS    RefSeq.
SOURCE      Gallaecimonas xiamenensis
  ORGANISM  Gallaecimonas xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Gallaecimonadaceae; Gallaecimonas.
REFERENCE   1  (residues 1 to 657)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 657)
  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   3  (residues 1 to 657)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..657
                     /organism="Gallaecimonas xiamenensis"
                     /db_xref="taxon:1207039"
     Protein         1..657
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=70285
     Region          4..653
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 meldmdrfrq iflqecaenl avlesdllal ergsgdedci hrvfraahsi kggagtfglk
       61 amsgfthhle tlldelrsgk rsidanlvsl mlkatdviaq mrgdaeggge gqspeadavr
      121 gqleaalgma aappeqakas aaqgsgdwql vmqphgdila sgneplrllr elaalgfkvi
      181 svslgalhqg nyqpehcylg wtlagpgqip eadireifew vedecdisls rqagpaeaap
      241 qpqaeakaqv aeakaapeqs iridirkida linlvgelvi tqsmlasleg lggeaieerf
      301 srglsllksn tkalqesvlg irmlpisfaf nrfprlvrdl akqlgkdvdl klvgeqteld
      361 ktvlerigdp lvhmvrnald hgieqpgqrr qagknpkgtl tlsacheggn vvidirddga
      421 glnkeklwqk acekglpltq ehkleelsdg qvydlifapg fstaaavsdl sgrgvgmdvv
      481 krniselggs veiqsqlgrg tlfrirlplt maildgqlva vgdelfvipl iniveslkve
      541 pdcllkaggg vvfyqlrqem lpviwlaell gtqgepgplp llcvveaagr klglvvdall
      601 aqqqvviksl eqnfrrlpgi sgatilgdgq vclildvpgl vsrqvgrdsd saavsaa
//
LOCUS       WP_008485364              98 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Gallaecimonas xiamenensis].
ACCESSION   WP_008485364
VERSION     WP_008485364.1
KEYWORDS    RefSeq.
SOURCE      Gallaecimonas xiamenensis
  ORGANISM  Gallaecimonas xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Gallaecimonadaceae; Gallaecimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Gallaecimonas xiamenensis"
                     /db_xref="taxon:1207039"
     Protein         1..98
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10705
     Region          1..97
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(23,50..51,53,78)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(23..24,33,35..36,38,41..42,44,50,55,63)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mstnparlyt lvalipegqv atygqlasil gwnprlvgry mgqcppelpw hrvvnaqgac
       61 svrdsqghli qhqrllaegv pltrsgrvnl rralwpgl
//
LOCUS       WP_008486386             124 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Gallaecimonas xiamenensis].
ACCESSION   WP_008486386
VERSION     WP_008486386.1
KEYWORDS    RefSeq.
SOURCE      Gallaecimonas xiamenensis
  ORGANISM  Gallaecimonas xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Gallaecimonadaceae; Gallaecimonas.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Gallaecimonas xiamenensis"
                     /db_xref="taxon:1207039"
     Protein         1..124
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=13403
     Region          1..122
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkrmlgvtll elmiviaila ilagiaypsy qryvleanrt naqgelaklq laqetyrvkn
       61 nsfatlaqlg gltsdhytys isnitassyt lqavakgsqs ndtgcttltl dhndnktpas
      121 cwkn
//
LOCUS       WP_008486450             212 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Gallaecimonas xiamenensis].
ACCESSION   WP_008486450
VERSION     WP_008486450.1
KEYWORDS    RefSeq.
SOURCE      Gallaecimonas xiamenensis
  ORGANISM  Gallaecimonas xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Gallaecimonadaceae; Gallaecimonas.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Gallaecimonas xiamenensis"
                     /db_xref="taxon:1207039"
     Protein         1..212
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22842
     Region          62..164
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 mnkkaclylg laalalfggy kgatrldpnp ahqvgevldn ldgvavyyng gvnhvlernl
       61 aadgynlglk yqcvefvkry yyqqlghkmp dsyghakdff dkalasgsln pkrglyqyrn
      121 gegelpafgd ilvfdaslln pyghvaivsn ldlaaghlei iqqnpgpfsg sraafsiave
      181 dgkarvassr llgwlrkadp avsqssysev al
//
LOCUS       WP_008487477             154 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Idiomarina xiamenensis].
ACCESSION   WP_008487477
VERSION     WP_008487477.1
KEYWORDS    RefSeq.
SOURCE      Idiomarina xiamenensis
  ORGANISM  Idiomarina xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Idiomarina.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 154)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Idiomarina xiamenensis"
                     /db_xref="taxon:1207041"
     Protein         1..154
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16529
     Region          1..148
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mstdtlyrdm lnqikalcad epdlianlan isaliydqld dinwagfylt rapqmlvlgp
       61 fqgkvacvri pfsqgvcgaa artqeaqlva dvhqfsghia cdsasnsevv ipivvdgntv
      121 avldidspsv nrfdkadqqg lqaigdylqs ldws
//
LOCUS       WP_008487520             322 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Idiomarina xiamenensis].
ACCESSION   WP_008487520
VERSION     WP_008487520.1
KEYWORDS    RefSeq.
SOURCE      Idiomarina xiamenensis
  ORGANISM  Idiomarina xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Idiomarina.
REFERENCE   1  (residues 1 to 322)
  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 322)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 322)
  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   4  (residues 1 to 322)
  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 322)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Idiomarina xiamenensis"
                     /db_xref="taxon:1207041"
     Protein         1..322
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35961
     Region          43..186
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          223..304
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mstiqlgasa kpsltptdls trmdrlvhrl lpllvedgmt etaiddislm rrdqpsapqa
       61 ivyrpavcfm lqgakelqvg sssvtyarln yllipvmipv sgrvslaspa qpyvglsfnf
      121 diaelhelml llgdripaak tnhsglsvgt mdadmmqlle rlvellekpd daavllplik
      181 remmyrlllg elggqlrdfh lidsqagria qviemlkqrf heplrvrdla davhlsesal
      241 yqafksvtam spiqfqkklr ldearrimlf egmdvssacy qvgyespsqf sreysrlfgr
      301 spkadidyfr qlpdttlnqm vs
//
LOCUS       WP_008487626             245 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Idiomarina xiamenensis].
ACCESSION   WP_008487626
VERSION     WP_008487626.1
KEYWORDS    RefSeq.
SOURCE      Idiomarina xiamenensis
  ORGANISM  Idiomarina xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Idiomarina.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 245)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Idiomarina xiamenensis"
                     /db_xref="taxon:1207041"
     Protein         1..245
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=27042
     Region          22..234
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mpgcgpctcq qrlpfdikma mqaivdlnag qifahealvr gsqgegagfv lsqvdddnry
       61 sfdqrcrvka ietaaqlqlp arlsinfmpn aiyepetcla ttlkaagryq fphqriifev
      121 teqesvvdra flidvfqayr ehgfmtaidd fgagyaglgl ladfqpdiik idmkllrdih
      181 lhnakqaivr gicqianelg iaiiaegies qeelqfvrel gvylvqgylf hkpqlgrlda
      241 pagls
//
LOCUS       WP_008489020             283 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Idiomarina xiamenensis].
ACCESSION   WP_008489020
VERSION     WP_008489020.1
KEYWORDS    RefSeq.
SOURCE      Idiomarina xiamenensis
  ORGANISM  Idiomarina xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Idiomarina.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 283)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Idiomarina xiamenensis"
                     /db_xref="taxon:1207041"
     Protein         1..283
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=33021
     Region          10..250
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mtyrqtllyi lsamnkqdig vrfqpivstf qnqtiwsyea lmwwpdaidk gyhteqiiel
       61 ieahqltfdf dlyifecvlk qlthwqltgq stprisinlc pdsiansnfi paahrllaqy
      121 aniqpqwlsf eltervswrn yqimqhnlta vknlgirigi ddfmtgyanf stliddtvdy
      181 lkidrsviaq iensentrif lsgflelakr lgkavvaegv ennqqfnflq qcgyrkyqgy
      241 yfakpllade vwefthfwdq qdhdlsllnq vhlhsnvmqg yln
//
LOCUS       WP_008489405             778 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Idiomarina xiamenensis].
ACCESSION   WP_008489405
VERSION     WP_008489405.1
KEYWORDS    RefSeq.
SOURCE      Idiomarina xiamenensis
  ORGANISM  Idiomarina xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Idiomarina.
REFERENCE   1  (residues 1 to 778)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 778)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 778)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Idiomarina xiamenensis"
                     /db_xref="taxon:1207041"
     Protein         1..778
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=85357
     Region          20..773
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mktllkvvla llvlsaavvy wllhgslaql dgqltvtgls qsvsvdrdaq givtiraasr
       61 ldaahalgvv haqeryfqmd llrraaagel sallgsstlt hdrnvrihrf raraeqafqh
      121 lpvnhqailq ayaegvnqgl nalakrpfey fllgqtpqpw qtsdsllviy smylqlqqsd
      181 gayergltql yqqyptavad fltplgsrwd aaidgsqlaq rgdtaaipel prqagggaga
      241 aafapvqfpg snnwavagal tpyragmlan dmhlgirvpn twfhtiietr spalrlagvs
      301 lpgtpgiivg snghiawgft nsygdwsdvi alktrhdnse yltpsgwkpi ltrqeaieva
      361 nadaetitir etqwgpilpa ektatpnkly ayrwvahdla gintrifdlt qaatvndalq
      421 vaagagmpaq nlvvsdsngd igwtimgaip rrqgfsgrlv sdwsdgsqsw qgyygetehp
      481 riiqprsgrl wtansrvvag eafskigngg halgaraqqi rdllaqqeqf tetdmlaiqr
      541 naearflqrw qaylvslleq qeslseqqqq llqlvnnwqa easvdsqgya lvklfrqqtl
      601 kllfadfddn iiravrsile vpawqilqqq prswlpngva dwhqfqqrti tatlaqvdte
      661 tladyrwghv nqahfahpls aalgplsrwl nmpqqalpgd tfmpfvqgsd fgaserlvva
      721 pgheqngils mptgqsghpl spyyrshhqd wlegratpll ggdsqhqlrl vpgngdaq
//
LOCUS       WP_008492080             500 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [unclassified Acidocella].
ACCESSION   WP_008492080
VERSION     WP_008492080.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidocella
  ORGANISM  unclassified Acidocella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidocella.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="unclassified Acidocella"
                     /db_xref="taxon:2648610"
     Protein         1..500
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=52676
     Region          7..500
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 msarkekilr lhprdnigia ladlrlgeel atqpvprghk ialdpikqge vvikygqiig
       61 satadipvgs hvhthnlgma qdrnqagqpp sppaiahagt dtfngyvrpd grvgtrnyvg
      121 vmttvncsgs varfiaedar gcglldefth idgivpithn tgcgmagrge gydmllrtla
      181 gylrhpnfga illvglgcev mqlsaltdmp nlrdptsfrf ltiqqsggtr atieaarpil
      241 relaglanta rrqpvsaahl tiglqcggsd glsgitanpa lgiasdllva qggtsilset
      301 peiygaehll lnratspdia ealksrlaww sdycarngge mdnnpspgnk rgglttilek
      361 slgavakags aplsgvyrya epittkgfvf mdspgydpcs vtgqvasgan lilfttgrgs
      421 vsgykpvpgi klstnndlwa rmsedidinc gdiidgvple qkgaeiyqml lsiasgqktk
      481 senlgfglve fvpwqigatm
//
LOCUS       WP_008492812             275 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Acidocella].
ACCESSION   WP_008492812
VERSION     WP_008492812.1
KEYWORDS    RefSeq.
SOURCE      Acidocella
  ORGANISM  Acidocella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Acidocella"
                     /db_xref="taxon:50709"
     Protein         1..275
                     /product="formate/nitrite transporter family protein"
                     /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=28396
     Region          2..260
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mdwlnppala gamleagtkk anlpaktill tgilsgmflg ftttlfvsal vatgnivvsa
       61 lffpvgfill vllglelftg naallpyaqm ggrisggqvv sglvlvyign ligsviyall
      121 faaidtkfft dapspigaki iaiatlkvvp ymsagaagwg tallkgvicn wmvslgavma
      181 lvtrstigki famylpimaf vaqgfehcvv nmfvipcgim lgakvsvaqw liwneipvti
      241 gniigaviit aaglylsfgr satpvaeqgs ipvqg
//
LOCUS       WP_008492872             348 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Acidocella sp. MX-AZ02].
ACCESSION   WP_008492872
VERSION     WP_008492872.1
KEYWORDS    RefSeq.
SOURCE      Acidocella sp. MX-AZ02
  ORGANISM  Acidocella sp. MX-AZ02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidocella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Acidocella sp. MX-AZ02"
                     /db_xref="taxon:1214225"
     Protein         1..348
                     /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=38220
     Region          8..279
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mnaeisarrq didmakglai tlvvfghiva rqdpaqvhwy eplrraiyaf hmpfflylsg
       61 fvaassgflv rgragfgaal qeraqrlllp ffalgllila gklvaarfia vdntppslta
      121 gltglfwhte aspalsvwyl fvlfvlvlat rwaldgqier lanllalall aywlpvpgyl
      181 yadrltgyap ffllgalagf araswerclt rlwrpallcl maglsvvalc gqdwpqpfym
      241 lplgvismpa lhgamralra qraraallvl grasfaiylg nticiglakg mmlrlgswng
      301 phfllfapal maaglfgpil craawlliqd hgwpplpprm rhshehhs
//
LOCUS       WP_008493489             282 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Acidocella sp. MX-AZ02].
ACCESSION   WP_008493489
VERSION     WP_008493489.1
KEYWORDS    RefSeq.
SOURCE      Acidocella sp. MX-AZ02
  ORGANISM  Acidocella sp. MX-AZ02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidocella.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 282)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Acidocella sp. MX-AZ02"
                     /db_xref="taxon:1214225"
     Protein         1..282
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=30913
     Region          41..274
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mtatrqesdh aaeaelraer elkqhnarhr iterrrviqk lrqalatnrl alhfqpiial
       61 asgracaaev qlrldhsrrg lipaghllpl aeqsdmiidl gawmlrqvcv qaaqmprdft
      121 lslalclrhl rsgqlvkhvl ealqhaqaep cqlellitee mlldanedtv falralqglg
      181 lrlaldhfgt gyaslaplrk lnfstlrldr slvrdieadg aagivqaave aghalgcqvl
      241 adgvesqtqy dllrrlradl aqgsffsaam dgaalgslla rr
//
LOCUS       WP_008493705             418 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Acidocella sp. MX-AZ02].
ACCESSION   WP_008493705
VERSION     WP_008493705.1
KEYWORDS    RefSeq.
SOURCE      Acidocella sp. MX-AZ02
  ORGANISM  Acidocella sp. MX-AZ02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidocella.
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
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 418)
  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   5  (residues 1 to 418)
  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   6  (residues 1 to 418)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 418)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 418)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Acidocella sp. MX-AZ02"
                     /db_xref="taxon:1214225"
     Protein         1..418
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44007
     Region          22..62
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          81..388
                     /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 maapsrqgsn amqirhyner vvleairrlg qaskaeiarg anltpqavag ivdalhkagy
       61 lvqagkrtgq igqpsvlyea nperafsigl hvgrraiqav lvdlsgkvlr qveheypypa
      121 petvpnlale aiatleasla prqrarllgv gvtmpyfldn wqeelgfpaa laqgwrdfnf
      181 prflmaqtrr evffendasa aataqlvrgq gmaernfiyl ylgtiigggl vlggnletgp
      241 ngnaaafntf pvsastlpga aapagpfell qhrasiyvll rhlrangvai drigdlaglg
      301 eaaqpwlgqw eddcaaalaq aiigalsvvd veaividgil ppaplariva lvdaalarlv
      361 psglmmpklr qgglgpdgpa igaallpfya hfapnnevla rkfsaeakpl lgsgpaaa
//
LOCUS       WP_008495454             328 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Acidocella sp. MX-AZ02].
ACCESSION   WP_008495454
VERSION     WP_008495454.1
KEYWORDS    RefSeq.
SOURCE      Acidocella sp. MX-AZ02
  ORGANISM  Acidocella sp. MX-AZ02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidocella.
REFERENCE   1  (residues 1 to 328)
  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 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   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 328)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Acidocella sp. MX-AZ02"
                     /db_xref="taxon:1214225"
     Protein         1..328
                     /product="CmpA/NrtA family 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=33832
     Region          5..243
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mndvirlgll rlcdaapvil aaqeglfaaa glnvalsvep swaniadkla fnlldgavml
       61 aplalacagg lrgakidlav pmslssngna itlaasmqsa faaggiaava aakrprlavv
      121 hgfsshdlll rhwlagqgvm perdvditvl ppaemvgala agaidgfcag apwglvaaka
      181 glgftaalsr diwpdhpekc lalradfata eparleallg vllhaqrlca apdgrqalsq
      241 llarpeyldl paplllaald paqggpafta pypapaygqw yarqmqlwgr apaglegvat
      301 riyrpdlflr aggeardiae ppananfd
//
LOCUS       WP_008495478             342 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [unclassified Acidocella].
ACCESSION   WP_008495478
VERSION     WP_008495478.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidocella
  ORGANISM  unclassified Acidocella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidocella.
REFERENCE   1  (residues 1 to 342)
  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 342)
  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 342)
  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 342)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="unclassified Acidocella"
                     /db_xref="taxon:2648610"
     Protein         1..342
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=36889
     Region          12..337
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mtknnnaltl trrtalagga alplfgiltr raqaaeftyk matgqapshp vnkraqeaid
       61 riaknsdgri kidlfpaaql gtdaqlisqv riggvqfinm assvlatyvp aagvvntgfa
      121 fngydqvwqa mdgalgkyig qsidkagltm igrswdngfr qittstkpik tpedlknfki
      181 rvppapilts lfaalgaspt pidfsevyta lqthlvdgqe nplpiiatak lyevqkycsl
      241 tghvwdgyli lgnpaalnrl paemkamvih efdqagkder tdiaalsksl qadmsakglq
      301 fldvdkanfr talaktdfyp hwkakfgdqa wsllesvsgt lg
//
LOCUS       WP_008495493             336 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [unclassified Acidocella].
ACCESSION   WP_008495493
VERSION     WP_008495493.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidocella
  ORGANISM  unclassified Acidocella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acidocellaceae; Acidocella.
REFERENCE   1  (residues 1 to 336)
  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 336)
  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 336)
  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 336)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="unclassified Acidocella"
                     /db_xref="taxon:2648610"
     Protein         1..336
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=36477
     Region          18..333
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 miklsrraav agaaalplvs vmsrparaad fsyklatnlp pthplnvris ealanikqqt
       61 agklditlfp nstlgtdpvm lsevrsgaiq fftlsplils tlvpasaing vgfafkdekt
      121 afaamdgklg eyvrgeiskr gliafenifd ngfrqittsn rpintpadlk alrirvppaa
      181 lwtsmfkdfd aapttisfne vytslqtkiv daqenplaii nsaklyevqk ycsltnhmwd
      241 gfwllanpaa fnklpadfqa ivrkelnaaa lrqrvdvaal nsslqsslak qglvfnntdp
      301 aafrdalaqa gfykywkgqf gaqpwslles ytgplg
//
LOCUS       WP_008496179             330 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Planococcus halocryophilus].
ACCESSION   WP_008496179
VERSION     WP_008496179.1
KEYWORDS    RefSeq.
SOURCE      Planococcus halocryophilus
  ORGANISM  Planococcus halocryophilus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Planococcus.
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   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   4  (residues 1 to 330)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Planococcus halocryophilus"
                     /db_xref="taxon:1215089"
     Protein         1..330
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=37271
     Region          1..317
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 misfknvtkr ygeeivavnd vdftveegki vvllgpsgcg kttllrmvnr lesisegeii
       61 innenskdld aielrrkigy viqsnglfpn mtieenvmlv pdllgwskke krerfeylmk
      121 ligldakdyg krfphelsgg qqqrigvvra laadppvmlm depfgaldpi irdkiqeefl
      181 qiqrevkkti lfvshdidea ikmadkivll rngeimqfdt pskmlshpkn efvsqffgkd
      241 raikslslht vedlqtiigl gpvdesiqdt ktinihqdlr ntlsmlmnqe adqvvvkndq
      301 denigtitid lvqkylhfei kgkmsasqeg
//
LOCUS       WP_008497196             159 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Planococcus halocryophilus].
ACCESSION   WP_008497196
VERSION     WP_008497196.1
KEYWORDS    RefSeq.
SOURCE      Planococcus halocryophilus
  ORGANISM  Planococcus halocryophilus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Planococcus.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Planococcus halocryophilus"
                     /db_xref="taxon:1215089"
     Protein         1..159
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17377
     Region          13..159
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mftqksysgs sleqytmlsk qldalldgek nsianlsnas allnqfleri nwvgfylmed
       61 gelvlgpfqg lpacvripvg kgvcgtavad krtmlvedvq afpghiacda atrseivvpl
      121 mkedqvigvl didspeldrf tkedqqglel fvnvlmkhl
//
LOCUS       WP_008496403             263 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Planococcus halocryophilus].
ACCESSION   WP_008496403
VERSION     WP_008496403.1
KEYWORDS    RefSeq.
SOURCE      Planococcus halocryophilus
  ORGANISM  Planococcus halocryophilus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Planococcus.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 263)
  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 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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Planococcus halocryophilus"
                     /db_xref="taxon:1215089"
     Protein         1..263
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29582
     Region          24..263
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <160..259
                     /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 msaatnptlf hsiqsfsipy gtseyhplhh hpatvelllv vagtvhckid gqtylapagt
       61 vlfiqagswh eqlyaasdmq sgyrltfsaq ipksyaelpp iipiseidsl nsllmqlkqe
      121 qehprpdsnq mahhlinsil lhvfrsankq esfgysnsee tiqeikhyme enytkslsle
      181 elatrfefnk yqlarlfkqv tgvsplqyii scrintakyl lctsdssvsk iaskigyksd
      241 tqfqaafkkv vgvtprqyrv nhk
//
LOCUS       WP_008502887             274 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Enterobacter].
ACCESSION   WP_008502887
VERSION     WP_008502887.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 274)
  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 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   3  (residues 1 to 274)
  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   4  (residues 1 to 274)
  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 274)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Enterobacter"
                     /db_xref="taxon:547"
     Protein         1..274
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31710
     Region          16..274
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <158..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 mqgvpeqfnd erdsarfrhl aqlpglelyh ahisdyafep htheafgigt ietgaerfry
       61 rgsqhlaaek svvtmnpdei htgesategg wryrmvyiep dlleevtglr hwwfsdvtrh
      121 dplrsqqigr liyglwhtdd plaqkgllld lietfqpfah haprvqegah rfervreylh
      181 dnymraltld elasvvslsp yhfqrqfkah fhvtphqmlm airlwrakaf lthgmpaaev
      241 aaatgltdqs hltrafthry gitpvryqkq vtrr
//
LOCUS       WP_008503148             495 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Enterobacter sp. SST3].
ACCESSION   WP_008503148
VERSION     WP_008503148.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. SST3
  ORGANISM  Enterobacter sp. SST3
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Enterobacter sp. SST3"
                     /db_xref="taxon:1216470"
     Protein         1..495
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54036
     Region          1..495
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mqyikihsld nvavaladlt egtevtfdnq svtlrqsvgr ghkfalipia kgenvvkygl
       61 pighaladia pgeyihshna rtnlsdldey syqpdlpaaq eqsadrevqi yrrangdvgi
      121 rnelwilptv gcvngiarqi qtrflketnd aegtdgvhlf shtygcsqlg ddhintrtml
      181 qnmvhhpnag avlviglgce nnqvdafret lgefdpervh fmvcqhqdde veagveqlhq
      241 lyevmrhdkr epgklselkf glecggsdgl sgitanpmlg rfsdyviang gttvltevpe
      301 mfgaerilms hcrdeetfek tvtmvndfkq yfiahnqpiy enpspgnkag gittleeksl
      361 gctqkagasq vvdvlryger lkmhglnlls apgndavats alagagchmv lfstgrgtpy
      421 ggfvptvkia tnselaakkk hwidfdagql ihgkampqll tefvdaivei asgkqtcnek
      481 ndfrelaifk sgvtl
//
LOCUS       WP_008504091             300 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Mucilaginibacter paludis].
ACCESSION   WP_008504091
VERSION     WP_008504091.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter paludis
  ORGANISM  Mucilaginibacter paludis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (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
REFERENCE   5  (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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Mucilaginibacter paludis"
                     /db_xref="taxon:423351"
     Protein         1..300
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34451
     Region          24..287
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          208..287
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mkdtfpiydi caisefkrdd ilisrfapyl kshknlalph khtfyhvvlf tegggthevd
       61 fttfavkpfq iyfmvpgqvh swsfegevdg yiinfsvpff qsfllrpdyl eefpffngtt
      121 dhsvidiphp lqsqitqlfe aiiheseine kagldmvkal mlqifilvsr lstgsksqna
      181 tsynytllks fqklveksfs elklpkdyae ilyitpnhln aickdmlgvp agevirnrvi
      241 leakrllinr dqsvtsiayg lnfadnsyft kffkkhtglt pedfrkqtlt hthhdsttyr
//
LOCUS       WP_008506478             359 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Brucella].
ACCESSION   WP_008506478
VERSION     WP_008506478.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..359
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39500
     Region          1..345
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mevrvagvrk efarfpalhn vsltiqsgel iallgpsgsg kttllrliag letptegmif
       61 fgdedasqks vqernvgfvf qhyalfrhmt vadnigfglk vrpggtrpst aeirrralel
      121 ldlvqlsgle krypaqlsgg qrqrvalara maieprvlll depfgaldaq vrkelrrwlr
      181 eihdktghtt vfvthdqdea leladrvvvm sqgrieqvgt pdevydkpns pfvygfiges
      241 stlpvrveng evwladrnig lgaenmpdgd aqlyfrphdv elldgcggci agtviasrrs
      301 ggkrrvelev ggarerieie ipaehpaaek sriafrpryw tlfragdsei papkaattt
//
LOCUS       WP_008506972             275 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Mucilaginibacter paludis].
ACCESSION   WP_008506972
VERSION     WP_008506972.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter paludis
  ORGANISM  Mucilaginibacter paludis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Mucilaginibacter paludis"
                     /db_xref="taxon:423351"
     Protein         1..275
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=30648
     Region          58..211
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkntyayfci lilaliiasc spkgpyaatn kvyqhqvdsf arvlqlqqpa mltdssgmav
       61 psewvgtvnl gmrkpnyvii hytaegsigq tihtftvkrt qvsahyvvak dgqvvhmvnd
      121 ylraqhaglg kwgsvidmns isigieidnn gnepytdaqi ksllalldrl kkayaipaan
      181 fighqdfapk rkpdpgpffp wkklaekgfg ywsddvlels penfdyaial rligydtsdl
      241 naavvafkrh fvqtdikpkl tqldlnilyn vyqky
//
LOCUS       WP_008508871             415 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Mucilaginibacter
            paludis].
ACCESSION   WP_008508871
VERSION     WP_008508871.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter paludis
  ORGANISM  Mucilaginibacter paludis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 415)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 415)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Mucilaginibacter paludis"
                     /db_xref="taxon:423351"
     Protein         1..415
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47134
     Region          2..414
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 madkidvwvy ahwrgmsapk ligilsahqa kgkkafsfsy dkewittkeq llldpdiawf
       61 gghqyptgke nfgifmdsmp dtwgrtlmrr raaifaqeqg kkspvlydid fllgvhdmsr
      121 mgalrfktap egdfldndpi fptppwssir elqygaslie snenanevkk wlamlmapgs
      181 slggarpkan ildeqghpwi akfpskndti dkgaweylay qlavnagiam aeskiekvag
      241 kyhtfftkrf drqgherihf asamtmtgkn edlirdeaps yldivefiqf sgatvvedlh
      301 qiwrrmifni fisntddhlr nhgfilkeeg wrlspafdin psvdknglal nidmdnnaln
      361 idlaksvgqy frlgvkemni iidevqtsvs twerlaneig itrseqmlmr rafml
//
LOCUS       WP_008510152             278 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Mucilaginibacter
            paludis].
ACCESSION   WP_008510152
VERSION     WP_008510152.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter paludis
  ORGANISM  Mucilaginibacter paludis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Mucilaginibacter paludis"
                     /db_xref="taxon:423351"
     Protein         1..278
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32179
     Region          9..272
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mkqtfdvlsa tcsrettrly stsfslgiff fnrevrrpih aiygfvrlad eivdsfheyp
       61 ksallaelke dcfkaiergi svnpvinsfq qvvnqygigl nlisqflnsm emdlgeqdyt
      121 pekyeeyimg saqvvglmcl hvftngnqeq ferlkipamk lgsafqkvnf lrdvnadyqd
      181 lnrtyfphvn lssfsdddkr vieqdilsel ndalsgirql pqpcrkgvyl ayvyyrqlfh
      241 kisrvpaqkv msqrirvsng hkfwlmfdsl iryklnli
//
LOCUS       WP_008510599             249 aa            linear   BCT 20-JAN-2025
DEFINITION  prolipoprotein diacylglyceryl transferase [Mucilaginibacter
            paludis].
ACCESSION   WP_008510599
VERSION     WP_008510599.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter paludis
  ORGANISM  Mucilaginibacter paludis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002130
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Mucilaginibacter paludis"
                     /db_xref="taxon:423351"
     Protein         1..249
                     /product="prolipoprotein diacylglyceryl transferase"
                     /EC_number="2.5.1.145"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008961 -
                     phosphatidylglycerol-prolipoprotein diacylglyceryl
                     transferase activity [Evidence IEA]"
                     /GO_process="GO:0009249 - protein lipoylation [Evidence
                     IEA]"
                     /GO_process="GO:0042158 - lipoprotein biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28061
     Region          3..239
                     /region_name="Lgt"
                     /note="Prolipoprotein diacylglyceryltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0682"
                     /db_xref="CDD:440446"
ORIGIN      
        1 mhfpinihig sfsipvhlvc etmayflgyr yyaylrkhtt dlintenrli ifigaavgaf
       61 lgshlvgvle npsqlphfsl vyfmgnktiv ggflggligv eltkkkigvt vssgdmmvyp
      121 lilamiigri gcfwagledg tfgiasnlpw aidfgdgirr hptnlyeilf wialwiglyi
      181 tekrftlang arfkilmvay llfrfmiefi kpdyffsfgl gviqlvclgg ilyyyklflh
      241 peklienya
//
LOCUS       WP_008511087             279 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Mucilaginibacter paludis].
ACCESSION   WP_008511087
VERSION     WP_008511087.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter paludis
  ORGANISM  Mucilaginibacter paludis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 279)
  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 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   3  (residues 1 to 279)
  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   4  (residues 1 to 279)
  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 279)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Mucilaginibacter paludis"
                     /db_xref="taxon:423351"
     Protein         1..279
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32186
     Region          23..270
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          186..265
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 merqiriekl sagidktagi dtlrdhlqll wirggkgdle ihykhykiqp qrifflpqgq
       61 riqidwqgtg wlirlepwll rlffqrhpee kllplflpag rkcytdiipa tahalqslaq
      121 fiqqeqeaeh nlsiaqtyly aillhvanay rlvnkipkvs fnyavaekll pliqehfhke
      181 rlpafyasql gmpvrklnet ckratgklvq ewiteqllse aerllaespl sikeiayeld
      241 fadmaqfnhf lkkhngqspt afrqalqtdk rsdtdgqag
//
LOCUS       WP_008513757              77 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Dethiobacter alkaliphilus].
ACCESSION   WP_008513757
VERSION     WP_008513757.1
KEYWORDS    RefSeq.
SOURCE      Dethiobacter alkaliphilus
  ORGANISM  Dethiobacter alkaliphilus
            Bacteria; Bacillati; Bacillota; Dethiobacteria; Dethiobacterales;
            Dethiobacteraceae; Dethiobacter.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 77)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 77)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 77)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Dethiobacter alkaliphilus"
                     /db_xref="taxon:427926"
     Protein         1..77
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8424
     Region          19..77
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mkvirvflhn fldtysgqgp eteleildgw qvrdvlaaig iepeiigvvl vnkkladkdt
       61 eikandrvdl yplfggg
//
LOCUS       WP_008515931             327 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Dethiobacter alkaliphilus].
ACCESSION   WP_008515931
VERSION     WP_008515931.1
KEYWORDS    RefSeq.
SOURCE      Dethiobacter alkaliphilus
  ORGANISM  Dethiobacter alkaliphilus
            Bacteria; Bacillati; Bacillota; Dethiobacteria; Dethiobacterales;
            Dethiobacteraceae; Dethiobacter.
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
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Dethiobacter alkaliphilus"
                     /db_xref="taxon:427926"
     Protein         1..327
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=36223
     Region          1..310
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mlrldsiskq ypnnvqavdn vslevadgei itligpsgcg kttllrlinr ltektsgqif
       61 iegkeinrwn pielrrqigy viqqvglfph ltveqnisyv lrimgtgkkk qreraaelis
      121 lvgmdpsylr rypaqlsggq aqrvgfaral agnpsiilmd epfgaldqit rlqlqdells
      181 lqnelkktvi fvthdiqeam kmgdkivlmr hgqliqagkp adffirpkep fvtqfiggsd
      241 ffrlltfitv deiitrekrl sakaslpsgt sladalqlmf qknipeidvl dgqgntlgqv
      301 sqkmirniaa tistdqgdnp lkhtigs
//
LOCUS       WP_008516443             103 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Dethiobacter alkaliphilus].
ACCESSION   WP_008516443
VERSION     WP_008516443.1
KEYWORDS    RefSeq.
SOURCE      Dethiobacter alkaliphilus
  ORGANISM  Dethiobacter alkaliphilus
            Bacteria; Bacillati; Bacillota; Dethiobacteria; Dethiobacterales;
            Dethiobacteraceae; Dethiobacter.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Dethiobacter alkaliphilus"
                     /db_xref="taxon:427926"
     Protein         1..103
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11385
     Region          6..97
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mfglseknli yiregiktfa eieravvfgs ramgnykrgs didiaiagkn vtgetvakls
       61 eylnevaplp yyvdvvdyne isneelrkhi dtkgielnin seg
//
LOCUS       WP_008516741             224 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Dethiobacter alkaliphilus].
ACCESSION   WP_008516741
VERSION     WP_008516741.1
KEYWORDS    RefSeq.
SOURCE      Dethiobacter alkaliphilus
  ORGANISM  Dethiobacter alkaliphilus
            Bacteria; Bacillati; Bacillota; Dethiobacteria; Dethiobacterales;
            Dethiobacteraceae; Dethiobacter.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 224)
  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   3  (residues 1 to 224)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Dethiobacter alkaliphilus"
                     /db_xref="taxon:427926"
     Protein         1..224
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24551
     Region          <62..212
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 maitvagavr hkkiypgkqv ristagrqed slgqivdlgt dtvglkiiap taslpevwqv
       61 qdqvtvsfvv pedaiysfaa hvvsfedaam slqvkqvtpl erreqrsdyr lktaklinva
      121 vekeveksge kwqeaslldi srggasilsp vsvtagtnvm vwipleevdy vleteakvrr
      181 avegeegqli igvsfenlpl adqekildyi lkvytenkdv etak
//
LOCUS       WP_008519166             806 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Dethiobacter alkaliphilus].
ACCESSION   WP_008519166
VERSION     WP_008519166.1
KEYWORDS    RefSeq.
SOURCE      Dethiobacter alkaliphilus
  ORGANISM  Dethiobacter alkaliphilus
            Bacteria; Bacillati; Bacillota; Dethiobacteria; Dethiobacterales;
            Dethiobacteraceae; Dethiobacter.
REFERENCE   1  (residues 1 to 806)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 806)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 806)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..806
                     /organism="Dethiobacter alkaliphilus"
                     /db_xref="taxon:427926"
     Protein         1..806
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=90555
     Region          23..806
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mrgtasvkvr hplmkrrwvr vvlwifgilv fllvsalvgg ywfisrshpv legtgtmpql
       61 qqevtvlrde rgvaqinagt ledlffiqgy vmaqdrlfqm dmtrrlaggr lsevigedtl
      121 evdrfyrtfg mhrataavve kfdaeasimv esyaagvnay ieeafaagrq pvefrilgyd
      181 pdpwtaedsv ivakymgytl sgdhrnelmn yrvaralgeh aqlifpdymi adfpliyels
      241 evspfsdeel eelaafapae fqgsnnwais gehaesgfpl vandphlafg ipnvwyqthl
      301 nlegdfnsig vtvpgvpgvv lghngymawg vtamsvdqed lyleqfnpen pqlylfdgkw
      361 eeatvieeei yvdgveepyi evveitrngp iinkvidegp yqaislrwtg lepgeefngi
      421 lklsrstnme efiegmegfv tpalswvfad regnigyrgq allpvrqnst gvlpvpgwdp
      481 ayqwdgfipg delpqiynpe rgyimtannr pagedypyei gkfffpyrae rldeliqgqi
      541 asgdaftleq mkemqldiln tqaralapvl tdavvraade qplsaieqda lnllqgwdyv
      601 edaasaetlv whqwynllgs alfeemlgfp wnnflvihhv lveadqdpgn vlfaflpqgy
      661 hlsldevarq tfaeaieevi aiqgnnpdrw ewgkwhrltv rhpigsvwpl nylfnvgewg
      721 lggsgntpka lfadetgqil ggggwrfvsd lssveesydi impgqsgqvf sphykdqieg
      781 wvqgelypmi yekegsqnvk rkvftp
//
LOCUS       WP_008518539             168 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Dethiobacter
            alkaliphilus].
ACCESSION   WP_008518539
VERSION     WP_008518539.1
KEYWORDS    RefSeq.
SOURCE      Dethiobacter alkaliphilus
  ORGANISM  Dethiobacter alkaliphilus
            Bacteria; Bacillati; Bacillota; Dethiobacteria; Dethiobacterales;
            Dethiobacteraceae; Dethiobacter.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Dethiobacter alkaliphilus"
                     /db_xref="taxon:427926"
     Protein         1..168
                     /product="TRAP transporter small permease subunit"
                     /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=18103
     Region          1..142
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mekiekfvka ltlrtaqvsq ialvftviiv vanvvsrriw spipgtvelv emsgaillam
       61 avaytainkg himvgvlver fppriqaivd lvvnaialff iyllaretfv yagrmmergy
      121 stgllrlpia psiylvavgf amlglvllld flkaaiiavk gsesngan
//
LOCUS       WP_008519266             676 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Dethiobacter alkaliphilus].
ACCESSION   WP_008519266
VERSION     WP_008519266.1
KEYWORDS    RefSeq.
SOURCE      Dethiobacter alkaliphilus
  ORGANISM  Dethiobacter alkaliphilus
            Bacteria; Bacillati; Bacillota; Dethiobacteria; Dethiobacterales;
            Dethiobacteraceae; Dethiobacter.
REFERENCE   1  (residues 1 to 676)
  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 676)
  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 676)
  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 676)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Dethiobacter alkaliphilus"
                     /db_xref="taxon:427926"
     Protein         1..676
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=73083
     Region          18..666
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mnideiikts rdidlheisd egkirnpggi lalvifiigl iwslfhfyta gfglltatlq
       61 rsahlsigla lcflyfpfnr kkevayhkip whdillaltg fmtiiytfvf yndlvwrvgm
      121 pnqidllvgg laiilvllaa hrafgpalpi vtivflfypf vgqylpeiig hggyrmvrvi
      181 ndlyltntgi fgipigvsst fvftfvlfgc ffqasgaaqy ivqlsfaamg rfkggpakaa
      241 vvasgfmgsi agssvantvv tgsitipmmk ktgfssevag gvetaastdg qflppimgaa
      301 afvmaeftgi pywqiciaaa lpaiisyaal lcivhlqaak tgmqampkaq ippllttfik
      361 gifywfpici lvyyliirrf tpntagfyai lavigmmivm raiklgqdsk keeisfaanl
      421 vthlkglghd ilqaldstar smagiavaca cagiivgvvt ltglgmsitq viataagdnl
      481 fillimaaai siilglglpt takyvimatl vapailmvep tlpvvgvhlf ilyyailadd
      541 tppvgvaaya aaaiarsdpi rtgllgfkfd lgafllpfmf iynpefllid ttwqkalmva
      601 stslfgiycf saviqrwlft qlkiweqvil laiafsmiwp twitdivgas vfifiylhqr
      661 avkkredetq nlsaga
//
LOCUS       WP_008520751             524 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Jonquetella anthropi].
ACCESSION   WP_008520751
VERSION     WP_008520751.1
KEYWORDS    RefSeq.
SOURCE      Jonquetella anthropi
  ORGANISM  Jonquetella anthropi
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Dethiosulfovibrionaceae; Jonquetella.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Jonquetella anthropi"
                     /db_xref="taxon:428712"
     Protein         1..524
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=59692
     Region          6..470
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mgnkleliwf gkedeikiep riliedkeks nctndqnten miihgdnlla lkaleskyag
       61 kvkciyidpp yntgsafery ddnlehstwl slmncrlhsl ytllrkdgfm fvnldeqeha
      121 yakilldsif grhnfigdmi wkkrkgggnd srylaldhdy ilvyakdask ethprkwktv
      181 qseeylkryk eievdgrryy wdtvardglq npipvsvfcp dgsilsinsq isqatinegl
      241 sngsvrltks kngwtlhhkv ymgngkvqrs ivddvgtnkt asdemmylfg dkkafpypkp
      301 ekliarildl stepndlvld sflgsgttca vaqkmnrryi giemgdhayt hckvrldkvi
      361 dgsdqggisk avgwqgggay kfyelapsli nkddfgefvi nkeydadmla savalhegft
      421 yapdehifwk qskgnensyl fvttrhlnaa yldsikstme deeyliiack syengadkly
      481 pnitvkkipm mllercefdk enynlniinp pvyedeeeev ggde
//
LOCUS       WP_008521620             632 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Jonquetella anthropi].
ACCESSION   WP_008521620
VERSION     WP_008521620.1
KEYWORDS    RefSeq.
SOURCE      Jonquetella anthropi
  ORGANISM  Jonquetella anthropi
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Dethiosulfovibrionaceae; Jonquetella.
REFERENCE   1  (residues 1 to 632)
  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 632)
  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 632)
  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 632)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Jonquetella anthropi"
                     /db_xref="taxon:428712"
     Protein         1..632
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=66420
     Region          1..615
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mrklqgpvak alylyvlamg lfhlytavfg sfeaylqrai hltwvlpmvf vlypfaknks
       61 gepetsvpwy dwvlaaaaaa pglysmftys qiimrmqgvd elttvqivlg tvlivllleg
      121 trrivglpiv lvalaftvyt lvcdshwlps vlqgvpteys rmvegmyltd egifssslgv
      181 satfvmifli fggfleksgv geyfmefaqa ftgtqaggpa kiavlssalf gsisgsavan
      241 vygtgsftip lmkrigyeph fagaveavss aggqimppvm gagafvmaal lgvqfnkiii
      301 aavlpallyy gavllmvhlt avknglkglk aselpsktsv akrlymmapi vllvymllag
      361 ytpmygavag ivtawavslp nkerrmgpvr ilqaihdgsv gipiicvaca saglvvgsva
      421 lsgigfkfvs avlsiaqgsr flalllialv slilgmglpt tsayilgaal gvpalvklhf
      481 mpiaahmfvf yyaiisnitp pvalaayaas siagaspnkt gwtacrlgfl afvipfafcy
      541 dpgllfqlgw genilsivsg mvtllavalg ftgyargpin ivwrallfag aavalhpstl
      601 lslagtavvi aliflsnipm akpqtaaatg ns
//
LOCUS       WP_008521810             418 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Rhizobium sp. Pop5].
ACCESSION   WP_008521810
VERSION     WP_008521810.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. Pop5
  ORGANISM  Rhizobium sp. Pop5
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 418)
  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 11482064
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Rhizobium sp. Pop5"
                     /db_xref="taxon:1223565"
     Protein         1..418
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=44814
     Region          1..417
                     /region_name="PRK06132"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:235709"
     Region          217..>257
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mfsrlvfglg llsatalvhp alaadtrllq ifvskdkqsl avydgtevva tskvstgkdg
       61 httpsgifsv lekqkyhesn lysaapmpfm qrltwsgial hesnsvpryp ashgcvrmpg
      121 afakmlygmt etgvpviisd relvpqpidh ptlfhpdvpa ampllsdvel rpampdspqk
      181 pvqvamndta ampmpaaepi atpepeppse pismlitrrt lretvidiqt llnqlgfsag
      241 dpdgllgsst vqaiktfktl rpaefagdrs lisdtllksv yaaagkgepp ngvimvrraf
      301 kpifeapvti adpslalgth fftlhavdet agtadwlgit lennlsream krlgitnqes
      361 aivmgkpitr slsritipde trrridalia pgstltisdt glgretgegt dfititrg
//
LOCUS       WP_008524338             500 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Rhizobium sp. Pop5].
ACCESSION   WP_008524338
VERSION     WP_008524338.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. Pop5
  ORGANISM  Rhizobium sp. Pop5
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Rhizobium sp. Pop5"
                     /db_xref="taxon:1223565"
     Protein         1..500
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=51888
     Region          3..500
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mdkqpwiils agdnvavata aiapgstvag vearqkidpg hkvaiadipl gspvvkygqa
       61 igrttaevka gdhvhshnlh fendrlaata nsapeaasae dtartfmgyr radgraatrn
      121 yigiiasvnc sttvcraiad eanrtilphy dgidgfvpiv hdqgcgmsst gdgmnvlhrt
      181 lagytrhvnf ggvlmiglgc evnqltlygq sgagaskrhf niqdaggsrr averamgvlr
      241 eiaadvgkek rvpisigeii iglqcggsdg fsgitanpal gvaadllaaa ggtailsets
      301 eiygaehllr sravsdevak kldekiawwe eyvalhgasl dnnpspgnkr gglttileks
      361 lgavakggrs pltavygyae rvtapglvfm dtpgydpvsa tgqvagganm iafttgrgsc
      421 fgcrpapslk lssnsalyas meedmdidcg tiatgdatis gkgreifdli vdtasgkktk
      481 seifgygdne fvpwhlgatl
//
LOCUS       WP_008527660             196 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Rhizobium sp. Pop5].
ACCESSION   WP_008527660
VERSION     WP_008527660.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. Pop5
  ORGANISM  Rhizobium sp. Pop5
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Rhizobium sp. Pop5"
                     /db_xref="taxon:1223565"
     Protein         1..196
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21592
     Region          1..165
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlrrlydwtm slasrksaev wlaviafves svflvpadvl flpmslakpe rsyryaviat
       61 vasvlggiag walgyyayet varpilefyg kldafeqmka yvtyetilll lvtsglahlp
      121 pikivtilsg vihvnlglfi vsaivargar flflawllrs ygepirdfie krlgqivgig
      181 agavivlyvg yrsfah
//
LOCUS       WP_008528960             348 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Rhizobium sp. Pop5].
ACCESSION   WP_008528960
VERSION     WP_008528960.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. Pop5
  ORGANISM  Rhizobium sp. Pop5
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 348)
  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   6  (residues 1 to 348)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Rhizobium sp. Pop5"
                     /db_xref="taxon:1223565"
     Protein         1..348
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38392
     Region          23..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          91..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msgapadrck iprafwlava dvgvppaall rqarlpatlh lngqglvsta qffalwrale
       61 eltadpglgi klvesaetav hppsslaafh ardyrdglsr larfkrlctp eqlhfseqgg
      121 ecaikvewly aaepepaiav dvdfatlvel grrgtgqrlt pvrvefqrad pqseahrsyf
      181 gcpilygqsr nalilksadl drpfpghnpe llelltpala salgeirarn sireqvkivl
      241 krslasgrpe lsdvafdlgm sertlqrrit degstfrell vearqelgrq llsdssagid
      301 evacllgyqd ttsfyrafrd wegvtpnqwr eryvqdvgtr papdvsvh
//
LOCUS       WP_008529427             618 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup, partial [Rhizobium sp. Pop5].
ACCESSION   WP_008529427
VERSION     WP_008529427.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. Pop5
  ORGANISM  Rhizobium sp. Pop5
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 618)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 618)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 618)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 618)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 618)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 618)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..618
                     /organism="Rhizobium sp. Pop5"
                     /db_xref="taxon:1223565"
     Protein         <1..618
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
     Region          1..618
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 rklfylalgs vgvvygdigt splyafreal kpvahdgltr sevislislm iwaltiivti
       61 kyvlfllrad negeggtlsl lallmktang htallmllgl igaalflgda mitpalsvls
      121 aveglklvtp slseyivpis vvilallfvv qsrgtgavak ffgpitavwf lvmaaagish
      181 isddygilaa fnpyyavsfl lhegfygvvv lgavfltvtg aealyadlgh fgrrpiqwaw
      241 fvlvfpsltl nylgqgalvl gkpetmsdpf ylmypqwall pvvilataat iiasqavitg
      301 afslvrqgin lgflprmeil ftsetntgqi fvpsvnavlf igviflvlsf ktsdalatay
      361 gisvtgamvv tsimafefvr trwnwslpva iialaplvvl emiflganll kihdggyipi
      421 liataftvim wtwrrgtail mektrhtdip lasfvssier ksehspaqvp gtaifltsdp
      481 esapaallhn lkhnhvlhdr nviltirtvn kprvpshdry kveqiserfs rvellfgfme
      541 sqnvsqalat lrktglkfdi mstsfylgrr klvpdaksgm pywqdrlyia lanaaanpsd
      601 yfrlpanrvv elgshvii
//
LOCUS       WP_008531841             346 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Rhizobium
            sp. Pop5].
ACCESSION   WP_008531841
VERSION     WP_008531841.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. Pop5
  ORGANISM  Rhizobium sp. Pop5
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Rhizobium sp. Pop5"
                     /db_xref="taxon:1223565"
     Protein         1..346
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38701
     Region          1..344
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mevrvqnirk efdrfpalhd vsldirsgel iallgpsgsg kttllrliag lesptegqif
       61 fgdedaskks vqqrnigfvf qhyalfrymt vldnvsfglr vrngarrppk adirrralel
      121 ldlvqlsgle krypaqlsgg qrqrvalara mavepnvlll depfgaldaq vrkdlrkwlr
      181 eihdrtghtt vfvthdqdea leladrvvvm sqgaieqvgt pdqvydnpns pfvfgfigqs
      241 nclqveisdg dirfdgrslg lnadgepdgp aqlyfrphdv rlcesaenci agqsvssrrv
      301 agtrhieldi gndrphieie lppseadrld rnrvafkptr wklfrg
//
LOCUS       WP_008532566             390 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Rhizobium sp. Pop5].
ACCESSION   WP_008532566
VERSION     WP_008532566.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. Pop5
  ORGANISM  Rhizobium sp. Pop5
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Rhizobium sp. Pop5"
                     /db_xref="taxon:1223565"
     Protein         1..390
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=41977
     Region          2..389
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mdtilvvnag ssslkfevfs vagslarqik gkmegigtap hltiksaggd rladedyphe
       61 avpdlpaamr vvgqwlrerh qgrliavghr vvhggpdhmr paridekllr elerytplap
      121 lhqpnnlapi rvllehqpql vqvacfdtaf hrghdpmadh yaipahyfde gvrrygfhgl
      181 syeyvagkla eiapdigggr vivahlgsga smcalhqgks vestlgftal dglpmgtrcg
      241 qidpgvllyl lqqhgmsaqe lqdllykesg lkglsgvsnd vrdllaseep gaalaldhfv
      301 hriglnagtl aaalggldaf vftagvgens pvmrerisrt lewlgvrlds rrnaagelli
      361 ssddsrvavy avptdeelmi arhtyaliaa
//
LOCUS       WP_008532796             379 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Rhizobium sp. Pop5].
ACCESSION   WP_008532796
VERSION     WP_008532796.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. Pop5
  ORGANISM  Rhizobium sp. Pop5
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
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
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 379)
  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   5  (residues 1 to 379)
  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   6  (residues 1 to 379)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 379)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 379)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Rhizobium sp. Pop5"
                     /db_xref="taxon:1223565"
     Protein         1..379
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40372
     Region          39..79
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          98..364
                     /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 mrylrsgprr lhtqemgapr aktvglrsge iadrnirvil eairrhgplt rtelgrhsgl
       61 tgpgitnilr rlaeeklvts nrrnglggga tatefalrpe gafsigvklr rtrgeivlid
      121 lsgqvhdrvy fdvepedgvg avhaavrdma drhaalpivg igiaandwsd arseqlsams
      181 miarpcvene ctasllaert igsavpeggl amiiidddvq agflirgipy sgmhgragsi
      241 gemltgpdnv elntvvgfgs lrsrigdedf arllkgeeff spslsqwire aaghlldpii
      301 amagfiapsv vmiggdlpqg viealihqls verrdtstrp lltpwispmr pasfsgggva
      361 lgaallpfln tlllppasa
//
LOCUS       WP_008532998             103 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Rhizobium sp. Pop5].
ACCESSION   WP_008532998
VERSION     WP_008532998.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. Pop5
  ORGANISM  Rhizobium sp. Pop5
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Rhizobium sp. Pop5"
                     /db_xref="taxon:1223565"
     Protein         1..103
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=11212
     Region          1..>45
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mnevrlelll gkqvfdvdgk avgrveeira eargadlyvv eyhlgayslf erlsalaigr
       61 avltaigaar sgskkavpwd kldmrdlehl qvtcrgstlq tld
//
LOCUS       WP_008533390             279 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Rhizobium sp. Pop5].
ACCESSION   WP_008533390
VERSION     WP_008533390.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. Pop5
  ORGANISM  Rhizobium sp. Pop5
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 279)
  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 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   3  (residues 1 to 279)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 279)
  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   5  (residues 1 to 279)
  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   6  (residues 1 to 279)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Rhizobium sp. Pop5"
                     /db_xref="taxon:1223565"
     Protein         1..279
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30967
     Region          18..101
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          127..278
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 msaiaraiwf ieshfesdls leeisgaagl sryhlsrvfg lvtghsisgy irgrrlsrav
       61 palvggssti levalcagyg sheaftrafr dqfgmtpdav rrqgharnlv llepirmdpa
      121 rlndlepprf etlqpmlfag lqeiypyggn aaipsvwqkf nahfghipgq kgnvaygict
      181 hidgetekfr ymaaaeisda gdlpadfktl klpgqryvvf shrghvsgip stmhrifdtw
      241 wptsglehgd tpdmferyde rfdpytgmgv teiwlpira
//
LOCUS       WP_008534542             196 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Rhizobium sp. Pop5].
ACCESSION   WP_008534542
VERSION     WP_008534542.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. Pop5
  ORGANISM  Rhizobium sp. Pop5
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 196)
  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 196)
  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   3  (residues 1 to 196)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Rhizobium sp. Pop5"
                     /db_xref="taxon:1223565"
     Protein         1..196
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21771
     Region          72..172
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mftvapgaps sdptghllpa gekgtadvaa spfsprgega rradegapca tkiikqdirk
       61 hrtnktdqar alrrgeteee yhlwsdlrar rlngskfarq vplgpfivdf lcrekrlive
      121 vdgfqhaena hdqrrtewln vngysvlrlw nrevsqerhs vletilaalq grieasselp
      181 gfyspaestd kngers
//
LOCUS       WP_008534653             373 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Rhizobium sp. Pop5].
ACCESSION   WP_008534653
VERSION     WP_008534653.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. Pop5
  ORGANISM  Rhizobium sp. Pop5
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 373)
  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 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   3  (residues 1 to 373)
  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   4  (residues 1 to 373)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 373)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 373)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Rhizobium sp. Pop5"
                     /db_xref="taxon:1223565"
     Protein         1..373
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38587
     Region          27..358
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(99..101,122..123,172,224,248)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkksllsava ltamvafsgn awadvliava gpltgpnaaf gaqlqkgaeq aaadinaagg
       61 ingeqikiel gddvsdpkqg isvankfvad gvkfvighfn sgvsipasev yaengileit
      121 paatnpkfte rglwntfrtc grddqqgaia gkyladhfkd akiavvhdkt pygqgladet
      181 kkamnaagvt evmyeginvg dkdfsaliak mkeagvsiiy wgglhteagl iirqaadqgl
      241 katlvsgdgi vsnelasiag davagtlntf gpdptlnpan kdlvakfkaa gfnpeaytly
      301 syaamqaiag aakaagstda eavaaamkek gpfptvlgdi sfdekgdpki pgyimyewkk
      361 gadgkytyvp qgm
//
LOCUS       WP_008535130             196 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Streptococcus sp. C150].
ACCESSION   WP_008535130
VERSION     WP_008535130.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sp. C150
  ORGANISM  Streptococcus sp. C150
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Streptococcus sp. C150"
                     /db_xref="taxon:435842"
     Protein         1..196
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=22803
     Region          13..195
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 msnkermlhh lahhngiity kdcktlgipt vyltrleqeg tifrvekgiy ldangdyddy
       61 yffqyrfska iysytsalyl lgitdeipqy fevtvprgyr fntppsnlli htttkkfiei
      121 gvtriktlmg nyvqaydler ticdliinrn hidtelfvkt lqsfaknpnk nigklydyat
      181 kmqaikdikq tlevlm
//
LOCUS       WP_008538287             191 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Megamonas].
ACCESSION   WP_008538287
VERSION     WP_008538287.1
KEYWORDS    RefSeq.
SOURCE      Megamonas
  ORGANISM  Megamonas
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae.
REFERENCE   1  (residues 1 to 191)
  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 191)
  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   3  (residues 1 to 191)
  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   4  (residues 1 to 191)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 191)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Megamonas"
                     /db_xref="taxon:158846"
     Protein         1..191
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21446
     Region          1..190
                     /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"
ORIGIN      
        1 msklkiviad nesiirmdlk emleeaghev vgecfnglka ieltqrlkpd lvimdikmpe
       61 mdgitaakri sdqklapvil ltafsqkdiv ekaknsgvla ylvkpikpsn lfpaieials
      121 rfneikqles elddiknsle mrklldrakg ilmdaynlse seayrriqky smakrktike
      181 vaqsiiraat k
//
LOCUS       WP_008538310             422 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: galactokinase [Megamonas].
ACCESSION   WP_008538310
VERSION     WP_008538310.1
KEYWORDS    RefSeq.
SOURCE      Megamonas
  ORGANISM  Megamonas
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   McAuley,M., Kristiansson,H., Huang,M., Pey,A.L. and Timson,D.J.
  TITLE     Galactokinase promiscuity: a question of flexibility?
  JOURNAL   Biochem Soc Trans 44 (1), 116-122 (2016)
   PUBMED   26862196
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Holden,H.M., Thoden,J.B., Timson,D.J. and Reece,R.J.
  TITLE     Galactokinase: structure, function and role in type II galactosemia
  JOURNAL   Cell Mol Life Sci 61 (19-20), 2471-2484 (2004)
   PUBMED   15526155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Megamonas"
                     /db_xref="taxon:158846"
     Protein         1..422
                     /product="galactokinase"
                     /EC_number="2.7.1.6"
                     /GO_function="GO:0004335 - galactokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0005534 - galactose binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0046835 - carbohydrate phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=46971
     Region          34..416
                     /region_name="GalK"
                     /note="Galactokinase [Carbohydrate transport and
                     metabolism]; COG0153"
                     /db_xref="CDD:439923"
ORIGIN      
        1 msniieflks qeakeklmsl ynldeqavdt qvkryqklad afaevypvdn asffsssgri
       61 eiignhtdhq lgrivaasid mdtiaivtpn adgkihvksl eydeftidvn dlavkeddsr
      121 tvklikgile rfvqngrkig gfttfmtttv lsaagvsssa sfemlicail ndlynnneis
      181 tlecakagqw aennkwdkks glldqlacat ggmitidfan yenpevvkld skviqdkydf
      241 fitptgedhs aldgeytait vemkaisqff gkeylkdvsm ddimanlpal rekagdravl
      301 raihfitete rvrklaaevk ehdytnfeka vtdsglsswr flqncatpdp khqgialfla
      361 mneiyfqnhk gvcrvhgggf agsilsvipk eespafrafl kdvlkneyye ihmrdagsvk
      421 vf
//
LOCUS       WP_008538364             263 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: prolipoprotein diacylglyceryl transferase
            [Megamonas].
ACCESSION   WP_008538364
VERSION     WP_008538364.1
KEYWORDS    RefSeq.
SOURCE      Megamonas
  ORGANISM  Megamonas
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002130
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Megamonas"
                     /db_xref="taxon:158846"
     Protein         1..263
                     /product="prolipoprotein diacylglyceryl transferase"
                     /EC_number="2.5.1.145"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008961 -
                     phosphatidylglycerol-prolipoprotein diacylglyceryl
                     transferase activity [Evidence IEA]"
                     /GO_process="GO:0009249 - protein lipoylation [Evidence
                     IEA]"
                     /GO_process="GO:0042158 - lipoprotein biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30469
     Region          1..262
                     /region_name="Lgt"
                     /note="Prolipoprotein diacylglyceryltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0682"
                     /db_xref="CDD:440446"
ORIGIN      
        1 mefvafylgd iniywyglii vfalliglgi skimfklyge kfspmwdlli fiipvslica
       61 rifyviihld aymsnigqif ciwqgglsiy gallgflats ivflrkygyn lwlwfdlmip
      121 silfgliilq lanfmmqfsl gtplgldipn dhslaeyvey ryrptgfeay qyfqpvalyq
      181 afaysivfii svlcllinrk ykflaegtvf lfsvilmaii rfgigfmyfs vnkdmllypm
      241 qwialtvmia tvfiyivkrf qhn
//
LOCUS       WP_008538554             197 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Megamonas].
ACCESSION   WP_008538554
VERSION     WP_008538554.1
KEYWORDS    RefSeq.
SOURCE      Megamonas
  ORGANISM  Megamonas
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Megamonas"
                     /db_xref="taxon:158846"
     Protein         1..197
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21383
     Region          9..195
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mktkgferkr riivgvsgas gatyayrliq vladsgievh fvaskaglev leyecgltmv
       61 qltqmvhkiy dvnridsaia sgsfpcesmv ivpcsmktlg slangiagnl ltraadvtlk
      121 egrklvlvtr etpvhaihle nmlklshaga rivpacpgfy hrpqtieelv dmlvgkicdt
      181 lnvdndlfer wtgpsev
//
LOCUS       WP_008538934             495 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [Megamonas].
ACCESSION   WP_008538934
VERSION     WP_008538934.1
KEYWORDS    RefSeq.
SOURCE      Megamonas
  ORGANISM  Megamonas
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Megamonas"
                     /db_xref="taxon:158846"
     Protein         1..495
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54277
     Region          1..494
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mdilqinkld nvavaltdlt kgkiiqideh diilkenipa ghkialknin kdeqiikysf
       61 sighatddii agshvhthnl ktnlgkilny sykptkisnl pkienctfkg yqrengdvgi
      121 rnnlwivptv ncvtstvryl ekigkelikn ypniddcigi thpygcsqig kdyqmtqkil
      181 adivnhpnag avlvislgce nnnltefkki lgnynsdrvk flvtqevede diigkqllte
      241 latfankytr ttcpisklri glkcggsdgf sgitanplig elsdlaigsg attvltevpe
      301 mfgaetllmn rainedifhk tvdlinnfkq yfkrydqpis dnpspgnkag gittledksl
      361 gcvqkgghap ivdvldygdt inkvglqlln apgndsvstt alaasgcqii lfstgrgtpw
      421 gtivptikia tnsklaqhks kwidfnagel iekssmeklr nelfdyilti isgkltkseq
      481 mhfneiaimk dgite
//
LOCUS       WP_008540132             377 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Megamonas funiformis].
ACCESSION   WP_008540132
VERSION     WP_008540132.1
KEYWORDS    RefSeq.
SOURCE      Megamonas funiformis
  ORGANISM  Megamonas funiformis
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Megamonas.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Megamonas funiformis"
                     /db_xref="taxon:437897"
     Protein         1..377
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43337
     Region          1..266
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          263..350
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkimhlsdlh lgknlngfsl yedqrhihkq ilqiakeeai davmiagdvf dksvptnqai
       61 qlfdefltsw aelhlpvfii sgnhdsaqrv afganlfkdn nifispiydg kishitlkde
      121 hgninfyllp fikpaivrsy fpdeeitsyn qavkvalkqi slnpnernil iahqfvtgay
      181 tcdseeiivg gidnvdaqlf qdfdyvalgh lhtpqnvlne kirycgtllk ysfseanqek
      241 tvtilnfpqk nkltiyekkl sflhdmrklk gsyaeltlks nyeqtntddy laitltdeed
      301 ipdainrlrs iypnimqlty dnlrtktvqn iettdianlk tplnlfeely ykqnnqnlnd
      361 nqidilqeli qdiweek
//
LOCUS       WP_008541403             743 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Bradyrhizobium sp. CCGE-LA001].
ACCESSION   WP_008541403
VERSION     WP_008541403.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. CCGE-LA001
  ORGANISM  Bradyrhizobium sp. CCGE-LA001
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 743)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Bradyrhizobium sp. CCGE-LA001"
                     /db_xref="taxon:1223566"
     Protein         1..743
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=82512
     Region          23..682
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mkrlkilrrw farkfgfarl mclallvlfa garlwdpppi qelrlrtfdm fqlidprhka
       61 arpvvivdid dkslaklgqw pwprtriadl iqnltsngaa aigfdvvfse pdrlnpdlva
      121 sqmrhlddat raklrelptn dqilaeaikr srvvlgetgl pavlseldks lpftgvatvg
      181 eegaerflfe fpgllrnvpd iekvaagrgl fsirkerdgf irrvpmvmra qgnimpslsl
      241 eilrvvtgtp tllvrtdktg vravrlkgve iptdkngqfw vhyarrdpsi yvsaadvldn
      301 svspskfagk lvlvgtsaag lndikttpvs atmpgveiha qvlesvlsga visqpnyalg
      361 ieliaalvig llviiftpnl gpvrlvlaga afaailvgvs wffytqyryl idftypllst
      421 tavyltlifa sfvreqrqrv qirgqfaqym spvlveqlvq speklvlgge eremtimfsd
      481 vrgfttises ykhdpqglie lmnrfltplt dviieqkgyi dkymgdaima fwnaplddnk
      541 hevnaceaai qmleqidtvn kereqeaadg ghvyiplnvg iglntgigvv gnmgsdlkkn
      601 ysvlgdsvnl asrlegqtke ygfpiivgsr talaakdkfa ileldfimvk gksepeviya
      661 iagredvmhs gafqrlrnit iemlgcyrsr dwqgaldaie rgrksedadt leklfrlyek
      721 rikdfqvdpp pegwtgayal ltk
//
LOCUS       WP_008542642             211 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Sutterella parvirubra].
ACCESSION   WP_008542642
VERSION     WP_008542642.1
KEYWORDS    RefSeq.
SOURCE      Sutterella parvirubra
  ORGANISM  Sutterella parvirubra
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sutterellaceae; Sutterella.
REFERENCE   1  (residues 1 to 211)
  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 211)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 211)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Sutterella parvirubra"
                     /db_xref="taxon:437898"
     Protein         1..211
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22558
     Region          1..208
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     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"
ORIGIN      
        1 maydleeqes idqmkawwdt wgtpvtaavc vvclgfagwn gwnwyqrnea akasvayiql
       61 qnavyqndvk nidsisagmi aqygstiygp laafsaaqaa laqgnfdeaa aklnwiiekg
      121 ghpeydtvar vrlagvyfda gklddalkvl egakpadgqk asvadrrgdv lrakgdaasa
      181 kkayeealas aeandplrrl ielklgslpa a
//
LOCUS       WP_008543489             363 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [unclassified Bradyrhizobium].
ACCESSION   WP_008543489
VERSION     WP_008543489.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 363)
  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 363)
  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 363)
  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 363)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..363
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39837
     Region          1..355
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkrrdflkvt gaslaastav aapaiaqgsp eikwryatsw pkaldtlygg ceyfckqvad
       61 ltdnkfqiqp faageivpgl qvldavsngt vemgntalyy ywgknpaftf atalpfglnt
      121 rqqiswllwg ggqdlvndll kehnvygipt gstgaqmggw frkeiksvdd lkglkmrigg
      181 fagtilsklg svpqqlaagd iypalekgti daaewvgpyd deklgfvkva kyyyypgwwe
      241 gtsqghnimn iekwnalpkh ykaaidaasr dtftwitgky davnapalkr livsgaqvkg
      301 fpqevleacy naaneiyadl sksnphfgkm hasmmafknd slpwtqvael sydsfmarmr
      361 akt
//
LOCUS       WP_008544142             164 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Candidatus Pelagibacter
            sp. HTCC7211].
ACCESSION   WP_008544142
VERSION     WP_008544142.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Pelagibacter sp. HTCC7211
  ORGANISM  Candidatus Pelagibacter sp. HTCC7211
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Candidatus Pelagibacterales; Candidatus Pelagibacteraceae;
            Candidatus Pelagibacter.
REFERENCE   1  (residues 1 to 164)
  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 164)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 164)
  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   4  (residues 1 to 164)
  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   5  (residues 1 to 164)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Candidatus Pelagibacter sp. HTCC7211"
                     /db_xref="taxon:439493"
     Protein         1..164
                     /product="TRAP transporter small permease subunit"
                     /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=18861
     Region          3..156
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mknkylkfcd ftakacgafa vlalllsilv ivelvferyf fqraitwqte lvtmllvast
       61 figsayvlse kahvsmewiy dfmskksvlr lkiftsflsl lfflilfyfg flmveeaftk
      121 nystgtvwdp plwipyssmm igavlmilqy iaeiikltde akqn
//
LOCUS       WP_008547950             291 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Pseudovibrio sp.
            JE062].
ACCESSION   WP_008547950
VERSION     WP_008547950.1
KEYWORDS    RefSeq.
SOURCE      Pseudovibrio sp. JE062
  ORGANISM  Pseudovibrio sp. JE062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Pseudovibrio.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Pseudovibrio sp. JE062"
                     /db_xref="taxon:439495"
     Protein         1..291
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31856
     Region          15..258
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mtpiitclld grfelaegll wdeltkhlff cdilgkqiha mhwdtkevtt wdfpkvvgsf
       61 glckdgrliv amkdeiilfn tvtkiyevia kiepdnprtr lndgkvgpdg afwvgtmddi
      121 sprtpiasly rvapdgnvtq iateirtsng lawspdtktm yhsdtgsgev faydfdrdfg
      181 avtnqrkfaq ldntvgrpdg atvdidgnyw sagvsagnin cfapdgqllq siampvprpt
      241 ipcfagpnlg tlvvaslrph gddellkefp ksggifamdv ehkglptyrf g
//
LOCUS       WP_008548188             172 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Pseudovibrio sp. JE062].
ACCESSION   WP_008548188
VERSION     WP_008548188.1
KEYWORDS    RefSeq.
SOURCE      Pseudovibrio sp. JE062
  ORGANISM  Pseudovibrio sp. JE062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Pseudovibrio.
REFERENCE   1  (residues 1 to 172)
  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 172)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 172)
  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   4  (residues 1 to 172)
  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   5  (residues 1 to 172)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Pseudovibrio sp. JE062"
                     /db_xref="taxon:439495"
     Protein         1..172
                     /product="TRAP transporter small permease subunit"
                     /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=18892
     Region          1..166
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mtsfvsklda inrlvghtir wfallmlllq fgivllrylf gvsyiflgeg vlymhasvfm
       61 lgagytllad khvrvdifyg qaspkakaii nligalffll ptvglllwis wpfvynswki
      121 legpisvggi pasfllksli pafcglliiq gissilrdgl flcgidveep kl
//
LOCUS       WP_008549376             585 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Pseudovibrio sp. JE062].
ACCESSION   WP_008549376
VERSION     WP_008549376.1
KEYWORDS    RefSeq.
SOURCE      Pseudovibrio sp. JE062
  ORGANISM  Pseudovibrio sp. JE062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Pseudovibrio.
REFERENCE   1  (residues 1 to 585)
  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 585)
  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 585)
  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 585)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Pseudovibrio sp. JE062"
                     /db_xref="taxon:439495"
     Protein         1..585
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=60943
     Region          11..564
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mnrihrsiwl vlglatvlfh lglifsglvp nlvsrplhma lalpwalilm arnplekvtg
       61 yvlttfgvfa agwiawnhsa lgdqygylid nfqvylalgl litvlemarr aigwplplva
      121 lialaygmfg qhipgefgya gvplesflgt mtiaegglwg kltgvsvgvv aifvifgafl
      181 nageagagfm nvaaaaagkl kggtakvsvi ssalfgsisg sasanvastg aitlpamtkl
      241 gypralaaav eavassggqi mpplmgagaf vmveltgvpy tgimaaailp aflyffavwm
      301 ginafarryd lkglapedqp dtrsviitsl fflvpftvll wamfvlgytp qyaaclsimv
      361 avalllidkn fkldlrkiga ryeqalmnsg kqvamiasii lcasiiigtl gvtglgvkit
      421 slilsgsggm lwpallltal acmvlgmevp ttaayvicvs vagpalidig leplqahlfv
      481 fwfallstit ppvcgavfia agmvnenwlk valfamalgi glyliplgmi anptlitlvs
      541 spawsllatv kvglalsais ygviapfspl irggligggg vllfi
//
LOCUS       WP_008551933             862 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Pseudovibrio sp. JE062].
ACCESSION   WP_008551933
VERSION     WP_008551933.1
KEYWORDS    RefSeq.
SOURCE      Pseudovibrio sp. JE062
  ORGANISM  Pseudovibrio sp. JE062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Pseudovibrio.
REFERENCE   1  (residues 1 to 862)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 862)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 862)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..862
                     /organism="Pseudovibrio sp. JE062"
                     /db_xref="taxon:439495"
     Protein         1..862
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=92538
     Region          57..>216
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          178..>363
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          325..>510
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          472..>657
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          601..>787
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 msdsvtatss nnlsnsdple tasslasvie vsvspseaeq etaakdeqsa vyhyeygqdq
       61 ntiidvhgds sevneliigs gyqpydvqfs rpsgadnddl lltfydggtl liknqfsegq
      121 giqtirfada dyfvlsgyei meatfnftdg ddvihggeqg dtlhgvggnd tlygyagddt
      181 liggygddtl eggsgndtyk yeygdgndti idvhgdssev neliigsgyq phdvqfsrps
      241 gtdnddlllt fydggtllik nqfsegqgiq tirfadadyf vlsgyeimea tfnftdgddv
      301 ihggeqgdtl hgvggndtly gyagddtlig gygddtlegg sgndtykyey gdgndtiidv
      361 hgdssevnel iigsgyqpyd vqfsrpsgtd nddllltfyd ggtlliknqf segqgiqtir
      421 fadadhfvls gyeimeatfn ftdgddvihg geqgdtlhgv ggndtlygya gddtliggyg
      481 ddtleggsgn dtykyeygdg ndtiidvhgd ssevnelvig sgyqpydvqf srpsgadndd
      541 llltfydggt lliknqfseg qgiqtirfad adyfvlsgye imeatfnftd gddvihggeq
      601 gdtlygvggn dtlygyagdd tliggygddt leggsgndty kyeygdgndt iidvhgdsse
      661 vnelvigsgy qpydvqfsrp sgtdnddlll tfydggtlli knqfsegqgi qtirfadady
      721 fvlsgyeime atfnftdgdd vihggeqgdt lhgvggndtl ygyagddtli ggygddtleg
      781 gsgndtfkfe glyfgndtvt dfnvdtevvq lefgmvtsfe ellavavdeg dsvtirfnee
      841 tsitltgvqt enlqadnfef li
//
LOCUS       WP_008552154             439 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Pseudovibrio sp. JE062].
ACCESSION   WP_008552154
VERSION     WP_008552154.1
KEYWORDS    RefSeq.
SOURCE      Pseudovibrio sp. JE062
  ORGANISM  Pseudovibrio sp. JE062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Pseudovibrio.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Pseudovibrio sp. JE062"
                     /db_xref="taxon:439495"
     Protein         1..439
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46220
     Region          <6..151
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          135..419
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mniqlgsgde nysttssedh hvlagagndt ivtaagndql ygeegddyld ggsgndilsg
       61 gaghntyffd rdydkdvikd tlgsdvvkfg agitmdniri aaggpdnkdl kiylidpsnp
      121 dqpfdeiadv ltiengvsnq ilagqfvfdd gstlpkfevh edgslryfgt deddtfvgsd
      181 adeeiygsag idiidggggr nairynnsae avsvnlatge msggdaegdq ltnisqvfgs
      241 ehndtiigdd nnnglygldg ddhleggggd dwlnaygsgs dyldggsgnd tvryrwseaa
      301 vtvdladqan ntgdaagdty vsienvmgtd kfddiiigda gnnklwgygg ndtltggdgn
      361 dtflfetnfe hdtitdftvg agsddtirft edsfvsfedv latasqvgtd tviqlnddns
      421 itlqnvsvad lhaddfafa
//
LOCUS       WP_008552873             678 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Pseudovibrio sp. JE062].
ACCESSION   WP_008552873
VERSION     WP_008552873.1
KEYWORDS    RefSeq.
SOURCE      Pseudovibrio sp. JE062
  ORGANISM  Pseudovibrio sp. JE062
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Pseudovibrio.
REFERENCE   1  (residues 1 to 678)
  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 678)
  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 678)
  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 678)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..678
                     /organism="Pseudovibrio sp. JE062"
                     /db_xref="taxon:439495"
     Protein         1..678
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=71365
     Region          6..672
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mshnttdqtl edlerkydpd ltfraagpvl avvitaalva mslyhyyasg fglirelvhr
       61 gihlsfvlgl vfvlfsfiks tssqsapsaw wrpsgvhlwd vvlavlavaa amylpllpae
      121 avasrvgapa pidvfmgtvl lvlvleaarr svgptlplia lifigyavfg mfapgalkhp
      181 gaswtglinh lymtnqgiyg iaigvvakyv flfvlfgvla triglgqlfi dlasviagry
      241 aggpakvaif ssamlgtisg ssiantvttg sltipamkkv gypphfagav eatastggqi
      301 tppimgaaaf imvefleipy revllaamfp allhyfgifv mvhleakrlg lrglsadelp
      361 kalvvmkqhw lsviplgilv ylivsgktpd faavwgitac vvvgflnphn rmglkdlies
      421 latgakysla vgaaaaavgi ivgvvtltgt gfrlsfvvtq aasdlggfia sgmlaeyvtq
      481 naltlfftll ftaiaciimg agipttatyi ilvsiaapal gllgvqplva hffvfyygvl
      541 advtppvala ayagagiaga npfktgntaf rlgiakalvp fvfvyspall lvtpeftwyd
      601 flitlsgamv gigllgvafs gymlaglnkl erywtafaam ffvapgiqtm aiggvlmlpv
      661 ivrqmlarkn qqlvmqda
//
LOCUS       WP_008559242             308 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Phaeobacter italicus].
ACCESSION   WP_008559242
VERSION     WP_008559242.1
KEYWORDS    RefSeq.
SOURCE      Phaeobacter italicus
  ORGANISM  Phaeobacter italicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Phaeobacter.
REFERENCE   1  (residues 1 to 308)
  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 308)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 308)
  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   4  (residues 1 to 308)
  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   5  (residues 1 to 308)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Phaeobacter italicus"
                     /db_xref="taxon:481446"
     Protein         1..308
                     /product="TRAP transporter small permease subunit"
                     /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=35022
     Region          84..>212
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mqdesgisff galfgglywl iqniagafyn fgyavthpql wldwsdkasi mrfvyyggsv
       61 efffvvftaf llltavgmyr rsimwgvvrg legfantlgr lfawagllmv lqqivivfmq
      121 rvfarpdmsf glgialekdi swfaeelkly nalvvclcvt ytfvqgghvr vdliysgisf
      181 rakrmvdmig slifmmpaav ltwmygwyfl wrhlivpkps asdtlerlvm ksralrwnve
      241 tigfspngfn gyflfkillv tfagivflha iaffyrsyle fvegqgsenk hldkdslgeg
      301 eeayegah
//
LOCUS       WP_008559394             343 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Bradyrhizobium sp.
            CCGE-LA001].
ACCESSION   WP_008559394
VERSION     WP_008559394.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. CCGE-LA001
  ORGANISM  Bradyrhizobium sp. CCGE-LA001
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 343)
  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 343)
  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 343)
  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 343)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Bradyrhizobium sp. CCGE-LA001"
                     /db_xref="taxon:1223566"
     Protein         1..343
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=37642
     Region          9..341
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mvfstrfsrr tllkasaata vlggigaphv araqsaefty kyannlpdth plnvrakema
       61 aaiktetngk fdlqifpnnq lgsdtdmlsq irsggvefft lsglilstlv paasingigf
      121 afpdydtvwk amdgdlgahv rgeikkagle vmdkiwdngf rqttssskpi tgpddlkgfk
      181 irvpvsplwt smfkafdaap asinfsevys alqtrivegq enplaiista klyevqkycs
      241 ltnhmwdgfw flanrrawek lpqdvrtvva kninaaavke redtaklnan lqqelagkgl
      301 afnqpavapf rdklrtagfy aewkgkygdq awdhlekavg kls
//
LOCUS       WP_008559759             517 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Phaeobacter italicus].
ACCESSION   WP_008559759
VERSION     WP_008559759.1
KEYWORDS    RefSeq.
SOURCE      Phaeobacter italicus
  ORGANISM  Phaeobacter italicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Phaeobacter.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Phaeobacter italicus"
                     /db_xref="taxon:481446"
     Protein         1..517
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53784
     Region          104..360
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          253..501
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mvnivvtata nyvpeydlyn ldldavrlvs ttssaitaaf gdfsltltgs fqydfngalt
       61 qssvvrgfsf qysgsqivta tgfslsgydl srydfatlit remagadtft sawnsgeyie
      121 tlggndtira gsgndtidgg tgydtvmvra tgnewsiswg ysrgvevssp dgedtllnve
      181 rvqfedqtal iaeggagndr listqtvign slwdmmngrg gddtiqgggg rdfligergn
      241 dlikgganhd yisggdgndi lhgqagndki rgfsgsdtiy ggagndtlya dfensvdsds
      301 adrlyggagk dllvgqrsad ylnggidkdt lrgdagqdtl lggngwdrll ggadrdllrg
      361 gngrdylagh sgadvldgga hadrllgggg ndtlkggtgt dllnggsgnd llfggggndt
      421 llggtgrdrl lgqagddqlt ggayadtfvf hqgygndtit dfsvgqdriq igrgangldd
      481 ltfntsgddi qitfadvtil venttlaeld sadnflf
//
LOCUS       WP_008560370             406 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Phaeobacter italicus].
ACCESSION   WP_008560370
VERSION     WP_008560370.1
KEYWORDS    RefSeq.
SOURCE      Phaeobacter italicus
  ORGANISM  Phaeobacter italicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Phaeobacter.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 406)
  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 406)
  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 406)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Phaeobacter italicus"
                     /db_xref="taxon:481446"
     Protein         1..406
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=42759
     Region          26..92
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          289..356
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 migrltqrkq ktheqssqpk gfddyelrlg dmmrgeratm gkslldvqre lrikasyiaa
       61 ienadptvfd tpgfiagyvr syarylsldp datfaafcqe sgfqvahgms aeasvrksaa
      121 apiatgmggl rsdaftspnt pfvpasssff ssvepralgs lavlvaligg igyggwavlk
      181 eiqqvqmapv dqtpivladl dpltgaegpt aegedpatea larlyrpqal dvpvliprdg
      241 piatldprgl gnfalpelps lalaeaslsa dlpgpavpqv veevapalqm vavrpswvqv
      301 taadgsviye timepgqhfe iplteeppll rtgesgaiyf avngahygpv gnrgqvtknv
      361 vlssdalter fqladlsadq nsalatlvae lqasslsadv apeitd
//
LOCUS       WP_008562853             290 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Phaeobacter italicus].
ACCESSION   WP_008562853
VERSION     WP_008562853.1
KEYWORDS    RefSeq.
SOURCE      Phaeobacter italicus
  ORGANISM  Phaeobacter italicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Phaeobacter.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Phaeobacter italicus"
                     /db_xref="taxon:481446"
     Protein         1..290
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31634
     Region          22..262
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 masdvtthps taeifsetrc tlgegplwhp trqqlfwfdi lgqqlfsvan gkeirwqfdd
       61 cvsaagwvdd htlimasasa lwrfdieagv rshlidlead kpltrsndgr adpwggfwig
      121 tmgynaetgl gaiyryfrge lrklvhsqti tnaicfspdg scayftdtat gkimrqplak
      181 ddgwpigaps vfldlssedf gpdgavvdat grfwnaqwga srvavytpsg dlteiyplpt
      241 aqascpafgg kdlsdlfvtt aadglddpaa gktyrietra kgqrehrvil
//
LOCUS       WP_008562467             299 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Phaeobacter italicus].
ACCESSION   WP_008562467
VERSION     WP_008562467.1
KEYWORDS    RefSeq.
SOURCE      Phaeobacter italicus
  ORGANISM  Phaeobacter italicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Phaeobacter.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Phaeobacter italicus"
                     /db_xref="taxon:481446"
     Protein         1..299
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30750
     Region          <5..199
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mialmtmlgv gllagiilhe sgdddtsdas nnesetgqne spaingselg dlllgtsgne
       61 visggegddn idarggndtv eggegndsid ggsandnlfg gegndvivgg ngddfmrgna
      121 gddilvdgrg edhlvggqgn dtivgsgifd egkyedllqg rltassqeev istleydirn
      181 dtddqgdtin agagddavvf gkddtvtggl gddvfetgvw mndesdqati tdftasddrm
      241 iyyyvageaa peldvvtrdn ddggtdaflv adgvevvrlv nagsdfnved hvslvelas
//
LOCUS       WP_008563509             404 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Phaeobacter italicus].
ACCESSION   WP_008563509
VERSION     WP_008563509.1
KEYWORDS    RefSeq.
SOURCE      Phaeobacter italicus
  ORGANISM  Phaeobacter italicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Phaeobacter.
REFERENCE   1  (residues 1 to 404)
  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 404)
  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
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 404)
  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   5  (residues 1 to 404)
  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   6  (residues 1 to 404)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 404)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 404)
  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 20021635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Phaeobacter italicus"
                     /db_xref="taxon:481446"
     Protein         1..404
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43384
     Region          8..>77
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          86..391
                     /region_name="ASKHA_ATPase_ROK_CYANR"
                     /note="ATPase-like domain of
                     cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and
                     similar proteins; cd24073"
                     /db_xref="CDD:466923"
ORIGIN      
        1 maksvklshs delressrqq vfdaireagq iaridiaqvt rispatvtai tadliaagli
       61 eevspdisrg akrgrprval kirgdahtia gmklshhait tlitdfegae lvcheiplpg
      121 gqldpdalce kivtaldesc aqgglerqqi sglaigmagv mdadrnfvyw ssslnvrnid
      181 fgsylaryls ipvfidndan lvakaellfg egdkrsnfvv vtvehgvgmg ividnqiyrg
      241 argcgaefgh tkvqlegalc qcgqrgclea yvgdyallre anvtsgverh kdlaslyaar
      301 eagdimaqst ldragrmfam glanvvnifd pqmillagaq lafgylssdk vvhemrrsvl
      361 qvdgplpevr vhgwgnkmwa kgaaahaiee isalrirevs ghav
//
LOCUS       WP_008564711             372 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [unclassified Bradyrhizobium].
ACCESSION   WP_008564711
VERSION     WP_008564711.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 372)
  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 372)
  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   3  (residues 1 to 372)
  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   4  (residues 1 to 372)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 372)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..372
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39528
     Region          27..358
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(100..102,123..124,173,225,249)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkslkligla fgaslalssa afaqdvtvav agpmtggesa fgrqmkngae mavtdinaag
       61 gvngkklals veddacdpkq arsiaekiag akipfvaghy cssssipase ayadgnvlqi
      121 tpastnplft erklwnvarv cgrddqqgli aaqyiaknyk gkniailndk ttygkglade
      181 tkkalnkagi tekmyesynk gdkdfnaivs rlkrdnidlv yvggyhqesg lilrqmrdqg
      241 lktvlmagda ladkeyasit gpagegtlft fgpdprnkpt akkiveafka kgidpegytl
      301 ytyaamqvws qaakkagttd akkvmeavka gkwdtvigpi eydakgdikq idyvvykwda
      361 kggyaeisgn gt
//
LOCUS       WP_008565174             498 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Segatella maculosa].
ACCESSION   WP_008565174
VERSION     WP_008565174.1
KEYWORDS    RefSeq.
SOURCE      Segatella maculosa
  ORGANISM  Segatella maculosa
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Segatella maculosa"
                     /db_xref="taxon:439703"
     Protein         1..498
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54661
     Region          5..498
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mkqtaylqin kadtvvvclr pidkgetlei ggrritvrqd tpaghkillr dtakgeniik
       61 ygypighake nleagewvne hnigtnlagt lnyeykpvke vldikdehrt fkgyvrknge
      121 vgvrnevwiv ptvgcvngia erlakqleqe trlegidavh awhhnygcsq lgddhentrk
      181 ilrdiclhpn agavlvlslg cennqpedfm rllgdydadr iqllitqkve gdemeegmkl
      241 lrqlyakaaq dkrsevsvsk lrvglkcggs dgfsgitanp lvgefsdwlv aqggttilte
      301 vpemfgaeti lmnrcktpql fqktvslind fkdyflshge pvgenpspgn kaggistled
      361 kalgctqkcg rapvsgvley gerlrhngln llsapgndlv aatalaasgc qlvlfttgrg
      421 tpfgtfvptm kistnsnlyn tkrnwidfna gelvegtdmd slrnrftdki iatasgdlvr
      481 neindyreia ifkngvtl
//
LOCUS       WP_008565215             158 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Segatella maculosa].
ACCESSION   WP_008565215
VERSION     WP_008565215.1
KEYWORDS    RefSeq.
SOURCE      Segatella maculosa
  ORGANISM  Segatella maculosa
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 158)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Segatella maculosa"
                     /db_xref="taxon:439703"
     Protein         1..158
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17322
     Region          2..157
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mqmsdkeqay etlcrqissl iegennlisi lsnvasalhf afpdrffwtg fylvcdtelq
       61 lgpfqgpvac mhigrgrgvc gtawagnrtl vvddverfpg hiacsslsrs eivaplhrsd
      121 gsvwgvidid skahsafdnt dacylekiai ilnkqlee
//
LOCUS       WP_008565391             234 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Segatella maculosa].
ACCESSION   WP_008565391
VERSION     WP_008565391.1
KEYWORDS    RefSeq.
SOURCE      Segatella maculosa
  ORGANISM  Segatella maculosa
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Segatella maculosa"
                     /db_xref="taxon:439703"
     Protein         1..234
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26398
     Region          151..227
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mkkfawlfcv aiamampaha qtfldhlrkn vpgqgtvtvt qskeidelin gnqpkktpat
       61 tepkkeivkk etaigktept kkenkkpqhi ltgdstktat nkveptekpv erhetptakt
      121 epikkqqeeg eldiptidmr kkvmrgshki tgyrvqafsg gnsrldrqka eqastaikmk
      181 ypdqpvyvhf ysphwicrvg nyrsfeeaet mlrkvkalgy rqacivrgki ivqd
//
LOCUS       WP_008565637             740 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Segatella maculosa].
ACCESSION   WP_008565637
VERSION     WP_008565637.1
KEYWORDS    RefSeq.
SOURCE      Segatella maculosa
  ORGANISM  Segatella maculosa
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Segatella maculosa"
                     /db_xref="taxon:439703"
     Protein         1..740
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=83798
     Region          10..740
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mnlhqtifai vcfisplsta haqqrshlnd tvillkevsv rarysltspn vmqalanqrr
       61 iagstslvei hadhqrmatm kealrlqpgv iiqeffgand qprlnirgsg iqsnpqrrgv
      121 yllqdgipvn fsdgsyvigi mdamtaryie vfkganalrf gagtlggaln fvsrtaltds
      181 tasvkleggs ygtfgltfsm gkrlgawdmf aastynrqeg yriynknqrl tasvnigwrn
      241 rkqtvenrtf vhfthlffqm pgpltldqlm tdpkqvstgv dlpfsmgpni lrdrphrnvd
      301 mfrianqtgf vlnaksnlsa svyyqyaddw fafpitisip hsfnndigat lyyhlsmskm
      361 rlsagvlgaf gwmdrryhin kdgkasfmfa rdrlhaanft vfteadyalh dqlhavldvh
      421 gvynkrnskd afgdpslrpw yshmskkyry fysqnstlrq hftafnprig liwspvrrkd
      481 iqlfanvsns yepptfdelv gtevtsnint spkklfsial kkqtattfel gskgrlsrls
      541 wnvafyhswv aneileikdy vrgqkrteny pntvhqglev giqmaskphl fgynigsfti
      601 gavydysrft fkggkydgky lagvpkhyin tsldyqhscg lngsislelk pgetpidhtn
      661 tmfqpayhvw narlgyqigt qwnlyvelkn ianrryassy iisdeihqpa ipfpeftakq
      721 ltffipgqpr smfagltwrw
//
LOCUS       WP_008567419             141 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Stutzerimonas degradans].
ACCESSION   WP_008567419
VERSION     WP_008567419.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas degradans
  ORGANISM  Stutzerimonas degradans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Stutzerimonas degradans"
                     /db_xref="taxon:2968968"
     Protein         1..141
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14735
     Region          1..140
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 maqhhnkgft lielmivvgi lgilaaiayp nymeyvqrsn rsegqallqd aaagqerffa
       61 qnnsyvttaa diaklglrgt ngttvksdng kytltvaggg ggytltatqs fgdvacgnlt
      121 lnalgvrgrt gsgktveqcw k
//
LOCUS       WP_008567576             182 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Stutzerimonas degradans].
ACCESSION   WP_008567576
VERSION     WP_008567576.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas degradans
  ORGANISM  Stutzerimonas degradans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
REFERENCE   1  (residues 1 to 182)
  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 182)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 182)
  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   4  (residues 1 to 182)
  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   5  (residues 1 to 182)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Stutzerimonas degradans"
                     /db_xref="taxon:2968968"
     Protein         1..182
                     /product="TRAP transporter small permease subunit"
                     /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=19977
     Region          8..177
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mshdappllr vaglidslnr rfgqlcawft lflvagtaiv vvlrygfgig aialqeavmy
       61 ahalvfmgaa awtlqrnghv rvdifyqklv srrqaivdgl ghvlflipvc lflawnswdy
      121 vanswatheg snesgglkfv ylqksiilvm vislalqava dliklgyrla grlpqdeevq
      181 hg
//
LOCUS       WP_008570104             288 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Stutzerimonas degradans].
ACCESSION   WP_008570104
VERSION     WP_008570104.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas degradans
  ORGANISM  Stutzerimonas degradans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Stutzerimonas degradans"
                     /db_xref="taxon:2968968"
     Protein         1..288
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31192
     Region          1..278
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mivdlhchst asdgvlapsl vverahgrgi ellaltdhdt legldeahaa asalgvrlin
       61 gielsclwng atihvlgygf srtapallha iaalhdgrwr raeliaerla akgmpgaldg
      121 araiqqelgd sgnaparphf aeflvraghv rdraeafrkw lgagklgdvk qhwpsleqtv
      181 ttlreadawi slahpwqyaf trskrrrlvt dfvqagghal evvngmqpld qvggltilar
      241 efglkasags dfhapgdwse lglyrplped lsplwrcfdh ecrrsaas
//
LOCUS       WP_008570174             340 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Stutzerimonas degradans].
ACCESSION   WP_008570174
VERSION     WP_008570174.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas degradans
  ORGANISM  Stutzerimonas degradans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
REFERENCE   1  (residues 1 to 340)
  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 340)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 340)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 340)
  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   5  (residues 1 to 340)
  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   6  (residues 1 to 340)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Stutzerimonas degradans"
                     /db_xref="taxon:2968968"
     Protein         1..340
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38825
     Region          29..210
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          254..336
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 maigyecdtr fipahhqpal lidlalsrgi dshrllrgtg lfyadiaegr aklspeqfvt
       61 lignaqrlld addssflfgq rllpghygea shtlehactl hqalerlqcf rallsplltp
      121 rlllddkqay lywldscgtg hsriflaeac mtavvamsrr lsaerlpwrf hfsyakpryi
      181 eqywvhlgee ltfdsqltmm slpreylhrp wpdasvtagq vaelasqtql aslgwqcsfl
      241 dqlyeylqan irtplnlerv alafgmspat lkrklqkhdt hfqeqldlar khvalylyqv
      301 rgygndevaa ylrftdttnf rrsfkrwtgm vpsglrrlfg
//
LOCUS       WP_008570640             118 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Pseudomonadaceae].
ACCESSION   WP_008570640
VERSION     WP_008570640.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonadaceae
  ORGANISM  Pseudomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (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   3  (residues 1 to 118)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 118)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Pseudomonadaceae"
                     /db_xref="taxon:135621"
     Protein         1..118
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12635
     Region          1..118
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mslpanlgpr ngilsltikd ksvlyaafmp fikngglfip tnksyklgde vfmllnlmde
       61 pekipvagkv vwitpkgaqs nraagvgvqf ndgdatarnk ietylagalk sdrpthtm
//
LOCUS       WP_008571070             713 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor family protein [Xanthomonas].
ACCESSION   WP_008571070
VERSION     WP_008571070.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..713
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=79114
     Region          46..713
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mstfrlhala iaiaastltl pqlarasdtp ttdaldasgg gtpiraldai qvqgsllgrs
       61 kpddvqryag srqvidreql rnggnrsldd alqrvpgiki fdetgtgalp qlmlrglyes
      121 rsgrvqvled giplalapyg qtslslfpvg lsqidridiv rggaavqygp nnvggvinlv
      181 skeipsawst tlahkvtagg qgrflqdsal ssggyltdnf gmqvdanrty geywrahsdt
      241 disnlrvrae wwlddtkllk asvqrylvdm dlagalspdd yrrdprqstr pldsfngrtt
      301 raslsyeqll gdwgpmqevr ldwsnfsars srnfivgmrq astetwrsdl ppqlrqtapr
      361 dfrvvgsepr lswsmgdagg vrqqwtagvr avredidflv gnlrlrdglf ttvrdwrfed
      421 ralaaylsna itlpgervti tpglryerld sryfnratgv stlnqtrdvl pgltlgfqan
      481 eqwffyadgq rsmrapqvtq iifgnnldae lawnyeagar yqpnertrvq lggylidfdq
      541 qiqldnttrv frnlgktrhq ggelelqwsp eqlraltlna syayldasqe sgafrglrvp
      601 ytsrnqitlg gtyalghttv alsgyyfska fsdaantvqe naiasvgqlp aymvwntqvs
      661 htlferdgqk fsaslainnl fdrqywfrgv dtspwgrqaa partvtagle ytf
//
LOCUS       WP_008573967             712 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor family protein [Xanthomonas].
ACCESSION   WP_008573967
VERSION     WP_008573967.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..712
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=77139
     Region          22..710
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 msrltllaaa cglfatgats pvlaadpvpp astpiqrlpa vqvdaarvrg vddfdlpasf
       61 tvvaadddnr rgaqvselld gipglvardr qnyaqdtqls irgfgarstf gvrgvrllvd
      121 gipasmpdgq gqlshfnvlg aqrvevlrgp fsalygnssg gvlqlwsadg qpddpwrlra
      181 tygsnatanv gaqllgqqga vhynvaanrf dtdgfrahsr arrdsvnakl gfdlaegrrl
      241 dlvlnyldap daqdplgltr aqftadpaqa tsvatqfdtr ksvrqsqaga iftqqldnqt
      301 lrlmayggqr sveqflaipv avqrnplhsg gvidldsnye gadarwawqs ealgrplqlt
      361 vgtnvdrqrq hrtgyenfvg dtlgikgalr rnqrdevqnv dqfaqlwwqw serwsallgv
      421 rhsdvrfesd dhyivgrnpd dsgkrdysat tpvagivfra dedlrfyasv grgfetptfn
      481 elgyrsdgga glaldlgaat srnyevgskw raqsgaalef avfradtdde lavasntngr
      541 styrnigatr rqgaelswqq pigaaqqlql aytfvdatvr dgyltcassg catptalvas
      601 gsrlpgvprq qlfarwqwqp aqwqlaaesv asgatvvndl aterapgyal vnleasrrwt
      661 taqgalrafa ridnvldrqy vgsvivndgn gryyepgpdr tytvglqwdf gg
//
LOCUS       WP_008574566             364 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Xanthomonas].
ACCESSION   WP_008574566
VERSION     WP_008574566.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..364
                     /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=39575
     Region          22..306
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 msvsampasp salpaadaqv atggrvrdpr idatkaiail lvvfchakgv phgmtlfays
       61 fhvplfflvs gwlaagyast ttgldrrsvg rhvrslllpy vtfyllgyay wlltrnigek
      121 aarwgshpww epivamftgi gpdlyvqppl wflpvmlvtv vsymvlrrll apiliaglal
      181 ivawfwmnwf ptqhvriffg ldvlpvslcf yalgallihv sprlptslvg salatvvlgl
      241 avawlavang ridvnmlefg rnhalflvsa llgslmvica arlvqswawl qwigrntlli
      301 lcthmlvffv lsgvaalagg fggarpglgw avfvtlfala asvplrwilm rfapwalgar
      361 rvaa
//
LOCUS       WP_008577777             669 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Xanthomonas].
ACCESSION   WP_008577777
VERSION     WP_008577777.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 669)
  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   3  (residues 1 to 669)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..669
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=70980
     Region          3..662
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msmdlqrfha tffeesregl dameagllsl eegnrdpeii nsvfraahsi kggaatfgfd
       61 avaglthvle tlldelrsnk rqlepnavda mlgsvdvlra llreaehgtp adpaavkavh
      121 trlnavlage apaaaavakp keeepeawhi gftpapslfm sgndplriir elehlgplqi
      181 aarlermpgf enidpleayl awdlgligki prskiedtfa wvvddceldi rpmavpgppp
      241 slavdapaaa pvaavaaapg aaaepaaaaa tpakaaaaea essirvsvdk vdalinlvge
      301 lvitqamlkq vstgldpaha eqlfagldll erntrdlqea vigvrmlpvd avfrrfprlv
      361 rdlssrlgkq vrlrtigest eldkglieki adplvhlvrn sidhglempd arrasgkdet
      421 gtitlaashq gghivievsd dgrglnraki lekaaergia vpdnptdaqv wdlifapgfs
      481 tadavtdlsg rgvgmdvvrr niqglggevq lesnagsgtr vlirlpltla ildgmtvsva
      541 getlilplsy vlealqpape dvramagdgr vlrvrgeylp ilsltnyygf ggqqsskesl
      601 vvvvegdgqk ialevdellg qqqvvvknie nnyrripgvs gatilgdgrv slivdigglv
      661 rslkvpqaa
//
LOCUS       WP_008579538             224 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SPOR domain-containing protein [spotted fever group].
ACCESSION   WP_008579538
VERSION     WP_008579538.1
KEYWORDS    RefSeq.
SOURCE      spotted fever group
  ORGANISM  spotted fever group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="spotted fever group"
                     /db_xref="taxon:114277"
     Protein         1..224
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25240
     Region          143..215
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 minnifikif lvflicvsai yfgyqyyqns kpvitiypde lptkikpsii ennqiaavhs
       61 tiyenliakd tniktvkllp dpekpmnidf rnqsqsdesf deisnliali epsnnaknet
      121 dlniiklekg skdkvsnakn cknnesykvq lgsvkseaea vqegerikkk fpkilknvvi
      181 ttkkvkyedg kffylilagd ygslsqakgv ckklaynkqs cvlk
//
LOCUS       WP_008580309             407 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [spotted fever group].
ACCESSION   WP_008580309
VERSION     WP_008580309.1
KEYWORDS    RefSeq.
SOURCE      spotted fever group
  ORGANISM  spotted fever group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 407)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="spotted fever group"
                     /db_xref="taxon:114277"
     Protein         1..407
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=47274
     Region          170..399
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mikiamseli tdykdlqdei dklekgvcfa crlvnydeie fieqdkhfii edldqiiedv
       61 skelnifskf kkikkdrilf ilnttdsdli knfarklylf sqlyineqkp aiymncyias
      121 ikfpkvsnna keiektlnml lsqnnnyyyr eyssiehdle nirksnlqln llrqalakkt
      181 mrftyqpiid rntmkihyye cllripdeng vyisvgpiip iaedkglifi idqivlemtv
      241 nelarnpnlm lavnisnigt sdealweiae nllkahnvrd hliieitets fnenydkitl
      301 finklrkygc kfalddfgsg ftsfkqlqsl pidiikidgk yvrsitsdvq sryfverlik
      361 isedlgietv aefvengeia kflidlkvgg lqgnfyseak fdrvdev
//
LOCUS       WP_008581726             305 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Niabella soli].
ACCESSION   WP_008581726
VERSION     WP_008581726.1
KEYWORDS    RefSeq.
SOURCE      Niabella soli
  ORGANISM  Niabella soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 305)
  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 305)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Niabella soli"
                     /db_xref="taxon:446683"
     Protein         1..305
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33412
     Region          42..301
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mnrrsfvknn vltatalgmg tglwarssgt taaadkpfnl dyaphdgmfa nsagkdfldq
       61 ikymyergfr siedngmtsr tpemqtkige alaklgmhmg vfvlpkggng antlatkkqe
      121 hidifldgcr ksvetakrcg gklttvvpgd fdrrlpldiq tanvvealrk gaailephgi
      181 vmvleplsdt pdlflrtsaq tyaickavns psckilydiy hmqknegnli tnmglaweei
      241 gyvqigdnpg rkepttgein yknvfkwlhe kgykgilgme hgisqpgkag edrliaayre
      301 sdafm
//
LOCUS       WP_008582917             299 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Niabella soli].
ACCESSION   WP_008582917
VERSION     WP_008582917.1
KEYWORDS    RefSeq.
SOURCE      Niabella soli
  ORGANISM  Niabella soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 299)
  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 299)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Niabella soli"
                     /db_xref="taxon:446683"
     Protein         1..299
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33109
     Region          47..293
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mekknptrrs vikalaltta magnvnlwaa gtaqkkkeam klkgninhsv cqwtfgkmpl
       61 delclnakkl glgaidllap kdwptlqkhg licsmcyipg kvsltdgfag tefhaglird
      121 yeegiplvak agyknlicfs gsrrgmddet gfkncvdglk kilplaeknk vtlvmellns
      181 kvdhhdymcd htawgvelck rlgsenfkll ydiyhmqvde gnvianirqh heyiahyhta
      241 gvpgrhelnd kqelyypaim naivatgfkg hvaqefiptg ktveeklqal kdaitvcdv
//
LOCUS       WP_008583381             157 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Niabella soli].
ACCESSION   WP_008583381
VERSION     WP_008583381.1
KEYWORDS    RefSeq.
SOURCE      Niabella soli
  ORGANISM  Niabella soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Niabella soli"
                     /db_xref="taxon:446683"
     Protein         1..157
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17388
     Region          8..156
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 maedllinkg tkeeqyqall pqiaaliege pdlianlsns aaalkeqfnw wwvgfylvkn
       61 delvlgpfqg pvactrikkg rgvcgsaweq aqtlvvpdve qfpghiacss lskseivvpi
      121 irdnsvmavl dvdsehlnhf detdqyyleq lvkllsf
//
LOCUS       WP_008586365             355 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Niabella soli].
ACCESSION   WP_008586365
VERSION     WP_008586365.1
KEYWORDS    RefSeq.
SOURCE      Niabella soli
  ORGANISM  Niabella soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Niabella soli"
                     /db_xref="taxon:446683"
     Protein         1..355
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=39724
     Region          139..289
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mfsskalfrm allmavlysc gtsqparrnv lspgapgsvd nrsgkhpsqt vftkpnqitk
       61 rqqeeerkki nttverreep aagsgdtala nasykspsyy kyitdsiqrt sakasyyrst
      121 eslfkqmavv pnpqnpavna qwyttvnfda rkpnfvilhh taqtsaeqtl ftfsitrtgv
      181 sahfvvgrdg ltyqmlneym rawhagksrw gaitdmnscs igieidnnge epfsepqves
      241 llkllgylkn kfgipqanfi ghadiapgrk ddpskyfpwk rladagfgyw ydstnlqqpp
      301 adfnallalr vigydvsnpa taiksfklhf vqtdttpvls dydkkilynv ylnym
//
LOCUS       WP_008586799             130 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Niabella soli].
ACCESSION   WP_008586799
VERSION     WP_008586799.1
KEYWORDS    RefSeq.
SOURCE      Niabella soli
  ORGANISM  Niabella soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Niabella soli"
                     /db_xref="taxon:446683"
     Protein         1..130
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=14406
     Region          21..125
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(45,77..78,80,106)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(45..46,54,57,59..60,62,65..66,68,77,82,89)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 msatkksrnd eklkpvrpsg ktddtifdli yaiarqiprg rvtsygaiak aigsgksari
       61 vgwamsnagr vkpkipahrv vnsmgllsgk hafktitymq elleregvkv kndkvmdfkt
      121 kfwnpleelf
//
LOCUS       WP_008589568             781 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Salimicrobium jeotgali].
ACCESSION   WP_008589568
VERSION     WP_008589568.1
KEYWORDS    RefSeq.
SOURCE      Salimicrobium jeotgali
  ORGANISM  Salimicrobium jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Salimicrobium.
REFERENCE   1  (residues 1 to 781)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 781)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 781)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..781
                     /organism="Salimicrobium jeotgali"
                     /db_xref="taxon:1230341"
     Protein         1..781
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=88308
     Region          11..781
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkkpgwkril trtaviagvl ilaaalfiiv fiqrtlpdte gelklealss evtvlrdeeg
       61 vphieaesve dlymaqgyvq aqdrllqmel srrqasgels eligsstveq dkffralglr
      121 raaeaslkey seegkaalea fasgvnayid kadaenrlpp aftllqakpe kwtpvdslti
      181 gkfmahdlgg hwerqafqyy amnnfseeka yevmahypen kpavlddvnl diagdfteav
      241 mpnpfngsnn wvvngertes gkplladdph lgiaspsiwy qmklsapshn vsgvifagvp
      301 giilghnddv awgvtnvgpd vqqlyvekrn penreqflfe gkwedavvhq epikvsgget
      361 ieyevvetrn gpiinefaeg agegealsmr wtahdpskel eailninqas nweefekgle
      421 dfhtpaqnfv fassngtiay kangkipvyd npddaglplr gwkeedqwkg fipfdelptv
      481 vnpdrgwiat annkitteey pyhitnnwaq pyryeriaem leeddavtve dvkkmqmdvk
      541 nlqaeefvpf fveemnennl taeeeealel lkewnyednk eapqpllfhh wlneiedrly
      601 asipddidsl fhgkaqttde ifrmeregke sawmeeaggs gevitqafrd sfnklqedyg
      661 knpeewawgd yhqvefthpl sniafldkfy nrkeplpvsg srvtvraagy ngngkvdhga
      721 swrfildtde mdkgyhivgp gqserfnskw yhnqysdwvd gdyhgtllde degeklilsp
      781 e
//
LOCUS       WP_008590223             207 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Leptospira licerasiae].
ACCESSION   WP_008590223
VERSION     WP_008590223.1
KEYWORDS    RefSeq.
SOURCE      Leptospira licerasiae
  ORGANISM  Leptospira licerasiae
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Leptospira licerasiae"
                     /db_xref="taxon:447106"
     Protein         1..207
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=23425
     Region          6..206
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mseekplrlv lamagasgsi yaarflralm eipgetwfvp spasirvfke eyetnvqtge
       61 dvlefvrkkw dpkqihkfhl rkfedigadi asgsniwegm vvlpcsmktv aairtgiten
      121 lieraadvtl kerrklilvp retpynrihl enmlalhdag aiiapaspgf yqmpksledl
      181 gdfmatrifr llgreidlyp rwnpekn
//
LOCUS       WP_008592057             350 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Leptospira licerasiae].
ACCESSION   WP_008592057
VERSION     WP_008592057.1
KEYWORDS    RefSeq.
SOURCE      Leptospira licerasiae
  ORGANISM  Leptospira licerasiae
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 350)
  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 350)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 350)
  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   4  (residues 1 to 350)
  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 350)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Leptospira licerasiae"
                     /db_xref="taxon:447106"
     Protein         1..350
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40186
     Region          <163..350
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          262..345
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mfetsslvqy lkaatiaqlg flilnflirv kfsvqsllgs lfnssliayf icpwldhsth
       61 ifililvhtg cfsvsvlfyl fvsslfedef rlkirhavlf lslnifcfyv fvasdirnqv
      121 sifskvlfsl pqvfylglil ftlgkvlkdk nvdlmesrre frvvfswvtg lysisvvlme
      181 vitkdagysv qldlinssfi fvlvffisfr ifqfrdnifp dgeiqkeeea eepldegllk
      241 kldsllkdqk vflqenltil alakqlnvpe kkvrrlinkg lgyrnfnefl nhfriqeakf
      301 ilsdpgkndl qvlriamdlg ygslapfnra fketvgmtps dfrkqnssak
//
LOCUS       WP_008590586             640 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Salimicrobium
            jeotgali].
ACCESSION   WP_008590586
VERSION     WP_008590586.1
KEYWORDS    RefSeq.
SOURCE      Salimicrobium jeotgali
  ORGANISM  Salimicrobium jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Salimicrobium.
REFERENCE   1  (residues 1 to 640)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 640)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Salimicrobium jeotgali"
                     /db_xref="taxon:1230341"
     Protein         1..640
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=73636
     Region          43..640
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mfsflkkksd aeetrekgyn pfllahiqpq ggikfhetft rkgdgyevcv hvysfpknvs
       61 dfwlepifnm envittmdiv sddrykvrdg lnkgmaeqss rminekdnag iieaqnnydd
      121 lrqlynqvse egeiikrvhl rhyvsaptre eledkvkvvl stlqdenfrg siflneqefe
      181 wkslltnyte qstyrnkreg hpipalglag gfpfhftsln dpygtfygtt ltggnvvfdl
      241 fhrdqqrksy ngvmvgamga gksttlkkim ldnaikgykv rtfdvtgefv eltealggkq
      301 ialdgsdgvi nplqvyrtae deytsftqhl sklttfykfl apeandselk eyenllrkly
      361 eklglwndds ksnitelsvh eypiftdfla fieeqlyeni kegkqkekls qerkrrlesi
      421 elnirnlvet yahlfngvst iehfdeqqvv tftlrglsqm raevfqaqlf nvlnllwdsm
      481 ltngspqfda ynrgelafed avrylilmde ahhiintkkk sesaldfltk fsrearkyfg
      541 allyashtir dfvpegsdqs mveeikklfe ltqykiimqq dsnnlemmqq ifmgqlsqse
      601 lkdipylqtg etmlsirave nirfkvevsd eelalfggga
//
LOCUS       WP_008593380             659 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Nitratireductor pacificus].
ACCESSION   WP_008593380
VERSION     WP_008593380.1
KEYWORDS    RefSeq.
SOURCE      Nitratireductor pacificus
  ORGANISM  Nitratireductor pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Nitratireductor.
REFERENCE   1  (residues 1 to 659)
  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 659)
  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 659)
  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 659)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Nitratireductor pacificus"
                     /db_xref="taxon:1231180"
     Protein         1..659
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=68745
     Region          15..609
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mtvdtdtqta itatwekrlv gglagaltiv avlqaadlps rlgysyyteq flaivlglsl
       61 alvflvrgsr aaeeggpvrs gpvdwalsal gltlsfyval aypslvsrtm mlpwdalivg
      121 talfllvleg lrravgwtlv vvvlviagyg llghlvpgal qtrevqpqrm avylafdpng
      181 llgltlnvaa tvvvafvffg qlllrsggad ffndialasm ghrrggaaki sivasglfgs
      241 isgvvvsniv atgivtirlm iqsgfrrtta aaveavastg gqiappvmga vaflmadilq
      301 rpyteivvaa ivpallyyva lfiqvdllaa kqrikqiege dipsasrvms rgwvfalpfa
      361 avvialfwfn qraetaalwg saaalliglt lgygktrmsl rdlwdgavet grsitdiimi
      421 saaagfiigv lnvtglgfav tfalvglgkg slfllllisa avclvlgmgm ptvgvyllla
      481 vliapslvqs gvdpiaahff ifylgmmsmv tppigigaff aatiakaspm atawesmrlg
      541 wtayivpflf vfspalllig epvevalava taiggvyais aafvgwlhcp lgmiqrilta
      601 aagvalllpp giggeatlwv naagllalls lrflgksths patiaepdaa rpeastkrv
//
LOCUS       WP_008593985             198 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Leptospira licerasiae].
ACCESSION   WP_008593985
VERSION     WP_008593985.1
KEYWORDS    RefSeq.
SOURCE      Leptospira licerasiae
  ORGANISM  Leptospira licerasiae
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Leptospira licerasiae"
                     /db_xref="taxon:447106"
     Protein         1..198
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22204
     Region          51..195
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mktesqelkn stenvisslv rqtliasvil llivlvlarf fnervtqvag lfldytgvwg
       61 vglsifvads vhvffppdtf lilavaakmp dfwviffasf gsllaggcsy sqgrfllpkl
      121 tvfskfirnh eeklevyvkr fgfwavvlaa ltplpyswts vaagvmkmrl dhffaaalfr
      181 iprfilyyyl ikggwigi
//
LOCUS       WP_008594116             404 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Nitratireductor pacificus].
ACCESSION   WP_008594116
VERSION     WP_008594116.1
KEYWORDS    RefSeq.
SOURCE      Nitratireductor pacificus
  ORGANISM  Nitratireductor pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Nitratireductor.
REFERENCE   1  (residues 1 to 404)
  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 404)
  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
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 404)
  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   5  (residues 1 to 404)
  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   6  (residues 1 to 404)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 404)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 404)
  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 20170230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Nitratireductor pacificus"
                     /db_xref="taxon:1231180"
     Protein         1..404
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41818
     Region          <15..112
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          75..372
                     /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 mndaprisrq fslcmvmeai vhcgpisras vakqtglskq tiseiarqle ddgwiretgr
       61 tsghvgrsav tyeivpdaac iatidlggtk vraaiadlsc qvlaevtept dergglhvvr
      121 qiarlcreaa ehngiayekl rmavvgvpgv pdpqhgrvvm apnvsgfdtl dvkaalgael
      181 gveillendv nlaaigehwi gsatgvddla yialgtgiga gvmvggtlvr gfgnaagelg
      241 flpfgtdpfe aeslkvgale rvtgtvgirr ryqeiagrgl dvpgifdaag kgdaaalqvl
      301 eetaryvara vasicaitnp gkvvlggsig graelvnrvr eflpqcfpyp veigvselgs
      361 rvaivggaav glthlhttlf aggvpgaeis lppakvvklv eaaq
//
LOCUS       WP_008594432             129 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Nitratireductor pacificus].
ACCESSION   WP_008594432
VERSION     WP_008594432.1
KEYWORDS    RefSeq.
SOURCE      Nitratireductor pacificus
  ORGANISM  Nitratireductor pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Nitratireductor.
REFERENCE   1  (residues 1 to 129)
  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 129)
  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   3  (residues 1 to 129)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Nitratireductor pacificus"
                     /db_xref="taxon:1231180"
     Protein         1..129
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14522
     Region          18..117
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mtphhdvsal nranarrmrk tmteaearlw nalrahrlmg lsfrrqmpva gyivdfacpt
       61 rkivvevdgs qhggsahdqs rdaalaalgw tvlrfwnddv erslddvcqh ilavvqefee
      121 drvgsevkr
//
LOCUS       WP_008594528             367 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Leptospira licerasiae].
ACCESSION   WP_008594528
VERSION     WP_008594528.1
KEYWORDS    RefSeq.
SOURCE      Leptospira licerasiae
  ORGANISM  Leptospira licerasiae
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 367)
  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 367)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 367)
  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   4  (residues 1 to 367)
  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 367)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Leptospira licerasiae"
                     /db_xref="taxon:447106"
     Protein         1..367
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42236
     Region          131..356
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          268..351
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 misqitdilh lfclsnlifi igllgwryfy dlririaggf sfgivcyiil sldpdlkipy
       61 siriflfagl islpfffwmi slaifedhfe ikywywllll skvgvsawsv ypvldlinmr
      121 gpivsetvla hiiiptllsl gfvvaaiiri ysgrkddlve trrrlrevhi lmtgsvitfn
      181 mfshlilrgk vlseildlan vilawglila fmylvfelke glvdprpeel edkeekavya
      241 dpalkkklvs afeetklyrk dgltigqlae dlevqeyklr rlinqamgfr nfpdflnryr
      301 iqeaceilld sgkdeipiir vamdlgyqsl gpfnrafkel tgvtptefrr nrgrdeslkn
      361 tadfeis
//
LOCUS       WP_008595745             399 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Nitratireductor pacificus].
ACCESSION   WP_008595745
VERSION     WP_008595745.1
KEYWORDS    RefSeq.
SOURCE      Nitratireductor pacificus
  ORGANISM  Nitratireductor pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Nitratireductor.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 399)
  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   5  (residues 1 to 399)
  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   6  (residues 1 to 399)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 399)
  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 15726307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Nitratireductor pacificus"
                     /db_xref="taxon:1231180"
     Protein         1..399
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40917
     Region          22..>92
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          84..388
                     /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 mkitsprriv gsnaertrlh nrqvvlghvs eqqpvgrael arisglstqa vsniiaelve
       61 dgflaeagrq vagrglpalq yrlnghgaaa lgievrpdam fgalvdlege tlfttrialt
      121 dsapasvaaa areiragalv arpmknqrll gagvvmpgpf gnvgisgagq salqgwgetd
      181 atalfeeale tavivendat aaavaervrg vasglrtycf iyfgaglglg mvadgevqrg
      241 afgnageigh vvvtpggrqc acgnrgclet yasriaarte laaagielas asdierlyhe
      301 nnpalmawld aaaaplsqai gmienlfdpe tvilggampn avldhliggl slaggsvavr
      361 pgrktprvmr gacgrltaal ggaalvihdt itpriaakt
//
LOCUS       WP_008596292             706 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Nitratireductor pacificus].
ACCESSION   WP_008596292
VERSION     WP_008596292.1
KEYWORDS    RefSeq.
SOURCE      Nitratireductor pacificus
  ORGANISM  Nitratireductor pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Nitratireductor.
REFERENCE   1  (residues 1 to 706)
  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 706)
  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 706)
  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 706)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Nitratireductor pacificus"
                     /db_xref="taxon:1231180"
     Protein         1..706
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=74540
     Region          30..696
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mtniqqgqae spaapellet ghgefgtdqm grilfwiava fsayqiataa hvlnlpsqvq
       61 rayhvgflml lvfplvvqar dkgralkala walaaagvav alyqhieykp lllragdplp
      121 ldivfgvval vtvfaaayvl mgpalpiisg aflayclfge ylpaplnhrg ydfaqvidhm
      181 aygtegiygi piyvsatyif lfilfgsfle ragmirlftd vslglvghar ggaakvsvis
      241 sglmgtisgs gvanvvttgq ftiplmkrfg yraafaggve stasmggqim ppvmgavafi
      301 maetlgieyy evvkaaiipa llyfasafwm vhleagkygl fglprselps praalrrgwy
      361 lilplavlvy llftgytplf agtiglsltv llilggsval glpsqvlrii fwvglgvvaa
      421 sffrfgiqpi liaavllila nvfvdggrrt lalcrdslae gaktalpvgv acavvgiiig
      481 tmtltgvant fgqfivsvge tslflslvlt mitcivlgmg iptipnyiit stiagpalle
      541 lgvplivshm fvfyfgilad ltppvalacf aagpiakesg lkismeaikv aaagfvipfm
      601 avytpalmlq dggplaeaig yypavayivf ktlvaialwg aavigflrar laiwerllaa
      661 vaaftlvaal pitdeigfal aalfagvhwy rtrgraaepa vertpe
//
LOCUS       WP_008596707             344 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Nitratireductor
            pacificus].
ACCESSION   WP_008596707
VERSION     WP_008596707.1
KEYWORDS    RefSeq.
SOURCE      Nitratireductor pacificus
  ORGANISM  Nitratireductor pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Nitratireductor.
REFERENCE   1  (residues 1 to 344)
  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 344)
  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 344)
  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 344)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Nitratireductor pacificus"
                     /db_xref="taxon:1231180"
     Protein         1..344
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=37277
     Region          1..338
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkkrlvaaal aatmlstapa iaesfdlqsv fglqvpsigp spmkwaervk lmtggevein
       61 vhgagdfvpp fevfgavssg aipmgfdwig ywaetipvan ligsmpfgps pdvalawmfe
      121 gggleiiqka ydphgvkvip chlvvpeagg wfnkeintve dfkglnmria glggktlakl
      181 gantqlvpag eifvsletgr idatefsapq ldlgfgfqkv vknyyfpgwh qpsswdsiii
      241 nmdvwngfse dtqnimveac kaniaynlgd qlnaqaeaia tireagvnvr rfpdevlmgi
      301 reqaeavlte eagkdpifke ayesltaymd rvgewerlqa iphk
//
LOCUS       WP_008596732             363 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Nitratireductor
            pacificus].
ACCESSION   WP_008596732
VERSION     WP_008596732.1
KEYWORDS    RefSeq.
SOURCE      Nitratireductor pacificus
  ORGANISM  Nitratireductor pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Nitratireductor.
REFERENCE   1  (residues 1 to 363)
  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 363)
  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 363)
  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 363)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Nitratireductor pacificus"
                     /db_xref="taxon:1231180"
     Protein         1..363
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39122
     Region          1..354
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkrrqflqta giagvatgla apaiaqdkrt wnmvtawpkn lpgpgvaaqm ladritalsg
       61 grlevklhaa gelvpgngvf davsegtaql yhavpsywgs ksrgillfgs qpfglradeq
      121 lgwlihgggq alydeiygrf glkpflcgns gpqwqgwfrn einsvddlkg lrfrttglas
      181 emcaklgmav qamgggdmfq glqsgtidag efigpwtdsa lgfyqvakny ywpgvgepss
      241 aeecavnkaa ydelpedlqq avayacesly npvwteystk haaalkqlva eqgvqvrqlp
      301 edvivamgna ageviaelre dddelvkriv esflayragi seymvyadng qmnaraldyk
      361 ygg
//
LOCUS       WP_008600242             794 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pacificimonas flava].
ACCESSION   WP_008600242
VERSION     WP_008600242.1
KEYWORDS    RefSeq.
SOURCE      Pacificimonas flava
  ORGANISM  Pacificimonas flava
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingosinicellaceae; Pacificimonas.
REFERENCE   1  (residues 1 to 794)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 794)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 794)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..794
                     /organism="Pacificimonas flava"
                     /db_xref="taxon:1234595"
     Protein         1..794
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=86037
     Region          12..792
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mldrrsffig taavlsalpe laraqgdvvr srktvpgaaa tieiiddewg iphiraqskp
       61 daffgqgyvv ardrmfqidf ghrarmgrla eafgegfadr delarlffyq gdvdaalaqv
      121 padvlactea yvagvnarva evesdpallp leyrilglsp lrwtlrdlvv argasignmd
      181 deirrarlaa ldlleldalt tplrpkwtls ipdgldtaav seadlgvlra srrglpfads
      241 vpatdadrra fdlerdqags nawtvagsrt atgrpiland phlgigsfsp rhiahmtapg
      301 ldvmgggapg lpgimqghtd yfafgrtnfh idqqdlfile thpddperyr haggwksfdr
      361 veetipvagg tprqvvhrys vqgpvvshdp arrrassvas vgmmdgpggi famvainlap
      421 dweglktafe lhpsptnfhy adrdgnhgwq vigyaplrrq gdgltpvpgd grydwtgrik
      481 ydqlpsaynp pagwfasanq nnipedypfe ahplafsfrd pyrydrvsev lesqtrhsia
      541 dsvalqhdvl stparqlaam mpaaapgdag raatmlrawd griagnsgaa alheilwkel
      601 drrlreavvp arageliesl spsvllgfla hpdarlgrdp aaardallqg alerawaeav
      661 rlmgddpaaw rwdtlhrvei khplsdipai aaafpviegg gsggdaytpm arwvpsssyh
      721 vgggasylmv vdvgewdnsv mlllpgqsgd prsphyddfy apwiegrmqp mtfsaakvda
      781 sarsrttltp gapd
//
LOCUS       WP_008600852             167 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Pacificimonas flava].
ACCESSION   WP_008600852
VERSION     WP_008600852.1
KEYWORDS    RefSeq.
SOURCE      Pacificimonas flava
  ORGANISM  Pacificimonas flava
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingosinicellaceae; Pacificimonas.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Pacificimonas flava"
                     /db_xref="taxon:1234595"
     Protein         1..167
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=18836
     Region          60..136
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 madffgsdtd rrggynpygg rdrdmsgrgs grrgnrgrdw dddesrgrrg ggrvsgdrli
       61 asdrvegtrv ydrrgnrlgt ienfmvdkrs ghveyailsf ggflgmgdrh yplpwdelty
      121 dqdeggyvvn vteqdleeap shragqnvry drnysndirs yyggmgw
//
LOCUS       WP_008602015             196 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Veillonella].
ACCESSION   WP_008602015
VERSION     WP_008602015.1
KEYWORDS    RefSeq.
SOURCE      Veillonella
  ORGANISM  Veillonella
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Veillonella"
                     /db_xref="taxon:29465"
     Protein         1..196
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22080
     Region          3..175
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mntleciktr hstrkfkadq lsrelidqvl dagrrapsgg ntqlthfmvi tnqdmlnelv
       61 tlvqeeygkm pitentlpym vniikmsaeg kfvfnynapv livlasqany annfadvsca
      121 mqnmmlacne lelgscwvnq irhlqdneri qakmrelgls edekvyasla igypdlpngl
      181 nrreikakgy pvtyid
//
LOCUS       WP_008602358             545 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Pacificimonas flava].
ACCESSION   WP_008602358
VERSION     WP_008602358.1
KEYWORDS    RefSeq.
SOURCE      Pacificimonas flava
  ORGANISM  Pacificimonas flava
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingosinicellaceae; Pacificimonas.
REFERENCE   1  (residues 1 to 545)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Pacificimonas flava"
                     /db_xref="taxon:1234595"
     Protein         1..545
                     /product="amidohydrolase family protein"
                     /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=60466
     Region          56..516
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mkngnartrf lagfigaala gtllaapvsa qlgtvelkpn psstqtygdl aqgpykslvl
       61 rnvmvlpghg gpargpydil ingnvisklq rynphapnae enrltgerii egdgkyvmpg
      121 mlnlhlhlre delpldyiyy lqlatgvtsv gpaeservqp tladvkanri laprlfpiyg
      181 wgsltdysde elrdpamaee vaeamaakgv rqvylnqlaw drdlfgaaae avdaagglta
      241 lhvqpsstsq inaldaaklg vtmivhhygy aesaldrgvq dyprdynffd enarfreaar
      301 vweevgrnpe trerllgdvv delietgvim qpnratyean rdivraqglp whekythqql
      361 wewhlpnpen haafqfdwts qdeaswsyly rlwgdlifef nkkggmiayg tddnfqwstg
      421 gfgnirelql lleaglhple vlqaatynsa ktlkeprlgl vqegyiadll lvdgnpaedf
      481 kylypfgsik mdesrqmyrt qgivhtikdg ivinnaavmd evarivaesk tgaepdivtt
      541 pfvte
//
LOCUS       WP_008603272             157 aa            linear   BCT 20-JAN-2025
DEFINITION  division/cell wall cluster transcriptional repressor MraZ
            [Pacificimonas flava].
ACCESSION   WP_008603272
VERSION     WP_008603272.1
KEYWORDS    RefSeq.
SOURCE      Pacificimonas flava
  ORGANISM  Pacificimonas flava
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingosinicellaceae; Pacificimonas.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Chen,S., Jancrick,J., Yokota,H., Kim,R. and Kim,S.H.
  TITLE     Crystal structure of a protein associated with cell division from
            Mycoplasma pneumoniae (GI: 13508053): a novel fold with a conserved
            sequence motif
  JOURNAL   Proteins 55 (4), 785-791 (2004)
   PUBMED   15146477
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449500
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Pacificimonas flava"
                     /db_xref="taxon:1234595"
     Protein         1..157
                     /product="division/cell wall cluster transcriptional
                     repressor MraZ"
                     /GO_function="GO:0000976 - transcription cis-regulatory
                     region 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=17813
     Region          6..142
                     /region_name="MraZ"
                     /note="DNA-binding transcriptional regulator and inhibitor
                     of RsmH methyltransferase activity [Translation, ribosomal
                     structure and biogenesis]; COG2001"
                     /db_xref="CDD:441604"
ORIGIN      
        1 mdaavfqgnw lntvdakgrm sipaafrdvi qqragdrrvv laphrgdwdc learttdhva
       61 dinratadry aadevspeed marlrafsls qqvqfedtgr vvipedlrdf adldgevlli
      121 glgnsfqiwn pdlfleqted ervkrfirrk lekarak
//
LOCUS       WP_008607783             354 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Alishewanella].
ACCESSION   WP_008607783
VERSION     WP_008607783.1
KEYWORDS    RefSeq.
SOURCE      Alishewanella
  ORGANISM  Alishewanella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Alishewanella"
                     /db_xref="taxon:111142"
     Protein         1..354
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39653
     Region          1..350
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msicieqvrk sfgnfvaldn vnlniktgel tallgpsgsg kttllriiag leqadsgiir
       61 fnseditgqh vsergvgfvf qhyalfkhmt vfenvayglt vkpkkfrpsk aeiakkvnnl
      121 lelvqlgwta drypsqlsgg qrqrialara lavepkmlll depfgaldak vraelrrwlr
      181 rlhdeihvts vfvthdqeea levadrivvm nkgrieqegt peqvydnpan pfvyeflgnv
      241 nlfharvkqg qssigqlrvp speytnseeq dglayvrphe idvfnlpqpd aikvkldlvt
      301 ivgpsvrlev laesdqqlih velpkeqfkq lnlkqgeqaw ilpryskvfl gegi
//
LOCUS       WP_008610004             720 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Alishewanella].
ACCESSION   WP_008610004
VERSION     WP_008610004.1
KEYWORDS    RefSeq.
SOURCE      Alishewanella
  ORGANISM  Alishewanella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae.
REFERENCE   1  (residues 1 to 720)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 720)
  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   3  (residues 1 to 720)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..720
                     /organism="Alishewanella"
                     /db_xref="taxon:111142"
     Protein         1..720
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76539
     Region          5..708
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msfdmdedil qdflveagei lellqeqlve lennphdtal lnaifrgfht vkggagflsl
       61 telvdachga envfdilrtg krsitpelmd vilqaldvvn emftevkarq pltpadpqll
      121 aalhfysepe tpgeaapqaa kaapavtapv apqvtkvqqp taspdsddvd sitedeferm
      181 ldelhgsaap grtevaasap aapvsagddi tddefealld qlhgkgsfkp evpaapavta
      241 tepaapaaka deitddefea lldqlhgkgk apvtpaaaka evpppapvaa paaapvkate
      301 apvapaagna aaadkgavaa ettvrvdtkr ldqimnmvge lvlvrnrlvs lsgsaqneem
      361 skaianldvv tadiqgavmk trmqpikkvf grfprvvrdl arslkkdidl vlegeetdld
      421 knlvealadp lvhlvrnsvd hgielpdvrq aagksrtgvv klaaqqagdh illtiqddga
      481 gmdpeklknl aikrgvidad taarmsdtda fnlifapgfs tkeqisdisg rgvgmdvvkt
      541 kitqlngtvh ihsklgegtl leikvpltla ilptlmvivg kqtfalplag vseifhldla
      601 ktnivdgqlt ivvrnkaipl fylehwlvkn sdkklrraqg hvvivqigqq qvgfvvdqli
      661 gqeevvikal dallqgtpgm agatitsdgg ialildvpnl lkhyakkski kfeqfkqlhg
//
LOCUS       WP_008610452             671 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Alishewanella aestuarii].
ACCESSION   WP_008610452
VERSION     WP_008610452.1
KEYWORDS    RefSeq.
SOURCE      Alishewanella aestuarii
  ORGANISM  Alishewanella aestuarii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Alishewanella.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Alishewanella aestuarii"
                     /db_xref="taxon:453835"
     Protein         1..671
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=73740
     Region          10..669
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mpgpslkpvt asimlavssg alaqtpeviv itanaqqqrw ldaaasievr alprsgllid
       61 sgqllqgipg lqvdsranfa qdtrlsirgf gsrsafgvrg iylsqdgipi sapdgqgqls
      121 svlldniaei evlrgplavl ygngaggvia lrtateatar agtalavsqq hqqyqlagrq
      181 qlgqhqlsla akhfesdgfr phsaarkqql qglwqtqlsd slsaslrldf aydpllqdpl
      241 sltptqwrad pkqtvsqaqq fdttkstrqr qlslalqqsg hspwqlalwr gerevtqrla
      301 ftgaaitsag gdialdrqyq gvngqyswrl tdvlqstvgg awvssdderq gfvnnfgqrg
      361 dlrrdetnla enrdlfwrlh wqataklsvd aglrytelsy qirdrfiqga npddsgrkny
      421 yqqaaamgln yrlndslswf istglgfeap tlaelaykpe gsglnlalla senrqwesgv
      481 kyaasrarfs vsafsirssd ellvassdng rtsfrnagat arqglefywq qqltpalsqq
      541 valtyldaqf dsaelagkri pgvarldshw qlswqpwltr plflewtsry rdqiaindqn
      601 sdfapaslsf dlslhstqql gqwqvrswlq lqnltdrnnv gavvvnqsng rafesapgrq
      661 lsaginldyl w
//
LOCUS       WP_008612565             474 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Galbibacter orientalis].
ACCESSION   WP_008612565
VERSION     WP_008612565.1
KEYWORDS    RefSeq.
SOURCE      Galbibacter orientalis
  ORGANISM  Galbibacter orientalis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Galbibacter.
REFERENCE   1  (residues 1 to 474)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Galbibacter orientalis"
                     /db_xref="taxon:453852"
     Protein         1..474
                     /product="amidohydrolase family protein"
                     /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=53504
     Region          35..443
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mkylkllrlf avisfnlnaq nnsklennqq enaiyvikdv nvipmtkenk viekativik
       61 enkihsinkt ipensividg kdkwlipgli dmhvhnlass spwviyhtkg plvnydtqnl
      121 mtlyiangvt tvfelgarpe higqrneitr gnvigprmal akviggnksn fiaknpsdgr
      181 navrfakeeg yefikvytwl neetfkavid eadkqnmkvv ghipvafkkk qakdffvphf
      241 gliahaeels kqtddysyek aqefarlake nntwlipnlt nmlsisqqak slqniknlqg
      301 fkyvhplmqs kwltsngyyg aseklieyyt nlydfhfliv kafkeagvpm vagtdagisg
      361 viwgfslhne lkllveaglt neealasatr lgaewleidd kigtietgkf adlillnnnp
      421 lanisntlki agvfvngkwi nknktdimls eienwnnink ekydwkelln slkn
//
LOCUS       WP_008614273             488 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Paramagnetospirillum caucaseum].
ACCESSION   WP_008614273
VERSION     WP_008614273.1
KEYWORDS    RefSeq.
SOURCE      Paramagnetospirillum caucaseum
  ORGANISM  Paramagnetospirillum caucaseum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Magnetospirillaceae; Paramagnetospirillum.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Paramagnetospirillum caucaseum"
                     /db_xref="taxon:1244869"
     Protein         1..488
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=52739
     Region          22..482
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mthqpppdws padtafrapp hnyeaeqall gavmlrgpal devaeivtae hfadpahgri
       61 faamlalaer gakpspvtlq syferdvala eiggvrylal ladcvvstan vvdyarlvrd
      121 madrraliva cqgavgeayd prvdlparai veqleaalte maadaalgvg pqpiggsala
      181 avsridsirr gdrkalglpt glapldrmig glkpgllyvg agrpsmgksv laeniarhvg
      241 glpdgpdvpr grvamfalem tgqdvsdrsl aaetgvplsa ilqgdptdwq feklavaage
      301 mgnlrldidd tpaltaqair ararrikrkh glrlvvvdhl hrmgraglne taeitaitga
      361 lkdmakelhv pvllmaqlnr dlekredkrp mmsdlrqsgs ieqdadvvll lyreqyyler
      421 aepakrpdet qekfndrhar wserceevmg tgdvivakqr qgkigvvrlg fngdfckffd
      481 leaanaar
//
LOCUS       WP_008614512             101 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Galbibacter orientalis].
ACCESSION   WP_008614512
VERSION     WP_008614512.1
KEYWORDS    RefSeq.
SOURCE      Galbibacter orientalis
  ORGANISM  Galbibacter orientalis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Galbibacter.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Galbibacter orientalis"
                     /db_xref="taxon:453852"
     Protein         1..101
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11558
     Region          7..91
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 maeflslcka hnvknlyafg ssitdqfned ssdidlliei dsvdpierge nlmniwdkfe
       61 vffqrrvdll tyvsiknpil kknidstkil iydgkeqkvs i
//
LOCUS       WP_008614873              97 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Paramagnetospirillum
            caucaseum].
ACCESSION   WP_008614873
VERSION     WP_008614873.1
KEYWORDS    RefSeq.
SOURCE      Paramagnetospirillum caucaseum
  ORGANISM  Paramagnetospirillum caucaseum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Magnetospirillaceae; Paramagnetospirillum.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Paramagnetospirillum caucaseum"
                     /db_xref="taxon:1244869"
     Protein         1..97
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10939
     Region          3..97
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mrsiddiigq lrtmqpdlrq ryrlremgvf gsyvrgeqre dsdldvlvef ddgttlldya
       61 glqmelsdal glpvelankk tlkprigrsi laevrtl
//
LOCUS       WP_008615635             236 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein, partial [Paramagnetospirillum caucaseum].
ACCESSION   WP_008615635
VERSION     WP_008615635.1
KEYWORDS    RefSeq.
SOURCE      Paramagnetospirillum caucaseum
  ORGANISM  Paramagnetospirillum caucaseum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Magnetospirillaceae; Paramagnetospirillum.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Paramagnetospirillum caucaseum"
                     /db_xref="taxon:1244869"
     Protein         <1..236
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
     Region          <1..182
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 tavtvnlgtg sasggeaagd vlsgienllg gnaadiltgd aganrlsgaa gndtlsggag
       61 ddilaggags drltggdgad tadysasaaa vnvdltrata qsggdaagdi lagienltgg
      121 vgndlltgdg gantltgggg sdtlnggggd dllvfrasdf pagsggtlad fvyggggadt
      181 ldisavgqnf qllingveqp lpagsheyvd tqgiqgdirf gdnsvihldg vekiiy
//
LOCUS       WP_008616194             522 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein
            [Paramagnetospirillum caucaseum].
ACCESSION   WP_008616194
VERSION     WP_008616194.1
KEYWORDS    RefSeq.
SOURCE      Paramagnetospirillum caucaseum
  ORGANISM  Paramagnetospirillum caucaseum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Magnetospirillaceae; Paramagnetospirillum.
REFERENCE   1  (residues 1 to 522)
  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   2  (residues 1 to 522)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Paramagnetospirillum caucaseum"
                     /db_xref="taxon:1244869"
     Protein         1..522
                     /product="aminoglycoside 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=57449
     Region          215..457
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mrigidfdnt iasydsafrs vaaewgllpe gftggkhqvr evirrlpdge tawmrlqgrm
       61 yghhmplaqp mpgvmdflrr akaggaelvv vshktqyghf dpdrvdlrqa ardwleangf
      121 feliarervy fektreekva riaamdldaf vddleevfre pgfparteac lfaaghqnlp
      181 qgpflafadf saisrhlltp leaaarmrgs pvsglsrang ggnnrlyrve taqgtlalks
      241 ypslaedsrd rlgteftala flgshgvaev pralaaepsd gfalyswieg qpvtgsgegd
      301 idaalafahr lhglreaega qalppaseac lsgmelvaqi swrlerltev apgypelaaf
      361 lerfsaaqar lvdtagrnmd laaelpprhr tlspsdfgfh nalrrpdggl tfldleyfgw
      421 ddpvkltadf vlhpgmnlta vqkerfldga grlygadpaf dlrlrlflpl yalrwcmiil
      481 neflperwvr ralagagdrr aaearqlaka qallsatlea hp
//
LOCUS       WP_008616740             694 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Paramagnetospirillum
            caucaseum].
ACCESSION   WP_008616740
VERSION     WP_008616740.1
KEYWORDS    RefSeq.
SOURCE      Paramagnetospirillum caucaseum
  ORGANISM  Paramagnetospirillum caucaseum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Magnetospirillaceae; Paramagnetospirillum.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Paramagnetospirillum caucaseum"
                     /db_xref="taxon:1244869"
     Protein         1..694
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=75696
     Region          21..694
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mpaqfsrral lcagtalcsi lalasnpapa addsgditev vvtdklqksk lnpnaaeaka
       61 airetaggvd svsaeefrdg rtqtvkdmld fvpgvfaqak wgedsrlsir gsglaqsaht
      121 rgvklmqdgv pfnaadgftd lqqidplsve hvdvwkggna lrygaamlgg ainmtsftgh
      181 taspaqarle lgsfgyrraq issgmalgaw dyyisptrlq sggyrnhsgt dsnrltantg
      241 yrfangaetr iyvnlndirq elnssltmaq franpkmagd nrnfsnntkr diqsmrfgnk
      301 tafqvadwem eagiygaykn lfhpltttvi dqvsedmgtf vrgthehslf glrnqltlgg
      361 nyawghtdak tfgiingtrg tltgksqqqa qniefygedr lyltpavsli aagqgliadr
      421 natdqflsng nssgyrtfta fnpkvgamwq pspdlqvfgn lsraveppii sdlnpsgltg
      481 nfapldpqes vtlelgtrgn hkgwgwdava yrswmkhelq rftlsdnnty tvnadrtihq
      541 gvelglsvpl aqglftgsds eklvwrnsyt lnhftfdgdr qygdnelpgv plhyyrgevr
      601 ythpsgayfg pnlewapqsy hidnantart igyhlwgvkt gwdvnehlsi fadarnladr
      661 ayiaqvnvlp tmgtsgtisp gegravymgv nvkw
//
LOCUS       WP_008618098             690 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Paramagnetospirillum caucaseum].
ACCESSION   WP_008618098
VERSION     WP_008618098.1
KEYWORDS    RefSeq.
SOURCE      Paramagnetospirillum caucaseum
  ORGANISM  Paramagnetospirillum caucaseum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Magnetospirillaceae; Paramagnetospirillum.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 690)
  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   3  (residues 1 to 690)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Paramagnetospirillum caucaseum"
                     /db_xref="taxon:1244869"
     Protein         1..690
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=74702
     Region          9..689
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mstaidpvet fraearelfe qlettlldie adpsdkdlid tafralhtik gsgamfgfda
       61 asafthhven afdlvrkgkl aatkelveva laakdhmrvl ieqpeaappg rseallaqla
      121 giigigpvvs vssndahppe ppperttyrl hfrlarnama mganpllllk elrelgdctm
      181 vtdtdgipml eemdpsgcyl awdgllstdq prsaiddvfm fviddmelsv evvepeakrl
      241 geilverhav sadaldkald qqprlgamlv keglvstdkv aaalaeqkhl kgevekvaka
      301 daadirvqas rldelmdqvg elviaqarlr qlanagndph lkslveeier lsselrdttm
      361 girmvpigsl fgrfrrlvrd lskelgkeia lttsgeetel dktvierlhd plvhlirnsl
      421 dhgveapdir eskgkprqgt ihlsaihsga qvlikitddg agidpvrvra kaeenglipp
      481 gaelsepeif qlilqpgfst aakvtsvsgr gvgmdvvkra idqlrgtidi dstlgsgstm
      541 tlrlpltlai idgllvrvge gryviplsav eecvelsaed drrasgrdfl nirdetvpfl
      601 rlkalfnvvt dpepyqkvvi vstgdarvgl vvdqiigdyq tvikslskih stvqtfsgat
      661 ilgdgtvali idvprlidfg qasesqkkas
//
LOCUS       WP_008619511             347 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Paramagnetospirillum caucaseum].
ACCESSION   WP_008619511
VERSION     WP_008619511.1
KEYWORDS    RefSeq.
SOURCE      Paramagnetospirillum caucaseum
  ORGANISM  Paramagnetospirillum caucaseum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Magnetospirillaceae; Paramagnetospirillum.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Paramagnetospirillum caucaseum"
                     /db_xref="taxon:1244869"
     Protein         1..347
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37566
     Region          2..343
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mievenvskr fgnfaaldqv slrvaqgklv allgpsgsgk ttllrilagl eqpddgrirl
       61 ggidatglgt rdrkvgfvfq hyalfrhmtv aeniafglkv rkganrpska aitekvhtll
      121 elvqleglag rypsqlsggq rqrvalaral aveprlllld epfgaldaqv rkdlrrwlrh
      181 lhdemgltgv fvthdqeeal evadevvvmn kgrieqigtp aeiydspatp fvyrflgnvn
      241 avacrvaggq aqvgglhige gradgpgtaf irphdvevle lspdlpqarv rqvvvlgpvv
      301 raelelaggv tveaelsrdi kdklglrrgl evsvflrkar vfvgenv
//
LOCUS       WP_008620249             297 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Paraprevotella clara].
ACCESSION   WP_008620249
VERSION     WP_008620249.1
KEYWORDS    RefSeq.
SOURCE      Paraprevotella clara
  ORGANISM  Paraprevotella clara
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Paraprevotella.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Paraprevotella clara"
                     /db_xref="taxon:454154"
     Protein         1..297
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34572
     Region          205..284
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 meqamipirv srlsdwkiyg sqwghlrstl drcgvffcra geveleidnt pyiikpgdic
       61 fyvasalvrv lrvggeidgv vvevdvdyil pisnkvlnvq dilfmrdhpc itltdaqcry
      121 vdkllelymr rikegdgqvg sskcrslkve likaggqalf yellmiyytn rpmhpvqrtq
      181 kdiifqrfiv dlfnhyraer evlfyaerqn lsaryfssvv keksgrsvlq wiiqmvisea
      241 kqllecsels ikeiavrlnf ctqsffgkyf kqyvgmspke yrersfyprk evvfdnq
//
LOCUS       WP_008622787             495 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Paraprevotella clara].
ACCESSION   WP_008622787
VERSION     WP_008622787.1
KEYWORDS    RefSeq.
SOURCE      Paraprevotella clara
  ORGANISM  Paraprevotella clara
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Paraprevotella.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Paraprevotella clara"
                     /db_xref="taxon:454154"
     Protein         1..495
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=53758
     Region          3..495
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mlkyivihpa dnvavalqpl eegesitcgs tavkvreqvp aghkvslahi aagqdvikyg
       61 spighateti epgrwvnerm lrtnlkgisd yryqpvpvpc pppdrlrtfs gyarrngevg
      121 irnelwiipt vgcvngvaer larmleketr aegidgiray thnygcsqlg ddhehtrril
      181 rdmalhpnag gvliiglgce nnqpdafral lgdydterir fmvcqheede mesgmkilrd
      241 lyarmvedrr tevpmrklrv glkcggsdgf sgitanpllg cfsdylvaqg gttvltevpe
      301 mfgaetllma rckdetvfrk tvslindfkn yfishgqpvf enpspgnkag gistleeksl
      361 gctqksgtta vcdvleyget lsspglnlls apgndlvast alaasgchiv lfttgrgtpf
      421 gtfvptvkis shtglagkks nwidfnagtl legepmptvl erftsfvldv asgrqtlnee
      481 ngyheiaifk sgvtl
//
LOCUS       WP_008622842             239 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein, partial [Paramagnetospirillum caucaseum].
ACCESSION   WP_008622842
VERSION     WP_008622842.1
KEYWORDS    RefSeq.
SOURCE      Paramagnetospirillum caucaseum
  ORGANISM  Paramagnetospirillum caucaseum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Magnetospirillaceae; Paramagnetospirillum.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Paramagnetospirillum caucaseum"
                     /db_xref="taxon:1244869"
     Protein         <1..>239
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
     Region          1..239
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 aavtvnlgtg sasggeaagd vlsgienllg gnaadiltgd agvnvidgga gndllagggg
       61 adtliggagv dtvsyaasgv alaadlaagt vaggdadgdv isgiesvtgt sfndilagdg
      121 nanrldggag ndslrggaga dslvggtgad tvgyensaag vtvnlsltta qasggdasgd
      181 vlatienaag safadsltgt tgvnlltggg gddvlrglag adtlvggdgs dtasyaaat
//
LOCUS       WP_008624683             447 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Mariniradius saccharolyticus].
ACCESSION   WP_008624683
VERSION     WP_008624683.1
KEYWORDS    RefSeq.
SOURCE      Mariniradius saccharolyticus
  ORGANISM  Mariniradius saccharolyticus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Mariniradius.
REFERENCE   1  (residues 1 to 447)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Mariniradius saccharolyticus"
                     /db_xref="taxon:1245591"
     Protein         1..447
                     /product="amidohydrolase family protein"
                     /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=49608
     Region          23..447
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mktyrylpai vfllllvsfp lyaqntkalv ggtlidgfgg pplrnsviii egerikeigq
       61 vgsteipana eiistegmsv mpglwdmhvh lminghsnyt hwdstyigvf esvimpssah
      121 qllmagvtsa rdlgapleas ikvrdrinkg eipgptiyvs gpfiqkapyp gteafrwgin
      181 gaadarakvk klvdagvdvi klidhdemtf eeakavvdea hkygkpviah shrpdeirig
      241 lkigvdcfeh tglasapeyp adivamiker takmnmgplf wtptveglfn yeytrnnpek
      301 lddpswhlgl pdsiirdira slrfpgrmpy fqltpvrkpt lekkfnqlke sgvvmligtd
      361 sgipmkfhsq stwneldvwv nefgydpmla ikaatywpav amkvdkdygt isegkyadii
      421 tvrgdvlrhv vllqnvdmvi khgkrvr
//
LOCUS       WP_008627860             150 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Paraprevotella xylaniphila].
ACCESSION   WP_008627860
VERSION     WP_008627860.1
KEYWORDS    RefSeq.
SOURCE      Paraprevotella xylaniphila
  ORGANISM  Paraprevotella xylaniphila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Paraprevotella.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Paraprevotella xylaniphila"
                     /db_xref="taxon:454155"
     Protein         1..150
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16559
     Region          7..150
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdamvdfliq ygywgmflaa flaasvfpfs seavmvglql agldpllllv wgtignvggs
       61 mfnysigrlg rmewvekylr vkresvekaq hwmerkgawv ggilcvvpvi gdaisvalgf
      121 mranwlicli sitigklvry ailvytvtlf
//
LOCUS       WP_008628490             255 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Mariniradius saccharolyticus].
ACCESSION   WP_008628490
VERSION     WP_008628490.1
KEYWORDS    RefSeq.
SOURCE      Mariniradius saccharolyticus
  ORGANISM  Mariniradius saccharolyticus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Mariniradius.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Mariniradius saccharolyticus"
                     /db_xref="taxon:1245591"
     Protein         1..255
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28239
     Region          <36..172
                     /region_name="rne"
                     /note="ribonuclease E; Reviewed; PRK10811"
                     /db_xref="CDD:236766"
     Region          183..254
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 meekeqealr rqedkdygfp fvdvrplsst enqksepaqs vdpvaesati epetsvpgsl
       61 snpihferke tqkrnqtpll itlvfmlavi laamayflyf tpaeetvkev aetpqpeamq
      121 evepvvdeva adtvelevpl tlekeeepvk eaaappvtqt qpaptgpigq lhlveskger
      181 piyhlivasl pneriareea qvflnsgrdv wmifpvgdtk nfrlsvgsfg sfksasealp
      241 qakndfgest wilky
//
LOCUS       WP_008630600              99 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Mariniradius
            saccharolyticus].
ACCESSION   WP_008630600
VERSION     WP_008630600.1
KEYWORDS    RefSeq.
SOURCE      Mariniradius saccharolyticus
  ORGANISM  Mariniradius saccharolyticus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Mariniradius.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Mariniradius saccharolyticus"
                     /db_xref="taxon:1245591"
     Protein         1..99
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11163
     Region          4..97
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mktleiplds iqtlcekhhv eklylfgsaa kgtmtegsdv dllvkfkemk tseyfenflv
       61 lknelqgvfg rkidlvelqt lknpvlidsi nqskeliyg
//
LOCUS       WP_008631458             283 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Thermus parvatiensis].
ACCESSION   WP_008631458
VERSION     WP_008631458.1
KEYWORDS    RefSeq.
SOURCE      Thermus parvatiensis
  ORGANISM  Thermus parvatiensis
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Thermus.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Thermus parvatiensis"
                     /db_xref="taxon:456163"
     Protein         1..283
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31246
     Region          1..271
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mepdwkallr vlrahsatfy lgsllfpkea rkgawavyaa crlgdeavdg egggpealea
       61 wwagverayr grplaewekg lawalerwdi pfeaflhmre gfqtdlgpvr lgteaellry
      121 cyqvagtvgr mmapiagggk eaearavklg qamqltnilr dvgedlgrdr vylpsellka
      181 ygvrlsdlea gritpeyral mahlegkara lyreglaglg hlkvgraaia laalqyrgil
      241 dklrlsgydn lgrrahlkaw eralllpkaf laarfpprpe esp
//
LOCUS       WP_008631952             358 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Thermus parvatiensis].
ACCESSION   WP_008631952
VERSION     WP_008631952.1
KEYWORDS    RefSeq.
SOURCE      Thermus parvatiensis
  ORGANISM  Thermus parvatiensis
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Thermus.
REFERENCE   1  (residues 1 to 358)
  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 358)
  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 358)
  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 358)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Thermus parvatiensis"
                     /db_xref="taxon:456163"
     Protein         1..358
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39945
     Region          1..353
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkrrsflrkm gvglgaslfy rafaqgsptv rwrlvssypr sldtlyggae elakrvaelt
       61 ggrfqirvyq agelvpggqv ldavqqgtve aghtygpfyv gknpalafdg gvpfgltyrq
      121 hnawmlmggg lellrrvyad fgvlqfpggn tgtqmggwfr revrtledlk glrmripglg
      181 glvmgrlgvv pqtlaagdiy palergaida tefagpydde klgfykvary yyypsfweps
      241 aqlsflvaqr awarlpkefq eafqaaasev nltmmakyda lnppalkrll aagvrlrkwp
      301 aevmrkaeee aralyeeqaa kdpgyrrvyt aywafreevf rwfavaelgy qafafpsv
//
LOCUS       WP_008632481             403 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Bacillaceae].
ACCESSION   WP_008632481
VERSION     WP_008632481.1
KEYWORDS    RefSeq.
SOURCE      Bacillaceae
  ORGANISM  Bacillaceae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales.
REFERENCE   1  (residues 1 to 403)
  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 403)
  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
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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   5  (residues 1 to 403)
  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   6  (residues 1 to 403)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 403)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Bacillaceae"
                     /db_xref="taxon:186817"
     Protein         1..403
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43626
     Site            order(11..12,16..18,32..34,43..46,48..49,52..53,55..56,
                     62..64,69)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Region          21..60
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          80..398
                     /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 mntnytrgsf qlmksinrsi ilnmirehgp isradiakqt rltpptvsni vkeliqtkfv
       61 iettqgeskg grkptllain adqfyilgvd vgtnqmkfvv tnlfgqlkrd fqleiplnps
      121 kediistmkn girelltcgd gdehkflgig igmhgivdpe egtslfapsf qlydipikee
      181 lekefnmivk vendahtmtl geywfgngnd adnlvginvg ngigagimin gklfhgenhl
      241 ageighvtid lsgtkcpcgn ygclqtfaag paiadrarke lktgkpslit elvdhdlekv
      301 dgatvhkaal qgdafsiqll nqtgrylgig lanlihtlnp kriivgggva rsgdfllegl
      361 retiqsrglt ikaketeivl sklganasai gacvlvleef fsr
//
LOCUS       WP_008634320             443 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Halobacillus sp. BAB-2008].
ACCESSION   WP_008634320
VERSION     WP_008634320.1
KEYWORDS    RefSeq.
SOURCE      Halobacillus sp. BAB-2008
  ORGANISM  Halobacillus sp. BAB-2008
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Halobacillus.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Halobacillus sp. BAB-2008"
                     /db_xref="taxon:1246484"
     Protein         1..443
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=50012
     Region          4..416
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mfineaaeqv vigsilldgg lmedallfpv hfsnpghrri yegmkniher nepvtiltvt
       61 telkgeigkv ggvgylaela gsiattttfr hdqrlvlday rhralgeact rymndptddg
      121 ieelyqfsek yrklsldctd kqieetllei vremdeaekg ktgygtgnel ldiktggiqp
      181 gdlvilaarp smgktayalh laanhceggg svqifslema vkpllqrmis adasvngrkw
      241 rsrmfsdsdy egvvesvgri seweldihth aptyedihah traylrrhkp prpmiiidyl
      301 qlmstndrhe rrdleighit rslkkmavky nipiillsql srqvdqrrek ppllsdlres
      361 gnieqdadmi tflyqsqdpq deahkdkihl higkhrngpv gdipmyfrke fgrfeergeg
      421 slealpeqgt fllqkkntpt ptv
//
LOCUS       WP_008635483             334 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Halobacillus sp. BAB-2008].
ACCESSION   WP_008635483
VERSION     WP_008635483.1
KEYWORDS    RefSeq.
SOURCE      Halobacillus sp. BAB-2008
  ORGANISM  Halobacillus sp. BAB-2008
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Halobacillus.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 334)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Halobacillus sp. BAB-2008"
                     /db_xref="taxon:1246484"
     Protein         1..334
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=37294
     Region          94..327
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 makdctycgt tvtipdngal iirahselsr rgvpadegvh iipyqnrenl qdiladllsk
       61 gvkeeewihl ssgsmaqtfp itiehlfarl cqpeleslih qgdfeahlqp ilnmkdssif
      121 gyeallrtkg rqvnpgelfd yaarsglqsm ldqkarraav qakaehlqpg qhifinflps
      181 tiyvpefclk htfqiveefs idpadlvfev vetenitdvr hlkgildtyk ssgmrvaldd
      241 vgagystiem lsllqpdivk idrsyingca gdpikqqflf evlqradklg idvlaegiet
      301 veewnwlqsq gvgygqgfyi dkprpvpske lilp
//
LOCUS       WP_008637546             337 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Bizionia argentinensis].
ACCESSION   WP_008637546
VERSION     WP_008637546.1
KEYWORDS    RefSeq.
SOURCE      Bizionia argentinensis
  ORGANISM  Bizionia argentinensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Bizionia.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 337)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Bizionia argentinensis"
                     /db_xref="taxon:456455"
     Protein         1..337
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37050
     Region          3..337
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mynskiiglg hyvpdnvvtn ddlskmmdtn dawiqertgi kerrwakkgs gdttatmgvk
       61 aakvaierag idkddidfiv fatlspdmyf pgpgvqvqha ldiktvgald vrnqcsgfiy
      121 amsvadnfik tgmyknilvi gselhshgld kttrgrgvsv ifgdgagaav ltreednskg
      181 ilsthlhsqg ehaeelvlva pgmgkrwvnd ilaeknpeed esyfphmngq fvfknavvrf
      241 sevimeglek nklavddidm liphqanlri sqfiqkrfkl nddqvfnniq kygnttaasi
      301 pialseaweq gkikegdtvv laafgsgftw gsviikw
//
LOCUS       WP_008638875             298 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Bizionia argentinensis].
ACCESSION   WP_008638875
VERSION     WP_008638875.1
KEYWORDS    RefSeq.
SOURCE      Bizionia argentinensis
  ORGANISM  Bizionia argentinensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Bizionia.
REFERENCE   1  (residues 1 to 298)
  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   2  (residues 1 to 298)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Bizionia argentinensis"
                     /db_xref="taxon:456455"
     Protein         1..298
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34652
     Region          159..227
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
     Region          229..295
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mniqkshftf trkqrngifl lvtvivflqv afylydkslg vhaetnfvid dlqkevdslk
       61 lvqlqklkpk vypfnpnyit dykgytlgms neeidrlhhf ratekwvnsa kdfqqvtkvs
      121 dsllerlspy fkfpdwvtnp kpknvnqnyd nnnnnnnnkp ktfaekidln tvtasqlkrv
      181 ygvgeklser iinyreeigs ifiadiqlte vyglspevil rikeqftvkt pksiqlinln
      241 tatrdqlvni nyidyevahn iieqrtlrdg fqslndltkv kdfpvskfei itlyllie
//
LOCUS       WP_008639371             284 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Halobacillus].
ACCESSION   WP_008639371
VERSION     WP_008639371.1
KEYWORDS    RefSeq.
SOURCE      unclassified Halobacillus
  ORGANISM  unclassified Halobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Halobacillus.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 284)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 284)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="unclassified Halobacillus"
                     /db_xref="taxon:2636472"
     Protein         1..284
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32696
     Region          20..103
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          127..284
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mwidsmqrav dymekhlleg lriediakea hmsvyhfqhl friltdtsvm dycrrrrmtl
       61 aagelmagrr kvldlaykyg ydspesfska frkqhgmspr darnyngslv fynrlviqvs
      121 lkgvepmryq imekeairim grkeriscke genlkiipqm wrqfnedgvl ddlddwndgv
      181 megligvcct igngesidyw igasyqgkqp dgsydmleip askwavfevh gsmpgaiqkv
      241 wkqiysewfp ssgftqgngp emevypdgdp ssdsyyseiw ipvk
//
LOCUS       WP_008641031             350 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Bacteroides].
ACCESSION   WP_008641031
VERSION     WP_008641031.1
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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..350
                     /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=40200
     Region          3..282
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 megnqsrrid fvdltkgvci ilvvmahvgg afeqldtnsm lscfrmplyf lisgvffksy
       61 egllgfilrk inkliipflf fylsaflmky ivwkiapgvf qlpvswnell vvfhghdlik
      121 fnppiwflla lfncnilfyl ihflrekhlp vmfavtilig cagfylgklq ielplyidvs
      181 mtalpfyvag fwirrynffl ypshrfdkli pvfivlalvv myftattlgm rtnnyagnif
      241 qvyiaafagi fmimllckkv kkikvvsylg rysiitlsih gpilhflgpl vsryihnswa
      301 qasalllitl sicllltpvf lkvipqmvaq kdllkvkqdh tkktvyedkq
//
LOCUS       WP_008642344             686 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate--CoA ligase family protein [Bacteroides].
ACCESSION   WP_008642344
VERSION     WP_008642344.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..686
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73876
     Region          4..686
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mittqllrpe sivvvgasnn vhkpggailk nlinggyqge lravnpkeke vqgvpafadv
       61 ndlpdtdlav lavpalmcpd mvetlaskkq trafiilsag fgeethegal leeriletvn
      121 kygasligpn ciglmntwhh svfsqpipnl npkgvdliss sgatavfile savtkglqfn
      181 svwsvgnakq igvedvlqfm denfdpekds hlkllyiesi qnpdrllfha sslirkgcki
      241 aaikagsses gsraasshtg aiassdsave alfrkagivr cfsreelttv gcvftlpelk
      301 gknfaiitha ggpgvmltda lskgglnvpk legevaeelk aqlfpgaavg npidilatgt
      361 pehlrlcidy ceekldnida mmaifgtpgl vtmfemydvl hekmqtckkp ifpilpsint
      421 agaevsafla kghvnfadev tlgtalsriv napkpavpei elfgvdvpri rriidsiped
      481 gyiapnyvqa llhaagiplv defvsdnkee ivafarrcgf pvvakvvgpv hksdvggvvl
      541 nikseqhlal efdrmmqipd araimvqpml kgtelfvgak yeekfghvvl cglggifvev
      601 lkdvssglap lsyeeaysmi hslraykiiq gtrgqkgvne dkfaeiivrl stllrfatei
      661 kemdinplla tqkavvavda ririek
//
LOCUS       WP_008643883             411 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Cupriavidus sp. HMR-1].
ACCESSION   WP_008643883
VERSION     WP_008643883.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. HMR-1
  ORGANISM  Cupriavidus sp. HMR-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 411)
  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 411)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 411)
  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   4  (residues 1 to 411)
  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 411)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Cupriavidus sp. HMR-1"
                     /db_xref="taxon:1249621"
     Protein         1..411
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44978
     Region          82..266
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <252..335
                     /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          311..392
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mhivatpahr hpvpgkqrst avpgpalagt tgttgttgtt gttgttgtti aplattatpa
       61 parhtiaihh vdqillgvrr lgfdidavlr raaispalla spnarvtqdq yaalirtlrr
      121 ttrdelwgll srpvppgvfa haagamvhsa tlgeaiqagl rqyrlhldef tprlhlspdg
      181 ktaslilhgh apatpcqifa kstfafhayg linwlvarrv plshvdlgsg ppqaltdter
      241 ifnttvrygq sctalhfdaa wlrlpvmqdp aglrefllet phkllvryrd nsclaerirl
      301 hlrshlddel psleqmaqml rltpqtlsrr lrdegrgyqn ikdnlrrdaa igmlehscls
      361 lqqvalrlgf selstfhraf kkwtgvapge yrqrgmqpis piqedsprqs a
//
LOCUS       WP_008643763             210 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Cupriavidus].
ACCESSION   WP_008643763
VERSION     WP_008643763.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 210)
  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 210)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 210)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..210
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23029
     Region          1..207
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 maydleeqeq leslkawwkq ygnavtwali villglaaws gwgywqrvqa rdasmlyeqv
       61 tkaaesrdad rvkraatdle ekfgrtaygp msalvaakvl yeagdlagak tqlqwaidhg
      121 gddyaplarv rmagvlldek aydqglallk depaapyaal fadrrgdlla aqdkreeart
      181 ayrsaldklg sgeaamrqii qfkldalgaa
//
LOCUS       WP_008644074             325 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Bacteroides].
ACCESSION   WP_008644074
VERSION     WP_008644074.1
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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..325
                     /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=37360
     Region          6..277
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 maeismqkss lriewidvck glgiflvvig htsiaqisqt iynwiysfhm pmfymlsgmm
       61 lndskysdfr syikrrlktl iipffclntl vwlivkglni shiqtdftel ltgclamyfi
      121 ralfvselwy ffinklasnw vlklfiifll ivlsdyfrgv pseyigltrn eaigvilpsm
      181 plfyyavghv irnmalnlnt heikywlvss vmivliiisc llqpvsygyf hilpafcgii
      241 ilgllsills rlsvtllnst vcfigrntli ivafhqiiyn smkiltkyls lstvqdatlr
      301 llllaltlyf lirsfnkyap wlvgr
//
LOCUS       WP_008645452             264 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Cupriavidus].
ACCESSION   WP_008645452
VERSION     WP_008645452.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  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   3  (residues 1 to 264)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..264
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29408
     Region          57..263
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mslqepigsk laqsqsqvdg eaderdaaah sderyrlths sqigtvlrdm awqkcllsvr
       61 skggseivts ilhvdpankt fifdwcradg erqalmsseq nafsgllrgv pvnfivgtpg
      121 atrfeggpaf iadfpeklyh fqrrrhfrar tlltkgyrce lripetekqa lqldiadlsl
      181 sgvglrsrav gadqlpvgtv ikrclldfae lgrleldmqv vghwlvgfdd ntvhhygcaf
      241 lnpdgrmenf lqrlvfqlel ahrg
//
LOCUS       WP_008645793             433 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Cupriavidus sp.
            HMR-1].
ACCESSION   WP_008645793
VERSION     WP_008645793.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. HMR-1
  ORGANISM  Cupriavidus sp. HMR-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 433)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 433)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Cupriavidus sp. HMR-1"
                     /db_xref="taxon:1249621"
     Protein         1..433
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48370
     Region          4..429
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mttsirylrl flytatgrrg vgylsqygdi lrisfdrdyi edenrptlsl gyvgeteaat
       61 railtalrdv rvvrtdghwp vffqnllpeg hnrerlaser gcstedefel laaagrdlpg
      121 avevepvppa egvpqivrnw htalgldvle pgfvedpved aaaipgvvtk fsaiqqgrry
      181 vvkrhgeagd filklpstrh pdlveneftg yqlcralgld caeatvisre eaelpeqvpf
      241 qrilavkrfd rapgghrvhm eefaqilgya prnkygrala ldygnmlrvl drlsarpapd
      301 vqefikrfva fllmgntdah lknwavrypd grapilsply dpvcvtaffd dvpvtdygin
      361 raidktlrty tfddldamvr sagllrrarl lsiaretvrq aqadwprile dapegvrrav
      421 serlaggval tra
//
LOCUS       WP_008646293             180 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Cupriavidus].
ACCESSION   WP_008646293
VERSION     WP_008646293.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 180)
  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 180)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 180)
  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   4  (residues 1 to 180)
  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   5  (residues 1 to 180)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..180
                     /product="TRAP transporter small permease subunit"
                     /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=20517
     Region          4..167
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mnyllglsrq idrlnqhtgr lanimillsc lisagnallr ygfnlsdnwp lelqwymfai
       61 avmfgasytf qrnehvrvdl iygsvseraq hwidifgivv fllpstilft wlsweslflp
      121 swrileqsgn sgglprypik lvvpigfall tlqgiselik rfaalqgllr ieskyerpvq
//
LOCUS       WP_008646427             381 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Cupriavidus sp. HMR-1].
ACCESSION   WP_008646427
VERSION     WP_008646427.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. HMR-1
  ORGANISM  Cupriavidus sp. HMR-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Cupriavidus sp. HMR-1"
                     /db_xref="taxon:1249621"
     Protein         1..381
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=40643
     Region          1..268
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          264..353
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrflhtadwh lgrlfharsl iedqshvldq fvalvrdlrp davliagdvy dravpppeav
       61 allddvlari vvdagvpvvm iagnhdsaqr lgfgarlmaa rglhvagrtg petscvtlrd
      121 ahgevriyal pyaepaavrd algtdlpthe aalnaqldai rathpagvrs vavahafvvg
      181 gavseserpl svggsgavaa dvfhgfdfva lghlhrpqci gdrihysgsl lkyslseaeh
      241 iktvslield aeggvrieai plrplrdlrv ltgtlaglle agatdpsrdd yvhavltdag
      301 alldpmarlr qvypnalaie ravlarsgqa geagrklrel dtvslfanff revadtdldg
      361 dqrralddll avmqaseres a
//
LOCUS       WP_008646563             686 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Bacteroides sp. 3_1_23].
ACCESSION   WP_008646563
VERSION     WP_008646563.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. 3_1_23
  ORGANISM  Bacteroides sp. 3_1_23
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Bacteroides sp. 3_1_23"
                     /db_xref="taxon:457390"
     Protein         1..686
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73888
     Region          4..686
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mittqllrpe sivvvgasnn vhkpggailk nlinggyrge lravnpkeke vqgvpafadv
       61 sdlpdtdlav laipavmcpd ivetlaskkq trafiilsag fgeethegal leeriletvn
      121 kygasligpn ciglmntwhh svfsqpipnl nprgvdliss sgatavfile savtkglqfn
      181 svwsvgnakq igvedvlqfm denfdpekds hlkllyiesi qnpdrllfha sslirkgcki
      241 aaikagsses gsraasshtg aiassdsave alfrkagivr cfsreelttv gcvftlpelk
      301 gknfaiitha ggpgvmltda lskgglnvpk legevaeelk aqlfpgaavg npidilatgt
      361 pehlrlcidy ceekldnida mmaifgtpgl vtmfemydvl hekmqtckkp ifpilpsint
      421 agaevsafla kghvnfadev tlgtalsriv napkpavpei elfgvdvpri rriidsiped
      481 gyiapnyvqa llhaagiplv defvsdnkee ivafarrcgf pvvakvvgpv hksdvggvvl
      541 nikseqhlal efdrmmqipd araimvqpml kgtelfvgak yeekfghvvl cglggifvev
      601 lkdvssglap lsyeeaysmi hslraykiiq gtrgqkgvne dkfaeiivrl stllrfatei
      661 kemdinplla tekavvavda ririek
//
LOCUS       WP_008647037             159 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [unclassified Bacteroides].
ACCESSION   WP_008647037
VERSION     WP_008647037.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bacteroides
  ORGANISM  unclassified Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="unclassified Bacteroides"
                     /db_xref="taxon:2646097"
     Protein         1..159
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17244
     Region          1..157
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdafidstiq lliewglpgl fisallagsi vpfsselvlv alvklglppi aclisatlgn
       61 tvggmtcyym grlgkiswiq kyfkvkkekv dkmvkflqgk galmafftfl paigeviaia
      121 lgfmrsntwl tivsmfvgkl iryilllyal esawdaiag
//
LOCUS       WP_008636403             513 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: response regulator transcription factor
            [Bacillaceae].
ACCESSION   WP_008636403
VERSION     WP_008636403.1
KEYWORDS    RefSeq.
SOURCE      Bacillaceae
  ORGANISM  Bacillaceae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales.
REFERENCE   1  (residues 1 to 513)
  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 513)
  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   3  (residues 1 to 513)
  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   4  (residues 1 to 513)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 513)
  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   6  (residues 1 to 513)
  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   7  (residues 1 to 513)
  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 14435958
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Bacillaceae"
                     /db_xref="taxon:186817"
     Protein         1..513
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=58824
     Region          7..123
                     /region_name="REC_YesN-like"
                     /note="phosphoacceptor receiver (REC) domain of YesN and
                     related helix-turn-helix containing response regulators;
                     cd17536"
                     /db_xref="CDD:381091"
     Site            order(12..15,18..20,23,109,111)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381091"
     Region          423..506
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 medlyrvviv ddemlirqgi inyidwesqg frivgeasng kealqlvdel hphllitdiv
       61 mpgmngielv kavkerhpsv eiivlssfen fdyvrsafqf giadyilkpk lngeelirtl
      121 nrispntadn pveyekdisl edllrkkleg qewtaeeeek lqafpqgayt llgltetrrn
      181 ggnsslislh qklseegaik giewiadves dfnvalliyd slhtaavqer lvrfsdeyeg
      241 vgdrapwvvs apffslkevg evyrdqvirl keyafympea pilmegllpd lerkerpfdl
      301 sgfidrfkqr kfdtaiqnlr rhldaltsdy tldifefksw menvifnsiv llgnmkypvd
      361 dletlkyeyf avineagnvn davapfydfl ekvqvvvqed tqrecptdvq rllqyieehy
      421 aeplslttla nyfhfnasyl styfsthlhi gfsdylnkvr iekakrlles tntpvsevse
      481 qvgysdpsyf gkvfkrlvgs spgkyrkkam aan
//
LOCUS       WP_008647279             579 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase
            [Burkholderiales].
ACCESSION   WP_008647279
VERSION     WP_008647279.1
KEYWORDS    RefSeq.
SOURCE      Burkholderiales
  ORGANISM  Burkholderiales
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Burkholderiales"
                     /db_xref="taxon:80840"
     Protein         1..579
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=64142
     Region          7..508
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mskqkleltw igkekrpkle prilledpgk syhakyrvtg ndifdnrlif gdnllalkal
       61 eheftgrvrc iyidppyntg safaqyedgl ehsiwlglir erlvllrnll aadgscwiql
      121 ddneaqyckv ladeifgrdn fianvvwnks yavrsnaqff ssahehilvy akdrtqlrln
      181 qfgrsakqte rysnpdddpr gpwqsvtmti slvggargrq yaktgvseni fevtspsgkv
      241 flpppnrcws rnpsgfkkld adgrvywgps genaprlkmy lseagegvmp ttlwadgaef
      301 ghnqdgirel raldigdfpt pkpeklisqv islasdpgdl vldsfagsgt tgavahkmgr
      361 rwimvelgeh cqthiiprlr kvidgedggg vtessgwegg ggfryyrlap slivndrwgn
      421 pvinpeynaa qlaealskle gftyapsevq wwqhghsser dfiyvttqnl sadqlqalsd
      481 evgsdqsllv ccaafhgvta akaserwpnl tlkkipkmvl arcewghddy slnvanlpma
      541 ektepveetv stagaatrkt kksaatnagq gglfgenee
//
LOCUS       WP_008648183             358 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-oxoacyl-ACP synthase III family protein
            [Bacteroides].
ACCESSION   WP_008648183
VERSION     WP_008648183.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 358)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..358
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39608
     Region          7..339
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 maflkykgvg vtalagavpq rivnnykyte ffpedqvrev vdkvgiyerr fadaetcssd
       61 lcfaaaekli adnnidrnei dllifisqtp dyrmpatsvl lqdrlelsns ciafdvnlgc
      121 safmyglsia fsmvkngslr kalvldgetr skvyspkdrr saflfgdggv aalvecdekf
      181 gdswfslnsd gsrgdlikin gggyrmpssa etikekvide ygnirsdeqg ymqggdvfnf
      241 vireiprdik kviewsgmdi qsldyyvfhq annfinsyla kklklnidki pstigkygnt
      301 ssvscpltia dqlkgkmgge kylmlsafgv gmtwttaivp fvdlkisdiv evahgerv
//
LOCUS       WP_008648757             279 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Bacteroides sp. 3_1_23].
ACCESSION   WP_008648757
VERSION     WP_008648757.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. 3_1_23
  ORGANISM  Bacteroides sp. 3_1_23
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 279)
  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 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   3  (residues 1 to 279)
  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   4  (residues 1 to 279)
  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 279)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Bacteroides sp. 3_1_23"
                     /db_xref="taxon:457390"
     Protein         1..279
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32515
     Region          46..279
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          195..273
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mlqqyhtklk gtlaltdsyl tekalqkekg lykfiwvrsg sitveidhqe mtltkdevis
       61 lthlqhlefk sidgeyltll fnsnfyciyg ndhevscsgf lfngsshlir ftlnekerke
      121 ldtitealen eftvsdslqe emlrillkrf iiqctriarh rmnitrekes gfeivrqyyn
      181 lvdehyrtkk qvqdyadmlh kspktlsnif stcklpsplr viherveaea krlllysnks
      241 akeiadilgf edqasfsrff knmtgqsavq frntqegkn
//
LOCUS       WP_008648856             507 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Cupriavidus sp. HMR-1].
ACCESSION   WP_008648856
VERSION     WP_008648856.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. HMR-1
  ORGANISM  Cupriavidus sp. HMR-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Cupriavidus sp. HMR-1"
                     /db_xref="taxon:1249621"
     Protein         1..507
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54060
     Region          5..506
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mtsnpvirlh andnvliarg dltlgqhlpd ldlrvraqvp aghkiaarai argeqvrkyd
       61 tvigvadrdi gpgdhvhshn lrlvdfyrdp sfcsdvrpid yvpeaeratf mgyarpdgrv
      121 gtrnfigils svncsatvik hiaahftper laaypnvdgv vafaqssgcg msspsehfdl
      181 lrrtlagyar hanlagvliv glgcernqva slvesqglvp genlhtlvmq dtggtratia
      241 agvhaverml paanaftrqr vsashlkigl ecggsdgfsg itanpalgaa mdilvrhggt
      301 ailsetpeih gveymltrra vtpevgqkll drlawweryt agqnaqfngv vghgnqqggl
      361 anifekslgs amkggttplq avyeyaepid tagfvfmdsp gydpvaatgq iasganlicf
      421 ttgrgsmfgs kpaptiklas nspmyrrlee dmdincglvl dgelsvaqmg erifehilra
      481 asgeptksel lglgdhefvp whvgivs
//
LOCUS       WP_008648954             366 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Bacteroides sp. 3_1_23].
ACCESSION   WP_008648954
VERSION     WP_008648954.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. 3_1_23
  ORGANISM  Bacteroides sp. 3_1_23
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 366)
  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 366)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 366)
  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   4  (residues 1 to 366)
  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 366)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Bacteroides sp. 3_1_23"
                     /db_xref="taxon:457390"
     Protein         1..366
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42448
     Region          115..366
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          286..366
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mldiiyyfni fgcltmgmal lliqtapqli nphyrnakrf lgiasiival cnalilynrv
       61 qesvaeifam pvlvaaqlqa alftfivlil fhspyvcrrn ilrhlcptlf fvglylltil
      121 lfpdvriysv deyianitnp vlllrtvfaa tyltqiviyv rlfrreqrny makienyfsd
      181 tdkyefrwas rlfyeaacig iavlvfsifp aplfdgiitv vitvyyfdfg vryinyqykl
      241 yyealpaiee keesqpakes egdreledem aklllylqqg vvlgdyaeal hiperklsvf
      301 instygvsfk rwvnnkrvey ateqmakhpd ytmeriaels gfahkshfck ifreitggsf
      361 teyknr
//
LOCUS       WP_008634607             374 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GerAB/ArcD/ProY family transporter [Bacillaceae].
ACCESSION   WP_008634607
VERSION     WP_008634607.1
KEYWORDS    RefSeq.
SOURCE      Bacillaceae
  ORGANISM  Bacillaceae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Bacillaceae"
                     /db_xref="taxon:186817"
     Protein         1..374
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=42606
     Region          15..367
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 mninirlnpd kavhafyvff iihtcqigag lmgvprilfl eagvdawvsv lvtgaymhvl
       61 vllmltilrn yentdligvq vdlfgpwigk glgvlyilyi flllltvmkn yievvqvfif
      121 pqipiwlmsa fmlilmvysi lggfrvvvgt sflfffltiw lvlpvykpvt fmdwkhltpi
      181 fmsspmeila gakqvaysvl gleilffiyp yiqnkkkiav aahagvfftt ilillvtvvs
      241 igyfspdelk etvwatlslf kiisfsiier fdflavalwm mviipnvvlf gwiiihslkr
      301 lfsfpkkpsl yitalmlffs silieerigi nyltsitgev gfwvvfiypw ilyvglllkk
      361 lfrkgksnek mghs
//
LOCUS       WP_008649154             367 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Cupriavidus].
ACCESSION   WP_008649154
VERSION     WP_008649154.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            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="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=40648
     Region          1..354
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvrnvhk rfgdfvaldd vsldfaegel tallgpsgcg kttllriiag leradagqvv
       61 lagqdastqh vrqrnvgfvf qhyalfkhmt vfenvafglr vkprgerpse akirekvksl
      121 lelvqldwla drfpaqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 rlhddlhvts vfvthdqeea levadqvvlm nrgsveqfgt peavynhpat pfvfgflgnv
      241 nlfhgrlevg dsggllhtge avlpvvgsgh etegdavayv rphdldlery apgtdgiavt
      301 lrraltlgpv aqleleredn qdvievalpl erfrhhgfke gellavrprq lrvfnqgrtt
      361 qeqgaar
//
LOCUS       WP_008651236             445 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Cupriavidus].
ACCESSION   WP_008651236
VERSION     WP_008651236.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 445)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..445
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=48001
     Region          186..423
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mdseakdapw gddhdrepal sesqpaafla alaghraeig tahplaiviv rldrfqface
       61 tigsrrtrll raevksriag vgvmpavmhw lspadlgiac llpatteema elsqsiatal
      121 rlpysvdgfe lflscsigta idspesater nlqqafdaml qinrrggggi anasqpvtpr
      181 mvtllaalpe avsrgefslq lqpralfdta eiaaytvrlr whhpvlgris pqdflpavea
      241 lgmmrevghw lvqqllqliq eskhvakvqf tllasspqll addaitmlqr avetsgispd
      301 rlcvevpvqc igavadatqk aarlhdcgiq islsdftddq vsrhalalva pdmvmldarh
      361 lgssaqarda asllraacvf arsrgvavha rgvetraqle avrdwgcdgv qgyllaqpfp
      421 aqwlvqthaa vaerarqllr ptnlv
//
LOCUS       WP_008651680             183 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Cupriavidus].
ACCESSION   WP_008651680
VERSION     WP_008651680.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 183)
  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 183)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 183)
  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   4  (residues 1 to 183)
  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   5  (residues 1 to 183)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..183
                     /product="TRAP transporter small permease subunit"
                     /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=19924
     Region          9..161
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 meapilrkrw ldhlldvcaa lgalcilavc ivmiamsisr etsitlkggd divawlcaas
       61 aflilgqtfq hggivrveml leavgtkrrw llevisltic lifagyaawa lgsfawqswd
      121 igdvsqgqiv iplwipqsfa vigalgflla vgdewlrvvr rqkpryqlaq eaklaagdfg
      181 etv
//
LOCUS       WP_008658299             242 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Bacteroides].
ACCESSION   WP_008658299
VERSION     WP_008658299.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 242)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..242
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=26563
     Region          52..214
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mqkvflflll fllplaevpn haptsepvsv astpetdeid qlfddmqldg ivsytafrqa
       61 vtgyrkieqk sksimtlidf skpstekrly vldmknkkll ytsvvshgkn sggnyatsfs
      121 nkngsykssl gfyltentyq grngyslvln glekgindqa kqraivmhga ayanpnitas
      181 agrlgrslgc palpqalakp iidtikkgsv lfiyannkdy lanstflspr qteylswaqp
      241 an
//
LOCUS       WP_008655713             411 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Rhodopirellula europaea].
ACCESSION   WP_008655713
VERSION     WP_008655713.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula europaea
  ORGANISM  Rhodopirellula europaea
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Rhodopirellula europaea"
                     /db_xref="taxon:1263866"
     Protein         1..411
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44034
     Region          1..409
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mlilvanlgs tsfkyklldm sgdfesanas pdsrvlarga vdrigepisq cevivtrshq
       61 getfreetqm pvpdhgvavq acldqlthpe ngclkeanev aaigfkavhg grksgtfvvd
      121 devleamdem saaapahnpp yiaamkllrq rfpelplvaa fetefhdtis perrtyaipa
      181 ewtremqiqk wgfhgsshrf iaeraaevlg rddakiisch lggsssltai dsgksimttm
      241 gmtpqtgvpq nnrvgdfdaf aiplimqrts qsleevlqtl asqgglkgls ggmadlrdie
      301 saasegnada klalgvytee irrhlggmmv algrldaivf tggigensdv vraavcsgle
      361 gfgieldask ndgmrgegsl htessktqil vlptneewiv akrslralaa q
//
LOCUS       WP_008658524             291 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Bacteroides].
ACCESSION   WP_008658524
VERSION     WP_008658524.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..291
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34280
     Region          211..290
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mhlkefiqyy nvsftsneei afwyinpkli nenknipaiq dlhsilfvid gelkievngk
       61 iflmnrncfa dintihkpty rllsasenlr ayhiimtkey vmrlvgnrrl fstryicerm
      121 nnpilqitps ntgifikyll dikqifkneg hlfrtailth clwnflaeva nfsllekekt
      181 peevgnkrkl yiqflemist einrkysvnf yasrlcvtpq ylqrvvkmfs nrtvhqwike
      241 aimgeimkll netdmtiqqi aedlgfpdqa alskffkqnk kvppsiyrnk e
//
LOCUS       WP_008661184              86 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Rhodopirellula europaea].
ACCESSION   WP_008661184
VERSION     WP_008661184.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula europaea
  ORGANISM  Rhodopirellula europaea
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 86)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 86)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 86)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Rhodopirellula europaea"
                     /db_xref="taxon:1263866"
     Protein         1..86
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8991
     Region          6..86
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mneprtievl lfagaseaad gadrvivrsh dhitaselmk qladqhaala plarrsrlai
       61 dqryvsadhv ipsgaevali ppvsgg
//
LOCUS       WP_008661205             114 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Bacteroides].
ACCESSION   WP_008661205
VERSION     WP_008661205.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..114
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12747
     Region          12..109
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(15..16,34..35,43,46,48..49,51,54..55,57,65,70,77)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(34,65..66,68,89)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mkdykenksn lsetfcnevy svvreipags vttygdiaal lgmpqysrmv gralrqlpag
       61 lnlpchrvvn aigrlvpgwd eqrrlldaeg vsfrkngcvd lrlhrwrdds vltd
//
LOCUS       WP_008662517             687 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate--CoA ligase family protein [Bacteroides].
ACCESSION   WP_008662517
VERSION     WP_008662517.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 687)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..687
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73826
     Region          4..686
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mitsqllhpa sivvvgasnn vhkpggailk nllsggytge lravnpkete vqgvaafadv
       61 kdipdtdlai laipaalcpd avemlaaekq vkafiilsag fgeethegav ledriletvn
      121 rygasligpn cigfmnswhh svfsqpipql hpqgvdliss sgatavfile savtkglqfn
      181 svwsvgnakq igvedvlqym dehfnpeads rikllyiesi gdpdrllfha sslikkgcki
      241 aaikagsses gsraasshtg aiassdsave alfrkagivr cysreelttv gciftlpelk
      301 gknfaiitha ggpgvmltda lskgglnvpk legpvaeelk gklfpgaavg npidilatgt
      361 pehlrlcley ceekfdnida vmaifgtpgl vtmfemydvl hekmlhckkp ifpilpsint
      421 agaevaafla kghvnfadev tlgtalsrim naprpannei elfgvdvpri rriidsipad
      481 gyiaphyvqa llrsagipiv eefvsdnkee vlafarrtgf pvvakvvgpv hksdvggvvl
      541 nikseqhlal efdrmmqipe asaimvqpml kgtelfigak yeekfghvvl cglggifvev
      601 lkdissglap lsyeeaysmi hslraykiik gtrgqkgvne dkfaeiivrl stllrfatei
      661 kemdinplla tekqviavda ririekk
//
LOCUS       WP_008663497             116 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Rhodopirellula europaea].
ACCESSION   WP_008663497
VERSION     WP_008663497.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula europaea
  ORGANISM  Rhodopirellula europaea
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 116)
  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 116)
  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   3  (residues 1 to 116)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Rhodopirellula europaea"
                     /db_xref="taxon:1263866"
     Protein         1..116
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=13446
     Region          16..116
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mpirqppqlt qnarelrtnq tkaeslvwtl lrnrrlnghk frrqfpippf iadfacvekr
       61 liveldvdyh ehqeqqdmsr taqlnregwt vlqfcnahvl enteavgvai lramge
//
LOCUS       WP_008663905             634 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase [Bacteroides].
ACCESSION   WP_008663905
VERSION     WP_008663905.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 634)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..634
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=71842
     Region          68..551
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 madilkhldl nsadgtqlnl dalyqiapsa ftevrddktg eisrkvnfev lrrllgdhat
       61 dgdgemyqft wvgknaarae aakptdktlr pvvensvdwd ntkniyiegd nlevlkllqr
      121 symgkvkmiy idppyntgnd fvyhddfart aaeedieagn vdelgyrfrr ntdtngkfhs
      181 dwcsmiyarl lvarsllted gvvfisiddn evrnlrnicd evfgehnfva qlvwerafsp
      241 kndakyvsns hdyilmyvkq iedftigrld rteeanlrys npdndprgvw mssdisvkty
      301 naacdypitt psgkiveppa grcwrlsaka faerlqdnri wfgpngdntp rikrflselk
      361 yegmaptsil fykevghsqe gaqevvslfg dkgvfdgpkp vrllqrlitl anlkedsivl
      421 dffsgsasta halmktnsek dkhcqfilvq lpeevsdskk dqgyknicei gkerirraga
      481 kikadfpltt qnldtgfrvy rldesnyekv sispkeykqd qldlfannik adrtdldlly
      541 gsmlawgvrl dlplqteivd gctiytvneg dlvacfsegi tdkvvaamag ksplrvlfrd
      601 acfkedaqki niyeqfkqal dwadndafnn irvi
//
LOCUS       WP_008665094             361 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Rhodopirellula europaea].
ACCESSION   WP_008665094
VERSION     WP_008665094.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula europaea
  ORGANISM  Rhodopirellula europaea
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Rhodopirellula europaea"
                     /db_xref="taxon:1263866"
     Protein         1..361
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=40070
     Region          <32..361
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mitqsqpttq wvlteygsgn qqrrtikvpn riatvgrtdd sdlciavssv skqhakiwve
       61 edglhvedlg stngthhngr piqeatlaeg dllqfanavf rvqcqqeelp dgtmeeglip
      121 waqtlmtfer llsqravvph yqpiitmdra stpgyevlar sdlpelkspa amfevaerlg
      181 qnaalselmr deasrrlkaa dktnakifln thpdemgtdr lfsslmelrn rypsisfnie
      241 vhegavthvd amrtfrdqla dlgmqlsydd fgagqgrlle lvevppdilk fdmqlirnid
      301 qasaarqdll qsliriaqds gsitlaegve tegehetcvq lgfelgqgfl ygrpatiehv
      361 l
//
LOCUS       WP_008665880             290 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Bacteroidaceae].
ACCESSION   WP_008665880
VERSION     WP_008665880.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidaceae
  ORGANISM  Bacteroidaceae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Bacteroidaceae"
                     /db_xref="taxon:815"
     Protein         1..290
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34791
     Region          190..269
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mkltdllrrt aeanpqavtl hsiadkaeel vekrysvrrm lremesfahd teamrltvda
       61 lrqlpylptl eqrdykpyma lvacspenfa ycylsndlva iyeagyrtae lmffcdllrc
      121 mrgrshlncv tnrvcdyffr arrdtlrhia tplkefeiqy aesrmkelek avfrlkvkmy
      181 kwhtftaenm armfgmsysr frekfeayyg csatewlrre risrimedmt yrpeltlrev
      241 aernhflsks nfhdfclkrm lkrpgklkre gyekwcerrl ayynnhsqac
//
LOCUS       WP_008667902             259 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Rhodopirellula europaea].
ACCESSION   WP_008667902
VERSION     WP_008667902.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula europaea
  ORGANISM  Rhodopirellula europaea
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 259)
  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 259)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Rhodopirellula europaea"
                     /db_xref="taxon:1263866"
     Protein         1..259
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28157
     Region          24..257
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mnsparlkas vcvdavlenl stvdamklva ecgypafefw kwwdkdldai nqareelqlq
       61 vaavctkfvs lvdpdvraey laglkesita agqlncpvli sqvgdarpgv draeqrdcmv
      121 aglkeaapml edsgvvlaie plnelidhag yylvrsdeaf siiqevdspn vkvtfdiyhq
      181 qiseghvian ltknvdaiah fhaagnpgrh eldrgelhyp sifaaiadtg ysghvgleyw
      241 pvndaaaglr eaaswikkv
//
LOCUS       WP_008674536             129 aa            linear   BCT 20-JAN-2025
DEFINITION  acyl carrier protein [Rhodopirellula sallentina].
ACCESSION   WP_008674536
VERSION     WP_008674536.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula sallentina
  ORGANISM  Rhodopirellula sallentina
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 129)
  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 129)
  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 129)
  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   4  (residues 1 to 129)
  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 10011594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Rhodopirellula sallentina"
                     /db_xref="taxon:1263869"
     Protein         1..129
                     /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=14177
     Region          5..80
                     /region_name="acpP"
                     /note="acyl carrier protein; Provisional; PRK00982"
                     /db_xref="CDD:179197"
ORIGIN      
        1 mslsqdeife kvqaalvdal gvdedettrd atlvgdlgae sidfldivfk leksfdiqip
       61 reelspedil tnsqyvqdgv vtsdgmaelk trmpwadlsk feenprvqdf gnlltvgdlc
      121 syvdskvna
//
LOCUS       WP_008674852             471 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Rhodopirellula sallentina].
ACCESSION   WP_008674852
VERSION     WP_008674852.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula sallentina
  ORGANISM  Rhodopirellula sallentina
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 471)
  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 18888537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Rhodopirellula sallentina"
                     /db_xref="taxon:1263869"
     Protein         1..471
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=50125
     Region          307..349
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
     Region          356..470
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mlrhqvrtan shrqgetavq tlktsaivvl mmtvlygayv smttppdplp qgvesllves
       61 gmdelpedfg sfgiddgtlt nfddfasapa amdseptlds atgpsndfgp vdqtfadles
      121 nldsidesfp adslptepts pesfqmsdig asqgasrlpe vsdsatpvai aadaardyps
      181 tgsdfslpdp neaiqmtess lasttnspan atnsigfqdi ppsastsits ptnrtasdva
      241 aaglanaiat adrqynedrr realatlslf yetpnlsseq reqllvrldp lardviysse
      301 hlleephrvg snetlmdiaq kydvpwqlla ningvsdpvt vlpgtdlkvv rgpfradvdl
      361 enkeltlflg dlyagrfpvg igndpeprpg tytiqekksa ktyydmagtp ippgsprnpy
      421 gsmwidlgqg islhgspksd sattegcisi agnysrdvfg ilsegssvti r
//
LOCUS       WP_008674707             419 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Phocaeicola
            dorei].
ACCESSION   WP_008674707
VERSION     WP_008674707.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola dorei
  ORGANISM  Phocaeicola dorei
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 419)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 419)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Phocaeicola dorei"
                     /db_xref="taxon:357276"
     Protein         1..419
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48074
     Region          2..415
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mkrlyvfadf dwlkeprlig elsyeslrgs dsygfcynde wlkdygglfl sddlnnypgq
       61 qytppgkdif gcfsdalpdr wgrilinrre qilakeenrp vrrlssfdyl igiedfsrmg
      121 afrfkesidg dyinaseilr ippltdirel iaasseieks edenrlpemr wiaqlvqpgs
      181 slggarpkas videnkilyi akfpsrkddy dvglwehfsh llakkagvna adtrvistsd
      241 kyhtllsrrf drredgkrih fasamtllgl ndgdnantgh gyldivdfil qnctnvednl
      301 qelyrrvafn icigntddhf rnhgflltak gwtlapaydi nptlneyqsl linsytnksd
      361 lnellnscee ymlqkhiaqq iisevlnavk ewrllatrlg iakseqerfa avferqihl
//
LOCUS       WP_008677229             342 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Clostridium].
ACCESSION   WP_008677229
VERSION     WP_008677229.1
KEYWORDS    RefSeq.
SOURCE      Clostridium
  ORGANISM  Clostridium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Clostridium"
                     /db_xref="taxon:1485"
     Protein         1..342
                     /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=40567
     Region          1..271
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 meklkkryyl ldnlkvilif fvvfghviey yindnsilmt lyifiyifhm plfifisgyl
       61 sknfykmkrk airnllipyi ifnmiwytav yigtrramfs vlypgwtlwy llslffwrit
      121 lkylikfkhi lllsfiagvl vglipsigsi lsisrtivfl pffllgyytt eehlekiksf
      181 kseyaitgil vflliaiyiv kndlfnykfl ynsysynale vslfegtifr iflyfgaiif
      241 sicvinlvpr keqffskigk atmniyvfhi ylvmlvyffi pkwnigllqn ililispfii
      301 ifilsrkkin kvydglfypv nisidtgkks ikkykkinkk ah
//
LOCUS       WP_008677993             274 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Clostridium].
ACCESSION   WP_008677993
VERSION     WP_008677993.1
KEYWORDS    RefSeq.
SOURCE      Clostridium
  ORGANISM  Clostridium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Clostridium"
                     /db_xref="taxon:1485"
     Protein         1..274
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30925
     Region          3..249
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mnyadlhihs sysdgsmtpe eivdkakslg vksisitdhd siasqyiikn dykdiniisg
       61 ielsteyddl eihilgyfid ikdknlnetv nrlnkarier ieeilfklnk ndihltldel
      121 aidldstvig rshvanamvk kgyfdsykaa ftnflvkgkp ayvkgfklny kdaikvinns
      181 ggiavlahpg qiykglaien iikdlkfygl rgvevyhpsh sreqtnnfyn ickkyklfit
      241 ggsdyhgkec ynenligsyg ineallnkli nfkk
//
LOCUS       WP_008678523             403 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Clostridium].
ACCESSION   WP_008678523
VERSION     WP_008678523.1
KEYWORDS    RefSeq.
SOURCE      Clostridium
  ORGANISM  Clostridium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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 403)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Clostridium"
                     /db_xref="taxon:1485"
     Protein         1..403
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47954
     Region          1..393
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mkvitmskee lrkflvvyqg lytnntfige egikdfikrv gcvqydplnv vgrnadlvmq
       61 sriedydpim ledllykkre lidrwdkmma iysaedwryf rrvrlerkke vegvlrnras
      121 inainyvdtv keyiekngat spskidlgfv ekgkwghgkl ssatmdymwn mgvlgvkekk
      181 ntqkiydlie rllpkeiisk vdpfkkddef ykwyfkrrig sigvywdrng egwlgnyvyh
      241 knlririlne lveegelifi kvenlkenfy lrkedisiln dsnrinenni kilapldnii
      301 wdrkltrdif nfdytwevyk pvdkrkygyy vlpilygdkf varfepelhr gneplviknw
      361 wwedsykitn ncvdavkisl dkfcrylkad giskdsleki nks
//
LOCUS       WP_008679285             694 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: molybdopterin oxidoreductase family protein
            [Clostridium].
ACCESSION   WP_008679285
VERSION     WP_008679285.1
KEYWORDS    RefSeq.
SOURCE      Clostridium
  ORGANISM  Clostridium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 694)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Clostridium"
                     /db_xref="taxon:1485"
     Protein         1..694
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=78468
     Region          1..694
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mkvvrstcny csiacnfdfh veddgfiqrv kpakdypvnr gfccvkglnl dkqntiyenp
       61 vlpllrnekg elehiswdka fnifaervkk iqdeygkesf aflstgqlct eemalaghig
      121 rtflggngdg ntrlcmatav vaykqsfgfd sppytfedle lsdvmifigc npvvahpilw
      181 srviknrnkd kkiisidprr tetvtnsdmw idikpksdlr llytlanvli ekgwidekfi
      241 knstedfegf knhvkkydin dveeytgisk grvlelakii hegkrvsfww tmgvnqgyqa
      301 vrtaqavinl almtgnigrp gtgansitgq cnamgsrlfs nttglyggge ytdkarrkvv
      361 akalgideem lpkkptipyn aiieginngt ikalwvlatn pvvswinsle fkkaaeklef
      421 lavqdiysdt etckyahlil pstnglkkeg vlinterrls kiqpvlekkk delsdydill
      481 gignalgmgs lldkwktprd afetlkectr nmpcditgvs ydmlkdskgi qwpfkegddi
      541 ekeerrlfed gkfytpnkka kfiyediinp pfeqseeypy ilntgrgtvg qwhtqtrtre
      601 ipdveaiimk kgyinintdl aeelgikend mvkvsspngi snqflvklsr tvkkdqlyap
      661 mhyieansvl psifdtyske pnykygpvki ekin
//
LOCUS       WP_008678831             183 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Clostridium].
ACCESSION   WP_008678831
VERSION     WP_008678831.1
KEYWORDS    RefSeq.
SOURCE      Clostridium
  ORGANISM  Clostridium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae.
REFERENCE   1  (residues 1 to 183)
  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 183)
  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   3  (residues 1 to 183)
  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   4  (residues 1 to 183)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 183)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 183)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Clostridium"
                     /db_xref="taxon:1485"
     Protein         1..183
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=20732
     Region          5..180
                     /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"
ORIGIN      
        1 maidvivaln neeigqkikt iliergynvl alctygneli rairqlspsi visgykfkdm
       61 tlidiynnvg evcsflavvn epyksfvqee tdifcisspi nnsilltsld miyqserkvk
      121 klkekvtvle tkinerkvie kakgilmqqk gmneneafry iqknsmnlgl kmidfsnkil
      181 lge
//
LOCUS       WP_008679815             464 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase family protein [Clostridium].
ACCESSION   WP_008679815
VERSION     WP_008679815.1
KEYWORDS    RefSeq.
SOURCE      Clostridium
  ORGANISM  Clostridium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae.
REFERENCE   1  (residues 1 to 464)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Clostridium"
                     /db_xref="taxon:1485"
     Protein         1..464
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=52950
     Region          88..195
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          207..319
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          344..462
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(414,417,435..438,440)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mksinlkelf knkitgniii ivtaiiftyl liaifftnhf ffnteingin lslksyeeap
       61 dilkksindy klqiierdek ieeilgkdig lqyneknsis nvqdrqaslk wivglikkqn
      121 ynigdlvdyn nenlnnkike ldclnkdiie pknvgfkysn gsyelieevy gnkvkkekly
      181 eaiensilng evkidlnekl cyenpeytvn sekamiakdi lnkyvstkit ylfgdksevl
      241 dgsrinewls vddnleviin eksvkdyvle lsakyntvgi arnfksstgk mvevkggyyg
      301 wkinyvaetr mlleniklga ilekepiytq kglnrdeddi gdtyveinlt sqhlwfykdg
      361 kliaqgdvvt gdpgkgystk lgtymlnykq keatlrgtny eakvtywmpf ngnigihdas
      421 wrysfggkiy kgngthgcvn spsylaktif enidegtpvi cyee
//
LOCUS       WP_008680645             397 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Clostridium].
ACCESSION   WP_008680645
VERSION     WP_008680645.1
KEYWORDS    RefSeq.
SOURCE      Clostridium
  ORGANISM  Clostridium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae.
REFERENCE   1  (residues 1 to 397)
  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 397)
  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
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 397)
  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   5  (residues 1 to 397)
  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   6  (residues 1 to 397)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 397)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 397)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Clostridium"
                     /db_xref="taxon:1485"
     Protein         1..397
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45048
     Region          23..>54
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          76..390
                     /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 mkltknqqkl rfkildkiya kgpisridis netgitpatv seitgnmiqe nliheigevi
       61 peenksgrkk illgispnhs fyigtelspk yisfcltdni gkiykektiq ldnsnleeil
      121 seefyinkls sfidsctnyn pkgigialpg hfdevnksii tnnsfwknfd itillerfdl
      181 piyfennvkc mtlserlfsf ngnddnfiff hvgrgmfcsy myngelyakd nflvgeighi
      241 vvhpngelce cgkrgclqty gseawiikks qilfdnsett ylkqlvsern kitietilka
      301 yrlgdegiik ilnsainyls itinnlsmmi dsskiiihge lfnedllknl leellkqnin
      361 llsknikqdi llkeynnyng alaaaalcvs kllikld
//
LOCUS       WP_008681991             178 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-hydroxyacyl-ACP dehydratase FabZ family protein
            [Rhodopirellula].
ACCESSION   WP_008681991
VERSION     WP_008681991.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula
  ORGANISM  Rhodopirellula
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae.
REFERENCE   1  (residues 1 to 178)
  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 10101294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Rhodopirellula"
                     /db_xref="taxon:265488"
     Protein         1..178
                     /product="3-hydroxyacyl-ACP dehydratase FabZ family
                     protein"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=19619
     Region          29..155
                     /region_name="FabZ"
                     /note="FabZ is a 17kD beta-hydroxyacyl-acyl carrier
                     protein (ACP) dehydratase that primarily catalyzes the
                     dehydration of beta-hydroxyacyl-ACP to trans-2-acyl-ACP,
                     the third step in the elongation phase of the bacterial/
                     plastid, type II, fatty-acid...; cd01288"
                     /db_xref="CDD:238615"
ORIGIN      
        1 mkseyiiqps ildfdkpiag ieeirkfnpq rhemeqltai lhedlethsc aaykqitede
       61 fwvrghmpgm plmpgvmmle avaqlssyyt qkhdllgaam vgfggvdevr frgvvvpgdr
      121 lilmvrldkt rrgrmivasf qgvvgenlvl egclrgipip ieavtgqlag kpdpttss
//
LOCUS       WP_008684120             387 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Rhodopirellula sallentina].
ACCESSION   WP_008684120
VERSION     WP_008684120.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula sallentina
  ORGANISM  Rhodopirellula sallentina
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 387)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Rhodopirellula sallentina"
                     /db_xref="taxon:1263869"
     Protein         1..387
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=41203
     Region          1..382
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mnilvfnvgs ttlkyaciev esgerlyegl vdrigqvggd apdhlsaarc vlekfgllpg
       61 aeasarddmp elsaiahriv qggdsypkpa ivnadvlaql ktldtlaplh npsarsvvva
      121 idslkiplpq vlvfdtayfs tlepaayrya ipepiyrahr vrkygfhgts hrfvtaqaiq
      181 hlkhdspvri islhlgggas vtasldgkav dtsmgmtple glvmatrcgd idpsvplhli
      241 rsagmsaddv drlmnkesgl vglcgeadmr ailsrreadd rsaklaidiy vrriqkvigg
      301 ylailgglda liftagvgeh atkirelvtg plahlgivid qaanespkle dgiadisdps
      361 asvrtlivat neelaiares aqrlaed
//
LOCUS       WP_008684574             292 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Desulfovibrio sp.
            3_1_syn3].
ACCESSION   WP_008684574
VERSION     WP_008684574.1
KEYWORDS    RefSeq.
SOURCE      Desulfovibrio sp. 3_1_syn3
  ORGANISM  Desulfovibrio sp. 3_1_syn3
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Desulfovibrio.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 292)
  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 292)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Desulfovibrio sp. 3_1_syn3"
                     /db_xref="taxon:457398"
     Protein         1..292
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32419
     Region          25..79
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mvakgknssf cllpwgksfr eggmlefsda eiavlpviai hadnkqkayp gyericalak
       61 vskatvakgi dgladkglia kttsltgaqs yneyrllfsy dknnddksyt rqwialhrel
      121 feygiwgemp pkkrrvylil kafawsglss tefgyngaef vevyerkkwr tlplsniqfl
      181 sgsahsaaef arlagvadrt yrdakawlid nsliiphseg kidgfvipfw pkayfrdvva
      241 aikkakeesa rrrnmgstgg arrsmgaalr rlnpvpkkvp lakrlqsdgg ge
//
LOCUS       WP_008685029             376 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Desulfovibrio sp. 3_1_syn3].
ACCESSION   WP_008685029
VERSION     WP_008685029.1
KEYWORDS    RefSeq.
SOURCE      Desulfovibrio sp. 3_1_syn3
  ORGANISM  Desulfovibrio sp. 3_1_syn3
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Desulfovibrio.
REFERENCE   1  (residues 1 to 376)
  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 376)
  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   3  (residues 1 to 376)
  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   4  (residues 1 to 376)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 376)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 376)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Desulfovibrio sp. 3_1_syn3"
                     /db_xref="taxon:457398"
     Protein         1..376
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39855
     Region          28..361
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(101..103,124..125,175,227,251)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkrgmtllaa mafcvamtap alaadpikig vqgahsgdla sygvpslnaa klviddanak
       61 ggvlggkvev vsqddqckpe matnaatkli sdkvavvigp icsgptkaal plfqdanlia
      121 vsptattpgl tedgkhplff rtvandnaqa rltsdfmlnk lkakkvaylh dngdygkgfa
      181 dnnrvfmekg gaetvlfeav tpdavdfsav vrklrrakpd ivvfggyqpv askliqqmrr
      241 drlttpfigp dgvkdetflk mtgkdsegvy asypkdtstl peykkareah vkaygsepgf
      301 gyynayaaaq cllaaiekag gtdtakikev lrtnpvdtpl gkisfnekgd aagmalsiyq
      361 vkngkfveld hsltlq
//
LOCUS       WP_008685926             285 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Desulfovibrio sp. 3_1_syn3].
ACCESSION   WP_008685926
VERSION     WP_008685926.1
KEYWORDS    RefSeq.
SOURCE      Desulfovibrio sp. 3_1_syn3
  ORGANISM  Desulfovibrio sp. 3_1_syn3
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Desulfovibrio.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Desulfovibrio sp. 3_1_syn3"
                     /db_xref="taxon:457398"
     Protein         1..285
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30746
     Region          1..253
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mklidlhtht lasdgtdsps alvqkahtag laavavtdhd tvsgldeaee agrdlgikvi
       61 rgcelsthte ygevhilglw lprdaaplqd qlgylrrkrc ernraivekl ralgldisle
      121 evraiakesv grphiaavla skgyvrdvge afreylgfyg kaylpkevle peaavhllag
      181 lgatvslahp llqkyplpwl egfvehlsgc gltaieawhs ehsdadtrlc vewarrfglg
      241 lsggsdyhgg nkpgirlgvg rgglrvpldv lekleaqrra qglpc
//
LOCUS       WP_008686201             256 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-deoxy-manno-octulosonate cytidylyltransferase
            [Desulfovibrio].
ACCESSION   WP_008686201
VERSION     WP_008686201.1
KEYWORDS    RefSeq.
SOURCE      Desulfovibrio
  ORGANISM  Desulfovibrio
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae.
REFERENCE   1  (residues 1 to 256)
  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 256)
  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 10793788
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Desulfovibrio"
                     /db_xref="taxon:872"
     Protein         1..256
                     /product="3-deoxy-manno-octulosonate cytidylyltransferase"
                     /EC_number="2.7.7.38"
                     /GO_function="GO:0008690 - 3-deoxy-manno-octulosonate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0033468 -
                     CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29013
     Region          1..245
                     /region_name="PRK13368"
                     /note="3-deoxy-manno-octulosonate cytidylyltransferase;
                     Provisional"
                     /db_xref="CDD:184007"
     Site            order(8..10,49,76,102,104)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133010"
     Site            order(127,144,150..152,158..159,161..167,176,201..202,
                     205..207,214..217)
                     /site_type="active"
                     /note="oligomer interface [active]"
                     /db_xref="CDD:133010"
ORIGIN      
        1 mniiaiipar mgssrypgkp lalihnvpmv ghvtfrtams kvlsdtyvat cdsiiedyck
       61 naglkcvmtg dhhvrcstrt aeallkieea tgkkadivvm vqgdepmvrp emidaavqpm
      121 lddpsinvvn lmaemdtlee fedpnevkvv vdrfnnalyf srepipsrkk gsdkvpmrkq
      181 vciipfrrdy llrfnemees pleiyesvdm mrileygekv rmvptdcrtw svdtpedlar
      241 varlmegddl mreysk
//
LOCUS       WP_008686306             342 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Desulfovibrio sp.
            3_1_syn3].
ACCESSION   WP_008686306
VERSION     WP_008686306.1
KEYWORDS    RefSeq.
SOURCE      Desulfovibrio sp. 3_1_syn3
  ORGANISM  Desulfovibrio sp. 3_1_syn3
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Desulfovibrio.
REFERENCE   1  (residues 1 to 342)
  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 342)
  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 342)
  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 342)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Desulfovibrio sp. 3_1_syn3"
                     /db_xref="taxon:457398"
     Protein         1..342
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=38300
     Region          10..342
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mkllqtmacm lalcaltlcg sarpasaaak evkllfpepy ssassyaegq avgiyygald
       61 fnmqnhpalr gkykmrwvgd vvkspadain avatgagqft ytlpqfieqf dpdwrvitap
      121 gvfkdmahfl ramdtpawka kqeslaetkg frilkwtnsi ghfwiwtkng padslaamkn
      181 qkirysgqqs yanafkalgl vgvalpytev vsalqtnmie gltndifgyt yydlprqtry
      241 mlpvplgfcp qalmvnrkww dslpeserka lefviaatdv hqyfedeeqr ilkwwdenpd
      301 tilvkmipea raeweavlrq atdefvrgvd palleairtt ag
//
LOCUS       WP_008686927             578 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein/permease
            [Longicatena].
ACCESSION   WP_008686927
VERSION     WP_008686927.1
KEYWORDS    RefSeq.
SOURCE      Longicatena
  ORGANISM  Longicatena
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Erysipelotrichaceae.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 578)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 578)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Longicatena"
                     /db_xref="taxon:1918536"
     Protein         1..578
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=65367
     Region          2..557
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 midkrllkem pqakvmvwkq vfmqwlgmls nigmvflfan ifvemfqdtl tlrnlmlcai
       61 gvilmiivrm ltsmqasrys yrascdvknh lrqriyekll elknsytqhi atselvqlsv
      121 egvdqletyf grylpqffys mlapltlfli lvwldwrssl vllvcvplip lsiiavqkfa
      181 kkllskywts yaslgdsfle nlqglttlki yqadgykhee mnkeaetfrr itmkvltmql
      241 nsvsvmdlia yggaaigsiv amiayrngsi slfavisivl lsseffiplr llgsffhiam
      301 ngiaasakif rlldiplqee akctlsdepi vmqlshvtfa ydqqrvvlqd vslnvlansf
      361 vsivgesgsg kstiaklccg fasdyqgsit vqgierssla dasfykkvmy vthkptiikg
      421 svrenlrmgn plasdealwk vlqdvciadf lqeqdgldtm leeggqnlsg gqrqrlamar
      481 alladrevyi fdeatsnidm esedailqli hrlkkektvl lithrlssvv dsdciyvmek
      541 gscveqgthe elrkqngvye rmfkqqqtle qfykeqtv
//
LOCUS       WP_008688270             117 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Rhodopirellula
            sallentina].
ACCESSION   WP_008688270
VERSION     WP_008688270.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula sallentina
  ORGANISM  Rhodopirellula sallentina
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 117)
  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 117)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Rhodopirellula sallentina"
                     /db_xref="taxon:1263869"
     Protein         1..117
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13217
     Region          29..82
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mtaktrrkpk rqtadrfavl nafadftake lrrsellvwl tlyrdtregv attsqrdian
       61 rcgidrktve rsiaslidrg llivvksggf rrgsasyrvl pmsrerldal prsrpnp
//
LOCUS       WP_008688556             188 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Longicatena].
ACCESSION   WP_008688556
VERSION     WP_008688556.1
KEYWORDS    RefSeq.
SOURCE      Longicatena
  ORGANISM  Longicatena
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Erysipelotrichaceae.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Longicatena"
                     /db_xref="taxon:1918536"
     Protein         1..188
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=20935
     Region          14..149
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mnlqafftlw qdvglilyai lkaflplpsl evvltplclk hpekwllysf egaigtcigg
       61 aigygiaysv grkalahias dediekgetl mrkhgllavf iggitpipdf llaylagftk
      121 mpflsftlcd gmarllrsii vtyglkslgt iihvdafgtw fsllilvwml yrwyqsrrkl
      181 rsqttskk
//
LOCUS       WP_008688822             301 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Rhodopirellula
            sallentina].
ACCESSION   WP_008688822
VERSION     WP_008688822.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula sallentina
  ORGANISM  Rhodopirellula sallentina
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 301)
  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 301)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Rhodopirellula sallentina"
                     /db_xref="taxon:1263869"
     Protein         1..301
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32489
     Region          55..293
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mshpedsvsr rsllsrslat aagaatlasa gsavaaesva eapagqsada kkgrlnqsvc
       61 kwcyrklsle emcqaatkfg lvgidllgpd dfptlkkhgl vctmvsshsl tnglcdrkfh
      121 dealekmnaa ieataaegwk nvicfsgnar gidrktgmkn cvdalkkivp vaeaagvtlq
      181 mellnskvnh adymcdnsew gvelvkqvgs dnfkllydiy hmqimegdii rtieknhpyy
      241 ghyhtagnpg rhelddtqel fyppiaraia dtgfqgyfah eflpvgdpla glenavaqci
      301 v
//
LOCUS       WP_008688926             666 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Longicatena].
ACCESSION   WP_008688926
VERSION     WP_008688926.1
KEYWORDS    RefSeq.
SOURCE      Longicatena
  ORGANISM  Longicatena
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Erysipelotrichaceae.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 666)
  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   3  (residues 1 to 666)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Longicatena"
                     /db_xref="taxon:1918536"
     Protein         1..666
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76393
     Region          10..666
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          167..>234
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 msffddslld mldvyiyesn dlfeqldril lthqqdhalt kedihaifrv mhttksssam
       61 mnlteiancm hrledvfgil rddpqrlqsh edtlftllyd vsdfmhqqld imkqesyqpa
      121 dpsffikrie elmnalqhke daetskipkq iqkpipepek avgantfylh llyeegcmme
      181 nvraymmvlq lkplcqqlht ypeelennkd aasyiqqhgf ylaitsdhpe qamkvaqnal
      241 fvqsckqkal kdtpfahdek kmnkkvgtlk eqketflsvr tdkldelqnl igemmiaret
      301 lkvymqttgn damvdfykqt fdklydhlee vvmsirlvpm ailvpklsrv vhdvavkegk
      361 dvvfkveged tefdkeivyr lfeplmhllr navdhglesk eerlrnkkss qceiilnveq
      421 sngevkiqvk ddgrglnaqr irekaiakgl lakdaqisdq elyqfllmpg fstkeeisei
      481 sgrgvgldvv kqminssngr laiqseagkg tsfilylplt lsiipaliir chtivyaipi
      541 haiehfcpwd tnvfsvqgqh vyyrykemsl pvlfldelyq qvgdktmqer knktliilns
      601 qgmkavlavd evietrnivd kplpgvlqdt yqqhtgisgy sllgdghicy dlraetllkn
      661 awkgre
//
LOCUS       WP_008689502             147 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Bacillota].
ACCESSION   WP_008689502
VERSION     WP_008689502.1
KEYWORDS    RefSeq.
SOURCE      Bacillota (firmicutes)
  ORGANISM  Bacillota
            Bacteria; Bacillati.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 147)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 147)
  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 147)
  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 147)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Bacillota"
                     /db_xref="taxon:1239"
     Protein         1..147
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17052
     Region          54..144
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(73,92..93,112,115,123..124,136,141)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mllsarqrqe lvnylldsqk qqknpadspf aisetnrgqt videpfteir mgdlyfcqeq
       61 rlvyigeqei kltakefdil allithpkrv ftyelimelv wnedysyysr kavnnhvsnl
      121 rrklkttpgs pdyiksvigv gykfevp
//
LOCUS       WP_008690729             400 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Longicatena].
ACCESSION   WP_008690729
VERSION     WP_008690729.1
KEYWORDS    RefSeq.
SOURCE      Longicatena
  ORGANISM  Longicatena
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Erysipelotrichaceae.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 400)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Longicatena"
                     /db_xref="taxon:1918536"
     Protein         1..400
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=46239
     Region          <94..397
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mltwkdmetl yerleaddci gvyieikqya qhylkdrqec qkaveildqm lsvmdpcicv
       61 sewmhgslft lwktiswtyi hdmiqqldda fphvafafgi cypkaqeels tlfykcqlaa
      121 ikskdhakyt tsyelydqll enrllqavst qemvekamak gnlrvfiqpk vdlatqticg
      181 geallrlyhe nqwlplsewm keiqrnsfir qtdvyvlhql fhmfalcqkq qfpllpisvn
      241 vseatlenaq eylmevkklt kasalsskll efeisedils kdnqalsdfl tvlhqegypi
      301 amddfgsgsa sltmlphlpf tsikldrsff pqpaneknnl mlqssirmlk qcgygivaeg
      361 vedecylpll keahcdqiqg hyyyqampms eylqllrswv
//
LOCUS       WP_008693434             657 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Fusobacterium animalis].
ACCESSION   WP_008693434
VERSION     WP_008693434.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium animalis
  ORGANISM  Fusobacterium animalis
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 657)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..657
                     /organism="Fusobacterium animalis"
                     /db_xref="taxon:76859"
     Protein         1..657
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=73357
     Region          1..657
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mkkkflllal ivlggisafa eespvlelkq tvvtsdsfgt pvretaknmt visakeikek
       61 gaktiadvlr gvpgvvvrqm dgaspmidlr gsgataqfnt villdgipvs glagfnlntv
      121 pvdeiekiev lqgagavmyg dgaiggvvni itkaptkkiv yggaglevgs wrtirenvyl
      181 ggkigdkfll nasysgntsk dyrdrspqyk nkkdkrdslw lrgkylldng siavnynhse
      241 dkdyytgsls kkqfddnprq vgswsgytyg indiinakyn qkkndkldif ltsgyyhnkd
      301 kfqknstsey flrpevkvty akdsyvtlgl dyrdgkrefk dgvfvngisq kapndkrksf
      361 agyimnkstf gnlqftqgyr rekvkyeyss kvydpmtwql keikpqsady anndsfefgv
      421 nylysdtgnv ffnytralrt ptiqdagawy gpvktqkndi feiglrdayk ntsistsvfy
      481 inskneiyyd ktnpfssnnq nfdgkvrrig aqlslahyfd kltlrervsy ivpkvtsgty
      541 dgkefagvsr wtanvgatyn itkgltanid gyyqsnayae ddfdnyfskg nnyvtvdanl
      601 syafengiel ytgvsnlfdk kyanavtstr stfgagprkv yypangrsvy agikytf
//
LOCUS       WP_008693989             258 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Novipirellula maiorica].
ACCESSION   WP_008693989
VERSION     WP_008693989.1
KEYWORDS    RefSeq.
SOURCE      Novipirellula maiorica
  ORGANISM  Novipirellula maiorica
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Novipirellula.
REFERENCE   1  (residues 1 to 258)
  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 258)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Novipirellula maiorica"
                     /db_xref="taxon:1265734"
     Protein         1..258
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28698
     Region          1..253
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mpnqlkpsvc idavfenvpl adavksvada gikafefwcw weknldeliq qrdangmsis
       61 acctkfislv dpekrseyla gleesiaaak qldcpvlisq vgdfrpgvsr qvqhqslvdg
      121 lreaapllea snitlviepl nelvdhagyy lvrsdeafei idkvnsprvk vvfdiyhqqi
      181 seghvihnlm qnidkighfh aagnpgrhel tlgelnyeqi faaiqsseyd gyvgleywpk
      241 hapseglrhv arwftaas
//
LOCUS       WP_008695516             191 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Fusobacterium ulcerans].
ACCESSION   WP_008695516
VERSION     WP_008695516.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium ulcerans
  ORGANISM  Fusobacterium ulcerans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Fusobacterium ulcerans"
                     /db_xref="taxon:861"
     Protein         1..191
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21278
     Region          2..157
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 milkalenvr shrsftdksl tktelskive garlgasakn sqsirffcvs dkklcdeife
       61 qikwaaavsw npvleespra yvilcacepl tqtsdpllhf dmgiasqnml lcageigygg
      121 civgsfnkke vekiiglqek yksyfilalg epkdkvkiva aenkdtryyr dtlnnhfvpk
      181 lslneliign k
//
LOCUS       WP_008695727             656 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Fusobacterium ulcerans].
ACCESSION   WP_008695727
VERSION     WP_008695727.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium ulcerans
  ORGANISM  Fusobacterium ulcerans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Fusobacterium ulcerans"
                     /db_xref="taxon:861"
     Protein         1..656
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=74253
     Region          1..656
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mkkalmvaai ltvsttimae eniasrrlte svistenfet svldtaknvt ivtqediqnk
       61 gastvaealr gvpgldirsm dgsdpvfdmr gsgatagsnt lvlldgvpln niegryftsq
      121 ipvdqidkie iipsggavmy gdgatggvin iitklpqdkk nygsvnmeag swntrkgtvn
      181 ygtkigdkfl ldtsytyteg dgyrtphpdy kdgdtkkslw lrgryllddg ylemrynynk
      241 vedsysdylt kekfddsikq hgasggkykn isneytltyn kklsdklsfl iyggytendy
      301 rykaiyypsa ynenkrniit qyyikpqlky tygedsyvif ggdykngkve dktsgnpdke
      361 kesyggyiln kttvgqfqft qgyrkersef dyfvtkygpg psftpsinnf kkkfssdaye
      421 lavnylysdt gsiylsftqg frtpstddlg awygdidvqe trsyefgikd mykntyisss
      481 iflidtdnei yynkyenfgd ganrnfdgkv rriggqislq hyfdkltlre nisyiqpkvt
      541 sgeydgkefa gvprwqgnig msynilsnmi fnidgyyfgk aynsddfsnk lgknddyitv
      601 dtnirynfnn gfeiyggirn lfdkeyanai lssrtgdkvy ypadgrsyya gfkysf
//
LOCUS       WP_008695992             223 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Fusobacterium ulcerans].
ACCESSION   WP_008695992
VERSION     WP_008695992.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium ulcerans
  ORGANISM  Fusobacterium ulcerans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 223)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Fusobacterium ulcerans"
                     /db_xref="taxon:861"
     Protein         1..223
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=25008
     Region          45..207
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mdlrkksial imglflsvvv fangtactqf hakelynemk lnglirydvf vqgvegfnki
       61 dkkeknilti vdfsrpstee rmyvldlenk eilfksyvsh gkntgdlyae nfsnvaesnk
      121 sslgfymtea pykgsngysl rlaglekgin dnamkrnivv hgadyanpem iktsgrlgrs
      181 fgcfavpvdm nheiidaikg rsiiyvyadk lkltkeryvs lnl
//
LOCUS       WP_008699647             286 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Fusobacterium ulcerans].
ACCESSION   WP_008699647
VERSION     WP_008699647.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium ulcerans
  ORGANISM  Fusobacterium ulcerans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 286)
  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 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   3  (residues 1 to 286)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 286)
  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   5  (residues 1 to 286)
  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   6  (residues 1 to 286)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Fusobacterium ulcerans"
                     /db_xref="taxon:861"
     Protein         1..286
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32994
     Region          22..102
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..284
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mdwifymqna idyiednlle sidyndvakr igfsnfhfhr tfallagmta neyirkrrls
       61 mageelsmsn akiidiafky gyetpesfsk afsrfhgfnp sdakksgtsl kkfsrfsikv
      121 kveggkimdy kieekgsmkf ltasksflne iinekgnrev sdfwtesfkn gtietlkkns
      181 vdsgiyglcl pvskesdsfk ygigvkstdi hnnvenfeiw tvkpsmwavf kcigndgqci
      241 admwerifse flptspykmt eqadleyyye nnenifcelw vpverk
//
LOCUS       WP_008700171             327 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LytR C-terminal domain-containing protein
            [Fusobacterium].
ACCESSION   WP_008700171
VERSION     WP_008700171.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 327)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..327
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=36928
     Region          161..244
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 matkkkkkkk grapvlvivl avilsillyf nfrgnnikls kdervliigk qnlyavyedk
       61 lavkipfely idseetvedl vdsqnyenvl ekinsivpek ltrytviksg eikldvenar
      121 nipetnigdr ryiltssvya mfkdlyhekn avdelnenil vdvlnangig gyarktgeli
      181 knslgmkyna anyettqdqs yvilndiske kaaeildklp ekyfkiknks siptlanivi
      241 iigsekkinf kidiyanqtn lkeasdkika agygnitshp ekedteqsii eynkedyfva
      301 qkiakvlgit dmvensdlen kigitik
//
LOCUS       WP_008618610             166 aa            linear   BCT 20-JAN-2025
DEFINITION  transcription termination/antitermination protein NusG
            [Paramagnetospirillum caucaseum].
ACCESSION   WP_008618610
VERSION     WP_008618610.1
KEYWORDS    RefSeq.
SOURCE      Paramagnetospirillum caucaseum
  ORGANISM  Paramagnetospirillum caucaseum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Magnetospirillaceae; Paramagnetospirillum.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Kang,J.Y., Mooney,R.A., Nedialkov,Y., Saba,J., Mishanina,T.V.,
            Artsimovitch,I., Landick,R. and Darst,S.A.
  TITLE     Structural Basis for Transcript Elongation Control by NusG Family
            Universal Regulators
  JOURNAL   Cell 173 (7), 1650-1662 (2018)
   PUBMED   29887376
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Liu,B. and Steitz,T.A.
  TITLE     Structural insights into NusG regulating transcription elongation
  JOURNAL   Nucleic Acids Res 45 (2), 968-974 (2017)
   PUBMED   27899640
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Steiner,T., Kaiser,J.T., Marinkovic,S., Huber,R. and Wahl,M.C.
  TITLE     Crystal structures of transcription factor NusG in light of its
            nucleic acid- and protein-binding activities
  JOURNAL   EMBO J 21 (17), 4641-4653 (2002)
   PUBMED   12198166
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415705
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Paramagnetospirillum caucaseum"
                     /db_xref="taxon:1244869"
     gene            1..166
                     /gene="nusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
     Protein         1..166
                     /product="transcription termination/antitermination
                     protein NusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
                     /calculated_mol_wt=18593
     Region          1..162
                     /region_name="NusG"
                     /note="Transcription termination/antitermination protein
                     NusG [Transcription]; COG0250"
                     /db_xref="CDD:440020"
ORIGIN      
        1 mswyvvytkp naernaethl grqgftsycp hfsrtrrhag reekvlrplf prylfvsmds
       61 essrwrairs tigvshlvcq getplpvpee vieairsrev gglivdgmpp tpqpgeqvrv
      121 idgpladqig tllkltdser vvvlmnmmqg evrvdlprda vracpq
//
LOCUS       WP_008682593             205 aa            linear   BCT 20-JAN-2025
DEFINITION  metallophosphoesterase family protein [Rhodopirellula sallentina].
ACCESSION   WP_008682593
VERSION     WP_008682593.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula sallentina
  ORGANISM  Rhodopirellula sallentina
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 205)
  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 205)
  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 10005392
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Rhodopirellula sallentina"
                     /db_xref="taxon:1263869"
     Protein         1..205
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21317
     Region          2..204
                     /region_name="COG2129"
                     /note="Predicted phosphoesterase, related to the Icc
                     protein [General function prediction only]"
                     /db_xref="CDD:441732"
ORIGIN      
        1 mkvlcfsdlh rdkdaalrlv emskgadvvi gagdfanqhq gladtleilr aielpsflvp
       61 gngetvdela dasrewksav vlhgngttat tstgsvelwg vgggipvtpf gawsydfdee
      121 sgaemlagcp sggilvvhsp pintvdhdss grirgsqsir dcvercspkl vvcghihsdw
      181 gkqvsvgdsl vvnagpsgvi vdvdv
//
LOCUS       WP_008702392             453 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Novipirellula maiorica].
ACCESSION   WP_008702392
VERSION     WP_008702392.1
KEYWORDS    RefSeq.
SOURCE      Novipirellula maiorica
  ORGANISM  Novipirellula maiorica
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Novipirellula.
REFERENCE   1  (residues 1 to 453)
  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 18888537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Novipirellula maiorica"
                     /db_xref="taxon:1265734"
     Protein         1..453
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=47544
     Region          288..330
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
     Region          337..451
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mqtlktaaii vllmtvmyta ymslttppds lppeverivm deggldiesg lpeslgemei
       61 sggvpesaat adsgvptfgq sfadlpdadv dgsamthggs spsgvsiqls dshgndnltv
      121 hqpsddapay mdlgastgtq aslasastgv sapaaspsyg atdmtfnmpd psseenklpe
      181 gdsvafdpsa gpgtamaela aagdgddnia tvsgvsdptk nniglanalq ladeqyksdq
      241 rkealetlsl fyhtpnlpaa qreellsrld plaaeviysr rhlleqphrv ghhetlmqia
      301 vkyevpwqll aningiedpi tvlpgtelkv vrgpfradvd lgkkemtlfl gdlyagrfpv
      361 avgndpqprp gtftvqdkqa erpfygasgs pvpanspdnp ygslwldlgg qlcihgspya
      421 trpsdqgcis vaadyaddly giltqgssvt irr
//
LOCUS       WP_008701863             242 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Fusobacterium].
ACCESSION   WP_008701863
VERSION     WP_008701863.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (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   2  (residues 1 to 242)
  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 242)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..242
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28121
     Region          18..72
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 merpgyygil pasvrydkkl kpmekimyse ltalsnkngy cnatnsyfae lyevgkntvs
       61 lwisdlekag yiktkliyet gtkiikerri yisdpitknn dtyhekevdp itknndtpit
      121 knrednntsi nntrliitnn nnleniiedq eqeekvvvns ngalqqeikm llgvrkikpy
      181 diiklnkpie rikfvidfcn knnkadgylf kalkddwelk evqqeekpcy ftkpkeayke
      241 lv
//
LOCUS       WP_008702769             192 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Fusobacterium].
ACCESSION   WP_008702769
VERSION     WP_008702769.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 192)
  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 192)
  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   3  (residues 1 to 192)
  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   4  (residues 1 to 192)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 192)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..192
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21900
     Region          1..191
                     /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"
ORIGIN      
        1 mslrvvvved etltridlie ilkengydvv geaadgieav evckklqpdi vlldikipyi
       61 sglkvanilk eegfkgcvii ltayniaeyi qeasntivmg yilkpidevi flerlnliyk
      121 nyklyddlri evedtkkkle erkvierakg ivmskytlse eeaykkmrdl smqkrismfk
      181 lseiiimtgg le
//
LOCUS       WP_008702915             185 aa            linear   BCT 20-JAN-2025
DEFINITION  transcription termination/antitermination protein NusG
            [Novipirellula maiorica].
ACCESSION   WP_008702915
VERSION     WP_008702915.1
KEYWORDS    RefSeq.
SOURCE      Novipirellula maiorica
  ORGANISM  Novipirellula maiorica
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Novipirellula.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Kang,J.Y., Mooney,R.A., Nedialkov,Y., Saba,J., Mishanina,T.V.,
            Artsimovitch,I., Landick,R. and Darst,S.A.
  TITLE     Structural Basis for Transcript Elongation Control by NusG Family
            Universal Regulators
  JOURNAL   Cell 173 (7), 1650-1662 (2018)
   PUBMED   29887376
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Liu,B. and Steitz,T.A.
  TITLE     Structural insights into NusG regulating transcription elongation
  JOURNAL   Nucleic Acids Res 45 (2), 968-974 (2017)
   PUBMED   27899640
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Steiner,T., Kaiser,J.T., Marinkovic,S., Huber,R. and Wahl,M.C.
  TITLE     Crystal structures of transcription factor NusG in light of its
            nucleic acid- and protein-binding activities
  JOURNAL   EMBO J 21 (17), 4641-4653 (2002)
   PUBMED   12198166
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415705
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Novipirellula maiorica"
                     /db_xref="taxon:1265734"
     gene            1..185
                     /gene="nusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
     Protein         1..185
                     /product="transcription termination/antitermination
                     protein NusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
                     /calculated_mol_wt=21249
     Region          21..184
                     /region_name="NusG"
                     /note="Transcription termination/antitermination protein
                     NusG [Transcription]; COG0250"
                     /db_xref="CDD:440020"
ORIGIN      
        1 mpilpeepdc fpedllshps aesmywwlmy tksrqekqlm rhlqkhevwh ygplipqrkr
       61 spagrmrtsy vplfsnyifv cgendearyq aicsgcvqka teitevddlv adlrqinsli
      121 dlgvpmties rlepgqnvri rsgsfagyeg tilrreqetr llvcvrfmeq gvsvkledcq
      181 lelig
//
LOCUS       WP_008704044             521 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Blautia wexlerae].
ACCESSION   WP_008704044
VERSION     WP_008704044.1
KEYWORDS    RefSeq.
SOURCE      Blautia wexlerae
  ORGANISM  Blautia wexlerae
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Blautia.
REFERENCE   1  (residues 1 to 521)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Blautia wexlerae"
                     /db_xref="taxon:418240"
     Protein         1..521
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=58132
     Region          <137..>256
                     /region_name="YoaR"
                     /note="Vancomycin resistance protein YoaR (function
                     unknown), contains peptidoglycan-binding and VanW domains
                     [Defense mechanisms]; COG2720"
                     /db_xref="CDD:442033"
     Region          253..374
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          394..518
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(471..472,475,493..496,498)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mgnkeeknnt vpngsmeitg rrhksarpgr isyvpisded lapyeppvrk khkglkitgi
       61 avamvilsag aayagmsyyy sdkffegtsi ngidcsgkta yeaeqkiakt venysievds
      121 rnldpqtisg dqigysyvsd gsvlkllkdq kpyewirgff ekksytaaen ttydkeklkk
      181 qvkalncaqk enqvapenay vaygdsqfei vpetegskld lknaynvlse avsgnktsvd
      241 fdsepdvyvk aditsdnpdl qaslnacnnf tkasitytfg detetldgnt ikdwlnfdek
      301 gqlimddtsf rqhiadyvaq laaahdtvgt erefqttsgr tvsvygsayg wqidqtseva
      361 qltqeiqsgt qttrepvysm tanahgyndi gntyievdls eqhmyfyqng edifesdivs
      421 gdmrysdrqt pagiytiyyk kspdvlrgkq langkyeyeq pvtywmpfng gigfhdanwq
      481 pyfggdrfme ggshgcinmp pekaaelyni idcnipivcf y
//
LOCUS       WP_008704904             184 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator [Blautia].
ACCESSION   WP_008704904
VERSION     WP_008704904.1
KEYWORDS    RefSeq.
SOURCE      Blautia
  ORGANISM  Blautia
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 184)
  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 184)
  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   3  (residues 1 to 184)
  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   4  (residues 1 to 184)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 184)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Blautia"
                     /db_xref="taxon:572511"
     Protein         1..184
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=20767
     Region          1..177
                     /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"
ORIGIN      
        1 msssivialp kiedakkirt ilnrhgltva svcssvsnal aniseldsgv licgykltda
       61 yykdalddlp qyfemlllas qriideapns vstvqmpmka salidtvndm lyhlerrikk
      121 ekkkpkprse keqnyisnak rllmeknqmt eeeayrhiqk csmdsgtnmv etaqmllmlm
      181 ydei
//
LOCUS       WP_008705215             412 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: galactokinase [Blautia].
ACCESSION   WP_008705215
VERSION     WP_008705215.1
KEYWORDS    RefSeq.
SOURCE      Blautia
  ORGANISM  Blautia
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   McAuley,M., Kristiansson,H., Huang,M., Pey,A.L. and Timson,D.J.
  TITLE     Galactokinase promiscuity: a question of flexibility?
  JOURNAL   Biochem Soc Trans 44 (1), 116-122 (2016)
   PUBMED   26862196
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Holden,H.M., Thoden,J.B., Timson,D.J. and Reece,R.J.
  TITLE     Galactokinase: structure, function and role in type II galactosemia
  JOURNAL   Cell Mol Life Sci 61 (19-20), 2471-2484 (2004)
   PUBMED   15526155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Blautia"
                     /db_xref="taxon:572511"
     Protein         1..412
                     /product="galactokinase"
                     /EC_number="2.7.1.6"
                     /GO_function="GO:0004335 - galactokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0005534 - galactose binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0046835 - carbohydrate phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=45201
     Region          22..390
                     /region_name="GalK"
                     /note="Galactokinase [Carbohydrate transport and
                     metabolism]; COG0153"
                     /db_xref="CDD:439923"
ORIGIN      
        1 mnipnknelt riygeaeksa arfqavadhf aeiyhhdiae fftapgrtei ignhtdhngg
       61 rviagsidmd tigaaypnns sviritsegy dkevvvdind lasvpkaqgt vslvagmvea
      121 iqkfgfkvag fdayvttnvi raagvsssas femlvcsiin yffndgamty inyakagqya
      181 envywlkasg lmdqlacavg gpilldfsdr enpkyekvnf sfhdydhhlv ivntgkghad
      241 lseeyseipm emkeaakaag aellcettle kvlanmdkid ndrailraih ffkenerver
      301 aakaveekdg etvlkllses gksswellqn cypikayteq kisvalaltd lfleklgkgi
      361 crihgggfag vimcvvpeee tenyvsyise fagkenvypm niravgavhi ek
//
LOCUS       WP_008707539             655 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter permease [Blautia].
ACCESSION   WP_008707539
VERSION     WP_008707539.1
KEYWORDS    RefSeq.
SOURCE      Blautia
  ORGANISM  Blautia
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 655)
  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 655)
  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 655)
  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 655)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Blautia"
                     /db_xref="taxon:572511"
     Protein         1..655
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=69790
     Region          22..655
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mkenkikkan tspegqagse nmstadvdav mkkydresni rvwtgkykla vrgllvafsl
       61 wciyvtlfat fleeirltsf lgliiligfl typakkgdir enympigdii fmiagtgafl
      121 yftfsanqii nqgtrfapyq ivigiigiaa lieltrrcvg lpilfvagff liyalavglt
      181 npaflgrvkf lvrnlfytke gifstpvnvc skyivvfiif gaflertgis nffiqlanci
      241 agkyaggpak vavissalcg mvsgssvgnt vttgsvtipm mkdtgykpef agaveaasst
      301 ggqimppimg aaaflmadfv gvpysniivr ailpallyft gifisvhlea kklglsgipk
      361 eklpvfklli rkiylllplv mlviwvsgny mtmqkaasya ivlsvivslf dkenrisvtk
      421 cidaleaggr gvisvavacg vagiisgsit mtglandlin giisvangkl iiallltmlc
      481 civlgmgvpt tanycimaat capilvrmgv ptlaahffvf yfgivaditp pvalaayags
      541 aiakanpmkt aftasklaia vfivpyvfcf npamllidtt plkvvqifit sligvfglss
      601 slegflsvkm svpvrvlmaa gglmlidpsl mtdvvgilli vgccvwqtaq kkkta
//
LOCUS       WP_008708554             251 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Novipirellula maiorica].
ACCESSION   WP_008708554
VERSION     WP_008708554.1
KEYWORDS    RefSeq.
SOURCE      Novipirellula maiorica
  ORGANISM  Novipirellula maiorica
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Novipirellula.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Novipirellula maiorica"
                     /db_xref="taxon:1265734"
     Protein         1..251
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=27943
     Region          6..>54
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
     Region          142..219
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mripfsrlkn aaiegadgfv gsvkdvlfds qewgvrylvv dtgkwlpgrq vllppavleh
       61 tdwrsgtakv sltrsqvkas pdvsvhqpis rqkeaelmsh yavpfywgpa gatlagggpp
      121 tfpletalsv qadshateig dphlrsasev qgydiratde aighvedfvl dddgwivryl
      181 vvdtrnwlpg rkvlvaihwi eaiswgeasv tvgltsdrik qspefdpsew idreyeerlh
      241 hhygrsgywm m
//
LOCUS       WP_008709247             641 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Cloacibacillus evryensis].
ACCESSION   WP_008709247
VERSION     WP_008709247.1
KEYWORDS    RefSeq.
SOURCE      Cloacibacillus evryensis
  ORGANISM  Cloacibacillus evryensis
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Synergistaceae; Cloacibacillus.
REFERENCE   1  (residues 1 to 641)
  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 641)
  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 641)
  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 641)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Cloacibacillus evryensis"
                     /db_xref="taxon:508460"
     Protein         1..641
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=68080
     Region          2..635
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mnklwkllte egkkrklsgf daltvkyvav imslyqlaqa tfltiqpqmh yaihltfimv
       61 lcaliytrtf qtnqrtstrv piedwiyaai lalagiyyct qmetyltrmp mvdelsslei
      121 viglltviav igltkrcmgf vlpsigcifl ayalwghlip gvlyhrklla idildqlvft
      181 tngiysspia aaatyvfmfv mfgsffaasg agdffykfsm avagryagga gkvaiitsgl
      241 fgmingspta nvvttgsfti pmmkkagydg tfsgavtava atgggimppi mgtaaflmve
      301 magisyknia iaafvpgvly ylalllivhf rakkcglvgl dvselpsvwg tlkegwiflv
      361 plvvlvvmlm rgytanlsav vgiaaviaas wvrketrmhl pavikaleda arsavivsls
      421 cavagcviag lmttglsgkl aslilslggn stlsalilta aictllgmgm pvaaayclta
      481 alcipslyel glqpleahmf vvyfatlsai tppvavasya aagiseanaa tvgwqacrig
      541 lvsfivpfif vfepmlmvtp anfclqsvwi vtsatlgvli lcaglegylk keipmllrgv
      601 lviggllliy pgaitdyigl gvmalllvqq fagtkfgret n
//
LOCUS       WP_008710160             357 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Cloacibacillus
            evryensis].
ACCESSION   WP_008710160
VERSION     WP_008710160.1
KEYWORDS    RefSeq.
SOURCE      Cloacibacillus evryensis
  ORGANISM  Cloacibacillus evryensis
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Synergistaceae; Cloacibacillus.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 357)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Cloacibacillus evryensis"
                     /db_xref="taxon:508460"
     Protein         1..357
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38337
     Region          11..344
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mpefalaevd nvrvagisaa vpsriidnav fgielygeei egvikttgvr errtspegsv
       61 tsldlcvkaa eslrdtgnid fntlggvvcv tqtpdcllpn nstyaqhqlg lpvstaafdv
      121 nlacsgyiyg lwlasisars lnkpvllldg dthshfaspq dratallfgd agtatiiepc
      181 egapawtfaf etdgskrdal iipeggyrnr inehsseyrt fpdggirrgi dmkmdgmevf
      241 nfvvrsvpkc leylmsevss tpedydvlal hqanlfmvrq vakkmkfpme kvpttiqkyg
      301 nsssatipvt laselhgqis skklkvlasg fgaglslasv smelgpchcp gvieyec
//
LOCUS       WP_008710941             661 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Cloacibacillus evryensis].
ACCESSION   WP_008710941
VERSION     WP_008710941.1
KEYWORDS    RefSeq.
SOURCE      Cloacibacillus evryensis
  ORGANISM  Cloacibacillus evryensis
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Synergistaceae; Cloacibacillus.
REFERENCE   1  (residues 1 to 661)
  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 661)
  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 661)
  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 661)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..661
                     /organism="Cloacibacillus evryensis"
                     /db_xref="taxon:508460"
     Protein         1..661
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=70606
     Region          16..642
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 meekkqnksl ledismdeaq vsslvekyda esryrrltgv qgifislwla amalfhlyta
       61 giatmpitiq ravhltfaiv avfilfpasr ksskmktpwy dwllaaaagg vtgyivfffn
      121 diarrgaepi dyeiylgiaa illvleagrr vvgnvlpcms vifllycyfg nyapgifqir
      181 gyslsriiqh myltpegifg lalgvsatfv ivfiifgayl sqsggakffn elalalagsk
      241 pggpakvavv asgllgting ssvanvattg tftiplmkkv gyppyyagav eacastggql
      301 mppimgagaf imseflnipy lsiaaaaiip aliyytaift nvhirarkqk lqgipkselp
      361 svgevmrsdg hllvpvivvi vtlllkytpl ragfigvvsv iivsslkknt rmtlrdnfna
      421 lvegargglg valacalvgf ivgtssltsl gltisnniie isggnlmltl vmamvaclvl
      481 gmglpttany ivcstiiapa ligmkvlpls ahlfvfyfgi madltppvcl aaftgagiag
      541 aspaktgmta trialasyll pycfvynpml llhnvevvel vvlvisavlg vvalagsfeg
      601 wfyrdlknye rvvfgviall sihhdfwisi aaivgialmi vyfkksshdg qlpekfeevs
      661 a
//
LOCUS       WP_008710319             327 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Cloacibacillus
            evryensis].
ACCESSION   WP_008710319
VERSION     WP_008710319.1
KEYWORDS    RefSeq.
SOURCE      Cloacibacillus evryensis
  ORGANISM  Cloacibacillus evryensis
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Synergistaceae; Cloacibacillus.
REFERENCE   1  (residues 1 to 327)
  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 327)
  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 327)
  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 327)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Cloacibacillus evryensis"
                     /db_xref="taxon:508460"
     Protein         1..327
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=36343
     Region          1..327
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mkksvfmfcc alciafwgit anqaeavmkl qlaheqpeih pyhigavefa klvkeyskge
       61 mevtifsngt mgkasalaes csmgtmdfas vfsiileays pkfgvltmpy cfrdwdhsdk
      121 vldgpigdel kasveskgik vlafwrngla evhsrmpirt pedikgkklr iqegpsyaal
      181 skalgtvttp msfgevysal qlgtvdaqtq tinniyaskm fevgkyftki nmnfntqpfi
      241 msmqlwkslt peqqdiiera algatkaera yhvkdtqtsy dgfvkgggkv ielnkaelek
      301 wkdvcapvyk apqfsavmei fnriqkq
//
LOCUS       WP_008713106             656 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Cloacibacillus evryensis].
ACCESSION   WP_008713106
VERSION     WP_008713106.1
KEYWORDS    RefSeq.
SOURCE      Cloacibacillus evryensis
  ORGANISM  Cloacibacillus evryensis
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Synergistaceae; Cloacibacillus.
REFERENCE   1  (residues 1 to 656)
  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 656)
  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 656)
  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 656)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Cloacibacillus evryensis"
                     /db_xref="taxon:508460"
     Protein         1..656
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=69239
     Region          28..643
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mseteakvid qveenaqidl ddlmrkydte arfraltgwq gkmvallava mscfhfytsg
       61 fglllaqkqg avhlaftlal vfllypassk qsktsgipfy dfilaglgva samylvvffn
      121 dlvtraglpt tvdlvmgfvl iatlleatrr isnpvlpcla vvallycyfg rympqmlahr
      181 gfsvarivnh mylgtegifg tplevsstfv fmfilfgsvl ektglgrfii dlsmalagws
      241 tggpakvaiv ssglmgtvsg ssvanvcttg mftiplmksv gyephfagav eavastggqi
      301 mppvmgagaf imaqflgvpy ievaiaavvp allyyfavmv qvhfeacrlg lkgipwaqlp
      361 piwpllrskg fllipliaii yfllagytpl maafngilvs fvlswlnket rltparifea
      421 fqsgargaig vacacatvgm vvgmgtltgl alriagaivs aaggskiltl vftmcasill
      481 gtglpttanf ivtstmaapa lfqlgvpaka aymfvfyfgi aadltppval aayagsgiag
      541 sdpmktgmta fklalagflv pyiyvyspml lfidvvplem vqaictalig vfllamftig
      601 ffkapmawym rilafagalg llipgtasdl aglavlvviy avqvakakkl aanaaa
//
LOCUS       WP_008711344             850 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Cloacibacillus evryensis].
ACCESSION   WP_008711344
VERSION     WP_008711344.1
KEYWORDS    RefSeq.
SOURCE      Cloacibacillus evryensis
  ORGANISM  Cloacibacillus evryensis
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Synergistaceae; Cloacibacillus.
REFERENCE   1  (residues 1 to 850)
  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 850)
  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 850)
  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   4  (residues 1 to 850)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..850
                     /organism="Cloacibacillus evryensis"
                     /db_xref="taxon:508460"
     Protein         1..850
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=95328
     Region          97..818
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mslikdkqls adklrraadl aalgfkttkg ldklagligq eravrsvgfg lsvqskgyni
       61 fmvgepgcgr tsyaleelrr aasdmpapdd wvyvynfddp slplaislpa gkgrelakda
      121 edaiedlkta lskafdnnef ednkaqlvks fqdevntime elrkwaeskd faikrtpqgf
      181 vnlplimapp lpqhdegqde addkdnktee gekqlvrrem qqdefeklsd eeqevlqkvs
      241 eeisqktlek lrlirereke lkekikeles qicrvaitpi laelrgkhmp neklakwlda
      301 ltedlianfs vflaavrdda aevdfsryev nafvsnnpnd gapvicetnp iyynlvgkvd
      361 yenrqgnlyt dfrritpgam hranggflll dadellrqfm swdvlkrvlr yrelsienlg
      421 eqlgyipvss lrpepipiem kvvivgtpyl yyllniydpe fqkvfkikae fdsemprtge
      481 seyqiaqfva gfvaregkln ftvtavgevi ewasrlaedr nklstqlnki advlvestay
      541 akaegkklvg vdhvrralee kihradmwed kvleeyrkgv iridtegsvv gqingltvsq
      601 lidhsfgspv ritanvfmga egvvnierev smtgpihnkg lmiltsylgr myardfplsv
      661 sariafeqty ggiegdsass telyclmsai agipleqgia vtgsvdqmgf iqpiggvnek
      721 iegffrycka ngftgkqgvi ipvqneqhlm lnhevteavr knkfhiwsvs tidegieilt
      781 gvpagtkdek ggypknsvhg rvqaalegwi ersfrykkvm tdrvdppkkr srrktapamn
      841 eeptvvkeae
//
LOCUS       WP_008713198             652 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Cloacibacillus evryensis].
ACCESSION   WP_008713198
VERSION     WP_008713198.1
KEYWORDS    RefSeq.
SOURCE      Cloacibacillus evryensis
  ORGANISM  Cloacibacillus evryensis
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Synergistaceae; Cloacibacillus.
REFERENCE   1  (residues 1 to 652)
  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 652)
  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 652)
  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 652)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..652
                     /organism="Cloacibacillus evryensis"
                     /db_xref="taxon:508460"
     Protein         1..652
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=69112
     Region          1..640
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mahteesnst tawgclfnar rfgarellaf livglsfafv tfhlytgmfg hpeahfyrsl
       61 hltgvlllcf tlfplnrksw sdkpniwtvi diaciilsva levyylwdie afelrqvtsp
      121 ntadicmgvi lwllvlegtr ralgvpmvli avfftfqaly sekmfwifyg psttlkslvl
      181 dmfmqeggif gmplgtiasf vvlflifgaf meetgtgrtf tdlalgafgs kvggpakaav
      241 vgsaffgmls gsscanvttt gtftiplmkr vgyestyagg veacastggm ftppimgata
      301 fvvaaylgls yatvalaaai palcyyfalf aavdfharka kipplskeem pvvkdvlkng
      361 ahlllpigll vyflvsgyta ttacfwsivg lfivsflkks srpgaeniis vceaagkatv
      421 vtamacaaag iivssstlsg vglklgtqiv sisgghlwla mllaavlavi lgmgltttav
      481 yiimvvtvip pimqmgvpal aahmyalfwg vlsniippva iasftaagia kagpmktaar
      541 gfviglpgll vfatfvynpg limigtvsdi vinsvgclia vvcfaavveg yaftkinilf
      601 ramlavcsli slsprwdltf aglaggviil tlnylaakke dlnfgqgqkq ea
//
LOCUS       WP_008713408             130 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Cloacibacillus evryensis].
ACCESSION   WP_008713408
VERSION     WP_008713408.1
KEYWORDS    RefSeq.
SOURCE      Cloacibacillus evryensis
  ORGANISM  Cloacibacillus evryensis
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Synergistaceae; Cloacibacillus.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 130)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 130)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Cloacibacillus evryensis"
                     /db_xref="taxon:508460"
     Protein         1..130
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=14406
     Region          2..127
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(6..9,41..43,46,70,109,123)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 migyfdgasr gnpgeagaga llldegenti wetarylgkk tnneaeynaa illltaaker
       61 gvkelkvygd sklvvcqlsk qwkinlphlr elakraweis egmtvryewv praknkrade
      121 lsneaidnak
//
LOCUS       WP_008714131             396 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Rhodococcus sp. AW25M09].
ACCESSION   WP_008714131
VERSION     WP_008714131.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. AW25M09
  ORGANISM  Rhodococcus sp. AW25M09
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Rhodococcus sp. AW25M09"
                     /db_xref="taxon:1268303"
     Protein         1..396
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42068
     Region          1..272
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          272..359
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrilhtsdwh igrtfhgvdl ladqgavlgs iaelvaaqsi dvvvvpgdiy dravpsadav
       61 lvcnrglesi raagavivat sgnhdsparl gagaafasag glhlmtrvgd vatpvviede
      121 hgdvafygip ylepettrle ldvpaartha evlgaamnrv rgdlaartea gqhvrsvvla
      181 hafivggeat gsersissgg ietapaaafd gvdyvalghl hspqvltdrv rysgsplpys
      241 fgershrkav wileldangl gsvarvdlpe vrglariegt veqllsdtay sefedhyvsa
      301 vltddvrpvd amrllqqrfr yaihlewrrp egsgelryrd rvrgrsdldi atsfltdmrs
      361 aptaaesall aralvsvqre seatdgtatt gdrgaa
//
LOCUS       WP_008715066             410 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: exonuclease SbcCD subunit D [Veillonella].
ACCESSION   WP_008715066
VERSION     WP_008715066.1
KEYWORDS    RefSeq.
SOURCE      Veillonella
  ORGANISM  Veillonella
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Veillonella"
                     /db_xref="taxon:29465"
     Protein         1..410
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46499
     Region          1..301
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          297..382
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrflhtadwh lgrifygqyl tedqahvleh qffnilkden idgillagdi fdravppiea
       61 ielwdsiitr lamdckvplf vvsgnhdgae rlemgrsmlg qsgihiwgsp hhalmpfefe
      121 gtdgkvaicp mpfseprrig ealfadvest ntettdteia divtpcyeqn cesvlnlhny
      181 dqmyqawsdh lykqvpkgmc siaishafvm ggevggsert lsvggseqvn pqvfkdfhyt
      241 alghlhgpqr mgadhirysg splkysfdeh mqkksftiid mdtkgnvdin tipveakrdv
      301 vilegyfedl lndkalqakh rddyvqarll dtmpimdgma klrqvyhrcm tidlvgrvag
      361 piadmgeaif kelnerdlfn qfaetvwkep ltekeqqyin svwdrilked
//
LOCUS       WP_008715651             404 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Rhodococcus sp. AW25M09].
ACCESSION   WP_008715651
VERSION     WP_008715651.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. AW25M09
  ORGANISM  Rhodococcus sp. AW25M09
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
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   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   4  (residues 1 to 404)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Rhodococcus sp. AW25M09"
                     /db_xref="taxon:1268303"
     Protein         1..404
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=43145
     Region          12..316
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 msekttvsga eivlenvtks ysgqkdaavd nvsmtipage vvvlvgpsgc gktttmrmin
       61 rlieptsgri tiggkdalsi npnelrrtig ysiqqaglfp hmtiaenvgm vpgligwkka
      121 kisdrtdeml dlvgldpaly rgryprqlsg gqqqrvgvar alaadppvll mdepfgavdp
      181 itrgllqdel mrlqaelgkt ivfvthdfde avklgdriav lgnqsrilqf dtpeavlanp
      241 addtvagfvg agaalkqltl mrvrdielsd vpvmaedqpv eamnaalgnd peawgiilda
      301 rkrpirwtdr rhltgakslr dvgvpmgemv stqstlqdal eallaegnat atvtgqrgey
      361 agtitieali dtiktirsqh ahdhdekahd tdtaaddvta gsps
//
LOCUS       WP_008715830             197 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Rhodococcus sp. AW25M09].
ACCESSION   WP_008715830
VERSION     WP_008715830.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. AW25M09
  ORGANISM  Rhodococcus sp. AW25M09
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Rhodococcus sp. AW25M09"
                     /db_xref="taxon:1268303"
     Protein         1..197
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21663
     Region          87..171
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 msidttphtr rrwplwlaac tvavvvvvgv lwlapsryfp wdteafpevn sselnsdqar
       61 vvellraehe qqrpgtfyae gvdeawcadf vswimkeadv plsnpnsgsw ripgvytlqe
      121 yyeqqgrfet vgtytpavgd vvlydnasws gqhtnvivav dgdeaitvgg neggkirvhs
      181 lhygsdsgvv gfgrlts
//
LOCUS       WP_008716305             323 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Rhodococcus sp. AW25M09].
ACCESSION   WP_008716305
VERSION     WP_008716305.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. AW25M09
  ORGANISM  Rhodococcus sp. AW25M09
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Rhodococcus sp. AW25M09"
                     /db_xref="taxon:1268303"
     Protein         1..323
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33993
     Region          9..314
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 msrmtapgks plllldgasl wfrayyalpe sitapdgrpv navrgfldmi saliartepg
       61 rlavcldldw rpqfrvdlvp sykahrvaea npevaeseev petltpqvdm imdvlaalgi
      121 atagaeglea ddvlgtlaar erqdpvvvvs gdrdllqvaa depnevrvly vgrglakael
      181 fdpalvsery gvplhragaa yaelallrgd asdglpgvkg igektastlm lqyesvaavr
      241 saaldpssdm akgiraklan asdyldaalp vvrvvtdadv vlsksdeipa eptdrerlng
      301 laeslgvena varlvaamaa tas
//
LOCUS       WP_008716706             493 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Clostridium pacaense].
ACCESSION   WP_008716706
VERSION     WP_008716706.1
KEYWORDS    RefSeq.
SOURCE      Clostridium pacaense
  ORGANISM  Clostridium pacaense
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Clostridium pacaense"
                     /db_xref="taxon:1917870"
     Protein         1..493
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=53210
     Region          1..493
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mqdivkinrn dnvavalrpv skgetldveg rkvaiqedip qghkfalkdi gsgaevikyg
       61 frigyakedi keggwvhvhn vrtalgdvlt ydytpdgtdv qptehvcfdg yrrsdgkagi
      121 rneiwiiptv gcvnsiakal eararelvkg svedviafph pygcsqmgdd qentrkvlad
      181 mihhpnaggv lvlglgcens nipvlmdyig dydkdrvkfl qcqdvedeme aamdllkela
      241 vyagaftrek idaselvigm kcggsdglsg itanpvvgaf sdllvskggt tiltevpemf
      301 gaetllmnrc atpelfektv nlingfkdyf tshnqtiyen pspgnkkggi stledkslgc
      361 tqksgsalvr gvleytemvk vkglnllsap gndlvastal alsgahmvlf ttgrgtpfas
      421 pvptvkissn sklaghkdnw idfnagrmve dmtkeelaee lldyvlavas grkvkseeag
      481 fhdmaifkqg vtl
//
LOCUS       WP_008717345             385 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Clostridium pacaense].
ACCESSION   WP_008717345
VERSION     WP_008717345.1
KEYWORDS    RefSeq.
SOURCE      Clostridium pacaense
  ORGANISM  Clostridium pacaense
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Clostridium pacaense"
                     /db_xref="taxon:1917870"
     Protein         1..385
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=40460
     Region          <1..382
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mrktfmgyar pdgrygvrny vaiistadns nfiarrvaqm ingtipvcpc fgrgeigpdm
       61 dlhiktmggm ganpnvhsav vvslepalae kiaaviratg kkaetfsmde cggsigcteq
      121 avraarrlii easmeqrvev giehlhlgve cggsdttsgl vsnpatglva dqlvdaggtv
      181 ilsettewmg aenillkrav tpelgerivk airwyedyik sigvdlngfn papdnikggl
      241 stieekalgs ikkggtrpiq dmltcseapg rpgmylmdap tggventtal agagcqliif
      301 stgkgnplgn piaptikvtg nertigksge nidvdlsavi tedmdiqaag nilyekmidh
      361 adgklttaea lgdleiavtr igftv
//
LOCUS       WP_008717569              94 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Rhodococcus sp. AW25M09].
ACCESSION   WP_008717569
VERSION     WP_008717569.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. AW25M09
  ORGANISM  Rhodococcus sp. AW25M09
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 94)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 94)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 94)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 94)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Rhodococcus sp. AW25M09"
                     /db_xref="taxon:1268303"
     Protein         1..94
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=9859
     Region          15..94
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mddvqasgda apqtrvevry faaavdasgc dseyvtvptg atlaelreli rsrhgapmep
       61 ilrvsaylvg ddltrdldra igsrvdvlpp fagg
//
LOCUS       WP_008717687             113 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Rhodococcus sp. AW25M09].
ACCESSION   WP_008717687
VERSION     WP_008717687.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. AW25M09
  ORGANISM  Rhodococcus sp. AW25M09
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Rhodococcus sp. AW25M09"
                     /db_xref="taxon:1268303"
     Protein         1..113
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11863
     Region          5..98
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(27,55..56,58,80)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(27..28,36,38,40..41,43,46..47,55,60,65)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mapitetqve rvralvasip agfvatygdi aaaadlssar ivgwimrtds adlpwhrvlg
       61 asgrpaahla trqletlrse gvaihdgrvp lnsirfdfgs lsspsepttn lge
//
LOCUS       WP_008717531             371 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Clostridium pacaense].
ACCESSION   WP_008717531
VERSION     WP_008717531.1
KEYWORDS    RefSeq.
SOURCE      Clostridium pacaense
  ORGANISM  Clostridium pacaense
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 371)
  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 371)
  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
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 371)
  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   5  (residues 1 to 371)
  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   6  (residues 1 to 371)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 371)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 371)
  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 20283677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Clostridium pacaense"
                     /db_xref="taxon:1917870"
     Protein         1..371
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40992
     Region          <25..60
                     /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(28,30..32,41)
                     /site_type="other"
                     /note="non-specific DNA interactions [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            41..47
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            order(42..43,47)
                     /site_type="other"
                     /note="sequence specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238044"
     Site            42..43
                     /site_type="other"
                     /note="putative cAMP binding site [chemical binding]"
                     /db_xref="CDD:238044"
     Region          78..344
                     /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 maemvgtprm ikllnkdvie giikvngpit kpeiarltnl slvtvnktvd ilvkenkvkl
       61 snvqdssvgr raqyfeinee lhyiiglhyd cnmyigavsn sigdiiyrke fpvrpdsyde
      121 vmedtyrald vlcgfctghe iaaiglgvpg vvkegvvtni pnipswegmd vahvleekyg
      181 apvllendin laamgvyygq ykdkvdslal vyleqgigsg lilgrelfkg stnfagelsy
      241 lpvsqgagrq dgnsrykgdf ehtmshleee irqssgtrrk elksllrrtv angllsiicv
      301 inpevvglvc srisradvkg ieellkecig eehvpklikl ddireqsiyg ligmcireit
      361 ptyslssrkr g
//
LOCUS       WP_008719956             375 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Clostridium pacaense].
ACCESSION   WP_008719956
VERSION     WP_008719956.1
KEYWORDS    RefSeq.
SOURCE      Clostridium pacaense
  ORGANISM  Clostridium pacaense
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 375)
  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 375)
  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
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 375)
  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   5  (residues 1 to 375)
  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   6  (residues 1 to 375)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 375)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 375)
  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 11973016
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Clostridium pacaense"
                     /db_xref="taxon:1917870"
     Protein         1..375
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41846
     Region          <23..>70
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
     Region          81..368
                     /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 mkinekamek krqnkarias hilhrkqisk pelavelgls mptvlqnvke lqeagiveev
       61 geyestggrk akalsvvrni ryaagvdita nhvsfviidl kgdavhsarv rrrfentaey
      121 yeglaaeleq fldagrvdke kilgvgislp giidrensrl irshilqvsd inlevlsrli
      181 pypvhfenda nsaavaelqg tdrnavylsl sntvggsiyl dndiyggdhf rsaefghmii
      241 ypegkpcycg krgcadpycs arvlssfvge dgglaeffql vkekdrdama vwdtyledls
      301 ivitnlrmcf dcdivlggyv ggylrpymsq lgrkvmvhnk fdndtlylrn csyekeasav
      361 giamtfmdey frtmi
//
LOCUS       WP_008722273             387 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Clostridium
            pacaense].
ACCESSION   WP_008722273
VERSION     WP_008722273.1
KEYWORDS    RefSeq.
SOURCE      Clostridium pacaense
  ORGANISM  Clostridium pacaense
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Clostridium pacaense"
                     /db_xref="taxon:1917870"
     Protein         1..387
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=42535
     Region          14..380
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mvvdsghdlr lgvdikkklk efsldigfea grgclgilgp sgcgksmtlk siagivrpds
       61 griaiqyaqg eaaggrvlyd sslkvnerpq vrrvgylfqn yalfpnmtve qniltglnsa
      121 ggrkavsrkr qpltqkekdg kvremlsrfr legleqrypa qlsggqqqrv alarilaygp
      181 evllldepfs amdtylregl rlelasvlkd ydgvsvmvth drdeayqlcd slllldrgsv
      241 laggktrdif qcpitcqaar ltgcknisri grlgprrika ldwggleltt drdvdgsita
      301 vgirahdfep lsdgeaeqwk grengnliqv gspnisempf ewyitlsngl wwkkekdiht
      361 hntaglvpgw lrvepsalll ltgelng
//
LOCUS       WP_008725096             644 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Clostridium pacaense].
ACCESSION   WP_008725096
VERSION     WP_008725096.1
KEYWORDS    RefSeq.
SOURCE      Clostridium pacaense
  ORGANISM  Clostridium pacaense
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 644)
  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 644)
  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 644)
  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 644)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Clostridium pacaense"
                     /db_xref="taxon:1917870"
     Protein         1..644
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=69835
     Region          21..639
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mnnfqqktgf feyalmqkrl syrsvlamfl saisvfmvvy flvtafcgtp vaiahrllfv
       61 lfimllaffl hptkrkgwee llnlwsiydf iciilavacv vyyisdldnw qlrmfrpsrl
      121 dtvfgsvfif lvmditrrvv gmtmfcvvlf fgihtcfany fpgflktapt swvrivdilv
      181 sdqgifsepv qsmasyiilf llfgsilees gagkyfidia yavggrftag paktaaissa
      241 lfgsisgssv snvvstgcft iplmkstgyt aeeagateav astggnympp imgavafvma
      301 qylkvpyiqi vkyaiipall yyialltyih fdglkkgvrp mdkaglpslk kgilegghli
      361 lalvclvifl iygyttsmga fwgvvtlfll tfvrkdtrlk prqmirsfek tartaisvgi
      421 acaaagiiig cmyssglsvs lssiiikaad gsllvtliyt alfslvlgcg mpsvgvylil
      481 vttiipavtq mgvtpiaahf fafyfavisn itppvcvaaf agaaiaeasp mktgfkafvi
      541 giaayvipfl fvyhpatlai gtageiavav ingvvavmcl avcvagyisr klnvfervma
      601 favcmlvvap faasnliays iftviavfqi iawlrrrktv tkcs
//
LOCUS       WP_008726101             701 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Clostridium pacaense].
ACCESSION   WP_008726101
VERSION     WP_008726101.1
KEYWORDS    RefSeq.
SOURCE      Clostridium pacaense
  ORGANISM  Clostridium pacaense
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 701)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Clostridium pacaense"
                     /db_xref="taxon:1917870"
     Protein         1..701
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=78546
     Region          1..692
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mkkvqstcny caldcnmdfy vedgrivkvl ptkgypvndg fccikglsld rqqtvvktsp
       61 lprirqadgs mkevswnegf shvadklkel qekygkesva gistgqltme efalfghvmr
      121 nylktnvdgn trlcmatavv ahkqsygfda pgytlkdlel sdtivfvgan pvvahpilwk
      181 rvrqnpdkkv ividprkset amnadywypv kcrgdlrmfy ilagvlidkg yvceeyieah
      241 tegyeefkgf vkdytldrae emtglskeqi lelaelihsg krvsfwwtmg vnqgyeavrt
      301 aqsiinialm tgnigrpgtg ansitgqcna mgsraysnta vlyaggdftn parrarvaea
      361 lgvdesvlae kptatynqii eginegrikg lwilctnprh swtnnetfas avkklelfvv
      421 qdiydtiesa eectvffpvv pgikkegtyi nlerrlsamr pclekkenei tdyeailgvg
      481 kalgmgslln gwetprdcfe lmkkcskgmp cditgitwem ledshgiqwp fregdalqed
      541 errlygdgcf ftpskkaqfk feapkenplp vteefpyiln tgrgsvgqwh tqsrtsevqf
      601 igdvsakeay lymnpdtaaa shieennwik vhsangqqaa frvriseqvr pgelyapihy
      661 iecnrltpsi ydpyskepsy katpvwfekt eggnayaadk n
//
LOCUS       WP_008726873             427 aa            linear   BCT 20-JAN-2025
DEFINITION  galactokinase [Brachyspira hampsonii].
ACCESSION   WP_008726873
VERSION     WP_008726873.1
KEYWORDS    RefSeq.
SOURCE      Brachyspira hampsonii
  ORGANISM  Brachyspira hampsonii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Brachyspirales; Brachyspiraceae; Brachyspira.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   McAuley,M., Kristiansson,H., Huang,M., Pey,A.L. and Timson,D.J.
  TITLE     Galactokinase promiscuity: a question of flexibility?
  JOURNAL   Biochem Soc Trans 44 (1), 116-122 (2016)
   PUBMED   26862196
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Holden,H.M., Thoden,J.B., Timson,D.J. and Reece,R.J.
  TITLE     Galactokinase: structure, function and role in type II galactosemia
  JOURNAL   Cell Mol Life Sci 61 (19-20), 2471-2484 (2004)
   PUBMED   15526155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Brachyspira hampsonii"
                     /db_xref="taxon:1287055"
     Protein         1..427
                     /product="galactokinase"
                     /EC_number="2.7.1.6"
                     /GO_function="GO:0004335 - galactokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0005534 - galactose binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0046835 - carbohydrate phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=47236
     Region          37..413
                     /region_name="GalK"
                     /note="Galactokinase [Carbohydrate transport and
                     metabolism]; COG0153"
                     /db_xref="CDD:439923"
ORIGIN      
        1 mynisqikdl lkekkmndkf syiygddeys iseaytrlsd tikhfesien tqeiyvfsas
       61 grtelsgnht dhnngcvlta sinldklavv skrddnkiiv ytdysntpdi idindleink
      121 eeygksnalt rgvcagiknk gcniggctvt lnnkvligsg lsssasfesl igeiqnalyn
      181 ddkiskvdia kigqyaeniy fgkpcglmdq mgcsvggims idfkdnenpi iekveydfes
      241 kgyalmivda kgdhsgltne yaaireemna vanyfgkkvc rditkkelid nasklrsevg
      301 draimrayhf ieenervinq inslkkddin tyiklmnesg lssfmylqnc ysvtssknmg
      361 valgltltkd flkeegacrv hgggfagtiq alipvskaee ykkymnsifg egsavkirvr
      421 qapvcai
//
LOCUS       WP_008730609             317 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Actinomyces massiliensis].
ACCESSION   WP_008730609
VERSION     WP_008730609.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces massiliensis
  ORGANISM  Actinomyces massiliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Actinomyces massiliensis"
                     /db_xref="taxon:461393"
     Protein         1..317
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=33543
     Region          90..>187
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mkrilaaals avaiastggv ataetpddvs ysslsvavaa ladddpaptd wtthtpdnds
       61 ashldafaas ggrtgwfgqs wydldgngcd trndilkrdl vgsvykdrsa cvvaagtled
      121 pytgatirfk rgketsqdvq idhviplgfv yahggwkwda dtrlaiandp lnllavdgra
      181 nssksdagpa tspkgtgady ivnggggwlp dnsdytcrya arfarvalky elglgktdsv
      241 alskiltqca ttedkpqpsp pneaapasgt adlltlpqpi rrlwgeiedw liehpiyvvg
      301 aalglylmat rmtrgrr
//
LOCUS       WP_008732673             227 aa            linear   BCT 20-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Actinomyces
            massiliensis].
ACCESSION   WP_008732673
VERSION     WP_008732673.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces massiliensis
  ORGANISM  Actinomyces massiliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 227)
  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 227)
  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 11443472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Actinomyces massiliensis"
                     /db_xref="taxon:461393"
     Protein         1..227
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=23525
     Region          92..226
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          179..225
                     /region_name="LysM"
                     /note="LysM domain; pfam01476"
                     /db_xref="CDD:396179"
ORIGIN      
        1 msaltplpsp rphavsaasa qeaereeefl vasrphlrlv tddfvpetsr adpvvelpae
       61 ltrrpvtpra arsalggggv aqarpadlap hhpavraqrr rqleaqrsrs vlahgadgad
      121 gahgeasplr vqdsaqrlpi glrrlvvtgg lvlvaalivs lgivisgfad apsrtttatv
      181 qagqslweva aatgtgdvdr tmsrivelng lessalqagq vlvvpae
//
LOCUS       WP_008734738             334 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Isoalcanivorax pacificus].
ACCESSION   WP_008734738
VERSION     WP_008734738.1
KEYWORDS    RefSeq.
SOURCE      Isoalcanivorax pacificus
  ORGANISM  Isoalcanivorax pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Isoalcanivorax.
REFERENCE   1  (residues 1 to 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 334)
  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   5  (residues 1 to 334)
  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   6  (residues 1 to 334)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Isoalcanivorax pacificus"
                     /db_xref="taxon:1306787"
     Protein         1..334
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36853
     Region          25..209
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          97..334
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mhntgetlhp aaisevmlnf aqrngidrqt cllgtgisdv slaggeglit rtqemrlien
       61 lmlalpdagp sgfelglqys latfgvwgfa lrtcktlrda ivlgirylpl staycrvaic
      121 edenafgvtf dadpipshlr qfllerdmat ainlvreitl hgvdfkavef igvpevnpel
      181 vkglcsvapv fnapahrimv syegadkpfp gyeptltrml eqqcrqrmva venigitgkv
      241 rqkllgdmgl gatlddmase lalssrslrr kleqegssyr elieeerrql alqlldntkm
      301 kveevaahlg ytdaggfvra fkrwmncaps eyrk
//
LOCUS       WP_008735225             330 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-oxoacyl-ACP synthase III family protein
            [Streptomyces].
ACCESSION   WP_008735225
VERSION     WP_008735225.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 330)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            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="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34957
     Region          4..330
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mnaysritha svhlptgrqs aceieqrlrr hspslalppg liqrafglre raladpadlp
       61 sdlaaraatr llntarlrpa didlllfaav sadvrepana hivaaktgls cpafdignac
      121 ngvinalqva dalirtgqhr rvlitcgetl srlsrweldr srlrtgltsl tgadvgaall
      181 veaspvpgit gsvflansts wpaatlydph hapgqpqglh vdsdallasf tgldaqaaqw
      241 lkeqdvdvre ldlvcvhqps qpfvdafrar mdidpaqiip tfphtgnaaa atlplqlaqa
      301 vhdrrlapgd avalfglasg asgavmllrw
//
LOCUS       WP_008736412             215 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease family protein [Streptomyces].
ACCESSION   WP_008736412
VERSION     WP_008736412.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..215
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=23492
     Region          <109..199
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mikklrrgll atalafavlt ptspaqadev tlmdgitalp vadeiregyk relyphwkdd
       61 dkngctarnd vliaeaieap tvgagcaltg gvwhsyyddv lvqgpsgvdi dhliplaevh
      121 dsggygwtte rrrryandlg sdvtlvgvsa rsnrqkadqd patwmpmasv hcrylgewva
      181 tkhrwglavd raereallry aascpnarit yepat
//
LOCUS       WP_008736963             340 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Isoalcanivorax pacificus].
ACCESSION   WP_008736963
VERSION     WP_008736963.1
KEYWORDS    RefSeq.
SOURCE      Isoalcanivorax pacificus
  ORGANISM  Isoalcanivorax pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Isoalcanivorax.
REFERENCE   1  (residues 1 to 340)
  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 340)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 340)
  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   4  (residues 1 to 340)
  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 340)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Isoalcanivorax pacificus"
                     /db_xref="taxon:1306787"
     Protein         1..340
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38017
     Region          23..209
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          257..335
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtslgsisga aldqylvsar aagldispal adagldeata rqpdsrvpge rfeillerli
       61 aisgdplfgl htsqfvqpgs ysvmgyiamn attlnealsk valyeklvgd mgttevmpag
      121 qlvevrwccr htrqpvrrhl ienvfgswvr ysrwlannda ltpelvlfeh dvhdssavaa
      181 yekvfgcevr fnqpcsalra dprvldvrlr hpdphllstl eahaasklqq lgidtslahk
      241 vreqiraslg erlprkeqia celginmrtl hrrlreegtt wqqvldelrq qlalqylrds
      301 dlpqasiaer lgysdirsfq rsfkrhngit pgdyrsrekp
//
LOCUS       WP_008737322              96 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Isoalcanivorax pacificus].
ACCESSION   WP_008737322
VERSION     WP_008737322.1
KEYWORDS    RefSeq.
SOURCE      Isoalcanivorax pacificus
  ORGANISM  Isoalcanivorax pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Isoalcanivorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Isoalcanivorax pacificus"
                     /db_xref="taxon:1306787"
     Protein         1..96
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10268
     Region          1..95
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(6..7,25..26,34,37,39..40,42,45..46,48,56,61)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(25,56..57,59,79)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mdapsfeeav wqivgavpqg rvcsygqvaa lagyprharh vgrtlshlpp gsklpwhriv
       61 radgqlpmga eqarrlraeg vvvragrvsv aqlgwp
//
LOCUS       WP_008737643              83 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Isoalcanivorax pacificus].
ACCESSION   WP_008737643
VERSION     WP_008737643.1
KEYWORDS    RefSeq.
SOURCE      Isoalcanivorax pacificus
  ORGANISM  Isoalcanivorax pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Isoalcanivorax.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Isoalcanivorax pacificus"
                     /db_xref="taxon:1306787"
     Protein         1..83
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8821
     Region          1..83
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mitvrffagv realqtdalq wphrpdltva alrtqladld plwsaqlgsa rllmcavnev
       61 maspetalnd gdvvaffppv tgg
//
LOCUS       WP_008737570             270 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Isoalcanivorax
            pacificus].
ACCESSION   WP_008737570
VERSION     WP_008737570.1
KEYWORDS    RefSeq.
SOURCE      Isoalcanivorax pacificus
  ORGANISM  Isoalcanivorax pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Isoalcanivorax.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Isoalcanivorax pacificus"
                     /db_xref="taxon:1306787"
     Protein         1..270
                     /product="formate/nitrite transporter family protein"
                     /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=29011
     Region          2..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msylvpsefv skmvdagesk lymatrdali raymagaila laavfavtvs vqtgfpilga
       61 mlfpvgfcil ylmgfdlltg vfvltplalf dkrpgvtpgv ilrhwgvvft gnflgaltva
      121 lmmaivftyg fstepnqvgq vishigedrt lgykeygaag mltifirgvl cnwmvslgvv
      181 gamisttvgg kviamwmpim lffamafehs vvnmflfpsa limggdfsvm dyliwneipv
      241 vlgnlvggls ltgltlytth lrtgaarvlr
//
LOCUS       WP_008737755             296 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Streptomyces].
ACCESSION   WP_008737755
VERSION     WP_008737755.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 296)
  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 296)
  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 296)
  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 12807598
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..296
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31254
     Region          32..99
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          <162..282
                     /region_name="PRK10856"
                     /note="cytoskeleton protein RodZ"
                     /db_xref="CDD:236776"
     Region          211..270
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 msignanspe eerpstddws edrtvepsve gpsigtalkk ariaagltvd evssttrvri
       61 pivhaieedd ftrcggdvya rghirtlara vhldpaplid sydaahggrp aptpaapmfe
      121 aerirperqr pnwtaamvaa ivavigfvgf tafnggdtgk rpvaegsasp kpapkqtagk
      181 paaqpqipqa pkpepsdsai aaapkdlvtv vltahdgesw isakdhsgrl lfdgtlqvge
      241 sktftdkesi dlvlgdagav nlfvngkeik ddfrpgqver ltytkddprq gqaqag
//
LOCUS       WP_008739094             214 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease family protein [Streptomyces].
ACCESSION   WP_008739094
VERSION     WP_008739094.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..214
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=22871
     Region          <113..210
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mpavyarrlg vlasaatlas ltslvnapaa qaappapisa saaraylatv tpttegstsg
       61 ysrtlfphws tvsgacntre tvlkrdgknv vqdsscaavs gswyseydda twtvatdldi
      121 dhvvplaeaw rsganswtta krqqfandlt rpqliavtdn vnqakgdqdp gtwlpsrtay
      181 rctyarmwve vkqyyalsmd srektaltgv lngc
//
LOCUS       WP_008741134             389 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Streptomyces sp. Mg1].
ACCESSION   WP_008741134
VERSION     WP_008741134.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. Mg1
  ORGANISM  Streptomyces sp. Mg1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Streptomyces sp. Mg1"
                     /db_xref="taxon:465541"
     Protein         1..389
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41834
     Region          1..271
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          267..358
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrilhtsdwh lgrsfhrvnl lgaqatfvdh lvetvrthev dvvlvagdvy dravpplpav
       61 elydralhrl adlgvptvmi sgnhdsarrl gvgagligra gihlrtdpdg cadpvvladv
      121 hgevafyglp ylepalvkdr fgagqvshea vlgaamdrir adlatrppgt rsvvlahafv
      181 tggqasdser ditvggveav pasvfdgvdy aalghlhgcq tiservrysg splaysfsea
      241 dhrktmwlie lgargeiaga dridtpvpra larlrgpled llddpalagy edrwveatlt
      301 dpvrpedpma rlaarfphvl slafdpegre edsgasyaqr lkgrsdqeia edfvahvrgg
      361 gapseaerav lqgafddvrt datrqetlr
//
LOCUS       WP_008741534             196 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Streptomyces].
ACCESSION   WP_008741534
VERSION     WP_008741534.1
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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..196
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=21394
     Region          31..179
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 maspmsadrf isalrheglt vvevgawrth nrnhkgpwgp vhgvmvhhtv thgtgytvrl
       61 cregdedlpg plchgvitkd grvhlvgygr anhagagdsd vlaaviaekr lpvdhradtd
      121 gnrhfygfec enlgngedpw pavqldaiar ataalcrvhg wtarsvighr ewqpgkidpr
      181 gftmdamrvr vaerlk
//
LOCUS       WP_008742507             320 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Streptomyces].
ACCESSION   WP_008742507
VERSION     WP_008742507.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (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   2  (residues 1 to 320)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 320)
  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   4  (residues 1 to 320)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..320
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=33990
     Region          1..313
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mirfehvtkr ypdgttaved ldfevaegel vtlvgpsgcg ktttmkmvnr lieptsgril
       61 lggediaaad pvelrrrigy viqqvglfph ktvlentatv pqligtpkak araraaelle
      121 lvgldpavyg grypeqlsgg qrqrvgvara laadppvllm depfgavdpv vrerlqnefl
      181 tlqktvrkti llvthdleea irlgdriavy gngtieqfar paavlaapat eyvagfvgad
      241 rglkhlavta vapadveaad gkaptaeval gaslrealal llredsgrig vkdpdtgalv
      301 gvltpegvhr alrraqlqea
//
LOCUS       WP_008742794             374 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: aminoglycoside phosphotransferase family protein
            [Streptomyces].
ACCESSION   WP_008742794
VERSION     WP_008742794.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 374)
  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   2  (residues 1 to 374)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..374
                     /product="aminoglycoside 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=40451
     Region          89..306
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 myaatssvsa pvrphrtipa gggpyldpgr saapaqggvr arrapgspsq ppsgridlsg
       61 pqgaqlrtal asvqricpef apvqvlrrsg rsvllvgttg rltavakvll dhspewrery
      121 rheiaayraf vrhrppvrvp rliaadpenc tlvvermagr vaalqrhple apprpdlraa
      181 lgavcrvnqw qppgelfghp vdyarrinrd helglltdrd fgdlqkllhg lklsgtpwqf
      241 nhgdallsnl llspagpvll dwehagwylp gydlatlwtv lgdapaargq isrlaqsagp
      301 aardaflvnl mlvltreirm aetavqrsmq aaapaqplqa gslssgeeqr lllrrlhddc
      361 gmarravraa vgtr
//
LOCUS       WP_008742905             404 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Streptomyces].
ACCESSION   WP_008742905
VERSION     WP_008742905.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 404)
  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 404)
  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
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 404)
  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   5  (residues 1 to 404)
  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   6  (residues 1 to 404)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 404)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 404)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..404
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41229
     Region          14..77
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          77..379
                     /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 mqtpgsqssl hranlervvr avrlagsltq aeiaratgls aatvsnivre lkeagtvevt
       61 dtsaggrrar svslsgdagi vigvdfghth lrvavgnlah qvlaeesepl dvdaswvdgf
      121 draealvgrl ilgigvgrek vigvglgvpg pidvesgtlg stailpgwag inprqelsqr
      181 lgvpvyvdnd anlgalgelv wgsgrgvkdl ayikvasgvg aglvingqiy rgpggtagei
      241 ghitldesgp vcrcgnrgcl etfaaaryvl pllqgshgpe ltmervvela regdpgcrrv
      301 iadvgrhvgs gvaslcnlln psrvvlggsl aeagelvlap iresvgryai psaarqlsvl
      361 tgslggraev lgalalvlse mgdstllaen gsgvrapavm ssvr
//
LOCUS       WP_008743923             395 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Streptomyces].
ACCESSION   WP_008743923
VERSION     WP_008743923.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 395)
  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 395)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..395
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43555
     Region          11..393
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mttaaapqpt ptvslsadea rrialraqgf igapdrrggv rgvlrhlgav qldtisvlar
       61 shelipyarl gavgrpaver aywsdghafe ywshaacilp ieewphfafr rrarrarghr
      121 whvlrdkels tkavldrlra dgpltstelg gaknggewfe wsetkiavew lldtgevvcs
      181 errgwkrvyd lperavpdal lhddlddrec lrrlvalagq slgvgtradi adyhrlkgeq
      241 fdavveesgl vpvevegwsk pawaapealt apprgrhrtt llspfdslvw drprterifg
      301 fthrleayvp kpkrihgyfa mpllaggrlq grvdparegt tlvarqlslt spkaagpmaq
      361 alreaaswvg cdavrveraa spaeaesvra elaal
//
LOCUS       WP_008744029             124 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein [Streptomyces].
ACCESSION   WP_008744029
VERSION     WP_008744029.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            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="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=13459
     Region          19..86
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mtenawgyre tsgrlegvdl tgykveaedg sigkvdkhsd eagsayivvd tgpwifgkev
       61 llpagtvsri daaeekiyve lskeqiksap efvredhldd tgyreqlgsy yglgpfggpf
      121 vghm
//
LOCUS       WP_008744225             437 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. SPB074].
ACCESSION   WP_008744225
VERSION     WP_008744225.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. SPB074
  ORGANISM  Streptomyces sp. SPB074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 437)
  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 437)
  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
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 437)
  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   5  (residues 1 to 437)
  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   6  (residues 1 to 437)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 437)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 437)
  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 20283677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Streptomyces sp. SPB074"
                     /db_xref="taxon:465543"
     Protein         1..437
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45097
     Region          1..71
                     /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            4..5
                     /site_type="active"
                     /note="putative switch regulator [active]"
                     /db_xref="CDD:238044"
     Site            order(29,31..33,42)
                     /site_type="other"
                     /note="non-specific DNA interactions [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            42..48
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            order(43..44,48)
                     /site_type="other"
                     /note="sequence specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238044"
     Site            43..44
                     /site_type="other"
                     /note="putative cAMP binding site [chemical binding]"
                     /db_xref="CDD:238044"
     Region          80..401
                     /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 mvqrhrrtvr dlrrgnraav lqrlyfdgpm srqallpatg lssgsisnvv teltadglle
       61 eagvvesdgg rprtllrvaa gagylvgvdi getkvrtelf dlamselsrt etsltgvgyd
      121 vdlivravae giaavlaeag vpadrllgvg vgvpgiverp egasalvygq tigwdavple
      181 tllrtatglp aevgffvnng akalgqaelw fgggrgsedv vivlfgsgvg acivtrgaiq
      241 ggmhgspsew ghltvnvrgr rcrcgargcl eayagaeall erwrevggtl pegageeegv
      301 tallaaadpg raggpdpvav avleetaeyl gaglsdlinl fspeqvligg waglqlgphi
      361 lhsvrrhads falrrpagkv siglgllgad avtvgaatlv ladffanggr reaplreedv
      421 aeavtdrrpa ahvlggh
//
LOCUS       WP_008744655             679 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Streptomyces sp. SPB074].
ACCESSION   WP_008744655
VERSION     WP_008744655.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. SPB074
  ORGANISM  Streptomyces sp. SPB074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 679)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 679)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 679)
  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 679)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..679
                     /organism="Streptomyces sp. SPB074"
                     /db_xref="taxon:465543"
     Protein         1..679
                     /product="M4 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=69442
     Region          41..674
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mrrtssrraa vtggallavs alltaatqtg vasaapsptg kaasaarpga lpaklspaqr
       61 agliaaaqkk saatagelsl gaqeklvard vvkdqdgtlh tryertyagl pvlggdlvvt
      121 tnpagetgkv vrasraklsg vkttakvpaa tarkqalgaa kaqgaaqpat dqaprkviwl
      181 aegkpvlaye tvigglqedg tpnalhvvtd aatgaklyey qgiengtant qysgtvtist
      241 tksgstynlt datrgghkty tlanktsgtg tlvsgpddvw gdgkgttpet aaadaaygaq
      301 etwdfykdtf grsgirgdgv aaysrvhygn qyvnafwdds cfcmtygdga gnaapltald
      361 vaghemshgv tsetaglnys gesgglneat sdifgtgvef ysntatdpgd yligekidin
      421 gdgtplrymd kpskdgasad nwsstlgnkd vhyssgpanh ffyllsegsg aktvngvnyn
      481 sptydglpvt gigrakalqi wykalttqft sttnyagart gtlaatssly gansaeykav
      541 qdawaainvg arsgggtdpg npggtvfsss tkvaipdags avsssiavtg rsgnapsnls
      601 vsvdithtyr gdlvvdllap ngtsyrlkns sssdsadnvk atytvnassv aangtwklqv
      661 rdvysgdsgt ingwsltfp
//
LOCUS       WP_008745502             236 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Streptomyces sp. SPB074].
ACCESSION   WP_008745502
VERSION     WP_008745502.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. SPB074
  ORGANISM  Streptomyces sp. SPB074
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Streptomyces sp. SPB074"
                     /db_xref="taxon:465543"
     Protein         1..236
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=25722
     Region          82..222
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 megtsgrghg prlpdgggrl grrallvgga aagvgagvla rgelrhlwwr tpgverprve
       61 gavdqpgaew vaaseanwrr adrpgdygvd rvvihvvqgs ypvalkvfkd pahgaaahyv
      121 vrkdghiaqt ireldvayha gnrsfnersv giehegwidr pqdfteamlr asarltasic
      181 arygfppdre hvighvevpg adhtdpgrdw pwdtymrmvr qartevegtk aaarrv
//
LOCUS       WP_008746207             309 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Streptomyces sp. SPB074].
ACCESSION   WP_008746207
VERSION     WP_008746207.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. SPB074
  ORGANISM  Streptomyces sp. SPB074
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Streptomyces sp. SPB074"
                     /db_xref="taxon:465543"
     Protein         1..309
                     /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=33053
     Region          58..>220
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 maaprrhpgp qetatmksaa pgraapapta ddpaagpapa pvpgapapgp pparakardp
       61 wfdntrfvaa tlivvlhtig simsrhealh afnvaawafr vpafvvlagv fssaspldsr
      121 rlrdllrtia lpaltfsllf slesyalggp stlhlaqlpw tlwflmslfc wrlllplvaq
      181 lrhpllvtta vaaglgyvee fgllfsasrt lvylplfwlg rrlgqgagrs gwraagvcrs
      241 rspvsparps rpgagtatsp argsrcgtrt rrtprwawra pgscawrssr rrrswscacc
      301 awsrsaacp
//
LOCUS       WP_008747433             249 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Streptomyces sp. SPB074].
ACCESSION   WP_008747433
VERSION     WP_008747433.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. SPB074
  ORGANISM  Streptomyces sp. SPB074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Streptomyces sp. SPB074"
                     /db_xref="taxon:465543"
     Protein         1..249
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=25954
     Region          88..224
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mrygarrgag tvvgavalgg lllgtagckd ievsdgdgga asapakgaeg salkavdglt
       61 vkgrapktgy drdkfgsawa dtdsnhcdtr ndilkrdlkd vkfktgdcvi asgvlnddpy
      121 sgddirftrg askididhlv slsdawqkga sqwegskria landplnlla vsagpnrskg
      181 egdtatwlpa nkgyrctyva gqvavkakyg lwvtaaekaa mkkvlttcpe qklpegtapt
      241 kaparfrar
//
LOCUS       WP_008747807             403 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. SPB074].
ACCESSION   WP_008747807
VERSION     WP_008747807.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. SPB074
  ORGANISM  Streptomyces sp. SPB074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  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 403)
  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
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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   5  (residues 1 to 403)
  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   6  (residues 1 to 403)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 403)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces sp. SPB074"
                     /db_xref="taxon:465543"
     Protein         1..403
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41806
     Region          30..69
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          91..390
                     /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 mttkrasatk tsirrgtnlp rmgdfnesvv ldairrhkag lsrvelaeat glsaqtvsni
       61 trrlldqgva resgkqstgs gkprtllqvt pgaryaigvh ldpavityvl ldllgtvvar
      121 rseptprgvh teallagmaa svgaliedsg vdqervlglg iaapgpvdpv aglvidppel
      181 pgwgsfplre rleadtgfpa lldkdvvaaa vaerwsgaat dsrnflffyl gtgsgmglvv
      241 ddtvlrgssg nvgevgglga acssralvee aielgalghe ftptdpqdaq rslqhlaria
      301 adgepraagi idrwgvrigr gvtaaatlld sdtivfggpl wpllaprllp liepmvaesp
      361 fvkpvhgttv tttaigedva avgaaclvld rtlsaqprsl lla
//
LOCUS       WP_008747937             383 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Streptomyces sp. SPB074].
ACCESSION   WP_008747937
VERSION     WP_008747937.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. SPB074
  ORGANISM  Streptomyces sp. SPB074
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Streptomyces sp. SPB074"
                     /db_xref="taxon:465543"
     Protein         1..383
                     /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=42138
     Region          50..320
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mhhdpaesgq lsavpadpaa rhprppessa hsapsdatkr tgavgarggr vrdpffdnak
       61 ylaivlvaia hswepllass rplsalyltv yafhmpafii isgyfsrtft lgapqvrkli
      121 ttvalpyvif qyaytlfarv mgpdpvptws vidpwwlnwf lialfvwrlt tplwrlvrwp
      181 lplalafavl gsmspeigad ldlqrviqfl pyfvlglllr prhfalfshk wpkivaapvl
      241 ltglaaawwl aprlpyawly hresaqdlga pwwsgplmtf alfsaslilt aaflalvprr
      301 atwctrlgag tlagyllhgf likaadwggw ydsafahsvp gtllfsagag cavtllcmpp
      361 vrgafrwale prldwafggt rga
//
LOCUS       WP_008749233             386 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Streptomyces sp. SPB074].
ACCESSION   WP_008749233
VERSION     WP_008749233.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. SPB074
  ORGANISM  Streptomyces sp. SPB074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces sp. SPB074"
                     /db_xref="taxon:465543"
     Protein         1..386
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41294
     Region          1..269
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          265..356
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrilhtsdwh lgrslhrvpl ldaqsafldh lvttvrerdv eavvvagdvy dravpslpav
       61 elfdralhrl aalgvptvli sgnhdsarrl gvgagllgra gihlrtrpae cgepvvlpda
      121 hgevafyglp ylepglvkde faapadhegv lgaaldrvra dlatrpagtr svvlahafvt
      181 ggapsdserd itvggvsavp aalfdgidya alghlhgsqv lgerlrysgs playsfseag
      241 hrksmwlidl dgtgaltaer vdcpvprpla rlrgtleall adpahtphed awieatltda
      301 vrpeepmarl aarfphllsl vfaperppap dgrsyarrlq grgdqeiaed fvahvrgeap
      361 sederavlra avdavrletq aaevrr
//
LOCUS       WP_008749563             263 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase, partial [Streptomyces sp.
            SPB074].
ACCESSION   WP_008749563
VERSION     WP_008749563.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. SPB074
  ORGANISM  Streptomyces sp. SPB074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 263)
  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 263)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Streptomyces sp. SPB074"
                     /db_xref="taxon:465543"
     Protein         1..>263
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
     Region          2..263
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 malvptgelv aeavaggrgl pafnvvtleh veavvtgaer agaavvlqvs enavlyrlgr
       61 laplaaaars vaaaaavpva lhldhvtdge llrqaagagf gsvmydgaal pyeenlaatr
      121 eavtwahahg lwaeaelgev ggkdgavplg phapgartdp aeaaafvtas gadglavavg
      181 sshamttpta aldhallgrl rgatavplvl hgssgvpdge lraavrggit kvnvgtalnv
      241 altaavrerl gadpglvdar ayl
//
LOCUS       WP_008750660             492 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Lachnoanaerobaculum saburreum].
ACCESSION   WP_008750660
VERSION     WP_008750660.1
KEYWORDS    RefSeq.
SOURCE      Lachnoanaerobaculum saburreum
  ORGANISM  Lachnoanaerobaculum saburreum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Lachnoanaerobaculum.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Lachnoanaerobaculum saburreum"
                     /db_xref="taxon:467210"
     Protein         1..492
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=53268
     Region          1..492
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mdyikinnsd nvcvalnalk agekitvgne svvinsdipa ghkvalkdik sgediikygs
       61 riglakedik agdhvhihni ktalgdlley qyipkikelk etahesfmgf rrkngkvgvr
      121 neiwivptvg cvnniaqaie rraknlikgs vedvtafvhp ygcsqmgddq entrkiladm
      181 inhpnaggvl vlglgcensn ipvlkdylge idekrvrfli sqevedeiet gvtlvkelie
      241 niadesreei daseliigmk cggsdglsgi tanpivgefs diliskggst iltevpemfg
      301 aetllmerck dretfektva lindfkmyfk nhnqtiyenp spgnkaggis tledkslgct
      361 qksgsakvsd vlgygetlkt kglnllsspg ndlvaatala msgahivlft tgrgtpfasp
      421 vptlkiatns rlakskenwi dfnagrmved kskdelandl fklvlevasg kkvkseiagf
      481 hdfaifkqgv tl
//
LOCUS       WP_008750904             580 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Lachnoanaerobaculum
            saburreum].
ACCESSION   WP_008750904
VERSION     WP_008750904.1
KEYWORDS    RefSeq.
SOURCE      Lachnoanaerobaculum saburreum
  ORGANISM  Lachnoanaerobaculum saburreum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Lachnoanaerobaculum.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 580)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 580)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Lachnoanaerobaculum saburreum"
                     /db_xref="taxon:467210"
     Protein         1..580
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=65112
     Region          2..557
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mikmrliril kgsgkyilyq vlwqwislim qiiiainitg liqeafldta feshiprvvi
       61 vviasvlirt icdklytkas fhaganvkri lrnriyekvl rlgpayreqv htseivqmag
      121 egveqlevyf srylsqffys llapltlfiv lmrismksav illiavplip ivimlvmtva
      181 kkllshyfdi yyglgdsfle klqgmttlki yqadktaadd mdreseqfrk itmkvlmmql
      241 nstsvmdiva yggaavgiis allqfykaei slfgmlmflf lvaefflpmr ilgsffhigm
      301 ngmkasdhif afldlpeqqr gskeindkei kislenlsfs ydprktilsg idmtispksf
      361 vsivgvsgsg kstiagilmg knlkysgslk inndehselt sktilshftf vghrswmfag
      421 tvrenllmgn pnatekemne alekvnllaf insqdgldtk ltsnasnlsg gqnqrlslar
      481 allhntpvyi fdeatsnvda gseeiimnvi helsktktvi lishrlanvv nsdeifmlkn
      541 gsivesglhf elmnnkgaye klfteqmnle nfskrkeise
//
LOCUS       WP_008751548             277 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Lachnoanaerobaculum
            saburreum].
ACCESSION   WP_008751548
VERSION     WP_008751548.1
KEYWORDS    RefSeq.
SOURCE      Lachnoanaerobaculum saburreum
  ORGANISM  Lachnoanaerobaculum saburreum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Lachnoanaerobaculum.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Lachnoanaerobaculum saburreum"
                     /db_xref="taxon:467210"
     Protein         1..277
                     /product="formate/nitrite transporter family protein"
                     /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=28976
     Region          6..277
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mnfsntaaev tsnlivagdt kvgrplhktv ilgifagmli gagamassva ihdianagla
       61 rlvaglvfpi gfvmmvlfgg elftgaclmi mgllkgkysl ismvrvlitv fisnliggii
      121 lailvaysgq fklgdgamga ftiklalska nisfgsafis gilcnffvcf gvvmaglskd
      181 isgkvlasfl pimtfvtggf ehcvanmfyi pagifassns kfaesamtky gisaeklatl
      241 nwqnfflkne lpvtlgnivg gmlfigvalf ilygree
//
LOCUS       WP_008753758             400 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Lachnoanaerobaculum saburreum].
ACCESSION   WP_008753758
VERSION     WP_008753758.1
KEYWORDS    RefSeq.
SOURCE      Lachnoanaerobaculum saburreum
  ORGANISM  Lachnoanaerobaculum saburreum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Lachnoanaerobaculum.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Lachnoanaerobaculum saburreum"
                     /db_xref="taxon:467210"
     Protein         1..400
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43359
     Region          2..399
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mknilvincg ssslkyqlin meneeplakg lferiaipgs klthepigrd kyivekdvkd
       61 hteaialvfe altdkehgvi kdaseiaavg hrvvqggvky pesvviddev kaeikkycdl
      121 aplhnpanlm gieavekamp gitnvaafdt sfgmgmpqka ykyaipseyy dkyhirrygf
      181 hgtshmyvsh eavefanldk dsakvivchl gngasisasv ggkcvdssmg ltpleglimg
      241 trsgdidpai vqyicdkenr svdevldiln kksgvlgmsg gissdfrdve naaadgnela
      301 qvaleafryr iikyvgayia amggvdaicf tagvgendke trrivgnafg ylgakideka
      361 ndvrgkrtmi stpdskikli lmptneelai ardayrlakk
//
LOCUS       WP_008754020             282 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: class II fructose-bisphosphate aldolase
            [Lachnoanaerobaculum].
ACCESSION   WP_008754020
VERSION     WP_008754020.1
KEYWORDS    RefSeq.
SOURCE      Lachnoanaerobaculum
  ORGANISM  Lachnoanaerobaculum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 282)
  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 282)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Lachnoanaerobaculum"
                     /db_xref="taxon:1164882"
     Protein         1..282
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=30728
     Region          1..282
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mivplavmqk earkkgyavp hflganfemt laaieaakec gsplalgfap evfamipley
       61 avpmlreaad ratvpvsiql ehgtgyeila raislgmqsv mfdgshlpve eniqktkeiv
      121 kmahafgcdv eaelgyvggs alcdiesees retdpdivle fiqqsqvdsl aisfgnvhgr
      181 yrgeaklnya lvekiagmte vpltmhggsg ltkeqykksi eagisnihfy tnitlglwrs
      241 leelakkrns qpvyheicga tiayfkkeil nimeicksag ka
//
LOCUS       WP_008754206             580 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Lachnoanaerobaculum
            saburreum].
ACCESSION   WP_008754206
VERSION     WP_008754206.1
KEYWORDS    RefSeq.
SOURCE      Lachnoanaerobaculum saburreum
  ORGANISM  Lachnoanaerobaculum saburreum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Lachnoanaerobaculum.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 580)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 580)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Lachnoanaerobaculum saburreum"
                     /db_xref="taxon:467210"
     Protein         1..580
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=65024
     Region          2..557
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mikmrlirll kgsgkyilyq vlwqwislim qiiiainitg liqeafldta feshiprvvi
       61 vviasvlirt icdklytkas fhaganvkri lrnciyekvl hlgpayreqv htseivqmag
      121 egveqlevyf srylsqffys llapltlfiv vmrismksav illiavplip ivimlvmtva
      181 kkllshyfdi yyglgdsfle klqgmttlki yqadktaadd mdreseqfrk itmkvlmmql
      241 nstsvmdiva yggaavgiis allqfykaei slfgmlmflf laaefflpmr ilgsffhigm
      301 ngmkasdhif afldlpeqqr gskeindkei tislenlsfs ydprktilsg idmtippksf
      361 vsivgvsgsg kstiagilmg knlkysgslk inndehselt sktilshftf vghrswmfag
      421 tvrenllmgn pnatekemne alekvnlldf insqdgldtk ltsnasnlsg gqnqrlslar
      481 allhntpvyi fdeatsnvda gseeiimnvi helsktktvi lishrlanvv nsdeifmlkn
      541 gsivesglhf elmnnkgaye klfteqmnle nfskrkeise
//
LOCUS       WP_008759700              97 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [Bacteroides].
ACCESSION   WP_008759700
VERSION     WP_008759700.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..97
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11162
     Region          3..96
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mkttneyltk irqfkqqcae kygiisigif gsvargeqhe gsdldvfvel kepdpfvmfd
       61 ikeelehicn ckidllrlrk nlrslisqri ekdgiya
//
LOCUS       WP_008759756             337 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Bacteroides].
ACCESSION   WP_008759756
VERSION     WP_008759756.1
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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..337
                     /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=38958
     Region          4..282
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mgdnqhrrid fvdltkgvci ilvvmahigg afdqldkhsm lscfrmplyf fisgiffkpy
       61 eglygfiirk tnkliipfif fyvsafllky ivwkiapgtf hlpvswrell fvfhghdlik
      121 fnppiwflla lfncnilfyl ihylrdkhls lmfaatllig ctgfflgkfh ielplyidva
      181 mtalpfyvag fwvrrynffl fpshrfdkii psfvllalvv myftattpgm rtnnypgnif
      241 qvyiaafagi fmimlickki krisivsylg rysiitlsih gpiihftrpv vshyihndwa
      301 easalllltl ticilftpil lkiipqlvaq kdllkvk
//
LOCUS       WP_008763500             278 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Bacteroides].
ACCESSION   WP_008763500
VERSION     WP_008763500.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
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   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 12122938
            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="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31444
     Region          199..278
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mkmevpqvdl plevlawtkv tedilniykq scrlqacifa ictegtmkvs inlleyevhp
       61 ndlitllpgt iiqfrekaek vslcfagfsa kcighinlla tigsaypkli eqpiiplsen
      121 iseylkeyfa llshascdes fkmnskladl slqtiltsvq lmyrnysgnn hsnrkkeicr
      181 kliqlitehy kdqrcaqfya dqlgislqhl sttvkqvtgk svldtiayiv iidakaqlkg
      241 tdmtiqeiay slnfpnpsff ckffrrhvgm splefrns
//
LOCUS       WP_008764355             104 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [Bacteroides].
ACCESSION   WP_008764355
VERSION     WP_008764355.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..104
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11810
     Region          1..104
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mrrtevieqi kdiirhvapt aktilygsqa rnearsdsdi dllilldgek itlkeeeait
       61 lplyelelkt gisispmvml kklwenrpfk tpfyinvtne givl
//
LOCUS       WP_008764678             366 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [Bacteroidales].
ACCESSION   WP_008764678
VERSION     WP_008764678.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidales
  ORGANISM  Bacteroidales
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 366)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 366)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Bacteroidales"
                     /db_xref="taxon:171549"
     Protein         1..366
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=41653
     Region          3..364
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mnsikrievi ydnrlvgrla ltkeslcafe ysaewlnsgf sispfelplr sgvfiakprp
       61 fdggfgvfdd clpdgwglli ldrylqrngv nprtlslldr lalvgstgrg alefrpdksv
      121 vskqeyadfe klaleaeqil dsdnyngegi eefqyrggsp ggarpkiftr ydgkewlvkf
      181 rakrdskhig edeyryslla kecgiempkt rlfedkyfgv erfdrtsngk lhvvsiagli
      241 gadyrlpsid ythifqvcat lthsvaemwk vyrlmvfnyl idnkddhakn fafiyrdgnw
      301 hfapafdllp sdgingfrtt sindrieptk edlfavmvkv glnekeavei feeiqgilsm
      361 tfdqsf
//
LOCUS       WP_008766205             416 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Bacteroides thetaiotaomicron].
ACCESSION   WP_008766205
VERSION     WP_008766205.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides thetaiotaomicron
  ORGANISM  Bacteroides thetaiotaomicron
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Bacteroides thetaiotaomicron"
                     /db_xref="taxon:818"
     Protein         1..416
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46913
     Region          2..289
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          287..388
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mirilhtadw hlgqtffgyd raeehkafld wlaeeirqne idalviagdv fdvsnpsaas
       61 qriyyefiyr vtaenpklqi vivagnhdsa arleaplpll qamrtevrgv vrkleggeid
      121 ydhltielkn regevevlcm avpflrqgdy pvvetegnpy megvrelyar llqrlwarrk
      181 tnqailavgh lqatgseiae kdysertvig glecvspdtf sekiaytalg hihkaqrvsg
      241 renvryagsp ipmsfaekhy hhgvvmvild egcavdirri ecpqsiplis vpggeaaspe
      301 kiieilrdlp evdgeapyle vkvlleepep mlrqeieeal agkkyrlari vsayrqeerv
      361 ekevdgwkkg lqemsplqia qsafekvyqa empadltdlf qeayisatrk eeeege
//
LOCUS       WP_008767209             686 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate--CoA ligase family protein [Bacteroides].
ACCESSION   WP_008767209
VERSION     WP_008767209.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..686
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73991
     Region          4..686
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mittqllrpe sivvvgasnn vhkpggailk nlinggyqge lravnpkete vqgvpafadv
       61 kelpdtdlav lavpavmcpd ivetlasekq trafiilsag fgeetregal leeriletvn
      121 kygasligpn ciglmntwhh svfsqpipnl nskgvdliss sgatavfile savtkglqfn
      181 svwsvgnakq igvedvlqfm denfdpekds rikllyiesi hnpdrllfha sslirkgcki
      241 aaikagsses gsraasshtg aiassdsave alfrkagivr cfsreelttv gciftlpelk
      301 gknfaiitha ggpgvmltda lskgglnvpk legelaeelk aqlfpgasvg npidilatgt
      361 pdhlricidy ceekldnida ilaifgtpgl vtmfemydvl hekmqtchkp ifpvlpsint
      421 agaevaafla kghvnfsdev tlgtalsriv napkpavpei elfgvdvpri rriidsipen
      481 gyiephyvqa llhaagislv deyvsnkkee vvdfarrcgf pvvakvvgpv hksdvggvvl
      541 nikgeqhlal efdrmmqipd akaimvqpml kgtelfigak yeekfghvvl cglggifvev
      601 lkdvssglap lsyeeaysmi rslraykiiq gtrgqkgvne dkfaeiivrl stllrfatei
      661 kemdinplla tekaviavda ririek
//
LOCUS       WP_008767474             159 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Bacteroides].
ACCESSION   WP_008767474
VERSION     WP_008767474.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..159
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17188
     Region          1..150
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdafidstiq lliewglpgl fisallagsi vpfsselvlv alvklglppt acilaatlgn
       61 taggmtcyym grlgkiswie kyfkvkkekv dkmvkflqgk galmaffafl paigevisia
      121 lgfmrsniwl ttasmfvgkl iryilllyvl esawnvvag
//
LOCUS       WP_008767227             303 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Bacteroides].
ACCESSION   WP_008767227
VERSION     WP_008767227.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 303)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..303
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34974
     Region          221..300
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mekenimtvd iedfkksqhi ldyidddfai vnsldgipys ndtvrlncfl iavcaegciq
       61 ldinyrtyql qagdlllglp ntlisrtmls pkykirlagf strflqriik mekktwntaa
      121 hihnnpvksi seggddpvfr fyrdlivaki ndephyyhre vmqhlfsalf cemlgqlhke
      181 idapdkgdsp kegikqadyt lrkfvellsk dkgmhrsvsy yadalcytpk hfskvikqac
      241 grtpldline ttiehikyrl krsdksvkei aeefnfpnqs ffgkyvkmhl gtspanyrnr
      301 ede
//
LOCUS       WP_008768038             324 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Bacteroides fragilis].
ACCESSION   WP_008768038
VERSION     WP_008768038.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..324
                     /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=37692
     Region          1..270
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mqridfidia kglaivlvvf ghtglrgfls dwiwsfhmpl fffvsglvfd psryntfslf
       61 ikkrlqtliv pyvifsivif igfwtlnynp clhsikellc gwdgialwfv pvlffveilf
      121 yalcknissv fvllllllfg sivgyflney nvrfyyklet vlsalfiygi gycsrfyiln
      181 kfrfsekcnl lvsfcfflll nvivvlinhp rldmawnqvg sylpgyigaf sgicwmfcfs
      241 riidlstlkl knvivylgkn tfiilafhqf lsalirkcle glpmssylns llrqiilwll
      301 liffisfinr yfscilgrkl paky
//
LOCUS       WP_008768394             157 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Bacteroides fragilis].
ACCESSION   WP_008768394
VERSION     WP_008768394.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..157
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17262
     Region          9..157
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 maeeltfisg skeeqylsll pqvrsliege vdlvanlanv aaalkeafdf fwvgfylvkq
       61 dqlvlgpfqg pvactrirkg kgvcgtawqe gatllvpdve vfpghivcss lsrseivvpl
      121 ikdgkvwgvl didsdllnff detdrkylee mcgylsk
//
LOCUS       WP_008771389             610 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase [Bacteroidales].
ACCESSION   WP_008771389
VERSION     WP_008771389.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidales
  ORGANISM  Bacteroidales
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Bacteroidales"
                     /db_xref="taxon:171549"
     Protein         1..610
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=70237
     Region          35..>450
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mnktelynki vqldgltnee ksellgllrk qkkyglvwed kpedveerlr delpvlieda
       61 mkaiisddan apnhiliegd nlealtslay thegkidviy idppyntgnk dfvyndcivd
      121 kedsyrhskw lsfmnkrlri akqllsdrgv ifisiddneq aqlkllcdev fgnnnfitni
      181 iwqstagsnt gneivtttey vlvytanrsk ahfdgqppsd dtfkltdehi kerghytldk
      241 ldrrrvgghy sealnfpikm pdgtlrypgg gqqqnegwny lwsktkvqwg ldndfivfkk
      301 nknewavyck ryqkvdnsnr qvdrttpyrn litsdlfnta qgtaeianif airpfafpkp
      361 stfvkfllss avvtspnamv ldffagsgtt lhatmqlnae dgghrkcilv tnnennicee
      421 vtyernkrvi ngyttpkgee vtglknntlr yyrtsfvgrs rsmknmrqlm nlstdmlcik
      481 edlyteqtkf geqptyknvf ryfdngkkrm miiykeeavp lladlirktd yegkmrvyvf
      541 spsedpwege feevqdkvql calpqaiyna ykrilpkkkd itleqendaa snddkafngm
      601 lnfdekedeq
//
LOCUS       WP_008771460             425 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [Bacteroidales].
ACCESSION   WP_008771460
VERSION     WP_008771460.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidales
  ORGANISM  Bacteroidales
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 425)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Bacteroidales"
                     /db_xref="taxon:171549"
     Protein         1..425
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48228
     Region          8..412
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mkkepiivnv ylwgtcigkl nwdfekhcsv fqftdeyrkq dydicpsthp krtplfasfy
       61 gnkdklyqgl pefladalpd kwgaslfdqw ltdnnikvte slpllklsyi gkramgalef
      121 epefnddaih esvnmsslat laskiyndrd aavispedsl tmkkliylgt saggmrpkav
      181 vaynleteef rsgqedlpen fkqyiikfke addsptteie mvysemakaa ginmvscflk
      241 eidgrnhfvt erfdrkdgdk ilsqplaaim pgaddymklc wlaetlklpq edkdqifirm
      301 vfnyvagisd dynknisfim dktgrwrlsp aydvmftant wenssahihs mgvmgkrsal
      361 ttsdfvnfae dfvenpekki lqvfdavskf qslcvtygid kaisdkiqhv ldglvtddln
      421 llqlt
//
LOCUS       WP_008771981             484 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Parabacteroides distasonis].
ACCESSION   WP_008771981
VERSION     WP_008771981.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides distasonis
  ORGANISM  Parabacteroides distasonis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Parabacteroides distasonis"
                     /db_xref="taxon:823"
     Protein         1..484
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=54306
     Region          26..462
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mantsknksd rpatlpdgla lpqeqeieka ilsglmashr hmptlaaqll pemftlpqva
       61 mafeaylniy nrgesadals vekelrriap dketlatdly qlalggryle tsdeymptha
      121 rhlreayvar qfmlscydsa lkasrpdrdt eallkemdsh vgrlmerlsh atnsvgmkea
      181 tllakermle iqrrvtegrt pgihtglegl drmtggmmpg tlnviaarpr vgktafalfm
      241 alnaarnghp vclyslemsk eqlvfrllgc iadiepskil kgtlsapemk riqrasdele
      301 rlpiwidert dlsvadlryq islrrkqgrc emvivdylql mlspsedrks tndqisaitr
      361 qlkliakend ipvvllsqln rncearptlk nmlsdlrdsg sieqdadtvf flrrlsvmni
      421 dedpetrlst egrgtlsiak nrhgesgevr fchnkgvtrf tddrtpvpnd rrpakaeldk
      481 dlfg
//
LOCUS       WP_008774415             370 aa            linear   BCT 20-JAN-2025
DEFINITION  transcription termination/antitermination protein NusG
            [Parabacteroides distasonis].
ACCESSION   WP_008774415
VERSION     WP_008774415.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides distasonis
  ORGANISM  Parabacteroides distasonis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Kang,J.Y., Mooney,R.A., Nedialkov,Y., Saba,J., Mishanina,T.V.,
            Artsimovitch,I., Landick,R. and Darst,S.A.
  TITLE     Structural Basis for Transcript Elongation Control by NusG Family
            Universal Regulators
  JOURNAL   Cell 173 (7), 1650-1662 (2018)
   PUBMED   29887376
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Liu,B. and Steitz,T.A.
  TITLE     Structural insights into NusG regulating transcription elongation
  JOURNAL   Nucleic Acids Res 45 (2), 968-974 (2017)
   PUBMED   27899640
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Steiner,T., Kaiser,J.T., Marinkovic,S., Huber,R. and Wahl,M.C.
  TITLE     Crystal structures of transcription factor NusG in light of its
            nucleic acid- and protein-binding activities
  JOURNAL   EMBO J 21 (17), 4641-4653 (2002)
   PUBMED   12198166
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415705
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Parabacteroides distasonis"
                     /db_xref="taxon:823"
     gene            1..370
                     /gene="nusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
     Protein         1..370
                     /product="transcription termination/antitermination
                     protein NusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
                     /calculated_mol_wt=42190
     Region          65..197
                     /region_name="NusG"
                     /note="Transcription termination/antitermination protein
                     NusG [Transcription]; COG0250"
                     /db_xref="CDD:440020"
ORIGIN      
        1 minvlrdgcs ergtvrvgkr hdlktvrwyv ltlpstgvar rdkispaksl daefsrrkrr
       61 getlfeyfap syvevrkvdg kmvntkrpll fnyvfvrasv eeifqmkrtl plynflprvs
      121 sggmthfpyl sddemgnlrw vaesysnelp vyvpdsdrll kgdrvritsg yftgmeaevv
      181 iqpggghkdv marildcmwv pllevkpgey elielntkgk hvythldndr lseglhaalg
      241 ryhasggvce edrrlagevl rsygslraet dvircklcsl llpayklsgd edefvrllat
      301 mrsmlpavka pqsralllvt lygctdscly rqmahevvdp wrcesspkks klslirrled
      361 ydrwlnheis
//
LOCUS       WP_008773796              99 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein
            [Parabacteroides].
ACCESSION   WP_008773796
VERSION     WP_008773796.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..99
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11582
     Region          11..90
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mdffskyrpg iialcekhkv krlfafgsvl tsrfteksdi dlvvdfdkak iedyfsnyfd
       61 lkysleklln rdidlleeqa irnpylkeni dttktliyg
//
LOCUS       WP_008774805             112 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Bacteroides].
ACCESSION   WP_008774805
VERSION     WP_008774805.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..112
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12327
     Region          12..109
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(15..16,34..35,43,46,48..49,51,54..55,57,65,70,77)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(34,65..66,68,89)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mkdykvdkas lsasfcqevy qvvreipvgk vstyggiaal lgmsqcfrmv gralkqipdd
       61 lsapchrvvn asgrlvpgwt eqkqllleeg isfkqngcvd lkkhlwnysv pe
//
LOCUS       WP_008776251             350 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Bacteroides].
ACCESSION   WP_008776251
VERSION     WP_008776251.1
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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..350
                     /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=40308
     Region          8..282
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 megnqsrrid fvdltkgvci ilvvmahvgg afeqldtnsm lscfrmplyf fisgvffksy
       61 eglfgfilrk inkliipflf fylsaflmky ivwkiapgvf qlpvswnell vvfhghdlik
      121 fnpsiwflla lfncnilfyl ihflrekhlp vmfavtilig cagfylgklq ielplyidvs
      181 mtalpfyvag fwirrynffl ypshrfdkli pvfvvlalvv myftattlgm rtnnytgnif
      241 qvyiaafagi fmimllckkv kkikvvsylg rysiitlsih gpilhflgpl vsryihnswa
      301 qasalllitl sicflltpvf lkvipqmvaq kdllkvkqdh tkktvyedkq
//
LOCUS       WP_008778402             316 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Bacteroidales].
ACCESSION   WP_008778402
VERSION     WP_008778402.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidales
  ORGANISM  Bacteroidales
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Bacteroidales"
                     /db_xref="taxon:171549"
     Protein         1..316
                     /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=35557
     Region          1..259
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 merdiridil kgigiilvvw ghatailike icifhmplff flagmfyhpk qgfiqsrakr
       61 llipfgeysl ifavfyfsmg lqgipldkls ihhiaafdgp lwflvalfyi cviyyfldkt
      121 vkeknviliv sfviglavay skinlpfyig qglfslpfya vgkwmndkgl tqaegaikka
      181 tviaiagyii aiafcrlahy qfdisqlkfs sfpfifyaga fcaiylllnf kpfnkitttn
      241 rilaslgans ltimaihapf lwlfrdfirt nssfyntklg ggvisnlitf vifitlsyli
      301 algieqlkkl taknhg
//
LOCUS       WP_008778869             242 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Parabacteroides distasonis].
ACCESSION   WP_008778869
VERSION     WP_008778869.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides distasonis
  ORGANISM  Parabacteroides distasonis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 242)
  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   2  (residues 1 to 242)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Parabacteroides distasonis"
                     /db_xref="taxon:823"
     Protein         1..242
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28061
     Region          102..172
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkwrdllyfs kgerqaltll lsliamawia iigtdfyrsq fqtvplantg ikqdssrihs
       61 nktpsnfirk ekeshsnetk ipsewkskri rreskphfps ypqaekwpqg tvvelnsadt
      121 talkmvpgig svfakriiky rdllggfysv eqlgevygid eeryeamksw fsvdpsvish
      181 lfvnqlsake lashpyvsyk qariiekmir kkgklqgwed lslleefpeh eqqrlryyls
      241 fh
//
LOCUS       WP_008779652             370 aa            linear   BCT 20-JAN-2025
DEFINITION  transcription termination/antitermination protein NusG
            [Parabacteroides distasonis].
ACCESSION   WP_008779652
VERSION     WP_008779652.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides distasonis
  ORGANISM  Parabacteroides distasonis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Kang,J.Y., Mooney,R.A., Nedialkov,Y., Saba,J., Mishanina,T.V.,
            Artsimovitch,I., Landick,R. and Darst,S.A.
  TITLE     Structural Basis for Transcript Elongation Control by NusG Family
            Universal Regulators
  JOURNAL   Cell 173 (7), 1650-1662 (2018)
   PUBMED   29887376
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Liu,B. and Steitz,T.A.
  TITLE     Structural insights into NusG regulating transcription elongation
  JOURNAL   Nucleic Acids Res 45 (2), 968-974 (2017)
   PUBMED   27899640
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Steiner,T., Kaiser,J.T., Marinkovic,S., Huber,R. and Wahl,M.C.
  TITLE     Crystal structures of transcription factor NusG in light of its
            nucleic acid- and protein-binding activities
  JOURNAL   EMBO J 21 (17), 4641-4653 (2002)
   PUBMED   12198166
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415705
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Parabacteroides distasonis"
                     /db_xref="taxon:823"
     gene            1..370
                     /gene="nusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
     Protein         1..370
                     /product="transcription termination/antitermination
                     protein NusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
                     /calculated_mol_wt=42046
     Region          53..195
                     /region_name="NusG"
                     /note="Transcription termination/antitermination protein
                     NusG [Transcription]; COG0250"
                     /db_xref="CDD:440020"
ORIGIN      
        1 mdiltgkcsd rfmahvlkrr dqeavrwyvl tlptagggrd rispskglda elsrrerrge
       61 alfeyfspsy vearkvggkm vntkrpllyn yvfvhasede ifslkrtlpl ynflprvssg
      121 grsyfpylsd remdtlrwva asysnelpvy vpdsgrllkg drvritsgpf tdmeaevvvq
      181 pggghkdvmv rildclwvpl fevrageyel ielntggkhv ythldndrls eglhdalgry
      241 hasgvvvded arlarevlrg yaslrgetdv ircklyslll paylllgeed efdrllstmh
      301 smlpvikagq sralllvtly gctdsslyqr mahelvdpwm eeaspkrskt vlirrlrdyd
      361 rwfghgngde
//
LOCUS       WP_008780519             485 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Parabacteroides distasonis].
ACCESSION   WP_008780519
VERSION     WP_008780519.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides distasonis
  ORGANISM  Parabacteroides distasonis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Parabacteroides distasonis"
                     /db_xref="taxon:823"
     Protein         1..485
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=53804
     Region          24..452
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mankktltpt slpasltlpe erkaekallf gllasrkslp eiafrirpem fthpdialai
       61 eaylslhgkg egtdilsvek eirrlspera gqlpdlfela rqdgymevgg efvrqhcqyi
      121 reafvarrli lrchelahka aaddrdtqkl iselgtvade lgeqlslthe ipdmptatae
      181 amarvreirk rvarggtagi htglggldrl mgglrtgslh vfaarpgmgk tafalfmavn
      241 aakqgvpvcv yslemsreql ifrmlgqiad vepskitkgt ateeemrale easrqlkelp
      301 icinqrsdiq ideircdisl rrrqgkcsla iidylqlvnr ddkgqtpnea isnitrkaki
      361 tamdeeipiv llcqlnrnce trgtysfrhq lsdlrdsgsi eqdadtvafi srlsvvnihe
      421 dpdthlptrg rgtillaknr qgelghvrfm hnegvasfwd dtqpacvrka raaepkpkgk
      481 glfec
//
LOCUS       WP_008781166             509 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [Parabacteroides].
ACCESSION   WP_008781166
VERSION     WP_008781166.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 509)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 509)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 509)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..509
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=58007
     Region          4..412
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mennvvsvml wgeevgklyw derskravfn yhpdfikkgv eiapltasvk gsaakgmpil
       61 gnrekiyqgl ppfladslpd rwgnmvfdqw aaqnhipkrk ltpvdklsfi gkrgmgafef
      121 ipatpgless stlqieslyq larrifeere eisvqddeal qlqsiyeigt saggqhpkai
      181 iainetthdi rsgqvplpeg ytyyilkfae gddfpftqme mvyyklakea gitmmpsrli
      241 qiegkhhflt erydringek ihtqtlaamn pdatsyedlf evcrklsipa seqselyrrm
      301 vfnvmggnvd dhiknfsflm erngtwhitp aydmtfttnl dgaayenvhs mnisgkdngi
      361 teddllqfar qngiknakri ieevslaish fydyatnyqi deywkdriee hlsglvspli
      421 getmkhylpt ivepyetedg flvseiniie ntrhdfriea vingkrqkyi agrksdlaae
      481 iiakgrnkmt aenkkeller lllplarrk
//
LOCUS       WP_008781167             529 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [Parabacteroides].
ACCESSION   WP_008781167
VERSION     WP_008781167.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 529)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 529)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 529)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..529
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=60608
     Region          6..429
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mndlivdvkl wgesvgslyw ekesnaalfd yerkfirsgl dispiimpid qyrntpyrfl
       61 enrtncfkgl pglfadslpd tfgnqiinew faskglsree itpldrlcyv gkrgmgalef
      121 epsspingmn essvlhieel telakfvftd rmafqaqlrq egrnildilk vgtsaggakp
      181 kaiiayndit gevrsgqvka pegfgywllk fdggkyseht qitdnpqgig nieyayhrma
      241 kacgidmmec rllqekesch fmtrrfdrme ngekihvqtl aglahydrdq rhsyeeifri
      301 mrqmnlpyps qeelyrrmvf nvmsrnhddh sknfsflmdk qgkwklspay dlcysytpgg
      361 kwtnrhqlsl ngkqdnftme dlqkvgenmg irehkqiiek vqetvshwhe takdcgvkpe
      421 hadfigksll lfgkqlhtiq mpdianeqeq afmkamrndd fnailelkmk gyqpsekvlk
      481 ilqpdisatt fiaaakifqm eevlksiqdi kpaqspiigg nkrsmelgd
//
LOCUS       WP_008781602             593 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase [Bacteroidales].
ACCESSION   WP_008781602
VERSION     WP_008781602.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidales
  ORGANISM  Bacteroidales
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Bacteroidales"
                     /db_xref="taxon:171549"
     Protein         1..593
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=68083
     Region          35..527
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mdknelvnki rgiegltnde ksaliemlrk qkkyglvwed kpedveerlr eelpmliedt
       61 dkaiistdtd apnhiliegd nlealtalay thegnidviy idppyntgnk dfvyndkfvd
      121 sedsyrhskw lsfmnkrlri akqllsdkgv ifisiddneh aqlkllcdev fglnnlcgni
      181 iwrkksgggq tdaffvtehe yilvyrktdq fiwqdetvai sedtfkymde rgrykitple
      241 kwgssahred rpsmyfaiks pdgkdyfpva pdglpgrwrv glermnrlim ndeidwrngk
      301 pqektyftsi sdkrkvnksr siyynigetg egtklltdif sqkdifgnpk plnlvkdlis
      361 hnnrdstild ffagsgttlh atmqlnaedg ghrkcilvtn nennicenvt yirnkrviqg
      421 yttpkgeeip gltgntlryy ktdfisrdqt prnmralvaa stdllciknd iykeaklagr
      481 ninskiaryf eegdsrmlii yderaisaia eilemvesgk ekikvyvfsp ssyayddefe
      541 evadkvqlca lpdaiyqayq kvlpkrrpkf lpeameeaeq sndsetglfm rea
//
LOCUS       WP_008782974             531 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Bifidobacterium longum].
ACCESSION   WP_008782974
VERSION     WP_008782974.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium longum
  ORGANISM  Bifidobacterium longum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 531)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Bifidobacterium longum"
                     /db_xref="taxon:216816"
     Protein         1..531
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=56752
     Region          393..530
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(480..481,484,503..506,508)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mtehlddstq qfaplfgann avsgtvadsv daaasdsiqg demrrrriwp wvviacllva
       61 lgaacgggvw ffqdhvlpgt tlwgnsvtgk teqeiadlin dqvdntavra kyqgqsatft
      121 lkdlgievdg eaiasdvina qrgdawwqqy afwithdvap qinpeladgs vvdkalnida
      181 qepvdaqval ndnnsgfnvi agengqgana tsiakqaist veslgsvqpq tvrveldvte
      241 ptitnaiade akttletlvn navaikvadk diatvnasml gsamridanq qsklkdnevr
      301 ngyvvfdadk lqqyydeqik pnlkleredk kvvvnnagev lsteteghdg iviadgadte
      361 vgarlaqvla tgtgsvnvdg kvdpkqevkv ahrvaidlsd rklyayendt vvktlnvvva
      421 egndnvtgec vgmmctptgd fnvwqklpsq dmsgtlnlad gtvetwdvkd vgfvnyfssg
      481 caihriaggy vadavmpsia ngshgcvgig wdvaewfynw cnmgtsvhiq v
//
LOCUS       WP_008782124             311 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Phocaeicola].
ACCESSION   WP_008782124
VERSION     WP_008782124.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola
  ORGANISM  Phocaeicola
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Phocaeicola"
                     /db_xref="taxon:909656"
     Protein         1..311
                     /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=36189
     Region          5..259
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mnniridwid ltkgiaiflm vcghtsipls isnwiwsfhm plffiisgil fnatkypnfn
       61 lfikkrgktl iipyiifsli tlltihdqtl kewlykgwin gcalwfipvl ffaeifsyfi
      121 iryinsncli lltaitigti gymlyffnih fpynidvsfy asffyligyi sknkiihypp
      181 khslaiclli vniilsqilp rtdmawnncg wyglnainai ggtfaiilit ktyfdniyat
      241 piklffkwag hntiiilgls qiistyikig fsyfsvpeim npflrhiflw iilyilsiii
      301 rkyfpriigq k
//
LOCUS       WP_008783047             209 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Bifidobacterium longum].
ACCESSION   WP_008783047
VERSION     WP_008783047.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium longum
  ORGANISM  Bifidobacterium longum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 209)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Bifidobacterium longum"
                     /db_xref="taxon:216816"
     Protein         1..209
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=22476
     Region          82..166
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mtyqvderea rkayvrrrqt ivfsisgavl avvlviallf nfhvfglgev etpasqpnyg
       61 naapcavkds sgkaqyvsna svgirvmngt shgqfakavg ealanrgfsv qkidnysstd
      121 verttiyfgk nainqaytli gnftdatmim taredqlidv vigatfndlq dtnsfpqsgk
      181 titniegcka adsmtklpad tkhdaytaq
//
LOCUS       WP_008783447             404 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator
            [Bifidobacterium].
ACCESSION   WP_008783447
VERSION     WP_008783447.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 404)
  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 404)
  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
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 404)
  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   5  (residues 1 to 404)
  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   6  (residues 1 to 404)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 404)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 404)
  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 11513089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..404
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42872
     Region          14..>66
                     /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"
     Region          81..364
                     /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 matntthats qasvsesnrs rivkhlyhng issraqiaka leltpaaitk itarlieagm
       61 ieetgdlegs knrrsiglkl ntthfriigi kfarslvqig vfdlcgntls fenlptvcdn
      121 tindsivtih qrveqlldnd psivaigmav pgpylrnvgr tavvsnmqgw rkinfidefa
      181 tafrvpvfie qdaragalah ylfdpsvhad dnlayylvge gvglgvidng rlingflgaa
      241 teighisidv ngrpcdcgnv gclerycstp aihdtliadg tvvpgaadmt hteaaralfa
      301 kagdgdeaai aivrevaryv gygcvtifng ynpehiiigd ivseagpill devratvaer
      361 aipeinasts islstlsada avsgaaavav tqflehpsvf fdvs
//
LOCUS       WP_008787936             396 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Coprobacillus cateniformis].
ACCESSION   WP_008787936
VERSION     WP_008787936.1
KEYWORDS    RefSeq.
SOURCE      Coprobacillus cateniformis
  ORGANISM  Coprobacillus cateniformis
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Coprobacillaceae; Coprobacillus.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Coprobacillus cateniformis"
                     /db_xref="taxon:100884"
     Protein         1..396
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43160
     Region          2..395
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mskviavnag ssslkfqlfe mdnetvitsg vierigmeds iftikyngek dvrtlaipth
       61 keavhllldt liekqivssl deikgvghrv vqggsyfqes aiidedvink idelkslapl
      121 hnpahltgyy afkeaipsag avavfdtafh qtlqpkcyiy pipykfyten kvrkygahgt
      181 shfyvsqrvi dklgqpehsk iivahlgagg sltavkdgks intsmgftpl agimmgtrsg
      241 dldpsiidyl ieqvgmdmkd vihmlnkesg llgvsgvssd frdvlnaane gneraklaid
      301 iffrrviayi gryfialggc daiaftagig ensayarkei lslvsealgi vvdddaneng
      361 egerlistpe skikvyvipt neelviardt krllnl
//
LOCUS       WP_008788305              73 aa            linear   BCT 20-JAN-2025
DEFINITION  acyl carrier protein [Coprobacillus cateniformis].
ACCESSION   WP_008788305
VERSION     WP_008788305.1
KEYWORDS    RefSeq.
SOURCE      Coprobacillus cateniformis
  ORGANISM  Coprobacillus cateniformis
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Coprobacillaceae; Coprobacillus.
REFERENCE   1  (residues 1 to 73)
  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 73)
  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 73)
  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   4  (residues 1 to 73)
  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 10011594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..73
                     /organism="Coprobacillus cateniformis"
                     /db_xref="taxon:100884"
     Protein         1..73
                     /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=8353
     Region          1..73
                     /region_name="acpP"
                     /note="acyl carrier protein; Provisional; PRK00982"
                     /db_xref="CDD:179197"
ORIGIN      
        1 mdyfdkikdr lssklkgkel mkessfkelg idsldlvdlv feleeeigve fqdeellkis
       61 tvqdlldlid skk
//
LOCUS       WP_008788421             493 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Coprobacillus cateniformis].
ACCESSION   WP_008788421
VERSION     WP_008788421.1
KEYWORDS    RefSeq.
SOURCE      Coprobacillus cateniformis
  ORGANISM  Coprobacillus cateniformis
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Coprobacillaceae; Coprobacillus.
REFERENCE   1  (residues 1 to 493)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Coprobacillus cateniformis"
                     /db_xref="taxon:100884"
     Protein         1..493
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=56323
     Region          244..343
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          366..492
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(443..444,447,465..468,470)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mdedhvkneh veeqetktks hkyilfikey ktkfligggi lficiyafgc iyyqnrfmsr
       61 ttingmnvag inyqkatqki qehidkrtmt lifldgekei ltqenigftf nqnndikkei
      121 kkqnaflwft hwfyqdnmti nnlfivdekk letslsqlkh lqddyqvapa dakvqykdhn
      181 fsiaketigs kiqkdiliqk ittafqnget elnveevggy vkpkttsede slkklleaak
      241 kycdvsityk tinedvvldg ntlvswlsid esgnyykddn efkkqatefv kklskninii
      301 gkkktftgah grkinisggn ygyklkqeke vegllkdiqa gkkgmrtpvt tgiqasydng
      361 glgqtfieid mtkqhfwyhk ngkivlesdi vsglpsdphk ktpagtyyiy fmqlnrtlrg
      421 eiqadgkpey etpvaywmaf nggiglhdat wqsrfggdvy ytrgshgcin lplkvaaely
      481 dmvkvntpvv cyy
//
LOCUS       WP_008788565             375 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Coprobacillus cateniformis].
ACCESSION   WP_008788565
VERSION     WP_008788565.1
KEYWORDS    RefSeq.
SOURCE      Coprobacillus cateniformis
  ORGANISM  Coprobacillus cateniformis
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Coprobacillaceae; Coprobacillus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Coprobacillus cateniformis"
                     /db_xref="taxon:100884"
     Protein         1..375
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43693
     Region          1..248
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          258..348
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkfvhigdlh lgkvihqysl ldiqrellfe llefmnqedi hilliagdvy drfipsqeav
       61 nllddflsca llkynlevfm isgnhdsndr mhfassilsa qglhietylk eemqyveidd
      121 vrfyllpfvk psqikgmyqv eelnnyqdal slymshqhid knyknimmth qfvghssvts
      181 eseiplsvgg seivdvslfq dfdyvalghl hapqkvsret vrysgslmry sfdevqqkks
      241 ivivdtddms vttyalhpsv tlekykatfe qfmdphyiyk kddflafele dqtliphaid
      301 qlrvlyprll qitysylinq qthqqikkiq sieqmdtpal ftqfyqdmkn selssqqqki
      361 vlellekvge dheny
//
LOCUS       WP_008788676             103 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Coprobacillus
            cateniformis].
ACCESSION   WP_008788676
VERSION     WP_008788676.1
KEYWORDS    RefSeq.
SOURCE      Coprobacillus cateniformis
  ORGANISM  Coprobacillus cateniformis
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Coprobacillaceae; Coprobacillus.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 103)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 103)
  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 103)
  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 103)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Coprobacillus cateniformis"
                     /db_xref="taxon:100884"
     Protein         1..103
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12238
     Region          9..99
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(29,48..49,67,70,78..79,91,96)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mfveqksdlt mniftrtitd kngnhlylts kefdlfyfly syrgqvftke qlyenvwgyd
       61 yapdaknlis firklrkkie pdpdkpqyii tvwgvgykfa kdi
//
LOCUS       WP_008788713             325 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Coprobacillus cateniformis].
ACCESSION   WP_008788713
VERSION     WP_008788713.1
KEYWORDS    RefSeq.
SOURCE      Coprobacillus cateniformis
  ORGANISM  Coprobacillus cateniformis
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Coprobacillaceae; Coprobacillus.
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
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 325)
  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   5  (residues 1 to 325)
  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   6  (residues 1 to 325)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 325)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 325)
  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 18263812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Coprobacillus cateniformis"
                     /db_xref="taxon:100884"
     Protein         1..325
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36871
     Region          93..>235
                     /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 mykskglkni siqkvkdyfi enkyatknqi aeethlshat itnilkelle nqfivrvedc
       61 estggrkakq ykicgsymvf glidlrvqnq tvsiecrivd ldfviienmk cqfdtlnlnv
      121 ftnliqdike khhiqylgis ipaivtngki eksdiesldg velqkhietv cgihtmiend
      181 vntvmlgyih thviesqsia fvyqpdnhhs gcglyingsl lygathfage laylpngtlk
      241 eqedilkkdp lsllikqaas iiaimnpslm ilytpcvete ifkatikkyi pvqhlpefqf
      301 inemetyife glaslciess rykrk
//
LOCUS       WP_008789396              90 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Coprobacillaceae].
ACCESSION   WP_008789396
VERSION     WP_008789396.1
KEYWORDS    RefSeq.
SOURCE      Coprobacillaceae
  ORGANISM  Coprobacillaceae
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales.
REFERENCE   1  (residues 1 to 90)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 90)
  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 90)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Coprobacillaceae"
                     /db_xref="taxon:2810280"
     Protein         1..90
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10429
     Region          15..70
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mnkdymyfyt kvsganispt arsvyrallq yanrktwscf psvntlsrdt glssrtirrs
       61 lqvlekeeli lrihrtrenn gntsnmyfln
//
LOCUS       WP_008791086             610 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: VirB4 family type IV secretion system protein
            [Thomasclavelia].
ACCESSION   WP_008791086
VERSION     WP_008791086.1
KEYWORDS    RefSeq.
SOURCE      Thomasclavelia
  ORGANISM  Thomasclavelia
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Coprobacillaceae.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Thomasclavelia"
                     /db_xref="taxon:3025755"
     Protein         1..610
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=69930
     Region          30..610
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mksfndmknl mfksravprg fheyanyyvi gdkfhramtf titkdfdegf lgmfvagqny
       61 rvemvtepsk akisnymktv vkdmeqeysk ttdriqrael reqmdgynay irelvrkrda
      121 tlnciitvfi eantleelde rtydldklfs tynvevraer flqqrilkcs spffesdgfr
      181 keasqnigql lstqtvsgly pftfdtldde kgmllgvess qkgmvcfdqf lylnnpakak
      241 kykrlngnli iigesgsgkt tamdlilmsh ichtrkviwi dpenknrtii kqaggsyfnl
      301 gtknarinif dlkpiscded eedevdkydt rlaiynvved ikivfrylsk disegaldil
      361 gelvleayet vgvninesfq ylkntdyptf svfsaivdeh iekfeksniv ndeytalkei
      421 riklkpicte waryldghtt itedemknpf fafgtkvffn ltpglknalm hiifqyawgl
      481 cldetsesvl avdeahmfvl agetakmieq fqrrsrkyhn vtilgtqeph dfadprvlae
      541 gkaifnnasy klilgldkda tkdlrkltal sdneikriar fsqgdailia gnkrlpieik
      601 atpdqlalmr
//
LOCUS       WP_008790740             280 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Coprobacillus cateniformis].
ACCESSION   WP_008790740
VERSION     WP_008790740.1
KEYWORDS    RefSeq.
SOURCE      Coprobacillus cateniformis
  ORGANISM  Coprobacillus cateniformis
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Coprobacillaceae; Coprobacillus.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 280)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 280)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Coprobacillus cateniformis"
                     /db_xref="taxon:100884"
     Protein         1..280
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32721
     Region          21..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          130..277
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mewidrfnqa idyieehlit einyeelaki tncsryhfqk iflymtsisl neyirkrrms
       61 laavdlqdlk mrivdiafky gyesptafnr afqsihgiap stlrkegiel vafpplhfsf
      121 siqgleelhf rienkqsfqi igksfplnke lsenflkipk hwnqaladgt lkqlmeinnc
      181 mptgllgvsi hyhddwryfi avsstlshpq feeytidkam wavfsgqgsn ktlqdlerrv
      241 itewlptsgy eyadipdiev yikadpqdai yeywlpiikk
//
LOCUS       WP_008791454             160 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Thomasclavelia ramosa].
ACCESSION   WP_008791454
VERSION     WP_008791454.1
KEYWORDS    RefSeq.
SOURCE      Thomasclavelia ramosa (Clostridium ramosum)
  ORGANISM  Thomasclavelia ramosa
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Coprobacillaceae; Thomasclavelia.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 160)
  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 160)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Thomasclavelia ramosa"
                     /db_xref="taxon:1547"
     Protein         1..160
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18273
     Region          28..75
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mldenkiqfi kyysklandr rldkfdvily glieylsnnd kgfctasnnt ladylgcsrs
       61 tvirsinklv ecdylkaenk hapnnknith relkpssvnd ttlvsemnkg ssaydttlvs
      121 nmiqpssvnd tlkelykknn ikeyikevkp ievnedlfkf
//
LOCUS       WP_008793009             377 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: exonuclease SbcCD subunit D [Thomasclavelia].
ACCESSION   WP_008793009
VERSION     WP_008793009.1
KEYWORDS    RefSeq.
SOURCE      Thomasclavelia
  ORGANISM  Thomasclavelia
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Coprobacillaceae.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Thomasclavelia"
                     /db_xref="taxon:3025755"
     Protein         1..377
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42740
     Region          1..267
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          262..351
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrfvhisdih lgkllyqqnl leiqadllnq vcdylvdnei dvlvmagdiy drsvpsneai
       61 dvlndfltkv ilkyhkkvlm iagnhdsasr lsfvsgllrq eglyieaypa kqmkpieieg
      121 vnfylmpffk psyirylyed eqivtyqdaf rcylehqkid ftkpnvlith qfiagnsevm
      181 rseseavlsv ggteiidvsl vkqfdyvalg hihapqkist etirysgslm rysfdevnqt
      241 ksivevtidn kkvsyqlvsl qpkqdlikit gsfdeimads favnnndfia veltdsmlvp
      301 naidylrtkf snvlqitypk lisnetsnnt kadpgfekld svalfeqfyq kikgtelsae
      361 akqivteimm ggkenva
//
LOCUS       WP_008793354             581 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Fusobacterium
            periodonticum].
ACCESSION   WP_008793354
VERSION     WP_008793354.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium periodonticum
  ORGANISM  Fusobacterium periodonticum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Fusobacterium periodonticum"
                     /db_xref="taxon:860"
     Protein         1..581
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=66411
     Region          2..555
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 midkrlynfs gnikkyisit tflscvklia niffyfifaf llvslinrdf sfsykyiiis
       61 iliivlirqf stikishmlg nlvvdvkrnl rklifektlk lglaysqlfk tqelihlsvd
      121 nveqlevyfg gfltqffycv vssfilffsi ayfnlkiafi llifslaipm slyiilnkvk
      181 kiqkkyfaky mnvgtlflds lqglttlkiy gtdekreeei akmseefrve tmrvlkmqll
      241 siavinwiiy agtilaiits iklfidgslg lfpmlfifml apeffipmrt ltslfhvamt
      301 gvsaaeniis fidspernsv gekefknere fkvsnlsfty pdgtqslkdi nmtfkkgslt
      361 avvghsgcgk stlvsvlage lksneneifv ddidihnikl edkvknilki thdshifsgt
      421 vrdnltmane kltdetmvev lktvklwdif skakgldtvl esqgknlsgg qaqrvalara
      481 llydasvyif deatsnidie seeiilniih flskektviy ishrlpaikn adciyvmdkg
      541 rvvengkhnd lyakkelyyn mykhqeeles yltkrgetne k
//
LOCUS       WP_008793939             379 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Fusobacterium
            periodonticum].
ACCESSION   WP_008793939
VERSION     WP_008793939.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium periodonticum
  ORGANISM  Fusobacterium periodonticum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 379)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 379)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 379)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Fusobacterium periodonticum"
                     /db_xref="taxon:860"
     Protein         1..379
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43145
     Region          3..374
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mnkskslqvf ynekkvgtla lmknnivafe ydsnwitngf sispfslplk kqvfipridp
       61 fdglygvfsd slpdgwgrll vdrmlnsqni npreisqidr laivgetgmg alsykpeynl
      121 ledkdyqedy dnlalsckki lnteysadld klfklggssg garpkiltki dnedwiikfp
      181 ssldesnigk leylysvcak kckidipetk lfpskissgy fgikrfdrkk lstgairklh
      241 misvsgllet shripnldyn dlmqltlnlt ksfeeveklf rlmcfnvfsh nrddhsknfs
      301 fiynedlnkw elspaydlty sysingehat tingngvnpd lndilkvaek igldkkkaek
      361 iaieiretvr kdleiflsk
//
LOCUS       WP_008794135             240 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Fusobacterium periodonticum].
ACCESSION   WP_008794135
VERSION     WP_008794135.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium periodonticum
  ORGANISM  Fusobacterium periodonticum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 240)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Fusobacterium periodonticum"
                     /db_xref="taxon:860"
     Protein         1..240
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=27127
     Region          58..221
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mkflkkmfml lfyfvlssiv fadfttielp sdfsisykkd fsdkeirnmy ydlklndkvs
       61 ftcfnnavsg lekisyatne llvlvdytkp steerlfvvd lskkrvvfss lvshgkgngg
      121 lyattftdrn nsyasssgfy ltgniyngkh grslvlygle egkndnaerr tivmhsadyv
      181 seefiqkngs lgrskgclal pvelnakiid lihdgvviyv htnfdenney dfsklssnri
//
LOCUS       WP_008794380             921 aa            linear   BCT 20-JAN-2025
DEFINITION  AAA family ATPase [Fusobacterium periodonticum].
ACCESSION   WP_008794380
VERSION     WP_008794380.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium periodonticum
  ORGANISM  Fusobacterium periodonticum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 921)
  AUTHORS   Liu,Y., Sung,S., Kim,Y., Li,F., Gwon,G., Jo,A., Kim,A.K., Kim,T.,
            Song,O.K., Lee,S.E. and Cho,Y.
  TITLE     ATP-dependent DNA binding, unwinding, and resection by the
            Mre11/Rad50 complex
  JOURNAL   EMBO J 35 (7), 743-758 (2016)
   PUBMED   26717941
REFERENCE   2  (residues 1 to 921)
  AUTHORS   Chen,Z., Luong,T.T. and Lee,C.Y.
  TITLE     The sbcDC locus mediates repression of type 5 capsule production as
            part of the SOS response in Staphylococcus aureus
  JOURNAL   J Bacteriol 189 (20), 7343-7350 (2007)
   PUBMED   17704228
REFERENCE   3  (residues 1 to 921)
  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   4  (residues 1 to 921)
  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
REFERENCE   5  (residues 1 to 921)
  AUTHORS   Hopfner,K.P., Karcher,A., Craig,L., Woo,T.T., Carney,J.P. and
            Tainer,J.A.
  TITLE     Structural biochemistry and interaction architecture of the DNA
            double-strand break repair Mre11 nuclease and Rad50-ATPase
  JOURNAL   Cell 105 (4), 473-485 (2001)
   PUBMED   11371344
REFERENCE   6  (residues 1 to 921)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..921
                     /organism="Fusobacterium periodonticum"
                     /db_xref="taxon:860"
     Protein         1..921
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=107504
     Region          1..919
                     /region_name="PRK03918"
                     /note="DNA double-strand break repair ATPase Rad50"
                     /db_xref="CDD:235175"
ORIGIN      
        1 miikrvklen yrshsnttvn fskgvnlilg kngkgktsil eaissvmfnt kdrsgketgk
       61 nfikfneksg kieieftand grdyilktef fktkpkkqsl tdingldceg diqenleelc
      121 gikkgfeety eniviakqne finifkakpk dreeifnkif ntqiykemyd gflkeatdky
      181 tkqidylskd inslkdnmed keeisnflke eevlkeslnt efsktteist klsneikdye
      241 adeinlknli sniedeenki ekysnllkdn ileakkakka ktivkenekp yleyleienk
      301 lkdfreihtn llqeqklniq yqnnieklel snktlktdia nleesiskns ekkdsldkni
      361 aelkskeedl tsklkeyenl likledlekt kkknsdkhle kkteinilgk elsakkdlfv
      421 ainiediekq ltvfkdleke iksleedkia feieiktlrn asnelsskic pylkencenl
      481 kdkeaddyfs skisirteti edlkkkieek kvilaeksvf eekkkqyfel dktiknlels
      541 lkteevnlke ievniksldi siqqlienqe fqdstslkeh kkglevelkn lnldekrenl
      601 knlieslefe kekilknqss iennlkeide yckkikadtd kniknvtsei kifenkltel
      661 ktsyneyikn nvlakdlenl llkveksike lyslrfnkns lkekvfnlen kiknikidel
      721 rekfnilkee lneiskklgs sqekienykk ilekiasqee kqkklldelk kledksnran
      781 lirnevgkmg raiskymlsg isniaslnfn kitgrterie wsndekdkyv lylvgqerki
      841 afeqlsggeq vsvaiairgt mteyftnsrf mildeptnnl dterkkllae ymgeilknld
      901 qsiivthddt fremaekiie l
//
LOCUS       WP_008795714             413 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Fusobacterium].
ACCESSION   WP_008795714
VERSION     WP_008795714.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 413)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..413
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=46850
     Region          58..222
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mkkvliifcl lliannnfae enivtenine niqkpveekp qkivldvksv ydslniknki
       61 dysifqkayl gyvqitnknp gvliiidysk psneerfyvl dlnkkklvys trvahsknsg
      121 leiplqfsdd pnsyqsslgf fvtlgeynga ygyslrlkgl eeninanaed raivihggni
      181 veddyikryg fagrslgcpv lpyslareii dfikhgrvlf iygndeeyid nstylsklaa
      241 vfegspkniv eiekpseiqk tspaptvttv atvnhpaatv lgdkkeninr etviaeanit
      301 kiheiikqea kytnnvnnnk vsytellkdv iqernnktsk tkenienkks neenndnqek
      361 iveqtitdns letkqesktt vqqnenieen kkeerkypee vikkslglei klk
//
LOCUS       WP_008796625             585 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein/permease
            [Fusobacterium].
ACCESSION   WP_008796625
VERSION     WP_008796625.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..585
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=66795
     Region          2..556
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 midkrlynfs gnikkyisit tflscvklia niffyfifaf llvslinrdf sfsysyiiis
       61 iliivfvrqf stikvahmlg nlvvdvkrnl rklifektlk lglaysqlfk tqelihlsvd
      121 nveqlevyfg gfltqfyyci vssfilffsi ayfnlkiafi llgfslaipl slyiilnkvk
      181 kiqkkyfaky mnvgtlflds lqglttlkiy gtdekreeei akmseefrie tmrvlkmqll
      241 siaainwiiy agtilaivts vklflngslg lfpmlfifml apeffipmrt ltslfhvamt
      301 gvsaaeniis fvdspernnn gnkefknene ikvsklnfsy pdgtqslkdi dmsfkkgnlt
      361 avvghsgcgk stlvsvlsge lkskeneifv ddidiqniki edkiknilki thdshifsgt
      421 vrenltmane nlsdetmiev lkkvklwdif lknkgldtsl esqgknlsgg qvqrvalara
      481 llydasvyif deatsnidie seeiilsiiy slskektviy inhrlpaikn adciyvmdkg
      541 kiiesgehik lyakkglyye myrhqeelet yltkrgenne ksvnf
//
LOCUS       WP_008797161             256 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Fusobacterium].
ACCESSION   WP_008797161
VERSION     WP_008797161.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..256
                     /product="formate/nitrite transporter family protein"
                     /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=27560
     Region          6..256
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 madghktpse lvdyminvgv dkatkplfkl mllgifggaf ialggagnii sgstlvktdp
       61 glakfvgacv fpvglimvvi lgselftsnc lltvaytnkk isftqlirni vivylfnyvg
      121 sfivsyitvk ggsfnsdsla ylqdiathkv hasayalfik gilcnvlvcg avllsytskd
      181 tigkligawl pimlfvligy dhsianmfyl tatklvdtsf eissilynlf yvtlgnivgg
      241 maiglplyfc yykkqd
//
LOCUS       WP_008798123             243 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Fusobacterium animalis].
ACCESSION   WP_008798123
VERSION     WP_008798123.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium animalis
  ORGANISM  Fusobacterium animalis
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 243)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Fusobacterium animalis"
                     /db_xref="taxon:76859"
     Protein         1..243
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=27724
     Region          55..224
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mkllkniftl ifyfifslsl faeinfsnnf nldikkkfsd rdiklmytel slndkvsfsc
       61 fnnamhglek iedleifnns ndsllvmvdy tkpsteerlf ivdlkekrll isslvthgrg
      121 tgdlyatkfs nknnsystss gfyltgniyn gkhgeslely glekgkndna rkrtivmhsa
      181 yyankkfaek ygrlgrskgc lalptelntk iinlisggvv lyvhtnfden keydfsklls
      241 nsy
//
LOCUS       WP_008798247             700 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase [Fusobacterium].
ACCESSION   WP_008798247
VERSION     WP_008798247.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..700
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=81662
     Region          57..620
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 melenkvpeq ldsikndnlk aleklfpsvi kdgeldidal keeignfeev knerydftwa
       61 gkqeakkkaq edvmartlkf iekdsvnpds tenlyiegdn levlkllrqn yrgaikmiyi
      121 dppyntgndf vyndnfkisq kesdkkqgyi dennqrlqkn skdsnrfhan wltmmyprlk
      181 iardllsedg vifihiddne menigkvcnd ifgeenfini itiktkiggv sgssegkslk
      241 dvtefiwafc knkneiflnp vynkirlfer iqdyidegks wkytsiitki gdkillkrde
      301 kndmnfygyn iletqsifsy akehkisiee vynkfadkif rttnaqssir qkviketkny
      361 kypifsceyi pikgknlgqk ieilyksgst seqrnmvmfl sdvvtkenge yfyldkitsl
      421 wddieynnlt kegniefqng kkpvkllqrl inlstnnndi vldffsgsas tahavmqlna
      481 edggnrkfim vqidekvked teaykflnei nkptniceig kerirrvgek ikkeieeknk
      541 nlkdeeelkk vpdigfkvfr tadtninwrk irdisnsesl pfnepdrldf ienyndkdiv
      601 yevllrqrdl plsekletld tignrtylya ssylicletd itenlikela dlnplpikfi
      661 frdsafksdi nlkestfryl ktlveknsgi nkrtytiefi
//
LOCUS       WP_008798262             398 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Fusobacterium animalis].
ACCESSION   WP_008798262
VERSION     WP_008798262.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium animalis
  ORGANISM  Fusobacterium animalis
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Fusobacterium animalis"
                     /db_xref="taxon:76859"
     Protein         1..398
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43619
     Region          1..398
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkilvincgs sslkyqlinp eteevfakgl cerigidgsk meyevvakdf ekkmetpmps
       61 hkealelvis hltdkeigvi ssvdevdaig hrvvhggeef aqsvlvndev lkaieanndl
      121 aplhnpanlm girtcmelmp gkknvavfdt afhqtmkpea fiyplpyedy kelkvrkygf
      181 hgtshlyvsg vmreimgnpe hskiivchlg ngasitavkd gksvdtsmgl tplqglmmgt
      241 rcgdidpaav lfvknkrglt daqmdermnk ksgilglfgk ssdcrdmena vkegderail
      301 aesvsmhrlk syigayaaim ggvdaicftg gigenssmtr ekaleglefl gieldkeins
      361 vrkkgnvkls kntskvliyk iptneelvia rdtfrlak
//
LOCUS       WP_008798450             581 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein/permease
            [Fusobacterium].
ACCESSION   WP_008798450
VERSION     WP_008798450.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..581
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=66127
     Region          2..552
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 midkrlykfs gnikkyisit tflscvklia niffyfifaf llvslinkdf sfsysyiiis
       61 iliivfirqf stikishilg nlvvdvkrnl rkiifektlk lglaysqlfk tqelihlsvd
      121 nveqlevyfg gfltqfyyci vssfilffsi ayfnlkiafi llgfslaipl slyiilnkvk
      181 kiqkkyfaky mnvgtlflds lqglttlkiy gtdekreeei akmseefrie tmivlkmqll
      241 sialinwiiy agtilaivts vklflggslg lfpmlfifml apeffipmrt ltslfhvamt
      301 gvsaaeniis fvdspernnn gnkefknene ikisklnfsy pdgtqslkdi dmsfkkgnlt
      361 avvghsgcgk stlvsvlsge lkskeneifv ddidiqniki edkiknilki thdshifsgt
      421 vrenlsmane nlsdetiiev lkkvklwgvl sldtilesqg knlsggqaqr valarallyd
      481 asvyifdeat snidieseei ilniiyslsk ektviyishr lpaiknadci yvmdkgkvie
      541 sgkhiklyak kglyyemykh qeeletyltk rgenneksvn f
//
LOCUS       WP_008798519             180 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Fusobacterium].
ACCESSION   WP_008798519
VERSION     WP_008798519.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (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   2  (residues 1 to 180)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..180
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21038
     Region          42..104
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkklmlllgi fslfslslyp apdlsnndyk iimssqnmkd ekeelmdink vseqemlark
       61 vsksyvskii eyreitggfd kledmkrikg igdatyqkls kffkvgsepn kkmlninsan
      121 eitlkyygfs kkeikkiqky ldkndritdn iefqkivnkk tyerlkdlin ydggkrewed
//
LOCUS       WP_008799394             243 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Fusobacterium].
ACCESSION   WP_008799394
VERSION     WP_008799394.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 243)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..243
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=27639
     Region          55..224
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mkllkyvfsl iiyfifslsl faeinfsndf nlnikkkfsd mdiklmytel clndkvsfsc
       61 fnnamhglek iedleifdns nnnllvmvdy tkpsteerlf iidlrkkqll isslvthgrg
      121 tgdlyatkfs nknnsystss gfyltgniyn gkhgeslely glekgkndna kkrtivmhsa
      181 yyankafaek ygrlgrskgc lvlptdlnak iinlisggvv lyvhtnfden keydfsklls
      241 ksf
//
LOCUS       WP_008800177             301 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Fusobacterium].
ACCESSION   WP_008800177
VERSION     WP_008800177.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..301
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=34469
     Region          51..213
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkkilafisl lflmvacsst edvkssgnrn inrgsnisrs qttirnigkf qvdsnsyvat
       61 gknervqfii lhytatdnlg sikeltssrv sshflvlded dnkiynlvpl eqrawhagas
      121 afrgrtnind tsvgieivsd giakefiadp npyhpydhyv dykpiqieka aqiikyvaek
      181 yniparnila hsdiapsrkk dpgakfpwke lydkynigaw ydeadkqefm deekfnatsi
      241 reikdelrky gyeinrfdew dkeskdvvya fqlhfnpknp tgemdletfa ilkalnkkyp
      301 d
//
LOCUS       WP_008800606             921 aa            linear   BCT 20-JAN-2025
DEFINITION  AAA family ATPase [Fusobacterium gonidiaformans].
ACCESSION   WP_008800606
VERSION     WP_008800606.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 921)
  AUTHORS   Liu,Y., Sung,S., Kim,Y., Li,F., Gwon,G., Jo,A., Kim,A.K., Kim,T.,
            Song,O.K., Lee,S.E. and Cho,Y.
  TITLE     ATP-dependent DNA binding, unwinding, and resection by the
            Mre11/Rad50 complex
  JOURNAL   EMBO J 35 (7), 743-758 (2016)
   PUBMED   26717941
REFERENCE   2  (residues 1 to 921)
  AUTHORS   Chen,Z., Luong,T.T. and Lee,C.Y.
  TITLE     The sbcDC locus mediates repression of type 5 capsule production as
            part of the SOS response in Staphylococcus aureus
  JOURNAL   J Bacteriol 189 (20), 7343-7350 (2007)
   PUBMED   17704228
REFERENCE   3  (residues 1 to 921)
  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   4  (residues 1 to 921)
  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
REFERENCE   5  (residues 1 to 921)
  AUTHORS   Hopfner,K.P., Karcher,A., Craig,L., Woo,T.T., Carney,J.P. and
            Tainer,J.A.
  TITLE     Structural biochemistry and interaction architecture of the DNA
            double-strand break repair Mre11 nuclease and Rad50-ATPase
  JOURNAL   Cell 105 (4), 473-485 (2001)
   PUBMED   11371344
REFERENCE   6  (residues 1 to 921)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..921
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..921
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=110714
     Region          1..919
                     /region_name="PRK03918"
                     /note="DNA double-strand break repair ATPase Rad50"
                     /db_xref="CDD:235175"
ORIGIN      
        1 mqikkvvlnn yrshshievv fskginlilg kngrgktsil eaiglalfhm tdrtgktkgk
       61 tfmkygekec sifieflgnd greysifhhy flkkpkvsil kdmqteeeyr dnieekleel
      121 cgvkaeyrdi yenvivakqn dfinifketp enrarvfnki fnteiynklf idlkgfveqy
      181 lkekemleve entlrltlen keermemlqq teekwklyal kkearleekq kiakkieqye
      241 fikrefetik skfsfqeqki rqnkkelqer lvlakkakka rflleehqes yqlymeldkk
      301 iqekkqeknf lqkrreenqk leeenrklel liknnqteee vlqermteqq vllldletri
      361 eedqkqqkel qtslarlqsf wkeieislek qkkweqenfn lqqkqslqek nhkqkteell
      421 klniveiqsf lqeiqedkae iqgkkeriav yqqniedyqf amhtlgqkic pflketcenm
      481 kghevdsyfq geiqktkklm etlqheikal eeklkkefvy rkeeasyqll qkevqelekd
      541 ilqteilwke illererqqy sfqtllsqhn fasleelqek lrnledalll lkieekeeew
      601 kslqkkqeil qerveklqkd rmsslerqkq nilniqedle eiwleflkem esletkmlsl
      661 qtsyriylen rkiadnleee kgkirvllle rdnlrisqre vnekyrllek dleqreqenw
      721 kdklmevere llavnetlge lgeklkndkq vlekivlqee kiaglskkrn kierkykkae
      781 slrknikemg tqvsknmlhy isegasinfh kitgrseriy wsneekdkyq vyllgenrki
      841 eyqllsggeq vsvaiairgt maqyfsnskf mildeptnnl diekrkllae yigeilnhle
      901 qsiivthdds fremaekiie l
//
LOCUS       WP_008801200             254 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Fusobacterium
            gonidiaformans].
ACCESSION   WP_008801200
VERSION     WP_008801200.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..254
                     /product="formate/nitrite transporter family protein"
                     /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=27044
     Region          8..244
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mydevigklt eaakkkvnll nsstfkylvs safagafigi gilliftigg ymggepsvkv
       61 vmglsfsval slvifsgtdl ftgnnlvmtv gvlnkgvkts dlikvwivsy ignllgaill
      121 sflfvnsglv dkgpvmeffq kmalakaspd aislifrgil cnimvclavf lsfkvqdett
      181 kiiliimclf vfitvgfehs ianmtvyavg vfsrsmtevt lgqaiynlat vtlgniigga
      241 ffigcgvfsl rsks
//
LOCUS       WP_008801676             384 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Fusobacterium
            gonidiaformans].
ACCESSION   WP_008801676
VERSION     WP_008801676.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 384)
  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 384)
  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
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 384)
  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   5  (residues 1 to 384)
  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   6  (residues 1 to 384)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 384)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 384)
  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 20283047
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..384
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43513
     Region          8..>67
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          73..384
                     /region_name="ASKHA_ATPase_ROK_YphH-like"
                     /note="ATPase-like domain of Escherichia coli protein YphH
                     and similar proteins; cd24072"
                     /db_xref="CDD:466922"
ORIGIN      
        1 mrkekeeril ecireqekis rislakllqw npttvgsiva ellkksyiqe vemeastggr
       61 katllslked mspsilgisf apsflqigig siqgkifete kivltpliie kiwqflfqii
      121 dkklnkwkei rqisviisgl vnsekgvsif sphyqwrnie ikkileeryq kkvfvendvr
      181 amalleksfg sckkkrnfvv lnigdgvgss ifidnklyig sysgsgelgh mqvnakglrr
      241 cscgkigcle sevsnlsild kissqiklgq ysilrqklkr dgnlsiedfl falgekdlla
      301 lqiaeesvem itraldaiis llnpervily gsifqseyly reilkkiqsi liseqgykis
      361 lsnfykeaya yapfavlryl sikn
//
LOCUS       WP_008803455             585 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Fusobacterium
            vincentii].
ACCESSION   WP_008803455
VERSION     WP_008803455.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium vincentii
  ORGANISM  Fusobacterium vincentii
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Fusobacterium vincentii"
                     /db_xref="taxon:155615"
     Protein         1..585
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=66810
     Region          2..556
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 midkrlynfs gnikkyisit tflscvklia niffyfifaf llvslinrdf sfsysyiiis
       61 iliivfvrqf stikvahmlg nlvvdvkrnl rklifektlk lglaysqlfk tqelihlsvd
      121 nveqlevyfg gfltqfyyci vssfilffsi ayfnlkiafi llgfslaipl slyiilnkik
      181 kiqkkyfaky mnvgtlflds lqglttlkiy gtdekreeei akmseefrie tmrvlkmqll
      241 siaainwiiy agtilaivts vklflngslg lfpmlfifml apeffipmrt ltslfhvamt
      301 gvsaaeniis fvdspernnn gnkefknene ikvsklnfsy pdgtqslkdi dmsfkkgnlt
      361 avvghsgcgk stlvsvlsge lkskeneifv ddidiqniki edkiknilki thdshifsgt
      421 vrenltmane nlsdetmiev lkkvklwdif lknkgldtsl esqgknlsgg qvqrvalara
      481 llydasvyif deatsnidie seeiilsiiy slskektviy inhrlpaikn adciyvmdkg
      541 kiiesgehik lyakkglyye myrhqeelet yltkrgenne ksvnf
//
LOCUS       WP_008803884             723 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Klebsiella].
ACCESSION   WP_008803884
VERSION     WP_008803884.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 723)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 723)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 723)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..723
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..723
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=81874
     Region          160..723
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mldkininik ktllaflvsl vaiplarfis pqtvidgnli yiawlpisvm fsvififgry
       61 aiaplilafa itnsflielt lsqalillfc qlfavfvsca vlrlmvgkrw rcgptakhmg
      121 arifwggffa pvllkitmyl agqyfafpls itsyfgsmpl iytvidiqsl isaalifttf
      181 lyypmrmiis phyarrfwrq eclpwlapkh rsftlywfis lalllillca pyqsefiagy
      241 lvpvifivyf igisrighal lriswsvsaf llvvynknfl qgvqseysls fvlsvlisft
      301 iclfymadty arsdrnkrrw rsqaeedplt glpnlralvs hlqssplqai cslridnldf
      361 lsrhyglmmg vdckrqiira lqpllgatdk vfqvpgseli lvldgpdpaa rlnhmvailn
      421 hkkfswhnqp ldlefgaaws rddgqgetlh qmlgqlswls eqagserril aldeeqelvv
      481 dqtteqvrll mrvkqvlker alvlyaqpiq naegegyhei ltrmrcgdgv impdqfipli
      541 vqfnlsqrfd mlvletlfss lhqhpgqrfs vnllpstlmq kdsaaqiial fqryrispdl
      601 itievteeqa fsnadtsqqn ldalrafgca iaiddfgtgy anyerlkhlq adiikidgcf
      661 vrdiltdpld aimvksivem arakqmsvva eyvesepqka rllelgvnyl qgylvgkpqp
      721 lge
//
LOCUS       WP_008804050             315 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Klebsiella].
ACCESSION   WP_008804050
VERSION     WP_008804050.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..315
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=34747
     Region          1..309
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 miefegvskv faghpavkdl tlelregafs vlvgtsgsgk sttlkminrl lepdrgtirf
       61 agedirqqpv ltlrrrmgya iqsiglfphw tvaqniatvp qlqkwprari adrvdelmal
      121 lgleatlrdr yphqlsggqq qrvgvarala adpevllmde pfgaldpvtr ealqqemlri
      181 hrllgrtivl vthdidealr ladhlvlmdg gevvqqgapl emllrpknsf vqtffgrsel
      241 gvrllslrev gdylrpgerl agegltvtmt lrealsqfva rrcealpvvd aegrpcgtlh
      301 fadllrqeas hegas
//
LOCUS       WP_008808067              79 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyl carrier protein [Streptococcus].
ACCESSION   WP_008808067
VERSION     WP_008808067.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus
  ORGANISM  Streptococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae.
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]
REFERENCE   4  (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 10011594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Streptococcus"
                     /db_xref="taxon:1301"
     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=8919
     Region          3..79
                     /region_name="acpP"
                     /note="acyl carrier protein; Provisional; PRK00982"
                     /db_xref="CDD:179197"
ORIGIN      
        1 mtqetiyqki vsiiqerqgk sfevtpelsf kdnlgadsvd mmefiltled efgidilded
       61 idrlcsvadv vayiekktk
//
LOCUS       WP_008808669             265 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Streptococcus].
ACCESSION   WP_008808669
VERSION     WP_008808669.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus
  ORGANISM  Streptococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptococcus"
                     /db_xref="taxon:1301"
     Protein         1..265
                     /product="formate/nitrite transporter family protein"
                     /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=28832
     Region          2..261
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 maessfitkv afacqkkeal fdsskakyav rsmyagaflt lstaagaiaa dvinkivpgs
       61 grllfpfifa wglvyilfln aelttsnmmy ltagtflkki kfskallill yctffnlvga
      121 aiigwifnqt vayagltlda fvgtvvankl srgnsvvlfe aiaanifvnv ailsflliks
      181 stakmwivis aiymfvfltn ehlaanfasf sliafnkivs qvqgfdvfnv lrhfsitfig
      241 nvigggllig lpyawmnkde etyvd
//
LOCUS       WP_008812504             206 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Hafnia].
ACCESSION   WP_008812504
VERSION     WP_008812504.1
KEYWORDS    RefSeq.
SOURCE      Hafnia
  ORGANISM  Hafnia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Hafniaceae.
REFERENCE   1  (residues 1 to 206)
  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 206)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 206)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Hafnia"
                     /db_xref="taxon:568"
     Protein         1..206
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22439
     Region          1..204
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 mevysteneq vdalrrffie ngkalaigvv igigallgwr ywqnhqqaem tgasqsyqqa
       61 sealtggkad gvalaekfie knannygvla alqlaqhevd qkdfakaehq lawaqgqakd
      121 enlkslidlr larvqlqenk lddalktldl vkatgwvama qdvrgdvlvk kgdvkgarea
      181 yskglasdas qslqallrmk lnnlsn
//
LOCUS       WP_008813591             163 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Hafnia].
ACCESSION   WP_008813591
VERSION     WP_008813591.1
KEYWORDS    RefSeq.
SOURCE      Hafnia
  ORGANISM  Hafnia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Hafniaceae.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Hafnia"
                     /db_xref="taxon:568"
     Protein         1..163
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17573
     Region          1..152
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mskkefyadl trdlaalsrg eynfiatlsn asaliyerle nvnwagfyli dgntlvlapf
       61 qgklacvrip vgkgvcgtay aknevqrvad vhafaghiac daasnaeivl plevngqvig
      121 vldidstvyd rfdeddetgl ksvvyalceh laecdsakfv tfa
//
LOCUS       WP_008815157             142 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Hafnia].
ACCESSION   WP_008815157
VERSION     WP_008815157.1
KEYWORDS    RefSeq.
SOURCE      Hafnia
  ORGANISM  Hafnia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Hafniaceae.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Hafnia"
                     /db_xref="taxon:568"
     Protein         1..142
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15456
     Region          7..140
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mnsfltlgam fassftsatl lpgnseivlt afllagqvsp wwlvltaivg nilggltnvi
       61 igrllpdvkp qrgvqlslrw lqrygavtll lswvpiigdl lcvlagwlrm pwvpvafyls
      121 igkavryval awltlqgmsw ws
//
LOCUS       WP_008819375             168 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Bacillota].
ACCESSION   WP_008819375
VERSION     WP_008819375.1
KEYWORDS    RefSeq.
SOURCE      Bacillota (firmicutes)
  ORGANISM  Bacillota
            Bacteria; Bacillati.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Bacillota"
                     /db_xref="taxon:1239"
     Protein         1..168
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18929
     Region          3..162
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 melqeaitar yscrsftera idsallktcv etaglapsac nsqpwkfhii qdpamvaltq
       61 pftkhaafiv veeqkpvvse rivnrmknqe fhqvdigiac aylclqaael gldtcmigyf
      121 hekkikellq ipdkkrirlv iavgygsqqr rktdrktlqd iltihesl
//
LOCUS       WP_008817125             397 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Bacillota].
ACCESSION   WP_008817125
VERSION     WP_008817125.1
KEYWORDS    RefSeq.
SOURCE      Bacillota (firmicutes)
  ORGANISM  Bacillota
            Bacteria; Bacillati.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Bacillota"
                     /db_xref="taxon:1239"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43131
     Region          2..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mskiisvnag ssslkfqlfe mpseevltsg ivekigfeda iftikvngek ikkvlpipdh
       61 tkavsmllea lveykivnsl deitgaghra vhggeifkes vpvtedvvek faslndlapl
      121 hnpaglvgyn afknnlpnck hvfvfdtafh stmpkesyiy alpmkyydey kirrygfhgt
      181 shkyvslrca elmnkkvedt kiitchlgng asitavdggk sintsmgftp lagvmmgtrc
      241 gdidpaivty imkktgatpd emddimnmqs gmlgvsgiss dardiedgck egnpaallta
      301 evyvnrvinv vggyyaqlgg adaivftggi gendtnmrkm icdrlsvafg iqldeelngk
      361 trgkevllst aeskvavwli ptneelmiar dtyrlia
//
LOCUS       WP_008820532             258 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Fusobacterium].
ACCESSION   WP_008820532
VERSION     WP_008820532.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..258
                     /product="formate/nitrite transporter family protein"
                     /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=27538
     Region          6..258
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 madghktpte lvdyiikvgi dkatkplfkl mllgifggaf ialggagnii ssstlvktdp
       61 gfakflgaav fpvglilvvt lgaelftsnc llsvafvnkk isftqmirnl vtvylfnyvg
      121 sfivayitvk ggsfnadsla ylqniathkv dasayalfik gilcnvlvcg aviqsytsrd
      181 tigklvgawl pimlfvligy dhsianmfyl taakladtsl fgvsgilynl fyvtlgnilg
      241 alaiglplyf syykksdn
//
LOCUS       WP_008820634             581 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Fusobacterium
            periodonticum].
ACCESSION   WP_008820634
VERSION     WP_008820634.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium periodonticum
  ORGANISM  Fusobacterium periodonticum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Fusobacterium periodonticum"
                     /db_xref="taxon:860"
     Protein         1..581
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=66154
     Region          2..555
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 midkrlynfs gnikkyisit tflscvklia niffyfifaf llvslinkdf sfsykyiiis
       61 iliivlvrqf stikvahmlg slvvdvkrnl rklifektlk lglaysqlfk tqelihlsvd
      121 nveqlevyfg gfltqffyci vssfilffsi ayfnlkiafi lllfslaipm slyiilnkvk
      181 kiqkkyfaky mnvgtlflds lqglttlkiy gtdekreeei akmseefrve tmrvlkmqll
      241 siavinwiiy agtilaiits iklfidgsla lfpmlfifml apeffipmrs ltslfhvamt
      301 gvsaaeniis fidspeknsi gdkefknere fkvsnlsfty pdgtqslkgi nmtfkkanlt
      361 avvghsgcgk stlvsvlage lksneneifv ddtdihninl edkvknilki thdshifsgt
      421 vrdnlsmane nlsdetmvev lktvklwdif skakgldtvl esqgknlsgg qaqrvalara
      481 llydasvyif deatsnidie seeiilniih slskektviy ishrlpaikn adciyvmdkg
      541 rviesgkhnd lyakkelyyn mykhqeelet yltkrgetne k
//
LOCUS       WP_008821777             299 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Fusobacterium periodonticum].
ACCESSION   WP_008821777
VERSION     WP_008821777.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium periodonticum
  ORGANISM  Fusobacterium periodonticum
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Fusobacterium periodonticum"
                     /db_xref="taxon:860"
     Protein         1..299
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=34162
     Region          45..211
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkkilallsl lifmvacsss dtpvketkgi stprrtssss ligsmgkfkv dsdtyvslgr
       61 neriqfvvvh ytatnneysi kelisnrvsa hflvldeddn iiynlvpldq rawhagassf
      121 rgrtnlndts igieivsdgi ardrrndpnr yppydayley kpiqiekvaq iikyvaaryn
      181 ipaknivahs diapsrkkdp gakfpwkely ekydigawyn esdkqafmne ekfnatsisd
      241 ikeelrkygy evnrtnewdr dsrdvvyafq lhfnqknatg nmdletyail kalnkkypn
//
LOCUS       WP_008827167             342 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Haloplasma
            contractile].
ACCESSION   WP_008827167
VERSION     WP_008827167.1
KEYWORDS    RefSeq.
SOURCE      Haloplasma contractile
  ORGANISM  Haloplasma contractile
            Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Haloplasmatales;
            Haloplasmataceae; Haloplasma.
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
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Haloplasma contractile"
                     /db_xref="taxon:471825"
     Protein         1..342
                     /product="aminoglycoside 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=40401
     Region          <94..265
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mcthlfkvep kyvltkehee dvlnqiitia neeesmhitn yeriitgqni iykliskktn
       61 csyqlkiiar kgypcietln acyeylemin inkpkiiyyd tkdyivpygy iiqswiegev
      121 yshkdkddte wivdfashlr dvhkiklngf gylgkgpvyp tlkeyfynmd qivdhsfgei
      181 fkdyysiwdl qkyelisdgf lettfanvky lanqikidpe pillhgdmlp nnliqtengt
      241 alidwdesks gwwvyeiart lfyidnkkeh lksflkaynd tqtplldiyn girlehirql
      301 lrklfmsaft fnttnlaeir lriryielki nelldsplld ei
//
LOCUS       WP_008827240              85 aa            linear   BCT 20-JAN-2025
DEFINITION  zinc ribbon domain-containing protein [Haloplasma contractile].
ACCESSION   WP_008827240
VERSION     WP_008827240.1
KEYWORDS    RefSeq.
SOURCE      Haloplasma contractile
  ORGANISM  Haloplasma contractile
            Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Haloplasmatales;
            Haloplasmataceae; Haloplasma.
REFERENCE   1  (residues 1 to 85)
  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 10577258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Haloplasma contractile"
                     /db_xref="taxon:471825"
     Protein         1..85
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=9671
     Region          6..84
                     /region_name="Zn_ribbon_2"
                     /note="Putative zinc ribbon domain; pfam12674"
                     /db_xref="CDD:463667"
ORIGIN      
        1 mdskpcqscg mtidhkklyg tnkngtinte yckycysnge fnkpdetfse mvescipfev
       61 eaegytedea rivlteklkp lkrws
//
LOCUS       WP_008827816             223 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Sphingomonadaceae].
ACCESSION   WP_008827816
VERSION     WP_008827816.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonadaceae (alpha-4 proteobacteria)
  ORGANISM  Sphingomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales.
REFERENCE   1  (residues 1 to 223)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Sphingomonadaceae"
                     /db_xref="taxon:41297"
     Protein         1..223
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=23682
     Region          54..220
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mmlagaavav ascsrssspl rstsplaapv lpksagpasv pamvrndgpr aafstvdptl
       61 lrkalasldr hgerirqrdr iaivdfsaps sdarmhfldv edgkairllv ahgsgsdphh
      121 tgylerfsna fgsnassega yltddyyvgk hgrsqrligl datnnnaler avvvhsawya
      181 nddmikahgk lgrsqgcfav genklddvfs flgkgrmifa ars
//
LOCUS       WP_008827345             368 aa            linear   BCT 20-JAN-2025
DEFINITION  GerAB/ArcD/ProY family transporter [Haloplasma contractile].
ACCESSION   WP_008827345
VERSION     WP_008827345.1
KEYWORDS    RefSeq.
SOURCE      Haloplasma contractile
  ORGANISM  Haloplasma contractile
            Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Haloplasmatales;
            Haloplasmataceae; Haloplasma.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Haloplasma contractile"
                     /db_xref="taxon:471825"
     Protein         1..368
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=42093
     Region          4..367
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 mikksngkig trelsalifi viaikgadst phglfidglt atwmfpiiwl ivmalpfmal
       61 lkllqhykrk nivqiiyhlt gkyfgfllal ilfflqfmal ilnsrgyvdi mvsrfyiltp
      121 mlviysalil ssyfvatrgy eglartsyli lpyliiamll lppllwadfs plflhpvagp
      181 gvkeiitggv khssligeym ifalfypytk dhktfrnani igfvfgcili slllaeyiml
      241 fdyvavqkml hpfsqltrht eimmfinnld alflgvwiiv giirfalyly gtagfygytf
      301 klkefeplil pfailtiiig fipynasmts ivlrqnylie kswlyffflp lllwgiakvk
      361 gefkhert
//
LOCUS       WP_008831207             212 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Sphingomonas sp. LH128].
ACCESSION   WP_008831207
VERSION     WP_008831207.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. LH128
  ORGANISM  Sphingomonas sp. LH128
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Sphingomonas sp. LH128"
                     /db_xref="taxon:473781"
     Protein         1..212
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22374
     Region          1..163
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlrglyewtm akashrhagw wlaafafmea sffpvpphpl lglmclaepk kairfaaiat
       61 iasvaggllg yaighfayaa fgeallralh lsesfpkaac ylrdygaeii ivkgatpipf
      121 klltitagfi gmnllvfvga siisrsisfm ivgvlfrlfg apikavidkh lgkvtvgfvv
      181 liiagflavs flgggskqtt ekcasavaak tv
//
LOCUS       WP_008831636             356 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Sphingomonas sp.
            LH128].
ACCESSION   WP_008831636
VERSION     WP_008831636.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. LH128
  ORGANISM  Sphingomonas sp. LH128
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
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
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Sphingomonas sp. LH128"
                     /db_xref="taxon:473781"
     Protein         1..356
                     /product="aminoglycoside 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=38919
     Region          97..286
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 msqvlerprp aqpqvtvpat leqaldpqwl agalgkiaag raiaqveqve virnvatkvr
       61 favtfedger lgfclkglld vdamtarggp tcvlesdfyn kvapviavrv pdcvatvidr
      121 eaqqavtimr dlivdgarfc saldpftadd aleslkqlal lharsdfldg adwirpraad
      181 lakmsyvtpe alqdlldgpr gdnlsprvrs aanlaaaire laardggrpq fmihgdahag
      241 nvfrtpegmg vidwqllqrg gwaldvayhl navlptevae veerrllgey lsmmrghgmd
      301 mpseadawmq yregvtygyy lwsitrrvdp piivqfvdrl gkavmrhdsf gllgaa
//
LOCUS       WP_008833897             199 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Allomesorhizobium
            alhagi].
ACCESSION   WP_008833897
VERSION     WP_008833897.1
KEYWORDS    RefSeq.
SOURCE      Allomesorhizobium alhagi
  ORGANISM  Allomesorhizobium alhagi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Allomesorhizobium.
REFERENCE   1  (residues 1 to 199)
  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 199)
  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   3  (residues 1 to 199)
  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   4  (residues 1 to 199)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 199)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 199)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Allomesorhizobium alhagi"
                     /db_xref="taxon:475067"
     Protein         1..199
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21590
     Region          12..196
                     /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"
ORIGIN      
        1 mtagrpipsf egwralvvhr phanvdatll qferlgisaa hcwpemagdt glsqwnvlvi
       61 dadmgydgqf pwqpgaapmp iialigseap grvswamnqg adahllkpig saglysalvi
      121 arhsfaqrta lageiaslrm rlqsrealae atallmvrdn issraafqkl rmqamserra
      181 ieliaeelia avdlerkqr
//
LOCUS       WP_008834281             188 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Allomesorhizobium alhagi].
ACCESSION   WP_008834281
VERSION     WP_008834281.1
KEYWORDS    RefSeq.
SOURCE      Allomesorhizobium alhagi
  ORGANISM  Allomesorhizobium alhagi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Allomesorhizobium.
REFERENCE   1  (residues 1 to 188)
  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 188)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 188)
  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   4  (residues 1 to 188)
  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   5  (residues 1 to 188)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Allomesorhizobium alhagi"
                     /db_xref="taxon:475067"
     Protein         1..188
                     /product="TRAP transporter small permease subunit"
                     /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=20286
     Region          5..166
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mvqfyiravg glsrafavva tllliaamlv vcqmifiryv fraatiwqtd fvvfaatgam
       61 flgapyvllk gghvgvdvve mvvadrtrha mrivasllgl lfcaimlyas wlqfhetwvg
      121 gwrhasvwap plwiplsalp lgfcmlclqy vaqilvlvsg vatpapthvp aealeaaaav
      181 spsretar
//
LOCUS       WP_008834987             154 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Allomesorhizobium alhagi].
ACCESSION   WP_008834987
VERSION     WP_008834987.1
KEYWORDS    RefSeq.
SOURCE      Allomesorhizobium alhagi
  ORGANISM  Allomesorhizobium alhagi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Allomesorhizobium.
REFERENCE   1  (residues 1 to 154)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Allomesorhizobium alhagi"
                     /db_xref="taxon:475067"
     Protein         1..154
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=16538
     Region          42..153
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(105..106,109,122..125,127)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mnatlsakli nviaaalagi alfleagtgs ahaagsqiva risiseqrmd vlidgrptfa
       61 wkvstagkgy rtptgsfkpt rmhkmwysrk ydnapmphsi ffhggyavha tphikrlgrp
      121 ashgcirlhp dnaadlyqlv qtfgpsntsi vivk
//
LOCUS       WP_008834953             390 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Allomesorhizobium alhagi].
ACCESSION   WP_008834953
VERSION     WP_008834953.1
KEYWORDS    RefSeq.
SOURCE      Allomesorhizobium alhagi
  ORGANISM  Allomesorhizobium alhagi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Allomesorhizobium.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Allomesorhizobium alhagi"
                     /db_xref="taxon:475067"
     Protein         1..390
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=39689
     Region          48..130
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
     Region          288..367
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mirnllatta iatllstaay aqdatapapa apdpavqapa eapiaradgh latnligetv
       61 yngtgddaen igkvndivig sngevesvvi gvggflglgq knvavnyaev dwaerdgdrw
      121 lvvaatkeql eaqadfdrra yepapattag tepppatdqt atapapaapt ddqtatapae
      181 papaddqtat apaepapadd qtatapaepa paddqtatap aepapaddqt atapaepapa
      241 ddqtatapap aapaddqtaa apadpaaptd qtttaavdks altempanem raenligttv
      301 ygandemige igdvvlegen vdsiivdvgg flgvgekeva vamdnlsfmt dadgnrylyt
      361 gftkeqldaq paydeatfaq nrddqrmmnq
//
LOCUS       WP_008835931             338 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein, partial
            [Allomesorhizobium alhagi].
ACCESSION   WP_008835931
VERSION     WP_008835931.1
KEYWORDS    RefSeq.
SOURCE      Allomesorhizobium alhagi
  ORGANISM  Allomesorhizobium alhagi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Allomesorhizobium.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Allomesorhizobium alhagi"
                     /db_xref="taxon:475067"
     Protein         1..>338
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
     Region          14..>68
                     /region_name="NuoF"
                     /note="NADH:ubiquinone oxidoreductase, NADH-binding 51 kD
                     subunit (chain F) [Energy production and conversion];
                     COG1894"
                     /db_xref="CDD:441498"
     Region          <66..>338
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mqnaglrglg gagfpagkkw gfvrsypapr lmsingepgt fkdhiylerd phrtfegali
       61 aahaveadci ivigarpttn hpvaatffkq aakrgakliv idprgqdlmr hashslrfka
      121 gsdvamlnal ihviieekly deqyiqanas gfealkakvk dfspeamaei cgieasvlrd
      181 vartyataer siifwgmgis qhthgtdnar clialalitg hvgrpgnglh plrgpnnvqg
      241 asdaglipmy fpdyksveni dirgqyenfw gqtldpkrgl tvveiidaih dgeikgmyim
      301 genpamsdpd qtharqalam ldhlvvqdif ltetawha
//
LOCUS       WP_008836578             355 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Allomesorhizobium alhagi].
ACCESSION   WP_008836578
VERSION     WP_008836578.1
KEYWORDS    RefSeq.
SOURCE      Allomesorhizobium alhagi
  ORGANISM  Allomesorhizobium alhagi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Allomesorhizobium.
REFERENCE   1  (residues 1 to 355)
  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 355)
  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   3  (residues 1 to 355)
  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   4  (residues 1 to 355)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 355)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 355)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 355)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Allomesorhizobium alhagi"
                     /db_xref="taxon:475067"
     Protein         1..355
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36940
     Region          26..344
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(88..90,111..112,164,216,240)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mrlgtsclag iaglllaaqa qaqesrlgis aplsgpsail gaqvlegast aanaaeleva
       61 ddactaegga gaarqfveak vrvvlgflct eaieaalpil klagipvitv gvrtdsltds
      121 rektgwpvfr lgpragdena aaaaiipklw rdelfaitdd gtiygrelae svraaaeqaa
      181 lkpvftdnfr pqmdnqvgli grlrragath vfvggdrddi aimtrdaavt gggmifagge
      241 alraapgevp laegtlmigl pewseiagkd alaalrerqt apdgyvlpaf aaveiaraal
      301 edadaagkpl ldilaeqefk taigpirfda kgdladnpyr afrydgerfv pmesy
//
LOCUS       WP_008838068             121 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Allomesorhizobium alhagi].
ACCESSION   WP_008838068
VERSION     WP_008838068.1
KEYWORDS    RefSeq.
SOURCE      Allomesorhizobium alhagi
  ORGANISM  Allomesorhizobium alhagi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Allomesorhizobium.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Allomesorhizobium alhagi"
                     /db_xref="taxon:475067"
     Protein         1..121
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=13033
     Region          9..87
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mttpsghtda iaasrvigta vyntagenig tiedvmldkm sngimfavig fggflgigek
       61 yhaipwsvld yeesrggyvv pftreqleaa psysidelsg sdgkaardas fdyykvdpyw
      121 y
//
LOCUS       WP_008839224             371 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Allomesorhizobium
            alhagi].
ACCESSION   WP_008839224
VERSION     WP_008839224.1
KEYWORDS    RefSeq.
SOURCE      Allomesorhizobium alhagi
  ORGANISM  Allomesorhizobium alhagi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Allomesorhizobium.
REFERENCE   1  (residues 1 to 371)
  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 371)
  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 371)
  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 371)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Allomesorhizobium alhagi"
                     /db_xref="taxon:475067"
     Protein         1..371
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40702
     Region          7..366
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 madkgisrrr flgttavgat aagtlaapav laqapvtlkm qsswpasdif qemaaqyvqr
       61 vqemsnnrlk idllpagavv gafqvqdach dgtidaahtv pvywygknka aslfgtgpvf
      121 ggdanqmiaw lyhgggnefy reltqdilgl nivgflsfgm paqplgwfks eitdaaqlqg
      181 lkyrtvglaa dlfqsmgasv aqlpggeivp amergvidgf efnnptsdmr fgaqdvakny
      241 mlasyhqase sfeyifnrdt fesldpdlqa ilkygvesah lanyalamqq ysadlqklqt
      301 esgvnvkrtp dsvlqaqlea wdkilpplme dpyfkkvvds qkawcervvy ysllnapdyk
      361 layqhyfpdk i
//
LOCUS       WP_008839226             409 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Allomesorhizobium alhagi].
ACCESSION   WP_008839226
VERSION     WP_008839226.1
KEYWORDS    RefSeq.
SOURCE      Allomesorhizobium alhagi
  ORGANISM  Allomesorhizobium alhagi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Allomesorhizobium.
REFERENCE   1  (residues 1 to 409)
  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 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   3  (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   4  (residues 1 to 409)
  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 409)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Allomesorhizobium alhagi"
                     /db_xref="taxon:475067"
     Protein         1..409
                     /product="CmpA/NrtA family 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=42785
     Region          8..265
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mtgnaehqit agfmplldsa llvaakeigf aagegvaltl vretswanir drlavghfgv
       61 aqmlapmpia cnlgltplas rtiapmalgl ggnaitvsna vwaameahga rpdldpkgag
      121 aaleavvaer agrggeplrf avvhphsghn yelrywlaac gvaeggieiv ivppplmada
      181 lragnidgyc vgepwntaaa lsgsgriatv kaaiwrsspe kvlgagakwa eanpealaal
      241 lralyraaiw cadkanhael asllsspayl gkpeewmlpa lsgrirtggd gerlvedffi
      301 plakaatfpw kshalwfytq mvrwgqirhs paheaiards yrpdiyrsal kplgvplpga
      361 nskvegalta ttpvgsagas ltlgpdgffd ggifdpdeid ayvaaqrqg
//
LOCUS       WP_008840438             254 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Allomesorhizobium alhagi].
ACCESSION   WP_008840438
VERSION     WP_008840438.1
KEYWORDS    RefSeq.
SOURCE      Allomesorhizobium alhagi
  ORGANISM  Allomesorhizobium alhagi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Allomesorhizobium.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Allomesorhizobium alhagi"
                     /db_xref="taxon:475067"
     Protein         1..254
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=28147
     Region          139..214
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mdcrtfvatl silvalgige aaaqcnisda kleeailqkp elrdrenrqm vrdlralrda
       61 afilwsygrh ddcerilgni relvaspsmg qlgandedea dqqlaagepm vreggqvlgn
      121 rgaegalpli dinelgpglr adeilgaevr ssddkiigev rnvvigtkdr wdyavvasgg
      181 fftpgkdsiv vplrylrvnq erssfflrip esemrtvplm pdqdyewlsd eawrarndai
      241 frslmpvser fgve
//
LOCUS       WP_008841692             385 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Pediococcus acidilactici].
ACCESSION   WP_008841692
VERSION     WP_008841692.1
KEYWORDS    RefSeq.
SOURCE      Pediococcus acidilactici
  ORGANISM  Pediococcus acidilactici
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Pediococcus; Pediococcus acidilactici group.
REFERENCE   1  (residues 1 to 385)
  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 385)
  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
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 385)
  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   5  (residues 1 to 385)
  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   6  (residues 1 to 385)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 385)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 385)
  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 20650276
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Pediococcus acidilactici"
                     /db_xref="taxon:1254"
     Protein         1..385
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43025
     Region          10..62
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          81..372
                     /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 mvihketmrt anersvlqri ftespisksq iardvklnkv tvsqivnrfi esglvveaga
       61 gdstqqggrk pnllqinary gyvvcidlgy helsalamti sgrkleirht tftdndiana
      121 iskikeliae lkseygeknl gilisvhgiv yqnqviyspf wnmhdvdiaa vltkslgitv
      181 lleneanlta iferdfsseg irnavsismh kgigagiimd gelyrgrkge ageigqtiaf
      241 etkdkslaen qkiedvasqe avldqikqak nldyinlpli rqmyddhdpe tleilqrfen
      301 niiklinnvi vsfdpdvlfi nayifkefpe lleriqtkfa kisvrdtpiv lsknvetasl
      361 yggcaqmiqe ilgfsklkld fkske
//
LOCUS       WP_008841713             286 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Pediococcus acidilactici].
ACCESSION   WP_008841713
VERSION     WP_008841713.1
KEYWORDS    RefSeq.
SOURCE      Pediococcus acidilactici
  ORGANISM  Pediococcus acidilactici
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Pediococcus; Pediococcus acidilactici group.
REFERENCE   1  (residues 1 to 286)
  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 286)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Pediococcus acidilactici"
                     /db_xref="taxon:1254"
     Protein         1..286
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=31292
     Region          1..281
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mlvsmkdils aanrgkyavl aincfnlesa catvkaaekr rspiiidllq ehmekhiake
       61 illpsvvkma klatvdvain ldhgksvdyv kecivdgftg vmidqsernf kdnvritkei
      121 mdcalpknig veaevgnmga vkndqftkqe mytdpkeaik firrtnvtal aisfgsshgv
      181 mpkdfipkfn fdivkeikka tgiplvmhgg sgcgkdniak avsvginkvn vgsdilkaqs
      241 eavyvqqedr ymdyvdllqi tmteaekavd eyidvvgstn ktsvtl
//
LOCUS       WP_008842071             410 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Pediococcus acidilactici].
ACCESSION   WP_008842071
VERSION     WP_008842071.1
KEYWORDS    RefSeq.
SOURCE      Pediococcus acidilactici
  ORGANISM  Pediococcus acidilactici
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Pediococcus; Pediococcus acidilactici group.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Pediococcus acidilactici"
                     /db_xref="taxon:1254"
     Protein         1..410
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=45965
     Region          2..409
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mntdiergvi gsllnhpekv gavalneewf gyedyrliyk aikettghdi ldvygkynql
       61 tkkamdfrtf kqivdeapav sqlnndislm rklaykrels saikdyqanp fseneekire
      121 ilaknqtlea tddgkldeaa aeladalthp kprgiktftq ldkslgggly gsmlltigar
      181 pstgktafsv nlayqamknd kevevdfftl emnkqemlnr fvsrmtgvss stlrsnadkl
      241 ngilkklvnq stsqllaskl rvydgletlg eivqtirkna srakqgkyma iidyiglvkv
      301 pnvkeryiev gevtrelkrl tnefnipiva lsqlsrgien rndktpvlsd lresgsieqd
      361 snvvaflhrp esvnddhvvq lsirknrege ladinftfig eemtfkevai
//
LOCUS       WP_008842446             269 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Pediococcus acidilactici].
ACCESSION   WP_008842446
VERSION     WP_008842446.1
KEYWORDS    RefSeq.
SOURCE      Pediococcus acidilactici
  ORGANISM  Pediococcus acidilactici
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Pediococcus; Pediococcus acidilactici group.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 269)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Pediococcus acidilactici"
                     /db_xref="taxon:1254"
     Protein         1..269
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=31519
     Region          <47..260
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mtlnqledfl fwlailmavl tvviigvyfw ktryrggnyl rdphiplryf iqkqvdrhgq
       61 itgyecllrt qdaagqwtlp qdfnslplrr vidlledtfv slptepvtls ikltyqqiis
      121 rdfeyfirwa itkiepmnla veisikamek rvnrrllrqq iqmgrnygmq fsvnnvgsel
      181 ndlksiewll peidilkasm rsfrkedphe wldlnlqfwn rlarknhikl vlvgienatd
      241 qalaeqlqid arqgylfgkp edvhrgaek
//
LOCUS       WP_008842833             288 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Aliiglaciecola
            lipolytica].
ACCESSION   WP_008842833
VERSION     WP_008842833.1
KEYWORDS    RefSeq.
SOURCE      Aliiglaciecola lipolytica
  ORGANISM  Aliiglaciecola lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Aliiglaciecola.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Aliiglaciecola lipolytica"
                     /db_xref="taxon:477689"
     Protein         1..288
                     /product="formate/nitrite transporter family protein"
                     /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=30890
     Region          2..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mayllpaefa tkmvdagesk ifmstrdtli rgymagaila laavfaitia vqtgmfllga
       61 ilfpvgfcml ylmgfdlltg vfvlcplawl dkrpgvtikg ilrnwglvfl gnfggaltva
      121 flmafiftyg fnvdpgaigt kvasigesrt lgyaeygtag wftifirgml cnwmvslgvv
      181 gamisthvsg kviamwmpif lfffmgfehs vvnmflfpfs iilggefsvv dyfvwneipt
      241 algnlvggla ftgltlysth vrtgskrkva kvapetlatg ttapnaas
//
LOCUS       WP_008843348             458 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Aliiglaciecola lipolytica].
ACCESSION   WP_008843348
VERSION     WP_008843348.1
KEYWORDS    RefSeq.
SOURCE      Aliiglaciecola lipolytica
  ORGANISM  Aliiglaciecola lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Aliiglaciecola.
REFERENCE   1  (residues 1 to 458)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Aliiglaciecola lipolytica"
                     /db_xref="taxon:477689"
     Protein         1..458
                     /product="amidohydrolase family protein"
                     /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=50490
     Region          20..447
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mcrfkrcwli lcvslsipla maeqtalvgg rlidgfghqp iansvilikd giiqqvgsvd
       61 tlvvpegyev istdgmdvlp glwenhahlm lnghsdyvhw dkayvnrlad eimpasavql
      121 llagitsard lgaalddtvs vkkriengei pgpnlyvsgp flqheaypgt eqfrwgikgv
      181 rdakqkvnkl adagmdiikl idhdkmtlee aqaivdqaha rglkvvahsh rpdeirrgle
      241 igvdnfehtg lttspeyped imrllkerta tgrvaggplf wtptveglwn ypatvanpek
      301 ldsqcwkrgl kqdtiediks slqnvgqley mqltplrkpt lkrkiaqlre agvvflvgtd
      361 sgipakfhcq stwnemavwv eqmnispmdt iraatywpav mmgvgdktgt vsagkaadii
      421 avhgdvlryi nllqrvdfvm kngtvykmdg vpveenln
//
LOCUS       WP_008844497             439 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Aliiglaciecola
            lipolytica].
ACCESSION   WP_008844497
VERSION     WP_008844497.1
KEYWORDS    RefSeq.
SOURCE      Aliiglaciecola lipolytica
  ORGANISM  Aliiglaciecola lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Aliiglaciecola.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 439)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 439)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 439)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Aliiglaciecola lipolytica"
                     /db_xref="taxon:477689"
     Protein         1..439
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=49916
     Region          4..436
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mvmevvivhy edyevgavsy dtekqlgafe ytsafiksgi qlsplkmpls kqvytfpead
       61 faafkglpgm iadslpddfg navinawvas qgkspkdisp lqrlkytgtr gmgaltfapa
      121 trhknlnasq qlevenlvei aqeivnqrse fnvslsqqgq edkeammalm svgmsaggar
      181 pkavlafndd ftqvrsgqtq apkgfnhylm kfdgvnehnt nqetfgdpmg ygameyvyyl
      241 matncqidmm pcylldegkr rhfitkrfdr ienekvhvqt lnglahvsfk qvgiysyael
      301 fdvarqlqls aqeaeqlfrr mvfnvvarnh ddhaknisfm fnknkewtla paydlaysyk
      361 pgskwvnshw mslnakrdnf drhdfytfss lspifnkrki driidevveq vskwkrlane
      421 yqvpkvlvde iqsnlrlsl
//
LOCUS       WP_008846038             113 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Aliiglaciecola lipolytica].
ACCESSION   WP_008846038
VERSION     WP_008846038.1
KEYWORDS    RefSeq.
SOURCE      Aliiglaciecola lipolytica
  ORGANISM  Aliiglaciecola lipolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Aliiglaciecola.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Aliiglaciecola lipolytica"
                     /db_xref="taxon:477689"
     Protein         1..113
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12550
     Region          1..103
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(5..6,24..25,33,36,38..39,41,44..45,47,55,60,66)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(24,55..56,58,84)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mnhqyqqqiw qtvlqipcgk vasygqiadl aglpgrarlv gkalgvapea lkvpwyrvlr
       61 sdgkiafaaq seqaknqtal lqqenvavfn nrvkltlfqw qpdladllfk lny
//
LOCUS       WP_008855737             138 aa            linear   BCT 20-JAN-2025
DEFINITION  3-hydroxyacyl-ACP dehydratase FabZ family protein
            [Lentilactobacillus kisonensis].
ACCESSION   WP_008855737
VERSION     WP_008855737.1
KEYWORDS    RefSeq.
SOURCE      Lentilactobacillus kisonensis
  ORGANISM  Lentilactobacillus kisonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lentilactobacillus.
REFERENCE   1  (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 10101294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Lentilactobacillus kisonensis"
                     /db_xref="taxon:481722"
     Protein         1..138
                     /product="3-hydroxyacyl-ACP dehydratase FabZ family
                     protein"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=15200
     Region          9..137
                     /region_name="FabZ"
                     /note="FabZ is a 17kD beta-hydroxyacyl-acyl carrier
                     protein (ACP) dehydratase that primarily catalyzes the
                     dehydration of beta-hydroxyacyl-ACP to trans-2-acyl-ACP,
                     the third step in the elongation phase of the bacterial/
                     plastid, type II, fatty-acid...; cd01288"
                     /db_xref="CDD:238615"
ORIGIN      
        1 mkpevndvip qrypfemidk ftnvepgvaa savklisine wffanqpath lvvprpimie
       61 amaqtgvaai lsmpenqgkn vffggiknav fqadfrpgdk lefevimkkl krniglghgt
      121 irrngqsice adlifave
//
LOCUS       WP_008855930             390 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Lentilactobacillus kisonensis].
ACCESSION   WP_008855930
VERSION     WP_008855930.1
KEYWORDS    RefSeq.
SOURCE      Lentilactobacillus kisonensis
  ORGANISM  Lentilactobacillus kisonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lentilactobacillus.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Lentilactobacillus kisonensis"
                     /db_xref="taxon:481722"
     Protein         1..390
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42532
     Region          3..390
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mtkvlivnag ssslkfklfd mskeavladg everlnmsgs ivkikygdgk tykttedkid
       61 yersagimln slkdlgiith lrdidavgnr vvagsdifdk vakisddvlq qivdlgeiap
      121 ihnpveaeyi kiiqrilpdt dqyaifdsaf fkdvpevnsi ygipyeltkk ftirrygehg
      181 inhgyiteqa ddmlgkkdak lvtlhlgsga svaaekdgkc ydtsmgftpm nglvmgtrag
      241 dvdpalvpff mkrmgakase viemfndrsg llgvsgvssd mrdlesskdp raqlaldmfv
      301 nrtvkftasy itelggvdai vfsggigehd kwvrdevckq lgifgiklda dlndqqkpgd
      361 lgtkdssari llipaneela mvrdvqgalk
//
LOCUS       WP_008857446             394 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Lentilactobacillus kisonensis].
ACCESSION   WP_008857446
VERSION     WP_008857446.1
KEYWORDS    RefSeq.
SOURCE      Lentilactobacillus kisonensis
  ORGANISM  Lentilactobacillus kisonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lentilactobacillus.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Lentilactobacillus kisonensis"
                     /db_xref="taxon:481722"
     Protein         1..394
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43085
     Region          4..394
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mvekilaina gssslkfkly lmpdeqvmih gmvdrighsd avftyqtedg akhdttesvk
       61 dhteatelvi kalnesgvik dkseivgigh rvshggnyyt qsveinddva kriselsvls
      121 plhnpanllg ieafekllpe arevavfdts fhstmppkay tyalpykyie kyhirrygfh
      181 gqshqyiysv vadrfgeqea dklischlgn gcsicaikdg ksvntsmgft plaglvmgtr
      241 sgdidpeilp fleekehlds edirsmlnhe sgvlgisgvs ndirdvlkae adgnkrakla
      301 ldvyahqiqq figayttdlg glkvlaftag vgehsapira rvcqgleylg ikideaknqa
      361 ndieiqasds kvkvvviptd eeliiareta kvig
//
LOCUS       WP_008857940             399 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Lentilactobacillus kisonensis].
ACCESSION   WP_008857940
VERSION     WP_008857940.1
KEYWORDS    RefSeq.
SOURCE      Lentilactobacillus kisonensis
  ORGANISM  Lentilactobacillus kisonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lentilactobacillus.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Lentilactobacillus kisonensis"
                     /db_xref="taxon:481722"
     Protein         1..399
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44038
     Region          6..394
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mgksiainag sstlkyklfq mpeekvlssg aidriglgss evsikygdgk kfkdtedidn
       61 heeaiqlvld kllslkiikd yneitgvghr ivaggelfpd svvidddvmk kiesltdfap
      121 lhepanllgi kafkkilpnv isvavfdtsf httlpevnym yslpyeyyqk yqvrkygahg
      181 tsyryvsqra aamlgkpled lklvvlhlga gasidaikdg ksfdtsmgfs pvagitmatr
      241 sgdvdpsalq yvmdkagiks mdemvdilnh ksglvglsgv sadmreiegv mhtnhramla
      301 reifknriir yigsyiaemd gidalvytag igendimirq evadkldyfg ikvdpekndi
      361 rgverdlsad gsrvktllip tdeelmivrd ierlrktqk
//
LOCUS       WP_008858585             192 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Dialister succinatiphilus].
ACCESSION   WP_008858585
VERSION     WP_008858585.1
KEYWORDS    RefSeq.
SOURCE      Dialister succinatiphilus
  ORGANISM  Dialister succinatiphilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Dialister succinatiphilus"
                     /db_xref="taxon:487173"
     Protein         1..192
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21064
     Region          3..190
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdiltlmker rsirkyqdkq vprelvdkiv eaglyapnag ggqrsmivtl hnaelakklg
       61 klnfstfdrs kllgghvsde qpsviddpni rngfydaptv cvifgqkdfl fsvadafcia
      121 enmilaahal gvdsciisra eetcalpegk afmeewgvpd tmeakafvtl gyhagdypkg
      181 kprkacrniv ie
//
LOCUS       WP_008859469             169 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Dialister
            succinatiphilus].
ACCESSION   WP_008859469
VERSION     WP_008859469.1
KEYWORDS    RefSeq.
SOURCE      Dialister succinatiphilus
  ORGANISM  Dialister succinatiphilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 169)
  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 169)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 169)
  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   4  (residues 1 to 169)
  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   5  (residues 1 to 169)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Dialister succinatiphilus"
                     /db_xref="taxon:487173"
     Protein         1..169
                     /product="TRAP transporter small permease subunit"
                     /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=19200
     Region          31..163
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mrsiyhiydr ilgyitnfaa aiaglaillt afmicyeiia rsifhsptvw vmeistyllv
       61 lagffgmayt mrknghitvd flysrfprpl qrgldivtsi lslfavyvcm testnymlms
      121 qamgvvspsl lrvpmwipqt fmvigfvllf leiinhllgd ffkeekegk
//
LOCUS       WP_008859737             191 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Dialister succinatiphilus].
ACCESSION   WP_008859737
VERSION     WP_008859737.1
KEYWORDS    RefSeq.
SOURCE      Dialister succinatiphilus
  ORGANISM  Dialister succinatiphilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Dialister succinatiphilus"
                     /db_xref="taxon:487173"
     Protein         1..191
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21176
     Region          3..152
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mnfkelsiqc rtyrrfsqkp vdpailqelm envrivssam ngqvlryvlv kdpalvkklq
       61 paihwaaalp kelgtpkege qptafilvck egrgnpwddi dagiavrnia lnacaygigs
      121 ailgavewnr vkdilsvpen wnprllmalg ypsceshivd vpesgsikyf ldenknycvp
      181 kralkdiclv k
//
LOCUS       WP_008859952             278 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Dialister
            succinatiphilus].
ACCESSION   WP_008859952
VERSION     WP_008859952.1
KEYWORDS    RefSeq.
SOURCE      Dialister succinatiphilus
  ORGANISM  Dialister succinatiphilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Dialister succinatiphilus"
                     /db_xref="taxon:487173"
     Protein         1..278
                     /product="formate/nitrite transporter family protein"
                     /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=30506
     Region          28..274
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mketadsrfe eevkqsktkv iveeyeklss slifeiirhd gekeldratv plifsalaag
       61 lmisfsfyfr avlsmyaghs pwadaisgig yttgflivil grlqlftent ittvipffes
      121 pswktllrig rlwaivllsn magtllsalf mtsscfasse itsfllstah himtptplen
      181 ifkgipagml iaavvwmipm srgfsfftif tftyfiaigg fahvvvgsge aayavlmgds
      241 svydyffrfl iptglgniig gtgiftllvs aqvkverk
//
LOCUS       WP_008860243             665 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Dialister succinatiphilus].
ACCESSION   WP_008860243
VERSION     WP_008860243.1
KEYWORDS    RefSeq.
SOURCE      Dialister succinatiphilus
  ORGANISM  Dialister succinatiphilus
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Dialister.
REFERENCE   1  (residues 1 to 665)
  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 665)
  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 665)
  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 665)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Dialister succinatiphilus"
                     /db_xref="taxon:487173"
     Protein         1..665
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=71283
     Region          21..659
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mnnekadvrl edveetkael dkkaqkmled kdadsrmriy dgplgkaivv llcvwtafql
       61 yfttigaisa inlraihcif llvftfllfp tykkekrrrk lpplwdwffi lgsagsflyl
      121 ifnytriaqt ggrissleig iafvaiicvf eaarrasgnl ailaalflay nwfgaylpgy
      181 lghngftlkr vlitqfwgtq gllgtgigvs atyiflfvvf gaflkysgfs hfindfsltl
      241 vgrtsggpak vaviasglmg mingsaianv attgtitipl mkrtgykkef agaveavast
      301 ggqftppimg avgfvmaefl nlsytyvala avtpallyyv glllavhfea krlglsgiak
      361 enipdamkvi reqghlvlpl isliglmfag ftplyaavis ifvtigaswl rkdtrmtpdk
      421 ilaavvegsk saisvgvccv iigviigtvt ltslglnmgy lilsvvnggs iylagflvmi
      481 msailgmgvp gvaayvivqa vavpvlikag ampliahlfc liyaclsnit ppvamsayva
      541 sgiadsdqtk tglwavrlgl igfiipfffl dnpvlligvs ktatlfdtgw avftamvgtf
      601 alvaglegwi lrrctlveri ilivsspfll lpgvltdaag aagiaavciy qwmrrnkekk
      661 eieaa
//
LOCUS       WP_008862895             346 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Barnesiella].
ACCESSION   WP_008862895
VERSION     WP_008862895.1
KEYWORDS    RefSeq.
SOURCE      Barnesiella
  ORGANISM  Barnesiella
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Barnesiellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Barnesiella"
                     /db_xref="taxon:397864"
     Protein         1..346
                     /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=39919
     Region          15..283
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mntncdksrs vklptqkrid sidlfkgiai lgivwkhtfh pqwcdlihis alffilsgif
       61 fkdepfipfl kkkirtilip flffyilsyl ariafyfrhf rtlhgfawds lleifsisnt
      121 pdyltvnipl wflvclfvmq iifwclnrvi prnkyrscwf lvilaalyag ygtieswhsp
      181 fmfnvaiecl pyfiagnlfg lqiarflsks slkyllaptc falfigfqyl pidisilafi
      241 kaltifvail sllscfensc smiwttvryf gksslfimgi hvlllapiqs maraitgkpd
      301 lltgliclal tmlliyflip ftekyipwai grqrqkqdtk ssqste
//
LOCUS       WP_008863004             156 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Barnesiella].
ACCESSION   WP_008863004
VERSION     WP_008863004.1
KEYWORDS    RefSeq.
SOURCE      Barnesiella
  ORGANISM  Barnesiella
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Barnesiellaceae.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Barnesiella"
                     /db_xref="taxon:397864"
     Protein         1..156
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17281
     Region          7..152
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mefiaglsew gyfglfiaaf lagsiipfss eavlglllia gydswgcvfs atlgnwlggv
       61 tcyyigylgk tewihtylki peeklskmqr flkgkgslfg ffvfipvigd imivalgllr
      121 anplgtllsm mvgkfsryyl vviginylke wfpnlf
//
LOCUS       WP_008863323             711 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Parasutterella
            excrementihominis].
ACCESSION   WP_008863323
VERSION     WP_008863323.1
KEYWORDS    RefSeq.
SOURCE      Parasutterella excrementihominis
  ORGANISM  Parasutterella excrementihominis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sutterellaceae; Parasutterella.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 711)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Parasutterella excrementihominis"
                     /db_xref="taxon:487175"
     Protein         1..711
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76509
     Region          1..697
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 msylnkimsp rsvavigasn kehtigsdim krlveygftg kifpinpkds eiqgmtayps
       61 vlevpeeidm avivinakyv lsavdqchqk gikgivvisa gfketggaga eleaklvnkv
      121 reygmtcvgp nclgvvntdp kfrldacfae slpvrgdigf vsqsgalggg ilnilqdlnl
      181 gfaqfisign qadvnadsai eywenvddvk qillymesia dpkrfralas rtskkkpiia
      241 lkagrsaaga saasshtgsl agadkaadal lkqsgviref slqdlfntak vfshcpipng
      301 nrvaivtnsg gpgimatdav cehgmeiahl sdqtkealrs flpaaasvkn pvdmiasapl
      361 ehykktletv laddgvdmvv viylpflglk didvakavme iraahpdkpi vgvfmtknef
      421 fahlsetevn vpffmfaeqa veglarlnqq rlwrertdtp aprysvdtet veavfkqaaa
      481 dnrvqlttge slqvlaaygv rvcrdgeakd adeavalank igypvvmkln skkishktdv
      541 ggvrvgikda dqlraefadl vnkltekglm dgfegviiqe mvksdremvc gcakdpqygq
      601 mmmfglggvf vevmkdvtfr lapltvedas dmihsvkayk llagargavp aqinkveetl
      661 lrlsqlvedf afideldinp lmisgkdgep iavdgrikfn atealvalsi a
//
LOCUS       WP_008869581             621 aa            linear   BCT 20-JAN-2025
DEFINITION  sensor histidine kinase [Desulfonatronospira thiodismutans].
ACCESSION   WP_008869581
VERSION     WP_008869581.1
KEYWORDS    RefSeq.
SOURCE      Desulfonatronospira thiodismutans
  ORGANISM  Desulfonatronospira thiodismutans
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfonatronovibrionaceae;
            Desulfonatronospira.
REFERENCE   1  (residues 1 to 621)
  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 621)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20493667
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Desulfonatronospira thiodismutans"
                     /db_xref="taxon:488939"
     Protein         1..621
                     /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=70070
     Region          37..272
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          319..616
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mnkkllfpgv lllailytai gglaynagqe legvvtqqfn dqqlilaeki addirghfqf
       61 letalatlsr qtvkilpeqp shdylhsthd ilkdwhvlsl giagnapdns lmapdgsvss
      121 wkdmgidfpr eefqlwldsd pdgqvffsrt frpdqgpyag twimvmvkpl srdlemsfes
      181 gnfegmppaa ffvvdamkvs rdyahgvisg qtgypwvine egyflyhied dfdgrdsftv
      241 rhernpdisy erintivsqr llagdegtdw yisgwhrevy temkkllafs pvffthqekk
      301 rdshlwsvgv aapdeevwgl iqpivvrqwv vaglflvgat lglfglyfls lrwnhvltrk
      361 vedktrhlme sreqlreeke kveqsmqklk dtqqrlvqse rfaaigeaas hmsheiknpl
      421 mlmagfagqv rrrlsedspe aekldiivne akrlekmlve vrdftrphkl sikpcqpndl
      481 iaetvkifqd slessgivcs qelstdltqv nmdpdqvkqv lvnliknave vmpeggtlgi
      541 sskrqnqwvv vsvqdsgpgi paeklknifs pfyttkdkgt glglavsyri iqdhggdifv
      601 dsqeghgarf tiylpleean l
//
LOCUS       WP_008869956             248 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: prolipoprotein diacylglyceryl transferase
            [Desulfonatronospira].
ACCESSION   WP_008869956
VERSION     WP_008869956.1
KEYWORDS    RefSeq.
SOURCE      Desulfonatronospira
  ORGANISM  Desulfonatronospira
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfonatronovibrionaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002130
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Desulfonatronospira"
                     /db_xref="taxon:488937"
     Protein         1..248
                     /product="prolipoprotein diacylglyceryl transferase"
                     /EC_number="2.5.1.145"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008961 -
                     phosphatidylglycerol-prolipoprotein diacylglyceryl
                     transferase activity [Evidence IEA]"
                     /GO_process="GO:0009249 - protein lipoylation [Evidence
                     IEA]"
                     /GO_process="GO:0042158 - lipoprotein biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=26894
     Region          1..247
                     /region_name="Lgt"
                     /note="Prolipoprotein diacylglyceryltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0682"
                     /db_xref="CDD:440446"
ORIGIN      
        1 mkpilidigg lsiyafgvfm aaayllamaw gmreagrkgl drgmvlefgf yvliaglags
       61 rlfyfllypg efegslirvl tfwdgglvli gggitgaval mfylslkkqd irawldalap
      121 atalglvvgw mgcmfagcgy grpsqvpwav tythpdslgp lfvslhpaql yhalaslvif
      181 ivllglrgrl kskgqvaglf lmlyavstma vdffryeyea mlwifspvqa vsmvllvvgl
      241 alfvhkka
//
LOCUS       WP_008870807             805 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Desulfonatronospira thiodismutans].
ACCESSION   WP_008870807
VERSION     WP_008870807.1
KEYWORDS    RefSeq.
SOURCE      Desulfonatronospira thiodismutans
  ORGANISM  Desulfonatronospira thiodismutans
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfonatronovibrionaceae;
            Desulfonatronospira.
REFERENCE   1  (residues 1 to 805)
  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 805)
  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 805)
  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   4  (residues 1 to 805)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..805
                     /organism="Desulfonatronospira thiodismutans"
                     /db_xref="taxon:488939"
     Protein         1..805
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=90072
     Region          75..805
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mtrkfqvpas rlsiklspsr igfshtgraa arrdkkhvfq qrafdalelt laikrsgyna
       61 ylsgekglgr nrfildflrp ragkmpapgd lvyvnnlqdp dqplaitlpp gsardlrrem
      121 qaaikkires ipagfeqdfy irkhgdlike ynetrenlls rmehkahksg fslsvdengs
      181 ltlyplvegr amdpeefekl esevrkdlmq qsnrimeall glsrqisrke qdlkdnerrl
      241 drevaggrid tclkkirqkf pdnqklmdyl eslkqdlldn idqfkprdqs sessqevqvg
      301 gpdaclsryg vnifvehcrn ggapvlvedn pnyfnllgci eretemgayy tdftlikpgs
      361 lhkanggfli iraedilaqp qawegllrcl rsgraeiedp adqyemvrtr tirpepidld
      421 ikiillgsde lyeilleade rfgklfkvka hlresiprte esirnqsmdl aeiavsnslm
      481 pfdreavaal vdqssriagd qqklslkysh ladlmveada yarmhgadrv nadsvcqalk
      541 srkyrlslye defmseyere aikvqtqgsa vgranglsis mygdyilalp hqiscttgvg
      601 hggimdlere aelggpihtk gmmiikgylq nlfaqekplv lsgslcfeqn yaqidgdsas
      661 gaelaallsa lsnipinlsy aftgaisqsg avmavgevtr kiegyfelcr rkgltggqgv
      721 iiprdnlthl mlsreviqav kdnmfqvyav tcieeameil tgtragkkla dgkyspgsiy
      781 rladerlqhl ahladkqvpg krkkk
//
LOCUS       WP_008871735             285 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Desulfonatronospira thiodismutans].
ACCESSION   WP_008871735
VERSION     WP_008871735.1
KEYWORDS    RefSeq.
SOURCE      Desulfonatronospira thiodismutans
  ORGANISM  Desulfonatronospira thiodismutans
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfonatronovibrionaceae;
            Desulfonatronospira.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Desulfonatronospira thiodismutans"
                     /db_xref="taxon:488939"
     Protein         1..285
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31260
     Region          4..253
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mseidlhths tasdgtmtpy elvsharnig lkalaltdhd ttkglmqalq agndlglevv
       61 pgcelsveyp glmhilglwl rsdapalnka mqelrdkrnm rneviieklq klgidisyae
      121 vqtlagdasv grphisrvlm dkgvvtsvqe cfdrylgstg kayvpkekfd pekaisvlkd
      181 enalvilahp fslqldtdal rrelvrlkdl gldgvevfys ehtieqteiy aslcreldll
      241 ptggsdfhgs vkpeiglgsg rgnlnlsyal lkalkekrle nglwv
//
LOCUS       WP_008872499             200 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Mesorhizobium
            metallidurans].
ACCESSION   WP_008872499
VERSION     WP_008872499.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium metallidurans
  ORGANISM  Mesorhizobium metallidurans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 200)
  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 200)
  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   3  (residues 1 to 200)
  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   4  (residues 1 to 200)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 200)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Mesorhizobium metallidurans"
                     /db_xref="taxon:489722"
     Protein         1..200
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22036
     Region          5..196
                     /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"
ORIGIN      
        1 mvrsslavlv idenrirasi ieaglreagh ervtvihdvt giarriaeie pdvividlen
       61 pnrdmlenmf qlsravkrpi amfvdrsdqa sieaavdagv sayvvdglrq ervkpildma
      121 vsrfnafsrm areleearse lksrkvidra kgilmksrgl seeaayallr ktamnqnrki
      181 sdiaqslvta agllgpaede
//
LOCUS       WP_008872543             201 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Mesorhizobium
            metallidurans].
ACCESSION   WP_008872543
VERSION     WP_008872543.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium metallidurans
  ORGANISM  Mesorhizobium metallidurans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 201)
  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 201)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 201)
  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   4  (residues 1 to 201)
  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   5  (residues 1 to 201)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Mesorhizobium metallidurans"
                     /db_xref="taxon:489722"
     Protein         1..201
                     /product="TRAP transporter small permease subunit"
                     /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=22506
     Region          4..171
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 maellalsrt idrvnefigk wvswlilisi lvsagnaiir kvfdtssnaw lelqwylfga
       61 afmlaaaytl kqnehiridi vygmfprrvq hwidllghlf flmpfvtlmv iyfvpyvsls
      121 frsgemsnns ggliiwpaka illagfflla lqgiseiikk iaimrgdmdd pnpfisvheq
      181 aeleakalad eakalagevr s
//
LOCUS       WP_008873689             400 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Mesorhizobium metallidurans].
ACCESSION   WP_008873689
VERSION     WP_008873689.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium metallidurans
  ORGANISM  Mesorhizobium metallidurans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Mesorhizobium metallidurans"
                     /db_xref="taxon:489722"
     Protein         1..400
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40225
     Region          41..268
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mtkkpalvsv gpdfslsaas vdlnlrvhtv qfeenvppsa tvtdeaayfa dgtavttdft
       61 ytgvytgsnf sdrmigddlt nlfsgghgnd flygragvda lngddgndfi aggagddlla
      121 ggagndting gadndtlrgg idsdvihggt gddliyggsg irdsdgqdht pgdtndalyg
      181 gagndtiygn agddylegga gndrlfgndt atsptvgndt ihggagddii ggfggtstly
      241 gdagndtilg gdqndtiygg rgadiilast gadwmsanng ittgdgardt fvffsghspa
      301 svqdtiqgfk hgediidlee shvalilnda pgssgtfvss eaalgylqah sisaegavvk
      361 vdtgssgliv gfsdaagtid lnvsvgetaa aqmtqsdflf
//
LOCUS       WP_008875372             312 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Mesorhizobium metallidurans].
ACCESSION   WP_008875372
VERSION     WP_008875372.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium metallidurans
  ORGANISM  Mesorhizobium metallidurans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
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
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Mesorhizobium metallidurans"
                     /db_xref="taxon:489722"
     Protein         1..312
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /function="7 : Transport and binding proteins"
                     /function="16.1 : Circulate"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33548
     Region          1..309
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mieiegitkr ydattvvddv smlieprtia vivgtsgsgk ttllrminrl vepssgvikl
       61 dgadnrslpg yelrrsigya iqghglfphr tvaqniatvp vllgwdkari karvdelmtl
      121 yqldpeafgp ryphelsggq qqrvgvaral aaepnvllmd epfgaldpii rnkaqedlla
      181 iqkrfgttii lvthdmeeav hmgdkiavmd agklvqyakp aeilakpasa fvetlvgase
      241 kpfrllslgr vrdavekgta egeaipgdas qrdalaellw sgrpalpvkg ddgkplgrvt
      301 vdglvkraar pa
//
LOCUS       WP_008876286             280 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Mesorhizobium
            metallidurans].
ACCESSION   WP_008876286
VERSION     WP_008876286.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium metallidurans
  ORGANISM  Mesorhizobium metallidurans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Mesorhizobium metallidurans"
                     /db_xref="taxon:489722"
     Protein         1..280
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30398
     Region          10..261
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 middakiime avraadhdry lsalyapadk rdalfslyaf naeisgirdr iheplpgevr
       61 lqwwrdaita edganighpi adalkaaisa hrlpkpafdn mlearifdly ddpmpsrtdl
      121 egycgetaaa liqlaamvld pieaprfael agragcaqam tglllllplh rrrgqcfvpa
      181 dvlaaagssp eefvngdggp gaqravaami alarehlaaf eqaapalpps lrpaylplal
      241 traylakmes rspldrvvrl salrrhwlll rraskgwpsi
//
LOCUS       WP_008876109             386 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Mesorhizobium metallidurans].
ACCESSION   WP_008876109
VERSION     WP_008876109.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium metallidurans
  ORGANISM  Mesorhizobium metallidurans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 386)
  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 386)
  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
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 386)
  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   5  (residues 1 to 386)
  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   6  (residues 1 to 386)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 386)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Mesorhizobium metallidurans"
                     /db_xref="taxon:489722"
     Protein         1..386
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40048
     Region          13..57
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          78..375
                     /region_name="ASKHA_ATPase_ROK_BsXylR-like"
                     /note="ATPase-like domain of Bacillus subtilis xylose
                     repressor (XylR) and similar proteins; cd24076"
                     /db_xref="CDD:466926"
ORIGIN      
        1 msksyirhfn anaifhriri epnvsqrdiv artgidksvv ssiinqfsel glverspvat
       61 snkpgrpmeg ltispesgli vgvqieadti gyvaaaldgi plssraqafn gkldgvadlv
      121 argvreivse cgrtgdtlgv gislpglltd egvllhapvl gwrgvpvvdm fsaaldapvf
      181 agndgkaaam aeymfgecid tkdfiylfsg sgvggalfld gdiyrgasgl agelghikvv
      241 pqgrycscga sgclspylse pglaeeigrl tgnrpssfkd imqragande vvvgvldnag
      301 avlgsaissl vnifnpplvc lggdmasaep ylrpaveral qrlahpsmsv qtkvifsqls
      361 tvspflggva laldgvtgld sphvlp
//
LOCUS       WP_008878566             668 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Geobacillus].
ACCESSION   WP_008878566
VERSION     WP_008878566.1
KEYWORDS    RefSeq.
SOURCE      Geobacillus
  ORGANISM  Geobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 668)
  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   3  (residues 1 to 668)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Geobacillus"
                     /db_xref="taxon:129337"
     Protein         1..668
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=73391
     Region          1..668
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          163..240
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 mdmsqyldif ideskehlqt inerlleleq tpgdmalvne ifrsahtlkg msatmgfedl
       61 anlthqlenv ldgirnqrli vtpelldvvf qavdhleami isiasggdgk rdvgetveql
      121 krieqgempn kptageqlpl ehtygefeyh vlqqakdqgf siyeirvrlr kdcmlkaarv
      181 ymvfeqlnea geivkstppa dmleeekfdq eflvtvvskt padelrmrlm siseidevei
      241 aavtvdepsa ksgeqddlep pvstaigqva atqtkaeaae klaakqagkt irvnierldm
      301 lmnlfeelvv drgrleqisr dlnhpeltet vermsrissd lqtiilnmrm vpvetvfnrf
      361 prmvrqlare lgkkvrldvi gaeteldrtv ideigdplvh lirnaldhgi eapdirvacg
      421 kpeegtvklr ayhsgnhvfi eieddgagis rekvlqkaid rgivsaeeaa hltdqqvygl
      481 ifspgfstad risdisgrgv gldvvkstiq slggtvtvds qpgkgslfsi qlpltlsiis
      541 vllvqiaaet yaiplssime talvkkedif sahnqpvidf rgkvvplvrl kdvfsvpnas
      601 degdavaavi vrkgeklaal avdsfigqqe vvlkslgnyl ssvfaisgat ilgdgrvali
      661 idcnalvk
//
LOCUS       WP_008878814             370 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GerAB/ArcD/ProY family transporter [Geobacillus].
ACCESSION   WP_008878814
VERSION     WP_008878814.1
KEYWORDS    RefSeq.
SOURCE      Geobacillus
  ORGANISM  Geobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Geobacillus"
                     /db_xref="taxon:129337"
     Protein         1..370
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=42401
     Region          11..365
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 mkqtlderfl ispflvffiv hatqvgvgml gfqrplmeda gqdawmavll aglathvliw
       61 lmyrllaysp sggdivslhk hyfgrwfggv lsigllayya laaftvlqsy ieiikvwmfp
      121 lmgawqfsli flmltyyvis ggfrvvaglc fwgvviplat ifpmmafafe yaqyrnllpv
      181 ldhsptqilk avndmafqyl gfevllmyyp flknapssqk wahasnvlti flylvvilis
      241 iifynkeqia hitwptltla kipevpfier meyivisiyv lvvfpnlvva vwamarvvkq
      301 lfsirqrrsl pvliaclfig tlffeeksdi erfiqwtsks glfligvyip llyvyvwvve
      361 kvkkslqqkq
//
LOCUS       WP_008879234             367 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GerAB/ArcD/ProY family transporter [Geobacillus].
ACCESSION   WP_008879234
VERSION     WP_008879234.1
KEYWORDS    RefSeq.
SOURCE      Geobacillus
  ORGANISM  Geobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Geobacillus"
                     /db_xref="taxon:129337"
     Protein         1..367
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=41007
     Region          1..367
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 messkinvrq lfvlivlfeh gsavviplgv sakqdvwisi llslaiglll ffvyrrlfey
       61 ypdqpltayl pqivgaplgk llaivyityf lyiaarvlrd fgellltfay petplfvlna
      121 imavtvmygv ykgievlart gelflivlyf laiigfvlvf vsgivdvtql qpmleegwrr
      181 vwktvftetl yvpfgemivf tmlfpyintp tkvgragvvg mvlsginlal imainvavlg
      241 pdtvsrssfp lldtirrvqv adflerldvf fmitlitggf fkisiffyag ivgaanlfgi
      301 ssyrrlvypl gllililsvv iasnyaehiq eglkivtfyl hvplqviipv llliiaairr
      361 rfnqpak
//
LOCUS       WP_008879838             396 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Geobacillus].
ACCESSION   WP_008879838
VERSION     WP_008879838.1
KEYWORDS    RefSeq.
SOURCE      Geobacillus
  ORGANISM  Geobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae.
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
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 396)
  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   5  (residues 1 to 396)
  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   6  (residues 1 to 396)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 396)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 396)
  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 20283869
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Geobacillus"
                     /db_xref="taxon:129337"
     Protein         1..396
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43062
     Region          <26..63
                     /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(26,28..30,39)
                     /site_type="other"
                     /note="non-specific DNA interactions [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            39..45
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            order(40..41,45)
                     /site_type="other"
                     /note="sequence specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238044"
     Site            40..41
                     /site_type="other"
                     /note="putative cAMP binding site [chemical binding]"
                     /db_xref="CDD:238044"
     Region          80..384
                     /region_name="ASKHA_ATPase_ROK_BsXylR-like"
                     /note="ATPase-like domain of Bacillus subtilis xylose
                     repressor (XylR) and similar proteins; cd24076"
                     /db_xref="CDD:466926"
ORIGIN      
        1 mrtgnitlvk kmnkqlvlkl irdqhpisra diakitglnk atvsalvdel idehlvhesg
       61 igvstggrrp lmlrfnadag sligvelgvn ylyavltnln aeiiweqrrs frpeegqeai
      121 vsemveliea airrapatpy gvmgigigvp givhtesgtv ifapnlrwgd vslasalqkq
      181 wpqypviven eaklaalgek wfgagkefah fvyisagigi gagvvlhhql yrgvnglage
      241 ighhtidlng vrcncgnigc wemyasqkyi errlaeegrv ewlddrfsia amalaaesdd
      301 qlarileetg rylgigllqv iyaynpeavi iggplasagd yilraarkev eerilvknen
      361 epymivselk ekscaigaaa svleavvlpp efessl
//
LOCUS       WP_008880899             158 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Geobacillus].
ACCESSION   WP_008880899
VERSION     WP_008880899.1
KEYWORDS    RefSeq.
SOURCE      Geobacillus
  ORGANISM  Geobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 158)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Geobacillus"
                     /db_xref="taxon:129337"
     Protein         1..158
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17183
     Region          8..155
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfhqltyngt reenyalvie qlkaliagep nmianlanas allnqfltdi nwvgfyladg
       61 delvlgpfqg lpacvripfg kgvcgtaaae rrtvvvpdvh qfpghiacda asqseivvpl
      121 ikegrvigvl didspiknrf ddidrryleq fasvlvse
//
LOCUS       WP_008884533             361 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Salipiger thiooxidans].
ACCESSION   WP_008884533
VERSION     WP_008884533.1
KEYWORDS    RefSeq.
SOURCE      Salipiger thiooxidans
  ORGANISM  Salipiger thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
REFERENCE   1  (residues 1 to 361)
  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 361)
  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 361)
  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 361)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Salipiger thiooxidans"
                     /db_xref="taxon:282683"
     Protein         1..361
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=38877
     Region          1..351
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mdrrsflrat taggaaaaas alaapayaqg krtltlvttw grglagvhds aqycadqita
       61 atdgeltvel kaagelvgaf evfdavsagq admyhgvdyy flgqhpalsf fsqvpfgmnf
      121 meyanwyyhd gglelcdely sifglkafpa gntgpqsggw fskeinsped fqglkfrmpg
      181 qggqvlgklg asvqnlpgae vyqalssgai dgtewigpwa dekagfqeit kiyytagfhe
      241 pgpnlnltmn levfegltpa qqkiveqvar asnlwsmslf mannsaalqr lqsggvklme
      301 fpdsvwdafg aaakevveep mgdelyarcy esyndslrss akwisrsega fsaqrnrvmg
      361 l
//
LOCUS       WP_008885510             194 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Salipiger thiooxidans].
ACCESSION   WP_008885510
VERSION     WP_008885510.1
KEYWORDS    RefSeq.
SOURCE      Salipiger thiooxidans
  ORGANISM  Salipiger thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
REFERENCE   1  (residues 1 to 194)
  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 194)
  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   3  (residues 1 to 194)
  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   4  (residues 1 to 194)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 194)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 194)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Salipiger thiooxidans"
                     /db_xref="taxon:282683"
     Protein         1..194
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21080
     Region          4..194
                     /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"
ORIGIN      
        1 mtaalsivvv epdrdralli vdslrdagny dihviseptg larriqalnp dvvlidiesp
       61 srdmleelal asgphdrpva mfvdrdgagl teaaieagvs ayivdgmkpq rvkpimdaai
      121 arfrmfqrmr telaetkral eerkmidrak gmlmkargin edeayallrk tamdqgrrva
      181 evaaalvtaa gllg
//
LOCUS       WP_008886915             281 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Salipiger thiooxidans].
ACCESSION   WP_008886915
VERSION     WP_008886915.1
KEYWORDS    RefSeq.
SOURCE      Salipiger thiooxidans
  ORGANISM  Salipiger thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Salipiger thiooxidans"
                     /db_xref="taxon:282683"
     Protein         1..281
                     /product="formate/nitrite transporter family protein"
                     /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=29845
     Region          2..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msyvtpkefa vkmvdagesk ifmstkdtli raymagaila laaafavtia vntgnflvas
       61 llfpvgfcll ylmgfdlltg vftlaplavi akrpgctwgg vlrnwglvft gnfagamtta
      121 vlmavvfttg fstepnavge kighigeart lgyaaaggag lltvfvrail cnwmvstgvv
      181 aammststsg kimamwmpil vffylgfehs ivnmflfpsg imlggqftwa dyfiyneipv
      241 vlgnlvgglt fvgamiyath frespkrnan rnddiagvpa e
//
LOCUS       WP_008888207             362 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Salipiger sp. HF18].
ACCESSION   WP_008888207
VERSION     WP_008888207.1
KEYWORDS    RefSeq.
SOURCE      Salipiger sp. HF18
  ORGANISM  Salipiger sp. HF18
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
REFERENCE   1  (residues 1 to 362)
  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 362)
  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 362)
  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 362)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Salipiger sp. HF18"
                     /db_xref="taxon:2721557"
     Protein         1..362
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39352
     Region          1..355
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mdrrsfirrg alagagaaal aspavaqdri twrmvttwpk nfpglgvgaq rmadritaas
       61 ggrltvqvys agemvpplqs ldavidgtae mshgaayywq nkstalnyft gvpygmtage
      121 laawvrhlgg qelwdevydq fgvqaflsgn tgtqaggwfr eeltgldslk gvrfrtpglg
      181 grvweklgat vtnmaageif qalqsgalda aefvgpyndl algfhqvakn yyfpsfvepg
      241 latelvvdka kfqelpddlq aivrdvcqae ydsvssdfva ndpralktlv edhgvqvrqf
      301 peeileagag aameiiaelr dsgdemtrkv tehfieslnm mrtrtegndl sfiqararyf
      361 tl
//
LOCUS       WP_008888990             264 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Thalassospira profundimaris].
ACCESSION   WP_008888990
VERSION     WP_008888990.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira profundimaris
  ORGANISM  Thalassospira profundimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Thalassospira profundimaris"
                     /db_xref="taxon:502049"
     Protein         1..264
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25545
     Region          2..240
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 matleggafd dallgsrfsd vifgrggddt ifgqgnddvl fgeegddvlf ggsgddvavg
       61 gegddvlfgg sgddaliggd gsdlmmggsg edvlsggads dillggsdnd vldggsgndv
      121 liggagddiv lggggddvml ggsgddvlqg gegddlmlgg sgddvlegga gddimsggsg
      181 adtfvfsggg gndvildfqa gedmlsissn indtgiasad dvaaratqvg antvidlgng
      241 dsitlnnvda edvqddpdsf fsvq
//
LOCUS       WP_008889170             488 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Thalassospira profundimaris].
ACCESSION   WP_008889170
VERSION     WP_008889170.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira profundimaris
  ORGANISM  Thalassospira profundimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 488)
  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 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   3  (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   4  (residues 1 to 488)
  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 488)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Thalassospira profundimaris"
                     /db_xref="taxon:502049"
     Protein         1..488
                     /product="CmpA/NrtA family 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=53602
     Region          127..366
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 msvkslgnpf sgdtdlrhsk scgcdvcssk dghthashkd hdhgvkhdla smpahsdmgd
       61 mdaktpesse emldraidsa ivrsvfghnd isrrsfakmv ggstmmaala svlpidkvka
      121 ailddlgtpe ksklnigfvp itcatpiima qpmgfyekyg ldvdviktag wavardksln
      181 neydashmlt pmplaismga gstatpflmp aveningqai vlhndhldkr dpkqwkgfkf
      241 gvpfeysmhn fllryyvaeh gldpdkdiqi rvvpppemva nlragnldgy lspdpfnqra
      301 vwekigflht ltkdiweghp ccafacskaf seelpntyga llksivdatq yaakaenrke
      361 isaaiapany lnqpvpvieq vltgryadgl gevknvpdri dfdpfpwhsm gvwiltqmkr
      421 wgyiegdvdy kkiaeevyva sdcakimkel gyeaptetyk sytimgkafd pdqpeayvns
      481 faigkgvs
//
LOCUS       WP_008889539             391 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Thalassospira profundimaris].
ACCESSION   WP_008889539
VERSION     WP_008889539.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira profundimaris
  ORGANISM  Thalassospira profundimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 391)
  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 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   3  (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   4  (residues 1 to 391)
  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 391)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Thalassospira profundimaris"
                     /db_xref="taxon:502049"
     Protein         1..391
                     /product="CmpA/NrtA family 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=43231
     Region          4..264
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mankvrlgfv plvdcaipvv aramgfaqqe nidlelvrem swaairdkls fgmfeaahll
       61 agipiaarlg lgglpvqniv vpmalgrggn aitvstqlyq rmleadpnam lgprgrsara
      121 lkkvidedka egrpilsfat vfpfsshnye lrywmaaagi dpdmdvnigv iapprmfdsl
      181 rngwvdgycv gepwnqravf hgdgvivalk ddiwsrspek vlglredwaq snpelvsalv
      241 ralvraaewa dqpgnrvela hilseeanvg apfevlkasl sgkpvlrpge ppidlpdrhv
      301 fyrytatfpw lsqgrwigeq mkrwrqipqd tdlkavipdv frpdlyrtav agldvlvpqd
      361 dwriegaada pdrslvgmdq flddtifkae f
//
LOCUS       WP_008889608             250 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Thalassospira profundimaris].
ACCESSION   WP_008889608
VERSION     WP_008889608.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira profundimaris
  ORGANISM  Thalassospira profundimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Thalassospira profundimaris"
                     /db_xref="taxon:502049"
     Protein         1..250
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=27280
     Region          13..166
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mgekitktrs agniishpsp nfgdrpdgcp idilvlhytg mqsgadaler lcdpessvss
       61 hylieedgri fqlvdedkra whaglgiwqg cqdvnshsig ieivnpghey gyrpfpeiqi
      121 qsvidltqdi lkrqeipasr iiahsdmapd rkedpgelfp wqqlaengig lwpgchgvae
      181 issgisgaav spdefyrlle aigygpadsd egkakrtiaf qrhwrqndis gnvdgeclai
      241 akvlasaitr
//
LOCUS       WP_008889796             414 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Thalassospira
            profundimaris].
ACCESSION   WP_008889796
VERSION     WP_008889796.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira profundimaris
  ORGANISM  Thalassospira profundimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 414)
  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 414)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Thalassospira profundimaris"
                     /db_xref="taxon:502049"
     Protein         1..414
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47109
     Region          10..399
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mpidsaaips ptvsisakqa rnlalvgqgf aanpdrdvtk rqilktirat nmlqvdsvnv
       61 ltrahympif srlgvydpkm ldemvwgtar qrklfeywgh easmipvedy plyrwrmrda
      121 ergmgtwgri arvqreqpdl idnilrhidq egavaassle tegrssekww gwsntktame
      181 ylfwsgqvma rkrrssfere ydlphriigd aahepdrdrq damcdlicqg iaamgvaaei
      241 dlrkyfrlpt detkaclarl veegrllqad vegwkqpgyl cpkvnprsra kptclmvpfd
      301 pvmwerdrve rifgfnyrie iyvpaekrqh gyyvlpfmln gefvarvdlk sdrqagvlrv
      361 qsahledhvk aadvagplme nlhrlavflg lggvevmpan dfskyigsap inlv
//
LOCUS       WP_008889658             194 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Thalassospira].
ACCESSION   WP_008889658
VERSION     WP_008889658.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira
  ORGANISM  Thalassospira
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae.
REFERENCE   1  (residues 1 to 194)
  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 194)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 194)
  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   4  (residues 1 to 194)
  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   5  (residues 1 to 194)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Thalassospira"
                     /db_xref="taxon:168934"
     Protein         1..194
                     /product="TRAP transporter small permease subunit"
                     /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=21649
     Region          3..168
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 meallkfsdi idaivtrvgk wasllaiplm ivilydviqr kfggqgsikl qelewhlhtg
       61 lfmlcfgfay irdahvriel irdnlrprtr aivemiggii cvlpfcalvl yfgfdfvars
      121 fesgevsast tglthrwiik stipigfgll amaglsiflk cfvyvfgptn lhkragyyvg
      181 thhleelgta kikd
//
LOCUS       WP_008889914             195 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Thalassospira].
ACCESSION   WP_008889914
VERSION     WP_008889914.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira
  ORGANISM  Thalassospira
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Thalassospira"
                     /db_xref="taxon:168934"
     Protein         1..195
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21546
     Region          1..163
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mirslydwtm nlaghrhagw alffiaaies svfpippdil lipmiiaapt rawryalicl
       61 vgsvlgglvg ygigfflfet vgqpvlelyg yadkfdqfrd yynewgawav fiagvtpfpy
      121 kvitilsgvt aldpvvftla silarglrff viaaliwkfg pvirdfierr lglvftifiv
      181 vlvggfaaik liphg
//
LOCUS       WP_008889951             364 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [Thalassospira].
ACCESSION   WP_008889951
VERSION     WP_008889951.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira
  ORGANISM  Thalassospira
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae.
REFERENCE   1  (residues 1 to 364)
  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 364)
  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 364)
  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 364)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Thalassospira"
                     /db_xref="taxon:168934"
     Protein         1..364
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39051
     Region          1..357
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkrrefltag vagagaaaaa tfatpaiaqd krqwnmvtaw pknlpgpgva aqkladritt
       61 lsggrlevkl haagelvpgn gvfdavaegt aeiyhavpay wgskskgill fgsqpfglra
      121 deqvgwlnyg ggqelydeiy gqfglkpflc gnsgpqwagw frneinsvdd lkglkfrttg
      181 lasemcsklg mavqamggrd mfqalqsgal dagefigpws dsalgfyqva knyywpgvge
      241 pssaeecavn akayadlpdd lkavvkfaad slynevwtey etkhamalkq lvaeqdvkvr
      301 klpdevveam akagaeviae lresddaltk kvtesfvayr dliggymtya dngqmnarak
      361 algf
//
LOCUS       WP_008890025             190 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Thalassospira].
ACCESSION   WP_008890025
VERSION     WP_008890025.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira
  ORGANISM  Thalassospira
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae.
REFERENCE   1  (residues 1 to 190)
  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 190)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 190)
  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   4  (residues 1 to 190)
  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   5  (residues 1 to 190)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Thalassospira"
                     /db_xref="taxon:168934"
     Protein         1..190
                     /product="TRAP transporter small permease subunit"
                     /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=21351
     Region          1..167
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 migfiefadk lsawfgkafg wliilmtlgm syevasrylf napttwsldv sfimygtlfm
       61 mggaytlsrg ghvrgdflyr lwkpttqakv dlvlyiffff pgvtalilsg wkyaarswgy
      121 gevsvnspag vpifqfkavi vaagillfiq giaqvmrcil ciregywrna dddvqeteel
      181 lmkqkvaked
//
LOCUS       WP_008890163             304 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Thalassospira
            profundimaris].
ACCESSION   WP_008890163
VERSION     WP_008890163.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira profundimaris
  ORGANISM  Thalassospira profundimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Thalassospira profundimaris"
                     /db_xref="taxon:502049"
     Protein         1..304
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33503
     Region          19..260
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mtggvmyqpe ilsdetftla ecpnwdaann rlywtdilnc klhaldvatg lrktwtfdse
       61 lgcfgltdqg riivalrkdi lfldpktdar aplcriedgi nsrtndgkig pdgafwvgtm
      121 ddnpekmpva slyritadgk ieekatgfki sngiawsgdg akmyhsdsrg pwvnrwdfdv
      181 atgnisnctr yldlddrlgr pdggavdaeg cywsagvsag nlnrfapdgt llksipmpmp
      241 nptmpcfggp dmktlyvtsh qegyspekra efphagklvk lrvevpgvpv tkfrenserr
      301 aypr
//
LOCUS       WP_008890630             199 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Thalassospira
            profundimaris].
ACCESSION   WP_008890630
VERSION     WP_008890630.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira profundimaris
  ORGANISM  Thalassospira profundimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 199)
  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 199)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 199)
  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   4  (residues 1 to 199)
  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   5  (residues 1 to 199)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Thalassospira profundimaris"
                     /db_xref="taxon:502049"
     Protein         1..199
                     /product="TRAP transporter small permease subunit"
                     /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=21660
     Region          28..180
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 msapsdpkti apdllhtdvl qlealpqagw lgraitvvar lfavcilaam ailvtevflr
       61 yvfnrptvwa hettiflsav tfiygglycv arnthirvvl vydvvrasar hvldvvisia
      121 clgaslffaw aswlmakkam frpdgsfale tsgsawnspa paalkifllc vlvamsfqfl
      181 iltfnyargt kapkghddv
//
LOCUS       WP_008890678             356 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Thalassospira profundimaris].
ACCESSION   WP_008890678
VERSION     WP_008890678.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira profundimaris
  ORGANISM  Thalassospira profundimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Thalassospira profundimaris"
                     /db_xref="taxon:502049"
     Protein         1..356
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=38748
     Region          113..348
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mtycekcdav peiapangtl flwppvahtt gkilagaksi gievektpsv atlsihytrp
       61 glralidais gnllpeelsd tkalimpgvq rpeiddiaqi tslgairaai gaewlgdllr
      121 dnrlnsvfqp ifdindlgkp yaheclvrge satgdvinpg qlfdaaqsat llfqldraar
      181 aanvrnahka gvkgnlfinf tpssiydpds clrstievve ecnldrsnvv fevietekvr
      241 stahlsailq syrdsgfrva lddvgsgyst lnmlpelrpd iikidrelvd hvdhdkfkqa
      301 ivsklialak qldieviaeg ierqeeldfl rdhdvdyvqg fllgrpaptp faakag
//
LOCUS       WP_008891003             281 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Thalassospira
            profundimaris].
ACCESSION   WP_008891003
VERSION     WP_008891003.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira profundimaris
  ORGANISM  Thalassospira profundimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Thalassospira profundimaris"
                     /db_xref="taxon:502049"
     Protein         1..281
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31815
     Region          7..259
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mpdtpklshc adyvrrhdrd rflcalfatp ekreslftly afnqevsktr emvsevmlgh
       61 irlqwwrdtl telgdgqvrk hevvepladl vrdghlaiad leaivaaref dledrqpatq
      121 qeldryidqt sgqisvlasr llgagsddad haarlagnay glvgimraiv fhgrskrlyl
      181 pkdrmehhev aqgdvfefrk kqeirefire laelararia earkhrsalp kqahaaalpv
      241 vladgylrkl aksgydpfsa efglarpasl rltlngmfkr y
//
LOCUS       WP_008891662             205 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Thalassospira profundimaris].
ACCESSION   WP_008891662
VERSION     WP_008891662.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira profundimaris
  ORGANISM  Thalassospira profundimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Thalassospira profundimaris"
                     /db_xref="taxon:502049"
     Protein         1..205
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21987
     Region          4..190
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mtqkdrliig itgasgviyg irflqllknt piethlvlsk aaertiayet dfkireikem
       61 advahdnadi gasiasgsfr argmiiapcs mkslaevasg vadnliaraa dvilkerkrl
      121 vlmaretplh aghirnmala tengaiiapp vpafyarpqs ldemvtqscg rildlfeidl
      181 petarwgdte aanpipvtgk pktga
//
LOCUS       WP_008891952             190 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Thalassospira
            profundimaris].
ACCESSION   WP_008891952
VERSION     WP_008891952.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira profundimaris
  ORGANISM  Thalassospira profundimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 190)
  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 190)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 190)
  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   4  (residues 1 to 190)
  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   5  (residues 1 to 190)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Thalassospira profundimaris"
                     /db_xref="taxon:502049"
     Protein         1..190
                     /product="TRAP transporter small permease subunit"
                     /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=20193
     Region          11..167
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mkstrteplp drvlglvvdi agwgaaisgl alvlvvggnv llrylfnsgs vamqelewhl
       61 vspialmgma ygmrhgghvr vdflyerlgp raqaiidlfs avlmvvlgaa liwfsipyva
      121 qsimmgegsp dpgglpyrfl lkafipigfg llliqaiaqg lmnyrqivag nrgepafdap
      181 dvvtqtgagd
//
LOCUS       WP_008892002             417 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Thalassospira profundimaris].
ACCESSION   WP_008892002
VERSION     WP_008892002.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira profundimaris
  ORGANISM  Thalassospira profundimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 417)
  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 417)
  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
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 417)
  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   5  (residues 1 to 417)
  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   6  (residues 1 to 417)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 417)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 417)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Thalassospira profundimaris"
                     /db_xref="taxon:502049"
     Protein         1..417
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45068
     Region          1..>57
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          92..394
                     /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 mmrrtesetp rqpsqtailr ylrmhgpaar idigtatgls patvtsltad lmaqglvkes
       61 egsnnngtan gngngttrgr pkvlldlvpn aacvigvkit inlieialgn fkgeiersie
      121 hcintrdlga deltrtlial idrflernrd fcihppagis iaiqgvtdsn sgeiiwspal
      181 rhrhiplvks lserygsavq msndanciat aisqntnlhn dgdfavimlg ygigmglvln
      241 gkvyngdfgt aaefghtkyq pdgplcncgr rgcleayigd yailrdargv idlpdtnnlh
      301 pseeqmmdlv ararrgdtgl aelfrhagkv lgygianlia llgpkqifit gsgarafdmm
      361 epelrrglde aqvpelsrnp titylpwdkd lalqgaigqs llrhdenmfq atatvre
//
LOCUS       WP_008892313             366 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Thalassospira
            profundimaris].
ACCESSION   WP_008892313
VERSION     WP_008892313.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira profundimaris
  ORGANISM  Thalassospira profundimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 366)
  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 366)
  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 366)
  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 366)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Thalassospira profundimaris"
                     /db_xref="taxon:502049"
     Protein         1..366
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39272
     Region          1..356
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkrraflgga gvaagafaat aaapsivkan etinwrmvmp wpkgtpglga ngelfaervn
       61 kmsggrlkit vygagelvpa lecmdaveqg vadlahstpy ywfgkdpavs ffttipfglm
      121 gwelsgwlrf gggqalwdel yaqfnvkpfl agntglqagg wfnkeinsve dlkglkvrya
      181 giggeamrrl gatpsllpaa dilpslqsga idaaewvgpw ndyafglasv akyyytpafa
      241 epgsgievfi nkdkfaelpe dlqeivavaa qanaeqtlsd fafnniqsyq ailekgteir
      301 hfnddlinaf ataskealee iaakneltgr iyasvmdfak kaapygkefe atalnqranv
      361 fangty
//
LOCUS       WP_008897228             625 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Rheinheimera sp. A13L].
ACCESSION   WP_008897228
VERSION     WP_008897228.1
KEYWORDS    RefSeq.
SOURCE      Rheinheimera sp. A13L
  ORGANISM  Rheinheimera sp. A13L
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Rheinheimera.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 625)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Rheinheimera sp. A13L"
                     /db_xref="taxon:506534"
     Protein         1..625
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=70247
     Region          67..616
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mlrirsahfi vislvvylla ivayvyyqyq qtyqtklaql dlqlvnavka vpyllgddyh
       61 nnisgpqhlp raeylklakk lslyakdlkl qylysmiqvd gkvhftsssy teddllrgql
      121 syfydyypea teankaafas ltpvfeesvd qfghfrsvlm pyqssdgtiy lagadiaitd
      181 ldqwllssmq qsvlsgsvff glalllalsy amvlrynltt drssgkrnal aleahlrhes
      241 gglsqlailq vnnleeichl ygtpiaeqaf nqfiqqlqlh lgrsfrlyrl sfeklairrv
      301 aaisdndlhd klksfdftqp vlndpyllft vtlgvalspa avvlenatla vntarlqqqs
      361 lvvysdnlla lkqhlhtnik makevreaig heqivpyfqp vvqistgeif qyeclarilr
      421 sdgsiltpdq flsiinrshl dteltkmmfi ksasqfvase vswsinvncr dlldddlqqf
      481 fldylqhypk pervyfelae agvlpqfdrc rdaiaalqka gakvllddfg vasgvgmadl
      541 lqlhvdglki hgsliemist dpdaqlfleh issfakqtql liiaemvesk qsldalercg
      601 isyaqgyyfg paapvplryy ergsv
//
LOCUS       WP_008897299             395 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Rheinheimera sp.
            A13L].
ACCESSION   WP_008897299
VERSION     WP_008897299.1
KEYWORDS    RefSeq.
SOURCE      Rheinheimera sp. A13L
  ORGANISM  Rheinheimera sp. A13L
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Rheinheimera.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 395)
  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 395)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Rheinheimera sp. A13L"
                     /db_xref="taxon:506534"
     Protein         1..395
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45609
     Region          8..385
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mtascpfspk elrqlvlqhq gllkpasgke alaevlkqls yvqldsiyvv erahhhvlyn
       61 rvknyqpkll eqaleqkqsf eywshaaafl paedyrfslq rklllqngnn hwfnpeqqlm
      121 nevldrieae gplkasdfas kngnagkkng awwdwqpakq aleqlfmqgk lmvarrdkfq
      181 kvydlaervw pdhhehipps eaefadylie rclqsqavat vqqigylrkn mqlalkqqln
      241 qqlaqgrlqt flldgktyyh rpqlaltnnl psklpnkvwl lspfdnlviq rdrlkqlfnf
      301 dyqievyvpa akrqigyysl pmlykdlfig qvdvkadras ktlllqhlvl deqvkltdal
      361 kaaltkavld yaafngcesw qlvktsartr dwfvg
//
LOCUS       WP_008898171             671 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Rheinheimera sp. A13L].
ACCESSION   WP_008898171
VERSION     WP_008898171.1
KEYWORDS    RefSeq.
SOURCE      Rheinheimera sp. A13L
  ORGANISM  Rheinheimera sp. A13L
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Rheinheimera.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Rheinheimera sp. A13L"
                     /db_xref="taxon:506534"
     Protein         1..671
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=74126
     Region          1..671
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mnylpfklsa lalsffsval saedrlpdei ivitaqaqqs pwmgsaassf rkdfnnpslq
       61 idaaallqhi pgiqadsran yaqdsrlsar gfgsrssfgi rgirllqdgi plsspdgqgq
      121 lssvlldqla svevltgpla vlygnaaggv valqsrwpte nsasvqlshs qfarqqllsg
      181 alvqgkhats lslknaelqs srphsnakkq qaqwlwqsaf dnelklqlry dwsydpllqd
      241 plgltaqewq dnprqtaana ltfdtrkfsk qqqwslnlsq qldrqswqla awsgqrdvgq
      301 ylgfdgaapt saggvidlsr pyqgldasys wqfkqlrlsv ggaleqstde rrgyvnnqgi
      361 qgdlrrdeeg evqsadlysr fvwdvnpdwq lsggvrrsel dfdvtdfyit pqnpddsgst
      421 sfgktsaala lnfaqsehls wyistgrgfe tptftemayq snsdglnlgl kastnqqwel
      481 gnkwqqnnwr ssvavflves enelvvdrsf ggrtsyrnas etkrtgvels alwfasaswq
      541 hqwtltqlna sfvqgdldgk llpgvakqqa qwqiswmpfq ssewmlqldt lyrskvatsd
      601 qnllfapsst vyhlklmggs tlpamqlsyw lgldnltdkn yvgavvvnqa ngrafepalp
      661 rsvslglsls f
//
LOCUS       WP_008898660             109 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Rheinheimera sp. A13L].
ACCESSION   WP_008898660
VERSION     WP_008898660.1
KEYWORDS    RefSeq.
SOURCE      Rheinheimera sp. A13L
  ORGANISM  Rheinheimera sp. A13L
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Rheinheimera.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Rheinheimera sp. A13L"
                     /db_xref="taxon:506534"
     Protein         1..109
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12317
     Region          19..105
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mpstdisklq leprhltlll qileqyvpqa evwaygsrvt gkahqgsdld ivlrnvenln
       61 vaqsdwselq ealqqstlpi lvdvhdwall pnsfypnieh dyvvlqksq
//
LOCUS       WP_008898614             696 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Rheinheimera sp. A13L].
ACCESSION   WP_008898614
VERSION     WP_008898614.1
KEYWORDS    RefSeq.
SOURCE      Rheinheimera sp. A13L
  ORGANISM  Rheinheimera sp. A13L
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Rheinheimera.
REFERENCE   1  (residues 1 to 696)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Rheinheimera sp. A13L"
                     /db_xref="taxon:506534"
     Protein         1..696
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=75647
     Region          20..696
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 msamffthnf rpsrialava vaatgyasss naedtatakk svmpamevvk vvgqkedhrf
       61 eatgsvnlve leeiqrvqpl stedvlrrip ginikseeet svianfgirg lsasesksll
      121 ledgvpvapg lfigndryfn priqrverve vlkgssslry gpstiggvvn yqtktpddgv
      181 elsaragsfn mkevgieagn knaagdafag ivathatsdg fmdkgytmnd vmakagvefa
      241 nnqklgvkls wyendvnmsy rglllndyka gadynpapdd dfladrvafd inhewqlsdt
      301 atlntlvyws dvtrdywrya vdtnasvaag rwvytdaltg nnrsfertga esrltleqpl
      361 fgleastefg lrlmheksnd lritttraad rtgtiaghlq dsadsvagyv qsrivlsekl
      421 altpglries yqqerlnlqs nalaktsnte ylpgvgltye ltdaaqlyag vyrafspasn
      481 slaldgltdq qldgersvny evgvrgvags tsyevaafim dfsnqvvsgn sntgtpssna
      541 getshygief svsqplmagl nldanatwvp esefeagtnq gnripyapki lanlglnyql
      601 eqlnlslnlh hrgeqfgnea ntiaiehptg kpndiwggll paytvvdlls qyqvsdnlsi
      661 sgsvknltdk ryisglrqgi yvgpersfei garyrf
//
LOCUS       WP_008899487             137 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Rheinheimera sp. A13L].
ACCESSION   WP_008899487
VERSION     WP_008899487.1
KEYWORDS    RefSeq.
SOURCE      Rheinheimera sp. A13L
  ORGANISM  Rheinheimera sp. A13L
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Rheinheimera.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Rheinheimera sp. A13L"
                     /db_xref="taxon:506534"
     Protein         1..137
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=15547
     Region          30..106
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mnyndkdqyg iyktsslpeh gnqgpgpslm gaetligndv ynhheeqvgd ikelmldmkd
       61 gkvsyavlsf gsflgmgekl favpwnalil dtenkrfkld idkdrlenap gfdkdnwpdm
      121 adntwrelih syynrtn
//
LOCUS       WP_008900357             796 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Rheinheimera sp. A13L].
ACCESSION   WP_008900357
VERSION     WP_008900357.1
KEYWORDS    RefSeq.
SOURCE      Rheinheimera sp. A13L
  ORGANISM  Rheinheimera sp. A13L
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Rheinheimera.
REFERENCE   1  (residues 1 to 796)
  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 796)
  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 796)
  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   4  (residues 1 to 796)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Rheinheimera sp. A13L"
                     /db_xref="taxon:506534"
     Protein         1..796
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88701
     Region          70..796
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mthnshkyal taehlgpqld knliqqaldv sglsstfigq drakaalnfa igmdmpgynl
       61 yvmgepalgr ytlvqdilqq aasekatpdd wcyinnfdde ripgtlrlvp gegkvlvkkv
      121 ealidelldt fpaafdnpgy qrkkkaihqe fddkyeaaia lverkaleqq vvlyeengav
      181 sfspvvdgka lddnefanls eekrqffydl vseletilne qllelpqwkr elsenlralr
      241 retieqaikp llkqlehdys aelgvlrylr emkpalvkam lellpeeaes dkleeldirg
      301 ifvgdfvpnv lmhhelmdga piifepnpsy gnlfgrveys smqgslytny rmirpgalhk
      361 anggylvlda drllsqpslw dalklalktg eilidtlsdh avtnstiitp kaiplsvkiv
      421 llgsrdlyyl vqdvddefne lfrvladfeh ylpfneqtvr ymslqiqdqi qqmdmetlsa
      481 cglkqllnfs frqaehqrkl sarfaevlel vreacfyaaq hdsaelraeh vqmalegkqy
      541 rtgrisesfl ediqegqili dtddwavgki ngltvleigd tafgtparis ttvfagstgv
      601 vdierevelg ksihskgvml ltgylgakya qhfpltlsan iameqsygli dgdsaslaev
      661 calisgiadi pitqslavtg sinqhgqvqa iggvnekieg ffrlcesrgl tgkqgciipa
      721 snqlnlvlnd evikaveqgq fhiyvvkgvd ealellmdmp agernskgqy pkrtinylal
      781 rrleeiaeiv ngssds
//
LOCUS       WP_008900541             141 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Rheinheimera sp. A13L].
ACCESSION   WP_008900541
VERSION     WP_008900541.1
KEYWORDS    RefSeq.
SOURCE      Rheinheimera sp. A13L
  ORGANISM  Rheinheimera sp. A13L
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Rheinheimera.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Rheinheimera sp. A13L"
                     /db_xref="taxon:506534"
     Protein         1..141
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14869
     Region          1..141
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mqstrshgfs lvelliaiti igtltaiavp syqgymlgsa rasataclle yaqfmervyt
       61 tnmtyatnng aatelptlqc sndlsdrfnf dldnlasrtf tltataksaq aaddctslsy
      121 nqagikgang gtgativkkc w
//
LOCUS       WP_008902810             360 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Acidovorax sp. NO-1].
ACCESSION   WP_008902810
VERSION     WP_008902810.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. NO-1
  ORGANISM  Acidovorax sp. NO-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 360)
  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 360)
  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 360)
  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 360)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Acidovorax sp. NO-1"
                     /db_xref="taxon:512030"
     Protein         1..360
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39791
     Region          1..354
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mdrrsairha giagvlatgl apavqaqpvv rwrlassfpk sldtiyggae vfaravrels
       61 ggrfevvvha agdlmpafgv leavqggqid lahtapyyfy aqnqafalgs aipfgfnarq
      121 mnawmlrgng rrlmdefyag ynivsfaggn tgtqmggwyl keirdvsdfk gmkmrlgggl
      181 vgevmarmga ipvdmpggei ysalqkraid aaewvgpydd qklgfnkvap fyyypgwweg
      241 gleldffvhr kafdalsaeh kaivnaassl ahadmlakyd alnpsalkql viaktkvlpf
      301 slpvldtafr tameifalne arspewkkiy tdmrnfqrdq ifwfrfaear ydsfmsaqri
//
LOCUS       WP_008902813             211 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit [unclassified
            Acidovorax].
ACCESSION   WP_008902813
VERSION     WP_008902813.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 211)
  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 211)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 211)
  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   4  (residues 1 to 211)
  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   5  (residues 1 to 211)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..211
                     /product="TRAP transporter small permease subunit"
                     /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=23244
     Region          3..171
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mqallkfsra idglnafvgk yviwlifaat avsainalvr kifgvssnaf leaqwylyaw
       61 sflaaagftl lhrehvridv vnsrlpkrvq vwidivgftl fltplcvlvl ylatplviqm
      121 yetgemsgnp gglvrwpvwv alpvgftllm lqgwselikr iaflrgqgpd pmgrlvekss
      181 eeelaellrq qqeeaaaaqa agatpsatpq r
//
LOCUS       WP_008903291             424 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Acidovorax sp. NO-1].
ACCESSION   WP_008903291
VERSION     WP_008903291.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. NO-1
  ORGANISM  Acidovorax sp. NO-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Magnet,S., Arbeloa,A., Mainardi,J.L., Hugonnet,J.E., Fourgeaud,M.,
            Dubost,L., Marie,A., Delfosse,V., Mayer,C., Rice,L.B. and Arthur,M.
  TITLE     Specificity of L,D-transpeptidases from gram-positive bacteria
            producing different peptidoglycan chemotypes
  JOURNAL   J Biol Chem 282 (18), 13151-13159 (2007)
   PUBMED   17311917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18654027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Acidovorax sp. NO-1"
                     /db_xref="taxon:512030"
     Protein         1..424
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=46757
     Region          157..298
                     /region_name="YafK"
                     /note="Murein L,D-transpeptidase YafK [Cell
                     wall/membrane/envelope biogenesis]; COG3034"
                     /db_xref="CDD:442269"
     Region          318..417
                     /region_name="DUF4440"
                     /note="Domain of unknown function (DUF4440); pfam14534"
                     /db_xref="CDD:434023"
ORIGIN      
        1 mlvprfahsh rvvagslama vllqaapala qgskkaqraa qaapaaaadl rdgeaearll
       61 avyrltaegr grealraaea lardyphfql aqlavgdllt artrpirrlg dlpepdsvrs
      121 ieaaatledl rtesrqrvda qrsrppanti ptqflelspr srhaiaidas rsrlylfens
      181 akglrlvady yasvgkmgie kslegdqrtp lgvyfitsrl dpatlkdfyg vgalpinypn
      241 pldlsrgktg sgiwlhgtps nqfaraplat dgclvlanpd lerilrtvep rstpvviarq
      301 lqwvapqaiq serksfdavl nawrdaktqg dlsrlmafya pdfqgqrnkp leqwaqvlha
      361 etralrgrel hlkdksylrw tdsadtmvvt fgevaegart gpvqrqywar rgqqwqiffe
      421 gvig
//
LOCUS       WP_008903706             708 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Acidovorax sp. NO-1].
ACCESSION   WP_008903706
VERSION     WP_008903706.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. NO-1
  ORGANISM  Acidovorax sp. NO-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Acidovorax sp. NO-1"
                     /db_xref="taxon:512030"
     Protein         1..708
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=74677
     Region          40..707
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 msaarwrrqg llaallagga caavqaqvpv pqgggnapga ltpalatvev idsaqaqrqf
       61 dsaashtsva vegfaattpl vhlsellagq agvvaqdrgn yaqdlqiavr gfgarstfgv
      121 rgvrvlvdgi pasmpdgqgq aatahlpsaa lvevlrgpla qlygnaaggv vqvttrdpqp
      181 ggaaqagvar gsyglrlvda sldvgaptlg glvsvshlet dgwrdhsaar rthvngklva
      241 rpdgrtrlta mlnlydqpla qdplgldllq fqsaprqvaa vatafdtrka vaqnqlgvvl
      301 erqlsptdsl qlrayggtrq ltqylsfsga gatsaggvvd ldrgyhgvgl awtralrtds
      361 glpltwtvgl eanrmsehrq gfvnqggtrg dlrrnerdsa antdlhaqld awitprwrav
      421 agvrasqvrv qvndrfitpa npddsgartw rhtspaaglv wsatdtlnly anvgrgfetp
      481 tlaemaysrs ntgpnfglsa arsrqwevga kwrgqnqqld lawfdtrsqg eivpvetvsg
      541 rsvfqnvdnv rrrglelawr asvgawthra sytyldayfg npfagaggaa vaagnrlpgt
      601 arhtallsad yaatarwqlg gtlhlaaavf andtntasap gyavaglhtg yqlgsaapgs
      661 trwqvwarvd nlfnrryagt livndgngrf fepaagrrlm vgvraqfl
//
LOCUS       WP_008903824             181 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Acidovorax sp. NO-1].
ACCESSION   WP_008903824
VERSION     WP_008903824.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. NO-1
  ORGANISM  Acidovorax sp. NO-1
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Acidovorax sp. NO-1"
                     /db_xref="taxon:512030"
     Protein         1..181
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=18142
     Region          1..177
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkrnlqkgft lielmivvai igilaavalp ayqdytirak vseglslasa aktavaetya
       61 nttqgtieay ggvgpitapa pgnttygyqy tagtnvatia iaetpvaapt atsgritity
      121 agtlgttlgn plvltpgsgt vtnsavpsav lvsgapvvwg cgiaatasfk yvpancrfnn
      181 l
//
LOCUS       WP_008903809             238 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SPOR domain-containing protein [unclassified
            Acidovorax].
ACCESSION   WP_008903809
VERSION     WP_008903809.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..238
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25802
     Region          128..191
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mlrlavivll lanagyyaws qgllkdwgfa peeqaepqrm nqqirpetlq ilrvnpsrta
       61 pssssqsaps gvavassnas sapsspsasd aaeclqagvf derqaetlra tlaplpqgsw
      121 qldptpipgr wmvymgrfdd letmdrkrae lrarkvdhdr aggtleygls lgrfsskeaa
      181 ereltnlank gvrtarvlqe rpdatgftlr lpavtdalrp qleplrtama gktlracs
//
LOCUS       WP_008904330             374 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [unclassified Acidovorax].
ACCESSION   WP_008904330
VERSION     WP_008904330.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..374
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=41566
     Region          1..368
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msieirnvsk qfgdfhalrd vsldiasgel iallgpsgcg kttllriiag letadvgtih
       61 fsgedttdvh vrernvgfvf qhyalfrhmt vfenvafglr vkprkerpse aqikqkvmdl
      121 lklvqldwla erfpsqlsgg qrqrialara lavepkvlll depfgaldak vrkelrrwlr
      181 rlhdelhvts ifvthdqeea levadrvvvi nqgrieqsgs pqqvwdqpas pfvygflgdv
      241 nlfhgraheg lvhldgmqid spehattqdt kafayvrphd ldveryspga gldaegrprg
      301 ivaqlsraiv vgpiarleli pegdhkpadn aspehlieaq ipaqqfkemg fkegetlvvt
      361 prrarvfldh aagi
//
LOCUS       WP_008904470             466 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Acidovorax sp.
            NO-1].
ACCESSION   WP_008904470
VERSION     WP_008904470.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. NO-1
  ORGANISM  Acidovorax sp. NO-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 466)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 466)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 466)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Acidovorax sp. NO-1"
                     /db_xref="taxon:512030"
     Protein         1..466
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=50625
     Region          2..419
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mqlsvyvlgr evatleqsgd fksvltyhph vaaddfvslt mpvrlesyvw ddqlppvlqm
       61 nlpegyllqv lqeqfgphig aspiallsvi grnmvgrlqv aasgaqlnep aqpievaall
      121 kgdnseaafa alvrqhatsg vsgvvpkfld aqttaasyqa etsprtvqae pveaphplra
      181 plaphpkasl ttrrhiikgs saqlpfvaln ehlcmqvarr vmpaaltevs ddgqalvvhr
      241 fdvdehgqpl wgmedfcsll glrpaakydt tweriakavr dhvpgaqrla tyrqlattll
      301 ltyalrnadc haknlallyt sranahlspa ydmlttsvya gfqhnppaid fmgkrtwapg
      361 knlqkfiaat fgiqpkeqqh mvqaisdava dvapqvrqam aqhpgfadig krmlmawaeg
      421 vqglrdarvy avgdwqagea fegfsappkl vspqekigrs pllgqr
//
LOCUS       WP_008904610             198 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Acidovorax sp. NO-1].
ACCESSION   WP_008904610
VERSION     WP_008904610.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. NO-1
  ORGANISM  Acidovorax sp. NO-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Acidovorax sp. NO-1"
                     /db_xref="taxon:512030"
     Protein         1..198
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21210
     Region          7..194
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 madaahtrrv ivaisgasga vygarllqvl qgqsgiethl vvsdagwrnl qheldmdraa
       61 vealahrvhd vanvgaaias gsfqchamvv apcsmrtlaa iahgladnll traadvalke
      121 rrrlvlmvre splhlthlrn mvaltemggi icpplpafyl rpqtvgevvd ysvaraldli
      181 dvqhdlaprw qglersap
//
LOCUS       WP_008904684             170 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Acidovorax sp. NO-1].
ACCESSION   WP_008904684
VERSION     WP_008904684.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. NO-1
  ORGANISM  Acidovorax sp. NO-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 170)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Acidovorax sp. NO-1"
                     /db_xref="taxon:512030"
     Protein         1..170
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=17765
     Region          15..138
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(20..23,56..58,61,88,132)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mttaraaapg lsspwvihcd gsawpnpgrm glgallvgpd gtvrhqisea ttftgcnnea
       61 elrallralq wlqgqaaaat tavqvfsdss vlveqlappa gaptlapiar laplfdeart
      121 vlqqfaqvnl qwvprhrnga adalaraalg lapkaatpag rvqrgkrrrr
//
LOCUS       WP_008907001             208 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Acidovorax sp. NO-1].
ACCESSION   WP_008907001
VERSION     WP_008907001.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. NO-1
  ORGANISM  Acidovorax sp. NO-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 208)
  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 208)
  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   3  (residues 1 to 208)
  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   4  (residues 1 to 208)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 208)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 208)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Acidovorax sp. NO-1"
                     /db_xref="taxon:512030"
     Protein         1..208
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22871
     Region          5..208
                     /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"
ORIGIN      
        1 mketlrivvv apdlavteag dehavlqaer sralriglle nnfnlvatlp advflseria
       61 qlqpdliivd aeseardale hvvmatrdar rpivmftndd dtshvkdava agvsayivag
      121 lapqrirpil dvamarfqhe qalraelada rtelkdrkti drakgllmqr qglteqaaye
      181 klrktamdkg lklgdvaqrm ldvmellg
//
LOCUS       WP_008907076             447 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Acidovorax sp.
            NO-1].
ACCESSION   WP_008907076
VERSION     WP_008907076.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. NO-1
  ORGANISM  Acidovorax sp. NO-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 447)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 447)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Acidovorax sp. NO-1"
                     /db_xref="taxon:512030"
     Protein         1..447
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=49047
     Region          39..412
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mnasctlqlf angawcdvgs vsllgpeaqg wrsktytgys vewaiehgga rdahafacrf
       61 pvglqafehp hwpvflidml pqgfgreell rrlglsvtag esvdwrllla gagnsvgnlr
      121 vkeaaswlaa nagplrgftd devaergddf aeylashglf vagssgvqge wpkilltrae
      181 dgllyldhtl pdararehyi vkfgrgsnea lasilrheap ymalarmlgl rvhadlvllk
      241 ralfiprfdr qvtgggvlrl gqesiatltg npgfdavpsh devcrqllrq cthplaevle
      301 yikrdvanla lgnkdnharn tavqrdfsgg irltplydfa pmylhpdgia rrirwegnds
      361 sapdwnrvid tvcemaqtlr dekrmssaqk kalrevcrpa lvdglrsmae plrkiaahgt
      421 dfglepavha hlklgieaqa qrltaln
//
LOCUS       WP_008907256             506 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase, partial [Acidovorax sp. NO-1].
ACCESSION   WP_008907256
VERSION     WP_008907256.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. NO-1
  ORGANISM  Acidovorax sp. NO-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Acidovorax sp. NO-1"
                     /db_xref="taxon:512030"
     Protein         <1..506
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
     Region          1..409
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 lksllpefeg kvkciyidpp yntgnegwvy ndavndpkik rwlgqvvgke gddlsrhdkw
       61 lcmmyprlkl lhrllhpegv lfvsidddea htlrlvldei fgrhgrlatf vwrtdgnfdn
      121 qakiknchey iymyskspda fpypsvvdpa tpadsklfrp virntvvkng tknppskitl
      181 pigfpadfea gtiarrtdkw phflnaakva gghltnevti ksgwssldml qafisngfkp
      241 lldrkqqetv frlmpsgaie svktrkpshv itvltgqgst qaasvdlaeh gitfsypkpr
      301 slvrylismi ddeecivlds fagsgttaha vldlnlqege rrrfilieme syassltser
      361 vkaaisgdvd tsdrpalggg fdyytvgepi flpdenlnea vgtdairayv aysegipsdd
      421 qttaenphsp yllglnreta wifhyepera trldmeflsg lrfgadtgar kpgtviiyad
      481 rcllsaafma khgiifkkip rditrf
//
LOCUS       WP_008908032             125 aa            linear   BCT 20-JAN-2025
DEFINITION  zinc ribbon domain-containing protein [Caloramator australicus].
ACCESSION   WP_008908032
VERSION     WP_008908032.1
KEYWORDS    RefSeq.
SOURCE      Caloramator australicus
  ORGANISM  Caloramator australicus
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Caloramator.
REFERENCE   1  (residues 1 to 125)
  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 12181465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Caloramator australicus"
                     /db_xref="taxon:515264"
     Protein         1..125
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14927
     Region          22..121
                     /region_name="zinc_ribbon_15"
                     /note="zinc-ribbon family; pfam17032"
                     /db_xref="CDD:465334"
ORIGIN      
        1 mffigiigie tkqyevkevs nvickkcgrm ssyklikqyn mfhfffipif kwniryflis
       61 rccesifeis mdygkelerq kapiiddnel telnfdygyl kkcpnclaei dthykycpyc
      121 ghkiy
//
LOCUS       WP_008908621             778 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: Lon protease family protein [Caloramator].
ACCESSION   WP_008908621
VERSION     WP_008908621.1
KEYWORDS    RefSeq.
SOURCE      Caloramator
  ORGANISM  Caloramator
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae.
REFERENCE   1  (residues 1 to 778)
  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 778)
  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 778)
  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   4  (residues 1 to 778)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Caloramator"
                     /db_xref="taxon:44258"
     Protein         1..778
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89520
     Region          65..776
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 makykklkye dlvvkldfvp dfktteeian yydligqera vqafemglkl dkpyyniyvc
       61 gtngsgrkkf vldklkqiak mqktpddwcy vynfndalsp lainlkggta eefksdietm
      121 ieslfeevpk mfsdeeyekq rediidyyqk etinildrly deaksknftv kstkegfvfi
      181 plidneemse iqyneleqse knkiaedvkt lkllalevlr ktkilrkema erlrkldeek
      241 sfelingkin kfinkysynd kivqylkdlq ndlinnidaf mqddentled dyfkkyyvni
      301 itcnkeegap viyeedpefn nligtieyen ykgalvsdft mikpgslhra nggylvidal
      361 qllstyqgwk alknalkngc isienlrnql eiipivslkp ekiplkikvv ligseflysl
      421 lyeydeefre lfsikaefds vikntpdnvn eflgfisyyc sqnniphvty kgflelykya
      481 lrlaeskkyf tarireiani idqsalicke rkgkhitdkd ikeaieklyk rhslykeril
      541 emykegkyii qlngykigei nalsvieled fafgkqnrit vttyrgkggv inierevkms
      601 gfihdkgvli ltgylgqmfg qkyplsfnas icfeqlyggi egdsasaael ialisslgdi
      661 pikqsiaitg svnqrgeiqp vgginekieg fydicklygl dgthgviipa snvgdlvlke
      721 eiieavrkgi fniysvsnie ecfeilcdek mvkdkkimdv irervenklk synegcpn
//
LOCUS       WP_008909286             396 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Caloramator].
ACCESSION   WP_008909286
VERSION     WP_008909286.1
KEYWORDS    RefSeq.
SOURCE      Caloramator
  ORGANISM  Caloramator
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae.
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
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 396)
  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   5  (residues 1 to 396)
  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   6  (residues 1 to 396)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 396)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 396)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Caloramator"
                     /db_xref="taxon:44258"
     Protein         1..396
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44295
     Region          20..113
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          80..384
                     /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 mkknmipgsf qlmkkintgl vldtirlyap isrveiskml nltpatvtni taellkrnii
       61 iesdfgkstg grkpvllkin pdsyyviavh igstklrvsv mnmeseiics lteklypnme
      121 fekvkdimid finqlikeyl peknkilgig vaahglvdfn ngtitfapnf gwkninlrei
      181 lerefdvpaf vdrdvramam aeswygegre vedficikvg ygigaafikd kqqlrgasdg
      241 lgefghmkve ingtkcicgn ygclenyase raivryamen gyrdeldiek iheevnkgnq
      301 kiidavkkag fylglgisnl inifnprliv iggdlidind lffdelllsa knyslqelfq
      361 nvnikrtqtg kdaitkgaal lvldnlfdsi qkevis
//
LOCUS       WP_008911191             289 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Providencia
            burhodogranariea].
ACCESSION   WP_008911191
VERSION     WP_008911191.1
KEYWORDS    RefSeq.
SOURCE      Providencia burhodogranariea
  ORGANISM  Providencia burhodogranariea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Providencia.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Providencia burhodogranariea"
                     /db_xref="taxon:516074"
     Protein         1..289
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32022
     Region          14..254
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 myqtnivant qtilgespiw sdarqsllwv dtlqgtllaf dpktsahtsy ptsapltfia
       61 enpekelivg igcqltrfdq qsnwqligla phsregyrln dakfdakgrl wcglmseqli
      121 ensgylysfd qngcwrtidt gftlingidw sqdnktmfvt dsikrviyay dfdlstgdvs
      181 hkriftqfsd tdgkpdglvv dadgyvlsvl fdgsaiaris pngddiqfcs lpvkrptscc
      241 fsengqvlyl tsarlglteq eliespasgt llkidyqkls eqlankplv
//
LOCUS       WP_008912378             338 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Providencia
            burhodogranariea].
ACCESSION   WP_008912378
VERSION     WP_008912378.1
KEYWORDS    RefSeq.
SOURCE      Providencia burhodogranariea
  ORGANISM  Providencia burhodogranariea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Providencia.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 338)
  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   5  (residues 1 to 338)
  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   6  (residues 1 to 338)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Providencia burhodogranariea"
                     /db_xref="taxon:516074"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38288
     Region          23..201
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <171..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkqrlndrik vpaalwigle kqgidlstll rqaqlplavf srqgeintrq yfslwqaicd
       61 laddvaigik lvkslptekl ppslldayha rdyrdalqrm arykrlcvpe hlqitedgdi
      121 crvefnwlht eqpeppalvd asmatlleig rlgtatpina rlvelvqakm dvsahqayfg
      181 cpvrlgaqrn clhlertslg lsfksynael ldlltpaldq qlaeyhskls fietvswllk
      241 rllsagrpei pavalelgvs ertlqrrlte egtnfqslla avrrsrayel ladpsldlme
      301 valllgyedq ssffrafklw enrtpsnwra mqqmtkmm
//
LOCUS       WP_008913092             295 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Providencia
            burhodogranariea].
ACCESSION   WP_008913092
VERSION     WP_008913092.1
KEYWORDS    RefSeq.
SOURCE      Providencia burhodogranariea
  ORGANISM  Providencia burhodogranariea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Providencia.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Providencia burhodogranariea"
                     /db_xref="taxon:516074"
     Protein         1..295
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33049
     Region          15..254
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mtfiiemads hcytlgespi wceknqrlff ldiieknlli ydpitgltqn relpyltsai
       61 tlttdhhkll litvngiyly diakdsleqk laeypdipcv trpneaaisp qgelffgtmg
      121 ylepekmgnw ykfchekqiv elcgqpvgis ntlcwvnqtl yfadsklnii yqsndqmktq
      181 qifahaergs pdgstlcven klwnarwgas elaiyslgnq attqidyisl painptsccf
      241 ggqdlttlyi ttaslgltvd dkwqgrvlai pfagkgkfmn rfklsningi kgise
//
LOCUS       WP_008915823             160 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Providencia sneebia].
ACCESSION   WP_008915823
VERSION     WP_008915823.1
KEYWORDS    RefSeq.
SOURCE      Providencia sneebia
  ORGANISM  Providencia sneebia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Providencia.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Providencia sneebia"
                     /db_xref="taxon:516075"
     Protein         1..160
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17607
     Region          1..151
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mdknkfyrel sdnlsallag eydliaslan tsallyerle gvnwvgfylk ngqelvlgpf
       61 qgkiacvrip ygkgvcgtay sqnkiyrvdd vhtfpghiac dsasnaeivl plevngqvlg
      121 vldidspnfn qfdqndeegl kylvsqlcqh ltmcsapnyh
//
LOCUS       WP_008925832             274 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [unclassified
            Pantoea].
ACCESSION   WP_008925832
VERSION     WP_008925832.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pantoea
  ORGANISM  unclassified Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="unclassified Pantoea"
                     /db_xref="taxon:2630326"
     Protein         1..274
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=30347
     Region          33..186
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkrglllila lllagchsgi esrdgywadl rhpaqgarpr vkvivihyta edfssslatl
       61 tdrevsvhyl iprqppqrag kgivwqlvpe qqlawhagps fwrgasrind tsigielvnr
      121 gyrrtltgle wqpftaaqii tlealvrdia qrygippeni vghsdiapqr kqdpgplfpw
      181 hqlaqrglga wpdagrvqfy lagqdphaqv pvqplmenlq rfgyaataem sareqqkvia
      241 afqmhfrpad yrgqpdaeta aiaaalleky gaae
//
LOCUS       WP_008925965             244 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Pantoea].
ACCESSION   WP_008925965
VERSION     WP_008925965.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  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   3  (residues 1 to 244)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..244
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27811
     Region          37..240
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mkeadqeqyl krgtlavlgv mkdllrlqtp llvrfprgqf isrmltadkd rvvfdlgsnn
       61 ldneyaltsd dlsitaetfg akvefsltsl ekiefeglpa fssplpdllw qiqrreffrv
      121 capmepqfwc htlwpdgskt rlrlqdlslg gigvlvdepl peglqngdsf nqfrvelgey
      181 gifevpvkll sigercvvnr knetlitprl sfrfatlnpa qerqlqqiif alerlardks
      241 trfq
//
LOCUS       WP_008927089             142 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Pantoea].
ACCESSION   WP_008927089
VERSION     WP_008927089.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..142
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15345
     Region          7..140
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 msdvltyasm fgssflsatl lpgssealli alliakktsv ygllvaaslg ntlggltnil
       61 igrllplkrq grwhdtamtw lhrlgpaall fswlpvigdl lcvlagwlrf awlpailfla
      121 vgktlryivi atatlqgmqw wh
//
LOCUS       WP_008926502             311 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein [Pantoea].
ACCESSION   WP_008926502
VERSION     WP_008926502.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..311
                     /product="formate/nitrite transporter family protein"
                     /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=33896
     Region          33..284
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mkpssgneqg pndveseekd kgtdievdee alpsraaaih eeirqdgeke lerdgmallw
       61 saiaaglsmg aslmakgifk vhldgvpgaf llenlgytfg fvivimarqq lftentvtav
      121 lpvmhkptwg ntglllrlws ivllgnligt algalafnem pifdeatrqa ftdismkvme
      181 ntpgemfana visgwiiatm vwmfpsagga kllvivmmtw lvalgdlahi vvgsvevlyl
      241 vfngsiswhe flwpfalptl lgnitggtli falishaqir ndmseaavak akaekrkqek
      301 rrqreekena e
//
LOCUS       WP_008927389             284 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Alcanivorax hongdengensis].
ACCESSION   WP_008927389
VERSION     WP_008927389.1
KEYWORDS    RefSeq.
SOURCE      Alcanivorax hongdengensis
  ORGANISM  Alcanivorax hongdengensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alcanivorax.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 284)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Alcanivorax hongdengensis"
                     /db_xref="taxon:519051"
     Protein         1..284
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=31185
     Region          44..>205
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mpltelvawf nreqrrqygq lvhtdtplrt sghevtgvya gftlrsefqa ifdsrtghpv
       61 afeallratt aqrtpvtpas vfsvpssaee viyldrlcrt lhalnfllqg geqkavltln
      121 vhprhvaavn tdhgqafesv lsqcglspsg ivlelssral hrpehlidav anyrqrgyqi
      181 aldgvrqvpd ishlqalqpd wvkfdptise lshnklrvll dsareglnqp akqvvlglsp
      241 splnrsivel vqanmaapaq prlhtrclpd vpvdarvaga irya
//
LOCUS       WP_008927420             340 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Alcanivorax hongdengensis].
ACCESSION   WP_008927420
VERSION     WP_008927420.1
KEYWORDS    RefSeq.
SOURCE      Alcanivorax hongdengensis
  ORGANISM  Alcanivorax hongdengensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alcanivorax.
REFERENCE   1  (residues 1 to 340)
  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 340)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 340)
  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   4  (residues 1 to 340)
  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 340)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Alcanivorax hongdengensis"
                     /db_xref="taxon:519051"
     Protein         1..340
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38161
     Region          29..211
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          255..336
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msqpqtdrlr paihptysrl lcahlqqlgf dnatifagtr lhweqllseh rylsleqlgr
       61 lihravdltg qpwigldigg mtavsahgsl gyavvsapdv rtvlevvtry vgvrlrltei
      121 aleetdsgva lvlhermdla etrefihggl latyfqlvdt vssrrlrdar vslpfeappw
      181 aavyeerlgc pvtfgaprfr ielsaatlat pcltadpalh rtavrdcehq lrqlqgggpl
      241 sqqignclle stdypsleam adrfamsrrt lirklkaegt syqelldevr relaawylle
      301 thepiervae rlgyqdtsnf srtfrrwfgv tplamrnras
//
LOCUS       WP_008928073             115 aa            linear   BCT 20-JAN-2025
DEFINITION  PilZ domain-containing protein [Alcanivorax hongdengensis].
ACCESSION   WP_008928073
VERSION     WP_008928073.1
KEYWORDS    RefSeq.
SOURCE      Alcanivorax hongdengensis
  ORGANISM  Alcanivorax hongdengensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alcanivorax.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 115)
  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   3  (residues 1 to 115)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Alcanivorax hongdengensis"
                     /db_xref="taxon:519051"
     Protein         1..115
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12393
     Region          1..115
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mkmpggrsgi lsltikdkav lysaympfit ngglfiptdk qyklgeeifl llnimdeadk
       61 ipvagkviwi tpkgaqgnrs agigvqfsdq ddtarvtien hlagslesdr pthtm
//
LOCUS       WP_008928371             341 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Alcanivorax hongdengensis].
ACCESSION   WP_008928371
VERSION     WP_008928371.1
KEYWORDS    RefSeq.
SOURCE      Alcanivorax hongdengensis
  ORGANISM  Alcanivorax hongdengensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alcanivorax.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 341)
  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 341)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Alcanivorax hongdengensis"
                     /db_xref="taxon:519051"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37765
     Region          23..209
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          257..335
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtdlgeicsa alkqylahgd aigldtaaal dhaglpeelv qqpearlpgr afqqllenli
       61 qqsadplfgl htsafiqpgs ynvigyiams agtllealsk vslyerlvgd mgttetrldn
      121 dqamiiwscc ypaparrhlv envlsswlcy arwltaneql apsqvwlehs apqdpallae
      181 yrrvflcdvl fdqpcsalvg dsgllahplt qpdplllstl eahaverlnq lgvatslsqr
      241 vrqciddamg rtlprkdqva erlgmnirtl hrrladeqvt wqqllddvrl qharqllqtt
      301 qlpqseiaea lgysdirsfq rsfkrhtgqt pgqfrsrpaa l
//
LOCUS       WP_008928948             329 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Alcanivorax hongdengensis].
ACCESSION   WP_008928948
VERSION     WP_008928948.1
KEYWORDS    RefSeq.
SOURCE      Alcanivorax hongdengensis
  ORGANISM  Alcanivorax hongdengensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alcanivorax.
REFERENCE   1  (residues 1 to 329)
  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 329)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 329)
  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   4  (residues 1 to 329)
  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 329)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Alcanivorax hongdengensis"
                     /db_xref="taxon:519051"
     Protein         1..329
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35820
     Region          23..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          258..329
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mankkqaaal lmgpllhllh ergvdgeail rrhgldpmmv rdpearldaa vstallddsl
       61 aalgdpamai daarhaqynt fgalglavaa ggdlhsvlnr itrfhrlisd lvsteltvdd
      121 rtvalhfass tdhqphpqai afvmasivrl lriridrdhn pvavaapawm dpalrsalar
      181 ycrcpvtesd syslafdkan aqqmlaasdt qlaamldatl sqrlaesehg slasrltlwi
      241 eqrlpdgepa qadaaaalcl strslqrrla deglswkkll eetrkmlver hlrtpgmtvt
      301 qmafllgfsd vsafsrafkk wygvspsqf
//
LOCUS       WP_008928902             338 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Alcanivorax hongdengensis].
ACCESSION   WP_008928902
VERSION     WP_008928902.1
KEYWORDS    RefSeq.
SOURCE      Alcanivorax hongdengensis
  ORGANISM  Alcanivorax hongdengensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alcanivorax.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 338)
  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   5  (residues 1 to 338)
  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   6  (residues 1 to 338)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Alcanivorax hongdengensis"
                     /db_xref="taxon:519051"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37859
     Region          30..209
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          89..338
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtilkmdpse yaisaeylal llevlgrrki apeavldgtd iapgswrdpq mritardyek
       61 vveravaltg epwlgwelga smtlsshgfl gyaamssatl gealdlavky frtrttlvql
      121 evfqdgdhav lqidemlalg vlapmmmesl fssfhfmgmk llpdmeiige lrfsypepdy
      181 fqslrplipv pvyfdcatnq mrfpverlny slrfadprla rmaaaqceqe masikappal
      241 lgkvrriils gagrfpgvde vatemhmssr tlkrklqqlg tsyqtvlddl rkglaveylt
      301 qsdktvdeia malgysdasn farafrrwtq rspsdyrq
//
LOCUS       WP_008929084             107 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Alcanivorax hongdengensis].
ACCESSION   WP_008929084
VERSION     WP_008929084.1
KEYWORDS    RefSeq.
SOURCE      Alcanivorax hongdengensis
  ORGANISM  Alcanivorax hongdengensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alcanivorax.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Alcanivorax hongdengensis"
                     /db_xref="taxon:519051"
     Protein         1..107
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11755
     Region          1..102
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(5..6,24..25,33,36,38..39,41,44..45,47,55,60,68)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(24,55..56,58,83)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mnptfreavy qivaaippgs vssygqvarq agfprhgrfv grllsqlpaq trlpwhrvlr
       61 gdghialagt pggeeqcrrl qaegvvvlgq rvamkryqwq pdavreq
//
LOCUS       WP_008929614             320 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Alcanivorax hongdengensis].
ACCESSION   WP_008929614
VERSION     WP_008929614.1
KEYWORDS    RefSeq.
SOURCE      Alcanivorax hongdengensis
  ORGANISM  Alcanivorax hongdengensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alcanivorax.
REFERENCE   1  (residues 1 to 320)
  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 320)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 320)
  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   4  (residues 1 to 320)
  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 320)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Alcanivorax hongdengensis"
                     /db_xref="taxon:519051"
     Protein         1..320
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35759
     Region          27..197
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          245..318
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mphtptvtvr ftqaisqaar rlgfalpddl qeafadrprv dlelqdriwe tfcqqasdpl
       61 vglqlgleiq vghldtvgmv lmscetvaea ldslldyhpi vgeggdfdyr vegercaidy
      121 rphfhtrqae rveavmasll nlsrwttger lhplgislah galddaaryt qrlgvpvefn
      181 rdrntlwipa sdlqlpliha npalcqhlrt ladqvleqlg sqslsaqvrd llrqhphwgk
      241 ektgeklnms grhlvrklse egtsfkllrd allqnmaeqa lgrgerpgev aeqlgfsdes
      301 afskafkrwt gktpaqfrtt
//
LOCUS       WP_008929831             341 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Alcanivorax hongdengensis].
ACCESSION   WP_008929831
VERSION     WP_008929831.1
KEYWORDS    RefSeq.
SOURCE      Alcanivorax hongdengensis
  ORGANISM  Alcanivorax hongdengensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alcanivorax.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 341)
  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 341)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Alcanivorax hongdengensis"
                     /db_xref="taxon:519051"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37909
     Region          26..206
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          250..331
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mnglqgsals vtyvrqladq lqdmqvdvag wlnghgfslq dlehaeklms welfcplleq
       61 alaltgepal gllfgqrlrv nshgivgyaa mnsssvrevl qvvsrflplr iglvtmrlve
      121 qgryldlrie esrplgalqp qvvgaivaal kngidfislg rcqlarvkfv spplaagadt
      181 lldcpvsyrq pwsglsmlve qadqplsngd peafrqacql ceremgrmrs qtsvraqvra
      241 lmlsrqpafp slpetaaalh mttrtlhrrl qeeqvtfqei ldgmrrglam eylrqrditi
      301 kelgytlgyh dtanfrrafk rwtglsplqf rqaspgrlpg p
//
LOCUS       WP_008930522             420 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Alcanivorax
            hongdengensis].
ACCESSION   WP_008930522
VERSION     WP_008930522.1
KEYWORDS    RefSeq.
SOURCE      Alcanivorax hongdengensis
  ORGANISM  Alcanivorax hongdengensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alcanivorax.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 420)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 420)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Alcanivorax hongdengensis"
                     /db_xref="taxon:519051"
     Protein         1..420
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=45483
     Region          3..411
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 misdkayiwi flpgqtepvv cgvvawdgse yvfrygksyl aranaiplsi pgrplgeltg
       61 dpyvldnels galrdaspda wgrriiqrei gkalnpagqp dnaidsepge idyllgagad
      121 rigaldtser pdvylprvkq aspladaqka agqmergeal nddldaalnh gtsiggarpk
      181 vlfrqgkeyw vakfsssrdt inmiaaehga mrlaaeaglr vaptqvldis gkgvllvrrf
      241 draihasgtl trrhmlsamt lmnldeyavr ageasyltla dvlrkyardf qrdgrelfrr
      301 mvfniligni ddharnhacf wdgqaleltp aydvcpqprl gysadlamiv gslgraatln
      361 naisqaerfg landeaaeci daltqtvatr wentfsaagl aagdieylak atlmspsild
//
LOCUS       WP_008931247             113 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Ectothiorhodospira].
ACCESSION   WP_008931247
VERSION     WP_008931247.1
KEYWORDS    RefSeq.
SOURCE      Ectothiorhodospira
  ORGANISM  Ectothiorhodospira
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 113)
  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   3  (residues 1 to 113)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 113)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Ectothiorhodospira"
                     /db_xref="taxon:1051"
     Protein         1..113
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12254
     Region          1..113
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mapgqgilsl aikdkhslya aympyvkngg lfiptqklyk lgdevfmllt lmeereripv
       61 agrviwvtpp raqgnrtpgi gvqfnaqdkg aarnkiegll ggalqsdrlt ntm
//
LOCUS       WP_008931304             194 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Ectothiorhodospira sp. PHS-1].
ACCESSION   WP_008931304
VERSION     WP_008931304.1
KEYWORDS    RefSeq.
SOURCE      Ectothiorhodospira sp. PHS-1
  ORGANISM  Ectothiorhodospira sp. PHS-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Ectothiorhodospira.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Ectothiorhodospira sp. PHS-1"
                     /db_xref="taxon:519989"
     Protein         1..194
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21429
     Region          3..164
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mrlfgplydr vmgwsrhrha prylaalsfa essffpvppd vmlapmaaar phqglylafi
       61 ttlfsvlggv lgymlgylaf gmlepvivna gygeelslaq ewftvwgvwv vlvagfspip
      121 yklftitaga lsmallpfii asflgrgarf favalliswl gprvepklrp yiewlgwltv
      181 vclllavaly qwlg
//
LOCUS       WP_008932050             360 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Ectothiorhodospira sp.
            PHS-1].
ACCESSION   WP_008932050
VERSION     WP_008932050.1
KEYWORDS    RefSeq.
SOURCE      Ectothiorhodospira sp. PHS-1
  ORGANISM  Ectothiorhodospira sp. PHS-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Ectothiorhodospira.
REFERENCE   1  (residues 1 to 360)
  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 360)
  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 360)
  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 360)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Ectothiorhodospira sp. PHS-1"
                     /db_xref="taxon:519989"
     Protein         1..360
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39701
     Region          1..357
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mhrrdflgka altalaagga ltgcgipqgs etsapdtgrr fhwrmitawp hespglggga
       61 qllartlhel sdgriqvrif aaddlvspfe ifgavsrgaa eighgaahyw qglsgaaqff
      121 tavpfgmgal etqawlhagg glelwrdlyr pfdvipfpcg ntgaqmggwf rreirtiedf
      181 rglriravgl gaevlrraga evirlpgddl peamqsglle aaewmgpyed malglhrqap
      241 yyyhpgwqap gsqvealinr dayealpqhl qiavaqacrl ageqmihefl arnqqtldrl
      301 vsehgvqlrr fpdtvldglr rltqdmllem taddpfirrv hasymgfese mvrwkeihsi
//
LOCUS       WP_008932484             211 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Ectothiorhodospira sp. PHS-1].
ACCESSION   WP_008932484
VERSION     WP_008932484.1
KEYWORDS    RefSeq.
SOURCE      Ectothiorhodospira sp. PHS-1
  ORGANISM  Ectothiorhodospira sp. PHS-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Ectothiorhodospira.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Ectothiorhodospira sp. PHS-1"
                     /db_xref="taxon:519989"
     Protein         1..211
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23029
     Region          65..136
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mrllffllll lnlayllygl arhapetppd ptvwqqpegi pmlrllregg vaaedvipdv
       61 gqaacvslgp fgtpqaaapl qarllgegla phvrpmtesr plsywvvlep vdgragaraa
      121 itlltargmn dhyiitegph rdglslglfs eharalrrle qvrgiglepi ietryrevsf
      181 ywvdvnaslp migalslelp egvfpverdc p
//
LOCUS       WP_008933122             211 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Ectothiorhodospira sp. PHS-1].
ACCESSION   WP_008933122
VERSION     WP_008933122.1
KEYWORDS    RefSeq.
SOURCE      Ectothiorhodospira sp. PHS-1
  ORGANISM  Ectothiorhodospira sp. PHS-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Ectothiorhodospira.
REFERENCE   1  (residues 1 to 211)
  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 211)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 211)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Ectothiorhodospira sp. PHS-1"
                     /db_xref="taxon:519989"
     Protein         1..211
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22991
     Region          3..202
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 msyatdeerv eaikrwwken gtavilglvv glggvvgwrl wtghvesrav daseiymamv
       61 saarqgseia hdhgttlmeg yrktpyaala alelarlave rddlvlaegr lrwamaqart
      121 pemvqvartr larvliadgr aqdaltlled pvpegflalv eelrgdahra lgdhararaa
      181 ydramlisgg lsdylqmkrd alntpvevtg s
//
LOCUS       WP_008933317             127 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Ectothiorhodospira sp. PHS-1].
ACCESSION   WP_008933317
VERSION     WP_008933317.1
KEYWORDS    RefSeq.
SOURCE      Ectothiorhodospira sp. PHS-1
  ORGANISM  Ectothiorhodospira sp. PHS-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Ectothiorhodospira.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Ectothiorhodospira sp. PHS-1"
                     /db_xref="taxon:519989"
     Protein         1..127
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=13799
     Region          1..127
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mqkfrytkgf tlielmivva iigilasiay psytryvert qvsdgktall mlaqqmercy
       61 tarlsynncp nlatespegf yaltvnadat tftltatgqk grvtsgscna ltinhlgert
      121 pagdacw
//
LOCUS       WP_008934009             277 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Brucella sp. NVSL
            07-0026].
ACCESSION   WP_008934009
VERSION     WP_008934009.1
KEYWORDS    RefSeq.
SOURCE      Brucella sp. NVSL 07-0026
  ORGANISM  Brucella sp. NVSL 07-0026
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Brucella sp. NVSL 07-0026"
                     /db_xref="taxon:520448"
     Protein         1..277
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30592
     Region          1..275
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mnqnethcla llreadrdry lsvlyapqek rgalaalyaf naeiarirdl vheplpgevr
       61 lqwwrdling eargsaeahp vaaalietie kyelpriafd nycearvfdl yddpmpsrnd
      121 legycgetas aliqlagfil drdaaqahae taghagvaqa vagllrllpi hrrrgqvyvp
      181 admlkaigvt rdmllssedk sateravtim lalarehlai fdkakaglpq mlhpaflpma
      241 lvpaylnave rlgaqaaqkv adisairkqw lmfranf
//
LOCUS       WP_008935262             312 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Brucella].
ACCESSION   WP_008935262
VERSION     WP_008935262.1
KEYWORDS    RefSeq.
SOURCE      unclassified Brucella
  ORGANISM  unclassified Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
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
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="unclassified Brucella"
                     /db_xref="taxon:2632610"
     Protein         1..312
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=34401
     Region          1..309
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 miefdritkn yngraavdev sftiephsia aivgtsgsgk ttllrmvnrl eeptsgeiri
       61 dgqsildepg helrrrigyv iqqhglfphr tvgeniatvp vllgwqkqri earvdellel
      121 fqlepdayrd ryphelsggq qqrvgvaral aagpnillmd epfgaldpvi rakaqedlka
      181 iqrrfgttil lvthdmeeai slgdriavmd egkllqfgpp aeilarpate fverlvgtge
      241 rpfrllsltd lktvlqpgda sgeplpvtas qrdalaellw sgrralpvld edgrslgrvt
      301 lekllhqaer pa
//
LOCUS       WP_008935341             372 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [unclassified Brucella].
ACCESSION   WP_008935341
VERSION     WP_008935341.1
KEYWORDS    RefSeq.
SOURCE      unclassified Brucella
  ORGANISM  unclassified Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 372)
  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 372)
  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 372)
  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 372)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="unclassified Brucella"
                     /db_xref="taxon:2632610"
     Protein         1..372
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40663
     Region          38..363
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mketlsrrsf ltkgaaigaa aatsgaalat paiaaelptl rwrltsgfpn nldtiyggav
       61 ymadavskmt dgkfqiqvfq ageivpgpqa idavqantve mahtcgyyft gknptfaigt
      121 alpfgmntrl qnawlyhggg nelyneflsd ygivgivggn taaqmggwyr keiksvedlk
      181 glkmriagva gevmsrlgvv pqqlpggdiy pslergtida aewvgpydde klgfyqiapy
      241 yyypafwegg asvhffinkk qyeslpeayk valntaaeaa tqnmialydv kntaairslv
      301 skgvklqplp rdvldaaykv sfdlyaeyne knpawakiyp awkkfrdegf ewfrvaeyty
      361 dsyvyaaqaa gk
//
LOCUS       WP_008935903             682 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter permease [unclassified Brucella].
ACCESSION   WP_008935903
VERSION     WP_008935903.1
KEYWORDS    RefSeq.
SOURCE      unclassified Brucella
  ORGANISM  unclassified Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 682)
  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 682)
  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 682)
  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 682)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="unclassified Brucella"
                     /db_xref="taxon:2632610"
     Protein         1..682
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=72993
     Region          16..681
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mteeqnakla pmeldevkar eleekfdsei rfrplapvaa rivgtlliil slfhyytagf
       61 gllpemihrg ihlafvlglv flvfpfsrkg ydepakpsll rplgisvidw glaiiavvav
      121 ihvplipldd lafrvgnpts tdivlgslli lilleatrrs vgwplpiisv lfmlyalygp
      181 smpgilvhpg atvsqlvdhl ylttqgiygi algvvatyvf hfvlfgvfat riglgqlfld
      241 caawvagrfa ggpakvsifg salfgmisgs svanavtvgs ltipamirlg ykrhfaaave
      301 sasstggqit ppimgaaafl mieflnlpyt tiilaaivpa fmhffgvlmq vhfeakrtgl
      361 rgmtkeempd lkealkrdwp tiiplvvlia vllsgytpyl aafwgitlci avgllnprkr
      421 mtigevfegl rdgakyalav gaaaatvgii vgvvtltgvg fkisyivtst aaqlatyfgt
      481 ilpvswfapq tltllftlvm tgmvcilmgc gipttanyii matiaapalg llgvepivah
      541 ffvfyygvla ditppvalaa yaaagmagad pfktgntafr lglgkvlvpf vfvfspslll
      601 vtsnfnwpdf fiaffgcvig italgaalsg fflvrtkiwe nvllifaaml lvapeiyssi
      661 vglilllpvi vrhlvasrrp ay
//
LOCUS       WP_008936089             253 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Brucella].
ACCESSION   WP_008936089
VERSION     WP_008936089.1
KEYWORDS    RefSeq.
SOURCE      unclassified Brucella
  ORGANISM  unclassified Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
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
REFERENCE   2  (residues 1 to 253)
  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 253)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="unclassified Brucella"
                     /db_xref="taxon:2632610"
     Protein         1..253
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28324
     Region          22..77
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msgarpfrdv klqwlqqlsc dkdlsdgars valyivtthl nghtekawps yqtiadatgk
       61 svktiqravr elevkgwfev qrgngvghnt eyrpsaasil rasdarektd kvvtlypdkg
      121 gqirperrsd vsseggqicp pnlekekink pnpregatpr vetrravplv fvaetkadqv
      181 eqwrswlrrh gfpsidalgl rtgktrkpgy alpgywppdd aspsaldwia ffsrrrdhia
      241 deparqsdlr ras
//
LOCUS       WP_008936097             440 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [unclassified Brucella].
ACCESSION   WP_008936097
VERSION     WP_008936097.1
KEYWORDS    RefSeq.
SOURCE      unclassified Brucella
  ORGANISM  unclassified Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 440)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 440)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="unclassified Brucella"
                     /db_xref="taxon:2632610"
     Protein         1..440
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48401
     Region          2..423
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mrltlqthfd gewhhaatle lkddaagfqg asivdydldy fvtvalaefs agktvrdhra
       61 lsvhypvdle nrysrswppf lldimpqgha rrklaehlgl tegsrasdlp lllrsatggi
      121 gnirikeaad aeaerlsgve rqgvagaeil ersdrfmeva drfgmlasgs sglqgewpkv
      181 smtlanngly ypdsfvtdde amrhvivklv rsnepadrli legealysri aqeiglnvse
      241 pstyaegvli iprfdrtkre gggtvrlgqe slvsavgvad fghvgtheay idvlrqysad
      301 pfadiveylk rdianlalgn pdnhgrnsal skhqdgtirl splfdfapmr lakegivrst
      361 rwammrdggr dhlpdwkric aelmpdpaeh kalaaalsef aerlrhapdm andmgtspei
      421 leramgrcve iadsvlatcq
//
LOCUS       WP_008937671             367 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Marinobacter
            santoriniensis].
ACCESSION   WP_008937671
VERSION     WP_008937671.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter santoriniensis
  ORGANISM  Marinobacter santoriniensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 367)
  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 367)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 367)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 367)
  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   5  (residues 1 to 367)
  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   6  (residues 1 to 367)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Marinobacter santoriniensis"
                     /db_xref="taxon:523742"
     Protein         1..367
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41161
     Region          32..214
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          105..347
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mprnqdathr nalgdismly vsvllraaee egadarglal qfgldetgla spearisipr
       61 fmrmghaair dsgnpalglr mgalsrpvda glagiaaeta ptvsqalrtl iryslltsqn
      121 srgrpsiepe rrtvhfysir pynpynyfvv dsvlaawtqf artltgrydl lekvsieyrs
      181 nglddlfesw frcpvefgag gnsltfkesa wrqpsnqahp amheqlgrlc eqelenirrg
      241 wqmsdrvrhl mtpmfrgetp slervaarlg mtpwtlqrhl asegtgfrql ldktrqqlae
      301 dylretdssl seiawllgfa nppafhkayq rwfgispger rkqlrqavnn nlppeqiqss
      361 vasstks
//
LOCUS       WP_008937749             339 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Marinobacter
            santoriniensis].
ACCESSION   WP_008937749
VERSION     WP_008937749.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter santoriniensis
  ORGANISM  Marinobacter santoriniensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 339)
  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 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 339)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 339)
  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   5  (residues 1 to 339)
  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   6  (residues 1 to 339)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Marinobacter santoriniensis"
                     /db_xref="taxon:523742"
     Protein         1..339
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38924
     Region          22..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          102..337
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msnltvsrhf vqaalvgaea qgldtramlr dagispdllr iemarvssdq fsrlmqilwn
       61 rtgdefmgmg prkartgtfa tmgalvidcp tleavyrray qfsrlfepmv tmelevgeet
      121 arlvlriegd ifdpsfflre silviwhrlg swligqpvel dcaefdysrp dhgdeyrhif
      181 hcplrfeare taltfdkrfl sapvirdqpe mhqflktspa dllsrpdesn twtgrirali
      241 grdfsrplpd fesiaaelht spqtlrrrlk qentsfqeik dllrrdmaiy ylsrqewain
      301 diaakvgfte pstfhrafkk wtgvtpgayr egersspdr
//
LOCUS       WP_008938763             166 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Marinobacter santoriniensis].
ACCESSION   WP_008938763
VERSION     WP_008938763.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter santoriniensis
  ORGANISM  Marinobacter santoriniensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 166)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Marinobacter santoriniensis"
                     /db_xref="taxon:523742"
     Protein         1..166
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=18365
     Region          13..154
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cl49639"
                     /db_xref="CDD:483979"
     Site            order(109,123,126,139..142,144)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mtfpdpniac lsisltdqtl svldpqdrvl tryavstgln gpgeqdgsgc tprgmhyira
       61 miggdlpent vfrarrptge iyspalaenq perdwilsri iwlcglepgr nrggrvdtfr
      121 rfiyihgtpd sepmgvaash gcirmrnrdv ielftrvrpg vrvsiq
//
LOCUS       WP_008938798             704 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Marinobacter santoriniensis].
ACCESSION   WP_008938798
VERSION     WP_008938798.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter santoriniensis
  ORGANISM  Marinobacter santoriniensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 704)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 704)
  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   3  (residues 1 to 704)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..704
                     /organism="Marinobacter santoriniensis"
                     /db_xref="taxon:523742"
     Protein         1..704
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=75355
     Region          6..701
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          <110..>294
                     /region_name="PHA03169"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:223003"
ORIGIN      
        1 mafdadeeil qdflveagei leklseqlvd leqhpddsdl lnaifrgfht vkggagflql
       61 dalvncchsa envfdilrnh krkvdaelmd vvlealdnvn amfeevrnhe eptpapdeli
      121 aaldalakpe gtggsatadt pasepastsa dadggditdd efeqlldale ggdqndqsas
      181 sapvndesag keggddeitd defeklldel hgegkfsgap padaapekps tegadgkpgs
      241 gseddlitdd efeklldelh gkggaptgad sadggqspak sqpkpesasr pepetarepa
      301 apkaaakpat ppreaapage ttvrvdtkrl ddimnmvgel vlvrnrlqrl gnasedeqmh
      361 kavanldvvt tdlqsavmqt rmqpikkvfg rfprvvrdla rslkkevslv mhgeetdldk
      421 nlvealsdpl vhlvrnsvdh giespdvrek agkpragtvt lsaeqegdhi lltieddgag
      481 mdpeklrqka vekgiydqda adrltdnecf nlifaagfst kdqisdvsgr gvgmdvvktk
      541 igqlngqini vselgkgtri likvpltlai mptlmimlgd qsfalplvnv veifhldltk
      601 tnivdgreci vvrdkvfplf hikrwlvrge agqaepenah vvivamgtkq vgfvvdqlig
      661 qeevvikplg ralqgtpgma gatitgdgri aliidvpsll qnys
//
LOCUS       WP_008938911             149 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Marinobacter santoriniensis].
ACCESSION   WP_008938911
VERSION     WP_008938911.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter santoriniensis
  ORGANISM  Marinobacter santoriniensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Marinobacter santoriniensis"
                     /db_xref="taxon:523742"
     Protein         1..149
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=15284
     Region          7..148
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkkmqinhaq kgftlielmi vvaiigilaa iaipqyqdyi artqvnrafg eiaslktave
       61 erlsrgitta tlgdlgytgs nlttetttsn anfpggvgsl vatmgqnaat gitgatitls
      121 rtadgvwsct vaangatawd ssfvpagcn
//
LOCUS       WP_008939266              89 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Marinobacter santoriniensis].
ACCESSION   WP_008939266
VERSION     WP_008939266.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter santoriniensis
  ORGANISM  Marinobacter santoriniensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 89)
  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   2  (residues 1 to 89)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Marinobacter santoriniensis"
                     /db_xref="taxon:523742"
     Protein         1..89
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9202
     Region          21..87
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkrtpiiatl vllfslfsgf aqaegeavni ntadvatlas lngigdskaq aivsyreshg
       61 pfasaedlal vkgigartve knaerltvk
//
LOCUS       WP_008939200             337 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Marinobacter
            santoriniensis].
ACCESSION   WP_008939200
VERSION     WP_008939200.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter santoriniensis
  ORGANISM  Marinobacter santoriniensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 337)
  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   6  (residues 1 to 337)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Marinobacter santoriniensis"
                     /db_xref="taxon:523742"
     Protein         1..337
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37644
     Region          21..208
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          116..335
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mssliratnl wgydelvrsk ggdplpllar yrippeeqrd dqsflvfrhl tallddtane
       61 lgdpafgmml aryqgmdilg pisviarssl tvgeainsia rylhlhcpal sltmsrvtmn
      121 desvirfvft idgegggyra qshelslana mqvmtllcgd gfaplavyfi harladesvy
      181 rkvfrcdaff eqdwcgfylp asvasmplps adhqtwqlar ryldaqqapn antltedvir
      241 lintllptgq ctsdaiaahl slhkrtlqrr lalegttyeq llnnertrla rqylrepdmg
      301 fgqisgllgy seqsafnrac rswfgltpkg yrkqllg
//
LOCUS       WP_008939439             236 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Marinobacter
            santoriniensis].
ACCESSION   WP_008939439
VERSION     WP_008939439.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter santoriniensis
  ORGANISM  Marinobacter santoriniensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 236)
  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 236)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 236)
  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   4  (residues 1 to 236)
  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   5  (residues 1 to 236)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Marinobacter santoriniensis"
                     /db_xref="taxon:523742"
     Protein         1..236
                     /product="TRAP transporter small permease subunit"
                     /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=27396
     Region          69..225
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mselsgfgfv lphwfywgwl avmplimmaw drwsskrgtq aidknalane klqeieaems
       61 ktiesdyenr ftrvidwisd ksgifisfwt vnavvfyffe vvmrylfnmp tiwvheasfl
      121 lfgmqyllag afamlhgahv rvdviynllp vrgrigmdif tsmfffmfsl gltitswtff
      181 qnsysmdert vetwqiqywp vkammllgai litlaglskl vkdialfvkl greqqa
//
LOCUS       WP_008939950             315 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Marinobacter santoriniensis].
ACCESSION   WP_008939950
VERSION     WP_008939950.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter santoriniensis
  ORGANISM  Marinobacter santoriniensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
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
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Marinobacter santoriniensis"
                     /db_xref="taxon:523742"
     Protein         1..315
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=35200
     Region          1..315
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mielkhvtrr fgnavavdni dltietgevc vlvgssgcgk sttlrminrl lprtegeilv
       61 dgediatmnp eqlrlnmgyv iqgtglfphw tvarniamvp qllkwpreri darvhelmtl
      121 ldldpsthan kypqqlsggq aqrvgvaral aadpnillmd epfgaldait renlqlemlr
      181 iqkqvrkttv fvthdideal klatriavmd qgriiqhdtp enilrrpate fvenlvgkqd
      241 rglklmslrr vrelmqahpa pkrpepgveg lreedslrla lsvmlwqdap qvpvfnsrge
      301 etgvitreri vqega
//
LOCUS       WP_008940145             212 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Marinobacter
            santoriniensis].
ACCESSION   WP_008940145
VERSION     WP_008940145.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter santoriniensis
  ORGANISM  Marinobacter santoriniensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 212)
  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 212)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 212)
  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   4  (residues 1 to 212)
  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   5  (residues 1 to 212)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Marinobacter santoriniensis"
                     /db_xref="taxon:523742"
     Protein         1..212
                     /product="TRAP transporter small permease subunit"
                     /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=23279
     Region          33..198
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mtvsdqgspq nprasiddpd eflhhhtelp ttrlsqwidg lltaigkgas wawvivtgfi
       61 iyavvgryaf ghgsvlleel ewhfagagwl lgmaytlvvd dhvrvdvlhe rfslrtqgwv
      121 elfgllvlll pflglaiyem vpyainaynv getsqapagl snrwvlkavl alafmliama
      181 avsrllkvta llfglprpir vqsdnakked vs
//
LOCUS       WP_008940569             351 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Marinobacter
            santoriniensis].
ACCESSION   WP_008940569
VERSION     WP_008940569.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter santoriniensis
  ORGANISM  Marinobacter santoriniensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 351)
  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 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   3  (residues 1 to 351)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 351)
  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   5  (residues 1 to 351)
  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   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Marinobacter santoriniensis"
                     /db_xref="taxon:523742"
     Protein         1..351
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39525
     Region          29..213
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          104..342
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mnapgitgnl piirahyadi lcqlaeelgv drrrllaesg irpallghpd nfitldqftn
       61 lcraalsrtg daalglafgl rlkftthgsl aqaaiscdtl aealqvliky frtrfvymel
      121 tfieegneav lqldpghdve dlyrfnvdvv maslmdvnql lfgnrlistg wckvnyppps
      181 dlepyrrlfg dqiefsagan qlrfdrrlls lpmslsnpvt rrvaeaqcee emrsieaatt
      241 iaarvtrile svrdgrlpgl eavaeqlsls trtlrrqlas egvrfqdlqd dlrhrralel
      301 lrrreltide vaeavgysdp snfgrafrkw egvspstwrn rrpdeerhss r
//
LOCUS       WP_008940812             148 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Marinobacter santoriniensis].
ACCESSION   WP_008940812
VERSION     WP_008940812.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter santoriniensis
  ORGANISM  Marinobacter santoriniensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Marinobacter santoriniensis"
                     /db_xref="taxon:523742"
     Protein         1..148
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15849
     Region          1..135
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mehkqrgftl iellivvaii gvitafayps yqdyvertrr adaqgalmef saameryyas
       61 nnsyegaasg gvdtgapamf adeaplegnn kfydltisaa dansytlrat pkggqagdgi
      121 leldstgarr wdqdnsggfg tgendwee
//
LOCUS       WP_008941007             339 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_008941007
VERSION     WP_008941007.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 339)
  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 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 339)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 339)
  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   5  (residues 1 to 339)
  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   6  (residues 1 to 339)
  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 11677366
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39244
     Region          38..210
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <140..334
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mqqqqipvip sryylrlidi liqtnqynnq lltvfrdqis asdllsiqqi eqfielglsl
       61 pntedlafql gkniklsshs lvgyalmtsp hlehalrlia qyfrlimpsf klsiqyltdq
      121 qkvellfepi lqmnkqclaf hieaiavafy ysllelagqq lqryqvylsv aepkykeqyv
      181 hlikanfhfn yawvaglrvv idqqqlalpl pladahslkv veqrcqeqiq kiyhqgeive
      241 wvsmmlrqan qiptlkecak vlnistktlq rylqqhgvef hrlkqeisve raidllenss
      301 ftithiayel gysnpanftr afnkvmgcsp qsyrlnlnk
//
LOCUS       WP_008941109             626 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Acinetobacter].
ACCESSION   WP_008941109
VERSION     WP_008941109.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 626)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 626)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 626)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 626)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..626
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=69715
     Region          2..626
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mqssakkaal pvmtlaalgv vfgdigtspl yairecfntg hmaiseasvl gilslifwcm
       61 nltisfkyvs vimradnnge ggiisllaln lrskvfsdkn kiylialgfi gaslffgdgi
      121 itpaisvlsa ieglsivtpa fnqwlvpial giltglfmvq rhgtatmgkl fgpvtllwfi
      181 siglvglwsi iqtpyvlmmi npywafnfvy eqptiafitm gaviltmtgg ealyadmghf
      241 grmpiklawf civlpcllfn yagqgalllr npaaienpfy llvpdwalfp miglataaav
      301 iasqavitgv fsvanqamql rylprltvhh tsdveqgqiy lpfinwvlfi svfilillfe
      361 sstelasayg vavtmtmlcg tilistlayg vwrwswwkva llaipfllld lvfvastslk
      421 ilaggwvpil igavvytilm twkrgreivf krmetnalsi elfiksigms ketqfvpgea
      481 ifltgtpniv phamlhnikh nkvlhernvi vtvytqdipy varedrikve klddhfyriy
      541 myygfkdqpn ipnaleqayq eldfefdmmq msffisrdri vhtvgdgmsp wreklfismq
      601 rntspvsdfy qiptnrvvel gsqiei
//
LOCUS       WP_008941609             122 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: endonuclease domain-containing protein
            [Acinetobacter].
ACCESSION   WP_008941609
VERSION     WP_008941609.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 122)
  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 122)
  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   3  (residues 1 to 122)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..122
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14127
     Region          14..117
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mkldpqllef aktmrsnatd aenlmwqllr akrfmnlkfr rqhviapyiv dfychdlglv
       61 ieldgsqhgt ndgkeydaer tkflealglk vvrywnhdal gctdvvledl wrrcaelknt
      121 sp
//
LOCUS       WP_008942430             291 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_008942430
VERSION     WP_008942430.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 291)
  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 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   3  (residues 1 to 291)
  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   4  (residues 1 to 291)
  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 291)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..291
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32721
     Region          24..175
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          202..284
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mmndqilisl flkliakegf fataidgitl mrvdhntppl avlqeptlvf vlqgskrgyi
       61 gtetyafqqg eclivsvsmp fdcdtvaspe lpmiamimkl eadtvnella ktylendkfk
      121 plttgmsviq ydetisnvli rllktlsseq dslilgeqik rellyrviqh sgadaltglv
      181 vqgnlrqiyk iceyiqhhft ekltvemlae qanmsisafh kafkqvtlhs plqylkvtrl
      241 hkakqmlqne nqsvaqaaya vgyqsssqfs refkkqfgfs pnqtevnidk e
//
LOCUS       WP_008942716             661 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Oceanibaculum indicum].
ACCESSION   WP_008942716
VERSION     WP_008942716.1
KEYWORDS    RefSeq.
SOURCE      Oceanibaculum indicum
  ORGANISM  Oceanibaculum indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Oceanibaculaceae; Oceanibaculum.
REFERENCE   1  (residues 1 to 661)
  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 661)
  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 661)
  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 661)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..661
                     /organism="Oceanibaculum indicum"
                     /db_xref="taxon:526216"
     Protein         1..661
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=70002
     Region          1..627
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mtsaendgaa gaqslsdvlq yrtihgplrt vfviltlaav llsvnqlfnl qlfglvvldn
       61 rylyslagif lcltyivfpl rgkgdaqgav pwydillgal slavagyfvw tgeealsagw
      121 eyaapqtami lsfvfwvlil eatrrtggti ifaivllfsl ypafadkvpg pisgyplple
      181 dtiafhiiss essfgipmra fgelvvgfiv fgaalqqtgg grffndlala lvgqfrggaa
      241 kvaifasgfm gsmsgsvisn vlttgvvsip amrrtgfsrs yaagteacas tggvlmppvm
      301 gttafvmasf lgipyidial aaalpsmlyy fglfvqldsy aarrglkgle raevpslret
      361 fregwqylfv favlifvmvv frqetlapfy atgllliinq ifprtrlsld gflkliqaig
      421 rslaelvsvl lgvglivgaf satglagtlv ndllfiagda tivllimgai tsfifgmgmt
      481 vtacyiflai vlapaltqag mnplavhlfi mywgmvsfit ppvalgafaa atiagtgpik
      541 aglaamrlgs viyfvpfffv lnpaligqgt tgevllvlat afpgvwmias atqgylaffg
      601 sfgdgwaslv nrallfvggi llifpgfeef hlsqieltgi alalvaasll letgrrklas
      661 a
//
LOCUS       WP_008942809             741 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Oceanibaculum indicum].
ACCESSION   WP_008942809
VERSION     WP_008942809.1
KEYWORDS    RefSeq.
SOURCE      Oceanibaculum indicum
  ORGANISM  Oceanibaculum indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Oceanibaculaceae; Oceanibaculum.
REFERENCE   1  (residues 1 to 741)
  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 741)
  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 741)
  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 741)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Oceanibaculum indicum"
                     /db_xref="taxon:526216"
     Protein         1..741
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=79456
     Region          15..737
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mtdrethaqp eealskdqid rlveeydpes nfrqliggaa iivtvmgvll slfhvytagf
       61 gllneiahrs ihlafvlali ylvfpeqrra rpavewpvsl gfvafylyla ydmaralegr
      121 gegegtwifv lliagvsflt lpfkflgter nriawrdwim aavaasvsly fvvffedifi
      181 nrvgdpigqd ymmgvlaiim vveatrrtmg lslpiigvac llygmlgpyl pgvlghrgys
      241 ilrivnhiyi gtegiygiav gvvatyvfhf vlfgvlmqlt glgqlfmnla tivagrysgg
      301 aakvsvvssg lfgmisgssi antvttgalt iplmkrsgfs prfaggveas ascggqitpp
      361 imgasafvma emlgvpynhl iliaifpaif hyfamllmvh leakrlglsg mdrrhipifl
      421 evmarswhll ipllamvtll lmqytpflaa fwgiiltilc gylplilrpl gfksldpssa
      481 lkprqliegf elgakyalgi gaacacvgfi lgiatlsgig fkfsgavlql assaaetvla
      541 fdftgwigqq gvtlffalvf iaiacilmga gipttptyii lasiaapalh dlgvpllvth
      601 ffvfyygvla dvtppvalaa yagagiagse pmrtgttafr lsmgkalvpf mfvyapsmll
      661 vdftwlefaq amlsgllsvl clsvayighf raavsgwtkl alsvagllli fndlrgilvg
      721 aaiaalalgg nwlaarrlss a
//
LOCUS       WP_008943669             206 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Oceanibaculum indicum].
ACCESSION   WP_008943669
VERSION     WP_008943669.1
KEYWORDS    RefSeq.
SOURCE      Oceanibaculum indicum
  ORGANISM  Oceanibaculum indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Oceanibaculaceae; Oceanibaculum.
REFERENCE   1  (residues 1 to 206)
  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 206)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 206)
  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   4  (residues 1 to 206)
  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   5  (residues 1 to 206)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Oceanibaculum indicum"
                     /db_xref="taxon:526216"
     Protein         1..206
                     /product="TRAP transporter small permease subunit"
                     /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=23300
     Region          1..170
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 meqyirfadk lsawfgkvfa wcvmvmalgv gyevfvryvl naptvwafdl tymmygtmfm
       61 iagaytlsrd ghvrgdfvyr lwkpatqakv elvlyfffff pgvlalifag wkyagrswry
      121 levstmspan ipiyqfksvi iaagilltiq giaqvfrcil tiqrgawper eadveeletv
      181 lqkegagalk hgseaidivt pkvdrs
//
LOCUS       WP_008944163             664 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Oceanibaculum indicum].
ACCESSION   WP_008944163
VERSION     WP_008944163.1
KEYWORDS    RefSeq.
SOURCE      Oceanibaculum indicum
  ORGANISM  Oceanibaculum indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Oceanibaculaceae; Oceanibaculum.
REFERENCE   1  (residues 1 to 664)
  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 664)
  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 664)
  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 664)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Oceanibaculum indicum"
                     /db_xref="taxon:526216"
     Protein         1..664
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=69646
     Region          2..636
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mepeeresay rsyggiigaa lmtaailwvl fhvvtagigt lpnyqqraih lggalalvfl
       61 lypgarrdsa llrfgdlila glsvvvlgyi vwnydtives twftnetlek lfglallllv
      121 legvrralgw lfvglilafy lyayfggyip gplghrglsi drliyafylg engllgplmg
      181 isatvvtlfl ilgallnssg agqvfiliam riggrirgga gmvavfgsaf mgmvngstva
      241 nvtstgvlti plmkrlgfrr nlagaieava stggqimppv mgpgaflmae llgvaylqvv
      301 taalvpsllf flalligvyl yalkydlkpl paelipsare afapfplasl lipigiliyf
      361 ivnqytiqla vfwaiiaiva mmlagillha rpaptirtta eqvpvadaas ieptpqrias
      421 marsirdgly daargvvfia miiaaaqiiv slinltglgv tfsqmivsig qgnvllslvl
      481 tmviaiilgm gmptpaayav gaavlaapli nlgfdllpah lflyffasvs aitppvaagv
      541 faavaisggt vmgtaafamt lacslflipf lfimnpeltl qgdpsaiata lvsatigiag
      601 isiaaighcr gavswlpril iaagalalie pdwktdligl alaglglalh lrldrrmrsa
      661 avpe
//
LOCUS       WP_008944381             157 aa            linear   BCT 20-JAN-2025
DEFINITION  division/cell wall cluster transcriptional repressor MraZ
            [Oceanibaculum indicum].
ACCESSION   WP_008944381
VERSION     WP_008944381.1
KEYWORDS    RefSeq.
SOURCE      Oceanibaculum indicum
  ORGANISM  Oceanibaculum indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Oceanibaculaceae; Oceanibaculum.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Chen,S., Jancrick,J., Yokota,H., Kim,R. and Kim,S.H.
  TITLE     Crystal structure of a protein associated with cell division from
            Mycoplasma pneumoniae (GI: 13508053): a novel fold with a conserved
            sequence motif
  JOURNAL   Proteins 55 (4), 785-791 (2004)
   PUBMED   15146477
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449500
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Oceanibaculum indicum"
                     /db_xref="taxon:526216"
     Protein         1..157
                     /product="division/cell wall cluster transcriptional
                     repressor MraZ"
                     /GO_function="GO:0000976 - transcription cis-regulatory
                     region 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=17387
     Region          4..140
                     /region_name="MraZ"
                     /note="DNA-binding transcriptional regulator and inhibitor
                     of RsmH methyltransferase activity [Translation, ribosomal
                     structure and biogenesis]; COG2001"
                     /db_xref="CDD:441604"
ORIGIN      
        1 matfigqhen kidrkgrvsv pskfraqlak edfqgvvvyp spkfqalegc sfrrieqiaa
       61 slddldmlsd kaddlaatil aearelpfdg egrimlprdl ldemgideta lfvgqgstfq
      121 iwspeaysrr keearqrire gevtlklrrd geaggga
//
LOCUS       WP_008944741             716 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Oceanibaculum indicum].
ACCESSION   WP_008944741
VERSION     WP_008944741.1
KEYWORDS    RefSeq.
SOURCE      Oceanibaculum indicum
  ORGANISM  Oceanibaculum indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Oceanibaculaceae; Oceanibaculum.
REFERENCE   1  (residues 1 to 716)
  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 716)
  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 716)
  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 716)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Oceanibaculum indicum"
                     /db_xref="taxon:526216"
     Protein         1..716
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=76589
     Region          1..707
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mqdqknsevl vqaadeppps nerklegwqk lllavlcigy atfhlmvlnv fpietwsfri
       61 mhiagalaig yllvaawttd gldgngtwir pieyppllia lglggysffc vvyafvaade
      121 mmpdpwifgt sgwplvlstv vaigagwlfk prdhrigwyd wilainslsv agyllfnlaa
      181 lqfragvmpi psdmlfsiag vllileltrr vagmallvia glfivytfag pylpgilnhd
      241 gyrmdrffsy iytdsgilgp ttavsstyii lfiafgaflq iskvgdyfvn fafaiagrar
      301 ggpakvavfa sglmgmingt sagnvvatgs ltiplmkrvg yrpqsagaie aaastggqim
      361 ppvmgagafi maeitgipyt elivaalipa clyfmsvffm vdfeaakmgm rgmrqdelpv
      421 lsklmkqiyl flpiiiliga lymgysvira gtlglvsalv vswlspnkmg pigvlralea
      481 ttkmsiqlia vcacagiivg vigltgvglr fssllldiad ksqlialffa mvisivlgmg
      541 mpttaayava asvvapgliq lgipplvahf fvfyyavisa itppvalaay aggaiagadp
      601 mktsvtafkl glaafivpym ffyshgllme gewhvilrna atatvgvyml sgavmnwfhg
      661 rlpmlmrvvl fiaalmlisg gfitdivgiv mgavlffwqk trkpsekapl kadaea
//
LOCUS       WP_008944679             285 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein, partial [Oceanibaculum indicum].
ACCESSION   WP_008944679
VERSION     WP_008944679.1
KEYWORDS    RefSeq.
SOURCE      Oceanibaculum indicum
  ORGANISM  Oceanibaculum indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Oceanibaculaceae; Oceanibaculum.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Oceanibaculum indicum"
                     /db_xref="taxon:526216"
     Protein         <1..285
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
     Region          202..284
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 gdgggkprsr alpifialfa vgafggivwy aytqgvqsgv stvapvikad dgptkarpeq
       61 pgglqvphqd kqvfqrllpe gqapqtverl lppppeplqp ppapepapsa tapaqpqsqp
      121 lpsqsvaerp vatpqpapqp vpqgtppvps aapapqppqd apantpanpp aqaqqvaqpp
      181 apqpapapap aqtqqasiaa vsgggfkvql aavrsdeaak qewnrlknry keelgalslt
      241 vqrvdlgagk giyhriqagp ldeaaaerac talkaknqac lvvrp
//
LOCUS       WP_008945233              88 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Oceanibaculum indicum].
ACCESSION   WP_008945233
VERSION     WP_008945233.1
KEYWORDS    RefSeq.
SOURCE      Oceanibaculum indicum
  ORGANISM  Oceanibaculum indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Oceanibaculaceae; Oceanibaculum.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 88)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 88)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Oceanibaculum indicum"
                     /db_xref="taxon:526216"
     Protein         1..88
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=9180
     Region          2..88
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 msvtvtlpaa llplfpgapg llqldagtva elmdalearw pgmrdrlcds rpairrhinv
       61 fvegkratld tnlapgaevf iitavsgg
//
LOCUS       WP_008945404             279 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Oceanibaculum indicum].
ACCESSION   WP_008945404
VERSION     WP_008945404.1
KEYWORDS    RefSeq.
SOURCE      Oceanibaculum indicum
  ORGANISM  Oceanibaculum indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Oceanibaculaceae; Oceanibaculum.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Oceanibaculum indicum"
                     /db_xref="taxon:526216"
     Protein         1..279
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27582
     Region          <39..232
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 matvpsahfa enpalspsek aaldglpsfd ailrpthpad vmsagsagyd lllldftida
       61 lpdaveavei tgtqgvslaa nalgnlvvgg lgadtvlgqq gddtllggtg sdllgggkgs
      121 drleggagdd tlfggrgsdi lsggagrnel qgnrgadtil ggdegdllrg gkdsdsirgg
      181 igddtihagk ggdtlaggdg adsfhfkagd eenlildfdl aedvillaad lgldaamala
      241 rigidgegna vidlghdsyi tlagidpaal tldhflvlg
//
LOCUS       WP_008945255             231 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Oceanibaculum indicum].
ACCESSION   WP_008945255
VERSION     WP_008945255.1
KEYWORDS    RefSeq.
SOURCE      Oceanibaculum indicum
  ORGANISM  Oceanibaculum indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Oceanibaculaceae; Oceanibaculum.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 231)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Oceanibaculum indicum"
                     /db_xref="taxon:526216"
     Protein         1..231
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=25857
     Region          1..218
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mafqpildas heeiyaheal vrgmngesag kilgqvtekn rywfdqqcrv kaielaaqlg
       61 lgpkqrlsin flpnavyqpt acirmtveta rkvglpldri ifevtegeqv vehdklvaii
      121 raykefgllt aiddfgagys glnlladfqp diikldmalt rnidsdrvrr sivagiltvc
      181 reldimviae gietpeeyat lremgvrhfq gylfarpvfr dfareivfpg v
//
LOCUS       WP_008945704             211 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Oceanibaculum indicum].
ACCESSION   WP_008945704
VERSION     WP_008945704.1
KEYWORDS    RefSeq.
SOURCE      Oceanibaculum indicum
  ORGANISM  Oceanibaculum indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Oceanibaculaceae; Oceanibaculum.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Oceanibaculum indicum"
                     /db_xref="taxon:526216"
     Protein         1..211
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=23066
     Region          13..197
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mtmesslekp lekqrlivgi sgasgvlygi rllhllrdhp vethlvmsrs aeitlahetd
       61 wklrdvqala nywhpqedig aaissgsfrt lgmvvapcsv ktlaeiasgv tsglltraad
      121 vvlkerrrlv lmvretplta vhlrnmltvt emggiiappv pafyarpeni gamvdhsvgr
      181 vldlfglevg avrrwgevps dekprrhrkg v
//
LOCUS       WP_008945782             203 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Oceanibaculum indicum].
ACCESSION   WP_008945782
VERSION     WP_008945782.1
KEYWORDS    RefSeq.
SOURCE      Oceanibaculum indicum
  ORGANISM  Oceanibaculum indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Oceanibaculaceae; Oceanibaculum.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Oceanibaculum indicum"
                     /db_xref="taxon:526216"
     Protein         1..203
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22127
     Region          12..173
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mssdtvsrps alrrlydwtl rwsahrhaek alfgvsfaes sffpippdvm lipmvladrs
       61 rafrfaaict lasvlggafg yaiglflfes vgravldfyg yaakfaefsa lyneqgwliv
      121 agagftpfpy kvitiasgvt amdfgifmla savsrgarff lvaallwrfg ppirkvieah
      181 lgkltaaffi llvggfvalk yll
//
LOCUS       WP_008946177             466 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Oceanibaculum indicum].
ACCESSION   WP_008946177
VERSION     WP_008946177.1
KEYWORDS    RefSeq.
SOURCE      Oceanibaculum indicum
  ORGANISM  Oceanibaculum indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Oceanibaculaceae; Oceanibaculum.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Oceanibaculum indicum"
                     /db_xref="taxon:526216"
     Protein         1..466
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47455
     Region          160..390
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mtaqiipfsa mtrpaqgwte qekaelfrcm emlakagvpy eatfgttdeg epwlvfenpe
       61 tdeiavhiar vgtefiayse ptdellragd frellnqmva arrqeaamss snvyhliana
      121 vtgfaifvat aliatdeara dqiatlvlnm lsgaalpeed sddgrpagdp salvgsqama
      181 aqaegktedt adataqqqdq adtapearna lavddtalqe eedagadala amaepardva
      241 adkvisgtag ndllqggdgn dvlhggagnd tllggagndl llggdgndll rggdgddtls
      301 gglgddslfg dagndvlygn agndtldgga gddllvggag ndvllggagn dtldggagnd
      361 tlyggsgndl lmggagddml ihigldefsg kdmliggega nqfvllgknn avivdykigi
      421 dalvisgyti esaqnlgegl kglfaseeia elvlaglppe vvdglf
//
LOCUS       WP_008946525             235 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Listeria].
ACCESSION   WP_008946525
VERSION     WP_008946525.1
KEYWORDS    RefSeq.
SOURCE      Listeria
  ORGANISM  Listeria
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 235)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Listeria"
                     /db_xref="taxon:1637"
     Protein         1..235
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=27140
     Region          6..235
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mglmkfqlfi qpkldvlqgn iveyeillrd dskvprfpls eleavladee lylafsewfc
       61 daffdvlaky pndrfainia pqqlfytetl hwldklkses hritvemted ifdvpahkrh
      121 lnandkdafi lnkikvihgl gyhiaiddvs cglnslervm sylpyiieik fslihfqnip
      181 ledlllfika wanfaqknkl dfvvegietk etmtlleshg vsifqgylvn kpfpv
//
LOCUS       WP_008947536             397 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Listeria marthii].
ACCESSION   WP_008947536
VERSION     WP_008947536.1
KEYWORDS    RefSeq.
SOURCE      Listeria marthii
  ORGANISM  Listeria marthii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Listeria marthii"
                     /db_xref="taxon:529731"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43031
     Region          2..388
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mqkimainag ssslkfqift mpgeevlvkg lieriglpda ifnmsfqnek iketrainnh
       61 geaveilleq lkahqvindl neitgvghrv ahggeafvas civtdevvkg iedvtslapl
      121 hnpaniigik tfrellpnav svavfdtafh qtipeenfly alpyelyekh hirkygfhgt
      181 shkyvaqkaa evlekplekl kiischlgng asvcaieagk svntsmgftp naglmmgtrs
      241 gtidatiipy lvdelgysld evmhmmsses gvlgvsgiss dfrdieiaae qgdsralltl
      301 rmftgqicny igayasamng cdallftagv gensplirkm vteqlsylgv tcnvtknnag
      361 dmiisddnea vkvciiptne elmiardvek yakqtis
//
LOCUS       WP_008948217             133 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Listeria marthii].
ACCESSION   WP_008948217
VERSION     WP_008948217.1
KEYWORDS    RefSeq.
SOURCE      Listeria marthii
  ORGANISM  Listeria marthii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 133)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 133)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 133)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Listeria marthii"
                     /db_xref="taxon:529731"
     Protein         1..133
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=14589
     Region          2..125
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(6..9,39..41,44,68,107,121)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mevfvdgasa gnpgpsgagi vlkadgiyeq laipleimtn heaefiaikl gleealkkqa
       61 tfirlysdsk vaieaihkrh aknplfkphl eailkmadsl elffaewrnv sqnkqadqla
      121 rqaikkqkqp gvk
//
LOCUS       WP_008949313             156 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Alishewanella].
ACCESSION   WP_008949313
VERSION     WP_008949313.1
KEYWORDS    RefSeq.
SOURCE      Alishewanella
  ORGANISM  Alishewanella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 156)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Alishewanella"
                     /db_xref="taxon:111142"
     Protein         1..156
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16494
     Region          2..153
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mssekhalya ellqqakall qeetdvianm anfsallfqs lpdlnwagfy imrqgelvlg
       61 pfqgkvacvr ipvgkgvcgt cvatgeiqrv advhefpghi acdaasnsei vlpvrqggdi
      121 iavldidsps lnrfddvdqq glaalvaafe qalvaa
//
LOCUS       WP_008949928             522 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Alishewanella jeotgali].
ACCESSION   WP_008949928
VERSION     WP_008949928.1
KEYWORDS    RefSeq.
SOURCE      Alishewanella jeotgali
  ORGANISM  Alishewanella jeotgali
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Alishewanella.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Alishewanella jeotgali"
                     /db_xref="taxon:545533"
     Protein         1..522
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=55234
     Region          23..522
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mtteqqagcs irlpeqssaa qlavlqvhqr dnvlvalqal qageplpapf shlsaqtavp
       61 aghklaltai aagepvlkyg faigratqpi aagehvhshn latalsgtie ysytgcqapa
      121 lsfpadlpqs fqgyrrsngk vgtrnelwii ntvgcvnraa mrvaeqarqh yadllalkni
      181 dgihafthpf gcsqlgddld htrqllagli qhpnagavli lglgcennql arllqacpdv
      241 dssrirafna qqvedeveqg laavgellql mandqrstcp vselvlgmkc ggsdgfsglt
      301 analvgrtad llaaaggkvv ltetpemfga eqvfmaraan qqvfadlvrl vndfkqyfid
      361 nqqpvyenps pgnkdggltt leekslgaiq kggsavvqqi irygeqahaa gltllegpgn
      421 davsstalta agatlllftt grgtplgfpa ptvkiasnsn laarkpqwid ydagqllqvg
      481 qdaqqftgqf fryllavasg ertrneisdn reiaiwkngv tl
//
LOCUS       WP_008949949             450 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Alishewanella jeotgali].
ACCESSION   WP_008949949
VERSION     WP_008949949.1
KEYWORDS    RefSeq.
SOURCE      Alishewanella jeotgali
  ORGANISM  Alishewanella jeotgali
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Alishewanella.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Alishewanella jeotgali"
                     /db_xref="taxon:545533"
     Protein         1..450
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=49183
     Region          6..430
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mealinfeae qaviggvlhd sasenalyai etckpgdfst kanqiawrai qalsargqya
       61 divtvtelin trepayqisy lgecyrntps qanlkayani vreygqlraa agalnaaltv
      121 lhdkahepae rinlvlselg sigadesdqq itnlkdhqaa llqhlgeitk kggnitglst
      181 gfenldymtg glrngdlviv aarpsmgktt lvlnmleria itnnapkwal ffslempaqq
      241 ilqkvyasis stplakilna svmdnnegca rigtamelmq qsrlmiddkg gqhltqiqar
      301 akrmaikqgs npalivvdyl qliraegesq tirignvsag lknlaklmnc pvialsqlnr
      361 nltgkptlin lrdsgsieqd admviflhde dyegqrdehs lteiifaknr mgrtgstflq
      421 pelhlsrfsd tkrlpeakpe sqakplkkly
//
LOCUS       WP_008949965             133 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Alishewanella jeotgali].
ACCESSION   WP_008949965
VERSION     WP_008949965.1
KEYWORDS    RefSeq.
SOURCE      Alishewanella jeotgali
  ORGANISM  Alishewanella jeotgali
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Alishewanella.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Alishewanella jeotgali"
                     /db_xref="taxon:545533"
     Protein         1..133
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14624
     Region          3..132
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mftrgfslle mlvvlailgi liqlsypsyq qfvlrsyrae avttllelan rqeqrlldtg
       61 rysdqladlg vssadtssgr yriqlvidsd gtafqiilta qgaqqhdsac qqfsinhlgq
      121 rnhgvsaals cwd
//
LOCUS       WP_008950037             209 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Alishewanella jeotgali].
ACCESSION   WP_008950037
VERSION     WP_008950037.1
KEYWORDS    RefSeq.
SOURCE      Alishewanella jeotgali
  ORGANISM  Alishewanella jeotgali
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Alishewanella.
REFERENCE   1  (residues 1 to 209)
  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 209)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 209)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Alishewanella jeotgali"
                     /db_xref="taxon:545533"
     Protein         1..209
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22480
     Region          1..202
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 meiysseeqq veaikrfwne ygkaivggvv iglatlygwr yyqaeqrasa ealsssysql
       61 iqqqgegdew laqaqsfiaa qgsnnyaifa allsakeavn sgdlamaaqq lswvqqqakd
      121 agikaiaqlr larvqremgd fsaalatvnq plpesfaaqq aelkgdilqq sgdlaaakaa
      181 yqlalskapq ntqlvqikld elahvavtn
//
LOCUS       WP_008950231             144 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Alishewanella jeotgali].
ACCESSION   WP_008950231
VERSION     WP_008950231.1
KEYWORDS    RefSeq.
SOURCE      Alishewanella jeotgali
  ORGANISM  Alishewanella jeotgali
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Alishewanella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Alishewanella jeotgali"
                     /db_xref="taxon:545533"
     Protein         1..144
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14728
     Region          6..143
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 minvqrakqq gftlielmiv vaiigilaav alpayqdytv rarvsegmva aasakalvle
       61 naatgrafdq gfdaptgsdn vtsvaidaas geitvtfear agggdivfap npalvagtpp
      121 atnvrwtctg gsleakyrps ecrs
//
LOCUS       WP_008950932              83 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Alishewanella].
ACCESSION   WP_008950932
VERSION     WP_008950932.1
KEYWORDS    RefSeq.
SOURCE      Alishewanella
  ORGANISM  Alishewanella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Alishewanella"
                     /db_xref="taxon:111142"
     Protein         1..83
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8812
     Region          1..83
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mlkilffaal rerlacants ldlqgqvlta rqvldrlagq salwqqhlad aellcavnqq
       61 lvtlshpvaa gdelaffppv tgg
//
LOCUS       WP_008952472             119 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Pseudogulbenkiania ferrooxidans].
ACCESSION   WP_008952472
VERSION     WP_008952472.1
KEYWORDS    RefSeq.
SOURCE      Pseudogulbenkiania ferrooxidans
  ORGANISM  Pseudogulbenkiania ferrooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Pseudogulbenkiania.
REFERENCE   1  (residues 1 to 119)
  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   2  (residues 1 to 119)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Pseudogulbenkiania ferrooxidans"
                     /db_xref="taxon:549169"
     Protein         1..119
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12099
     Region          16..80
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkklllilas vlafcssama ainlntatqq eleslngigp akakaimdyr tkqgpfktvd
       61 elknvpgigd ktleklrkdi avsgksaapt akpaapakag sspvvpakpv akpvapakp
//
LOCUS       WP_008953074             267 aa            linear   BCT 20-JAN-2025
DEFINITION  phosphonate ABC transporter ATP-binding protein [Pseudogulbenkiania
            ferrooxidans].
ACCESSION   WP_008953074
VERSION     WP_008953074.1
KEYWORDS    RefSeq.
SOURCE      Pseudogulbenkiania ferrooxidans
  ORGANISM  Pseudogulbenkiania ferrooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Pseudogulbenkiania.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
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   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Pseudogulbenkiania ferrooxidans"
                     /db_xref="taxon:549169"
     Protein         1..267
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=28389
     Region          3..245
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 msltfervgl rlgrstildd islalgdgeq aaligpsgag kssllllant vyrpsqgtvs
       61 vlgqdpwrca prqlqslqad igtvyqappl parqrvvnav aagrlgrqgt lasllallrp
      121 hdaagvaevl qrvdladklw arcdqlsggq rqrvgiarvl yqaprlmlad epvsaldprl
      181 aeetvkrlad darargatll mslhsvdlal ahfpriiglq ggrilfdlpr aevhggliqa
      241 lyagerlaed dtlpadaepg fprgvrc
//
LOCUS       WP_008953167             219 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Pseudogulbenkiania ferrooxidans].
ACCESSION   WP_008953167
VERSION     WP_008953167.1
KEYWORDS    RefSeq.
SOURCE      Pseudogulbenkiania ferrooxidans
  ORGANISM  Pseudogulbenkiania ferrooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Pseudogulbenkiania.
REFERENCE   1  (residues 1 to 219)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Pseudogulbenkiania ferrooxidans"
                     /db_xref="taxon:549169"
     Protein         1..219
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24045
     Region          61..219
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cl49639"
                     /db_xref="CDD:483979"
     Site            order(159,173,176,189..192,194)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mnrlklvlat glalasally aaegentppp paeagfilaq qttgpllpth pnpqqygkpw
       61 ivvgvksqsl tfydgwglmq hrysvstarn gvgelansfm tprgwhrvce kigdgaeent
      121 iifrrqvtpw kytpalhaqy pekdwiltri lwlcgmepgk nqggdvdsyd raiyihgage
      181 hvafgtptsl gcvrmrnpdv ielfqqaelg tdvlidens
//
LOCUS       WP_008953302             275 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Pseudogulbenkiania ferrooxidans].
ACCESSION   WP_008953302
VERSION     WP_008953302.1
KEYWORDS    RefSeq.
SOURCE      Pseudogulbenkiania ferrooxidans
  ORGANISM  Pseudogulbenkiania ferrooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Pseudogulbenkiania.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 275)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Pseudogulbenkiania ferrooxidans"
                     /db_xref="taxon:549169"
     Protein         1..275
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=30499
     Region          26..263
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mtdeflpyqd daterlmsas amsideiwra lvndqlvpyf qpvvelrsrk vlgvealarw
       61 rhpalgvlsp vtfvpimeer gmirelteli lekslyacrd wldhgrqltv sinlsalslt
      121 drnlpglles kcriaglpss slilelsent lrqhwelaep qlgqlrergf gvavdeygig
      181 sglatrlnge hfstmkidra fvhgagsnph lrailqenll laqrhglftv amgieesadl
      241 allselgcda vqgylcsapl paegllpwiy qwekg
//
LOCUS       WP_008953774             722 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Pseudogulbenkiania ferrooxidans].
ACCESSION   WP_008953774
VERSION     WP_008953774.1
KEYWORDS    RefSeq.
SOURCE      Pseudogulbenkiania ferrooxidans
  ORGANISM  Pseudogulbenkiania ferrooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Pseudogulbenkiania.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 722)
  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   3  (residues 1 to 722)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Pseudogulbenkiania ferrooxidans"
                     /db_xref="taxon:549169"
     Protein         1..722
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=77828
     Region          1..717
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdelltvfvt esreqlaale aallqleaas gdadtlhaif raahtikgga gviecdyiva
       61 fthvvenvld qlrngdiavs aelialllac gdhiglllge feirrvhpta elqlagdall
      121 arlqrdarta ppglppagas satqpslgqd miesecwhis lrferhvlkn gmdplsflhy
      181 lgtlgtivhl etvadamppa dqmdaeacyl gfeirfasca dkttiervfe fvrddctlhi
      241 lppdsrlady idllqslped tmrlgeilvr igaltqaeld dgllmqqppm agaappdvvp
      301 lgeilvqqqv vqpklveaai irqarvsdkk taearliriq adkldrlidl vgelviasas
      361 vsllasrsgr aelleasslm mrlvestrds alqlrmvqig etfsrfnriv rdvskelgkd
      421 ielvitgget eldksvveki gdplihlvrn aidhgiepta rrtaagkppr grlelnashd
      481 sgsivitvsd dggglnrdki vakatergll qpghnlseae idnlifepgf stadhvssls
      541 grgvgmdvvk rniqslrghv dvrsapgagt rfsirlpltm aiidgflvgt gqanyvvpld
      601 mvveclelsp qtsdnhylnl rgevlpfirl helfnlpgkr parenvvvvr tgaqkvgivv
      661 dqllgefqtv ikplghlfqs lrgiggstil gsgevalild vpalvaiatr resreaastp
      721 at
//
LOCUS       WP_008953868             400 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Pseudogulbenkiania ferrooxidans].
ACCESSION   WP_008953868
VERSION     WP_008953868.1
KEYWORDS    RefSeq.
SOURCE      Pseudogulbenkiania ferrooxidans
  ORGANISM  Pseudogulbenkiania ferrooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Pseudogulbenkiania.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Pseudogulbenkiania ferrooxidans"
                     /db_xref="taxon:549169"
     Protein         1..400
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42046
     Region          5..388
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msssilvinc gssslkfali dtttqhaslt glaeklgldd aqitfkhqge ktvqtlaegn
       61 haaamraila qlqgrglfds vqaighrvvh ggerfkastl iddeviaaie dcarlaplhn
      121 pahvlgirta iacfpglpqv avfdtafhqs mpqraylypv pmalyrehgv rrygfhgtsy
      181 rfvsaeaarm lgkpleetal vcahlgngas aaailggksv dttmgltple glvmgtrsgd
      241 vdpglfgyla selkldvnai tellnkqsgl lglselssdc reledaalag dgaaqlalev
      301 fsyrlakqia altvalgrld avlftggige nssylrervv kllgflglrl dtdandrcvr
      361 gqagcitapg svpalvintn eelmialdta alatpaaltr
//
LOCUS       WP_008954973             626 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Pseudogulbenkiania ferrooxidans].
ACCESSION   WP_008954973
VERSION     WP_008954973.1
KEYWORDS    RefSeq.
SOURCE      Pseudogulbenkiania ferrooxidans
  ORGANISM  Pseudogulbenkiania ferrooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Pseudogulbenkiania.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 626)
  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   3  (residues 1 to 626)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Pseudogulbenkiania ferrooxidans"
                     /db_xref="taxon:549169"
     Protein         1..626
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=66990
     Region          7..608
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msefggmeel lqdflmesnd llsdvdnklv elekrpedra llndifrgfh tikggagfln
       61 vapmvtlchr tenlfdklrn aelqlnpevm dvildatasv rdmfgtlgqg lmprdadgal
      121 laaldavlsg rmpqapvpqa tpatppvasa pqrsdepdwn slyqavvpaa rtttptapap
      181 apvevvpaaa lvpetepvta vaaasraaap aknvtasksa sggghentir idtnrldmvl
      241 nlsgeigltk nrlttlrtei lqgnndsntl rsldeaisql dllvgdlqna vmktrmqpig
      301 rlfqkyprla rdlarqlgkd velvlsgeet eldktmiedl ndplvhlvrn avdhgvesta
      361 eriaagkkpq sliqltaeqv gdhilieitd dgrgmnadal rrkavekgli dteaanalde
      421 kqclqliflp gfstkdqiss vsgrgvgmdv vrtniqklng ridinsipge gtrisislpl
      481 tlailpvlvv racnqpfavp lamvreiiti dpeaiqevsg nptivvrdei lplktlagll
      541 gwaptqkpgf gvlmqsaers filaidsfvg rddvvikplq nirpkgvaga tlsgdgsvvl
      601 vldmedllta kdgvsgmvkt seliti
//
LOCUS       WP_008955146             138 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Pseudogulbenkiania ferrooxidans].
ACCESSION   WP_008955146
VERSION     WP_008955146.1
KEYWORDS    RefSeq.
SOURCE      Pseudogulbenkiania ferrooxidans
  ORGANISM  Pseudogulbenkiania ferrooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Pseudogulbenkiania.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Pseudogulbenkiania ferrooxidans"
                     /db_xref="taxon:549169"
     Protein         1..138
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14656
     Region          1..131
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mrkawagftl ielliaivvv ailmslavpa yqdyvrrsri naalaqlsqt rvsleqyyad
       61 nrsyaasgtt cgatpstvdy ftlactasgs tgytlgatgt tvmagyvysl dqsnsksttq
      121 ykgstvsksc wlikgdec
//
LOCUS       WP_008955488             172 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Pseudogulbenkiania ferrooxidans].
ACCESSION   WP_008955488
VERSION     WP_008955488.1
KEYWORDS    RefSeq.
SOURCE      Pseudogulbenkiania ferrooxidans
  ORGANISM  Pseudogulbenkiania ferrooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Pseudogulbenkiania.
REFERENCE   1  (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   2  (residues 1 to 172)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Pseudogulbenkiania ferrooxidans"
                     /db_xref="taxon:549169"
     Protein         1..172
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16203
     Region          16..83
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkyhpirshl vgalllavss saalaldina assvelvqag fsktqaeriv ayhkahgdfr
       61 sssdllkvkg vtkatlqkvn dklnsdasaa vraegaataa gqapagktga agagsasadq
      121 rpmetssgan agagvgagag vgvgvgvgvg agssggaagv ktqggvgigi gq
//
LOCUS       WP_008956121             143 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Halomonas sp. HAL1].
ACCESSION   WP_008956121
VERSION     WP_008956121.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. HAL1
  ORGANISM  Halomonas sp. HAL1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Halomonas sp. HAL1"
                     /db_xref="taxon:550984"
     Protein         1..143
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15932
     Region          1..141
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlslffvalv satllpggse vwlarlwcmg epplalwlva ttgntlgsmi nvalgryarq
       61 fqdrrwfpas prslvraegw yhrfgelsll vswapiigdp ltvlagvfrl pwwralawiv
      121 iakgaryavv lllahywlap lcq
//
LOCUS       WP_008956360             229 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Halomonas sp. HAL1].
ACCESSION   WP_008956360
VERSION     WP_008956360.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. HAL1
  ORGANISM  Halomonas sp. HAL1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 229)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Halomonas sp. HAL1"
                     /db_xref="taxon:550984"
     Protein         1..229
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=25987
     Region          1..215
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mafqpivdvs qreiiyyeal vrgpngesaf sileqvtqdl myrfdqacri kaielaselg
       61 mqeklsinfl pnavyeprac mqatletahr igwpierlnf eitetervtd rghlrriies
      121 yremgvttsl ddfgngyanl dlltdlqpds lkldrdlvmt cnsdkrrqai lrslvalast
      181 lgipliaegv etreesrclv elgipmqqgy yfsypnleal teidhakyd
//
LOCUS       WP_008956516             186 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Halomonadaceae].
ACCESSION   WP_008956516
VERSION     WP_008956516.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 186)
  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 186)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 186)
  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   4  (residues 1 to 186)
  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   5  (residues 1 to 186)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..186
                     /product="TRAP transporter small permease subunit"
                     /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=20644
     Region          7..176
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 msdttqlpaf igaldrasew fgrtlawlii immliqfaiv llryafsvns ifmqelvmym
       61 hasvfmlaaa ytfrhdghvr vdifyrgmtp rrqalinvvg iitllipvmi fiiasslgyv
      121 answrilets sdyggipavy alktliplfa vlmivqgvve ivrnsyvmag rivpaaaggn
      181 hleerv
//
LOCUS       WP_008956904             668 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Halomonas sp. HAL1].
ACCESSION   WP_008956904
VERSION     WP_008956904.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. HAL1
  ORGANISM  Halomonas sp. HAL1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 668)
  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 668)
  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 668)
  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 668)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Halomonas sp. HAL1"
                     /db_xref="taxon:550984"
     Protein         1..668
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=71043
     Region          3..598
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mttetapant qqvkekisqi rqlptalrwi paavtvvlml mtldylfnig wltfvtglet
       61 qfyyavvall lplvfllwpm rnsqqeqpip wydyllsaat livggyfvyn avpilergwa
      121 faapdlaiya syafwlliie asrragglpi aiiagvfsly plvadivpgp iqafpstlee
      181 tamyhtmste simgvplqaf aglvigflvf gvvlqksggg kffinlafal lghvrggpak
      241 vsifssglmg smsgsvisnv lttgvlsipa mrrigmsrsf aggveacast ggvlmppvmg
      301 atafvmamfl dvpystiala avipsilyfl glfiqidaya arndikglpv helpsikqtl
      361 kegwyfifvf allvwmllim qreavapfya talllvlnql skhnrwgwkd vadtlssaak
      421 lfaeliaila gvgmlvgals mtglsgtian dfiniaggsv pllllmgavt sfvlgigmtv
      481 taayiflava lapaliqggg ldpmavhmfi lywgmlsfit ppvalgafaa atvagarpma
      541 tglqamrlgs viyfipflfv lnpalimqge plvivavfiq avigiilfas amqgylmgvg
      601 rlgygalqei iiralvliag lllalpgggm vplsqwelig laaaallpav vlarlsqryh
      661 qrslatsa
//
LOCUS       WP_008957595             167 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Halomonadaceae].
ACCESSION   WP_008957595
VERSION     WP_008957595.1
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            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 subunit"
                     /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=18706
     Region          1..164
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mnaiakaida ineafgrvia pliaiitliv lydiasrflf grpsdwafdv tkmlfgahfm
       61 lmaayglrhh ahvevdvlkr llsrrkqavl evlgyliffv pfiwmlitlg wsfferawsr
      121 gettygmvsi pvypikgviv vaailillqa iaivlraimq lreetsa
//
LOCUS       WP_008957704             240 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Halomonas sp. HAL1].
ACCESSION   WP_008957704
VERSION     WP_008957704.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. HAL1
  ORGANISM  Halomonas sp. HAL1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 240)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Halomonas sp. HAL1"
                     /db_xref="taxon:550984"
     Protein         1..240
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=26422
     Region          52..215
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 malrlnvatl lfslpftlft lplhaasffa qvestpprgv lplhhqllql apqatpealr
       61 laaqalncad ptaerlavid yslpsteprl wvfdlrqhel lfeelvshgq gsgdaqaetf
      121 sntpdshqss iglfrtmnsy ygrngyslrl eglepnvndl aferaivihg adyvsdafit
      181 qtgrlgrshg cpavredvty plidslkedq yvfayypdae wlatsaflgc tadvaqlarr
//
LOCUS       WP_008957727             269 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Halomonadaceae].
ACCESSION   WP_008957727
VERSION     WP_008957727.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            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="formate/nitrite transporter family protein"
                     /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=28769
     Region          2..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msyllpaefa tkmvdageak lhmstrdali rafmagaila iaavfavtva vqtgypiiga
       61 ilfpvgfsil ylmgfdlltg vfvltplawl dkrpgvtinr ilkhwgivfi gnfggaltva
      121 flmaivftyg fstepsevgr vigevgegrt vgykeygagg matifirgil cnwmvslgvv
      181 gamisttvsg kviamwmpim lffgmgfehs vvnmflfpsg lmmggnfsim dyliwneipv
      241 vlgnliggla ltgltlytth vrtapqkal
//
LOCUS       WP_008959642             733 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Halomonas sp. HAL1].
ACCESSION   WP_008959642
VERSION     WP_008959642.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. HAL1
  ORGANISM  Halomonas sp. HAL1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 733)
  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 733)
  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 733)
  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 733)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..733
                     /organism="Halomonas sp. HAL1"
                     /db_xref="taxon:550984"
     Protein         1..733
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=77347
     Region          36..723
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mshktdqept glkddahaas aipesiadgv dddvvepnrr lftgwqfllf aalaiayssf
       61 hlislnvypm etwsfrivhi agalilgygl fagarfaedd hqasgawikw vsyallipaa
      121 ytlaqvfvmy qtlsgsamri dpsvenwhyg yplmattaga ivlswfyrqa rhrfnpadlv
      181 lmvcamasag yllvayntni rmstgtsfap sgiswaaiag sllileltrr vaglalvvis
      241 avfltyvfag pylpgflgyp glslqrffsq vytdagilgp ttavsstyii lfiifaaflq
      301 askvgdyfvn fafaaagrar ggpakvaifa sglmgmingt sagnvvstgs ltiplmkkvg
      361 yparsagaie aaastggqim ppimgagafi maevtgipyt eiaiaaiipa ilyfasiyfm
      421 vdfeaarkgm rgmrkdeipl fsklvkqvyl fapiiiliva lfmgysvira gtlatasaav
      481 vswispnkmg lrailkalqi agtmsiqiia vcacaglivg visltgvgar fsslllglag
      541 vsqllalvfa mlisillgmg mpttaayava asvvapglin igiepliahf fvfyfavvsa
      601 itppvalasy aaagisgdnp mgtsvasfki glaafivpfm ffyspamlme gspmqilrvg
      661 vtatlgivll sgmvqawffg pvnawqrvvm lvgamfmiyg giytdvlgla igivlfvmqr
      721 klhgggnkia qag
//
LOCUS       WP_008960137             689 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Bradyrhizobium sp. STM 3809].
ACCESSION   WP_008960137
VERSION     WP_008960137.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. STM 3809
  ORGANISM  Bradyrhizobium sp. STM 3809
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 689)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 689)
  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   3  (residues 1 to 689)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..689
                     /organism="Bradyrhizobium sp. STM 3809"
                     /db_xref="taxon:551936"
     Protein         1..689
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /function="16.5 : Explore"
                     /function="16.12 : Sense"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=73811
     Region          14..660
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mpvtsdseay pvaqfrktyf eecaelmdal qsnlellang qeddetlhai frsvhsvkgg
       61 agafgctdlv afshtfesll dalrdhkipa theikqlllr asdaladivn aarleqqlpp
      121 nfaadisaam rdtlqgagqs advssapata daktlteqty rirfrphtem lrkaneplll
      181 irqlgklgsl rtevdssslp pldsldpeaa ylnwtftldt avprsaiqdv fefveddcdl
      241 eiesseparl paetatsdat gasdtsgtva atvaavgaaq sirvdvdkvd rlvnlvgelv
      301 isqamlteqg lglpadkype liqgiealaq sarelqesvm airaqpvksv farmprivre
      361 laatlgkevr ivtsgemtei dktvieqlnd plthmirnal dhgiespver iaagkvrqgt
      421 ihlsaaqrsg rivievsddg rginkekila kakarglvpa ganltddein eliflpafst
      481 aevvsnisgr gvgmdvvkrn vqalggrisv rsrfgqgsaf tlslpltlav vdgmvvsvgr
      541 etfiiplvai venlrpqtad ihpvvgrghv lalrgeylpl vylhrlfsis daigdpcrgi
      601 viivqsesag rvgivvdell gqqqvvvksl eanyepvdgi sgatilgngr valildvarl
      661 heidvrgtam rlpppdaptp tekdmthaa
//
LOCUS       WP_008960264             163 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Bradyrhizobium sp. STM
            3809].
ACCESSION   WP_008960264
VERSION     WP_008960264.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. STM 3809
  ORGANISM  Bradyrhizobium sp. STM 3809
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 163)
  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 163)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Bradyrhizobium sp. STM 3809"
                     /db_xref="taxon:551936"
     Protein         1..163
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18079
     Region          54..109
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mtdtskttge vvalplpsls akdkrraeak ygkavmahgy tlvpnlmlqg qahlkispta
       61 fnvlmqlllh wwdanepphp sikriaqrmn ksprslfryf deleeaglve rearyrgkka
      121 qttsayklng ltaklkeiep amtaakkfkd krvekaeaas taa
//
LOCUS       WP_008961128             346 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Bradyrhizobium sp. STM
            3809].
ACCESSION   WP_008961128
VERSION     WP_008961128.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. STM 3809
  ORGANISM  Bradyrhizobium sp. STM 3809
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Bradyrhizobium sp. STM 3809"
                     /db_xref="taxon:551936"
     Protein         1..346
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /function="6.15 : Photosynthesis"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38250
     Region          5..277
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mswnddiaic rrmlrggskt ffaaskvlpr evgdaaialy afcreaddai dgpsrrvdav
       61 ellherleri yegtpddspv dralagvvar faipraipea lleglawdaq grryetlsdv
      121 layavrvagt vgvmmsllmn rreadtigra cdlgiamqlt niardvgeda ragrlylprq
      181 wlreagldve twraapffdd riarvtarll avadvfyara sagiaelpwn crpgihaarl
      241 iyaeigreva raefdslsrr avvstprklq llgkaaivsl aqaqpslapl rpearilida
      301 vvtadaqrph alvprrrtlh dralwvidlf erlerrdqvl rsgras
//
LOCUS       WP_008961153             201 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Bradyrhizobium sp. STM
            3809].
ACCESSION   WP_008961153
VERSION     WP_008961153.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. STM 3809
  ORGANISM  Bradyrhizobium sp. STM 3809
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 201)
  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 201)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 201)
  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   4  (residues 1 to 201)
  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   5  (residues 1 to 201)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Bradyrhizobium sp. STM 3809"
                     /db_xref="taxon:551936"
     Protein         1..201
                     /product="TRAP transporter small permease subunit"
                     /function="16.1 : Circulate"
                     /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=21345
     Region          24..188
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 maeiaqapsp geraslnaaa paplrilldv idrlgrldgw igggclltlt glmlaevttr
       61 alsnvlpffp ptisiaweys sylmaasftf gaamtlrvgg hirvvlllkn vppplqrale
      121 vlaatagfaf mafltsamtk fafgsfirgq vstssdtplw fpqavvtfgm llltlqflar
      181 aiqaalglpl edhrmkaspv e
//
LOCUS       WP_008962803             632 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Bradyrhizobium sp. STM 3809].
ACCESSION   WP_008962803
VERSION     WP_008962803.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. STM 3809
  ORGANISM  Bradyrhizobium sp. STM 3809
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 632)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 632)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 632)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 632)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Bradyrhizobium sp. STM 3809"
                     /db_xref="taxon:551936"
     Protein         1..632
                     /product="potassium transporter Kup"
                     /function="16.1 : Circulate"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=67975
     Region          6..632
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mtasatsteg qetastsgfw gltlgsigvv fgdigtsply afreaaigaa hgqpvsrviv
       61 lgvlslilws lfivvtakyv llllradnng eggtlslmal gqralgrrsm flmalgvvga
      121 smfigdsmit paisvlsave glklaapale hyvvpltvfi lvvlfavqsk gtarvatafg
      181 pvmvtwfasl avmgivhisd dpsvlaainp yyavhfllsh gtvglvtlga vflavtggea
      241 lyadlghfgr kpiqsawlff vlpallinyf gqgalvlsdp aaiensfyrm vpellllplv
      301 vlataatvia sqavitgays lvsqavqlgl lprfevryts eshagqiylp rvnrllligv
      361 mllvlmfrts snlasaygia vsttmvadgi mgfvviwklw nlrvavaaav iapfvivdlt
      421 ffsanllkll egawvpllfg aamvvtiwtw rrgsailmlk trkievpldd lvaslekrpp
      481 hivkgtavfl tsdptsvpta llhnlkhnkv lhehnvilti etaqtprvdv servrmekis
      541 ekfskvrlrf gfmespnvpr alavarklgw qfdimstsff vsrrslkpss qsgmptwqdh
      601 lfiglsrsan datdyfqipt grvvevgtqv ti
//
LOCUS       WP_008963572             286 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Bradyrhizobium sp. STM
            3809].
ACCESSION   WP_008963572
VERSION     WP_008963572.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. STM 3809
  ORGANISM  Bradyrhizobium sp. STM 3809
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Bradyrhizobium sp. STM 3809"
                     /db_xref="taxon:551936"
     Protein         1..286
                     /product="formate/nitrite transporter family protein"
                     /function="16.1 : Circulate"
                     /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=30781
     Region          31..284
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mrskanaptf spaadiegvs drqrreiqaq srpnaalihe tiraegesel errwfaills
       61 glaaglsmsl slivqgefqa fvadeaarrl faplgytagf lvvvlgrqql ftentltpil
      121 pllhhrdakt lvqvarlwsl vlianvagtw aagaalaytd vfdprivdaf teisrhtveg
      181 pfsttfmrav fagwlialma wllpavrgar ahivmvmayl valgqfahvi agsvecaflv
      241 lkgqatlsdy vavffvptll gnvvggttlv amlnygqvaa eldqts
//
LOCUS       WP_008964012             507 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Bradyrhizobium sp. STM 3809].
ACCESSION   WP_008964012
VERSION     WP_008964012.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. STM 3809
  ORGANISM  Bradyrhizobium sp. STM 3809
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Bradyrhizobium sp. STM 3809"
                     /db_xref="taxon:551936"
     Protein         1..507
                     /product="UxaA family hydrolase"
                     /function="16.11 : Scavenge (Catabolism)"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=53530
     Region          4..507
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 maaapvirlh pedsvliars slppglavad gvttvdripa ghkvavrpia qgepirrygq
       61 iigfattaia pgqhvhtqnc emgdfakdya fgvdvkptpn fdlpatfegi rrpdgrvatr
      121 nyigiltsvn csahvagmva dvfkknpftg dnpladyphv dgvvalthkt gcgmtldepl
      181 kllrrtlggy arhanfsavi vlglgcevnq igglmeeqkl agrlramdiq evggtrktve
      241 agiafvkeal vdankvkret vpaseltval qcggsdgysg isanpalgaa sdllvrhggt
      301 vilsetpety gaehlltrra vsrevgeklv slmrwwedyt aregaemnan pspgnkaggl
      361 ttilekslga makagstnlv dvlhyaeavt kkgfvfmdtp gydpvaatgq vagganlvcf
      421 ttgrgsvfgc kpapsiklat ntpmykrmed dmdvncgtil dgeesvqecg qrifelmlkt
      481 asgqptkses fdfggaefap wvlgatm
//
LOCUS       WP_008964651             264 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Bradyrhizobium sp. STM 3809].
ACCESSION   WP_008964651
VERSION     WP_008964651.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. STM 3809
  ORGANISM  Bradyrhizobium sp. STM 3809
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 264)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Bradyrhizobium sp. STM 3809"
                     /db_xref="taxon:551936"
     Protein         1..264
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=29418
     Region          25..137
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mrttlfavag fallfatpal akiditvdkn nqimtvavdg veryrwpvst gipsretpng
       61 tfrafrmead hfskefddap mphsifftkv ghaihgtdse grlgtpashg cvrlskanat
      121 tlydlvqkdg vlnttvtltg saevalarnp rrgtavarre tqpqqyddsg epvvltpqpq
      181 llpgrqvvpq qrpddgyiyp adgsdngvry paprgtsrrv ydaqaypqqq pqyyydngnp
      241 syaqpryyqp rqyyqprgyy tyqd
//
LOCUS       WP_008964883             525 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Bradyrhizobium sp. STM 3809].
ACCESSION   WP_008964883
VERSION     WP_008964883.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. STM 3809
  ORGANISM  Bradyrhizobium sp. STM 3809
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 525)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Bradyrhizobium sp. STM 3809"
                     /db_xref="taxon:551936"
     Protein         1..525
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=55384
     Region          <227..468
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 miristifia icmvlvaasl glilysvagi sgsesaivsl aaltflilyn avsmrlrdrs
       61 dvgsqiadls rgtadlarqv aefgrrlsav egrivssssv ssdrlqgvvs einelgglmk
      121 qlavtvaqhe dliaaipqqp aapvadtpap areaspapaa pvasaiypdp kappsasstp
      181 kpkeatatfs aapaiapvvr pptappitaa patplpaapa mprsqpqila avkgaiednr
      241 ldiylqplvt lpqrkvrfye avtrlrderd qivaaedfig iaeaaglvgr idhmvllrcv
      301 qvlrrlmvrn kdvgifcnls satlsspasf aqcldflean ralapsfvle fkqstlrslg
      361 ptetehlaal aqrgyrfsvd hvtdlrfepr eladrgvrfi kvpaallldp kqssvsdihp
      421 tdlsdllgrf gidliaerie gensvvdlld ydvrfgqgfl fapprplrpe gasatgeaaa
      481 spsggqeiki qdpnaagtpt ldasntnaat rsgnaalarr iagti
//
LOCUS       WP_008965164             169 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Bradyrhizobium sp. STM 3809].
ACCESSION   WP_008965164
VERSION     WP_008965164.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. STM 3809
  ORGANISM  Bradyrhizobium sp. STM 3809
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Bradyrhizobium sp. STM 3809"
                     /db_xref="taxon:551936"
     Protein         1..169
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=17627
     Region          68..141
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 msalrhgrrr vgavsgfval sllmlpvyga aaqqtspvpa tketpaaake papppsvtil
       61 gardahgvlg rdvrsstged mghivdvivd ptgtvraavi dfggflgvgs rkivvdwtal
      121 dfkhiaaksd qvtldltkeq vkaapeyked kpvvvlgaag klspwdfdh
//
LOCUS       WP_008965201             193 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Bradyrhizobium sp. STM 3809].
ACCESSION   WP_008965201
VERSION     WP_008965201.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. STM 3809
  ORGANISM  Bradyrhizobium sp. STM 3809
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Bradyrhizobium sp. STM 3809"
                     /db_xref="taxon:551936"
     Protein         1..193
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=20919
     Region          1..163
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlrriydwcv daahkphalw imaaiafaes sffpvppdvm lipmslakpq rawlfagvct
       61 aasvaggvvg yaigallyds lgqwlihlyg lgdkveafra syaewgaiii llkgltpipy
      121 klvtitsgfa gynlflfivc sivarggrff iaaivlnryg ewirvhiekh lglwvalgaa
      181 vlvagfvval kli
//
LOCUS       WP_008967138             338 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Bradyrhizobium sp. STM
            3843].
ACCESSION   WP_008967138
VERSION     WP_008967138.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. STM 3843
  ORGANISM  Bradyrhizobium sp. STM 3843
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 338)
  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   5  (residues 1 to 338)
  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   6  (residues 1 to 338)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Bradyrhizobium sp. STM 3843"
                     /db_xref="taxon:551947"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37202
     Region          23..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          114..338
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mrrtgytras tlgpiaevvt atggsiervf rraelpirll espdtllplr dhfrllaass
       61 relrdevfaa rlgrqtsiag lgvygkwvtq aptlleaiqr agtslphmlq satrllvrrh
      121 gkevhwsyel adtatdgrpq nemlaiwymi avvrhfagag wlpsrimigg ltaraqrsid
      181 eqmgaatvic dapgtiifdr rllvavnphl drtegldade larifdipap ddlpghvaal
      241 idlellgarp tlsgivrrag vskrtlqrrl geiglsysdl lrnalqrqai rllcqserpi
      301 tdiagmlgyr dpahfsrafe swsgiapsrw relvksag
//
LOCUS       WP_008968860             214 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Bradyrhizobium sp. STM 3843].
ACCESSION   WP_008968860
VERSION     WP_008968860.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. STM 3843
  ORGANISM  Bradyrhizobium sp. STM 3843
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Bradyrhizobium sp. STM 3843"
                     /db_xref="taxon:551947"
     Protein         1..214
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=23517
     Region          19..214
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mppaaetqqd raiallsrqg marlsefkea gitaatvsrm kekglvlqls rglyqladas
       61 ldthhtlaea aklvpkgvic ltsalsfhgl tdtipprvwm aigpkdrlpr ietpplqfvr
      121 fgekmltsgi kdhmiegvrv riynpaktvv dlfryrrsag kryqkspgln laleglreal
      181 rqrkatpaei aryageagvw kvvepyleam tana
//
LOCUS       WP_008968898             122 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Bradyrhizobium sp. STM 3843].
ACCESSION   WP_008968898
VERSION     WP_008968898.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. STM 3843
  ORGANISM  Bradyrhizobium sp. STM 3843
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Bradyrhizobium sp. STM 3843"
                     /db_xref="taxon:551947"
     Protein         1..122
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=13299
     Region          12..>75
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mamsideref gnligsdkve gtavygagda kigniervmi dknsgqvsya vlgfggflgl
       61 gndhyplpwq slkydtrlgg yvtgitenql rgaphysddr ewnwsdmstt ravndyygvp
      121 iv
//
LOCUS       WP_008970791             576 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Bradyrhizobium sp. STM 3843].
ACCESSION   WP_008970791
VERSION     WP_008970791.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. STM 3843
  ORGANISM  Bradyrhizobium sp. STM 3843
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 576)
  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 11482063
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Bradyrhizobium sp. STM 3843"
                     /db_xref="taxon:551947"
     Protein         1..576
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=60173
     Region          6..576
                     /region_name="PRK06132"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:235709"
     Region          <167..420
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 mlcvhsavrr rfycaailsg siaigagsqa aaqgysywnp sfyrperqif hhqrpkarhh
       61 qtqsavtqke avkpqgpliv avsinrqqvk vydsnglfae apvstgmkgh stptgvfsvi
      121 qkqkfhrsni ysgapmpfmq ritwsgialh agvlpgypas hgcirmppsf avkmygwtrv
      181 garvfvtpae vepsdfthpl laslkapqps asalpeattp aapkadkgaa lipvtvnanl
      241 dlrstighde lsgsagpaap lrgqthtada svapgsttis dvprvqvtpr vdvsenvtpv
      301 nagqssasgs dpaagdiptk pgagaaaeag trpeskpadg epskhddmpt tttkgpekpq
      361 dvtavpasgv pasnvdksad vnsadkpaep akasadgpaa padkdqtrls esekaplakp
      421 elkrnspvai fisrkdskly vrqnfaavfk vavtiapadr plgthvftat adkadsnvmh
      481 wsvvsvpvsa ratarnedge rtarhshkkg gdapieakav plpdspteal dritipadvq
      541 awlgdalssg sslivsdqgi nqgetgegte filslr
//
LOCUS       WP_008970943             698 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Bradyrhizobium sp. STM 3843].
ACCESSION   WP_008970943
VERSION     WP_008970943.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. STM 3843
  ORGANISM  Bradyrhizobium sp. STM 3843
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 698)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 698)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..698
                     /organism="Bradyrhizobium sp. STM 3843"
                     /db_xref="taxon:551947"
     Protein         1..698
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=71795
     Region          1..698
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mnaiarlirp rsvavigasa dpsktsgrpv aflqkhgfgg eiypvnpkvg higgltcypd
       61 vaalpavpdv givllgaera hlavrelaar gaaaaivlas gyaetgeega lrqrqlmqaa
      121 gamrilgpnt iglvnltdni vlsasgalam dhftagsigl vsqsggilga llsraaargi
      181 glsklvstsn eadlelsdfi eflaeddatk vialyveair rpdrfraavq tarqagkpvv
      241 afkigrseag akaavshtga lagsdrmyda lfrqlgvira ktfedlldip avlaagrkln
      301 gkrvailtst ggagtivsds lgvagfetpa pdaetaarlk slqsgshanl drnpvdltla
      361 glqpdilrga isallaspsy daltiiagss avgspallad avhdclsmsd kpviayvspy
      421 apnvgltltq qgvpaytsae scasalsgll qaarpvrseh ttplgaridi sdfrsgslde
      481 aeakalfsrf girgvaeriv ttsaeavaaa relggrvvlk ilsgeithks dvggvavnlt
      541 pdtiserlta mtaqveaatg rrpqrflvqe mvsggtelil glhrdplgta vllgmggvta
      601 elfkdttmrm lppgsglsrd earsmlhdlv awplldgfrg rpkadvealv saivafsmma
      661 aqlgdrliea einpvfvlpa cdgvraadgv vvlgaaag
//
LOCUS       WP_008971923             239 aa            linear   BCT 20-JAN-2025
DEFINITION  prolipoprotein diacylglyceryl transferase [Bradyrhizobium sp. STM
            3843].
ACCESSION   WP_008971923
VERSION     WP_008971923.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. STM 3843
  ORGANISM  Bradyrhizobium sp. STM 3843
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002130
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Bradyrhizobium sp. STM 3843"
                     /db_xref="taxon:551947"
     Protein         1..239
                     /product="prolipoprotein diacylglyceryl transferase"
                     /EC_number="2.5.1.145"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008961 -
                     phosphatidylglycerol-prolipoprotein diacylglyceryl
                     transferase activity [Evidence IEA]"
                     /GO_process="GO:0009249 - protein lipoylation [Evidence
                     IEA]"
                     /GO_process="GO:0042158 - lipoprotein biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=25218
     Region          <60..227
                     /region_name="Lgt"
                     /note="Prolipoprotein diacylglyceryltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0682"
                     /db_xref="CDD:440446"
ORIGIN      
        1 mdgaalhatf dvvawlaaga agwwlsrvqr lsfpqqstaw pyvaallfga gvgaylfgtl
       61 nlwlsglagv arsvegalag givavelykw rhgitlrtga rfalplalgi avgrigcyva
      121 glddftygtp ttlpwghdfg dgiprhpvql yesaamaafa aayvaavlrr neaiiangfy
      181 lalgfygaqr flwellkpyg pivgpltlfh llslgivays aamlatappa kvmherava
//
LOCUS       WP_008973463             390 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Bradyrhizobium
            sp. STM 3843].
ACCESSION   WP_008973463
VERSION     WP_008973463.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. STM 3843
  ORGANISM  Bradyrhizobium sp. STM 3843
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 390)
  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 390)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Bradyrhizobium sp. STM 3843"
                     /db_xref="taxon:551947"
     Protein         1..390
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44859
     Region          6..387
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mlraitpihl tqlqarriwl qaqrldeeap fgagpdavaa atahlgyvqi dtihvierch
       61 hhilftrnpa yrradlrqaq svdksvfeyw thalayvpsk dfrlflptmr qyrraghrwl
      121 ksvkpedmrk vmrlirqgga ltirdidddv ltekehlwas rkpskralql gfyqgvltis
      181 gregmlktye ltsrhfgwdk ppkpaseaet aaylldralr aqgvvsldsi chldapakpk
      241 vrrliearmr rgelvavdve gagkqahwmr petldgigdl gsdrvhilsp fdpliiqrkr
      301 telffdyahr feayvpkekr qfgyfalpvl vgedivaald lktdrqkrkl lmqkwtwvgp
      361 graakgeark alkrriedel hrferfqlgd
//
LOCUS       WP_008977024             168 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Faecalimonas umbilicata].
ACCESSION   WP_008977024
VERSION     WP_008977024.1
KEYWORDS    RefSeq.
SOURCE      Faecalimonas umbilicata
  ORGANISM  Faecalimonas umbilicata
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Faecalimonas.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 168)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Faecalimonas umbilicata"
                     /db_xref="taxon:1912855"
     Protein         1..168
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17982
     Region          11..161
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mkqiaitypd dktlmyrllr tqltglvdgv phltanlant sallagalrd inwvgfyllk
       61 ddtlilgpfq gkpacveikv gkgvcgtava edctmlvpdv hafpghiacd sasnseivvp
      121 ihcsgkvvgv ldidspclhr fddedrhgle clvhtlegml sesllelc
//
LOCUS       WP_008984767             691 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Alishewanella agri].
ACCESSION   WP_008984767
VERSION     WP_008984767.1
KEYWORDS    RefSeq.
SOURCE      Alishewanella agri
  ORGANISM  Alishewanella agri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Alishewanella.
REFERENCE   1  (residues 1 to 691)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..691
                     /organism="Alishewanella agri"
                     /db_xref="taxon:553384"
     Protein         1..691
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=74938
     Region          10..691
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mlstkrqpva lavalslgav nlaavaeeaa tessagkvmp sievirvkgq qqvhrfeetg
       61 svilidrtqi eqvqplsted vlrrvpgini kgeeetsiva nfgirglsag esksllledg
      121 vpvapglfig ndryfntriq rvesvevlkg saslrygpst iggvvnyitk tpddgvqlsa
      181 ragsfnmrem tveagaknqs edafagvvat kassdgfmdk gydmsdvmvk aglaisdkqk
      241 vgvkfsyhen eanisyrgll ladylngery npapddwylt drtaldlnhe vilgnnakln
      301 tlvywsettr dywrydvnta asnaagrwvy tdtltgnnrg ferlgiesrl sfdqqlfgya
      361 aasevglrlm eeesndtrir atraadrsgn ndrhivdsat svagyaqsri qltdelavtp
      421 glriesyeqk rviltdnnns akttntellp gvgltyelta qaqlyggvyr afspasngva
      481 ldgltdqqld gersvnyelg lrgtagaany evsafymnfa nqvvtgnsdp nlsqsnagkt
      541 ehtgmefllg yelgggfrid tnatwvptse fksgvnagnr ipyapkilan lalsytgeal
      601 svaltahhrg eqyadptniv dipanaaggi wggllpaytv ydlmaqynvf egftvygsvk
      661 nladkqyisg lrqgiyvgpe rsfeagfryr f
//
LOCUS       WP_008985639             209 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Alishewanella].
ACCESSION   WP_008985639
VERSION     WP_008985639.1
KEYWORDS    RefSeq.
SOURCE      Alishewanella
  ORGANISM  Alishewanella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae.
REFERENCE   1  (residues 1 to 209)
  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 209)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 209)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Alishewanella"
                     /db_xref="taxon:111142"
     Protein         1..209
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22433
     Region          1..202
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 meiynseeqq veaikrfwne ygkaivggvv iglatlygwr yyqaeqrasa ealsssysql
       61 lqqqssddaw ltqaqsfisa qgtnnyaifa alltakeava kgdlalasqq lswvvqnskd
      121 ssvkaiaqlr lariqretgd ltaalatvnq ampasfaaaq aelkgdilqq sgdlvaakaa
      181 yqlafdnagq ntqllqikld elahisaan
//
LOCUS       WP_008985906             233 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Alishewanella agri].
ACCESSION   WP_008985906
VERSION     WP_008985906.1
KEYWORDS    RefSeq.
SOURCE      Alishewanella agri
  ORGANISM  Alishewanella agri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Alishewanella.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 233)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Alishewanella agri"
                     /db_xref="taxon:553384"
     Protein         1..233
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=24681
     Region          74..232
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 msnsvsltqy lqlsglaewa tpaftaavae qqqalqqylq qaadtavnwq yqvpelgegg
       61 acslfgvlaa epydltailg gqtaanqqal sklsqitafy qqqagvawfg iyqarqnpag
      121 eavlvklsyf gapsraefpl taefaaisnn stvglsgkar vinsvasylq qggeyytcdp
      181 kvqaeaclpl yaqsgrilgi vdaedfqpev fnpqalallv avcltipdyl pav
//
LOCUS       WP_008987133             477 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Photobacterium leiognathi].
ACCESSION   WP_008987133
VERSION     WP_008987133.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium leiognathi
  ORGANISM  Photobacterium leiognathi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 477)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Photobacterium leiognathi"
                     /db_xref="taxon:553611"
     Protein         1..477
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=55026
     Region          243..471
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mrknnknvml ivftlffvfi ygvlisinys fykreiidke vndlqtlish seqllnkvgf
       61 nvlykkqrdk nylhkilare anvninsiai iysgkyiyst lvgdedrafi tpvnlglnak
      121 eksnlsgrpv isfvaevgnk tllqvffkkh dltmvnklgr afyqigdvki ghdnkliklv
      181 nddkvyvakc dkygfslvie ydrktafinf vkdsvfllsf iffllffiff mlikynnvdy
      241 yvlkkalskn eicpfiqpiv dqnknvigge vlarwikkng eiisplsfip rlekyslips
      301 ltvnlltqvf nsdlvkksnd lilsfnltek clhdekvqqq ciklssrcql ileftessef
      361 envqltletm qklraygiqf alddygtgys slqylnlydf dslkidksfv dtiesseltl
      421 hiiesivlla tklnikliae gvenieqket lqrlgvhkyq gflfykpesl dsfsmri
//
LOCUS       WP_008987922             134 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Photobacterium leiognathi].
ACCESSION   WP_008987922
VERSION     WP_008987922.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium leiognathi
  ORGANISM  Photobacterium leiognathi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Photobacterium leiognathi"
                     /db_xref="taxon:553611"
     Protein         1..134
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=13745
     Region          2..134
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkkqqgftli elmivvaiig vlaaiavpqy qkyvskseas aalasitglr tniethiidk
       61 gtfpttalva ppssalgvvs yvnvtsaagt vqflfnstgv spdtvgkkis lvrtgtgsws
      121 cttdvdasik pkgc
//
LOCUS       WP_008988796             213 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Photobacterium leiognathi].
ACCESSION   WP_008988796
VERSION     WP_008988796.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium leiognathi
  ORGANISM  Photobacterium leiognathi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 213)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Photobacterium leiognathi"
                     /db_xref="taxon:553611"
     Protein         1..213
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=23960
     Region          47..206
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mifspffllk iryliiaifl fgchdalalr athawkvydh aklqnyvdfd iflnayrehl
       61 rvankpimsi idysqpsdar rfliidiekr allhrtfvah ginsgtlyat efsntinsrq
      121 tslgtyrvge vyygkygisl rldgmspsns narrraivlh gasyaepnvi neigmlgrsw
      181 gcpaispeit sevvellkeg gsiyahahnh rng
//
LOCUS       WP_008988797             204 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Photobacterium leiognathi].
ACCESSION   WP_008988797
VERSION     WP_008988797.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium leiognathi
  ORGANISM  Photobacterium leiognathi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 204)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Photobacterium leiognathi"
                     /db_xref="taxon:553611"
     Protein         1..204
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=22733
     Region          42..201
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mkvwmtslii mllsvshasy aahtinqqak iiydktklgk hlkydvflta ykehmrvadk
       61 pimsiidysk psdrrrffii nteekkllhh tfvshginsg dlyatefsni vdskqtslgt
      121 frvaeayhgk ygislrldgm spsnsnarkr aivlhgakya epstikklgm lgrswgcpai
      181 pmqlaakvvh llkeggsiya harg
//
LOCUS       WP_008988873             335 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Photobacterium leiognathi].
ACCESSION   WP_008988873
VERSION     WP_008988873.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium leiognathi
  ORGANISM  Photobacterium leiognathi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 335)
  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 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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 335)
  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   5  (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   6  (residues 1 to 335)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Photobacterium leiognathi"
                     /db_xref="taxon:553611"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38872
     Region          27..194
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <217..334
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mldiafirtl fikpldyaiq khyglsfqql dipellires mslipfkdyl fwldrieelt
       61 ndpsymitla dqmtfssmgg lgewylscpd lplalrriny glsclqsgas yhselsgkii
      121 kwtyenpysk gkgsrhdhlr vavlftqtlr dymgedfspl kieinaqeir sekiaeffqc
      181 pirwgapktq vwlpmsilga snnqppkstk pmlvsnlqld dflnmpqpad taklmfelin
      241 ysryyqypnl efiaeqlsls kqqlqrrlhh fgwtftdttn yvlcniaiky mqqalpieqi
      301 aanlsyknvq sftkafqrnr gitplqyqqq llekq
//
LOCUS       WP_008990545             739 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Galbibacter marinus].
ACCESSION   WP_008990545
VERSION     WP_008990545.1
KEYWORDS    RefSeq.
SOURCE      Galbibacter marinus
  ORGANISM  Galbibacter marinus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Galbibacter.
REFERENCE   1  (residues 1 to 739)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 739)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 739)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Galbibacter marinus"
                     /db_xref="taxon:555500"
     Protein         1..739
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=82524
     Region          32..721
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 maklpvhvdk liedfgphka yapqsgfhgs nepdklvkth ccycglqcgi klkvkdnkia
       61 gfepwedfpy negrlcpkgv mrymqnnhpd rilspikrve gkgfvptswe eamsktvsei
      121 kriqdtygkd sfamlsgvsl tneksymigk farvalktan ldyngrlcmv sagggnkkaf
      181 gldrssnswa dlkhaevili aganvsetfp tlthyiwqar dngaklivvd prmiplarta
      241 dlhlpvrpgg dsalfgailk imvdndwldh dfinnhttgf qetieavkdy dldwaeehtg
      301 ipkekiyqaa qmwgkaktsf llhargiehh tkgvdnvisc inivlasgri grpycgygti
      361 tgqgngqggr ehghkcdqlp gnrditnpeh rkyisevwgi dekdmpgkgl sayeqieaih
      421 rgeikgmisi cfnplislpn nnfvrealek lefyvcidtf lsetarysdi vlagslheee
      481 egtvttaegr vvkineavtp pgkarrdgei imeladrlge gdkfsfptse difnelrvas
      541 kggtadyygi tyqkivdnyg vfwpcktldh pgtprlwedm kfetpdgkah fnpvkyrpas
      601 empnkdypvv lttgrvvsqy lsgsstrrig klvdqypepl leihpklafq ygienrdlik
      661 vktrrgeaef paqvvetire dtvfipyhwg gkfsanqlti dnldpvskip efkvcacqle
      721 ktgkkasqer raeayqsgl
//
LOCUS       WP_008990816             351 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Galbibacter marinus].
ACCESSION   WP_008990816
VERSION     WP_008990816.1
KEYWORDS    RefSeq.
SOURCE      Galbibacter marinus
  ORGANISM  Galbibacter marinus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Galbibacter.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 351)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Galbibacter marinus"
                     /db_xref="taxon:555500"
     Protein         1..351
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38973
     Region          1..351
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mhtriigtgs yipsvitkne dfinhnflni dgstfgsete eiiekfesit giqqrryvre
       61 dqnssdiafl aaekaiedak idketldyii vahnfgdvas gsvqgdtvps iatrvkhslg
      121 innpkcvayd llfgcpgwie gcnhatafik anmaknclvi gaetlsrivd khdrdsmiya
      181 dgagaavlta steegilsql satytseeay ylffgesynk elqenrkyik mfgrkiyefa
      241 vthvpkamke cldksgvpid evkkiflhqa nekmdnailk rfyrqynssv pehimpmnih
      301 tlgnssvati ptlfdmvrkg nmahqelhkg dviifasvga gmninalvyk y
//
LOCUS       WP_008991316             107 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Galbibacter].
ACCESSION   WP_008991316
VERSION     WP_008991316.1
KEYWORDS    RefSeq.
SOURCE      Galbibacter
  ORGANISM  Galbibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Galbibacter"
                     /db_xref="taxon:379068"
     Protein         1..107
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12050
     Region          1..104
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(5..6,24..25,33,36,38..39,41,44..45,47,55,60,67)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(24,55..56,58,84)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 meqnffkqvy kvtrcipygr vttygaiaky lgaaksarmv gwalngnsen envpahrvvn
       61 rkglltgkhh fqgtnlmqql lesegiivkd nqiqnlenyl wdpskel
//
LOCUS       WP_008992133             336 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Galbibacter marinus].
ACCESSION   WP_008992133
VERSION     WP_008992133.1
KEYWORDS    RefSeq.
SOURCE      Galbibacter marinus
  ORGANISM  Galbibacter marinus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Galbibacter.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 336)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Galbibacter marinus"
                     /db_xref="taxon:555500"
     Protein         1..336
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36950
     Region          3..336
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mynskitglg yyvpsnvvsn ddlskimdtn dawiqertgi kerrhvekdg getttsmgve
       61 aakvaiersg ldkndidfvi fatlspdyyf pgpgvlvqrd lglrtvgald vrnqcsgfvy
      121 alsvadqyik tgmyknilvi gselhskgld mttrgrgvsv ifgdgagaai lsreedttkg
      181 ilsthlhseg ehaeqlalia pgmgkrwvtd ilededsenp syfpymngqf vfkhavvrfs
      241 evivealevn nltkedidll vphqanlris qfiqhkfkls ddkvynnimk ygnttaasip
      301 ialteaweqg kikegdtvvl aafgsgftwa saiikw
//
LOCUS       WP_008992554              79 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Galbibacter marinus].
ACCESSION   WP_008992554
VERSION     WP_008992554.1
KEYWORDS    RefSeq.
SOURCE      Galbibacter marinus
  ORGANISM  Galbibacter marinus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Galbibacter.
REFERENCE   1  (residues 1 to 79)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 79)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 79)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 79)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Galbibacter marinus"
                     /db_xref="taxon:555500"
     Protein         1..79
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8304
     Region          1..79
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mqvllfgitr eitsqdvldi pasenlkdvg qlkaylkqky pglgrlssla vavnsayane
       61 dvqitcsdel alippvsgg
//
LOCUS       WP_008993232             166 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Novosphingobium sp. Rr 2-17].
ACCESSION   WP_008993232
VERSION     WP_008993232.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. Rr 2-17
  ORGANISM  Novosphingobium sp. Rr 2-17
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 166)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Novosphingobium sp. Rr 2-17"
                     /db_xref="taxon:555793"
     Protein         1..166
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16995
     Region          27..155
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfdltpaldl pkselyaela saaaalvdge pdsianmanv aaaisqfvpd lnwagfyrvi
       61 rrevggegel vlgpfigkpa ciripmgqgv cgtaaasget qivpdvhafp ghiacdaasr
      121 selvvpvvka gqvvavidld sptpgrfded daagmariae iaarai
//
LOCUS       WP_008994680             239 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Novosphingobium sp. Rr 2-17].
ACCESSION   WP_008994680
VERSION     WP_008994680.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. Rr 2-17
  ORGANISM  Novosphingobium sp. Rr 2-17
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Novosphingobium sp. Rr 2-17"
                     /db_xref="taxon:555793"
     Protein         1..239
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=25832
     Region          2..>228
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mingisirlk qtgrivldva ielapgqtla lvgpsgagkt tvlrsvagly rprqghiacd
       61 getwldsrgg idrpardrrt glvfqsyalf phltaaanva eamldtrpqv rrerveille
      121 rvhlgdlggr lpaalsggqq qrvalarala rnpkvlllde pfsavdqptr rslhrllsei
      181 rattpmpiif vshdvedaar cadqvcfisg grtveqgetr sildnpesql slwlanega
//
LOCUS       WP_008995569             234 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Novosphingobium sp. Rr 2-17].
ACCESSION   WP_008995569
VERSION     WP_008995569.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. Rr 2-17
  ORGANISM  Novosphingobium sp. Rr 2-17
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Novosphingobium sp. Rr 2-17"
                     /db_xref="taxon:555793"
     Protein         1..234
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=26414
     Region          8..158
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mnrwlvnriv espnwnerkl pvsmavlhyt gmrsaqeald rmcdpeaevs ahymidedgq
       61 vtllvpedkr awhagqaywr gvtdvnsasi gielvnpghe wgyrpfpepq mdallpllad
      121 imdrhdipra nvvghsdiap arkqdpgeyf dwgrlgelgl aleiptakmn lfydnpgafy
      181 lamerfgydi tegraavtaf qrrwrpevid gvidgqlggi lfelllerdi grar
//
LOCUS       WP_008993689             249 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Novosphingobium sp. Rr 2-17].
ACCESSION   WP_008993689
VERSION     WP_008993689.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. Rr 2-17
  ORGANISM  Novosphingobium sp. Rr 2-17
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 249)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Novosphingobium sp. Rr 2-17"
                     /db_xref="taxon:555793"
     Protein         1..249
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=26804
     Region          16..236
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mqigclgcks adhdldiama fqpivdtetg lpfayealvr grqgegaaqi lagvtaqnry
       61 afdqqcrvaa iegavaagil dsdarlsinf lpnavyspaa ciqltlktar etgfpterli
      121 fefteneeml dvehvknive syhrmgfata lddfgaghag lgllaqfqtd likldmnlir
      181 gidaslprrm ivegvvrmat glgitlvaeg vetvaeydvl raigvryiqg yllarpgfma
      241 lpeialprs
//
LOCUS       WP_008995775             511 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Novosphingobium sp. Rr 2-17].
ACCESSION   WP_008995775
VERSION     WP_008995775.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. Rr 2-17
  ORGANISM  Novosphingobium sp. Rr 2-17
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Novosphingobium sp. Rr 2-17"
                     /db_xref="taxon:555793"
     Protein         1..511
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=53183
     Region          16..511
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 maetlvplaa rtadafqiae eddvavalrs ldaghvvtlg drrvqllgav paghkfaias
       61 iacgqpvhry rapignatqd iapgehvhsh nlrtalsgeq ayrfagarpv iaptanspar
      121 vfqgyvrpng svgtrnelwi lptvgcvgrl gerlavrgqa mlsamtanga vdgvhafnhp
      181 fgcsqlgadl dgtaailasl alnpnaggvl llglgcesnq ldalleripr qhrdrlkilr
      241 aqsegdefaa gealiadllt amamdkrerv plsklrlgvk cggsdamsgl tanpligrma
      301 davtqaggva ilteipelfg aegllleraq saevfeklaa lvngfkryfl dhgepvsenp
      361 spgniaggit tleekslgav qkgglapvcd virygehlsr agltvleapg ndavsttala
      421 aagatltlfs tgrgtplgsp vptmkiasnh dlaqrkpgwi dfdaalaldi gialaadvll
      481 driiaiasge ltcnernder sigiwkrgvt l
//
LOCUS       WP_008995810             813 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Novosphingobium sp. Rr 2-17].
ACCESSION   WP_008995810
VERSION     WP_008995810.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. Rr 2-17
  ORGANISM  Novosphingobium sp. Rr 2-17
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 813)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 813)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 813)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..813
                     /organism="Novosphingobium sp. Rr 2-17"
                     /db_xref="taxon:555793"
     Protein         1..813
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87326
     Region          60..111
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          89..813
                     /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 mtirnwsvah atlaialsai palviplpaa aqsraavldl dlpagpldas lvrlgrqagv
       61 mivippelar akrtaglrgr hpidqalerl lrgtglrats dgaggfvvsq avsiaprrra
      121 apvpparapm lsanpvsape ieeivvsgyr ateqrsvtkt pqalkdtpqs vsvvtadvia
      181 drgaqslaea myfipnvvtf ndgatggagg ggnslgveyn irgiyesgql nyrrvnglrt
      241 hnrasidlaa lervevvrgp asmfggavpp ggiinlipkr asetfkgfvt arvgsydakv
      301 ieadvggalt sdgalrgria gkyvdegswi dfregdlwvv taalgadltp dttiditgsf
      361 qrrtfveggs faigddgwip diprsrfvgi ptprsegelg widvelrqal asdwmltvrg
      421 ryedgfnaqr atefsyyidr eaglaslnkl nrrysydtfa tdifvsgglp lfgltsnfvf
      481 gadyfdndet vyggrtsdva tinifdpdyg tdigtfsndl aatyasgqsg wgiygqaivr
      541 pvdrlavhlg grydwartta glvaatrqkn naftaraslt yevtdtvtay atynesfips
      601 sgttiegdlv epetgyqvev glkaslikdr lnasiaayrm vrgnvatydp rsgtgeyfvi
      661 avgeqvhkgi eveivgsplp glqlvasaaw qdarvtknnd gmegtipyda qeftaaflat
      721 yelqsgplkg lgfggsvrdl gkyypytypq nllaynpppi vdlqifyrgi ekwdfrlnvf
      781 nifderylss asiygsstfg rprsamlsas rrf
//
LOCUS       WP_008998242             366 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Bacteroides].
ACCESSION   WP_008998242
VERSION     WP_008998242.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 366)
  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 366)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 366)
  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   4  (residues 1 to 366)
  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 366)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..366
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42482
     Region          115..366
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          286..366
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mldiiyyfni fgcltmgmal lliqtapqli nphyrnakrf lgiasiival cnalifynrv
       61 qesvaeifam pvlvaaqlqa alftfivlil fhspyvcrrn ilrhlcptlf fvglylltil
      121 lfpdvriysv deyianitnp vlllrtvfaa tyltqiviyv rlfrreqrny iakienyfsd
      181 tdkyefrwas rlfyeaacig iavlvfsifp aplfdgiitv vitvyyfdfg vryinyqykl
      241 yyealpaiee keesqltkes egdkeledem aklllylqqg vvlgdyaeal hiperklsvf
      301 instygvsfk rwvnnkrvey ateqmakhpd ytmeriaels gfahkshfck ifreitggsf
      361 teyknr
//
LOCUS       WP_008998905             350 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Bacteroides].
ACCESSION   WP_008998905
VERSION     WP_008998905.1
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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..350
                     /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=40399
     Region          8..282
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 megnqsrrid fvdltkgvci ilvvmahvgg afeqldtnsm lscfrmplyf fisgvffksy
       61 eglfgfilrk inkliipflf fylsaflmky ivwkiaprvf qlpvswnell vvfhghdlik
      121 fnppiwflla lfncnilfyl ihflrekhll vmfavtilig cagfylgklq ielplyidvs
      181 mtalpfyvag fwirrynffl ypshrfdkli pvfvvlalvv myftattlgm rtnnytgnif
      241 qvyiaafagi fmimllckkv kkikvvsylg rysiitlsih gpilhflgpl vsryihnswa
      301 qasalllitl sicllltpvf lkvipqmvaq kdllkvkqdh tkktvyedkq
//
LOCUS       WP_008999679             496 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Bacteroides sp. D2].
ACCESSION   WP_008999679
VERSION     WP_008999679.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. D2
  ORGANISM  Bacteroides sp. D2
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Bacteroides sp. D2"
                     /db_xref="taxon:556259"
     Protein         1..496
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54238
     Region          4..496
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 metkylrinp adnvavaivn lpagehlsid gieitlnedi paghkfalkn faegenviky
       61 gypigharma kkqgdwmnet niktnlagll dytynpiqvs ldiphkdltf kgyrrkngdv
      121 gvrneiwiip tvgcvngiig qlaeglrret egkgvdaiva fphnygcsql gddhentkki
      181 lrdmvlhpna gavlvvglgc ennqpdifre flgefdedrv kfmvtqkvgd eyeegmeilr
      241 dlyakaskde rtdvplselr vglkcggsdg fsgitanpll gmfsdfliaq ggtsvltevp
      301 emfgaetilm nrckneelfe qtvylindfk eyflshgepv genpspgnka ggistleeka
      361 lgctqkcgks yvsgvmpyge rlqkkglnll sapgndlvaa ttlaasgchm vlfttgrgtp
      421 fgtfvptmki stnstlaknk pgwidfnagv ivenepmekt cerfidyiik vasgefvnne
      481 kkgyreiaif ktgvtl
//
LOCUS       WP_008999731             348 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Bacteroides sp. D2].
ACCESSION   WP_008999731
VERSION     WP_008999731.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. D2
  ORGANISM  Bacteroides sp. D2
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 348)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Bacteroides sp. D2"
                     /db_xref="taxon:556259"
     Protein         1..348
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=39432
     Region          213..346
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mhcinnmngi asgliiascv fysctsrtge ispvheqqtd slsqdtivqp evkpvnkklt
       61 aeqieiskdl lydqytledt ypykdttrqf qwdkikerla lleniqlqps twailqnykn
      121 rngeaplvrs fkrnaygrva dtlgieryqs vplylltdtl vperygqdge ltrfiedgek
      181 fikaepmftg dewmipkkyv kvigdtivfn kavfvdrhnq niaslersgk gqwvvrsmnp
      241 sttgrhlppy aqetplgmfv lqekkvkmvf lkdgsketgg yapyasrftd gayihgvpvn
      301 aprktqieys pslgttprsh mcvrnatsha kfiydwapvn gtiifvle
//
LOCUS       WP_009001644             350 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Clostridium sp. D5].
ACCESSION   WP_009001644
VERSION     WP_009001644.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. D5
  ORGANISM  Clostridium sp. D5
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Clostridium sp. D5"
                     /db_xref="taxon:556261"
     Protein         1..350
                     /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=39916
     Region          1..290
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mivskgriew idyakaigif civlghtmkg sliwqfvftf qvplffflag vtfnskldyk
       61 afllkktkti lipywtvmai siivfyfmgs faaerlgeei esfswikylc gslygnsksg
      121 ymranlplwf lpclfvvenl lyginklmdk ivvkywikls slmlvslsis fvnyyftrie
      181 glpfametav svlpyailgy gfkkfniprf skmkiaiypt vlmmiclvmg cfintatdcr
      241 sdiygnlfiy viaavcgifg icllcrnips nrylsyigqn tmivlllhkf pvlffqvlfk
      301 ptvnlvsrnq piaciivall smlmcliage vldrvcpwiv gknrfkkeik
//
LOCUS       WP_009002148             255 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Clostridium sp. D5].
ACCESSION   WP_009002148
VERSION     WP_009002148.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. D5
  ORGANISM  Clostridium sp. D5
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
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   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   4  (residues 1 to 255)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Clostridium sp. D5"
                     /db_xref="taxon:556261"
     Protein         1..255
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=28500
     Region          5..>241
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 msaaitfsnv skqfpgtsyy averlsfsve egefvtilgs sgcgkttllk minrlyepde
       61 gsiflfgedt akidvvrlrr gigyviqqtg lfphmtiaen vatvpkllkw dkeriqnrvr
      121 ellelvkldp defqgrypsq lsggqqqrvg laralavepe vmlmdepfga vdaitrtglq
      181 dellslhrgl gktfllvthd iheafklgtr vmimnegkis qfdtpesiir qpadeftaal
      241 irsakeqekm wegyi
//
LOCUS       WP_009002511             577 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Clostridium sp. D5].
ACCESSION   WP_009002511
VERSION     WP_009002511.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. D5
  ORGANISM  Clostridium sp. D5
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 577)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Clostridium sp. D5"
                     /db_xref="taxon:556261"
     Protein         1..577
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=63549
     Region          2..556
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mfhkrllkef rdnqkyvagm vatqwvtlla nvvlmlaaad figkmrsgil gtagiaqilm
       61 ilagvllvrg vmntlnsrfs fqastevkcr lrekvyaklm klggryrdti atseavqist
      121 egvdqleiyf gkyvpqffys llapltlfii vgmmnmkvag vlllcvplip lsivavqkfa
      181 kkmlkrywgt ytelgdsfle nlqglttlki yqadgryaek mdeeaekfrk itmrvlimql
      241 nsisvmdlva yggaaagiil gilefgkgsi sleecffmim isaefflplr llgsffhiam
      301 ngnaaadkif rlldapvpqk gtvcltkgnd vqfqnvsfgy deekqvlkgv sfevpqrgft
      361 alvgesgcgk stiasllmqd hasykgkvtv ggvsvcdlae dtlyskitri rhdsylfkgs
      421 vadnlrmgre dasesemadv lkkvnlydtv mekgglsmql dgkasnlsgg qkqrlalara
      481 ilhdsdiyif deatsnidae senqimkvih glagtktvfl ishrlanvts adqilmikdg
      541 qiaergthle lmgmqgeyar lykgqkelek ytgegaa
//
LOCUS       WP_009003599             172 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Clostridium sp. D5].
ACCESSION   WP_009003599
VERSION     WP_009003599.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. D5
  ORGANISM  Clostridium sp. D5
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Clostridium sp. D5"
                     /db_xref="taxon:556261"
     Protein         1..172
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18607
     Region          4..166
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mnetlkclee rrsirkykae qvpeeileei lragmyaptg mgmqspvmvv vqdadmirrl
       61 salnaavmgt dsdpfygapt vivvladksr gtcvedgslv mgnllnasas lgigscwihr
      121 arevfageeg reilsgwgld sdryigvghc ilgyaaeegk akprkegyvi rv
//
LOCUS       WP_009003839             317 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Clostridium sp. D5].
ACCESSION   WP_009003839
VERSION     WP_009003839.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. D5
  ORGANISM  Clostridium sp. D5
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Clostridium sp. D5"
                     /db_xref="taxon:556261"
     Protein         1..317
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35521
     Region          8..284
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 meksnftcdl hthttrsdga dtpmeviqra aalgvrvlal tdhdtvprrv yseagsetdl
       61 palakaagvk lllgteisce tevedvhiic lgcswedawf semeravsvs rresyqillk
      121 rlgedginit wdevldndgh pikeehvmkk mifeqmawkg yaqnwkqakl mikntpryqi
      181 krekpdpaav irevhrtggi ailahpflia rhaekngetm trkeyidllv eagldgieac
      241 ytydktsyeg plskreiegf irenyegrve imsggsdyha dqkkgvanpr eigecgvtea
      301 yfygnrllag lvskaee
//
LOCUS       WP_009005239             349 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Clostridium
            sp. D5].
ACCESSION   WP_009005239
VERSION     WP_009005239.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. D5
  ORGANISM  Clostridium sp. D5
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Clostridium sp. D5"
                     /db_xref="taxon:556261"
     Protein         1..349
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39558
     Region          7..347
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mavemkfkkk lgtfmldmhl esnsrrigil gasgcgksmt lksiagivtp degriaidqk
       61 evfdsenkvn wkpqkrnvgy lfqnyalfpt mtvkdnisag lkgtkaekad rveemlqkfq
      121 lnglgdrlpg elsggqqqrv alarimayep dmilldepfs aldvflkdrl qqemleilad
      181 yegtvilvsh srdeiyrfse ellimddgri vccgktkeif enpqwkeaar ltgcknitqi
      241 rrlgphslqv pewgielelq kevpadiqyi gvrahdfipv wgdavenclp vevnsiaelq
      301 fekkyflkga edgaeeicwf vqrddwnilv ekgmpdyllv penkilllk
//
LOCUS       WP_009004387             125 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Clostridium sp. D5].
ACCESSION   WP_009004387
VERSION     WP_009004387.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. D5
  ORGANISM  Clostridium sp. D5
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Clostridium sp. D5"
                     /db_xref="taxon:556261"
     Protein         1..125
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14475
     Region          17..123
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mpvnfrpccn kiiksqrhqk aleyaleqir assiapyvna vylygscarg retwnsdvdl
       61 lleldeekyn qselkielri lkaevmtddv kdpetdlkiv vgkewkvntm pfyenirkeg
      121 iliwp
//
LOCUS       WP_009005394             178 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Clostridium sp. D5].
ACCESSION   WP_009005394
VERSION     WP_009005394.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. D5
  ORGANISM  Clostridium sp. D5
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Clostridium sp. D5"
                     /db_xref="taxon:556261"
     Protein         1..178
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19781
     Region          3..175
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mntieciksr rsirkykpdp idhsmidsiv saasyspswk ntqitryiai edpsiigkit
       61 eeftyehnag iikqapmlia vtflkgrsgf erdgsyttkk gdrwqmfdag iasqsfclaa
      121 qeyglgtvim gifdedgisg llelpedqel aaliavgypd hepeapnrks vedllqyr
//
LOCUS       WP_009005528             195 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Clostridium sp. D5].
ACCESSION   WP_009005528
VERSION     WP_009005528.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. D5
  ORGANISM  Clostridium sp. D5
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF004685.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK06029
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Clostridium sp. D5"
                     /db_xref="taxon:556261"
     Protein         1..195
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21325
     Region          2..185
                     /region_name="VdcB"
                     /note="non-oxidative hydroxyarylic acid decarboxylases
                     subunit B; NF041206"
                     /db_xref="CDD:469110"
ORIGIN      
        1 mriivgvsga tgvemsyylm ralrsieeck ihlvmssgak vtwnleskip iekltaladv
       61 vhdeknmaas issgsfvtdg mivmpcsmkt lagiaagyad tliiraadvc lkegrkvvlv
      121 premplnrih lrnlkevada gctivppllt fyngartied qinhivgkil mqfgiaydkf
      181 vpwtgeeeev iedee
//
LOCUS       WP_009006481             398 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Fusobacterium].
ACCESSION   WP_009006481
VERSION     WP_009006481.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium
  ORGANISM  Fusobacterium
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Fusobacterium"
                     /db_xref="taxon:848"
     Protein         1..398
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43643
     Region          1..398
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkilvincgs sslkyqlinp eteevfakgl cerigidgsk meyeviakdf ekkletpmps
       61 hkealelvis hltdkeigvi ssvdevdaig hrvvhggeef aqsvlvndev lkaieanndl
      121 aplhnpanlm girtcmelmp gkknvavfdt afhqtmkpea fiyplpyedy kelkvrkygf
      181 hgtshlyvsg vmreimgnpe hskiivchlg ngasitavkd gksvdtsmgl tplqglmmgt
      241 rcgdidpaav lfvknkrglt daqmdermnk ksgilglfgk ssdcrdmena vkegderail
      301 aesvsmhrlr syigayaaim ggvdaicftg gigenssmtr ekaleglefl gieldkeins
      361 vrkkgnvkls kntskvliyk iptneelvia rdtfrlak
//
LOCUS       WP_009008549             578 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Thomasclavelia
            ramosa].
ACCESSION   WP_009008549
VERSION     WP_009008549.1
KEYWORDS    RefSeq.
SOURCE      Thomasclavelia ramosa (Clostridium ramosum)
  ORGANISM  Thomasclavelia ramosa
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Coprobacillaceae; Thomasclavelia.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 578)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 578)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Thomasclavelia ramosa"
                     /db_xref="taxon:1547"
     Protein         1..578
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=65371
     Region          2..554
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 minkrlvsyl kedkkyiylq vlmqwlalis qvviiaiian minelyqghq vnnfsikvii
       61 iivlilikgy fgklvssfsf kaaknikgkl rcdiyqkvll lnnhysdvis tasltqlmse
      121 gveqleiyfg kylpqffysm lapltlfiil grvefkaalv lfvcvplipv sivlvqkfak
      181 rllnkywgly gnlaerfldn vrglttlkgy qgdqakhlem neeaqrfrni tmkvlvmqln
      241 sisimdlvay ggaalgiiis lysyqggaid lgqtfmmiml saeffiplrl lgsffhiamn
      301 gnaasekifr lldtpvndhk eleiteieki eitrlsfgyd eeivlkdvsl eidepgiygv
      361 vgssgsgkst iakllmgyyd nyqgvlsyng nqvnqvkhqs lmkqitmveh npyifagtvr
      421 snlsdgndnc ddsimievlk kvnlwnyfdg vngldseiee rgnnlsggqk qrlsiarall
      481 hdtsvyifde atsnidiese eiimkvieqm rdekivilis hrlasvenck cnyvfsqgrl
      541 igwgnhkelm rnnpeyielv ntqkeienyg gqanakte
//
LOCUS       WP_009009084             216 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Thomasclavelia].
ACCESSION   WP_009009084
VERSION     WP_009009084.1
KEYWORDS    RefSeq.
SOURCE      Thomasclavelia
  ORGANISM  Thomasclavelia
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Coprobacillaceae.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 216)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Thomasclavelia"
                     /db_xref="taxon:3025755"
     Protein         1..216
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=24730
     Region          2..207
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mirycdnagt lipplfflpl legielvdli dffvldtvcq kikywldkem kiiplsinfs
       61 ieslrgksfv eriletckky qiptkyieie itervhdekn feiktviskl rsagfivaid
      121 dfgteyanla llsdaefdil kldkslisnv alnprtkiim eyiskichrl gvdmiaegie
      181 seeqfftlcs ygvetvqgyl fskplainvf eekyls
//
LOCUS       WP_009010723             150 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Prevotella].
ACCESSION   WP_009010723
VERSION     WP_009010723.1
KEYWORDS    RefSeq.
SOURCE      Prevotella
  ORGANISM  Prevotella
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Prevotella"
                     /db_xref="taxon:838"
     Protein         1..150
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16349
     Region          11..144
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mesltqilvd ygywgmflsa flagsflpfs seavmlglla agvdpvlllv ygsignvlgg
       61 mlnyglgrlg klewleryfh vkqksldray rfmdgrgawm gffaflpilg saitivlglt
      121 ranivlsvls itlgkvlryi vliwgatslf
//
LOCUS       WP_009009534             274 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Thomasclavelia ramosa].
ACCESSION   WP_009009534
VERSION     WP_009009534.1
KEYWORDS    RefSeq.
SOURCE      Thomasclavelia ramosa (Clostridium ramosum)
  ORGANISM  Thomasclavelia ramosa
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Coprobacillaceae; Thomasclavelia.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Thomasclavelia ramosa"
                     /db_xref="taxon:1547"
     Protein         1..274
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31612
     Region          1..248
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mvyadlhvht aysdgihsie etiklakekg ikviaitdhd tvfhfeevqk vcrqngleti
       61 rgvemscydy dvhkkvhvvg lglnnhpyhv eklcqktlqc rdeyhhelik ilnqkglnit
      121 yedakeyapy nivfkmhlfl aivhkypeyn dinkyrelfm setsldvdsk mgyidikegi
      181 kairedggia iiahpceykn ydeiekyvsy glqgieishp smesedyplt qelanrfhli
      241 rsggsdfhni hltaigdfgl tkeqfdelke emgr
//
LOCUS       WP_009011403             131 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: endonuclease domain-containing protein [Prevotella].
ACCESSION   WP_009011403
VERSION     WP_009011403.1
KEYWORDS    RefSeq.
SOURCE      Prevotella
  ORGANISM  Prevotella
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae.
REFERENCE   1  (residues 1 to 131)
  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 131)
  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   3  (residues 1 to 131)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Prevotella"
                     /db_xref="taxon:838"
     Protein         1..131
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15451
     Region          30..128
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mtkenrkkct yktaspdryh ilkdfakenr mdmtlaeevl wkelkgtrgd chfrrqhpig
       61 dfivdfvcls qnlvievdga yhkqplqevd detrteylne mgfnvlrftn eeiytdidnv
      121 ieqitefinn e
//
LOCUS       WP_009011526             159 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Prevotella sp. C561].
ACCESSION   WP_009011526
VERSION     WP_009011526.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. C561
  ORGANISM  Prevotella sp. C561
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Prevotella sp. C561"
                     /db_xref="taxon:563031"
     Protein         1..159
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17710
     Region          1..152
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mtrkeqyeql tvqiaglikd etnligilan vsaalheafp erffwvgfyl qahgnmlrlg
       61 pfqgsvacyt ipygkgvcgk aweeghtliv pdvetfpghi acsslsrsei vvpmyddaht
      121 frgvldidst rlndfdeddk eglgriidll meetqdlfl
//
LOCUS       WP_009011577             171 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Prevotella].
ACCESSION   WP_009011577
VERSION     WP_009011577.1
KEYWORDS    RefSeq.
SOURCE      Prevotella
  ORGANISM  Prevotella
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Prevotella"
                     /db_xref="taxon:838"
     Protein         1..171
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18896
     Region          3..163
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mealealltr rsvrsyearm peqelidkvm eaglyaasgk nmqtaiivev tnkevrdrls
       61 vinaeimgvt sdpfygapvv lavladkssp nhvydgalmm gnlmnaahav glgscwinra
      121 kemfereegk qmlrewgveg dyegigfcil gyttkegkta prkanrifyv r
//
LOCUS       WP_009012309             221 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Prevotella sp. C561].
ACCESSION   WP_009012309
VERSION     WP_009012309.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. C561
  ORGANISM  Prevotella sp. C561
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Prevotella sp. C561"
                     /db_xref="taxon:563031"
     Protein         1..221
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24998
     Region          133..208
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mkrlltiivl mltsivaana qgsvtvsqsa eidalvngkk askknnkdrq kvesqnetar
       61 qniktpdtrq ltvpklnehk peiarpdnst lqpvrtkmvk rlvrrphvps wdevdetriv
      121 tkrikkgtqk vrgfrvqvys ggntrvahqq adkagqkake lfpdqpvyvh fysprwmclv
      181 gnftnynaak kimrtlrteg yphanvirmm vtiktsqvvn n
//
LOCUS       WP_009015250             282 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Acidaminococcus].
ACCESSION   WP_009015250
VERSION     WP_009015250.1
KEYWORDS    RefSeq.
SOURCE      Acidaminococcus
  ORGANISM  Acidaminococcus
            Bacteria; Bacillati; Bacillota; Negativicutes; Acidaminococcales;
            Acidaminococcaceae.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Acidaminococcus"
                     /db_xref="taxon:904"
     Protein         1..282
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31335
     Region          1..249
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mladlhmhtt fsdgvntpee lvreaekahl camaitdhdn tlaydeakkv idarqdgihl
       61 irgvemdtdy kgkdvhvlgf hfdpavpifq qalawnrsgr vervmkiiek iqslgyelsf
      121 qevkreaaga hslgrphiar vlvkkgyfpt vkdvfdtlia agkpaylrqv kmspfeaari
      181 ihkaggiavl ahpaeienls yveeilhsgv mdgmevfhps vlqeknkhdw laiakkyhlm
      241 vsggsdlhgn pgrfpmhlge fsipydavse ivtypqnrgn ak
//
LOCUS       WP_009015708             194 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Acidaminococcus].
ACCESSION   WP_009015708
VERSION     WP_009015708.1
KEYWORDS    RefSeq.
SOURCE      Acidaminococcus
  ORGANISM  Acidaminococcus
            Bacteria; Bacillati; Bacillota; Negativicutes; Acidaminococcales;
            Acidaminococcaceae.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Acidaminococcus"
                     /db_xref="taxon:904"
     Protein         1..194
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21134
     Region          7..158
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mtrkeqetlf ekcrtyrrfl qkplpeglls ylvgiahkrs cgrngqvlsf yaavsskala
       61 allphlhwaa alpkeigtpq keeepvalif lvrpkdaspi slidagiavd smaycamceg
      121 vgsailaald raaiqgilgl ekdqevflcl algypahkst vvpvpesgtl dyyvdekrny
      181 fvpkknlsdv mtvl
//
LOCUS       WP_009016267             270 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Acidaminococcus].
ACCESSION   WP_009016267
VERSION     WP_009016267.1
KEYWORDS    RefSeq.
SOURCE      Acidaminococcus
  ORGANISM  Acidaminococcus
            Bacteria; Bacillati; Bacillota; Negativicutes; Acidaminococcales;
            Acidaminococcaceae.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Acidaminococcus"
                     /db_xref="taxon:904"
     Protein         1..270
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29697
     Region          4..249
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mnrkvdlhlh tiasdgswtp reavlaakka glgimavtdh dslgsvapvm klapkegiev
       61 iagvemcsty egrcfhilgy gfdcsnpill ahlahncrll eetderaigi lseegwpvsi
      121 keyrayvydp rrggfkalfy lidkglcrdv kdffsrifik krgldfpvfp sieetvatlh
      181 kaggvallah aashfhgpgl artleavgek pldgfecyhp ahskedtktl laycqqhhkl
      241 isggsdchgr fvdgriighp diheseirlf
//
LOCUS       WP_009016289             398 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Acidaminococcus].
ACCESSION   WP_009016289
VERSION     WP_009016289.1
KEYWORDS    RefSeq.
SOURCE      Acidaminococcus
  ORGANISM  Acidaminococcus
            Bacteria; Bacillati; Bacillota; Negativicutes; Acidaminococcales;
            Acidaminococcaceae.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 398)
  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 398)
  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 398)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Acidaminococcus"
                     /db_xref="taxon:904"
     Protein         1..398
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44804
     Region          1..69
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          325..383
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mkhigeylkq rrceknitle evasqtgire qyltalesgd fekipgdvfi kgfirnygnf
       61 leengndlve aytkglatpe alheplkaap sdvkeqpevl qepasspast adatpendee
      121 rtmvvtpsmm eearrsweee eafeeeqekt tpkvqavike iddepepden qkeesgivkk
      181 lrhfiesily eevdeddded ddaddealen gedrqesply ayqkkerqdn rkgvsaylni
      241 rifgivfaif fgifcvvmay flfggktmpe ipattslsds vksensstrk aeeakkeekq
      301 petkeekkgd tkafgkeqkn gvtvtvtynk pvwteadidg krvetatvsa gstrtyngks
      361 tvklsfgsir dvsikvngkd yklkdtewgt msktfraq
//
LOCUS       WP_009016542             686 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Parabacteroides].
ACCESSION   WP_009016542
VERSION     WP_009016542.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 686)
  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   2  (residues 1 to 686)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..686
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=80475
     Region          52..120
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkrlfiilsi illinsyyan sqieysvdkw meyveelale tedteriesl yadlsylteh
       61 pfdlnavtee qlkrlpflsd rqieqllsyr krygnmvsiy elkniedidf qtislllpfv
      121 yigdnlvekr lltvknllky grnelqiryd qcfqqkkgyg eqtdsilsly pnrkyrgepf
      181 yhslrysytf edrlqagfva ekdagepfwn ayhkgydfys ahlflkdinw lkslaigdyk
      241 msfgqglvis ndfspsrtav vaqaerrtng frrhfstneq dffrgvasti tiknldisvf
      301 ysyrkmdaav dsltftslkt dglhrlqrdw ekrkmitmqv yggniryats hfhvgltals
      361 ysfgkfkmdp dpkpynlfyf rgsnnfnigv dymlksnrik fygetalskn gaistlnalq
      421 ltpasyisfl vlyryydrry qalfgnafsq gstvqneqgv ymglqltpia rwklsvyadl
      481 frfpwlkygi dapsggqeym aqidytpsrn ysaylrykyr qkekngtfen dnllrinsyk
      541 qhrirfqqvy nfsspfifkt sldgilfddp ikklnkgimi sqsigwkptt lplqmdgyla
      601 wfhtddynsr vssyeknily afnmpsfygd gmrfaltfrl diwkrlslsa klahthywdr
      661 dligtdteei sgsdktdlya llrwkf
//
LOCUS       WP_009017162             293 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: hydroxypyruvate isomerase family protein
            [Parabacteroides].
ACCESSION   WP_009017162
VERSION     WP_009017162.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 293)
  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 293)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..293
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32473
     Region          46..293
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 menisrrtai ktflaggval attgieaaaa akkktdvkep lkgnvrhsvs kwcfgdykld
       61 efceickhig iesvelldpv dwpivqkhgl tvamaqgagl gidrgfndpa lhdelvasye
      121 kvipmvadag ltnlicfsgr rngvtdlqgw encekglkrl iplaekhkvv ltmellnsvg
      181 hkdylcdhtv wgaelcrrig spnfkllydi yhmqimegni ienirkyhpy fshvhtggsp
      241 graeidetqe lyypaiikal metgykgfvg qefvpaqedk iaslekciri cdv
//
LOCUS       WP_009017489             158 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Parabacteroides].
ACCESSION   WP_009017489
VERSION     WP_009017489.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 158)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..158
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17439
     Region          8..155
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 maeelrikng dkqemyetll pqiaslvgne tdlianmani aaalkqtfgf fwvgfyrvid
       61 nqlvlapfqg piactrikyg kgvcgtawke artiivpdvd afpghiacss asrseivvpv
      121 iwedkviavl didsdkldsf netdqiflek ivellphq
//
LOCUS       WP_009017799             569 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Parabacteroides].
ACCESSION   WP_009017799
VERSION     WP_009017799.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 569)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..569
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=65566
     Region          481..561
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mrksplalll sliclisshn eiqgqghppt dslrqlaatc egkekhdllm riamstndia
       61 dwdatlndai drcdtpaicq srlnriqclf nfysvdsaii eaqeslpfil dakqysfyfs
      121 tyntyisglf kqrrfdeare eatamfetaq qvkqpvgmtm alqvqgsmyy klglydqalt
      181 slekgiaicp tyengenqvl yisavlyewl fmtalkvndt erisryadsy aalvkwrdeh
      241 gkvdptghyp vtsrslqals flkkgqiket rrlldeaarf ihpqipanay ehfyearrel
      301 remtgdyqga ikdmdillaa hegdlsfymd dllkkaella hsgdprscis lyhtyiqakd
      361 svnrldiasr mdqlrtiyev drlnqerqya rnwmfaaftg clllvlllag yiiysqslka
      421 knqvlyrriq eqirqenkav etikqipend lsrelrlfin lnellkkekl ytdptlnrdd
      481 laqrlgtnrt ylmeavrtyg gnmtvreyiy dfrlkhaael lsspsalsid qicydsgfas
      541 rsvfyrlfrq syglspneyr klaekeken
//
LOCUS       WP_009018125             269 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Parabacteroides].
ACCESSION   WP_009018125
VERSION     WP_009018125.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (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   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12122938
            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="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30876
     Region          3..111
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          48..255
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 myheftpcaa lvpfidkfwv fkgftdigtr fkiladgctd fifsignmtv ptdehsmimq
       61 pyrsyfvgpm rvysdltatt ntlhmlgvrf hpcglaaftn eplgqfadlr iqssdinllf
      121 dnsfaemlce qpddsvriri iegylirllt qsiqvdrqii yatsfikqsr gqlpvqnlid
      181 kicicqrhfq rkfkdttgyt pkefsriikf qyaievlrna phtdlssial dcgyydhshf
      241 ikefkrlagd vpsyfltlpn ptdepltyi
//
LOCUS       WP_009020693             100 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Luminiphilus syltensis].
ACCESSION   WP_009020693
VERSION     WP_009020693.1
KEYWORDS    RefSeq.
SOURCE      Luminiphilus syltensis
  ORGANISM  Luminiphilus syltensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Halieaceae; Luminiphilus.
REFERENCE   1  (residues 1 to 100)
  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   2  (residues 1 to 100)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Luminiphilus syltensis"
                     /db_xref="taxon:1341119"
     Protein         1..100
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10696
     Region          37..95
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mqslpvlphh fsrlvgslfl alalllaadf slaedlpvni ntataeqlsd alkgigmska
       61 vkiveyrean gpfehidels evngigestv dknrqiivld
//
LOCUS       WP_009020834             186 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Luminiphilus syltensis].
ACCESSION   WP_009020834
VERSION     WP_009020834.1
KEYWORDS    RefSeq.
SOURCE      Luminiphilus syltensis
  ORGANISM  Luminiphilus syltensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Halieaceae; Luminiphilus.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Luminiphilus syltensis"
                     /db_xref="taxon:1341119"
     Protein         1..186
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=19950
     Region          1..186
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mdrivigisg asgviygvra lqllaplpie vhlvmsksae ltvhyeldlk paeiremade
       61 yhpvrnvgas iasgsfsgmg mmiapcsirt lgeivsgnts slltraadva lkerrrlvlm
      121 vretplhlgh lrnmvaatem gaviappvpa fytqpdsvda mvtqsvgrvl dlfgidvegt
      181 rrwtes
//
LOCUS       WP_009025863             143 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Bradyrhizobium sp. ORS
            375].
ACCESSION   WP_009025863
VERSION     WP_009025863.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. ORS 375
  ORGANISM  Bradyrhizobium sp. ORS 375
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 143)
  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 143)
  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   3  (residues 1 to 143)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Bradyrhizobium sp. ORS 375"
                     /db_xref="taxon:566679"
     Protein         1..143
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=16213
     Region          17..119
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mgkrpisdfk rrtakrlrek atgaedilwr hlrrleiegt hfrrqvvigp yiadfacltr
       61 rliievdgsq hgedaniqrd eartrwlnse gyrvlrfwnn dvmtrteavl eaihtvlaat
      121 pprlssagdp ppqgegdpsr get
//
LOCUS       WP_009026954             507 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Bradyrhizobium sp. ORS 375].
ACCESSION   WP_009026954
VERSION     WP_009026954.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. ORS 375
  ORGANISM  Bradyrhizobium sp. ORS 375
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Bradyrhizobium sp. ORS 375"
                     /db_xref="taxon:566679"
     Protein         1..507
                     /product="UxaA family hydrolase"
                     /function="16.11 : Scavenge (Catabolism)"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=53488
     Region          4..507
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mapapvirlh pedsvliara slppglavad gvvtldripa ghkvavrpia qgepirrygq
       61 iigfatapia pgqhvhtqnc emgdfakdya ygvdvkptpn fdlpatfegi rrpdgrvatr
      121 nyigiltsvn csahvaslva dvfkknpftg dnpladypnv dgvvalthkt gcgmtldepl
      181 kllrrtlggy arhanfsavi vlglgcevnq igglmeeqkl agrlraldiq evggtrktve
      241 agiafvkeal adannvrret vpaseltval qcggsdgysg isanpalgaa sdlvvrhggt
      301 vilsetpety gaehlltrra vsrevgeklv slmrwwedyt aregaemnan pspgnkaggl
      361 ttilekslga makagstnlv dvlhyaeavt kkgfvfmdtp gydpvaatgq vagganlvcf
      421 ttgrgsvfgc kpapsiklat ntpmykrmed dmdvncgtil egqesvqecg qrifdlilkt
      481 asgqptkses fdfggaefap wvlgatm
//
LOCUS       WP_009026645             515 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Bradyrhizobium sp. ORS 375].
ACCESSION   WP_009026645
VERSION     WP_009026645.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. ORS 375
  ORGANISM  Bradyrhizobium sp. ORS 375
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Bradyrhizobium sp. ORS 375"
                     /db_xref="taxon:566679"
     Protein         1..515
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=54191
     Region          432..507
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 madryqdrpf padgfgrggn qsgdadplae larligqndp faasgrgtpq aqqrpmprpa
       61 apvpeqpaaa mppagapawm qraqpaaanp fadmgreqpq papappafpa gfqdprgqpg
      121 fpeqdfapaa prpqpgypna efadqlskld ysvgdsrhgf aendrdynrd gyddndqdss
      181 ryddalfgqm gggqqgfqgd nefqdgqygy qdgydegeee erprrrggms tvlavltlav
      241 vgtggaygyk tyissgrtge ppiiradnsp tkimaqqdtt pkvpdrllgg dggeklvsre
      301 etpmdlntrg gnprvvfpqm sqnggppptt ppsvtpaqia nangilpnsd prpiktlsvt
      361 ggnqagaadp gmppanpppt kqamkgkksp ananasaate tpmpltpqpa tapariaaav
      421 pvteqtqter tggylvsiss qaseaeamts ykavqdkyta vlgkyepiik rmdlgdkggv
      481 kyraavgpfa tkeeankmcg tlktaggqcf pfsnn
//
LOCUS       WP_009027202             169 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Bradyrhizobium sp. ORS 375].
ACCESSION   WP_009027202
VERSION     WP_009027202.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. ORS 375
  ORGANISM  Bradyrhizobium sp. ORS 375
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Bradyrhizobium sp. ORS 375"
                     /db_xref="taxon:566679"
     Protein         1..169
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=17699
     Region          68..141
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mrapnrcrrg vgvasgival amltlqahea aaqqvaptpa vkeaptpake pppppsvtil
       61 gardahgvlg rdvrsstged mghivdvivd ltgtvraavi dfggflgvgs rkivvdwtal
      121 dfkhiaeksd qvtldltkeq vkaapeyked kpvvvlgaag klspwdfdh
//
LOCUS       WP_009026504             177 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Bradyrhizobium sp. ORS
            375].
ACCESSION   WP_009026504
VERSION     WP_009026504.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. ORS 375
  ORGANISM  Bradyrhizobium sp. ORS 375
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Bradyrhizobium sp. ORS 375"
                     /db_xref="taxon:566679"
     Protein         1..177
                     /product="TRAP transporter small permease subunit"
                     /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=19385
     Region          7..173
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mpsialfvrg vetlngwvgr avawlslgtv lvcfatvylr yalntnftwl qeayvwqhaa
       61 aivlggaytm mtggfvrvdi fyskmtprrr awvdlfgtll flfpfmavvg wafgrhfwsa
      121 avvsegspnp gglpawwllk gtlvifvalt vlqglamigr sllvfggree fagtssh
//
LOCUS       WP_009027427             193 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Bradyrhizobium sp. ORS
            375].
ACCESSION   WP_009027427
VERSION     WP_009027427.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. ORS 375
  ORGANISM  Bradyrhizobium sp. ORS 375
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 193)
  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 193)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 193)
  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   4  (residues 1 to 193)
  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   5  (residues 1 to 193)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Bradyrhizobium sp. ORS 375"
                     /db_xref="taxon:566679"
     Protein         1..193
                     /product="TRAP transporter small permease subunit"
                     /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=21573
     Region          3..172
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mqallklsrg idaftswtgk rlawlillav iistvnaiir ktldtssnsw lelqwvlfaa
       61 vfllcspwtl ldnehiridi inamlpkwlr dtidvvghvl fliplcvvmi itsvpfflrs
      121 feineqssna gglpqwpaks limigfvfll vqaiselikr iavmrglipd phaarshgie
      181 aevehlveai ekk
//
LOCUS       WP_009028113             287 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Bradyrhizobium sp. ORS
            375].
ACCESSION   WP_009028113
VERSION     WP_009028113.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. ORS 375
  ORGANISM  Bradyrhizobium sp. ORS 375
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Bradyrhizobium sp. ORS 375"
                     /db_xref="taxon:566679"
     Protein         1..287
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31685
     Region          6..280
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 msetnatsda afcaalvreh dfdryastlf vapeirrall slyafnveis rirdvvsqpl
       61 pgevrlqwwh dalsgqahgg iegnpvaael lstvqrfalp vtrltrlide hqfdlyndpm
      121 ptmaaldgyl gdtrgtlfal aaqimsppfe gadhlahhag ialgilqvia slprdaahrq
      181 lyvpldllar hgvgredmfa gkttsairsm ladlreqarq hldhtlelag qappavrpal
      241 lplalvrrdl sraernvsdp fqpqqrsrla tlwtlwraar tvsfrgr
//
LOCUS       WP_009028927             346 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Bradyrhizobium sp. ORS
            375].
ACCESSION   WP_009028927
VERSION     WP_009028927.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. ORS 375
  ORGANISM  Bradyrhizobium sp. ORS 375
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Bradyrhizobium sp. ORS 375"
                     /db_xref="taxon:566679"
     Protein         1..346
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /function="6.15 : Photosynthesis"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38220
     Region          3..277
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mswqtdiaic rrmlrggskt ffaaskvlpr mvgdpaialy afcreaddai dgpgrrvdav
       61 eilherldri ydgrpddnpv dralagvvah faipralpea lleglawdaq grryeslsdv
      121 layavrvagt vgvmmsllmn rreaetigra cdlgiamqlt niardvgeda rngrlylpqq
      181 wlreagldve twraapffdd riarvtarll avadvfyara aagitdlpws crpgihaarl
      241 iyaeigreia raefdsmsqr avvsasrklq llgkaavvsl aqaqpslapl rpearmlida
      301 vviadaqrph alarpgrtmh dralwvidlf erlerrdqfl rsgrts
//
LOCUS       WP_009028844             389 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Bradyrhizobium sp. ORS 375].
ACCESSION   WP_009028844
VERSION     WP_009028844.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. ORS 375
  ORGANISM  Bradyrhizobium sp. ORS 375
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 389)
  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 389)
  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
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 389)
  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   5  (residues 1 to 389)
  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   6  (residues 1 to 389)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 389)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 389)
  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 11513089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Bradyrhizobium sp. ORS 375"
                     /db_xref="taxon:566679"
     Protein         1..389
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40778
     Region          8..>58
                     /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"
     Region          78..321
                     /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 mrlvrsrhdt rsailgylwc sggsfrpdla agvalteasi sriisdlkae gvieetrraa
       61 pyrggpslfi tlsnaisvaa ieisnnrlya aigtlagetl yaerydlpdg igaaavtatv
      121 travcelgsw aaprgivleq lavsipgydp dlraspivpl dvaaladalq relpetparl
      181 tnsmvarava hrlqmgtgvl ggsyffvfvg hgvgaaivde laesgdvetc eighvvidrg
      241 grccrcghgg clepyvstva ladilqvqes dligrgdrwp ddydispaar aeikarlgll
      301 glaignalnl trqrnvviag wpgalpaedr avvmeaigas rlgglqgial tfstaslgre
      361 pvsglalaaf sfirrsgarr aqqqqlisn
//
LOCUS       WP_009030688             461 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Bradyrhizobium sp. ORS 375].
ACCESSION   WP_009030688
VERSION     WP_009030688.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. ORS 375
  ORGANISM  Bradyrhizobium sp. ORS 375
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 461)
  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 461)
  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 461)
  AUTHORS   ter Beek,J., 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 461)
  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 461)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Bradyrhizobium sp. ORS 375"
                     /db_xref="taxon:566679"
     Protein         1..461
                     /product="CmpA/NrtA family ABC transporter
                     substrate-binding protein"
                     /function="16.1 : Circulate"
                     /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=50378
     Region          101..340
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 msifddpfda dsrvnagcic gqhrspaehe hatlalrcep vvasqekrye nvvasavlra
       61 vfpevttrra flksvgaata laavsqffpl ktateafaea gtpekkdlkv gfipitcatp
      121 iimaaplgfy akaglnvevv ktagwavird ktinkeydaa hmlapmpiai slglgaqpip
      181 ftvpaienin gqgivlsmkh kdkrdpkdwk gmkfaipfdy smhnyllryy laehgidpdt
      241 dvqlrsvppp emvanlradn idgflapdni cqraiydgvg ylhilskeiw dghpccsfaa
      301 srefitsapn sfaaltraiv datayaskae nrkqiaeaia panyinapvt vleqvltgty
      361 adglggvktd pkrvdfdpfp wqsfavwmlt qmkrwgqikg dvdykavaeq iylatdtrkv
      421 mtdmglappk dsyksfsvmg ksfdptkpdd yvasfkikka s
//
LOCUS       WP_009032535             359 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Indibacter
            alkaliphilus].
ACCESSION   WP_009032535
VERSION     WP_009032535.1
KEYWORDS    RefSeq.
SOURCE      Indibacter alkaliphilus
  ORGANISM  Indibacter alkaliphilus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 359)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Indibacter alkaliphilus"
                     /db_xref="taxon:579922"
     Protein         1..359
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39610
     Region          4..356
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 msvysvitgs gkyipeivvk nqdflknhfv nekgedlpks nedivnklqe itdiqerryl
       61 skeyntsdmg yfaadqaika sgidpekldy iicahnfgdi lhdnkksdlv palasrikhl
      121 lkiknpycva ydlpfgcpgw vqgviqadyf iksgdancvl vigaeslsri adphdidsmi
      181 ysdgagavvv eaknsekpvg ilahktrsdt yseahylkmg vsyhpnfedn tlfmkmngrk
      241 lyeyalntvp qlvvdtieks gipfkkikkv lihqanakmd eaiiqrvfkl agisgvksee
      301 impmtisklg nnsvatvpil ydmivknels ghqissgdhi vfasvgagmn vnafvylvp
//
LOCUS       WP_009032893             448 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Indibacter alkaliphilus].
ACCESSION   WP_009032893
VERSION     WP_009032893.1
KEYWORDS    RefSeq.
SOURCE      Indibacter alkaliphilus
  ORGANISM  Indibacter alkaliphilus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae.
REFERENCE   1  (residues 1 to 448)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Indibacter alkaliphilus"
                     /db_xref="taxon:579922"
     Protein         1..448
                     /product="amidohydrolase family protein"
                     /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=50118
     Region          29..448
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mkksytfcfc lfivltsipq llyaqeikal vggtmidgfg gpplrnsvii ienerikeig
       61 qvgflpipeg aevistegms vlpglwdmhv hlmlnghsny thwdttyidi lepvimpssa
      121 hqllragvts ardlgaplea sinvrdrink geipgptiyv sgpfiqkepy pgtkafrwgv
      181 ngpadarakv kklvdagvdv iklidhdemt feeakavvde ahkygipvis hshrpdeiri
      241 glqigvdcfe htglasapey pediiamike rtakmnmgpl fwtptvegly nyeymrnnpe
      301 klddpdwhld lpdsiirdir aslrfpgrmp yfqltpvrkp tlerkinqlk dagvvmmigt
      361 dsgipmkfhs qstwneldvw vnefgfdpml tikaatywpa vsmkvdqdyg tisegkyadi
      421 iavkgdvlry isllqnvdmv ikhgkrvk
//
LOCUS       WP_009031156             689 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Bradyrhizobium sp. ORS 375].
ACCESSION   WP_009031156
VERSION     WP_009031156.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. ORS 375
  ORGANISM  Bradyrhizobium sp. ORS 375
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 689)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 689)
  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   3  (residues 1 to 689)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..689
                     /organism="Bradyrhizobium sp. ORS 375"
                     /db_xref="taxon:566679"
     Protein         1..689
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /function="16.5 : Explore"
                     /function="16.12 : Sense"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=73622
     Region          14..660
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mpvtsdseay pvaqfrktyf eecaelmdal qsnlellang qeddetlhai frsvhsvkgg
       61 agafgctdlv afshtfesll dalrdhkipa thdikqlllr asdaladivn aarleqqlpp
      121 nfggdisaam rdalqgagqs advasapavp eaktlteqty rirfrphtem lkkaneplll
      181 irqlgklgsl stevdgsnlp plesldpeaa ylnwsftldt avprsaiqdv fefveddcdl
      241 eiessepaap raeaaasdtt gasdstgava atvaavgvaq sirvdvdkvd rlvnlvgelv
      301 isqamlteqg lglpadkype liqgiealaq sarelqesvm airaqpvksv farmprivre
      361 laatlgkevr ivtsgemtei dktvieqlnd plthmirnal dhgieppver iaagkvrqgt
      421 ihlsaaqrsg rivievsddg rginkekila kakarglvpa ganltddein eliflpafst
      481 aevisnisgr gvgmdvvkrn vqalggrisv ksrfghgssf tlslpltlav vdgmvvsvgr
      541 etfiiplvai venlrpqtad ihpvvgrghv lalrgeylpl vylhrlfsis daigdpcrgi
      601 viivqsesag rvgivvdell gqqqvvvksl eanyepvdgi sgatilgngr valildvarl
      661 heidvrgtam rlpppdapte tekdlthaa
//
LOCUS       WP_009033079             305 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Indibacter alkaliphilus].
ACCESSION   WP_009033079
VERSION     WP_009033079.1
KEYWORDS    RefSeq.
SOURCE      Indibacter alkaliphilus
  ORGANISM  Indibacter alkaliphilus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae.
REFERENCE   1  (residues 1 to 305)
  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 305)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Indibacter alkaliphilus"
                     /db_xref="taxon:579922"
     Protein         1..305
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33490
     Region          42..301
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mqrrnfikni slggaaaava ggqslsayas tkkagetfnl dyaphfgmfk ghagddlmdq
       61 lkfmadqgfr sledngllgr pievqnkige qleklgmrmg vfvidagdnw kislttgkke
      121 fvdtfvkvck dsveaakrvn akwatvvpgf fernlpigvq tgnviealkr gteilephgl
      181 tmvleplsdt pelflrtsdq tyaickavgs ssckilydiy hmqknegnli fnmdkcweei
      241 ayiqigdnpg rkepgtgein ylnvfkhids kgfkgilgme hgnalpgkeg eqaliaayrk
      301 adqfk
//
LOCUS       WP_009033454             805 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Indibacter alkaliphilus].
ACCESSION   WP_009033454
VERSION     WP_009033454.1
KEYWORDS    RefSeq.
SOURCE      Indibacter alkaliphilus
  ORGANISM  Indibacter alkaliphilus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae.
REFERENCE   1  (residues 1 to 805)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 805)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 805)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..805
                     /organism="Indibacter alkaliphilus"
                     /db_xref="taxon:579922"
     Protein         1..805
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=92587
     Region          55..789
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mryfaflfsl laslslgval siqfgtvppl gklldpnqgf wqnafsedyt vkekialenl
       61 ssavevhyde hliphvfaen eedlfrvqgy itakhrlwqm efqtmaaagr iseivgpial
      121 dvdklarrkg lpysaenatq fiqqndpdml vlveaytdgv nqyiaeldya qlpleykvln
      181 yrpepwsvfk sflllkymad mlvgdsdlqy snlrkilget llnklypdfp edqdpviepe
      241 rnwnfsplki ekpedidyps edillsmlpr pepgigsnnw avapkktkng haliandphl
      301 slnlpslwya mqlstpefrv kgatlpgalg iisgfnenia wgvtnatrdt rdwykiqfrn
      361 serteylynd rwiqsnfrie eikvkgqptv kdtvvythhg pvvfdknfra erqdvnfalk
      421 wtahlesneq ktflllnkgr thadyieale hytspaqnfv fasttgdiam kvqgrfplkw
      481 egqgkflmdg ndpkyewqgf ipsahnpatl npargfvssa nqhavsqsyp yyvfdnsyeh
      541 yrnrrlnnkl remdqitled mkslqfdsfh lhaaealpvm lnlmdvenmq dldestakyl
      601 eylkewnfnt fpnqeaptlf qvwwnnlyks vwtfmerdsl pitypnkyqt vrllreepes
      661 sifamndnvk ktavdhvkva fekmveemki wedekgeftw atykstsinh lvpnfesfsr
      721 kgiytgggsg ilnatgsrhg aswryvaemg dkvkaygiyp ggqsgnpgsk fydnfikiwa
      781 ngeyvnfdfr svndkngllf stefy
//
LOCUS       WP_009034468             700 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Indibacter alkaliphilus].
ACCESSION   WP_009034468
VERSION     WP_009034468.1
KEYWORDS    RefSeq.
SOURCE      Indibacter alkaliphilus
  ORGANISM  Indibacter alkaliphilus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae.
REFERENCE   1  (residues 1 to 700)
  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   2  (residues 1 to 700)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Indibacter alkaliphilus"
                     /db_xref="taxon:579922"
     Protein         1..700
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=81845
     Region          61..121
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkmrfcvivl llwiiplsif sqtyrkgein leilvedlfg mqredqdydd lyesllqlfl
       61 npinlnktnp eelqsifils paqinsffqh rshfgrilsl yelqaipefd letiykilpf
      121 vvldetegkq gplldrikes kdaylilran rvletrrgyt ppdtlangrl ssrylgdpnn
      181 lyvrfriqqs rdfslgftmd kdpgeqftwd petkrygfnf fsyhftvynq grwkaislgd
      241 fqmqtgqglv fgagfatgkg getittvrrs tigirpytsa lefgffrgva asyqagpisi
      301 tllasnaprh gnvqvlsdsl erdeaiitsl qtsglhrtat eiryknqire knlganihfq
      361 nnaknlqlgf nslltqfsqp fvrrpqpynq fefhgqenqi hslyfaynfq nyfffgesav
      421 sqsrgqghif gmmsslhpkl slsllwrsfd rdfhtfygna fsegtrpine rgiylglnfk
      481 pnrkynwafy ydqftfpwlr frtyapsqgy ewlsrftysp srkillfaqi reeskgrnis
      541 eyprfqssyi ldqgkrwnyv fnldyslsqn wsiksrvmgs sfdfggkvtr gfaisqdlnv
      601 dyqkwrlssr laffdtddfd nrqflyernv lwlfsipslh gqglryyilg qyrinpklei
      661 warfsrtqyt drnqigsglq liqgnritea viqmrykfnr
//
LOCUS       WP_009034725             307 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Indibacter alkaliphilus].
ACCESSION   WP_009034725
VERSION     WP_009034725.1
KEYWORDS    RefSeq.
SOURCE      Indibacter alkaliphilus
  ORGANISM  Indibacter alkaliphilus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 307)
  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 307)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Indibacter alkaliphilus"
                     /db_xref="taxon:579922"
     Protein         1..307
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35645
     Region          35..192
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          220..302
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mlktnyipcv pwrnerdlkt lvenrttytl hdcelnifet hqeakdvnlv fgdlvlttml
       61 kgkkvmhlfe kpgfdylpge svivppnevm ridfpeakmd nptqcialsi skemientfn
      121 llnerlpdke ltkewgldls nfhlintkdl seiinrfiri gvkerskekd liasfalkel
      181 lirltqtqar dmlektyqsl assnrlayvv dyiksniren ftldqlsaka cmskahfsrt
      241 fknelgispm eyilkerlkl aknflklgtk qiqevcymsg fnnptyfira fknefgmtpk
      301 vfqnqyp
//
LOCUS       WP_009037237             589 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Bacteroides].
ACCESSION   WP_009037237
VERSION     WP_009037237.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 589)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..589
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=67542
     Region          106..384
                     /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          506..583
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mkyktsliti lwgsllcftl pvvaqnslqh qkdslrqvie hsegidklks ynrlyylyms
       61 evaddqkmdt llmlftqvea eaikqgnvem qgmvygntii shinrkeyde iiqkapgyld
      121 fyirhelwkf yyqinmqlit aynlkgdykq aaeaaelmfd rarkredkag malalyatgi
      181 tynvqnrwke eeecfrecag llwevsgydn iltqsyaflc talraqaqyd kllqlvpdye
      241 kaiarfekss grtqpeargn lyvalmntyi dtkdydkage ylsklesivn nniskyelar
      301 akalifqsqg dyrkalavid satagidesd fslndtrkik meilarmgrv dealalldqf
      361 iatndtiknv evnarfdelr tqyevekhia gkernfhyll falaiclvla lllagafyyn
      421 rtialknrkl yerikeqdrl adelsrleni rqsesspeds gktagatelf apsgeqqnlv
      481 irlqeyllsd dnlsntdinr ddiisalgtn kntltdavka vtgkspmeym rtlkveearr
      541 kldshpelti eaiafscgfn ipstfyrlfr kqygisptey rkmatsqek
//
LOCUS       WP_009036647             418 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [Bacteroidaceae].
ACCESSION   WP_009036647
VERSION     WP_009036647.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidaceae
  ORGANISM  Bacteroidaceae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 418)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Bacteroidaceae"
                     /db_xref="taxon:815"
     Protein         1..418
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47431
     Region          2..415
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mkklyvyadf dwlkevelig elgyeslrga dsysftfnne wlrqhsdlfl sddlnnypgq
       61 qytqpgkdif gcfsdalpdr wgrtlllrre qivaaeeqrp vrrlssfdfl tgiddfsrmg
      121 gfrfkedldg efinvseslk ippltdirel iaasaeiekc eennmlpdrk wiaqlvqpgt
      181 slggarpkan vvdadktlyv akfpsrkddy dvglwehfgh llatktgina aktkmlatge
      241 kyhtllsqrf drtqegkrih lasamtllgl sdgdnattrh gyldivdfii qsctdvernl
      301 qelyrrvafn icignsddhf rnhgflltak gwilspaydm nptlneyqsl lvsstsnkae
      361 lsilldaced ymlnrktaek iisevigavk gwrelatrlg iskremdmfa gvlderck
//
LOCUS       WP_009038848             349 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Bacteroides].
ACCESSION   WP_009038848
VERSION     WP_009038848.1
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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..349
                     /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=40092
     Region          8..282
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 megnqsrrid fvdltkgvci ilvvmahvgg afeqldtnsm lscfrmplyf fisgvffksy
       61 egllgfilrk inkliipflf fylsaflmky ivwkiapgvf qlpvswnell vvfhghdlik
      121 fnppiwflla lfncnilfyl ihflrekhlp vmfavtilig cagfylgklq ielplyidvs
      181 mtalpfyvag fwirrynffl ypshrfdkli pvfvvlalvv myftattlgm rtnnyagnif
      241 qvyiaafagi fmimllckkv kkikvvsylg rysiitlsih gpilhflgpl vsryihnswa
      301 qasalllitl sicllltpvf lkvipqmvaq kdllkvkqdh tkktvyedk
//
LOCUS       WP_009035202             232 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Indibacter alkaliphilus].
ACCESSION   WP_009035202
VERSION     WP_009035202.1
KEYWORDS    RefSeq.
SOURCE      Indibacter alkaliphilus
  ORGANISM  Indibacter alkaliphilus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae.
REFERENCE   1  (residues 1 to 232)
  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   2  (residues 1 to 232)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Indibacter alkaliphilus"
                     /db_xref="taxon:579922"
     Protein         1..232
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=27218
     Region          94..161
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
     Region          170..230
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkariyfflk tyfgftkres rgfilivpvf lllyfvpdfy grlvqkqnke iyeeyqqvid
       61 smvqagflhy kpdfvkensl lpqdtlkkkd dfpkraspkl nrlnfneads vtlqvvpgig
      121 qtlagrivkf regmggmlyk eqllevyglk qevmerifdy fefqpgifrl ldinhaevae
      181 iakhpyvnyg aakvivayrd qhgpysnaed llkikifnee wldrlrpylk fd
//
LOCUS       WP_009039291             156 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Bacteroides].
ACCESSION   WP_009039291
VERSION     WP_009039291.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 156)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..156
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17033
     Region          9..156
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 maenliigtg nkedkyrell pqlhalvste tdlianlanv aaalkqtfgf fwvgfylvke
       61 delvlgpfqg piactrirlg kgvcgtawke artlivpdve qfpghiacss dskseivvpi
      121 lqqsevigvl didsdeldsf dtidarylee ictyig
//
LOCUS       WP_009039321             343 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Bacteroides sp. D22].
ACCESSION   WP_009039321
VERSION     WP_009039321.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. D22
  ORGANISM  Bacteroides sp. D22
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Bacteroides sp. D22"
                     /db_xref="taxon:585544"
     Protein         1..343
                     /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=39242
     Region          21..278
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mreppcggfp wgtrqnwtlt gfailcvlvg hiliiytqek tryplveiiy sfhmplfffv
       61 sgyvgyksqs tqkgvysflk gkvksllipy itwlfvmplm lnneypsnls aiiqkinfvp
      121 nlnywflplm ftfhviylfw hkysffggak kelegllvlf stivltgllf ksyytcvyai
      181 yglsfffgyf iskytiiekf ccqrrvaifs ifflillwki fpldtsinps ptysllnlgs
      241 flvtsllsii lflcffktvt mpsfvssvli elgkstmaly llpiyllpsg yvfpsnlpys
      301 lvtilaiiis lvqgfvsyli fkaclqipii pnilfgsksk ttl
//
LOCUS       WP_009039631             367 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [Bacteroides].
ACCESSION   WP_009039631
VERSION     WP_009039631.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 367)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 367)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..367
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=41794
     Region          5..356
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mklvnklsvl yrdqkigelt mthdnrccaf qydkkwlisg fsispldlpl esslfiakpe
       61 pfwgnfgife dslpdgygry llnrllkkqg indalltpiq rlsivgisgm galsyvpesy
      121 igeekslpdl dnlqqmalev lsekseeged ilyfnsgnsg gcrpkclwhd regawlvkfr
      181 htydpkdigr meykynevar kcginvpdyk lldgkyfask rfdiengkrl hiatagalln
      241 esisnpkldy kvllhltgyl tqdsqqvdem fqrmvfnvlt dnkddhvknf sficregkws
      301 lapaydltlc kegyhgehat sannkgnpdi edmlavgesi riprrkgmei inhminhcqe
      361 ilstrfe
//
LOCUS       WP_009041559             826 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas chlororaphis].
ACCESSION   WP_009041559
VERSION     WP_009041559.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 826)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 826)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 826)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..826
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..826
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90528
     Region          68..118
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          97..826
                     /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 mivhfhhsss glrhavrval lssalgvaal pclaqaaesg aaslshsyni pggalsdvln
       61 rfareagitl smtpaqlqgr qsaglkgeys tdqalgqlln gsglealsqd gssyvlralp
      121 etgalalptt dikgfalgna lgsmegynat hsqiatktst alletsqsvs vvtreqmddq
      181 gsqtvsqamr ytpgvltnpy gathrydyva mrgfndgsvd niyldglksm gdsgtystmq
      241 vdpyflervd ilkgpssvly grsspgglva ltskkplfep yhqiqatvgt qgqrgmgfdf
      301 sgpvdddkri ayrltgladr sdtqfdhnke kryalaptls idftddtslt lqaylqhdpd
      361 ggyhsgmpad galhprngrr isenffegep gidrykrdqq sfgyqfehrf ndvftarqnf
      421 ryldskvkld qvygygwttp tsnelnryyt ggdeklhafi vdnmlqaefl tgatkhtvlm
      481 gvdyqrrktv vdwtsgsvap inafdpvygn saisyydpvs ylrrleqtgv ylqdliemdk
      541 wrfslglrqd wvetsdenrl aeasrpvgte indkrtkltg ragalylfdn glapyisyse
      601 sfnpnsyads agnplaptdg tqwelglkyq ppgtddlyta slfridqenl atklpqenfy
      661 ravgavrsqg leleahlqln dnlkllgsyt ftdieysksm istlstatdi ienkgnsptq
      721 aprhmaslwa dykfdsgsld glrlgggvry vgyswadaen tmkvpsytlf dasvgydlgk
      781 vglkgvdvrl nannltnesy iascaslsfc ymgeernvaa tvsyqf
//
LOCUS       WP_009041926             378 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Pseudomonas chlororaphis].
ACCESSION   WP_009041926
VERSION     WP_009041926.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 378)
  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 378)
  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   3  (residues 1 to 378)
  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   4  (residues 1 to 378)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 378)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 378)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..378
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39822
     Region          30..365
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(104..106,127..128,177,229,254)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 msqtfykkgf lalavaaalg vsafaqadlk igvagpmtga naafgeqymk gaqaaadein
       61 akggvngeki vlvkgddace pkqavavanr lvdqdkvagv vghfcsssti pasevysdag
      121 viaitpgstn pqvterglsa mfrmcgrddq qgivagdyiv dvlkgkkvvv lhdkdtygqg
      181 ladatkaqlg krgvtpvlye gltrgekdfs avvtkiraag advvyfgglh peagplvrqm
      241 reqglkdvkf msddgivtde lvttaggpqy vdgvymtfga dprllpdskt vvdafrkagt
      301 epegytlyay asvqalaagf ggaksnkged aakwlkanpv ktvmgektwd akgdlkvsdy
      361 vvyqwdkdgk yhqlekqk
//
LOCUS       WP_009042405             254 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Pseudomonas chlororaphis].
ACCESSION   WP_009042405
VERSION     WP_009042405.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..254
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=28378
     Region          1..169
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
     Region          167..>243
                     /region_name="GH25_muramidase"
                     /note="Endo-N-acetylmuramidases (muramidases) are
                     lysozymes (also referred to as peptidoglycan hydrolases)
                     that degrade bacterial cell walls by catalyzing the
                     hydrolysis of 1,4-beta-linkages between N-acetylmuramic
                     acid and N-acetyl-D-glucosamine residues; cl10448"
                     /db_xref="CDD:447900"
ORIGIN      
        1 mipidynsyr tlapynkrvr flvlhytaln feasvkaltt gaasahylip alqdptyqaa
       61 gfqeqrifnl vaeedrawha gvsdwagrsg lndtsigiei vneatdvngv ftfpdyersq
      121 vealkqlaln ilqrypdlsp knvvghsdia vgrksdpgpk lpwkelykag igawydeptk
      181 rkyvqqfraa glparaevlk afatygygvp aqatddffqs lvrafqmhfr pknytgkldv
      241 etcailyaln ekys
//
LOCUS       WP_009042455             117 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Pseudomonas].
ACCESSION   WP_009042455
VERSION     WP_009042455.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..117
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12645
     Region          10..112
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(16,34..35,43,46,48..49,51,54..55,57,65,70,77)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(34,65..66,68,94)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 miepldadqs paeirrtaly ltlaqvpegk vvsygqlaem aglgraarwv grtlsqlpad
       61 ttlpwhrvlg aggrislpvg sasgdeqrar lrmegvsiln nrvdirrhgw rpvehsg
//
LOCUS       WP_009042463             807 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pseudomonas chlororaphis].
ACCESSION   WP_009042463
VERSION     WP_009042463.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 807)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 807)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 807)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..807
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..807
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=88152
     Region          12..807
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 maspafshfl prfgvaaava gvlslagcqs wntqdslppt sgvqplkgla qnvsvrrnam
       61 gmpliesntf hdalfalgyv hasdrinqmv tlrllaqgrl aemsgadald vdrymravnl
      121 knragelyka ssprikrffe vyargvnayl fryrdklppd laatgykpey wkpedsalif
      181 cllnfsqsan lpeeintlvl aqkvgadkla wltpsypdea lplaesdklk glnlnvpgls
      241 eissaagklg elnplsvaga snwaiapqrs rsgrsllaad shspawnlvq irapkyqaag
      301 asiaglpmiv qgfngqvaws mtsvagdnqd lfleklkrqg nalyyeangk wlpavvrnet
      361 yfvkgqrpir eavyetrhga llnsssnlna gyglalqqpn laddksldaf fdltraqnve
      421 rasdasreir aiglnmlfad ashigwqvtg rfpnrregeg llpspgwegr ydwdgyadpm
      481 lhpydqdpaq gwlgtanqri iphgygmqls nswyyperge rlaelagsgk hdgrsmiamq
      541 ydqttpfaak lkkmfeapgm aqplkkaida lpeadrskar eaysrlmafd gklspvsada
      601 aiyelflqes arqifldklg pesspawkal vangalsysa qadhllgqed spfwddsrtp
      661 qkedkpaila rslaaaisag esqlggdrra wqwgklhsys wknasgqvir gplqaggdhs
      721 tlnsspyrwg qdfnvtqapa lrlivdfgqs eplsvmnssg qsgnpaspny lngidawlkg
      781 qylslplqpq nfdrlygktr ltlapgk
//
LOCUS       WP_009043148             343 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas chlororaphis].
ACCESSION   WP_009043148
VERSION     WP_009043148.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 343)
  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 343)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 343)
  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   4  (residues 1 to 343)
  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 343)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..343
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37516
     Region          24..211
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          255..337
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mnmlelsrgp asallmvdfg rargfsparl lagsglslar ladpnlelsc aqelrlinnl
       61 lnlsghpqgl gyqvgeryhf styglfgygl issatagdal klalrflplt yaftriayhe
      121 qpplgiltft epaladeslr dfvierdmaa aavllkeiag refslagftl kkkrpvdqaa
      181 asagnilgmr payladrnsl afdrsllsrp lpqantvtva mceqmcaqlm errsprtgta
      241 elvrqylnia plgvppdlpg maslinlser tlkrrlheeg tcyrhlleqs rsaaalellg
      301 dptlklteia eklgysdlss fsqtfkrwyg vsprsyrhas rat
//
LOCUS       WP_009043315             294 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Pseudomonas chlororaphis].
ACCESSION   WP_009043315
VERSION     WP_009043315.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..294
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=32857
     Region          19..196
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkkyttvlsl llamtgctss hqdtsearlt esegyvlskg eravaqnhri rflvlhytal
       61 dqaqsfetlt rsehvsanyl ipdrpktykg lpvadqlvdd hdrswhagvs qwknrsnlnd
      121 tslgieivna gwdkdtgqll gepynerqie llisltrdlv rkydiqptdi vghsdiapgr
      181 kidpgpffpw krlaeagiga wpdertiddy larfsvspps mvqvtkalqt ygygyldqqp
      241 ervveafqmr fnqenvsgiv dirtaailfs lidkyhgkdk asaillppev aalg
//
LOCUS       WP_009043708             145 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Pseudomonas chlororaphis].
ACCESSION   WP_009043708
VERSION     WP_009043708.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..145
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16088
     Region          5..143
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 miftaclglf laafgaatll plqseavlvg lllngqhpvw lllavatlgn vlgslvnwwl
       61 gqrlehykdr rwfpvgprhl qrarnhyqry ghwslllswl piigdpltlv agimgeplkr
      121 fllivtlakg arygvlawmt lgwvg
//
LOCUS       WP_009043498             708 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Pseudomonas chlororaphis].
ACCESSION   WP_009043498
VERSION     WP_009043498.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..708
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=77148
     Region          48..707
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mpsprplpaa llglalvcpt laeaqglelg qvligaeers gedasieeak arlaqvpggg
       61 nvvdlrrplq grvasnqdvl ayqpgvyaqs agnegvkisi rgsginrapg ahasglytml
      121 dglplsgpgg tpyelleplw lervevlrga ngfdrgalal ggaidyisht gydapklqvr
      181 yatgshgyqq rqvssgqvlg dfdyylsltd arsdgyqdhs asksqgvian fgyrfnpnle
      241 trfyirhrqt dndlagrvtk gsiehdpraa npayvtrnds rdqpgstfig nkttwyiddd
      301 ssiqtglvyh dypmdlregp nrlkvaytdv sgtfdykrrd tlwgleshst lglrvtkhlp
      361 nsgaselvri pggntagyap gtpmrnftyq gsdsvlhlgn dleiaddlwl ttglaalytr
      421 resavtypdg ggktslgdwd yaprlglryq ltpdlqlfgn lsrsveaphp wsliyssnir
      481 fpagsgaatg tqrdpiklqn qtattlelgg rgdsaigqws lawyyaqvrh ellsvlpdan
      541 attpyelnas pavhqgveas lqsklwsgkd ggqlslrqsy tfsdfhyrdd erfgdnrlpg
      601 lpmhyyqgel rydwplgffa alntqlvskv avdyansyya dpyalfgatl gynapkgdwq
      661 twldlrnlsd qhyaatvtpg yddkgldaar stpgegmamy lgvswslr
//
LOCUS       WP_009043468             816 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas chlororaphis].
ACCESSION   WP_009043468
VERSION     WP_009043468.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 816)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 816)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 816)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..816
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..816
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89107
     Region          59..109
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          88..816
                     /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 mqrllppgfq gqslvpalsr isllcalipg lalaepmqfd igaqplgsal nrlaaqsglq
       61 viydgnmvqg kssravsgrq epqdalgqml qgsgltwrat gsgsvmlekl peqggplelg
      121 attiggqqlg ettegtgsyt taitqtatkl plsiretpqs vtvvtrqqmd dhgalavgdv
      181 lrnvpgitqq aydsdrmefs argfaitnyq ydgvnriydg vygeapthvd tatfdrievi
      241 kgstglmtgs gdpsatvnlv rkkptkefka sisgtvgswd nyrsegdisg plndsgsvrg
      301 rfvgayqdrn syldhynqkk dlfygilead ltpdtlltlg idkqsvtprg tswtgtptyf
      361 adggrtdfsr sfnpgadwsr rdfdsvtyfa aleqalandw klkvsldqkt tdhdtrlasa
      421 sggnpdratg egmflywgrw eghrvqntad vnvsgpftlg grqhdlvagv mashsrqtgs
      481 tydtsafslv pgsiydwngk lpeqefpkng kyertqsqna vylatrlrpt ddlsfilgsr
      541 lstfkynedy rynagagldd thasykehgv ltpyagvvyd lndvysvyas ytsiyqpqiy
      601 kddsgttlap vegksyetgl kaayldgaln aslaffrieq dnvaesigtn pitnegiyka
      661 idgtttkgve lelagelqkg wnlsagytya rtrdadeqri fgyplsttrp ehavrvfsty
      721 rlpgvldkvt vgggiswqsg yygkiysasv gdytrirqgg yslvdlmsry qynehlsftv
      781 nannvfdkky ltglgnfdtt yygeprnlml tskwef
//
LOCUS       WP_009044319             249 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: hydroxypyruvate isomerase family protein
            [Pseudomonas].
ACCESSION   WP_009044319
VERSION     WP_009044319.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 249)
  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 249)
  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 11466508
            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="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27176
     Region          1..245
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mlkfnahlgf qfnewpflqr ieaaaaagfr avefpspyef daslladhla rhslsliqfa
       61 apagvtkgia alqgkeeefr dglrqavsya kalacsdvhi msgvttqdea altfgsnley
      121 avkyfedqgv rplievisaq ampdyymsdf nkaqqvlesf psvglildly haqlltgdaa
      181 evlarfydrt vhvqiadcpg rhepgtgsmd faalfaaleq rgypgwigce yrpsgatvas
      241 ldwikqlsa
//
LOCUS       WP_009044500             345 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas chlororaphis].
ACCESSION   WP_009044500
VERSION     WP_009044500.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 345)
  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 345)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..345
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38447
     Region          31..214
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          259..339
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqmkavdpqy qlalvspfll qtlaevagsh gvdphalcrg lgftlddlqd paqrisyrqa
       61 vamiqralka lprqglglwv ghqnvlgtlg llghvlslck tlrdafdigi rhqhtsggiv
      121 sctvrqqgde ffveaecrlp ysdvqifave effaslpvyg ralvgadfka lrvefmhaap
      181 ayqdeylrll gpdvhfgclh nrmviagewl dtrlpnhhav alrqalklle lesaqvhrkl
      241 dliqaverai srdltqgshi eqvasdlnms grtlrrrlse hdltfdalle qvrrartlsl
      301 lanpqlsier iteavgysdv rsfrrafkrw tglspsayre eggqa
//
LOCUS       WP_009044949             403 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Pseudomonas
            chlororaphis].
ACCESSION   WP_009044949
VERSION     WP_009044949.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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 403)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..403
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45253
     Region          2..403
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mpaelsfslk qarrlalaaq gfsgrpapat irpaqlnrli arlgilqids vnalvrshyl
       61 plfsrlgdyp aqlldqaaws qgrqrtlfey wgheasllpl slyplmrwrm qrasqgqgiy
      121 qqlarfgqeq qatirrvlaa veeqgalgag slstreerag pwwdwsaekh alewlfaage
      181 vtvagrrgfe rlydlpervi pssilqhspl seadaqrgll lhaasalgva tekdlrdyfr
      241 lepadsrarl aelleggell acevagwkqa ayclpeakvp rsvpasalls pfdsliwers
      301 rterlfdfry rleiytpqhk rvygyyvlpf lhheriaarv dlraeraqgr lavhavheed
      361 qgldeqgmqa lasslrsmad wlgladvqln cprasaqrlr afl
//
LOCUS       WP_009045130             332 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas chlororaphis].
ACCESSION   WP_009045130
VERSION     WP_009045130.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 332)
  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 332)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 332)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 332)
  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   5  (residues 1 to 332)
  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   6  (residues 1 to 332)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..332
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38042
     Region          22..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          92..330
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mrertiashf araalggarr rgydcsellq tlgislelln epkariapeq fasllqqlwq
       61 vlddeylgfg dgpskrgtfa mmchalihcs nlekalqrgl lfyslfpqap rlslthegdm
      121 trlslddagl wdpehflses llviwhrlgs wligqrirle qacfsypkpe hgneydllfp
      181 cplvfsrdcs sllfhsryls mpllqdertl khflerspad llarpddgds lssqlrrlls
      241 rdsnhwpdle siaqhlhisp qtlrrhlree gtsfqelkdq lrrdiaiyhl rradlslqqi
      301 aeqtgfseps afhrafkkwt gltpgayraq et
//
LOCUS       WP_009045140             248 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Pseudomonas].
ACCESSION   WP_009045140
VERSION     WP_009045140.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  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   3  (residues 1 to 248)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            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="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28154
     Region          37..242
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mfnavnaeda pqppkvlttp leinstlrll qdshdpliit fhersqrfqs ylveidrdsn
       61 mialdemipr dgerfmlage pfrvegfheg vriawesngi ptidesnggr cyrgtlpdev
      121 vyhqrrnafr aalklaqlvn ielggeklka piagklldis atgcklrfeg disgrlqlgq
      181 vyerfiaalp fgsmtapvel rylhheekid ttfagvrfhn msglvqrqve rfvyqlqrea
      241 rrfdkddl
//
LOCUS       WP_009045716             812 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: Lon protease family protein [Pseudomonas].
ACCESSION   WP_009045716
VERSION     WP_009045716.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 812)
  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 812)
  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 812)
  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   4  (residues 1 to 812)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..812
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..812
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88843
     Region          65..800
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mpdpvaaslr lapealtrpf saeqfsfstt ndlepfrgvl gqeravealq fgvamprpgy
       61 nvfvmgepgt grfsfvkryl kaegkrlqtp sdwvyvnnfd eprepralel psgaagafis
      121 dinglidnll atfpavfehp syqqkksaid rafnqrydra ldvierlale kdvalyrdss
      181 niaftpmldg kaldeaefaq lpeadrerfh edisaleerl neelaslpqw kressnqlrh
      241 lneetitlal qpllaplsek yaenagvcgy lqamqvyllk tvveqlvdds ktdavarkll
      301 eeqygpslvv ghpanggapv vfephptydn lfgrieystd qgalyttyrq lrpgalhran
      361 ggflileaek mlsepfvwda lkralqsrkl kmesplgelg rlatvtltpq hiplqvkvvi
      421 igarqlyytl qdldpdfqem frvlvdfded ipmvdesleq faqllktrts eegmapltad
      481 avarlatysa rlaehqgrls arigdlfqlv seadfirhla sdemtdaghi eralkakatr
      541 tgrvsarild dmlagiilid tdgaavgkcn gltvlevgds afgvparisa tvypggsgiv
      601 dierevnlgq pihskgvmil tgylgsryaq efplaisasi aleqsygyvd gdsaslgeac
      661 tlisalsktp lkqcfaitgs inqfgevqav ggvnekiegf frlcearglt geqgaiipha
      721 nvatlmldek vlaavragqf hvyavrqade alsllvgepa gepdadgqfp egsvnarvve
      781 rlrviaemvs eedlkeaeke qaqealaqtk pa
//
LOCUS       WP_009046083             803 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pseudomonas chlororaphis].
ACCESSION   WP_009046083
VERSION     WP_009046083.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 803)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 803)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 803)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..803
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=88559
     Region          2..800
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkrsltvlvv lilalaaggg wylyskqpsr qgqvelerlq gsvtvryder gvphiraene
       61 tdlyralgyv haqdrlfqme vmrrlargel aeilgpklld tdklfrslri reradsyvag
      121 ldrqspawkg lqayldgvnq yqnshpqpie fdvlgipkrs ftaedsisva gymaysfaaa
      181 frteplltyv rdqlgndylk vfdldwqpkg alakgrgpla pslaasdwqd lgaiarlseq
      241 aladaglpqf egsnawavsg srtksgkpll agdphirfav psvwyeaqls apgfelyghh
      301 qalvpfaflg hnldfgwslt mfqnddldli aekvnpnnan qvwyrgkwvd lvnseqqiav
      361 kgqppvtqil rqsphgpivn dvlganagkt piamwwafle tpnpildgfy qlnradtlak
      421 arsaaskvqa pglnivwana kgdigwwaaa llpkrpigak gtfildgsts ladkegfypf
      481 sanpqeenpa rgyivsanfq pvsptgmeip gyynladrgq qldrqlsdks vkwdidatqk
      541 lqlgtttayg prllapllpv lrevvsdpqe lklveqlaqw kgdypldsts atlfnqflfn
      601 ltdaafhdel gdaffdtlls trvidaalpr laasadspww dnrntlgqes radtvrvawr
      661 aslahlkatf gddstkwlwg qahtlthghp lglqkpldrv fnvgpfaapg thevpnnqsa
      721 kigpapwpvt ygpstrrlid fadpahslsi npvgqsgvlf dkhyqdqaea yiegvyqqah
      781 fneeevtant hstlkllpar taq
//
LOCUS       WP_009046311             831 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas chlororaphis].
ACCESSION   WP_009046311
VERSION     WP_009046311.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 831)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 831)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 831)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..831
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..831
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=91138
     Region          73..123
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          102..831
                     /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 mivhlhhfss arpalglrha vrvallssal gvaalpglaq aaetgaasls hsynipggtl
       61 sdvlnrfare agitlsmtpa qlqgrqsagl kgeystdqal gqllngsgle alsqdgsryv
      121 lralpetgal alpttdikgf algnalgsme gynathsqia tktstallet sqsvsvvtre
      181 qmddqgsqtv sqtmrytpgv ltnpygathr ydyvamrgfn dgsvdniyld glksmgdsgt
      241 ystmqvdpyf lervdilkgp ssvlygrssp gglvaltskk plfepyhqiq atvgtqgqrg
      301 mgfdfsgpvd ddkriayrlt gladrsdtqf dhnkekryal aptlsidftd dtsltlqayl
      361 qhdpdggyhs gmpadgalhq rngqrisenf fegepgidry erdqqsfgyq fehrfndvft
      421 arqnfrylds kvkldqvygy gwttptsnel nryytggdek lhafivdnml qaefltgatk
      481 htvlmgadyq rrktvvdwts gsvapinafd pvygnsaity ydplsylrrl eqtgaylqdl
      541 iemdqwrfsl glrqdwvets denrlaeasr pvgteindkr tkltgragal ylfdnglapy
      601 isysesfnpn syadsagnpl aptdgtqwel glkyqppgtd dlytaslfri dqenlatklp
      661 qenfyravga vrsqglelea htqlndnlkl lgsytftdie ysksmistls tatdiienkg
      721 nsptqaprhm aslwadykfd sgsldglrlg ggvryvgysw adaentmkvp sytlfdasig
      781 ydlgkvglkg vdvrlnannl tnesyiasca slsfcymgee rnvaatvsyq f
//
LOCUS       WP_009046392             334 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_009046392
VERSION     WP_009046392.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  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   4  (residues 1 to 334)
  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 334)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..334
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37782
     Region          22..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          248..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mteptslasw tralrkqlda lgldstalch qagldpqlmd dpnaryplsg ttrlwqlavq
       61 asgdpaiglr vsrfvspttf halgyalvas gslrevferi vryhqvvsda leleltrted
      121 ryrfrlkvpe gnpepafeai dafvaiyvrt crnrlgrdya plavylrrpe pvdpkqwhtv
      181 frapvffsad edrlefglhd fdshlddanp elaehneavl krtlmqlqpl twerkvrgvi
      241 esqlpegeps aervaqalhl slrslqrhla degcrfdtll necrenlall hlrdpqcsls
      301 eisyllgfad assfsrafkr wtgmtpgqfr dglr
//
LOCUS       WP_009046713             378 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Pseudomonas].
ACCESSION   WP_009046713
VERSION     WP_009046713.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 378)
  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 378)
  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   3  (residues 1 to 378)
  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   4  (residues 1 to 378)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 378)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 378)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..378
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40003
     Region          30..365
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(104..106,127..128,177,229,254)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 msqtfykkgf lalavaaalg vsafaqadlk igvagpmtga naafgeqymk gaqaaadein
       61 akggvngeki vlvkgddace pkqavavanr lvdqdkvigv vghfcssnti pasevydeag
      121 viaitpgstn pqvterglsa mfrmcgrddq qgivagdyiv dvlkgkkvvv lhdkdtygqg
      181 ladatkaqls krgvtpvlye gltrgekdfs avvtkiraag advvyfgglh peagplvrql
      241 reqglkdvkf msddgivtde lvttaggpqy vdgvymtfga dprllpdskt vvdafrkagt
      301 epegytlyay asvqalaagf ngaksnkged aakwlkanpv ktvmgektwd akgdlkvsdy
      361 vvyqwdkdgk yhqlekqk
//
LOCUS       WP_009048597             708 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Pseudomonas chlororaphis].
ACCESSION   WP_009048597
VERSION     WP_009048597.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..708
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=77463
     Region          9..707
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mpsprplpsa llglalvcpa laeaqglelg qvligaeers gedasieeak arlaqvpggs
       61 nvvdlrrplq grvasnqdvl ayqpgvyaqs agnegvkisi rgsginrapg ahasglytml
      121 dglpltgpgg tpyelleplw ldrvevlrga ngfdrgalal ggaidyisht gydapklqvr
      181 yatgshgyqq rqvssgqvlg dfdyylsmtd arsdgyqdhs asksqgvian fgyrfnpnle
      241 trfyirhrqt dndlagrvtq rsiehdpraa npayvtrnds rdqpgstfig nkttwyiddd
      301 sslqtglvyh dypmdlregp nrlkvaytdv sgtfdykrrd tlwgleshst lglrvtkhlp
      361 nsgaservri psgntagfap gthmrnftyq gsdsvlhvgn dleiaddlwl ttglaaiytr
      421 resavtypeg ggktslgdwd yaprlglhyq ltpdlqlfgn lsrsveaphp wsliyssnlr
      481 fpagsgaatg tqrdpiklqn qtattlelgg rgdsaigqws lawyyaqvrh ellsvlpdan
      541 attpyelnas ptvhqgveas lqstlwsrdd ggqlslrqsy tfsdfhyrdd erfgdnrlpg
      601 lpmhyyqgel rydwpqgffa alntqlvskv avdyansyya dpyalfgatl gynapkgdwq
      661 twldlrnltd qhyaatvtpg yddkgldaar stpgegmamy vgvswslr
//
LOCUS       WP_009049481             385 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Pseudomonas chlororaphis].
ACCESSION   WP_009049481
VERSION     WP_009049481.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 385)
  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 385)
  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   3  (residues 1 to 385)
  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   4  (residues 1 to 385)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 385)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 385)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 385)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..385
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40267
     Region          33..368
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(108..110,131..132,181,233,257)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mktcvpfkha vllglalssl asalaqaeqq vliglagplt gpsarigkdl engaqlaidq
       61 anarhpqing eavtyklvse ddqsdprtav svaqrlvdae vvgvvghwnt gtsipaarvy
      121 hdagiaqvap vatghaytqq gfdssfrimg hdddggrvag dyalnslkar riaviddrta
      181 fgqgladqfa kaveaggasv vareyvddkt idfsavltni rsqnpdliff ggvdsqaapl
      241 arrikqlgik aplmgaggfv sqtflqlaqn egegvialep glavaqmpgg kafeqayqqr
      301 fkhgielhap faydgvgvli aaiekagstd prqylpvlra snypgvtgti afdaqgnlkn
      361 psftvyqvka gqwqpvsvag gepaq
//
LOCUS       WP_009049713             345 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_009049713
VERSION     WP_009049713.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 345)
  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 345)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..345
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38461
     Region          31..214
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          259..339
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqtnavdpqy qlalvspfll qtlaevagsh gvdphalcrg lgftlddlqd paqrisyrqa
       61 vamiqralka lpqqglglwv ghqnvlgtlg llghvlslck tlrdafdigl rhqhttggla
      121 sctiqqqgde ffveaecrlp ysdvqifave effaslpvyg ralvgadfkp lriefthaap
      181 ayrdeylrll gpdvhfgclh nrlviashwl dtrlpnhhav alrqalklle lesaqvhrkl
      241 dliqaverai srdltqgshi eqvasdlnms grtlrrrlse hdltfealle qvrrartlsl
      301 lanpqlsier iteavgysdv rsfrrafkrw tglspsayre eggql
//
LOCUS       WP_009049746             237 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Pseudomonas].
ACCESSION   WP_009049746
VERSION     WP_009049746.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 237)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..237
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=26142
     Region          41..208
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mltflrrlcl amttlgaics palaannttp llynslahaa pelnpqvlks alsamqcavn
       61 sgarqarhla vidysqpsta rrlwifdlnk rtlvlrdlva hgqksgenfa tqfsnrmgsf
      121 qsslglfrtq esyegshgys lrmdglepgf ndlardrdiv ihaadyvspl wsrrqgrigr
      181 slgcpavrpq varqvidrlk dgqfmfswyp dqqwlksspy lncqprqvas ivaasgg
//
LOCUS       WP_009050121             403 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Pseudomonas
            chlororaphis].
ACCESSION   WP_009050121
VERSION     WP_009050121.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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 403)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..403
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45362
     Region          2..403
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mpaelsfslk qarrlalaaq gfsgrplpat irpaqvnrli arlgilqids vnalvrshyl
       61 plfsrlgdyp aqlldqaaws qgrqrtlfey wgheasllpl slyplmrwrm qrasqgqgiy
      121 qqlarfgqeq qatirrvlaa veeqgalgag slstreerag pwwdwsaekh alewlfaage
      181 vtvagrrgfe rlydlpervi pssilqhspl seadaqrgll lhaasalgva tekdlrdyfr
      241 lepadsrarl aelleggell acevagwkqa ayclpqvkvp rsvpasalls pfdsliwers
      301 rterlfdfry rleiytpqhk rvygyyvlpf lhheriaarv dlraeraqgr lavhavheee
      361 qgldeqgmqa lasnlrdman wlgladvqln cprasaqrlr gfl
//
LOCUS       WP_009050160             110 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Pseudomonas].
ACCESSION   WP_009050160
VERSION     WP_009050160.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (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   2  (residues 1 to 110)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..110
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11421
     Region          41..108
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mriayfpslv falmaslssi tyaapavnte akapaaaqva sseqagridl ntadaaalqr
       61 elsgvgavka qaivkyresn gpftsvdell evkgigkail esnreklkvn
//
LOCUS       WP_009050306             248 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Pseudomonas].
ACCESSION   WP_009050306
VERSION     WP_009050306.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  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   3  (residues 1 to 248)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            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="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28200
     Region          37..242
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mfnavnaeda pqppkvlttp leinstlrll qdshdpliit fhersqrfqs ylvevdrdsn
       61 mmaldemipr dgerfmlage pfrvegfheg vriawesngi ptidesnggr cyrgtlpdev
      121 vyhqrrnafr aalklaqlvn ielggeklka piagklldis atgcklrfdg dissrlqlgq
      181 vyerfiaalp fgsmtapvel rylhyeekid ttfagvrfhn msglvqrqve rfvyqlqrea
      241 rrfdkddl
//
LOCUS       WP_009050907             138 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: pilin [Pseudomonas].
ACCESSION   WP_009050907
VERSION     WP_009050907.1
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 11471942
            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="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=13934
     Region          1..134
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkyqkgftli ellvvvaiig ilatfamply skyqarakvt aalaeasalk vnfedvlnqg
       61 sdptlelvgg kaatsnctmt aagsastgag sigctilnap apvlnktvtl trttadgwvc
      121 tttvpadysp kgctasgs
//
LOCUS       WP_009051209             809 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas chlororaphis].
ACCESSION   WP_009051209
VERSION     WP_009051209.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 809)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 809)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 809)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..809
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..809
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87877
     Region          61..111
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          92..809
                     /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 msrsldtllr psllavaial caplastpli aaeqasgvra ynlpaaplas tlnqiasqag
       61 lalslnpsla agktsapvkg qfdaagalre alrgtglqle qssagtyslv aipdgvvalp
      121 etsitgqqay esawgpvdgy latrtaagtk tdtslveapr sisvatrqqm edrnvqnldd
      181 avrympgivs asygsdtryd wmrvrgfept qfldglplpr gvyanpkaet wnldrlallr
      241 gpassvygqt ppgglldmvs rrpsaessha iqlqygsdny rqinfastgk iddegqflyg
      301 lsgvvrdagt qvdhidnkry niapsltwni dtdtrltlls qftrddtgat sqfmpiqgtk
      361 iksplgdvsh hknlgdpdye fydrtyyalg yafehrfndv wqfrqnlryt kselsfqqlt
      421 vgsyayspad aagnisrtst nvdedisqfa vdnnfqgdfa tgdithtvli gldhqrtdts
      481 ylsiygdggt tnifnpvygk pivrparssa yydynqktvq tglyvqdqma ldqwrltlgg
      541 redwvhqgtt yfnkndvtnt drsknfsgna alsyvfdsgl vpylsyaesf qpasnasvsp
      601 tesykptegk qwelgikyqp pgsntllsaa vydltqknvl vtsigagges vtnqtgevkv
      661 kgleleavsd vtdnlkviaa ytlaksevqk giykgnrlql mpnqqaslwt dytwhsgvld
      721 gfgigagary tgntygdqan twlgkanayt vfdaavhydl grlgsslkga slklnatnlf
      781 dkdylstcdg sycyfgdqrs vvasatyqw
//
LOCUS       WP_009051372             803 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pseudomonas chlororaphis].
ACCESSION   WP_009051372
VERSION     WP_009051372.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 803)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 803)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 803)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..803
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=88675
     Region          18..800
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkrsltvlvv lilalvaggg wylyskqpsr qgqvelerlq gsvtvryder gvphiraene
       61 tdlyralgyv haqdrlfqme vmrrlargel aeilgpklld tdklfrslri reradsyvag
      121 ldrqspawkg lqayldgvnq yqnshpqpie fdilgipkrs ftaedsisva gymaysfaaa
      181 frteplltyv rdqlgsdylk vfdldwqpkg alakgrgpla pslaasdwqd lgaiarlseq
      241 aladaglpqf egsnawavsg srtksgkpll agdphirfav psvwyeaqls apgfelyghh
      301 qalvpfaflg hnldfgwslt mfqnddldli aekvnpnnan qvwyrgkwvd lvnseqqiav
      361 kgqppvtqil rqsphgpiin dvlganagkt piamwwafle tpnpildgfy qlnradtlak
      421 arsaaskvqa pglnivwana kgdigwwaaa llpkrpigak gafildgsts ladkegfypf
      481 sanpqeenpa rgyivsanfq pvsptgmeip gyynladrgq qldrqlsdks vkwdieasqk
      541 lqlgtttayg prllapllpv lrevvsdpqe lklveqlaqw kgdypldsts atlfnqflfn
      601 ltdaafhdel gdaffdtlls trvidatlpr lvasadspww dnrntlgres radtvrvawr
      661 aslahlkatf gddsskwlwg qahtlthghp lglqkpldrv fnvgpfaapg thevpnnqsa
      721 kigpapwpvt ygpstrrlid fadpahsltv npvgqsgvlf dkhyqdqaea yiegvyqqah
      781 fneeevmant hstlkllpar svq
//
LOCUS       WP_009051615             330 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_009051615
VERSION     WP_009051615.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 330)
  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   6  (residues 1 to 330)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..330
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36740
     Region          23..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <153..329
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mlhshlttln avslvlntfk dqgqdseall agsginaadl sradtrittn qemlvcanav
       61 alqrdiglel grrmhvssyg mlgyalltsa tlgdalrlal rypallgtlf elsleadgel
      121 iwltaadyre npalatfnie fclvslkvic ddllghplpl rgarfdypap dyqsryaerf
      181 dcplqfdavs nafafdrrwl eqplpladai thqamaercr kqnteftgrq awlgrirqll
      241 aaqldaapgl eglaeqmncs artlrrhlkd lgcsyqelld elrferakqm lceddlpiyr
      301 iaealgfset asfrhafvrw sgvapsqfrp
//
LOCUS       WP_009051950             400 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Thermoanaerobacter sp. X514].
ACCESSION   WP_009051950
VERSION     WP_009051950.1
KEYWORDS    RefSeq.
SOURCE      Thermoanaerobacter sp. X514
  ORGANISM  Thermoanaerobacter sp. X514
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Thermoanaerobacter.
REFERENCE   1  (residues 1 to 400)
  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 400)
  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
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   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   5  (residues 1 to 400)
  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   6  (residues 1 to 400)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 400)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 400)
  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 19603220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Thermoanaerobacter sp. X514"
                     /db_xref="taxon:399726"
     Protein         1..400
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43589
     Region          <14..79
                     /region_name="COG3398"
                     /note="Predicted transcriptional regulator, contains two
                     HTH domains [Transcription]"
                     /db_xref="CDD:442625"
     Region          80..392
                     /region_name="ASKHA_ATPase_ROK_BsXylR-like"
                     /note="ATPase-like domain of Bacillus subtilis xylose
                     repressor (XylR) and similar proteins; cd24076"
                     /db_xref="CDD:466926"
ORIGIN      
        1 mitadqllvk qinksivlnt irkkgnisra diahitglnk stvsflvdel inegfvreeg
       61 pgaskggrkp iilsinnnag ciigidldvn yilivltdlm anviwekkvd ikigesqqai
      121 ierlielide ailnapntir gilgigigvp givdykkgsi lmapnlkwqd vplkeiienk
      181 fkikvhidne anvgaigekw fgtgikynnf vyvsagigig tgiiingely rgtvglagem
      241 ghmtinihdh qcscgntgcw enyasekalf dyihtqlimg ksdnyinkdn fntlsaldii
      301 nyaqkgseia vealkeigrk lgvgivnvin tfnpelviig ntlslagdli ldevlkevek
      361 kclvyryykv kiktsklqfh agaigavslv iselfaypgl
//
LOCUS       WP_009052229             276 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Thermoanaerobacter sp. X514].
ACCESSION   WP_009052229
VERSION     WP_009052229.1
KEYWORDS    RefSeq.
SOURCE      Thermoanaerobacter sp. X514
  ORGANISM  Thermoanaerobacter sp. X514
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Thermoanaerobacter.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 276)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Thermoanaerobacter sp. X514"
                     /db_xref="taxon:399726"
     Protein         1..276
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=32365
     Region          <1..275
                     /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 mfeakklgks kyvifdktie dkiiektemm vnikkamlnn efyllfqpiy dlrenrikev
       61 ealarwrnnk ygdispsrfv pvleetglik efgifiiedv fkqikdwrnk gielkvninv
      121 splqlrddef ffkfdelisk ynipsnligi eftetqildi keqkvnkide flrrgikisl
      181 ddfgvgyssl inmiefpist ikmdkslidr idenkvktli kgilyiskem nyevvaegve
      241 tgeqlsmlke wgcdkiqgyy isrpktseei elmfrt
//
LOCUS       WP_009052381             278 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Thermoanaerobacter].
ACCESSION   WP_009052381
VERSION     WP_009052381.1
KEYWORDS    RefSeq.
SOURCE      Thermoanaerobacter
  ORGANISM  Thermoanaerobacter
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Thermoanaerobacter"
                     /db_xref="taxon:1754"
     Protein         1..278
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31416
     Region          1..246
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mfadlhmhsk asdgtnspse vvrlakehgl scisltdhdt vdgleeamea sakyeievip
       61 giefncyyqn qevhilgyfi nykdkkffek leemkklrnd rakailkkln elgidisied
      121 vleftsekfi grphiaramv kknyvesvke afekyigvga payveryrit pfeainlile
      181 nggvtvlahp gllqddniie elapkgligi evyhskhtte dvekylnkak kykliitggs
      241 dfhgievdgr dllgtikldy eyvkilkska knfveisk
//
LOCUS       WP_009054383             111 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Nitritalea halalkaliphila].
ACCESSION   WP_009054383
VERSION     WP_009054383.1
KEYWORDS    RefSeq.
SOURCE      Nitritalea halalkaliphila
  ORGANISM  Nitritalea halalkaliphila
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Nitritalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Nitritalea halalkaliphila"
                     /db_xref="taxon:590849"
     Protein         1..111
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12411
     Region          3..106
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(26,57..58,60,86)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(26..27,35,38,40..41,43,46..47,49,57,62,69)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mgkeenyfdl vyevvrlipr grvtsygaia hylgmksgar mvgyamnaah sqpdvpahrv
       61 vnrlglltgk hhfgapdema rrllaegipv eedqvqdfqr yfwdpaqela l
//
LOCUS       WP_009054822             294 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Nitritalea
            halalkaliphila].
ACCESSION   WP_009054822
VERSION     WP_009054822.1
KEYWORDS    RefSeq.
SOURCE      Nitritalea halalkaliphila
  ORGANISM  Nitritalea halalkaliphila
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Nitritalea.
REFERENCE   1  (residues 1 to 294)
  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 294)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Nitritalea halalkaliphila"
                     /db_xref="taxon:590849"
     Protein         1..294
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32013
     Region          42..286
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mkrrtwlksi gisslalgta slhglagagq lrtpaakdsr irhafcswlf pelslteqcg
       61 vaqklgfqai dlvgpagwpt lkahglacsm cngaeislte gfaqadlhee lftryaalip
      121 evaaagytnl icfsgnqgrq sdaeclanca aglrpllpla kehgvilhme llnsrldhpd
      181 ywaatsakgi alceeldspq fkllfdiyhm qvmegdlirs irmhhqhfgh yhtagnpgrg
      241 eltnrqeiqy pavmaaimet gytgyiahef ipknpdkqqa laeakaicds ytkl
//
LOCUS       WP_009054972             114 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein, partial [Actinomyces sp.
            ICM58].
ACCESSION   WP_009054972
VERSION     WP_009054972.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces sp. ICM58
  ORGANISM  Actinomyces sp. ICM58
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 114)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Actinomyces sp. ICM58"
                     /db_xref="taxon:1105030"
     Protein         <1..114
                     /product="LytR C-terminal domain-containing protein"
     Region          33..113
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 ssaapaesgt eatpspspss saassapdhg aviqvlngtg tqgyagqqat ilnqagyagt
       61 saanadgwat qtstvyyedp smegtakdia sklgidnvrq esglgnpdiv vvlr
//
LOCUS       WP_009056112             332 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Nitritalea
            halalkaliphila].
ACCESSION   WP_009056112
VERSION     WP_009056112.1
KEYWORDS    RefSeq.
SOURCE      Nitritalea halalkaliphila
  ORGANISM  Nitritalea halalkaliphila
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Nitritalea.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 332)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Nitritalea halalkaliphila"
                     /db_xref="taxon:590849"
     Protein         1..332
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36241
     Region          2..332
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mkrarisgvg hylpervitn eylstlmntn newivertgi esrrwftpgk dtvtsmsvea
       61 tkmaleragl gpkdidfivf atitpdyflp gngvllqrel gmegigaldi rnacsgfiya
      121 isvadqfirt gmyknilvvg aeiqssaldk sdegrssavi fadgagaail taveddqphi
      181 lsthlhadgn faeelyckdp gssredrlsa alletgshfl rmngnavfkh avvrfqevil
      241 ealqansmqp adidllvphq anlrisnyiq qkmglpdekv fnnimyvgnt tagtipials
      301 eaweqgrlke gdlvclaafg sgfawasall rw
//
LOCUS       WP_009057123             533 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Actinomyces sp.
            ICM58].
ACCESSION   WP_009057123
VERSION     WP_009057123.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces sp. ICM58
  ORGANISM  Actinomyces sp. ICM58
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Actinomyces sp. ICM58"
                     /db_xref="taxon:1105030"
     Protein         1..533
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=55777
     Region          24..532
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mkraivvvcs waaalclala ylaigwgidd vvggaawstw wialaaalas gffawavsal
       61 gaitmkqlep slrhsmirqv falgpsqrtn eragrvvnsa tdgvervaay kgiflapmia
      121 slttpilvvi vvaltldpas ggflaiaipl vpicvmgfrk afkpvssryr hasrqlsake
      181 ldaiqglgdl almnagkdmg krlaeaaeev rskvmsylag nqlillvids vfslgmitga
      241 itlaliryeq galsaggais lvllssimld pldrigqffy igmggiaank eikkfneqtp
      301 pvvdakgvsv paipaapgei alsgvsfsyt kdtpvlrgan ltvspgehva lagpsgagks
      361 tisallqgfl rptrgrvsln gvdlatapls wvraqsavve qttylfsgtl rdnlllaapt
      421 atddqlieal raahlgefyd alpggldarv garglavsgg eaqriaiara flknasimil
      481 deptahvdla sereilasld tvcagrttlt ishrdatikd adrvatlqeg tir
//
LOCUS       WP_009057620             282 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [unclassified
            Actinomyces].
ACCESSION   WP_009057620
VERSION     WP_009057620.1
KEYWORDS    RefSeq.
SOURCE      unclassified Actinomyces
  ORGANISM  unclassified Actinomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="unclassified Actinomyces"
                     /db_xref="taxon:2609248"
     Protein         1..282
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29942
     Region          4..255
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mvkridphth saysdgtdtp aqllaiaaqa gldaialtdh dttagwdeaa aavantgvsl
       61 irgaemscsa sgitvhllay lfdptspglv enfrrtredr etraqrmvan laadypitwe
      121 dvvafapegg pvgrphiada lvaagafpdr saafvealhp sgpyyvhhwa pdpveavrcv
      181 reaggvpvla hprarkrqrl lpeaviadma aaglfgierd hrdhgpedra dveriaremg
      241 lamfgssdyh gtgkpnrige nttdpdviae vvaqgcigvv rp
//
LOCUS       WP_009057730             281 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator, partial [Actinomyces sp.
            ICM58].
ACCESSION   WP_009057730
VERSION     WP_009057730.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces sp. ICM58
  ORGANISM  Actinomyces sp. ICM58
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 281)
  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 281)
  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
REFERENCE   3  (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   4  (residues 1 to 281)
  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   5  (residues 1 to 281)
  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   6  (residues 1 to 281)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 281)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Actinomyces sp. ICM58"
                     /db_xref="taxon:1105030"
     Protein         1..>281
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          15..>54
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          74..>271
                     /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 mhyptrhplp tledrivaql alspatrsql cealdtsrtn lgralstlld egsvgavrsn
       61 aagrgrptql lalnataaha vgllitrtsc agvmlnrsga vlaavhivsq sspsmsrsle
      121 qtcetlaesa aaqgidvthv ravgvgvpip mgrnarlssn aypsveelas ltgrwwpaap
      181 vvdntvrmaa laeglwgagt gmssfiylrl sggvggcvvs dfrlvggatg lagelghitv
      241 agndalcacg klgcletlas ipalceraga qdltalraav h
//
LOCUS       WP_009057895             221 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Actinomyces sp. ICM58].
ACCESSION   WP_009057895
VERSION     WP_009057895.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces sp. ICM58
  ORGANISM  Actinomyces sp. ICM58
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 221)
  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 221)
  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   3  (residues 1 to 221)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Actinomyces sp. ICM58"
                     /db_xref="taxon:1105030"
     Protein         1..221
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24959
     Region          88..171
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mhysklrrfd dvcihwepvl skeeerthva sigtvlervl vcmplkvslp mldaarnrgl
       61 ydvstlaipp tgsrlphlre alslsserar siletvarlq lidmgltpqv gvwiegvgev
      121 dmiildfivi evdgwafhss keqrekdlkr drellrrgyv vlrftyddvm ngdfarevpi
      181 svaalrrlvp etgledahat vknagfldil sgylpsyhlq r
//
LOCUS       WP_009058409             146 aa            linear   BCT 20-JAN-2025
DEFINITION  division/cell wall cluster transcriptional repressor MraZ
            [Candidatus Methylacidiphilum fumarolicum].
ACCESSION   WP_009058409
VERSION     WP_009058409.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Methylacidiphilum fumarolicum
  ORGANISM  Candidatus Methylacidiphilum fumarolicum
            Bacteria; Pseudomonadati; Verrucomicrobiota; Methylacidiphilae;
            Methylacidiphilales; Methylacidiphilaceae; Methylacidiphilum (ex
            Ratnadevi et al. 2023).
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Chen,S., Jancrick,J., Yokota,H., Kim,R. and Kim,S.H.
  TITLE     Crystal structure of a protein associated with cell division from
            Mycoplasma pneumoniae (GI: 13508053): a novel fold with a conserved
            sequence motif
  JOURNAL   Proteins 55 (4), 785-791 (2004)
   PUBMED   15146477
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449500
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Candidatus Methylacidiphilum fumarolicum"
                     /db_xref="taxon:591154"
     Protein         1..146
                     /product="division/cell wall cluster transcriptional
                     repressor MraZ"
                     /GO_function="GO:0000976 - transcription cis-regulatory
                     region 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=17181
     Region          12..145
                     /region_name="MraZ"
                     /note="DNA-binding transcriptional regulator and inhibitor
                     of RsmH methyltransferase activity [Translation, ribosomal
                     structure and biogenesis]; COG2001"
                     /db_xref="CDD:441604"
ORIGIN      
        1 mgkkratytd ifehafdekg ritvpsewrq egydsrlfvf pskfhhlkvy peswmeeihq
       61 kietlrlqdp irqqlellaq isqavswdqq grisikerlr khsqigkeav lvgrldhfei
      121 wdqrkwqeet agkstsfeea iegmgl
//
LOCUS       WP_009058609             360 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Candidatus Methylacidiphilum fumarolicum].
ACCESSION   WP_009058609
VERSION     WP_009058609.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Methylacidiphilum fumarolicum
  ORGANISM  Candidatus Methylacidiphilum fumarolicum
            Bacteria; Pseudomonadati; Verrucomicrobiota; Methylacidiphilae;
            Methylacidiphilales; Methylacidiphilaceae; Methylacidiphilum (ex
            Ratnadevi et al. 2023).
REFERENCE   1  (residues 1 to 360)
  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 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   3  (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   4  (residues 1 to 360)
  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 360)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Candidatus Methylacidiphilum fumarolicum"
                     /db_xref="taxon:591154"
     Protein         1..360
                     /product="CmpA/NrtA family 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=40284
     Region          17..262
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mkrgevtqgg rtlrigskit vgyiplidca plvvalemgl fkkwgfdvql spepgwatir
       61 gkivyeeldf aqavcglplv lnyglksipc rcstafvlnl ngnaitlskk yssilenesl
      121 enygrilkat sglpllfgva stfsshyfll rrwlqkigln pqkdirfvpl pppqmpihlk
      181 egfidgfcvg epwnsvslfe ktgycvatsl dlaprhpekv llanakyker kreehirivg
      241 clieacqwad splnrqalae mlhyggwiaq plevlqhsli gpfrmgknif ipgqafhvfs
      301 qgnanspske keqwivnemv dagllkreer knrsffdtei ykqaekivaq qkantlpisi
//
LOCUS       WP_009058611             716 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Candidatus
            Methylacidiphilum fumarolicum].
ACCESSION   WP_009058611
VERSION     WP_009058611.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Methylacidiphilum fumarolicum
  ORGANISM  Candidatus Methylacidiphilum fumarolicum
            Bacteria; Pseudomonadati; Verrucomicrobiota; Methylacidiphilae;
            Methylacidiphilales; Methylacidiphilaceae; Methylacidiphilum (ex
            Ratnadevi et al. 2023).
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 716)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 716)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Candidatus Methylacidiphilum fumarolicum"
                     /db_xref="taxon:591154"
     Protein         1..716
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=80254
     Region          13..701
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 miekhikdri yakypthcpf csyqcaiwvv qdshgfrvep refttnkgei cikgwhaaal
       61 ighpkrvlnp lirykkdnaf resnweeais ftvdkisqir srwgnssifv ygsgsltnek
      121 ayllgkfarv alqtsaidyn grycmasask alemalgidr glpfpidyia htdllllvgt
      181 npletmppir shfdclkkrn kkiiaidprp tptatyadvh lqikpgtdgi langllylli
      241 qknkidhyfv rnytsgfeki lnsvssfwpa kvetltgisq relfrvaell gteknivilt
      301 grgceqqtqg vfnvlsfinl slalgivgkv nsgfgtltgq gngqgarelg lkpdqlpgar
      361 snldsfdrny iaslwqidek dlpssdksvt eifeslekpq gikamlvfga npivsspnns
      421 klkrlfpqle fllvcdpfls etaamadvvl ptaiwaeetg tvtnlegrvl lrpkildppk
      481 nvktdleiih llaekfgygl rfssdpqaif eelrrataga aadysaityq rlsrgeelyw
      541 pchsflskgq kdifltkrfp tdkgkakfhp vyptaspeep nieypfyltt grtlhhyqtg
      601 vqtrliqklq ekepsvivei npavarhfgi kdgqyvlvet krgkgyfkak fspnlrldtl
      661 fipfysnaqa eanaltishf dplskmpsfk lcaakiqslt eqtphtehte irkekk
//
LOCUS       WP_009059626             119 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Actinomyces sp. ICM58].
ACCESSION   WP_009059626
VERSION     WP_009059626.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces sp. ICM58
  ORGANISM  Actinomyces sp. ICM58
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Actinomyces sp. ICM58"
                     /db_xref="taxon:1105030"
     Protein         1..119
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=13025
     Region          1..97
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(24,51..52,54)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mreelveavl rvvesipagh aatygmiara vgtgprvvgr imhdwggsvp wwrvvnvhgt
       61 fpttvrgdgl shweqegmrh dpvrgrlals aclvdqdwld tvaqtvlenl rnsaemsdl
//
LOCUS       WP_009059945             184 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Candidatus Methylacidiphilum
            fumarolicum].
ACCESSION   WP_009059945
VERSION     WP_009059945.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Methylacidiphilum fumarolicum
  ORGANISM  Candidatus Methylacidiphilum fumarolicum
            Bacteria; Pseudomonadati; Verrucomicrobiota; Methylacidiphilae;
            Methylacidiphilales; Methylacidiphilaceae; Methylacidiphilum (ex
            Ratnadevi et al. 2023).
REFERENCE   1  (residues 1 to 184)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Candidatus Methylacidiphilum fumarolicum"
                     /db_xref="taxon:591154"
     Protein         1..184
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20185
     Region          1..182
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mrivigitga sgaiyaqrll hflsstehei hviisnrgkq viglelgrnl eipkkfglys
       61 dntmeapfvs gssrfdamvi ipcsmgtvgr iaqgisnsti trsadvflke rrklilvire
      121 tplhlihlrn latlteagal ilpacpsfyg lpstieelvd svnarvldhl gienslsvrw
      181 rehf
//
LOCUS       WP_009060868             740 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Candidatus
            Methylacidiphilum fumarolicum].
ACCESSION   WP_009060868
VERSION     WP_009060868.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Methylacidiphilum fumarolicum
  ORGANISM  Candidatus Methylacidiphilum fumarolicum
            Bacteria; Pseudomonadati; Verrucomicrobiota; Methylacidiphilae;
            Methylacidiphilales; Methylacidiphilaceae; Methylacidiphilum (ex
            Ratnadevi et al. 2023).
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Candidatus Methylacidiphilum fumarolicum"
                     /db_xref="taxon:591154"
     Protein         1..740
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=83355
     Region          62..740
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mnheiiyimk ycnyslvrkl filciinnsi nfgslngqqs qespnpntrv vmpevevses
       61 epsltvpsaq kmqellnelp assnlieakr vrqgraatlq dlflfqpgiw tqpgftgpna
      121 frisirgsgl stgagtergi wflqdglpln ppdgvlfnqg efdplayqys visrgaeafn
      181 ygfatlfgav nfvtytgyta ppysayftag sfgwlqgsie aagvesktdy favlsdasae
      241 gyrfhnsfnn awlntnigyk itpnaenriy ftysnqqwqv pgplaleevl tdpttanpay
      301 vegdyrqfwd ttrladkaty tidqhqtvnm giswtnlhqi tfyglffqss nnffslpcny
      361 tntmdlyghr nlivagampm gefyqenwnk llgtiqgapm atynmtvvni piyaydqfwv
      421 nekfsinlal qavydrltne aykdlihrsv dttltfsqfn pklgllyqvd phnqvytsva
      481 rsfeppslye taispnalpp nlalypnraq naitaeigtr gqwdrfnwsf affqswvtne
      541 llevslnppl ntliytinap ptthrgieis lnttlarglm vsdsdpqnqd qivlyqifdw
      601 yrfylngnff sptthqeihl sgnqlfgvpe ysymaqllym hpsgfyigpn vmawstypvd
      661 lvnttfapgt allgfrigyq npkkhlsiyl dgrnltnehy vamvsdvfda snggkiplsk
      721 qtyfwpgdgw aiyggiswnf
//
LOCUS       WP_009061198             139 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Clostridium sp. MSTE9].
ACCESSION   WP_009061198
VERSION     WP_009061198.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. MSTE9
  ORGANISM  Clostridium sp. MSTE9
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (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   2  (residues 1 to 139)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Clostridium sp. MSTE9"
                     /db_xref="taxon:1105031"
     Protein         1..139
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14714
     Region          66..134
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mdqdarqvrw llavaiilca lmigynvlfv pqvtltavvk tdlssaaqaa vpsapddvsq
       61 pegyepepve qtalvnlnta daeeletlpg igpataqkii ayresvgafq steelmqvgg
      121 igektfeklk elvtveaae
//
LOCUS       WP_009061980             288 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Clostridium sp. MSTE9].
ACCESSION   WP_009061980
VERSION     WP_009061980.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. MSTE9
  ORGANISM  Clostridium sp. MSTE9
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 288)
  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 288)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 288)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 288)
  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   5  (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   6  (residues 1 to 288)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Clostridium sp. MSTE9"
                     /db_xref="taxon:1105031"
     Protein         1..288
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33009
     Region          19..99
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          124..285
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mlqelnraie yieehltdel ylekisehvg isdyhfrtvf fylagmtlse yvksrrlsqa
       61 nqdllmgekv tdiaykygyg smdgfarafk kwsgflpsda vkkriskpfp klsfvitikg
      121 gntmecriee kpafylagvs krvpmqfegv nnaivdlams itneqreemh alqnmephqi
      181 vnasyeadag flkeegelth ligvlttkee vsdrlvkvpv eacvwavfpn egpfpftlqn
      241 tmariysewl ptsdyevlnm pafsfskmde rkkdyaysev wtpvrkkk
//
LOCUS       WP_009062586             510 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Clostridium sp. MSTE9].
ACCESSION   WP_009062586
VERSION     WP_009062586.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. MSTE9
  ORGANISM  Clostridium sp. MSTE9
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Clostridium sp. MSTE9"
                     /db_xref="taxon:1105031"
     Protein         1..510
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54821
     Region          5..509
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mttekkspvi rldsadnivv arepvaagty ipdedftvqs dipighkias rairqnepil
       61 kyntvigyaa rdveagthmh netiyfdsvs kqyefcrdyh pvnilppeqc rtfqgyvrpd
      121 gqvgtrncia vavcsncaat varkianyft perlkdypnv daivplitss gcglektgtp
      181 msylrrilgg hvknpniaga vvcalgcesn nidaffeeae ltpgpllgrl viqevggsrk
      241 ameqgiamve amlpianqcq rqpvpishlk igmecggsds fsgssanpal gkamdllieq
      301 ggtavlteit elfgiegafv rrakspevaq klidlmnwwl dyckgrdaqi ngkvtpgnna
      361 ggltnileka lggakkggst plngvfdyge kiteqgfvim napaydpmaa aalfaggcnl
      421 cvfttgrgsc fgaqhfptlk issntplfqr qeddmdmnag vvidgektle emgedifeai
      481 ievasgkptk selfgmgnde fvvwwlgits
//
LOCUS       WP_009065562             279 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            SPB78].
ACCESSION   WP_009065562
VERSION     WP_009065562.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. SPB78
  ORGANISM  Streptomyces sp. SPB78
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 279)
  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 279)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Streptomyces sp. SPB78"
                     /db_xref="taxon:591157"
     Protein         1..279
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31737
     Region          6..69
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          104..270
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mtfdpetlgq srndlaemlr dqrrragktq twlarrcams qtkvsniesg kltpslldve
       61 mmlealgvre siaaqifsva rtantewqdh wssrrrgldk kqnelsrles astefrffll
      121 smitgllatp dyvrasiadv pgdqsktiak klerqqvlyd pkksftfvlt eqavrwpllp
      181 pvamamqldr lasvsripsv rlgviplsgy lperplntft vydrklatve tgtgalllrd
      241 rrdvlaylsd fesyeryaaf gdecrellse wsvfftrqr
//
LOCUS       WP_009066544             494 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Clostridium sp. MSTE9].
ACCESSION   WP_009066544
VERSION     WP_009066544.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. MSTE9
  ORGANISM  Clostridium sp. MSTE9
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Clostridium sp. MSTE9"
                     /db_xref="taxon:1105031"
     Protein         1..494
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=53784
     Region          2..494
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mnqfyqinpk dtvivalqpi pagtvldvdg qelitvndvp pghkialkem ekgepiikyg
       61 fpigtaarpi qrgewvhthn vkttlgelld ytytsdfhel eaiapksfqg yrrkdgkvgv
      121 rnevwiiptv gcvnsivkqi elqsqqfltp eldgifcyth pygcsqlsgd hvntqlalag
      181 mahhpnagav lvvglgcenn tmeqmkkvlg dydperikfm icqefedeve egvrlmeelc
      241 ryasqfhree csvsdlvigl kcggsdgfsg itanplvgaf sdllvaqggt siltevpemf
      301 gaetilmnrg kdrqtfektv dlinnfkkyf mrygeeidsn pspgnkaggi ttledkslgc
      361 iqkggsskvv dvlnygqavt qkglnllqgp gndlvastal aisgahivlf ttgrgtpfac
      421 pvptikissn talsrkksgw idfnagqlle grsmrdvaee ffnfvvdvas gskhaksesl
      481 dkrdlpifkd gvtl
//
LOCUS       WP_009068239             408 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Streptomyces sp.
            SPB78].
ACCESSION   WP_009068239
VERSION     WP_009068239.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. SPB78
  ORGANISM  Streptomyces sp. SPB78
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 408)
  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 408)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Streptomyces sp. SPB78"
                     /db_xref="taxon:591157"
     Protein         1..408
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45197
     Region          5..394
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mttqplplsa dearrialra qgllgapdrr agargvlrhl gavqldtisv larshelvpy
       61 arlgaigrqa vesaywappe apahafeyws haacvlpvee wphfafrrra yrdrplwghe
      121 mppgayekvl aqlrdegplt atelggakng gewwdwsgsk vaveraltyg dvvcvrrtgw
      181 rrvydlpera ipaellhddl ddlecvrrli rlaarslgvg trsdladyhr lkteqfdavi
      241 edcglvrvrv egwgkpawad pqalessprg rhrttllspf dsliwerara erlfgfshrl
      301 eayvpkpkrv hgyfampvls ggrliarvdp aregttlvar qitlggdvpg tatprkavdg
      361 takalaeaat wvgctrvrvd rvdppelrep lereatralt arlegaev
//
LOCUS       WP_009069117             406 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. SPB78].
ACCESSION   WP_009069117
VERSION     WP_009069117.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. SPB78
  ORGANISM  Streptomyces sp. SPB78
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 406)
  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 406)
  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
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 406)
  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   5  (residues 1 to 406)
  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   6  (residues 1 to 406)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 406)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 406)
  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 15726307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Streptomyces sp. SPB78"
                     /db_xref="taxon:591157"
     Protein         1..406
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42476
     Region          10..>124
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          69..382
                     /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 mahtqasagh llrlirsgaa itrgelqeat glsrstvghr ldqlfaagwl rgssgtstgg
       61 rpsarlefdt ghavvlvadl etpharaavv dlagtvlaeh rdalviadgp dvvldqlarw
      121 faelldasgq ppervcgvgl svpgpvdwer allvqppimp gwdgyplrer lreyyaahvg
      181 rppreeplpv fvdndanlma lgeqralhpd crafvfvkts tgigagvvvd galyrgidgg
      241 agdighirlh drpdvvcmcg stgclaavas ggaiaaqlte agvptasghd vrahlaagqp
      301 davrlsrrag qrigevlvtv vtllnpgvlv lggdlastpf ltgvrellyq ramprttahl
      361 qvltselgdr agllgaaimv vdhlyapera darlhaltra ttgaar
//
LOCUS       WP_009070663             386 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Streptomyces].
ACCESSION   WP_009070663
VERSION     WP_009070663.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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   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   4  (residues 1 to 386)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..386
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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]"
                     /note="Members of the family are the ATP-binding subunit
                     of ABC transporters for substrates such as betaine,
                     L-proline or other amino acids, choline, carnitine, etc.
                     The substrate specificity is best determined from the
                     substrate-binding subunit, rather than this subunit, as it
                     interacts with the permease subunit and not with substrate
                     directly.; Members of the family are the ATP-binding
                     subunit of ABC transporters for substrates such as
                     betaine, L-proline or other amino acids, choline,
                     carnitine, etc. The substrate specificity is best
                     determined from the substrate-binding subunit, rather than
                     this subunit, as it interacts with the permease subunit
                     and not with substrate directly."
                     /calculated_mol_wt=42070
     Region          1..306
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mirfegvgkr yadgtvavhd lsldvaegql vtlvgpsgcg ktttmmmvnr lveptsgrie
       61 vdgediahvd pvalrrrigy viqqvglfph rtvldntatv lsllgtkrgr arerarelld
      121 lvgldpetfg pryphqlsgg qrqrvgvara laadppvllm depfgavdpv vrerlqnqfv
      181 dlqrrlrktv lfvthdieea vrlgdrmavy gpgrieqfdt pqtvlgrpat pyvaefvgtd
      241 rglkrlsvte irpedleepp lvrrsepaar aaerlraega rwavvldeag elhgwvgvde
      301 lggggdravg elahrmnawv pvgaplkqaf gemlqhdagw vavldgarfl gvltpgklhe
      361 alrrsvdada rgvrrgdvdf esvada
//
LOCUS       WP_009070687             389 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Streptomyces].
ACCESSION   WP_009070687
VERSION     WP_009070687.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 389)
  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 389)
  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
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 389)
  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   5  (residues 1 to 389)
  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   6  (residues 1 to 389)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 389)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 389)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..389
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39764
     Region          18..69
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          84..377
                     /region_name="ASKHA_ATPase_ROK_BsXylR-like"
                     /note="ATPase-like domain of Bacillus subtilis xylose
                     repressor (XylR) and similar proteins; cd24076"
                     /db_xref="CDD:466926"
ORIGIN      
        1 mtaalpdtqq gmrrrnlarv lhtvaahgpl sraavaarig ltraavstlv deliragfld
       61 elgperpgrv grpgsalavs argpaglgae igvdhlsvca vdlsgtvrar vvrpvdnrer
      121 aakpvlaelv alvdevrvaa ealglrpagl avavpglver drpfvvrapn lgwtdtdlgp
      181 llpeglpvtv dneanfgala elwtgggahe nfvhvsaaig igaavvlgge llrgtrgfag
      241 elghvpvrpe gpscpcggrg cleqyagqea vwraaglapg qepvgllaqr aaegdkavlk
      301 alrgagsalg ialsgavnll dpegvvlggs lsplaewllp plrreltrrt atanrpvtvs
      361 rlgregpllg aahsvvravl ddpvsltae
//
LOCUS       WP_009072993             678 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: molybdopterin oxidoreductase family protein
            [Actinomycetes].
ACCESSION   WP_009072993
VERSION     WP_009072993.1
KEYWORDS    RefSeq.
SOURCE      Actinomycetes (high G+C Gram-positive bacteria)
  ORGANISM  Actinomycetes
            Bacteria; Bacillati; Actinomycetota.
REFERENCE   1  (residues 1 to 678)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 678)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 678)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..678
                     /organism="Actinomycetes"
                     /db_xref="taxon:1760"
     Protein         1..678
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=72282
     Region          1..678
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mphvdthcpy calqcgmrld etrvtprdfp vnagglcqkg wtsgallesa arltspllrr
       61 dgelqpvswd ealdfvadrl lasrrehgad svavfggggl tnekayllgk farvalgtsq
      121 idyngrfcms saaaagmraf gvdrglpfpv tdlanadvvl laganpaetm ppfmqhldna
      181 elivvdprrt ptaeratlhl apapgtdlal algilhavva eghldksyvd lrttgfdemw
      241 riaatwwper aervtgvsaa dqrraaemla ragnayvlta rgteqhasgt atvggwinla
      301 lalglpgrag sgfgcltgqg ngqggrehgq kadqlpgyrk iddpaaraqv aqvwgvepes
      361 lpgpgrsave lldalgesik allvfgsnpv vsaprssrvq erlagldllv vadfvlseta
      421 eladvvfpvp qwaeeegtlt nlegrvllrq rsidppdgvr sdlsllrela vrigqpaerf
      481 pddaaevfee lraaskggaa dysgvtydrl rsgealhwpv pgethpgtpr mfldgfahpd
      541 grarfagvdh sgpaelpdea fplqattgrv lqhyqsgaqt rriaeltavv pevfvevhpd
      601 taarsgladg dravvrsrrg etvaqvrcvp smrvdlvflp fhfpgaaran lltnpaldpv
      661 srmpefkvca vslaraea
//
LOCUS       WP_009073019             109 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Actinomycetes].
ACCESSION   WP_009073019
VERSION     WP_009073019.1
KEYWORDS    RefSeq.
SOURCE      Actinomycetes (high G+C Gram-positive bacteria)
  ORGANISM  Actinomycetes
            Bacteria; Bacillati; Actinomycetota.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Actinomycetes"
                     /db_xref="taxon:1760"
     Protein         1..109
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11831
     Region          1..96
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(5..6,24..25,33,35,37..38,40,43..44,52,57,62)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(24,52..53,55,77)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mndelherir aviadvpagt vatygdvaal sgapsprmvg ralaedghdl pwhrilrang
       61 tpaphllheq lerlraegvl adgdkvdlrk yrwrpdgdep gedeppglf
//
LOCUS       WP_009073056             409 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Actinomycetes].
ACCESSION   WP_009073056
VERSION     WP_009073056.1
KEYWORDS    RefSeq.
SOURCE      Actinomycetes (high G+C Gram-positive bacteria)
  ORGANISM  Actinomycetes
            Bacteria; Bacillati; Actinomycetota.
REFERENCE   1  (residues 1 to 409)
  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 409)
  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
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 409)
  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   5  (residues 1 to 409)
  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   6  (residues 1 to 409)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 409)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 409)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Actinomycetes"
                     /db_xref="taxon:1760"
     Protein         1..409
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42284
     Region          16..56
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          81..373
                     /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 mragsprtlr emndraaiea llrngpmtrg eleaaiglsk pataqlltrl eqenlvgkag
       61 eragggrgpr aqlwavngal ahvaavdltp rvadfvvadv agavlaeyrv qlpvaedadv
      121 vgsfgqalrr vakaaglqld dlanvvigaq gafdprtgll ssaphipgwl gfdvpkrlsd
      181 elgvtvkien dvnlvaveem tvgnaqdvdd fvlvwlsegv ggavvigrrl lrgatgggge
      241 idwmrvpdpa tvdtgdswps agarygnlvd ssaivrlaka hgitadsgwd avtqarrtah
      301 lgflddfarr vasgvaslva vadpqlillc getsraggde fagivaeklh elvlprtpvg
      361 vasvqgnavr agalqsalat aredvfgvvt ptllgprrsa geqapspte
//
LOCUS       WP_009076016             282 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Actinomycetes].
ACCESSION   WP_009076016
VERSION     WP_009076016.1
KEYWORDS    RefSeq.
SOURCE      Actinomycetes (high G+C Gram-positive bacteria)
  ORGANISM  Actinomycetes
            Bacteria; Bacillati; Actinomycetota.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Actinomycetes"
                     /db_xref="taxon:1760"
     Protein         1..282
                     /product="formate/nitrite transporter family protein"
                     /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=28261
     Region          6..240
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mpipvpeald lqadvadgki aelrrpgryl vssmlagafi gvavvlllsa tgplnaassp
       61 wtktvqglvf gialtavvfa gaelstgnmm tmvqgalvrr rgagtaaavi vvsfagnllg
      121 sivfawlvhe ggvlsigaag ghpgpgaall aslvkaktae sasalffrgv lcnflvclav
      181 wmaartksdg aklalifwcl lafvssgfeh vvanmttfsl glmdgvpgat igafgrnllf
      241 vglgnlvggg llvgaayall gsrsratapp vpaaeelatt gs
//
LOCUS       WP_009075522             389 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Actinomycetes].
ACCESSION   WP_009075522
VERSION     WP_009075522.1
KEYWORDS    RefSeq.
SOURCE      Actinomycetes (high G+C Gram-positive bacteria)
  ORGANISM  Actinomycetes
            Bacteria; Bacillati; Actinomycetota.
REFERENCE   1  (residues 1 to 389)
  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 389)
  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
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 389)
  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   5  (residues 1 to 389)
  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   6  (residues 1 to 389)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 389)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 389)
  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 15726307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Actinomycetes"
                     /db_xref="taxon:1760"
     Protein         1..389
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40209
     Region          1..>76
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          84..383
                     /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 mssppvarpd evrrhnrttl lrllhvggps traalatelg lnrstiktlv dglaeagvve
       61 ekvprpgrga grpsllvlpq phaavvlavd lqvehvaial vglggqilgr nswnlhartr
      121 tadevithvi estrvlasdl gvepvaagvs vpgvvrradg lvheapnlrw tdvalgdrls
      181 avlripvlva ndaelgavae hlrgaargss dsvyvsadvg vgggvisqgs slrggagyvg
      241 eighmairpg gracycgsrg cweteigeaa lcralglped tprgvilvel relgldaaaa
      301 asrlaeyaew ltlglvnvvn llgpelvvlg dlltvlpesv mravaeevrg rslvsravgg
      361 trivssalga dvkllgaaev afevvldmv
//
LOCUS       WP_009080057             195 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Actinomycetes].
ACCESSION   WP_009080057
VERSION     WP_009080057.1
KEYWORDS    RefSeq.
SOURCE      Actinomycetes (high G+C Gram-positive bacteria)
  ORGANISM  Actinomycetes
            Bacteria; Bacillati; Actinomycetota.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Actinomycetes"
                     /db_xref="taxon:1760"
     Protein         1..195
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21774
     Region          15..190
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mefqevvrrr rmvrkftgep vseesirrim rnalrgpsag fsqgqaflvl qgddvrrfag
       61 tleswtlddn vksapvivip fsvkdayldr yaqpdkgwtd rsedhwpvpf wyidtgmavl
      121 lilqtvvdeg lgavyfgiga qdfdrlraef gvpdthepig aiaighdada kispgaspat
      181 rrrkpesetv hfgqw
//
LOCUS       WP_009084014             220 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LytR C-terminal domain-containing protein
            [Actinomycetes].
ACCESSION   WP_009084014
VERSION     WP_009084014.1
KEYWORDS    RefSeq.
SOURCE      Actinomycetes (high G+C Gram-positive bacteria)
  ORGANISM  Actinomycetes
            Bacteria; Bacillati; Actinomycetota.
REFERENCE   1  (residues 1 to 220)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Actinomycetes"
                     /db_xref="taxon:1760"
     Protein         1..220
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=21753
     Region          124..213
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 msvfsglsrp lkaagvalig vavvaavigg itvlntsgdq nagpttsgep tapggsssaa
       61 pgqsssaaps sapsspassa passsaassa pasnpagqpg aqpgqqpgqp gqagpdqqas
      121 nkwvtlrvyn nslikhlaeq aaadfrgsgw nvaevgnykd gviptttayf rpgtdeeaaa
      181 kqlakefgfq aqprfegiqn sspgviviit kdyqprhsgs
//
LOCUS       WP_009084737             251 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: aminoglycoside phosphotransferase family protein
            [Actinomycetes].
ACCESSION   WP_009084737
VERSION     WP_009084737.1
KEYWORDS    RefSeq.
SOURCE      Actinomycetes (high G+C Gram-positive bacteria)
  ORGANISM  Actinomycetes
            Bacteria; Bacillati; Actinomycetota.
REFERENCE   1  (residues 1 to 251)
  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   2  (residues 1 to 251)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Actinomycetes"
                     /db_xref="taxon:1760"
     Protein         1..251
                     /product="aminoglycoside 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=27560
     Region          10..166
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mtedrqvfrg glntvvrigs tvrrdrgpws drvaallrhl edvgfrqapr yfgsegdtdv
       61 leflpgevsd ypltpaarst talisaakll rryhdatadl vlpggwmlpd repaevichg
      121 dfapyncvlr geevvglidf dtahpgprlh dlgyavyrfa pltdpanqdg fgsieeqaar
      181 aklfcdsygf tdraavlesa varlrdlvhl mrtqaasghe gfashlaagh drvylrdlah
      241 ieanraqysl s
//
LOCUS       WP_009084267             298 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Actinomycetes].
ACCESSION   WP_009084267
VERSION     WP_009084267.1
KEYWORDS    RefSeq.
SOURCE      Actinomycetes (high G+C Gram-positive bacteria)
  ORGANISM  Actinomycetes
            Bacteria; Bacillati; Actinomycetota.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 298)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Actinomycetes"
                     /db_xref="taxon:1760"
     Protein         1..298
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32704
     Region          27..286
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          44..134
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
ORIGIN      
        1 mrpsqppfaa avlklrdall fsamrripsg ilnertartk ftltryppap elrdfvehhw
       61 vlrwnlteph dqhvlpnlsv hvtffpgacg vygpahqlft hrlsgrvhgi garirpgcfr
      121 pflgapvrtl adrsagvaei fgptaartek firnartdee mitaidnlli asrrpipret
      181 raaaeaveti aadpgitrvs elaaalglsi ravqrlfaeh vgttpkwair iyrlneaarl
      241 laapippdya dlatrlgysd qphfirdfra vtgappaeya rsarqlmsaa pdgakpgn
//
LOCUS       WP_009086292             401 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Elizabethkingia
            anophelis].
ACCESSION   WP_009086292
VERSION     WP_009086292.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
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   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 401)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..401
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46639
     Region          1..397
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mkkiltlqdl qritlesqgl ahspmfgtgk navvnalehl gyvqidtlsv verahhhtlw
       61 sriddykthy lndllkerkv feywfhaasy lpmkdyryal pqmlsfkhne sqyynadpkv
      121 mqyvidtirt egprkakdfe negkaagnww nwkpaklale klfmqgdlmv sgrdgmqkiy
      181 diservlpqt tnltiptpie laeylvkthl raygltslkq ithlrsdpvl rknveqvlqs
      241 mvedkviqkt eidgissmyi qkdliekgae fpnseiklls pfdnslihrd rfkqlfnfdf
      301 rlecylpkek rqygyfclpi lygnifigrv dckahrsikk lelinmhien tnidieswir
      361 vfaeaierfa nfngcnsitl tkvspskytk llkqalsgyk i
//
LOCUS       WP_009087348             496 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Pantoea sp. Sc1].
ACCESSION   WP_009087348
VERSION     WP_009087348.1
KEYWORDS    RefSeq.
SOURCE      Pantoea sp. Sc1
  ORGANISM  Pantoea sp. Sc1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Pantoea sp. Sc1"
                     /db_xref="taxon:593105"
     Protein         1..496
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54156
     Region          1..496
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mqdaikidpr dnvavalrdl aagatvelpp qrvvlhqavg rghkfalqpv gqnepvikyg
       61 lpighatqpv aagelihsqn artnlsdldh yayqpdvvtl ppqrgdrevq iyrrasgevg
      121 irnelwilpt vgcvngiarq ilqrflqetq qaedidgafl fshtfgcsql gqdhdntrtm
      181 lqnmvrhpna gavlviglgc ennqvdvfrd tlgafesdrv efmvcqqhdd eveaglerlh
      241 alyqkmrhdr repgrlselk fglecggsdg fsgitanpll grfsdqmian ggttvltevp
      301 emfgaerilm srcrdeetfh ktvamindfk qyfidhqqpi yenpspgnka ggittleeks
      361 lgctqkagqs qvvdvlkyge rlttpglnll sapgndavat salagagchm vlfstgrgtp
      421 yggfvptvkl atntplaekk phwidfnagr liegmsmeam ledfvdtiva iasgqptnne
      481 kndfrelaif ksgvtl
//
LOCUS       WP_009088721             289 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Elizabethkingia anophelis].
ACCESSION   WP_009088721
VERSION     WP_009088721.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 289)
  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 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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..289
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34280
     Region          59..284
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          207..285
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 medfliepfl hsddsqqyin tkeidellqi rptelfqshk tmfniihlft egkgkltvdf
       61 ntfdieerhi lfisqhqisq fhnpvnyksk iliftedffg knvfqtqffg qthlfndpll
      121 lpyfdlgdry eevvslfnfi stelnrpyne vqttilnnyl fnillivesl cerkdiklvv
      181 ndekllvskf ksivnanlnw qynldyytek lnvglrtlqn afqltekqtp kqwlidrmil
      241 eikrnliyke vgisaiaynl gfkevtnftk ffksktgltp tqfrelsyw
//
LOCUS       WP_009090087             255 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: prolipoprotein diacylglyceryl transferase
            [Elizabethkingia].
ACCESSION   WP_009090087
VERSION     WP_009090087.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia
  ORGANISM  Elizabethkingia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002130
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Elizabethkingia"
                     /db_xref="taxon:308865"
     Protein         1..255
                     /product="prolipoprotein diacylglyceryl transferase"
                     /EC_number="2.5.1.145"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008961 -
                     phosphatidylglycerol-prolipoprotein diacylglyceryl
                     transferase activity [Evidence IEA]"
                     /GO_process="GO:0009249 - protein lipoylation [Evidence
                     IEA]"
                     /GO_process="GO:0042158 - lipoprotein biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28601
     Region          4..238
                     /region_name="Lgt"
                     /note="Prolipoprotein diacylglyceryltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0682"
                     /db_xref="CDD:440446"
ORIGIN      
        1 midfpatlhl fgkdillhpv leslgiflgm ryyfflkrks peklpltisl aiiagataga
       61 llgskiignl enpytlfstd fsikrfwsnn tivgglafgl igvelakkiv ghkestgdli
      121 tfplmlaiii grigcfftgi yeetyglptd sifgmhlgdq ylrhpvalye iaflvllwgi
      181 lkviqkkhfp sgfvfqifml syftfrffld flkprieivg nlgaiqltcl lviiyyiykv
      241 nitlkskyla pnnli
//
LOCUS       WP_009091347             346 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Elizabethkingia].
ACCESSION   WP_009091347
VERSION     WP_009091347.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia
  ORGANISM  Elizabethkingia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Elizabethkingia"
                     /db_xref="taxon:308865"
     Protein         1..346
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=38823
     Region          92..250
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mrntlyfigl savlfscgss knvtpqkkni pvnknnssnv tsksqtpsvq tpvkpaiqkd
       61 hgvefyttni aditkndnta sygsivtakp mgyqitknyf paigqnfrqr ylilhytald
      121 ndrsitaltq rgvsahylvs dindqeiyqi vdenkrsyha gvsnwrkdsn lndtsigiei
      181 vnsgfttnas gqrifadfpd yqikkvaala kdivqrynip ptnvlahsdi apgrkqdpgp
      241 kfpwkklyde yqigmwydeg vragflnqle tgtfesdknt ppfiykvqsq lqalgyqvdl
      301 sgewdnqtkl vvqsfqyhfw pqigdgvldm gtyatllall qkypsk
//
LOCUS       WP_009091874             148 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Elizabethkingia].
ACCESSION   WP_009091874
VERSION     WP_009091874.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia
  ORGANISM  Elizabethkingia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 148)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Elizabethkingia"
                     /db_xref="taxon:308865"
     Protein         1..148
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16498
     Region          4..148
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mknlkqrlsy llaadesven rlkkvcvlld qeipyynwtg fyfrngdkee lvlgpyvgae
       61 tdhtvipfgk gicgqvavsg etfvvpdvys qdnylscsid tkseivvpif kdgknigqid
      121 idshtidpft dedtellewl cgevakvl
//
LOCUS       WP_009092538             371 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Pantoea].
ACCESSION   WP_009092538
VERSION     WP_009092538.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 371)
  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 371)
  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
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 371)
  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   5  (residues 1 to 371)
  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   6  (residues 1 to 371)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 371)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 371)
  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 20682457
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..371
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39847
     Region          9..49
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          75..358
                     /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 mtapnvtari lrlivenapi sqsdlkvrsg lsmstvsqat nrlltqeivq elglrrvsmg
       61 rpktllglnp drasvigiql naernlivmt dlsgnllgeq qmpkgtltpr qlgdalakfl
      121 rgveekrvga iglalsglvd aengycirsk vlgwdnvpia rlleerfslp vfiendanam
      181 amaalvfgql gnaqsaviat ygkgigagii lnrqlyrgrh gkageigngl vgdgslrlle
      241 dvassrailq rvaeqdaegv tlqaldqrpt pevlaaleea grelgislan lsvaydpdvv
      301 ylamephmas rilldhitqs fqayrlkltp qmtplqflte snrmwalgaa gfavnrlldl
      361 laaqadeepv t
//
LOCUS       WP_009095298             407 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Halomonas sp. GFAJ-1].
ACCESSION   WP_009095298
VERSION     WP_009095298.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. GFAJ-1
  ORGANISM  Halomonas sp. GFAJ-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Halomonas sp. GFAJ-1"
                     /db_xref="taxon:1118153"
     Protein         1..407
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43711
     Region          1..396
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mqimvinsgs ssikfglyla hneapltlda ltlkveghfs gigsrgreav hlndaqgndl
       61 slnglapsts hgealsslma wleadkngsi avighrvvhg grdyqapikv taehldvlgg
      121 lnslaplhqp hglapimhlm qrypevaqia cfdtafhaeq pnvarhfalp reltqkglir
      181 ygfhglsydy isrvldnylp eeaskkrviv ahlgngaslc alqnkrsvas tmgftalegl
      241 pmgtrsgsvd pglvlhliqq egmtpeevet mlykrsgllg vsgisgdvre llesdapeae
      301 ealslyayri areigslaaa lggldqlift agvgenaayv reqvvrqcaw lgialdsdan
      361 dsnahcispa dspvgawvip tdearmmawy caqfmrqyst qstaqee
//
LOCUS       WP_009095588             385 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Rhodopirellula sp. SWK7].
ACCESSION   WP_009095588
VERSION     WP_009095588.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula sp. SWK7
  ORGANISM  Rhodopirellula sp. SWK7
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Rhodopirellula sp. SWK7"
                     /db_xref="taxon:595460"
     Protein         1..385
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=40763
     Region          1..382
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mnilvfnvgs ttlkyacvkv stgerlyegl vdrigqvggd apdhlsaarc vleqvgllpg
       61 mqtpkdmpkl saiahrivqg gdsyptpavv naevlaqlet ldtlaplhnp sarsvvvaih
      121 slgvplpqvl vfdtayfstl kpaayryaip epiyrahrvr kygfhgtshr fvtqlaierl
      181 eiespariis lhlgggasvt asidgaavdt smgmtplegl vmatrcgdid psvplhlirs
      241 agmsvndvdr llnkesglvg lcgeadmrai lsrreagdca aelaidiyvr riqkviggyi
      301 ailggldali ftagvgehav kirelvtgpl ahlgividpd anesppmrds vaeishpsaa
      361 vrtlvvatne elaiaresaq llmda
//
LOCUS       WP_009096774             260 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Halomonas sp. GFAJ-1].
ACCESSION   WP_009096774
VERSION     WP_009096774.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. GFAJ-1
  ORGANISM  Halomonas sp. GFAJ-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 260)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Halomonas sp. GFAJ-1"
                     /db_xref="taxon:1118153"
     Protein         1..260
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=29018
     Region          21..238
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mancarvngt ckrcegelpf eftmafqpiv dvslakvvty ealvrginge sawsvisqvt
       61 demlyrfdqa crvkaiemas alnmqtdlsi nflpnavyep eaciqatlev servgwpthr
      121 lifeitetek vrdrqhlrni idayrsmgfk talddfgngy anldlltdlt pdklkidrel
      181 vmncdqdprr qallnaiill akeldttlia egvetraeal wlakagitrq qgfffakpai
      241 nslghhltpl llalraevqa
//
LOCUS       WP_009097958             137 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Halomonas sp. GFAJ-1].
ACCESSION   WP_009097958
VERSION     WP_009097958.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. GFAJ-1
  ORGANISM  Halomonas sp. GFAJ-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Halomonas sp. GFAJ-1"
                     /db_xref="taxon:1118153"
     Protein         1..137
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14939
     Region          13..137
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mlylfiryag hqrknhknhq rgftliemli tvaiisiiag igypsymryv esslrtdgka
       61 gllqaasele rcysrqytyt dctitptspd gnytisadsg svndggflit atasrsdgca
      121 sditlnalge rlpeacw
//
LOCUS       WP_009099319             111 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Halomonadaceae].
ACCESSION   WP_009099319
VERSION     WP_009099319.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 111)
  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   3  (residues 1 to 111)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 111)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..111
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11910
     Region          2..111
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 maaqkalslt lpdvptllsa ympfldrggi fvptktpyal gqevfllltl pgeserlsvt
       61 gkviwvspeg vsgrripgig vhfsqqdysv rdrietllag qldkappsft l
//
LOCUS       WP_009101537             444 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Rhodopirellula sp. SWK7].
ACCESSION   WP_009101537
VERSION     WP_009101537.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula sp. SWK7
  ORGANISM  Rhodopirellula sp. SWK7
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 444)
  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 18888537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Rhodopirellula sp. SWK7"
                     /db_xref="taxon:595460"
     Protein         1..444
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=47326
     Region          280..322
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
     Region          329..443
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mqtlktsaiv vlmmtvlyga yvsmttppdp lpqgvesllv esgmdslpdd fgsfgiddgt
       61 ptafddfsms apanesepsl dnangpsssf nsvdqtfadl etnldssdnq fpnesfqmsd
      121 ldtprgvsrl pdvdesatav tisadpgrdy pttgadfslp dpneairmte nsvtsisdsq
      181 tsatdslgyl dvpstpnqts alpsaksaas dvaaaglana iatadrqfna drrrealatl
      241 slfyetpnls sdqreqllvr ldplardviy spehlleeph rvgsnetlmd iaqkydvpwq
      301 llaningvsd pvtvlpgtdl kvvrgpfrad vdlenkeltl flgdlyagrf pvgigndpap
      361 rpgtytiqek ksaktyydma gtpippgspr npygsmwidl gqgislhgsp ktdsatnegc
      421 isiagnysrd vfgilsegss vtir
//
LOCUS       WP_009103371             129 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyl carrier protein [Pirellulaceae].
ACCESSION   WP_009103371
VERSION     WP_009103371.1
KEYWORDS    RefSeq.
SOURCE      Pirellulaceae
  ORGANISM  Pirellulaceae
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales.
REFERENCE   1  (residues 1 to 129)
  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 129)
  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 129)
  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   4  (residues 1 to 129)
  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 10011594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Pirellulaceae"
                     /db_xref="taxon:2691357"
     Protein         1..129
                     /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=14103
     Region          5..80
                     /region_name="acpP"
                     /note="acyl carrier protein; Provisional; PRK00982"
                     /db_xref="CDD:179197"
ORIGIN      
        1 mslsqdeife kvqaalvdal gvdedeatrd atlvgdlgae sidfldivfk leksfdiqip
       61 reelspedil tnsqyvqdgv vtadgmtelk trmpwadlsk feenprvqdf gnlltvgdlc
      121 syvgskvna
//
LOCUS       WP_009105031             389 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Rhodopirellula sp.
            SWK7].
ACCESSION   WP_009105031
VERSION     WP_009105031.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula sp. SWK7
  ORGANISM  Rhodopirellula sp. SWK7
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 389)
  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 389)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Rhodopirellula sp. SWK7"
                     /db_xref="taxon:595460"
     Protein         1..389
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=42845
     Region          40..87
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mnrqqdlftd lprgeqlaal rrlklsthea asgrvsgavq kavlkaiddh egdrasfasq
       61 ktiaeetgyg vstvrraiaa lvdrdlitrd rpnhwspnhh rvnwtevtrr srqdgerpmv
      121 qgersraqsg tcessgrhpr eftevspsvq gdprnahrnd qlnapstatp dewvrlrrrl
      181 sdlgmkaatq ataaarergl sieyiedlit aatkpsgpep pagvgwlchw ltgksappfd
      241 eaeserrrae reakaateae sirervhgdp kaidadpwvi hgiafrklaa agldrfatda
      301 erdgaatmda vdrqrgdnpp epekqtpvfd ahgaarqgvt vepsnqqsvt qsdsrddrqf
      361 gnvfrrvplg krgnravaqr raeildaln
//
LOCUS       WP_009111896             206 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Brenneria].
ACCESSION   WP_009111896
VERSION     WP_009111896.1
KEYWORDS    RefSeq.
SOURCE      Brenneria
  ORGANISM  Brenneria
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
REFERENCE   1  (residues 1 to 206)
  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 206)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 206)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Brenneria"
                     /db_xref="taxon:71655"
     Protein         1..206
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22267
     Region          1..204
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Region          88..116
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(89,92..93,96..97,99,126,129..130,133..134,136..137,
                     159,162..163,166..167,170)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          124..153
                     /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"
ORIGIN      
        1 mevytteneq vdalrrflae ngkalvvgvv lgvgalvgwr fwlnhqsnsa measvsyqqi
       61 seqlaggkae gvtsaekfaa enknnygala slelarhyae rkdfakaeqq laqarsqtkd
      121 adllavvnlr lariqlqekk tdealktlea iksdgwvala aevrgdalvs kgdnqaarea
      181 ynkglaanpp qalqallrmk lnnlss
//
LOCUS       WP_009112809             419 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Brenneria].
ACCESSION   WP_009112809
VERSION     WP_009112809.1
KEYWORDS    RefSeq.
SOURCE      Brenneria
  ORGANISM  Brenneria
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
REFERENCE   1  (residues 1 to 419)
  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 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   3  (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   4  (residues 1 to 419)
  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 419)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Brenneria"
                     /db_xref="taxon:71655"
     Protein         1..419
                     /product="CmpA/NrtA family 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=45464
     Region          42..293
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 msdsktkdmt vsrrqfllgg aalgggfmlp glmnsawaag sdapekqeir vgfipltdca
       61 svvmaaikgf dkkygitiip skeaswaavr dklvsgelda ahilygqlyg lqmglsgpqs
      121 nmaalmtlnq ngqgitlanq lrdagvtdlg tlqkhiaasp agtytfaqtf ptgthamwly
      181 ywlacagihp lndvrtvvvp ppqmvmnmki gnmvgccvge pwnqraisdk lgftaaasqd
      241 iwpdhpekvl gtradwvdan pngaraltaa ileasrwida sdenrretag vvagrayint
      301 reetivgrml gryenglgks wqdehamrfy hdgsvnypyl sdgmwfltqh krwglltedp
      361 dylavarkvn ridiykqaaa avgdvplpds emrssvlidg vrwdgsdpag yadsfsvkk
//
LOCUS       WP_009115809             168 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein, partial [Neisseria wadsworthii].
ACCESSION   WP_009115809
VERSION     WP_009115809.1
KEYWORDS    RefSeq.
SOURCE      Neisseria wadsworthii
  ORGANISM  Neisseria wadsworthii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Neisseria wadsworthii"
                     /db_xref="taxon:607711"
     Protein         1..>168
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
     Region          4..168
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mtpffqllqq rvsaygfsds hisepelhyl ikaachapsa yhlqnwhfta vcsekakqal
       61 yhaafrqhki mqaaavivis gkltgyqdln eklqasvqtg iidndtaqnw isaahaafhd
      121 npraqrdeai rsaslaamtl mlaaqeqgwa scpmsgfdte avrqtagl
//
LOCUS       WP_009103373             168 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-hydroxyacyl-ACP dehydratase FabZ family protein
            [Pirellulaceae].
ACCESSION   WP_009103373
VERSION     WP_009103373.1
KEYWORDS    RefSeq.
SOURCE      Pirellulaceae
  ORGANISM  Pirellulaceae
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales.
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 10101294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Pirellulaceae"
                     /db_xref="taxon:2691357"
     Protein         1..168
                     /product="3-hydroxyacyl-ACP dehydratase FabZ family
                     protein"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=18416
     Region          1..124
                     /region_name="FabZ"
                     /note="FabZ is a 17kD beta-hydroxyacyl-acyl carrier
                     protein (ACP) dehydratase that primarily catalyzes the
                     dehydration of beta-hydroxyacyl-ACP to trans-2-acyl-ACP,
                     the third step in the elongation phase of the bacterial/
                     plastid, type II, fatty-acid...; cd01288"
                     /db_xref="CDD:238615"
ORIGIN      
        1 mrwfwvdrft efvsgshasg iknvaldeev ldgyslgfpv lpptliiegl aqvggilvhe
       61 hfqftkrvvl akvgtvkyha pakpgdtlny hvrlgrtqgl gaivsgtshc ngelqaevdl
      121 mfafleeghl vdgplfnpgd lramlrlmnf fhvavtaegk pipyyknl
//
LOCUS       WP_009116449             592 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Neisseria wadsworthii].
ACCESSION   WP_009116449
VERSION     WP_009116449.1
KEYWORDS    RefSeq.
SOURCE      Neisseria wadsworthii
  ORGANISM  Neisseria wadsworthii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 592)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Neisseria wadsworthii"
                     /db_xref="taxon:607711"
     Protein         1..592
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62377
     Region          <57..190
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          104..353
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          318..542
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mdnnvlnvlp edqlvvedta tgqenpftnn npaqntpids qpdavdtqip vnvpvsgnpq
       61 tpaddtqpta pnhpddtfat sdapidpvad dnsdvekpvt dvpavtdvpa nddeqnptap
      121 apvdpqtsnd vptgdngtqn padqepanvp ntatpdnatn dpaqndvtti nisapvddpn
      181 tpdqnapssa edgvenkpat dngcgdhpcd kkwvdnngtg ekiiitgtdq ndiihgtard
      241 edisgragdd klysgpgddv ldgeagndsm ygchgddvyy vdsegdkvie fanqgndhvf
      301 ssisytlpen venvhlmtdd dlnavgneld nvlhgndgkn dlsggagndn myghagddil
      361 dgesgadfmv ggegddiyyv dqagdtvvec adegidtvlt sisytagdhv enltllgddd
      421 lnltgnelnn llhgndgnni llggdgcdqi fahdgndild ggtgndllng gsgfdtylfg
      481 rgygndtivd ydqseisndr isfgrgisad dlelsrsggd lviglkdsdd tltisqwfdd
      541 adyqieeflf nngdawsyeq iqeatqalyt tvsansqldd iqqqaqtags gl
//
LOCUS       WP_009116920             217 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Neisseria
            wadsworthii].
ACCESSION   WP_009116920
VERSION     WP_009116920.1
KEYWORDS    RefSeq.
SOURCE      Neisseria wadsworthii
  ORGANISM  Neisseria wadsworthii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Neisseria wadsworthii"
                     /db_xref="taxon:607711"
     Protein         1..217
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=24012
     Region          7..>213
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mlfdfslqkk ftafeldvsl qsdspniaiv gasgsgktlt lnmlagllka dsgyiriqge
       61 qwfdgkrhlp pqerrvglvf qdyalfphlt vaqniafgln rglanpkqkh aqvqaaswle
      121 rmqlshvaah ypseisggqk qrtalarala nrpkllllde pfsaldtdlr gqmrqevgal
      181 areqcvplil ithdtqdaea ladqiwrmea grlmrvn
//
LOCUS       WP_009117364             163 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Neisseria wadsworthii].
ACCESSION   WP_009117364
VERSION     WP_009117364.1
KEYWORDS    RefSeq.
SOURCE      Neisseria wadsworthii
  ORGANISM  Neisseria wadsworthii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Neisseria wadsworthii"
                     /db_xref="taxon:607711"
     Protein         1..163
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17848
     Region          7..158
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mheitfsssd kseiyqellp qiealidgep nfianlanit avlksafdwl wvgfylvdnd
       61 nlvlgpfqgp pactriahgr gvcgqswaqa qtiivpdvnq hldhiacssl sqseivvpvf
      121 nqagqvaavl dvdaeetnqf dqtdaeflqk ichlisrqhf ska
//
LOCUS       WP_009117675              98 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Neisseria wadsworthii].
ACCESSION   WP_009117675
VERSION     WP_009117675.1
KEYWORDS    RefSeq.
SOURCE      Neisseria wadsworthii
  ORGANISM  Neisseria wadsworthii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 98)
  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   2  (residues 1 to 98)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Neisseria wadsworthii"
                     /db_xref="taxon:607711"
     Protein         1..98
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9960
     Region          19..80
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkklmlgala alscawslaa vnintataee lkalpgigpa kaaaiveyrq angafksvee
       61 lkkvkgigdg ifnklkeeat vsgaakakaa kplqpkak
//
LOCUS       WP_009118280             121 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Neisseria shayeganii].
ACCESSION   WP_009118280
VERSION     WP_009118280.1
KEYWORDS    RefSeq.
SOURCE      Neisseria shayeganii
  ORGANISM  Neisseria shayeganii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Neisseria shayeganii"
                     /db_xref="taxon:607712"
     Protein         1..121
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13672
     Region          13..103
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mhaaletltl speqleiirq ilhrhvpqya vwafgsrtkg takpysdldl avittreplp
       61 lsvhadltda fsesdlpwkv dladwqllse afrteiakhy vvlqkadktn rlpenprppk
      121 h
//
LOCUS       WP_009119050             156 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Neisseria shayeganii].
ACCESSION   WP_009119050
VERSION     WP_009119050.1
KEYWORDS    RefSeq.
SOURCE      Neisseria shayeganii
  ORGANISM  Neisseria shayeganii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Neisseria shayeganii"
                     /db_xref="taxon:607712"
     Protein         1..156
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=17366
     Region          1..108
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mnglsfsrks gftltellit iavlailaai aypsyqsfvr ksrleeanaa llensrfmer
       61 fysrqrsfka nsttwpalpv tqtghfcikf qgnargvlgd kytikavafd pqyeprvlli
      121 nqdqsvrvce ssrsrcdsrd tfsggsgidr nctllh
//
LOCUS       WP_009120084             337 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Neisseria shayeganii].
ACCESSION   WP_009120084
VERSION     WP_009120084.1
KEYWORDS    RefSeq.
SOURCE      Neisseria shayeganii
  ORGANISM  Neisseria shayeganii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 337)
  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 337)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Neisseria shayeganii"
                     /db_xref="taxon:607712"
     Protein         1..337
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37037
     Region          89..334
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          259..334
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mpdwhclads qahlpagygs gqptsasale glaellgegp qaaqlrsava ayqaqnplyr
       61 elnyisrdle eycflqcvaa gdaaewgcrl grhlhfsyyg llgylmllsa dlgtalatal
      121 qfplqlgsyf girllhcpds gqaqlrfehy rgrpelfrfh lrlcaeayrq iiatlgvvdg
      181 gafatqyrdq ggeadalcfs aellalplpy aqssvfaqtl rqccaleqqi gallmqplvl
      241 kvrtlmagdl krysampava aelhmtertl hrhlrkcgta fqtllddirl heavallhdr
      301 qhnlaqiada lgfadpaafk hafkrwtgss patwygr
//
LOCUS       WP_009120653             402 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Bacteroides].
ACCESSION   WP_009120653
VERSION     WP_009120653.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 402)
  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 402)
  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
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 402)
  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   5  (residues 1 to 402)
  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   6  (residues 1 to 402)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 402)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 402)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..402
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44542
     Region          19..61
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          81..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 mrqqllkeie lgsksalvkk riithyiyng sstitdlske ldlsiptvtk fisemcedgy
       61 indygklets ggrhpslygl npesgyfigv dikkfavnig linfkgdmme lkmnipykfe
      121 ntpeameelc rlissfikkt kvntekilni ninisgrvnp esgysfsqfn fserplaevl
      181 tdkigcqvci dndtramtyg eylqgcvkge kniifvnisw glgigiiidg kiytgksgfs
      241 gefghinvfd neilchcgkk gcleteasgs aiyrilqeri kkgecsilsg rannqelplt
      301 ldeiisavnk edllcieive eigqklgkqi aglinifnpe lviiggtlsl tddyiaqpik
      361 tairkyslnl vnqdsvitvs klkdragivg acmlarsrmf ey
//
LOCUS       WP_009121763             496 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Bacteroides clarus].
ACCESSION   WP_009121763
VERSION     WP_009121763.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides clarus
  ORGANISM  Bacteroides clarus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Bacteroides clarus"
                     /db_xref="taxon:626929"
     Protein         1..496
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54292
     Region          4..496
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 metkylkinp adnvavaiva lpageklivd gkeivlnedv paghkfalqd faegenviky
       61 gypigharta kkqgdwmnen niktnlagll eytynptevn ldiphknltf kgyrrkngdv
      121 gvrneiwiip tvgcvngiin qlaeglrret egkgvdaima fphnygcsql gddhentkki
      181 lrdmvlhpna gavlvvglgc ennqpdvfre flgeydsdrv kfmvtqkvgd eyeegmkllr
      241 elyekaskde rvdvplselr vglkcggsdg fsgitanpll gmfsdfliaq ggtsvltevp
      301 emfgaetilm nrcrnkelfe etvklindfk eyflshgepv genpspgnka ggistledka
      361 lgctqkcgks yvdgvlpyge rlqvkglnll sapgndlvaa talascgchm vlfttgrgtp
      421 fgtyvptmki stnstlaknk pgwidfnagv ilenepmekt cerfidyiir vasgefvnne
      481 kkgykeiaif ktgvtl
//
LOCUS       WP_009124204             337 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Bacteroides fluxus].
ACCESSION   WP_009124204
VERSION     WP_009124204.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fluxus
  ORGANISM  Bacteroides fluxus
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Bacteroides fluxus"
                     /db_xref="taxon:626930"
     Protein         1..337
                     /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=37694
     Region          2..284
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mankknmsie tlrgiaillv vvghvigsdp dggmkidfph plrylyvwid yiqmplftai
       61 sgwvyalkpv aapggfstfa rkkalrllvp maavgtlyfm vqyfmpgtng kgefgrlwri
      121 yvfpytiywy lpslflmlva qwwidrckgm etlrqwgvwc tvavllslvn drgfmhglpn
      181 lfsfkgalgq lpyffagvaa crfapyirqa gwkvrsalws galagigliq lvwlssagma
      241 siardlyvvt vlptlflllg mkwynrffsw lggyaysiyl fhgfgtsggr illkmagvgt
      301 ivlvfpaatv fatffpvlad kvmsryrgmr vlllgkr
//
LOCUS       WP_009124216             496 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Bacteroides fluxus].
ACCESSION   WP_009124216
VERSION     WP_009124216.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fluxus
  ORGANISM  Bacteroides fluxus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Bacteroides fluxus"
                     /db_xref="taxon:626930"
     Protein         1..496
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54166
     Region          4..496
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 metkylkinp adnvavaita lpagekltvd gkeivlnedv paghkfalkd faegenviky
       61 gypigharka qkqgdwmnen niktnlagll eytynpvnad ldipkknltf kgyrrkngdv
      121 gvrneiwiip tvgcvngiin qlaeglrret ggkgvdaima yphnygcsql gddhentkki
      181 lrdmvlhpna gavlvvglgc ennqpdvfre flgdydedrv kflvtqkvgd eyeegmqllr
      241 elydkasrdq reevplselr vglkcggsdg fsgitanpll gmfsdflvaq ggtsvltevp
      301 emfgaetilm nrcrnkelfe etvslindfk eyflshgepv genpspgnka ggistledka
      361 lgctqkcgks yvegvlpyge rlkvkglnll sapgndlvaa talascgchi vlfttgrgtp
      421 fgtyvptmki stnstlaknk pgwidfnagv ivenepmekt cerfieyvik vasgefvnne
      481 kkgykeiaif ktgvtl
//
LOCUS       WP_009124850             102 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Bacteroides fluxus].
ACCESSION   WP_009124850
VERSION     WP_009124850.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fluxus
  ORGANISM  Bacteroides fluxus
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Bacteroides fluxus"
                     /db_xref="taxon:626930"
     Protein         1..102
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11383
     Region          1..100
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(6..7,25..26,34,37,39..40,42,45..46,48,56,61,68)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(25,56..57,59,80)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mdkdlfqkev ynvvaaippg rvltygqiay llgkpqysrm vghalrnass glglpchrvv
       61 nsqgrlvpfw eeqrgllese gvkfrgngcv dmkvsqwefm ke
//
LOCUS       WP_009124885             236 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Bacteroides fluxus].
ACCESSION   WP_009124885
VERSION     WP_009124885.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fluxus
  ORGANISM  Bacteroides fluxus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 236)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Bacteroides fluxus"
                     /db_xref="taxon:626930"
     Protein         1..236
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=25831
     Region          55..217
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mqrfilfivl lfvpcslflg gkppvgmaea pgpgamtear acadlyrsmn legivnwkaf
       61 rqavagynki egrkrevltl idfsrpstek rlyvfdmkqr kllfssvvsh gknsgdtyat
      121 sfsneygsyk sslgfyltea tyqgkngysl ilnglekgin drareraivm hgaayanpsv
      181 vskggrlgrs fgcpavpqkl srpiidaikg gsvmyiyaev pdylahsavl kdygql
//
LOCUS       WP_009126093             292 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Bacteroides fluxus].
ACCESSION   WP_009126093
VERSION     WP_009126093.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fluxus
  ORGANISM  Bacteroides fluxus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 292)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Bacteroides fluxus"
                     /db_xref="taxon:626930"
     Protein         1..292
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33905
     Region          213..292
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 metksirnvd isliqhlpmi dfigndfaif ddikdmplsp yptrlnaacf cvclkgwcrm
       61 hinlqkyels egmmgiilpd qivqqggrsd dfsgifiais ksfidgvlpt mqqlfplffl
      121 ikerpcvhit peeqqafkdy hsflwsrvkl kdnpfrkeit qgllvslfye iyhiyqghtt
      181 qeripktrke dlferflryi sesykenrsv syyadkmflt akhlstvvkd vsgktagewi
      241 dslvileaka llksselsvq eiadelhfan qsffgkyfkh htgmspkeyr rq
//
LOCUS       WP_009126749             594 aa            linear   BCT 20-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Bacteroides
            fluxus].
ACCESSION   WP_009126749
VERSION     WP_009126749.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fluxus
  ORGANISM  Bacteroides fluxus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 594)
  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 594)
  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 10478507
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Bacteroides fluxus"
                     /db_xref="taxon:626930"
     Protein         1..594
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=67479
     Region          <22..75
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          <30..242
                     /region_name="PRK06347"
                     /note="1,4-beta-N-acetylmuramoylhydrolase"
                     /db_xref="CDD:180536"
     Region          <75..130
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          <485..543
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
ORIGIN      
        1 mkkinriics lllagacsyg aaqenqsyfl htiekgqsly siasmyginq sdiiklnpgs
       61 dekiyigrtl riprgaante ketfhtieag etlyrltvky nvsakaicda npglsaenfr
      121 igqviripss teavatteas nnksvannsn ipapvqsrcr dmhkvkrket vfsisreygi
      181 seaeliaanp elkgenkikk gsflcipyps aqpqpstqpq diptdselfr enkkkaerfs
      241 tikaaiilpf ldgvpkgesa rmveyyegfl mavdslkrtg tsidlytyns gpetaslngi
      301 lgksemkdmd iifgplyqqh ikplsdfakk ndirlvipft skdntvfrnp svyqintpqs
      361 ylysevydhf vrqfpnanvi fieasqetkd kvefikglkd elrnrsipmk slkedatves
      421 lkavlsadre nifiptsdsn ltlikilpql tllvrdqpes rvhlfgypkw qtytkdhiea
      481 ffeldtyfys sfytnnllpa ainftknyrr wygkdmdery pkygmlgfdt gyfflkglsr
      541 ygsefeknmq glnltpiqtg fkfqrvnnwg gfinkkvffv rftknyelvk ldfd
//
LOCUS       WP_009126463             529 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Bacteroides
            fluxus].
ACCESSION   WP_009126463
VERSION     WP_009126463.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fluxus
  ORGANISM  Bacteroides fluxus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 529)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 529)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 529)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Bacteroides fluxus"
                     /db_xref="taxon:626930"
     Protein         1..529
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=60392
     Region          6..429
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mndlivdvkl wgqsvgslyw ekesnaalfd yerkfirsgl dispvimpvg qyrntpyrfl
       61 enrtdcfkgl pglfadslpd tfgnqiinew faskglsgee itpldrlcyv gkrgmgalef
      121 epsspingmn essvlhieel telaksvftd rmafqaqlrq egrnildilk vgtsaggakp
      181 kaiiayndit gevrsgqvka pegfgywllk fdggkyceht qitdnpqgig nieyayhrma
      241 kacgidmmec rllqekesyh fmtrrfdrme dgekihvqtl aglahydrnq rhsyeeifri
      301 mrqmnlpype qeelyrrmvf nvmsrnhddh sknfsflmdr qgkwklapay dlccsytpgg
      361 kwtnrhqlsl ngkqdnftme dlqkvgenmg irehkqiiek vqetvshwhe takdcgvkpe
      421 hadfigenll lfgkqlytiq mpdiaseqeq afmkamrndd fntilelkmr gyqpsenvlk
      481 slqpdvsatt fiaaakifqm egmlkslqdi kpaqspiigg nkrsvelgd
//
LOCUS       WP_009127137             187 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Bacteroides fluxus].
ACCESSION   WP_009127137
VERSION     WP_009127137.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fluxus
  ORGANISM  Bacteroides fluxus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Bacteroides fluxus"
                     /db_xref="taxon:626930"
     Protein         1..187
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20740
     Region          4..177
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mnetlqtika rrsvrayteq qvsaedlnli leaatyapng mhletwhfta iqnkevleel
       61 ndrikgafak sddphtrerg hsrtyccyyh aptlvivsne parwwagmdc acalenifls
      121 akslgigscw inqlgqtcdd pdvrafltkl gvpenhkvyg caalgyapad apvkekkvke
      181 gtvtiir
//
LOCUS       WP_009127255             110 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Bacteroides oleiciplenus].
ACCESSION   WP_009127255
VERSION     WP_009127255.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides oleiciplenus
  ORGANISM  Bacteroides oleiciplenus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Bacteroides oleiciplenus"
                     /db_xref="taxon:626931"
     Protein         1..110
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12168
     Region          17..102
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mnsilwdkyg lsvangkrit dilsqfaevr eailfgsrak gnykpgsdvd lavkgpiskd
       61 vlsalltafe dsilpyffdv viyehitnka lkehidrvgi siykpfitfs
//
LOCUS       WP_009128339             285 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pantoea sp. GM01].
ACCESSION   WP_009128339
VERSION     WP_009128339.1
KEYWORDS    RefSeq.
SOURCE      Pantoea sp. GM01
  ORGANISM  Pantoea sp. GM01
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 285)
  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 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   3  (residues 1 to 285)
  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   4  (residues 1 to 285)
  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 285)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Pantoea sp. GM01"
                     /db_xref="taxon:1144320"
     Protein         1..285
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32328
     Region          23..272
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <177..272
                     /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 mpanndwvdf rrddetgies vnahfrghay dphdhdellv gvtqqglqrf nchralhtst
       61 pgrailiepg avhdghapda egftyvmlyl pqrwvaemmq rrglgdvsqi egafrhtltd
      121 dallasaiqq awfavhqgeg rlardqsldh lltllsrhld tkpsvqhsea mrqmqllrdy
      181 lhdfmaqdig ldylsrlsgi drfrltrqfk qafgqsphay lvrlrlrsar allaqgiepv
      241 qvaaqvgfad qshlgrwfqr ayrmtpaayq rqctnvlyas lpalr
//
LOCUS       WP_009128808             105 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Bacteroides].
ACCESSION   WP_009128808
VERSION     WP_009128808.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..105
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11693
     Region          1..98
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(6..7,25..26,34,37,39..40,42,45..46,48,56,61,68)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(25,56..57,59,80)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mdqvsfrnev ysvvasipsg rvltygqiay lvgrpqcsrm vgqamhnase ernlpchrvv
       61 nsqgrlapfw peqrelleke gvafrkngcv dlkacgweil kesis
//
LOCUS       WP_009128816              90 aa            linear   BCT 20-JAN-2025
DEFINITION  zinc ribbon domain-containing protein [Bacteroides oleiciplenus].
ACCESSION   WP_009128816
VERSION     WP_009128816.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides oleiciplenus
  ORGANISM  Bacteroides oleiciplenus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 90)
  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 10577258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Bacteroides oleiciplenus"
                     /db_xref="taxon:626931"
     Protein         1..90
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10335
     Region          5..89
                     /region_name="Zn_ribbon_2"
                     /note="Putative zinc ribbon domain; pfam12674"
                     /db_xref="CDD:463667"
ORIGIN      
        1 memkfcqscg mpltsnevcg tnadgslsad yctycyqngk ftqdytmdem iehcaqfvee
       61 fnkdseqkvt keeaiammkq efpklkrwqn
//
LOCUS       WP_009129074             357 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-oxoacyl-ACP synthase III family protein
            [Bacteroides].
ACCESSION   WP_009129074
VERSION     WP_009129074.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 357)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..357
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39402
     Region          8..336
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 maffkidnvk iagisacvpp kqvenidsil iedkkeleky iettgvkrry iaeegicssd
       61 lcleaaerli ekldwekeei eclifvsqtp dyifpatacv lqdrlklssn cmsfditmsc
      121 pgwiyglsai sailsagkik kglllvgets tkakspydrv nllagdagta talefntsas
      181 piifdmhtdg snfksliipd ggyrnpvtke sfeyvmckdd ilrnrlqanm egdsifsfav
      241 ntapkeinal lsklavdkad vdyflihqan qminkfiqkr lkvddskciy nitdfgntss
      301 tsiplmiisk lrekfngkki vcsafgtgla wgtmvmdtst dgvfpeliry agdktdn
//
LOCUS       WP_009130111             158 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Bacteroides oleiciplenus].
ACCESSION   WP_009130111
VERSION     WP_009130111.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides oleiciplenus
  ORGANISM  Bacteroides oleiciplenus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Bacteroides oleiciplenus"
                     /db_xref="taxon:626931"
     Protein         1..158
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17250
     Region          15..150
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdafvdsliq lmidwgylgl fisavlagsi vpfsselvmi alvkvglspt mcvlfatlgn
       61 tiggmtcyym grlgnvvwie kyfkvkkeki dkmqrflqgk galmaffafl pfvgealaia
      121 lgfmrsnvwl ttssmfvgkl iryavmllal egaisvfs
//
LOCUS       WP_009130298             688 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Bacteroides oleiciplenus].
ACCESSION   WP_009130298
VERSION     WP_009130298.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides oleiciplenus
  ORGANISM  Bacteroides oleiciplenus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 688)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Bacteroides oleiciplenus"
                     /db_xref="taxon:626931"
     Protein         1..688
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=74199
     Region          4..688
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mitnqllrpa sivvvgasnn vhkpggailr nlinggytge lravnpkete vqgvtayadv
       61 kdipetelai laipaqmcpd avevlaaekq vrafiilsag fgeethegal ledriletvn
      121 kygasligpn ciglmntwhh svfsqpipql hpqgvdliss sgatavfile savtkglqfn
      181 svwsvgnakq igvedvlqym denfrqeeds kikllyiesi gdpdrllfha sslikkgcki
      241 aaikagsses gsraasshtg aiassdsave alfrkagivr cysreelttv gciftlpelr
      301 gknfaiitha ggpgvmltda lskgglnvpk legpvadelk sklfpgaavg npidilatgt
      361 pdhlrlcley ceekfenida vlaifgtpgl vtmfemydvl hekmqtcskp ifpilpsint
      421 agaevaafla kghvnfadev tlgtalsrim naprpaanei elfgvdvpri rriidsiped
      481 gyiqphyvqa llhaagipiv eefvsankde vlafarrtgf pvvakvvgpv hksdvggvvl
      541 nikgeqhlaf efermmqipe vtgilvqpml kgtelfvgak yeekfghvvl cglggifvev
      601 lkdvssglap lsyeeaysmi hslraykiik gtrgqkgvne dkfaeiivrl stllrfatei
      661 kemdinplla tekhviavda ririekke
//
LOCUS       WP_009133085             136 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Alistipes indistinctus].
ACCESSION   WP_009133085
VERSION     WP_009133085.1
KEYWORDS    RefSeq.
SOURCE      Alistipes indistinctus
  ORGANISM  Alistipes indistinctus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Rikenellaceae; Alistipes.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Alistipes indistinctus"
                     /db_xref="taxon:626932"
     Protein         1..136
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15159
     Region          1..112
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 metqsakrlp afslpellvv lviigilvli alpnlmplis raksteaqqq lvflhtlqkn
       61 nfytyskyss sveelgfeqq plvtdgghan yrieiiease kgfratatav vdfdgdgeyn
      121 vweidqdknl retvkd
//
LOCUS       WP_009135515             279 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Odoribacter laneus].
ACCESSION   WP_009135515
VERSION     WP_009135515.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter laneus
  ORGANISM  Odoribacter laneus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Odoribacter laneus"
                     /db_xref="taxon:626933"
     Protein         1..279
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32273
     Region          6..264
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mdslyartgf disrtitrny stsffsavnl lakdireaif giygfvrlad eivdsftdyd
       61 rqyllnrfeq dyaeaiqqgi stnpvinafe ltvrkyridr hlieaflksm radlshpgys
      121 rksdieeyiy gsasavglmc lrvftgtddv lyeklqqpam klgsafqkvn flrdlrtdle
      181 vldrvyfpel nrqnfnevhk qqiiteiese faeayqgirq lpsnsrlgvf iayryytkll
      241 qkikktpahk lithriripd vskalllsht lllnkinli
//
LOCUS       WP_009136032             399 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Odoribacter laneus].
ACCESSION   WP_009136032
VERSION     WP_009136032.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter laneus
  ORGANISM  Odoribacter laneus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Odoribacter laneus"
                     /db_xref="taxon:626933"
     Protein         1..399
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43489
     Region          1..399
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mnilvlncgs ssikyqllnm eaqpvllakg ivekiglplg ifthkpegke kyilekpipd
       61 hvdgmdlilk altdkkygvi asldeifavg hriahggeyf shsvlideev kakikacsei
      121 aplhnpahlk gietmerllp tipqvavfdt sfhqtlppka fiygipyeyy enysvrrygf
      181 hgtshkfvae kackilgwdi tekkiitchl gngasitaid kgksvdtsmg ftpvaglvmg
      241 trcgdldtga llyicdkkgy tsldavrltn kesgvfgisg vssdfrelts aadagnyrae
      301 laldvfcynv kkyigayaav lngvdliift ggigenderv rnsvctgley lgvefdeavn
      361 lkargvdril stphsktfvm tittdeelvi atdtlnlvk
//
LOCUS       WP_009136163             153 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Odoribacter laneus].
ACCESSION   WP_009136163
VERSION     WP_009136163.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter laneus
  ORGANISM  Odoribacter laneus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Odoribacter laneus"
                     /db_xref="taxon:626933"
     Protein         1..153
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17248
     Region          2..149
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mskklekyer lyeqishyvv ttpdrwarla tieavlhhkm qlffwtgvyv lvegelivrs
       61 yqgpvacqkl rqhtgvcwaa vdsgktvivk nvaefsghia cnpatkseiv lplrdekgqi
      121 ygcldidsdq lgafdeedeq gllkilqlvd kek
//
LOCUS       WP_009137055             316 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Odoribacter laneus].
ACCESSION   WP_009137055
VERSION     WP_009137055.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter laneus
  ORGANISM  Odoribacter laneus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 316)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Odoribacter laneus"
                     /db_xref="taxon:626933"
     Protein         1..316
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34731
     Region          8..316
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mdlyvnkish yipegvvens yfkevnglde ewiysrtgik trskagkeen tntmgikavd
       61 ngvedlpypm esidlivaat yspydtvati ahmvqrryha erakcvsvss acssfiname
      121 vvegyfamgk ahralviase hntayanetd pqsghlwgdg avaffispek yresdaqils
      181 iytqglghig kstsavylrp rnggigmpeg rdvfinachy mvealerage rcgkklsdln
      241 yisshqanqr iirniarqtg fpeecflmni enrgntgcps caislsenlh riqkgdlvgl
      301 tvfgggyscg amllqf
//
LOCUS       WP_009137080             166 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Odoribacter laneus].
ACCESSION   WP_009137080
VERSION     WP_009137080.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter laneus
  ORGANISM  Odoribacter laneus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Odoribacter laneus"
                     /db_xref="taxon:626933"
     Protein         1..166
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=18846
     Region          10..159
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mgldiitlti aellskygyy glfagsflss lflpigadil fvgmlaagin pwgclfiatt
       61 gnwlggliiy yigysgnkek mkrwfhlkee qlekqkkkid kygsllallv wipvvgdvss
      121 valgfyrtkp kltlflmyls rmsrfllwvi lyliyanrfv hfidhl
//
LOCUS       WP_009137261             313 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Odoribacter laneus].
ACCESSION   WP_009137261
VERSION     WP_009137261.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter laneus
  ORGANISM  Odoribacter laneus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (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   2  (residues 1 to 313)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Odoribacter laneus"
                     /db_xref="taxon:626933"
     Protein         1..313
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35999
     Region          220..298
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mnelflsedl wqtfiieenf qrrrmpyadl krnfivgpei kgsllemykn pcrlkagifv
       61 lclqgelkaa ihgnlweirk ndfigimpgs viqyyqqsad lricfvafss svmesmnfqq
      121 ltidfvsvmq enpvlsleek tatwfkdyfh llaranglvk dnlpleivkn ilqsllcgvd
      181 flytshswsk qilsrgeeiy rdvlravrqh yckehsvify anllsispqh lgatvrrvsg
      241 ytfsdilagi vitdakaqlr stefsiqeia yslgfrntsf fgkyfkryvg ispqkyregt
      301 epknerlgaa eny
//
LOCUS       WP_009137775             411 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Odoribacter laneus].
ACCESSION   WP_009137775
VERSION     WP_009137775.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter laneus
  ORGANISM  Odoribacter laneus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 411)
  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 411)
  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
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 411)
  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   5  (residues 1 to 411)
  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   6  (residues 1 to 411)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 411)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 411)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Odoribacter laneus"
                     /db_xref="taxon:626933"
     Protein         1..411
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45443
     Region          22..63
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          82..398
                     /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 mlstnknslp glkekryqqk kdiigflykm gelskpeicr ltnmttptis rmidelieeg
       61 wvtdqgqgms iggkrphifs lnpdaayimg vdvgrehlki aifnlrkeii geikiyrsvl
      121 edektneenl qyiqdkinqt lselnisykk ikvagfaipg lidsdgnsft yfvyedtnik
      181 kvlekmlgip vfidndskvm alaehtfgva kgisdalcis vneciglgmi lnsqpytgyk
      241 gmagefghir isglngqcyc gkvgcletva sgraivrnar eaiqkgtkta iqtlakdeei
      301 tlgmiikaak qddifaidll qkagekigeg istlihlfnp qvlviggema dsgdliiapi
      361 qqilnkytlt rlknqceikl sdlnshstim gtlmlvmknl yydsesnfsl y
//
LOCUS       WP_009139021             257 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Slackia piriformis].
ACCESSION   WP_009139021
VERSION     WP_009139021.1
KEYWORDS    RefSeq.
SOURCE      Slackia piriformis
  ORGANISM  Slackia piriformis
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Slackia.
REFERENCE   1  (residues 1 to 257)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Slackia piriformis"
                     /db_xref="taxon:626934"
     Protein         1..257
                     /product="amidohydrolase family protein"
                     /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=26740
     Region          2..>200
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 marpsskvvf idatvldgtk gmeprphttv vvedgkisdv asngaasqpg darvidlnga
       61 ylmpglvnmh vhfcgsgkpv saggagslmk mldnplgrav lrrivkehar tqlasgvttv
      121 rgagdplfsd iavrddiekg ryigprivap gtgvtvpggh gaglfaqvae spreaaeqvr
      181 dlaargadvv nlfitggvfd avepgsrafs gcrsrlrkrh agpptiracp swrtsrarra
      241 caslwsrgst psstarl
//
LOCUS       WP_009140636             143 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: division/cell wall cluster transcriptional repressor
            MraZ [Collinsella].
ACCESSION   WP_009140636
VERSION     WP_009140636.1
KEYWORDS    RefSeq.
SOURCE      Collinsella
  ORGANISM  Collinsella
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Coriobacteriales; Coriobacteriaceae.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Chen,S., Jancrick,J., Yokota,H., Kim,R. and Kim,S.H.
  TITLE     Crystal structure of a protein associated with cell division from
            Mycoplasma pneumoniae (GI: 13508053): a novel fold with a conserved
            sequence motif
  JOURNAL   Proteins 55 (4), 785-791 (2004)
   PUBMED   15146477
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449500
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Collinsella"
                     /db_xref="taxon:102106"
     Protein         1..143
                     /product="division/cell wall cluster transcriptional
                     repressor MraZ"
                     /GO_function="GO:0000976 - transcription cis-regulatory
                     region 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=16280
     Region          3..128
                     /region_name="MraZ"
                     /note="DNA-binding transcriptional regulator and inhibitor
                     of RsmH methyltransferase activity [Translation, ribosomal
                     structure and biogenesis]; COG2001"
                     /db_xref="CDD:441604"
ORIGIN      
        1 miltgtyern ldakgrlslp aavrdelssh vyvlpapdve alyvfssdey ekwvmglfdk
       61 rggfdprkre dqalmrkins matpmdidsa srigltealr ekkhltrevt vvgnfdhlei
      121 wdravweqtq qaddddladl fys
//
LOCUS       WP_009140658             389 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Collinsella tanakaei].
ACCESSION   WP_009140658
VERSION     WP_009140658.1
KEYWORDS    RefSeq.
SOURCE      Collinsella tanakaei
  ORGANISM  Collinsella tanakaei
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Coriobacteriales; Coriobacteriaceae; Collinsella.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 389)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Collinsella tanakaei"
                     /db_xref="taxon:626935"
     Protein         1..389
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42175
     Region          1..389
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mnvlvvnags sslkyqllnt qsgevfakgn cerigidgsf igheekgagk stlevalpdh
       61 rtaikhvfei letvdapveg ighrvvqggw yfpesavvtd etlaqvreva plaplhnyae
      121 advieicrdm fpelgnvivp dtafhynmpe rawryalprd vvekhhvrky gahgtshrfi
      181 wrtvnefmeg kahklvschl gsgaslcaie dghcmdttmg ltpldglvmg trcgtldpat
      241 vfylsrvggy sideidtmmn kqsgllavsg vssdsrdvce gadkgdence malemfsyrv
      301 gqlfaemaas mggvdtmaft agigensvel rqrvadklaw lgveidpeln avrsddprvi
      361 stpnskitcl vvptneelmi aldveallg
//
LOCUS       WP_009141433             405 aa            linear   BCT 20-JAN-2025
DEFINITION  galactokinase [Collinsella tanakaei].
ACCESSION   WP_009141433
VERSION     WP_009141433.1
KEYWORDS    RefSeq.
SOURCE      Collinsella tanakaei
  ORGANISM  Collinsella tanakaei
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Coriobacteriales; Coriobacteriaceae; Collinsella.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   McAuley,M., Kristiansson,H., Huang,M., Pey,A.L. and Timson,D.J.
  TITLE     Galactokinase promiscuity: a question of flexibility?
  JOURNAL   Biochem Soc Trans 44 (1), 116-122 (2016)
   PUBMED   26862196
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Holden,H.M., Thoden,J.B., Timson,D.J. and Reece,R.J.
  TITLE     Galactokinase: structure, function and role in type II galactosemia
  JOURNAL   Cell Mol Life Sci 61 (19-20), 2471-2484 (2004)
   PUBMED   15526155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Collinsella tanakaei"
                     /db_xref="taxon:626935"
     Protein         1..405
                     /product="galactokinase"
                     /EC_number="2.7.1.6"
                     /GO_function="GO:0004335 - galactokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0005534 - galactose binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0046835 - carbohydrate phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=43070
     Region          9..389
                     /region_name="GalK"
                     /note="Galactokinase [Carbohydrate transport and
                     metabolism]; COG0153"
                     /db_xref="CDD:439923"
ORIGIN      
        1 mpatnnqaal aaarelfekt fgeissnakv lavhapgrse isgnhtdheg ghviagaldv
       61 avdgvavang tnvvrvidan fplvevdlsd lsvrederet taalvrgmaf elaqtgrtpa
      121 gfdfasvcsv paggglsssa aveaaygram ealwegpsid pvelakmsqf aenryfgkpc
      181 glmdqaavcl gglaymdfev psepktakld fdfdkagyal clvkvgsdht dltfeyaaip
      241 demqaiagef gckrlcevdp avfdaavpql rekygdravl raihywyeng lvdkrwedlv
      301 agdiesflvh trasgassam flqnvsatvg dvreqhamla lglaerildg rgaarihggg
      361 fggsiqcfvp ldlvdefiar mdawlgegsc rkysiteega catwm
//
LOCUS       WP_009142142             284 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Collinsella tanakaei].
ACCESSION   WP_009142142
VERSION     WP_009142142.1
KEYWORDS    RefSeq.
SOURCE      Collinsella tanakaei
  ORGANISM  Collinsella tanakaei
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Coriobacteriales; Coriobacteriaceae; Collinsella.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 284)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 284)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Collinsella tanakaei"
                     /db_xref="taxon:626935"
     Protein         1..284
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31152
     Region          25..102
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..281
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mtqlenlnra lavieasleg dvdyeaaara agcsryqler mfpylanvsl aeyvrrrkmt
       61 raasdlldrd arvidvalry gydsptafar afkrvhgvsp seaksegvkl asyprlvftl
      121 svkgeepmdy kivempafrv vgvpstgewe ledagekavq ywvdvepqvd allglsdgep
      181 agllgvqfcr dgafdgymac vatqapcpdg mavrvvpaat yavfectgdv stamgelwhr
      241 vlsewlpssg fswesgsdve rylsrdmhaa dsrselwlpv vrae
//
LOCUS       WP_009142262             102 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Succinatimonas hippei].
ACCESSION   WP_009142262
VERSION     WP_009142262.1
KEYWORDS    RefSeq.
SOURCE      Succinatimonas hippei
  ORGANISM  Succinatimonas hippei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Succinivibrionaceae; Succinatimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Succinatimonas hippei"
                     /db_xref="taxon:626938"
     Protein         1..102
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11538
     Region          12..100
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(28,59..60,62,83)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(28..29,37,40,42..43,45,48..49,51,59,64,70)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mskvltqtli yeilsvveei pegkvatygq iakligrdrn arlvgfvlsk veyygrypch
       61 rvvnhqgrta pmwseqrsll eqegvvfksd gkvdldkclw kv
//
LOCUS       WP_009143886             281 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Succinatimonas hippei].
ACCESSION   WP_009143886
VERSION     WP_009143886.1
KEYWORDS    RefSeq.
SOURCE      Succinatimonas hippei
  ORGANISM  Succinatimonas hippei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Succinivibrionaceae; Succinatimonas.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Succinatimonas hippei"
                     /db_xref="taxon:626938"
     Protein         1..281
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30684
     Region          1..272
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 msfidlhcht nasdgalspe gvvdravnyk lthlaitdhd tvngikaaqa aacgricvip
       61 gieisttwqh qqihivglfi npecsymlnl vkeqngkrie raekigykls rigfpnayer
      121 tkamagdgai itrgnyarfl vsvggasstd dafnaflkkg krayvctewm eigtaveaik
      181 qsggvavlah prrydltntk lrklieefkd cggialevss cqqglndrdy laslcrqydm
      241 lgsvgsdfhs egpyrdigrn idlpegitpv wtcseakaya f
//
LOCUS       WP_009143939             261 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Succinatimonas hippei].
ACCESSION   WP_009143939
VERSION     WP_009143939.1
KEYWORDS    RefSeq.
SOURCE      Succinatimonas hippei
  ORGANISM  Succinatimonas hippei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Succinivibrionaceae; Succinatimonas.
REFERENCE   1  (residues 1 to 261)
  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 261)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Succinatimonas hippei"
                     /db_xref="taxon:626938"
     Protein         1..261
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28747
     Region          1..259
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mfkvasnltm mfkevefsqr fekaaksgfs avemlwpyel akadlkklld dnglklalfn
       61 tkggdtangq wgraaipggf ndakedidla ldyavfagck tvhvmsavvk dftkeaayda
      121 laksveyaaa qakphgitvt lealcpevkp dylyksqyet lafvnkvnld nvkvqfdfyh
      181 aqmvdggitk flkdniakvg hvqiasvpdr hefdhgeldg ayclkllndl nyegfvgcey
      241 npqgiteegl tflspylkkp a
//
LOCUS       WP_009144082             294 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Succinatimonas hippei].
ACCESSION   WP_009144082
VERSION     WP_009144082.1
KEYWORDS    RefSeq.
SOURCE      Succinatimonas hippei
  ORGANISM  Succinatimonas hippei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Succinivibrionaceae; Succinatimonas.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 294)
  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 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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Succinatimonas hippei"
                     /db_xref="taxon:626938"
     Protein         1..294
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33555
     Region          27..176
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          206..286
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtsnlytdlk qqilnialcd gvydigisdl kickrsktsn lkkcfydami lfmvqgekqt
       61 vvnhnkfqyh egqcivtgva mpslsavtra dsnhpmlcig ldfndslmle vlnsienhyl
      121 dnslpsdifv idasetlada flrllklrne dpfsrnflsq niikeiyfri iisplgnflr
      181 hfykegtpsn qiakaikflk dhfkeeinin dlsdkihmsp saffrnfskv tgttplqyqk
      241 qlrlyeaqri llqqdintqk aaflvgyksa nqfcrdykkl fgnppktnik llsa
//
LOCUS       WP_009146524             203 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Thiorhodovibrio frisius].
ACCESSION   WP_009146524
VERSION     WP_009146524.1
KEYWORDS    RefSeq.
SOURCE      Thiorhodovibrio frisius
  ORGANISM  Thiorhodovibrio frisius
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiorhodovibrio.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Thiorhodovibrio frisius"
                     /db_xref="taxon:631362"
     Protein         1..203
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=22383
     Region          12..202
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 msasqdaila ltrqqgllrp idldaqglpr vsltrlvrqg rlarvgrgly alperpvseh
       61 aalaevarrs phavicllsa lrfhelttqn pfevwlaipg kahapalsyp plrvvrfsea
      121 gmtegvdqhe idrvrvrvtn lartvadcfk yrnkigldva lealkealgq dggprrvsid
      181 alwrfaemnr vgkvirpyld sla
//
LOCUS       WP_009148018             623 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Thiorhodovibrio frisius].
ACCESSION   WP_009148018
VERSION     WP_009148018.1
KEYWORDS    RefSeq.
SOURCE      Thiorhodovibrio frisius
  ORGANISM  Thiorhodovibrio frisius
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiorhodovibrio.
REFERENCE   1  (residues 1 to 623)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..623
                     /organism="Thiorhodovibrio frisius"
                     /db_xref="taxon:631362"
     Protein         1..623
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=70895
     Region          63..585
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mdklkmhspd ltqnniaklr elfpgcvtea rgedgqlrla vdfdllrqel sdelvegpqe
       61 ryhldwpgkr ealfiasapi aktlrpclde senfftaknl fiegdnleal kllqetylgk
      121 vkmiyidppy ntgsefiydd nfiennrqyl aksnqtdnsg srlvantetn grfhsdwltm
      181 iyprlklarn llsydgvifi siddgevasl qkicseifge enfvgniiwq srtsisndqe
      241 islnhnhtlv yardreqlvf fgepldpndy enpdndtrgp wklvpidank pggdtqypir
      301 npktgeefwp pngrswamnp reyerlfldg rikfgktdds apkkklfyhe rikkgdtktp
      361 ssilldagtt kdgttemmel fdgkkifdyp kptsfmerll nfgcykdrns ivldffagsc
      421 slahaclktn nvsfitvqia epvdeskpsg knaikfglnv iadigkerlr ralrklqtvn
      481 destpersgf rvlkvdtsnm advyytpdqt dqrdllgqva nikpdrtped llfqvlvdwg
      541 vdltlpiree tvqgrrvffv neppydllac fddnvteelv kqlathqplr avfrdtgyat
      601 datrtnvvqi frqlspgtev ksl
//
LOCUS       WP_009148692             147 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Thiorhodovibrio frisius].
ACCESSION   WP_009148692
VERSION     WP_009148692.1
KEYWORDS    RefSeq.
SOURCE      Thiorhodovibrio frisius
  ORGANISM  Thiorhodovibrio frisius
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiorhodovibrio.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Thiorhodovibrio frisius"
                     /db_xref="taxon:631362"
     Protein         1..147
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16082
     Region          4..140
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdvylglfav sfvaatllpa ysevvfaglq aaghdpwalw awatagntlg aalnwvigrw
       61 llrfqdrqwf pfkgaglkta qrwfqrwgvw slllawapvg gdaltfvagl mrvrfpvfll
      121 ltatgkglry avllglvgig rqlwsss
//
LOCUS       WP_009149283              86 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Moorena].
ACCESSION   WP_009149283
VERSION     WP_009149283.1
KEYWORDS    RefSeq.
SOURCE      Moorena
  ORGANISM  Moorena
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Coleofasciculales; Coleofasciculaceae.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 86)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 86)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 86)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Moorena"
                     /db_xref="taxon:1155738"
     Protein         1..86
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=9362
     Region          7..86
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 msepsitvtv klfaayqety glpelqlgfp pqtsvsavld rllsehpele qwrevtrfgi
       61 nlqfvppdtp lqdgdevvli ppvsgg
//
LOCUS       WP_009150403             118 aa            linear   BCT 20-JAN-2025
DEFINITION  PilZ domain-containing protein [Thiorhodovibrio frisius].
ACCESSION   WP_009150403
VERSION     WP_009150403.1
KEYWORDS    RefSeq.
SOURCE      Thiorhodovibrio frisius
  ORGANISM  Thiorhodovibrio frisius
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiorhodovibrio.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (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   3  (residues 1 to 118)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 118)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Thiorhodovibrio frisius"
                     /db_xref="taxon:631362"
     Protein         1..118
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13094
     Region          4..118
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 megekksgrq rilsfaikdk nalyayympf vkngglfipt tkryqlgdel flllqlmqes
       61 eripvageii witpvgaegn raagvgiqfs dqdkgiarrk ieeylagale sdrgthtm
//
LOCUS       WP_009150490             237 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Thiorhodovibrio frisius].
ACCESSION   WP_009150490
VERSION     WP_009150490.1
KEYWORDS    RefSeq.
SOURCE      Thiorhodovibrio frisius
  ORGANISM  Thiorhodovibrio frisius
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiorhodovibrio.
REFERENCE   1  (residues 1 to 237)
  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 237)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 237)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Thiorhodovibrio frisius"
                     /db_xref="taxon:631362"
     Protein         1..237
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=24937
     Region          1..231
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 mvelqtdeek aeaikkwwke nglavvsgva iglaiifgwr awmsyqdqlg qqaslafeel
       61 mvtvnqvslm apapadadpa ssdsesasde lsalltvase qqarlnedfg stayayfgql
      121 alakahsdqg qleaaaealr galdqaptal lktlaglrla rvliaaqdya aagavidqhe
      181 qdnsfaadfa alrgdiavae driedaraay rqalegdvaa aglielklqd lptstgs
//
LOCUS       WP_009151600             338 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Thiorhodovibrio frisius].
ACCESSION   WP_009151600
VERSION     WP_009151600.1
KEYWORDS    RefSeq.
SOURCE      Thiorhodovibrio frisius
  ORGANISM  Thiorhodovibrio frisius
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiorhodovibrio.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  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   4  (residues 1 to 338)
  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 338)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Thiorhodovibrio frisius"
                     /db_xref="taxon:631362"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36811
     Region          22..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          254..334
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mhipvvraqh vidnigvlrd agvpierele rsrlpafieq tpdayvslpr aldwawrssr
       61 elgimevgfl agratslsrl hpavqravig aptglsriea lshqvhrens alqidirreg
      121 vdrrvlcevr gfqnspfvgf aewkaivgvi nivrsaagsd wcpteitfvs rgrpshaare
      181 aygnariltg qqhcsilvaa adiaqicigr rssavdvngp tspprtpfgl gdawdfvtav
      241 ralirpylaq ghpplslvae ivgmserslq rrlakcgaty sdivqdarfa iasdllvdsd
      301 lniadiafaa gyenaphfsr afkrltgmtp rdyrgalv
//
LOCUS       WP_009151742             650 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Saccharomonospora
            marina].
ACCESSION   WP_009151742
VERSION     WP_009151742.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora marina
  ORGANISM  Saccharomonospora marina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 650)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 650)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..650
                     /organism="Saccharomonospora marina"
                     /db_xref="taxon:632569"
     Protein         1..650
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=70018
     Region          36..600
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mttrtrrgqr rpntrpaahh raaaftpdal svgarhlevg newvssfavt gfprevhpgw
       61 laplltypgr ldvalhvepi dpataaarlk kqlaklesgr rhtaehgrlh dpqveaated
      121 aydlssrvar gegklfrvgl yltihapser aladevaalr slaaslllda khttyrslqg
      181 wvstlpmgld ligmrrtfdt salsaafpft spdlpaadpt svaapsgvly gynvgsqglv
      241 hwdrfgegmh nhnsvilgrs gagksylvkl ellrslyrgi eiavvdpede yarlaaavgg
      301 tyvhlgardv rlnpfdlpih tradgrrtap kdalvrrslf lhtviavlvg seleaaeraa
      361 ldrgiaatyq svgitadart wtrpsptlrt lrdqlatagq agdraaaela arlhpfvega
      421 fkqlfdgptt tnpeghlvvf slrdlpdelk aigtlltlda vwrrvsnpai rrprlvvvde
      481 awllmkeksg aeflfrmaka srkhwagltv atqdtadvlg ndlgkavvan aatqvllrqa
      541 sqaideitqt fdlsagerqf llsadrgqgl lsagtqrvaf qsiasptehy lvtsnpaela
      601 gyaadvdpge adaeeqsfvd lgfaseqaya aegdefgsfg adedieldaa
//
LOCUS       WP_009152677              95 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Saccharomonospora marina].
ACCESSION   WP_009152677
VERSION     WP_009152677.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora marina
  ORGANISM  Saccharomonospora marina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Saccharomonospora marina"
                     /db_xref="taxon:632569"
     Protein         1..95
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10367
     Region          1..95
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(5..6,24..25,33,37..38,40,43..44,52,57,62)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(24,52..53,55,77)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mdeelhervr dvvraipsga vatygdvaaa agartprlvg rilsedghdl pwhrvlradg
       61 tpaphlarrq lellraegvl adgqrvslar yrwrg
//
LOCUS       WP_009155987             386 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Saccharomonospora marina].
ACCESSION   WP_009155987
VERSION     WP_009155987.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora marina
  ORGANISM  Saccharomonospora marina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Saccharomonospora marina"
                     /db_xref="taxon:632569"
     Protein         1..386
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41552
     Region          1..270
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          266..352
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrllhtsdwh vgrtfhgtdl laeqesvleh laavvvdeav dvvlvagdvy dravpsaeav
       61 rvagkalsri rdagaqlvit sgnhdsaarl gafadfaaqg glhlrttvaa idrpvlldde
      121 hgpvavygip ylepeparha lgvpqarght gvlteamrrv radlaakpgs trsvvlahaf
      181 vtgaapsese rtiavggveq vpasvfdgvd yvalghlhgp qrvaehlrya gsplaysfse
      241 tarksvwlvd ldadglaevr rrelpvprrl atatgtlehl lraaeyddvv dcylsvtltd
      301 rvrpvdamrr lrerfphavh ldwrpeagta tvlryaeavr grsdieiasg fltdcrgapp
      361 terehallat aleaagkaep rerdre
//
LOCUS       WP_009156327             101 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Saccharomonospora marina].
ACCESSION   WP_009156327
VERSION     WP_009156327.1
KEYWORDS    RefSeq.
SOURCE      Saccharomonospora marina
  ORGANISM  Saccharomonospora marina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharomonospora.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 101)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 101)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Saccharomonospora marina"
                     /db_xref="taxon:632569"
     Protein         1..101
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=10302
     Region          20..101
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mssatsgpts ldegeqhatt vlvryfasar aasgvdselv rlppgasvge avdqlramhp
       61 gelarildaa sflldgmavr dvtrqlpdga eldvlppfag g
//
LOCUS       WP_009157494             250 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Thalassobium sp. R2A62].
ACCESSION   WP_009157494
VERSION     WP_009157494.1
KEYWORDS    RefSeq.
SOURCE      Thalassobium sp. R2A62
  ORGANISM  Thalassobium sp. R2A62
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Thalassobium.
REFERENCE   1  (residues 1 to 250)
  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 250)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Thalassobium sp. R2A62"
                     /db_xref="taxon:633131"
     Protein         1..250
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27442
     Region          1..249
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mphycanltf lfkelpfrer fsaareagfd avevlfpyda daadmgqlla dnrltlalin
       61 cpppnytegp rgfaavpelq drfqydfrrt lryagalgaq rvhimagvad gpearacfve
      121 nlkwaaafap kqqltiepin slampgyfln dfdqaaeild evaapnvslq ldayhahtmt
      181 gdlmvtwaah ghrathiqva gphphraeph sgeidfagff aaldksgfkg wvsgeynpsa
      241 atqdglhwrv
//
LOCUS       WP_009157862             237 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Thalassobium sp. R2A62].
ACCESSION   WP_009157862
VERSION     WP_009157862.1
KEYWORDS    RefSeq.
SOURCE      Thalassobium sp. R2A62
  ORGANISM  Thalassobium sp. R2A62
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Thalassobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Thalassobium sp. R2A62"
                     /db_xref="taxon:633131"
     Protein         1..237
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=25557
     Region          17..161
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mgsapvpfgs kqltlshpsq nfgprrnglr pslivlhyta mndadgacrw lcnpesqvss
       61 hyvvtevgav wslveeadra whagagtwgg lddinsrsig ieisnagthg faaaqmdave
      121 alvagimdrw dipaegvigh sdfapgrkid pggrfdwrrl algglavwse gqqvdpdwdg
      181 fraaavrfgy pvaqddvlla tmrmrfrpwa rgpldavdmg rmcdlaaryp avrgvmv
//
LOCUS       WP_009158514             510 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Thalassobium sp. R2A62].
ACCESSION   WP_009158514
VERSION     WP_009158514.1
KEYWORDS    RefSeq.
SOURCE      Thalassobium sp. R2A62
  ORGANISM  Thalassobium sp. R2A62
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Thalassobium.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Thalassobium sp. R2A62"
                     /db_xref="taxon:633131"
     Protein         1..510
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55674
     Region          <186..366
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 matydgshns nggqihwfgg fvddifeirl nnltsigtyr hdshhiygng ghdvynfrdf
       61 adlgdrtigr ldtfdpsrdv iqiegqaidl yalptvvagi tvevvmfhgq qwlrmqdgde
      121 ksalfalega rlsenaiedt paafrqgaee thfyklskae idalpvvdye npmnfvpleh
      181 yedrendlin vraddvmvta tddaeyihgf kfgtgpdqss qtiyagggdd vvnarsgndi
      241 vyggtgddal gggtgrdtlf geagddalfg gteedilhgg agndllngas dndvldggsg
      301 admmiggsgq dvfqfgaddl ilwsetegtk lermgeldvv mdfvigedli hfdassgvtg
      361 fsdlaiwkav idgnshfsih vkgtgerflv dteddaswkd lvsednflfg dntalitdan
      421 myewndlngd rasknaqlhv vedftlgvdt irflsssgve sfdelkmwkt vlegntyytv
      481 sekgtgerfl idvaddvsws diyiadhfef
//
LOCUS       WP_009159420             276 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Thalassobium sp. R2A62].
ACCESSION   WP_009159420
VERSION     WP_009159420.1
KEYWORDS    RefSeq.
SOURCE      Thalassobium sp. R2A62
  ORGANISM  Thalassobium sp. R2A62
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Thalassobium.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Thalassobium sp. R2A62"
                     /db_xref="taxon:633131"
     Protein         1..276
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27617
     Region          2..233
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mgtdnadtid llagndtydg gkgadiidgg dgidtiqggn gsdlinggdg dddlsggndg
       61 dimnggegnd slqgdigndi lnggagndti eggdgadiis ggadndfifg gggqddidgg
      121 sgndtigggt gadvirgkrg ddvidggdqg dnisggtgnd tiiggkgndt lygnngndvf
      181 vftqggnvdt ikdfelgvdk ldvtdfgtis isdalaalel agsdtiinfg ngdkvilenv
      241 svfdlglddf ifeeliddii vpeepevftv taysyy
//
LOCUS       WP_009160003             259 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Thalassobium sp. R2A62].
ACCESSION   WP_009160003
VERSION     WP_009160003.1
KEYWORDS    RefSeq.
SOURCE      Thalassobium sp. R2A62
  ORGANISM  Thalassobium sp. R2A62
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Thalassobium.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Thalassobium sp. R2A62"
                     /db_xref="taxon:633131"
     Protein         1..259
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26697
     Region          14..236
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 malvvnapvq evigtkvndd iidgfagnsg tvmdtsapea iksnglegdd kivtkdandl
       61 aagdmfgdew tfidgewvyd esavvlsdyg maysyhdviv tgqgndvllg nggndhldag
      121 aggdriiagr gddvafggag ndriylengn dvaegghgdd vinvgagddi vygdnkddnl
      181 lenlssnstt fdglvegggw tmtdkdgqsq isqsastvag etytisfdla anfggghaag
      241 avqvicfevr nvpqdidnn
//
LOCUS       WP_009163606             386 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Pyramidobacter piscolens].
ACCESSION   WP_009163606
VERSION     WP_009163606.1
KEYWORDS    RefSeq.
SOURCE      Pyramidobacter piscolens
  ORGANISM  Pyramidobacter piscolens
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Dethiosulfovibrionaceae; Pyramidobacter.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Pyramidobacter piscolens"
                     /db_xref="taxon:638849"
     Protein         1..386
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=40713
     Region          <1..379
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mqfwgykrqe gragirnhvl ilptcacgse sarivasevr gavniifntg csdvaantam
       61 sqkvlmgfac npnvygvvii glgcetvgha qlrekirgmt gkpvvsfgiq eeggtlktie
      121 kavraardma aaaamqqker cdmsnlllgi ecggsdatsg iasnpavgel sdllvdlgas
      181 timsesiewi gaehvvarra atpelhnkii eicrdyeehl kaagqdcrag qptpgnkagg
      241 lstldekslg cirkggtrpi vevlaqaerp tkhgaivmdt agydissvts mvaggcnavi
      301 fttgrgtptg naivpvlkvt anartyrmmd dnmdvdlsgi ikgtttyres grelleiigd
      361 vcngkmtkae aygfsdiaid hvcrfv
//
LOCUS       WP_009164024              77 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein, partial [Pyramidobacter piscolens].
ACCESSION   WP_009164024
VERSION     WP_009164024.1
KEYWORDS    RefSeq.
SOURCE      Pyramidobacter piscolens
  ORGANISM  Pyramidobacter piscolens
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Dethiosulfovibrionaceae; Pyramidobacter.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 77)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Pyramidobacter piscolens"
                     /db_xref="taxon:638849"
     Protein         <1..77
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          <1..65
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 aavragksql vpdvrafpgh iacddasrse lvvpltvggr twgvldldsp eparfdetdr
       61 aalekiaaqi eaqaarl
//
LOCUS       WP_009164084             191 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Pyramidobacter piscolens].
ACCESSION   WP_009164084
VERSION     WP_009164084.1
KEYWORDS    RefSeq.
SOURCE      Pyramidobacter piscolens
  ORGANISM  Pyramidobacter piscolens
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Dethiosulfovibrionaceae; Pyramidobacter.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Pyramidobacter piscolens"
                     /db_xref="taxon:638849"
     Protein         1..191
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20284
     Region          3..155
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mtlselyvgc rtyrrfeqrp lpdgllravl enariastga naqtlrfiav qssalvaqmq
       61 plvrwaaylp keigtpaege rpvafvvivk kagsgafadv dvgiaantia ttaweagvgs
      121 clmasvnrae iaallgvpae dtvflvvalg ypahkstlvp vgadgsvkyy vdekrdyfvp
      181 krafddvaki v
//
LOCUS       WP_009164235             352 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Pyramidobacter
            piscolens].
ACCESSION   WP_009164235
VERSION     WP_009164235.1
KEYWORDS    RefSeq.
SOURCE      Pyramidobacter piscolens
  ORGANISM  Pyramidobacter piscolens
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Dethiosulfovibrionaceae; Pyramidobacter.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 352)
  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 352)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Pyramidobacter piscolens"
                     /db_xref="taxon:638849"
     Protein         1..352
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=39551
     Region          26..85
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mdntsfqvld faqpfcvien yvlederlta ydvtvylalr syagarredg slvcwpsvet
       61 lakkarcvrs tcfkslahle dlgylrresr yvnnqykktt lyqllpnpra agpsdgsdes
      121 atrtesvirt davrltdsts psngrrtrfn eldsenynpp lippkggage aaspsepeip
      181 geqrmiadsp dealaeeltq kiqadfprad agklrvavrr wieaygrerv egeipaalll
      241 qcekggryrd pvryigawlr rgrkapppva sridelfeef wtmwpglrdg kegarrewrr
      301 rfsalpdaaa rngalralep qiealierae rgedlrflgk aqnfirdadl ag
//
LOCUS       WP_009164926             345 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Pyramidobacter
            piscolens].
ACCESSION   WP_009164926
VERSION     WP_009164926.1
KEYWORDS    RefSeq.
SOURCE      Pyramidobacter piscolens
  ORGANISM  Pyramidobacter piscolens
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Dethiosulfovibrionaceae; Pyramidobacter.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 345)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Pyramidobacter piscolens"
                     /db_xref="taxon:638849"
     Protein         1..345
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37866
     Region          3..338
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mnrgmsvrgi swclperfet nedlvrefgt wtpekiykkt givrrhiadv dkpvshylam
       61 agekffaerp avsrdsidml vvcceardyi apatacvvhh klglrkscga vdyelgcsgy
      121 vyglsiakgy iaagiadrvl litgdevtry vnkhdkairt ifgdgytatl leaserdrvt
      181 gfdlgtdgsg lrdiiieage talprsesta vervnrfgnv hsqenvvmdg rqvlefslre
      241 vpgsvqrcle ragvgkeeld livfhqasrl lleqvrdemr fpedkfvisl edkgntvsst
      301 ipialgecae qgrlkagmkv llsgfgvgls wgtvlvewgt ddgae
//
LOCUS       WP_009164932             218 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Pyramidobacter piscolens].
ACCESSION   WP_009164932
VERSION     WP_009164932.1
KEYWORDS    RefSeq.
SOURCE      Pyramidobacter piscolens
  ORGANISM  Pyramidobacter piscolens
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Dethiosulfovibrionaceae; Pyramidobacter.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 218)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Pyramidobacter piscolens"
                     /db_xref="taxon:638849"
     Protein         1..218
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=23961
     Region          2..127
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(7..10,41..43,46,70,109,123)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mirahfdgas rgnpgeagag mviydgerai wrralplgmk tnneaeymal sllvdelerr
       61 glknaeirgd sklvisqvtg qwkikeprlk aladpiieri ralqarcrwv praqnaeadr
      121 lsnvaldege fiesapsdpg epipekqadi saaapelpar mpggpelrhv gakvwlvken
      181 geefavdvah rcctckegrk tgrcrhielv lmknptvl
//
LOCUS       WP_009165867             420 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Pyramidobacter piscolens].
ACCESSION   WP_009165867
VERSION     WP_009165867.1
KEYWORDS    RefSeq.
SOURCE      Pyramidobacter piscolens
  ORGANISM  Pyramidobacter piscolens
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Dethiosulfovibrionaceae; Pyramidobacter.
REFERENCE   1  (residues 1 to 420)
  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 420)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Pyramidobacter piscolens"
                     /db_xref="taxon:638849"
     Protein         1..420
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=46220
     Region          29..279
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mnvndklyrk aldrrplnvr nrwesedvgl fsgrdifaam keneaivlaa narhpltakg
       61 vlraakkhda avlieiakse tnycganfgn lvdyavqysr elghgavfam hvdhygikgk
      121 ddvmkavtqm geivakgwts vaidashldd wnnlcatrdv amhippyfgl eaevgeikgp
      181 gefstveeal yfigglnswg ifpdliaisn gskhgtydkt mgqdeginld rtqeiaaalr
      241 pygvgiaqhg isgtdiekca rfrkygivkg nvatlfqnvi fgikmepdtg naviegdsyv
      301 keadrgipvd lwdeivaycd gkgmsrksgd ykkanlpfcd kilalpdkyl drildeteyw
      361 aerfikafna egtaekviev vnrrgtwnpl perkiiadra dfradtaptk ggndggdyse
//
LOCUS       WP_009165939             387 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Pyramidobacter piscolens].
ACCESSION   WP_009165939
VERSION     WP_009165939.1
KEYWORDS    RefSeq.
SOURCE      Pyramidobacter piscolens
  ORGANISM  Pyramidobacter piscolens
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Dethiosulfovibrionaceae; Pyramidobacter.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Pyramidobacter piscolens"
                     /db_xref="taxon:638849"
     Protein         1..387
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=40821
     Region          <1..387
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mklmgyrraq gphgirnyll vlptsvcaad taekiacqvp gavsvptqhg ccqigsdlal
       61 tertlagfgm nanvgavlvv glgcdgiqar hlagmiepmg kpvqsiviqe eggtlktiae
      121 ggriaadmar aisadvreef digeiilgme cggsdptsgl asnpaigyvs dklvdmggss
      181 ilsettevig aehllaarfa deeerrkflr mvrdvedrai mlgqdlrsgq ptpgnkeggl
      241 stieekslgc mykagtrpft galeyaerip egkrglyfmd tpgqdidsit gmvaggaqvi
      301 vfstgrgtpt gspiapvvki tgnsetfrsm rdnmdinagr iitegaslsq igeelfemmv
      361 kvcngrqtka ealghrefgi yklagtf
//
LOCUS       WP_009169253             189 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Clostridium sp. DL-VIII].
ACCESSION   WP_009169253
VERSION     WP_009169253.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. DL-VIII
  ORGANISM  Clostridium sp. DL-VIII
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Clostridium sp. DL-VIII"
                     /db_xref="taxon:641107"
     Protein         1..189
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21382
     Region          2..155
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mikelvlknr syrrfhqeks ierdtlkdlv dlarlspsga nkqsirfils nseeendkis
       61 kcifwagyyk dwdgpedgek psayivvvrd ttfgsgmpqd egiavqsill gavekgfggc
      121 iianidrkhl resisldeky eislvvalgy pkeevvveti gqsgdikywr dekqvhhvpk
      181 rtldeliln
//
LOCUS       WP_009169966             164 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Clostridium sp. DL-VIII].
ACCESSION   WP_009169966
VERSION     WP_009169966.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. DL-VIII
  ORGANISM  Clostridium sp. DL-VIII
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 164)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Clostridium sp. DL-VIII"
                     /db_xref="taxon:641107"
     Protein         1..164
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=18587
     Region          45..163
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(113..114,117,137..140,142)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkilskifks krddkknsra ddakqnasts nyvnknniss tteylilvnl rsfkvniykg
       61 stnkwnlihs yictigknst ptpkgtftvg ikglyfgvsk gykcwyytqf kgnylfhsii
      121 ynldgsirdg rlgmklsdgc irlskenakw iydnvprgtk viin
//
LOCUS       WP_009170672             166 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Clostridium sp. DL-VIII].
ACCESSION   WP_009170672
VERSION     WP_009170672.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. DL-VIII
  ORGANISM  Clostridium sp. DL-VIII
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 166)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Clostridium sp. DL-VIII"
                     /db_xref="taxon:641107"
     Protein         1..166
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18306
     Region          8..162
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfdikvfedm steskldnml imleglvsde dlpitklcna salinaligr inwcgfylvn
       61 dnalklgpfq gmpactkiei gkgvcglaal kretllvndv hnfeghiacd aasnseivip
      121 ivrddkligv ldldsaefgr ftelerkyle kaisilnkyi ewnaii
//
LOCUS       WP_009172106             213 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Clostridium sp. DL-VIII].
ACCESSION   WP_009172106
VERSION     WP_009172106.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. DL-VIII
  ORGANISM  Clostridium sp. DL-VIII
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (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   3  (residues 1 to 213)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Clostridium sp. DL-VIII"
                     /db_xref="taxon:641107"
     Protein         1..213
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24620
     Region          17..211
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mnnfnlevnd klevvmgdki yraliidvqe dflrinlpvn ngeylmlnpk eeiemnsyld
       61 engcfnfysk iisrgregni iyyeiskpfn itkiqrrnff rvslvdevey kiitnakeee
      121 fdnipyekgl mvdlsagglk lkgngkidgt dlilvnfkln siqfevkcdi vrientmdkq
      181 klcglrfldi tnaqsekiiq glfeivrrqr ana
//
LOCUS       WP_009172163             685 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Clostridium sp. DL-VIII].
ACCESSION   WP_009172163
VERSION     WP_009172163.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. DL-VIII
  ORGANISM  Clostridium sp. DL-VIII
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 685)
  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   3  (residues 1 to 685)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Clostridium sp. DL-VIII"
                     /db_xref="taxon:641107"
     Protein         1..685
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=75904
     Region          1..685
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          174..249
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 mdtsqymsmf leesldnlqt lneslldleq npedtdkvne ifrvahtikg maatmgftdl
       61 aelthkmedv laefregelk vtqdvvtvlf dcldtlekmv dnvqegsdek vemegimqal
      121 adiknngnkg adnqvkqvqa sevsdeatan dldlnqydas virqarekgy nsieikvtls
      181 entllksara flivkdledh geilksepst qdieneefdf elkfvlvtkd tvdeimdvvn
      241 gisevakvea sliefddldi epkdaeakei keikevkvee raevqkaeap keeaknapak
      301 ktaqkkevkk ahqsvrvdle ridnlmnmvs elviyrtrle qivnvhksqe lnetleqvgr
      361 ttsdlqdlvm kirmlpldtv fnrfprmird vsvelnkein fiiegadtel drtvideige
      421 plihllrnaa dhgiesaekr vaqgkppvgt irlvayqegt kalikvtddg aginvekvka
      481 kaeqkgintd gmsdsdiknl ifaqgfstnd vvtdisgrgv gmdvvktkis alggtvdvvs
      541 eegkgssfvi klpltlqiiq allvkvgeet laislgfidr vidykeenik rsngkevivy
      601 renviplirl nesldiease tnkkfviivn vgdktigllv dsllgqqeiv ikplgktlkn
      661 ldqyigatil gnglvtlild igall
//
LOCUS       WP_009172223             255 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Clostridium sp.
            DL-VIII].
ACCESSION   WP_009172223
VERSION     WP_009172223.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. DL-VIII
  ORGANISM  Clostridium sp. DL-VIII
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Clostridium sp. DL-VIII"
                     /db_xref="taxon:641107"
     Protein         1..255
                     /product="formate/nitrite transporter family protein"
                     /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=27097
     Region          12..255
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mfceefnsvi maakakvnll kknslgyfls silaglyvgm gimliftigg llsasnspat
       61 kivmgvsfgi alslvimags elftgnnfim taaslskevk wsdtlkvwiv cfignllgsi
      121 iagymfyatg lsagavgefi aktsatkmsi pflpllmrgi fcnilvclat wcsfklkses
      181 gklimifwcl fafitagfeh svanmtllti gllnpgaanv svmgyaynig vvtlgniigg
      241 avflalpyyi isrkk
//
LOCUS       WP_009172766             362 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Clostridium sp. DL-VIII].
ACCESSION   WP_009172766
VERSION     WP_009172766.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. DL-VIII
  ORGANISM  Clostridium sp. DL-VIII
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Clostridium sp. DL-VIII"
                     /db_xref="taxon:641107"
     Protein         1..362
                     /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=42872
     Region          21..298
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 msnysnrlly tlednsielk kdkmgrilfw dnlkfllilv vvvghfadfy stssmkmkel
       61 flfiyifhmp lfifvsgyfs kkiinvkqfk iekvfsylvl yfllkvcffi lnkylfgkve
      121 tyftlfneng vpwyllamsi wlcltyvvkd iksiyvlfss ilisvlagyd ktvgdficls
      181 rilvffpyfv vgyyiseerl ikilkcnwlk cmslifllit iiaicmygqn lyqfrgyftg
      241 rnsyivlnep lyggvyrilf yglsviislg vifatpkcnv fftkfgsrtl qvyflhylil
      301 slyihyklnd yliksfpksw kfiylclaim ltyllslkmf eypfkrimgi nlnklkvsqy
      361 dm
//
LOCUS       WP_009172882             532 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Clostridium sp. DL-VIII].
ACCESSION   WP_009172882
VERSION     WP_009172882.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. DL-VIII
  ORGANISM  Clostridium sp. DL-VIII
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 532)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Clostridium sp. DL-VIII"
                     /db_xref="taxon:641107"
     Protein         1..532
                     /product="amidohydrolase family protein"
                     /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=58711
     Region          95..513
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mkqrnilmti gfalllvllf gvvlvlmiss gerwfaylil aacvsllvfl rstrfwrgwr
       61 illcwilalv vawtglfasq pstniqpytt qkleqpsapy qlllnnltiv dtrtgnltsn
      121 msilcvngki kdiapagtik adndtkiida tgkyvvpgyl nmhmhvigee ntsesmalll
      181 angvtgfrqm sgsvellkew rsgaftsstn epalltmpvd imtpinaptp eiavefvrqq
      241 qkagvdfikv ggvspdvfna iqaeanklgi pvvghvlpdm dlkevskngf hciehfginf
      301 galiscstde kalrsqatgi ptkftenpif vqlmkirgiq hfvneqfikw gtktsggakd
      361 etqlmhiint yseekakela nvyvqyntwq cptmvrmhag lfngsdeata qrlydiylsl
      421 vktydlegvk mmagtdgseg naihkefdel ekagisplhv lqmttlngae flnrlddmgt
      481 aevgknadlv lldanpiesv qnlhkidavi ragsyhskee ldsikekytn ek
//
LOCUS       WP_009173064              96 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Neisseria sp. oral taxon 014].
ACCESSION   WP_009173064
VERSION     WP_009173064.1
KEYWORDS    RefSeq.
SOURCE      Neisseria sp. oral taxon 014
  ORGANISM  Neisseria sp. oral taxon 014
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 96)
  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   2  (residues 1 to 96)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Neisseria sp. oral taxon 014"
                     /db_xref="taxon:641148"
     Protein         1..96
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9840
     Region          22..77
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkhilfgila llavplalaa vnintataae lealpgigpa kakaivayrq qngqfktved
       61 lkkvkgigeg ifsklkdeas vappaakkav pavkqq
//
LOCUS       WP_009174441             165 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Neisseria sp. oral taxon 014].
ACCESSION   WP_009174441
VERSION     WP_009174441.1
KEYWORDS    RefSeq.
SOURCE      Neisseria sp. oral taxon 014
  ORGANISM  Neisseria sp. oral taxon 014
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Neisseria sp. oral taxon 014"
                     /db_xref="taxon:641148"
     Protein         1..165
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18259
     Region          7..163
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mhtihiassd ktsvyreilp qiesltdgep cftanlania avlkeafgwf wvgfylvera
       61 snelvlgpfq gpaactripy grgvcgqawa gdkavvvedv nrhpdhiacs slsqseivip
      121 lfdrnrrcfg vldadsdrla qfdetdaryl nqlaelvgrl yerdi
//
LOCUS       WP_009175013             154 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Neisseria sp. oral taxon 014].
ACCESSION   WP_009175013
VERSION     WP_009175013.1
KEYWORDS    RefSeq.
SOURCE      Neisseria sp. oral taxon 014
  ORGANISM  Neisseria sp. oral taxon 014
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Neisseria sp. oral taxon 014"
                     /db_xref="taxon:641148"
     Protein         1..154
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=15768
     Region          1..151
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkamqkgftl ielmivvaii gilaaialpm ygdytaraqa tegyellggl ktplveavaa
       61 ssnavackgt tgandnqpwf qsavttgkyv dnvvaavdgs ncgltatfka asagvndkva
      121 ghkivmtlnp sdgkwtcksd ldknvspaac rdai
//
LOCUS       WP_009181884             726 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Solidesulfovibrio carbinoliphilus].
ACCESSION   WP_009181884
VERSION     WP_009181884.1
KEYWORDS    RefSeq.
SOURCE      Solidesulfovibrio carbinoliphilus
  ORGANISM  Solidesulfovibrio carbinoliphilus
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Solidesulfovibrio.
REFERENCE   1  (residues 1 to 726)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 726)
  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   3  (residues 1 to 726)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..726
                     /organism="Solidesulfovibrio carbinoliphilus"
                     /db_xref="taxon:345370"
     Protein         1..726
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76728
     Region          5..726
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mvlndetral fqeevlenla eldgallele kaptdldlvn rifravhtlk gacdmfglsp
       61 vvglahdies lfdhvrggwr rvskelldas faakdrfaam laegadpaae ddpalrarlk
      121 ellrtpdmpv adeaapaaga epeacagpep ddgpdratpr swrvcvapsd hghlakadpl
      181 avldelramg ntqvrcdlgq vpdlaglape dcllrfevvl taeagavpda nalrdvfffl
      241 enqadleitp cdealaeplp aaslaaapag avadwpdlsa vpaatpaaav aaaarpapaa
      301 srpasgttpa tasgpgpvag hkpgeaapdp akkpqaaark eamqslrvda aklddlvnlv
      361 gelviaqarl tqlatgfghp altsvaeeie rlsnelrdnt lgirmlpigt tfsrfrrlvr
      421 dlssemqksi elvteggete ldktvieqlg dplvhllrns idhgieppge rlaagkpetg
      481 tivlsaehag gevvlsitdd grgmdpdrir akaeekglip pdarltesei fnlvflpgfs
      541 taekvtnvsg rgvgmdvvkr smdslrgkid iqstlgkgsr itiklpltla iidglqikag
      601 ddqyiiplsl veecvelpre rteasgrgrt ihlrgeivpy irlreafelr geapaieqvv
      661 vtrfegertg iavdqvmgqq qtvikslgny igsvsgisga tingdgtmsl ildvptlvas
      721 vkraaa
//
LOCUS       WP_009183338             530 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Cecembia lonarensis].
ACCESSION   WP_009183338
VERSION     WP_009183338.1
KEYWORDS    RefSeq.
SOURCE      Cecembia lonarensis
  ORGANISM  Cecembia lonarensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Cecembia.
REFERENCE   1  (residues 1 to 530)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Cecembia lonarensis"
                     /db_xref="taxon:645110"
     Protein         1..530
                     /product="amidohydrolase family protein"
                     /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=60343
     Region          37..499
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mkrlihilfv gliafpftlf sqimpspdrk egegpydrli irgvtlvdgt gappigpvdi
       61 vvekniiaev kvvgypglpi keerrpkage ndmvmdlegh yllpgfidmh ghiggtgqgt
      121 paeyvfklwm shgittvrdp aasngldwvl dhkrkaaans itaprllayt vfgqgagkti
      181 ttaeeakawv nenkrrggdg ikffganpev mqaaleenkr iglrsamhha qmdvarwnvl
      241 hsaraglttm ehwyglpeal ftdrtiqdyr ldynyqneqh rfaeagklwk qaaapysdhw
      301 nkvmqelldl dftivptfni yeanrdlmrt rraewhdeyt lpslwrfykp sreshgsywf
      361 dwtteeeiqw kenyrlwmtf ineyknrggr vvtgsdsgfi yqlygfayir emellreagf
      421 hplevirast lkaaeaigme keigsvevgk ladfvileen plqnlkvlyg tgairidedn
      481 epirvggvky tvkdgivyda kqlledvrti vqqhkdrena rklkqpgldw
//
LOCUS       WP_009182133             189 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Solidesulfovibrio
            carbinoliphilus].
ACCESSION   WP_009182133
VERSION     WP_009182133.1
KEYWORDS    RefSeq.
SOURCE      Solidesulfovibrio carbinoliphilus
  ORGANISM  Solidesulfovibrio carbinoliphilus
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Solidesulfovibrio.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Solidesulfovibrio carbinoliphilus"
                     /db_xref="taxon:345370"
     Protein         1..189
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=19813
     Region          1..188
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mkrlivgisg asgvilgvrl levlgqtpdv ethciispga avtlrletgr tvesvaalag
       61 vvhdhdnlaa aissgsfpva gmvvapcsmk slaqialslg dnllaraadv tlkerrklvl
      121 vpretplhlg hlrhmvavte mggiilppap sfyhapktim dvvdqtvgki ldqfgilhdl
      181 farwggrda
//
LOCUS       WP_009183489             251 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Cecembia lonarensis].
ACCESSION   WP_009183489
VERSION     WP_009183489.1
KEYWORDS    RefSeq.
SOURCE      Cecembia lonarensis
  ORGANISM  Cecembia lonarensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Cecembia.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Cecembia lonarensis"
                     /db_xref="taxon:645110"
     Protein         1..251
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28384
     Region          179..250
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 maeenkdsls eqnendygfp fvevtplkak adqkpsieqe nlekpvsvar aetkeelpqf
       61 ekqivgtsse kgrkksqlpl qfslvmlili ilaamayfly flpetetvpv itetvessee
      121 mipeatsaps edpvaereee alqeeeetnm eeiispspvn aqtfgeifqv rqrstpiqyy
      181 iiiasmpsed laidraeelq senrdvwviy pygetsnyrl sigkytafee atqalenfka
      241 dfgasiwilk y
//
LOCUS       WP_009183745             565 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Cecembia lonarensis].
ACCESSION   WP_009183745
VERSION     WP_009183745.1
KEYWORDS    RefSeq.
SOURCE      Cecembia lonarensis
  ORGANISM  Cecembia lonarensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Cecembia.
REFERENCE   1  (residues 1 to 565)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Cecembia lonarensis"
                     /db_xref="taxon:645110"
     Protein         1..565
                     /product="amidohydrolase family protein"
                     /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=60818
     Region          37..438
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mnirfkpkvf ssllclalcf tlhafgqsdp rgerrvtgty aivnatvita pgktlegati
       61 lvknglvenv gknislppea qvikgdslfi ypgfidgass igiskpadpe rpanfdpsnp
      121 pdelagitpw rnaldyydkn nnqitdwrkv gftiaqivpe ggmlpgksai vtyggkestn
      181 ilanntalna rfrnvgggrg mypgtqlgim akfrdlykna elsakhnrlf astsgltrpe
      241 inktleaffp vldknmpilf evsndletkr aaslqrelgf plvlagvsdi nysidaikts
      301 naqvligfrl pndktanadl egktdemrgr tirikeayqe ilegpaqlek agipfgftsm
      361 ggrssemfkn irlmiengls eeaalaalti nnanilgiqk fagtlekgkl anmvistapi
      421 fsedaqiqhv madgylfdyd iskksksnga ngktiditgi wdytsdtpag ssngtmeikk
      481 egdslrgtit ydnpagsgka ssemnnitls gnnlsftfnv saggmslevt vagdvseldf
      541 rgnmslsdfg sfplnankkp nqrnq
//
LOCUS       WP_009184545             399 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Cecembia lonarensis].
ACCESSION   WP_009184545
VERSION     WP_009184545.1
KEYWORDS    RefSeq.
SOURCE      Cecembia lonarensis
  ORGANISM  Cecembia lonarensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Cecembia.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Cecembia lonarensis"
                     /db_xref="taxon:645110"
     Protein         1..399
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43416
     Region          1..398
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkilvlnsgs sslkyqlfem pneqalctgl vdriglehss ithktffkgk eskhqvelai
       61 pdhegallrv tellkdpkvg vlkdnteiea ighrvvhgge qfaattlite evkakikglf
      121 alaplhnppn ylgitvaerv fpqakqvavf dtafhqsmpa layryalpks mytdlgiray
      181 gfhgtshqyv skkaseylnn skakiitihl gngcsmtavd sgksvdtsmg lgpmgglvmg
      241 tragdidpsi ifhlinergf saqevndiln kksgllglsg lsdmrdvkna itegspdakl
      301 ayelyayriq kyigafaavl kgldaivfta gvgendadmr eavcknmdff gimldtklnr
      361 agnknirevn ksssavkilv iptneeleig qqtfelirk
//
LOCUS       WP_009185029             306 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Cecembia lonarensis].
ACCESSION   WP_009185029
VERSION     WP_009185029.1
KEYWORDS    RefSeq.
SOURCE      Cecembia lonarensis
  ORGANISM  Cecembia lonarensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Cecembia.
REFERENCE   1  (residues 1 to 306)
  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 306)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Cecembia lonarensis"
                     /db_xref="taxon:645110"
     Protein         1..306
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33841
     Region          41..301
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 merrnfiknl glgaalaata sgnafakgsg plkraeppfn mdyaphfgmf rshagedlad
       61 qlkfmaeqgf rslednglls rsvedqnrig rtleqlgmrm gvfvvdggdn wkisltsgkq
      121 efidnfvntc krsveaakrv natwatvvpg fferrlpigi qtanviealk rgaevfephg
      181 lvmvleplsd tpelflrhsd qtyaickavd spackilydi yhmqrnegnl iplmdacwde
      241 iayiqigdnp grkepgtgei nylnvfkhid tkgykgilgm ehgnakpgke geadliaayr
      301 kvdqfk
//
LOCUS       WP_009185232             229 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Cecembia lonarensis].
ACCESSION   WP_009185232
VERSION     WP_009185232.1
KEYWORDS    RefSeq.
SOURCE      Cecembia lonarensis
  ORGANISM  Cecembia lonarensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Cecembia.
REFERENCE   1  (residues 1 to 229)
  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   2  (residues 1 to 229)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Cecembia lonarensis"
                     /db_xref="taxon:645110"
     Protein         1..229
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26668
     Region          92..160
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
     Region          163..227
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkrnlffhlk ayfgfsrres kgfilvipal vilysipsly dwslqkhsih lyehyenkld
       61 sllqngweis eyvgvqsliq qdssnkkrnl pasrtavlnk ldfneadsiv lqivpgigqt
      121 magrivkfrd nmgglhdreq lldvygmnpe lmervfeyft frpgiqekin inhmevsdla
      181 rhpyisygaa kvivayreqh gpykspedll eikifnenwl erlrpylvf
//
LOCUS       WP_009181798             784 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Solidesulfovibrio
            carbinoliphilus].
ACCESSION   WP_009181798
VERSION     WP_009181798.1
KEYWORDS    RefSeq.
SOURCE      Solidesulfovibrio carbinoliphilus
  ORGANISM  Solidesulfovibrio carbinoliphilus
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Solidesulfovibrio.
REFERENCE   1  (residues 1 to 784)
  AUTHORS   Magnet,S., Arbeloa,A., Mainardi,J.L., Hugonnet,J.E., Fourgeaud,M.,
            Dubost,L., Marie,A., Delfosse,V., Mayer,C., Rice,L.B. and Arthur,M.
  TITLE     Specificity of L,D-transpeptidases from gram-positive bacteria
            producing different peptidoglycan chemotypes
  JOURNAL   J Biol Chem 282 (18), 13151-13159 (2007)
   PUBMED   17311917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18653986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..784
                     /organism="Solidesulfovibrio carbinoliphilus"
                     /db_xref="taxon:345370"
     Protein         1..784
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=83244
     Region          1..169
                     /region_name="YafK"
                     /note="Murein L,D-transpeptidase YafK [Cell
                     wall/membrane/envelope biogenesis]; COG3034"
                     /db_xref="CDD:442269"
     Region          476..>547
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
     Region          673..>757
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mkrtgrvlal acfllvlpcr waagewtadi vdmeaspsrf vavdkkaqsf allsrqsplr
       61 llaaipcatg qelgdkfkeg dlktpegvyf itrrktagln yelygdlafp lnfpnpadvv
      121 rrksghgiwi hgrghaiipy etqgcvalst pdihrvdpel aegmpvviad evrlggedta
      181 rlrdeardvv aatvawgkaw qdkspaffdf hdpekfaite gqpfasfksh kerlfkalpw
      241 iqvtlsdira lagpdywvty fvqvyrsptl isqgvkrlyw qraadgrfri igmeyeempv
      301 tladkggvra gkaaspdeke adtrrpdsps eeevqvrqlv saqqaamekv aqkafhtlhl
      361 kpqptpedqa ilevaqtgav rpgvspfatd amtpappppv paalavappv pavpavvaav
      421 avapaapaap vapipavavq apapppapaa qpavvaagpa taapaasaka apvaperaae
      481 iaalmegwrt awekgrlddy mayyadgarq gdlrgkdair rqkagvwrgr epgrvgievv
      541 sivadgdgfa vvcaedyqgk ggrpsqgyki lslvpsgrkl liakerwsrn rpdearlaaa
      601 sapsapvgaa atpavpaaqp eskalaaapa apattpspaa qpvqaaaasa eaptatpapa
      661 paakapakad rtaevaalve awrtawesgr lgdyagfyae kavqgtergr eairdqkagl
      721 wkdkapkrva lsdvrikprk dgfvvtcvqd yesrdggsdr gvktlylapa gngfaiveek
      781 wsrl
//
LOCUS       WP_009186424             332 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Cecembia lonarensis].
ACCESSION   WP_009186424
VERSION     WP_009186424.1
KEYWORDS    RefSeq.
SOURCE      Cecembia lonarensis
  ORGANISM  Cecembia lonarensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Cecembia.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 332)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Cecembia lonarensis"
                     /db_xref="taxon:645110"
     Protein         1..332
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36196
     Region          2..332
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mkksriigvg hyvperivtn dylssimdtn ndwivertgi ierrwytpgk etvtsmsvaa
       61 srmaieragi resdidfivf atitpdyflp gngvllqrel evgnigaldi rnacsgfiya
      121 lsvadqfikt gmyknilvvg aeiqssaldk sddgrssavi fadgagaail savdvdqpgi
      181 lsthlhsegq yaeelfclap ssstevrisq emidrgdffl kmngnavfkh avvrfseviq
      241 ealdangkdk seidllvphq anlrisnyiq qkmglpdekv fnnimhlgnt tagtipials
      301 qaweqgkike gdliclaafg sgfawasall nw
//
LOCUS       WP_009186100             450 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Cecembia lonarensis].
ACCESSION   WP_009186100
VERSION     WP_009186100.1
KEYWORDS    RefSeq.
SOURCE      Cecembia lonarensis
  ORGANISM  Cecembia lonarensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Cecembia.
REFERENCE   1  (residues 1 to 450)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Cecembia lonarensis"
                     /db_xref="taxon:645110"
     Protein         1..450
                     /product="amidohydrolase family protein"
                     /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=50278
     Region          31..450
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mkkyfqlgtw iyflisilly pslgmgqeik alvggtlidg fggppirnsv iiiegerike
       61 vgqvgtlkvp egaeiisteg msvmpglwdm hvhlminghs nythwdstyi dlfesvimps
      121 sahqllmagv tsardlgapl easinvreri nngeipgptl yvsgpfiqke pypgtkafrw
      181 gvngpadara kvkrlidagv dviklidhde mtfeeakavv deahkygkpv iahshrpeei
      241 riglkigvdc fehtglasap eypedimemi kertakmnmg plywtptveg lynyeytrnn
      301 peklddpswh lglpdsiird iraslrfpgr mpyfqltpvr kptlerkinq lkdagvvmli
      361 gtdsgipmkf hsqstwneld vwvnefgfdp lltikaatyw pavamrvddd ygtisegkya
      421 diiavrgdvl ryisllqnvd mvvkhgkrvk
//
LOCUS       WP_009186707             221 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Cecembia lonarensis].
ACCESSION   WP_009186707
VERSION     WP_009186707.1
KEYWORDS    RefSeq.
SOURCE      Cecembia lonarensis
  ORGANISM  Cecembia lonarensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Cecembia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Cecembia lonarensis"
                     /db_xref="taxon:645110"
     Protein         1..221
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=25259
     Region          58..212
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkkryfivlv lclswigisv aagqtfrife kpilfneert qlsleylknr hgieketati
       61 tpqmvvvhwt avstlestfd vfnpvhlggr peltaasnln vsahflvdrd gvifrllpdt
      121 tfarhtigln ymaigienig gpdapltraq lkanaeliry lqkkypityv ighheyyafq
      181 gtplwketdp dyitqkqdpg drfmkrlrkr lrdldvkskp e
//
LOCUS       WP_009187447             464 aa            linear   BCT 20-JAN-2025
DEFINITION  AAA family ATPase, partial [Streptomyces sp. e14].
ACCESSION   WP_009187447
VERSION     WP_009187447.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. e14
  ORGANISM  Streptomyces sp. e14
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Liu,Y., Sung,S., Kim,Y., Li,F., Gwon,G., Jo,A., Kim,A.K., Kim,T.,
            Song,O.K., Lee,S.E. and Cho,Y.
  TITLE     ATP-dependent DNA binding, unwinding, and resection by the
            Mre11/Rad50 complex
  JOURNAL   EMBO J 35 (7), 743-758 (2016)
   PUBMED   26717941
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Chen,Z., Luong,T.T. and Lee,C.Y.
  TITLE     The sbcDC locus mediates repression of type 5 capsule production as
            part of the SOS response in Staphylococcus aureus
  JOURNAL   J Bacteriol 189 (20), 7343-7350 (2007)
   PUBMED   17704228
REFERENCE   3  (residues 1 to 464)
  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   4  (residues 1 to 464)
  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
REFERENCE   5  (residues 1 to 464)
  AUTHORS   Hopfner,K.P., Karcher,A., Craig,L., Woo,T.T., Carney,J.P. and
            Tainer,J.A.
  TITLE     Structural biochemistry and interaction architecture of the DNA
            double-strand break repair Mre11 nuclease and Rad50-ATPase
  JOURNAL   Cell 105 (4), 473-485 (2001)
   PUBMED   11371344
REFERENCE   6  (residues 1 to 464)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Streptomyces sp. e14"
                     /db_xref="taxon:645465"
     Protein         1..>464
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          1..>464
                     /region_name="sbcc"
                     /note="exonuclease SbcC; TIGR00618"
                     /db_xref="CDD:129705"
     Region          1..>174
                     /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            35..42
                     /site_type="other"
                     /note="Walker A/P-loop"
                     /db_xref="CDD:213179"
     Site            159..162
                     /site_type="other"
                     /note="Q-loop/lid"
                     /db_xref="CDD:213179"
ORIGIN      
        1 mrlhrleita fgpfgsrqcv dfdalsaagl fllhgptgag ktsvldavcy alygsvpgar
       61 qsgqgatlrs dhadaatrte vtldltvagr rleitrqppw erpkrrgkgt tmdkaqtwlr
      121 eydaaagawk dlsrshqeig eeitqllgms reqfcqvvll pqgdfarflr adaeargkll
      181 grlfdtrrfa everrlaerr rateaqvreg daalladahr mqqaagdame lpdlapgdpg
      241 laeavltaaa varstareql taahcrltaa eadrlaagra lddvrelarl qqrfaeardr
      301 aerlaeraga heetrarmer grkaetvapa lelrdaadae hrraaaadas ararlperfh
      361 dagaaglaaa arraaeelgs lesarraerr lagllaerde adqeeradad alqeaeswla
      421 gwettrealr srveaaqdaa graeqlavrr epaqarlraa rerd
//
LOCUS       WP_009188797             411 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces sp. e14].
ACCESSION   WP_009188797
VERSION     WP_009188797.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. e14
  ORGANISM  Streptomyces sp. e14
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 411)
  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 411)
  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
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 411)
  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   5  (residues 1 to 411)
  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   6  (residues 1 to 411)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 411)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 411)
  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 20283677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Streptomyces sp. e14"
                     /db_xref="taxon:645465"
     Protein         1..411
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40671
     Region          51..101
                     /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(65,67..69,78)
                     /site_type="other"
                     /note="non-specific DNA interactions [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            78..84
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            order(79..80,84)
                     /site_type="other"
                     /note="sequence specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238044"
     Site            79..80
                     /site_type="other"
                     /note="putative cAMP binding site [chemical binding]"
                     /db_xref="CDD:238044"
     Region          115..402
                     /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 mtaetgsggg aeraqaessa aggvsgapgg aarlpggpsg vnllglrshn aalvldllrr
       61 agadgisrle laertgltpq avskitarlr erglaaeagr rastggkprt vlrlvpeagh
      121 svgvhvdrde vravlvdlng tvvgerlrpl dletaagaqa vveavaaqae alvgqvlgad
      181 saraasaatl vgvgvalpgp ldhrrgvlhr vtgfpqwdgf plrdalvrrl gvpvvvdkdt
      241 naaalgfalt aaedgggsfa yvhlgtglga glviggtvhr gartgagefg hqviqldgpp
      301 cgcgdrgcle alclaaverg dveeaarvlg vgaanlvgll didrvllggr tvaaapgvfa
      361 agvgervaar aaregvpgea vpvlavpgga rtvaegaaql llapvfgrge g
//
LOCUS       WP_009190704             548 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: M4 family metallopeptidase [unclassified
            Streptomyces].
ACCESSION   WP_009190704
VERSION     WP_009190704.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 548)
  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 548)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..548
                     /product="M4 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=56498
     Region          39..547
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mtpryarrtt lavatavaag allstgltts asaqvpadat tlaaaptdlt aaartsliqq
       61 aqtdaaetaq siglgakekl vvkdvvkdad gtvhtryert yaglpvlggd livhskagkt
      121 egvtkavkaa ikvasltpkv tpakaekqav glakdagsaa saadqaprkv iwagdgtpvl
      181 ayetvvgglq ddgtpnqlhv itdaatgkkl feyqgienat gtgktlysgs vsltttlsgs
      241 tyqlydtsrg ghktynlahk tsgtgslftd adnvwgtgaa sssstdqtaa adaaygaqet
      301 wdfykatfgr sgiknngvga ysrvhygnsy vnafwddscf cmtygdgsgn nhpltsldva
      361 ghemshgvts ntaglnysge sgglneatsd ifgtgvefya nnasdkgdyl igekiningd
      421 gtplrymdkp skdggsadyw sssvgnkdvh yssgvanhff yllsegsgak tingvsynsp
      481 tyngaavtgi grdkalqiwy kalttymtst tnykgartat lsaasalygs tsaeykavaa
      541 awtavnvs
//
LOCUS       WP_009194253             683 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Cesiribacter andamanensis].
ACCESSION   WP_009194253
VERSION     WP_009194253.1
KEYWORDS    RefSeq.
SOURCE      Cesiribacter andamanensis
  ORGANISM  Cesiribacter andamanensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cesiribacteraceae; Cesiribacter.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 683)
  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   3  (residues 1 to 683)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Cesiribacter andamanensis"
                     /db_xref="taxon:649507"
     Protein         1..683
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=74091
     Region          2..680
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 miehlkqkyl eeahdlllel eqtlllleqn paaaegveta frvmhtlkgs sgmfgyqqig
       61 elvhllesgy dairasgspf phallnlsle avdhirllld aaaaateacq tthrlllkra
      121 aemlyevvpa tdsstaptrq eltswallfa pqadlfkngt nplyiledla slgqlhtfad
      181 tqllppaqal dprccylswk lllvtdapes dirdcflfve gscrlelhpl gpgnclssls
      241 epataelarq vreglsweqf leqlqqpgaa vaagpgqlpt adslpeaegg aaglqtrgaa
      301 sirvasdkld dlmnlvselv anqerlslla elslqpelag vaeeiekitr qlrdktfdic
      361 lvpigsmltr fkrlvrdlsq elnknivfea egveteldkn viqnlsdclv hifrnsidhg
      421 iegeqerlrk gkpaqgkivl kaytsgtnvv ievqddgagi dlqkvqqkal qkgligpedt
      481 lseqevlell fmpgfstaqg vtavsgrgvg mdvvrrnmre lrgevtlssr qdagttltlt
      541 lpltisiidg lmvrigdtdf vlplsfveks ysitpgqlsa afnnqlvldg epmlyanlad
      601 afgcpgvgrq sfgvvvktgq qkmlllvdai lgeyqavlkp lgrfyleqdf lsggslkgdg
      661 tvalvidpqk liqdiiqkta isi
//
LOCUS       WP_009195861             295 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Cesiribacter
            andamanensis].
ACCESSION   WP_009195861
VERSION     WP_009195861.1
KEYWORDS    RefSeq.
SOURCE      Cesiribacter andamanensis
  ORGANISM  Cesiribacter andamanensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cesiribacteraceae; Cesiribacter.
REFERENCE   1  (residues 1 to 295)
  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 295)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Cesiribacter andamanensis"
                     /db_xref="taxon:649507"
     Protein         1..295
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32866
     Region          5..>41
                     /region_name="DUF839"
                     /note="Bacterial protein of unknown function (DUF839);
                     cl23843"
                     /db_xref="CDD:474079"
     Region          47..287
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mnettrrdvl kkmlagsvam vaagglpaca gasaeqtqpp vlkkninhsv crwtydflsl
       61 ealcrmvkei gfsaidlvgp aewhilkaqg idssmcngae isledgwnep anharllqny
      121 rdmipkvaqa gyknlicfsg nrrgmseeeg lqnsvaglqq lmplaeqhrv vmqlelfnsk
      181 vnhpdymads sawgielcrr lgsqnfklly diyhmqimeg diirtiqdhh awfghyhtag
      241 vpgrheidqs qelyypaimr aivasgytgy vaqefipqke dkvaslreai llcdv
//
LOCUS       WP_009196163             329 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Cesiribacter
            andamanensis].
ACCESSION   WP_009196163
VERSION     WP_009196163.1
KEYWORDS    RefSeq.
SOURCE      Cesiribacter andamanensis
  ORGANISM  Cesiribacter andamanensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cesiribacteraceae; Cesiribacter.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 329)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Cesiribacter andamanensis"
                     /db_xref="taxon:649507"
     Protein         1..329
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35760
     Region          2..329
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mrnavilssg ayapenivpn tyfnellged vdswlrqnvh iwerrwased qstsdlvlka
       61 aataleragv aaseldliiv atdtpeyvsp staskvqyll gagragtfdl ntacagfvta
      121 ldvgskyira daqynkvlvv gaylmskyld kldkktanlf adgagavvlg aeeggsrgfl
      181 asqlrtqgqy hdwmgiyagg tfqpvteevv akkdhllkfv krfpselnpn mwsemilqlc
      241 qrigvdiqev dhifftqini naiwatlell glprerahti mhhygytgsa cipmaldeal
      301 qlgkvkagdl vifmgsgggl sfacaafrl
//
LOCUS       WP_009197622             160 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Cesiribacter andamanensis].
ACCESSION   WP_009197622
VERSION     WP_009197622.1
KEYWORDS    RefSeq.
SOURCE      Cesiribacter andamanensis
  ORGANISM  Cesiribacter andamanensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cesiribacteraceae; Cesiribacter.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Cesiribacter andamanensis"
                     /db_xref="taxon:649507"
     Protein         1..160
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17651
     Region          9..158
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 maeelhisqt atraekyesl ipqiealtsg epdlyanlan taaalrqafg ffwvgfylvk
       61 geelvlgpfq gpiactrirr gkgvcgaswe rresilvpdv dqfpghiacs sasrsevvvp
      121 gfkgdevalv ldvdsdqlnd fsdtdqhyle qlmrvvekwf
//
LOCUS       WP_009196486             277 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Cesiribacter
            andamanensis].
ACCESSION   WP_009196486
VERSION     WP_009196486.1
KEYWORDS    RefSeq.
SOURCE      Cesiribacter andamanensis
  ORGANISM  Cesiribacter andamanensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cesiribacteraceae; Cesiribacter.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Cesiribacter andamanensis"
                     /db_xref="taxon:649507"
     Protein         1..277
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32581
     Region          9..271
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mdlfskttfe csklitqrys tsftlgirtl hkrfhfpiya iygyvryade ivdtfhshdk
       61 arllerfrhd trqaldekis lnpvlhsfqq vvheygiewe lieaflhsme mdldhtqyer
      121 vgyekyiygs aevvglmclr vfcegdedqy qqlkaparsl gaafqkvnfl rdirsdfeer
      181 grvyfpgvdf tefttaakkq iekdieqdfa daysgilrlp kgaqmgvyla ylyykklfyk
      241 icscppsril kervripdqn kllllaqtml ryqfnil
//
LOCUS       WP_009195179             388 aa            linear   BCT 20-JAN-2025
DEFINITION  prolipoprotein diacylglyceryl transferase [Cesiribacter
            andamanensis].
ACCESSION   WP_009195179
VERSION     WP_009195179.1
KEYWORDS    RefSeq.
SOURCE      Cesiribacter andamanensis
  ORGANISM  Cesiribacter andamanensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cesiribacteraceae; Cesiribacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002130
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Cesiribacter andamanensis"
                     /db_xref="taxon:649507"
     Protein         1..388
                     /product="prolipoprotein diacylglyceryl transferase"
                     /EC_number="2.5.1.145"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008961 -
                     phosphatidylglycerol-prolipoprotein diacylglyceryl
                     transferase activity [Evidence IEA]"
                     /GO_process="GO:0009249 - protein lipoylation [Evidence
                     IEA]"
                     /GO_process="GO:0042158 - lipoprotein biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44037
     Region          10..378
                     /region_name="Lgt"
                     /note="Prolipoprotein diacylglyceryltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0682"
                     /db_xref="CDD:440446"
ORIGIN      
        1 mellhfivwd pdpsifsifg ldvrwyglmf avgfligqqi mfylyrqegk paqdvetlti
       61 fmvvatiiga rlghvffyep dkylsdpiqi lnirggglas hgaaigilta lflyvnylir
      121 fhkgkfevkk rkrpgqsylw vvdkvvivta figalirign fmnseivgmp tqtpeygvvf
      181 ghwleesivr nsqgqivsae asaeesgrwn erfeapvlle lefrkgidta aaaqyirsdi
      241 qqmvryqsrg eafftdpgpe plpyslqqrs gvvsarvvan gvprhptqly eaasylfiff
      301 llfaiwsryk grapegllfg iflvtlfgfr fiwefmkenq vafeegmvln mgqwlsiplv
      361 lagvyfilqs lrrkrseepp vpsqqkvs
//
LOCUS       WP_009200625             392 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Acetomicrobium hydrogeniformans].
ACCESSION   WP_009200625
VERSION     WP_009200625.1
KEYWORDS    RefSeq.
SOURCE      Acetomicrobium hydrogeniformans
  ORGANISM  Acetomicrobium hydrogeniformans
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Acetomicrobiaceae; Acetomicrobium.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Acetomicrobium hydrogeniformans"
                     /db_xref="taxon:649746"
     Protein         1..392
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=41702
     Region          <2..385
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mlhdnqmtfl gykrpdgkig irnhvlilpa svcasdttri iasqvqgcvt fnnqngcsqv
       61 pkdltltldl msgfaanpni ygtivvalgc enaqesivva eikkrtnkpl esliiqdegg
      121 tlkaiekavr cakimveeas tlqkeefpis nlilgtecgg sdttsgiaan pvmgslsdkl
      181 valggtiils etteligaeh ilakrakder ikrriyeiiq ryemslafvg envregnpsp
      241 gnkagglttl eekslgcihk ggtssinevy dyakdvdakg lvimdtpgnd pssiagmvag
      301 gaqiivfstg rgtptgnpia pvikitgnre tykkmqdnid ldcsgvifgt htlnelgdtl
      361 ldevkkvasg kltkaeqlgy teiaimraan yv
//
LOCUS       WP_009200707             120 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Acetomicrobium
            hydrogeniformans].
ACCESSION   WP_009200707
VERSION     WP_009200707.1
KEYWORDS    RefSeq.
SOURCE      Acetomicrobium hydrogeniformans
  ORGANISM  Acetomicrobium hydrogeniformans
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Acetomicrobiaceae; Acetomicrobium.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Acetomicrobium hydrogeniformans"
                     /db_xref="taxon:649746"
     Protein         1..120
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13932
     Region          24..118
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mdtdaftagw terleierks rckrmreayi varkcahily dkyrvrrvyl igslanpedf
       61 hersdidlav eelpshlyfk alaelwrelp agleldlipl edvdpvflsr ilkegviidd
//
LOCUS       WP_009201090             384 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Acetomicrobium hydrogeniformans].
ACCESSION   WP_009201090
VERSION     WP_009201090.1
KEYWORDS    RefSeq.
SOURCE      Acetomicrobium hydrogeniformans
  ORGANISM  Acetomicrobium hydrogeniformans
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Acetomicrobiaceae; Acetomicrobium.
REFERENCE   1  (residues 1 to 384)
  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 384)
  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   3  (residues 1 to 384)
  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   4  (residues 1 to 384)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 384)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 384)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Acetomicrobium hydrogeniformans"
                     /db_xref="taxon:649746"
     Protein         1..384
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42037
     Region          29..373
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(103..105,126..127,177,233,257)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkkawfclfi vflfvlsvga vaaeekpiki glqapitgqw ayegemakns vevalqmiqe
       61 qggilggrki eivvaddasn prdsalaaqr lvsqrvaavi gtygssvnep aadiyeaskm
      121 idigygstav kltmakerky ffrtcgrddt qgqffseyav gtmkarriai mhdnttfalg
      181 vaeearkalq eyldagvael vfydaitpge kdftpiltkl retnpdvwyf tgyfpeagll
      241 vrqgrelgik cpfvggnaai nedfvkiagi eyakgclmtq epmptdldtp kakrflelyr
      301 qkhntlptsp wpvyaadali alswaidkag stdteamlev lrtgmegceg itgsiafter
      361 gdrkgiiykm yvvteggdmv vyqp
//
LOCUS       WP_009201664             673 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Acetomicrobium hydrogeniformans].
ACCESSION   WP_009201664
VERSION     WP_009201664.1
KEYWORDS    RefSeq.
SOURCE      Acetomicrobium hydrogeniformans
  ORGANISM  Acetomicrobium hydrogeniformans
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Acetomicrobiaceae; Acetomicrobium.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 673)
  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   3  (residues 1 to 673)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Acetomicrobium hydrogeniformans"
                     /db_xref="taxon:649746"
     Protein         1..673
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=74553
     Region          1..669
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdmseylsaf ldessdqleq lndlilllek dpqsrdtvne ifriahtlkg maaamgyegi
       61 anlthaledm ldmvrngeyq lrvedidlif kcldllsaav geirekgneg emgrqlsema
      121 kriksklahg saiqkkeesa eidawdaleh gwfdkareqg ldvykitiki asdcalksar
      181 aflvltrlee ageviktqps vedlerenfg dgfvlyfitk epkeeiekil ssisdislfc
      241 velidadeds skskpneqnq eefevkpqik dnvkmnrine slnsikqqqt ttvrvdigrl
      301 dklmnlvgel vigrarierl aaeaglsefe epllqlgris teiqeivtkl rmvpvayvfd
      361 rfprmvrdlc rnlgkeaelf iegseteldr tvideigdpm ihllrnaldh gietpqeris
      421 kgkprkgsit iaafqegnsv lievmddgrg idpgeikkka vekgvitkee aefmpedeal
      481 alvclpgfst sekvtdlsgr gvgmdvvknk veslggqfhi tskvdegtkv tiklpltlai
      541 vlallirigd etyaislenv eetllvdksd tkyvhgslvt tvrgeilslh nlktllnypg
      601 elddkeefpv vvvrvgasgk rrglivdeli gqqdivikpl gkllskvrgm agatilgdgk
      661 valildvagv gnw
//
LOCUS       WP_009201666             227 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Acetomicrobium hydrogeniformans].
ACCESSION   WP_009201666
VERSION     WP_009201666.1
KEYWORDS    RefSeq.
SOURCE      Acetomicrobium hydrogeniformans
  ORGANISM  Acetomicrobium hydrogeniformans
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Acetomicrobiaceae; Acetomicrobium.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  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   3  (residues 1 to 227)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Acetomicrobium hydrogeniformans"
                     /db_xref="taxon:649746"
     Protein         1..227
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26524
     Region          20..222
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mderswaeff ekvintkvvi kvkyglykgs ypsriedvrd gavavshpfl knglvplykd
       61 tildlitfek qppmiiqmkv lrrsisngip llwlfpsgep vkiqrrryar vscymeiaff
      121 slsrekkapf sasweeargl dislggirmr skvreeslee gdrlylrfnm dpneeiymis
      181 nvvrvirege flesglqfeg yprfterrli qfirskelrn akdvfhd
//
LOCUS       WP_009201903              80 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Acetomicrobium thermoterrenum].
ACCESSION   WP_009201903
VERSION     WP_009201903.1
KEYWORDS    RefSeq.
SOURCE      Acetomicrobium thermoterrenum
  ORGANISM  Acetomicrobium thermoterrenum
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Acetomicrobiaceae; Acetomicrobium.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 80)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 80)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 80)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Acetomicrobium thermoterrenum"
                     /db_xref="taxon:1120986"
     Protein         1..80
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8759
     Region          3..80
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mitvhvrlfa tllrffpdlq lgetmqvnlp dgatvgqlid rlnipveeik ivfvnnifrd
       61 mgyslkngdm vsifppvggg
//
LOCUS       WP_009202377             301 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Acetomicrobium
            hydrogeniformans].
ACCESSION   WP_009202377
VERSION     WP_009202377.1
KEYWORDS    RefSeq.
SOURCE      Acetomicrobium hydrogeniformans
  ORGANISM  Acetomicrobium hydrogeniformans
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Acetomicrobiaceae; Acetomicrobium.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 301)
  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 301)
  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 301)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Acetomicrobium hydrogeniformans"
                     /db_xref="taxon:649746"
     Protein         1..301
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33605
     Region          10..76
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          221..281
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 makdkdlksk siselgdilr rtreerglsl ddvakdtkip rshllaiesg emdrlpgrif
       61 arffikeyls ylglselwsq ydsflpmdeq veissvlgty spppkgfkat srwwiyavli
      121 lllgasgsll ylrrehvidi ikqprnvvsv etgvgadasp edilavingf ednqeqsiiv
      181 erqdedvslq atlphvegge amkaqekeke etakeiskil eikasrgrcw vrvsrgdeki
      241 yegtlqlnet ktfettgepi kvrfgnvaav dvtwmgtkve mprgsvvtvl yqadgkvvka
      301 d
//
LOCUS       WP_009203362             496 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Anaerostipes hadrus].
ACCESSION   WP_009203362
VERSION     WP_009203362.1
KEYWORDS    RefSeq.
SOURCE      Anaerostipes hadrus
  ORGANISM  Anaerostipes hadrus
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Anaerostipes.
REFERENCE   1  (residues 1 to 496)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Anaerostipes hadrus"
                     /db_xref="taxon:649756"
     Protein         1..496
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=56143
     Region          <262..327
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          376..495
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(446..447,448,468..471,473)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mritkkqggi iggavavvli aaaigvhahy qnrwypgstf nkvdvsgmty eesvkkvkks
       61 idsyklkikg rnngqevisg keidlafkte shvkdaykkq hsqsvfstif ggkktkvtav
      121 alseqklktk lkqsvlikgs dtykitkpvd ativysadkk ygviqkedeg nylnrkafyd
      181 aveksiesls ntlnltdekk npdvykkpgl yhddeelkqm qttyneyllh fiqwdmgnnv
      241 ketlgpdalk dcikvntkrh tvkldqpave kwlesfclky ktqgiartfk thsgkkikvs
      301 ggdygwridy dkviaqtmka lkkapdesai kayekdpske neqalltslk pvyshkgyrm
      361 dytnkqndwd tqnysevdls aqevfvykkg klvfsttcit gkatpdritr tgvydikekk
      421 ltktltgady svptrywtri mwtgtgyhys srgdwgswsp tyyktngshg cvnltlsdar
      481 svynltkigd pvfihy
//
LOCUS       WP_009204621             232 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Anaerostipes hadrus].
ACCESSION   WP_009204621
VERSION     WP_009204621.1
KEYWORDS    RefSeq.
SOURCE      Anaerostipes hadrus
  ORGANISM  Anaerostipes hadrus
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Anaerostipes.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Anaerostipes hadrus"
                     /db_xref="taxon:649756"
     Protein         1..232
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25992
     Region          39..125
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 makastilkk aksyigtken pansnnvkfn tdyyghsvkg ssypwccafv wdifrmcnas
       61 dlffggkkta ycpdvenyyk khdrwhstgq agdlclmdfg kgrashigiv ekankdgtyt
      121 tiegntskss ddnggavmrr trsksvirgf arpaydpeky ttvkktsdkg aikwmqkkln
      181 eltpgtniev dgiwekmtta qlkrywkrlg wstagsycgk ktckalyanr kk
//
LOCUS       WP_009205263             201 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Sulfuricella
            denitrificans].
ACCESSION   WP_009205263
VERSION     WP_009205263.1
KEYWORDS    RefSeq.
SOURCE      Sulfuricella denitrificans
  ORGANISM  Sulfuricella denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Sulfuricellaceae; Sulfuricella.
REFERENCE   1  (residues 1 to 201)
  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 201)
  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   3  (residues 1 to 201)
  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   4  (residues 1 to 201)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 201)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 201)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Sulfuricella denitrificans"
                     /db_xref="taxon:649841"
     Protein         1..201
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22235
     Region          11..201
                     /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"
ORIGIN      
        1 mnppvkpsef plrvllvdet feraallkha lqdagckiva hvsssadlpg lvaelkpdli
       61 ildtespdrd tlenlcvirr dqprpivmft hdddsdkiha airagvsayv vnglkserlr
      121 pimdvaiarf nefqamradl akaegqlser kdverakgil mkqrgwseee ayqalrkaam
      181 dkgsrladva rqlveitell g
//
LOCUS       WP_009205270             734 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Sulfuricella
            denitrificans].
ACCESSION   WP_009205270
VERSION     WP_009205270.1
KEYWORDS    RefSeq.
SOURCE      Sulfuricella denitrificans
  ORGANISM  Sulfuricella denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Sulfuricellaceae; Sulfuricella.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 734)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 734)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="Sulfuricella denitrificans"
                     /db_xref="taxon:649841"
     Protein         1..734
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=81611
     Region          19..719
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mlfgrkqknp ikiadkgvve wkyaacgycs tgcsievgln aegkpvtsrg vadadvnrgk
       61 lclkgifehe lftsagrgte plmreqwhqd wqpatwdsal dkvhdeivri qakygrdsva
      121 iistgqmlte efytlgkltr gligtnnydg nttlcmasav sgykrsfgsd gppgcyedfe
      181 htdclfawgs nlpeqhpiiy wrmkeaqekr gfplivvdpr vtmlaqnahi hlaitpgtdv
      241 vlmnammhvi faekledssy ietntngidm lraevakydp vtaskicgid edtirvvarl
      301 yakagaamai wtmginqsth gsdgvvginn lalitgnigk pggtslsitg qcnamgtrew
      361 sscsglpnyr alenpdhrae iadfwgidpe ffpkkrgmfq tdiyhaiesg qikglwliat
      421 nplsslpnsa rvrkamesle fcavqdcyhd tesaqyahvy lpagtwaekd gvmtnterri
      481 svvkpvtppp gqaqpdlwif nrmaerfnqs gkvnfpekaa diflemgkls vgrladisgm
      541 nhellekqrg iqwpytqeqv kngeappkgg krlytvdgtf syadgkakli plpfidnnev
      601 pdekfpiwln tgrliehwhg rtktgkignn nkyspipfie inpdlaaeln iergeyvrlv
      661 srrsdavvma mptqrvpknm vflpfhfhdc anrltlglld phsrqpaykq savrierian
      721 qmaaaklsme mrkf
//
LOCUS       WP_009206671             244 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Sulfuricella denitrificans].
ACCESSION   WP_009206671
VERSION     WP_009206671.1
KEYWORDS    RefSeq.
SOURCE      Sulfuricella denitrificans
  ORGANISM  Sulfuricella denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Sulfuricellaceae; Sulfuricella.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  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   3  (residues 1 to 244)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Sulfuricella denitrificans"
                     /db_xref="taxon:649841"
     Protein         1..244
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26954
     Region          38..239
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mteqlddkqe srfllnnead irallnklqk krshmtghfd nsyhifstcl levgkdtvil
       61 ddvsdeaisq rilacsrlhf ssvyagvpvs fvssqiehcl fegaaafsip ipsairwpqr
      121 relfrvptpi gkpvlceial nngeitrnpl sdisvggigm ltkvsspslk egalfggchi
      181 dlpgfgelts diricssadi tlrngnharr ygcqfidlpq qeqsllqryv tklelamrap
      241 qart
//
LOCUS       WP_009206141             417 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Sulfuricella
            denitrificans].
ACCESSION   WP_009206141
VERSION     WP_009206141.1
KEYWORDS    RefSeq.
SOURCE      Sulfuricella denitrificans
  ORGANISM  Sulfuricella denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Sulfuricellaceae; Sulfuricella.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 417)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Sulfuricella denitrificans"
                     /db_xref="taxon:649841"
     Protein         1..417
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47109
     Region          7..416
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 makpnltrdt fevfleaeel ghscqvgtiy rdkvrtalpv sfeyteewit qhpfmldprl
       61 elyageqhpv gasvlfgifl dsapdrwgrm lmdrreaiqa rkegrsrkal qemdyllgvn
      121 dltrqgalrf rrpggpfldn selptpsvmd laeleaicdr ieeegaeglp eyekwlslli
      181 apgsslggar pkanfeeedg slwiakfpak ndtydvgawe yvihrladka kiwvptsrmv
      241 slasryrtfc vkrfdragas rrmyasamtl lekkdgedgs ylemaelisn ygasgfietd
      301 laqlfrrvlf nvlvsnrddh lrnhgfiwva dgwrlseafd mnpnlsketh slalddanpe
      361 pdiqmamsta afyrltenqa ldilaevvda lsgwkkvakd mklsvaeidr mspafmi
//
LOCUS       WP_009206788             649 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Sulfuricella denitrificans].
ACCESSION   WP_009206788
VERSION     WP_009206788.1
KEYWORDS    RefSeq.
SOURCE      Sulfuricella denitrificans
  ORGANISM  Sulfuricella denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Sulfuricellaceae; Sulfuricella.
REFERENCE   1  (residues 1 to 649)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 649)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 649)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Sulfuricella denitrificans"
                     /db_xref="taxon:649841"
     Protein         1..649
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=71691
     Region          81..648
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mklsrllvii isalwllifi gtlsitirns rdylvnqmls haqdtatslg lslttsvehn
       61 dlattnsmvd aifdrgyyry ivirkisgdt lversqalwi sdvpewftha ftletpqgka
      121 limhgwkqvg tvevvshpgh aykelwrvsm qafwwtlvvg ivsllavvlv mrfalaplsv
      181 meaqalgisr rrftimkkip warelrrvaq amntmcsave rmlneqtalt ekmhskayld
      241 svtglangrn fnerlfhlln spdefaaggl ifvrldkfke ynetyghaag nallcqagei
      301 lvqlcgqher tllarmngae failvpdiaq dgmstladvm ihklselqrt sdtgettavv
      361 yagtafhqag qsttallsta dnalhsalkq gtscwqlysg eqsgkameld stqwkdlitt
      421 slqsgkiilh fqpvvscqnr simhhealar matqdgslla asafmpiakg lglareidry
      481 vvekvlthld avdqphavva inlsaaslrd egfiewlctk laddkvaakr lifetaehgv
      541 vadiqtarha iqqihdagak fsidrfghsa asfgylrnlh adyikidgsy irhiarneds
      601 qffvqslagi ahgleiivia eyvetaedye alkalsvdga qgyyigkpe
//
LOCUS       WP_009208545             214 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Aurantimonas
            manganoxydans].
ACCESSION   WP_009208545
VERSION     WP_009208545.1
KEYWORDS    RefSeq.
SOURCE      Aurantimonas manganoxydans
  ORGANISM  Aurantimonas manganoxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Aurantimonas.
REFERENCE   1  (residues 1 to 214)
  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 214)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 214)
  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   4  (residues 1 to 214)
  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   5  (residues 1 to 214)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Aurantimonas manganoxydans"
                     /db_xref="taxon:651183"
     Protein         1..214
                     /product="TRAP transporter small permease subunit"
                     /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=23228
     Region          3..171
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 msallsfsrg vdrvttfvgr gvswlvllvv lvsagnavir klfdvssnaw lelqwylfga
       61 ifmlaaawtl lknehirvdi vsnilskrtr dwidflghil allpftglmi wlltpyvlqs
      121 fnrgeyspna gglilwpaka lllagfillf lqglselikr gailfggmed ttpmasshae
      181 pvelaalapd rpeggteppp ldddarnggs gair
//
LOCUS       WP_009208541             373 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Aurantimonas
            manganoxydans].
ACCESSION   WP_009208541
VERSION     WP_009208541.1
KEYWORDS    RefSeq.
SOURCE      Aurantimonas manganoxydans
  ORGANISM  Aurantimonas manganoxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Aurantimonas.
REFERENCE   1  (residues 1 to 373)
  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 373)
  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 373)
  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 373)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Aurantimonas manganoxydans"
                     /db_xref="taxon:651183"
     Protein         1..373
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40849
     Region          1..358
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mdrrkfirns tvgalgvaga gslaapaiaq stpkvqwrct ssfpksldti yggaedmakf
       61 vreatdgnfd iqvfaageiv pglqaadavs dgtvqmchta syyyvgkdpt yalgatvpft
      121 lnarglhawl yyggglglln effnteglqy lpggntgtqm ggwfrkeint vqdldglkmr
      181 iaglagqalq klgvvpqqia ggdiypslek gvidaaewig pyddeklgfy kvapfyyypg
      241 wwegslalcf ftnkveydkl pdayksllat asravtleml seydyknpaa lktlvqsgaq
      301 lrpfsqeimq asfdatqevy aeingknpaf kkiydsmvay rndtylwqqv aeytfdtfmm
      361 ikqregalvp qgn
//
LOCUS       WP_009208701             194 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Aurantimonas
            manganoxydans].
ACCESSION   WP_009208701
VERSION     WP_009208701.1
KEYWORDS    RefSeq.
SOURCE      Aurantimonas manganoxydans
  ORGANISM  Aurantimonas manganoxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Aurantimonas.
REFERENCE   1  (residues 1 to 194)
  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 194)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 194)
  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   4  (residues 1 to 194)
  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   5  (residues 1 to 194)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Aurantimonas manganoxydans"
                     /db_xref="taxon:651183"
     Protein         1..194
                     /product="TRAP transporter small permease subunit"
                     /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=21713
     Region          1..167
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 miafirfada lsaafgkafa wliilmtfgt syevfvryvl gsptawaldv sfimygtlfm
       61 mggaytlsrs ghvrgdflyr mwkprtqamv dlvlyvffff pgvtalilag wkyaarswry
      121 gevsvnspag ipiyqfktvi vaagillfiq giaemmrciq cirggewirp eedvqetedt
      181 ilnkataaer dahp
//
LOCUS       WP_009209002             370 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Aurantimonas manganoxydans].
ACCESSION   WP_009209002
VERSION     WP_009209002.1
KEYWORDS    RefSeq.
SOURCE      Aurantimonas manganoxydans
  ORGANISM  Aurantimonas manganoxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Aurantimonas.
REFERENCE   1  (residues 1 to 370)
  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 370)
  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   3  (residues 1 to 370)
  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   4  (residues 1 to 370)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 370)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 370)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 370)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Aurantimonas manganoxydans"
                     /db_xref="taxon:651183"
     Protein         1..370
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38771
     Region          24..357
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(97..99,120..121,171,224,248)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkkallagaa lnlvfagaaf aditigvagp mtgqyasfge qlrtgaeqav adinaaggvn
       61 gemlklsvgd dacdpkqava vanqfasqgv pfvaghfcsg ssipasqvya deqivqispa
      121 stnpdftdkr pgdgvfrvcg rddqqgevag kyisdnfpda nvaiindkta ygkgladqtq
      181 kfyeeasgkk palveaytag ekdytalvtk mkeaginlly iggyhteagl marqmreqgm
      241 dtvlmsgdal vaeeywaitg dagqgtlmtf spdprkneaa apvvaeleka gktaegyvly
      301 tyaaiqawad avnkagstdf dpvvaalndg dyttvigdls fddkgdvtlp gyvvyewkdg
      361 kydyvdgaaq
//
LOCUS       WP_009209065             597 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Aurantimonas manganoxydans].
ACCESSION   WP_009209065
VERSION     WP_009209065.1
KEYWORDS    RefSeq.
SOURCE      Aurantimonas manganoxydans
  ORGANISM  Aurantimonas manganoxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Aurantimonas.
REFERENCE   1  (residues 1 to 597)
  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 597)
  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 597)
  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 597)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Aurantimonas manganoxydans"
                     /db_xref="taxon:651183"
     Protein         1..597
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=61907
     Region          4..597
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mstmvaddaa vrppmwfvwp vlgllsivfh lglifsglvp alvarpihma lalpwlfvfl
       61 aktrmqlltg wvllilgeig clyialnagp lsdqygfidn gfqmavaitl laitlemarr
      121 aigwplplva liclaygllg qyvpgeyghp gfpfasflgt mtiteggiwg sltgvsvgiv
      181 sifvilgavl nageagqgfm nvatlaagrl rggagkvsvl ssamfgsisg sasanvastg
      241 avtipamtrl gypralagav eavassggqi mpplmgagaf vmveltgtpy atimgaalpp
      301 ailyflttwi gidlfarryg lgavdaadrp svrdvvitsm ffavpfgill ermfvggftp
      361 qyaaclaila aalllfvnvr gevslhrfve raggaavsag qqiavigaii icasivigvl
      421 gmtglgvkvt stilsvadds lwpalfltai acillgmevp ttaayvicvt iagpalerlg
      481 iepllahlfv fwfallstit ppvcgavfia agmvgenwlk vagsamrlgi glyviplami
      541 anpaiihmad rpaeaglafv kiaialwals lafiwkgpvw mrlaaglggl ivcfasl
//
LOCUS       WP_009209508             302 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Aurantimonas
            manganoxydans].
ACCESSION   WP_009209508
VERSION     WP_009209508.1
KEYWORDS    RefSeq.
SOURCE      Aurantimonas manganoxydans
  ORGANISM  Aurantimonas manganoxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Aurantimonas.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Aurantimonas manganoxydans"
                     /db_xref="taxon:651183"
     Protein         1..302
                     /product="formate/nitrite transporter family protein"
                     /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=32778
     Region          48..299
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mdeqtsakav hdagkrrhsn dvteqrieke gstltegelh qiddrlklrp lavyeivrqe
       61 gedeltrpta slwwsglaag lsigfsvytm aalraylpda pwrslleswg ytvgflivil
      121 grqqlfteit lsatlpvlar rrwkgvvalv rlwavvlaan mvgtavfgag iaydvlnape
      181 ireaalalsa eamepafhym llrgiaagwl matvvwllps adrsgflvia lltylialfh
      241 lahvvagsve amalmfagrm avqdalvgfy lpallgnvlg gsalfslisy gqvvneldqr
      301 gn
//
LOCUS       WP_009210398             346 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Aurantimonas
            manganoxydans].
ACCESSION   WP_009210398
VERSION     WP_009210398.1
KEYWORDS    RefSeq.
SOURCE      Aurantimonas manganoxydans
  ORGANISM  Aurantimonas manganoxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Aurantimonas.
REFERENCE   1  (residues 1 to 346)
  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 346)
  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 346)
  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 346)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Aurantimonas manganoxydans"
                     /db_xref="taxon:651183"
     Protein         1..346
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=37665
     Region          5..341
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mtidrrrlit ttgavalasa lglrttrqaa aaqkltgvty lppsyadlay gsqglvdrin
       61 ekagetvaid fydsgrllsa deqlpalrsg tidfmfhtts yitrslpilg itglpgvvgd
      121 laknpdrlkr gsplfqliqd elkkngltvl slgggimepe yiwstesapi rslddvkgkk
      181 irvvsfeatk vmedlggaav ripsselyla mqrgtvdaav anistingrs iqeqvgqvyr
      241 mpltafaigv fvqtdrweam dqavrdafmd gvewfdthsa kvanteyfee kywpafrelg
      301 ieeiepdaaa verfneisag vrdswvqevg edvgrraial ahgeda
//
LOCUS       WP_009211327             417 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Aurantimonas manganoxydans].
ACCESSION   WP_009211327
VERSION     WP_009211327.1
KEYWORDS    RefSeq.
SOURCE      Aurantimonas manganoxydans
  ORGANISM  Aurantimonas manganoxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Aurantimonas.
REFERENCE   1  (residues 1 to 417)
  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 417)
  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
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 417)
  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   5  (residues 1 to 417)
  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   6  (residues 1 to 417)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 417)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 417)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Aurantimonas manganoxydans"
                     /db_xref="taxon:651183"
     Protein         1..417
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44704
     Region          30..74
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          94..401
                     /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 mdpqaegvpp eipsssgrmr gsnqsglrah nertvlslir qhgelakaei arrtglsaqt
       61 asvimralea eelvlrdkpr rgrvgqpsip mrlnpsgaft fglkigrrsv elvlmdflgv
      121 vrsrerltya ypdvalvldf vreaqprvas aiearlrlri vglgvampye mwswaeeiga
      181 paermdawrq vdivaeliai tglpvnland ataacaaenv fgtttsldyv yffvgafvgg
      241 givmggdlvt grtanagalg smpvpraare gvagvrldgf eqlinfasih vlekmiaaeg
      301 gdplvlwkda gawdelgtvl dhwlgiaarg layaivsasa vydfecavid ggfpenvrar
      361 lveatqramv rlrrqgltpl diragtmgas areigsaslp ffarflldhr glsaeaa
//
LOCUS       WP_009212203             401 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Actinomyces sp. oral taxon 180].
ACCESSION   WP_009212203
VERSION     WP_009212203.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces sp. oral taxon 180
  ORGANISM  Actinomyces sp. oral taxon 180
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Actinomyces sp. oral taxon 180"
                     /db_xref="taxon:651609"
     Protein         1..401
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42711
     Region          1..290
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          289..375
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mlilhtsdwh lgrtlhgapl gdsadafidw lvalvrergv davlisgdvf dravppvdal
       61 armrralrel taittvilts gnhdgaarlg lfadmlspsl hvvtdpeaig saveaggalv
      121 ypmpylepdl vrqvlsdlep dgesgaarpl prshqavlaa alrrirrdls arreagdqrp
      181 aiamphafvt gahpsdserd iqvggvpsvs adlfdtlgge aplahgldyv aaghlhrpqd
      241 vagahvpiry sgspiaysfs eagspksvtl vrtddtdvag idvvpiptlr gitvlegtmd
      301 ellaapdket tasyvsvtvt ddarpermva rirevypfal vvvhrpsqap sldparalaa
      361 srdprevtee fyeavggrpl daqeralaqd vwaalrrkda s
//
LOCUS       WP_009212412             118 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Actinomyces sp. oral taxon 180].
ACCESSION   WP_009212412
VERSION     WP_009212412.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces sp. oral taxon 180
  ORGANISM  Actinomyces sp. oral taxon 180
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Actinomyces sp. oral taxon 180"
                     /db_xref="taxon:651609"
     Protein         1..118
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12880
     Region          1..92
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(24,51..52,54)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mreelveavl rvveaippgr aatygmiaaa lgtgprvvgl imrdwgggvp wwrvvnvhgt
       61 fpttirvrgv deweregiph drvrgrlvls acvverewld gvarevlanl rnsgkmsg
//
LOCUS       WP_009214495             588 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Oribacterium sp. oral
            taxon 078].
ACCESSION   WP_009214495
VERSION     WP_009214495.1
KEYWORDS    RefSeq.
SOURCE      Oribacterium sp. oral taxon 078
  ORGANISM  Oribacterium sp. oral taxon 078
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Oribacterium.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 588)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 588)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Oribacterium sp. oral taxon 078"
                     /db_xref="taxon:652706"
     Protein         1..588
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=65478
     Region          2..558
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mirkrlfslm sessrgavlq nvlwqwgall ssvlsmsivg rlleslylgr irsetlllsa
       61 allllslllr llctrraaea saragsevkq alreklyrkl talgaayhek lgsaeavqls
      121 aegveqlevy fsqylpqlfy sllapltlff flsfyclkas lalllcvpli pltillvqki
      181 akrllkkywg sytelggsfl enlqglitlk iygadgkkae emdreaerfr rmtmrvlsmq
      241 lnsiivmdli ayggtvlgmg icllefqkga vslrglltll llsadfflpv rllgslfhva
      301 mngmaasdrl fsildlpegk rgekellege teirlsdvrf sydgdrrilk gislflpdrg
      361 lsalvglsgc gkstiaglls grvrdyegqi llngtelsel seeslmrtvt lvrhdsylfr
      421 gtvrenllma spgtseqkmw dalrevrleg yllsqqgldt flsergenls ggqrqrlaia
      481 rallrdtpvy lfdeaasnid seseekimea irrlserrsv llishrlkna vqadciyrme
      541 dgriaergsh eelmrrkggy aalflaqsel esyaaglcpl segrkcya
//
LOCUS       WP_009214768             455 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Oribacterium sp. oral taxon
            078].
ACCESSION   WP_009214768
VERSION     WP_009214768.1
KEYWORDS    RefSeq.
SOURCE      Oribacterium sp. oral taxon 078
  ORGANISM  Oribacterium sp. oral taxon 078
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Oribacterium.
REFERENCE   1  (residues 1 to 455)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Oribacterium sp. oral taxon 078"
                     /db_xref="taxon:652706"
     Protein         1..455
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=50521
     Region          82..188
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          215..312
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          336..454
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(405..406,409,427..430,432)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkkkgigayw liplaglsga yfmialilsg rmmpgdrvng ydmslrsrsa lngilneyrg
       61 gehqllirdi hgkdftlrgs eidfrvdypi selpkrnsll fpkflltkes fslepeihyd
      121 eeklagiler eflstesegt rprnafltdy ipgagfrvap eqdgdildpg alkeavrkal
      181 lelspeldls eascyqkpei rrddpglqae akekndklks sitydfgnqr ltlnadtyfs
      241 wmtpgkngst qfdpakikey vaelkrrtdt sgsnrsfrta tgqlialggp ygyninqkke
      301 qeqlaadlls gkeltrepiy ttvgvsrsgp dygnsyvevd lgnqhvyvfe dgkvsletdc
      361 vsgnmslgrg tpagiyplsy kttnatlkgp dyeakvsywm pfnrgiglhd akwrgkfggk
      421 iyqhagshgc inlpfaaaqa iyqkvqqgea iichy
//
LOCUS       WP_009222772             215 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [unclassified
            Paenibacillus].
ACCESSION   WP_009222772
VERSION     WP_009222772.1
KEYWORDS    RefSeq.
SOURCE      unclassified Paenibacillus
  ORGANISM  unclassified Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="unclassified Paenibacillus"
                     /db_xref="taxon:185978"
     Protein         1..215
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23820
     Region          6..211
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdfalfrdil qtrrsireft qepvsvsdik dlidcaryap sdtnsqtwef ivvmnadkik
       61 qiedftwesl heiaarataq gkdreakllv ksfgpyataf sgapalivvl stpytskfre
      121 rifdpisfvt peiwdeeglk ssclaaqnlm laahakglas cpmtgpvlla edklrefldi
      181 padrgvnmvi alghpaispk pvprkevsei lrive
//
LOCUS       WP_009223583             290 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Paenibacillus sp. oral
            taxon 786].
ACCESSION   WP_009223583
VERSION     WP_009223583.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. oral taxon 786
  ORGANISM  Paenibacillus sp. oral taxon 786
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Paenibacillus sp. oral taxon 786"
                     /db_xref="taxon:652715"
     Protein         1..290
                     /product="formate/nitrite transporter family protein"
                     /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=30500
     Region          2..257
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mdyvkpgevl gsmietgknk anlsilqllv kgflggaila fattlaftat qqaslgivga
       61 vifpvgfvmi vllglelvtg sfaliplavm erqaspgrml ssfgwvilgh ligcavyavl
      121 ygltitkmgt dlshplvqml iqtseaktla ykqmggsgla lvtikavlcn wmvtlgvvma
      181 mtskstagki aamwlpilif faqgfehavv nmfvipagmm lgadvsmadw wlwnqipvli
      241 gnflggvvft glmlyvaqkg slrrgvaaqv agtemaepdg ralsvagerl
//
LOCUS       WP_009225534             661 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: VirB4 family type IV secretion system protein
            [Paenibacillus].
ACCESSION   WP_009225534
VERSION     WP_009225534.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 661)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 661)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..661
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..661
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=74070
     Region          56..654
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mfwrkskksv gliedsqpll dignasgvdf aapsfvreti pqdtssnqvk lddyavevgg
       61 titptryfrs fyaeissgnt wagmldslir gdhgkgdvdl aihvqpssnd reldeigrri
      121 agllsdlade kdvrkvdamr deiadlkerq krirlnvers frvsiqvivs apewkelmkl
      181 crslvqrfag ksiylrsadg qqlaalqsvl ptvkasavqk ehvlslessn vadlfpwggg
      241 slnhrsgvvi gkdrmgrpvw ldnwhpelan ynmciigrsg agktfvtlli thrsshigrq
      301 igiidwkgey gdflralgcp fielhehskh rinpydvdit eladgtrfvd ieeaansvqa
      361 lvfkmisvyd rsvltgevkv figrairqqy aeyeittdpe slyttdqtmq gqgifrtgkv
      421 rkampeligl wekmnahkse airkasellq pftrkgemss ysifdgqsti elksapifgf
      481 ainrldpeim rpiglfvter wmmerwakkh pevkklliie ecqniflded fgavwaesaf
      541 regratntgi vpvtqglevf trsqagmaai knspikiigi qealdidavr gklaltegea
      601 dflvyqarkg dmlvkvdnqs vivhvdaspy ehmlfttdpn dplyaerkry ikeraraegt
      661 a
//
LOCUS       WP_009227810             745 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Prevotella sp. oral taxon
            299].
ACCESSION   WP_009227810
VERSION     WP_009227810.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. oral taxon 299
  ORGANISM  Prevotella sp. oral taxon 299
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 745)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..745
                     /organism="Prevotella sp. oral taxon 299"
                     /db_xref="taxon:652716"
     Protein         1..745
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=84388
     Region          59..745
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mknnlldiyk tifaflsfic sfvavhaqqk rnlndtiill kevsvkpkys ltspdimqal
       61 ahqrriagst slveirpdnq riatikdalk mqpgviiqef fglndqprln irgsgiqsnp
      121 qrrgvyllqd gipvnfsdgs yvvgimdamt aryvevfkga nalrfgagtl ggalnfvsrt
      181 aqtdsttsvk leggsygtig ltfttgkrmg awdmfvasty naqkgyriyn ennrlttsln
      241 igwknqerti enrtfmhfth lyfqmpgplt ldqlltnpkq vsvgvdlpfs mgpnilrdkp
      301 hrnvdmfris nqtgvvlnak snllasvyyq yaddrfafpi vvsiphsfnn dlgatlyyny
      361 stsklqlsag mlaslgwmnr rhyinkdgke sfmfawdklh sanftafiea dyalnkqlhv
      421 vldvhgvhni rnskdvfsdp tlrpwyshms rkyryfysen stlnqhftaf nprigvvynp
      481 iqqkdiqlfa nisnsyeppt fdelvgtevt snintspkkl fsialkkqta ttfevgskgr
      541 ltqlswnvaf ynswvtneil eikdyvrglk rtenypktlh qglevglqva skphllghni
      601 gsftlgavyn ysrfifkggk ydgkylagvp qhyinssldy qhscglngsi slelkpgntp
      661 idhtntmfqp tyhvwnarlg yqfnskwhiy vemkniankr yassyvisde ihnpaipfpn
      721 ftakqltffi pgqprsifag ltwrw
//
LOCUS       WP_009228098             307 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Prevotella sp. oral taxon 299].
ACCESSION   WP_009228098
VERSION     WP_009228098.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. oral taxon 299
  ORGANISM  Prevotella sp. oral taxon 299
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Prevotella sp. oral taxon 299"
                     /db_xref="taxon:652716"
     Protein         1..307
                     /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=34674
     Region          5..250
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mkparieeld ylkgilitlv vlfhltyfat eytlakqfvy tfhmpaflvi sgwlmnieap
       61 lprfgrmitk illpyivfes gyivisalkm vavpiaelnv stflyhffis pvgpywflht
      121 liicavvykf whtifassts kqalamllti wflaqyvhii sfasgcffia gavlrrtnih
      181 itnvlspnil alialavlct npaffveesl sgiaivyvmm svmllannls phflrskvcy
      241 igertlpiyl ysplftflfk afklyfsfds trfvfaivat tcciigslcv dkvvktiing
      301 vqkvvkr
//
LOCUS       WP_009228545             342 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Prevotella sp. oral taxon 299].
ACCESSION   WP_009228545
VERSION     WP_009228545.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. oral taxon 299
  ORGANISM  Prevotella sp. oral taxon 299
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Prevotella sp. oral taxon 299"
                     /db_xref="taxon:652716"
     Protein         1..342
                     /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=38835
     Region          25..284
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mkpsqsttte qhliqnnaka glspriewld varglcmlli iydhsdsyft llnpllpynw
       61 yvanvlcafv fisgylfpth nhlivskkik sifrtlvvpy lffstlftfp kafihqqdvs
      121 iseslfnivs gqsswfical vvvellfvgl vqlfkdnkia vfivslacfi latlypepnn
      181 nywsavqali fmpflcmgwi akqnsfkisn khftlvlvlf ivlkvvgtqi hfneviapll
      241 inqpllfmvd mlvgivllif iaqkinrntf iehvgkhsli cyflcggvpl lftklfekig
      301 lgfnnapyll pliflfstfi ivvaatliqk ylgflwsskr kq
//
LOCUS       WP_009228837             150 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Prevotella sp. oral taxon 299].
ACCESSION   WP_009228837
VERSION     WP_009228837.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. oral taxon 299
  ORGANISM  Prevotella sp. oral taxon 299
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Prevotella sp. oral taxon 299"
                     /db_xref="taxon:652716"
     Protein         1..150
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16624
     Region          11..150
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdaitdllvn ygywgmllsa flagsflpfs seavmvalla akldswqlii yatignvlgg
       61 mfnywlgtfg ridwiekylh vkeeklkrtq rfmegrgawm gffafvpivg saitivlglt
      121 raniaisvts itvgkflryv llvygaslff
//
LOCUS       WP_009231180             422 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Prevotella sp.
            oral taxon 317].
ACCESSION   WP_009231180
VERSION     WP_009231180.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. oral taxon 317
  ORGANISM  Prevotella sp. oral taxon 317
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Prevotella sp. oral taxon 317"
                     /db_xref="taxon:652721"
     Protein         1..422
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47411
     Region          2..415
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mekldvvacf dwlekeekvg tlghetlrgs dvfsfefdgd wlkryadicf grdlqpftgi
       61 qyspsnnrif gcfsdalpdr wgrrlidlrm aqeqrgkgmg kptlsdwdyl kgvedslrmg
      121 gfrfkdlasg ayvnaasgya vppvlhidel lqaageieks eykhmvpeek wvqrlfqpgs
      181 smggarpkac vesgghlfla kfpsvkdein vsrwehfahl maracgisva qteivkagng
      241 qdillskrfd rnddnqrvhm assltllgfa dgdgektgkg yldivdfivs sggrkvgvdl
      301 eelyrrvafn iclgntddhf rnhafmlakg gwelspaydl npsnsryqal lidndtndsd
      361 lnrlfevhen ymlddaaarr iigdvtqnmk cweamaqdvg lsrgemvhfa erfekgmnfi
      421 lr
//
LOCUS       WP_009231626             292 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Prevotella].
ACCESSION   WP_009231626
VERSION     WP_009231626.1
KEYWORDS    RefSeq.
SOURCE      Prevotella
  ORGANISM  Prevotella
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 292)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Prevotella"
                     /db_xref="taxon:838"
     Protein         1..292
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33321
     Region          213..292
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mrklqlndlt ipivkencdv vsmdddlvlv ddlnklsdlm gpykmqclvl aicaqgsary
       61 tvdtityelq pnhimvvpag pilnsgelst nckgiaills kdfmneiimg ihelsslilf
      121 srtnpvftln aeeggemllh lsliekkmqq aghryrkdtv rsmittmiyn asdaiyrvqq
      181 ttdlkktrae aifakfikmv eqnfkkerrv swygeqlgit pkylsetvrn vskrtpnqwi
      241 dkyitlelrv qlknttksvk eiaqelnfpn qsflgkffke qvgvspsqyr kr
//
LOCUS       WP_009231706             762 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Prevotella sp. oral taxon
            317].
ACCESSION   WP_009231706
VERSION     WP_009231706.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. oral taxon 317
  ORGANISM  Prevotella sp. oral taxon 317
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 762)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..762
                     /organism="Prevotella sp. oral taxon 317"
                     /db_xref="taxon:652721"
     Protein         1..762
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=85255
     Region          53..761
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mdarlklgla fwfamtscma arpsyalsna lpsatdndst qadkvrntlp hvvnlkevnv
       61 laprqltqpt vaqalneqrl iagstslvqm splrqrlstl kdalamqpgv iiqeffglnd
      121 qprlnirgsg iqsnpqrrgv yllqdgipvn fadgsyiigv mdpmtahfve vfkganalnf
      181 gastlggain fvsptankqh gantlvkveg gsygyravaa smgyrwqtsd ahistsysaq
      241 dghrlynhnt rwsiaanygl qslngqvenr tylhftwlkf qfpgplnmqq lmdnpkqvna
      301 gvdlpfsmgp nvlrdkprrf armirvanrt girlnansdl vaavyyqyad dqfvfpitis
      361 iphsyhhdgg ltvsyrlntg khhlraglva sagqidrrty inkdglesfm fahddlqarn
      421 lalfaedlir ltsklnfvvd ahlvynerns sdrfpqpdlr pwyshmskky ryfrsqsttl
      481 nqhwtafnpr igliyspfkg edvqlfgnls rsyepptfde lvgtevttni ntspkrlyai
      541 aldkqtattl elgskgrttr fswnvaayrs wvhneilevk dyvrgikrte nypttlhqgv
      601 evglnavvad npwginagkl tlggvydfsd frfsggkyqg krlagipqhy lnlsaeyehs
      661 cglslaaqve wkpgetpidh tntmfqpayr vwnvraayal gknislyvem knvansryas
      721 syvisdeihn ppipfpnfsa kqmaffipaq prcifggitw qm
//
LOCUS       WP_009232027             290 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Actinomyces].
ACCESSION   WP_009232027
VERSION     WP_009232027.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces
  ORGANISM  Actinomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Actinomyces"
                     /db_xref="taxon:1654"
     Protein         1..290
                     /product="formate/nitrite transporter family protein"
                     /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=31454
     Region          17..257
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mpaeqdalfp gkqfistvle aletktrmtg aiahrylmra amagmivavf yivnyaivgi
       61 fsglhvgets lagigkmlga lafgpalvfi yytksellts nmmvvvigyy ykrisawrtl
      121 rvlfmclagn fmgglvfavm yhfsslvegp tgeqalhsve aklgylssas gigdlfvrai
      181 lcnfminlam lliyngfire dwskifsmim avfvfaflgf ehsvantvlf tviglthgid
      241 vlpalgnvav allgnfvggg lliggyyaya nddsrwlgrq lhkdevqage
//
LOCUS       WP_009234100              94 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Actinomyces sp. oral taxon 849].
ACCESSION   WP_009234100
VERSION     WP_009234100.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces sp. oral taxon 849
  ORGANISM  Actinomyces sp. oral taxon 849
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 94)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 94)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 94)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 94)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Actinomyces sp. oral taxon 849"
                     /db_xref="taxon:653385"
     Protein         1..94
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=9600
     Region          13..94
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mppspesppe tlsvtlryfa aaaeaagrpe erldlpagtt laglreqlag rdlemarivp
       61 icsflvnsvs tpadsltpla dgeavdvlpp fagg
//
LOCUS       WP_009237118             292 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Hoylesella loescheii].
ACCESSION   WP_009237118
VERSION     WP_009237118.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella loescheii
  ORGANISM  Hoylesella loescheii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 292)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Hoylesella loescheii"
                     /db_xref="taxon:840"
     Protein         1..292
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33302
     Region          213..292
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mrklqlndlt ipivkescdv vsmdddlvli ddlnklsdlm gphkmqclvl aicaqgsaqy
       61 tvdtityelq pnhimvvpag pilnsgemst nckgiaills kdfmneiimg ihelsslilf
      121 srtnpvftln aeegsemllh lsliekkmqq aghryrkdtv rsmittmiyn asdaiyrvqq
      181 ttdlkktrae aifakfikmv eqnfkkerrv swygeqlgit pkylsetvrn vskrtpnqwi
      241 dkyitlelrv qlknttksvk eiaqelnfpn qsflgkffke qvgvspsqyr kr
//
LOCUS       WP_009237294             223 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Hoylesella loescheii].
ACCESSION   WP_009237294
VERSION     WP_009237294.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella loescheii
  ORGANISM  Hoylesella loescheii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Hoylesella loescheii"
                     /db_xref="taxon:840"
     Protein         1..223
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24644
     Region          141..216
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mkrlvtllli wvctvtaiea qtftdhlrrr dtkthgivtv tqsaaieqlv ngkgnagkwa
       61 npnpndratp satngttnsg sattsrlpnd kremeqahkn dpnkrettqk nnalgddgdd
      121 lnipvvdtrk kvmkggykvd gyrvqafagg nsredknraq qagnrikaay pdqpiyvhfy
      181 sprwicrvgn yrsieeatrm lsaiqalgyk qavivkgkit vqy
//
LOCUS       WP_009238291             369 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Ralstonia].
ACCESSION   WP_009238291
VERSION     WP_009238291.1
KEYWORDS    RefSeq.
SOURCE      Ralstonia
  ORGANISM  Ralstonia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Ralstonia"
                     /db_xref="taxon:48736"
     Protein         1..369
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=40609
     Region          1..356
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvqhitk rfgnfvalnd vsldfkqgel tallgpsgcg kttllriiag lehadsgsih
       61 lngedasdqh vrerqvgfvf qhyalfkhmt vfenvafglr vkpraqrpse aqirakvkel
      121 lelvqldwla dryppqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 rlhddlhvts lfvthdqeea levadnvvlm nrgqveqvgs paavyntpat pfvygflgnv
      241 nlfhgrleeg eggsvlhvgd saiavpsggv dssradqava fvrpheidle ryapgaegip
      301 vtlrraltlg aiaqlelere dtddiievsl pierfraegf regetlvvrp rairvfaqgn
      361 arpvaqaav
//
LOCUS       WP_009238855             134 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Ralstonia].
ACCESSION   WP_009238855
VERSION     WP_009238855.1
KEYWORDS    RefSeq.
SOURCE      Ralstonia
  ORGANISM  Ralstonia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Ralstonia"
                     /db_xref="taxon:48736"
     Protein         1..134
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14319
     Region          1..133
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkyryaaftl veltialvia alltgaaiqt wsrhherarr taahaalvst mvelerqyah
       61 tgnssspani peyisgyhll agpcdgraaa hcievvaqpv hagtdcgali lrntgerftq
      121 igntrqpasp acwp
//
LOCUS       WP_009239049             167 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: pilin [Ralstonia].
ACCESSION   WP_009239049
VERSION     WP_009239049.1
KEYWORDS    RefSeq.
SOURCE      Ralstonia
  ORGANISM  Ralstonia
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Ralstonia"
                     /db_xref="taxon:48736"
     Protein         1..167
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=16873
     Region          8..137
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkslrlnkrv qkgftlielm ivvaivgila aialpaynny mvksklteat tlldsaraai
       61 seayanggnt fpstanapip tapasnakyv tavnytasta asqvgvvvtl gntgssqidg
      121 kllglfgvgg pdgtvswtcg tatsatatas gasqvamypy lpancqh
//
LOCUS       WP_009239050             170 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: pilin [Ralstonia].
ACCESSION   WP_009239050
VERSION     WP_009239050.1
KEYWORDS    RefSeq.
SOURCE      Ralstonia
  ORGANISM  Ralstonia
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Ralstonia"
                     /db_xref="taxon:48736"
     Protein         1..170
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=17248
     Region          15..153
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 msikhskgpr sqaggftlie lmivvaivgi laavalpvyn nymvksklte atttldaarv
       61 avneayssns gifpsasspp iitqavasna qyvtgikynn pgtssgvgvv vtlgntgnaq
      121 idghylgmfg tgkadgtvvw icataqtand sasgaavqsm ypylpaacqn
//
LOCUS       WP_009239195             426 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Ralstonia].
ACCESSION   WP_009239195
VERSION     WP_009239195.1
KEYWORDS    RefSeq.
SOURCE      Ralstonia
  ORGANISM  Ralstonia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 426)
  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 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   3  (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   4  (residues 1 to 426)
  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 426)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Ralstonia"
                     /db_xref="taxon:48736"
     Protein         1..426
                     /product="CmpA/NrtA family 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=45882
     Region          51..301
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 maapdktdal vnpinpkrrs imkaaatiag gsavalidpl vragawaags dapektelkv
       61 gfipltdcas vvmastlgld kkygikitps keaswagvrd klvsgdldaa hvlygliygv
      121 qlgiggpkkd mavlmtlnnn gqaitlsskl keagvkdgas lkavmakdkr eyvfaqtfpt
      181 gthamwlyyw laahgihplq dakaitvppp qmvanmrvgn mdgycvgepw garaiadnig
      241 ftaettqaiw kdhpekvlgt taefvqkypn taraltaavl easkfidasa snrrktaeti
      301 aaksyvntdm diildrmlgr ytnglgktwd dpdpmrfyhd gavnfpylsd gmwfltqhkr
      361 wgllkahpdy lavakqvnrv difkqaatat gtplpksdmr taklidgvvw daknpaayad
      421 gfklka
//
LOCUS       WP_009239576             381 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Ralstonia].
ACCESSION   WP_009239576
VERSION     WP_009239576.1
KEYWORDS    RefSeq.
SOURCE      Ralstonia
  ORGANISM  Ralstonia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 381)
  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 381)
  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   3  (residues 1 to 381)
  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   4  (residues 1 to 381)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 381)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 381)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Ralstonia"
                     /db_xref="taxon:48736"
     Protein         1..381
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39976
     Region          30..367
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(106..108,128..129,178,230,254)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mklkqlclaa alcalaggam taasaqevik lgfaapmsgp qaqygtdmkn gatlaveefn
       61 athpkiagke vkfqlmaedd qadpktgtav aqklvdsgik gmlghfnsgt sipasrvynq
      121 agiaqiamat apeytkqgyk ttfrmmtsdt qqgsvvgtfa vkklgyknia ivddrtaygq
      181 gladefekaa kaagativrr eftndkasdf kailtqiksk npdavfygga egqsapllkq
      241 mrelgmkstl msgemsktdd fiklagpqaa egmvaslagl pleqmpggag ykaryekrfg
      301 tpvqtyspya ydgamalmka mvaagssdpa kylpilaatn tqgvtakhya yddkgdlkdg
      361 gitvykvtgg kwtplesvgg k
//
LOCUS       WP_009240214             638 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sensor histidine kinase [Ralstonia].
ACCESSION   WP_009240214
VERSION     WP_009240214.1
KEYWORDS    RefSeq.
SOURCE      Ralstonia
  ORGANISM  Ralstonia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 638)
  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 638)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20493667
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Ralstonia"
                     /db_xref="taxon:48736"
     Protein         1..638
                     /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=68642
     Region          42..307
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          291..631
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 msptdghpdl appargrgwr vavalamaac caaagwgaya valqryvatr aeeagqrttf
       61 haqnlrstla ryeslprlaa lehvlhvalq enphagdavt rraanaylke vqaatdlaaa
      121 hlinttglti aasnwdlpts fvgqnyafrp yfveamregl grfygvgntt getgyfvaap
      181 vrednkpigv vvvkvnldaf eatlsrsgdt vllvdrhgvi flssvpewky rtlgtlnadq
      241 raaldatrqy aphiltplgm ndgraasvpf sadhppqtvr valpgksvst lrvqyrpvgl
      301 lgwqvavlid prdeqrtalv agasaafama lifavlvalr lrqrrreeqh raraalrevq
      361 rdleariaqr taeltsanta lagkvealda aqrilretrd aavqagklav lgqmaagith
      421 elnqpltalt tlsdnanqla ergridevrg nlthisqlae rmgrivshik afsrkgdaar
      481 aavsvdeair qalmlvetrr rqagvtviad pvpadlavwa navrleqvlv nlirnaidat
      541 aeapaaesst vrvsvepiek wvritvrdfg pgipadvlpr lfepffttkd dgqglglgla
      601 islaiiedfg grlegrnagd daggaefiie lervvkpt
//
LOCUS       WP_009242381             386 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [[Ruminococcus] torques].
ACCESSION   WP_009242381
VERSION     WP_009242381.1
KEYWORDS    RefSeq.
SOURCE      [Ruminococcus] torques
  ORGANISM  [Ruminococcus] torques
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Mediterraneibacter.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="[Ruminococcus] torques"
                     /db_xref="taxon:33039"
     Protein         1..386
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43923
     Region          1..276
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          273..362
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkfihlsdlh igkhlyhynm kedqehilee vigyteklrp davviagdiy dksvpsaeav
       61 avfddfltrl ssvspqvsil iiagnhdsaq rldyasrllg srgiyiagka petekehlkk
      121 vvlkdeygpv nfyllpflkp gyvrllcene tpgsyteald avlrredidf sernvlvshq
      181 fytgngetpe tcdselfsvg gidnvdisai srfdyaalgh lhkaqrvgae hirycgtllk
      241 ysvseadlek slhlvtigqk keavtiekfp lhplrdvqkv rgclsgilss adpkkrddyv
      301 svtltdeidp yrpkeqlekv ysrilevrtd nertrkklef kdedirmenp letfsdfyee
      361 mhgrkmslee aemmtqifdd vkgeer
//
LOCUS       WP_009241693             201 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Ralstonia].
ACCESSION   WP_009241693
VERSION     WP_009241693.1
KEYWORDS    RefSeq.
SOURCE      Ralstonia
  ORGANISM  Ralstonia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Ralstonia"
                     /db_xref="taxon:48736"
     Protein         1..201
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21630
     Region          <45..168
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlrlslqsgl lraltrrads rafplvvaga alaaelsmsv pfasllmaav llaprrwvsi
       61 atlaslgaav galvlylvfh hlgwnrlfaa ypdvvrstaw rdathwlehy gvvslsviaa
      121 lpvpltpalm faaisrlpva eviaalwlgk lakyhvyawl asrfpdrlvr hgrrhvdtlr
      181 avlgngtkad ggttptrggr r
//
LOCUS       WP_009243600             382 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator
            [Mediterraneibacter].
ACCESSION   WP_009243600
VERSION     WP_009243600.1
KEYWORDS    RefSeq.
SOURCE      Mediterraneibacter
  ORGANISM  Mediterraneibacter
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 382)
  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 382)
  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
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 382)
  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   5  (residues 1 to 382)
  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   6  (residues 1 to 382)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 382)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 382)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Mediterraneibacter"
                     /db_xref="taxon:2316020"
     Protein         1..382
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42331
     Region          12..56
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          81..370
                     /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 mkiynptdig drnklmilrl ikvydgisrq eiskrmhlsa pavsnnvaal iengivyeng
       61 cddtslgrkp rqlsykgdly yvisvelmpk kvragiadly gevqqwteke iivengvdev
      121 lgqldsaide llekrkkdvd viaiavgvpa ltgqndlndl fgtylpewkn vdlkehilqk
      181 ynveaiivnd velaligere rgvgkkqtni vyikygegfa araivdgyll kgnnmaagel
      241 gyylesleem tdefvcpgrf ekkvcqnifs ecgeknglsd lilraeqgde aadaivkkii
      301 rkiavviant vlmlnsemvi lggdseifte eniveikkil ekvcpfvpev vtsklgadap
      361 iiggikvald yaeeqiimlw ks
//
LOCUS       WP_009208931             306 aa            linear   BCT 20-JAN-2025
DEFINITION  uracil-DNA glycosylase [Aurantimonas manganoxydans].
ACCESSION   WP_009208931
VERSION     WP_009208931.1
KEYWORDS    RefSeq.
SOURCE      Aurantimonas manganoxydans
  ORGANISM  Aurantimonas manganoxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Aurantimonas.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Lee,D.H., Liu,Y., Lee,H.W., Xia,B., Brice,A.R., Park,S.H.,
            Balduf,H., Dominy,B.N. and Cao,W.
  TITLE     A structural determinant in the uracil DNA glycosylase superfamily
            for the removal of uracil from adenine/uracil base pairs
  JOURNAL   Nucleic Acids Res 43 (2), 1081-1089 (2015)
   PUBMED   25550433
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Zharkov,D.O., Mechetin,G.V. and Nevinsky,G.A.
  TITLE     Uracil-DNA glycosylase: Structural, thermodynamic and kinetic
            aspects of lesion search and recognition
  JOURNAL   Mutat Res 685 (1-2), 11-20 (2010)
   PUBMED   19909758
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Stivers,J.T. and Drohat,A.C.
  TITLE     Uracil DNA glycosylase: insights from a master catalyst
  JOURNAL   Arch Biochem Biophys 396 (1), 1-9 (2001)
   PUBMED   11716455
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Pearl,L.H.
  TITLE     Structure and function in the uracil-DNA glycosylase superfamily
  JOURNAL   Mutat Res 460 (3-4), 165-181 (2000)
   PUBMED   10946227
REFERENCE   5  (residues 1 to 306)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The alpha/beta fold uracil DNA glycosylases: a common origin with
            diverse fates
  JOURNAL   Genome Biol 1 (4), RESEARCH0007 (2000)
   PUBMED   11178247
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Aurantimonas manganoxydans"
                     /db_xref="taxon:651183"
     Protein         1..306
                     /product="uracil-DNA glycosylase"
                     /EC_number="3.2.2.27"
                     /GO_function="GO:0004844 - uracil DNA N-glycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=32882
     Region          <16..>125
                     /region_name="PRK05035"
                     /note="electron transport complex protein RnfC;
                     Provisional; cl47132"
                     /db_xref="CDD:481472"
     Region          107..301
                     /region_name="Udg4"
                     /note="Uracil-DNA glycosylase [Replication, recombination
                     and repair]; COG1573"
                     /db_xref="CDD:441181"
ORIGIN      
        1 mamnaephpi dreaaialle wyraagvdav tgehprdrfa etqaeiaark arrgqpagva
       61 paatgepprp aqearvapar tpqpaeepgf papriavpdd iavadarera rsattlaelr
      121 aalddfdgcn lrisarstvf gdgsetadvm lvgeapgree dtagvpfvgr sgqllnrmle
      181 siglereavr vtntvpwrpp gnrpptpaet qiclpfvqrh ielvapkilv clgspsakai
      241 lgaqegilrv rgrwttysfg leqcdaidav amlhpayllr qpaqkrlawr dlialrerla
      301 qkstag
//
LOCUS       WP_009248847              82 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [[Clostridium] scindens].
ACCESSION   WP_009248847
VERSION     WP_009248847.1
KEYWORDS    RefSeq.
SOURCE      [Clostridium] scindens
  ORGANISM  [Clostridium] scindens
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 82)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 82)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 82)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 82)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="[Clostridium] scindens"
                     /db_xref="taxon:29347"
     Protein         1..82
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=9185
     Region          3..81
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mskifyygal reitgrkeev fdihdvkgcl asirvkygrl aykearrsli tlngisivsl
       61 dnyrtkvkpe devrfltvcg gg
//
LOCUS       WP_009249118             386 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [[Clostridium] scindens].
ACCESSION   WP_009249118
VERSION     WP_009249118.1
KEYWORDS    RefSeq.
SOURCE      [Clostridium] scindens
  ORGANISM  [Clostridium] scindens
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="[Clostridium] scindens"
                     /db_xref="taxon:29347"
     Protein         1..386
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43774
     Region          1..276
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          273..362
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrffhlsdlh igkqlhrynl redqeailee vvayakdlrp daiiiagdiy dksvpsaeav
       61 avfdefltsl seitpaipll iisgnhdsaq rldyasdilk nhqiylagta prtegehirk
      121 vtlndeygev dfyllpflkp syvrnvfpee ppqtygdsva elirreeidy cgrrnvlish
      181 qfytgnelpk tcdsetfsvg gidnvdigav kafdyvalgh lhgaqcvgmp hicycgtllk
      241 ysvsesgqek altlvtlsqk gappkaerla lhplrdvkkk rgnlaeileg anekerddyv
      301 sitltdevdp ykpkeqleev fdrilevkad ntrtrnklre mdeelvlkdp letfcdfyqe
      361 mqgrqlaqee leimkkmfde aegeer
//
LOCUS       WP_009251186             199 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Eisenbergiella tayi].
ACCESSION   WP_009251186
VERSION     WP_009251186.1
KEYWORDS    RefSeq.
SOURCE      Eisenbergiella tayi
  ORGANISM  Eisenbergiella tayi
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Eisenbergiella.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Eisenbergiella tayi"
                     /db_xref="taxon:1432052"
     Protein         1..199
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=23617
     Region          16..193
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mvkeeyvrni fkkhggvmrt kelseqgiyy rrlrtlieeg kvekirygyy qwqddkafse
       61 asivvslfpe gilcmetall yydytdripd ewhiavdnrs grtrffiehp kvkphfikqd
      121 rldigksege idgikvniyd rervicdclr hinrmdgeif nkaikryvtd srkdiarlme
      181 yakklgvedk vrrtvaiwl
//
LOCUS       WP_009251563             175 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Eisenbergiella tayi].
ACCESSION   WP_009251563
VERSION     WP_009251563.1
KEYWORDS    RefSeq.
SOURCE      Eisenbergiella tayi
  ORGANISM  Eisenbergiella tayi
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Eisenbergiella.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Eisenbergiella tayi"
                     /db_xref="taxon:1432052"
     Protein         1..175
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18335
     Region          3..158
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 metmkaiakr kstrafnpek giakadldai laagcaapvg agdysslhlt iiqskemldk
       61 inkavqaafk tdrdvlygap vlvlvsssep kfpniqyanv gcvmenmlla atdrgvdniy
      121 lwgaanavaq mpelrkelgi pegftpisga algyaaesss aekelgitla anyvs
//
LOCUS       WP_009252750             418 aa            linear   BCT 20-JAN-2025
DEFINITION  galactokinase [Eisenbergiella tayi].
ACCESSION   WP_009252750
VERSION     WP_009252750.1
KEYWORDS    RefSeq.
SOURCE      Eisenbergiella tayi
  ORGANISM  Eisenbergiella tayi
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Eisenbergiella.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   McAuley,M., Kristiansson,H., Huang,M., Pey,A.L. and Timson,D.J.
  TITLE     Galactokinase promiscuity: a question of flexibility?
  JOURNAL   Biochem Soc Trans 44 (1), 116-122 (2016)
   PUBMED   26862196
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Holden,H.M., Thoden,J.B., Timson,D.J. and Reece,R.J.
  TITLE     Galactokinase: structure, function and role in type II galactosemia
  JOURNAL   Cell Mol Life Sci 61 (19-20), 2471-2484 (2004)
   PUBMED   15526155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Eisenbergiella tayi"
                     /db_xref="taxon:1432052"
     Protein         1..418
                     /product="galactokinase"
                     /EC_number="2.7.1.6"
                     /GO_function="GO:0004335 - galactokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0005534 - galactose binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0046835 - carbohydrate phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=46361
     Region          29..396
                     /region_name="GalK"
                     /note="Galactokinase [Carbohydrate transport and
                     metabolism]; COG0153"
                     /db_xref="CDD:439923"
ORIGIN      
        1 mlkitdtfkq sllevygeke nscerfmalt kkykeyfhme epeyftspgr melignhtdh
       61 nggkvlaasi qmdtiaaaga nrtetvtils egyeqpfmln leeletipgd egtlsllagi
      121 fqgcraygfh vhgfqacist nvlsaagvss sasfemlica iinyyfnenk mscidyarig
      181 ryaenhywnk qsglmdqlac aaggmifldf sdselpcver mesksilegy diilvntgkg
      241 hgdlsrdyse ipsemkkvaa qmgktvlsea slplllkklp mirencgdrs flrslhfyee
      301 nnrvdkakaa linrdtkell elinesgnss wkylqnchip sdtteesvcv alalselfiq
      361 ntgrgacrvh gggfagvils iipsgasqdy irfmseymgg knifrmslrd tgaihlkq
//
LOCUS       WP_009253912             163 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Eisenbergiella
            tayi].
ACCESSION   WP_009253912
VERSION     WP_009253912.1
KEYWORDS    RefSeq.
SOURCE      Eisenbergiella tayi
  ORGANISM  Eisenbergiella tayi
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Eisenbergiella.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 163)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 163)
  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 163)
  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 163)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Eisenbergiella tayi"
                     /db_xref="taxon:1432052"
     Protein         1..163
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18618
     Region          70..159
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(89,108..109,127,130,138..139,151,156)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mkkinfvald sstlqwlrqv llerrtesea aaelyrgvee lisgqldslm lepgssvsvl
       61 andgltcgdl tiharsrqvl rggkeiqltp kefdilyfla rnrgivftke qiyqaiweed
      121 yyttdsnima firklrkkie pnpdapeyil tiwgigykfn dkl
//
LOCUS       WP_009255434             289 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Eisenbergiella tayi].
ACCESSION   WP_009255434
VERSION     WP_009255434.1
KEYWORDS    RefSeq.
SOURCE      Eisenbergiella tayi
  ORGANISM  Eisenbergiella tayi
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Eisenbergiella.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 289)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 289)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Eisenbergiella tayi"
                     /db_xref="taxon:1432052"
     Protein         1..289
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33834
     Region          22..105
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          131..288
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mktnldtire mmdyiekhle erldldslcr eagysryhls rmfsvisgfs vhtyiqrrrl
       61 teaarllvft dkpvmeialf agyetqqsft igfkamykcs prafrrkkef fplqlkmtvd
      121 gsgklrgdrm mdiqmveggr mllagyrknt rfgfnvigqc wkkmhagkgs ipdrinrefl
      181 vglndyarwd tdsekqpvfd yyaaseveri galpkgmegr elpatkyivf cfrgikedsm
      241 qpvadyiyre wfpqstcrln enarydfvry geetdengrs rieywvpvl
//
LOCUS       WP_009256260             413 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Eisenbergiella tayi].
ACCESSION   WP_009256260
VERSION     WP_009256260.1
KEYWORDS    RefSeq.
SOURCE      Eisenbergiella tayi
  ORGANISM  Eisenbergiella tayi
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Eisenbergiella.
REFERENCE   1  (residues 1 to 413)
  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 413)
  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
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 413)
  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   5  (residues 1 to 413)
  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   6  (residues 1 to 413)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 413)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 413)
  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 11448795
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Eisenbergiella tayi"
                     /db_xref="taxon:1432052"
     Protein         1..413
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45111
     Region          <13..>58
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          79..401
                     /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 mltsrkpkni kyhnqrlila llrsrevmta gelaeqahls vptitkilae lqarglvrsm
       61 gkgnsteegg kkpelfalng ahryvisita gserikcall dltckvldkr slpytdgssy
      121 elcmddisal vlaaceagkl eekeicgiai gfegivdapr gilrfpihnq awgrdlpvke
      181 elqarlpgfa gitinngsrf agyaelsehp eyascrvvti stgtstggcv lengvlmqga
      241 ngfigelghi tvreteekac acgnkgcfet avspdalcgy mqelekafpr ekepaadrsg
      301 scdyekilrl aakgdacark aveksidyys ilirnimlly dphiiviqgi ytlagdfflk
      361 rlqelvkqsp ffhipqglsi vfsgldfdra adlggalysv dryfegeqlf eei
//
LOCUS       WP_009257240             190 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Flavonifractor plautii].
ACCESSION   WP_009257240
VERSION     WP_009257240.1
KEYWORDS    RefSeq.
SOURCE      Flavonifractor plautii
  ORGANISM  Flavonifractor plautii
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Flavonifractor.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Flavonifractor plautii"
                     /db_xref="taxon:292800"
     Protein         1..190
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20635
     Region          3..190
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 manrrlivgv sgasgapvti ellqqlqtek dlevhlicsk wglatlehea gvtrqdlegl
       61 ctraydeedr gaapasgsfs avgmavvpcs mktlagivsg ysdslllraa dvtlkerrpl
      121 vlmprecpls tlhlryltav selgavvvpp vpawydhprt mevvnrqiaa rivrmlplgr
      181 qlpwewrgls
//
LOCUS       WP_009257252             142 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Flavonifractor
            plautii].
ACCESSION   WP_009257252
VERSION     WP_009257252.1
KEYWORDS    RefSeq.
SOURCE      Flavonifractor plautii
  ORGANISM  Flavonifractor plautii
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Flavonifractor.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 142)
  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 142)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Flavonifractor plautii"
                     /db_xref="taxon:292800"
     Protein         1..142
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16446
     Region          25..80
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
     Region          <56..132
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 mrfhrwnsqq klkhffslpn eifllglahg elavycylky lenrkthqcw psywnigkav
       61 gmsentvrky vamleargli ttayttmrar dgrpmnghlm yticpfhevv ndhyrvqmea
      121 lelqarqksv aalasqkevp aq
//
LOCUS       WP_009259238              77 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyl carrier protein [Flavonifractor].
ACCESSION   WP_009259238
VERSION     WP_009259238.1
KEYWORDS    RefSeq.
SOURCE      Flavonifractor
  ORGANISM  Flavonifractor
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae.
REFERENCE   1  (residues 1 to 77)
  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 77)
  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 77)
  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   4  (residues 1 to 77)
  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 10011594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Flavonifractor"
                     /db_xref="taxon:946234"
     Protein         1..77
                     /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=8426
     Region          1..76
                     /region_name="acpP"
                     /note="acyl carrier protein; Provisional; PRK00982"
                     /db_xref="CDD:179197"
ORIGIN      
        1 mifeklaall seqfgvdvds itmdtsfedl gadsldivem tmaveeefgl edmdeedlsg
       61 istvadlvry lkskled
//
LOCUS       WP_009259485             138 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Eubacteriales].
ACCESSION   WP_009259485
VERSION     WP_009259485.1
KEYWORDS    RefSeq.
SOURCE      Eubacteriales
  ORGANISM  Eubacteriales
            Bacteria; Bacillati; Bacillota; Clostridia.
REFERENCE   1  (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   2  (residues 1 to 138)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 138)
  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 138)
  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 138)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Eubacteriales"
                     /db_xref="taxon:186802"
     Protein         1..138
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15527
     Region          47..132
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(66,85..86,104,107,115..116,124,129)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mgkllilsvt ngeeqildri kdflaeepgi evveppaakh tltipglelh lrkqtvkwqg
       61 qplhlthlef ftlaylarhp gwiftqeqiy eavwhefped cgaavvniis qlrrkmgpgn
      121 pirtvphsgy kfelpsad
//
LOCUS       WP_009259629             180 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Flavonifractor].
ACCESSION   WP_009259629
VERSION     WP_009259629.1
KEYWORDS    RefSeq.
SOURCE      Flavonifractor
  ORGANISM  Flavonifractor
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae.
REFERENCE   1  (residues 1 to 180)
  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 180)
  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   3  (residues 1 to 180)
  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   4  (residues 1 to 180)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 180)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Flavonifractor"
                     /db_xref="taxon:946234"
     Protein         1..180
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=20027
     Region          3..179
                     /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"
ORIGIN      
        1 mekiivafes ektalrvkel legggaaacl vcrtadqvrr ainklpvpav vcgyklgdqt
       61 aelffedlpp scamlvlahq drldllgndd ifrlpspvsr gdllaavrll lqvgrrlery
      121 grpchsgedr rlidrakall mdrhgiteeq ahyylqkksm dsrtklaqta rlvldsktme
//
LOCUS       WP_009259659              98 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Flavonifractor].
ACCESSION   WP_009259659
VERSION     WP_009259659.1
KEYWORDS    RefSeq.
SOURCE      Flavonifractor
  ORGANISM  Flavonifractor
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Flavonifractor"
                     /db_xref="taxon:946234"
     Protein         1..98
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10389
     Region          2..98
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(3..4,22..23,31,34,36..37,39,42..43,45,52,57,64)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(22,52..53,55,78)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mnfyervyel vrripagkca sygqlalmlg nprasravgh amracrtpgv pchrvvradg
       61 sttpafgpgv qramleaegv pftadgrvel ggcrwdga
//
LOCUS       WP_009259991             608 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Flavonifractor
            plautii].
ACCESSION   WP_009259991
VERSION     WP_009259991.1
KEYWORDS    RefSeq.
SOURCE      Flavonifractor plautii
  ORGANISM  Flavonifractor plautii
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Flavonifractor.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 608)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Flavonifractor plautii"
                     /db_xref="taxon:292800"
     Protein         1..608
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=67539
     Region          33..603
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mlgtkkkeet lpvneallnv itpmgleikr nslvigenmg kvygavrypq kvemgwlski
       61 tnipstivsv gitpidnstl isalsksivq qrgaadsakd pltrqraeka aedgehimqk
      121 idqegetvam msltvmpvaq deaafskicr rvesafsvqk ckvrtlanlq kegfqsispt
      181 ypangtvdsi vsriipmstf vggfpfassg ysdgrgyyfa kdssgglvil dpwtrgndrt
      241 nssfvvmgva gigkstvvkh imlseymkgt kilcidpese ykdmcrnlng swlnagggkn
      301 grsnllqirp aprddedetd klytdegngm sdmalhiktl eiifslylps ltdmqkavlk
      361 qtvielynqf gifwdtdirq lkaadfpime dlhslietka eanpdnpvfr dlamllydaa
      421 kgsdsflwng hstleadshf vcldthslqn aadnikrtqy fnlltwcweq msnnrgervl
      481 lvcdeaylmi dpqvpqslaf lrnvekrsrk yesalaiish svvdflapei kmygqalldi
      541 pcykilmgcd gknlqettdl ynltdaeqel leskrrghal flvgskrlhv nfeipaykfa
      601 ymgkaggr
//
LOCUS       WP_009260615             683 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Flavonifractor plautii].
ACCESSION   WP_009260615
VERSION     WP_009260615.1
KEYWORDS    RefSeq.
SOURCE      Flavonifractor plautii
  ORGANISM  Flavonifractor plautii
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Flavonifractor.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 683)
  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   3  (residues 1 to 683)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Flavonifractor plautii"
                     /db_xref="taxon:292800"
     Protein         1..683
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=74487
     Region          6..678
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mgngndsile aylfetnsll eqldslvlaa eekdsfseed vntifrimht ikgssammey
       61 sslmtiahra edlfaivrdk smeivpealr palfdllfqi idffrgeier iengqpltqt
      121 idsllqkvns fiqqiqngaa aapaevppaa peapapadsg paavpgfpya lqiffdegag
      181 menlrafmlv stirdggsed sfqylpadve hnpdtaaqiv dsgftlyfrd qaqrdaaiha
      241 vtnagsvrty qaidqeappp vapehqsppa ekpaapassr eapkaesapq phreslisvn
      301 lskldqlsav vgeivitesm vtsspelkgl rldeftksar qlrkltdelq dvsmslrmvp
      361 vsatfqkmhr ivrdmckkln kqakltlvge eteidktivd sigdpimhiv rnsmdhgiee
      421 dvqdriragk dpvgeitlsa rqtgseviie irddgqgvnd eavlrkavkn glaspdveys
      481 hreilnflms pgfstntevt efsgrgvgmd vvkqnveavg gtvsltselg kgmtttlkip
      541 lttaimdgme vsvggsifti pihnirqsfk ihsdqlvhda aggeifkcmg sfypvvrmre
      601 lyqieegctq vedgiliwle agelsyclfv dellgeqqvv vkplpsylns fnikrsgiag
      661 ctilgdgnis iildvanlys pfr
//
LOCUS       WP_009261498             613 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Flavonifractor
            plautii].
ACCESSION   WP_009261498
VERSION     WP_009261498.1
KEYWORDS    RefSeq.
SOURCE      Flavonifractor plautii
  ORGANISM  Flavonifractor plautii
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Flavonifractor.
REFERENCE   1  (residues 1 to 613)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 613)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Flavonifractor plautii"
                     /db_xref="taxon:292800"
     Protein         1..613
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=69138
     Region          42..610
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 maksqkmqkk paekpaqlfq pkdfldriap aavkfntdsy vlgglyrcvl alrgypavte
       61 elallahvcn ragialhlyt rqvtaaeeea iyhkavnklr ldrsnqdnlk rsvtaeanlq
      121 dvaaiiaaar qnreplihca vflelaaksp eelrrlrdev gaeltrakls adplllrqre
      181 gflsanpvgr nalgarferv lpasstanly pinysgrsdp hgfyigndhy gsdvlldldr
      241 rtpdktnssv lilgnsgegk syllklllcn llesgktvic ldpeqeltrl cdkldgcyad
      301 lmggqyrinf leakrwdvgd drdddptapn afrqrsplsq hisflkdffr aykpftyqqi
      361 dalelmlerl yrmrgisdkt dfsalepedw piaedlyavl enayehydwe dsplyprell
      421 relllglhsm crgaesvyfn gytnitsarf lvfgvkdlih anssvkdall fnllsylsdr
      481 lltqgntvaa ldelylwlsn lttieyirnc lkrvrkrnsa lilasqnled fdvqgvrelt
      541 rplfaipthq flfhggkvdr kfymdnlqme saeydlissp qrgvclfksg adrnlldvha
      601 pphkhvlitg gdg
//
LOCUS       WP_009261356             293 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Flavonifractor plautii].
ACCESSION   WP_009261356
VERSION     WP_009261356.1
KEYWORDS    RefSeq.
SOURCE      Flavonifractor plautii
  ORGANISM  Flavonifractor plautii
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Flavonifractor.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Flavonifractor plautii"
                     /db_xref="taxon:292800"
     Protein         1..293
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31291
     Region          168..249
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 matytispls aptrslnias sasitngtqv niyatsgsnd qnwvvdslts tsrqyikhfs
       61 nqayalnayr sgtnwnctlr kasgnidgyv iltkvanktn vytirlseys nryltadgtg
      121 nsakcswras tggteqqwkf tkvstggsgs ggatnvseir akfqkvgnyd gvnglqcvdi
      181 vrwyidtytt lkstsghgkd lvanlannyg laidstpkap gifsvaggys kwgssgsqyg
      241 htgivvsvdt knkkatviht gnsldgknpn swvdtysypa tgvtfvylgn ylk
//
LOCUS       WP_009264883             219 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Anaerostipes
            hadrus].
ACCESSION   WP_009264883
VERSION     WP_009264883.1
KEYWORDS    RefSeq.
SOURCE      Anaerostipes hadrus
  ORGANISM  Anaerostipes hadrus
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Anaerostipes.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Anaerostipes hadrus"
                     /db_xref="taxon:649756"
     Protein         1..219
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=24738
     Region          1..>204
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mslevkikkk lkeftlesel nvetgctglm gpsgsgksit lkciagveta dsgrivldgk
       61 ilydsekkid lppqkrkigy lfqgyalfpn mtieeniktg lrakgfpkde ieqktndmmk
      121 rfhieelakr yprqisggqk qrtalarmlv cepevilmde pfsaldeylr eqmqdelsnm
      181 lamldkpail vshsskeven lcdkkyhiqr ghmeratll
//
LOCUS       WP_009265435             379 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Anaerostipes hadrus].
ACCESSION   WP_009265435
VERSION     WP_009265435.1
KEYWORDS    RefSeq.
SOURCE      Anaerostipes hadrus
  ORGANISM  Anaerostipes hadrus
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Anaerostipes.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Anaerostipes hadrus"
                     /db_xref="taxon:649756"
     Protein         1..379
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44187
     Region          1..269
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          265..358
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkilhlgdlh lgkrvneism iedqkfildq ivtlvkeeki dvillcgdiy dkaiptieai
       61 hlldefleel sdlkvkvlmi sgnhdsserl sfgrnlfkrs nlyiasqfnq eiekitiked
      121 gyninfymlp fvkpayinhv lkiqtetyee cfkhlmeqvk inedetnill ahqfvtvgkn
      181 spelsdsets slggidnidy rlfdafdyva lghihkpqam gremvryags ilkysfseir
      241 kdkqatilti sknkqislsh hllkplrdmr emecslesll krkceignee dymhviltde
      301 eqildaigkv rtvypnvmqi sfknrrhmmq yetiqmkenq iadqnpmelf eqfykmqnhi
      361 dldekraqma isifeevir
//
LOCUS       WP_009268254             178 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Mediterraneibacter
            glycyrrhizinilyticus].
ACCESSION   WP_009268254
VERSION     WP_009268254.1
KEYWORDS    RefSeq.
SOURCE      Mediterraneibacter glycyrrhizinilyticus
  ORGANISM  Mediterraneibacter glycyrrhizinilyticus
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Mediterraneibacter.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Mediterraneibacter glycyrrhizinilyticus"
                     /db_xref="taxon:342942"
     Protein         1..178
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20039
     Region          3..169
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mnvnecirsr rsirkyqsrl vdhsiidsiv sdasyspswk ntqitryiai edlsiletia
       61 eqftpdynsn iikqipvlia vtfvkgrcgf erdgsyttkk kdrwqmfdvg aacqtfclsa
      121 kdhglgtvim gvfdedgite llqlpddqel aalialgypd idpeapkrkt tdillqyr
//
LOCUS       WP_009270172             579 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein/permease
            [Bacillota].
ACCESSION   WP_009270172
VERSION     WP_009270172.1
KEYWORDS    RefSeq.
SOURCE      Bacillota (firmicutes)
  ORGANISM  Bacillota
            Bacteria; Bacillati.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 579)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 579)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Bacillota"
                     /db_xref="taxon:1239"
     Protein         1..579
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=65654
     Region          2..557
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 midkrllkem petkpyimkq vamqwfsllc nivfvallan vlshifyktv neqllllttc
       61 gvilcialra vcvrkaslys heaschvreq lrmrlfkkll emksgytesa ptselvqlsv
      121 egidqleiyf grylpqffys mlapvtlfli lvwmdvksal vlllcvplip msiiavqkfa
      181 kkllskywss yttlgdsfle nlqglttlki yqadewkqqe mnreaenfrk itmkvltmql
      241 nsvsvmdlia yggaalgsiv ailgfqngsl slfqvicivl lsseffiplr llgsffhiam
      301 ngiaasdkif rildkpqkqa eqkqwkaetv diqlrdlsfs ydeqrtilkh vymqlkpgqf
      361 taivgesgsg kstiarliag iikdyhgqll iadtqrrdid ddafyqsfly vshqpfifkg
      421 svrenlaiak dslseeamle alrkvalldf vmeqggldme lqeqgnnlsg gqkqrlsiar
      481 allaqrdvyi fdeaasnida esedaivsvi hklaetktvi mithrlksik dcdqiyvidq
      541 gtcqehgrhe ellrlrgtya rmyekqqele amegaeqya
//
LOCUS       WP_009270362             976 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chromosome segregation protein SMC [Bacillota].
ACCESSION   WP_009270362
VERSION     WP_009270362.1
KEYWORDS    RefSeq.
SOURCE      Bacillota (firmicutes)
  ORGANISM  Bacillota
            Bacteria; Bacillati.
REFERENCE   1  (residues 1 to 976)
  AUTHORS   Cobbe,N. and Heck,M.M.
  TITLE     The evolution of SMC proteins: phylogenetic analysis and structural
            implications
  JOURNAL   Mol Biol Evol 21 (2), 332-347 (2004)
   PUBMED   14660695
REFERENCE   2  (residues 1 to 976)
  AUTHORS   Jessberger,R.
  TITLE     The many functions of SMC proteins in chromosome dynamics
  JOURNAL   Nat Rev Mol Cell Biol 3 (10), 767-778 (2002)
   PUBMED   12360193
REFERENCE   3  (residues 1 to 976)
  AUTHORS   Harvey,S.H., Krien,M.J. and O'Connell,M.J.
  TITLE     Structural maintenance of chromosomes (SMC) proteins, a family of
            conserved ATPases
  JOURNAL   Genome Biol 3 (2), REVIEWS3003 (2002)
   PUBMED   11864377
REFERENCE   4  (residues 1 to 976)
  AUTHORS   Strunnikov,A.V. and Jessberger,R.
  TITLE     Structural maintenance of chromosomes (SMC) proteins: conserved
            molecular properties for multiple biological functions
  JOURNAL   Eur J Biochem 263 (1), 6-13 (1999)
   PUBMED   10429180
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11493846
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..976
                     /organism="Bacillota"
                     /db_xref="taxon:1239"
     Protein         1..976
                     /product="chromosome segregation protein SMC"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003682 - chromatin binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0030261 - chromosome condensation
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=110689
     Region          2..962
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
ORIGIN      
        1 mflkrielqg fksfadksii tfdsdvigiv gpngcgksni ndairwvlge qsvkslrgnn
       61 msdvifsgst arkavnmaev tlvfdnsrhi mnvefeevev trrlhrtsge geyfinkapc
      121 rlkdivnlvm dtglgrdsls iisqgnisaf adakpedrra lfeeaagvak ykkrknesls
      181 klnrtqdnls rlediimele rqvnplkrqa kkaevylekk kqlevievsv lvdeieklse
      241 qidmlkkkaf dldsqkamhe ttiqvedvkn selrnemyql drevnklqeq yaklseesrm
      301 letrkiemde krkyalefas naekakelka mmeeahyeye drskrlknle tdialqkeaa
      361 arlehdvsyc tqenaqatsi lnrlenrrav lenlakqpfn hqqavksvld aglngilgvv
      421 sqlfkplmny etaisnalgg alyhivtvde eaarhaitfl kknqsgratf lplpvmkpry
      481 mqkehrmlae nsvgflgvas efvendtqfd tlrdalfgnv vitdnlihan aiakllrfqy
      541 kivtlegdiv nrggsmtggk grnnstplti qkelnqvlqs legqqmkveg lknqlyalqa
      601 kkeqnsanlv qmqissaqld pivkakwaky drlksdyeqi apkedldkae lleddivvkl
      661 snvhsridev sssmkskrer rmkagsever kdaqirqlrr dlnilqneqr evevaqakae
      721 tklettlerl sstyemtfey aqsqkaeidi vearkqvvil rqeisslgnv nldapqeyke
      781 vserfeflsr qrddlmaakd kileaidemd dimvkqfqem fdkinaqlnd vfralfgggk
      841 arlfmvdped vlntgididv qppgktvqni rlfsggeksl iaicvlfsil kartmplcif
      901 deveaaldqa nverfakyia qfrgesqfiv vthrpgtmaq cdalygvtmq qngvsqllkv
      961 klqdainmid keevka
//
LOCUS       WP_009274911             416 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: exonuclease SbcCD subunit D [Parabacteroides].
ACCESSION   WP_009274911
VERSION     WP_009274911.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..416
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46093
     Region          4..291
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          289..395
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 malklihtad whlgqtffgy dreaeheafl gfltnllver qtdvlliagd vfdvtnpsag
       61 aqrrfyrflr eanrlnpglq iviiagnhds airleapnpl leelntsivg ivgrtdsgei
      121 dlaslvvplr nragerealc lavpflrqgd ypavpegepd syvagigrmy rrlyayadar
      181 rnpgeaival ghlhatgael seddrserai mgglesvsad tfdagiayta lghihkaqri
      241 ggreavryag splpmsfsek nyrhqviave ieegsvteie aigiprvadl mripdsplpp
      301 eevlrclagl pepeegrede srwpyveirv lltepdptfr hrveealvgk avrltsivps
      361 yprregeaee ralsyndlqk iapldmlrht faaryggelp eeietlfnev mrevsl
//
LOCUS       WP_009275758             269 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Parabacteroides].
ACCESSION   WP_009275758
VERSION     WP_009275758.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (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   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12122938
            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="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30860
     Region          3..111
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          48..255
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 myheftpcaa lvpfidkfwv fkgftdigtr fkiladgctd fifsignmtv ptdehsmimq
       61 pyrsyfvgpm rvysdltatt ntlhmlgvrf hpcglaaftn eplgqfadlr iqssdinllf
      121 dnafaemlce qpddsvriri iegylirllt qsiqvdrqii yatsfikqsr gqlpvqnlid
      181 kicicqrhfq rkfkdttgyt pkefsriikf qyaievlrna phtdlssial dcgyydhshf
      241 ikefkrlagd vpsyfltlpn ptdepltyi
//
LOCUS       WP_009276202             325 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-oxoacyl-ACP synthase III family protein
            [Parabacteroides].
ACCESSION   WP_009276202
VERSION     WP_009276202.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 325)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..325
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35793
     Region          8..311
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mktiipdvsi rsiaswlpsn kislssfaeq ygeketrdvi rttgvewvyr tdanqkssdl
       61 cfnaaeylis kdnidresid glvvltvtrd walpdtsvyl qhklglknet vcldinygct
      121 gyiyglmqaa mwihsglcqn vlvlggdmlk ncldpkavgs idasdigtas liskgttgma
      181 fhlcsdgary drimmphggy iyqdgmgvfs fsivngpksi rtvmdlmqwe dsdvdiyalh
      241 qssqliiknv rmalkssqek fpvnmkdfgn sssstipnll cdlyglnkan rprhavfcsy
      301 gagltcgsva ldlskthfye plnkq
//
LOCUS       WP_009276600             376 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [Parabacteroides].
ACCESSION   WP_009276600
VERSION     WP_009276600.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 376)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            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="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42663
     Region          7..372
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mrikkierli vkyheqivgt lsltpdnkqc afeydkawls ngfsisplel plkpglfiak
       61 pspfygnfgv fedslpdgyg ryllhkallk egindtqlsa ldrlslvgng gmgaltyepe
      121 tsigtshepl dfdllqekal evlheknddd velllfnsrn sggcrpkalf snneghwmvk
      181 frhtydpqdm gliefhynel arqcgirvpd fklingkyft trrfdisqdg erlhtvtagg
      241 llniplsnpi ldysnllalt gyltqnplev eemfrrmvfn yftdnkddhc knfsftiqks
      301 dtstwqwhla paydltlcte gyngehatsv ngtghptiqd mitigtknkm nkphciriie
      361 evrtgcgdll rnkdwe
//
LOCUS       WP_009276613             339 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Parabacteroides].
ACCESSION   WP_009276613
VERSION     WP_009276613.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 339)
  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 13014342
            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="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=38817
     Region          205..337
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mmtrtvfill isslctlsyc tprtepaqte vlipvdsisk dsavivetlp lrieiekell
       61 ydkhtledty pykdttrefq wekmkerlsl lesiqrepsq wailqnyknr ngeaplvkvf
      121 krdaykrvsd tlgveryqsv plylltdtvt peiygrdgsl vrikamdeds kfariqtvyd
      181 geeewyapkk yikqigdtvv fdkaifvdrh nqniatlehv gskwlvrsmn pattgqhrpp
      241 yaqetplgmy vlqekksrmi ylvdgsketg gfapyanrft ngayihgvpv naprksliey
      301 spslgttprs hmcvrnatsh aqfvydwapv netivfvle
//
LOCUS       WP_009280649             396 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Fibrisoma limi].
ACCESSION   WP_009280649
VERSION     WP_009280649.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma limi
  ORGANISM  Fibrisoma limi
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Fibrisoma limi"
                     /db_xref="taxon:663275"
     Protein         1..396
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /function="Acetate kinase"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43101
     Region          1..394
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mhilvinsgs sslkyqlfam psdqplcvgq verigldgsf vrhqvtgadr lertepiadh
       61 avglqrvlel lsdpvsgvis spdvieaigh rvvhggesfa satritpavk etikalfpla
      121 plhnpinylc ieiaettfpr atqiavfdta fhqtmpeyaf ryaipealyr qegirvygfh
      181 gtshryvskk aaawlnkpda klisihlgng ssitavragq svdtsmgfsp laglvmgtrs
      241 gdidpavifh lisrgyspdd vnrllnkqsg mqgltgfsdm rdirkameag dqaatlayel
      301 yayrvrkyig ayaailngld aliftagige ndatmramic nelaflniyl dpdknttssr
      361 qirdisatds pvkilvvptn eeleiaqqsy ellqst
//
LOCUS       WP_009280083              83 aa            linear   BCT 20-JAN-2025
DEFINITION  acyl carrier protein [Fibrisoma limi].
ACCESSION   WP_009280083
VERSION     WP_009280083.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma limi
  ORGANISM  Fibrisoma limi
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
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   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 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   4  (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 10011594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Fibrisoma limi"
                     /db_xref="taxon:663275"
     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=9462
     Region          <29..77
                     /region_name="acpP"
                     /note="acyl carrier protein; Provisional; PRK00982"
                     /db_xref="CDD:179197"
ORIGIN      
        1 mkerviqllk nfgvqesala eqnghplhfn rdlgfdslds vdlimqleqe fgiripdedy
       61 pklttlqgvy eylqneqqva evv
//
LOCUS       WP_009281498             290 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Fibrisoma limi].
ACCESSION   WP_009281498
VERSION     WP_009281498.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma limi
  ORGANISM  Fibrisoma limi
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Fibrisoma limi"
                     /db_xref="taxon:663275"
     Protein         1..290
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32410
     Region          15..114
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          186..264
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mkppkeesvq mlsrqptgal slfvdkiwsv qadslslsgt nlpmlhselm fnfseffsiq
       61 sagaqpantg hgcwlstlqt apsqsrtigy hetlgvllkp wglypltnvp ahefgrlfvs
      121 geavfsaait pltdamqqaq saaeklivle kflnaryahk dvpaylyyad aylrrqpfrd
      181 givtelcrhl risrksltet frkylglspg qyvrllrfra aadaiatqpd lsltdltyrh
      241 dffdqshfih lfrafadmtp gayrsyfrtq rrasfglpet tspafipsgg
//
LOCUS       WP_009281777             453 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Fibrisoma limi].
ACCESSION   WP_009281777
VERSION     WP_009281777.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma limi
  ORGANISM  Fibrisoma limi
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 453)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Fibrisoma limi"
                     /db_xref="taxon:663275"
     Protein         1..453
                     /product="amidohydrolase family protein"
                     /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=50379
     Region          25..434
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mrhlllvfli gittssfaqe lvsnrqrdiv fqgvnvipmd rervlenqtv vvrngkitam
       61 gnassvrfgr dalvinangk ylmpgwaemh ahvppiddie pmkevlmlyl tngittirgm
      121 lghpkhlelr skinngeilg phfyatgpsf ngqsvktper gaemvreqka agydflklhp
      181 gltnqtfpai aktaqevgip fvghvsfnvg vwraidakys sidhldgfve altpgidtla
      241 eqetglfgsw iayraddsqi pklmnglrqn kvrvvptqal aerwlsplpa seftddpemk
      301 ymkpqevqsw eraktsynsn pnfskehaek liqvrrklia ecqkngvdll lgsdapqvfn
      361 vpgfsihhem kymvdagltp yqtlrtgtvn vasylnkpds gtirtgnvsd lvllngnplt
      421 dinqtrtieg vmmgtnwlsk ayiqkelkkl ekq
//
LOCUS       WP_009279310             516 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Olsenella sp. oral taxon 809].
ACCESSION   WP_009279310
VERSION     WP_009279310.1
KEYWORDS    RefSeq.
SOURCE      Olsenella sp. oral taxon 809
  ORGANISM  Olsenella sp. oral taxon 809
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Coriobacteriales; Atopobiaceae; Olsenella.
REFERENCE   1  (residues 1 to 516)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Olsenella sp. oral taxon 809"
                     /db_xref="taxon:661086"
     Protein         1..516
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=54071
     Region          119..229
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          255..362
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          387..515
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(466..467,470,488..491,493)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mslqedpktt pfvpdpalss lshsrigshf spsdgptpqd eipgrggsgr apkvaaavma
       61 glaavylggv avwsnvfmpn tsvngvdvsl etpasvarqq tvatssyala vsgegldlkv
      121 sasdvdlscd vdvfardala qtnawawpva airgskvdvr pqasfdaskl delvgkavda
      181 vnahatqpvn asvgydptss gfvvspekag taldaasvtk avgsalkega tslaldesal
      241 vqpsilsgdg rlaeaaktan sylaatqtlt vdgnavatvd agriaewvhv qddlsvtldd
      301 eaikawttge lsrqldtvgt trtytrpdgv tikvsggryg wnlngtelae tlaqnvrtgs
      361 atsvelpwss taaqygkrga adwgdryidv dltnqharmy dggslvwesd fvsgntsqdh
      421 gtpegvysvn shmgtnqtlk gidedhdgep dyvshvsywv pfidnlyafh daswrsrfgg
      481 siyqtdgshg cinlpsakae elydlakvgd vvvvhy
//
LOCUS       WP_009283405             276 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Fibrisoma limi].
ACCESSION   WP_009283405
VERSION     WP_009283405.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma limi
  ORGANISM  Fibrisoma limi
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 276)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Fibrisoma limi"
                     /db_xref="taxon:663275"
     Protein         1..276
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31150
     Region          19..111
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          179..261
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mnsqlieade rlatvfshyy cvqqgpqdap lqqqlvpnye mllvfnfgpa isgslgdapy
       61 visrtavlgp lqktltyelp agadlivvnf tlngfyrllr vpmqelktqd ihnpdvllnk
      121 pcfediwsql aqmttladrl qllneyalty aapadsttns miesipyvnn tvvepvklla
      181 tqqqvsarmi qltlqkqlgy sarelvrflr fkkvltflfq qptpsvdwls lvseygyhdq
      241 shlikdfqqy mgisprqfin qlaqggmcis kpgkfy
//
LOCUS       WP_009284105             335 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Fibrisoma limi].
ACCESSION   WP_009284105
VERSION     WP_009284105.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma limi
  ORGANISM  Fibrisoma limi
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 335)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Fibrisoma limi"
                     /db_xref="taxon:663275"
     Protein         1..335
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36847
     Region          4..335
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mekmysaitg lgfyvpetvv tnddltqyme tsdawiqert giqqrrffty gkdtnasmat
       61 aasrmalera gidagqvdli vyatitpdyy fpgsaflmqr elglegigvi dirnqcsgfv
      121 yalsiadqfi ktgmyrtilv vgsevqssll nkstegrnva vifgdgagaa vlqattdpeh
      181 rilsthlhad gryaedlyvk dpgssrdgrw iseatitqgd ynvtmngnav fkhavvrfme
      241 vineslnang yqpddlallv phqanirise yvrqqmnlpe ekvfnniqyy gnttaasipi
      301 amteafeqgr iksgdlicla afgsgftwas alikw
//
LOCUS       WP_009284520             297 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Fibrisoma limi].
ACCESSION   WP_009284520
VERSION     WP_009284520.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma limi
  ORGANISM  Fibrisoma limi
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 297)
  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 297)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Fibrisoma limi"
                     /db_xref="taxon:663275"
     Protein         1..297
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32578
     Region          50..289
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mirrtalktl tgsaalslvg tetfaqfmke sepaapgtgv aptllkgrin hsvcrwcysk
       61 ipledlakaa keigiksiel tgpdewpilk kygltsalpq gagkgiengf ndpklhdelv
      121 asyeaifpkl kdaglntiic fsgnrrgmsd adgiancakg lkrlmpsaek ygitmimell
      181 nskvnhkdym cdhtawgvel ckavgsdnfk llydiyhmqi megdiirtir enskyighyh
      241 tggnpgrnei ddtqeiyypa vmkaivdtgf kgyvaqefip krdplvslke avllcdv
//
LOCUS       WP_009285354             278 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Fibrisoma limi].
ACCESSION   WP_009285354
VERSION     WP_009285354.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma limi
  ORGANISM  Fibrisoma limi
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Fibrisoma limi"
                     /db_xref="taxon:663275"
     Protein         1..278
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32474
     Region          7..272
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mmalfnqtal ecskliteyy stsftlgirt ldrkfhlpiy aiygfvryad eivdtfhdyn
       61 kkallakfkd dtyqaieegi slnpilqsfq mvvreyniey dlidaflksm emdlyfqdyd
      121 tdgyqeyiyg saevvglmcl rvfcegdcka ydhlkepark lgsafqkvnf lrdlksdyvd
      181 rgrtyfpgvd fnafgrdtkq lieddiqrdf deayqgilnl prgarmgvyl aytyyqtlfn
      241 kikqlpasri qnerirvpnp qklallaqty lkyrlnvi
//
LOCUS       WP_009285323             161 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Fibrisoma limi].
ACCESSION   WP_009285323
VERSION     WP_009285323.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma limi
  ORGANISM  Fibrisoma limi
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 161)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Fibrisoma limi"
                     /db_xref="taxon:663275"
     Protein         1..161
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17309
     Region          9..157
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 maetllipqt tdrkaiydsl ipqlaalteg epdltanlan iaaalkeafg ffwvgfylkk
       61 enqlvlgpfq gpiactriaf nkgvcgaayt rretilvpdv eqfpghiacs sasksevvvp
      121 vfdkqgevsm vldvdsdqln dfsevdvegl ervaalitaf v
//
LOCUS       WP_009285446             543 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Fibrisoma limi].
ACCESSION   WP_009285446
VERSION     WP_009285446.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma limi
  ORGANISM  Fibrisoma limi
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 543)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Fibrisoma limi"
                     /db_xref="taxon:663275"
     Protein         1..543
                     /product="amidohydrolase family protein"
                     /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=60555
     Region          42..503
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mtkylpkkiv ccsyfllsls wqlvnaqvpk aparaegdgp ynrllirgvt linstgappv
       61 gpvdivvekn riaqirqvgy pgvpidpksr pqvnpgdkel ncegmylmpg fidmhghigg
      121 naqgtpseyv fklwlghgit tirdpscgng ldwvlehrtk serneitapr ikaytvfgqg
      181 akepittaeq arawvrdnak kgadgikffg aeptvfkaal eenkklglrs achhaqleva
      241 rmnvlataka gltsmehwyg lpealfadrt iqdypanyny nneqnrfeea gklwqqaakp
      301 gterwnqvld elialdftid ptfniyeanr elmlarraew hdeytlpslw rfygpsrish
      361 gsywhnwgte qevewkrnyq lwmafvneyk nrggrvttgs dsgfiyqlyg fayirelell
      421 reagfhplev iraatlkgae algmadqigs vevgkladfv ivdqnplanl kvlygtgaih
      481 lndrneverv ggvtytvkdg vvynakklla dvrrivaeak qkegfeitqp gvtpkagkvg
      541 ggk
//
LOCUS       WP_009285619             346 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Fibrisoma limi].
ACCESSION   WP_009285619
VERSION     WP_009285619.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma limi
  ORGANISM  Fibrisoma limi
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 346)
  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 346)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 346)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 346)
  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   5  (residues 1 to 346)
  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   6  (residues 1 to 346)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Fibrisoma limi"
                     /db_xref="taxon:663275"
     Protein         1..346
                     /product="AraC family transcriptional regulator"
                     /function="AraC-type DNA-binding domain-containing
                     proteins"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39276
     Region          21..207
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          94..335
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 meeyslqfvy gllayavqkd vsperlckls gldwetirrr gklvitpkqv ndlwmnashl
       61 shdplfglhl gesmqlaalg ivgqivqnsr tvgealthaa eflhlvtdlf gmavsqgder
      121 ftvrfvpdkd kaqeypfvfr hmidlslafv mhevdglvlq rikpkrvmlp ydaaefseye
      181 rilrckpiek adeyalefdd rywnepilta nyelqsvllq kasvmsdtie erqplkeric
      241 tyllanaylg iptlegiaan fnssarslqr klqeegvtyq qladsirksl avyylesgky
      301 pvkevsyilg ynelsaftra fkrwtgttpv sylkagpgvg mlkelp
//
LOCUS       WP_009286257             328 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Vreelandella
            titanicae].
ACCESSION   WP_009286257
VERSION     WP_009286257.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella titanicae
  ORGANISM  Vreelandella titanicae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 328)
  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 328)
  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 328)
  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 328)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Vreelandella titanicae"
                     /db_xref="taxon:664683"
     Protein         1..328
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=35564
     Region          1..310
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mklssfnpll vglacaagsl mvsataqaet lrlstpvpps hifskvsgrl aenlgersdg
       61 ryaievspyg rlgndneliq llqhgavqlg vvpaaslssr epsfngwflp gefenydeag
      121 aatqlpaars mleklepqgm iglgyiiagm rhvlstdsve siddftnqki rvfpnpvfnd
      181 wwlangaapt alptsevapa lttnllnavd vdldfvtalk lyqqaphlal tnhmafpgvv
      241 lvskawwdrq seadqkmire vfqeaeqwgi eeqarveken latlkdagve vveintagya
      301 etaaavrqty idsdpliaef yhqvvanq
//
LOCUS       WP_009286765             672 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Vreelandella titanicae].
ACCESSION   WP_009286765
VERSION     WP_009286765.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella titanicae
  ORGANISM  Vreelandella titanicae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 672)
  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 672)
  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 672)
  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 672)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Vreelandella titanicae"
                     /db_xref="taxon:664683"
     Protein         1..672
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=71013
     Region          24..665
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 msesnqpssv vpggnviqpr mvlwsitiva vglslfqlys agiqplglfy qrsihlalim
       61 vlaflmfpaf gptrkrgvlg wgldlvffag ailtggylvl nldeifsrag fwnstdilva
      121 ciatvtvlea srravgfgmt vigllaivya fagprgelpw lgewmpgile hrgytidrva
      181 gqlylgqegi fglplgvaat yififvlfga flectgagkf fidmayaatg rqrggpakaa
      241 vlasagmgsi sgsaianvvt tgaftiplmk rlgykakqag gieaaastgg qimpplmgag
      301 afliaeytnt pyldivkvsi lpaimyfatv ylfvhiialk qgmqglpkde lpqmrqvmkd
      361 gwhfllplav lvwllamsms pmrvgyyavi tilavavlry vlwfffvapr qgqpvtatav
      421 kdvvrtgfak lieglelgar navavsmaca vagiivgvvg ltglglkfss mmlafsggnl
      481 vlalvmvlla slvlgmglpv tasyivlivl vgpaltaefg vpllvahlvv fwysqdsnvt
      541 ppialagfag aaiagskpme tsfqawkfak glyliplfmv fnpeiiiggp vpvviwngvi
      601 ailalgafaa alegylftkm swlpriaita aifgvfypnl mteiagvavm ivaiganwla
      661 skreapatpv sg
//
LOCUS       WP_009286830             336 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Vreelandella
            titanicae].
ACCESSION   WP_009286830
VERSION     WP_009286830.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella titanicae
  ORGANISM  Vreelandella titanicae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 336)
  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 336)
  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 336)
  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 336)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Vreelandella titanicae"
                     /db_xref="taxon:664683"
     Protein         1..336
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=36750
     Region          8..334
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mkkqfknmkl kalacsfalg tlvhtgmasa dihikfhhdl pedsaqhlaa erfrdmvaer
       61 sggeisveif pnntlgddve vtqqlqmgav eaaiiptakl sgfvpamqiv dlpflfpspd
      121 iahtvldgqa gddllatveq vglkgvtfwe sgfkqftcdq pvngpedfag qkvrvmqspi
      181 imeqfkamga npvpiafget ynalqqrivd cqenplvsit qmkfyevqsd vvisnhayla
      241 yaflfsqswf dslspenqal ltdaarettv fqreetarre tgyiatieas gtnvstldda
      301 qltafresta svhdefanei gadlmaefqq aiadae
//
LOCUS       WP_009287282             270 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Halomonadaceae].
ACCESSION   WP_009287282
VERSION     WP_009287282.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            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="formate/nitrite transporter family protein"
                     /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=29383
     Region          2..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msylmpsefv tklvdqgesk vymgtrdtli rafmagatla lavifaitia tqtghfliga
       61 llfpvgfvml ylmgydlltg vfmlvpiawl dkrpgvtlpr mlkcwalvgl gnlggalfia
      121 tfgylnftmg gteeinavgq tmmavgesrt vgyqeaglag wivlflrgmf cnwmvsmgvv
      181 gaaisttvsg kimamwmpii vffylgfehs vvnmflfpig lmlgadftly qyimwneipt
      241 vlgnlvgglt lvglvlytth vrtqpkkvls
//
LOCUS       WP_009287952             633 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Vreelandella titanicae].
ACCESSION   WP_009287952
VERSION     WP_009287952.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella titanicae
  ORGANISM  Vreelandella titanicae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 633)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Vreelandella titanicae"
                     /db_xref="taxon:664683"
     Protein         1..633
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=69573
     Region          77..628
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mslikqlwia iiallllsfi gslaisitts rdyieqevri knadnatala lsmsqldkdl
       61 vtlelliaaq fdtgyyrrit lrdtddsvli ersaeeysgd vpawfrqlie fdvpngtati
      121 qdgwrqygtl elesqhsfay tslwrsmlel aawfllagvi slaiatvivr gikhplsrvv
      181 tqaqdisarr fttikeprtl elrqvtqamn vlsanvhqml sheshkldel rrhlqhdrvt
      241 galnrdvfmg klssqlgsed aratgmlimv rvqaleslne qlgyaatdql lntlvtqlgq
      301 ldsasaepmv grlngsdfif mlplmddvee lriqvmaala evaatqpdve iylptaivpy
      361 aphddrgtll atlddalaqa esltsfeqvv vrqrkrisly sshaewrnal eaailigpel
      421 ayfpvvdahg diihyecpar lllggewqta gvfipwitrf emepaldlav vkkalanled
      481 dlkpvginls aasitntqfv nelrtllaah pllakqlcfe vpatlsthai gslrglctal
      541 rplgctfgie hvgaeftkla dlhdvglayl kmdsslihql hasneqqtiv rgmatlchsl
      601 giqvigegva ddeeiaclfr vgvdgatgpg vrl
//
LOCUS       WP_009289442             288 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Anaerostipes].
ACCESSION   WP_009289442
VERSION     WP_009289442.1
KEYWORDS    RefSeq.
SOURCE      Anaerostipes
  ORGANISM  Anaerostipes
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 288)
  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 288)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 288)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 288)
  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   5  (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   6  (residues 1 to 288)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Anaerostipes"
                     /db_xref="taxon:207244"
     Protein         1..288
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33447
     Region          24..107
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          130..283
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mewneklqmi idyvehhlqr vqepidpgei skiaecsfgf fqkvfsymng isfaeyvrfr
       61 kltlagydlk stdqrvvdvs ylygydspts ftrafqqfhg vspkearisk tklkvvpkmq
      121 vlvkqeytwr veqkpafrli gksirffcdd eekpskilef wsecqrngvf sclvsmdkge
      181 ppglfglfhn vedsrnemqy simaaadgev pegygeliip etswavfdls gpvpqaihsg
      241 wkyleeewlv kypfrhakcp elewyssgnf ydknylsqiw ipildgeq
//
LOCUS       WP_009289947             100 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [Anaerostipes].
ACCESSION   WP_009289947
VERSION     WP_009289947.1
KEYWORDS    RefSeq.
SOURCE      Anaerostipes
  ORGANISM  Anaerostipes
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Anaerostipes"
                     /db_xref="taxon:207244"
     Protein         1..100
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11291
     Region          4..96
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mdimktsgik kkvieeirql avdyniqkvi lfgsrargdy hersdidlav lggdtnnfal
       61 avdeetstll mydivdlslp vqeelkdriy qegiviyeki
//
LOCUS       WP_009290415             347 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Anaerostipes
            caccae].
ACCESSION   WP_009290415
VERSION     WP_009290415.1
KEYWORDS    RefSeq.
SOURCE      Anaerostipes caccae
  ORGANISM  Anaerostipes caccae
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Anaerostipes.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Anaerostipes caccae"
                     /db_xref="taxon:105841"
     Protein         1..347
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39472
     Region          1..334
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mslyvdiekh lpefhlktsf eagnemlsil gasgcgkslt lkciagietp drgrivlngr
       61 vlfdsqkrin lpardrkvgy lfqnyalfph mtvreniacg lpsrdrsftd swiekfylsg
      121 lgdhypsqls ggqqqrtala rmlasapsli mldepfsald dylkwqmeqe lmhiirdfpg
      181 talfvshnrd evyrmsdria vmgngrlkti qrkkelfqnp esleaalltg cknishaeyi
      241 ddhtffasdw nivltssvpv pkdikyagfr ahyfsiepda tlpntmectv tniiedtfsm
      301 illfrekqnk ksgdwtglrf elpktlwdgq ikkiqsfsgf rktsffl
//
LOCUS       WP_009290486             397 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Anaerostipes].
ACCESSION   WP_009290486
VERSION     WP_009290486.1
KEYWORDS    RefSeq.
SOURCE      Anaerostipes
  ORGANISM  Anaerostipes
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Anaerostipes"
                     /db_xref="taxon:207244"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42287
     Region          1..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkvlvincgs sslkyqlids dtedvlakgl cerigidgal thepagkdki kttpampdhk
       61 taigivleql tdkengvits ldeisavghr vvhggekftk sciitedvlk eieacnvfap
      121 lhnpaaligi eacrelmkdk pmaavfdtaf hqtmpekafl ygiprkyyde dgirrygfhg
      181 tshqfvsrea akmlgkdikn iniivchlgn gasvtavkgg esvdtsmglt pleglimgtr
      241 sgdldpaile fiankenktv sevvnilnke sgvlglsggi ssdfrdvkaa raegnkaaaa
      301 amdayvyrva kyigaytvam ngvdaiafta glgenddatr aaigeyldci gakidaeknd
      361 vhgkaavist ddsrvkvlci ptneevmiar dtvalvk
//
LOCUS       WP_009291058             187 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Anaerostipes].
ACCESSION   WP_009291058
VERSION     WP_009291058.1
KEYWORDS    RefSeq.
SOURCE      Anaerostipes
  ORGANISM  Anaerostipes
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Anaerostipes"
                     /db_xref="taxon:207244"
     Protein         1..187
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20506
     Region          3..187
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mkqkrllvgi sgasgmpiav ellralkvsq tevhlictds avktlsletd npineiqsla
       61 davydshnig aapasgsfpm dgmavvpcsm ktlagihsgy sdnlllraad vtlkerrklv
      121 lvtrecplsn ihlrnmyevs qagavilppv lsyynrpqsv eemtrhivgk ildqfeiefn
      181 efrrweg
//
LOCUS       WP_009291601             336 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Bacteroides
            fragilis].
ACCESSION   WP_009291601
VERSION     WP_009291601.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 336)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 336)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..336
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=38110
     Region          <57..317
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mieltccpst lqkgfstysp valkelfnsq kvnhilpyng mdnneteqke fqdnnkhmsi
       61 sgaqqkyslv vdngqmrlsl eqeqatlllk tklseyanke ispanehltm riasqvynip
      121 taanglcffq ndepayitrr fdiapngrkf rkedfaslag iskgnkgpny kydvlsyeem
      181 adiikqyvsa ssvevlkffr lvifnflfsn gdahaknfsl letpsgdfil apaydllntr
      241 lhifddhvfa lqrglfkent lngndgavtg kefiefgiri gippkrvhke lisfcqkaeq
      301 vqdlveksfl pnqlkkqyll hyqmrkdsyl svgilt
//
LOCUS       WP_009292183             189 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Bacteroides fragilis].
ACCESSION   WP_009292183
VERSION     WP_009292183.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..189
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20906
     Region          6..171
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mktnevleti karrsvrayd rkqipaddln aileagayap sgmhyetwhf tavcntvkle
       61 elnerikgaf aksddkhlre rghsetyccy yhaptlvivs nepkqwwagm dcacaienmf
      121 laatslgias cwinqlgttc ddpevraylt slgvpenhkv ygcvalgyka egtllkektv
      181 kagtitive
//
LOCUS       WP_009292714             281 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Bacteroides fragilis].
ACCESSION   WP_009292714
VERSION     WP_009292714.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 281)
  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 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   3  (residues 1 to 281)
  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   4  (residues 1 to 281)
  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 281)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..281
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32260
     Region          <79..280
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          199..277
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 merrnpltlt ldqpfvagtd dfspfynrlh klncaiilyc ragrgtmaid lkkyeitvnt
       61 qvvllpgvvi sldeksddfr vsffashiem freacirfep sffhfikekp cytlpsefta
      121 pingllyats aiyadtdhrf rnqiarnhlq sflldvydkv hrlfthkeie ggsrpnelfh
      181 kfvalvheyc csqrdvvfya gklcistkyl tsicrsltgh sakkviddft aleikvllqs
      241 tdlsiqeiad rlnfpdqsyl gryfkrhegv spmeyraela g
//
LOCUS       WP_009293936             248 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YaaA family protein [Campylobacter].
ACCESSION   WP_009293936
VERSION     WP_009293936.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter
  ORGANISM  Campylobacter
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Prahlad,J., Yuan,Y., Lin,J., Chang,C.W., Iwata-Reuyl,D., Liu,Y., de
            Crecy-Lagard,V. and Wilson,M.A.
  TITLE     The DUF328 family member YaaA is a DNA-binding protein with a novel
            fold
  JOURNAL   J Biol Chem 295 (41), 14236-14247 (2020)
   PUBMED   32796037
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Liu,Y., Bauer,S.C. and Imlay,J.A.
  TITLE     The YaaA protein of the Escherichia coli OxyR regulon lessens
            hydrogen peroxide toxicity by diminishing the amount of
            intracellular unincorporated iron
  JOURNAL   J Bacteriol 193 (9), 2186-2196 (2011)
   PUBMED   21378183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006857
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Campylobacter"
                     /db_xref="taxon:194"
     Protein         1..248
                     /product="YaaA family protein"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=28837
     Region          4..230
                     /region_name="YaaA"
                     /note="DNA-binding protein YaaA associated with the
                     oxidative stress response [Replication, recombination and
                     repair]; COG3022"
                     /db_xref="CDD:442258"
ORIGIN      
        1 malkilfsps eskislntnd kfdgknlifs elfnkraeil krydeflksa nldeikklfg
       61 lkeledseql reslfqkgsi kailrydgva ykhlnyrgls ddaqkyidnn vlifsnlfgp
      121 ilakdeiaey klkqgeklag fdiskfyeqn fskavdsfle ndeildlrak fyekfyvikk
      181 efttfcflkn kkilshhaka yrgevlrqia nakvtnkdel mdlnfenlkl idmkkiglkn
      241 eltfeice
//
LOCUS       WP_009294313             173 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Campylobacter].
ACCESSION   WP_009294313
VERSION     WP_009294313.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter
  ORGANISM  Campylobacter
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae.
REFERENCE   1  (residues 1 to 173)
  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 173)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 173)
  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   4  (residues 1 to 173)
  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   5  (residues 1 to 173)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Campylobacter"
                     /db_xref="taxon:194"
     Protein         1..173
                     /product="TRAP transporter small permease subunit"
                     /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=19879
     Region          1..161
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mdkiekffdk agdivgyicm fimalmiidv ffnvvaryff sygnvafqel ewhffavifl
       61 lgmsyalked ahvrvdifya kfserqkalv nmlgtiffvi pfallvsnls fgfvgdayss
      121 aeasadpggl thrwiikami pvsfyilvff aigffirnln rykkaskeki wrd
//
LOCUS       WP_009296225             791 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [[Clostridium] symbiosum].
ACCESSION   WP_009296225
VERSION     WP_009296225.1
KEYWORDS    RefSeq.
SOURCE      [Clostridium] symbiosum
  ORGANISM  [Clostridium] symbiosum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Otoolea.
REFERENCE   1  (residues 1 to 791)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="[Clostridium] symbiosum"
                     /db_xref="taxon:1512"
     Protein         1..791
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=85044
     Region          <18..>164
                     /region_name="COG4913"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal ATPase domain [Function unknown]"
                     /db_xref="CDD:443941"
     Region          448..561
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          585..703
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(654..655,658,676..679,681)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
     Region          <712..>773
                     /region_name="PRK10856"
                     /note="cytoskeleton protein RodZ"
                     /db_xref="CDD:236776"
ORIGIN      
        1 madikktadg vdndspyral eadaaqmkie eaqgelepge amtecemeve admllqaale
       61 eklkaearle aaleekraae aklqaaldek reaearlega avirpeaaas epehgapefa
      121 gtyresaele qeaagsdead eperkmagqe relhetepei dklepvwens aangsdsget
      181 yreeragrgr srarrsrkkn agqgiempeg vhdsqnnhek tafpagqtea aaalqegrgn
      241 knqkgkkaai iaacvlaavi vagggayaam aqkykkvffp ntiingmnas grtvaevkem
      301 iaggienyvl tieereggqe qltgediklk akfdgtleqi vttqnpyawl syqlnpaeyt
      361 igtmieydee aftdavkglk cmdtalmkep vnagisdyvp gqgyhivpet agtyvsedvl
      421 rssitdavmn lkdtlsleea gaykqpeitq ddaalkerle tmnryvsttv tykfgdksev
      481 lngdrthewl vtdesggvsi dtaraagyve elaaayntsn kaknfktsyg qtiqvkggty
      541 gwkinqkeet aeliailksg qsqerepvys qkaashgend ygdtyveinl taqhlffykn
      601 gslvvesdfv sgnlskgwgt pagtypltyk qrnavlkgeg yrtpvdywmp fnggigmhda
      661 twrssfggti yktggshgci nlphsvakki yeniqagmpv icynlagtek gtsatpppaq
      721 vpaevptqap aevptqapae vptqppaeip tqapvvpetq apappettap agpgsdtghg
      781 ggafgpgsei r
//
LOCUS       WP_009296360             362 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [[Clostridium]
            symbiosum].
ACCESSION   WP_009296360
VERSION     WP_009296360.1
KEYWORDS    RefSeq.
SOURCE      [Clostridium] symbiosum
  ORGANISM  [Clostridium] symbiosum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Otoolea.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 362)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="[Clostridium] symbiosum"
                     /db_xref="taxon:1512"
     Protein         1..362
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39331
     Region          9..331
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 maffeikdik ieavscavpd nlvpvqsfep vfgaeacekf testgiremy kalpeqtagd
       61 layaaaenlf ektetdrski galvfvtqsp dyrrpatacv lqkrlglslg caamdiglgc
      121 sgfvyglqta aslmassdme yalvligeta sklvnpldks ivmmygdaga aillkreegt
      181 smktllksdg nrfkaivlpa ggfrdmnpsd etfmcsdgie rslydifmdg tsvfsfsitd
      241 vpetvkeyls ltesaieeyd clafhqanrf ilkqitrklk apkekvlisl drfgntggms
      301 ipltlcdhfg dtedgkknil msgfgiglsw gvtsaavdte kifpvirtkd fyaegkfepg
      361 ay
//
LOCUS       WP_009297455             637 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [[Clostridium] symbiosum].
ACCESSION   WP_009297455
VERSION     WP_009297455.1
KEYWORDS    RefSeq.
SOURCE      [Clostridium] symbiosum
  ORGANISM  [Clostridium] symbiosum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Otoolea.
REFERENCE   1  (residues 1 to 637)
  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 637)
  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 637)
  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 637)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="[Clostridium] symbiosum"
                     /db_xref="taxon:1512"
     Protein         1..637
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=68333
     Region          4..628
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 menkiskiag kifpvvafam svyhlwqvmm psidptkhmd ihlafalslv flsamiikdd
       61 khsgrtclsq iasicflima lvstayifvn fnallnragr ytgmdtiigf ililavleat
      121 rrtyglllpg lvvisllygh fgkylpgifh hagyswprli asvttylygi fgtvlnvsat
      181 yivlfmifgg llessgagqf finiaialgg ktrsgaaqaa vigsglvgsi ngsavanvas
      241 tgtftipmmk drgyepyyag aiesvastgg mimppvmgvg afimagiigv pyakialcal
      301 paalmyyvtt gisvhmralr cgfkplpdem ipdkkklmke dglfflplla iiillisgts
      361 vmrsaflgcv ilvicyivkn svrnpkfvlt rqfwgflyng lisgaksamt vaaacaamgi
      421 vtqifvmtgl amnivffikt lsgsvglval iltmavtilf gmgvpttaay vlvaslagsv
      481 lvelgfdkla vhlfiyyyaa lanitppvas aalvaskiak adyfktsvta trlglpgfil
      541 pfmfvyhqel llqgniisiv aivfssfvgl fcmcacfegf vfrklnvier ilmavcavcg
      601 iwpgtktdii cyvifivvig gqymqsrklk ravsgqr
//
LOCUS       WP_009297783             667 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [[Clostridium] symbiosum].
ACCESSION   WP_009297783
VERSION     WP_009297783.1
KEYWORDS    RefSeq.
SOURCE      [Clostridium] symbiosum
  ORGANISM  [Clostridium] symbiosum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Otoolea.
REFERENCE   1  (residues 1 to 667)
  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 667)
  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 667)
  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 667)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="[Clostridium] symbiosum"
                     /db_xref="taxon:1512"
     Protein         1..667
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=70931
     Region          32..658
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 msednqknrl plstdettaa getarrllee kdadartrsy ngffgilltv lltfwavfqi
       61 yvntigvmss mdlrmwhcmf llvftfllyp tvkkekkvrn appvwdvlli alaigafgym
      121 llnysriaqs ggyltkreiv iaalamlvvf eaarracpsl avlgliflay nffgkyipgp
      181 lghtgfsmkr vlshmvwgsq gifgvgigvs atyiflfvlf gsflkysgfs kfindlsltl
      241 vgrspggpak vavlasallg mingsaianv attgtitipl mkktgyrkef aaaveavast
      301 ggqfappimg avgfvmaefl gisyskvmia acipaflyym glllavhfea krlglkglap
      361 enipnavevl knqghlvipl vvligmivlg ytplyaavfs ifatilaswl rretrmsfkd
      421 ivdaavegsr gavsvgvscv vigviigtvs ltglgltigy lilevvgenq lylgglmvmi
      481 msiilgmgvp gvaayvivva vaipvlieig avpiaahmfc liyaclsnit ppvamssyva
      541 agiadsnqtk tsllavklgl tgfilpfffl gnpvlligvt datvlttiqa tltaclgvva
      601 lasglqgmlf crcgwaerav llvvaflsid pnmvtdvigi glfagvfiyq rmkvkkggee
      661 apavkaq
//
LOCUS       WP_009297890             134 aa            linear   BCT 20-JAN-2025
DEFINITION  zinc ribbon domain-containing protein [[Clostridium] symbiosum].
ACCESSION   WP_009297890
VERSION     WP_009297890.1
KEYWORDS    RefSeq.
SOURCE      [Clostridium] symbiosum
  ORGANISM  [Clostridium] symbiosum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Otoolea.
REFERENCE   1  (residues 1 to 134)
  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 12181465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="[Clostridium] symbiosum"
                     /db_xref="taxon:1512"
     Protein         1..134
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15218
     Region          20..131
                     /region_name="zinc_ribbon_15"
                     /note="zinc-ribbon family; pfam17032"
                     /db_xref="CDD:465334"
ORIGIN      
        1 mifiggissg mkqieymktv icsrcgaygr yqvfmtymyf sfffiplfkw nrrfyvkmsc
       61 cgavyeldpe igrkllrgmd aeiretdltl crdgsgnpwa qdgslpghsg krcpecgyea
      121 aeefaycpkc grkl
//
LOCUS       WP_009298569             350 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [[Clostridium] symbiosum].
ACCESSION   WP_009298569
VERSION     WP_009298569.1
KEYWORDS    RefSeq.
SOURCE      [Clostridium] symbiosum
  ORGANISM  [Clostridium] symbiosum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Otoolea.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="[Clostridium] symbiosum"
                     /db_xref="taxon:1512"
     Protein         1..350
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38434
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mtltvdikkk lhdytlelkl ehtggclgil gpsgcgksmg lksiaglvtp dcgrillgdk
       61 tfyssaerin rkpqlrktgy lfqsyalfpn mtvaenvgsg ispknrerdk iisacihrfr
      121 lsglenyypg klsggqqqra alarilassp alllldepfs amdaalkevl rlellhvlrd
      181 yhglsilvth dkdeayqlcd sliimdqgqv lcsgatkdvf dnpgkyqaar ltgcrnispv
      241 rrlgdnrila ldwnltltta ektteqtkav airphclvpv seeaaavwke rpganlipvn
      301 aplvsplpfd wefclennlc wtvkkdsgss sqppvpswlr vlpedllllt
//
LOCUS       WP_009298712             484 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Streptomyces ipomoeae].
ACCESSION   WP_009298712
VERSION     WP_009298712.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 484)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..484
                     /product="amidohydrolase family protein"
                     /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=51428
     Region          38..431
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mtvtedtmwr rrrgllpdgd plvraleela ergrdhrfra vglvdpatgr pgppqdltvt
       61 ggtvtartpt pptadgreap ytsyalpgfv dshahvssas dlvgllvhgv tgfrqlwgep
      121 ahlyaagvhr arhavlprpw vtagvvdgpr sripqgvtvv dgvravrqvi edalafgfdg
      181 ikvyddverp vfdvlvreae raglpvvghi peavplaaaq rtmrssehly glvpnvfrlp
      241 perrwdalar aladrtaepg gapghfvcpt lvcwrarsge rrytrpsraa lqavdegrrr
      301 swqaaardal rldpaeahrr gglvdalggi artlaetgtr llvgsdcgnp fvlagpsfhk
      361 elaelsragl dfttllraat thayeatgra gspaagslta gspapgapad lvfyrrppdd
      421 aelsalarpd avlvdgvlld gddldrlwal rlaasglgas gwargeldpp vttgrptkea
      481 ahag
//
LOCUS       WP_009298670             133 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Lachnospiraceae].
ACCESSION   WP_009298670
VERSION     WP_009298670.1
KEYWORDS    RefSeq.
SOURCE      Lachnospiraceae
  ORGANISM  Lachnospiraceae
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 133)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 133)
  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 133)
  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 133)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Lachnospiraceae"
                     /db_xref="taxon:186803"
     Protein         1..133
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15387
     Region          40..129
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(59,78..79,98,101,109..110,121,126)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mlsfndaeeq ivnkildsla tmdfqqinfs aesvlsfsni tiypqecrie ingesltlsr
       61 rqfallylla rnvgriltke qiyshvwnei vpinvdetir yhiseirkkl neladidcie
      121 tvwgigyrfk esk
//
LOCUS       WP_009299983             501 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Thomasclavelia ramosa].
ACCESSION   WP_009299983
VERSION     WP_009299983.1
KEYWORDS    RefSeq.
SOURCE      Thomasclavelia ramosa (Clostridium ramosum)
  ORGANISM  Thomasclavelia ramosa
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Coprobacillaceae; Thomasclavelia.
REFERENCE   1  (residues 1 to 501)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Thomasclavelia ramosa"
                     /db_xref="taxon:1547"
     Protein         1..501
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=55307
     Region          <1..>89
                     /region_name="PknB_PASTA_kin"
                     /note="Stk1 family PASTA domain-containing Ser/Thr kinase;
                     NF033483"
                     /db_xref="CDD:468045"
     Region          107..216
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          373..500
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(450..451,454,473..476,478)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mdkqeenmsn tndtieskqk semtkkvrsg kktgvqkkii iigilvsllv iiyligsfyf
       61 nkkflsgtyi ndinvsgltl teaneklaeq idarslklif ndeatetvsg secgvrynsn
      121 nnvknilkkq nsfgwigayf nksknvvndl aevdetvlra kvaslghlqe evqvapvdak
      181 veylnnefti tnevngstid qekliseikl afsegkesln ltekkcyvep avkandaklq
      241 nlldaarkya saaityktrs gdvvldgstl vtwlsidesg nyyrddavfk ekvtdfvgsl
      301 akkinsvggs rtfvgannrt itvsggnygl rlqnskeisg llediyankv gvrtpvtsgr
      361 eassdngglg dtfveidlsg qhmwyhkngq ivlesdivsg tyniadrrtp agayylynke
      421 rnrvlrgtkl pdgtwpyetp vsywmpfnkg iglhdssswr skwggtiymn ngshgcinlp
      481 tgiasqlyns ievncpvvcy y
//
LOCUS       WP_009302406             385 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Desulfovibrio sp.
            6_1_46AFAA].
ACCESSION   WP_009302406
VERSION     WP_009302406.1
KEYWORDS    RefSeq.
SOURCE      Desulfovibrio sp. 6_1_46AFAA
  ORGANISM  Desulfovibrio sp. 6_1_46AFAA
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Desulfovibrio.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 385)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Desulfovibrio sp. 6_1_46AFAA"
                     /db_xref="taxon:665942"
     Protein         1..385
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42210
     Region          6..343
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mfhtfhnvki salrtavpan eirledeihf yggsvkkitr lratlgmdrr rvcppdvtas
       61 dlcahaalsl ldavpdarqa idalifvsqm pdwhqpatac elqhrlgltr hcaafdvnqg
      121 ctgyiyglwl sasliasgaa rqvlvlvgda hpserdirnr itapvfgdgg satllarden
      181 aapmsfglgt dgsgfetiii pagkaripfl rehaenerlv rditdpygni wqlgdtymdg
      241 gavfnftmdv vpehlhyale yasigptdid wlilhqankq ivesvaakag fpedrapwqs
      301 fskygnlasa sipvalcdvf gqrapgkvlm sgygiglswg sclcnidawd caapidyepd
      361 pkrptrqqri erweqiimge mtrhd
//
LOCUS       WP_009304647             283 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: class II fructose-bisphosphate aldolase
            [Eggerthella].
ACCESSION   WP_009304647
VERSION     WP_009304647.1
KEYWORDS    RefSeq.
SOURCE      Eggerthella
  ORGANISM  Eggerthella
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae.
REFERENCE   1  (residues 1 to 283)
  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 283)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Eggerthella"
                     /db_xref="taxon:84111"
     Protein         1..283
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=30168
     Region          1..254
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mlaslssvla waeengcaaa afdtpnlell laaigaaehr gepviiqhaq lheeetsidv
       61 igpimvarae asrvpvcvml dhgedmdyvr raldlgfsav midgsqlpye envaltlgav
      121 elareygadv eaeigfttgh eglenadddr envytdpdea arfvadtgid alaasvgtvh
      181 gfyraepnld fklieelrir cgvplvmhgg sglscedtra airagirkin yfsymsnagv
      241 ravealiaee hpkyfhalan aataamqada eaamdmfsmv psa
//
LOCUS       WP_009305377             492 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase family protein [Eggerthella].
ACCESSION   WP_009305377
VERSION     WP_009305377.1
KEYWORDS    RefSeq.
SOURCE      Eggerthella
  ORGANISM  Eggerthella
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae.
REFERENCE   1  (residues 1 to 492)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Eggerthella"
                     /db_xref="taxon:84111"
     Protein         1..492
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=51381
     Region          99..211
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          368..491
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(442,445,464..467,469)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkhaapadqt papasspett arrrfsapki igivagsivg llliayvags lyftdrfmpn
       61 tvlgdhdvsl ktssevqail ddalsdytva vsgqgfsmkl sakdagvsfd gqaivadalg
      121 ntnpwlwple itrehdetds laassgssla navrtavdef natatpptda vvafdeqkna
      181 favqpeatgt aldadavaka igsaiasmqp takltadalq qpavpatdpk lqaaaeaanq
      241 lvkadmqlmm ggdvaaevnp alvstwisfd esltpsldee alvawakqle vacdtvgter
      301 tytrpdgkvi tvaggpygwl tdgeallelv kegvangtvg avdipckttg tayngagaqd
      361 wsarycdidl seqhvrfyde tgtliweapc vsgtpngahn tptgvfwlnq kaspsvlkgt
      421 nldgskyesa vrywmpfvgn viglhdadwq aafggtlyqq grgshgcvnl pvgsaadlfg
      481 iiqsgdvvvc hw
//
LOCUS       WP_009306377             370 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Eggerthella].
ACCESSION   WP_009306377
VERSION     WP_009306377.1
KEYWORDS    RefSeq.
SOURCE      Eggerthella
  ORGANISM  Eggerthella
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Eggerthella"
                     /db_xref="taxon:84111"
     Protein         1..370
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=40959
     Region          1..367
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mslevnirks fssftldvaf eagdetlgfl gasgcgkslt mrciagietp degrivvndr
       61 vffdserkin ltpqqrktal lfqsymlfpn ltvaenvaag igreaskadr dalvaaelkr
      121 fglegfdrry paqlsggqqq rvalarmlaa rpgilmldep fsaldahlks vleqnlvslf
      181 dafhgtvlyv shdidealrf cdriavvetg ritemgtgdd lvnrpqslag vklsgcknat
      241 aavrvdersv rlpkwgieaa tsaavpedvk algvrafflq rvdgpgency rvrvdrvsds
      301 rfertvllgf ldrdeseapt vsrtddemky lhqhlfwrvd klavpadelp hegeelwiri
      361 ppnkvylvsr
//
LOCUS       WP_009306751             281 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Streptomyces ipomoeae].
ACCESSION   WP_009306751
VERSION     WP_009306751.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..281
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29880
     Region          14..251
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mstyevavre yatlgegptw daeaqrliwi dilgsrvytf dpadgrrtvl vteqhvgavk
       61 praggglvln lrdgvglrda dggfrwlhhe pvpgrranda avapdgslfa gtmrydeapg
      121 ggtlrritgd gtvtpilddv avsngtgwsp dgrlmyyids ptrridvfdy dghlpvdrrp
      181 fvtieegagf pdgltvdaeg cvwvalwegg avrrytpsgd ldrvidlptp rptacafagp
      241 dltdlyitta rvgtdtphpl sgsllvvpga gkglaqppfa g
//
LOCUS       WP_009306770             183 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LytR C-terminal domain-containing protein
            [Eggerthella].
ACCESSION   WP_009306770
VERSION     WP_009306770.1
KEYWORDS    RefSeq.
SOURCE      Eggerthella
  ORGANISM  Eggerthella
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae.
REFERENCE   1  (residues 1 to 183)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Eggerthella"
                     /db_xref="taxon:84111"
     Protein         1..183
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=18816
     Region          70..>134
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 magirhifla gafaclatgm llcscstgsp aapestssha eesvpsheas apepasadsa
       61 epvrigkdqv tvlvlngcgi egaaaevaek vraagfenvt vdnatyfnvp strvsyyhee
      121 nsaeaeelgd llkvvglasv ycydgddwag gwnkdydilv mvgdpsaadn piyvgagpeg
      181 esk
//
LOCUS       WP_009307595             418 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Klebsiella].
ACCESSION   WP_009307595
VERSION     WP_009307595.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 418)
  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 418)
  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 418)
  AUTHORS   ter Beek,J., 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 418)
  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 418)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..418
                     /product="CmpA/NrtA family 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=45893
     Region          38..289
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mgdkfsisrr rllqagaalg samllpgvmq aawaggsdkp eqtrvrvgfi pltdcaplai
       61 aaakgfdqky gitlvaskea swaavrdklv ageldaahil ygllyglelg iaskpqaman
      121 lmtlnrngqa itlsselqek gvtdlgglkr lidrsapgsy tfahtfptgt hamwlyywla
      181 sagidpfndv rtvvvpppqm vmnmrignms gfcvgepwna raindrigft aatsqdiwpe
      241 hpekvlgtrr dwvernpnta ralvaalmea qrwiaaspen tretarllar rgwlntkeqy
      301 ltgrmlgeyd nglgrrwqda hpmrfwagge vsfpwlsdgm wfltqfrrwg llkqapdyla
      361 vasrinridv wqaaaqavgg isapaarmrs stlmdgtvwn gsdpegyarh fsiqrkga
//
LOCUS       WP_009308263             409 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Klebsiella].
ACCESSION   WP_009308263
VERSION     WP_009308263.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 409)
  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 409)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..409
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47371
     Region          1..405
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 msvlqlslne arhlhlaaqg llkkprrrar pkdilstiqq msllqidtin vvarspylvl
       61 fsrlgsypqh wldeslrnge lmeywaheac flprsdfalv rhrmlnpdnm gwkyhrawme
      121 ehvgsiaelv ahigqngpvr sadfthprkg asgwwewkph krhleglfta gevmvverrn
      181 fhrvydltrr vmpdwdderd alsredaeai mlrnsarslg ifraqwlady yrlrqpslpg
      241 llaawqeegl vvpvnvealg emwlhheala qletapggkl tashsavlsp fdpvvwdrkr
      301 aeqlfnfsyr lecytpapkr qygyfvlpll hqgklvgrmd skihrksrel eifalwleeg
      361 vkitrgleqg lrraindfar wqsaerilcr rlpeglfvgq eqgweidad
//
LOCUS       WP_009308332             462 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: replicative DNA helicase [Klebsiella].
ACCESSION   WP_009308332
VERSION     WP_009308332.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..462
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=50762
     Region          5..415
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mtpqeleacv lagllnggas pdafdviast peesfsigfh rrafseikkq alanglidml
       61 fvsealggss ladlseitrm patvpnlkgy agkmvkawrs rrmaellqqg adgirqannq
      121 eqrdqvveta vaqlldmtgd tgdvqpvhms ellpvymetm qkrmdgeegt rnlktgieel
      181 ddatgginlq dlivvagrpg mgktefalkl vdgvtaaggg alifsmemaa aqiverslag
      241 sgnmsvsrlr npldmhdedw arftaametm ngrdiwivda tdltieqira vaethkrryp
      301 hlamivvdyl glikkpkaer ndlaiahisr nlktmamrlh tptfalsqls ravdsrpatq
      361 rrpvmsdlrd sgsieqdads imflyrdevy npespaagia eiilgksrfs aagaviyqef
      421 knghflhvdq hvgkektriq leatkprkqp rrysekyntd af
//
LOCUS       WP_009308458             290 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Klebsiella].
ACCESSION   WP_009308458
VERSION     WP_009308458.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..290
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32653
     Region          14..255
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 maepqplfdy tgylpecptw seaeqalywa dimeceihry dirsgehrvl qfpeevgcfa
       61 lrekggfiva lrsgiwltda hgllrrkvcd npsnpelarf ndggtdrdgr fyagtfwgpg
      121 dyngallmrv dndlqpkviq cdihgangla fsadrrwmyt sdtpnaviyr tpldeqgepg
      181 rrevfrrfqp gegipdgaai dvegcywsam fdgwriarfs pqgeelesyp mpvrcptmvc
      241 fggadmktly itttrenmed delaqyplsg aiftlpvava gmkklpfrec
//
LOCUS       WP_009309063             276 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Klebsiella].
ACCESSION   WP_009309063
VERSION     WP_009309063.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 276)
  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 276)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..276
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29138
     Region          20..67
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msmdlmvqam kikvgnplrk lvllkladna sdlgecwpsy qhiadqceis krsvmnhiea
       61 lcecglikke lrtgpkgnss nvyqlnlrsa gdspggsanr slpgagdslp gagdspggsa
      121 gaaprishsf epviesvnep ikhtgasada saparsakqd yspefetawq dypkraggns
      181 kaaawkawka rlkdgvnpea mlagvkryat yaratgsvgt qyvkqaatff gpdrhfeesw
      241 qapsapgggh nstiarlsgl grmsddfges genlnf
//
LOCUS       WP_009309648             495 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [Klebsiella].
ACCESSION   WP_009309648
VERSION     WP_009309648.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..495
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=53963
     Region          1..495
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mqyikihsqd nvavaltdia agsvvtidnd svtlgqdivr ghkfalraia kgenvvkygl
       61 pighaladia pgehvhahnt rtnlsdlday ryqpdlvaqp pqpadrevqi yrrangdvgv
      121 rnelwilptv gcvnamarqm qnrflketyg aedidgvhlf shtygcsqlg ddhintrtml
      181 qnmvrhpnag avlvvglgce nnqveafret lgefdpqrvh fmvcqhqdde veagvehlhq
      241 lyevmrqdkr qpgklselkf glecggsdgl sgitanpmlg rfsdyviang gttvltevpe
      301 mfgaeqllms hcrdeatfdk lvtmvndfkq yfiahdqpiy enpspgnkag gittledksl
      361 gctqkagssq vvdvlryger lkvhglnlls apgndavats alagagchmv lfstgrgtpy
      421 ggfvptvkia tnselaakkk hwidfdagql lhgktmpqll eefvdvivaf angkptcneq
      481 ndfrelaifk sgvtl
//
LOCUS       WP_009311639             476 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Neisseria sp. GT4A_CT1].
ACCESSION   WP_009311639
VERSION     WP_009311639.1
KEYWORDS    RefSeq.
SOURCE      Neisseria sp. GT4A_CT1
  ORGANISM  Neisseria sp. GT4A_CT1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Neisseria sp. GT4A_CT1"
                     /db_xref="taxon:665946"
     Protein         1..476
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50812
     Region          206..436
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mtyhyggyss kghfnaycpp vkpynpycpp shggfgykgg fhnygsshgf kmphgkfghg
       61 aycpppkpay kciiidfncn pgkpyypkpa pkpvppkhvd pycppvepkp qpqphpqphp
      121 qpqpkpqpqp qpqpkpqpqp kpqpkpqpkp ndkdckdcvd dqnqqntygh ddknpgniih
      181 vdgstkdkdg ltktvgtdkk dtiygtggdd viyggdgadv iyggdgndtl qgdnngdsly
      241 gqggkdylqg gdgndylngg sdadimrggd gndvyfvdhk gdqvieygna nggidtvrsv
      301 idytltdnve hlflqgsgni ngtgnalnnd ingnsgnnhl yglagddclv gkdgndyldg
      361 gigndvligg tgddtyffdk gygrdtiqde sgndtlqfgk gisasdvlls ktgnsltvsv
      421 gggdtvtidd wfsgnnhkie nfkfadgsty evtghgdyys lsavnsiqqq tqvpsi
//
LOCUS       WP_009311795             259 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein, partial [Neisseria sp. GT4A_CT1].
ACCESSION   WP_009311795
VERSION     WP_009311795.1
KEYWORDS    RefSeq.
SOURCE      Neisseria sp. GT4A_CT1
  ORGANISM  Neisseria sp. GT4A_CT1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Neisseria sp. GT4A_CT1"
                     /db_xref="taxon:665946"
     Protein         <1..259
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
     Region          1..>165
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 ngddilegge nndvldgghg ndtldggygv dkmtggdgnd iyyvdnvndt vtersgegtd
       61 tiyssvsyta aanvenltlt gsnnifgign hndniltgnk gdnrlsgedg ndtlygmggn
      121 dtllggngnd hlnggdgddy iaggsgsdti itgegndtva ftasdiregs idrvvefdpn
      181 tdkldlsgmr slltgsnanl swskmfvekd pevilqkdrp ylifdteqht layreagsss
      241 stifakfdfv wlgpsniig
//
LOCUS       WP_009313703             267 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phosphonate ABC transporter ATP-binding protein
            [Pseudomonas].
ACCESSION   WP_009313703
VERSION     WP_009313703.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
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   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            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="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=28503
     Region          3..247
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mslsldgvdl vhadgqrala dirlrlaage rvaligpsga gktsllrvla sqwrpsagrv
       61 ellgeepwgl saaarqrlra riglvhqapp lpprqrvvsa vlagrlgqwp lwkslaslvy
      121 pldragahda lqrldlgdkl fqrcdqlsgg qlqrvgiarv lyqraelila depvsamdpv
      181 laghtlalln reaaargstl laslhavela lqhfprvigl ragriafdlp agevdraald
      241 alyaneqlqa eraspasepa vvhiprc
//
LOCUS       WP_009314629             402 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Pseudomonas].
ACCESSION   WP_009314629
VERSION     WP_009314629.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 402)
  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 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   3  (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   4  (residues 1 to 402)
  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 402)
  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 10596738
            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="CmpA/NrtA family 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=43455
     Region          16..267
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mtdrairsqa waggsdapek saldigfmal tdsaslivaa tqgfaqpygl tlnlrrqpsw
       61 atlrdkllsg eldaaqclyg lvygvqlglg gsvasemavl mglcqngqai nlseplkqag
      121 vtsaeallrh rrqngarltl aqtfptgtha lwlnywlasi glhplhdvhs vvvppaqmvg
      181 hlqagridgf caggpwgala vdqgqgftia tsqaiwpdhp ekvlgttraf vdaypntara
      241 lvmavldasr fieqnaenrl gtaqlisgrd yvdaplgaiq prffgryqdg lgnawqdphp
      301 lrfyadgevn rpwlsdgmwf mtqfrrwgll redpdylgia rrvqqtalyr daatalglcl
      361 dgadmrrstl idgrtwdgsd pagyarsfpi halaetgqgi dl
//
LOCUS       WP_009314967             795 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [Pseudomonas].
ACCESSION   WP_009314967
VERSION     WP_009314967.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 795)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 795)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 795)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..795
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..795
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86520
     Region          57..106
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          83..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 mtpfprfalr tlpalflslg claataqaae avryrfsqaa aplaqalnaf srasgqtlly
       61 taelppqata palhgsldae ealqrllqgs glrarrider tltlepipas galdldattv
      121 saaapaqgyr paanasisrg daplldipqa isvvpaqalq dqrprnldda lgnisgitqa
      181 ntlggtqdav mkrgfgdnrd gsimrdgmps vqgrnftata dhvevlkgpa sllygiqdpg
      241 gvvnvvskkp qlqqanaltl rgsayahgrn gsggqldstg plgdsglayr mildhededy
      301 wrdfgksret lvapslawyg edttvnlsye hrefttpfdr gtaidprtnr pldiprsrrl
      361 depfnitegr seltrldler qlddtwkahf gygysretyd dnqarvmavn adgtltrrmd
      421 gthgavssds fatlglsgtl qlagmqhdlq fgmdhekrki fradllrdsk tsrfdyldpv
      481 ygqvvpstrv vagdsdqtdk lrsdslyfqd sihlderwil vggaryqiyd qlagrgrpfn
      541 antdingqkw vprgglvyrl sdevslygsy trsfkpnsti aplstgetid sailpeeats
      601 welgakldvp grlsgtlalf dirkknvlvn eldgagnssv raagrvrsrg leldltgqls
      661 erwsligsya wlaaevtedp tlegkrlqnv arntaslsav yelgqlfggd rlrlgggary
      721 vgkrpgdpan sfdlpsytva dafasydtrf gghgvkfqln vknlfdrtyy pssanrlyva
      781 mgeprqfqvs ttvef
//
LOCUS       WP_009316799             314 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Coprobacter
            fastidiosus].
ACCESSION   WP_009316799
VERSION     WP_009316799.1
KEYWORDS    RefSeq.
SOURCE      Coprobacter fastidiosus
  ORGANISM  Coprobacter fastidiosus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Barnesiellaceae; Coprobacter.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 314)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Coprobacter fastidiosus"
                     /db_xref="taxon:1099853"
     Protein         1..314
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34401
     Region          1..297
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 myinatgyyi ptervsndhf feingltsdw ilqrtgintr skagegensd tmgleairta
       61 ipylpyditd vdlivsacys prdtvatlah vaqrefkiek akalyissac ssfsnalevv
      121 egyfamgkat kalivcsehn tyysnesdpk cghlwgdaav alfvskdlqk egeaeitsiy
      181 trglghigkg pdavhlkpke dgitmpegrd vfmhackymv evlehltsdn qmsiddlnyi
      241 ichqanmriv anvahqlklg edrflnnire lgntgsasam lvlaqhihem kkgdkaavtv
      301 fgggyssggf lvkf
//
LOCUS       WP_009317344             167 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Coprobacter fastidiosus].
ACCESSION   WP_009317344
VERSION     WP_009317344.1
KEYWORDS    RefSeq.
SOURCE      Coprobacter fastidiosus
  ORGANISM  Coprobacter fastidiosus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Barnesiellaceae; Coprobacter.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Coprobacter fastidiosus"
                     /db_xref="taxon:1099853"
     Protein         1..167
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19189
     Region          80..144
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mkrrtvlsiv llslvgwcga yaqvqvadts ivqslervtg narvrlfqda rltdrlarrt
       61 gnvalsgtss rdmnyvtvrg yriqvfsdnn qrrskdeayq kasmikdadp elstyvtfts
      121 pfwrlrvgdf rsfeeanlkl ielkntfpqf remrvvkdmi rltrive
//
LOCUS       WP_009322047             401 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Streptomyces ipomoeae].
ACCESSION   WP_009322047
VERSION     WP_009322047.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..401
                     /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=45266
     Region          54..325
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mtnslrsqdh rsdhrsdqrs epqraplaqa aspqspadgg saprsttapg agpakqrdaf
       61 fdnakylaiv lvamghawep ltdhsraaea lymvvyafhm pafilisgyf srsfdmrpdr
      121 lrrlitgvav pyvlfeiays lfkryadddp shpislldpw yltwflialf vwrlttplwk
      181 varwpiplal giaalasvsp digddldlqr vlqflpffvv glfmkpahfq fmrrrevril
      241 svpvmacala laywvgpdmn sawfyhrdsa qelgapwwag vvmtfalfgc smvltacffs
      301 wvprrkmwft vlgagtlygy llhgflakgs rfwdwydana wvyqplgelf vtfvaavvit
      361 llctppvqrm frfamepkme wafkrdaael argrgkvgak a
//
LOCUS       WP_009323222             231 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Streptomyces ipomoeae].
ACCESSION   WP_009323222
VERSION     WP_009323222.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..231
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=24087
     Region          13..221
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mnpvkpgetp rtpwivgvsg asgtpyaaav lrallaages vdlvvsrasr ltlldetgis
       61 frdahwrddl rewlslgadg kpgtfpvdld gdrvrhwsag dlaagpssgs ypvkgmlivp
      121 astacvagva lglskdllqr aasvtlkerr plvvavretp lggqilrhlv tlddagatvl
      181 paspafyaga thiqdlvdfv agrvldaagv phtlyrrweg dvggarasri t
//
LOCUS       WP_009318744             409 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Coprobacter fastidiosus].
ACCESSION   WP_009318744
VERSION     WP_009318744.1
KEYWORDS    RefSeq.
SOURCE      Coprobacter fastidiosus
  ORGANISM  Coprobacter fastidiosus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Barnesiellaceae; Coprobacter.
REFERENCE   1  (residues 1 to 409)
  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 409)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 409)
  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   4  (residues 1 to 409)
  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 409)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Coprobacter fastidiosus"
                     /db_xref="taxon:1099853"
     Protein         1..409
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=47497
     Region          188..408
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          324..405
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mntkipeyad ilqvlltmsv vicvggatll flrsggnrsr rllslvmftw gliymtrvig
       61 mltgilnfdf tstgvldvlv lvagnffliv lllypleivr pgwlnlrrig llllpyimlv
      121 lfyyavlpll gqkilvlhdi ddffehigef nvwyrllllv sigfyllsll rltwryrevy
      181 qqwcqsnyaa tedmeiswlr nyiigvflig cayfwllfdg ntrcfvvhnl mvqlffcytl
      241 ykglfhynpy tedffshtld emtarreavc keeqllsgdi fenfnlsedd saflgklsty
      301 rdevarwmtd kkpylnkdfk lmdvseflpl nrtylsrvfn egfgdsfssv vrsyrmreae
      361 illvsnpdip vgqigercgf sspavfhrsf vqchdgmtps ryrkrsakp
//
LOCUS       WP_009319267             260 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Coprobacter
            fastidiosus].
ACCESSION   WP_009319267
VERSION     WP_009319267.1
KEYWORDS    RefSeq.
SOURCE      Coprobacter fastidiosus
  ORGANISM  Coprobacter fastidiosus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Barnesiellaceae; Coprobacter.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Coprobacter fastidiosus"
                     /db_xref="taxon:1099853"
     Protein         1..260
                     /product="formate/nitrite transporter family protein"
                     /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=27989
     Region          2..260
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mstlppseiv isaeksalqk iefstrktvi lgilagiyia mggllsllig sgfpeitnnn
       61 pglqkllsgc mfplglilvv iagaelftgn nailipgvln dkykwtavwk nwvivyfsnf
      121 lgalffvyvm vhstgvvasd pwhsaiknia vakvsmswit vflkgiganw lvclavwlgm
      181 sssstagkfi glwfpvmgfv aigyehsian mffiplgmlq gadisvydfl vsnlipatlg
      241 niiggalfvg sfywyaylkk
//
LOCUS       WP_009327002             314 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Streptomyces ipomoeae].
ACCESSION   WP_009327002
VERSION     WP_009327002.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..314
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33858
     Region          5..308
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 maygmmrdvt rrlmlldtas lyfrayfgvp esvkapdgtp vnavrglldf idrlvrdhrp
       61 tdlvacmdad wrpqwrvdli psykahrvae eheagpdeed vpdtlspqvp vieevldalg
      121 iarvgvtgye addvigtfta rakdpvdivt gdrdlyqlvd dvrgvrvlyp lkgvgtlqlt
      181 deswlrekyg vdgggyadla llrgdpsdgl pgvpgigekt aakllaqfgd lagimaavdd
      241 pkagltpsqr krldearpyv avaptvvrva advplpevdt alpkaprdpv aletlaarwg
      301 lggslqrllt tlqg
//
LOCUS       WP_009327290             387 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Streptomyces ipomoeae].
ACCESSION   WP_009327290
VERSION     WP_009327290.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..387
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41593
     Region          1..270
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          266..357
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrllhtsdwh lgrafhrvnm lgaqaefigh lvttarergv davvvsgdvy dravpplaav
       61 elfddalhrl aelgvptvmi sgnhdsarrl gvgagligra gihlrtapsa agtpvvlpda
      121 hgdvafyglp ylepalvkde fgvekaghea vlaaamdrvr adlatraagt rsvvlahafv
      181 tggapsdser disvggvsav pagvfdgvdy valghlhgsq aitervrysg splpysfsea
      241 dhrksmwlvd lgadgsveae ridcpvprrl arirgrleel ladpelarhe eawveatltd
      301 pvrpaepmar lcerfphtls lafdperapd dpdvsyarrl agrddqeiae dfvahvrgtg
      361 pdeheqavlr dafdavrade tlretar
//
LOCUS       WP_009328613             341 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Bacillus].
ACCESSION   WP_009328613
VERSION     WP_009328613.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..341
                     /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=39441
     Region          2..272
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mansrdsyfd nakflliflv vfghiirsyi hdndallhiy kfiytfhmpa filisgyfak
       61 gfnrpgyvkk iawklivpyl ifqgiytlfy sfiddqslta anpfepqwsl wfllslffwn
      121 lllfpftklp akwafaasfa iavlvgyidm isntlslsrt fvffpvflag yylqkdqfkm
      181 lkgwkgkqaa lavlaatfvf yffadfdysw lfgskpysef gdvgiksgln rvallvitfa
      241 stfafmalvp erryfftlwg trtfyvyllh gfiiksfrkt gaeewladyq sltllfiata
      301 iltfclssgf vktvaqpfie lkmtnlirll kkdngynpyl k
//
LOCUS       WP_009330580             385 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [Cytobacillus].
ACCESSION   WP_009330580
VERSION     WP_009330580.1
KEYWORDS    RefSeq.
SOURCE      Cytobacillus
  ORGANISM  Cytobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Cytobacillus"
                     /db_xref="taxon:2675230"
     Protein         1..385
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=41136
     Region          <1..385
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mnntlmgyrr engkvgirnh viilpvddis naaceavarq vqgtmalpha ygrlqygpdl
       61 dlhfrtmigt gsnpnvaavi vigieenwsk kiaegiaetg kpvsyfsieg ngdfetirqa
      121 swkakeyvqw aselqrepie lkdltisikc gesdtttglg scptvsqavd rlvdagatvf
      181 fgetseltgg ehliaqrmat pelhekfmai yedyvgeies kgvdllgsqp tqgniaggls
      241 tieekalgni aktgtkevig vldpaenpdn gnglyfmdts saaaecitlm aaggavlhlf
      301 ptgqgniign piepvvkita npitagtmse hidvdvqgll srqisleeag dklmevicrt
      361 vngrltsaea lghrefvmtk lyrsa
//
LOCUS       WP_009331074             346 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Cytobacillus oceanisediminis].
ACCESSION   WP_009331074
VERSION     WP_009331074.1
KEYWORDS    RefSeq.
SOURCE      Cytobacillus oceanisediminis
  ORGANISM  Cytobacillus oceanisediminis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Cytobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Cytobacillus oceanisediminis"
                     /db_xref="taxon:665099"
     Protein         1..346
                     /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=40744
     Region          1..272
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mkqrdyyfdn tkfiliffvv fghllrsfie dnetiytlyk viytfhmpaf ilvsgffakg
       61 fykkgyikki akklilpyii fqviysifyy flynkgtfel dpfnphwslw flismfcwni
      121 mllffakyka vyslaaafii glavgyadwv snylslsrtf vffplfllgy ylkkehfyal
      181 fqpkfrisal aifavvfigf ylypevdykw llgskpytem gaasigavlt rlgfyvlsli
      241 mvfsffafvp rkqyfftdlg kntlyvyllh gffvrvfres dvqgffskpe nflllagisl
      301 lltlllsskl itsfaqpiie lrtsqlkklk drskayarfy rkklts
//
LOCUS       WP_009331167             652 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Cytobacillus oceanisediminis].
ACCESSION   WP_009331167
VERSION     WP_009331167.1
KEYWORDS    RefSeq.
SOURCE      Cytobacillus oceanisediminis
  ORGANISM  Cytobacillus oceanisediminis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Cytobacillus.
REFERENCE   1  (residues 1 to 652)
  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 652)
  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 652)
  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 652)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..652
                     /organism="Cytobacillus oceanisediminis"
                     /db_xref="taxon:665099"
     Protein         1..652
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=69577
     Region          9..643
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 menkgetlsl eeqqklleky dpeagtrklg gvlgwivffg llafslfhly tgvfgmltaq
       61 lqrsihlgfa lalifllfpa rkkdrgrkhk vawydiilai lgiavgaywp lfideivmra
      121 grlteidfyv gliavllvle atrravglpi tiiaviflay amfgpympaf lahrgldler
      181 lvqtmfftte gilgtplgvs atfiflfllf gsflvktgvg qyfndlavsi agkrtggpak
      241 vaifssalqg tisgssvanv vtsgsftipm mkklgykkef agaveatast ggqimppimg
      301 aaaflmvefi gggitywdia kaaaipally fagvwimthf eakrvglrgl kdeempnrke
      361 vlkkiylllp ilaviillms gmsviraalw sivitvavsm isketrigfr daidalvdga
      421 rtalgvaaat aaagiivgvv vktglglkma nglldlsggl liptlmltmv aaiilgmgsp
      481 ttanyvitst iaapaiillg vpdlsahlfv fyfgivadvt ppvalaafaa agvsggdpik
      541 tgvtasklai gafiipymfv lspellmidt twyyliwvvf talagmmaig agvigywlrk
      601 lniferllgi aggllliype gvtdivglvi fillialqvf ikkddqpkpq ta
//
LOCUS       WP_009331758             366 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GerAB/ArcD/ProY family transporter [Cytobacillus].
ACCESSION   WP_009331758
VERSION     WP_009331758.1
KEYWORDS    RefSeq.
SOURCE      Cytobacillus
  ORGANISM  Cytobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Cytobacillus"
                     /db_xref="taxon:2675230"
     Protein         1..366
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=42048
     Region          11..356
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 mkeqpvperl qispflvfyl vmsmqigigv lgyqriiamd agydawisil fagacihviv
       61 wmiykigdtv ggdivtahky vvgnflgkal cfifigyfil ysltvvrtfi eviqvwmfpe
      121 lstfwfsfgf milcvyiifg gfrtvvgtaf fglvlpayll ltfgwaikfs nfynllpiwd
      181 hsikelltas yhmsltfigf eiilffypfi kepkksqkwa hlavltttli ytilaiitfa
      241 yfsedqlakq iwasltmwki vempfverfe yigianwnli ilpnvcisiw iasrlikrvf
      301 nirqkvgvff vvaavlsvih fldtrekinm lnnyvgkmgf aftflyipll faavmiakkl
      361 kkgkkk
//
LOCUS       WP_009332070             281 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Cytobacillus].
ACCESSION   WP_009332070
VERSION     WP_009332070.1
KEYWORDS    RefSeq.
SOURCE      Cytobacillus
  ORGANISM  Cytobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 281)
  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 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   3  (residues 1 to 281)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 281)
  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   5  (residues 1 to 281)
  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   6  (residues 1 to 281)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Cytobacillus"
                     /db_xref="taxon:2675230"
     Protein         1..281
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32330
     Region          21..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..279
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mdwlermnnv ldyieqnldg eidykkmaei aytsefhfsr mfssisgipl seyirrrrlt
       61 aaafeiqkkd vriidiaaky gydsvdsfsr afkkthgmtp saarkngmql kafpkisfqi
      121 sikgdvemey rienldfelr ivgkgspvkt skafktipsi wnnarkngym qklidmswen
      181 pkctlegllg vcgkeaaitd eefeyfmgir ydgetpsdme tliippgtwa vfpnipeawk
      241 rlysewvpas gyelanlpci ecyygpkhkp khelwvpvrn r
//
LOCUS       WP_009333437             425 aa            linear   BCT 20-JAN-2025
DEFINITION  TerD family protein [Streptomyces ipomoeae].
ACCESSION   WP_009333437
VERSION     WP_009333437.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            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 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..425
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=44901
     Region          11..425
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 msmpkgsnvv vpttalrvel gwrsgpgvpe adasalllva gkvrtdadfv fynqpahssg
       61 avrhegkrdt ggqvtdsllv dlarvepave tvvlaassdg gtfgqvpgly irvlddragt
      121 evarfdskda gvetafvlge fyrrqgawkf ravgqgyssg leglatdfgi tvdepqhaap
      181 appapvappv tapppvtaap pvppapptpp papvrltkvt ltkeapavsl tkqggtsgam
      241 rvnlnwevrk qftgwgsklg ravamhadld ldlcalfels dgskgvvqal gnafgalhrp
      301 pyihldgddr tgavasgenl tinldhkhaf rrilifvtiy egarsfadlh atvtlqpqhg
      361 apvdfsldec tvpstvcala litnqggdli vqrearylvp ergvspqrtv dyaygwgmnw
      421 tpgrk
//
LOCUS       WP_009333498             722 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: molybdopterin oxidoreductase family protein
            [Cytobacillus].
ACCESSION   WP_009333498
VERSION     WP_009333498.1
KEYWORDS    RefSeq.
SOURCE      Cytobacillus
  ORGANISM  Cytobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 722)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 722)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Cytobacillus"
                     /db_xref="taxon:2675230"
     Protein         1..722
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=81444
     Region          15..717
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mqrdkffkei enlnhpnekl ikthcsycgm qcgmnlrvnt qtnkiigvep rydwpvtvgk
       61 mcpkgvtayq qtnhkdrllk plirddaslk gttegfreas wdeaydliak kfkelqtefg
      121 kdslsvfsgv smtnekcylt gkfarvalat ryidyngrfc mssaaggflr sfgvdrgstl
      181 pwtdihetdc lfiagsntae chptsmfriw nvqerggyii vvdpretpia rradlhldlq
      241 pgtdlalang ivnqliemgy ideefinkht ngfeetkelv kdftpeytsm ltgvaeekii
      301 raaeifgkap navvmfargv eqqhkgvdnv saytnmalvt gkigrpkagv atftgqgngq
      361 ggrehgqksd llpgyrkitn pkhveevcsv wgitpeempq pgvsayemie lmeqktirgl
      421 yllcsnpavs apnqnfvrka fkaldfmvcs dfylsesaef advvlpavtw sedegtvtni
      481 egriikinka qepvgeskpd wqiqvelaer lgkgkyfshl ktardvadef rlatkggyad
      541 yygatwdkid kqdgvfwpck nekdegtphm fldkkfyhpd gkakicalpy rppaeepcek
      601 yplrlttgrv vyhylsgnqt rripflhdmc pepfveihpe taskynmehe ervrlftrrg
      661 eaiykvkite airkdtvfvp yhfghedsin lltiaaldpi srmpefkaca aqlekvelkk
      721 vq
//
LOCUS       WP_009333703             318 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-oxoacyl-ACP synthase III family protein
            [Cytobacillus].
ACCESSION   WP_009333703
VERSION     WP_009333703.1
KEYWORDS    RefSeq.
SOURCE      Cytobacillus
  ORGANISM  Cytobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 318)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Cytobacillus"
                     /db_xref="taxon:2675230"
     Protein         1..318
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34124
     Region          4..310
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mfsagvlgig vnipeniitn emiarrfgit qeeicrktgi lerryespds sltdmceiag
       61 kraiedagvn pkdidmviig tnthdthita alvqdrigaa hcagldlhsg cssfitalat
      121 gaqfvqtgly knvlviavdk cssllnpmdk ktallfsdga aavvlgqvdk sngilgihmq
      181 mdgsggkylh ldenkhikmd gravfefavd rfpkavhkvl elsglslqev dfiiphqsnl
      241 riieagtarl gfpmekvhtk tiqyygnssa ptiaiglhee vkegkikdgd vvvlagygag
      301 lgwgaivmrw gqtsrvli
//
LOCUS       WP_009333779             288 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Cytobacillus pseudoceanisediminis].
ACCESSION   WP_009333779
VERSION     WP_009333779.1
KEYWORDS    RefSeq.
SOURCE      Cytobacillus pseudoceanisediminis
  ORGANISM  Cytobacillus pseudoceanisediminis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Cytobacillus.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Cytobacillus pseudoceanisediminis"
                     /db_xref="taxon:3051614"
     Protein         1..288
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31994
     Region          1..255
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mkvelhchtn isdcplside vlnlaianev shlaitnhdt tkglqeaier gkryrvevip
       61 gieisafdfd rarrvhilgy fiepghkaie tlcqpiierr hklsfemvqr lisagysitw
      121 drclelsagg tgvykqhime alietgyads iygsqykklf grgqngeskg vafipmeyvd
      181 arlavkaile aggvpvlahp gqygnfekvp elveaglqgi evwhplhnkq heemarklai
      241 qygltmtggs dfhgaygekp vvlgcmspgv ervhelaarr qrlksqrl
//
LOCUS       WP_009333803             384 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Cytobacillus].
ACCESSION   WP_009333803
VERSION     WP_009333803.1
KEYWORDS    RefSeq.
SOURCE      Cytobacillus
  ORGANISM  Cytobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 384)
  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 384)
  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
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 384)
  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   5  (residues 1 to 384)
  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   6  (residues 1 to 384)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 384)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 384)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Cytobacillus"
                     /db_xref="taxon:2675230"
     Protein         1..384
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42296
     Region          16..>57
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          81..376
                     /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 mekhdqllmk rqnknlvldi lktkspisri diakmtgmsp tsitrivtel qlqgylrete
       61 avasgvgrka tllevrgdvl ytvgieidks llkvgivnyi gemvslhksk rnesesymet
      121 lhkidavirk imdeneipaa kimglavglp gyidykngiv kisdqlkwkd aslaedlqkl
      181 tsfnvivdne lkmkivaesf tgkaknsqns iligigsgig ssimlngdiy rgetnnagei
      241 ghtvidptgn vcncgkigcl atyisegail adsrkvkdvs sikdvfqsyr drepwalnim
      301 drastyiala isnllclynp eviilsgnti eklpemkqai eqkcelyiwe plkqsvrivy
      361 selsengvvl gaaiqaqnlm lele
//
LOCUS       WP_009333851             369 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GerAB/ArcD/ProY family transporter [Cytobacillus].
ACCESSION   WP_009333851
VERSION     WP_009333851.1
KEYWORDS    RefSeq.
SOURCE      Cytobacillus
  ORGANISM  Cytobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Cytobacillus"
                     /db_xref="taxon:2675230"
     Protein         1..369
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=43129
     Region          7..365
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 mnvkvekqfq vsafftffli hssqtgigil nfqsqvikda eqdawislii twvttqiily
       61 mifkllgget ndlvavhqyc fgkalgsims ilalvyfwla sftvlrayie viqiwvypti
      121 ktwqlcfifg ltfyyiissg frslagfsfw gvilpsflff liyfplkhtn fiyllpafsh
      181 slkelfvssk ayallflgfe wilmyypfir ssnnkdiskw ayygntytfi vylvitlisf
      241 syfnqdvlkh lpwptlmmvk ivkfsfierf eyvfifiwll viispicisl wactrivkrt
      301 fsippkatll flliaemias vylqefrsid ylvqitsnag igfvyvylpl lliikwiksh
      361 fmkhklnki
//
LOCUS       WP_009336130             701 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: VirB4 family type IV secretion system protein
            [Cytobacillus].
ACCESSION   WP_009336130
VERSION     WP_009336130.1
KEYWORDS    RefSeq.
SOURCE      Cytobacillus
  ORGANISM  Cytobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Cytobacillus"
                     /db_xref="taxon:2675230"
     Protein         1..701
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=80688
     Region          74..701
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mnltkknsek kieqkkakqv keskvkkkkq sgkdeaisdh qmvtkptmwd iispeglkin
       61 sedfgiikqs lgtktyfrpi yiprdgyprk mqtnwlynls ssgevdvlid vhkvgksdai
      121 rtlqrqitml qsnltfqtkr gnidqindle skirdtdllm seiqfsendm ynvsslgvly
      181 gqsekelnry seaiedemss qffslvstwg rvkkgfksvi pfgkneipds frnidrrals
      241 tfapfisgsg kymggiplgi nkitgqlefi nsfgneeyrp qnynmfvvgi sgsgksvtlk
      301 lliareltga niysrlidpe gefvritrrl gginlnisee edicinplai nftdvpmdeq
      361 deeldlledt dereviekeg kkfirfvplr ekmndildff diicrgknse drgldvfern
      421 yleeavqyif neklkltshp dslfsnevvq vdnqliqskv rkpeptisdv feylkdhyee
      481 epkalrliaa irpflrdgsk pifdgqtylg kgvtqslqda rlvnfnisqm eegflrpiay
      541 hvilnylweh fvknldnatk kkfvyadeaw tlidseqtvs flekmarrar krntglrlas
      601 qdfvrfvtnn kargilqnth aylflqqnki dlkvikenfd lsageinilf gnpdkgegil
      661 rmgkssvwlq tnpseeelff iesnqavyee qmkrkqlmeq r
//
LOCUS       WP_009337385             201 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Afipia sp. 1NLS2].
ACCESSION   WP_009337385
VERSION     WP_009337385.1
KEYWORDS    RefSeq.
SOURCE      Afipia sp. 1NLS2
  ORGANISM  Afipia sp. 1NLS2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Afipia.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Afipia sp. 1NLS2"
                     /db_xref="taxon:666684"
     Protein         1..201
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21376
     Region          6..174
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 msgrlrivvg isgasgaalg vrvvellaet gqcdihlvvt hhaertllhe vgrnalsala
       61 amatrhhade digasiasgs frtagmivap csirtlsaia tsaaknllvr aadvqlkerr
      121 rlvlmvretp lhlghlramt aateigaiia ppvpafyhkp asmaavidqi arraidlldl
      181 dlhlpvhewe gedrirdagq r
//
LOCUS       WP_009335155             161 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Cytobacillus].
ACCESSION   WP_009335155
VERSION     WP_009335155.1
KEYWORDS    RefSeq.
SOURCE      Cytobacillus
  ORGANISM  Cytobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Cytobacillus"
                     /db_xref="taxon:2675230"
     Protein         1..161
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17907
     Region          3..157
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdiqkiittr rnikkfksdk vehslitswl eaasmapnhk mtepweilfv gpetraklnh
       61 ktdfcqapvv lailsrhgat dlertenmaa vscfiqnfml mawesgvgtf wsslgvsaaa
      121 rtalnvpddy dvvgilgvgf peevpeaker tpierkirhl s
//
LOCUS       WP_009337509             286 aa            linear   BCT 20-JAN-2025
DEFINITION  MJ0042-type zinc finger domain-containing protein [Afipia sp.
            1NLS2].
ACCESSION   WP_009337509
VERSION     WP_009337509.1
KEYWORDS    RefSeq.
SOURCE      Afipia sp. 1NLS2
  ORGANISM  Afipia sp. 1NLS2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Afipia.
REFERENCE   1  (residues 1 to 286)
  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 10020205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Afipia sp. 1NLS2"
                     /db_xref="taxon:666684"
     Protein         1..286
                     /product="MJ0042-type zinc finger domain-containing
                     protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31450
     Region          1..38
                     /region_name="MJ0042_CXXC"
                     /note="MJ0042 family finger-like domain; TIGR02098"
                     /db_xref="CDD:131153"
ORIGIN      
        1 mqiicphctt fydvdsskfg aagrnvrcar cgetwlakpe sasamagpdp feevdagwgl
       61 aaetpvreed tphvqspsia adwqdeyash eatdgedepr asrrpewlqs llrplqpmlq
      121 trflsgitsr ipgvphlrpp kvslaftsta maavclglii wradvvrlmp qtgpffkiag
      181 lgvnlrglef dklqlssemv ngksvlviqg amknitrkpv elprlrfivr dqngtdiyaw
      241 nsvleqpvlk anerlafksr lasppaegre iavrffqrrd igagat
//
LOCUS       WP_009339144             362 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Afipia sp. 1NLS2].
ACCESSION   WP_009339144
VERSION     WP_009339144.1
KEYWORDS    RefSeq.
SOURCE      Afipia sp. 1NLS2
  ORGANISM  Afipia sp. 1NLS2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Afipia.
REFERENCE   1  (residues 1 to 362)
  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 362)
  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 362)
  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 362)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Afipia sp. 1NLS2"
                     /db_xref="taxon:666684"
     Protein         1..362
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39655
     Region          1..354
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkrrdflkvt aagaataava spaiaqsspe vkwrltssfp ksldtiygaa elmakqvaem
       61 tdnkfqiqvf aagevvpglq aldatsngtv emchtatyyy vgkdptfaiy aavpfglnar
      121 mqnswwyqgg geqlaneffk khgviahpcg ntgtqmggwf rkeiktvsdl sglkmriggi
      181 agqvlaklgv vpqqlaggdi ypslekgtid aaewigpydd eklgfnkvap yyyypgfweg
      241 glmvhsltnl ekwnalpkhy qsilananan antlmaaryd lqnpgalkrl vaggtqlrpf
      301 snevleaslk atntlwaeis aknpdfkksi damqayrgde ylwwqvaeyt fdsfqirsrt
      361 rg
//
LOCUS       WP_009339171             633 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Afipia sp. 1NLS2].
ACCESSION   WP_009339171
VERSION     WP_009339171.1
KEYWORDS    RefSeq.
SOURCE      Afipia sp. 1NLS2
  ORGANISM  Afipia sp. 1NLS2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Afipia.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 633)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 633)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 633)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Afipia sp. 1NLS2"
                     /db_xref="taxon:666684"
     Protein         1..633
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68504
     Region          11..633
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 maatepptdl pteaapahgf wsltvgsigv vfgdigtspl yafreaahsa agagvitrpi
       61 vlgvlslvlw alfvvvtaky vllllradnn geggtlslma lgqralgrra wvllalgvvg
      121 aamflgdsmi tpaisvlsav eglklaapef ehyvvpltvl ilvilfavqs sgttriaaaf
      181 gpvmilwfil lavlgawhia ddptvlaain pyyavsfmlt hgeislvtlg avflcvtgge
      241 alyadlghfg rkpiqaawly fvlpalliny fgqgamllah pdkidntfyh mvpsyllvpv
      301 iilataatvi asqavitgay sltrqaiqlg llprfevryt sevhagqiyl prvntlllig
      361 vlllvglfrt ssglasaygi avsttmvadg imgfivvwkl wnwraataaa liaplvfvdt
      421 sffianllkl fegawvpllf glclvamiwt wrrgtgilln ktrrtevplr dlikslekrp
      481 phvvkgtavf ltsdpefvpt allhnlkhnk vlhehnvilt irtattprvd pidrveyegi
      541 sekfsivrln fgfmetpnvp kalaiarklg wqfdimatsf fvsrrslkpa aqssmplwqd
      601 hlfiamsksa ndatdyfqip tgrvvevgtq vti
//
LOCUS       WP_009339509             438 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein [Afipia
            sp. 1NLS2].
ACCESSION   WP_009339509
VERSION     WP_009339509.1
KEYWORDS    RefSeq.
SOURCE      Afipia sp. 1NLS2
  ORGANISM  Afipia sp. 1NLS2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Afipia.
REFERENCE   1  (residues 1 to 438)
  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 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   3  (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   4  (residues 1 to 438)
  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 438)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Afipia sp. 1NLS2"
                     /db_xref="taxon:666684"
     Protein         1..438
                     /product="CmpA/NrtA family 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=47498
     Region          45..306
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 msksstdvig kstsrravlk agagavalma aarlnfpgga faqtagpett karlgfialt
       61 daaplfvake kgffakhgmp dvtvekqasw gttrdnlvlg segngidgah iltpmpyqis
      121 agtvtqnnvp tpmhilarld lncqgisvan eyadlkvgld akplaaafek kraagksika
      181 amtfpggthd lwirywmaag gidpdkdvet ivvpppqmva nmkvgtmdcl cvgepwneql
      241 ihqkagysal ttgeiwkdhp ekvlgmraaw veknpraaka llmavmealq wcdkdsnkde
      301 laaisakrqw mnvpvgdide rikgnfdygt grvernspll mkfwrdhasy pfqshdlwfl
      361 tenirwgkmp astdtkalia kvnredlwrd aaktlgvaaa dipastsrgk etffdgkvfd
      421 penpaaylks ltikrvda
//
LOCUS       WP_009340466             423 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Afipia sp. 1NLS2].
ACCESSION   WP_009340466
VERSION     WP_009340466.1
KEYWORDS    RefSeq.
SOURCE      Afipia sp. 1NLS2
  ORGANISM  Afipia sp. 1NLS2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Afipia.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Afipia sp. 1NLS2"
                     /db_xref="taxon:666684"
     Protein         1..423
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=45570
     Region          15..423
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mslgnivemk spfpgtatdq lttkispntr askdfknakf wgwrrengrv gvrnhvlilp
       61 lddlsnasce avannikgti aiphsygrlq fgedlelhfr tligtgsnpn vaavvvigie
      121 egwtsrvveg iaktgkpvvg fgiethgdia tiakasyqak rfvqwatelr reecsiselw
      181 vstkcgesdt ttglsscptv gnmydklipq giygvfgets eitgaehlck eraaspeiad
      241 kwykmwkayq ddvieahktd dlsdsqptkg niagglssie ekalgnleki ghkskfidal
      301 epaeapakgp glyymdtssa aaecvtlmaa agyvihtfpt gqgnvignpi vpvikisgnp
      361 ktvrtmgehi dvdvsgvlrr dmtldqagda lidmisrtan grltaseslg hrefvltkly
      421 rsa
//
LOCUS       WP_009340666             288 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Afipia sp. 1NLS2].
ACCESSION   WP_009340666
VERSION     WP_009340666.1
KEYWORDS    RefSeq.
SOURCE      Afipia sp. 1NLS2
  ORGANISM  Afipia sp. 1NLS2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Afipia.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Afipia sp. 1NLS2"
                     /db_xref="taxon:666684"
     Protein         1..288
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31762
     Region          9..280
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 msgadvsgad dasycaqlvr dhdferyaat lfmpprarrp vlalyafnte lrrirdhvsq
       61 plpgeirlqw wrdlvdgdar gsveanpvaa elmaavanhd lprnelsrlv darvfdlydd
      121 pmlsldmler ycddtagrlf slsarilggt seavahaalh agiaqgivra veglplhasr
      181 kqlylpqdvl seagvkeadi fagrstpqlq tairvlaeva rshrgkaadl liavpadakr
      241 vflplalvrr aldparmpaq npfalvpqsr lrmlwtlwra tkseefrd
//
LOCUS       WP_009339794             710 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter permease [Afipia].
ACCESSION   WP_009339794
VERSION     WP_009339794.1
KEYWORDS    RefSeq.
SOURCE      Afipia
  ORGANISM  Afipia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 710)
  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 710)
  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 710)
  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 710)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Afipia"
                     /db_xref="taxon:1033"
     Protein         1..710
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=76258
     Region          28..700
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mlqeqgtqeh vsveldnfeh gfppgfgpgw wghlayvigi afsafqimva awnflptqsv
       61 rgihvgflil lsyglvanft aktnwqrllg watggvgfyc glyqwlyyad liqrdgdpsr
      121 ldlvvgtvla ilifdatrrl mgwalplmcg acivywafgq ylpspfnhrg yyfdqivthl
      181 sygtegfygv piyvsatyif lfilfgsfle ragmiqlftd fslglfggtr ggpakvavva
      241 sgmmgtisgs gvanvvtvgq ftiplmirfg yrrafaagve atasmggqim ppvmgavafi
      301 maetlgvqys vivqaavipa ilyfasafwm vhleagkygl vgmkkeeipn awralvkgwy
      361 lvlplaalvf mlfegftply agsmglaltv tlilgtsiva gfptqviryv fwiglalvvg
      421 slfrngtsvd iryvaavvla lvllsaltrg gratlvacrd slaessksal tvgmacaivg
      481 tiigmmtqtg vgtvfgswvi glgkqslfla limtmllsil lgtgiptipt yiivaalaap
      541 alahlgvpli vshmfafyyg imadlsppva laalaaapia kenpdkigwe amrialagyv
      601 ipfiavyspa lmmqasdpmv atlgfygavf yaflkalvai alfgmvaigf lftrmtvier
      661 mvafaaalml lgefaysdel gyvlaiavfl wqwrkrpapp lkvapestvp
//
LOCUS       WP_009343641             228 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Cylindrospermopsis raciborskii].
ACCESSION   WP_009343641
VERSION     WP_009343641.1
KEYWORDS    RefSeq.
SOURCE      Cylindrospermopsis raciborskii
  ORGANISM  Cylindrospermopsis raciborskii
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Aphanizomenonaceae; Cylindrospermopsis.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Cylindrospermopsis raciborskii"
                     /db_xref="taxon:77022"
     Protein         1..228
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25632
     Region          31..223
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mvvnfaptta greylrrvfq gldkqscpkl fnfhahtvfs dgklhphilm eqaitiglkg
       61 laitdhhsve gyekaknwle ewqwhhpfsp vphlwsgvei naelldvevh ilgygfevgh
      121 hrmkpylqre ptrgedhkal nviaavhdag giavlahpvr ykkshfelip kaaelgidgv
      181 esfyayknpi pwepcpqpta evqmlaeeys lvstcgtdth glnllqrl
//
LOCUS       WP_009345585             123 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: zinc ribbon domain-containing protein
            [Peptoniphilus].
ACCESSION   WP_009345585
VERSION     WP_009345585.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus
  ORGANISM  Peptoniphilus
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae.
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 12181465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Peptoniphilus"
                     /db_xref="taxon:162289"
     Protein         1..123
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14369
     Region          24..120
                     /region_name="zinc_ribbon_15"
                     /note="zinc-ribbon family; pfam17032"
                     /db_xref="CDD:465334"
ORIGIN      
        1 mfficgitng kddlsydedl fvhscgaygr yqvfmtyfkl slffitilkf nkkyfvkttc
       61 cdriygldks lgqkiensid viineddlie ieyeqnsnfk ickncnyktd keflycpkcg
      121 qkl
//
LOCUS       WP_009347484             399 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Alloprevotella rava].
ACCESSION   WP_009347484
VERSION     WP_009347484.1
KEYWORDS    RefSeq.
SOURCE      Alloprevotella rava
  ORGANISM  Alloprevotella rava
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Alloprevotella.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Alloprevotella rava"
                     /db_xref="taxon:671218"
     Protein         1..399
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43641
     Region          1..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkilvincgs ssikyklydm tdksvlaagg iekvglagsf nkvalpngek kiishecpth
       61 tegiklmfdt lldpeigaik sldeidaagh rivaggtytk sqivtdemle gwkpfmelap
      121 lhssahlkgy lavraqlpnl pqvfvfdtaf hqtmppkafm yglpynyytd ynfrrygahg
      181 tshryvtara gevlgfdpkd vrmitchign gasisavdhg kcvdtsmglt plegvmmgtr
      241 tgdidssail yimekehqtp eeaidllnkk sgllgisgvs sdmrevedaa ekgneraqla
      301 ldmysyrikk yigaytavmg gvdvivftag vgehqwdvrk atmegmeylg iqldqekner
      361 nngeeelisl peskvkvavi ptdeelmias dtkslvakq
//
LOCUS       WP_009347708             152 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Alloprevotella rava].
ACCESSION   WP_009347708
VERSION     WP_009347708.1
KEYWORDS    RefSeq.
SOURCE      Alloprevotella rava
  ORGANISM  Alloprevotella rava
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Alloprevotella.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Alloprevotella rava"
                     /db_xref="taxon:671218"
     Protein         1..152
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16515
     Region          2..149
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 meqkykdvis avralisgek eemsvlanva aelhdsmgyf wvgfylvreg elhlgpfqgp
       61 vacyrirhgr gvcgtaweqa ktlivpdvea fpghiacssl srseivvplr nakgevvgvl
      121 didskelnaf tpaegemlee vcaaitetly se
//
LOCUS       WP_009348491             658 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Alloprevotella rava].
ACCESSION   WP_009348491
VERSION     WP_009348491.1
KEYWORDS    RefSeq.
SOURCE      Alloprevotella rava
  ORGANISM  Alloprevotella rava
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Alloprevotella.
REFERENCE   1  (residues 1 to 658)
  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   2  (residues 1 to 658)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Alloprevotella rava"
                     /db_xref="taxon:671218"
     Protein         1..658
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=75547
     Region          52..100
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkhaalvlfl lfpitlfaqe ryiswtdfad tyfdeqssee lqeqlenlyl hpmnlntvsr
       61 ddllrlpfld eaqadsilay rdrhhqfltl gelqfitgls ytdrcylslf lqalplpqqv
      121 aplkvrlfsg rheletrldi plyrrrgeqd daylgsglyn nlryrydwhr rvqygltlek
      181 dagepigryr nypydalsay ahyhspnnry ellagdytvt igqgllfgca tygakatlld
      241 aprrtamvlh nhsslsearf frgmaggirh gnwqltafls yrqldsrqeg dtvrsflydg
      301 yhrtarelsr rrnvdnltag gqllylrpqw rigvsglyth ydhfllperr aytqyfmrgk
      361 daaglsvsyy lhshrftlsg eaatdrrlhl avtntlvysp fsscqltlqh rafaprfvsp
      421 hgdalqegsr vanehglflg gkysgfrrle lrgyvdffrf ptstfratga sqgfdamaqv
      481 lwqlktggql llryrakakq qnipkyagll qyatthrlra qlnlrnyrwe lhpaidiala
      541 gkqttgntlg wmlslrtgfr ptstlklaal aavfftddya sacyvyepyl rhaggfgacy
      601 yhglrtallg qwqltkkwdi gvkysllhyf nksaigageq lissaskndf slqlrwrf
//
LOCUS       WP_009348963             381 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Selenomonas artemidis].
ACCESSION   WP_009348963
VERSION     WP_009348963.1
KEYWORDS    RefSeq.
SOURCE      Selenomonas artemidis
  ORGANISM  Selenomonas artemidis
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Selenomonas.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Selenomonas artemidis"
                     /db_xref="taxon:671224"
     Protein         1..381
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41529
     Region          1..268
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          265..355
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrfihtadwh lgklfgqrhm tedqayvlde lialcddlrp dalviagdiy draipppeav
       61 alfsetlakl alrgvkvlfi agnhdsavrl gfgaellras gvylagmvra aeppvvlsdd
      121 ygdiyfslip ygdpphvkda faletmpsfd aalgvqiaaa raqipagars vavahafvig
      181 gqtsesehal svggsdqvga enfatydyta lghlhapqra gaehirysgs llkysfdevr
      241 qkkgaelvei dgagaashtf ypltprhdvr ivsglmnelm aegfdplphd dyicvellds
      301 davlaahekl rhiypnlfsi trpnvnmgrl ssneriyerg kselhlfaef fadvtrekls
      361 aeeehalirv idglekeare a
//
LOCUS       WP_009352738             205 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein, partial [Veillonella sp. oral taxon
            780].
ACCESSION   WP_009352738
VERSION     WP_009352738.1
KEYWORDS    RefSeq.
SOURCE      Veillonella sp. oral taxon 780
  ORGANISM  Veillonella sp. oral taxon 780
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Veillonella.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Veillonella sp. oral taxon 780"
                     /db_xref="taxon:671229"
     Protein         1..>205
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          1..>204
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mlvdfhmhtn vsdgtymprd lvalakekrl qaisitdhde vgayaqlttn drtgiqifhg
       61 cefstyyhek evhvlgyqfs lehpelqdyi shfkevrrsr ihkmvdkcad agydisyeel
      121 vntftdavsf grphiaqlli ahgyvetvge afdtmlnpkg pcfvpkekye pqqaidlihr
      181 aggiavlahp klvendtyvn elldl
//
LOCUS       WP_009353598             190 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [unclassified Veillonella].
ACCESSION   WP_009353598
VERSION     WP_009353598.1
KEYWORDS    RefSeq.
SOURCE      unclassified Veillonella
  ORGANISM  unclassified Veillonella
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Veillonella.
REFERENCE   1  (residues 1 to 190)
  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 190)
  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   3  (residues 1 to 190)
  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   4  (residues 1 to 190)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 190)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 190)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="unclassified Veillonella"
                     /db_xref="taxon:2630086"
     Protein         1..190
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21098
     Region          1..190
                     /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"
ORIGIN      
        1 mrvlvvddes lirmdlrdil esqghtvvge gcngveaiql cqavqpdivl mdvkmpeldg
       61 ieaarqirhq rlapvvllta ysqddliqka sqsgvygyli kplresdlgp alqmamgrfq
      121 eeenlleqvk glessleerk yvakatgilm elhgfseeka yekirafsmd krisvvdtck
      181 kiiaaheaks
//
LOCUS       WP_009358054             349 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Arthrobacter
            nitrophenolicus].
ACCESSION   WP_009358054
VERSION     WP_009358054.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter nitrophenolicus
  ORGANISM  Arthrobacter nitrophenolicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Arthrobacter nitrophenolicus"
                     /db_xref="taxon:683150"
     Protein         1..349
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=36693
     Region          15..344
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mtldlnaalh arnfdvsftl eatetvavlg pngagkstll giiaglirpd sgnavlgqkr
       61 lfkldrgtnh flpphtrgta llaqepllfp hmsvlenvaf gpraaganrt nalqtawhwl
      121 teveaeefad rrpaqlsggq aqrvaiaral atdpelllld epmaaldiha apmlrrllkr
      181 vlanrraiii thdvldalvl adratiiegg riteegstrq vlekprskfa aglagmnllp
      241 gtitghglts hgglditahp edgavpgqng vavfsptavs vfpsaehgsp rnsfavtitd
      301 lephgdqirv hagglsadit paasvdlglt pgmrvhfvik ataiavypa
//
LOCUS       WP_009357744             283 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Arthrobacter
            nitrophenolicus].
ACCESSION   WP_009357744
VERSION     WP_009357744.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter nitrophenolicus
  ORGANISM  Arthrobacter nitrophenolicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 283)
  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 283)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Arthrobacter nitrophenolicus"
                     /db_xref="taxon:683150"
     Protein         1..283
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29022
     Region          1..249
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mrtrldhlvt salqqgsavp aftcydftta lavvgaaees glgaillvap ktaatpnglr
       61 lisalrglad aasvpvavql dhamdlnvma davaagadsv ladgsslpye dnialvvsar
      121 allgpdvvle aelgdlagde drafgadksg asvagltdsa qvedfvartg aqllavavgn
      181 vhgkykgdpq lrwdvlqdia vrthiplvlh gasgipaeel vkaaamnvgk vnfntelrtg
      241 vlatlqkqlp ghradgenlq allghwtrta kdfaagtlat ltr
//
LOCUS       WP_009358436             207 aa            linear   BCT 20-JAN-2025
DEFINITION  phosphonate ABC transporter ATP-binding protein [Arthrobacter
            nitrophenolicus].
ACCESSION   WP_009358436
VERSION     WP_009358436.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter nitrophenolicus
  ORGANISM  Arthrobacter nitrophenolicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
REFERENCE   2  (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   3  (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   4  (residues 1 to 207)
  AUTHORS   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 207)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Arthrobacter nitrophenolicus"
                     /db_xref="taxon:683150"
     Protein         1..207
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=22388
     Region          1..200
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mrsltgfapi tagtarvagy dvtnlrrgdl rklrsdvgqv fqqfnliprl svltnvltga
       61 lheagpinlt ggfgsrhrrq ameyldrvgi ahkakdpars lsggqqqrva iaralmqqpr
      121 vifadepvas ldpklagsvl ellreiared gipvlvslhv lplalrhcdr ivglrhgrvl
      181 vsapaaqlda qqlsvlydee gqpgdhh
//
LOCUS       WP_009359135             173 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Arthrobacter nitrophenolicus].
ACCESSION   WP_009359135
VERSION     WP_009359135.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter nitrophenolicus
  ORGANISM  Arthrobacter nitrophenolicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Arthrobacter nitrophenolicus"
                     /db_xref="taxon:683150"
     Protein         1..173
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=18755
     Region          28..168
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mkgrapktgy sreefgpawa dvdrngcdtr ndilardltg etfkpgtnnc vvvtgtladr
       61 ytgtiidfvr gqdtssavqi dhlvalsdaw qkgaqqltae erkdlandpl nlmaadgptn
      121 gakgdkdaat wlppnrafrc eyvvrqtavk akyklwvtqa ehdaitgvln gcr
//
LOCUS       WP_009359227             398 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Arthrobacter
            nitrophenolicus].
ACCESSION   WP_009359227
VERSION     WP_009359227.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter nitrophenolicus
  ORGANISM  Arthrobacter nitrophenolicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 398)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Arthrobacter nitrophenolicus"
                     /db_xref="taxon:683150"
     Protein         1..398
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=41841
     Region          12..388
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mpddlrylkf vrsadvykgg rlaghlnrtd rgsvvfsytp gyleaegkpv attlplasgp
       61 veapsgalpa ffsgllpegh rltalkdavk tsfgdelsll lavgadvpgd vqvvpegapa
      121 adppaladts rpedldfaal ahavdthglp gvqakasasm lttpltlahh ryllkldppr
      181 hpnlvvneaa hlagakrlki pvarhsvvtd rnglpgllve rfdrgqdngl vrlaledaaq
      241 vlnlppasky avsseevala lgglcrakav aarnlylqfv fawltgngdl haknaaileg
      301 rnggwmvapm ydipctllyg ddsmalpiag kvknlkarhw rdfaagiglp eraaaaankv
      361 alsaasaidl ealpftgspl rgtlrelrfr rgelagsa
//
LOCUS       WP_009363713             196 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Brucella].
ACCESSION   WP_009363713
VERSION     WP_009363713.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            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="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20972
     Region          1..189
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mkrivigvsg asgcliplki lerlavmeev ethlvisdaa qqtlryelga ngysllyrla
       61 artyavedvg aaiasgsvpt agmiiapcsm rtlsaiangy sdslltraad vhlkerrklv
      121 liaretplhl vhlrnmctvt emgaivmppv pafylqpqtv edvasqvaar aidligvgtp
      181 qaqswnpeek prrkag
//
LOCUS       WP_009363299             277 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phytoene/squalene synthase family protein
            [unclassified Brucella].
ACCESSION   WP_009363299
VERSION     WP_009363299.1
KEYWORDS    RefSeq.
SOURCE      unclassified Brucella
  ORGANISM  unclassified Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="unclassified Brucella"
                     /db_xref="taxon:2632610"
     Protein         1..277
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30509
     Region          1..275
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mnqnethcla llreadrdry lsvlyapqek rgalaalyaf naeiarirdl vheplpgevr
       61 lqwwrdling eargsaeahp vaaalietie kyelpriafd nycearvfdl yddpmpsrnd
      121 legycgetas aliqlagfil drdaaqahae taghagvaqa vagslrllpi hrrrgqvyvp
      181 admlkaigvt rdmllssedt sateravtim lalarehlai fdkakaglpq tlhpaflpma
      241 lvpaylnave rlgaqaaqkv adisairkqw lmfranf
//
LOCUS       WP_009364783             312 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella sp. BO2].
ACCESSION   WP_009364783
VERSION     WP_009364783.1
KEYWORDS    RefSeq.
SOURCE      Brucella sp. BO2
  ORGANISM  Brucella sp. BO2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
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
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Brucella sp. BO2"
                     /db_xref="taxon:693750"
     Protein         1..312
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=34356
     Region          1..309
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 miefdritkn yngraavdev sftiephsia aivgtsgsgk ttllrmvnrl eeptsgeiri
       61 dgqsildepg helrrrigyv iqqhglfphr tvgeniatvp vllgwpkqri earvdellel
      121 fqlepdayrd ryphelsggq qqrvgvaral aagpnillmd epfgaldpvi rakaqedlka
      181 iqrrfgttil lvthdmeeai slgdriavmd egkllqfgpp aeilarpate fverlvgtge
      241 rpfrllsltd lktvlqpgda sgeplpvtas qrdalaellw sgrralpvld edgrslgrvt
      301 leklvhqaer pa
//
LOCUS       WP_009368379             401 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease, partial [Bilophila sp. 4_1_30].
ACCESSION   WP_009368379
VERSION     WP_009368379.1
KEYWORDS    RefSeq.
SOURCE      Bilophila sp. 4_1_30
  ORGANISM  Bilophila sp. 4_1_30
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Bilophila.
REFERENCE   1  (residues 1 to 401)
  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 401)
  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 401)
  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 401)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Bilophila sp. 4_1_30"
                     /db_xref="taxon:693988"
     Protein         <1..401
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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]"
     Region          <1..393
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 alfgtisgsa aanvygtgtf tiplmkkvgy tphfagavea vastggqmmp pimgaaafim
       61 advigvsylt iakaalipsv lyyltllaii hleavsknmg tlppelvpsa asvlrrlyyl
      121 fplvflitil lmgrsviaca yygtvcivil smirsetrft fkrlcgalel saknammvss
      181 ccacagiiig visltgigyk finvitalag snllllmaml mvtciilgmg vptapayiiv
      241 atlgapalmk agvpiiaahm fvyfyailsv itppvclaaf agaaiaetna mktgvtamkl
      301 givafiipfm fvfepallmq gstteivtaf tsalvgvigv asgiqnwllv rcrlwerall
      361 lasglmlifp glitdtigls sllivlfaqr lrrsgspvaa a
//
LOCUS       WP_009368623             645 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Bilophila sp. 4_1_30].
ACCESSION   WP_009368623
VERSION     WP_009368623.1
KEYWORDS    RefSeq.
SOURCE      Bilophila sp. 4_1_30
  ORGANISM  Bilophila sp. 4_1_30
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Bilophila.
REFERENCE   1  (residues 1 to 645)
  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 645)
  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 645)
  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 645)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..645
                     /organism="Bilophila sp. 4_1_30"
                     /db_xref="taxon:693988"
     Protein         1..645
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=68518
     Region          8..634
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mrlglffkeg rrrklsplws rivgvlvvlf aavelygapf gfidsfilrs lfvsfaitlt
       61 ficytpirte pgqsenvpvl dillacisla agaymvmnga elvtrwtgvd pltpadwvvt
      121 atfvlltlev trrtvgpvll giilvfivyn fvgeylpgyf ghrgstmevf ldrmvytydg
      181 ifgtpvgvac tyvfmfvlfg qvfnaagggn fffrlaasia grmrggpaki cviasalygt
      241 lsgspvsdvv ttgsitiplm krlgygetfs gavaasacsg asilppimgt aaflmvdvag
      301 ipyieiaiaa tlpaiiyyfg lmmqvhyrav lkgirpised tdhesawtvl kenwlyiipi
      361 allvtliiqr vnptvvglla tasvvviswl ipghrmgike lyevirktgl giltvanasa
      421 aagmviggim ltglggkfts lvfaatggqs glclsmvaiv ciilgmgmpv paayvltatl
      481 aapallefkf slmsahlfiv yfsaisaitp pvavaayaaa gisegdpnat gvqavrlava
      541 ayivpfvfmy rpalildgsl peilwtavva taavysfasg legylhgrlr fplrlalmaa
      601 gvvfvwpdtw adltgfailg avtahqyair knnpdpvcla qpqge
//
LOCUS       WP_009368655             374 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Bilophila].
ACCESSION   WP_009368655
VERSION     WP_009368655.1
KEYWORDS    RefSeq.
SOURCE      Bilophila
  ORGANISM  Bilophila
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae.
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   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   3  (residues 1 to 374)
  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   4  (residues 1 to 374)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 374)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 374)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 374)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Bilophila"
                     /db_xref="taxon:35832"
     Protein         1..374
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39914
     Region          27..363
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(100..102,123..124,172,225,249)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkkrmgivaa vatamlcssf afaapikigl mapitgafas egqdmqkice lmteelnkag
       61 gingnkvqlv ieddgstprs aataasrlva advcaaigty gsavteasqd iydeagivqi
      121 gtgstsirlt akgmkrffrt cprddeqgrv aqstlakfgf kkvailhdns ayakgladea
      181 kqrildkksa divffdalvp gerdysailt kikgvkpdai lftgyypeag lllrqmqemk
      241 wavpiiggda tnntdlvkia gdaaagyrfi spimpadidt pmakaflkay eakyhslpss
      301 iwsvlagday nvliaaikak gpdpaaiagy lhndlknldc ftgqisfdek gdrvgdlyrl
      361 yevnakgefi lqpk
//
LOCUS       WP_009368700             287 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease, partial [Bilophila sp. 4_1_30].
ACCESSION   WP_009368700
VERSION     WP_009368700.1
KEYWORDS    RefSeq.
SOURCE      Bilophila sp. 4_1_30
  ORGANISM  Bilophila sp. 4_1_30
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Bilophila.
REFERENCE   1  (residues 1 to 287)
  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 287)
  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 287)
  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 287)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Bilophila sp. 4_1_30"
                     /db_xref="taxon:693988"
     Protein         1..>287
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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]"
     Region          10..>287
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 msfaltregi kpvakgfala lalfqiwftt gfgvldgsmm rvmfvsfitv lvflfipgrk
       61 ykenekeptl fllidlccag laiatavyfa lhlteittrm ryiddvtpaa kffaaatvll
      121 vleitrrttg walvivastl ilyaffgdml pravkhtgft fdvivehlfl lnegvygipi
      181 gvatstlfgf imfgaflers kmssifmdla clltrnsqgg pakvaifasa lfgtisgsaa
      241 anvygtgtft iplmkkvgyr apfagaveav astggqlmpp vmgtaaf
//
LOCUS       WP_009369000             107 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Bilophila].
ACCESSION   WP_009369000
VERSION     WP_009369000.1
KEYWORDS    RefSeq.
SOURCE      Bilophila
  ORGANISM  Bilophila
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae.
REFERENCE   1  (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   2  (residues 1 to 107)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Bilophila"
                     /db_xref="taxon:35832"
     Protein         1..107
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11744
     Region          27..93
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkklmsfvca alfafsfcav mpsnafsadp nrqevenrfe lnsataeela gtgavsleva
       61 kkivelrdql gsfqsyddln elelpkdqmd klrwnttiqg iasdcnc
//
LOCUS       WP_009370081             271 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Megasphaera lornae].
ACCESSION   WP_009370081
VERSION     WP_009370081.1
KEYWORDS    RefSeq.
SOURCE      Megasphaera lornae
  ORGANISM  Megasphaera lornae
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Megasphaera.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Megasphaera lornae"
                     /db_xref="taxon:1000568"
     Protein         1..271
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30374
     Region          1..241
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mkvdlhmhtt csdgvytpqe lirraaqani rilaitdhdt veahvsgytr sqevevirai
       61 emssrygeed vhilgydidv rnqalqsycr dysqrrkira rrmfqrcldl gytldaqafe
      121 allakkgsvg rphiarllie kgyftevgev fhailhrgap ayvpyeresi aaciqlihqa
      181 ggmavlahpg liadgleavl qypfdgmevy hpkqrgyfdt yeklacghhf lmtggsdyhg
      241 tkgrfpenvg gftvesgqie aflqarqrsn a
//
LOCUS       WP_009370895             318 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Lysinibacillus capsici].
ACCESSION   WP_009370895
VERSION     WP_009370895.1
KEYWORDS    RefSeq.
SOURCE      Lysinibacillus capsici
  ORGANISM  Lysinibacillus capsici
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lysinibacillus.
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
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Lysinibacillus capsici"
                     /db_xref="taxon:2115968"
     Protein         1..318
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=35642
     Region          1..306
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mitfdnvskq ydnnqiavka lnveikkgef fviigpsgcg kttllkminr lipltagtiw
       61 indkrisdyn ihelrwsigy vlqqialfph mtieeniavv pelkkwsktk ihqrvdella
      121 lvglepakyr qrkpkelsgg eqqrvgvvra laadpeiilm depfsaldpi srtklqddll
      181 emqrtiqkti vfvshdmqea lklgdrlcim kdgeivqigt pqqllqnpvn dfvqqfiggk
      241 qldqlftihd vlqpitvtnd fghtipvdap fpmileklae hdllgveeng kligmvtras
      301 tlrylaadsk krghghgg
//
LOCUS       WP_009375201             112 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Brevibacterium].
ACCESSION   WP_009375201
VERSION     WP_009375201.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium
  ORGANISM  Brevibacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Brevibacterium"
                     /db_xref="taxon:1696"
     Protein         1..112
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12507
     Region          1..83
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
ORIGIN      
        1 mddvvvervl rivefvpsgr vvsygtvglv arcspryvgr vmkeygsnvt wwrvinaagr
       61 lpdpllgrar ekwedegtah rhdkaltsaf itfeeldalw sahgrdpgeq ld
//
LOCUS       WP_009375666             258 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YaaA family protein [Brevibacterium].
ACCESSION   WP_009375666
VERSION     WP_009375666.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium
  ORGANISM  Brevibacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Prahlad,J., Yuan,Y., Lin,J., Chang,C.W., Iwata-Reuyl,D., Liu,Y., de
            Crecy-Lagard,V. and Wilson,M.A.
  TITLE     The DUF328 family member YaaA is a DNA-binding protein with a novel
            fold
  JOURNAL   J Biol Chem 295 (41), 14236-14247 (2020)
   PUBMED   32796037
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Liu,Y., Bauer,S.C. and Imlay,J.A.
  TITLE     The YaaA protein of the Escherichia coli OxyR regulon lessens
            hydrogen peroxide toxicity by diminishing the amount of
            intracellular unincorporated iron
  JOURNAL   J Bacteriol 193 (9), 2186-2196 (2011)
   PUBMED   21378183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006857
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Brevibacterium"
                     /db_xref="taxon:1696"
     Protein         1..258
                     /product="YaaA family protein"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=27697
     Region          2..255
                     /region_name="YaaA"
                     /note="DNA-binding protein YaaA associated with the
                     oxidative stress response [Replication, recombination and
                     repair]; COG3022"
                     /db_xref="CDD:442258"
ORIGIN      
        1 mkillppseg ktppatgdpl dltalsspdl npkrkqvlga lkkvskrrda ltalgvgasl
       61 tedvarnvti dfqpcapall tytgvlyeam gaadlvaaae adasmaerlr dvhvfsavfg
      121 qvngldpipa yrlamktdlg qlgrlstwwk pilaksfsvg seevvldcrs sdyraawpgp
      181 nsqvvtlgav kdtgakrsvv shwakfyrge fvgrllrder elpadinalv eragehyeve
      241 faaatrsrpa gltivlrd
//
LOCUS       WP_009377503             230 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Brevibacterium].
ACCESSION   WP_009377503
VERSION     WP_009377503.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium
  ORGANISM  Brevibacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 230)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Brevibacterium"
                     /db_xref="taxon:1696"
     Protein         1..230
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=24470
     Region          15..92
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          161..229
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 myreirihrl havlwvnape avdaqpstat itpdgcmdll atgsgvviag adtaartvpa
       61 tgetiaglrf dsgvlpqlla tsaaeladrl tplaevappk rvripgarla eatspsvrvr
      121 sllglaedll arteidrrpl aladalaarg dgssvsiaea aadfaysprq lrrlsaqwyg
      181 ygpkhlakil rwrraralid agltrteaaa rsgysdaahl wreerallgr
//
LOCUS       WP_009377994             270 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: hydroxypyruvate isomerase family protein
            [Brevibacterium].
ACCESSION   WP_009377994
VERSION     WP_009377994.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium
  ORGANISM  Brevibacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae.
REFERENCE   1  (residues 1 to 270)
  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 270)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Brevibacterium"
                     /db_xref="taxon:1696"
     Protein         1..270
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28100
     Region          15..269
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mstfdftqad syilncstll telpvleraq aakdagfakv efwwpfdgdp tpspaevdaf
       61 iaslesagve lkglnfwagn maagdrgmvs ipgsqadftk naeivagige rtgcrafnal
      121 yglrvddstp eeqdavalen lavaaravag iggtvlvepv sgadayplkt aadaaavvea
      181 vraggaenia vladffhmav ngddvaaaie sgaadfghiq iadaegrgap gtgqlplrew
      241 idrsfalgys gqialeykqd retafawlah
//
LOCUS       WP_009378873             399 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator
            [Brevibacterium].
ACCESSION   WP_009378873
VERSION     WP_009378873.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium
  ORGANISM  Brevibacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 399)
  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   5  (residues 1 to 399)
  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   6  (residues 1 to 399)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 399)
  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 11973053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Brevibacterium"
                     /db_xref="taxon:1696"
     Protein         1..399
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41418
     Region          <11..62
                     /region_name="COG3398"
                     /note="Predicted transcriptional regulator, contains two
                     HTH domains [Transcription]"
                     /db_xref="CDD:442625"
     Region          81..364
                     /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 mpadhetrep liglkqrntg lilrhllhnp glsrsevaks vglsaptvtn ltgelidhgf
       61 lrglvsksgs mgrprvplav dpdrravlgi hlgpqvtglt imgldgtekv selvphgdlp
      121 gpeaiakvvt aaerltadre pgellgtgia tggqvdvgeg vvldhpsagw rdldaispfr
      181 aalsgpivfd hnvraaaqwe llygvgrvtd dflllvvasd vgcisvrqga irhgasrrag
      241 iishltvpgs tvvcecgrtg cfaaaasdda lvrqahtagl tdisyldllv rladtgdata
      301 sallsernra isctaaalfd lddpgrlvia gspaevadhf eeirtgvgre svlgeaaser
      361 vvvsnghlms lthyaassmv akvledplah vsgdarlga
//
LOCUS       WP_009380434             207 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Bilophila sp. 4_1_30].
ACCESSION   WP_009380434
VERSION     WP_009380434.1
KEYWORDS    RefSeq.
SOURCE      Bilophila sp. 4_1_30
  ORGANISM  Bilophila sp. 4_1_30
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Bilophila.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Bilophila sp. 4_1_30"
                     /db_xref="taxon:693988"
     Protein         1..207
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23440
     Region          3..196
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdvyeairar rtirdfedrq vgmgiierii daglkaptnn hlrqwefviv ngkeergdll
       61 rvknmtsrde ceqmldgfgm tdevqrnmyr eamprqfsml ynagclilpf fkirepllqp
      121 sslsslndfa siwccienml laaasegllg vtripmaees ehiktavghp enyvmpcyia
      181 lgypaknasv paqksicakd kihiniw
//
LOCUS       WP_009379475             292 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Bilophila sp. 4_1_30].
ACCESSION   WP_009379475
VERSION     WP_009379475.1
KEYWORDS    RefSeq.
SOURCE      Bilophila sp. 4_1_30
  ORGANISM  Bilophila sp. 4_1_30
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Bilophila.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Bilophila sp. 4_1_30"
                     /db_xref="taxon:693988"
     Protein         1..292
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31683
     Region          6..256
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mqprfvdlht httasdgtda prdlirraas lklaavavtd hdtvsgldea eaagreygve
       61 iirgcelgvq gqygeihllg lwlprhsapl daelarlrgh reernlkild rlrsiginig
      121 yqevldeagg esvgrphiar vlqkrgvvsn faqafelylg yygaayvprt lltpeegvsl
      181 madlgavvsf ahpmlircpp swfdeiiprl keaglgaiea yhsehsarde rfcvelaary
      241 glglsggsdy hgmakpgvel grgkgglrvt valldalkar rkrpvddape vl
//
LOCUS       WP_009380440             297 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Brevibacterium].
ACCESSION   WP_009380440
VERSION     WP_009380440.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium
  ORGANISM  Brevibacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae.
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   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 297)
  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 297)
  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 297)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Brevibacterium"
                     /db_xref="taxon:1696"
     Protein         1..297
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30987
     Region          159..246
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(178,197..198,216,219,227..228,238,243)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mrilhvcpap alsaplapqa leylghqver isaeeipgss ttadvavvda cldlslapri
       61 gavldsagls lpivvvlteg glatasakwe vtdiilttag paevearlrl ardhfrsags
      121 paagqgpsrl geragaggtg pvggwnenge pmvvvtgalr idetsftadl ggrsldltyr
      181 efsllkffam hpervftrde illgvwgddy yggtrtvdvh vrrlraklgk dlenaihtvr
      241 nvgyrfspda gagdddeegd pgdttgsvdp aeprdpgsgr tpaaastshp adeemsa
//
LOCUS       WP_009381149             716 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Bilophila sp. 4_1_30].
ACCESSION   WP_009381149
VERSION     WP_009381149.1
KEYWORDS    RefSeq.
SOURCE      Bilophila sp. 4_1_30
  ORGANISM  Bilophila sp. 4_1_30
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Bilophila.
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 716)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Bilophila sp. 4_1_30"
                     /db_xref="taxon:693988"
     Protein         1..716
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=77360
     Region          1..713
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 msdliplfrp ksvaligass dtkkygywta kslidnkfqg eihlisrsgg eilgqptypd
       61 ilsvpgevdl aiiaiapkhi lpiieqcvek gvktgivvst gfgetgpegk eierrmleia
      121 rkgnmrimgp ncmgmyssav slnasiidla pgpmslvlqs gnfgidlnfn akkrgmgysc
      181 watignqmdv rfndfvryie qddhtkvmll ymeglrvene edgrkfleaa rrtsvskpia
      241 aikigrsaag araaashtgs lagserifda alaqsgvvrv ntpnelldaa eafskckpah
      301 gkriavltdg gghgvmatdf ceansleapv lseatqeklr ailkphcpik npvdlagtpe
      361 gdmwvfdrcl evllddpdvd givivglygg yadlseefrv lemdvaksma erirkgdkpv
      421 vmhsiyqpqq pdclkylseq gvpvfgavde avrtmgvlve yserraalle eaasvppelp
      481 agrrekaeai farvrsegrv nlvetearev lraygvdlap hylaatadea aemwekiggk
      541 avmkivspdi lhktdaggva lniesaeaar eaferlvang rnykadanif gvmltpmlkg
      601 gveciigssw dstfgptvmf glggifveil kdvsfrvapv nmpscrrmvr einglamlqg
      661 argskpcdle alaeaaclis hmvdelrdia evdlnpvfaw ekglavadar ivlqar
//
LOCUS       WP_009381484             710 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Megasphaera lornae].
ACCESSION   WP_009381484
VERSION     WP_009381484.1
KEYWORDS    RefSeq.
SOURCE      Megasphaera lornae
  ORGANISM  Megasphaera lornae
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Megasphaera.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Megasphaera lornae"
                     /db_xref="taxon:1000568"
     Protein         1..710
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=80574
     Region          604..675
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 mgkklkkdfr erhkaslere vihsetftts eesklkdadd yrgkivhdkd rfqdkvhkki
       61 nkvssdneka ygtskrnvry rasdkdsvaa vsetgrsdyi tevkdgkiyd plgkdldndg
      121 iidrydndfr dsdyfestyd vednlshkek slensfknhk tqksrykrkn yseslytrrk
      181 ddapkenkse gkktgkdaas ekvhsslske qrkklkkdmv kvsalsglak gsetvrdyls
      241 hgsdenkgve agektadass klihgikkys dkkkakkgyd lknkdykirk rksklefhda
      301 kenlkktney kranaykrfq kknqvkaair renksrlrnr ikenligslk gskkfivrka
      361 kglmiifigl iilgtffinf agtgmtgfmn stssvlttsy lskpnvlnei nqsfsamese
      421 lqnevdhvkn nypgydeyil nnteyighnv hellsyitsr cgevksvsev esilkelfes
      481 mydleyreev eiryrtvtet ytdedgneyt esheepyeyk klivtlhkke mdsiirkifa
      541 nypdnlkhye alflaqgnmg eafgnsdlis anggvgggve yeassevqkk ivnaayitps
      601 pgagwcamwv sqvyqnaglg yiggnacdmy rnytftsdrs klkvgmlvav essssgstag
      661 ltyghvgiyi gdgkvmdnig rirvttldnw iasfckhhpv gfgfppnvkk
//
LOCUS       WP_009383187             291 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Staphylococcus massiliensis].
ACCESSION   WP_009383187
VERSION     WP_009383187.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus massiliensis
  ORGANISM  Staphylococcus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Staphylococcus massiliensis"
                     /db_xref="taxon:555791"
     Protein         1..291
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31236
     Region          <12..70
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          <19..165
                     /region_name="PRK06347"
                     /note="1,4-beta-N-acetylmuramoylhydrolase"
                     /db_xref="CDD:180536"
     Region          172..291
                     /region_name="COG3942"
                     /note="Surface antigen [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443142"
ORIGIN      
        1 mkklafsvtm asgaaallsq qesdastqht vesgeslwti aqkynttads ikqennltsn
       61 mlfpgqvitv ggessqgtgn ttttnettsq ggsthtvlng eslqiianqy gvsaqdiise
      121 nnlngylihp gqeltipgsg stntntntnt dtndtelpgn etgsngdese htnggyetpi
      181 fnhqnlytwg qctwhvfnrr aqtgkpisty wwnadhwaga aqqdgytvdn npevgsimqn
      241 fegpvghvay vervnpdgsl lisemnyhtp pgvvdyrtip asevasnsyi h
//
LOCUS       WP_009383788             129 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Staphylococcus massiliensis].
ACCESSION   WP_009383788
VERSION     WP_009383788.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus massiliensis
  ORGANISM  Staphylococcus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 129)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Staphylococcus massiliensis"
                     /db_xref="taxon:555791"
     Protein         1..129
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=14662
     Region          3..126
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(7..10,40..42,45,69,108,122)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 makiafdaat rgnpgesvcg vvialeneri ketkylgitd nhsaeweall yalhlaiqhg
       61 vknafiqtds klvedsildd qvksekfkhy fqtykslehe fdlvfvkwvp rdqnkeanql
      121 aqqalrkmk
//
LOCUS       WP_009384154             520 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Staphylococcus massiliensis].
ACCESSION   WP_009384154
VERSION     WP_009384154.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus massiliensis
  ORGANISM  Staphylococcus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 520)
  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 520)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Staphylococcus massiliensis"
                     /db_xref="taxon:555791"
     Protein         1..520
                     /product="M4 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=57599
     Region          45..520
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mnkkliltlg vatlvsapls tqalhakedt kertsllqsa nkdveqktvt snadakkalq
       61 signngggts srsktssvag yknyevtesk kdeqgfthyt lkpkvngvea dneiklhtnk
      121 snkvemings vdkknvtvsn qqkvskqqai ksafkgigkk qsevkningh kvvdeaklqi
      181 dsdknklvyn vkinyikpnl kswevkvdae tgevlskann lkeenvqgsg tgvkgdtkep
      241 lnvfnnngty elkdttkptv ietfdaqntn giqskitnds pnftkenhra gvdahynvdk
      301 tykyykdtfn resydnnaap mesivhyqyn lnnaywngqy mifgdgdgqr ftslaasddv
      361 iahelthavt dktaklvyqn qpgalnesfs dvfgyfvdde dwlmgedsyt pgqegdalrs
      421 msnprqfnqp dhmdmyqyts qdnggvhins gipnkaaynt ineigkekse kiyyraltqy
      481 ltgnsqftda kqaliqsaed lygpteaqav eqawnqvgvn
//
LOCUS       WP_009385893             301 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio sp. N418].
ACCESSION   WP_009385893
VERSION     WP_009385893.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. N418
  ORGANISM  Vibrio sp. N418
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 301)
  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 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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Vibrio sp. N418"
                     /db_xref="taxon:701176"
     Protein         1..301
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34937
     Region          <110..266
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          186..263
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mtynknkdvn flfnqkstik tenfrlinhq lvtyvdgarg efhfdnsnpi ysgkfiilis
       61 nskkcitfen gtrktlcndn qlilvkdsfk aqinektqfi fieksfyvni gmpkfhdlle
      121 thiherlvri lleallssps pfyeimaian iigvdnyknn lnctfsklig iiesnasnee
      181 fnlnslceka ymsrrkvqyi lsnnntnfve lvnnyrvevl knlllsypkt pvnnliykag
      241 fknyntavrv fktkfrigir efkskqfseh chskldihti klslgkkkir ipdlfnknny
      301 a
//
LOCUS       WP_009386065             357 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Vibrio sp. N418].
ACCESSION   WP_009386065
VERSION     WP_009386065.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. N418
  ORGANISM  Vibrio sp. N418
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 357)
  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 357)
  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 357)
  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 357)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Vibrio sp. N418"
                     /db_xref="taxon:701176"
     Protein         1..357
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40109
     Region          23..354
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkkwftptlt lltalsvglv snsalaqekv yrlklaetwg pntpilgdas knmaklaeem
       61 sngrlqirid sankhkaplg vfdmvksgqy dmghsasyyw kgkvpntlyf sampfgmmst
      121 eqyawfyhgg gmelmqevya phhllsfpgg nsdiqmggwf qkeiktiddl kglkmripgf
      181 agevmarvga kptniapgel ytslergtid alewagpafd lrmgfhkiap yyytawqepg
      241 setqflvnkr awdklpkdlq viletafrva afdmytqaid ananswasms eeypeiqvle
      301 fppevlgrln qekqtlleel aakdslakri iesqrqylsk vrswtdistk aylnskq
//
LOCUS       WP_009386895             177 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit [Vibrio].
ACCESSION   WP_009386895
VERSION     WP_009386895.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..177
                     /product="TRAP transporter small permease subunit"
                     /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=20149
     Region          4..169
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mrrliyierl fnrfgdwlgw lssilfilll invvydvvmr yafndvsiaf qemewhlfsa
       61 vfligvpyai kagghvrvdl fyerlsnkaq aiidllgtvf fllpfcllva wygidfakes
      121 yvlgetsgdp gglpyrwiik gmiplsflfm avsgiglmlh slnrivnphl mhaqank
//
LOCUS       WP_009387057             113 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Acinetobacter].
ACCESSION   WP_009387057
VERSION     WP_009387057.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 113)
  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   3  (residues 1 to 113)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 113)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..113
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12262
     Region          2..113
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mqpqmggiiq vnipdratlq asymgyvqgg glfvpskqkv kmgqeifila tlpeqsqkip
       61 ltgkviwish kqsgfkpqgf aiqlsgdkgv yykaeaervl agsmsldrps ytm
//
LOCUS       WP_009388070             104 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Vibrio sp. N418].
ACCESSION   WP_009388070
VERSION     WP_009388070.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. N418
  ORGANISM  Vibrio sp. N418
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (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   2  (residues 1 to 104)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Vibrio sp. N418"
                     /db_xref="taxon:701176"
     Protein         1..104
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11058
     Region          43..102
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mnikalvlsv vltfslpfta vlaeqqpdsp penpkydgie ivvnvnqasa qeiadllkgi
       61 gltkaqaivd yrdqqgpfkr ieelakvsgv geatvaknvg riel
//
LOCUS       WP_009387410             281 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Vibrio sp. N418].
ACCESSION   WP_009387410
VERSION     WP_009387410.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. N418
  ORGANISM  Vibrio sp. N418
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Vibrio sp. N418"
                     /db_xref="taxon:701176"
     Protein         1..281
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32212
     Region          188..269
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 miawkqslag yewlihqiwy levetdevis pkphlipnar ahllftpaeq sysydngeqc
       61 lfgcgshllt aneslllldd naplkrigit frpeslyvln sgsvsninqc awfdwlnllf
      121 deqfqqelwq hstskmklla yihqhldkiq lqpssnnafv iaqrataafe asiknpnatp
      181 almgienlas aaacsrrtle rsfkqvlgls vkqylqmmrl eqmilalyqq ehdvdwsqfs
      241 lqfgfsdqsh lirtlkqqlk qtpskylkqr dltidiygdf e
//
LOCUS       WP_009390759             263 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Acinetobacter].
ACCESSION   WP_009390759
VERSION     WP_009390759.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   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 263)
  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 263)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..263
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28757
     Region          24..91
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          191..252
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 meinpnsqqp tgsslptsal gniqrpgeyl rqirvaqnke lgqvssdlnm pvktltaleq
       61 ddykslpeat fikgyyrsya kylntdatai iqrfdeiyan dtgllpnhal nnspikimgk
      121 lpgsnsdrnk kwlkrallai iviavvsliv mgvqkwtskk edadlpkvnq snvevlpmkg
      181 natstvgdql vlnfnrptsv hivdatgkvl atgrqsstlt lngespfqir lddatavsls
      241 lnqeqislsp ytvngkaefr lsr
//
LOCUS       WP_009389614             298 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_009389614
VERSION     WP_009389614.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 298)
  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 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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..298
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33487
     Region          28..184
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          214..294
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpqnhltvhl vdaflhlapt eglyptfisn itlmrvdhst ppvavlqeps ivlviqglkr
       61 gyigkeifqf qqgqclfisi aipfdcdtvv ennepmlaia ikfepqmmad litkmdkqqq
      121 vvtedphted lklscglrvi dmnatiseva lrllnllrsk qdtfilgeqi krelvyrvvq
      181 asggnlvesl samasrngvi yticeiiqrd yyhnltvqdl akqagmsisl fhqtfkkvtn
      241 ysplqyikit rlhkarelim nnkmgvaeaa yevgyvsasq fsrefkrlfg vppkssii
//
LOCUS       WP_009390824             134 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Acinetobacter].
ACCESSION   WP_009390824
VERSION     WP_009390824.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 134)
  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   2  (residues 1 to 134)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..134
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15139
     Region          62..133
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mqismslwks kyyifiilfg slisstmiqa qsfdqnfkew kakqqmydqk lsmqhsshsn
       61 aaksttmtds sgqihlnqat idelqklkgi gekkaqaive yrqknggfkn idefknvkgi
      121 gpaifeknka rlsl
//
LOCUS       WP_009391223             101 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein
            [Capnocytophaga].
ACCESSION   WP_009391223
VERSION     WP_009391223.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga
  ORGANISM  Capnocytophaga
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Capnocytophaga"
                     /db_xref="taxon:1016"
     Protein         1..101
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11650
     Region          2..98
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mnhllednkl kidalcqnhk vktlyafgsv ltpkfnensd idlivdfkqq dvseyaanyf
       61 nlkfalqaif nreidlleek avknpyflah inskkrliya d
//
LOCUS       WP_009391152             385 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Acinetobacter].
ACCESSION   WP_009391152
VERSION     WP_009391152.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 385)
  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 385)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..385
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44848
     Region          13..373
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mtsslkqltl fnqglgktsr fakgvngtlq aiehlgyvqi dtisvverah hhilwsrvpd
       61 yelshlnylv rerqifeywy haasylpmkd yryalpamms irngesryfn rgdqhlmnei
      121 larvraegki rlrdidknnk kslgnwwntg pgrhafeqly mqgdlmicer ngmekvydlt
      181 erclpenidl smptlyeyaq ylfnntlrah gvftwkqlvh lkkndlkeam rvvlkeqvda
      241 gvvsavkltd gqtlyvdvaa ieqkvetdfg lkilspfdns lihrdrltsl fefdyriecy
      301 vpaakrifgy fclpilfqde lvgrvdckah rsvkelevis lhlektvknk elfffeleqe
      361 lsrfaafnqc stindkvikl irtki
//
LOCUS       WP_009391728             336 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_009391728
VERSION     WP_009391728.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 336)
  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   6  (residues 1 to 336)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..336
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38145
     Region          22..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <143..334
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mvplahtasl knylavaqql ainpyhllsr vglsqtqlnd lnqripvdka itlledsaqm
       61 sscdvfglhm aeqreiadfg eislllnyqh tlrdalqtlv ryrnllnnsl eiyieeiddt
      121 vvireevvtt tcgysrqate lalgithrfc aallmqkwrp lsvhfthnpp sdltlhrrif
      181 gcalefgsdf ngivcttael dttnpqanla manhaqryld ilqnsdestm ifdirksiyl
      241 llpmgratid qvaqthgihv rtlqrrleea qtsfsdline vrkdlvfryl knlnyslaqv
      301 sdilgysmps sftrwfisqf gmsptmwrsh nkslhs
//
LOCUS       WP_009392044             141 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Acinetobacter].
ACCESSION   WP_009392044
VERSION     WP_009392044.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..141
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15109
     Region          1..122
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkngftliel mivvaiiail aaiatpsylq ylrkghraav qsemmniaqt lesekmvhnr
       61 ypsnatitsi ygsnvspqqg qalynlafas itdsswvlta tpipttsqag dgiiclndqg
      121 qkfwakgatn calsatsnwl q
//
LOCUS       WP_009392153             401 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Capnocytophaga].
ACCESSION   WP_009392153
VERSION     WP_009392153.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga
  ORGANISM  Capnocytophaga
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Capnocytophaga"
                     /db_xref="taxon:1016"
     Protein         1..401
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43965
     Region          1..401
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 meiliinsgs sslkyqlids ktgeskargi vdrinidgsy vkyvavkngk evevkkeqpi
       61 pthevgmnlv adlltdpevg viqnpsdikg vghrvvhgge kfvqptvitd evvaeikrli
      121 plsplhnpgh legirvaqkl fdkathvavf dtafhqtmpa kafryaipne yyekyglray
      181 gfhgtshkyv daqarkylnn phiknitihl gngasmaavn eegkcvdtsm gltpldglim
      241 gtrtgqidas vafflgqelg mnyeevktlf nkksgmlglt ghsdardvaa lyhkgdanaa
      301 lcyemygyri qkfigaytaa lngldsivft aglgendalt rsfackhldf fgikldekkn
      361 eelnhptkpv eiqaadsrvk iliiptneel qivneivdlv k
//
LOCUS       WP_009392381             278 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Acinetobacter].
ACCESSION   WP_009392381
VERSION     WP_009392381.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..278
                     /product="formate/nitrite transporter family protein"
                     /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=30685
     Region          28..278
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mdheieekkv dqtlswrekm aveeheklsp rlvyeiirrd gaeeldrpta alifsgiaag
       61 lvisfsfvfk aiiasylpad aiwtdlitni gytigfliai lghmqlften tittvvplfk
      121 pftldklrav grlwgivilc niigtalasl ffltthlftp didkaldela lhvgsfsatq
      181 nllkgimsgl liaalvwmlp svsnkfllif fmtyliglgd fthvvvgste msylvwqgea
      241 sindylftfl vpttignivg gtgvftlliy gqvteele
//
LOCUS       WP_009392556             583 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase [Acinetobacter].
ACCESSION   WP_009392556
VERSION     WP_009392556.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 583)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..583
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=66200
     Region          3..>391
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mptlnwigke avekhhkdvp yrllepvvel scgeeqsgnl ivqgdnlhal kallpryagk
       61 vkciyidppy ntgnekwtyn dnvnspeirk wlgetvgkeg etldrhdrwl cmmyprlill
      121 kqfltddgvi fisiddnelh nlrllmneif eernfianii wkkktngnnv ghipavhdyi
      181 vtyaknessl klfevqqsde yikssysnpd ndsrgpwtts dlsanhkgpy feitnpvtge
      241 kffppkgryw vfnedevnkr iqegriifgk sgtarpvqrv flferettqk vdtwfdkqgy
      301 nadgmktlsd ilggkvfdhp kppnlikfll nfatdknsiv mdsfagsgat ahavlqknee
      361 dggnrkfili eldennakni tskrvrkvih gydfkgklkk tlsshklnfq alkkantile
      421 dfeklkaqys qefnkiksev ndgclqlvge ieveqkmppl pgdflyctls vdplfeangh
      481 irsnvsfsel aefvwfcetg tgytgkadsp llgiyegrai yllyngilkd lteqggnilt
      541 kqvfdvlpkf egvkviyaaa nrlggkakre nivfkqtpya lev
//
LOCUS       WP_009392828             346 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_009392828
VERSION     WP_009392828.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 346)
  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 346)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 346)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 346)
  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   5  (residues 1 to 346)
  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   6  (residues 1 to 346)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..346
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39895
     Region          34..206
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <155..341
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          259..340
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mevsleqnfl ennipsnyvr iigrelglsi refaqllest qlttkeimqa drmvnayqfi
       61 qiltnasfis cdpnlglklg qrltpathgl mgfvvnnspn lvgvleafqk ymptrlsfgr
      121 vslkqerdli kcelnflvnl pldvkrllse icmvilyesi efiigrkpne viiyfehasr
      181 kdldlyhhif napinfasiq tamhipfhic qiinpsadkn iyrlaleqce klikqlksek
      241 dsytnkvqri ilsnpsktit eefiaselfi skrtlarklk iegtryqsiv ddvrsrqaie
      301 ylkednlsia aiasllnfhd stnfrrafkr wfkltpteyr nvlkkt
//
LOCUS       WP_009393420             353 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Acinetobacter].
ACCESSION   WP_009393420
VERSION     WP_009393420.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..353
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39383
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msiqvkniek hfgafhalkn isldfpegel vallgpsgcg kttllriiag lesadggqvl
       61 legedatnvh vrerqvgfvf qhyalfrhmt vfdniafglr vrpratrpse aeikkrvtrl
      121 ldlvqlgfla drypaqlsgg qrqrialara laveprvlll depfgaldak vrkelrrwlr
      181 nlhdelhits ifvthdqeea levadqiivm nkgnveqigs prevyekpst pfvfdflgqa
      241 nrfegentdg iirigndriq lptlveapqg kviafarpde lhihsqpqan tieatfvrei
      301 wiagkvvael qdrngrliei alsneaaklh afkpnqtvwv sasqlhlfad qva
//
LOCUS       WP_009393549             872 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: Lon protease family protein [Acinetobacter].
ACCESSION   WP_009393549
VERSION     WP_009393549.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 872)
  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 872)
  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 872)
  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   4  (residues 1 to 872)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..872
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..872
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=97904
     Region          109..830
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mtqkldqvti stlslakttt tnvtvnafps afeqpdikmt ldktvlkpeq lthipdfeki
       61 pastkrikpl nnflgqdrak asveagislp ysgynifavg taglgkrtmi krllqqhakt
      121 mptpddwvyv ynfkqarqpi alrfpagqgt kfqqaheqtw qiilkqlerr fsaetyhnri
      181 erirqetgdv qqqalveltk egeeldlkli srnekhgfvp vqvkddqvqe ltqndidaln
      241 skqraeiaan irymdkkldr lglhlgdled dardkvsvln rdiatqvvmp rmdlilnkyg
      301 qvkgledylk qyaqdiidnv elileqeedd yapsmfnrvp aryqanviva nkpnsgapvi
      361 fedfpthynl lghveqlthn gtittdftli rpgslhqang gflmleaeql leqpyawqgl
      421 kralksgqlr lsslehmltl tgsisiepaa ipldikvilm aepeiyyeil evepelgsvf
      481 kiradftdtl qrneaneqay mqliadyvqa dkllpfdrsa laalltdssr qaedqsslsl
      541 hastlgdlir eahhhafkad dkivteqhin lalqhrqyrl gylrelywqd lsrgtqliet
      601 sgyrlgqina lsvihyadve fglpsrltas vyqgggdild iersvelggs lhakgvllms
      661 sflkahfgrq qilhfsaala feqsygqvdg dsatvaelsa lisaisqipi dqswaitgsm
      721 nqlgqvqpig gvnakiegfy dacklqgltg kqgviiprqn mqhlmlrqdv ieavrsgqfh
      781 ihaidtidqa leilmarpvg tldkkgkysk nsiyaavmeq leywqaiedg aeieeepkkk
      841 kknkkkikkh eeltaddlpq enaeevatlk qk
//
LOCUS       WP_009395768             414 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Actinomyces sp.
            oral taxon 171].
ACCESSION   WP_009395768
VERSION     WP_009395768.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces sp. oral taxon 171
  ORGANISM  Actinomyces sp. oral taxon 171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 414)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 414)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Actinomyces sp. oral taxon 171"
                     /db_xref="taxon:706438"
     Protein         1..414
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=45363
     Region          15..400
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mttieivsda ngshrlvgqa hvtrsrgqvs ttflydptyl adggmnidpg lslvsgaqyh
       61 pglvgafads tpdrwgrnli rkaersrard egrvprqldd ldfllgvsdd trqgalrfra
      121 pgsdeflgep srvlrlvalp ellyasdela sdddpsdavk rlldtgttgl ggarpkasvr
      181 lddgglaiak fphssdswdv maweataldl letagvrapq hqltqvgnrs vlilrrfdrt
      241 rdgsrigyis amtatgssdg dqkdyadlae airdlsrspv qdlhefydri iasialgntd
      301 dhlrnhgfla drglwrlspv fdvnpnpdps rpramsimga dampdeidgl laiandyrlt
      361 qsearerirr itvplsgwrg qaranrvler eitmmsesie prlealtraa hsed
//
LOCUS       WP_009395814             417 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Pseudomonas
            bharatica].
ACCESSION   WP_009395814
VERSION     WP_009395814.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas bharatica
  ORGANISM  Pseudomonas bharatica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 417)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Pseudomonas bharatica"
                     /db_xref="taxon:2692112"
     Protein         1..417
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=46114
     Region          2..396
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 msnealnvav rgldvgslar adstlgatsf ryrdsaaegq avsltmpvrr ddylwerglh
       61 pifemnlpeg flrsrlqqmf akvihgfddl dllgivgphq lgrvivggds egsmpgtsih
      121 ellvhdgaqg lfedllarya kysgvsgvqp kvlvrdedve gvervthrga thivkawrde
      181 dypelaanef fcmraaklag levpgfqlsn ggkfliverf digeqgylgl edfcvlngwg
      241 anrkydgsye ggvrqintwv epslrqasll qyfrcvalsa avrggdahmk nfalmydsts
      301 edaviklapa ydivtttpys pqdmmalmme gskafpkhkr laqfgrvtcg fservveqtl
      361 qqiadgisda rkemleylgq npqfeligtr mldawnigva rslmsekrak vfdkvkk
//
LOCUS       WP_009397715             352 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Actinomyces sp. oral taxon 171].
ACCESSION   WP_009397715
VERSION     WP_009397715.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces sp. oral taxon 171
  ORGANISM  Actinomyces sp. oral taxon 171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Actinomyces sp. oral taxon 171"
                     /db_xref="taxon:706438"
     Protein         1..352
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=37719
     Region          106..>218
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mnasgrtltr ltvlgalsas gmtaalpvha dtspepsqks aatelaalhe apwdqrgdfi
       61 lspsasleal selpedapaa qswaeggsrt gwfgeawtdv dgdgcdtrne ilardltdtd
      121 fsrddgvqpr edgrgrgagv cpdatvwagi lhdpytgrri tftrgqdtsa avqidhvvpl
      181 nylyahgawq wdertrllva ndplnliavd geanqakgac gpascpvgst etgswrpsgp
      241 ggwwpantsy rctyarrfvs vaaayrlglp qadkealntt lnsclaggdg tdslperatr
      301 takevgsvvw rspgyaalaa fgtlvlgwgl ivrgrrrwrr asrrrshrrv rh
//
LOCUS       WP_009398624             378 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Pseudomonas].
ACCESSION   WP_009398624
VERSION     WP_009398624.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 378)
  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 378)
  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   3  (residues 1 to 378)
  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   4  (residues 1 to 378)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 378)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 378)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..378
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39948
     Region          30..365
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(104..106,127..128,177,229,254)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 msqtfykkgf lalavaaalg vssyvqadlk igvagpmtga naafgeqymk gaqaaadain
       61 akggvngeki vlvkgddace pkqavavanr lvdqdkvagv vghfcsssti pasevydeag
      121 viaitpgstn pqvterglga mfrmcgrddq qgivagdyii dvlkgkkvvv lhdkdtygqg
      181 ladatkaqle krgvkpvlye gltrgekdfs avvtkiraag advvyfgglh peagplvrql
      241 reqglkdvaf msddgivtde lvataggaqy tngvymtfga dprllpdske vveqfrkggt
      301 epegytlyay asiqalaagf egaksnkged aakwlkanpv ktvmgekkwd skgdltvsdy
      361 vvyqwdangk yhqlekqk
//
LOCUS       WP_009398643             191 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LytR C-terminal domain-containing protein
            [Actinomyces].
ACCESSION   WP_009398643
VERSION     WP_009398643.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces
  ORGANISM  Actinomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 191)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Actinomyces"
                     /db_xref="taxon:1654"
     Protein         1..191
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=19883
     Region          67..154
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mqhrqatvig tilavmvvav avsllvslgi lpaynpgfsq pkstatyvpq pcppsgaktv
       61 dvttiekini yngsesvgla ttvqqdlkea dlhitsandw pggiyngevq imaskgglin
      121 ayslaqifpn stvqldrsls dsdttvsvvl gkeylqnalk sdeikllgad kpitapsdcv
      181 padkaatskp s
//
LOCUS       WP_009399419             199 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator [Frankia].
ACCESSION   WP_009399419
VERSION     WP_009399419.1
KEYWORDS    RefSeq.
SOURCE      Frankia
  ORGANISM  Frankia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae.
REFERENCE   1  (residues 1 to 199)
  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 199)
  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   3  (residues 1 to 199)
  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   4  (residues 1 to 199)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 199)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 199)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Frankia"
                     /db_xref="taxon:1854"
     Protein         1..199
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22018
     Region          8..199
                     /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"
ORIGIN      
        1 msqpssnprr vliaedeali rldlremlqe egyevvgeag dgemavnlag klrpdlcild
       61 vkmprmdgie agakiakdri apvviltafs qrelverare agamayvvkp fqkkdllpti
      121 emamsrftei vsleaevedl qgrlearkii erakgvlqte hgmtepdafr wiqrtsmnqr
      181 rtmravaeav lsgealpgs
//
LOCUS       WP_009399957             740 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Pseudomonas bharatica].
ACCESSION   WP_009399957
VERSION     WP_009399957.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas bharatica
  ORGANISM  Pseudomonas bharatica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 740)
  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   3  (residues 1 to 740)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Pseudomonas bharatica"
                     /db_xref="taxon:2692112"
     Protein         1..740
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=77946
     Region          6..739
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msfgadeeil qdflveagei leqlseqlve lesrpddadl lnaifrgfht vkggagflql
       61 nelvecchia envfdilrkg errvdaelmd vvlealdtvn smfgqvrert ditpatpell
      121 galarlaepa gaepaapvvv aepepvaasg ditdsefeql ldslgampde vpateaggde
      181 itdaefesll dqlhgkgqfa adnlqgasvp apvaeagaep sdeitdaefe alldqlhgkg
      241 sfavdslpgv aaaapaatav eaapaaagsd eitehefeal ldqlhgkgkf aadavgaaat
      301 aapaaaaapa aavakpaarp apaakpaaaa parqaaapaa aagdkhppas eaettvrvdt
      361 arldeimnmv gelvlvrnrl vrlglnsgde amskavsnld vvtadlqtav mktrmqpikk
      421 vfgrfprlvr dlarqlkkei nlelvgeetd ldknlveala dplvhlvrna vdhgvetpee
      481 reaagksrgg kvvlaaeqeg dhillsisdd gkgmdpavlr akavekglmd kdaadrlses
      541 dcynlifapg fstkteisdv sgrgvgmdvv ktkisqlngs iniysakgqg skivikvplt
      601 laimptlmvm lgnqafafpl vnvneifhld lsrtnvvdgq evvivrdkal plfylkrwlv
      661 ssaaheeqhe ghvvilsvgt qrigfvvdql vgqeevvikp lgkmlqgtpg msgatitgdg
      721 rialildvps mlkryaarri
//
LOCUS       WP_009401005             696 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Pseudomonas bharatica].
ACCESSION   WP_009401005
VERSION     WP_009401005.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas bharatica
  ORGANISM  Pseudomonas bharatica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 696)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Pseudomonas bharatica"
                     /db_xref="taxon:2692112"
     Protein         1..696
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=76851
     Region          53..695
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mpsplslrss lcllgltlag sagaqqpesi klesieleqv liqeqdqddl qvarerleqv
       61 pgatnlidmk rvgqgrvasn qdvlayqpgv faqsagndgi rlsirgsgin rapgahgsgt
      121 yvmldglplt gpggtpyelf eplwlnraei lrgangfdrg alalggainy vphtgydaap
      181 lqlryeagsr gyqkrhissg qvlgdfdyyv altdtgydgy qdhssgsgkg vaanfgyrfn
      241 pdletrfylr yretdndlag rltkdqikhh praanpayls rndsrpqpgs twlankttfy
      301 ldddsqlvag lvwhdypmdl regpmrlkva yadvsgtldy qrrhtlfghd skttvgwrtt
      361 khlpnsgasq yarandivga rtrdfsyqgs dtvlhignel elvpnlwlts glaaiytrre
      421 sdvtysnvts gpggkvsmhd wdyapriglr ydaspslqly gnlsrsvepp hpwsliwsap
      481 tqyqpielkn qtattlelga rgdsdlgrwd lswyysavrh ellmveiqpp irsesnaspt
      541 ihqgieasld stlwqrgdvg rlslrqaytl ndfhyrndkv fgdnrlpgip mhyyqgelrf
      601 dlpsgfyagi nttmaskvqv dyansydada yailgatfgy napkqdwqtw ldlrnltnkr
      661 yaaivapgyn dngadvarsv pgegfgvyag vsytfh
//
LOCUS       WP_009401168             299 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_009401168
VERSION     WP_009401168.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 299)
  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 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   3  (residues 1 to 299)
  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   4  (residues 1 to 299)
  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 299)
  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 12071874
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33499
     Region          30..181
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          209..288
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mssaepldpa leslrealad lvrrhvdspa inglflvrhe enirsmptla hpalcilaqg
       61 skavhlgder yvydplhymv vsvampisgv yldaspenps lgirldidpa einnliadag
      121 pmgvpaaser glfverldpa lldalirlir lldtpkdipv laplirreil yrllrgkqgh
      181 rlyeiamsns qthrvcqaiq wlndyydkpl riedlarevn lsvsalhhrf ksvtsmsplq
      241 yqkqlrlqea rrlmlndgle aavagyrvgy espsqfsrey srlygapplr dmarlrnai
//
LOCUS       WP_009402350             293 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Actinomyces sp. oral
            taxon 170].
ACCESSION   WP_009402350
VERSION     WP_009402350.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces sp. oral taxon 170
  ORGANISM  Actinomyces sp. oral taxon 170
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Actinomyces sp. oral taxon 170"
                     /db_xref="taxon:712117"
     Protein         1..293
                     /product="formate/nitrite transporter family protein"
                     /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=31666
     Region          33..257
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mpaeqdalfp gkqfistvle aletktrmtg viahrylmra amagmivavf yivnyaivgi
       61 ldglrfgdts lagvgkmlga lafgpalvfi yytksellts nmmvvvigyy ykrisawrsl
      121 rvlamclagn fvgglifavm yrfstlvdga tgeqalhsve aklgylssas gvgdlfvrai
      181 lcnfminlam lliyngfihe dwskifsmii avfvfaflgf ehsvantvlf tvvglthgid
      241 vlpalgnvav allgnfvggg lliggyyaya nddsrwlrrq prkdgvqaae sae
//
LOCUS       WP_009403935             575 aa            linear   ENV 20-JAN-2025
DEFINITION  L,D-transpeptidase [uncultured Actinomyces sp.].
ACCESSION   WP_009403935
VERSION     WP_009403935.1
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 575)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="uncultured Actinomyces sp."
                     /db_xref="taxon:249061"
                     /environmental_sample
     Protein         1..575
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=59961
     Region          456..571
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(530..531,534,547..550,552)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
     Site            order(534,550)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mrrqsvfqaa angtaphars tsttssdtne dlgsteeiev vapsavaapg tenklheqas
       61 tektgdadgv yltapaapaa ptspavsafa thqdkdfyld eprrrrrwpl gvaaaallll
      121 gvvgaggyay aahydgrvvp gttvagtdvs gksreevvaa ienraksakv disgdvtasa
      181 sladlgttvd aqatadavma hgdtfgekfq allskgevpv vtttdktavd syatsliped
      241 rakarnatvv lsedgttfst tsaskgaald adalaqaaqk aatslgsssi sltmtnadpk
      301 vsdndaqkva dtannwvsqd vtitlddesy taedtdkasw itvnnsadsa ptiavdstkv
      361 sqwvkaqade anvdpvtgqr nvnasgqvvs tpteakdgkt vnnvdtvats itqslgsdka
      421 ytgsfetttv kaewkertia dgaenlpyqa apgekwvdln lssktvtaye gatvvhgpvs
      481 ivdgaaetpt vtgtykvylq yesqtmrgen adgspyvaed vpwvsyfhsg yafhgagwrs
      541 sfgysgshgc vnmpvseaqw iynwvdtstv vqshy
//
LOCUS       WP_009404937             214 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Actinomyces sp. oral
            taxon 170].
ACCESSION   WP_009404937
VERSION     WP_009404937.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces sp. oral taxon 170
  ORGANISM  Actinomyces sp. oral taxon 170
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 214)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Actinomyces sp. oral taxon 170"
                     /db_xref="taxon:712117"
     Protein         1..214
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=21791
     Region          125..212
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mrvsnydype defdvgeddg pvpvgvhraq vprwrswvpl lailiivpal awgavtlfln
       61 gsgggssdav sstqpaqsgq agknqasggk taeaskpadn ksadasakps asasatgnid
      121 fntgvtvsng tetsglakga gdkltnggft avnvtpgiye naepakstvy fgspenrpaa
      181 eevgkklgit nvvesaenaq snpivvilrd dyka
//
LOCUS       WP_009405115             287 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Pseudomonas sp. GD04058].
ACCESSION   WP_009405115
VERSION     WP_009405115.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GD04058
  ORGANISM  Pseudomonas sp. GD04058
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Pseudomonas sp. GD04058"
                     /db_xref="taxon:2975429"
     Protein         1..287
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31356
     Region          1..278
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mnvdlhchst asdgsltpte lvarayeqgv rvmaltdhdt legqpearqa mhergmqwvs
       61 gvelsctwsg itihvlgygf pldappllea veslhrgrwl raeeisrrla akgmpgaleg
      121 aralqqalgd sgnaparphf adflvsaghv kdraeafrkw lgagklgdvk lhwptlddtv
      181 etlrqsgawv slahpmhydl trskrrrlia dyiqaggqal evvngmqpae qvgtlsiltr
      241 efgllasags dfhgpgtwse igvyrplped lpplwrrfkh eqpsada
//
LOCUS       WP_009405124             359 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_009405124
VERSION     WP_009405124.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 359)
  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 359)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 359)
  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   4  (residues 1 to 359)
  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 359)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..359
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40056
     Region          22..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          248..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mnerttsasw asgivkalel egldcpalfh klgldfaals dpdarftqds mtrlwllaee
       61 lsgnraigln marvvrpasf hvvgyalmss rtlaegferl vryqriiaes sdlslqlgpe
      121 ghaliltvhg dhlpptrhss easlacalal cswlsgrtiq prrvliqgpq pediepyria
      181 fhsplvfnap ydalifepsd lqsplptane amavlhdrfa geylarfses rvthqarqvl
      241 crvlpqgepk relvaqalhl sqrtlqrrlq eegtsfqall ddtrrelaeq ylsqpgmtll
      301 etayllgfad psnffrafrr wfgltpgeyr arrhglshdd aeadavsaar tpayreqir
//
LOCUS       WP_009406444             827 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas sp. GD04058].
ACCESSION   WP_009406444
VERSION     WP_009406444.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GD04058
  ORGANISM  Pseudomonas sp. GD04058
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 827)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 827)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 827)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..827
                     /organism="Pseudomonas sp. GD04058"
                     /db_xref="taxon:2975429"
     Protein         1..827
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90757
     Region          65..113
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          91..827
                     /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 mkypharllt pvavairlgf ctlgalslpg lahaaeagam qswhipagsl atvlstfasa
       61 sgtalsfdaa llqgrqsggl dgtysvdqgf aillqgsglq avpqsngsya lrplhneqgs
      121 meldattiss qrldpttegt dsytaravti gkgvhtlket pqsltvitrr mmddqnlntl
      181 ekvlektpgi tvydspmggk yffsrgfnmd gqyqydgvpl dvggnyvqan sfssdmafyd
      241 rvevlkgaag mlkgsgssag gvnfvrkrgl ettatkltms agswddyrgq idvggplnes
      301 gsvrgravat lqdrqyfydn akrqdqvlyg aldwdispdt tlgfglayed vdaspcyhgl
      361 pryadgsdlk lsrstclgas wndlqsqrit gfadlkhrfn ddwslnfasv ythndqdiey
      421 gysegavavg astaamgrya grfdydqtdy gfdtyldgkf rafglehevi vgmnasrqkn
      481 hdyfalmrls gsqnpfdpss dfphpskady lvnptrggsv ptdsltrqfg tyanvrlkla
      541 epltlvlggr vswyrnhsds ytqaydywvp nrsqengqvt pfaavlydln eqwtayasya
      601 difqpqsnkv tadgqtlqpk tganyeigik gelfngelnt afnlfrtiee hraetdyvgt
      661 cmgsgdqycy tdngkvraqg feaeisgspv erlqvlagyt ytqtkflksi nevdsndltf
      721 sssfvprhml rvwgdyqldg alerwslgag vssqsensry nrtlkieqpg ytlwsgrvqy
      781 rvdqnwtval ngnnlfdkky yatigapgwg nyygeprnfm vtvqgaf
//
LOCUS       WP_009407590             105 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Pseudomonas].
ACCESSION   WP_009407590
VERSION     WP_009407590.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (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   2  (residues 1 to 105)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            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="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11031
     Region          35..103
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mrktylasll itlfgilslp lnaapanpaa aaapsvqaes drldlnkada malqsqlsgi
       61 gkskaeaiva yreehgdfas idelleikgi gkalldrnrd kltvn
//
LOCUS       WP_009408899             397 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Actinomyces sp. oral taxon 181].
ACCESSION   WP_009408899
VERSION     WP_009408899.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces sp. oral taxon 181
  ORGANISM  Actinomyces sp. oral taxon 181
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Actinomyces sp. oral taxon 181"
                     /db_xref="taxon:712121"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43143
     Region          3..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mtdtvlvins gsssikyqli npdngdaiak glverigese ghiqhkygek vvdvnepiad
       61 hevgmrevlr lfdevgpsla eanivavghr ivqggkyfdg palitdevrd lidelcalap
      121 lhnpahlkgi dvarelmpdt phvavfdtaf fqrlpeetat yalkqevaek yavrrygahg
      181 tshqyvsgqv arlmgndalr qivlhlgnga svsavkagrp idtsmgltpl eglvmgtrtg
      241 didpavvfhl qrqtgwsade vddlfnkqsg lkgltgendm ravrhmvdse dpevarrarl
      301 aldiyvtrii kyigsytael ggldvitfta gigendadlr revcerllpf gvrindevnn
      361 qrfsaattis tndssitvmv vptneelaia rqaltli
//
LOCUS       WP_009409476             472 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Actinomyces sp. oral taxon 181].
ACCESSION   WP_009409476
VERSION     WP_009409476.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces sp. oral taxon 181
  ORGANISM  Actinomyces sp. oral taxon 181
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 472)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Actinomyces sp. oral taxon 181"
                     /db_xref="taxon:712121"
     Protein         1..472
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=50421
     Region          77..189
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          350..469
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(424..425,428,444..447,449)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkklslkvwt llglcgllca glvfsgwfys ahalprtsia gqsfssssrv qidealkhrv
       61 esaqvtlqlg dttqqatled lgitvdipat vdaafsensg llsrflgifr srsitpvvhl
      121 dnaqlsrfgv slaqrvgtpv sdaalspked gsgfavvpsh egialntadl akvqqdvaqd
      181 lgasprsinv evqepkintq raeealaqaq sliapsvtit dgiddfaask adkmkwvkvs
      241 aegdraavld sdalsawvnd lakstnvese kgiqgvnsrg dvvgvlkagt vgyranntqs
      301 visgiedaln ngksysgdfd ydkiqpeydr qdipdgygdd vyqasagekw ididlskntv
      361 sayegrtivh gptpmvpgap ntptvtgkfh vylqyasqtm egenadgtny rtegvpwvty
      421 fyagyalhga pwrssfgwsg yggshgcvnm pvdgahwiyd wadngtvvis hy
//
LOCUS       WP_009410862             770 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Capnocytophaga sp. oral
            taxon 324].
ACCESSION   WP_009410862
VERSION     WP_009410862.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sp. oral taxon 324
  ORGANISM  Capnocytophaga sp. oral taxon 324
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 770)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..770
                     /organism="Capnocytophaga sp. oral taxon 324"
                     /db_xref="taxon:712211"
     Protein         1..770
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=86899
     Region          4..768
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mkkisifill llfftsfava qqgtqekdsv hyleevtvsa qqilgskfqa rnrtgsayyi
       61 spqeiqkmgy tdinrmlkav pgvnvyeedg yglrpnislr gtkaerseki tlmedgilaa
      121 papyaapaay yfpnaarmqa vevvkgssqv qygpfttgga inmvstaipt kfsaklnatc
      181 gtnntlkthi nagdskkhfg ymveylryqs dgfkhfenkq nagfkrndwv akfkvntakt
      241 eganhsfelk agyadedsne tyvgltqsdf artpflryvg sqkdhlttrh tqwvgtyllq
      301 fsnrlkftth fyyntffrnw yklesvkygt sanekrtigq ilsdpetnap yfdilsgktd
      361 srvfyndyer lknnpglfvr anyrnyfsrg vqtkaeykai wgncyldnew glryhtdeed
      421 rnqwddiyam knqqmqllwk gvqgsqanki tranalaayw lskltykqlt vtvglrfehi
      481 ellekdytta dtrrtgqkri ettnvanavi pslglhynls dglsafagvh kgfsppgvsk
      541 ekrvmdrngn itlltenqkp essinfeagl rvnykqlkte ligfynnysn mlgsdlaamg
      601 gtgtleqfnv geavvkgaef iaqyqpfpee spiktplqls ytftdtemkn sfesnswgrv
      661 iagdeipyin rhslnlsiga eykkyelnig iryngavrte pgqgliaerh kipaytiidv
      721 aakahfarrf tltlnainlt nrtylvsrhp sglrpghplg ifggiiykvn
//
LOCUS       WP_009409838             364 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Actinomyces sp.
            oral taxon 448].
ACCESSION   WP_009409838
VERSION     WP_009409838.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces sp. oral taxon 448
  ORGANISM  Actinomyces sp. oral taxon 448
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 364)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 364)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Actinomyces sp. oral taxon 448"
                     /db_xref="taxon:712124"
     Protein         1..364
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=40590
     Region          10..356
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mlgrwfeehp rkqpratnrv pawfsnllpe grlreliare qgvstqreid llvriggdlp
       61 gavevipdsg acviegfera sdvpvnipep sgrlrfslag vglkfsmrqe gdrlvlpahg
      121 esgdwivktp dgrypglvan eaammrlage vgievpevhv rhydqvdelg eglwpsdede
      181 ayvvrrfdrl pggrihiedf aqvlgcfgag eekyrstvet vaaiayrgrd haslremvrr
      241 tvfnlligng dahlknwsli ypdrkiarls paydlvctaa ypdhadlglp ffgtarlsei
      301 srdhfvrlqa glnvddddvl nvvdemidrf scawaagaae rvpsrvaawi eehlerirrq
      361 laqe
//
LOCUS       WP_009412944             336 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Capnocytophaga sp. oral
            taxon 326].
ACCESSION   WP_009412944
VERSION     WP_009412944.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sp. oral taxon 326
  ORGANISM  Capnocytophaga sp. oral taxon 326
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 336)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Capnocytophaga sp. oral taxon 326"
                     /db_xref="taxon:712212"
     Protein         1..336
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36762
     Region          4..336
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mlyrsrikgl gfyvpdnvvt nddlsklmdt sdewiqertg ikerrhalkg sdtttsmgvk
       61 aslkaieaak inkeeidfiv fatlspdfyf pgcgvlvqke lglpnvgald irnqcsgfly
      121 alsvadqyik tgmyknilvi gaetqspald mstrgrnmav lfgdgagaai vsrsdnpkra
      181 ilsthlhsqg ehaeqlamia pgvgtkwvpq ilaendpddv syypnmngqf vfknavvrfa
      241 evieeglkan glsredinml iphqanlris qfvqhqfklt deqvfnnimk ygnttaasvp
      301 ialteavqqg kikdgdlvvl aafgsgftwa saiirw
//
LOCUS       WP_009412966             101 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Capnocytophaga sp. oral
            taxon 326].
ACCESSION   WP_009412966
VERSION     WP_009412966.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sp. oral taxon 326
  ORGANISM  Capnocytophaga sp. oral taxon 326
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Capnocytophaga sp. oral taxon 326"
                     /db_xref="taxon:712212"
     Protein         1..101
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11880
     Region          2..98
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mnhflehnkt kidtlwknhk vkslyafgsv ltpkfnensd idlivdfkqq dileyasnyf
       61 nlkfalqaif nreidlleek avknpyfleh inskkqliya d
//
LOCUS       WP_009414134             407 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Capnocytophaga sp. oral taxon 326].
ACCESSION   WP_009414134
VERSION     WP_009414134.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sp. oral taxon 326
  ORGANISM  Capnocytophaga sp. oral taxon 326
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Capnocytophaga sp. oral taxon 326"
                     /db_xref="taxon:712212"
     Protein         1..407
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=45826
     Region          1..284
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          282..384
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mnflhtadwh lgqtfyqydr yeeqqfflnt llqlleteai evllisgdvf dtanpsvaat
       61 kqfyhflhqa terfphlqii aiagnhdspv rlempqplle ntqvhlighi krneiheidy
      121 dalilplysk geivayclav pflrlgdtpk tddfsdygkg iatfyqeite ralaiangkp
      181 liamghlhas gaelseedta erpiiggmes vqpssfpkal kyvalghihk aqalgdahir
      241 yagspiplsf sekhythqvv tfsiengqvq gikpiplpih ipllsipert lppeevlhll
      301 talpeatses vapylevkvl lkepapelkn silktiankh vrlaridvry qqqnktqqtv
      361 lqseltlndl qpyevlqrvy enkyhaplpd fykplfeeam glvesee
//
LOCUS       WP_009416180             249 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Capnocytophaga sp. oral
            taxon 332].
ACCESSION   WP_009416180
VERSION     WP_009416180.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sp. oral taxon 332
  ORGANISM  Capnocytophaga sp. oral taxon 332
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Capnocytophaga sp. oral taxon 332"
                     /db_xref="taxon:712213"
     Protein         1..249
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28515
     Region          15..111
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          23..246
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mqsvipaeek evtyteflpc ealrsfiycy welkslprnt pfsyrvvadg cidlffecnn
       61 pqmsslmgyc ntyveilitg afhyvgvrfl psafpllfgq dafeisaqei plrevlpala
      121 tyiaqqleip lslaaiaqhl dnyflrhlsq rplqtdnrff sallqilqsk gsihisqldt
      181 gistrqlrrl fdyyigdspk afsnivrfqh ilstkayhnh sfldtyydqa hfiksfktfy
      241 gdtpskvlg
//
LOCUS       WP_009416225             236 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Capnocytophaga sp. oral taxon
            332].
ACCESSION   WP_009416225
VERSION     WP_009416225.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sp. oral taxon 332
  ORGANISM  Capnocytophaga sp. oral taxon 332
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
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
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Capnocytophaga sp. oral taxon 332"
                     /db_xref="taxon:712213"
     Protein         1..236
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=25763
     Region          1..>234
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mitfshihks yngkeiiadl nltiesgtfl tiigtsgsgk ttvlkmingl vlpdkgeiri
       61 dgknianenl ialrrnigyv iqgnilfphl svaeniayvl vlknypksdi srivaeklql
      121 vnlapelaer fphelsggqq qrvgiarala anpniilmde pfgaldsitr kqlqhelkal
      181 hqlsgativf vthditealt lgtkvlvldk gaiqqydtpe miksnpanef vrqlan
//
LOCUS       WP_009417008             407 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Capnocytophaga sp. oral taxon 335].
ACCESSION   WP_009417008
VERSION     WP_009417008.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sp. oral taxon 335
  ORGANISM  Capnocytophaga sp. oral taxon 335
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Capnocytophaga sp. oral taxon 335"
                     /db_xref="taxon:712215"
     Protein         1..407
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46298
     Region          1..286
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          280..386
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mnllhtadwh lgqtfyqydr ynehqyflnn llqiieeqht dvllisgdvf dtanpavvsv
       61 kqfyhflhqa terfpqlqii aiagnhdspv rlempqplle dtqvhlvgyv krneqreidy
      121 krliiplyer ggvmayclav pflrlgdtpk nettnpdytq gveafyreit ekalaiakgk
      181 pliamghlha lgaelsdedt aerpiiggme gfkptnfpnv lqyialghih kaqalggkah
      241 irysgspipl sfsekhyqhq vvafsleegr vqdiktvpip lhtpmlsvpe rplpvkevln
      301 alaslpkgtt htpapylevk vllnepapel knsilkaiah khvrlaridv ryqqqqnttk
      361 etlqkeitln dlqpydvlqr vyqnkfqkel pefykplfde amekand
//
LOCUS       WP_009418636             248 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Capnocytophaga sp. oral taxon 335].
ACCESSION   WP_009418636
VERSION     WP_009418636.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sp. oral taxon 335
  ORGANISM  Capnocytophaga sp. oral taxon 335
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 248)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Capnocytophaga sp. oral taxon 335"
                     /db_xref="taxon:712215"
     Protein         1..248
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=28676
     Region          55..223
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mnkkyfflfl ifvlssflyf vhaqnshlsk ekllalkkve lnikdlynel naaqydlsfe
       61 afryayigyq slrkqhrlne kdlfsiidft kdssskrfyt idlekmkivy ytyvahgrns
      121 geiksssfsd amesnkssig fyitgttyig skgfslmlyg dekgynsnla kravvihtan
      181 yanenyiart grmgrslgcp vlpeniykqv ietikektmi fayyddakyl rsskylnvlk
      241 liddesvf
//
LOCUS       WP_009418245             401 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Capnocytophaga sp. oral taxon
            335].
ACCESSION   WP_009418245
VERSION     WP_009418245.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sp. oral taxon 335
  ORGANISM  Capnocytophaga sp. oral taxon 335
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Capnocytophaga sp. oral taxon 335"
                     /db_xref="taxon:712215"
     Protein         1..401
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43998
     Region          1..401
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 meiliinsgs sslkyqlids ktgeskakgi vdrinidgsy vkyvavkngk eievkkeqpi
       61 pthevgmnlv aelltdpevg vihnpsdikg vghrvvhgge kfvqptvitd evvaeikrli
      121 plsplhnpgh legirvaqkl fnkathvavf dtafhqtmpa kafryaipne yyekyglray
      181 gfhgtshkyv daqarkhlnn qhiknitihl gngasmaavn ekgqcvdtsm gltpldglim
      241 gtrtgqidas vvfflgqelg msyeevktlf nkksgmlglt ghsdardvaa lyrsgdtnaa
      301 lcyemygyri qkfigaytaa lngldsivft aglgendalt rsfacknmdf fgikldekkn
      361 eelnhptkpv eiqasdsrvk iliiptneel qivneivdlv k
//
LOCUS       WP_009419263             465 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: replicative DNA helicase [Capnocytophaga].
ACCESSION   WP_009419263
VERSION     WP_009419263.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga
  ORGANISM  Capnocytophaga
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Capnocytophaga"
                     /db_xref="taxon:1016"
     Protein         1..465
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=53509
     Region          8..409
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mkkttdknie iekmvlgali vdsqamaenh sllnvnlftt pehqniykti eevwrrshtv
       61 dlilltarlt ekkieaytty cieltkivss saniafhihl liqnyirrnf ienfsslvek
      121 akeeatdvfe lldsafncid hlypnnqqtk kiseltekfw eshqktlsek tmlsslnivn
      181 kvlggwqksn lsivagrpnm gksaffsqei iniaeqnysv gvfsldmsnk kivinfisni
      241 tripsnsiik keldeleyri lsngiekleq mnvyiddtps isiedlikka kimkleynid
      301 ilfidnlqli cynkapnreq evsfivrslk dlakeldipi ivlsqlsrnv eqridkrpil
      361 sdlkdsgtie evaddvlfly rpehydidnw gkeysfeste nqveiiiaks hhyvkkfsec
      421 chiymeklsi enlssefvpi adpamafgva pnktednney edipy
//
LOCUS       WP_009419352             318 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Capnocytophaga sp. oral taxon 380].
ACCESSION   WP_009419352
VERSION     WP_009419352.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sp. oral taxon 380
  ORGANISM  Capnocytophaga sp. oral taxon 380
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Capnocytophaga sp. oral taxon 380"
                     /db_xref="taxon:712217"
     Protein         1..318
                     /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=37590
     Region          1..266
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mkernplidv lkgfaiilvv ighasqwflg ddrtnplyvt iyafhmplfm flsgyvnfni
       61 rgelnlskrf qvlvipffvw flisatyhgy ildiekvweh lcvliykptq gmwflwllfw
      121 ecallylalk inkhreiwvm iglwsilifl hrvtgaqpif yglpelcwyf iyfslgyath
      181 kykpqalkvl rpmgwvsvia fpllllfpvd kthyilhslr lyalaltgia asyvlwewcc
      241 rsenkatqcl kylggislei yvthyymrfl vvyikeyisd nfylnvaift vlaiiacdii
      301 qrlvqrvkwl rrilygrf
//
LOCUS       WP_009419888             444 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Capnocytophaga sp. oral taxon 380].
ACCESSION   WP_009419888
VERSION     WP_009419888.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sp. oral taxon 380
  ORGANISM  Capnocytophaga sp. oral taxon 380
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Capnocytophaga sp. oral taxon 380"
                     /db_xref="taxon:712217"
     Protein         1..444
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=51025
     Region          6..437
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mnenididie kyvlgnlvse sqlitqyynm lsvylfsapq hqsiyetivr vwkqygtvdl
       61 illgkeferk klnsytayci dlanfaissa nieyhimllv qasvkrdfvn kfsvllsmaq
      121 kkendifdir dkafeyfnnl fidkfiennr qtrefpelve avqknfesih qgkltglqss
      181 ltiinkvfgg wqksnltiva grpgmgkttf lvqqivdmva qgysvgvfsl emsaeqiask
      241 iitnytdipn ssilrkglkd eevyryislk dnltqmkihi ddtssisien lkmkaksmal
      301 ryhinilfvd ylqlitypka gnreqeisfi srslkglake ldipvialsq lsrnveqrtd
      361 krpflsdlrd sgaieqdade vvflyrpeyy gidhwdkeyn nestknevei iisknrhggi
      421 lsercvvsma tskfrdlkke insm
//
LOCUS       WP_009422021             336 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Capnocytophaga sp. oral
            taxon 412].
ACCESSION   WP_009422021
VERSION     WP_009422021.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sp. oral taxon 412
  ORGANISM  Capnocytophaga sp. oral taxon 412
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 336)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Capnocytophaga sp. oral taxon 412"
                     /db_xref="taxon:712218"
     Protein         1..336
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36822
     Region          4..336
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mlyrsrikgl gfyvpenvvt nddlsklmdt sdewiqertg iqqrrhalkg sdtttsmgvk
       61 aslkaieaak inkeeidfiv fatlspdfyf pgcgvlvqke lglptvgald irnqcsgfiy
      121 alsvadqyik tgmyknilvi gaetqspald mttrgrnmav lfgdgagaai vsrsdnserg
      181 ilsthlhsqg ehaeqlamit pgvgtkwvte llaendpndv syypnmngqf vfknavvrft
      241 evieeglksn glshkdinml iphqanlris qfvqhqfklt deqifnnimk ygnttaasip
      301 ialteavqqg kikdgdlvvl aafgsgftwa saiihw
//
LOCUS       WP_009423659             188 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Fusobacterium sp. oral taxon 370].
ACCESSION   WP_009423659
VERSION     WP_009423659.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium sp. oral taxon 370
  ORGANISM  Fusobacterium sp. oral taxon 370
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Fusobacterium sp. oral taxon 370"
                     /db_xref="taxon:712288"
     Protein         1..188
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21445
     Region          2..150
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 miekikntrs hrkftdkkis keeilkileg arysssakns qflrysytvd dekckklfsa
       61 ialggllkae dkptleerpr ayilisakkd idipdflqyf dvgiasqniv llanelgyga
      121 cmvmsynkni frevlelped yetravivlg eakdivklid lkdendtkyf iengihyvpk
      181 lsldkill
//
LOCUS       WP_009425036             139 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [unclassified Neisseria].
ACCESSION   WP_009425036
VERSION     WP_009425036.1
KEYWORDS    RefSeq.
SOURCE      unclassified Neisseria
  ORGANISM  unclassified Neisseria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="unclassified Neisseria"
                     /db_xref="taxon:2623750"
     Protein         1..139
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15950
     Region          1..130
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkhhnqrgft lielmiaiai iailaaiayp sydnfirktr lenargdlln naqrlerfya
       61 rnrtfnkfnd lkndnkyfei tyvynddnqn mtdpdvghyl ltatpkanna nekrymqlnd
      121 dgivtvctga gadkdcemy
//
LOCUS       WP_009425037             155 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [unclassified Neisseria].
ACCESSION   WP_009425037
VERSION     WP_009425037.1
KEYWORDS    RefSeq.
SOURCE      unclassified Neisseria
  ORGANISM  unclassified Neisseria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="unclassified Neisseria"
                     /db_xref="taxon:2623750"
     Protein         1..155
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=17218
     Region          1..106
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkrhfsfsgf tlievmvaaa ilavlaaiay psyqrhvkna rmkqasavlf dnaraleqfy
       61 arnrsfkads ttwtdipftr nghfcfkmqg dargaltdsf tvkavaldkd neprvlrinq
      121 dhilticess nsscsdtspy fsnangtdkd ctvye
//
LOCUS       WP_009427253             209 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [unclassified Neisseria].
ACCESSION   WP_009427253
VERSION     WP_009427253.1
KEYWORDS    RefSeq.
SOURCE      unclassified Neisseria
  ORGANISM  unclassified Neisseria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 209)
  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 209)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 209)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="unclassified Neisseria"
                     /db_xref="taxon:2623750"
     Protein         1..209
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22760
     Region          1..204
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 mashldeqqe lenfkylwnk wgrwvfaalv laaaayfasv myahhrlekn geaaaalaal
       61 vekaqgssdd kavraellnl qqnhpdsisa aqatmmaaad dfdkgryaea ekqlgwvlqn
      121 qqdafvrala vqrlssvqaq qkkyaaalat lktpvddafs gvlletqgdv lyaqgkskea
      181 aeayrmaldk tpkgtpgret lemkagelk
//
LOCUS       WP_009429437             452 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Oribacterium sp. oral taxon
            108].
ACCESSION   WP_009429437
VERSION     WP_009429437.1
KEYWORDS    RefSeq.
SOURCE      Oribacterium sp. oral taxon 108
  ORGANISM  Oribacterium sp. oral taxon 108
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Oribacterium.
REFERENCE   1  (residues 1 to 452)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Oribacterium sp. oral taxon 108"
                     /db_xref="taxon:712414"
     Protein         1..452
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=50197
     Region          79..181
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          327..451
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(402..403,406,424..427,429)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkkiklflsa lllsvllpms ayaldrfvmg tygngiplse ktveeaksyl egeysrnyvl
       61 yikgrdkvee ikgsdigyql saatnleeil kreekeglep kadgrydfsl egssakfdea
      121 klkeriaqls vlkyskktan ayiqkdgtys ivpevegdsl deakfyanly salqrgentl
      181 dltqrgiydt vtvhksdlep kleavrrles veivtnilgn kevlsgdtls dmvlgingng
      241 vifdeakvla yanylegkyg npgntvsfhs asgkdiamlt pyalhinvqg ekealkqais
      301 afktmerepv ysyrpaqyaq pqfgttfvei dlslqhvyyy eggnlvwesp tvtgmlsgdr
      361 atpsgifflk gketnrtlrg klvngkpeye ahvdywmpfn ggiglhdasw rskfggniyv
      421 rggshgcinl prnkaaelyn riqkgcpivv he
//
LOCUS       WP_009431413             278 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Urinicoccus
            timonensis].
ACCESSION   WP_009431413
VERSION     WP_009431413.1
KEYWORDS    RefSeq.
SOURCE      Urinicoccus timonensis
  ORGANISM  Urinicoccus timonensis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Urinicoccus.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Urinicoccus timonensis"
                     /db_xref="taxon:2024205"
     Protein         1..278
                     /product="formate/nitrite transporter family protein"
                     /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=29271
     Region          5..276
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mgkllkpgei leatsnigla kantkpinqv ilgilagafi afaaqgsnma afnllakpet
       61 fglgklvsgl vftpglifvl iagaelftgn mlmfaalfdk kitwaslirt lvlvyignfi
      121 gslliawmvs qsgqwgaaan algartilia ngkvgltfgk afilgilcnw lvclgvwmsf
      181 gadsqvgkml saffpimlfv tsgfehsian myyipagima kanpdflaat glgadelanl
      241 twsgfftnnl ipvtlgnivg gvvfvalayw ivyrkksa
//
LOCUS       WP_009433728             407 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Porphyromonas].
ACCESSION   WP_009433728
VERSION     WP_009433728.1
KEYWORDS    RefSeq.
SOURCE      Porphyromonas
  ORGANISM  Porphyromonas
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Porphyromonadaceae.
REFERENCE   1  (residues 1 to 407)
  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 407)
  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
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 407)
  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   5  (residues 1 to 407)
  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   6  (residues 1 to 407)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 407)
  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 11973053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Porphyromonas"
                     /db_xref="taxon:836"
     Protein         1..407
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44545
     Region          <9..59
                     /region_name="COG3398"
                     /note="Predicted transcriptional regulator, contains two
                     HTH domains [Transcription]"
                     /db_xref="CDD:442625"
     Region          81..399
                     /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 mtpkllddls qetkkglhkl rvinyllrnk tatmtdiake lyvsvptask ilqdlqdggc
       61 iqsqgkleig vgrfpllfgl npdggyfigv dikrsgmhig linlqselic adydlpytle
      121 ntpealetic reirgfitrh giqpkeilni nvnlpgrinp vtghsyslfn ffgdrplsei
      181 lssklalrvs idndtrgmaf geftagctkd mevnsvlyvn iswglglgii qdkqiyfgks
      241 gfsgefghis vfdnqilchc gkkgcletev sgqamcrkiq eriragessv lssivhsgre
      301 lrmsdlisac aqedmlclqv lselgrelgk qvanlinvfn pelviiggsl adasgyltqq
      361 veasvriysm svvtrdtqir tatlgdragl igacmlarsr rfaepsk
//
LOCUS       WP_009434660             632 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Prevotella sp. oral taxon
            306].
ACCESSION   WP_009434660
VERSION     WP_009434660.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. oral taxon 306
  ORGANISM  Prevotella sp. oral taxon 306
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Prevotella sp. oral taxon 306"
                     /db_xref="taxon:712461"
     Protein         1..632
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=71195
     Region          65..>500
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mefkkqplts athseftlea lrqiapsaft evrgadgelt qkvdfkvlre llgdaiadad
       61 eesfgfqwvg kqeakraaae ptrqtlrpvv ddsvdwdtte nlyiegdnle vlkllqrayl
      121 gkvkmiyidp pyntgndfvy eddfamsgee mdeamgnvde egnrlrrnld snpryhsdwc
      181 smiysrllva rtllandgvi fisiddnevh hlrkicdevf gagnflaqvv werayapinl
      241 mkhfspshdy ivcyakdvdl akcngiprss eadarysnpd ndprgvwkas dlsvgpaies
      301 nvypittpsg rvveppagrs wslsanafae rlrqnriwfg sdgnnvpamk rflselrktg
      361 vtpmtiwkyg evghsqgatq alaemfdgkk yfdypkpvdl ikrcislyss pdslildffs
      421 gsattahavm qlnaedggkr kyicvqipek tpegsearka gynticeigk erirragkki
      481 keeaglmgqd ldtgfrvlrv dssnmeevyf epagleqqnl ftqvdsvkad rseldllfgc
      541 mvdwgvelsy plrmeevdgk hlhivnegal vacfdkeisv eavsriaelk plrvifreec
      601 fatdadklni yekfkqfcgw ndeevykrih vl
//
LOCUS       WP_009435755             158 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Prevotella sp. oral taxon 306].
ACCESSION   WP_009435755
VERSION     WP_009435755.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. oral taxon 306
  ORGANISM  Prevotella sp. oral taxon 306
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 158)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Prevotella sp. oral taxon 306"
                     /db_xref="taxon:712461"
     Protein         1..158
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17771
     Region          1..155
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mtrkeqyeql ipqiaglikd etnlvgilan vsaalheafp erffwvgfyl qengnmlrlg
       61 pfqgsvacyt ipygkgvcgk aweegrtqiv pnvetfpghi acssrsrsei vipmydsqrh
      121 frgvldidst rfddfsaedk dglehiiqll maqiedlf
//
LOCUS       WP_009439366             642 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter permease [unclassified Selenomonas].
ACCESSION   WP_009439366
VERSION     WP_009439366.1
KEYWORDS    RefSeq.
SOURCE      unclassified Selenomonas
  ORGANISM  unclassified Selenomonas
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Selenomonas.
REFERENCE   1  (residues 1 to 642)
  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 642)
  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 642)
  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 642)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="unclassified Selenomonas"
                     /db_xref="taxon:2637378"
     Protein         1..642
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=67566
     Region          1..639
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mndkntvntd eilkkydres dtvhyegipk kiiaaiaitf svfqlytatf gvldaqlqra
       61 vhlgfglala yllypfrrkw trdaffhpid vlfavlgaaa payiviqyre lvtragsvsg
      121 vdtvvgvlgi llvieaarrv vglpmvtvvl lflayaflgp ympgvlahrg ltleqlvghl
      181 yfttegifgi plgvsstfif lfilfgayle stglgkffid lanavagwas ggpakvavls
      241 sglmgtvsgs svanvvgtgs ltipmmkklg ydanfagave aaastggqlm ppvmgaaafl
      301 maefvgvpyi evvkaaaipa llyftgvwlg vhfeakrknl kgiprselpn pltllkergh
      361 laiplvvivy llvsgytpmr aalvaivlsi icamlrsstr mkpmeivygl ergakavlgv
      421 liacaaagii igvvtktgvg lrlasglida aggmllpamf ftmitaivlg mgvpttanyv
      481 itstiaapal vqmgvpilaa hmfvfyfgii advtppvala ayagagisgg nplktgvhas
      541 klavaafiip yifvlspvil mvdatpfalv tatltalvgm iavssalcgf laddcklyer
      601 vllvmagllm ikpgsttdmi glvlfaailv iqnlrkkrkn re
//
LOCUS       WP_009440856             639 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Selenomonas sp. oral taxon 138].
ACCESSION   WP_009440856
VERSION     WP_009440856.1
KEYWORDS    RefSeq.
SOURCE      Selenomonas sp. oral taxon 138
  ORGANISM  Selenomonas sp. oral taxon 138
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Selenomonas.
REFERENCE   1  (residues 1 to 639)
  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 639)
  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 639)
  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 639)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Selenomonas sp. oral taxon 138"
                     /db_xref="taxon:712532"
     Protein         1..639
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=67013
     Region          1..638
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mtdqktaeav lkkydresnt ahyaglpkki iaaiaitfsi fqlytatfgv ldaqlqravh
       61 lgfglalayl lypfrrawtr dtffhpidvv favlgaaapa yiviqyrelv tragtvttpd
      121 vivggigill vieatrrvvg lpmvtvvllf layaflgpym pgvlahrgls ieqlishlyf
      181 ttegifgipl gvsstfiflf ilfgaylest glgkffidla navagwasgg pakvavlssg
      241 lmgtvsgssv anvvgtgslt ipmmkklgyn anfagaveaa astggqlmpp vmgaaaflma
      301 efvgvpyiev vkaaaipall yftgvwlgvh feakrknlkg iprselpnpi tlikerghla
      361 iplvvivyll vsgytpmraa lvaivlsitc amlrkstrmk pieivygler gakavlgvli
      421 acaaagiiig vvtktgvglr lasglidlag gmllpamfft mvtaivlgmg vpttanyvit
      481 stiaapalvq mgvpilaahm fvfyfgiiad vtppvalaay agagisggna lktgvhaskl
      541 avaafiipyi fvlspvilmv datpltlila tlsalagmia vssalcgfla dhcrpyerll
      601 liiagvlmik pggttdligc vifavilvmq yqrvkkaae
//
LOCUS       WP_009441146             276 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Selenomonas].
ACCESSION   WP_009441146
VERSION     WP_009441146.1
KEYWORDS    RefSeq.
SOURCE      Selenomonas
  ORGANISM  Selenomonas
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Selenomonas"
                     /db_xref="taxon:970"
     Protein         1..276
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30268
     Region          1..247
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mpsdlhihtt fsdgkdtpee iveaakaagl ryiaitdhds vegvtalyes ghyasgslhi
       61 ipgvgfstgd gqneihilgy nidiydaglq ekleeisear wtrfteiver lkdigyeige
      121 tevltdeglc kavgrshvar vlvkkgyfds iracfdqllk rgrpayvphf ylpieeival
      181 ikgaggipvl anpkaigdea averiaqqgm ggieafypsy dvrdtqhyld vaqkygllvs
      241 ggsdyrgfag repdavgkft iediyaenfy rppqhm
//
LOCUS       WP_009450109             350 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Nitratireductor indicus].
ACCESSION   WP_009450109
VERSION     WP_009450109.1
KEYWORDS    RefSeq.
SOURCE      Nitratireductor indicus
  ORGANISM  Nitratireductor indicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Nitratireductor.
REFERENCE   1  (residues 1 to 350)
  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 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   3  (residues 1 to 350)
  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   4  (residues 1 to 350)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 350)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 350)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 350)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Nitratireductor indicus"
                     /db_xref="taxon:721133"
     Protein         1..350
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37238
     Region          24..341
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(90..92,113..114,166,218,242)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mrclalplvf llaaatpsna edfrigvaap fsgsfsilgs qirdgarval aqdndavelf
       61 eqdtacspeg gaaaaralia drvsvvvgfi cteaveaalp llteagipti tpgvrtatlt
      121 dgrersgflv yrtapradae rdavarilse rwrkeffaiv ddgtiygrel aeslrasael
      181 rklepvfkdt frpqldnqvg lagrlkraga thvfvggdrs diailardak gmdyvltiag
      241 gealraenst vplaegtlmv glprwadias pqalqalkaa eilpdgyvlp ayaaaqtala
      301 asekgdvnaa lakerfetvl gpfafdgkgd ldtsfyrlfr fdgedfreve
//
LOCUS       WP_009409705             496 aa            linear   BCT 20-JAN-2025
DEFINITION  ferrochelatase [Actinomyces sp. oral taxon 448].
ACCESSION   WP_009409705
VERSION     WP_009409705.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces sp. oral taxon 448
  ORGANISM  Actinomyces sp. oral taxon 448
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Ferreira,G.C.
  TITLE     Ferrochelatase
  JOURNAL   Int J Biochem Cell Biol 31 (10), 995-1000 (1999)
   PUBMED   10582332
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Ferreira,G.C., Franco,R., Lloyd,S.G., Moura,I., Moura,J.J. and
            Huynh,B.H.
  TITLE     Structure and function of ferrochelatase
  JOURNAL   J Bioenerg Biomembr 27 (2), 221-229 (1995)
   PUBMED   7592569
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Taketani,S.
  TITLE     Molecular and genetic characterization of ferrochelatase
  JOURNAL   Tohoku J Exp Med 171 (1), 1-20 (1993)
   PUBMED   8122254
REFERENCE   4  (residues 1 to 496)
  AUTHORS   Cole,S.P. and Marks,G.S.
  TITLE     Ferrochelatase and N-alkylated porphyrins
  JOURNAL   Mol Cell Biochem 64 (2), 127-137 (1984)
   PUBMED   6390167
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11477763
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Actinomyces sp. oral taxon 448"
                     /db_xref="taxon:712124"
     Protein         1..496
                     /product="ferrochelatase"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0004325 - ferrochelatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51535
     Region          9..385
                     /region_name="hemH"
                     /note="ferrochelatase; Reviewed; PRK00035"
                     /db_xref="CDD:234585"
ORIGIN      
        1 mndpldplsp ydavlllsyg gpqgpddvlp fmrnatagrg vpdsrllqvs ghygrfggis
       61 pinarnaell ealrtelaar gshlpvvvgn rnwfpfvsea lraladggar rvlavttsay
      121 gsysgcrqyr edvagalell aagadgttgr gaeadaaarv ggaggapvrl tvdktrpfyn
      181 tdgmlranvd aiveayerlr ergidpravr lalvthsipe smergsaprd grsashpgpa
      241 aldpgvaadl steisyvaqh rrfidvllpv laerlglkap pdhdlvfcsr sgpprsrwle
      301 pdindhlesl aagrltdgmp vtapagvvva pvgfvadhme vvfdldieaa ntaerlgmpy
      361 vraatagthp afvsslgdvl aeraavarge garptsttgt gpfhtvcppd cclpatrppr
      421 ardgsgghda hagragrpga cgalrttgpg asgpsddlen pvvpadetda vnlttsvpls
      481 pgrphtapia eegdpr
//
LOCUS       WP_009451082             701 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Nitratireductor indicus].
ACCESSION   WP_009451082
VERSION     WP_009451082.1
KEYWORDS    RefSeq.
SOURCE      Nitratireductor indicus
  ORGANISM  Nitratireductor indicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Nitratireductor.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Nitratireductor indicus"
                     /db_xref="taxon:721133"
     Protein         1..701
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=74546
     Region          9..701
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mtyanpdrre tisrllnpks iavigassdf gkvngrplkh liekgyagri lpvnpkyeei
       61 aglvcypsie alpeaadlai ialpaahvcd cveklgrkgi rtavifssgf gemgdegkvl
      121 ekrlaetaka arvillgpnc lgfvnafdnv yatfsqyadg etgagpiafv tqsgafgtai
      181 aalvrqrglg lgyflntgnq adlsfaelmm aivedprikv aagylegitd gdalvrlark
      241 cqelgkplil tkvgrmssga raaashtgal avsdavfdav vrqygvlrar neeqmldmle
      301 vfcqprracg sglgiatqsg gagvmmadra eevgltvpel gaatqarlaa vmpafgaagn
      361 pvdvtgqfva rpelltesvv sllddpdidv aivwlqlmta hvepllgifr eiqqrtvkpf
      421 lvcwvaapda aikglraadi pvytagerav eaaaalaryg mqrktsedav spsgspacpg
      481 ttgsgmqptv easswlreag ipmaharlae sedhavalwr dsarpvalki espdiphkte
      541 idgvilnidd eagirsgyra lierartamp darlsgvlvq emaeghvelv igvqrdpvfg
      601 mivmvgfggi lvevlkdvtf rrapfdrsea ysmlddlrms rildgvrgkp avdreaisll
      661 lfrlshwaaa meprlseldl npvlvgeagp svvdcvmile e
//
LOCUS       WP_009451731             276 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Nitratireductor
            indicus].
ACCESSION   WP_009451731
VERSION     WP_009451731.1
KEYWORDS    RefSeq.
SOURCE      Nitratireductor indicus
  ORGANISM  Nitratireductor indicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Nitratireductor.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Nitratireductor indicus"
                     /db_xref="taxon:721133"
     Protein         1..276
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=29608
     Region          2..269
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mavtraadrd rylsvlyape ekrgalfaly afnsaiagir drvseplpga vrlqfwrdal
       61 amgvshggge aegaplvial tqtirehglp ldpflnmlda refdlyddpm psrndlegyc
      121 getasaliql aslvldpaaa rgvaeiagha gcaqaiagll rllpihrrrg qcyvpadvma
      181 aagidreafl sgrdgsgaer viaamvalgr dhaarfetla rdlvpalrpa flpaglapay
      241 fgrlegkgvr aldevaeipa wrrhwimfrr atsgwg
//
LOCUS       WP_009452066             328 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Nitratireductor
            indicus].
ACCESSION   WP_009452066
VERSION     WP_009452066.1
KEYWORDS    RefSeq.
SOURCE      Nitratireductor indicus
  ORGANISM  Nitratireductor indicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Nitratireductor.
REFERENCE   1  (residues 1 to 328)
  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 328)
  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 328)
  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 328)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Nitratireductor indicus"
                     /db_xref="taxon:721133"
     Protein         1..328
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=35302
     Region          1..316
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mkisklllaa vaafgmggsa saadfnlrih tlvksphpyn dmaaflkedi eaksdgriav
       61 rifdsgqlgq dpaviseigl gtidmmistt snavqqvpey aiftmpyift smddalakvg
      121 pgtpieahfq kvyeerglnm kllalgasgt rnmstaetvv ngpddlkglk mrtppspmds
      181 ktwaafgmlp vtvawgelya amqtgvaqam esslpgytgs klyevapnla ltahtiqvnh
      241 tsisnrtwnk lpedlqkivq asaieanklg vekakqydde lvseletkhg vkvtrpdtaa
      301 fievlapiqt elakeldled eyalvkak
//
LOCUS       WP_009454764             246 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Alcaligenes].
ACCESSION   WP_009454764
VERSION     WP_009454764.1
KEYWORDS    RefSeq.
SOURCE      Alcaligenes
  ORGANISM  Alcaligenes
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  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   3  (residues 1 to 246)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Alcaligenes"
                     /db_xref="taxon:507"
     Protein         1..246
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27310
     Region          35..242
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mtstlppted dpyqiqskfe ilrvlqaiek gglllhmean qgndrivtti ldidldnnvv
       61 vidtankeek trnllqseht hfetsldkik vtfqgptpev vsyegqpala ipipesirrl
      121 qrreffrvnv pvsepamvil rlnnesksfl lhdisgggls lvdesqslae vigthktesl
      181 lelpqagsfv valqvartet qqlpngkqiq rlgctfidls astqmaiqhy igrlerqqia
      241 kqrghg
//
LOCUS       WP_009454844             370 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ferrochelatase [Fischerella].
ACCESSION   WP_009454844
VERSION     WP_009454844.1
KEYWORDS    RefSeq.
SOURCE      Fischerella
  ORGANISM  Fischerella
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Hapalosiphonaceae.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ferreira,G.C.
  TITLE     Ferrochelatase
  JOURNAL   Int J Biochem Cell Biol 31 (10), 995-1000 (1999)
   PUBMED   10582332
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Ferreira,G.C., Franco,R., Lloyd,S.G., Moura,I., Moura,J.J. and
            Huynh,B.H.
  TITLE     Structure and function of ferrochelatase
  JOURNAL   J Bioenerg Biomembr 27 (2), 221-229 (1995)
   PUBMED   7592569
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Taketani,S.
  TITLE     Molecular and genetic characterization of ferrochelatase
  JOURNAL   Tohoku J Exp Med 171 (1), 1-20 (1993)
   PUBMED   8122254
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Cole,S.P. and Marks,G.S.
  TITLE     Ferrochelatase and N-alkylated porphyrins
  JOURNAL   Mol Cell Biochem 64 (2), 127-137 (1984)
   PUBMED   6390167
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Fischerella"
                     /db_xref="taxon:1190"
     Protein         1..370
                     /product="ferrochelatase"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0004325 - ferrochelatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=41747
     Region          19..348
                     /region_name="HemH"
                     /note="Protoheme ferro-lyase (ferrochelatase) [Coenzyme
                     transport and metabolism]; COG0276"
                     /db_xref="CDD:440045"
ORIGIN      
        1 mvatpekleh nheqssgqqr vavllmgyge vesyedfany neqalhllta kfapvpawiy
       61 pplarilalf drhewghqhn dfisphnaif ekqragiekn lqqkwgdrvq vfkafnfcap
      121 flphqvlaei knqgfdklli ypllvvdsif tsgiaieqvn kalsqltdgs ehwvkglryi
      181 psfyneaayi dmmvhlveek iasdlaaayl paeigivlmn hgcphkakgf tsgitesqal
      241 ydlirdklin ryplisigwl nhdtpliewt qpnveqaakn liqlgakavm fmpigfaten
      301 hetlldvhhi ihalekkhsq vnyvqmpcvn dhpdflamaa qwanphiadl lseeattvnp
      361 qlavahhhhh
//
LOCUS       WP_009455121             441 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Fischerella thermalis].
ACCESSION   WP_009455121
VERSION     WP_009455121.1
KEYWORDS    RefSeq.
SOURCE      Fischerella thermalis
  ORGANISM  Fischerella thermalis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Hapalosiphonaceae; Fischerella.
REFERENCE   1  (residues 1 to 441)
  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 441)
  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 441)
  AUTHORS   ter Beek,J., 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 441)
  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 441)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Fischerella thermalis"
                     /db_xref="taxon:372787"
     Protein         1..441
                     /product="CmpA/NrtA family 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=48370
     Region          59..311
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 msnlsrrkfi ltastaaaas ilahgcssgg sqsattggdk psattaanvs tvanapkvet
       61 tkaklgfipl tdaapliiak ekgffakygm tdvevvkqks wpvtrdnlki gsagdgidga
      121 hilspmpylm tindkvpmyi larlntngqg isaanklkdl kvglqskalk qaadqakank
      181 qvmkvamtfp ggthdlwmry wlaagginpd qdvvlepvpp pqmvanmkvg tvdafcvgep
      241 wnaqlvsqkl gytalvtgel wkdhpekafa mrkdwvdknp nateallmai meaqqwcdqa
      301 enkeemckic sdrkyfnvav tdilerskgn idygdgrtqq nfphrmkfwa dnasypyksh
      361 dlwflteeir wgylpkdtkv keivdqvnre dlwkkaakai gvddseipts vsrgvetffd
      421 gvkfdpdkpe aylsslkikk v
//
LOCUS       WP_009455148             747 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Fischerella
            thermalis].
ACCESSION   WP_009455148
VERSION     WP_009455148.1
KEYWORDS    RefSeq.
SOURCE      Fischerella thermalis
  ORGANISM  Fischerella thermalis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Hapalosiphonaceae; Fischerella.
REFERENCE   1  (residues 1 to 747)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 747)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 747)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Fischerella thermalis"
                     /db_xref="taxon:372787"
     Protein         1..747
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=82699
     Region          1..733
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mtevtktlcp ycgvgcglev sppaqpgkat hrdgqgnpiw rvrgdkahps sqgmvcvkga
       61 tiaesldknr lhypmvrdsl dqkfrrvswd eafdlitkri qavrftqgpe aicmygsgqf
      121 qtedyyiaqk llkgclgsnn fdansrlcms savagyiqsf gadgppccye dleltdcafl
      181 igtntaechp ivfnrlekyh krnrkvkmiv vdprrtptae aadlhlairp gtdidllngi
      241 ahllmrwnyi dvgfiddcts nfpayaevic hyspeivadr cgidikdlet aarywgesqr
      301 vlslwsmgvn qssegtakvr tiinlhlmtg qigkpgagpf sltgqpnamg greagglahl
      361 lpgyrlvknp qhraeveefw glkrgqispn pgltawdmit gledgtvgll wiaatnpavs
      421 mpdlertkaa lmrspftiyq dayyptetat yahvllpaaq wsektgvmtn sertvtlcpa
      481 frrppgeaka dweifaevgr rlgfvgefaf ansaevyaef vkltrdrpcd mtglsheqlr
      541 sqgptqwphp aeemgrtgdg einftppphh kspntqsskr lytnlrfhtp dgrarfgayh
      601 srglaeppdp dypfvlttgr lyghwhtltr tgriektrqm hpepfieihp rdaarleitd
      661 nqlvevrsrr sktffpakit kaiapgtvfv pmhwgalwad naeanalthp escpdslqpe
      721 lkacavqlip vtaeltvnak vsiaaki
//
LOCUS       WP_009455434             276 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: hydroxypyruvate isomerase family protein
            [Alcaligenes].
ACCESSION   WP_009455434
VERSION     WP_009455434.1
KEYWORDS    RefSeq.
SOURCE      Alcaligenes
  ORGANISM  Alcaligenes
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 276)
  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 276)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Alcaligenes"
                     /db_xref="taxon:507"
     Protein         1..276
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30315
     Region          1..257
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mqlsanlswl yrhldwserf eaaaadgfqg veillpydya pdwyasqlka akleltlint
       61 pigegqgrlg waaipgaqaq fqeafdhara vtqatgcrri hvmagdvslf aqqdcraall
      121 snleqalala eaddlvltle alnrsdmagy fyylpeqvie vlqhfnsprl rlqfdyyhcv
      181 kesldvpssv avcapwigyv qiagadgrye pdlaqhdlla gvaalpalay dswlgceyqp
      241 rglpseglaw cqplrdrgvl aaprqrdaac mqaagr
//
LOCUS       WP_009455588             243 aa            linear   BCT 20-JAN-2025
DEFINITION  phosphonate ABC transporter ATP-binding protein [Fischerella
            thermalis].
ACCESSION   WP_009455588
VERSION     WP_009455588.1
KEYWORDS    RefSeq.
SOURCE      Fischerella thermalis
  ORGANISM  Fischerella thermalis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Hapalosiphonaceae; Fischerella.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
REFERENCE   2  (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   3  (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   4  (residues 1 to 243)
  AUTHORS   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Fischerella thermalis"
                     /db_xref="taxon:372787"
     Protein         1..243
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=26285
     Region          3..238
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mspaiechnl ktayspslqr pilngiscqi hhgefvallg lngagkstll rslvglvple
       61 rgniningvq vnprtlpqir qdigmlfqgg glirqlpaid nvlcgklgir ttwqtlfgfp
      121 khdrrqalei leqlglraqa yqktsqlsgg qqqriaiara liqspqilla depitgldvm
      181 ackqvmdtls qlhsqqgiti vtvlhdlgia aeyaqraivl dagrivydgv cenlqaqfsg
      241 mrg
//
LOCUS       WP_009455707             385 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Alcaligenes].
ACCESSION   WP_009455707
VERSION     WP_009455707.1
KEYWORDS    RefSeq.
SOURCE      Alcaligenes
  ORGANISM  Alcaligenes
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 385)
  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 385)
  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   3  (residues 1 to 385)
  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   4  (residues 1 to 385)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 385)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 385)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 385)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Alcaligenes"
                     /db_xref="taxon:507"
     Protein         1..385
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40820
     Region          33..369
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(109..111,131..132,181,233,257)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mqsitsfkla lvstavfgal aaspafaadk viklgfsapl tgpqahyged mrnglvlale
       61 eanaqkieid gatarfelva kddqadprta vqvaqqivdd gvdgvlghfn sgttipasrv
      121 yndagipqia matspeytqq gydntfrmmt sdtqqgaavg qfivkdlaak kvaliddrta
      181 ygqgltdqva ravekaggqi vareyttdka ndftsiltni kskapdaiff ggldaqsgpm
      241 krqmqtldik aplvsgemtr sdtflrlaga aadgtyasla gvplstmaag ekfakdyqar
      301 fkaepgvyap yaydgawnmi tamkeagssk aedylpklaa lkrngatssn iaydqngdlk
      361 eiavtiyevk dgkwtmvktm vsqan
//
LOCUS       WP_009457721             388 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [Alcaligenes].
ACCESSION   WP_009457721
VERSION     WP_009457721.1
KEYWORDS    RefSeq.
SOURCE      Alcaligenes
  ORGANISM  Alcaligenes
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 388)
  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 388)
  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 388)
  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 388)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Alcaligenes"
                     /db_xref="taxon:507"
     Protein         1..388
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=42125
     Region          18..378
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mrnrikksta pqaqtgasrr kflsgaaagt aaaatmgfpa iaraqgpinf rfqstwptvd
       61 ifhefaldfa kkindmtggd lkievlpaga vvpafgllda vskgtldggh gvlgynygkq
      121 nalalfssgp afgmdanmvl awhkygggke llaklydaig gnvvsfltgp mptqpfgwfk
      181 kpitktedlk glkfrtngla idlftemgaa vnalpggeiv paldrglldg aefnnaasdr
      241 algfpdvskv cmlqsfhqas etfeimfnkd kynalptqlk aivdnaveaa sadmswkavd
      301 rysqdyqrlq kedgvkfykt pdtilqqqlv vwdqivakka etnplfkeid asqrafaara
      361 mawdmdtnnn rrmaynhyfg rkapqaks
//
LOCUS       WP_009458446             346 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Fischerella thermalis].
ACCESSION   WP_009458446
VERSION     WP_009458446.1
KEYWORDS    RefSeq.
SOURCE      Fischerella thermalis
  ORGANISM  Fischerella thermalis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Hapalosiphonaceae; Fischerella.
REFERENCE   1  (residues 1 to 346)
  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   2  (residues 1 to 346)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Fischerella thermalis"
                     /db_xref="taxon:372787"
     Protein         1..346
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=37773
     Region          47..116
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
     Region          55..>213
                     /region_name="rad50"
                     /note="TIGR00606"
                     /db_xref="CDD:129694"
ORIGIN      
        1 mkkfrylyla vtacaivtls scndgtstte nspsastpns vaqtteavsh sshgskkqin
       61 intailseld kfeaqlgvpa lsnkiqanrp yaspeelvnk kvitqeqfdk ikdqvtvqev
      121 iltgeakdid ymtklglmkg hlivaqelld qnqpkqaeph ighpveeiyv dvedqlnerq
      181 vkefkttlvn lqdlvksnpk dskvktnftt smqsvdraia alpetqrtqp sfvlqvingl
      241 ldsanseyga avadgkitaa ieyqdsrgfv lyadelyksi ssqvakdkpe adkaiqasma
      301 qlkktwpsvi paakpvntpe evtkqikaie sasqkvidaa ktqaqr
//
LOCUS       WP_009458438             166 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Alcaligenes].
ACCESSION   WP_009458438
VERSION     WP_009458438.1
KEYWORDS    RefSeq.
SOURCE      Alcaligenes
  ORGANISM  Alcaligenes
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 166)
  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 166)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 166)
  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   4  (residues 1 to 166)
  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   5  (residues 1 to 166)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Alcaligenes"
                     /db_xref="taxon:507"
     Protein         1..166
                     /product="TRAP transporter small permease subunit"
                     /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=19121
     Region          2..156
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mvlrlidsin ewigklisfi aiifsaiiiy evfmryvmnq ptrwtfdvtk qlygfyflml
       61 gayalkhqah vrvdllinrf sptvrkwtei agylifffpf awvfltrsyd famrslaqge
      121 ttygavqlpv yplkmsmvla aallllqgia evirlltqke aahhda
//
LOCUS       WP_009459181             454 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Fischerella thermalis].
ACCESSION   WP_009459181
VERSION     WP_009459181.1
KEYWORDS    RefSeq.
SOURCE      Fischerella thermalis
  ORGANISM  Fischerella thermalis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Hapalosiphonaceae; Fischerella.
REFERENCE   1  (residues 1 to 454)
  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 454)
  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 454)
  AUTHORS   ter Beek,J., 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 454)
  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 454)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Fischerella thermalis"
                     /db_xref="taxon:372787"
     Protein         1..454
                     /product="CmpA/NrtA family 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=49686
     Region          57..317
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mseffhqisr rkfivtatas asavflkgcl gnppetgggs aqtqsgaqpv anispeqtpe
       61 tktvklgyvp iveaapliia kekgffakyg mtdvelskqa swgsardnve igsagggidg
      121 gqwqmpmphl iteglitkgn qkipmyvlaq lithgngiav askhqgkgig lqlasakslf
      181 tqlksstpft aaftfphvnq dlwirywlaa ggidpdadvk lltvpaaqtv anmktgtmda
      241 fstgdpwpyr ivrdkigfma altaeiwknh peeylairad wvdknpkatk allkgvmeaq
      301 qwldnfdnrk eaaailagrn yfnlpeeila gpfqgkydmg dgrtiddksm apyywkdekg
      361 svsypykshd lwfivenvrw gflpkdyltk analidkvnr ediwkeaake agiaaadipt
      421 stsrgveeff dgvefdpkqp eaylkslqik kvsv
//
LOCUS       WP_009460277             229 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Fischerella thermalis].
ACCESSION   WP_009460277
VERSION     WP_009460277.1
KEYWORDS    RefSeq.
SOURCE      Fischerella thermalis
  ORGANISM  Fischerella thermalis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Hapalosiphonaceae; Fischerella.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Fischerella thermalis"
                     /db_xref="taxon:372787"
     Protein         1..229
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25490
     Region          32..224
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mtvnfirtaf asrefleevf qninaqscpk cfnfhmhtvy sdgklhpcgl meqaiaigle
       61 glaitdhhsi sgyqvakqwl edwqwsnpgv riphlwsgve inanllgiev hilayafdtt
      121 hpsikpyiqr rvttgeeyqa anvitaiqka gglavlahpa ryrkshleli paaaelging
      181 vetfyaynnp kpwqpsmtes qqiqqlaaey glyntcgtdt hglsllqrl
//
LOCUS       WP_009461299             173 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Alcaligenes].
ACCESSION   WP_009461299
VERSION     WP_009461299.1
KEYWORDS    RefSeq.
SOURCE      Alcaligenes
  ORGANISM  Alcaligenes
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 173)
  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 173)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 173)
  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   4  (residues 1 to 173)
  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   5  (residues 1 to 173)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Alcaligenes"
                     /db_xref="taxon:507"
     Protein         1..173
                     /product="TRAP transporter small permease subunit"
                     /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=19314
     Region          1..159
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mlqpisklid fialasarla emaaailvta mvwevfaryv lhaptvwafd vaymmngaif
       61 llgmawvmrq nehisidvvr khlpkslarm sdvllyllvl fplfailskv giqkawmawk
      121 lnevemvspw apvmwpfyac iaigliaftl qllahglrca vkeqntadve vsp
//
LOCUS       WP_009461727             365 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Alcaligenes].
ACCESSION   WP_009461727
VERSION     WP_009461727.1
KEYWORDS    RefSeq.
SOURCE      Alcaligenes
  ORGANISM  Alcaligenes
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Alcaligenes"
                     /db_xref="taxon:507"
     Protein         1..365
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=40430
     Region          1..355
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msievrhlsk qfgaftalgd vtldfpagel vallgpsgcg kttllrivag lehadagqvl
       61 ingkdvaavg trdrqvgfvf qhyalfrhmt vfenvafglr ikprkqrlpe aqirqrvhel
      121 lelvqldwla drypaalsgg qrqrialara lavepgvlll depfgaldak vrkelrswlr
      181 rlhddlhist lfvthdqeea ievadrivvl nkgrveqega pqdvynhpas pfvyeflgaa
      241 nrlpgqfqhg rfvadpqlgq fesnqalnaq dagqgeavgy vrphdldlqr qldgqgivva
      301 vqriiplgat vrvelalneg eraweaefdh qrwsqlglrp geralalprk fsafpiesqt
      361 earls
//
LOCUS       WP_009462141             205 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Alcaligenes].
ACCESSION   WP_009462141
VERSION     WP_009462141.1
KEYWORDS    RefSeq.
SOURCE      Alcaligenes
  ORGANISM  Alcaligenes
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 205)
  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 205)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 205)
  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   4  (residues 1 to 205)
  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   5  (residues 1 to 205)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Alcaligenes"
                     /db_xref="taxon:507"
     Protein         1..205
                     /product="TRAP transporter small permease subunit"
                     /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=22665
     Region          3..171
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mkfflrlssl idrlntvvgk svtwltlivv lvsainavvr kvygvssnqw lelqwylfga
       61 ifllaagytf fvnehvrvda laerfpprvq iwidiigvif fllpatllif wlsipffeqs
      121 yvlneqssnt gglvrwpvkl lipvgfalla lagvshlikc igfllgacpn pllrngglsa
      181 eeelaqeire maqaneatts vskgq
//
LOCUS       WP_009460768             700 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate--CoA ligase family protein [Alcaligenes].
ACCESSION   WP_009460768
VERSION     WP_009460768.1
KEYWORDS    RefSeq.
SOURCE      Alcaligenes
  ORGANISM  Alcaligenes
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 700)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Alcaligenes"
                     /db_xref="taxon:507"
     Protein         1..700
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=74239
     Region          10..700
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 metvtcastl dalldpasia lvgasedqsk fggrlfrmll khgyggkvlp inpsrsslfg
       61 lpavpglaal dsapdlavft vgadtvleqa qiaaqmgvrg llvisagfad agerglereq
      121 allricrdsg mrligpnclg mispsrslvl csspvldrds lperpigfvs qsgalmttyf
      181 drawamgggf tygfsvgnqa dldlcdfvdf liddpktqvi ctyiegikdt qslrrtarra
      241 qaagkpwlav kagrssagka aafshtasva gdhdvfasvc rdegislmdd mgamlllans
      301 mvrftsnkis kvaivtpsgg ggalaadala ehgvelssfs attkqalaah ypagqadnpv
      361 dlgarltqds tevaratlda lmqdqqsdav litasmcpqe wmaaliekii hpephwakpv
      421 mvafdagvts eplrqklaqh ghayasssle aalalsawkr hgqfvprqqa lrpsacqapt
      481 vmprgvlned qskrllahyg lpvnlgqvce dveqavvqae qigypvvmki vspdivhkte
      541 aggvaldvad daslrrdfar lyanakayka darlegvlvq amakgdvell igarqdaqfg
      601 pvvvfgaggi lvemlsdrvi aaapltlada drllstlmid kllkgyrgrm ldrdgvldai
      661 mrvsflahdl rdtnfeldin plivaatrch avdarlsige
//
LOCUS       WP_009464573             181 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Ahrensia sp. R2A130].
ACCESSION   WP_009464573
VERSION     WP_009464573.1
KEYWORDS    RefSeq.
SOURCE      Ahrensia sp. R2A130
  ORGANISM  Ahrensia sp. R2A130
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Ahrensiaceae; Ahrensia.
REFERENCE   1  (residues 1 to 181)
  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 181)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 181)
  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   4  (residues 1 to 181)
  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   5  (residues 1 to 181)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Ahrensia sp. R2A130"
                     /db_xref="taxon:744979"
     Protein         1..181
                     /product="TRAP transporter small permease subunit"
                     /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=19522
     Region          3..164
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 maeriliglr slnrgvaiit gvmflacaal vlvdivlrrl gnslggtdei sgyvmaigta
       61 wgmayallel shvridflrs ntstkwkavf dlvsmftlas tvsiiavqcw qvvaatlknn
      121 shantpletp lalvqvpwfa gwiwfaimaw ltfiaamalv akgefqkaes ftgvfpeveg
      181 a
//
LOCUS       WP_009463188             812 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Alcaligenes sp. EGD-AK7].
ACCESSION   WP_009463188
VERSION     WP_009463188.1
KEYWORDS    RefSeq.
SOURCE      Alcaligenes sp. EGD-AK7
  ORGANISM  Alcaligenes sp. EGD-AK7
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Alcaligenes.
REFERENCE   1  (residues 1 to 812)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 812)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 812)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..812
                     /organism="Alcaligenes sp. EGD-AK7"
                     /db_xref="taxon:1386079"
     Protein         1..812
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90128
     Region          55..105
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          82..812
                     /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 mnrtaflprl rpvllalmma sastpalaqd npvpihipaq plseallkla eqtqlqvffs
       61 pslvqglstt piqgrmrpee alrsllqgsg leyrrennti tlsrpntdat mldpvrvvgr
      121 rlpvtegsqt yashgattta trlnmtlret pqtvsvmtrq riedqsldni gsvlqqapgi
      181 siqhigsdry tiysrgyaid nyqldglstl sdivsqnipq gladmaiydr vevlrgasgl
      241 lagagepsgv vnmvrkrpta dfqghaevsy gswdqmraqv dlggpineng slrgrlvgah
      301 qegnsymdyf ttkkdvvygi leaditdttl vtlgmdyqkn dprgssgsgf plfydtgeqt
      361 dfdistnaga rwntntlesh ntfvkldqql gadwslamsl nylkarrsgk sadaswgypn
      421 retgdgvqly ggvsnatqyq tsfdihakgp ffqlfgqdhe livgfnssry knrhdtmddd
      481 iegtsinlhd wnnnpalpht tgeklfdydl tvkqyggysa lrlkpsdkla vilggrlsny
      541 ryslsqsypd pgmqrfnslk tmhednvftp yagivydlne ehsiyasyts ifkpqsyrdr
      601 sgnfldprkg dnyeiglkse mldgrvnssi alyeirqdnl avadsgfivp gtereaayta
      661 vkgaktqgld mevtgelldg wnmafsytys qtkdaqgeri ktlvprhmak lwttyrlpgs
      721 wnrltigggv nwqsqihfta tpwdlgktvt geqssyavvn lmgrydfskq ltatlnvnnl
      781 fnreylsald qtfytgyyga prnamlnlry sf
//
LOCUS       WP_009464952             848 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Ahrensia sp. R2A130].
ACCESSION   WP_009464952
VERSION     WP_009464952.1
KEYWORDS    RefSeq.
SOURCE      Ahrensia sp. R2A130
  ORGANISM  Ahrensia sp. R2A130
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Ahrensiaceae; Ahrensia.
REFERENCE   1  (residues 1 to 848)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 848)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 848)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..848
                     /organism="Ahrensia sp. R2A130"
                     /db_xref="taxon:744979"
     Protein         1..848
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=88076
     Region          533..782
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mltlvntpsn ldslddgief tiasktlang ntltvygvvd fsafggeggf ttravqtdan
       61 gqpvagsgfd vfplqsfdda dnfsaegiaq fgdgsvgifg egaldtgtli yrqfsidpst
      121 qaasfvqqvd ftydyaasgg lqadpfnnae vltlrenadg svtalvgyea ltnapanggy
      181 vphvveldfs stgtaqdtan tgteifdetw ngwvalsdgs yvamdqfdpp iagtegyiag
      241 vqvkfisgqa gtqsanvqsn nflfhgplge faylssanlv eigdgriaav wtwvdrfade
      301 tetvrtytai vdpalqgsgt npvvtqpvll qqsvgsdewd pqiaalpdgt yvvvfseaat
      361 dpnlpavrsy vqhldtnavp lgprmdigas lgelgfalsv lpsgqvqist stedgadfdv
      421 qaevynvsaa tpgvinqvaa gnagelfetv vlegdltsvt ptqinlvgsd ptktgivtgt
      481 gfivdstgyi ndivdgtvns lqlfdngvli lewsglqmpi haigsaivqs etgatyidrl
      541 idvfvgdysg atstgpidgg spfynttgst fddtleggdg nnnidggtga damtggagdd
      601 yyvvenvgdt vtelagegsd iidtfvsydv pvnvevlrmq gtadlgtngs vnrdiiqgns
      661 gnnyingagg ldlmvggsgn dtytiddsqd avieaagggd dviytsvdyv llgdqeieta
      721 iltenavilr gdnsdnqlig ndfinvlegk ggtdyllglg gddifqvsle anatdldvfg
      781 dfegagvvgg drialdaaiw gmdgivyqvs qtsfivataq ntmqqqfqia nitapttnli
      841 agddyyfg
//
LOCUS       WP_009464075             145 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Ahrensia sp. R2A130].
ACCESSION   WP_009464075
VERSION     WP_009464075.1
KEYWORDS    RefSeq.
SOURCE      Ahrensia sp. R2A130
  ORGANISM  Ahrensia sp. R2A130
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Ahrensiaceae; Ahrensia.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Ahrensia sp. R2A130"
                     /db_xref="taxon:744979"
     Protein         1..145
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15611
     Region          6..145
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 msaltayggl flsafvaatl fpaqseivli alissgtwsv fwlvvvasvg ntlgsvvnyy
       61 igratgtfsn awwfpvsels lkkaegwyhr ygrwslllsw apfigdpitv vagflkepis
      121 sfvvlvaiak tcryivlali vmgvl
//
LOCUS       WP_009465568             345 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Roseibium sp. TrichSKD4].
ACCESSION   WP_009465568
VERSION     WP_009465568.1
KEYWORDS    RefSeq.
SOURCE      Roseibium sp. TrichSKD4
  ORGANISM  Roseibium sp. TrichSKD4
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 345)
  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 345)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Roseibium sp. TrichSKD4"
                     /db_xref="taxon:744980"
     Protein         1..345
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39406
     Region          36..206
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <161..338
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          250..332
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mrslkfwvrs dfikflktqp ytrtlnweqi eekhsideea vqnpigivpa styfsifeet
       61 atslgsdaly fdlmyeapvg pfstsdylfv capdlrtsmq skvdyapars navdyifeen
      121 dnygifewrf veglgewrqs mfgraaitvr qieivlgdek ppisieiaae ppqarsafls
      181 kyegkiafnt lrnrilvprh mlsrpnarye enlfhiiqks aaqdletfrd fdsdisrvtt
      241 qiveslkagn ctlaevakal gmsqrtlqrv lenegtsfrn lvdkvrksaa rryivnshlp
      301 fkeiayllgf selstfsrav kswygvsprg lrdkrkselg nrlkt
//
LOCUS       WP_009465881             158 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Roseibium sp. TrichSKD4].
ACCESSION   WP_009465881
VERSION     WP_009465881.1
KEYWORDS    RefSeq.
SOURCE      Roseibium sp. TrichSKD4
  ORGANISM  Roseibium sp. TrichSKD4
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Roseibium sp. TrichSKD4"
                     /db_xref="taxon:744980"
     Protein         1..158
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17121
     Region          63..157
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mpslqpskpe qqtaylsarv pvalknrfka laaergakvq dllqklvndy vagegaqtls
       61 atdiiarlrs qkeelqkqgi ahlylfgsva rgsatassdi dlsyvategt qlslfdigrf
      121 kqvleevlec sgkvdlsprs qladhvweta ssdeiqvf
//
LOCUS       WP_009469417             677 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Roseibium sp. TrichSKD4].
ACCESSION   WP_009469417
VERSION     WP_009469417.1
KEYWORDS    RefSeq.
SOURCE      Roseibium sp. TrichSKD4
  ORGANISM  Roseibium sp. TrichSKD4
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 677)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 677)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Roseibium sp. TrichSKD4"
                     /db_xref="taxon:744980"
     Protein         1..677
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70429
     Region          1..670
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mpplnrllrp ksiavigggt wceqvieqnr kfgfsgeiwa vhltrtevag vaafqsinel
       61 pgapdaafvg vnrhatidvv ralsdkgagg aicfasgfre asaeledagd lqsaledaag
      121 smpilgpncy gllnatanva lwpdqhglvp vkrgvaivsq ssniainltm qsrglptaav
      181 vtvgnqaqtg lsdicsalla ddaisaiglf ieglddlkaf eafaerarla gkpvvalkig
      241 rseqaqaati shtaslagss agasalfrrl giaevtnlpt llealklaha vgrlpntqva
      301 slscsggean lmadtatgrk isfpalsdhq kaslrnvlgl kvalanpldy htyiwgdvda
      361 msrtfshmvd ggaelglvvl dfprpdrcsm aewmkvidav eqaksitgkp fgilsslpet
      421 mpetiaqdll ergivplcgf dealsaieal gslapqtaap lhsvppandi rtmneakska
      481 llkdhgvrip vnksasgade aadvakaigf pvvlkgtgia hkteagavil gltdraavqe
      541 aanrmptnqf lveemvtgti aelligvvrd pahgfvltla aggvltellk dsvsllvpss
      601 reavreslls lkvarqltgy rgqpacdlda vldtieavqa cvmahpieei einpllcgpd
      661 faiaadalir cggqddg
//
LOCUS       WP_009473756             313 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Rhodococcus sp. JVH1].
ACCESSION   WP_009473756
VERSION     WP_009473756.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. JVH1
  ORGANISM  Rhodococcus sp. JVH1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Rhodococcus sp. JVH1"
                     /db_xref="taxon:745408"
     Protein         1..313
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34656
     Region          4..303
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mtdlagsyry cgavtaehgr tyhlatrllp errraavhsl ygfartvddi vdvdpgrtag
       61 dcaaeldrid aalrlgftdr tavgpdacsr emrrvlpafl dtvasfdiph dyffaflqsm
      121 rmdvpgtveh rseygtmtel rtymygsavv iglqmlpvlg tigpvadaep haaalgeafq
      181 ltnflrdvge dldrgrvylp adelaafgvd tellahsrrs gttdqrivra lahlisvtrs
      241 vyrdaepgia mldrrvqpgi rtafvlysri ldeierggyr vldrratvsr rnrwatalpq
      301 farlavparg rvr
//
LOCUS       WP_009473975             337 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Rhodococcus].
ACCESSION   WP_009473975
VERSION     WP_009473975.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..337
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=36589
     Region          2..325
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mitvtgarkn ygsfaalddv tidipsgslt allgpsgsgk stllrsiagl esldsgtvvi
       61 ggndvtdisp qkrdigfvfq hyaafkhmtv rdnvafglki rkrpkpeidk kvnelleivg
      121 ldgfqhrypa qlsggqrqrm alaralavdp kvllldepfg aldakvrtdl rtwlrrlhde
      181 vhvttvlvth dqeealdvad riavlnkgri eqigepedly drphndfvms flgsvaklng
      241 qlvrphdirl grdpdlalaq eagtaeslgv tratvervvh lgfevrvdlr neatgepfsa
      301 qvtrgdsaal glqegetvya ratrapelpe aevpvsl
//
LOCUS       WP_009474593             411 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Rhodococcus sp.
            JVH1].
ACCESSION   WP_009474593
VERSION     WP_009474593.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. JVH1
  ORGANISM  Rhodococcus sp. JVH1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 411)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 411)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Rhodococcus sp. JVH1"
                     /db_xref="taxon:745408"
     Protein         1..411
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44070
     Region          7..405
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mvenlsnvdr advykgerla gslareggdv vfrydatylq dpgapqvawt iptsstevra
       61 sggsvppffa gllpegirlr gavaatktse ddhltilmav gadtigdvrv lpagapppet
      121 apvfdpdave rqdlralfeq msgheavkld ptslpgvqak vsaqmystpi atdkgpailk
      181 lsppqgypql venehffmgl aakcglpvad hqlvrdgkgn agllvarfdr rvdpsgrvir
      241 tpqedacqvm gmfpaakyrl ktesvitala gvcergggsa rvatlellrl vaysyaigng
      301 dlhgknfsvq laasglwsvt paydllctqp ylgwrdpmal dfygkankln rrhfvesggr
      361 lgvperavtr mldgvrkgig rgieeietig ftakenaqlr tlmerrsdel g
//
LOCUS       WP_009475282             371 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Rhodococcus].
ACCESSION   WP_009475282
VERSION     WP_009475282.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (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   2  (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   3  (residues 1 to 371)
  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   4  (residues 1 to 371)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..371
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=39453
     Region          1..304
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mitfdkvtka ypdgttavne ldlecpsgki talvgpsgcg kttslrminr lieptsgtis
       61 ldgestadmd pallrrrigy viqhaglfph rtivdnvatm prllgktkke artramelle
      121 tvglaanfad rypwqlsggq qqrvgvaral aadpafmlmd epfsavdpvv rsqlqdeflr
      181 lqkdigktii ivthdideal qlgdqvvvlr tggilaqaat plelltepad efvadfvgrd
      241 rgyrslgfsn lggrvetiae pvarlgdsas daltrttddw llvvdpankp igwvqpakvv
      301 drirpddvnl sgtvadahgt mralldaals apskrgvvvd gdgvlvgtvt ahaavaaies
      361 adlvateama r
//
LOCUS       WP_009475268             273 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: hydroxypyruvate isomerase family protein
            [Rhodococcus].
ACCESSION   WP_009475268
VERSION     WP_009475268.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 273)
  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 273)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..273
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28945
     Region          6..268
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mdtlaytlnc silltdvpll qrpqaardag fdavefwwpf dtavprdsdv dafvaaiena
       61 gvqltglnfa agnmpagdrg llsdpaqvsa frdniditvg igerlgtkaf nalygnridg
      121 tdpkiqdgta tenlaqagka adrigavvlv epvsgtpayp lksaadaiav idrvkaehgv
      181 dslrlladly hlevngddvg aaidtyadri ghvqiadapg rgepgtgtld idgylkrlag
      241 hgyrgyvgle ykstrpdtfd wlpreqrasr agh
//
LOCUS       WP_009476859             336 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Rhodococcus sp. JVH1].
ACCESSION   WP_009476859
VERSION     WP_009476859.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. JVH1
  ORGANISM  Rhodococcus sp. JVH1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 336)
  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   6  (residues 1 to 336)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Rhodococcus sp. JVH1"
                     /db_xref="taxon:745408"
     Protein         1..336
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37047
     Region          21..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          87..332
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkplaryasl ngyvelcrsl glepapllrs agldpsglgl qdrwipaaai awlleasvsa
       61 sgyddfglrl aerrqfsnlg plslvvreep dvrsalrvlt ryehtyneal rtrmserggl
      121 vtlrveldvg etteirqsve lavgvlhrll rgflgggwkp lavcfthpap adtathrrlf
      181 gpvvnfdhef agivieagdl aapnkmsdpl lrpytqqlle swepsddvti vsrvreliel
      241 llptgrcsve qvarslgvdr rtvhrrlaes getfstvlda trvelaermv anprlsltei
      301 admlafsaps nfsrwfggrf gcspsrwrtq rsgdtg
//
LOCUS       WP_009477978             335 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Rhodococcus].
ACCESSION   WP_009477978
VERSION     WP_009477978.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 335)
  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 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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (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   5  (residues 1 to 335)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36187
     Region          93..329
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          249..329
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mvaldpfavg rppaaerrts edwseiqlws drvympyvvr plgvglsprs smystkigdi
       61 tvtrfsygip vsvgdfssda gnalvlttir gnarhhldhd atadtpagdt fvadcsrvdy
      121 lvefspdhvq lnltvphtll adtavrwwgf dpggllwqrk cviggggsgw qallgyamrt
      181 tgelpghate griglnlqel lvghlltewa aragvdpdrs tgpaapgyvr havqyireya
      241 relptasdia davgvsvrtl sgafrkyldt tpaeyvreqr lqgireellt aspgetvasi
      301 agawgyvnlg lfaaayrrrf genpsqtraf gpvsg
//
LOCUS       WP_009475033             397 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Rhodococcus].
ACCESSION   WP_009475033
VERSION     WP_009475033.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 397)
  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 397)
  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
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 397)
  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   5  (residues 1 to 397)
  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   6  (residues 1 to 397)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 397)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 397)
  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 15726307
            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="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40975
     Region          1..>68
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          78..379
                     /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 mrtprsttsp atggdvfali ragqattrte igtltglsrt avaarvsslq asglvveree
       61 gvstggrppv klsfhvqagv vlsaaigrsr tqlaicdlag dvivaedveq eigtspaelm
      121 pviaqrlial reslgetagr tvgigislpg tvdtergcsl nspmmsgwdg vplqpfladv
      181 tdapvfvdnd anvmvlaerr gerrdfadml likastglga glvsggvlqr galgaageig
      241 htktaaaqgv vcrcgdvgci eavaggwalv rnlqeqgrev thirdvitla lagdaearrm
      301 iresgrqige vlsgainlln pevvivggdm aqaydtfvag lretlygnai avatqqlqil
      361 pwthgelsgv vgsatmaldh vlsvravdrl lagaprp
//
LOCUS       WP_009479577             102 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Rhodococcus].
ACCESSION   WP_009479577
VERSION     WP_009479577.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..102
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10758
     Region          3..99
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(27,55..56,58,80)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(27..28,36,38,40..41,43,46..47,55,60,65)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mvatteeqve avralvasip pgrvatygdi asaaglssar tvgwimrtds adlpwhrvlg
       61 asgrpaphla hrqiaklele gvpirdgrvd laaarhrfdr sg
//
LOCUS       WP_009479999             410 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Rhodococcus sp.
            JVH1].
ACCESSION   WP_009479999
VERSION     WP_009479999.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. JVH1
  ORGANISM  Rhodococcus sp. JVH1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 410)
  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 410)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Rhodococcus sp. JVH1"
                     /db_xref="taxon:745408"
     Protein         1..410
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46001
     Region          1..396
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mremtaaaar rsalwaqgfa drkpagaptr rhvrsvldrv rlfqidsvsv avrahyvplf
       61 srlgvydrgl vdsaawshsa raprmlaeyw aheaafipve dwplmrwrmh ryrhgrwsge
      121 srvldrsptl aadvldviga vgacsasdve khlevdrpdr kgpwwdrsdt kvvceqlfas
      181 galavdkrva ftrhydlser vlpkailaee vseedavrgl vqrsaqalgv atepdlrdyy
      241 rlspaqtasa igelvedgvl ervgvrgwda pafvhrdvrv prkvegsall cpfdplvfcr
      301 prterifdfr yrleiytpah krvhgyyvyp fllngelvar vdlkadrasg tlavrsafve
      361 pdrnpgrvve allpelrrma twlglddirv ddrgnlgall aaaaprprge
//
LOCUS       WP_009481998             107 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Mobilicoccus pelagius].
ACCESSION   WP_009481998
VERSION     WP_009481998.1
KEYWORDS    RefSeq.
SOURCE      Mobilicoccus pelagius
  ORGANISM  Mobilicoccus pelagius
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermatophilaceae; Mobilicoccus.
REFERENCE   1  (residues 1 to 107)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Mobilicoccus pelagius"
                     /db_xref="taxon:746032"
     Protein         1..107
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=10525
     Region          9..94
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mpapppagit vdvynatsra glagvtadtl raqrfevgtv tnapagttvt apaeirhgkn
       61 gaagaavlar hirgavlrei pregttvdlf vgpdlgavta psgspsc
//
LOCUS       WP_009482098             259 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Mobilicoccus pelagius].
ACCESSION   WP_009482098
VERSION     WP_009482098.1
KEYWORDS    RefSeq.
SOURCE      Mobilicoccus pelagius
  ORGANISM  Mobilicoccus pelagius
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermatophilaceae; Mobilicoccus.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Mobilicoccus pelagius"
                     /db_xref="taxon:746032"
     Protein         1..259
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=27921
     Region          18..246
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mvtdngeprg agdavvtyfq pfynlrtgrl qglealarre rtdrsdderl hagflaeaqe
       61 rgrlrevdlq vldealgrfa hlhvptdgdg daprlivrvn vsrdtiahpy lvadvtgale
      121 rhgvapdrll vdiptglfrd lhaedaaldr lrrlqdleis fcldgftakd ldllpaaaav
      181 pvdiitlhps vlagedgplt dlaravqdeg lpvvaagvet peqlttvqdl gfewaqgfll
      241 gkpapagatl shpvflpea
//
LOCUS       WP_009482305             281 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Mobilicoccus pelagius].
ACCESSION   WP_009482305
VERSION     WP_009482305.1
KEYWORDS    RefSeq.
SOURCE      Mobilicoccus pelagius
  ORGANISM  Mobilicoccus pelagius
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermatophilaceae; Mobilicoccus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Mobilicoccus pelagius"
                     /db_xref="taxon:746032"
     Protein         1..281
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29708
     Region          1..253
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 miidlhahtl vsdgtdtpaq lveqaeaagl dvvaltdhdt aagwreaida aerlrvgllp
       61 gieiscswdg isvhllayll dpadpdlaae ldaaresrdv rarrivdlls rdvpvtwddv
      121 vaqvgegatm grphiadalv argvvpdrsa afetylhtgs pyyvthyapd pvdavrlvra
      181 aggvpvmahp faakrgrlvp dtvieemtra glfaleadhp dhdeaqraka havaadlglh
      241 vtgssdyhgt gkpqglaact thpdvldall aeptsrgivr p
//
LOCUS       WP_009482373             410 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Mobilicoccus
            pelagius].
ACCESSION   WP_009482373
VERSION     WP_009482373.1
KEYWORDS    RefSeq.
SOURCE      Mobilicoccus pelagius
  ORGANISM  Mobilicoccus pelagius
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermatophilaceae; Mobilicoccus.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 410)
  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 410)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Mobilicoccus pelagius"
                     /db_xref="taxon:746032"
     Protein         1..410
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45322
     Region          9..407
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mstkavlapv etlslrearr aaltaqgfga rfrprgdvra shlrsvadrl gviqidsvnv
       61 vtrsqylpff srlgpydtar ldrlrdrgpr hlveywahea slvpvstwpl lgvrmrraee
      121 swgsmqraad qhpevveavl aevarsgpit araldarlah dvprreghwg wnwsivkaal
      181 ehlfwtgrvt sagrttqfer ryavpeavlp revvdagphg atpvseddal aalveisara
      241 igvgsaqclr dhfrlspaqa apaitrlvee gtllpvrveg wrrpcylhrd avvprrrpdv
      301 aallspfdsl vwqrdrtral fgfdfrleiy vpaaqrvhgy yvlpflldda lvarvdlkad
      361 raagilcaha ihwepgaggg dhrerldgqf sslasflgld svevgrvvsa
//
LOCUS       WP_009482907             310 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Mobilicoccus pelagius].
ACCESSION   WP_009482907
VERSION     WP_009482907.1
KEYWORDS    RefSeq.
SOURCE      Mobilicoccus pelagius
  ORGANISM  Mobilicoccus pelagius
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermatophilaceae; Mobilicoccus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Mobilicoccus pelagius"
                     /db_xref="taxon:746032"
     Protein         1..310
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32671
     Region          1..306
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mlldtaslyf rafygvpdrs gpgetprnav tglvdmmttl vrthrpsglv acwdddwrpa
       61 frveaipsyk ahrvdegsvh egvptgvaee vpetlavqvp vivdllaaig iprigypgye
      121 addvigtltt raseagrpvl vvtgdrdlfq lvdddagvrv lytarggirg gdvvdeaflq
      181 ehygvphgaa yadlallrgd psdglpgvkg igektavrll aeygsvaalq eavaagdppk
      241 gavgrrlvds gdyldrarpv vlvardipve gsidggvper vadpaalahl vethrltgvp
      301 rlldalgirl
//
LOCUS       WP_009483281             423 aa            linear   BCT 20-JAN-2025
DEFINITION  ferrochelatase [Mobilicoccus pelagius].
ACCESSION   WP_009483281
VERSION     WP_009483281.1
KEYWORDS    RefSeq.
SOURCE      Mobilicoccus pelagius
  ORGANISM  Mobilicoccus pelagius
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermatophilaceae; Mobilicoccus.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Ferreira,G.C.
  TITLE     Ferrochelatase
  JOURNAL   Int J Biochem Cell Biol 31 (10), 995-1000 (1999)
   PUBMED   10582332
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Ferreira,G.C., Franco,R., Lloyd,S.G., Moura,I., Moura,J.J. and
            Huynh,B.H.
  TITLE     Structure and function of ferrochelatase
  JOURNAL   J Bioenerg Biomembr 27 (2), 221-229 (1995)
   PUBMED   7592569
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Taketani,S.
  TITLE     Molecular and genetic characterization of ferrochelatase
  JOURNAL   Tohoku J Exp Med 171 (1), 1-20 (1993)
   PUBMED   8122254
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Cole,S.P. and Marks,G.S.
  TITLE     Ferrochelatase and N-alkylated porphyrins
  JOURNAL   Mol Cell Biochem 64 (2), 127-137 (1984)
   PUBMED   6390167
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11477763
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Mobilicoccus pelagius"
                     /db_xref="taxon:746032"
     Protein         1..423
                     /product="ferrochelatase"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0004325 - ferrochelatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=43894
     Region          5..346
                     /region_name="hemH"
                     /note="ferrochelatase; Reviewed; PRK00035"
                     /db_xref="CDD:234585"
ORIGIN      
        1 mnalapydav lllsfggpeg peevlpflrh vtggrgipdg rlaevahhyd irggvsping
       61 enrrlvaale aqlaergesl pilwgnrhaa pftadalrea rergltrlva lvtsaypsys
      121 gcrqyrqdla dsmvelgldl taeggrdggg tlvvdkvrpy adhpgfveav asrtvaavqd
      181 flaahelarp hlafvthsip tamagasgpa gdeyvrrhee iaelvtaavr ealagttaad
      241 aldmslvycs rsgpphqpwl epdicdhlrd ladagvdgvv vspigfvadh mevvhdldte
      301 aaevaadlgi afvrvptvrd dpafvialad lleeraaear gedvspatvs psgalpslcv
      361 pgccpdlrpg gprpalcgvd spgpaddtdp gpggaatssr tpssaagapa tacptplstk
      421 enr
//
LOCUS       WP_009489149             629 aa            linear   BCT 20-JAN-2025
DEFINITION  sensor histidine kinase [Microvirga lotononidis].
ACCESSION   WP_009489149
VERSION     WP_009489149.1
KEYWORDS    RefSeq.
SOURCE      Microvirga lotononidis
  ORGANISM  Microvirga lotononidis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Microvirga.
REFERENCE   1  (residues 1 to 629)
  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 629)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20493667
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Microvirga lotononidis"
                     /db_xref="taxon:864069"
     Protein         1..629
                     /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=67469
     Region          66..258
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          308..628
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 maglenavae dgidkgtlqh aplmfpgrsa agrslwlavl lallgaalgf vvfatgqiag
       61 agaeyalrnr alaalplvad slkadvekqr liplilardg avqemfcsps sakeaalddk
      121 lrgiardata svvyvinteg iavaasnage ptsfvgndyr yrhyfteama ngtatqyalg
      181 ttsarpglyl asrvdgsegp lgvvvvkvel drvesswres gfvvfttder gavlatsvpq
      241 wrfgdlspls eeetettrdh lqlsgatfkp vplsqrggnm vtaspagrsa gfvavsrdlg
      301 kavpgwrlsl lipadaeiss aaitgrvttl lalillgfvv fvivrrrrai rqrqealari
      361 nteleyrvnl rtadlrrtdq alaheiaere naeervrrlr delaqanrls ilgqiaagva
      421 heinqpvaai rtyaesaarl lqngrsqdta gnlssivamt grigsitetl rsfsrratga
      481 iwplpaeeai dgalsllsgr irdsgvmier krtdsspmvm asrirleqil vnllqnalda
      541 ledqpepqve ialtakeemv aisvrdngpg lapdirrnlf mpfttskekg lglglvisee
      601 iarelggslr ldtnhekgas ftvelrraa
//
LOCUS       WP_009489786             386 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Microvirga lotononidis].
ACCESSION   WP_009489786
VERSION     WP_009489786.1
KEYWORDS    RefSeq.
SOURCE      Microvirga lotononidis
  ORGANISM  Microvirga lotononidis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Microvirga.
REFERENCE   1  (residues 1 to 386)
  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 386)
  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
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 386)
  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   5  (residues 1 to 386)
  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   6  (residues 1 to 386)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 386)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Microvirga lotononidis"
                     /db_xref="taxon:864069"
     Protein         1..386
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40417
     Region          13..54
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          77..374
                     /region_name="ASKHA_ATPase_ROK_BsXylR-like"
                     /note="ATPase-like domain of Bacillus subtilis xylose
                     repressor (XylR) and similar proteins; cd24076"
                     /db_xref="CDD:466926"
ORIGIN      
        1 mhpsvvrqih asrifhairl ypfmsqreia erveadkstv saivrefeas glvertrgpg
       61 tgpgrpgeri slsphgglli gvhprpseir fvaagldgnp lgtlsrpmps aaadlsqavs
      121 lgiqdltgei grrpmdirai gvsisglvdt eghlaqspnl gwhdvplrkl lrktvkhply
      181 ignnsnsaai aeqmfghgte tdnflyvesg sgvggglild gslyrgaagf sgeighikvv
      241 pggrpcrcgs sgclsayvad hailrqlqhd gvdihtpaei laraeagdkv tlatleeagn
      301 hlglalanlv nllnpplivl ggglarfaph impslrqtls amsmpaplra csievstvsl
      361 epiprggial alegctslaa sedtpw
//
LOCUS       WP_009489993             339 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Microvirga
            lotononidis].
ACCESSION   WP_009489993
VERSION     WP_009489993.1
KEYWORDS    RefSeq.
SOURCE      Microvirga lotononidis
  ORGANISM  Microvirga lotononidis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Microvirga.
REFERENCE   1  (residues 1 to 339)
  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 339)
  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 339)
  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 339)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Microvirga lotononidis"
                     /db_xref="taxon:864069"
     Protein         1..339
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=37543
     Region          5..337
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 milsrrrllt vgstalagav vgapfiaraq qaeftykyan nlpdthpmna raremaeaik
       61 ketngrvdiq ifpnsqlgsd tdtlsqvrsg gvefftlsgl ilstlvpaas ingvgfafpn
      121 ydavwkamdg dlgayvraqi akanlvamdk iwdngfrqtt sstkpintpe dlksfkirvp
      181 vsplwtsmyk afdsapasin fnevysslqt kvvegqenpl aiiataklye vqkycsltnh
      241 mwdgfwflan rrawerlpqd vrtivakhin aaaekeredv aklnanlqqe laskglifnq
      301 pdptpfrdkl rqagfyaewk gkygdeawai leksvgklv
//
LOCUS       WP_009492400              73 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Campylobacter].
ACCESSION   WP_009492400
VERSION     WP_009492400.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter
  ORGANISM  Campylobacter
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae.
REFERENCE   1  (residues 1 to 73)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 73)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 73)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 73)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..73
                     /organism="Campylobacter"
                     /db_xref="taxon:194"
     Protein         1..73
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=7741
     Region          <18..73
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mveieflgpi kmnnlkleaa nlsevkeklg eyaelsewlk icavavndei assldaplkd
       61 gdkisilppv cgg
//
LOCUS       WP_009491704             659 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Microvirga lotononidis].
ACCESSION   WP_009491704
VERSION     WP_009491704.1
KEYWORDS    RefSeq.
SOURCE      Microvirga lotononidis
  ORGANISM  Microvirga lotononidis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Microvirga.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (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   3  (residues 1 to 659)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Microvirga lotononidis"
                     /db_xref="taxon:864069"
     Protein         1..659
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=70217
     Region          3..658
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mtddllehfi vearelvqqa tddllalerd pasavhldsa fraihtlkgs vglfdfapmg
       61 halhaaedll salkgrqarl dgdaidillq cigqtdrwvg fieesgqlpp eaveegqcla
      121 gglrsqlgqe seapapmvpv adigwvdalq atidakarda sliavryspr vdcffagddp
      181 lallrsvpdl valrvvgrdp wpppaeidpf acnllieais aapfdavkav frfvpdqvai
      241 hdlsahgtre pdragaegpt ghdplasdgs garviridat ridrladlvg emvvaknvla
      301 hlvslgdgld raalvqgiqt shaaidrlvg dmhravmdvr mmpmrkvfrr fpravreiaa
      361 qlgktvdffv dghdveadks vveglseplv hvlrnavahg aepdamrlat gkpakaridl
      421 rarreadwvv vevsddgsgi dpatirrtal grgvvsgdql armsdaevtd lifapgfsta
      481 ekvtdlsgrg vgmdavrtav krlggqisvh svpgrgttir falpltvvmt kamlirvgge
      541 tygipmddil ettfvpasri lpiqeseafv lrdrtlplvr ladlldipsq vvpgtgtkvv
      601 vmrvegekvg lavdgfaerm dvlmrpmtgl lagmpglmgt tllgdggvlm ildvpglig
//
LOCUS       WP_009493252             356 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Microvirga lotononidis].
ACCESSION   WP_009493252
VERSION     WP_009493252.1
KEYWORDS    RefSeq.
SOURCE      Microvirga lotononidis
  ORGANISM  Microvirga lotononidis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Microvirga.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Microvirga lotononidis"
                     /db_xref="taxon:864069"
     Protein         1..356
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36365
     Region          53..304
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 matafrvnmt gsqvvpstns tatgvgtviy dsiavtasyt frvsgldfgs vtgtgpqtad
       61 pnddvtgfhf higpagsnad lvfgqinpdq dpnlkitpns dgswtlsgvw dpadpasfwi
      121 vglasllkfs ppgfdapfyt dattsgfpng airgqwfais ndnsntvrgt adadflpglg
      181 gndsifgrag ndlldggrgn drlfgesgnd tliggpgndr ldggigndsl sggtgrdtln
      241 gglgndilng grgadafvfn salgssnidt irdfnpasdt iqlassvfvg lpkgvltada
      301 fhigtaaaht tdriiydtat galyydadgt gtasaqvqfa tvegnpaltr adflii
//
LOCUS       WP_009493005             505 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Microvirga lotononidis].
ACCESSION   WP_009493005
VERSION     WP_009493005.1
KEYWORDS    RefSeq.
SOURCE      Microvirga lotononidis
  ORGANISM  Microvirga lotononidis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Microvirga.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Microvirga lotononidis"
                     /db_xref="taxon:864069"
     Protein         1..505
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54313
     Region          4..505
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mstprtirls pddnvviaid lvnqgadaag ltarerilkg hkmaaeaire gepirkfgqi
       61 igfakthiap gewvhehnvg lhdferdyaf gveareddli apdlrgtfqg yrrasgktgt
      121 rnyigiltsv ncsasvarfa aaeversgll rdypgidgiv aivhgtgcgh aaygegfdil
      181 rrtqwgyash pnfagvimvg lgcevfqigr mkqeygltes dtfrtltiqe tggtrrtvqa
      241 ivdavkdmlp iaakarretr paselvlalq cggsdgysal tanpalgvas dllvrhggts
      301 ilsetpeiyg aehlltrraa treigeklis rihwwedyta rnggemnnnp spgnkagglt
      361 tilekslgaa akggrstlra vyeyaepvke hgfvymdtpg ydpvaatgqv agganliaft
      421 tgrgsafgck pvpslklatn sdiyrrmldd mdincgdild gisledkgre ifdillrvas
      481 gehtkseelg ygdlefvpwq vgatm
//
LOCUS       WP_009496661             743 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Sporosarcina newyorkensis].
ACCESSION   WP_009496661
VERSION     WP_009496661.1
KEYWORDS    RefSeq.
SOURCE      Sporosarcina newyorkensis
  ORGANISM  Sporosarcina newyorkensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Sporosarcina.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 743)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Sporosarcina newyorkensis"
                     /db_xref="taxon:759851"
     Protein         1..743
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=81092
     Region          41..741
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mekplcydsi qaskkkklir krrgeemmkm mnevlpsnie ldplfnpkrv avlgasentn
       61 kigylqlkal ldagfegeiy pihptskeig elpcyasvgd tpeqvdlail cvgihqvekc
      121 lidcgksgvk avivfasgys eigeegivaq nrlkeiaeqy qmrligpncv gllnttnglm
      181 gtfspgltnv plgrkrevgf vtqsgafgvl tyiaaaqhgl tfnyfvsvgn evdvsfsdvi
      241 eymlhdsktk vasgylegek naaklrklak falqinkpiv imksgrssag sraaashtgs
      301 lagadkvydg ffkqagivra ddyddilsfs klflanklpt gkntvivtss ggrgineadr
      361 cesyglniha lsdkvrkeie knipdfasas npvdltaaas itnpelylap lkvlvndpdt
      421 diilfpefpi hwdentpllq efveicknsd kfvmisnfpl kgmsipkgvq yledngipfi
      481 lgdmnpirsl aklvdyaeay rkahkisdgp arteldvsni rhllpanqtl sesqsseils
      541 aygirtakri taktedaavq aannmgypvv mkidspdiph ktevngirln vqngqevrqa
      601 fkeiygsake hcptadlhgi svqemlpegv evivgvtsdp tfgpvimfgl ggvfvevfkd
      661 vsfrvapitr qdaidkmesl kgyqilqgvr nkkpvdqeai idvllkvsrl iedysdiiqe
      721 idinplivye dgivaadali itk
//
LOCUS       WP_009493524             193 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Campylobacter showae].
ACCESSION   WP_009493524
VERSION     WP_009493524.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter showae
  ORGANISM  Campylobacter showae
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 193)
  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 193)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 193)
  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   4  (residues 1 to 193)
  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   5  (residues 1 to 193)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Campylobacter showae"
                     /db_xref="taxon:204"
     Protein         1..193
                     /product="TRAP transporter small permease subunit"
                     /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=22240
     Region          5..163
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mernlkkver ffdkvgnivg yicifvmflm iadvffnvta ryffkygnvg lqelewhffs
       61 viillgmsya lkddthvrvd ifyekmsvkk ralinmagvi lfilplallv awlswdyvve
      121 ayesgegsad pgglpyrwvi kafipfsfwl liffsvgyfv kwlnvyldar snlseegkfd
      181 anlnqtaqqg egk
//
LOCUS       WP_009499214             189 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Sporosarcina].
ACCESSION   WP_009499214
VERSION     WP_009499214.1
KEYWORDS    RefSeq.
SOURCE      Sporosarcina
  ORGANISM  Sporosarcina
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae.
REFERENCE   1  (residues 1 to 189)
  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 189)
  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   3  (residues 1 to 189)
  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   4  (residues 1 to 189)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 189)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 189)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Sporosarcina"
                     /db_xref="taxon:1569"
     Protein         1..189
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21449
     Region          1..188
                     /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"
ORIGIN      
        1 mrkriviaed esiirmdlkm tlqdhgyevv geagdgdrai elaflhkpdl ilmdikmpkm
       61 nglkasriig eqldlpilii taysqkefve kaqqdnvvgy lvkpisesnl ipavevalhq
      121 sdkakrlken vqqakqevek rkiverakgi lmdaeqlteq qafkqmrdas msrqmtmesl
      181 aqeiidkyk
//
LOCUS       WP_009499583             157 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Haemophilus sp. oral taxon 851].
ACCESSION   WP_009499583
VERSION     WP_009499583.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus sp. oral taxon 851
  ORGANISM  Haemophilus sp. oral taxon 851
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Haemophilus sp. oral taxon 851"
                     /db_xref="taxon:762964"
     Protein         1..157
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17245
     Region          11..151
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdifsffsad fwqthalclm fvsaflsatv lpgnsevvfv alavpklvlg slfstdilal
       61 vlfatlgngl gslttygigr wmpkfdpknh rtlwvtnqik rygaitllls wvpvvgdlfc
      121 aiagwlrlnf vassififlg klvryvallf fsapfll
//
LOCUS       WP_009500132             961 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Haemophilus sp. oral taxon
            851].
ACCESSION   WP_009500132
VERSION     WP_009500132.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus sp. oral taxon 851
  ORGANISM  Haemophilus sp. oral taxon 851
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 961)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..961
                     /organism="Haemophilus sp. oral taxon 851"
                     /db_xref="taxon:762964"
     Protein         1..961
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=110744
     Region          406..>764
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mtpqlaqlia klqeifqinq pdldfgiyri lnsrqtqind flektlpnki naalngnfeq
       61 annvcnhlyt ffsryydqgd fisqrrykgd tyaipyagee vmlhwankdq yytksgesfs
      121 nyaftlengk kvqfrlvead takdnrkdnd qtrvfaliep kiktetdeng eeiqtdirpi
      181 eengdlltir feykavnkke kqsdyitqav ekiqnfaisd efqgifkamp teknknrtll
      241 ekyltdytak ntadyfihkn lgkflnqeld fyiknevmnl dniqdstdfs hieqnlqtik
      301 tiktvakeii aflaqledfq kklwlkkkfv agchylitld hlteaqiqat ldnpkqttqw
      361 qalfnvnisg lnaaelckny phlvvdtslf elkfqadiln nlhdldektn gllihsdnfq
      421 alnllqeryk eqvkciyidp pyntgsdndf iykdnyqhss waammssrfe lardliqdns
      481 giwvstddge yarlqilmad sfgndnfvgd iiwnsrksms sdalisgain httffaknkv
      541 vldknkskfr lpetkdgfen pdndprgawk ldpmdaaeir enlsygitnp ntgetfyppe
      601 grhwrfeest vldylkdgri lfgktgkgkp afkrfyedak ekgkttntlw ddvgtttngt
      661 kllhalfnnt ipkeklnkik pkpiefmqki fqlhneklpv ymdyfagsgt tahavinlnr
      721 edngnrkyil veqgeyfdsv lkprvqkvif akdwkdgkpq adngefggvs qivkvlkles
      781 yedtlnnlel kqpasdlfaq nealqndyll hymldvesrd sllntqhftk pfdyqlniat
      841 tsagayeaki idlvetfnyl iglrvseind krenglvtvq gtntsgektl viwrdcekyd
      901 ydrlndylnr hkinpqesef dvvyingdhn vvtawedsdg glktlkvrsi eseflarmfg
      961 e
//
LOCUS       WP_009500234             400 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Acinetobacter].
ACCESSION   WP_009500234
VERSION     WP_009500234.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..400
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43011
     Region          5..387
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 matsvlvinc gsssikyalv sdrredriyg laenlgaada rikgitvgge plelsipyad
       61 hakaletlla rlanykpqai ghrvvhggsl tkaelltpei ieriraatpl aplhnpahli
      121 gieatmrlfp elpqvavfdt afhqtmpaha yryaipkfly tdhnvrrygf hgtshayvsd
      181 rgselagnfq kggwltahlg ngsstcavwn gqsvdtsmgl tplegvvmgt rsgdvdpslh
      241 sflaknlgwd lakidkvlnn esgllglsql sndmrtviea sengnedacl aievfsyrla
      301 kslaalscgl psidgliftg gigensayir ektlaylphf glqldkdqnn slkrgtegri
      361 dsgtgpqiwv iptdeegria ketrqvvdva qntspeisla
//
LOCUS       WP_009501275             166 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Moraxella macacae].
ACCESSION   WP_009501275
VERSION     WP_009501275.1
KEYWORDS    RefSeq.
SOURCE      Moraxella macacae
  ORGANISM  Moraxella macacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
REFERENCE   1  (residues 1 to 166)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Moraxella macacae"
                     /db_xref="taxon:765840"
     Protein         1..166
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=18333
     Region          7..164
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cl49639"
                     /db_xref="CDD:483979"
     Site            order(121..122,125,138..141,143)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mtiypliqif iakqqlvlhl sdhqfetfsv stgkngtgqq ngsgctplgk hqicakfgen
       61 lppnsvfvar qftgeiynta lacqfvdrdw iltrilwldg cepsinqgen algncdsrsr
      121 yiyihgtpds epmgiprshg cvrmrnadim tvfakvnigt iveiyp
//
LOCUS       WP_009501440             624 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Moraxella macacae].
ACCESSION   WP_009501440
VERSION     WP_009501440.1
KEYWORDS    RefSeq.
SOURCE      Moraxella macacae
  ORGANISM  Moraxella macacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
REFERENCE   1  (residues 1 to 624)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..624
                     /organism="Moraxella macacae"
                     /db_xref="taxon:765840"
     Protein         1..624
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=71340
     Region          74..602
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mtlkmhtpnl vdnnitklak lfpnciteta ktddsgnpvt dkngkilyel gvdfeilkqe
       61 lshtvidgsk eryrldwvgk reaivtansp iaktlrpvrs esvdfdttqn lfiegdnlea
      121 lkilqesylg kikmiyidpp yntgndfiyn ddfaedtqef fersgqidee gnrliantes
      181 ngrfhsdwls mmysrlklar nlladdgvif isiddneqan lknlanelfg senvemfiwn
      241 keaegksgtl kqtkrfrkih eyimvaykni elsnfnkire aligkentlq tanlavntdk
      301 entshenyft itnpsgleft rqwkwdkthi eqlikddliy wgsdgnkqpr liiptddrrt
      361 tflesilnyg gttigrkdfe dlmgeglfty pkplilikki iesvigkdds ildffagsst
      421 tahavmqlna edggkrkfim vqipeatdek seaykagfan iadiskerir rarakikadn
      481 qdkdlshldt gfrvlkidtt nmrdvyyyph eytqemlvdl idnikpdrta edllfqflld
      541 igvslslpiv sieinnhpvy qvgndenliv asmdyidtam vneivklkph kfvtseraiv
      601 ndsdktnike rfkqlssqte vwfi
//
LOCUS       WP_009501630             246 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Moraxella
            macacae].
ACCESSION   WP_009501630
VERSION     WP_009501630.1
KEYWORDS    RefSeq.
SOURCE      Moraxella macacae
  ORGANISM  Moraxella macacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Moraxella macacae"
                     /db_xref="taxon:765840"
     Protein         1..246
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=27568
     Region          1..>237
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msieirdvtk rfgnftalqp lnltvatgkl tallgpsgcg kttllrivag lecadtgrvl
       61 fdgvdvtdtp vqkrhigfmf qhyalfrhmn vfdnvafglr vmpkhkrpnk deidkkvnhl
      121 lelvqlahmi kkyphqlsgg qrqrialars laiepkllll depfgaldak vrkelrawlk
      181 smhqklgvts ilvthdqeea veladeivvm nhgqieqvgd yktlknspks hfvasflqdg
      241 ydkidr
//
LOCUS       WP_009502463             380 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Salipiger aestuarii].
ACCESSION   WP_009502463
VERSION     WP_009502463.1
KEYWORDS    RefSeq.
SOURCE      Salipiger aestuarii
  ORGANISM  Salipiger aestuarii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
REFERENCE   1  (residues 1 to 380)
  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 380)
  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
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 380)
  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   5  (residues 1 to 380)
  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   6  (residues 1 to 380)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 380)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 380)
  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 11973053
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Salipiger aestuarii"
                     /db_xref="taxon:568098"
     Protein         1..380
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38994
     Region          <1..57
                     /region_name="COG3398"
                     /note="Predicted transcriptional regulator, contains two
                     HTH domains [Transcription]"
                     /db_xref="CDD:442625"
     Region          73..359
                     /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 mrngtgeilt rlrdggplsr aelarqtgis sagvtkitaq lhgeglvier egqgrpvgrp
       61 pvalslaags rqvlaihlga graqvalsdl algmgpvral dfdledpvde iiaatsslaa
      121 dvladadpar grvlgvglgv pgsvdatgrv nthsilagwr nvafadafea alglptvleh
      181 nataiamaea rygagrdaas ilhlflgkgv gagfaqtgpe ercapveigh vvvrpggpvc
      241 rcggqgcler yfsedalrti tgaadgpgad ligaamhspa wpeiyelflq avstavallg
      301 pervvlgghl gsapaaflae lrrdlpprvm pqqrerlaie lpslpepvgv ngaacialer
      361 ffytagpvsa plsmrrtvga
//
LOCUS       WP_009502874             391 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Salipiger aestuarii].
ACCESSION   WP_009502874
VERSION     WP_009502874.1
KEYWORDS    RefSeq.
SOURCE      Salipiger aestuarii
  ORGANISM  Salipiger aestuarii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
REFERENCE   1  (residues 1 to 391)
  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 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   3  (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   4  (residues 1 to 391)
  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 391)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Salipiger aestuarii"
                     /db_xref="taxon:568098"
     Protein         1..391
                     /product="CmpA/NrtA family 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=41486
     Region          4..257
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 miaatlslgf lplvdaapli vahemgfaae esialdlrra pswssvrdml sfgrveaahm
       61 lspvpvaval glggagtpls avsvlsmngd gigvsnelaa rmragghdfd yvdarkagea
      121 liahashplr lgvpfpfsmh aellyywlta lgmpapqnvd irtvppalma qameageida
      181 fcvgepwgsm avengvgtll lpgnaiwkss pekvlavrsd waeaepdllg rliravwrag
      241 rwlaepgapt laaellsrke yldlpaeild raltgrmvis argeerqvdr fiefhrggas
      301 fpwrsqaewi giqlaartgl drasaaraar avfrsdlyra alqgtradlp gasskiegal
      361 seatavasvs grlflgpdsf fdgrifeptg s
//
LOCUS       WP_009503247             265 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Salipiger aestuarii].
ACCESSION   WP_009503247
VERSION     WP_009503247.1
KEYWORDS    RefSeq.
SOURCE      Salipiger aestuarii
  ORGANISM  Salipiger aestuarii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
REFERENCE   1  (residues 1 to 265)
  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 265)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 265)
  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   4  (residues 1 to 265)
  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   5  (residues 1 to 265)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Salipiger aestuarii"
                     /db_xref="taxon:568098"
     Protein         1..265
                     /product="TRAP transporter small permease subunit"
                     /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=29552
     Region          26..181
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mseqtkaaaa isdpgengra ehnrgdrltv qlgnvaawlf pvlmvaicaq vvlrqaghnq
       61 awlddlqwwl ygaavlvgig yavvtdshvr vdilydnfdr akrvridifg lvwlflpfii
      121 lcwdvtldya ltsiragegs dspnglhnlw ilksfmnlaf vfiaiavwst yvrllgdltr
      181 pvlwkqlfwa fpsvayavnl alyyalfgff yltrgentss rdvgrlpvfg elefgahdmr
      241 ytvlgalilt vlliavlrav aprea
//
LOCUS       WP_009503314             192 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Salipiger aestuarii].
ACCESSION   WP_009503314
VERSION     WP_009503314.1
KEYWORDS    RefSeq.
SOURCE      Salipiger aestuarii
  ORGANISM  Salipiger aestuarii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Salipiger aestuarii"
                     /db_xref="taxon:568098"
     Protein         1..192
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21087
     Region          1..163
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlrrlydwtm sladhpralw alaavafiea svfpippdvl mipmvlaapr rawlialvat
       61 vasvigglag ygighfffeg vgrpileslg kadsmdafnt rfndvgfwav lvagitpfpf
      121 kvitimsgwt amplgtffvt aiiaralrff ivagllwvfg apirdfierr lglvfslfml
      181 llvggfyivr yl
//
LOCUS       WP_009503487             408 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Salipiger aestuarii].
ACCESSION   WP_009503487
VERSION     WP_009503487.1
KEYWORDS    RefSeq.
SOURCE      Salipiger aestuarii
  ORGANISM  Salipiger aestuarii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Salipiger aestuarii"
                     /db_xref="taxon:568098"
     Protein         1..408
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43170
     Region          8..392
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mtntpvaltl nagssslkfg lfsigatpva mavglvdsig rtptlkasfg agmpplgrdl
       61 tpaeasdhks alatalallr qhfpdaqvav vghrvvhggp sydgpmrltp qvmaelrrls
      121 pfapihqphn lagidaavaa fpdaiqvacf dtafhrshpw vndtfalprd yydkgvrryg
      181 fhglsydyis gelnriapli hagrvivahl gngasmcaml ggrsvastmg ftaldglpmg
      241 trtgqidpgv ifylvqqegm tidevrdlfy trsgllglsg lsndmralea agstqaneai
      301 dyfvfrirre lgglaaalgg ldalvfcggi gensrlirer vcegmgwigl dldrarnaag
      361 dtvistdmsr arvmviptne elviaraakr vvdadsacaa grpnvrnt
//
LOCUS       WP_009503982             341 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Salipiger aestuarii].
ACCESSION   WP_009503982
VERSION     WP_009503982.1
KEYWORDS    RefSeq.
SOURCE      Salipiger aestuarii
  ORGANISM  Salipiger aestuarii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
REFERENCE   1  (residues 1 to 341)
  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 341)
  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 341)
  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 341)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Salipiger aestuarii"
                     /db_xref="taxon:568098"
     Protein         1..341
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=36856
     Region          12..341
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mfkrfskkta hllaagclma gmattaqaae lrfvhaypta sqhhknvlwf teqvsektdg
       61 evtfrifpsa qimpinqelp ailsgqvsmt ysiapvvasv eplwgifdlp flfdikvddt
      121 slgrkffese kgggilakam ekrgfklisi aptdypssfy ltdsnaietm ddlkglkiri
      181 aggrigqlag eaygyspiai agaelvpals qgvvdggilp plyaydnklp vkgltiapfa
      241 wvgltpiims laefealted qqqvmldtgk elgaralaiv eertakglka ledegatvvi
      301 lsdedtpawq akakpvwdaf veengedari mleeaialrs e
//
LOCUS       WP_009504571             173 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit [Salipiger].
ACCESSION   WP_009504571
VERSION     WP_009504571.1
KEYWORDS    RefSeq.
SOURCE      Salipiger
  ORGANISM  Salipiger
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 173)
  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 173)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 173)
  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   4  (residues 1 to 173)
  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   5  (residues 1 to 173)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Salipiger"
                     /db_xref="taxon:263377"
     Protein         1..173
                     /product="TRAP transporter small permease subunit"
                     /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=18982
     Region          1..144
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mesvivrlgw vsriityaat alatlmmvhv tldvilsqfi aeplpgtvdy vsyyymvglv
       61 flplpfveyg nehikvdlih dllptgartv ldmlalalsa vfyglltwqt sidavekyli
      121 geqsmgmaav tvwpgrfflp igaglmvlll lakliqrpft dagmagpnhd mye
//
LOCUS       WP_009504578             655 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter permease [Salipiger].
ACCESSION   WP_009504578
VERSION     WP_009504578.1
KEYWORDS    RefSeq.
SOURCE      Salipiger
  ORGANISM  Salipiger
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 655)
  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 655)
  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 655)
  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 655)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Salipiger"
                     /db_xref="taxon:263377"
     Protein         1..655
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=69446
     Region          1..621
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 msqeiqddaa qpvgmgtlpp ylrwllaasa illstasinh lfnlgffmnv rlleihylyv
       61 mllltlplvy lifpcsrtnp ygstrwwdyf lallalstca ffayygrsvv nkgwdfsapt
      121 haviasfafw flllvaarrt ggwmlfgvil vfsvypmvan yapgpiqgfq rppvetaifh
      181 amsgesvlgi pmrsfvnlvv gfmifgvamq htgagpffid iafaalghvr ggpakvgvlt
      241 saltgsmsgs vitnvlttgs itipamkkvg frpsyaagie aaastgavlm ppimgatafv
      301 masflltdya nivvaavlps llyffglfaq idaysarhgl kgvpradlpr fgkvlregwy
      361 flavfglliw mllylkreai apfyatalli glnqlmsksr wgrqelmnfl iatgrlfvel
      421 vailaavgli vgglavtgms gtisndllfi aggntfllll lgaltsfilg mgmtvtaayv
      481 ilavslapal iaggldpigv hlfilywsml syitppvala afaaaaiaqa rpfaaafeam
      541 klgtiiyivp fffvldpayt lqaglfdsaf tvlragvgvl licaglqgyl lgvgriepgp
      601 tgaiarlllg faglafalps tailaipiaa avgvgvavta laavivtfsr nrkaa
//
LOCUS       WP_009505453             281 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Salipiger aestuarii].
ACCESSION   WP_009505453
VERSION     WP_009505453.1
KEYWORDS    RefSeq.
SOURCE      Salipiger aestuarii
  ORGANISM  Salipiger aestuarii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Salipiger aestuarii"
                     /db_xref="taxon:568098"
     Protein         1..281
                     /product="formate/nitrite transporter family protein"
                     /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=29844
     Region          2..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msyvmpkefa skmvdagesk ifmatkdtli rsymagaila laaafavtia vqtgdflvas
       61 llfpvgfcll ylmgfdlltg vftlaplavi akrpgctwkg vlrnwglvfc gnfagamtta
      121 vlmavvfttg fsaepnavgq kigsigeart lgyaaaggag lltvfvravl cnwmvstgvv
      181 aammststsg kimamwmpii vffylgfehs ivnmflfpsg imlggeftwa dyfiyneipv
      241 vlgnlvgglt fvggmiyath frespkrnaa rnddvvsvpa e
//
LOCUS       WP_009505934             278 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Salipiger aestuarii].
ACCESSION   WP_009505934
VERSION     WP_009505934.1
KEYWORDS    RefSeq.
SOURCE      Salipiger aestuarii
  ORGANISM  Salipiger aestuarii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 278)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Salipiger aestuarii"
                     /db_xref="taxon:568098"
     Protein         1..278
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=30647
     Region          33..262
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mamqgrntqg ipqgqspldl avaerdrtil dtvrnairhk qvmlsfqpvv qarkpdslaf
       61 heglvrvlde tgrivpardf isavegteyg rmldcialee glselanvps lrlavnmsar
      121 sigyprwmdi lhkgiaenpt vgerlileit essamlvpel vtsfmadlqp dgitfamddf
      181 gagytalrhf kdfsfdilki dgefirgiar dpdnqvltra mvsiaeqfdl ftvaesvera
      241 ddaaflteig vdclqgyyfg aptvspdwri iepdralg
//
LOCUS       WP_009506185             309 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Salipiger aestuarii].
ACCESSION   WP_009506185
VERSION     WP_009506185.1
KEYWORDS    RefSeq.
SOURCE      Salipiger aestuarii
  ORGANISM  Salipiger aestuarii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
REFERENCE   1  (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   2  (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   3  (residues 1 to 309)
  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   4  (residues 1 to 309)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Salipiger aestuarii"
                     /db_xref="taxon:568098"
     Protein         1..309
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=32872
     Region          1..306
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mieidgitkr ygdttavdav smtaqtgtit aivgtsgsgk ttllrminrl vepskgevri
       61 ngtptsaikp hllrrrigya iqghglfphh svarnigavp qllgwspdki rarvdelldl
      121 fsmapdefrd rypsdlsggq qqrvgvaral asrpdlllmd epfgaldpii raraqddlrr
      181 iqralgstim lvthdmeeai rladriavmd agklvqhgpp adiiatpatp fvaemvgead
      241 rplrllslip vteiaedgaa dgpplpadat lrdalsaclw tgrsalpvvg aspahvtlda
      301 irarvgghg
//
LOCUS       WP_009506630             276 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter sp. WC-323].
ACCESSION   WP_009506630
VERSION     WP_009506630.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. WC-323
  ORGANISM  Acinetobacter sp. WC-323
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 276)
  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 276)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 276)
  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   4  (residues 1 to 276)
  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 276)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Acinetobacter sp. WC-323"
                     /db_xref="taxon:903918"
     Protein         1..276
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31622
     Region          51..273
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <175..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 msrrpreqvd ylhleelggl emlkasyyqq efsrhvhegf cigvieegaq rfyrtggnhv
       61 apqgdiilvn adevhtgssa vdtgwryrai yptpevfnel trdlttvhgt apwfreavlh
      121 deglaqqfrl lfdlleqpnn sllkqtlfls tiawlvskys qvkphvndls nakqrilnik
      181 elmatmpeqe fslaelaema nlsqwhflrq fkkhvglsph awlvqarlqk sqrllrqgln
      241 lsevsqqcgf sdqshfsrhf rqtfgitpgg yiaylk
//
LOCUS       WP_009509504             344 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter sp. WC-323].
ACCESSION   WP_009509504
VERSION     WP_009509504.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. WC-323
  ORGANISM  Acinetobacter sp. WC-323
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 344)
  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 344)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 344)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 344)
  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   5  (residues 1 to 344)
  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   6  (residues 1 to 344)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Acinetobacter sp. WC-323"
                     /db_xref="taxon:903918"
     Protein         1..344
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39471
     Region          44..210
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <140..340
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mqkqqipvip aryylrliei ligthqydnh vlsalqqqla qtellsiqqi eqfiemglsl
       61 pnthdlafvl gknlklsshs lvgyalmtsp nlehalrlia qyfrlimpsf klsiqfpags
      121 qkvellfepi lqmnkqclaf hieaiavafy ysllelagqq lqryqiylsi peptyqeryl
      181 slvkasfqfn yswlsgirve idqqqlalpl pladahslkv veqrcqeqiq kiyhqgeive
      241 wvsmmlrqan qvptltecar vlnistktlq rylqqqgvef qelkqqiste raidllenss
      301 ltitaiayel gysnpanftr afnkvigcsp qayrlkhqdq irsl
//
LOCUS       WP_009509780             141 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Acinetobacter].
ACCESSION   WP_009509780
VERSION     WP_009509780.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..141
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15975
     Region          1..136
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 msyfllflsa fgaatllplq seavlmtllv qglsnpfyli lvatignvlg scvnwwlglk
       61 iehfkdkkwf pvseqrlqqa qqiyhkygfy slllswtpvi gdpitliagl mkenfwrffv
      121 ivtiakggry ltlyalyvgi f
//
LOCUS       WP_009509856             264 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Acinetobacter sp.
            WC-323].
ACCESSION   WP_009509856
VERSION     WP_009509856.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. WC-323
  ORGANISM  Acinetobacter sp. WC-323
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acinetobacter sp. WC-323"
                     /db_xref="taxon:903918"
     Protein         1..264
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29640
     Region          1..257
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mshlavnlsm iftevplier falahahgfq qveiqfpyel dvvdlrtqle qhnlslclin
       61 vpagdlmqgg nglagipgke iefhqalela iryatalnvp rvnilagkqp ldadllpcln
      121 tlasnlklac hmlseqgiep vfemindtdm prfliqniaq gqemleavnh palkmqydcy
      181 hmammgedvl aglqenlhqi ghiqfadcpg rhepdtgnip ykqifdwllq sdyrglitae
      241 yrpknqsdqs fawkkkyfsn dvnt
//
LOCUS       WP_009510766             453 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Acinetobacter sp. WC-323].
ACCESSION   WP_009510766
VERSION     WP_009510766.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. WC-323
  ORGANISM  Acinetobacter sp. WC-323
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Acinetobacter sp. WC-323"
                     /db_xref="taxon:903918"
     Protein         1..453
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=50893
     Region          10..439
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mdylhsvpte qgvlvsllsl tdgvdqfver ltrdhfsgkh qiifdaiqai hsrgeqidfi
       61 lvwdeinknp lnlnyideqy mlklnadapt listleqhie kldrlmmrrk flnisnlmqg
      121 makdfttnvd eminktqnmi adigdnkqsk elafvnefva rlyvdleetr iarengtfvd
      181 mgiktgfial dnkigslrrg nfviigarps mgkttfaqni msdmainqdm vvqfhscemt
      241 eeeirdrivs gvgqirlsni kgkcledddw grlvqankml ehskfaiddt anatlsdvrr
      301 karllkakfg rvdaifvdyl qimkspivtd nqvraigeis kglkaiakef dcvvfalsql
      361 srnlenrpnk rpvnadlres gqleqdadvi lfiyrdeiyn kgskdagtae iiigkcrdge
      421 vgtvrlgtdl aratfadldp fylaslqevg gaa
//
LOCUS       WP_009513936             144 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acinetobacter sp. WC-323].
ACCESSION   WP_009513936
VERSION     WP_009513936.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. WC-323
  ORGANISM  Acinetobacter sp. WC-323
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Acinetobacter sp. WC-323"
                     /db_xref="taxon:903918"
     Protein         1..144
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15921
     Region          1..126
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mknesgftli elmiviaiig ilaaiaypsy iqykvrtnra evqtemmria qqlqsyhvvn
       61 hnytnakldn dttpliqdfp athaiytlsl nigtaqnwil tatpisttiq kdngavvlns
      121 qgqkcwtktt tactpstttn wdsr
//
LOCUS       WP_009515044             446 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [Hydrogenophaga].
ACCESSION   WP_009515044
VERSION     WP_009515044.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenophaga
  ORGANISM  Hydrogenophaga
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Hydrogenophaga"
                     /db_xref="taxon:47420"
     Protein         1..446
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=49939
     Region          20..441
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mattkpkskp trkspyspvr avevrawgkl vgavaleptk nyyafsydps wvkrgielap
       61 lrmpleqase pflftdlpea tykrlpamla dalpddfgna lidawmaerg lskgmvsald
      121 rlaymgkrgm galtfgplrg ppaskptvie mgklvesark avqgdfdgdd haitalkqii
      181 qvgtsaggar akatiawnpi tdevrtgqfd ipdgfeawll kfdgmgvdne lgpsksygri
      241 eyayylmada anidmspcrl lrengrahfm tkrfdregne rlhmqtlcam ahldyklvgt
      301 hsynqllqta qalkldrkam vqllrrmifn vlavnnddht knfsfllrqg eqwelapayd
      361 ithayrvdsd wvsqhqmsin gkfdritlad vrvvadrfgl ladlaaaved vrravsrwve
      421 fadeaqvdpi erdeierqmg erdrvf
//
LOCUS       WP_009515068             732 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Acinetobacter sp. WC-323].
ACCESSION   WP_009515068
VERSION     WP_009515068.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. WC-323
  ORGANISM  Acinetobacter sp. WC-323
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 732)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="Acinetobacter sp. WC-323"
                     /db_xref="taxon:903918"
     Protein         1..732
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=81360
     Region          20..729
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 msllrlnrlh ygilmsmgci ssplvwaeal aqevtvlptl rveatrtdtt ymqtpasifr
       61 vdipkndqsa qvnltevvkg ipsvqlrnre nyaqdlqlsm rgfgarstfg vrgirlytdg
      121 ipatmpdgqg qtsnidlssl shlevltgpf sslygnssgg ailattqegq gkdsiemsya
      181 ggshnknrag lvlqggaknq nepsyivsss yfdtdgfrdh sgaekvlnna kltwnldegs
      241 kinwvtnyvk ihaddpqgls reqwqknprq vndakntynv rkdieqtqtg vtwskpindq
      301 helyamayfg nrqvtqyqsi pkgkvtleng kpiysgqasp khaggvidfk rnyygadlrw
      361 tgkellpnmm fsagialdmm dedrkgfenf ntkdvygvkg nlrrdedntl wnidpylqas
      421 wqflpkwrld tgvrysnvhy kskdyfttep dqygtvngdd sgktnydkvl psaalswqil
      481 pellayasya kgfetptfte mayqadkdks gfnfalkpst sdnyevglks qnylgdftfa
      541 lfqsktkddi vsagtsngrs tfrnadktlr egveftwnkk lwrdlaatas yayldatfda
      601 dvpvnldkeg nvlaaaipsg naipgiaknq afiniawqpe qgfyagldaq fmdkvyvndi
      661 nsdaaasytv asiytgyawk yadwgingfa rvdnlfdkny agsvivndan krffepadgr
      721 nwsagikvsk qf
//
LOCUS       WP_009515094             473 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Hydrogenophaga].
ACCESSION   WP_009515094
VERSION     WP_009515094.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenophaga
  ORGANISM  Hydrogenophaga
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 473)
  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 473)
  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 473)
  AUTHORS   ter Beek,J., 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 473)
  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 473)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Hydrogenophaga"
                     /db_xref="taxon:47420"
     Protein         1..473
                     /product="CmpA/NrtA family 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=52434
     Region          112..351
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 msdffdpyna dkplmlkcsc grdhtvaehq aeqaakdsaa eqavatlrar setpefeays
       61 refieatlvk alfpqdavrr rflravgkgt amaaiasvlp iaslqamaqe kgklektnlk
      121 igfipitcat plimahplgf yskqglnvev tktagwalvr dkminkeyda shflspmpla
      181 islglgsnav pmnvatvqni ngqaitmalk hkdnrdpknw kgfkfgipfe ysmhnfllry
      241 ylaenglnpd tdvqlrvipp aemvanlrag nidgflgpdp fnqravfeev gfihvltkdl
      301 wnghpccafg tstefikqnp ntfaalyrav lnaaamarqp knreliakvi apsqylnqpe
      361 avvtqvltgr fadglgkvqn vperadfdpm pwqsmavwml tqmqrwgyik gevnynqiae
      421 rvflitdark hmkelgqdfk agpgyekhti mgkvfdpakp aeylksfsis kaa
//
LOCUS       WP_009515545              83 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Acinetobacter].
ACCESSION   WP_009515545
VERSION     WP_009515545.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..83
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8922
     Region          6..83
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mqtieikiea fgaierllpk alafefaenq svkdvltriv klypeadqam ekcacaiged
       61 ivtrqtaldr sctlvllspv agg
//
LOCUS       WP_009515679             420 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [Hydrogenophaga].
ACCESSION   WP_009515679
VERSION     WP_009515679.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenophaga
  ORGANISM  Hydrogenophaga
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 420)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 420)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Hydrogenophaga"
                     /db_xref="taxon:47420"
     Protein         1..420
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47143
     Region          32..407
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mtsereayiy iqmpgtletv paallrvqtl sdgtqigrfr ygdrylqrpe avaldpfhlp
       61 larevfeftq lkgipgavrd agpdawgrrv iehklersaa dlqeidyllh gpqdgagyls
      121 fgltaeppap krrynrthql deliaatqai eagrpvaahl leqidpgtsm ggarpkatie
      181 dahslwlgkf parddrfnlq rvefatldla rrcglnvaqa rlqsvgecdv lmlqrfdrdy
      241 tdqgylrfgl vsgltvldcg dshldrerws yllmadnlrr wsdkpqadca elfkrmvfna
      301 avtnnddhpr nhallrrqkg wrlapaydlv papvvslerr dlaltvgdyg rtasiynlls
      361 qagrfglsaq eargeidrlv dvvrhwresf facgvpakdi eyiapailpd cfffesnpha
//
LOCUS       WP_009517081             207 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Hydrogenophaga].
ACCESSION   WP_009517081
VERSION     WP_009517081.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenophaga
  ORGANISM  Hydrogenophaga
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 207)
  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 207)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 207)
  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   4  (residues 1 to 207)
  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   5  (residues 1 to 207)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Hydrogenophaga"
                     /db_xref="taxon:47420"
     Protein         1..207
                     /product="TRAP transporter small permease subunit"
                     /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=23073
     Region          1..167
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mqkllltvda istwfgkaca wsvvaltlli swevfsryvl ndphawvlda qimlygvlfm
       61 tagaytlakn ghvrgdvlyg ffrprtqati dltlyvlffl pgivaltwag wtfaneslai
      121 reqtfnadpl pvypfkffvp iagaflllqg iaeiircvic irtgawpske edveevdvdk
      181 lkemvhvkda diealdkslt pqqkggq
//
LOCUS       WP_009517623             219 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Hydrogenophaga].
ACCESSION   WP_009517623
VERSION     WP_009517623.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenophaga
  ORGANISM  Hydrogenophaga
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 219)
  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 219)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 219)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Hydrogenophaga"
                     /db_xref="taxon:47420"
     Protein         1..219
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23672
     Region          4..209
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Region          92..120
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(93,96..97,100..101,103,130,133..134,137..138,
                     140..141,163,166..167,170..171,174)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          125..157
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          162..190
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 makhldleeq eqldqlkhfw akygnliswa livvfgsfaa yngwnwwqrn qsakaavlye
       61 evdravqskd ldrvgrvlsd mradfggttf aaqasllagk aqfeggqldq aretlqavln
      121 dskdeglqav arlrlasvel qagkpdaalq vlqakapaaf eplladrrgd vllaqgkade
      181 akaqyeaawk aldagnelrr lvavklaslg vavdagakp
//
LOCUS       WP_009517219             359 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [Hydrogenophaga].
ACCESSION   WP_009517219
VERSION     WP_009517219.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenophaga
  ORGANISM  Hydrogenophaga
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 359)
  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 359)
  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 359)
  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 359)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Hydrogenophaga"
                     /db_xref="taxon:47420"
     Protein         1..359
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39516
     Region          1..353
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mdrrslirha giagvlaagv apsvhaqaai rwrltssfpk aldtiygasd vfassvkams
       61 ggkfevsvha pgelvpalgi vdavqagtve mghtapyyff gkdptfamat aipfglnsrq
      121 ltawmydgng mklfrefydq ykivnfpggn tgaqmggwyr keiktaadmk glkmriggfa
      181 gqvltrmggv pqnipggeiy qalekgtida tewvgpydde klgfqkvakn yyypgwwegg
      241 aqlefyvnkd aynalsaehk amvenaasha htvmqaryda rnpaalkrlv aggakvlafp
      301 kaimdlayke smalyselsa snphwkkiya dysnfrrdqn lwfrfteaqf drymqsakl
//
LOCUS       WP_009518062             711 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Hydrogenophaga intermedia].
ACCESSION   WP_009518062
VERSION     WP_009518062.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenophaga intermedia
  ORGANISM  Hydrogenophaga intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Hydrogenophaga.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Hydrogenophaga intermedia"
                     /db_xref="taxon:65786"
     Protein         1..711
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=76268
     Region          1..708
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mrfaahlpli galaatavha qnrppeggal apvvirgsad aaqrwlgsas vdvvdgselr
       61 egqlqinlse glgrvpglvi rqrenyaqdl qvsirgygsr atfgvrgvrl fvdgipasap
      121 dgsgqaanfp lgsadrievv rgpfaalyga ssggaillyt edgarpgewr tglavgpdgl
      181 wrlstqvlgq tgtaeapgws yaldvgrfet dgqrpqsaah rstanarlsr ahdggrttlv
      241 fnrqsafsld plgltraqfd adptqtdaaa infntrksvs qtqagiaweq aiggghnvel
      301 mgyagqrrvv qfqsiptgaq aapgssggvi dldrdywgfn arwrlqrewq ggeldlsagl
      361 amdrqndarr gynnfvgtal gvqgplrrde tnradtldpy lraawtredw tleggvrrvr
      421 trfessdrfl angddsgsar ysgtlpvvga rwriapnlqa fgsvgrglet ptlneaayrs
      481 gggaglntel naarstsaei glrgrhgagl wnatlfdirt rdeivvqnnt ggrstfqnag
      541 rterqglela gewafgefal tsaytamsar yrdgfltcta tlcpnvnapt pipagqrmpg
      601 lpaqqffaql awtprwaatv ggvftlearr sgrvqvndln tdaaeaytlf algarfeqst
      661 gpwtwrqfvr ldnltdrrha gsvivnegng rffepgagrs lsagieltrr f
//
LOCUS       WP_009519804             199 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Hydrogenophaga].
ACCESSION   WP_009519804
VERSION     WP_009519804.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenophaga
  ORGANISM  Hydrogenophaga
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Hydrogenophaga"
                     /db_xref="taxon:47420"
     Protein         1..199
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=21810
     Region          15..198
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mdttadklle lvraqgllrp hdlaplgipr valtravrrg qlervgrgly glaarpvsah
       61 gtlaevarrv pkgvvcllsa lrfhdlttqa pfevwlaidn kaatpkldyp plrlvrfsga
      121 altegveehv vdgvtvrvtg vaktvadcfk yrnkigldva lealrdawng krmtsdeiwh
      181 yakidrvanv mrpylesla
//
LOCUS       WP_009524308             405 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Peptoanaerobacter stomatis].
ACCESSION   WP_009524308
VERSION     WP_009524308.1
KEYWORDS    RefSeq.
SOURCE      Peptoanaerobacter stomatis
  ORGANISM  Peptoanaerobacter stomatis
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Filifactoraceae; Peptoanaerobacter.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Peptoanaerobacter stomatis"
                     /db_xref="taxon:796937"
     Protein         1..405
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46122
     Region          1..290
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          301..381
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrilhssdwh lgktldgysr ieeqekflef fveksreiqp diiiiagdif dtsnpsaiae
       61 kmfydvltni ssntsslivi ipgnhdspkr lasakllart hgiiiyennd dkidigmyks
      121 sevlscndgv ikvkvngkia nimalpyise arlnenvqdl fdseeenars fqtkfealvg
      181 kkekffntde yniiiahlft trarlsedei gysiggayav dasafpksad yialghihkk
      241 qcisgvdkra yycgspihyn ktevktakkv ilqvdiqedk sidlteinvp iykkieiwna
      301 esiedaikms eeksdessfv yiniktdrii sneeirqiks nkkdiieirp imsieniist
      361 senmleksem ekftefykek ngaeptknii drymdiisye deeni
//
LOCUS       WP_009525442             166 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Peptoanaerobacter stomatis].
ACCESSION   WP_009525442
VERSION     WP_009525442.1
KEYWORDS    RefSeq.
SOURCE      Peptoanaerobacter stomatis
  ORGANISM  Peptoanaerobacter stomatis
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Filifactoraceae; Peptoanaerobacter.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 166)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Peptoanaerobacter stomatis"
                     /db_xref="taxon:796937"
     Protein         1..166
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18943
     Region          1..150
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mqdylllels iksiansddr fisklsnlsa viyqymdrln wagfyildet wnnlylgpfq
       61 gkmacsniki segvcgkavr dnavqrvsdv hsfeghiacd sdskseivlp lkkdckiwgv
      121 ldidspkknr fsqedeeflt rmaqiigenv feekkvyegl ftnqwi
//
LOCUS       WP_009527070             694 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Peptoanaerobacter stomatis].
ACCESSION   WP_009527070
VERSION     WP_009527070.1
KEYWORDS    RefSeq.
SOURCE      Peptoanaerobacter stomatis
  ORGANISM  Peptoanaerobacter stomatis
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Filifactoraceae; Peptoanaerobacter.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 694)
  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   3  (residues 1 to 694)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Peptoanaerobacter stomatis"
                     /db_xref="taxon:796937"
     Protein         1..694
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=77351
     Region          2..694
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          183..260
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 mmdfdqyidi fldeskdhlq nlneallrle edpenldtvn eifrmahtlk gmsatmgfei
       61 iaklthkmen ildgirshkf tlnrdmidil fegldilegq vktiesdgke qqidisdiin
      121 rldvlekggs lgggaasepn kntvketeds tqssdlsfei skedkealya sakemlkdgy
      181 nlykievdle ensmlksara fivfknleda geviyshpss ddiekdsfeg hftilllthe
      241 tideikssie gvsevekvlv dnfdiellns ekeeekqeqp ketvqapqaq qpkkeepkkp
      301 aqaakapadk kaksgktirv didrldnlmn lvseliivkt rledneifsk rqnmteaiey
      361 lerittslhd avtkvrmvpi ervfnrfprm vrdlskdlnk einlimagee tevdrtvide
      421 igdplvhllr nsadhgiesp edriakgkpe vgtvrlvayq dgntvvievt ddgagintek
      481 vkqkaiergi ltqaqadele inkaaelifa agfstadkis dvsgrgvgld vvktkiesls
      541 gtvevrtekd kgsafiirlp ltlaiiqall vivgnekyai plnnikeitn idtidirnie
      601 dkeiilyrgv plelkrmsev ldcenqerke gnvtvvivrk gekdigliid sligqqeivi
      661 kslgpylsfv kliagatilg nggvaliidt neif
//
LOCUS       WP_009527072             218 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Peptoanaerobacter stomatis].
ACCESSION   WP_009527072
VERSION     WP_009527072.1
KEYWORDS    RefSeq.
SOURCE      Peptoanaerobacter stomatis
  ORGANISM  Peptoanaerobacter stomatis
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Filifactoraceae; Peptoanaerobacter.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 218)
  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   3  (residues 1 to 218)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Peptoanaerobacter stomatis"
                     /db_xref="taxon:796937"
     Protein         1..218
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25240
     Region          17..213
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mtsnypkiwq nvkltkikit gemeeyaski vgieddgmfl letplkktql vllingsivn
       61 mvymhenlgm ysvdleviek irddnnipli rakkvsdirk iqrrnffrll tsmdivirkv
      121 ddvvvektkt vdisgggikl lskqnfevnd ivkldfkles kefsfdakvv kidntdirdm
      181 keislqfidi lekdrneiir fifdkqregi kkgmfsnd
//
LOCUS       WP_009527496             493 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Peptoanaerobacter stomatis].
ACCESSION   WP_009527496
VERSION     WP_009527496.1
KEYWORDS    RefSeq.
SOURCE      Peptoanaerobacter stomatis
  ORGANISM  Peptoanaerobacter stomatis
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Filifactoraceae; Peptoanaerobacter.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Peptoanaerobacter stomatis"
                     /db_xref="taxon:796937"
     Protein         1..493
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54582
     Region          4..493
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mleyikinnk dnvavaltdl ekdyavnidg eeiilkesik rghkfalknm kkddkvikyg
       61 mligilikdt ekgcllhtsn iktslgdiln yeynpnltsl ekressyfyg yprkngkigi
      121 rndiwiiptv gcvnavckql eldfnakinn pdlraiafph pygcsqmgdd qestrkalad
      181 milhqnagav lvlglgcent gieilkeyig eydkervvfl scqefddeya kslevldnly
      241 nlikdeqrvk tdasklvvgl kcggsdglsg itanplvgef sdiliskggs tiltevpemf
      301 gaetnlmnrc enkdifdktv slindfkmyy knydmpiyen pspgnkeggi stledksngc
      361 iqksgtanvv dvleygqrie kqglnllsap gndlvsstal alsgahivlf ttgrgtpfsc
      421 pvptikissn tnlykrkknw mdfnagsive dkdkktlaee lfefvlsias gektssekmn
      481 sydwaifkkg vtl
//
LOCUS       WP_009527669             283 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Peptoanaerobacter stomatis].
ACCESSION   WP_009527669
VERSION     WP_009527669.1
KEYWORDS    RefSeq.
SOURCE      Peptoanaerobacter stomatis
  ORGANISM  Peptoanaerobacter stomatis
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Filifactoraceae; Peptoanaerobacter.
REFERENCE   1  (residues 1 to 283)
  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 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   3  (residues 1 to 283)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 283)
  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   5  (residues 1 to 283)
  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   6  (residues 1 to 283)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Peptoanaerobacter stomatis"
                     /db_xref="taxon:796937"
     Protein         1..283
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32290
     Region          27..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          127..281
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mdtihlfndt vdyiestlng eiddkkisal sgysysmfar ifsmltgytl seyiryrklt
       61 ksavklrdts dkiidialey gyessdsftf afkkfhgytp sdvrcgkpfk ifspirlslt
      121 ikggesmktr ierkegfkva gvsksaskst mfneiwedlf kkadintlis lgngmcygac
      181 yehesfnmdi nfkymagfdv ndtekakslg leildvppae yaivsmkgkm peiihdawky
      241 ilqdffpmqg yrhagtpdfe vypkenmgsk nyemelwvpi eki
//
LOCUS       WP_009528126             587 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Peptoanaerobacter
            stomatis].
ACCESSION   WP_009528126
VERSION     WP_009528126.1
KEYWORDS    RefSeq.
SOURCE      Peptoanaerobacter stomatis
  ORGANISM  Peptoanaerobacter stomatis
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Filifactoraceae; Peptoanaerobacter.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 587)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Peptoanaerobacter stomatis"
                     /db_xref="taxon:796937"
     Protein         1..587
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=66782
     Region          2..555
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mikkrliqea pegmkhikni vffnwiclic nivsiycisi ilqktvdrsi dietvninvt
       61 iiiiltairy ffrlkvakqs flasgkikyt lrdklyqkmi sfgtnyaqkv sisqvtqlfs
      121 egieqmeiyf srylpqffys liapltlfiv isvlsiktal vlmlcvplip lsiiavqkfa
      181 kklfakywgk ytklgddfye nlqglttlki ygaderqqek mndnaenfrk itmsvlvmql
      241 nsvslmdlia ymgaalgvif atvelingri nigqaffimm isseffiplr ilgsffhiam
      301 ngmsasdrlf aildmpedng dtqdveefad ievknvsfsy neqrtvlqdv ntvikkgsfv
      361 givgesgsgk stlanlltlq yrhytgdilv gdvqikdiss sslwnniclv knenyifkgt
      421 vrenliiakk scndkdmidv lqrvnlwdfl qtkegldtkl aenasnlsgg qkqrlaiara
      481 llkdvniyif deatsnidve seeiilncin slkkkktill ishrlenvkq adnilvfeeg
      541 rlveqgnlnq llenkkqfyt lytkqqdlen fkkgaddyeq eqvvfni
//
LOCUS       WP_009528644             271 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Peptoanaerobacter
            stomatis].
ACCESSION   WP_009528644
VERSION     WP_009528644.1
KEYWORDS    RefSeq.
SOURCE      Peptoanaerobacter stomatis
  ORGANISM  Peptoanaerobacter stomatis
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Filifactoraceae; Peptoanaerobacter.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Peptoanaerobacter stomatis"
                     /db_xref="taxon:796937"
     Protein         1..271
                     /product="formate/nitrite transporter family protein"
                     /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=29389
     Region          1..270
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mlsakevaeq yielgekksg yplykmigla ilagifiala svasntvsvt vesgsiakll
       61 aglvfpggli mvlccgtelf tgdcllvisl lkkkislfrm lrcwffvyig nligsviiag
      121 linmsgqlsf fnnelaltti kvavkkvsyt fsqglamgil cnilvctavi mafsgktlsd
      181 kvlgtffpil lfilsgfehc vanmyyipsg mmalsnseyv kiavehnihi eklnigsffi
      241 nnllpvtign iiggaifiga fywflylree h
//
LOCUS       WP_009528956             587 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Peptoanaerobacter
            stomatis].
ACCESSION   WP_009528956
VERSION     WP_009528956.1
KEYWORDS    RefSeq.
SOURCE      Peptoanaerobacter stomatis
  ORGANISM  Peptoanaerobacter stomatis
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Filifactoraceae; Peptoanaerobacter.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 587)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Peptoanaerobacter stomatis"
                     /db_xref="taxon:796937"
     Protein         1..587
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=66849
     Region          2..555
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mikkrliqea pegmkhikni vffnwiclic nivsiycisi ilqktvdrsi dietvninvt
       61 viiiltavry ffrlkvakqs flasgkikyt lrdklyqkmi sfgtnyaqkv sisqvtqlfs
      121 egieqmeiyf srylpqffys liapltlfiv isvlsiktal vlmlcvplip lsiiavqrfa
      181 kklfakywgk ytklgddfye nlqglttlki ygaderqqkk mndnaenfrk itmsvlvmql
      241 nsvslmdlia ymgaalgvif atielingrv nigqaffimm isseffiplr ilgsffhiam
      301 ngmsasdrlf tildmpedng dkqdveefad ievknlsfsy neqrtvlqdv ntvikkgsfv
      361 givgesgsgk stlanlltlq yrhytgdilv gdvqikdiss sslwnniclv knenyifkgt
      421 vrenliiakk schdkdmidv lqrvnlwdfl qtkegldtkl aenasnlsgg qkqrlaiara
      481 llkdvniyif deatsnidve seeiildcin slkkkktill ishrlenvkq adnilvfeeg
      541 klveqgnlnq llenkeqfyt lytkqqdlen fkkgaddyeq eqvvfni
//
LOCUS       WP_009529054             697 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Peptoanaerobacter stomatis].
ACCESSION   WP_009529054
VERSION     WP_009529054.1
KEYWORDS    RefSeq.
SOURCE      Peptoanaerobacter stomatis
  ORGANISM  Peptoanaerobacter stomatis
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Filifactoraceae; Peptoanaerobacter.
REFERENCE   1  (residues 1 to 697)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 697)
  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   3  (residues 1 to 697)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Peptoanaerobacter stomatis"
                     /db_xref="taxon:796937"
     Protein         1..697
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=77624
     Region          2..697
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          182..259
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 mmdfdqyidi fldeskdhlq nlneallrle edpenldtvn eifrmahtlk gmsatmgfei
       61 iaklthkmen ildgirshkf tlnrdmidil fegldilegq vktiesdgke qqidisdiin
      121 rldilekggs laggvsepsn svtkeseavs kssglsfeis kedkdalyvs skemlkdgyn
      181 lykidvdlee ssmlksaraf ivfknleeag eviyshpssd diekesfegh ftilllthet
      241 ldeirssieg vsevekvsvd nfdiellnse keeekseekq eqpkeavqap qaqqpkkeep
      301 kktaqaaksq tdkkaksgkt irvdidrldn lmnlvselii vktrlednei fskrqnmtea
      361 ieyleritts lhdavtkvrm vpiervfnrf prmvrdlskd lnkeinlima geetevdrtv
      421 ideigdplvh llrnsadhgi espgdriakg kpevgtvrlv ayqdgntvvi evtddgagin
      481 tekvkqkaie rgiltqsqad eleinkaael ifaagfstad kisdvsgrgv gldvvktkie
      541 slsgtvevrt ekdkgsafii rlpltlaiiq allvivgnek yaiplnnike itnidtvdir
      601 niedkeiily rgvplelkrm sevldcenqe rkegnvtvvi vrkgekdlgl iidsligqqe
      661 ivikslgpyl sfvkliagat ilgnggvali idtneif
//
LOCUS       WP_009529530             708 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Peptoanaerobacter stomatis].
ACCESSION   WP_009529530
VERSION     WP_009529530.1
KEYWORDS    RefSeq.
SOURCE      Peptoanaerobacter stomatis
  ORGANISM  Peptoanaerobacter stomatis
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Filifactoraceae; Peptoanaerobacter.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 708)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Peptoanaerobacter stomatis"
                     /db_xref="taxon:796937"
     Protein         1..708
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=79463
     Region          <3..>325
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          601..673
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 mskkrkrdln erikakeeas vsgndslfds lgskrkvgdd yrnkltnden rfdeklheke
       61 skriteasdt slsnksknai krnlknaeak setgsekvsa tsnyqtevke nriydplakd
      121 qdgdgvadry dtdfrdseis yeplsnkksk lhemqkkaik rknysddift rkgaedktik
      181 dtiskteest kassgkkvae drakknrlyn rhnketllga savsvarasd vasrylstgs
      241 denkgveaae kgldtsskli hgiknysdkr rmkksydlse nslrvrkkks klefreakee
      301 ikkndeykka saykkfqkrk qmkaaingsn qtrirdrikk gmidtlkgsk elivkkakgv
      361 lliligiifl gtfviqfsgg amsgvvnsts svlttsylss eeqlkginqy fsglendlyd
      421 kienvesdyp gydeyivnqn gfighnvhel lsyitarfge vknlsevrgi ldglfndmyk
      481 lsydeeieir yrtvtetytd edgneytesh eepyeykkli vtldkkemds iirevfaeyp
      541 dnlkhyealf laqgnmaeif gntdlinslg gvgngaeyea ssevqkkivd aafitpspgp
      601 gwcamwvsqv yqnaglgyig gnandmyrny tftsdrsklk vgmlvavess ssgstaglty
      661 ghvgiyigdg kvidnighir vttlddwiat fckhhpvgyg fppnvkgh
//
LOCUS       WP_009530503             166 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Peptoanaerobacter stomatis].
ACCESSION   WP_009530503
VERSION     WP_009530503.1
KEYWORDS    RefSeq.
SOURCE      Peptoanaerobacter stomatis
  ORGANISM  Peptoanaerobacter stomatis
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Filifactoraceae; Peptoanaerobacter.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 166)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Peptoanaerobacter stomatis"
                     /db_xref="taxon:796937"
     Protein         1..166
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18884
     Region          1..150
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mqdylllels iksiansddr fisklsnlsa viyqymdrln wagfyildet wnnlylgpfq
       61 gkiacsniki segvcgkavr dnavqrvadv hsfdghiacd sdseseivlp lkkdgkiwgv
      121 ldidspeknr fsqedeeflt rmaqiigenv feeknfyegl ftnqwl
//
LOCUS       WP_009531366             697 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Peptoanaerobacter stomatis].
ACCESSION   WP_009531366
VERSION     WP_009531366.1
KEYWORDS    RefSeq.
SOURCE      Peptoanaerobacter stomatis
  ORGANISM  Peptoanaerobacter stomatis
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Filifactoraceae; Peptoanaerobacter.
REFERENCE   1  (residues 1 to 697)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 697)
  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   3  (residues 1 to 697)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Peptoanaerobacter stomatis"
                     /db_xref="taxon:796937"
     Protein         1..697
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=77798
     Region          2..697
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          183..260
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 mmdfdqyidi fldeskdhlq nlneallrle edpenldtvn eifrmahtlk gmsatmgfei
       61 iaklthkmen ildgirshkf tlnrdmidil fegldilegq vktiesdgke qqidisdiin
      121 rldvlekggs lgggaaseln kntvketeds tqssdlsfei skedkealya sakemlkdgy
      181 nlykievdle ensmlksara fivfknleda geviyshpss ddiekdsfeg yftilllthe
      241 tideikssie gvsevekvsv dnfdiellns ekeeekeekq eqpketvqap qaqqpkkeep
      301 kkpaqatkap adkkaksgkt irvdidrldn lmnlvselii vktrlednei fskrqnmtea
      361 ieyleritts lhdavtkvrm vpiervfnrf prmvrdlskd lnkeinlima geetevdrtv
      421 ideigdplvh llrnsadhgi espedriakg kpevgtvrli ayqdgntvvi evtddgagin
      481 tekvkqkaie rgiltqaqad eleinkaael ifaagfstad kisdvsgrgv gldvvktkie
      541 slsgtvevrt ekdkgsafii rlpltlaiiq allvivgnek yaiplnnike itnidtidir
      601 niedkeiily rgvplelkrm sevldcenqe rkegnvtvvi vrkgekdigl iidsligqqe
      661 ivikslgpyl sfvkliagat ilgnggvali idtneif
//
LOCUS       WP_009531409             157 aa            linear   BCT 20-JAN-2025
DEFINITION  transcription termination/antitermination protein NusG
            [Peptoanaerobacter stomatis].
ACCESSION   WP_009531409
VERSION     WP_009531409.1
KEYWORDS    RefSeq.
SOURCE      Peptoanaerobacter stomatis
  ORGANISM  Peptoanaerobacter stomatis
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Filifactoraceae; Peptoanaerobacter.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Kang,J.Y., Mooney,R.A., Nedialkov,Y., Saba,J., Mishanina,T.V.,
            Artsimovitch,I., Landick,R. and Darst,S.A.
  TITLE     Structural Basis for Transcript Elongation Control by NusG Family
            Universal Regulators
  JOURNAL   Cell 173 (7), 1650-1662 (2018)
   PUBMED   29887376
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Liu,B. and Steitz,T.A.
  TITLE     Structural insights into NusG regulating transcription elongation
  JOURNAL   Nucleic Acids Res 45 (2), 968-974 (2017)
   PUBMED   27899640
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Steiner,T., Kaiser,J.T., Marinkovic,S., Huber,R. and Wahl,M.C.
  TITLE     Crystal structures of transcription factor NusG in light of its
            nucleic acid- and protein-binding activities
  JOURNAL   EMBO J 21 (17), 4641-4653 (2002)
   PUBMED   12198166
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415705
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Peptoanaerobacter stomatis"
                     /db_xref="taxon:796937"
     gene            1..157
                     /gene="nusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
     Protein         1..157
                     /product="transcription termination/antitermination
                     protein NusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
                     /calculated_mol_wt=18583
     Region          2..>112
                     /region_name="NusG"
                     /note="Transcription termination/antitermination protein
                     NusG [Transcription]; COG0250"
                     /db_xref="CDD:440020"
ORIGIN      
        1 mfvlrimsge eltakklled kgykvicprk lkvernktve riiftgylfl dinsisdrdy
       61 ykikdtvnvi sfldskynls etdekyirll nnndkaldki dvyfdkdkka iiymneydey
      121 intknvirvn ardktitfrf niddivkdvt fnyneia
//
LOCUS       WP_009531916             398 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Stomatobaculum longum].
ACCESSION   WP_009531916
VERSION     WP_009531916.1
KEYWORDS    RefSeq.
SOURCE      Stomatobaculum longum
  ORGANISM  Stomatobaculum longum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Stomatobaculum.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Stomatobaculum longum"
                     /db_xref="taxon:796942"
     Protein         1..398
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42834
     Region          1..398
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkilvmncgs sslkyqlidm enesvlakgl cerigidgsl lthtpaggek ykveaampsh
       61 keaielvmqa lvdpshgvik stdeisaigh rvvhggtyyn esvlvnedvk kaiadcfdla
      121 plhnpanlmg ieaceaampg kpnvavfdta fgmsmpekay lyalpyeyye kykvrrygfh
      181 gtshnfvage virkggldpk sakvvvchlg ngasvsasig gkcvdtsmgl tpleglimgt
      241 rsgdidpaii qficeheklt veemtdvlnk ksgvlglsng issdfrdidd aanggnhlak
      301 valeaytlrv akyigayvaa mngvdaiaft agvgendkfm rknicaylgy lgvkiddern
      361 nvrgeerlis tddskvqvyl lptneelaia rdtlkltk
//
LOCUS       WP_009532845             581 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Stomatobaculum
            longum].
ACCESSION   WP_009532845
VERSION     WP_009532845.1
KEYWORDS    RefSeq.
SOURCE      Stomatobaculum longum
  ORGANISM  Stomatobaculum longum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Stomatobaculum.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Stomatobaculum longum"
                     /db_xref="taxon:796942"
     Protein         1..581
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=64413
     Region          2..557
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mikmrlirll kgagqyvvyq ilwqwlsllv qivivwniag liedagkqgi rterilvalg
       61 iiipglllrf vcdrlytaas frasadvkri lrgriyqkil rlgpsyreqi gsaelvqmsg
      121 egveqletyf grylsqffya llapltlffv lspidlrtat llllavplip lvimlvmlva
      181 krllsryfdi yyglgdsfle klqgmttlki yqadraaadd mdreserfrk itmkvltmql
      241 nstsvmdiia yggaavgivs alarfasgel slagvlmfil laaefflpmr ilgsffhigm
      301 ngmkasdrif afldlpepev gkaelgtgni dirmealsfs yeesrpilkg itlelpaqsf
      361 vslvgvsgsg kstiagilmg rnrgyggslr lngeelsrvs teslmnhltm vghdsrffra
      421 svrenlllak peatelemke alrkvnllsf ieaqgglemq lasngsnlsg gqkqrlalar
      481 allhdtpvyi fdeatsnida eseemimkvi heltksrtvl lishrlanvv gsdniymlkd
      541 gkiaeagsha elmrqagayr rlfeeqsqle rfaggrrdsh a
//
LOCUS       WP_009532416             609 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Stomatobaculum longum].
ACCESSION   WP_009532416
VERSION     WP_009532416.1
KEYWORDS    RefSeq.
SOURCE      Stomatobaculum longum
  ORGANISM  Stomatobaculum longum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Stomatobaculum.
REFERENCE   1  (residues 1 to 609)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Stomatobaculum longum"
                     /db_xref="taxon:796942"
     Protein         1..609
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=65631
     Region          489..609
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(560..561,564,582..585,587)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 merkqkkilg gaaaalcvcy lagaaffagh typnstvdgk daslisytra qelitaaate
       61 gslgirvkdl syslhrkdvl gvesrdnwke alkdgssfaw pvaifqrhel lskrtvdvhr
      121 daveklleeq glfevsipaq daklsdytad agysvlsaet gwsaskedil navvealqsd
      181 qseldltdtf avqpavtadn atlaekaaar nalvnhdftf figqatvqld setlnswlre
      241 trdgttgldy aaledyvngl qgqfepqlaa lsaehggeny vvdsermmqi lcaklginrp
      301 areseaqkaa rlaanakklk aakraarrek dkakaeqllk eaeaqqtqap eyiatlksee
      361 draadaaspv ltaslrdgif ienpdpdpap aqaaagaeat aaesqtaaet vqtesvngdt
      421 iavgaapvet etvesltaeg nsgdeseggs avketpksln geivmakddl fvpvlaadpe
      481 fqlghglnyi disiekqrvi lfengrkvme sacvtglptr erathygnfr iaykqrnril
      541 rgsqnlyaaf vsywmpfdgg iglhdaswrg kfggniyqsn gshgcinlps afakqlyeri
      601 tvgmpvyvh
//
LOCUS       WP_009533558             630 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Stomatobaculum longum].
ACCESSION   WP_009533558
VERSION     WP_009533558.1
KEYWORDS    RefSeq.
SOURCE      Stomatobaculum longum
  ORGANISM  Stomatobaculum longum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Stomatobaculum.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Stomatobaculum longum"
                     /db_xref="taxon:796942"
     Protein         1..630
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=71284
     Region          63..571
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mdklkmhtpd iakenyrkla alfpdavtet kdeegnvvra idkdvlmqei naqviddgqe
       61 ryqftwpdkr ksvvlanapi aktlrfekek svgrdgtlgg tdseniyieg dnldalkllq
      121 etylgkvkmi yvdppyntgs dfvyrdsfni dadeyednsg qtdedgnqlv qnlesngrfh
      181 tdwlnmlypr ikiakdllse eglifisidd neqqnlrkic deifgegnfv atfiwekrkt
      241 renrkaisvr hdyivcyskn yserdqalgl eemnedaigr yknpdndprg pwtsvpaiaq
      301 gghgtksqfy tfespsgkkf dppsgscwrm twpkmqeaia dnriwfgedg nnvprikkfm
      361 tegkqgltpe silaadfvgt ndsakrdlvs lfdglavfet pkpvgliqhf isitakaedg
      421 ifldffsgta asaqalfeqn vkdnikrkfi lvqlpeetde kseaykagyk ticdigeeri
      481 rragkkikee tgadidygfr cfkvdssnmk dvyyrpaelg qaslddytdn ikedrtpedl
      541 liqvmldlgv llsskveqte iggkkvfsva dgyliscfdk dvtedvvtei akrhpfyfvs
      601 rdssmasdsv atnfeeifkt yspetvrkvl
//
LOCUS       WP_009533977             197 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Oribacterium parvum].
ACCESSION   WP_009533977
VERSION     WP_009533977.1
KEYWORDS    RefSeq.
SOURCE      Oribacterium parvum
  ORGANISM  Oribacterium parvum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Oribacterium.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Oribacterium parvum"
                     /db_xref="taxon:1501329"
     Protein         1..197
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=23007
     Region          14..197
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mnevnifdql leeqngyirl idaqnegvsk savldyvhkk emekvapgiy ispdawedrl
       61 yliqlrnrki ifshetalyi hnlsdrepfa pvitvergyn akhlkdkgii vhtvrpewie
      121 lglteektft gntvriydre rcicdiiknk nrmdiqvfqm alrsyfsgsd knihklmeya
      181 rimgisdkvr qytevll
//
LOCUS       WP_009535044             280 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Oribacterium parvum].
ACCESSION   WP_009535044
VERSION     WP_009535044.1
KEYWORDS    RefSeq.
SOURCE      Oribacterium parvum
  ORGANISM  Oribacterium parvum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Oribacterium.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 280)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 280)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Oribacterium parvum"
                     /db_xref="taxon:1501329"
     Protein         1..280
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31498
     Region          27..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          127..277
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mniiksfnnt idyletvldd eidekkvtql sgysysmfsr lfsiltettl seylrsrklt
       61 eaavilrdtd ekiidvalkf gyessdsfgt afknfhgftp sevrngkpfk lvsrvqlals
      121 vrggrsmnit iqkkkaftva ginkqsinss lcpsvwdtly ekyshdelas lgsgqrvgic
      181 hdvenpstin ymagyivtga dkarsmgldv leveeaeyav veligsvpdc ihngwkyame
      241 vffpehgyvh sgkpdfeyyy egdmhsndyk melwipitka
//
LOCUS       WP_009535301             625 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Oribacterium parvum].
ACCESSION   WP_009535301
VERSION     WP_009535301.1
KEYWORDS    RefSeq.
SOURCE      Oribacterium parvum
  ORGANISM  Oribacterium parvum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Oribacterium.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Oribacterium parvum"
                     /db_xref="taxon:1501329"
     Protein         1..625
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=69641
     Region          2..557
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mikmrlirll egagkyivqq ivwqwislla evvivyniah llenawrenl stegialtmg
       61 ivllglgfrf lcdrlytkas fhasadvkri lrnkiyekml slgpsyresv nsaeivqmag
      121 egveqletyf grylsqffys llapitlffi lsrisvqtal llllavplip ivimlvmiva
      181 kkllsnyfai yyglgdsfle klqgmttlki yqadqaaaed mdreaelfrk itmkvlsmql
      241 nstsvmdiia yggaavgiis algqfskgai slsgvlmiil laaefflpmr llgsffhigm
      301 ngmkasdrif afldlpeaed gkavleekei rismeklcfs yeesreilrd veleiparsf
      361 vslvglsgsg kstiagilmg knkgykgsvk lngreltefs srsildkmtm ighdswifkg
      421 tvrenlllgk psateeemke alrkvnllsf veaqgglemp llsngsnisg gqkqrlslar
      481 allhdspvyi fdeatsnida eseemimevi helaksrtil lishrlanvv gsdcifmlen
      541 grvaeagkhe ellkkggsys rlfkeqkele cysdknkess agrhkesfve tqrdtgmeep
      601 ghmedlqdkt geredtveeg gekhe
//
LOCUS       WP_009535796             393 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Oribacterium parvum].
ACCESSION   WP_009535796
VERSION     WP_009535796.1
KEYWORDS    RefSeq.
SOURCE      Oribacterium parvum
  ORGANISM  Oribacterium parvum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Oribacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Oribacterium parvum"
                     /db_xref="taxon:1501329"
     Protein         1..393
                     /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=46908
     Region          18..249
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mresirkeer kekgrdktkk rvkeldsfkg fliflvvlgh fllplsdspy plfnrsfyli
       61 ysfhmpaflf lsgyfaygkw kkrgtsfrsl fsylllyilm kfmlhradil fydvhttwpd
      121 ffhesstpwy llvlfflelt llpmeifrrk ktgeqvisfy flclillsip lsfmkigeew
      181 kdflasdril gfapffylgm laklgdfsfq kihrppfvlg fcftliiilf lpkllpytrv
      241 fygtwgyrie geailpffkk hptliriafi pfslciayff yglliflrqk kesiqpeits
      301 rgsqiyfgme rvfqdretfl mkmghysmpi yvfhrpfrda ffaggleqpf whegipfwli
      361 llfyifllll sllllfvlgr ktldnlcrfr ftg
//
LOCUS       WP_009535987             237 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Oribacterium asaccharolyticum].
ACCESSION   WP_009535987
VERSION     WP_009535987.1
KEYWORDS    RefSeq.
SOURCE      Oribacterium asaccharolyticum
  ORGANISM  Oribacterium asaccharolyticum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Oribacterium.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 237)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Oribacterium asaccharolyticum"
                     /db_xref="taxon:1501332"
     Protein         1..237
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=27147
     Region          4..235
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mveraiqqna fymvyqpqve ckgrkivgfe sllrirneac spdqfipvae qygyitklgk
       61 iaveqvvrql arwkdegrtl cpisinfssy qiydddfvdf llyqmerhgi pheyvvleit
      121 esilfeeskq tkavfkrlve egielhlddf gtgyssfayl pyiplntvkm dksivdnfls
      181 sngdvvrnli sivhdlgmvv ivegveeewq yeklveygcd riqgylfggp vlateis
//
LOCUS       WP_009538189             593 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Oribacterium parvum].
ACCESSION   WP_009538189
VERSION     WP_009538189.1
KEYWORDS    RefSeq.
SOURCE      Oribacterium parvum
  ORGANISM  Oribacterium parvum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Oribacterium.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 593)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 593)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Oribacterium parvum"
                     /db_xref="taxon:1501329"
     Protein         1..593
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=69330
     Region          40..276
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mervhndgrd kkgirsyths kkekrnlarl elekhieshi eeaiaekqvk vylqpnvrgl
       61 tqrvcgaeal srwidpkygm iypgdfisvl ektlkihlld lyvfreickn lgerlerket
      121 vfpislnfsr ldfnigdfld qleliveqyh vpknllhiev tesvvmhneg ymkyvvkklh
      181 elgyqvwmdd fgsgysslnl lkefefdtfk idmrflsdmg kksliiiysi lymakeigih
      241 tvaegvetee qfrflkhagc ermqgyyfgr pepmenwlsd liekngvesr kedylfdqvg
      301 lvniisptpf vldrlddspn iygfetvipi avcsetggki chlnftepyr dnlldlgyag
      361 thdfqdalnn rkvllaekir dimmlardsm evesmdfiss gkhchlqarl vtsmdecfiy
      421 liridvltnn rvfrkikdmn dtlrtlysvy dmvillnlrs dtllpvymce lfdrieesdn
      481 lsaeinkyvy knvhpedkeh craflnpqdm werlkdseeg fllsyfrsrn khgkfvwkrf
      541 vlvrsydigd eekvvlgvha lsmdklsill qesksffsed fneesegald ffk
//
LOCUS       WP_009539071             363 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Caenispirillum
            salinarum].
ACCESSION   WP_009539071
VERSION     WP_009539071.1
KEYWORDS    RefSeq.
SOURCE      Caenispirillum salinarum
  ORGANISM  Caenispirillum salinarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Novispirillaceae; Caenispirillum.
REFERENCE   1  (residues 1 to 363)
  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 363)
  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 363)
  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 363)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Caenispirillum salinarum"
                     /db_xref="taxon:859058"
     Protein         1..363
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39491
     Region          21..362
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mgqrtvirtr rrrrwktavp rraaaglvil alavlfppra dardlvvqsa fpsgmaafse
       61 serrisegve sltggsltlr fvgaggivep qhlleavreg avpvgfdwmg yhadrvplgg
      121 lvgsmpfgpt prelsgwlya ggglsllerg yarlgivvlp cdmlpsaagg wfkteirsve
      181 dfkglriria glgaevlerl gsessqepva qiynaleegr ldavefaapl vdqsfgfhhf
      241 tkyyyfpgwh qpaslnillv nrdvwdslke geraalrktc renvllglae gvarqteavd
      301 aavargievr rfpdpvlarl ravsrevvae aasrdplaad alaslseyve qarrwsalqa
      361 lpr
//
LOCUS       WP_009539344             821 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Caenispirillum salinarum].
ACCESSION   WP_009539344
VERSION     WP_009539344.1
KEYWORDS    RefSeq.
SOURCE      Caenispirillum salinarum
  ORGANISM  Caenispirillum salinarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Novispirillaceae; Caenispirillum.
REFERENCE   1  (residues 1 to 821)
  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 821)
  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 821)
  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   4  (residues 1 to 821)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Caenispirillum salinarum"
                     /db_xref="taxon:859058"
     Protein         1..821
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=90563
     Region          72..785
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mpltplscdr lytpcpedrl gfetteelpd qdetvgqdra veavdfgigi radgfnifaa
       61 gpegtgktsl irhfigraaa qqprpsdway vhnfddpncp ralrlpggra rdfqramdrl
      121 vedmqaaipa afegdeyrtr rqaiedefke rqekafgeiq nkarengval vrtpqalala
      181 pmkdgevisp edfnelpede rkqrketmeh lqeeleqqmr qlprwereqr ekvreldeev
      241 teyavghqid dlkeqwkdcp avldhldrvr gaivervedf lpeseemrql psalrqqigg
      301 rkelrlddyk vnvlvgheng ngapvvvedh ptqpnvigri ehqqqygalv tnftlirpga
      361 lhranggylv idarkllmqp fayedlkral rnkearieap gsawgifttt slepepipld
      421 ikvvligepm vyyllshhdp efrelfkvqa dfdfrmhrtd etvgklasll gtmarrdglk
      481 plhrsavara veqaarladd serltthmgs lgdliready wagkrgaevv eradvqqaid
      541 akthrtdrvr ehiqeeiarg tllvdtdgek agqinglavl qlgtfafgrp sritcrarmg
      601 rgevldiere vqtggalhsk gvmilsgfla arfgqsgpls lnaslvfeqs yglidgdsas
      661 caelyallst laeapikqgl avtgsvnqfg qvqaiggvne kvegffdvca argltgdqgv
      721 lipatnvkhl mlredvreac gqgrfhiyav etvdegieil tgipagapse sgidggagwp
      781 tgsinrrvaa rlaawrrram emmragggpg ggngngaggg r
//
LOCUS       WP_009540091             788 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Caenispirillum salinarum].
ACCESSION   WP_009540091
VERSION     WP_009540091.1
KEYWORDS    RefSeq.
SOURCE      Caenispirillum salinarum
  ORGANISM  Caenispirillum salinarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Novispirillaceae; Caenispirillum.
REFERENCE   1  (residues 1 to 788)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 788)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 788)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..788
                     /organism="Caenispirillum salinarum"
                     /db_xref="taxon:859058"
     Protein         1..788
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=85551
     Region          27..788
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 maihrrlrlh hwitalllvl lslvilamlg awlllhgnlp rttgaldlpa ldapvevard
       61 ahgiptirag strdaylalg fvhaqdrfqq mefmrrlgeg rlaevigega vgmdrwsrtl
      121 glhrraqqsy ralgdearaa ldayaagvna wlrrrdswlp ppltlldvrp dpwtpadslv
      181 wqrlmafrla gnwqdeaara rlldaglppe rvadlwhetq gvtvsepvtm pqpvreaalp
      241 pappaalaat lasnawtvap arsatggall andphlgyqt pilwylarle tpdwqvsgat
      301 vpgvpfhlig hngrigwgit tthadtkdlf ietvtgdgta ylapdgprpf etreevievr
      361 ggepvtftvr etrhgpvvtd lrgmagvagg tdvvalaatg lmegdrtaea imrlnragnr
      421 aefleamrlf hapmqnvffa atdgdtgfis agrvpvrkag dgrvpvpgag gshdwtgfvp
      481 fedlpqafap asgtllnann rvvgdgyphl itahwpppwr alrgeallag reahtvadmi
      541 amqhdmrstm aetlvpvllg alpaspdtae arrrleawdg tmdpdrpepl ilsawlprie
      601 kaltadelgd ragdwrenge rfiaavvssr dtwwcdrkdt gasetcgdil dlslsdaltd
      661 lrarhgedmd gwrwgdvhea aldnrlygri pliggwfnlr pevgggnhtl lragywngge
      721 sgrfdavhga glrmvldmad pgasrfiiat gqsenplsdh yadqmplwsr gatltldgep
      781 asvlrlep
//
LOCUS       WP_009540059             290 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Caenispirillum
            salinarum].
ACCESSION   WP_009540059
VERSION     WP_009540059.1
KEYWORDS    RefSeq.
SOURCE      Caenispirillum salinarum
  ORGANISM  Caenispirillum salinarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Novispirillaceae; Caenispirillum.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Caenispirillum salinarum"
                     /db_xref="taxon:859058"
     Protein         1..290
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30176
     Region          29..287
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 msatttaarp gtagagafts igrldaldwa lplvprdrrg aaravlafra evqavadgaa
       61 prpekrgrla awrleldale aglpatpvti alqqplhrhr lprtelenlv laadmdaggv
      121 mvappqcdlr lytrrsggal iillaavlgd tshaagcfgl algeamrltt llrdlgpaar
      181 agrlclpres laeagivaas taevldhpal daacapvaat aserfadarl mlpevalpar
      241 pflravleah edlletlhar grgaavqppp spgrvalaar vlrhrfrgaa
//
LOCUS       WP_009540098             184 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Caenispirillum salinarum].
ACCESSION   WP_009540098
VERSION     WP_009540098.1
KEYWORDS    RefSeq.
SOURCE      Caenispirillum salinarum
  ORGANISM  Caenispirillum salinarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Novispirillaceae; Caenispirillum.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Caenispirillum salinarum"
                     /db_xref="taxon:859058"
     Protein         1..184
                     /product="TRAP transporter small permease subunit"
                     /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=19961
     Region          3..171
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mqalhslarg idrtndligr avawltlamv liqfvvvvlr yvfglgfiwm qesilymhgi
       61 vflvgagytl lkdghvrvdi fyrearptrk alvdllgvif llvpfcalvw tvalpyvmns
      121 wavlegsket sgiqgvyllk tsilvftvlv glqglatalk silvlsgvld dngdttgaer
      181 ggah
//
LOCUS       WP_009540819             140 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Caenispirillum salinarum].
ACCESSION   WP_009540819
VERSION     WP_009540819.1
KEYWORDS    RefSeq.
SOURCE      Caenispirillum salinarum
  ORGANISM  Caenispirillum salinarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Novispirillaceae; Caenispirillum.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Caenispirillum salinarum"
                     /db_xref="taxon:859058"
     Protein         1..140
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=14713
     Region          63..132
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mtrcrllaaa llllpvplla qtaegldatd lrlveqadng itwpddwalp adygrgesli
       61 avvrgmpvvg slgrplgeve gvlagrdgra ralavetdgl ldlgdpvvlp lskasmsttg
      121 dafvttlteq elealprwrd
//
LOCUS       WP_009541168             372 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Caenispirillum
            salinarum].
ACCESSION   WP_009541168
VERSION     WP_009541168.1
KEYWORDS    RefSeq.
SOURCE      Caenispirillum salinarum
  ORGANISM  Caenispirillum salinarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Novispirillaceae; Caenispirillum.
REFERENCE   1  (residues 1 to 372)
  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 372)
  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 372)
  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 372)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Caenispirillum salinarum"
                     /db_xref="taxon:859058"
     Protein         1..372
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40499
     Region          27..349
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mlkrvtkhal aigvaaavta gvtagaqaqd kvrwqmtmgf pstlpaladt gpwvaeqldk
       61 msggnidlrv fepgklvkgt evydavssgk vdsgyvwagy eigklpasal ygavpfgmep
      121 aqfaawmlek ggqemmeeiy apqnivplfc gtispesagw ftfplesldq veglkirfag
      181 lggeilqklg asvtllpgse lfealekgvi datefslpvv deqlgfykva kfyhlpgwhq
      241 pstnqylyin kekwdalddq tqamfrtact agvaksiara egtqgaalqr lqeehgveav
      301 evpeevlvel kkaanevmae ysakdenfkr vydsmtafma enaqwhrmgy lprdwranhp
      361 elygddaatt gn
//
LOCUS       WP_009541459             226 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Caenispirillum salinarum].
ACCESSION   WP_009541459
VERSION     WP_009541459.1
KEYWORDS    RefSeq.
SOURCE      Caenispirillum salinarum
  ORGANISM  Caenispirillum salinarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Novispirillaceae; Caenispirillum.
REFERENCE   1  (residues 1 to 226)
  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 226)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 226)
  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   4  (residues 1 to 226)
  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   5  (residues 1 to 226)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Caenispirillum salinarum"
                     /db_xref="taxon:859058"
     Protein         1..226
                     /product="TRAP transporter small permease subunit"
                     /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=24657
     Region          48..197
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mtnntsrptd peayeelsdt dagqqpvdrs gqeghirtvl dfavaesakv fawlvfvgav
       61 isvyevvmry afnnptswvh ettvflisvi falggpiala rdkhirvrli ydwvgpkarr
      121 wldvvnsiit fvflsgmtya awimfyksth splgviqler sgtswnppfp aftktiilis
      181 vavmlvqtil hlvkafrgkg ydddhgggkg kgggpgpast tlgkeg
//
LOCUS       WP_009542454             114 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Caenispirillum salinarum].
ACCESSION   WP_009542454
VERSION     WP_009542454.1
KEYWORDS    RefSeq.
SOURCE      Caenispirillum salinarum
  ORGANISM  Caenispirillum salinarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Novispirillaceae; Caenispirillum.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Caenispirillum salinarum"
                     /db_xref="taxon:859058"
     Protein         1..114
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12321
     Region          19..109
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mtlpldiaar akasrerirg eilsclreil sgaekaprve riatfgsvar gdfhglsdvd
       61 lavigegvrp gdldtaallp lerpvdviyl dpardphmma eidrdgvtvw hrsp
//
LOCUS       WP_009543981              97 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Crocosphaera subtropica].
ACCESSION   WP_009543981
VERSION     WP_009543981.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera subtropica
  ORGANISM  Crocosphaera subtropica
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae;
            Crocosphaera.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Crocosphaera subtropica"
                     /db_xref="taxon:2546360"
     Protein         1..97
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11076
     Region          1..97
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mninqliqek reeiimiaak hgasnlrifg svargeaden sdldllidyd skkrspwfpl
       61 rlireletll gckvdivteq glkdrikerv lqeamrl
//
LOCUS       WP_009546893             366 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Crocosphaera
            subtropica].
ACCESSION   WP_009546893
VERSION     WP_009546893.1
KEYWORDS    RefSeq.
SOURCE      Crocosphaera subtropica
  ORGANISM  Crocosphaera subtropica
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae;
            Crocosphaera.
REFERENCE   1  (residues 1 to 366)
  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 366)
  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 366)
  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 366)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Crocosphaera subtropica"
                     /db_xref="taxon:2546360"
     Protein         1..366
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40079
     Region          1..363
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkrrhflsna algattatvl gscqsqsveg ngggsslpnl rwkmqtswpk sldtifggaq
       61 tvcdrvkams ggkftitpya ageivpglev ldavqqgtve cghspsyyyv gknpalgfgt
      121 ampfgltaqq qnawfyhggg letmhklyad fnvinfpagn tgaqmggwfk rqvnsvndlk
      181 glkmripglg gevmsrlgvn vqvlpggevf laldtgaida aewvgpydde klglnkaany
      241 yyypgwwepg atldlqinrn awdqlpqeyq ailqaaamea nlnmlsqyda qnrvalqsll
      301 qggtqlipys deiltaaqti afdlyeenas qdatfkevye swnkfrqeii qwnkinelsy
      361 tnfvfk
//
LOCUS       WP_009558554             395 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Lactobacillus equicursoris].
ACCESSION   WP_009558554
VERSION     WP_009558554.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus equicursoris
  ORGANISM  Lactobacillus equicursoris
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Lactobacillus equicursoris"
                     /db_xref="taxon:420645"
     Protein         1..395
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43370
     Region          2..393
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mdkvlainsg sssfkykifs lddeqvlasg lgdrigidgs tfsiklange kheaevdlpn
       61 qeaavqtllk wlkeydvied vkeivgvghr ivsggdlfld saiidkdnlh kvfdladyap
      121 lhnpaegrgi qafmellpnv pqvgvfdtsf hqsmdavhyl yslpyeyyek ykvrkygahg
      181 tsvrfvsqra aelmgkdlkd lklivchlgs gasvtavkdg kcydtsmgfs plagvtmgtr
      241 sgdvdpsalq himhkegmtd fdemidilnh ksgllgisgi ssdkrdirds dspraqlasd
      301 ifddrvvryi gsyiaemnga daiiftagig ehddpmrkdv lskftymgve vddaanesne
      361 egfittkdsk lkalviptde elmierdvvr laklk
//
LOCUS       WP_009559264             103 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Lactobacillus pasteurii].
ACCESSION   WP_009559264
VERSION     WP_009559264.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus pasteurii
  ORGANISM  Lactobacillus pasteurii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Lactobacillus pasteurii"
                     /db_xref="taxon:872327"
     Protein         1..103
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11407
     Region          5..101
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(27,58..59,61,82)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(27..28,36,39,41..42,44,47..48,50,58,63,70)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mmkldedliy evlsavseip tgkvasygvi akltghdkna rlvgrilhqa edfgdypchr
       61 vvnsagrlvp gwqqqrqllk aegiefkang nvdmkkclwp pfe
//
LOCUS       WP_009561366             118 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Acidithiobacillus].
ACCESSION   WP_009561366
VERSION     WP_009561366.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus
  ORGANISM  Acidithiobacillus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (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   3  (residues 1 to 118)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 118)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Acidithiobacillus"
                     /db_xref="taxon:119977"
     Protein         1..118
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12414
     Region          6..112
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 melqaeagga akalsvvlrd atavqryymp nikgggvlve tanllpigte vllmitlpdg
       61 qprapvmgkv vwvtppdnre grppaigvqf vndrsgvlir iqnalsglpr ndgevlsf
//
LOCUS       WP_009564907             206 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Cereibacter sphaeroides].
ACCESSION   WP_009564907
VERSION     WP_009564907.1
KEYWORDS    RefSeq.
SOURCE      Cereibacter sphaeroides
  ORGANISM  Cereibacter sphaeroides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Cereibacter.
REFERENCE   1  (residues 1 to 206)
  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 206)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 206)
  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   4  (residues 1 to 206)
  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   5  (residues 1 to 206)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Cereibacter sphaeroides"
                     /db_xref="taxon:1063"
     Protein         1..206
                     /product="TRAP transporter small permease subunit"
                     /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=22023
     Region          32..169
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 makgsapagp dappgppsse tvppagtlph tapslridag liaigkaasw lwlvtvglia
       61 wavvsrylfg tstialdelq whlvgsawll glsytlalde hvrvdviher lrprarcwie
      121 fagilllllp flavaaheti pfaleayrsg erstapaglg hrwiaksvma lsvllllvaa
      181 lsrlmrvtav lfglprplpi etrtdr
//
LOCUS       WP_009567924             392 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptococcus intermedius].
ACCESSION   WP_009567924
VERSION     WP_009567924.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus intermedius
  ORGANISM  Streptococcus intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus anginosus group.
REFERENCE   1  (residues 1 to 392)
  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 392)
  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
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 392)
  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   5  (residues 1 to 392)
  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   6  (residues 1 to 392)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 392)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Streptococcus intermedius"
                     /db_xref="taxon:1338"
     Protein         1..392
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44052
     Region          14..62
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          75..386
                     /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 mnqtkkqael rtiildkiya kgpisridis ketgitpatv saitgsliqe kllyelgede
       61 ehtkvgrkki llgikkqhsy figcelseky fsfvlsdntg nvidkekatv ssekilsega
      121 dsfchllrqf isqhvsypiq avgvaipgry lhndlittnn qtwkqfdlak iknefsfpiy
      181 fsnnvncmal akrlfsayql denfiyfhfa rgmhcsymyn gkiygktniv igeightvvc
      241 pdgevcgcgr rgclqtyase swlikkakii fetaelthlk slvtdkeeit iqtiltaynl
      301 gdqsvlnilh lafkylaqsl lnlsmiidak kiylhspilt ddkviaafyq eiaqqpkllf
      361 kdlpeliiep yddftgatag valclqkefl si
//
LOCUS       WP_009568762             165 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Streptococcus intermedius].
ACCESSION   WP_009568762
VERSION     WP_009568762.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus intermedius
  ORGANISM  Streptococcus intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus anginosus group.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Streptococcus intermedius"
                     /db_xref="taxon:1338"
     Protein         1..165
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18093
     Region          23..156
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mnqsekisny qllldqleal legernalan lsnssallnq alphsvftgf ylsngnelvl
       61 gpfqggvscv higfgqgvcg eaaasrqtvi vedvtqydny iscdsrarse ivvpmvkdgr
      121 lvgvldldsh llgdydeidr eylenfiail lektnwnfem fgdks
//
LOCUS       WP_009569176             107 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Streptococcus intermedius].
ACCESSION   WP_009569176
VERSION     WP_009569176.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus intermedius
  ORGANISM  Streptococcus intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus anginosus 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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Streptococcus intermedius"
                     /db_xref="taxon:1338"
     Protein         1..107
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11861
     Region          12..102
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(28,59..60,62,83)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(28..29,37,40,42..43,45,48..49,51,59,64)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mnkvlnekli nqilsvvaci pvgevatygq itrligrekn arlvgrvlsq aglygkypch
       61 rvvnsagrla paweeqrhll waegvtfktn gcvdlkkhqw kptinkv
//
LOCUS       WP_009570326             266 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-deoxy-manno-octulosonate cytidylyltransferase
            [Roseobacteraceae].
ACCESSION   WP_009570326
VERSION     WP_009570326.1
KEYWORDS    RefSeq.
SOURCE      Roseobacteraceae
  ORGANISM  Roseobacteraceae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales.
REFERENCE   1  (residues 1 to 266)
  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 266)
  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 10787365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Roseobacteraceae"
                     /db_xref="taxon:2854170"
     Protein         1..266
                     /product="3-deoxy-manno-octulosonate cytidylyltransferase"
                     /EC_number="2.7.7.38"
                     /GO_function="GO:0008690 - 3-deoxy-manno-octulosonate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0033468 -
                     CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28756
     Region          1..259
                     /region_name="KdsB"
                     /note="CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell
                     wall/membrane/envelope biogenesis]; COG1212"
                     /db_xref="CDD:440825"
ORIGIN      
        1 msvlivipar yastrypgkp lveltgatge akslirrswd aaiavsgvdr vvvatdddri
       61 rtaaeafgae vvmtseacan gtercaeale nlgggydivv nlqgdapltp awfvedlvag
      121 lrahptaeva tpvlrcdgra lngfledrra grvggttavf gsdhkglyfs kevipytskt
      181 yaddeetpvf hhvgvyayrp salaaypkwp tgpleslegl eqlrfleqer pvlcvevesr
      241 grqfwelnnp edvprleaml semgas
//
LOCUS       WP_009570592             150 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Celeribacter baekdonensis].
ACCESSION   WP_009570592
VERSION     WP_009570592.1
KEYWORDS    RefSeq.
SOURCE      Celeribacter baekdonensis
  ORGANISM  Celeribacter baekdonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Celeribacter.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 150)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Celeribacter baekdonensis"
                     /db_xref="taxon:875171"
     Protein         1..150
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16076
     Region          1..143
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mdyaalsdri kslcegeedm valmatface vhlsddrfdw tgfyrvvskd llkigpyqgg
       61 hgclvipfsr gvcgacartg eaqlvedvea feghiacsst trseivlpvr nakgtllgvf
      121 didsnlpaaf tqedvmalse ilddtfasca
//
LOCUS       WP_009571905             192 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Celeribacter baekdonensis].
ACCESSION   WP_009571905
VERSION     WP_009571905.1
KEYWORDS    RefSeq.
SOURCE      Celeribacter baekdonensis
  ORGANISM  Celeribacter baekdonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Celeribacter.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Celeribacter baekdonensis"
                     /db_xref="taxon:875171"
     Protein         1..192
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21159
     Region          1..163
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlkrlynwtm slaesphalw alavvafves svfpippdil miplivarpk dafkiagiat
       61 lasvlggmlg ywigfgafet igrpvlefyg kdayfdefav kynewgawav liagvtpfpy
      121 kvitilsgtt qlslpvfiva sivarsfrff vvaallwkfg dpirdfierr lgavftvlil
      181 llvggfyavk fl
//
LOCUS       WP_009572163             194 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Roseobacteraceae].
ACCESSION   WP_009572163
VERSION     WP_009572163.1
KEYWORDS    RefSeq.
SOURCE      Roseobacteraceae
  ORGANISM  Roseobacteraceae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales.
REFERENCE   1  (residues 1 to 194)
  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 194)
  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   3  (residues 1 to 194)
  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   4  (residues 1 to 194)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 194)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 194)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Roseobacteraceae"
                     /db_xref="taxon:2854170"
     Protein         1..194
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21089
     Region          4..194
                     /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"
ORIGIN      
        1 msaplsiivv etdrtraqli vdslrqagdf diyiiaevtg larqiqarnp divlidienp
       61 srdtmeeltl asgpldrpva mfvdrsdegl saaaieagvs ayivdglhsn rvkpildaai
      121 arfrmfqrmr telaetkkal eerkvidrak gmlmrakgig edeayallrk tamdqgrrva
      181 dvaqalvtaa glla
//
LOCUS       WP_009572212             252 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Celeribacter
            baekdonensis].
ACCESSION   WP_009572212
VERSION     WP_009572212.1
KEYWORDS    RefSeq.
SOURCE      Celeribacter baekdonensis
  ORGANISM  Celeribacter baekdonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Celeribacter.
REFERENCE   1  (residues 1 to 252)
  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 252)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Celeribacter baekdonensis"
                     /db_xref="taxon:875171"
     Protein         1..252
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28201
     Region          1..249
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mpkfaanlsf lfkeypfler faeakacgfe avevlfpyee pasevakrma dlnlkmvlin
       61 tpppnytgge rgfaavpgle drfrkdfkra lryaqflgaa hmhimagkak glvaletfkk
      121 nlawaaaeap tmsltiepin pidmpgyfld dfdlaievld svaelnlglq fdayhaqiit
      181 gdamlaweky apyvrhiqia gppdrhepik glvdypaffr avdasgyqgw vsaeyipkkr
      241 teegldwfrq aq
//
LOCUS       WP_009572371             275 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Roseobacteraceae].
ACCESSION   WP_009572371
VERSION     WP_009572371.1
KEYWORDS    RefSeq.
SOURCE      Roseobacteraceae
  ORGANISM  Roseobacteraceae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 275)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Roseobacteraceae"
                     /db_xref="taxon:2854170"
     Protein         1..275
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=30555
     Region          <16..257
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mntsfyghdd lgsplsaava erdqntmdmv hsalrkkqvm layqpivqtl rpdrpaffeg
       61 lirvldqtgr viparefidv aettetgrql dclalelglt alnkhptlrl ainmsarsig
      121 yprwketlhi glaknatvae rlileitess amvmpdlvsv fmkelqsmgi sfalddfgag
      181 ytafrylkef yfdivkidgs firgiatnpd nqvltqalvs vakhfdmytv aefveteada
      241 qylssigidc mqghyfgaat idpawqtket rrkas
//
LOCUS       WP_009573199             344 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Celeribacter
            baekdonensis].
ACCESSION   WP_009573199
VERSION     WP_009573199.1
KEYWORDS    RefSeq.
SOURCE      Celeribacter baekdonensis
  ORGANISM  Celeribacter baekdonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Celeribacter.
REFERENCE   1  (residues 1 to 344)
  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 344)
  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 344)
  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 344)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Celeribacter baekdonensis"
                     /db_xref="taxon:875171"
     Protein         1..344
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=36639
     Region          5..342
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkthikslvt lavtvstlva apvmakgtrl diqsawpltm pasganaayl getlnessgg
       61 sldvtvygag klvpslqifd avqqgtldag itsplyvagr fpavqlfggi pfgpdaitht
      121 awlydgggre iwseiyakqg vvtipcglmd seaggwynfe intvddfkgk kvrfaglage
      181 amvkvgasiv llpggeiypg lekglidgte lsmpaiditl glqqvgkyyy lpgwhqpaam
      241 nelivnqakw dsldasqqal ieesckavnl esitstmaln akavaefeaa gveiksfppe
      301 vlehlhaafd eviaeqtskd adfkrvwesl tayrasvapw aerr
//
LOCUS       WP_009573178             342 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Roseobacteraceae].
ACCESSION   WP_009573178
VERSION     WP_009573178.1
KEYWORDS    RefSeq.
SOURCE      Roseobacteraceae
  ORGANISM  Roseobacteraceae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales.
REFERENCE   1  (residues 1 to 342)
  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 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 342)
  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   4  (residues 1 to 342)
  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 342)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Roseobacteraceae"
                     /db_xref="taxon:2854170"
     Protein         1..342
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37849
     Region          27..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          254..334
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 madathghaa irstvlgsvl drliargvst qpllskhgms ldilkdpyar lsvmeyagfm
       61 esaaalsgde higarigsdi ragdlgpmgi llslsrsiyv gidrivrstr slqtgteval
      121 iengddvfws yrlvdghiwp rrqdaeftlv attqvirdnf isrwapqqvh fehvepesaq
      181 flrryfgcpv lygqatnrlv mdrgpmleiy raedtalvsm lerhiadlie ktprrstlte
      241 atrsivsssl glrpvsverv aetlglssrn lqrklaeegt svrilldeir rtraemllqe
      301 gtqsvgriat algyadgtaf wrahkrwseh sprqvkasgs sl
//
LOCUS       WP_009573857             390 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator
            [Roseobacteraceae].
ACCESSION   WP_009573857
VERSION     WP_009573857.1
KEYWORDS    RefSeq.
SOURCE      Roseobacteraceae
  ORGANISM  Roseobacteraceae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales.
REFERENCE   1  (residues 1 to 390)
  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 390)
  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
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 390)
  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   5  (residues 1 to 390)
  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   6  (residues 1 to 390)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 390)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 390)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Roseobacteraceae"
                     /db_xref="taxon:2854170"
     Protein         1..390
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42568
     Region          22..>67
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          87..380
                     /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 mndievrqlr sgvnqigvre inerlilsli qrhggmpgse lakrtdlsaq tvsnilrkle
       61 negflkrgtp krgkvgkpsi pmeidsdgal sfglkigrrs sdlavmdlsg rvleqrlity
      121 rypmpdqift flregmeala galtpyqrkr lcgigvaaps eiwrwsdalg apedfniwre
      181 idfateiatf sdlpqytdnd ataacraehf fgrgrafsdy ayffigsfig ggivmassvv
      241 egrqhnagaf gslphitaeg kevqlidaas lylleaavlk aggdtaamwr mpqdwtgfgt
      301 dlddwitqsa kalasasrtv csvidfeavl idgafpadvr erlvaetrte lqaldlrgli
      361 tpriepaqig gnarvigaaa epmfsqfflt
//
LOCUS       WP_009574729             502 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Aequoribacter fuscus].
ACCESSION   WP_009574729
VERSION     WP_009574729.1
KEYWORDS    RefSeq.
SOURCE      Aequoribacter fuscus
  ORGANISM  Aequoribacter fuscus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Halieaceae; Aequoribacter.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Aequoribacter fuscus"
                     /db_xref="taxon:2518989"
     Protein         1..502
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=53030
     Region          1..502
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mltltlsned nvavartala kdvllpehrg lacrsdvpqf hkvaiksiak gqpvikyrqv
       61 igvaltdiaa gehvhdhncg mtderiapat kaktaelppd ietsfegylr adgevgtrny
      121 vgiittvncs asvakaieqy ysqaevagry pnvdgviait hgsgcgmnkg egyellmrvc
      181 agmsqhpnfg gvmliglgce vlqlsallda lpddvrkrsn tlviqeqggt ratieagiek
      241 mavlcevsnt lsrtpqpvsk lrvglqcggs dalsgitanp algramdilt slggtailse
      301 tpelygaeqm lraraasdev adklndrlaw wreyagknga qldnnpspgn kagglttile
      361 kslgaqakgg tstmtdvvay aqlirksglv imdspgydpv svtgqmasga nlicfttgrg
      421 svygsrpaps iklatntpmy ekmtldmdyn cgeifdgeis ledaaveiyr tivrvasgek
      481 tkselhgiga leflpwpvga vl
//
LOCUS       WP_009574743             350 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Aequoribacter fuscus].
ACCESSION   WP_009574743
VERSION     WP_009574743.1
KEYWORDS    RefSeq.
SOURCE      Aequoribacter fuscus
  ORGANISM  Aequoribacter fuscus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Halieaceae; Aequoribacter.
REFERENCE   1  (residues 1 to 350)
  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 350)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 350)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 350)
  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   5  (residues 1 to 350)
  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   6  (residues 1 to 350)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Aequoribacter fuscus"
                     /db_xref="taxon:2518989"
     Protein         1..350
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39270
     Region          32..216
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          95..348
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mdvnlthydk nkpllmssei llgslevaee lglsvepslv laqidakqlk dpdqflplhc
       61 vvnflndmaq rsncehfgfl vglkqpptrf arigqlvkfa atlreaidda lrfsllnsqf
      121 srwelesdei yatlirrtrv aydepmiqlq tlaltvvyka mtglvggrdi glqqvsfsya
      181 phahkqrmea ffgcpvhfnq pfnaliftck alelpiptsd pkvyhlikaq lenlskglth
      241 qddlitrvih hiqqamgsry cslefisqtm gahpralqrq laeegvtfkq llnrvrqgla
      301 eeylinssis vaelssflgy rnpsafsraf kresglspdh wkasklaavs
//
LOCUS       WP_009574745             545 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Aequoribacter fuscus].
ACCESSION   WP_009574745
VERSION     WP_009574745.1
KEYWORDS    RefSeq.
SOURCE      Aequoribacter fuscus
  ORGANISM  Aequoribacter fuscus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Halieaceae; Aequoribacter.
REFERENCE   1  (residues 1 to 545)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Aequoribacter fuscus"
                     /db_xref="taxon:2518989"
     Protein         1..545
                     /product="amidohydrolase family protein"
                     /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=60190
     Region          63..521
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mklgkqllis lvaassmlah lsyaagaaqe geeiissila mgvpaptiap psgeeklgkf
       61 ehlvianamv idgtgappqg plsihiegdr ivnitgvgvs smhldgdqyg pdvkvidatg
      121 kyvlpgfids hvhygtpshi fggaltdsey vgklmlahgi ttlrdagglm glgwtlehkr
      181 laeegvissp diesyvvfpe tlndpdkard wvravkkrga dgikflgaap qaleaaitea
      241 kklgigamfh hsqiavtrwt vldsakagld smehwyslpe vmfeeqtvqh ypldynynne
      301 qhrfveagkl wrqsakrgsd kwletidqlm aydltlvptf siyeanrdfs rartlewhde
      361 ytmpymmraf dpnpkahgsy hfdwttqnev dwqenfrywm sfvndyknag grvaagsdng
      421 fiygtygfgy irelemlqea gfhplevvka atsvgaqllg lndtgtiekg kkadlvivse
      481 nplrnfkvly gtghyrynka lgrtervqai dytikdgivf dakilltqvr dlvqarkdle
      541 akaak
//
LOCUS       WP_009574894             332 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Aequoribacter fuscus].
ACCESSION   WP_009574894
VERSION     WP_009574894.1
KEYWORDS    RefSeq.
SOURCE      Aequoribacter fuscus
  ORGANISM  Aequoribacter fuscus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Halieaceae; Aequoribacter.
REFERENCE   1  (residues 1 to 332)
  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 332)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 332)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 332)
  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   5  (residues 1 to 332)
  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   6  (residues 1 to 332)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Aequoribacter fuscus"
                     /db_xref="taxon:2518989"
     Protein         1..332
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37579
     Region          23..202
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          93..332
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mlrklsisvd fvhatlanav aagldpnqll iknrisprll lepdarisme rfadlqthtm
       61 ramkdeslgy hvrplplgtw ammchatiga gtlleaverl cqfyqlfdfd ihcdtrsssk
      121 dtsitlrhls sapnrnfldh tflfnchryl swlgnafvpi hkvclqapqr fsqqdyhrmf
      181 lgatvsfaes stlvlsrkal lanieqtpls lrhysrhpnl imltqshaas gwagkvygil
      241 rrsidqppel ekvalelgih tqtlrrrlds egtsfseika fmrrdyalhl lgkqglsiee
      301 iayrtgfses safirafktw tgvtpytyrk gl
//
LOCUS       WP_009575290             169 aa            linear   BCT 20-JAN-2025
DEFINITION  YaaA family protein, partial [Aequoribacter fuscus].
ACCESSION   WP_009575290
VERSION     WP_009575290.1
KEYWORDS    RefSeq.
SOURCE      Aequoribacter fuscus
  ORGANISM  Aequoribacter fuscus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Halieaceae; Aequoribacter.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Prahlad,J., Yuan,Y., Lin,J., Chang,C.W., Iwata-Reuyl,D., Liu,Y., de
            Crecy-Lagard,V. and Wilson,M.A.
  TITLE     The DUF328 family member YaaA is a DNA-binding protein with a novel
            fold
  JOURNAL   J Biol Chem 295 (41), 14236-14247 (2020)
   PUBMED   32796037
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Liu,Y., Bauer,S.C. and Imlay,J.A.
  TITLE     The YaaA protein of the Escherichia coli OxyR regulon lessens
            hydrogen peroxide toxicity by diminishing the amount of
            intracellular unincorporated iron
  JOURNAL   J Bacteriol 193 (9), 2186-2196 (2011)
   PUBMED   21378183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006857
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Aequoribacter fuscus"
                     /db_xref="taxon:2518989"
     Protein         1..>169
                     /product="YaaA family protein"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
     Region          2..>169
                     /region_name="YaaA"
                     /note="DNA-binding protein YaaA associated with the
                     oxidative stress response [Replication, recombination and
                     repair]; COG3022"
                     /db_xref="CDD:442258"
ORIGIN      
        1 mlmvispakt ldfetpaatd tytqpiftey sealvdglra lapddiqnlm gvstaiaeln
       61 hkrfmdftlp fspdnakqal fafkgdvytg ldaeslspaa leyaqthlvm lsglygvlkp
      121 ldlmqpyrle mgtkfgvgea atlyqfwgdr itqalnaqlr aagaetlln
//
LOCUS       WP_009577377             153 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Aequoribacter fuscus].
ACCESSION   WP_009577377
VERSION     WP_009577377.1
KEYWORDS    RefSeq.
SOURCE      Aequoribacter fuscus
  ORGANISM  Aequoribacter fuscus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Halieaceae; Aequoribacter.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Aequoribacter fuscus"
                     /db_xref="taxon:2518989"
     Protein         1..153
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16497
     Region          5..148
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mftaqddlkl alrglldqey dvtansanfg sllyhslpdl nwvgfywlqd nelvlgafqg
       61 kpacvriplg rgvcgtaaat qepqivadvh afpghiacda dsrselvlpv ivnnsllgvl
      121 dldspianrf dsqtvtlvsd llsiwcahqy ani
//
LOCUS       WP_009577881             822 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Fulvivirga imtechensis].
ACCESSION   WP_009577881
VERSION     WP_009577881.1
KEYWORDS    RefSeq.
SOURCE      Fulvivirga imtechensis
  ORGANISM  Fulvivirga imtechensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Fulvivirgaceae; Fulvivirga.
REFERENCE   1  (residues 1 to 822)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..822
                     /organism="Fulvivirga imtechensis"
                     /db_xref="taxon:881893"
     Protein         1..822
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=93109
     Region          101..499
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 makksspksi aqyqhsdker annphigmvn eatetygkve kkiyqydphl dpqlqwagka
       61 ertsfevptv slhvheridp ktiieavkkd eeedsqlslf eqskkplrea iefykhkegw
      121 tnrlisgdsl lvmnslieke gmagkvqmvy fdppygiryg snfqpfvnkr dvrdgkdedl
      181 tqepemikaf rdtwelgihs ylsylrdrll lakellherg sifvqisden vhhvreimde
      241 vfgsenfvsm isyvtttgfk svtlsrsgdy iiwygkkkdt ikykqlflek tlgsqgatay
      301 kelenlpvan fqvkkfgakr lgtsadltsq gasstnqavv fngiehypps glhwkttveg
      361 mkrlidegrv fkvgntlryl rlyddfpvyp innfwsdtgv agftgekvyv vqttkkvier
      421 cllmttdpgd lvvditcgsg ttammaeewg rrwitcdtsr iaitltkqrl ltanfdyfkl
      481 arpteglsga feyktvphit lksiannepp geetlydqpk vdnsitrvtg pftvesipap
      541 fvknleeaid eqgeadnsva ksgetlrqdq wrdellrtgv rakggammef srieaqqgtk
      601 yiqalaetre enpknvlvvf gpehspmdar lvelaldeak ylkpdillfc afqfdeeaak
      661 didetpenli gfkllkaqmn mdlqtedlkk nrntnqsfwl igqpdvrina vegekvtvev
      721 agfdyynpkt gevnsggqkn iamwmldtdy dgrsifprqv ffpmagakeg wtklaktlka
      781 eideekieay rgtvslpfkp gkqiavkiid drgieslkvi kr
//
LOCUS       WP_009576756             314 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Aequoribacter fuscus].
ACCESSION   WP_009576756
VERSION     WP_009576756.1
KEYWORDS    RefSeq.
SOURCE      Aequoribacter fuscus
  ORGANISM  Aequoribacter fuscus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Halieaceae; Aequoribacter.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Aequoribacter fuscus"
                     /db_xref="taxon:2518989"
     Protein         1..314
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34944
     Region          19..271
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mvtqpltsdq vtapestmet lashgktfyw asffltrrqa kaaaelyacc ralddladsa
       61 tqskltkkqt lkalklaleh adqpthyplg ealrrltsqh qipatalasl ldglitdtes
      121 vaitskseld rycfrvagtv glmmcpilgv sderalpfai dlgiamqltn icrdvledae
      181 lgrrylpvdl tpvelrfase tikirvqhal adqlqraevf yqsglcglay lprrsrvaif
      241 iaahlyraig rklqdrrlaw wegrtviapm eklmltlkll ptllyvllqp kptrhkshlh
      301 anleglphvd hpqg
//
LOCUS       WP_009578628             112 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Fulvivirga imtechensis].
ACCESSION   WP_009578628
VERSION     WP_009578628.1
KEYWORDS    RefSeq.
SOURCE      Fulvivirga imtechensis
  ORGANISM  Fulvivirga imtechensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Fulvivirgaceae; Fulvivirga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Fulvivirga imtechensis"
                     /db_xref="taxon:881893"
     Protein         1..112
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12627
     Region          7..106
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(8..9,27..28,36,39,41..42,44,47..48,50,58,63,70)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(27,58..59,61,87)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 meqkhkdffd qvyqvvrlip kgcvtsygai anylgakgss rmvgwamnaa hdlddvpahr
       61 vvnrvglltg rhhftppdqm qhlleqegik vendrvknfk avfwdptvel el
//
LOCUS       WP_009579065             690 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Fulvivirga imtechensis].
ACCESSION   WP_009579065
VERSION     WP_009579065.1
KEYWORDS    RefSeq.
SOURCE      Fulvivirga imtechensis
  ORGANISM  Fulvivirga imtechensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Fulvivirgaceae; Fulvivirga.
REFERENCE   1  (residues 1 to 690)
  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   2  (residues 1 to 690)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Fulvivirga imtechensis"
                     /db_xref="taxon:881893"
     Protein         1..690
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=79378
     Region          57..119
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkftiilslc lllhislhgq rtadythlqd lvddiyaiqd tdlnyeelye slllyysspi
       61 dlnsvsaeel kalyilsdqq vnsfmnyrqq ygkllslyel qaiptfdlst iykltpfvrv
      121 aesginthnr pllkriwqep nnylllryer tledkkgyqk hedrsyykgn pdklytrfrt
      181 shindfsigi taekdagerl tydknshtyg adfysfhfql knkgelknlv igdyqiqsgq
      241 slllaagfnv gkgaetittl rrantgirpy ssvveggffr gaaatvalns rfqvtsyysr
      301 lredarlqsd tavsgadfis sihttgyhrt eteladkdqi vqqsfggifl ytnesgnlqi
      361 gatligdhls rplirpdkpy nrfrfagten yntglfysyg wrnfsffgem arsksggiga
      421 vtgfvssltp kleaavlirs ydrdfhslhg aafaesagqn qnemgwywgi kykpsrkysf
      481 tayfdqfkfp wlkyrvdaps agyeylmran ytpkrsvlly aqyrgeskgi npasedqlqv
      541 rtpfnglkrs ylanlrllad kkislqsrvq wssydfleqr thgflilqdl nldlkrlris
      601 trfalfdtdn yenkqyayer dvlyafslpp ysgrgtrqyl llqyrvtahi dvwakyarth
      661 yrdretigtg leeiagsvkt dvklqarirf
//
LOCUS       WP_009579665             747 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Fulvivirga
            imtechensis].
ACCESSION   WP_009579665
VERSION     WP_009579665.1
KEYWORDS    RefSeq.
SOURCE      Fulvivirga imtechensis
  ORGANISM  Fulvivirga imtechensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Fulvivirgaceae; Fulvivirga.
REFERENCE   1  (residues 1 to 747)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 747)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 747)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Fulvivirga imtechensis"
                     /db_xref="taxon:881893"
     Protein         1..747
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=83030
     Region          32..724
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 maklpvtvdk iiekfgphka yppqvgfhga hepdklvkth ccycgmqcgi qlkvkdnkia
       61 gfepwmefpf negrlcpkgi qrymqnnhpd rlmdplqrve gkgfepvswe hamsttvsei
      121 kriqntygnd afamlsgvsl tneksymigk farvalktan ldyngrlcmv sagggnkkaf
      181 gldrtsnswa dlkhaevilv aganisetfp tlthyiwqar dngaklivvd prviplarta
      241 dlhlavrpgg dsalfgamlk ilvdndwldh dfiknhtsgf qetieavkdy dlewaeettg
      301 ipkeqimeaa tlwgkaktsf llhargiehh skgvdnvlsc inlvlatgri gkpycgygti
      361 tgqgngqggr ehghkcdqlp gnrditnpeh rkyiagvwgi dekdmpgkgl tayeqieaih
      421 rgdikgmisi cfnplvslpn nnfvrealek lefyicidtf lsetarhadi imagslheee
      481 egtvttaegr vvkineaitp pgntrrdgqi lmelaarlgt gdkfsyntse difnelrvas
      541 kggtadyygi tykkvvdnmg vfwpcpsedh pgtprlwedr kfktpdgkah fnpvtykpaa
      601 ertdkefpvv lttgrvvsqy lsgtstrrig klvdqypepl leihpklayq ydikdrdlik
      661 vktrrgeasf paqlvetire dtvfipyhwg gkqsanqlti gtldpvskip efkvcacqli
      721 ptgekatvel tetayqsylp aensndk
//
LOCUS       WP_009579735             212 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Fulvivirga imtechensis].
ACCESSION   WP_009579735
VERSION     WP_009579735.1
KEYWORDS    RefSeq.
SOURCE      Fulvivirga imtechensis
  ORGANISM  Fulvivirga imtechensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Fulvivirgaceae; Fulvivirga.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Fulvivirga imtechensis"
                     /db_xref="taxon:881893"
     Protein         1..212
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23253
     Region          95..179
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 makakanyly llcflvcssa sstgavaqgc deadysstpg kevcyvasea speakekqlr
       61 aklkqiyssq vgvreeggan rgkmveqyla vtglgpsfpw caafvswcyi hagvdapvsa
      121 wvpsfaiqrn iiykrgkptk kipqtgdvfm iwydrlnrpa higfvdtwgn eyvitvegnt
      181 ndngsregdg vyrkkrlkrq vwavsdfvss ae
//
LOCUS       WP_009579838             257 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Fulvivirga
            imtechensis].
ACCESSION   WP_009579838
VERSION     WP_009579838.1
KEYWORDS    RefSeq.
SOURCE      Fulvivirga imtechensis
  ORGANISM  Fulvivirga imtechensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Fulvivirgaceae; Fulvivirga.
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
REFERENCE   2  (residues 1 to 257)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Fulvivirga imtechensis"
                     /db_xref="taxon:881893"
     Protein         1..257
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28750
     Region          4..109
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          <134..253
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtiqtytpsa glapfidryv viecseevsn rvfpgtslvv afrykghvsy tangvknvlt
       61 psvvtgmrks arlinyldgs gnvlvkfkea garafikepl helfedsisl mhltgysdts
      121 fieerladas cnyqrinlie sfltsklhhe qgdplimtal ahmraaggrv rirllaasln
      181 isldpfekrf rrvvgvspkq fsylikmqsv vrsrlkeksl aevaidagyf dqahfnkdfr
      241 lytgqtptef akapvyw
//
LOCUS       WP_009579883             357 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Fulvivirga imtechensis].
ACCESSION   WP_009579883
VERSION     WP_009579883.1
KEYWORDS    RefSeq.
SOURCE      Fulvivirga imtechensis
  ORGANISM  Fulvivirga imtechensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Fulvivirgaceae; Fulvivirga.
REFERENCE   1  (residues 1 to 357)
  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 357)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 357)
  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   4  (residues 1 to 357)
  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 357)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Fulvivirga imtechensis"
                     /db_xref="taxon:881893"
     Protein         1..357
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41454
     Region          98..348
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          265..347
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 meakasldtw tiiflvvgiq glflavmiym rrsgvnyllg sliltfslcl lyyvafwtry
       61 vqflpfhvgi tqgftylfgp laylyirsnk kelafnawhl lpyilfvvff fsrtylhpsl
      121 qtkaitiqvi iqnlhllsyt alifhwlqrq ktlqngmlkd flwkrkvawa ffgyalsflg
      181 yyllvwtstl kieydyaisf assffiyfig yqgfqhpdvl kvqetprydr stlsdsaars
      241 ilatikmhma tqkpyldsdl klqqlaeqls fsahhisqvi ndlekqnfsd finiyrvnaa
      301 rqmladptmc dkkiihvayd sgfnnkasfn nafkkftgqp pseyrnkqln pneahsn
//
LOCUS       WP_009580303             329 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Fulvivirga imtechensis].
ACCESSION   WP_009580303
VERSION     WP_009580303.1
KEYWORDS    RefSeq.
SOURCE      Fulvivirga imtechensis
  ORGANISM  Fulvivirga imtechensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Fulvivirgaceae; Fulvivirga.
REFERENCE   1  (residues 1 to 329)
  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 329)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 329)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 329)
  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   5  (residues 1 to 329)
  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   6  (residues 1 to 329)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Fulvivirga imtechensis"
                     /db_xref="taxon:881893"
     Protein         1..329
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36861
     Region          21..206
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <202..329
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mqepkkqlal gllayavqrd lpadrlcela eidypallts dttvsdiqig rlwkhastlt
       61 ddpyfglhfg eslqlaalgi vgeiikssdt vgegiktavs ltpgitdvvr talevaedsf
      121 tislitiqtt dessaflsrq iaemlmvfav heldglvlek icplsvtlpy pvseikeylr
      181 vlrctnykqa pnysltfdrk ywdlpllsan hemqafllkq vmetesqtpe glsariyqfl
      241 kahpylgmpt ldevasnfnt tprtlqrklk qegksfqeit neirkslaid yvvsdkyqik
      301 eiahllgyne vsafsrafkr wtgkapiey
//
LOCUS       WP_009580397             765 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Xanthomonas graminis].
ACCESSION   WP_009580397
VERSION     WP_009580397.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas graminis
  ORGANISM  Xanthomonas graminis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas; Xanthomonas
            translucens group.
REFERENCE   1  (residues 1 to 765)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..765
                     /organism="Xanthomonas graminis"
                     /db_xref="taxon:3390026"
     Protein         1..765
                     /product="TonB-dependent receptor family protein"
                     /function="Outer membrane receptor proteins mostly Fe
                     transport"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=83088
     Region          16..765
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mtrssttlrl halvlavasa lpafaalaet apadadatat agssdatmld aitvvstgtt
       61 rqvqritred igiaapgtsa lkvldklpgv qfqsadawgs yewstaitlh gfdqsrlgft
      121 ldgvplgtmn ygvsdglqvt raiisenvgs velsqgagal gtasssnlgg tvryysddpd
      181 atpgirfsqt fgsdstrrty lrgdigding fsmytsivhg evdkwkgygn neynqanvka
      241 lyqwgdgnrv slfldsskrk eydimdlslt sqkalgwdwd ylmpdwnsav qianalngng
      301 sypaslnalp adygkadaty ysgaglrddn laalsgafnl ggnatlnlag yyhdntgegq
      361 wttpylassa tvplsmrttd yrlnrhgvta slnftvagne ieiggwyqna ktvqernyfl
      421 ldgaftdlfy fnkagtrfer gfsqhyetdt rmfyaqdtlr llddrltvnv gakklqvdtt
      481 vqslvpspak aageleadsd llpqvgvnyk fdehqelyas ynknmagfdl spfdvgqntf
      541 daskqslqpe taqtyelgyr vrgagieasl alyhttfdnr llrtspcsai etcaarinnv
      601 gsvrsqgadl avmwrpiaql rwlnslsydd styqddylsg gvvatsgkrv vgipewmfss
      661 slayenagwh aaldgkytgr ryisylndss vpsywrfdls agydfgevgm fqnlglsanv
      721 tnlfdkryfa tvgtngyvvt dpngdnqtlm agaprqffvt fsgkf
//
LOCUS       WP_009580437             270 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Fulvivirga
            imtechensis].
ACCESSION   WP_009580437
VERSION     WP_009580437.1
KEYWORDS    RefSeq.
SOURCE      Fulvivirga imtechensis
  ORGANISM  Fulvivirga imtechensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Fulvivirgaceae; Fulvivirga.
REFERENCE   1  (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   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Fulvivirga imtechensis"
                     /db_xref="taxon:881893"
     Protein         1..270
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31476
     Region          196..270
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 msrinvifph eetsylktar psshlqpyvd hynevfldvp tgkaiwhtsi pvlnasicih
       61 ldgpgwsyvd psdretvldg sgllghsldv rksrhpggmr nffvslkpgf islllktqhr
      121 elenatvdin ylfknvfled qlrecesfee rvrwfesflt pfvlgrecny kfhivqeglv
      181 mfqretfqrg ehlhvicrel avsyptlyry fmevtgyspk fcqkllrfrk glekykaegy
      241 nfthwqygfa dfshfvkvtr qltgmapgef
//
LOCUS       WP_009581447             639 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Xanthomonas graminis].
ACCESSION   WP_009581447
VERSION     WP_009581447.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas graminis
  ORGANISM  Xanthomonas graminis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas; Xanthomonas
            translucens group.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 639)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 639)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 639)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 639)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 639)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Xanthomonas graminis"
                     /db_xref="taxon:3390026"
     Protein         1..639
                     /product="potassium transporter Kup"
                     /function="K+ transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=69498
     Region          1..639
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mssnhtstpa pcdgndaahg ktgfavvlga igvvfgdigt splytlkeaf sphygltpdh
       61 dtvlgilslv fwalmivvtl kyvaiimrad ndgeggimal talaqrtlpg gsrsvyvvgi
      121 lgifgaslff gdgvitpais vlsaveglev aaprlhsfvv pitvmvlvml fvaqrfgter
      181 vgkafgpitv lwflalgaig vynltkapev lhalnpwwgv rffaehnwha vfvlgavvla
      241 vtggealyad mghfgakair yswnflvlpm ltltylgqga lmlrdpaavr npfyesvpew
      301 glypmivlat aatviasqav itgaysvasq aiqlgyiprm hirhtshsti gqiyipgvnw
      361 mllalvimav lgfgnstala taygvsvtgt mlittvlmvi yaranprvpr vllwmmavvf
      421 vavdcaffya niikfmdgaw fplllglilf tlmrtwrrgr kllqgeirkd gikldtflpg
      481 lmlappvrvp gtavfltadp lvvphalmhn lkhnkvlher nvfltvetlp vpyatakqrl
      541 kmdaigdefy rvivrfgfme tpdvplalmr scdqggiyfd pmdttyfasr etivasanrg
      601 mpiwrdklfa vmhrnaapat gffripgnwl velgaqvei
//
LOCUS       WP_009581577              80 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Fulvivirga imtechensis].
ACCESSION   WP_009581577
VERSION     WP_009581577.1
KEYWORDS    RefSeq.
SOURCE      Fulvivirga imtechensis
  ORGANISM  Fulvivirga imtechensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Fulvivirgaceae; Fulvivirga.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 80)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 80)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 80)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Fulvivirga imtechensis"
                     /db_xref="taxon:881893"
     Protein         1..80
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8896
     Region          4..80
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mdlkillfgi trdiigdhsf tirlneggyv gdlkkylyae ypemkklrsl liavnneyap
       61 ddlrlsekde ialippvsgg
//
LOCUS       WP_009582164             392 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Fulvivirga
            imtechensis].
ACCESSION   WP_009582164
VERSION     WP_009582164.1
KEYWORDS    RefSeq.
SOURCE      Fulvivirga imtechensis
  ORGANISM  Fulvivirga imtechensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Fulvivirgaceae; Fulvivirga.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 392)
  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 392)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Fulvivirga imtechensis"
                     /db_xref="taxon:881893"
     Protein         1..392
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45949
     Region          3..373
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mkpkrtfska earniiihsq llsdekqqsr diirqlgyvq idtlavaera hhhvfharnt
       61 dyskdelatm lknrqvfeyw shaasylpmd dyryslirkr eyakgkshwf khdkkmtryv
      121 vkrikeegpl qskdfkdprn vsgawydwkp akialeqlfm egklmvaerv nfqkvydlte
      181 rvlppgints mptarefyey lirkalsahg laslaeisyl rkgireglqk aikklvrege
      241 vlpvkvegqd qmyytltntp epkcnkkvhi lspfdnlviq rkrtlelfdf dyqlecylpe
      301 kkrkfgyycl pllykdrlig kfdpkadrat giftirtfwl epdftpddif lnelaislkn
      361 fmafcgcykl evdtsitspv pqtvqqfvnd lq
//
LOCUS       WP_009581884             548 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Fulvivirga imtechensis].
ACCESSION   WP_009581884
VERSION     WP_009581884.1
KEYWORDS    RefSeq.
SOURCE      Fulvivirga imtechensis
  ORGANISM  Fulvivirga imtechensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Fulvivirgaceae; Fulvivirga.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 548)
  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   3  (residues 1 to 548)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Fulvivirga imtechensis"
                     /db_xref="taxon:881893"
     Protein         1..548
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=60861
     Region          6..544
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mndrekeyra iflaeaqqsy dqistdivkl erdpgneqvv aeifrllhnm kanagtmele
       61 aiaelahrle nvfsairngd itfegskvnl ifkavdylgy linniakprv qqhnnelldg
      121 lnevisgged rieglqsegg asvvsnklhl sdsvsislkk lddllnlvge liisrdhlis
      181 faeiienqqi kvitqslsrv adsiqetvmt arlvtvsslf nkfpriirdi aakekkvvnl
      241 vvegadttid rnvlkvisdi mihlirnait hgieapqdrk kqkkkeegsl kisassdkgl
      301 vfisisddgr glnpkaiksr avekkmitsa karsltdnea lgllfvpgfs madkvtefag
      361 rgvgldivks vidsiggdlk iesevgkgtn fimslpisma vkaallfkvg ennfalplln
      421 ihsvvtvsrr sihtiagvlt lerkdetiel iymndflfke eyqtsfinlk reimdivivw
      481 ynnkkygliv dqllrqqeim ikplqkpldn nhlfsgitll gsgevcyvld vanatkiyeq
      541 kesslqiy
//
LOCUS       WP_009583303             124 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Fulvivirga imtechensis].
ACCESSION   WP_009583303
VERSION     WP_009583303.1
KEYWORDS    RefSeq.
SOURCE      Fulvivirga imtechensis
  ORGANISM  Fulvivirga imtechensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Fulvivirgaceae; Fulvivirga.
REFERENCE   1  (residues 1 to 124)
  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 124)
  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   3  (residues 1 to 124)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Fulvivirga imtechensis"
                     /db_xref="taxon:881893"
     Protein         1..124
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14628
     Region          21..121
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mkdysffhna kpstfsnara lrnnmtaaek alwkslrrkq iaglrfrrqh pvgnfildfy
       61 chdiklaiev dgpihdrpeq keydqardqq irnkgiqmlr fsndevfdni qmvieeikrf
      121 iphp
//
LOCUS       WP_009583367             283 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Fulvivirga
            imtechensis].
ACCESSION   WP_009583367
VERSION     WP_009583367.1
KEYWORDS    RefSeq.
SOURCE      Fulvivirga imtechensis
  ORGANISM  Fulvivirga imtechensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Fulvivirgaceae; Fulvivirga.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Fulvivirga imtechensis"
                     /db_xref="taxon:881893"
     Protein         1..283
                     /product="formate/nitrite transporter family protein"
                     /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=31178
     Region          27..271
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mklqnifrsk pqkvedvsne pktvyhifre qintglavhn rssqglfass laaglevgft
       61 lflsgvlytl lhphiseyam hlviafaypi gfifviigrs elftehttla vipvlrgsas
      121 ikslarlwsi iyvgnliggy vmamilsglg ptmgiisdna fyhlahnmvk ynwlvilgss
      181 ilagwlmgql swlvtssqet isrilmivli tsliglgglh hsivgsievf agvitsriei
      241 vdyfhfqfwt tlgniiggvv fvsvikfsti kfsemkkkdk tle
//
LOCUS       WP_009584407             264 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: hydroxypyruvate isomerase family protein
            [Acinetobacter].
ACCESSION   WP_009584407
VERSION     WP_009584407.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..264
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29752
     Region          1..257
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mtklavnlsm iftevplier falahchgfq hveiqfpyel sieeiqaqle qydlhiclin
       61 apagdlmqgg nglagvpgke lefhqaleqa leyadalnvp ninilagkqp edadllpcln
      121 tlannlklac hmlseydiqp vfemingtdm prflvqniaq gqemleavqh palkmqfdcy
      181 hmammgedvl palqenidwi ghiqfadcpg rhepdtaqid yssifswlkq shytgfiaae
      241 ykpqshsnqs fawkekyfsn nhsy
//
LOCUS       WP_009584424             119 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acinetobacter bereziniae].
ACCESSION   WP_009584424
VERSION     WP_009584424.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter bereziniae
  ORGANISM  Acinetobacter bereziniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Acinetobacter bereziniae"
                     /db_xref="taxon:106648"
     Protein         1..119
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=12774
     Region          1..>69
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mmkknngfsl ieiiivvaim gilvaisypa ynnysrkakq taclseakay ansvfyiifv
       61 seantfpdsp kssacevitd asswndsttn lvieakskhs stvdircdls kgagctiih
//
LOCUS       WP_009586318             104 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Acinetobacter].
ACCESSION   WP_009586318
VERSION     WP_009586318.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..104
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11622
     Region          1..104
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(25..26,34,37,39..40,42,45..46,48,56,61)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(25,56..57,59)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mqnhelaqmi lnvivqipkg kvasygqvak faglpkharl vgrvlgqlpe dhdipwyrvv
       61 nsqgrislnk ldehgmciqt aklreeevvv vdgkinlkky qwap
//
LOCUS       WP_009586422             443 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [Acinetobacter].
ACCESSION   WP_009586422
VERSION     WP_009586422.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 443)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 443)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..443
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=51003
     Region          40..431
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mkkftiqalf dthwldiael kildpekgsa spceleyqie yaisyldkrd ehacslslpv
       61 qliikheakt wfgflddiip sgaarrywin ylnlqkfsha eqdsillekg viapvgnlri
      121 kesippinle stlhlrkfst advadrnadf leyaqqmgai sggatgagge apkllvryta
      181 dqkvwidtyq qsfdtpdqhy lvkfprnnrs eidcnilrae yyyyhelnel gfstidtanm
      241 rliegeryps lwlprfdtew cdqrwhrygl esvysilnks agshlnhfev idslcillkt
      301 idtkfnstqf vcewlerdll niifgnsdnh grntsflkkt gnvflspiyd fapmkadpeh
      361 virsttwgsp yeeggeyqwi qisqklapwc dpdisletlk slankllglk qrlidkgipk
      421 qiiempvlsf dyieaklkrw ell
//
LOCUS       WP_009589373             314 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Paenibacillus sp.
            HGF5].
ACCESSION   WP_009589373
VERSION     WP_009589373.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. HGF5
  ORGANISM  Paenibacillus sp. HGF5
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 314)
  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   2  (residues 1 to 314)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Paenibacillus sp. HGF5"
                     /db_xref="taxon:908341"
     Protein         1..314
                     /product="aminoglycoside 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=36166
     Region          24..235
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mdrlqgilke yyglghpviv pqqggwaala ykvsngaqdy flkvyeksra stpkwtalid
       61 dyvpillwle ehsrlkgsip vpmlttdqry rcednegiyl vyeyidgdti adrklmenqv
      121 rqlaeiiael hrygadfplv tsamtesfsv pflgqlreal dtkkpvdige vvnphidslk
      181 glmleveals eelkkrdlrl alchtdvhaw nlmsdgqqli lidweglkla pveadmmffv
      241 aepyfesfmr iykethsdye mnsealtfyq grrklediwe fmeqllcdvq ndeerastlh
      301 slkkelkeit isks
//
LOCUS       WP_009589495             266 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Paenibacillus sp.
            HGF5].
ACCESSION   WP_009589495
VERSION     WP_009589495.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. HGF5
  ORGANISM  Paenibacillus sp. HGF5
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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
REFERENCE   2  (residues 1 to 266)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Paenibacillus sp. HGF5"
                     /db_xref="taxon:908341"
     Protein         1..266
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31218
     Region          22..266
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          26..118
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
ORIGIN      
        1 miqhshqpsl gilnmkkage kfqllrvpps edlshfikhy wiihwdltdh eshlqdvvpn
       61 pcanlvvqpc rtafygvast rhshhlegrg qvfgvkfrpg gfypfmntsm drltdssigt
      121 meilqvephk leqelltaee pehkvrymee lirrilpeed eqierihami dqihhnrdii
      181 rveqvsewfq msprslqrlf kqyvgvspkw virlyrlqna aemlegldhq dvlelamdmg
      241 yydqshfird fkavigktpe vymker
//
LOCUS       WP_009593867             284 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Paenibacillus sp. HGF5].
ACCESSION   WP_009593867
VERSION     WP_009593867.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. HGF5
  ORGANISM  Paenibacillus sp. HGF5
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 284)
  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 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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Paenibacillus sp. HGF5"
                     /db_xref="taxon:908341"
     Protein         1..284
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32428
     Region          <78..279
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          197..275
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mpqidrhknr tvniefvaae dfahipyper ftlvfvtngc ikgifnerpv tisapailcl
       61 saedtiqvie khnasassfc fhpdflnstp hsetedyfps dlkiqtglsl frkspertgi
      121 pritekaypq lfewffvlgt evyaqsdalw acrikkyfiq ilgvledlnr hseqspvdlv
      181 leyihthysd kiiledltkc aylnrvslnk mfqercgcta mgyllshrlk vagnllthtd
      241 mslneiarat gfeydtyfik qfsakkgmsp ttyreisrkf saaq
//
LOCUS       WP_009595633             288 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Paenibacillus sp.
            HGF5].
ACCESSION   WP_009595633
VERSION     WP_009595633.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. HGF5
  ORGANISM  Paenibacillus sp. HGF5
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 288)
  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   2  (residues 1 to 288)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Paenibacillus sp. HGF5"
                     /db_xref="taxon:908341"
     Protein         1..288
                     /product="aminoglycoside 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=32727
     Region          34..243
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mnignplrei nwveksntle vllehegsfh avsldsglea evmkiaapta dyvlkvwnka
       61 skpnvhaqyq ilsalfthgs svsepvgwgt nrngdstllt sydgmpvqtv dpgklaklvq
      121 iladihklpl edfigdrlpr yefidyffpr ieehpdiril leellqradm kpsclihgdy
      181 hlgniletkd kltvidwtna qwgdprydva wsiiimwifa seeqadmyra accaeygyee
      241 hdlelfeaia clrgimlfka ndepighhii arfrsilskn eylndqll
//
LOCUS       WP_009595997             269 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Paenibacillus sp.
            HGF5].
ACCESSION   WP_009595997
VERSION     WP_009595997.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. HGF5
  ORGANISM  Paenibacillus sp. HGF5
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 269)
  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   2  (residues 1 to 269)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Paenibacillus sp. HGF5"
                     /db_xref="taxon:908341"
     Protein         1..269
                     /product="aminoglycoside 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=30037
     Region          40..183
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mnsdnppgqg edlilsaeks vvrrgqvvyr pcgewtpsvh sllrhlkqag ftslpdiigp
       61 gwneegqetl syvegefvhp gpwsdeaiva vgrllrqlhd asatfspgpk gvwkpwflre
      121 lgdsgvvysh gdiapwnmvt rdgmpyalid wefagpvhpl velarvcwlf sqlhdddvae
      181 rvglpdanar awqlrllvda ygvepslrtd lldmivevvv retaeeaieq qvspetegll
      241 wgiawrarsa awimrhrgil ekalntrfy
//
LOCUS       WP_009597645             100 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Alistipes].
ACCESSION   WP_009597645
VERSION     WP_009597645.1
KEYWORDS    RefSeq.
SOURCE      Alistipes
  ORGANISM  Alistipes
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Rikenellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Alistipes"
                     /db_xref="taxon:239759"
     Protein         1..100
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10930
     Region          2..96
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(7..8,26..27,35,38,40..41,43,46..47,49,55,60,67)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(26,55..56,58,79)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mrmpenfdae vyavvaeipa grvvsykqia rlvgmpdhar rvgralaeap aglpchrvvn
       61 sagrtvpgwt rqrelleaeg vrfktngcad larcgwmeir
//
LOCUS       WP_009597601             182 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Alistipes].
ACCESSION   WP_009597601
VERSION     WP_009597601.1
KEYWORDS    RefSeq.
SOURCE      Alistipes
  ORGANISM  Alistipes
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Rikenellaceae.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Alistipes"
                     /db_xref="taxon:239759"
     Protein         1..182
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=19267
     Region          1..182
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mkivvaitaa sggiyarltl erllrlsevs qialvcsara revlahedvv lpedgrirlf
       61 gnddlfappa sgsarydamv vvpstvgtvg rvaagaaqsl ieraadvmlk errrlvfvvr
      121 etplslihlr nmtalteaga vilpacpsfy agaqdvealc gtvadraval lgvdaehyew
      181 ge
//
LOCUS       WP_009597849             357 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Xanthomonas graminis].
ACCESSION   WP_009597849
VERSION     WP_009597849.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas graminis
  ORGANISM  Xanthomonas graminis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas; Xanthomonas
            translucens 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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Xanthomonas graminis"
                     /db_xref="taxon:3390026"
     Protein         1..357
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /function="Fucose 4-O-acetylase and related
                     acetyltransferases"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=39022
     Region          24..302
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 msaptqavqt vlaeqpartg vrgtrdarid aakalaillv vfghakgiph ayvilaysfh
       61 vpmffvlsgw vgeafgkrpl glatwtklar slllpylaff lvayaywmlt rhigskaqlw
      121 gdrpwwepll glvsgigpkl yvmpalwflp alfvttlsyl ylrrrlsldv lavlslllaw
      181 gwaiwfptqd yrlpfaldvl pvslcffalg aaaakrsgrl ptsrtgnava alllaaawfa
      241 iawnngrvdv nmmkfgyspl gflaasllgs amalcaarlv qewawvqwig rntllilcth
      301 tllfsvmagv asrtglvhgd awgpawavsv svfavlasvp mravivrvap wmigvrr
//
LOCUS       WP_009599821             153 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Vibrio caribbeanicus].
ACCESSION   WP_009599821
VERSION     WP_009599821.1
KEYWORDS    RefSeq.
SOURCE      Vibrio caribbeanicus
  ORGANISM  Vibrio caribbeanicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Vibrio caribbeanicus"
                     /db_xref="taxon:701175"
     Protein         1..153
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16850
     Region          5..153
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlaafndafq slalwfsdsa lwvlffsgfl satllpggse agllavlnlk qftplsvvlv
       61 atlgntlggm tnyglgwclp srldkesqan kalkwlnkyg ywslffswlp vigdplclaa
      121 gwlrmrfwqc lgiifigkal rysllaaify gff
//
LOCUS       WP_009600288             352 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio caribbeanicus].
ACCESSION   WP_009600288
VERSION     WP_009600288.1
KEYWORDS    RefSeq.
SOURCE      Vibrio caribbeanicus
  ORGANISM  Vibrio caribbeanicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 352)
  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 352)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 352)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 352)
  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   5  (residues 1 to 352)
  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   6  (residues 1 to 352)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Vibrio caribbeanicus"
                     /db_xref="taxon:701175"
     Protein         1..352
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39974
     Region          68..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <232..345
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 maldsdvwkl iaqyqpndsr hqlgtmdidl ckrcmedgsi dlrldasalf pskytghdkm
       61 tyadklfffr rfievvpttg vgllvgskat lsdfgilgya iinsrsteea vitgfkylnl
      121 ngpiftvklf ksknvtmlva envlqvddil pfcceyflsa lcslcdelsg epldikclsf
      181 pyskplyask ymasfncgdv rfdqpklimq fctsffsrsl kqsyvsvvdn ylyqcdrilq
      241 slqspytlpn qiksmlyqhv gyfpsfeyfa tqfgcstrtl rrqlvqcgtd yqsllsevrg
      301 diakeyllgt nltieeialr lgycdgssfr rkfkrlsgyt prayryvgkg lr
//
LOCUS       WP_009601218             260 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Xanthomonas graminis].
ACCESSION   WP_009601218
VERSION     WP_009601218.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas graminis
  ORGANISM  Xanthomonas graminis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas; Xanthomonas
            translucens group.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  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   3  (residues 1 to 260)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Xanthomonas graminis"
                     /db_xref="taxon:3390026"
     Protein         1..260
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28934
     Region          46..255
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 maegtnsdsp epsaheateq ddrflltnpr eilqllrsli nqrsqisahv dgrdqsfsta
       61 llelddhsvl ldlsvndann hsaeqaeyll cfaqvdkvrl rfrivgleri ahgdapgfra
      121 plpeslyylq rrehfrletp itespmcvlr lddaspptel vlrvidisgg glavalvpgq
      181 plpeerqsyp ccvlqlpdad airltlqvcn mypqklangq dtlriglrfa dlprgadaai
      241 qryifrierq rsarksgvls
//
LOCUS       WP_009601357             286 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Vibrio caribbeanicus].
ACCESSION   WP_009601357
VERSION     WP_009601357.1
KEYWORDS    RefSeq.
SOURCE      Vibrio caribbeanicus
  ORGANISM  Vibrio caribbeanicus
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Vibrio caribbeanicus"
                     /db_xref="taxon:701175"
     Protein         1..286
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=32587
     Region          30..191
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mlkqcvfstv rllgvgvatf alascssfsr vetpnqnkrv nsivvhftav dkketfrlfq
       61 detksvsahf vvteeriyqm adlsartyha gksywhgrhs lndtsigiei vqevncnqre
      121 egthkfppqv cvypdfspkl vnnilkaldk iyhyypdika vdvvghqdia plrkldpgpr
      181 fpwqylsqqg ygawyetady ldeyqklsdt tlsqtqflqa ltmygyqdve plyqafliga
      241 fqthftpdki tgtvtkesma ailallkkyy pekyeqitat fstene
//
LOCUS       WP_009607152             160 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Turicibacter].
ACCESSION   WP_009607152
VERSION     WP_009607152.1
KEYWORDS    RefSeq.
SOURCE      Turicibacter
  ORGANISM  Turicibacter
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Turicibacteraceae.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Turicibacter"
                     /db_xref="taxon:191303"
     Protein         1..160
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17613
     Region          8..159
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfqkeaytgt leenyelvla qlkaliages dlianlsnas allnvfleei nwvgfylvkn
       61 nqlvlgpfqg lpaciripfd kgvcgyvatt kqtalvqnvh efvghiacds atnseivvpi
      121 ikdnelmgvl didspllnrf sktdqhylek fvqilvesli
//
LOCUS       WP_009607434             194 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Turicibacter].
ACCESSION   WP_009607434
VERSION     WP_009607434.1
KEYWORDS    RefSeq.
SOURCE      Turicibacter
  ORGANISM  Turicibacter
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Turicibacteraceae.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Turicibacter"
                     /db_xref="taxon:191303"
     Protein         1..194
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21468
     Region          1..191
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mkkivvgitg asgsiyakrl ieelaskgyl vhviatdkgk qvfkyelsld lkqwiqelnq
       61 ptvklednhn lfagvasgsh gfdavivmpc smgtlaeish glsrnllcra advalkegrk
      121 liivpretpf ntihlenmch lskvgatiip ampgfyhhpq tledlvnfvv gkvlsylnin
      181 hnlfkkwedt nyed
//
LOCUS       WP_009607596             591 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Turicibacter sp.
            HGF1].
ACCESSION   WP_009607596
VERSION     WP_009607596.1
KEYWORDS    RefSeq.
SOURCE      Turicibacter sp. HGF1
  ORGANISM  Turicibacter sp. HGF1
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Turicibacteraceae; Turicibacter.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 591)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 591)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Turicibacter sp. HGF1"
                     /db_xref="taxon:910310"
     Protein         1..591
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=65911
     Region          3..572
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mminkrlisi ceeskkymfl tllcswigii cniaiifmmg lfinamvage tlskglshfy
       61 ltkhltlava ipliiillia kfiahhyygk fsykssakar stlrsliyek llrlgmdyqk
      121 sqptstivqi siegveqlei yfgkylpqff ysllapltlf vvistiswkv alvfiacvpl
      181 ipisiialmk vakrimkdyw nnyadlgdtf lenlqglttl kvygqddikh lemneeaekf
      241 rritmkllsm qlnsinimdl iafggsalgt ivalyqfqkg ainvgelivi illsseffip
      301 mrllgsyfhi amngmaasdr ifalldteev avknpcdfkk dssvkieven infsydgerq
      361 vlndisfdlt nggltaivge sgsgkstmat lligqkrpts grilingvdl tqlktealye
      421 hvslvsahsh ifkgsikenl lmakrdatse evnqtlkmar ldqfiaglpk gletevseng
      481 sslsggqkqr lalarvilan rdviifdeat snidveseea iwdaiyelsq qktilvishr
      541 lasvkrakai hvfklgtlve sgthdhlmsq ngvyahmves qqqlemirev e
//
LOCUS       WP_009607601             695 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: molybdopterin oxidoreductase family protein
            [Turicibacter].
ACCESSION   WP_009607601
VERSION     WP_009607601.1
KEYWORDS    RefSeq.
SOURCE      Turicibacter
  ORGANISM  Turicibacter
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Turicibacteraceae.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 695)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Turicibacter"
                     /db_xref="taxon:191303"
     Protein         1..695
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=77743
     Region          1..694
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mkkvqstcny cslacnidfm vedetikkvi ptkgypvnng fscikglnld kqhsiikpnp
       61 lprlkqedgs fkhvswdeaf qytaskltei sekygresva gistgqltle emalyghvmr
      121 nfmganvdgn trlcmatsvv ahkqsfgfda ppytlndfel sdtiiligan pvvahpiiwg
      181 rikankipgk kvividprns etakradyfy rlkaksdltl mytlantlie kgwideayie
      241 ahtenfeafk efvkdytldq veekthitaq qvlelatmih egknvslwwt mginqgyeav
      301 rnaqaiinia lmtgnigrpg tgansitgqs namgsrlfsn taglygggdy dnpvrraava
      361 nalgieesll ptkptlpyna iiekinagei kalwilctnp rhswinnetf keameklelf
      421 ivqdiyddte ssencdvffp vvsglkkegt iinterrlsa vrpalqmeen emndfnviln
      481 vgkalgmgsl ldawqtprdv fnlmkkcskg mpcditgvdy dglvdskgiq wpfkegdvlt
      541 edqrrlyedg qfytpskkak fmfenpmdnp lklsedfpyi lntgrgtvgq whtqsrtrei
      601 pyvndavshq ayihinekla kelgienqei ievssingvs kqfmamisdt vaydelfapi
      661 hyietnaltp slydsyskep sykstpvqik kvkga
//
LOCUS       WP_009607876             552 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase family protein [Eggerthella].
ACCESSION   WP_009607876
VERSION     WP_009607876.1
KEYWORDS    RefSeq.
SOURCE      Eggerthella
  ORGANISM  Eggerthella
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae.
REFERENCE   1  (residues 1 to 552)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Eggerthella"
                     /db_xref="taxon:84111"
     Protein         1..552
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=58862
     Region          85..>264
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
     Region          283..391
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          423..549
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mtpehetrgk heaqqpapqp aprpapqrtr ridsidppfa dgapesyasf vpasrggrpg
       61 pvhggrpesp gggrqgssnr kppfakkagl iaggalvavi aivylagalv fmdrfmpntt
      121 imgkdvslkt taevqdlltd vaksyqlsvs gerfsltlts sdmgtavnss svtdamhada
      181 spwawpvevf vvhdetdklv tsngkldeav rkaveafneq aeaprnagld ydsggsrfvv
      241 raetvgtald adkvaetvna avaamgssat lsedalqqpt llsdderlak aadeannllk
      301 adfslklgdt pvaqvnadai agwvrlhddv tvgvdeglva awvqdlasac ntyqarrtft
      361 radgkevtvs ggvygwiidk gklqeavtng vgsaqtgdma ipceqeagay dglhgrdwgk
      421 ryvdvdlteq harfyddegs lawesdvvtg tpdgehdtpe gvyvingkes pskligqmkp
      481 etgepeyqte vkawmpfvdn yigfhdadwq pafgdsryks gygshgcvnl ppekavelyd
      541 likvgdvvvs hw
//
LOCUS       WP_009607891             370 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Eggerthella].
ACCESSION   WP_009607891
VERSION     WP_009607891.1
KEYWORDS    RefSeq.
SOURCE      Eggerthella
  ORGANISM  Eggerthella
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Eggerthella"
                     /db_xref="taxon:84111"
     Protein         1..370
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=40842
     Region          1..367
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mslevnirks fssftldvaf eagdetlgfl gasgcgkslt mrciagietp degrivvndr
       61 vffdserkin ltpqqrktal lfqsymlfpn ltvaenvaag igreaskadr dalvaaelkr
      121 fglegfdrry paqlsggqqq rvalarmlaa rpgilmldep fsaldahlks vleqnlvslf
      181 dafhgtvlyv shdidealrf cdriavveag ritetgtgdd lvnrpqslag vklsgcknat
      241 aavragersv rlpkwgieaa tsaavpedvk algvrafflq rvdgpgency rvrvdrvsds
      301 rfertvllgf ldrdeseapt vsrtddemky lhqhlfwrvd klavpvdelp hegeelwiri
      361 ppdkvylvsr
//
LOCUS       WP_009609748             594 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Caldanaerobacter
            subterraneus].
ACCESSION   WP_009609748
VERSION     WP_009609748.1
KEYWORDS    RefSeq.
SOURCE      Caldanaerobacter subterraneus
  ORGANISM  Caldanaerobacter subterraneus
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Caldanaerobacter.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Caldanaerobacter subterraneus"
                     /db_xref="taxon:911092"
     Protein         1..594
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=66252
     Region          29..591
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mkkkentsvl tglidmispq alefnarqiv fndqlarilv iagyppkvna awlsriagmp
       61 gvvcsvhiep tdptdlinsl nkaigeyagr lemggnaltm qrteqalkda eelmrkidqe
      121 qqqvfyvtvv lmvlasdqqe ldrrtrqvea alaasgmrgr vlifrqeegl kavgpfctlp
      181 devkeagarn mpaetvaasf pftasgindg tgvvlgkdrd gglvlvdiwk rggdrtnsnw
      241 tilakpgagk sftakmlllr eymqgsriii idpereykdm chrlggvwin ctggegkinp
      301 lqvrlrpvee eeeengrlqs plalhiqtlr tffslylkdl tdtekaaled alvevykeag
      361 itwdtdprdv pnekwptvre lykylvkkae enpetytrla vllkraaega dsylwagpta
      421 veadsdfivf dvhdlqnaed qvkraqyfnv lsfawniler drrertvlvv deawmlvdpq
      481 tpqaiaflrd tskrirkyng slivisqnvi dflapevqry gqalldnpty klllaqgekd
      541 leaitalmnl seaehdllan akrgeglfva gtqrihikie aapyelqylt gggs
//
LOCUS       WP_009613942             338 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_009613942
VERSION     WP_009613942.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  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   4  (residues 1 to 338)
  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 338)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37571
     Region          29..212
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          258..337
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msavqlpeqr tlttlhtvvl atevlsqagi prgrllegsg iaeadlltpe kfvshaqelr
       61 vfanalscyq dpalglylgl rmhvsaygml gysmlasrtl rdalqlalah pdllgtyfrl
      121 alqdhgdevw lsaegyryap eltvfntelc ltslltvvrd llgesvrprr lllayrpplh
      181 agtyserlgc pvefgaatsa lclgpalldr alpladpvsc hnglqqcqrl saamsgrddi
      241 lelirrhlan hlqearglde varhlhrssr tlrrhlqqhn tsyqqvldev rydkarqllk
      301 dtdlpiylia erlgysetas frhafqrwsg aspslyrg
//
LOCUS       WP_009614022             329 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Pseudomonas].
ACCESSION   WP_009614022
VERSION     WP_009614022.1
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 11438136
            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="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=36972
     Region          1..322
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msieirnvsk nfnafkaldd inldihsgel vallgpsgcg kttllriiag letpdvgniv
       61 fhgedvsqhd vrdrnvgfvf qhyalfrhmt vfdnvafglr mkakkerpse ariaekvhel
      121 lnmvqldwla drypeqlsgg qrqrialara lavepkilll depfgaldak vrkelrrwla
      181 rlheeinlts vfvthdqeea mevadrivvm nkgvieqigs pgevyenpas dfvyhflgds
      241 nrlhlgndeh llfrphevsl srqaveahra aevrdirplg aitrvtlkvd gqdelieaev
      301 vkdhdslvgl argetlyfkp kayqqvani
//
LOCUS       WP_009614050             349 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_009614050
VERSION     WP_009614050.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 349)
  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 349)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 349)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 349)
  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   5  (residues 1 to 349)
  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   6  (residues 1 to 349)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..349
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38495
     Region          27..214
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          117..347
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mqapvplags isiayvqglv dhlerrgvap qrllagvqle psildqrear iaasvyvdll
       61 elglalsgda dlglhlgeav rpghfgvlgy llmscatlgd alhrqaryae lvgslgrvel
      121 adeppraghe plvrhswepl lprqqrqlae etlacwlrfg hwisgleqap vevrfrhpap
      181 adttehrrif rcpvlfgqad nalvfprrll alplgqadsq iqrtldayag rllesirrge
      241 gvlerarqcl aerlpeqavd lealagelal sprtlqrrlr dsglsfsrlv detrqqlvlh
      301 hlrdpalela dvaslvgfse tgslarafrr wtgqslgqyr rtlqplads
//
LOCUS       WP_009614820             696 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate--CoA ligase family protein [unclassified
            Pseudomonas].
ACCESSION   WP_009614820
VERSION     WP_009614820.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 696)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 696)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..696
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72954
     Region          1..696
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mntenlkrll aprhlafigg rsmaralkrc aeggfagplw lvnpqydele gvpcvrsvae
       61 lpegpdavfi atnrdltlna vaelaakgag gaicyasgfa etgaegqalq qclldvagdm
      121 allgpncygl ldylhgaalw pvahgghive kgvavltqsg nfaynlsmsd rslpiaymas
      181 vgnqaqlgva elmdvlldep rvtaiglhle glknvpgfar aaykalqkgi pvialktgvs
      241 qigaelalsh tsslagsdal ydalferlgv irvsgpvsfi etlkaaacgn lpagpslaal
      301 acsggdagli adyaernglp lprlvdaqra elaqvlpdya nianpldftt aiwgdgpale
      361 kmldsalrtp adaallvldy pgeetgerpq cdlllelyca alkrhdkvgf iasalpellp
      421 aharellhgh gvaalqgved glaawgriah yrqrrdalla rgeaalvplc pqaidgqgrl
      481 ldewqskqvl kpfglplpaa vlstpgqare aaadlgyplv lkavsaelph kteaggvaln
      541 lrneaaleaa lfdmrenlak hapqlkfeqv llermasppl aelivgikre vgfglalvlg
      601 aggilvellk dsrslllptt daairdallg lrsapllsgf rgrpavdmdk lvdairavad
      661 yacehadsll eldvnpllvn aegavavdal irlada
//
LOCUS       WP_009616026             338 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Pseudomonas].
ACCESSION   WP_009616026
VERSION     WP_009616026.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  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   4  (residues 1 to 338)
  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 338)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37564
     Region          28..211
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          255..336
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkqplnftae lvpvayaqal ldlaeelgvp rqrllelarv rpevlqspag rlsfvdfnll
       61 agaalancge pafglllgqr lnvsthgilg yavlssanle kaidfalkyy rvlglaydle
      121 rveeqdrsql rasesiplgp mqrfageglm tslytiarfl vgeplqgvev gfafpappya
      181 erytevfgva aafdqpfhfi slpreylnrp malanpatvq mceqqceall asldvqegll
      241 trirrlllar pgefpdldta arelhtsgrs lrrhlsslgt tyqqvlddvr krlalqyltt
      301 thlplyeial llgfndpsnf rrafrkwtgk lptdyrad
//
LOCUS       WP_009617648             398 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [unclassified Pseudomonas].
ACCESSION   WP_009617648
VERSION     WP_009617648.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 398)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..398
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43656
     Region          4..388
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mpatlkvstp egpsgrlfss addylfryqe gtdaraavsl lmpvrleeyr hrelhpifqm
       61 nlpegyvleq lrnrlaklvn vdpmlllals gssapigrvl vnsqevdall qrrqfpgekl
      121 eeilawdgtd difaelvdry ilragisgvq pkvlvpehrd slpqrftskt sdliiksgra
      181 elpglainef lcmsmakacg vpvpefylsd narlfvmrrf drdaqldpig fedmaalmgl
      241 saqqkysksy aaiakairlf cppehvpasl eqlfgivsls civgngdahl knfgllysdp
      301 tqgdarlapa ydivnttayi pedvlaldla gnkslfasrq glldlarvcd varpaevira
      361 qlqavekvla nhpglceqap qvvaairhsa epfartfg
//
LOCUS       WP_009617856             104 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Desulfosporosinus sp. OT].
ACCESSION   WP_009617856
VERSION     WP_009617856.1
KEYWORDS    RefSeq.
SOURCE      Desulfosporosinus sp. OT
  ORGANISM  Desulfosporosinus sp. OT
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfitobacteriaceae; Desulfosporosinus.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Desulfosporosinus sp. OT"
                     /db_xref="taxon:913865"
     Protein         1..104
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=11441
     Region          <3..67
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mlhdqrisqg ffwdhgiaaq sillgateqg lggcqfnain rvglaqelsl pdylviatvi
       61 algkpkemvv iekldesgdv kywrdqqgvh hvpkraledl iysl
//
LOCUS       WP_009618168             632 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase [unclassified
            Pseudomonas].
ACCESSION   WP_009618168
VERSION     WP_009618168.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..632
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=70163
     Region          63..502
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mqkidatspe aqsadlvasn ieqlkalfpe litegqngta vnvdvlkalv gdatvtdade
       61 kyglnwhgkr rarqlaltps tgtlrpcpee svdwdstqnl miegdnlevl kllqksyagk
      121 vkliyidppy ntgkdfvypd nfqdniknyl eltgqveggq kissnteasg rfhtdwlnmi
      181 yprlklahsl lrnegvifvs iadheihnlr avmnevfgee nfvaaviwqk vfspknsarh
      241 fsedhdyivv yaknaevwtp rllprteeme aryanpddda rgpwtsgdls arnfygegty
      301 avtcpsgrvi dgpppgtywr vskakfdeld adkriwwgad gnnmprlkrf lsevksgrvp
      361 qtlwtydevg htqeakkell aavtfpnsdv vfdtpkptrl mrrilqlata pdsadlvvdf
      421 fagtgttmda vfaqnaedgg krrcilvqlp epldgaaasg wktiadvtra rirsagkrhr
      481 eadplftgdv gfrvfkldts nirawnpnpa dleqtlfahr dhlvdgrtes dilyelllkl
      541 gldlcvpiek rsihgkdvhs vgggvlmacl aehitrddve plaqgivawh eelqpagdtt
      601 cvfrdsafad dvaktnlaai leqhgiqnvr sl
//
LOCUS       WP_009618356             190 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Desulfosporosinus sp.
            OT].
ACCESSION   WP_009618356
VERSION     WP_009618356.1
KEYWORDS    RefSeq.
SOURCE      Desulfosporosinus sp. OT
  ORGANISM  Desulfosporosinus sp. OT
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfitobacteriaceae; Desulfosporosinus.
REFERENCE   1  (residues 1 to 190)
  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 190)
  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   3  (residues 1 to 190)
  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   4  (residues 1 to 190)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 190)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 190)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Desulfosporosinus sp. OT"
                     /db_xref="taxon:913865"
     Protein         1..190
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=20964
     Region          1..189
                     /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"
ORIGIN      
        1 msslsiliad dealirldik emlqgaghiv cgeanngeka vdlakslapd laiidvmmpg
       61 ldgleaakil hsmnipvlll taysqpkfin raekvsvygy lvkpiterdl lpaiqiayar
      121 wremqevrak lkntqhelqs qkmiararai lakregvsdy eahqllihqa mdlritvvkl
      181 anrlvngatf
//
LOCUS       WP_009619087             246 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Pseudomonas].
ACCESSION   WP_009619087
VERSION     WP_009619087.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 246)
  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 10614777
            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="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=26689
     Region          46..211
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mpsistvwgk lrpllavgal yalgsslaqa alpsaeelhr lapatnlqal rlalsayqca
       61 naaqlggrde lltvidyska srdkrlwvfd lqrrkllfee wvahgknsgd dlatsfsnrp
      121 nsyqssigly qtgqtyrgkh grslrllgle pgfndnseer aivmhaaaya dprvvpglgr
      181 lgrsqgcpav rpqvaqklid tlqkgsyvfa yypqqewlsn sqflagascs vakaqnlgrs
      241 atlakr
//
LOCUS       WP_009619132             715 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate--CoA ligase family protein [unclassified
            Pseudomonas].
ACCESSION   WP_009619132
VERSION     WP_009619132.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 715)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..715
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=74657
     Region          15..713
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 msvshsqhpg nasrfasltp llqprsvavv gassdphrig grpiaymlrn gfggrilpvn
       61 pnrseiqglp afasvealpe apdvaivalp apqvletiqa lgrkgarsai vfssgfsevg
      121 gegvlmqeam veaaraanmr llgpnalgvf nanlgyyaff stslergipl agrvgiatqs
      181 gaygahllgl arqrglgtpi cvatgneadv tlgdaigwlv espevdvvma yaesirnvds
      241 flaalaaahr agkpvilhkv grselggraa mshtaslagd dkvldavlad yavvrarnte
      301 elidiaylat qriypvansl gmitvsggag iivsdaaedv glpmppmpea aqarlkqrls
      361 faspinpvdc taqalndlsl vhdftesmvv dggyksliaf ftqagtvasi gpklaeqfgr
      421 ikadhpdrlf vvsvmgegde lepyrkagfa lfedptravh aiqamgrlge afarplrqvp
      481 avggvelppr tpgeaeakql laragiesap ervlvsaaea aafaeqigfp vvlkiasadi
      541 lhkseiggvl lgvdsaaavr egfdlllqra aehapqarid gvlvarqlqg gvecfmgiqr
      601 dplfgpvalf glggifvevl kdvvfrrcpf gaeeaeamir sikgaplllg argrpvtdvk
      661 alaqvlsrls qfaaqagprl rsvdlnpvfa mpegqgawaa davlevqeva dgaes
//
LOCUS       WP_009619380              99 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein, partial
            [Desulfosporosinus sp. OT].
ACCESSION   WP_009619380
VERSION     WP_009619380.1
KEYWORDS    RefSeq.
SOURCE      Desulfosporosinus sp. OT
  ORGANISM  Desulfosporosinus sp. OT
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfitobacteriaceae; Desulfosporosinus.
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   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 99)
  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 99)
  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 99)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Desulfosporosinus sp. OT"
                     /db_xref="taxon:913865"
     Protein         <1..99
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          11..97
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(29,48..49,67,70,78..79,90,95)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 qtdllehrga ilntsdaslt yndikvelsk ndykilkmll enkgkavgre aimarlwetd
       61 syidentltv nmtrlrkkle aaglagfivt kkgigymvt
//
LOCUS       WP_009619951             272 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Desulfosporosinus sp.
            OT].
ACCESSION   WP_009619951
VERSION     WP_009619951.1
KEYWORDS    RefSeq.
SOURCE      Desulfosporosinus sp. OT
  ORGANISM  Desulfosporosinus sp. OT
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfitobacteriaceae; Desulfosporosinus.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Desulfosporosinus sp. OT"
                     /db_xref="taxon:913865"
     Protein         1..272
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31506
     Region          <44..103
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          179..258
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mkpvqpyfvf atyqyhkriv msngiahlyh ycyncdefgn isaipdgcvd iyfekdssgv
       61 hpracgtvlk rtlinnqkeh eyfgirfmpg vlpanlkvqm kdligletdl iyllknkdlv
      121 krieetqdwq qcirlfledy saslnevscf ssgnsrqqla gylkdtiist mgcikiqels
      181 ektgysaryi nmlfeqyigl spktferilk fqnainllnh hqeghltqvg meagyfdqah
      241 firefkkhta mtpaeyrkli rehsylqrls id
//
LOCUS       WP_009620229             746 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Pseudomonas].
ACCESSION   WP_009620229
VERSION     WP_009620229.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 746)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 746)
  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   3  (residues 1 to 746)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..746
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..746
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=80459
     Region          8..711
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          <263..>327
                     /region_name="nfrB"
                     /note="phage adsorption protein NrfB; PRK11234"
                     /db_xref="CDD:236884"
ORIGIN      
        1 mldgeqwsel lrgfieeard larqaeecll elernpadge aitrlframh tlkgsaglfs
       61 llplvnfthh lenllmavrd geraltaelv slmlrcldei tsmvalidpa sgelpvdaah
      121 qrelldalaa ltgnepelip tqaidcparg rldacascea qgawhislrf dgellrngfd
      181 patfvrylgr lgevlclhli ddavpaleel daercylgle ialctsaera aieeafefir
      241 dfcslrllpp gsqvddylal mrelpesder igailvasgl ldeqdlargl alqaqhsdal
      301 kpalgsvlvd qglvpaqavn aalaqqqkar erapesslir vaahkldeli nlvgelvisa
      361 aaaqlharas gdsassesaq tvnrhvelir eaalklrmve igetfsrfhr vvrdvsqqld
      421 krirleihga dteldksvid kladplthlv rnamdhgiep agqrieagka pegllrlnaf
      481 hesgtvviev sddgrgldtr rirakaverg lieagatlge qelqrlifaa gfstadsvsd
      541 lsgrgvgmdv vrsaiealrg sieidsragq gstfrirlpl tlaiidgfqv slgdeqfvvp
      601 lglvtecmel pphagdgacg yidlrgrplp cidlaahfgl pgsrggrrni vvvshgrqqa
      661 glvvdhlhge lqtvikplgp lfqhlqgiag stilgsgqva lildiatlfa sldeqpthhp
      721 vdsdpqqshr hpqaagaqet pheihp
//
LOCUS       WP_009620816             249 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [unclassified Pseudomonas].
ACCESSION   WP_009620816
VERSION     WP_009620816.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  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   3  (residues 1 to 249)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..249
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28467
     Region          37..242
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 maspfaeeng pqppktlkaa veiqanlril mdshdplvis faernqrfqs fvvavdrern
       61 rvaldelipn dgerflqnge nfrieafheg vriawecqqa aqfseldgar cywlpmpaem
      121 lyhqrrnayr aplkqtqpva velagdklka alsgnlldis atgckvrfag dvherlqpgq
      181 lyerftarlp fgaitvevel rhvhfdekvn asfaglrfnc lsgleqrhie rfvyqlqrea
      241 rrfekdelf
//
LOCUS       WP_009621882             321 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Pseudomonas].
ACCESSION   WP_009621882
VERSION     WP_009621882.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 321)
  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 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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..321
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35281
     Region          27..196
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          236..317
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpnspsitvh yaqgilqaat rlglqlpadl relgrqarip larqdelweg lcaasadpll
       61 glrlgsalqv ghldmvgall mscesfgeal ealleyypii aegsefalrr eaggvalvyr
      121 psyrvrrear veavlaslvr lsawitgerv hplalrmdhs argeagryre llgllpdfsa
      181 gedgllfaen dlqvpliqan apmrehlrql adaqlqrlga qslaaqvqgl lrehpqwgke
      241 riaerlglsg rhlnrrlaee gssfkllrer vlhamaeqll hgparlaeva erlgfsdesa
      301 fakafrrwsg mtpgqfrqga d
//
LOCUS       WP_009623995             738 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Desulfosporosinus sp. OT].
ACCESSION   WP_009623995
VERSION     WP_009623995.1
KEYWORDS    RefSeq.
SOURCE      Desulfosporosinus sp. OT
  ORGANISM  Desulfosporosinus sp. OT
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfitobacteriaceae; Desulfosporosinus.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 738)
  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   3  (residues 1 to 738)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Desulfosporosinus sp. OT"
                     /db_xref="taxon:913865"
     Protein         1..738
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79943
     Region          12..738
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          185..263
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 msqdddknqg vdlgeflefy lldsqeqiek lgagllqlek eggniglind lfrsahslkg
       61 asgtmgftpi vamthaaedl ldrlrqgkid vslemidill avtdrvkaml sqveqrleit
      121 lgyedlvssm kdlisgeksa aqtslqpvpg neqaleddfv plnfsldqpe sakinnahmm
      181 gygiyqvdvk lapntlmkav ravmatqrle gmgtviklfp siedleagnd egfsllvlcd
      241 epieemrrel leiselvdvv ihpypdgigg tektahttkd taevletiis elettpsiss
      301 kavtqakslk tipsqkamve pkgigsdsav ltdgiangeg ntqvhtirvd tvrmdnlinl
      361 vgemvitrtr lvqigldlka qyqtdnmvns lneanvylgr lmndlqesvm rlrmvaigtv
      421 fsrfprlvrd lakktgkeie lvlkgedtel dktvvevigd plmhlirnsv dhgiespeer
      481 raagkpelgt vtldayhegn hiailisddg aglpldkirn iavskglige reelserdia
      541 nliflpgfst aekvtdisgr gvgmdvvkka lnnlggmvdi ttrqglgttf tirlpltlai
      601 iqallvevge eiyavplssv letllvnrtd iktvgrlpmv qlrgntlpli slqekfglpa
      661 penessevfv vvvgfgdkal glivdelrgq qevvikslgd ilsnlpgiag atilgdgkvt
      721 lildigsliq dvlvtrks
//
LOCUS       WP_009624761              84 aa            linear   BCT 20-JAN-2025
DEFINITION  acyl carrier protein [Desulfosporosinus sp. OT].
ACCESSION   WP_009624761
VERSION     WP_009624761.1
KEYWORDS    RefSeq.
SOURCE      Desulfosporosinus sp. OT
  ORGANISM  Desulfosporosinus sp. OT
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Desulfitobacteriaceae; Desulfosporosinus.
REFERENCE   1  (residues 1 to 84)
  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 84)
  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 84)
  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   4  (residues 1 to 84)
  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 10011594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Desulfosporosinus sp. OT"
                     /db_xref="taxon:913865"
     Protein         1..84
                     /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=9438
     Region          1..71
                     /region_name="acpP"
                     /note="acyl carrier protein; Provisional; PRK00982"
                     /db_xref="CDD:179197"
ORIGIN      
        1 mmlarikvii dqqfiyegel neqtriiddl gadsfdipvm vnaledefev tisdeeliki
       61 rtigdlikii qdskrlgein sgtk
//
LOCUS       WP_009626421             445 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Pseudanabaena].
ACCESSION   WP_009626421
VERSION     WP_009626421.1
KEYWORDS    RefSeq.
SOURCE      Pseudanabaena
  ORGANISM  Pseudanabaena
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Pseudanabaenales; Pseudanabaenaceae.
REFERENCE   1  (residues 1 to 445)
  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 445)
  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 445)
  AUTHORS   ter Beek,J., 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 445)
  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 445)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Pseudanabaena"
                     /db_xref="taxon:1152"
     Protein         1..445
                     /product="CmpA/NrtA family 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=48407
     Region          56..316
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mstfsrrkfl ttaglstvsa ialnactgge apktettsaa spsaskspta svsaagapev
       61 tkaklgfial tdaapliiak ekglfekygm kdvevlkqas wgttrdnial gsdaggidga
      121 hilspmpyll tegkitngkk vpmyilarln tngqamsian dfkelkitlk sdslkdsftk
      181 iksggkeikc avtfpggnhd lwmrywlaan gidpdkdvst ivvpppqmva nmkagnmqaf
      241 cvgepwnarl vaqnsgytaf itgefwkdhp ekaftmradw vdknpkaaka ilaavleaqv
      301 wceqaankee mckivgadkw lkvppaeilg rlqgkvdygd grtldnpdla mkfwkdsasy
      361 pykshdiwfv tedmrwgyld aetdakklvd kvnredlwke aakmigkead ipkstsrgve
      421 tffdgvkfdp enpseylkgl kikka
//
LOCUS       WP_009626568             106 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Pseudanabaena].
ACCESSION   WP_009626568
VERSION     WP_009626568.1
KEYWORDS    RefSeq.
SOURCE      Pseudanabaena
  ORGANISM  Pseudanabaena
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Pseudanabaenales; Pseudanabaenaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Pseudanabaena"
                     /db_xref="taxon:1152"
     Protein         1..106
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11970
     Region          1..104
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(7,25..26,34,37,39..40,42,45..46,48,55,60,69)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(25,55..56,58,85)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mnsrtaydri yeivqkiprg qvatygqiae lsnlagkarl vgyalfrvqn advpwqrvin
       61 akgeislspl rmgtdylqrs llesegiifs dtgkidlrky qwrpqp
//
LOCUS       WP_009628942             120 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Pseudanabaena].
ACCESSION   WP_009628942
VERSION     WP_009628942.1
KEYWORDS    RefSeq.
SOURCE      Pseudanabaena
  ORGANISM  Pseudanabaena
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Pseudanabaenales; Pseudanabaenaceae.
REFERENCE   1  (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   2  (residues 1 to 120)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Pseudanabaena"
                     /db_xref="taxon:1152"
     Protein         1..120
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12697
     Region          47..116
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mlnklsrgll krevpmliag lltvtscaea pkqannpann pvssptaaap eksnsklkin
       61 intapiaeld klelpgtkps lseriqaarp yktiddlvtk kaisaeelgl ikslvtiedk
//
LOCUS       WP_009628584             320 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Pseudanabaena].
ACCESSION   WP_009628584
VERSION     WP_009628584.1
KEYWORDS    RefSeq.
SOURCE      Pseudanabaena
  ORGANISM  Pseudanabaena
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Pseudanabaenales; Pseudanabaenaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudanabaena"
                     /db_xref="taxon:1152"
     Protein         1..320
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=34854
     Region          122..302
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mqlkrlvaia iflltlvgli lsaepaktng iatfksannr nkvalngssq apqdiyfsaa
       61 inqsapvfgc evqppanppe pslpaaltsi pitlerfrks vatskttits qkaitaspre
      121 ivalaaasny gdrylkdlsg kpanyapiiv lhetvgstng tinffqefht dediqasyht
      181 liaidgsviy lvppdkrafg agdsefvsal gqeavqtnpr yprsvnnfay hisletpedg
      241 mnedythsgy teaqylslaw lvaktnvple ritthkiidr sgsridprsf dfnlfkkllt
      301 ayprtneiei gcsalrkfqs
//
LOCUS       WP_009630573             326 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Synechocystis sp. PCC 7509].
ACCESSION   WP_009630573
VERSION     WP_009630573.1
KEYWORDS    RefSeq.
SOURCE      Synechocystis sp. PCC 7509
  ORGANISM  Synechocystis sp. PCC 7509
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Merismopediaceae; Synechocystis.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 326)
  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 326)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Synechocystis sp. PCC 7509"
                     /db_xref="taxon:927677"
     Protein         1..326
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36797
     Region          38..188
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          216..295
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mhqkeaelek rkmqinqeal iermmrlape nsllevfpgi fiyhsskpte seisvlkpaf
       61 ciiaqgskdv llnnelfhyd sghylistld lpimsnvvea seekpylnlr idldsalvaa
      121 vmiesgietk ksgtgvkamd vspvdadlld avvklvklcd tpdemkflap piireiiyrl
      181 lkgnqgarln qlittegdaq ristvvrqir enieqplkie dtareigmsv sgfhqhfksv
      241 tamsplqfqk qirlqearrl mlgenldats aayhvgyens shfnreykrl fgeppmrdve
      301 rmreavreip ssitlsskhp nlarnr
//
LOCUS       WP_009632003             443 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Synechocystis sp. PCC 7509].
ACCESSION   WP_009632003
VERSION     WP_009632003.1
KEYWORDS    RefSeq.
SOURCE      Synechocystis sp. PCC 7509
  ORGANISM  Synechocystis sp. PCC 7509
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Merismopediaceae; Synechocystis.
REFERENCE   1  (residues 1 to 443)
  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 443)
  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 443)
  AUTHORS   ter Beek,J., 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 443)
  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 443)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Synechocystis sp. PCC 7509"
                     /db_xref="taxon:927677"
     Protein         1..443
                     /product="CmpA/NrtA family 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=47781
     Region          56..313
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 msnfsrrqfi itagaatags llahgcssgp tetassggaa spvasvgaaa napkvettta
       61 klgfialtds aplivalekg lyakygmtdv kvekqaswpv trdnlvlgsg gggidgahil
      121 spmpylmalg kitqgkpipm yilarlntng qaisvanayk dmkvgldssp lkaafsksks
      181 sgkeikaavt fpggnhdlwm rywlaaggid pnaeisvvpv pppqmvanmk vgnmeafcvg
      241 epwnaqlvnq kvgysalvtg elwndhpeka ftmradwvdk npnsakamlm avqeaqqwce
      301 kaenkeemie iiskqkwfkv pakdiiersk gnidygdgrt vqdfpykmkf wadnasypyk
      361 shdlwflten irwgnlpadt dtkkiidqvn redlwkeaat algvpaaeip tstsrgvekf
      421 fdgvtfdpen paaylkslki kka
//
LOCUS       WP_009632383             267 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Synechocystis sp. PCC
            7509].
ACCESSION   WP_009632383
VERSION     WP_009632383.1
KEYWORDS    RefSeq.
SOURCE      Synechocystis sp. PCC 7509
  ORGANISM  Synechocystis sp. PCC 7509
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Merismopediaceae; Synechocystis.
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   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 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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Synechocystis sp. PCC 7509"
                     /db_xref="taxon:927677"
     Protein         1..267
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29388
     Region          22..92
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          193..252
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mkwcgkrnse sirrpiaeqq aellrhigdk lrqkrleqsl slekaaaktl irqhllvaie
       61 kglleelpep vyiqkfirqy aevlgldaeq lansfptdkh drpannnqpa wslilpvvql
      121 rpihlyvlyi vaialavsml srslsrnqlq tnsplpelpi vanspkpvap tdsnkvesvs
      181 atpkinnqiq igvtlkassw irvvadgkia fqgllpsgtq rtwvakdnlt vlagnaggvl
      241 ltinqkeskq mgnlgevqel tfaaprl
//
LOCUS       WP_009632950             260 aa            linear   BCT 20-JAN-2025
DEFINITION  phosphonate ABC transporter ATP-binding protein [Synechocystis sp.
            PCC 7509].
ACCESSION   WP_009632950
VERSION     WP_009632950.1
KEYWORDS    RefSeq.
SOURCE      Synechocystis sp. PCC 7509
  ORGANISM  Synechocystis sp. PCC 7509
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Merismopediaceae; Synechocystis.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
REFERENCE   2  (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   3  (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   4  (residues 1 to 260)
  AUTHORS   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 260)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Synechocystis sp. PCC 7509"
                     /db_xref="taxon:927677"
     Protein         1..260
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=28548
     Region          16..256
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 miektnniaa nksinpifel knvtkqfgnf ssikkinlki ypgervallg ssgagkstli
       61 nllngtvrpt sgevwvlgkn lalkpatvrq iqrqigtiyq qlhlvdnlqv ihnvnaghlg
      121 rwtfwqaafs lvfplevata traltqvgia eklyqrcgvl sggqqqrvai arvlvqnpav
      181 iladepiasl dpersreiiq llcqlntqln ktlvtslhdw evarnyyqri vglsggevlf
      241 dspanlvtle mvdglykqan
//
LOCUS       WP_009635219             387 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Serratia sp. M24T3].
ACCESSION   WP_009635219
VERSION     WP_009635219.1
KEYWORDS    RefSeq.
SOURCE      Serratia sp. M24T3
  ORGANISM  Serratia sp. M24T3
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
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
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 387)
  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   5  (residues 1 to 387)
  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   6  (residues 1 to 387)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 387)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 387)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Serratia sp. M24T3"
                     /db_xref="taxon:932213"
     Protein         1..387
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40912
     Region          2..61
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          73..373
                     /region_name="ASKHA_ATPase_ROK_CYANR"
                     /note="ATPase-like domain of
                     cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and
                     similar proteins; cd24073"
                     /db_xref="CDD:466923"
ORIGIN      
        1 mlnslqrqil gainsaagls rtelaqfcrm skaaisspvr emleagylfe adsingpgqg
       61 rpsvklmirp qgayfigvsl lqepaqmali nlngeiiara cfalnrdptl laeniahalp
      121 elldgqaeaa erlmgmgvtl sgfidetqsi cvqsallgwr nvalatlitq atglevfien
      181 dakalavsek rfgqardlet ftlvshgagi gsahfiagkl hrglhggage iahctmelng
      241 tpcrcgkrgc ldtiasvnai memareenlt iaslpelerl aangqaaair ilhragsalg
      301 lgiahliqii dpsliliawq eetidgllgt vvqqsietnv lpgfagltpv rtfainqdtw
      361 vraaasiaah rfldgpesin dgaksar
//
LOCUS       WP_009637230             625 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Serratia sp. M24T3].
ACCESSION   WP_009637230
VERSION     WP_009637230.1
KEYWORDS    RefSeq.
SOURCE      Serratia sp. M24T3
  ORGANISM  Serratia sp. M24T3
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 625)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Serratia sp. M24T3"
                     /db_xref="taxon:932213"
     Protein         1..625
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68686
     Region          1..625
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mssdnvtedq apagtkllal galgvvfgdi gtsplytlkt vlylsgggss hevvlgllsl
       61 iiwtlvivtt lkyamfamrm snngeggila lmsllftqkk nrpwvvfagi fgaaliygdg
      121 aitpaisvls aiegvnivlp esksyivpvt vailialfai qamgtakigk lfgpimalwf
      181 vviaglgiwg ivqhpavlaa vnpyyafkfl fshglssflv lggvflcvtg aealyadmgh
      241 fgkrpvwlaw falvfpslll nyagqsalil sgadvtqnif yrlcppgmli plvilatlat
      301 iiasqaiisg afsmtrqamq lgwlprlrik qtseesygqi yigsinwllm iatvfltiff
      361 qssdrlaaay giavsftmim tsgliyvsmr evwrwgivis gliaglffiv dlsfltanlv
      421 kileggyvpl lmalalysvm miwhhgvria tlvvrektmp vkefltdiet hqiprvpgta
      481 vfltrstetp timrwhvtrn gslhaqvisl niqieniprv sakerleiee iapnfwhvia
      541 hygfieepni aqllgykeia dldvdrenlt fyvghenivr gegrkrlpsw qrhifslmvr
      601 nnihitdhyr lpsdrvveis rqval
//
LOCUS       WP_009640626             153 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: division/cell wall cluster transcriptional repressor
            MraZ [Capnocytophaga].
ACCESSION   WP_009640626
VERSION     WP_009640626.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga
  ORGANISM  Capnocytophaga
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Chen,S., Jancrick,J., Yokota,H., Kim,R. and Kim,S.H.
  TITLE     Crystal structure of a protein associated with cell division from
            Mycoplasma pneumoniae (GI: 13508053): a novel fold with a conserved
            sequence motif
  JOURNAL   Proteins 55 (4), 785-791 (2004)
   PUBMED   15146477
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449500
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Capnocytophaga"
                     /db_xref="taxon:1016"
     Protein         1..153
                     /product="division/cell wall cluster transcriptional
                     repressor MraZ"
                     /GO_function="GO:0000976 - transcription cis-regulatory
                     region 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=17467
     Region          7..147
                     /region_name="MraZ"
                     /note="DNA-binding transcriptional regulator and inhibitor
                     of RsmH methyltransferase activity [Translation, ribosomal
                     structure and biogenesis]; COG2001"
                     /db_xref="CDD:441604"
ORIGIN      
        1 mihssvtyec kadskgritv psglkvvldk elqngfvlkp svfnrciely pqgewqeime
       61 kmraklnlfs kqhldylrkf tagvkevevd aaarflipks lveyaqidke vvlvplinfi
      121 eiwdrelfea qnnsideeaf mqltekimgn dgv
//
LOCUS       WP_009642346             615 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase [Capnocytophaga].
ACCESSION   WP_009642346
VERSION     WP_009642346.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga
  ORGANISM  Capnocytophaga
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 615)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Capnocytophaga"
                     /db_xref="taxon:1016"
     Protein         1..615
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=70198
     Region          65..493
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mkptqldtqt perkiyyleq lrqlfptcmt etqnqqgqwq qvvdwdalkq llgdavadst
       61 deryqftwag kqaarleane atdqtlrpvp edsidwdtte nlyiegdnlq vlkllqqaym
      121 gkvkmiyidp pyntgsdfvy kddfarsrae edlatgdide qgnryrpnnr sngrfhsdwc
      181 smiyprllva rsllsedgvi fisiddnevh nlrkigdevf geenfvgeli hqrakgggqa
      241 kyivkghdyi lvyaynisci slvrkkviqq ktveidgelf iknddilrkt fgkydksngd
      301 rrcfyeqieq ykgiekkeei drlleegalf lelnkegmht icryekvsea tsklytiikv
      361 lseegkkele algisffsyp kpvellkqlv eagsdknsli ldffsgsatt ahavmqlnae
      421 dggrrkyicv qlgeptpkds eahkagyasi pevakerirr agkkikeenp tsqldtgfrv
      481 lrldssnfse verhpseydq glldlfatni kedrsdldll fgamlswgip lslpisteei
      541 dgcrvynvne gdlvacfaeh iseavvkama skvslrvlfr dscfsedkhk inlfeifkqq
      601 lgwdekeamd kirvi
//
LOCUS       WP_009643029             327 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Capnocytophaga sp.
            CM59].
ACCESSION   WP_009643029
VERSION     WP_009643029.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sp. CM59
  ORGANISM  Capnocytophaga sp. CM59
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 327)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Capnocytophaga sp. CM59"
                     /db_xref="taxon:936370"
     Protein         1..327
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36216
     Region          2..325
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mmksyikais tyfpkniltn daisaqfpew nsekilqkig ieqryiaqtd ecasdmatqa
       61 vlnlikehhl dkntidflll ctqtpdhilp ttacivqekv glpttcaald inqgcsgyiy
      121 glslasslia sgnfknvilv tadtytkyvh pkdkgnlsif gdaatatlvs tegtycigkp
      181 tlgtdgagae nliirnggtr sprnenpndl dnfvdmkggk ifnfivkrtp evvydnlkin
      241 gfdindidlf vfhqanthil nkvredmeip qekfviemry ygntisstip ialsehlrky
      301 pekpskriqf vgfgvgyswg aiciekq
//
LOCUS       WP_009643052             255 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Capnocytophaga].
ACCESSION   WP_009643052
VERSION     WP_009643052.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga
  ORGANISM  Capnocytophaga
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 255)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Capnocytophaga"
                     /db_xref="taxon:1016"
     Protein         1..255
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=29466
     Region          63..231
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mkritsfals ffcfitattf ygqqsnvvss klsrivldsl hsphenfeya ikrmyvdikg
       61 reydldfkaf ryayigyqnm klqnklndkr llsiidftkd sdkkrfytid ldsrqilyht
      121 yvahgkktgt sastyfsnee eshksslgfy vtgktyngda gfslklygne hnynsnaykr
      181 givihtadym nedflkrngr fgrslgcpvl ptniykevie tikdgtmvfa yytnkrylas
      241 skylkvsslt ednif
//
LOCUS       WP_009643562             457 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Mogibacterium].
ACCESSION   WP_009643562
VERSION     WP_009643562.1
KEYWORDS    RefSeq.
SOURCE      Mogibacterium
  ORGANISM  Mogibacterium
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Anaerovoracaceae.
REFERENCE   1  (residues 1 to 457)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Mogibacterium"
                     /db_xref="taxon:86331"
     Protein         1..457
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=49125
     Region          335..456
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mrsnnvvqel adkktgvskr vkiiiaiaai ivigtcafgg yrysnastfa kgvridgvdv
       61 sglnledaid kvtaennsft iaedghetke vktsftydik asmrvkmgla sidprvifck
      121 nvnydvtlkk ksgieksada igaavpdaqg vkytedayid ynsmtlvpev qgdsvdfkki
      181 akeiadkkaa dykftkykmd rkklisepkv tadslkdefe fakqylskpi ylnnitgtpy
      241 eiepnalakv ilysktgpky sqtgaqeiak eiadkyagss lkvktlagyk ilgnhalkin
      301 vnvdktaesi lnaaksgeag sivtdqgaas aggshieinl sgqsvryvkn gnvvftssmv
      361 sggpghrtrt gifkinakqr natlkgrndd gtdyespvsy wmpfdggngl hdapwrgafg
      421 ggiylsggsh gcvnmppama aqlynmipvg tivyvys
//
LOCUS       WP_009644377             470 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate--CoA ligase family protein [Mogibacterium].
ACCESSION   WP_009644377
VERSION     WP_009644377.1
KEYWORDS    RefSeq.
SOURCE      Mogibacterium
  ORGANISM  Mogibacterium
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Anaerovoracaceae.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Mogibacterium"
                     /db_xref="taxon:86331"
     Protein         1..470
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50944
     Region          11..>465
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mivkhprdyv idnlqyalnp ksiavvgasr ystkvgykvv dglklwgykg eiypvnprad
       61 qvnglkaypt vkdipedvdl aflavpahiv ksvledcvak kvkivviats afkeigrgal
      121 qdeltqycrd nklpligpnl vgmgspyldf ncgfipylpi kgpvamisqs ganllaalgs
      181 sqkdhygmsf fvglgnkadv dfcefiayag rdkdtrclav yiegldspda fieacrsvnk
      241 pivtikvggs kigekaafah tasenagtsd efydevfkea gairattwee fldismalgm
      301 qppakgdniv mitngggsgl lscdhferrg mpmhelheis pslsdriray mpmfgsplnp
      361 vdisgtaspi qykgafiqai rdpnvhgiig sicptavtdv davtdvviri hdtyrhlgkp
      421 fimecqggne cqeailklrd hgipayatae qavnamvaly rygqislnrk
//
LOCUS       WP_009644924             227 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Selenomonas].
ACCESSION   WP_009644924
VERSION     WP_009644924.1
KEYWORDS    RefSeq.
SOURCE      Selenomonas
  ORGANISM  Selenomonas
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  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   3  (residues 1 to 227)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Selenomonas"
                     /db_xref="taxon:970"
     Protein         1..227
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25734
     Region          18..216
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 magdlmnaat vlkigqrvef yledddiryt srieditadr livampvder rrpiipaage
       61 qlyglavgea cryrffsvfk gkardpipvw mitkpevver hqnrsfvram vrlpiqvrii
      121 dtegreselm klyttdvsgg gvsfivprhv kvnsrasivf tnfpnigtls vmarivrslp
      181 lepsdrgwql gahfleldrg tmnkivhfvf selrrqltlh pdspare
//
LOCUS       WP_009645642             265 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Selenomonas sp. CM52].
ACCESSION   WP_009645642
VERSION     WP_009645642.1
KEYWORDS    RefSeq.
SOURCE      Selenomonas sp. CM52
  ORGANISM  Selenomonas sp. CM52
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Selenomonas.
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   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 265)
  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 265)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Selenomonas sp. CM52"
                     /db_xref="taxon:936381"
     Protein         1..265
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28930
     Region          2..67
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          188..251
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 migdllrrer erqnlsikdi ekatsiraly idaiekgeyk tlpgevyakg fvrnyanylk
       61 lnaneivnaf neemhpqeel qdaagsssae earqeqster nreeyrgpki tslesypmek
      121 rshgvrnalm vavavfvvaf aaliafggde epsapaprak tqtqqgqkpg qkqteaapka
      181 aadgvevkls ftdrcwtevv vdgktefegt aekgkvltlk gkdkvritag nagalnysln
      241 gkdmgaigqk gevvektftk enaak
//
LOCUS       WP_009647333             276 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase
            [Actinomycetaceae].
ACCESSION   WP_009647333
VERSION     WP_009647333.1
KEYWORDS    RefSeq.
SOURCE      Actinomycetaceae
  ORGANISM  Actinomycetaceae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Actinomycetaceae"
                     /db_xref="taxon:2049"
     Protein         1..276
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=31337
     Region          30..>236
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mlddyvqgtq teksdefays eradlepqdd nllilgesgd vlealtrvpe lakkyvgqvk
       61 liyidppfnt aqtfasyedn lehsiwltmm rdrllhmkkl ltddgsiwvh lddvevhrmr
      121 llmdevfgae nfqaevvwqk adsprrglgf svdqnfvivy rrseafepnk alrtaadnar
      181 fsnpdndplg pwwddnpsgn hgdgsggmcy aiqnpltgem mrppkgaswr ysqqrilagl
      241 qgwvpyrlen lhnaewrasn egalarrrpm tcarss
//
LOCUS       WP_009648256             295 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Actinomyces sp. ICM47].
ACCESSION   WP_009648256
VERSION     WP_009648256.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces sp. ICM47
  ORGANISM  Actinomyces sp. ICM47
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
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
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Actinomyces sp. ICM47"
                     /db_xref="taxon:936548"
     Protein         1..295
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=31203
     Region          1..276
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mirfdhvskt ypggaraved fsltiergst tvflgtsgcg kttlmrmvna mvtptsgtvf
       61 vrdqdvagad pvrlrrsigy vlqegglfph rsiadniatv prlegvskae sreralellt
      121 lvgleremad rypsqlsggq rqrvgvaral anradillmd epfgaldpiv radlqrelke
      181 irralgttil fvthdvdeaf tlgdqvavls tggrieqvgt paellsspas pfvakfvgas
      241 raarpvrvag pgglvldedg tpvgtlardg deasaalgvs saprgsarpv arers
//
LOCUS       WP_009648335             480 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase family protein [Actinomycetaceae].
ACCESSION   WP_009648335
VERSION     WP_009648335.1
KEYWORDS    RefSeq.
SOURCE      Actinomycetaceae
  ORGANISM  Actinomycetaceae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales.
REFERENCE   1  (residues 1 to 480)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Actinomycetaceae"
                     /db_xref="taxon:2049"
     Protein         1..480
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=50810
     Region          80..182
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          358..479
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(432..433,436,452..455,457)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mlknlstktr waigaasalv llvvcaiivy aanysgrvlp gttvagisve gmsrdqvisa
       61 vtaradaakv sltvegkttt vslneagisv daeataneam kdstslpsfi galfsrrale
      121 pvttvsedsi kkltatvnst ltsemkdaqv iiapdeesft vtpaqngngi ardevaaavk
      181 qagatlasvs qnvtvsqmep svttadaqqa aqkgndlldt sieisdgidl fvaersdkvh
      241 wvefltkddg sldepsistv kvadwvnala aktdvkaenr venvdssgnv lttaregkkg
      301 lktnnteeit kgvvkamtng tsyeglfhyd diepgsetkq vaegtenlvy qaaegekwvd
      361 inltdatvtp yvggkvaggp fymvpgapdt ptvtgtfhvy lkydvqtmrg enadgtkyet
      421 egvpwvtyft gsyamhgapw rssfgwsgyg gshgcvnmpv daakfiydwt dmgdtvvvhy
//
LOCUS       WP_009649376             248 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YaaA family protein [Campylobacter].
ACCESSION   WP_009649376
VERSION     WP_009649376.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter
  ORGANISM  Campylobacter
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Prahlad,J., Yuan,Y., Lin,J., Chang,C.W., Iwata-Reuyl,D., Liu,Y., de
            Crecy-Lagard,V. and Wilson,M.A.
  TITLE     The DUF328 family member YaaA is a DNA-binding protein with a novel
            fold
  JOURNAL   J Biol Chem 295 (41), 14236-14247 (2020)
   PUBMED   32796037
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Liu,Y., Bauer,S.C. and Imlay,J.A.
  TITLE     The YaaA protein of the Escherichia coli OxyR regulon lessens
            hydrogen peroxide toxicity by diminishing the amount of
            intracellular unincorporated iron
  JOURNAL   J Bacteriol 193 (9), 2186-2196 (2011)
   PUBMED   21378183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006857
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Campylobacter"
                     /db_xref="taxon:194"
     Protein         1..248
                     /product="YaaA family protein"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=28538
     Region          4..230
                     /region_name="YaaA"
                     /note="DNA-binding protein YaaA associated with the
                     oxidative stress response [Replication, recombination and
                     repair]; COG3022"
                     /db_xref="CDD:442258"
ORIGIN      
        1 malkilfsps eskstfagds yirkenftfa klfhlrleil kkyasfvkta sdkelcklfg
       61 fknldtddtl rddifakgci kailrydgva ykhlnyrsld tkaqgyiden vlifsnlfgp
      121 imagdlipey klkqgeking ldiekfynen fsaaideflq dddvldlrag fyekfysikk
      181 eyisfkflkn gkvishhtka yrgkilkeis knsvndktql mtlnfeglrl idmkkiglkt
      241 efaleiee
//
LOCUS       WP_009650698             525 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sensor histidine kinase [Campylobacter].
ACCESSION   WP_009650698
VERSION     WP_009650698.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter
  ORGANISM  Campylobacter
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae.
REFERENCE   1  (residues 1 to 525)
  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 525)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20493667
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Campylobacter"
                     /db_xref="taxon:194"
     Protein         1..525
                     /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=60175
     Region          30..246
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          <287..502
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mfsknklfii fsviflslmv gnytlnrsfa keilineqls ilkssssrie kwlenkkssl
       61 qainsliakf dpvrdeatik difeksqeia nfssvyagye nnvtisgkif nrppdyiptl
      121 rpwyintare dkiyitrpyv dvglqisvis icesikegkv lkgvlcgils fsdikneild
      181 lrlddgfifl idenfnillh pdskfeltka kfdvpdldil ktsnyetnde iltfnpiens
      241 kltlvaktpk kdiykkineq fiinlaiyva savsflllmy fynkkdkese rmlfqqtkma
      301 elgemiaais hqwiqplnsl giflgnlvqf krlgklsdev fyenikrsls nidymantmd
      361 ifknfyrfea spqsfdikqa ieetvfilfs qkskievkin lkrgvdtacl nyinefkqii
      421 acliqnskqa lqtsknkkra kivvsirqnd thfeirvidn adgidrayrd kiftpflstk
      481 gggglglyis kliankklng dlmlvksknp tifmlkiskk vkddr
//
LOCUS       WP_009653276             276 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Klebsiella].
ACCESSION   WP_009653276
VERSION     WP_009653276.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..276
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=30632
     Region          43..189
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mricragvll alllagcase kgiidrdgyq ldtrhpaqaa yprikvlvih ytaddfdvsl
       61 atltdnqvss hylipekppl hggkpriwql vpeedlawha gvsfwrgstr indtsigiel
      121 enrgwqktag vksftpfnpa qidaliplak diiaryhiap qnvvahadia pqrkddpgpl
      181 fpwrrlaeqg igawpdarrv afylqgrpsy epvdaaalld vlarygyqvt pemtpaqqkr
      241 vimafqmhfr parwdgvada qtlaiaeall ekygrg
//
LOCUS       WP_009653305             409 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Klebsiella].
ACCESSION   WP_009653305
VERSION     WP_009653305.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 409)
  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 409)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..409
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47049
     Region          1..405
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mpvlslslke arhlhlaaqg llkkprrrak pwdilqtikq msllqidtin vvarspylvl
       61 fsrlghypqr wldealrage lmeywaheac flprsdfslv rhrmltpdkm gwkyhkawmt
      121 enaesiqall ahiaengpvr sadfehprkg asgwwewkph krhleglfta gevmvierrn
      181 fqrvydltqr vmpdwdderd glsqeqaeam mlrnsarslg ifraqwlady yrlrqpplpl
      241 llaswqeegl vvpvnvealg emwlhrdala llesspggrl aasrsavlsp fdpvvwdrkr
      301 aeqlfnftyr lecytpapkr qygyfvlpll hqgrlvgrmd skmhrktgvl eiialwleeg
      361 vkvtsglesg lkraiddfal wqdatrvscg klpaelfagr qqgweidaa
//
LOCUS       WP_009654274             531 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [Klebsiella].
ACCESSION   WP_009654274
VERSION     WP_009654274.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..531
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=57111
     Region          2..527
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mqtilkidpt dnlivalqdl rkeqrvhwnd eayvlrsdvk tkhkfatedi apgdivslyg
       61 vpvgkatrpi trgeaitten ikhyaapvsl ddvapydwqq pdvsawqqrt fkgivredgr
      121 vatanywlvi plvfcenrnv qrvtdalnda lgyannglkn farqvtsaga lndtrhlpfp
      181 hldgircitv nsgcggatsd smtmcdvlaa ysdhpnvlgv tvfalgceka rivdfnaala
      241 krnpnfnkpi iyfrqqdwss eekmmqdalt etynaireap vaerqdvpls hlkigvkcga
      301 sdgfsgisan pamgevsdrl valggasgla efpelcgaeg divqrcatre lkekflslmk
      361 nyehvanffg ttiadnpspg niadglitda iksagaakkg grapvsavcd yaepmgesgl
      421 slvctpgndv davtglvaag cnvvifstgl gtptgnpivp vlkvstntal akkmpdiidy
      481 dcgpiiegtp ladiadglfe kiiatasgtw rtkadaleqy dfmlwkrsle l
//
LOCUS       WP_009655367             184 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Selenomonas sp. FOBRC6].
ACCESSION   WP_009655367
VERSION     WP_009655367.1
KEYWORDS    RefSeq.
SOURCE      Selenomonas sp. FOBRC6
  ORGANISM  Selenomonas sp. FOBRC6
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Selenomonas.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Selenomonas sp. FOBRC6"
                     /db_xref="taxon:936572"
     Protein         1..184
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=19911
     Region          1..184
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mkrlvvgitg asgsvyalrl idvlreqgie vhavvtasgl rvlgyecgit eeklarrvsi
       61 lypnadvgaa iasgsfrmda mvvlpcsmkt agaiahgvtd dlltraadvt lkegrrlllv
      121 pretpmheih lenllrlara gavimpaapg fyhrpetldd lvnmmvgkil drlgieaelf
      181 trwr
//
LOCUS       WP_009658985             184 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Selenomonas sp. FOBRC9].
ACCESSION   WP_009658985
VERSION     WP_009658985.1
KEYWORDS    RefSeq.
SOURCE      Selenomonas sp. FOBRC9
  ORGANISM  Selenomonas sp. FOBRC9
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Selenomonas.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Selenomonas sp. FOBRC9"
                     /db_xref="taxon:936573"
     Protein         1..184
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20143
     Region          1..184
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mkkiivgitg asgsiyavrl mevlcrrgie ihavvttsge kvldyecgit reelsrrvtk
       61 lyanddvgaa iasgsfrmda mvilpcsmra agalahgvtd dlltraadvt lkegrrlllv
      121 pretpmheih lenllrlara gavvmpgapg fyhrpetvdd lvnmmvgkic drlgleeelf
      181 lrwr
//
LOCUS       WP_009656045             348 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Selenomonas
            sp. FOBRC6].
ACCESSION   WP_009656045
VERSION     WP_009656045.1
KEYWORDS    RefSeq.
SOURCE      Selenomonas sp. FOBRC6
  ORGANISM  Selenomonas sp. FOBRC6
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Selenomonas.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Selenomonas sp. FOBRC6"
                     /db_xref="taxon:936572"
     Protein         1..348
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38645
     Region          1..345
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mklvvniekr lrdftlaanf tltdttlall gasgsgksmt lkciaglerp dcgqivlner
       61 ilfdsekgin lppqarsvgy lfqnyalfpn mtvreniifa ldgtreeker ifkenvarfs
      121 leglenaypa glsggqqqrv afarilarga dvllldepls aldthlkwqi etalreilam
      181 qniaailvth drdeafriar eiatvdrgql tpptdkhelf rnpgtraatt ltgcknisaa
      241 rrvdethvta tdwgitlrva dattnvrhia vrahylvlal esdadalpar iaeviestft
      301 yivmlrfadg ampirweidk ttwhaheagi gdtlhfnfpv eelmllrd
//
LOCUS       WP_009660278             201 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Streptococcus sp. AS14].
ACCESSION   WP_009660278
VERSION     WP_009660278.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sp. AS14
  ORGANISM  Streptococcus sp. AS14
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Streptococcus sp. AS14"
                     /db_xref="taxon:936577"
     Protein         1..201
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22674
     Region          3..198
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mkflelnkkr hatkhfndkp vdpkdvrtai eiatlapsah nsqpwkfvvv rernqalaet
       61 afggnvdqik eapvtialft dtdltkrark iarvagvknf sdeqlqfymq nlpaefarys
      121 eqqksdylsl naglvamnlv laltdqgigs niilgfdksk vnevleider frpellitvg
      181 ytneklepsy rlpvdeiiek r
//
LOCUS       WP_009662045             276 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Lachnoanaerobaculum sp.
            ICM7].
ACCESSION   WP_009662045
VERSION     WP_009662045.1
KEYWORDS    RefSeq.
SOURCE      Lachnoanaerobaculum sp. ICM7
  ORGANISM  Lachnoanaerobaculum sp. ICM7
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Lachnoanaerobaculum.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Lachnoanaerobaculum sp. ICM7"
                     /db_xref="taxon:936594"
     Protein         1..276
                     /product="formate/nitrite transporter family protein"
                     /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=29183
     Region          6..276
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mnfsnttaev tqnlieageg kvkrplhkmi llgilagmli gagamassva ihdisntgia
       61 rlvaglvfpi gfvmmvlfgg elftgaclmi igvlkgrykv sdmirvliiv fisnliggil
      121 failvsfsgq fkysdglmga ftiklalska nisfgsalis gilcnffvcl gvvmaglskd
      181 isgkvlasfl pimtfvtggf ehcvanmfyi pagifaagns kyaevamtky gitaeklatl
      241 nwknflltne lpvtigniig gmlfigvvmy ivyske
//
LOCUS       WP_009661297             189 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [unclassified Veillonella].
ACCESSION   WP_009661297
VERSION     WP_009661297.1
KEYWORDS    RefSeq.
SOURCE      unclassified Veillonella
  ORGANISM  unclassified Veillonella
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Veillonella.
REFERENCE   1  (residues 1 to 189)
  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 189)
  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   3  (residues 1 to 189)
  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   4  (residues 1 to 189)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 189)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 189)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="unclassified Veillonella"
                     /db_xref="taxon:2630086"
     Protein         1..189
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21423
     Region          1..187
                     /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"
ORIGIN      
        1 mrilivddes lirmdlrdil eseqhevvge asngveaitm ckelkpdavl mdvkmpeldg
       61 ieaarqigfn hlapvvllts ysqqdlvtka resgvygyli kpvreeqlip tlemacgrfl
      121 ddlesrqqma dlektleerk iiqkatgilm dlykitedea ynrirqlsmk kresivnick
      181 liiqqastn
//
LOCUS       WP_009663129             400 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Lachnoanaerobaculum sp. ICM7].
ACCESSION   WP_009663129
VERSION     WP_009663129.1
KEYWORDS    RefSeq.
SOURCE      Lachnoanaerobaculum sp. ICM7
  ORGANISM  Lachnoanaerobaculum sp. ICM7
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Lachnoanaerobaculum.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Lachnoanaerobaculum sp. ICM7"
                     /db_xref="taxon:936594"
     Protein         1..400
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43444
     Region          2..399
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mknvlvincg ssslkyqlin meneevlakg lferiaipgs klthepegre kfkiekdvkn
       61 hteaialvle altdkdhgvi kdaseiyaig hrvvqggvky pesvvitdev kkdiekysdl
      121 aplhnpanlm gieavekamp gvpnvaafdt sfgmsmpeka ykyaipneyy enyhirrygf
      181 hgtshmyvsq eaikfagldk dtarvivchl gngasisasv ggkcidssmg ltpleglimg
      241 trsgdidpai vqyickkenk svdevldiln kksgvlgmsg gvssdfrdie naeadgnnla
      301 kvaleafryr iikyvgayva amggvdalcf tagvgendki trqivgnalg figakvdeea
      361 nnvrgkrtmi stpdskvkim lmptneelai ardtyrlakk
//
LOCUS       WP_009662863             343 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Lachnoanaerobaculum sp. ICM7].
ACCESSION   WP_009662863
VERSION     WP_009662863.1
KEYWORDS    RefSeq.
SOURCE      Lachnoanaerobaculum sp. ICM7
  ORGANISM  Lachnoanaerobaculum sp. ICM7
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Lachnoanaerobaculum.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Lachnoanaerobaculum sp. ICM7"
                     /db_xref="taxon:936594"
     Protein         1..343
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39202
     Region          5..341
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mlelnikkkl nnftldieck lnrnrigilg gsgagksmil kmlagiekpd igyiklddrl
       61 lfdsekkidi kpkdrhigyc fqnyalfpnl tvyenivigl skseradadk ylekfeltki
      121 kdskpnkisg gqaarvamar ilirkpkall fdeafsaldi ylrdhiqeei aqiledfegs
      181 aifvshsrde vyrlcdsmmv idsgkisnlg ntkkifkype tkitailtgc knisdiryis
      241 dntieaidwg ikfkflkelp kdinaigira hefvpvweet gnnliefklk sraklpfedn
      301 yylytngssd itwlvqkdik ekidsrglpk flqiyeenil llk
//
LOCUS       WP_009663904             183 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Lachnoanaerobaculum].
ACCESSION   WP_009663904
VERSION     WP_009663904.1
KEYWORDS    RefSeq.
SOURCE      Lachnoanaerobaculum
  ORGANISM  Lachnoanaerobaculum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae.
REFERENCE   1  (residues 1 to 183)
  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 183)
  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   3  (residues 1 to 183)
  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   4  (residues 1 to 183)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 183)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 183)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Lachnoanaerobaculum"
                     /db_xref="taxon:1164882"
     Protein         1..183
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=20520
     Region          4..175
                     /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"
ORIGIN      
        1 msdiiiafpn pgdskvlrsi likngysivg vvasgaqain lsddidygiv vcayqlndmq
       61 ymelkenmne tcelllvcsp gklneapddd inflpmpfkv ielvkkvsei sdklyyerkr
      121 kkkqeerggk nfmaiqkake llikhknmte peahkylqis smkngetiin takkicllyg
      181 gke
//
LOCUS       WP_009671983             211 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Paenibacillus].
ACCESSION   WP_009671983
VERSION     WP_009671983.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..211
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=23302
     Region          1..199
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mkkrgwvvgi tgasgaiygv tlvkellkrg vpvhlvitda gwrvlheeld wvaakrketl
       61 eahfggfpgp ytyyplqdig agiasgsfrt egmvvmpcsm gtlagisrga sdnlleraad
      121 vmlkegrrli lvpretplha ihlenmlvla kmgvklipam pafyqrpetl edivaflvgk
      181 vldnmdldhe lfrrwgesnd dnreetahre n
//
LOCUS       WP_009672682             301 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: aminoglycoside phosphotransferase family protein
            [unclassified Paenibacillus].
ACCESSION   WP_009672682
VERSION     WP_009672682.1
KEYWORDS    RefSeq.
SOURCE      unclassified Paenibacillus
  ORGANISM  unclassified Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 301)
  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   2  (residues 1 to 301)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="unclassified Paenibacillus"
                     /db_xref="taxon:185978"
     Protein         1..301
                     /product="aminoglycoside 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=33734
     Region          50..219
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mpnnsslisk tvliaekagl kditplelgn ggnlivhlap ypivariatv lsknhadyay
       61 kvlvrelraa rhlhskgvlv rlptdrtdag pydiggtwmt fwkyvpptel rrpspseavd
      121 lvnrlslalk dftdeipllg vwertcqsaf rlmkhpdrri qnllslfvai drqmrletsl
      181 llpshgdahs rnllpspegw vwsdfedlsw mpaywdlasy vgnlalfngi qeptfqyiws
      241 qmnnqadkqa fgfavtaril mstlgnldfa fsgsgdlefa ykqlglakdf ihqinliieg
      301 e
//
LOCUS       WP_009672743             369 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GerAB/ArcD/ProY family transporter [unclassified
            Paenibacillus].
ACCESSION   WP_009672743
VERSION     WP_009672743.1
KEYWORDS    RefSeq.
SOURCE      unclassified Paenibacillus
  ORGANISM  unclassified Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="unclassified Paenibacillus"
                     /db_xref="taxon:185978"
     Protein         1..369
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=40860
     Region          2..362
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 mdkitplqty mlftqyllst lvsflaapli qnagysvwip viagsllggv ltylayklgc
       61 rrpgrymaey greiigrplh yllvlfmafv ylftaalvlr qltdfiveiy lpgtplwava
      121 gllglcttrl vhsgvtnifr sgqgvffval alvvliavas cqdivpysvv slvtnfdgrg
      181 ifsatamitg lfgemtfial ffpkfketgr tmkalvwaiv taavltlgnl ipmvllfgps
      241 laanltyanl emtryiqlgn fiqnmdpili lmwlftllvk islflyisvi avtqtlkmkd
      301 trpltlpfgv tvvflclwmv nssetldrfa gtaevpmmll aelipvvyll vdalrsrfkk
      361 rqpvrepst
//
LOCUS       WP_009673872             365 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GerAB/ArcD/ProY family transporter [unclassified
            Paenibacillus].
ACCESSION   WP_009673872
VERSION     WP_009673872.1
KEYWORDS    RefSeq.
SOURCE      unclassified Paenibacillus
  ORGANISM  unclassified Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="unclassified Paenibacillus"
                     /db_xref="taxon:185978"
     Protein         1..365
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=40959
     Region          6..365
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 mkiepkdtit qgqlflliik lqigvgilsl pyrlhqlakg ggwisvliag vflqlilvmm
       61 wmlmkrfpsy svfriasavt gryagafigi ayvayfllvg gvvmmgafdi inrwilqntp
      121 rwavlflfml tgvylirgtf rtitrifilf tfligpmmfl igygvhranf lyllplneag
      181 iwnilisske titamygfel iliiypyvkg nhagklkavs agtwfvvlfy aftvftcmav
      241 fsphqlnmip epvmyllrsl pfgamdradl lflpiwmism vasmtgycya aafgighllk
      301 hknhkkaapf aviiscaiay lpqtkdqfel fsyiadasay ffligfplll lllsyalkkk
      361 egeta
//
LOCUS       WP_009675362             217 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [unclassified
            Paenibacillus].
ACCESSION   WP_009675362
VERSION     WP_009675362.1
KEYWORDS    RefSeq.
SOURCE      unclassified Paenibacillus
  ORGANISM  unclassified Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 217)
  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   2  (residues 1 to 217)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="unclassified Paenibacillus"
                     /db_xref="taxon:185978"
     Protein         1..217
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=22152
     Region          145..214
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mlnwnfqswk srgvlagsaa viaaglgvwl lvsprgtvpq gftalnasma qtiegtkpvs
       61 psekpsspss sakteakeev gagskqagae dsaagatggg seqapassrk gaaaddnpaq
      121 adqqrnvagg neavpgkkes ggpaadkkip pgpkidinta nlqqlmelpg igeskgkail
      181 ayreqhgkfk raeqlldikg igekmlakmk pylqinp
//
LOCUS       WP_009674839             436 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: amidohydrolase family protein [unclassified
            Paenibacillus].
ACCESSION   WP_009674839
VERSION     WP_009674839.1
KEYWORDS    RefSeq.
SOURCE      unclassified Paenibacillus
  ORGANISM  unclassified Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 436)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="unclassified Paenibacillus"
                     /db_xref="taxon:185978"
     Protein         1..436
                     /product="amidohydrolase family protein"
                     /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=46633
     Region          8..431
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mekiiqnaal eqvtaitnvr ifdgvqiiap rhvvikgesi isvggdlptd atiidgenat
       61 llpglidahv htsigglrda lkfgvttele mngdftkrgr eiqlknvndv advrsagtai
      121 tapgghpdel lpdgdeipef vlkeleklse edreamlaay ahdheeipqv ttveeaikhv
      181 htqvengady ikimieegtv mgapglpvls deilktavte ahkfdklvia hvltarssqe
      241 aidfgvdglg hlfidrpeyt selvksiads gafvtpclvl nssiignpas elandprvhs
      301 klspdwidil nssfntfpqg nlensfknvm dlhragvdil vgtdvapvpv pnlgglahga
      361 svhhemqllv kagftpieal qsatskparc fglhdrgrit egaradlilv ngdptttisd
      421 tlsiksvwfn gsqqlg
//
LOCUS       WP_009673892             289 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Paenibacillus].
ACCESSION   WP_009673892
VERSION     WP_009673892.1
KEYWORDS    RefSeq.
SOURCE      unclassified Paenibacillus
  ORGANISM  unclassified Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 289)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 289)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="unclassified Paenibacillus"
                     /db_xref="taxon:185978"
     Protein         1..289
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32273
     Region          21..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..287
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mnglekmnsa layieanlad didfkevarl avcseyhfkr mfstlagvtl seyirrrrlt
       61 laafelantd lrlldvavky gysssdsfar aflslhginp seartrgqsl kayprmtfql
      121 tiqggsemny rlvekdafri vglkkrvpli yngvnpeiaa mwgnlnmeti tllkslsnve
      181 psglisasvn fsegrlesge ldhyigaatt kdcpdhltql evkastwavf eavgpfpetl
      241 qnvwgriyse wfpssgyest egpellwnes kdtssptyrs eiwvpvvkq
//
LOCUS       WP_009675842             258 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: prolipoprotein diacylglyceryl transferase
            [unclassified Paenibacillus].
ACCESSION   WP_009675842
VERSION     WP_009675842.1
KEYWORDS    RefSeq.
SOURCE      unclassified Paenibacillus
  ORGANISM  unclassified Paenibacillus
            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 10002130
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="unclassified Paenibacillus"
                     /db_xref="taxon:185978"
     Protein         1..258
                     /product="prolipoprotein diacylglyceryl transferase"
                     /EC_number="2.5.1.145"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008961 -
                     phosphatidylglycerol-prolipoprotein diacylglyceryl
                     transferase activity [Evidence IEA]"
                     /GO_process="GO:0009249 - protein lipoylation [Evidence
                     IEA]"
                     /GO_process="GO:0042158 - lipoprotein biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28499
     Region          3..252
                     /region_name="Lgt"
                     /note="Prolipoprotein diacylglyceryltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0682"
                     /db_xref="CDD:440446"
ORIGIN      
        1 mtfpvyinlg firlhphlvf ealayfigfr lylytrskek lqasqalwvl vgatlgaaag
       61 skalywledp altlqrwndv sylmegktiv ggllggligv ewtkkright rstgddmalp
      121 lltgmmigri gcfltglddh tygtptgwvt gvdfgdgilr hptqlyeiaf llllgitila
      181 lknrarhrsv plpdgmsfii fmggyllfrl lidfikptph pyaglnniql aciagliyyt
      241 lllwrklsak ptligkgt
//
LOCUS       WP_009676651             394 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [unclassified
            Paenibacillus].
ACCESSION   WP_009676651
VERSION     WP_009676651.1
KEYWORDS    RefSeq.
SOURCE      unclassified Paenibacillus
  ORGANISM  unclassified Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 394)
  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   2  (residues 1 to 394)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="unclassified Paenibacillus"
                     /db_xref="taxon:185978"
     Protein         1..394
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44333
     Region          328..389
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mhskttqeai ivlkesikel esskgsvlvg iqkllrvskm isdesciiwg eiqlgntkyt
       61 qplenyidml vatnksntka nltklnevte elkklgvdid ehcsleelnv kanksgggyk
      121 nigfieeryn dlvrtkkgnd gtyyknnlnn hlnyvrktah erasllyntl afsdapqsaf
      181 dilkfviddk lldinpelae klmqafksvs tdnseewsha ltscrrlien ladelfpatd
      241 elyngrslgk nqyinriwaf mdrsissdsn rdlakihvdf vgsylqrlhk ltnkgvhaql
      301 sraeaikavf hvylicasil eyhdvqqkgv sekmnihtas ldeleavldi nrnmakeivk
      361 mrvakgrlsl ddistikgvg aktiskiqdt vsfd
//
LOCUS       WP_009676159             368 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GerAB/ArcD/ProY family transporter [unclassified
            Paenibacillus].
ACCESSION   WP_009676159
VERSION     WP_009676159.1
KEYWORDS    RefSeq.
SOURCE      unclassified Paenibacillus
  ORGANISM  unclassified Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="unclassified Paenibacillus"
                     /db_xref="taxon:185978"
     Protein         1..368
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=40492
     Region          1..360
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 mndqrltnwq amcilistia gvgvlplprl avtagetaap lvtaggillg allimlwsll
       61 gmrfpdlspv aysklilgkw asgallvvia lfylvatafs frefsevtgt fvlrrtplev
      121 ilfmmlllvv lsarkdiysf tlihafytpf vvgpvvvimm lsfkevelln lqpfttnpdf
      181 tfwigslgit tlfrnvviyt fivprmrnpq kalkvgltgt aisgglylvi vittvgvfga
      241 eeikrlvwpt lelgrativp geflermdai flvtwiisvf nsllsgyyli lliikeelgl
      301 kdhrmlatfl mpfmflaamm pqnviqlyrl sthilpwgli amivipsall liagirgkgg
      361 vahapdkd
//
LOCUS       WP_009681404             100 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [Pseudomonas].
ACCESSION   WP_009681404
VERSION     WP_009681404.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..100
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10994
     Region          1..100
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mrptdairgk eadirrliea ygfiepklfg saargddheg sdldllaiip pamagkislf
       61 diaeledelq amvgvpvdfh ahnnmpehlr qsieremvtl
//
LOCUS       WP_009679169             363 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Gordonia
            neofelifaecis].
ACCESSION   WP_009679169
VERSION     WP_009679169.1
KEYWORDS    RefSeq.
SOURCE      Gordonia neofelifaecis
  ORGANISM  Gordonia neofelifaecis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Gordonia neofelifaecis"
                     /db_xref="taxon:945692"
     Protein         1..363
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37995
     Region          10..343
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msgerlaari evrrsgftva adfvvpggec lailgpngag kstvlgavag lvgmadgeir
       61 lgdrlldghe hdrrvhvppe rrrialleqk srlfphltva enlafgpraq grsrrearav
      121 aagwlerigl pdvgawkpnr lsggqqqrva iaralaaepe allldepfaa ldaesapair
      181 rmladelart gttgllvthe ltdawqlasr clvldegavv eaatpaelaa apghpfsavl
      241 agysvvegrw tdgalvvgda vlpavgdgei rdgarafgiv vpqevtlstt sgavrsrvsa
      301 vsvhagrvrv esesglvaei pvgatapavg ervwltpvgm rvlgeadgir aarrqtrace
      361 prf
//
LOCUS       WP_009683307             378 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Pseudomonas].
ACCESSION   WP_009683307
VERSION     WP_009683307.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 378)
  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 378)
  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   3  (residues 1 to 378)
  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   4  (residues 1 to 378)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 378)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 378)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..378
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40080
     Region          30..365
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(104..106,127..128,177,229,254)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 msqtfykkgf lalavatalg vssyvqadvk igvagpmtga naafgeqymk gaqaaadkin
       61 aaggvngeki vlvkgddace pkqavavanr lvdqdkvigv vghfcssnti pasevydeag
      121 viaitpgstn pqvterglsa mfrmcgrddq qgvvagdyiv dvlkgkkvav lhdkdtygqg
      181 ladatkaqle krgvkpvlye gltrgekdfs avvtkiraag advvyfgglh peagplvrql
      241 reqglkdvkf msddgivtde lvstaggaqy vdgvymtfga dprllpdska vveefrkagt
      301 epegytlyay aslqalaaaf ngaksnkged aakwlkanpv qtvmgekkwd skgdltvsdy
      361 vvyqwdkdgk yhqldkqk
//
LOCUS       WP_009683498             797 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [Pseudomonas].
ACCESSION   WP_009683498
VERSION     WP_009683498.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 797)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 797)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..797
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86273
     Region          68..119
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          95..797
                     /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 msstpvpqrh plsramhaai lglvvsspal palaqpagad halqlqqwni pagplapald
       61 rfarqagvsl afdaqtvanr ttpgvqggla tpaalsallq gtdlqveqqg pqayqiiaqa
      121 paagplelga tedyrlapvi inakvkasad ddlnsvvake lwvggkvats ilntpasvsv
      181 vtrkemeqrs vstteealqy spgvvsdfyg sddrndyfqi rgfqattyrd gltlssmrgv
      241 redpyayeri eilrganstl fgpadpggsv nfvtkqprfe kfgqgyvtyg sydhaetgid
      301 vgdalndeqt lagrftaklq nsdreydhsq ddnrfvmggl twapsdftsa tvildylktn
      361 sspnsggypl dkeydrsdfy gepgynfhdv ertslsasit hdfdngftlr snlryselsd
      421 dfgyvylsds aervgtvipr yvfgtdtdad qlngnlmlqy daqfehidss tlvgveylds
      481 tnkqrsvysl apsidianpv ftgvpggitp ysrekndatt kavflqqnls fydrviatvg
      541 mrndsmdlts teyvggvnrq sdtfsetsyr galtyivnde vstyvsmves vsppqvgvtp
      601 qtgrqyevgv kysplgmdam fsaavydltq envtiavvlp sgiieqqtvg esrargldle
      661 akaqvtqnls ligaysymdt evlrgslydg sslkgkaftv apkhtaslws yydipdtdvs
      721 vglgaryvgg yfmdaantkk sdgttlfdaa lnykiakgtd lalnvsnlfd eqhvvgsgta
      781 dyynpgrevt aklsysw
//
LOCUS       WP_009683581             262 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Pseudomonas sp. TJI-51].
ACCESSION   WP_009683581
VERSION     WP_009683581.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. TJI-51
  ORGANISM  Pseudomonas sp. TJI-51
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Pseudomonas sp. TJI-51"
                     /db_xref="taxon:985010"
     Protein         1..262
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=29272
     Region          22..178
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mlstlkktli tfllftvagc stglridrsh psanqdnriq fvvlhytnas lerslallth
       61 gevsshylig dgpatvyqlv desrrawhag dsqwqgrtwl nsssigieiv npgfadtpng
      121 rvwypyseaq iqaliallkd ivkrnniepr hiighsdiap lrkldpgplf pwkrladagl
      181 gvwpdanava qqqayfnvnp psvgwyqqel arfgyqieqt gvldvatrhv iaafqmrfrp
      241 qrfdgmpdaq tsamlqvlnr tr
//
LOCUS       WP_009683660             353 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_009683660
VERSION     WP_009683660.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 353)
  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 353)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 353)
  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   4  (residues 1 to 353)
  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 353)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..353
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39364
     Region          22..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          248..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mserttsasw asgivkalel egldcramfk qlgldfaald dpdarfpqds mtrlwqlave
       61 lsgneaigln marvvrpasf hvvgyalmss rtlaegferl vryqriiaes sdlsfvlgpe
      121 gysliltvhg dhlpptrhsa easlacalal ckwlsgrpvq prrvlvqgpq prniepykva
      181 fhsplifdap ydalvferad meaplptane amavlhdrfa geylarfses rvthrvrqvl
      241 crilpqgepk retlaqalhl sqrtlqrrlq eegtsfqall ddtrrelaeq ylaqpgmtll
      301 etayllgfad psnfyrafrr wfdttpseyr arlgavgegl sdartpactt lar
//
LOCUS       WP_009684638             298 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Pseudomonas].
ACCESSION   WP_009684638
VERSION     WP_009684638.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            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="formate/nitrite transporter family protein"
                     /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=32750
     Region          24..277
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msveqsektp glsadeeqev shnqppraav lhetiryqgd qelertlaal wwsavaagls
       61 mglslmamgl fyarlpeges aqvvasigys agflavilar qqlftentlt avlpvmtspt
      121 lanfgrllrl wgvvllgnla gtllvawvml elpifdsktd mafleigrkv msndisqmfa
      181 kgivsgwmia tmvwmipsme nakiwiilmi tylmaigdft hivvgsvevs ylvwageetw
      241 rsfwlefalp tlagniiggs fifalishaq vrsdsgkaps rlleheraqr qrgkddtk
//
LOCUS       WP_009683757             361 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_009683757
VERSION     WP_009683757.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 361)
  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 361)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 361)
  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   4  (residues 1 to 361)
  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 361)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..361
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39715
     Region          27..210
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          260..339
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 marprvrlge lsvgfvqplt ealrelghap epllrrygle aprlseanar lsiprymhlg
       61 haaieqcgea alglhmgrls rlaqaglagv taaqaptvge aartllrfep lyaanyrgqs
      121 sfhedaegaw lrfysispyn aynrfvvdsv lagwlaqlad lagvalqaer leiefaapay
      181 aaqyqalcst pvqfaadgnq lrlsratlql anprhcpstw qhllqlcead mlqrtrvrsl
      241 gerithllgp llnggrepel vevalhlqlp twtlrrklae egtrfrdlln etrrdlaety
      301 irdtelafge iayllgfasa eafqrafkrw tgltpgefrr sqrragqssv assagsgvss
      361 s
//
LOCUS       WP_009685274             244 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Pseudomonas].
ACCESSION   WP_009685274
VERSION     WP_009685274.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 244)
  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 244)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..244
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26993
     Region          20..67
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msmelmvkam ktkvgnplrk lvlikladna sdqgecwpsy qhiadqceia rstvkthire
       61 lekaglvrre frrngelnqs nvfhlnlwgg aadalwgraa enppgaaenp gggaaaaprt
      121 shlsepvkep kpmctsvadg feqfwklypk kksrkdalka wnklspeael qavmitalaq
      181 hcvsrdwtkd ngqyipmast wlngerwhdv lqpagataqg gafnnlphht ddmyqeshdg
      241 rpnf
//
LOCUS       WP_009685500              84 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Pseudomonas].
ACCESSION   WP_009685500
VERSION     WP_009685500.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 84)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..84
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9176
     Region          5..79
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mregatrlat sertlarlve sttglsfgrw rqqlhlmial sqlaegvsvq rvagilgyds
       61 vnafitmfkk algksptqyf sslr
//
LOCUS       WP_009692001             285 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Burkholderia pseudomultivorans].
ACCESSION   WP_009692001
VERSION     WP_009692001.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 285)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..285
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=30664
     Region          36..263
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mievsgigmg skpdgmmspv slesdvsesd kdermhasrq peisveyqpv aslrtglvtg
       61 fdavprwhrp saglsaadre tappfpllva evcaqlerwn aqgnkpafvs lalplqqdsr
      121 sdgvgllgea vrqhrlsssq itleisaqfl stdtarlgae lkllrktgyr valanfgpgh
      181 asisklmelp ltgvkfgtsf tatladsats railtsvthl ardlglsvtv agidrqrefd
      241 vlrdyldlyw qgallcpplp aealakrles sfsqrfrsqc agvdk
//
LOCUS       WP_009689390             278 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Burkholderia cepacia complex].
ACCESSION   WP_009689390
VERSION     WP_009689390.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..278
                     /product="formate/nitrite transporter family protein"
                     /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=29356
     Region          2..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 maylapaefv akmvdagesk lsmstrdtli raymagaila lsaafavsit vntgnplvgs
       61 llfpvgfcml yllgfdlltg vftlaplavl dgrpgatwsg vlrnwalvfc gnfagaltva
      121 vfmaviftfg fseapnligq kiggigeart lgyaahgaag mltlfvrgim cnwmvstgvv
      181 aammstsvsg kviamwmpil vffymgfehs vvnmflfpsg lmlgghftll dyllwneipt
      241 vlgnlvgglt fvgatlysth yktapkrrps agiatrea
//
LOCUS       WP_009692963             132 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_009692963
VERSION     WP_009692963.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (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   2  (residues 1 to 132)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 132)
  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 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   5  (residues 1 to 132)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..132
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14998
     Region          11..100
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(30,49..50,68,71,79..80,92,97)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mdckylyidd ikinfvrrti eiankpvdvt prefdvvefl ldnmnkivpr qaiqeavwgr
       61 elgvssrtld thisrirskl qldhdknlri ipiyavgyrl vlfgaamthv erheaapilr
      121 aapqpamaad ya
//
LOCUS       WP_009693193             233 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_009693193
VERSION     WP_009693193.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..233
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=25531
     Region          1..>225
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mslvvdirkt yataerrftl dvsftattqr vvlfgpsgag ksmtlqaiag llapdegtim
       61 lngeplfdaa rgidvptrar rvaylfqdya lfphlnvrqn iafgltsglr npraktlppe
      121 vaywlrafel ealagqypsq lsggqkqrva laralvaqpr mllldepfaa ldgamrqrmr
      181 helaelqarl dipmvlishd pddvaafgdq vvqlndgrvq aatphtewpt rva
//
LOCUS       WP_009696245             333 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Vibrio].
ACCESSION   WP_009696245
VERSION     WP_009696245.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 333)
  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   6  (residues 1 to 333)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..333
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37838
     Region          31..197
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <249..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mktvrfiram gilnmhnlal skynlsseel gipssvfhnp mtlvplkava ewyrrveqls
       61 ndpdvvlnls rgielqklgp vgrwlfsgnd lastirrvny gvsnlqsgaf fageqsgkii
      121 kwtyhnpfve tsvkvhdsir caifmikilr eflgqdykpl rvmisgsrkn gelykeyfgc
      181 evewsqpkte iwingddrla srqvihredn rlamsfsdld dllnmpdped elkviyevvh
      241 ysshyglptl ervsallgls dqqfqrrlhk lglnfstvsg yvlsnvaagl lskhvsiedi
      301 avrlgytnva sfnrmfkkhr gltpkqyaar lek
//
LOCUS       WP_009696507             270 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio harveyi].
ACCESSION   WP_009696507
VERSION     WP_009696507.1
KEYWORDS    RefSeq.
SOURCE      Vibrio harveyi
  ORGANISM  Vibrio harveyi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 270)
  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 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   3  (residues 1 to 270)
  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   4  (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   5  (residues 1 to 270)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Vibrio harveyi"
                     /db_xref="taxon:669"
     Protein         1..270
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30172
     Region          16..268
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <174..268
                     /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 msdsdnpkap lykeimlpkp aelitlpsym dchdhaytqi viglkgqaef evrgqgnlvg
       61 pgqgcivtas sdhafggvih qsdilvlnmp kpanddpeml qkinnlersh lyfqldgqiq
      121 kliqmlvqem rnhpddllls racndtvial mqrhisafet srkesrfdld aidryieqhl
      181 shkisvaqla gsvflgesqf hslfkdqmgi tphqyvlgkr idmardlieq ghltlgqiae
      241 ftgfssqstf thtftrlqgl spsqykkqvg
//
LOCUS       WP_009696782             265 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Vibrio].
ACCESSION   WP_009696782
VERSION     WP_009696782.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 265)
  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 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   3  (residues 1 to 265)
  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   4  (residues 1 to 265)
  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 265)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..265
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30206
     Region          26..262
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <164..262
                     /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 mehiqyyatd hdnlslieak yqkfafqrhy hldfhlglit hgaqkfqyqg nshqvghgqi
       61 vimppdelhd gqsklesgye vnvfaiephl lsdladlkqn gqiihfneli isdpqifsql
      121 snlhgllrre nlsqltkdcl pfegfnqlfd rygslerqkv vplgnqslgt lkdylmanld
      181 qavrldslse lcqlsptqfq rhfkaqtgmt pyawfarlrl eqgmkllqsg qcgtdvahqi
      241 gfydqahfsk afkqtygvsp sqvtr
//
LOCUS       WP_009698760             153 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Vibrio].
ACCESSION   WP_009698760
VERSION     WP_009698760.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..153
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16750
     Region          5..153
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mleafnaafe nlalwfsdsa lwvlfitgfl satllpggse agliatlsln qysvssiiiv
       61 atigntlggl tnywlglwip nrtqdekhgh talkwlskyg ywglffswlp vigdplclaa
      121 gwlrmkflpc lvliflgkaa rysllaaiyl glf
//
LOCUS       WP_009699139             706 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Vibrio harveyi].
ACCESSION   WP_009699139
VERSION     WP_009699139.1
KEYWORDS    RefSeq.
SOURCE      Vibrio harveyi
  ORGANISM  Vibrio harveyi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Vibrio harveyi"
                     /db_xref="taxon:669"
     Protein         1..706
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=78031
     Region          50..706
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mlyqnmdgnp qaklrlsvla taiasvtsmn afaasepqtt tmetvvvtas vignsaiedv
       61 keypgartvl tseqiektaa hsidsalqsv pgikvqdetg tgvlpnisvr glkasrsgha
      121 qflmdgvplt lapyghtgqs ifpatlsmid ridivrggaa vqygpnnvgg vinlvtkpip
      181 ntwqteisnr ltvfeggdtp lndfylrtgg wltdtfaiql egnflkgesf rehsdtdvkn
      241 fqvkanwlls dtqelqafiq rydadtqmpg alspddykkd rnqskrpyde yqgkstrwsl
      301 kyiqdlniad saelqvqafg hnserffqwg fngagghwad palpstdvrt sprefkvygv
      361 epklamhfge gsavtqnwiv garyvnedid ykltqtpiag gatkvprdwh ldtdafagyi
      421 snevglfnda lkvtpgirye svdmtfddlg kaqstdnkvt ewlpgltvay nlteqwvgya
      481 naqkslrapq iayirglgke gselawnyel garythdsts fnaalyridf kdqlqwqsat
      541 qtfenigktl hqgielsary vpesvqalsl gasynyldat leeegankgn qlpytskhql
      601 swdatyafsk vdttlsgyyf sdaysdnant sdedatgakg kvpaymvwnf nlgtdlykdd
      661 kgklrmnvav nnlfdedyyf rgidtspvgr ypapgrsytl dlnyqf
//
LOCUS       WP_009699381             379 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Vibrio harveyi].
ACCESSION   WP_009699381
VERSION     WP_009699381.1
KEYWORDS    RefSeq.
SOURCE      Vibrio harveyi
  ORGANISM  Vibrio harveyi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Vibrio harveyi"
                     /db_xref="taxon:669"
     Protein         1..379
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42806
     Region          1..270
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          267..353
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkfihtsdwh lgrqfhnvsl lddqqavldq lihyiennpv davvvagdiy drsvpptiai
       61 ellnkvvkri cgelntpmil isgnhdgaer lgfgseqmkn aglhiisnfe dmltpvviet
      121 esagqvafyg mpyndpeqvr fayqepvsth dqahkllaek iaeqfqseqr nvlvshcfvd
      181 gaieseserp lsiggsdrvs hehflnfdyv alghlhqpqk kgeeyirysg slmkysfgeq
      241 nqkkgftlve idqngfvsae hinlaaphem rivegeleqv ieqgktdpkn edyllvrlmd
      301 khailnpmek lrtvypnvlh lekpgmligv eqemaqakla rseidmfrdf fseaqdsqls
      361 qeqdqaisdi ikqlsqqaq
//
LOCUS       WP_009704598             193 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Vibrio sp. HENC-03].
ACCESSION   WP_009704598
VERSION     WP_009704598.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. HENC-03
  ORGANISM  Vibrio sp. HENC-03
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 193)
  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 193)
  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   3  (residues 1 to 193)
  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   4  (residues 1 to 193)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 193)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Vibrio sp. HENC-03"
                     /db_xref="taxon:992012"
     Protein         1..193
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21786
     Region          <54..193
                     /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"
ORIGIN      
        1 mtqstsktpi ivccdslqeq arlsgllskd ydnimgcqla qletlmqrep sasvvvgwqq
       61 ptaelrlivd fcrrksapll ivlkqlsshd inrlsekmdy vlmphdsefa lqpwiehatl
      121 vrtkfesmqs eieslthkie erklvekakg llmkmhsvde eqaykalrns amqssqtlaq
      181 vaknlittle vld
//
LOCUS       WP_009703629             288 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Vibrio].
ACCESSION   WP_009703629
VERSION     WP_009703629.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 288)
  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 288)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 288)
  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   4  (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   5  (residues 1 to 288)
  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 12820790
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33813
     Region          37..285
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <168..285
                     /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 mahiekvpqr pgfswryrri depkkeydfh fhddvyelvi hrhfsgtlhi ghhelevthn
       61 qmlliapgvp hsihstlven ncethviwfk rewianlmfy ctelrkldpl lkaankgvvf
      121 sertaqqvvg llhelmkvpa meqlarfihv lsllahdeaa ktlmthsyls mseheqqere
      181 rvakvsayle qhfarkitla dlandlslse savtrlfkkh fkepfsqrlm klrinhaadl
      241 lqstelpigi vfervgyrnq alfnrhfkty kgltprdyrq hyqqriqp
//
LOCUS       WP_009704962             786 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: Lon protease family protein [Vibrio].
ACCESSION   WP_009704962
VERSION     WP_009704962.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 786)
  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 786)
  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 786)
  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   4  (residues 1 to 786)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..786
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..786
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=87831
     Region          65..786
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mavqrlepkq lysvadlenm pckstkelpp ideivgqera qkavefamsi kekgyniyai
       61 gqnglgkrtm ilrylnrhqh daaalfdwcy vanfedtrip kvlklpcgig sklkvdiekl
      121 mgkllnalpl afdnemyysr adrlknqlan kqqheldsis keakekgisl titaqgdyqf
      181 vamdgeelht eesfealskk eqeyfgssid elevslrnmv reltewedsf sekikklndd
      241 vtldvithfi kqlkvdyaey peiktyltdl qkdivenadi fleqsgeqge iatasldkkl
      301 prrykvnvlv srkdcefpiv veenpnyhsl fgsietatfk gtvftdfsli ragslhkang
      361 gvllmdaqkv leqpyvwdgl kralrsrqls ftslekevtl tgavsldpep ipldikiilf
      421 gdyrtyqllq hydpefgelf rvtadfedem krtpdselqy arfissvvnd nnmlhcdkka
      481 iariieyssr lsgdqtklsl hsanianllr esnyvarqan snmirighve ealsnqemrv
      541 srlqdsvmet fvngttlirt egsavgqvna lsvlstsdhm fgapnritat tcygdgevid
      601 iersvdlggs ihskgvmils aylssvfgkt arvpltttit feqsyggvdg dsasmaefca
      661 vvsafskqpn rqdiaitgsm nqfgeaqpig gvnekiegfy dvceikgrha gqgviiprsn
      721 vhnlmlrpdi vkavekgdfh iwaidhvtea velftgkdag eatdegtypi dtifglaqak
      781 lnalrk
//
LOCUS       WP_009704992             738 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Vibrio sp. HENC-03].
ACCESSION   WP_009704992
VERSION     WP_009704992.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. HENC-03
  ORGANISM  Vibrio sp. HENC-03
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 738)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 738)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Vibrio sp. HENC-03"
                     /db_xref="taxon:992012"
     Protein         1..738
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=83378
     Region          205..723
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mnkaasarri kamlfltlgv tlsvfagfal sqmfviekda fqlisvvssv mvvsflryqw
       61 ralpaivlsl mayyfftgrs fehallyslt vpilpfafss lfhylnsrsl hqpaarrisl
      121 ffiiigclfp fvntvkmmlv ntfvdgqfls adflfyatlg nyltqllvtp ilyvvvsllt
      181 dtdtqsylal dkrlrvsnnr cqsyitwlvs cvaiffaaal ssssfmlnsl sffavllvvv
      241 glakhglirp lfvgspfill ilndgirhfn egligdkqfy glliiitvlt tlayllggys
      301 vklfemtqrq irseridpys glsniaqlke dishqsrsll iyldltptls mltdlghegk
      361 sqlimqlsef lysrnnsinr cyrppfstgl lsfthysdta eddlnevaky lesfqfywrg
      421 tsvalvspti fctlvsqdqd iekvvsilcd qppqndssih wvniqsfemd rvdklnhiqq
      481 vfkreqfelf cqpymklses epskhsfevl lrlkerdgqv lppsaffpli nqfglelkld
      541 hwvilntfrm lsdkvknwde ighcainlta ktlsaenlaa riiesaqsfs iplnkicfei
      601 tessalineq qaiatlnylr nqgckiaidd fgtgyasfay lrrlpldilk iegafvreit
      661 qnetdrlivs siatvakemh letvaefves tvhiailrgl gidfaqgygv akpmplseyl
      721 delfkashka qqpeletl
//
LOCUS       WP_009705311             378 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Vibrio sp. HENC-03].
ACCESSION   WP_009705311
VERSION     WP_009705311.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. HENC-03
  ORGANISM  Vibrio sp. HENC-03
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Vibrio sp. HENC-03"
                     /db_xref="taxon:992012"
     Protein         1..378
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42709
     Region          1..270
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          267..353
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkfihtsdwh lgrqfhnvsl lddqqavldq liqyiennpv davvvagdiy drsvpptiai
       61 ellnkvvkri cgelntpmil isgnhdgaer lgfgseqmkn aglhiisnfe dmlnpvviet
      121 esagqvafyg mpyndpeqvr fayqepvsth dqahkllaek iteqfqpeqr nvlvshcfvd
      181 gaieseserp lsiggsdrvs hehflnfdyv alghlhqpqk kgeeyirysg slmkysfgeq
      241 nqkkgftlve idqngfvsae hvdlaaphem rivegeleqv ieqgktdpkn edyvlvrlmd
      301 khailnpmek lrtvypnvlh lekpgmligv eqemaqakla rseidmfrdf fteaqdsqls
      361 qeqdqaisdi ikqlsqqa
//
LOCUS       WP_009707170              99 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Vibrio].
ACCESSION   WP_009707170
VERSION     WP_009707170.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 99)
  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   2  (residues 1 to 99)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..99
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10701
     Region          38..97
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkwmltlcll llapmswaee gksattkaak yegieitvnv ntataeeiat llngigkkka
       61 qdiveyrneh gpfktaadls kvkgigeatv kknqdrill
//
LOCUS       WP_009711103             351 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Kroppenstedtia eburnea].
ACCESSION   WP_009711103
VERSION     WP_009711103.1
KEYWORDS    RefSeq.
SOURCE      Kroppenstedtia eburnea
  ORGANISM  Kroppenstedtia eburnea
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Kroppenstedtia.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 351)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Kroppenstedtia eburnea"
                     /db_xref="taxon:714067"
     Protein         1..351
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38099
     Region          20..342
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mgaellnver tvntsglsvp vgisgtgmyv pdqlvtnedl vqnldtsdew ivtktgirer
       61 rflregelts dmcvkaaeaa madagvtpgd ldaiiistft fdqllpstal ivrerlgadr
      121 aipidlnqaa cagsiyaiwt gchlmqnqqi rcvlvigaea lsritdpedr strvffgdaa
      181 gavvlnrtqs nygilswdld aalsysvevp aggaksptta dtvrqrehfl kmdgrkvwte
      241 anqrlpntiq svikkaglhf geidhflihq anlnivkevf ntlgesmska tnnvdrfgnt
      301 gaatvftvlh ealargrikh gdriimaaig agfiwgslcf rysdeswkgd q
//
LOCUS       WP_009713023             298 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Streptomyces
            himastatinicus].
ACCESSION   WP_009713023
VERSION     WP_009713023.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himastatinicus
  ORGANISM  Streptomyces himastatinicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            violaceusniger group.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Streptomyces himastatinicus"
                     /db_xref="taxon:998084"
     Protein         1..298
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31273
     Region          19..262
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mtsaaeqpvt iavqggyela eggrwvggrf vyvdilsgrl felrdgigrt prqlarldvp
       61 lgavapvrdr pdtwiaaagt gialltadgt lewldrpedr tpvpsrmndg vadpagrfwa
      121 gsmpydgtpg agslyrtdhd gtvvrvldgl tivngpafda dgttlylads aagtihrcrv
      181 dpatgdltgp etfarfrtde gspdgmtvdd egclwvavwg ggavrryhpd grllhtlevp
      241 apqptsvclh psdsrilitt arhgltnpta asgavlsapa parapdthsw grggpapr
//
LOCUS       WP_009713473             280 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptomyces
            himastatinicus].
ACCESSION   WP_009713473
VERSION     WP_009713473.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himastatinicus
  ORGANISM  Streptomyces himastatinicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            violaceusniger group.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 280)
  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 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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Streptomyces himastatinicus"
                     /db_xref="taxon:998084"
     Protein         1..280
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30132
     Region          5..265
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          181..264
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mrfaprlggm vasavgyrsg gqppalhrgl pspwltlifs ldgpvtsglt leqargadav
       61 rtdivvgglh qspayiiqpe hetgvqlalh plaarrllgl pagaltdqlv vsgtevlgar
      121 aaeihermre qpgweerfal lgsylraraa aadeatpvrr eiveawawla rhrgagtlrg
      181 laehvalspr rltalfraet glspkqaarl mrfehakgtv vrsyaagapa dlarvaadcg
      241 yydhshlvrd frqytgvspt vwlaeecrni qagghrngee
//
LOCUS       WP_009698650             370 aa            linear   BCT 20-JAN-2025
DEFINITION  ATP-grasp domain-containing protein [Vibrio harveyi].
ACCESSION   WP_009698650
VERSION     WP_009698650.1
KEYWORDS    RefSeq.
SOURCE      Vibrio harveyi
  ORGANISM  Vibrio harveyi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10792831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Vibrio harveyi"
                     /db_xref="taxon:669"
     Protein         1..370
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=41846
     Region          1..370
                     /region_name="PRK06849"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:235876"
ORIGIN      
        1 mrilitgara pvalewaamc mnhghdvvlt dslaqplgaf lrgiehyvkt asprfsfpty
       61 qqqilnlltq qridmviptc eevyylahia qqcprvhffl pnstllrslh nkftvfdqlr
      121 dlpkislpkt rlvtdkhdie idagsvlkpv ysrfggevir ditrqsistl tmstqhpwvq
      181 qekihgapic nyaifehgqm rahqaylpkn cvngsaasaf qpvfddrlda fmtafghrhr
      241 yhgqvsfdfi qtnnelyiie cnpratsglh llspqciqlf pelafsfptk pqlhhlgavs
      301 liaqgllslf ktntwrdwls gvnvmqqhnl pirsqmlsvf ellqlarknk vklaaastvd
      361 iewngeelps
//
LOCUS       WP_009713523             415 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces himastatinicus].
ACCESSION   WP_009713523
VERSION     WP_009713523.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himastatinicus
  ORGANISM  Streptomyces himastatinicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            violaceusniger group.
REFERENCE   1  (residues 1 to 415)
  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 415)
  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
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 415)
  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   5  (residues 1 to 415)
  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   6  (residues 1 to 415)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 415)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 415)
  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 15726307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Streptomyces himastatinicus"
                     /db_xref="taxon:998084"
     Protein         1..415
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43243
     Region          13..>69
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          75..392
                     /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 mkrtsrdirt anrygvlrhi vaespvsrqe vaaatglsla tvanlvgell elgmlvevgy
       61 edsdggrprg lvavnssgga ligvdvaety vhvelfdlal tvlaradqel rperpeendp
      121 tkvvahiaaa vasvvgqaei apdrvlgvgi smpgqvdreg gvsvfapnwd whdvpllrml
      181 adhipyplyl dnplractva eqwfgaargr gdavvvnlgt gvgaglalgg alhrgvsnsa
      241 gewghttlil dgrqchcgnr gcvetyvgap gimrnlrels pdspllradd qtatiealgr
      301 gladgdpvaa qvvrdtaryl gagladlinl lnpevivlss wvaaalgegl laevreavag
      361 ralrrplast eivlcpipsn pvslgaatfv legslasvgl khrrptaart gatsa
//
LOCUS       WP_009715993             224 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Streptomyces himastatinicus].
ACCESSION   WP_009715993
VERSION     WP_009715993.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himastatinicus
  ORGANISM  Streptomyces himastatinicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            violaceusniger group.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Streptomyces himastatinicus"
                     /db_xref="taxon:998084"
     Protein         1..224
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=23531
     Region          4..214
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 msrrrpwvvg vsgasgtpya asvlrallha geavdlvisr asrltlldet gigfrdahwr
       61 edlrrwlarg adgtpdafdv pvdsadvthw aagdlaagps sgsyevkgml ivpastacva
      121 gvalglskdl lqraasvtlk errplvvavr etplngqtlr hlvtldeaga vvlpaspafy
      181 agathiqdlv dfvagrvlda agvphklyrr wegelggdrg petg
//
LOCUS       WP_009716661             423 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Streptomyces himastatinicus].
ACCESSION   WP_009716661
VERSION     WP_009716661.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himastatinicus
  ORGANISM  Streptomyces himastatinicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            violaceusniger 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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Streptomyces himastatinicus"
                     /db_xref="taxon:998084"
     Protein         1..423
                     /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=45803
     Region          36..299
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mnisslrraq rapapgpvpp pvsssvplpv psssaapkqr daffdnakyl aivlvamghs
       61 weplrdgsra asalymfvya fhmpafilis gyfsrnfdfr adrlkrlltg vvvpyvifes
      121 vysllkgwag ddpsypisll dpwyltwfli alfvwrvatp vwrivrhpvp lslaiaalas
      181 cspdigddld lqrvlqflpf fvaglhmrpe hfrmvrrrev rmvalpvaaa alvfaywavp
      241 rmnagwfyhr dsaqemgapw wsgivmtfal fgcsmvltac ffawvpgrtm wftalgagtl
      301 ygyllhglli kgshfagwye pswlhtpaga ivvtviaavv vtalcsplvq rmlrfamepr
      361 mewafrsasa sassgsgsea gaaaaaagsg avvagsgpga vvarsaampp ravvpaqatr
      421 ppg
//
LOCUS       WP_009718204             285 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Streptomyces
            himastatinicus].
ACCESSION   WP_009718204
VERSION     WP_009718204.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himastatinicus
  ORGANISM  Streptomyces himastatinicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            violaceusniger group.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptomyces himastatinicus"
                     /db_xref="taxon:998084"
     Protein         1..285
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29416
     Region          16..254
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 msprgwdvav rataelgegp twdatagrli wvdilsarvh tydpatgrst tlateqhvga
       61 akpraggglv vnlrdgvgly dpvegfrwlv rdpvpgrrgn daavapdgsl wagtmrydea
      121 agggtlsrig sdgsaaeilp dvavsngtgw spdgrlmyyv dsptrrvdvf dvteeggvag
      181 rrplahiedg agfpdglcvd adgcvwvalw dgaairrytp dgtldrvirl pfprptacaf
      241 ggaglsdlyv ssarvglgaa applagsvlv ipdagrglaq pafag
//
LOCUS       WP_009719212             373 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein, partial [Streptomyces
            himastatinicus].
ACCESSION   WP_009719212
VERSION     WP_009719212.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himastatinicus
  ORGANISM  Streptomyces himastatinicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            violaceusniger group.
REFERENCE   1  (residues 1 to 373)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Streptomyces himastatinicus"
                     /db_xref="taxon:998084"
     Protein         <1..373
                     /product="amidohydrolase family protein"
                     /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]"
     Region          1..332
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 wdahthpwqy tyggrqtalq laygittavs fggfayeqar lreavaagal agprllatge
       61 lldgprvays mgrahrtreg lrrsldraaa ldwdfvktyv rapgwimeea arfahdklgv
      121 rsgshlctpg iqlgqdltth lqatqrlefg hvttgtgrae qdvteiytas dfrliatpfa
      181 aqplvgadps laqdervtrl mppwdtalvr qlagapptda qlatlrteid iyrrilaggg
      241 vvalgtdqpl apvglhlhvg lralhrfgms paealrtvtv lparafgadr dlgtlevgkl
      301 adltvvdgdp ftdfdslvrt vsvlrggvpf eqrklveafp apagaraahg gsaehwlevg
      361 rqlrrdgccd lhi
//
LOCUS       WP_009719964             289 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Streptomyces himastatinicus].
ACCESSION   WP_009719964
VERSION     WP_009719964.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himastatinicus
  ORGANISM  Streptomyces himastatinicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            violaceusniger group.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Streptomyces himastatinicus"
                     /db_xref="taxon:998084"
     Protein         1..289
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29078
     Region          124..>287
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 maqhrilata alavalggaa lwapaahadt aattdaaaap tratlshedg vlsylaaagq
       61 tnkvtvsten idvdpsqfgg dflitfrdqs gmgidasaaq wdackypsaa dhtvvqcvia
      121 eplgsddstt felflgdgad tatvdgkagt iaalrggagd dvlrgtgqna fqgedgddri
      181 dggdgmgvrg gegddtitga csyecrgdag ndtltgtgda dnlygddgdd ilragsendy
      241 vyggkgndtl ygedgndtmy gnsgndtlyg gkgtdtlsgg pgtnkvyqd
//
LOCUS       WP_009720022             265 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            himastatinicus].
ACCESSION   WP_009720022
VERSION     WP_009720022.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himastatinicus
  ORGANISM  Streptomyces himastatinicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            violaceusniger group.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptomyces himastatinicus"
                     /db_xref="taxon:998084"
     Protein         1..265
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=28783
     Region          5..250
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mianvlgplr vtlnggsvvp aapkarkvla llvlnrgrvv qidamerevw gaatpksaat
       61 slqnyvmqir khlgmvlpgg pgsalakqil vteqtgyrla vpddefdvrr yqdlvaeagr
      121 aeeagqlaqa sallrcaldl wrdepladlp tgpvlqshvl rleedrksvl rrrilldlrl
      181 qryevvgelr altalhpyde mlheclmial nrsgrrndal svyqglrsal aegiglepsm
      241 rlqelqksil vaggsltpal psvgl
//
LOCUS       WP_009722290             682 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Halomonas sp. TD01].
ACCESSION   WP_009722290
VERSION     WP_009722290.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. TD01
  ORGANISM  Halomonas sp. TD01
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 682)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Halomonas sp. TD01"
                     /db_xref="taxon:999141"
     Protein         1..682
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=74869
     Region          10..682
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mthtlppsll lasvvlaspv waqapsseet vlatvevsap rlarelyatp aaistleree
       61 iaqgqqrvrl dealnrvpgv flqnrdnfaq gqriairgfg arapfgvrgi tvmvdgipyt
      121 lpdgqaqlda idldsaerie virgpssvly gnasggvidv ttadgrdnpg trlrmgagsd
      181 gyqkvalqng gvqgdwshhi sltalnvdgy reqsstekyl lnaklrrelg seramtaiin
      241 lldnprsedp galnarevaa grdqaapnsi aldarqsvdq qlfglqyedl avgdgelylk
      301 gfiakrsfeq qlpfvgssrl gyqrdymgas aeyhhevalg slplsyivgv dvarqederf
      361 rnrvnaqgvv geqlaketqt atangvfaqg dltlseqltl slgarfdrva ldvddtflad
      421 gdqsgkrtfn ewsgsaglsy ryrpqhqayv ntgtafetpt fsefanptgg gfnpavepqk
      481 awnreiglrg yieplamdyd lalfsvrvrd elvpydeggr tfyqnagdtn rdglelalgw
      541 qladhwrlns altlaryefd kfatpserfd gnripglpeq twvnqltwen ldqrfatlet
      601 eyigdlvadn anatevdsyw llnlrigdgw qlsegtrlsa ylglrnvlde ehyanvrlng
      661 tfgrfyepal grsvyggvel sf
//
LOCUS       WP_009722359             160 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Halomonas sp. TD01].
ACCESSION   WP_009722359
VERSION     WP_009722359.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. TD01
  ORGANISM  Halomonas sp. TD01
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Halomonas sp. TD01"
                     /db_xref="taxon:999141"
     Protein         1..160
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=17550
     Region          30..116
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mrktmlttai stallgslaf gvqastepqg mysaddimda evffsggsge eigevedilf
       61 deemrisalv iesgavlglg greivintdq ftlethtesd gdtehrimle asqeeiesfp
      121 tydrdwweqt kssardawqt tkegaqsawq streavndnq
//
LOCUS       WP_009722397             394 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Halomonas sp. TD01].
ACCESSION   WP_009722397
VERSION     WP_009722397.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. TD01
  ORGANISM  Halomonas sp. TD01
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Halomonas sp. TD01"
                     /db_xref="taxon:999141"
     Protein         1..394
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=41937
     Region          5..391
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mntpvlvinc gsssikyali dsdpqaprla glaerlgsse arlkgknsvg esftqalpna
       61 dhaealsail krlegrvpga vghrivhgge hftqaamidd sviaaietta alaplhnpan
      121 lagiaatrhv fpdlpqvavf dtafhqtlpp rayryalpea lytehgirry gfhgtshayv
      181 sqraaklssr gaggwltahl gngcstsaiw nnqsldtsmg ltpleglvmg trsgdvdpgl
      241 hahlhrqlgw sldeidnvln kqsgllglsg ltndmreved qalaghkgak lalevfcyri
      301 akslaalsca lpqldgvift ggigenspiv rrdvlallsh frfslddvan eatirgkegk
      361 ldnaghngpe vwviptdeeg riametrhcv ettk
//
LOCUS       WP_009722711              94 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Halomonas sp. TD01].
ACCESSION   WP_009722711
VERSION     WP_009722711.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. TD01
  ORGANISM  Halomonas sp. TD01
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 94)
  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   2  (residues 1 to 94)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Halomonas sp. TD01"
                     /db_xref="taxon:999141"
     Protein         1..94
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9666
     Region          26..90
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkitfkglla alllslslgv snlalaqdia pinvntanae llaelpgvgp sraaaiieer
       61 enngafanvd dltrvsgigp atvdrmrdqv aiee
//
LOCUS       WP_009723776             600 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Halomonas sp. TD01].
ACCESSION   WP_009723776
VERSION     WP_009723776.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. TD01
  ORGANISM  Halomonas sp. TD01
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 600)
  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 600)
  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 600)
  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 600)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Halomonas sp. TD01"
                     /db_xref="taxon:999141"
     Protein         1..600
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=61675
     Region          24..598
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mhalsssqta dnatpnaavs pgwialgvvs vgfhlglify gltpalvsrp lhmalllpwv
       61 liyiaktpfq risgwgltll gvaacayial neaalanqyg fidthlqmai glflimlale
      121 aarraigwpl plvallally gafgqyvpga fghpglplqs mvgsltiaeg glwgsltgvs
      181 vgvvaifvif gavlnageag qgfmnlasav agrltggaak vsvissalmg sisgsasanv
      241 astgaitips mvrlryprsf agaveavass ggqimpplmg agafvmvelt gtpytqimaa
      301 atlpavlyfl tvwvginaya trhdlqpida seqpaakevl itslffavpf vlllerifng
      361 gytpqyaasi aifagaalll fdvtlrfslp gfatrladav vtagrqigti gaiilcaslv
      421 igvlsltglg vkitsgilsl sndllwpall ltalaclilg mevpttaayv icvsvagpal
      481 islgleplla hlfvfwyall stitppvcgg vfiaagmvge nwlkvalkam algiglyiip
      541 lamvanpevi rlafnptgal ldglkiaagl taisfgviar kaiwlrvilv vagaaviflv
//
LOCUS       WP_009724179             344 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Halomonas sp.
            TD01].
ACCESSION   WP_009724179
VERSION     WP_009724179.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. TD01
  ORGANISM  Halomonas sp. TD01
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
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
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Halomonas sp. TD01"
                     /db_xref="taxon:999141"
     Protein         1..344
                     /product="aminoglycoside 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=38373
     Region          44..239
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mptplaarlq tlentlqqak iayqslspma dtglahdhvw mqrdgddwva rlpkqsqmnl
       61 apadnlayea acyerasesg hvprlhdilp vsdalprggl lvdaiegrla qlpedlpria
      121 etlaslhqlp ppsqpaplla pndpwqamle evsrqaewle kanlssdvia rvrdelealp
      181 vtlpdaercl isfdthpgnf liteegravl vdlekcrygl pgidlahtsl ytsttwdins
      241 qavltledvv afyqrwqahv gkspsaetlv acrratwlws ltwcakwraq hlqskdaehr
      301 gqdwsaeltd adviahvrdr vehylslpii ehvhnellhl kasl
//
LOCUS       WP_009724311             321 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Halomonas sp. TD01].
ACCESSION   WP_009724311
VERSION     WP_009724311.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. TD01
  ORGANISM  Halomonas sp. TD01
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
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
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Halomonas sp. TD01"
                     /db_xref="taxon:999141"
     Protein         1..321
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=35226
     Region          1..311
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mielshvskh fgedtavddi slhvakgkfc alvgssgcgk sttlrminrl iehssgdivi
       61 dgqaighydp vklrrrigya iqstglfphw tvarniglvp rllkwsaadv karveelmrl
      121 lglpteefah kyphqlsggq aqrvgvaral aadpdillmd epfgaldpit reklqdelak
      181 lqaqlhktvv fvthdmdeal kladhlvvmr egrivqqgap lallrnpadp fvesllggle
      241 rglkqaaltr vkdhmsslgq slpapsripg dfslrqalsm mlrdhcdrlt vvdqqdmpig
      301 elslrkvvke aqldkvghre a
//
LOCUS       WP_009724933             337 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Halomonas sp. TD01].
ACCESSION   WP_009724933
VERSION     WP_009724933.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. TD01
  ORGANISM  Halomonas sp. TD01
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 337)
  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   6  (residues 1 to 337)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Halomonas sp. TD01"
                     /db_xref="taxon:999141"
     Protein         1..337
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38272
     Region          22..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          95..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtvtvsmhfv nellcglpat ehspvrylel agispfllsa pngrvtveqf aelyrllale
       61 lddetpcffs rplrcgtlkl lclslldapt lhvalhrytq ffrillddfg ygftieggfa
      121 rvaleerapp qgsrilihel mlklfhgiss wmiarkippi lmecgyaqpa hsadylyfyp
      181 gkvrfdqpqt avyfdkafln hpirqtkqhl gaflqrapad wfyvsfedrl vthrvrehls
      241 rhlpasctvq hvadalhmsv rtlsrhlkle gthfqavkde yrrdyaiqal trstqpltai
      301 aeklgfedla clsrafkqwt gnspaayrka qtaglkr
//
LOCUS       WP_009724964             293 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Halomonas sp. TD01].
ACCESSION   WP_009724964
VERSION     WP_009724964.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. TD01
  ORGANISM  Halomonas sp. TD01
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 293)
  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 293)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 293)
  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   4  (residues 1 to 293)
  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 293)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Halomonas sp. TD01"
                     /db_xref="taxon:999141"
     Protein         1..293
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32135
     Region          16..253
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <159..260
                     /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 mpstirqipl esatkhhshd fhqivitlcg ssefeieglg grvnafsgci vpanhehfys
       61 gngynrqlil dlpedapalt gehrelvalf daprffaldn plrhylafve selvqgfdts
      121 amsfqqdrla atllgslkar lgasestsqr rlnldqidrf irlhladelr vadlaklacl
      181 seahfserfr vqtglspwqy vrrqrlhaar qlvlqsrlpl tdiaiqtgfa nqsalshafr
      241 rsyglsprql rqgvgvanpp ldsatpstsy stplaptasp sgasiragal ssr
//
LOCUS       WP_009725358             406 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Methylophaga lonarensis].
ACCESSION   WP_009725358
VERSION     WP_009725358.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga lonarensis
  ORGANISM  Methylophaga lonarensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Methylophaga lonarensis"
                     /db_xref="taxon:999151"
     Protein         1..406
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44478
     Region          9..395
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mptpqtqllt inggsssikf tlynvgaslt atlsgkltgl glqtarlrin nlqtdeqsit
       61 eveaadysqa isllmvwfrq nldigavkai ghrivhgghr ykkpqwvdpa linellsmta
      121 mdpqhlpgei qlieafseqf pklkqmvcfd tefhqhlpav arllpiprry hdagiyrygf
      181 hglsyqylmq mlhalqgnqi qhqkivlahl gngasmtavi nqqsidttma mtpaagimmg
      241 srsgdldpgl fgllnrtegm saeqfdqmih hqsglagvse yssdmqqlla krandsnvad
      301 aidsfcyqar kqigayaaal ggldsvvfsg gigenlpeir sqicqqlafl gihlddalnr
      361 qnalkiskad spiavwvipt deeliiaqsm cdllnlhyqk eghnes
//
LOCUS       WP_009726539             117 aa            linear   BCT 20-JAN-2025
DEFINITION  PilZ domain-containing protein [Methylophaga lonarensis].
ACCESSION   WP_009726539
VERSION     WP_009726539.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga lonarensis
  ORGANISM  Methylophaga lonarensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (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   3  (residues 1 to 117)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 117)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Methylophaga lonarensis"
                     /db_xref="taxon:999151"
     Protein         1..117
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12821
     Region          2..117
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mtsnprkgil slrisdqnml yhsfmpflkn gglfiptnkp yqmgeevfil lslldepeki
       61 pvagtvawvt pqgaqsnqta gigvqfsdin gssnvirgki enylvdklks dkvtytm
//
LOCUS       WP_009726846             304 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Methylophaga
            lonarensis].
ACCESSION   WP_009726846
VERSION     WP_009726846.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga lonarensis
  ORGANISM  Methylophaga lonarensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
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
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Methylophaga lonarensis"
                     /db_xref="taxon:999151"
     Protein         1..304
                     /product="aminoglycoside 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=34673
     Region          34..277
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mvdfnrspys flseqqqetl pdfnkavrlm spyedstnst wlletdsgrl vlklcdlqwv
       61 eestfwtgmr llfdlhlpvq mqkfdlvygf inqhsplsip allaagasch egmypgyvma
      121 ealagkaltn davtdasvrd larhlaslha qqqsqwgsla sadftaelwp vrlrdsmlsl
      181 askqnfvake lldamtqqal lcrpavfspi mpdlrwdqfl mhegqlaalv dldafvwgpv
      241 emefvlleyl ltadqwrift eqyqqycplp vldivrapyr mmlflmnvlg ekdvqkwmha
      301 phyl
//
LOCUS       WP_009726994             167 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Methylophaga lonarensis].
ACCESSION   WP_009726994
VERSION     WP_009726994.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga lonarensis
  ORGANISM  Methylophaga lonarensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
REFERENCE   1  (residues 1 to 167)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Methylophaga lonarensis"
                     /db_xref="taxon:999151"
     Protein         1..167
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=18602
     Region          34..166
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cl49639"
                     /db_xref="CDD:483979"
     Site            order(109,123,126,139..142,144)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mqssqsrnep ylkisiadqh cwlwqgetll fdapvstaln gpgeqknsgc tprglhqvra
       61 kighdlpint vfvgrrptge iyspelgrkf pdrdwiltri lwlsgleqgr nrlanvdtmq
      121 ryiyihgcpd elpmgvalsh gcirmhnddl ltlfalipvg ttveita
//
LOCUS       WP_009727078             426 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Methylophaga lonarensis].
ACCESSION   WP_009727078
VERSION     WP_009727078.1
KEYWORDS    RefSeq.
SOURCE      Methylophaga lonarensis
  ORGANISM  Methylophaga lonarensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Methylophaga.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 426)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Methylophaga lonarensis"
                     /db_xref="taxon:999151"
     Protein         1..426
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=48865
     Region          <38..260
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mldsglyeql hkalwvqkkl setvarhwvt teyqgltlss hfqpifsish rrpvgyegll
       61 rastdsgali pppavlvlpn nskenleldr acrqlhlqnf arqetgdcwl flnlnsqclv
      121 teqpdagfmn rlfettgihp srlvieiles eitdrsylkq likhfrslgc liaiddfgag
      181 hsnfdriwel epdivkidrs lvqeagkssr veriltgivs liheagslvv legvetrrea
      241 lvsiaanadm vqgfyfakpq qlissnheef vsvidellqh qqrqrfknth qinenfrkie
      301 rlfkrainhf svtqnfeess eilfaekrsv rcyllddagy qmarniysph yqqtmdvrft
      361 pllsgdnanw shkhyhfrav qhpgqmqlsr pylsvadsrm citvsqtvts sdkqfvfccd
      421 ldwqdn
//
LOCUS       WP_009728100             305 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Selenomonas sp. F0473].
ACCESSION   WP_009728100
VERSION     WP_009728100.1
KEYWORDS    RefSeq.
SOURCE      Selenomonas sp. F0473
  ORGANISM  Selenomonas sp. F0473
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Selenomonas.
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   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 305)
  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 305)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Selenomonas sp. F0473"
                     /db_xref="taxon:999423"
     Protein         1..305
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32060
     Region          2..67
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          189..252
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mvgdilrker ekqgmtvadi eratsiraly iqyieqgnie alpgmvyakg fvrnyaaflr
       61 lnaeqlalqf aeeqgmaapp pppaveekpr rislssvgde slshisiggt rssyagifgk
      121 laagiivlva vvgggmalls yintprqeaa sappvqaekp aaaavaaead asdeargada
      181 ansqdvrvsv rvgapcwaev qtdgntvfeg mleqgktenw qgkeavfira gnagalevta
      241 ngrrlgkfga egevverrft rstkdlkdtl sasaaaepak etktagakng aegtakdskr
      301 tknrq
//
LOCUS       WP_009728568             185 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Selenomonas sp. F0473].
ACCESSION   WP_009728568
VERSION     WP_009728568.1
KEYWORDS    RefSeq.
SOURCE      Selenomonas sp. F0473
  ORGANISM  Selenomonas sp. F0473
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Selenomonas.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Selenomonas sp. F0473"
                     /db_xref="taxon:999423"
     Protein         1..185
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19961
     Region          3..176
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 melqealakr aslrkftgem ptdaeigavl daaylgpvla fhdmrisvit npelleeaqe
       61 ngeafnrmgn paymygapvw vllsakrhte nmpntpytad mlnanmywtl gsiiqnmhlk
      121 avelglaacp mnttvvalgd naalrrrlgi pdghiaagsi vigkgtqgyk erpvkpallp
      181 taflk
//
LOCUS       WP_009729309             681 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Selenomonas sp. F0473].
ACCESSION   WP_009729309
VERSION     WP_009729309.1
KEYWORDS    RefSeq.
SOURCE      Selenomonas sp. F0473
  ORGANISM  Selenomonas sp. F0473
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Selenomonas.
REFERENCE   1  (residues 1 to 681)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 681)
  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   3  (residues 1 to 681)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..681
                     /organism="Selenomonas sp. F0473"
                     /db_xref="taxon:999423"
     Protein         1..681
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=73641
     Region          1..681
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          173..252
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 mdnqymdmfl deshehlqsl negllrleen meeigavndi frnahtlkgm satmgfakia
       61 elthemedvl dlvrkeqlkl nedimdtlfk cldsleqmvd svgngeaedv vdvtdlvakl
      121 ssiskgtpap aapaaaapsa aesaaasang dlgideidld vmkkakesgl rifhvkvtlm
      181 etcvlkaara vmvmhaldev gdviksvpda edleqekfer sfdvvvttas daeavqnavd
      241 tvseiediqv eeldpdqlsk aaeaaqttsa agapaagapa kkpaaaakpa aggpakkqhq
      301 sqsvrvdiek ldtlmnlmge lvinkvrleq igqthrmsdl metleqmdrv tgdlqnivmk
      361 vrmvpvsavf nrfprmvrdv skelgkeinl tiegeeteld rtvideigdp imhllrnsld
      421 hgvespekre akgkprigev gliarhegnn vvimitddga gidaevirrk avekgmisqe
      481 eadrlddaea vrliflpgfs taekitdisg rgvgmdvvrs kiealsghvd vethidkgsi
      541 fkiklpltla iiqamlvqvq gemyaiplgs idstiniept diqtiqnkev ivlrgeiipi
      601 irmeealqvp htkdadelfv vvvhageaka givvdnligq qeiviktlgn lfaglklfgg
      661 atvlgdgrva lildvatmiq q
//
LOCUS       WP_009730266             165 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Streptococcus].
ACCESSION   WP_009730266
VERSION     WP_009730266.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus
  ORGANISM  Streptococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Streptococcus"
                     /db_xref="taxon:1301"
     Protein         1..165
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18157
     Region          4..156
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mldsekqsqy qllneelsyl legesnvlan lsnasallks rfpntvfagf ylfdgselvl
       61 gpfqggvsci riplgkgvcg eaaefqetvl vgdvstypny iscdsmakse ivvpmlkngr
      121 lvgvldldss liddynaidr dyleqfvail lektewdftm feeka
//
LOCUS       WP_009730802             292 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Streptococcus sp.
            F0442].
ACCESSION   WP_009730802
VERSION     WP_009730802.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sp. F0442
  ORGANISM  Streptococcus sp. F0442
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 292)
  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   2  (residues 1 to 292)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptococcus sp. F0442"
                     /db_xref="taxon:999425"
     Protein         1..292
                     /product="aminoglycoside 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=34380
     Region          8..226
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mnfsskiain kgwsddkkyc vtdqnqqkyf lrvsdkekld skkfefdmme kvaslgipmc
       61 kpisielcdd evhslhewid gkdaretilt vskeqqyiyg leagrilrki hsllvtevrd
      121 dwevfynrki ddkiskykec pvqyengqif ieflnanrel lkdrpqvfqh gdyhignfmi
      181 gedrkiyvid fdrfdvgdpw eefnrivwsa qvspsfasgm idgyfdhkvp dlfwkllaiy
      241 ilnnivgals wavpygveei vvmqhqakei lewyddmnqi ipswylnkkk te
//
LOCUS       WP_009730850             397 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Streptococcus sp. F0442].
ACCESSION   WP_009730850
VERSION     WP_009730850.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sp. F0442
  ORGANISM  Streptococcus sp. F0442
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Streptococcus sp. F0442"
                     /db_xref="taxon:999425"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43666
     Region          3..395
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msdkilaina gssslkfqll empseaviak gifdrigfkd gkvkyqtkrn qvqksvcips
       61 hefavqvllg tlvesgeihs ieeivgvghr vahggesfkg svlideknee iisdlgdlap
      121 shnpvslsvi ksfkthfpsi knvavfdtsf hqtmdpvhyl yplpyslyek fhvrkygfhg
      181 ishayiaetv ekifqqeeha kenvkiisch lgngasicai keqqsvntsm gftpidglmm
      241 gsrcgsidpm iipylverqq mpihevkkll neasgllgis emsndmrdli qaategnqka
      301 alaiemfvnr vahtiasyiv dldgldalvf tggigenaal irslivdklq vfgmsvnkel
      361 nengslyiqd snsnckilvv qtneelmiar etyrlsv
//
LOCUS       WP_009730851             192 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Streptococcus].
ACCESSION   WP_009730851
VERSION     WP_009730851.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus
  ORGANISM  Streptococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae.
REFERENCE   1  (residues 1 to 192)
  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 192)
  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   3  (residues 1 to 192)
  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   4  (residues 1 to 192)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 192)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Streptococcus"
                     /db_xref="taxon:1301"
     Protein         1..192
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21321
     Region          1..190
                     /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"
ORIGIN      
        1 mkgrilicdd dpiirldikq ileqsdyeva aeasdgfeai elcqkhffdl vimdiklpll
       61 dglsagkkil ddglaygvii lsafsddhyv qkasltgasa ylvkpldaks liptiavcie
      121 kgrqqqllsk elikiskkld drillekakg llmtrdnlse peafkqirti smqkrvpmie
      181 iakllllnne aq
//
LOCUS       WP_009732132             242 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Streptococcus sp. F0442].
ACCESSION   WP_009732132
VERSION     WP_009732132.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sp. F0442
  ORGANISM  Streptococcus sp. F0442
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
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
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptococcus sp. F0442"
                     /db_xref="taxon:999425"
     Protein         1..242
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=26871
     Region          1..>237
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mieykhvalr ytdtdilkdv nlriedgefm vlvgpsgsgk ttmlkminrl leptdgniyr
       61 dgkrikdyde relrlstgyv lqaialfpnl tvaenialip emkgwskeqi askteelldk
      121 vglpatdyah rlpselsgge qqrigivrai iaepkillmd epfsaldais rkqlqtltkd
      181 lhkefgmtti fvthdtdeal klgdriavlq egeivqvads etilaqpvnd fvadlfggah
      241 hv
//
LOCUS       WP_009731661             280 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptococcus sp. F0442].
ACCESSION   WP_009731661
VERSION     WP_009731661.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sp. F0442
  ORGANISM  Streptococcus sp. F0442
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 280)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 280)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Streptococcus sp. F0442"
                     /db_xref="taxon:999425"
     Protein         1..280
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31615
     Region          27..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          127..277
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mniiksfndt idyletvldd eidekkvtql sgysysmfsr lfsiltettl seylrsrrlt
       61 eaavilrntd ekiidvafkf gyessdsfgt afkyfhgftp sevrngkpfk lvsrvqlals
      121 vrggrsmnit iqkkqaftva gvneqsinss lcpsvwdkly ekyshdelas lgngqsvgvc
      181 hdvenpstin ymagyivndv dkatsmgldv leveeaeyav velvgsvpec ihngwkyame
      241 vffpehgyvh sgksdfeyyy egdmhskdyk melwipitka
//
LOCUS       WP_009732907             669 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Anoxybacillus gonensis].
ACCESSION   WP_009732907
VERSION     WP_009732907.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacillus gonensis
  ORGANISM  Anoxybacillus gonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Anoxybacillus.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 669)
  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   3  (residues 1 to 669)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Anoxybacillus gonensis"
                     /db_xref="taxon:198467"
     Protein         1..669
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=74696
     Region          1..669
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          161..240
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 mdmsqylevf ideskehlqt ineqllelek npddvsivne ifrsahtlkg msatmgfedl
       61 anlthqmenv ldairngkia vtpelldvif ravddleamv vsiaeggdgk rdvtavvaql
      121 kqiekgevvt pqksapiqeq tydefeytil kqsaeqgfhs yevsvklrsd cllkaarvfm
      181 ifevieqige viksvpsvem leaeqfddqf vvtvvtkvsq delqkrimkv seveevnvqp
      241 vdlhrpentv eqkeeqkkeq keetkaveqt vekkqeaqee kqtgkqvsnk tirvnierld
      301 ilmnlfeelv idrgrleqis relnnpelhe tvermsrisg dlqniilnmr mvpvetvfnr
      361 fprmvrqlar dlgkkinlei igaeteldrt videigdplv hllrnaidhg ietpdvrrak
      421 gkpeegtvkl kayhsgnhvf ieieddgagi srekvlkkai skgiiseqna anltdkqvye
      481 lifasgfsta dkvsdisgrg vgldvvksti eslggsvsid seegvgsifs iqlpltlsii
      541 svmlveiqne kyaiplssii etaivkkedi lhahnqkvid frgkvvpllf lkdifevpvv
      601 keeddflsvv mvrkgekmag lvvdsfigqq evvlkslgny ltsvfaisga tilgdgqval
      661 iidcnalik
//
LOCUS       WP_009733348             371 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Bilophila].
ACCESSION   WP_009733348
VERSION     WP_009733348.1
KEYWORDS    RefSeq.
SOURCE      Bilophila
  ORGANISM  Bilophila
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae.
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   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   3  (residues 1 to 371)
  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   4  (residues 1 to 371)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 371)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 371)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Bilophila"
                     /db_xref="taxon:35832"
     Protein         1..371
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39031
     Region          29..362
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(102..104,125..126,176,228,252)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 marawmkaal agmaimamta pvhaadtiki gvpgahsgdl vsygmpslna arivadeyna
       61 kggilgkqie ivaeddqckp elgtnaatkv lsegavavmg sicsgatkaa lpiyndakiv
      121 sispsattpe ltqkgdhpyf frtiasddvs ghlagsfakd klglkkvall hdkgdygrgf
      181 vnyaremlek ggvqivleeg itpgavdyga viqkirkaga dgiifggyhp easklvqqla
      241 kkkidipfig pdgvkdeqfi kvagknaegv yatgptdvsk lpmniqahen hkkkygtepg
      301 afydnaysat valleaikaa gstdsqkime alrtnmvetp lgkikfdakg daegigfsiy
      361 evkdgkfvel k
//
LOCUS       WP_009733743             496 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Vibrio sp. N418].
ACCESSION   WP_009733743
VERSION     WP_009733743.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. N418
  ORGANISM  Vibrio sp. N418
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Vibrio sp. N418"
                     /db_xref="taxon:701176"
     Protein         1..496
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=53987
     Region          2..496
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mkqfikinak dnvlvclhsl vaghtldvdg qritltqdvd rgskvalsqi tagedivkyg
       61 gsigyatedi svgewvhthn iktklsetds yqylpnfhsm kpshlaerff dgyqrsngdv
      121 airneiwvip tvgcvngiaq qavnrfkqry pdlecdgiyl fphnygcsql gddhdntkti
      181 lanmvnhpna ggalviglgc ennqigpfke hvgevdeqri rfmiaqneqd evevamthle
      241 aiyqsvkqdk rtnisigklr vglecggsdg lsgitanpll gefsdyliel ggtsvltevp
      301 emfgaehllf ercidrptfd kavsmvndfk qyfidhnqpi yenpspgnkk ggistledks
      361 mgctqkagms pvigvlnyge rltkpglnll sapgndavat salaasgchi vlfttgrgtp
      421 yggfvptikl atnselatnk phwidfnags lvegvematl leqfvdyvta iasgtptnne
      481 rndirelaif ksgvtl
//
LOCUS       WP_009738843             234 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Frankia sp. QA3].
ACCESSION   WP_009738843
VERSION     WP_009738843.1
KEYWORDS    RefSeq.
SOURCE      Frankia sp. QA3
  ORGANISM  Frankia sp. QA3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae; Frankia.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Frankia sp. QA3"
                     /db_xref="taxon:710111"
     Protein         1..234
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25029
     Region          3..199
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdvrealytt rtmrrvkpdp iplsvqerim daavrapngg nlqkwrfilv dspevkavlg
       61 plyrdavarg lqgyygdaaa iatstpdsee gvlarrmvrs anwladnfeq vplflfalip
      121 atksvgsvfp avwsamlaar aegvgasltt mlgvghglet laalgvpfee nwinaccvsf
      181 gyptgrwava rreppqsvty rnrwlapsgf hgtgplwpdg apaaaiepdp agap
//
LOCUS       WP_009739379             171 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Frankia sp. QA3].
ACCESSION   WP_009739379
VERSION     WP_009739379.1
KEYWORDS    RefSeq.
SOURCE      Frankia sp. QA3
  ORGANISM  Frankia sp. QA3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae; Frankia.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Frankia sp. QA3"
                     /db_xref="taxon:710111"
     Protein         1..171
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18947
     Region          5..166
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mqtwdairar rnvrsyqdrp vpagdleril eagwrspsas nrqqwdfvlv tdravlgela
       61 tiwrgaghia ssaativlvl pepeteryrl mdeydlgqat mlmlltatdl giggghsavg
      121 dqeaarrilg vppthrvaym iglgypgdgp lrpverldrr pfdevvhrgh w
//
LOCUS       WP_009739936             263 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Frankia sp. QA3].
ACCESSION   WP_009739936
VERSION     WP_009739936.1
KEYWORDS    RefSeq.
SOURCE      Frankia sp. QA3
  ORGANISM  Frankia sp. QA3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae; Frankia.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Frankia sp. QA3"
                     /db_xref="taxon:710111"
     Protein         1..263
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=29013
     Region          1..250
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mlefnvlgel evigggrdla psaprvktvl allalnvnrv vstetlaeel wddlpprsaa
       61 ttlqtyiyql rrilggtvgg gaqgcdivtr rpgymlrtag vrvdaaifld mvgegrnlwk
      121 eervdeaahr lrqalelwrg paladvrsgp rlrihvahls evrlralelr vhayarlgrh
      181 relipelrsl vaehrlnesf haqlidslss agrraealqa yqdlrhmlkt elgldptpev
      241 qrlqtevlsg vrggtlssll rag
//
LOCUS       WP_009740599             235 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Frankia sp. QA3].
ACCESSION   WP_009740599
VERSION     WP_009740599.1
KEYWORDS    RefSeq.
SOURCE      Frankia sp. QA3
  ORGANISM  Frankia sp. QA3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae; Frankia.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Frankia sp. QA3"
                     /db_xref="taxon:710111"
     Protein         1..235
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=23736
     Region          2..226
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mvgvsgasgt pyaaavlrgl laaelpvdlv lsraarltll detgiawhda dwsrplaawl
       61 saplggnvad saadsaadsa tddaedsssa ladavaalva vhasgnlaap tssgsyptrg
      121 mivvpastac lagialglsk dllqrsadvt lkegrrlvvv prempytaat lrhmlalhda
      181 gtvvaaaspg fyagartaad lvdfvagrvl daagvphtlf rrwtgelgga rrpph
//
LOCUS       WP_009741372             255 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Frankia sp. QA3].
ACCESSION   WP_009741372
VERSION     WP_009741372.1
KEYWORDS    RefSeq.
SOURCE      Frankia sp. QA3
  ORGANISM  Frankia sp. QA3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae; Frankia.
REFERENCE   1  (residues 1 to 255)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Frankia sp. QA3"
                     /db_xref="taxon:710111"
     Protein         1..255
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=26442
     Region          134..254
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(200,211,214,227..230,232)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mtisrlgprt aagilaavlg gavltgcggg dgshnaatdl spqvrnqlaa iaglgqskst
       61 ivtavgtsvd iysaptdtqp sstlaspnen gvkrvflvqa kmpgwwqvml pvqpngstgw
      121 vkadqvtase tpyrlvvsrg rhllqvfsdg kqiaqepvai gtsdtptpgg rfylmellqp
      181 rnpkgpygpy afglngfsts lssfegrkpv iglhgtnepk migkdvshgc irlsndaisr
      241 laqtvplgtp vdiva
//
LOCUS       WP_009741253             374 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Frankia sp. QA3].
ACCESSION   WP_009741253
VERSION     WP_009741253.1
KEYWORDS    RefSeq.
SOURCE      Frankia sp. QA3
  ORGANISM  Frankia sp. QA3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae; Frankia.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 374)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Frankia sp. QA3"
                     /db_xref="taxon:710111"
     Protein         1..374
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39480
     Region          12..367
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mpetsssrng erhvsvlstg aelpgdpidn aalarlcgpl pddvldgiqv rrrhwiidpa
       61 tgehrtstsa mataaarqal rraglepgdv dlivmstasp dhplpvaaty vqqrlglahc
      121 avievragcv gavqafdiar rllgdgtyrt alvigaesvs pllapmylgq dpyrvrmrdr
      181 ltvhtfgdga gamvlragee gsagnhrrpv fatqsmggdr gpgmlilggg tevplaeqqr
      241 rkrlmdirid ipgtarfgpr vfvrgihdll drsglaladi dacvlpegna eyfsgeygta
      301 glsgddqttl nkiivenltd vgatgsaavp laldtgwtag rvrpgdtvll laieasryly
      361 agltltweap tpar
//
LOCUS       WP_009741625             216 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Frankia sp. QA3].
ACCESSION   WP_009741625
VERSION     WP_009741625.1
KEYWORDS    RefSeq.
SOURCE      Frankia sp. QA3
  ORGANISM  Frankia sp. QA3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
            Frankiaceae; Frankia.
REFERENCE   1  (residues 1 to 216)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Frankia sp. QA3"
                     /db_xref="taxon:710111"
     Protein         1..216
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=22433
     Region          121..210
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mthgtsappr rrppdrradr lhalaagvia vlavlagill vnllngnsdp drsrpvaapt
       61 rtpdggspsp spavrrttpa aspthrpspa attppserps sptpappptp qtrrapavta
      121 pvvvlnnsri sglaeaaagr veaagfpver tgnfqsiynv pvstvfydds daeaaqalkd
      181 avpgiekiip rsqtriistd tlilvitrdf padpek
//
LOCUS       WP_009745940             335 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-oxoacyl-ACP synthase III family protein
            [unclassified Capnocytophaga].
ACCESSION   WP_009745940
VERSION     WP_009745940.1
KEYWORDS    RefSeq.
SOURCE      unclassified Capnocytophaga
  ORGANISM  unclassified Capnocytophaga
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 335)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="unclassified Capnocytophaga"
                     /db_xref="taxon:2640652"
     Protein         1..335
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37102
     Region          3..335
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mynsiivgtg yyvpenivtn ndlskmmdts dewiqertgi rerrfatrgk dtttsmgvra
       61 aqmamdkani akedidflif atlspdyyfp gcgvlaqkel glntigaldi rnqcsgfiya
      121 lsvadqfikt gmyknilvia setqspaldl ttrgrnmavl fgdgagavvl srceqsnrgi
      181 lsshlhsega yaeelaiitp gvgkkwitdl lkendpedts yfpymngqfv fknavvrfse
      241 vimeglkanh lteedidlfi phqanlrisq fiqqkfklsd erifnniqky gnttaasiai
      301 alaeaveqnr vkendilila afgsgftwgs vvikw
//
LOCUS       WP_009747356             281 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Actinomyces sp. oral taxon 175].
ACCESSION   WP_009747356
VERSION     WP_009747356.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces sp. oral taxon 175
  ORGANISM  Actinomyces sp. oral taxon 175
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Actinomyces sp. oral taxon 175"
                     /db_xref="taxon:712119"
     Protein         1..281
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30125
     Region          1..254
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mridphthsa csdgtdspae lmekaaeagl dvvgltdhdt magwqeaaqa vpfagvallr
       61 gteiscaadg vtlhllsylh raddagleaa fararrsrds raqrmverls qdypvtwedv
      121 lsqsadshti grphiadalv aagsfpdrna afagplatss pyyvhhwald pveacrlvra
      181 aggvpvaahp raasrqrrlv pdetfaqmae aglaalemnh rdqdpeqreq vrllaqrlgl
      241 glsgasdyhg tgkpnrlgen lmppelleqi ldegaldlvr p
//
LOCUS       WP_009747244             394 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Actinomyces].
ACCESSION   WP_009747244
VERSION     WP_009747244.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces
  ORGANISM  Actinomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Actinomyces"
                     /db_xref="taxon:1654"
     Protein         1..394
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42217
     Region          6..394
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mtqrtvlvin sgsssikyql vdpdsgasla sglverigee tgaithkhge erteitepvp
       61 dhgyglsevl rlfeeqgpsl adahivavgh rvvqggryfs gpalidddvv arieqlvplg
      121 plhnpahlkg ievgrrllsd vphvavfdta ffqdlpeeaa ryaldrevad tysirrygah
      181 gtshqfvsga vsellgrddl kqvvlhlgng asasavvagh avdtsmgltp leglvmggrt
      241 gdidpaavfh larvagmsid eidhlfnrgs gmkglagdnd mrevwkriga geqeareamd
      301 iylhrlvkyv gaytavmggl daltftagig endanlrrel gerlgfmgvk inqevnetrs
      361 deprvistpd skvtvlvvpt neelaiarqa ltli
//
LOCUS       WP_009750678             469 aa            linear   BCT 20-JAN-2025
DEFINITION  RHS repeat-associated core domain-containing protein
            [Capnocytophaga sp. oral taxon 326].
ACCESSION   WP_009750678
VERSION     WP_009750678.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sp. oral taxon 326
  ORGANISM  Capnocytophaga sp. oral taxon 326
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 469)
  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 10264210
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Capnocytophaga sp. oral taxon 326"
                     /db_xref="taxon:712212"
     Protein         1..469
                     /product="RHS repeat-associated core domain-containing
                     protein"
                     /calculated_mol_wt=50321
     Region          <52..227
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
     Region          <169..352
                     /region_name="PPE"
                     /note="PPE-repeat protein [Function unknown]; COG5651"
                     /db_xref="CDD:444372"
ORIGIN      
        1 mlkhyshdgs teivcnktdn stkfilylgg daysvpaili sdgevqklyy lhrdylgsiv
       61 mltdedgnia errhfdpwgq pikvedgagk vlqgltlldr gftghehlqt vglihmngrl
      121 ydpalhrflm pdnfvqdpfn tqnfnrygyc lnnpliyvde ngefwhivig alvggvvnlv
      181 aninnsqgfw ehlaafgvga lggavtaavg gsdggasfla itgtaagmga ltmgtnsiia
      241 qtgpnfsgmn nvnwgavgks slvggasgfa sgavgvwatn sgmlvngins pvlrslaasp
      301 lasgaghvvg gttynllegq slgnafsnsf ngigqsiamg tmlgvtttiv nsyahkvnpw
      361 virskpqsid ydftpdpyge nltlyrgttg setdnsrflf mtdnpeyart yitnggslik
      421 vtiphytlyk mrfngdviyy ngthnttipn teyrfsprvk pliiknikd
//
LOCUS       WP_009752989             342 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Selenomonas sp. oral
            taxon 149].
ACCESSION   WP_009752989
VERSION     WP_009752989.1
KEYWORDS    RefSeq.
SOURCE      Selenomonas sp. oral taxon 149
  ORGANISM  Selenomonas sp. oral taxon 149
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Selenomonas.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 342)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Selenomonas sp. oral taxon 149"
                     /db_xref="taxon:712535"
     Protein         1..342
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36257
     Region          44..331
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 migllkdvgi ealtatvakn cvpveevlkd lmsekkakrl ahgtgieals iappeictsd
       61 lcfdsaqrlf aeidqseiga lifisqtady ltpatsyylq drlglphdil afdvnlgcsg
      121 fcygvflagt llpalggrkv liccgdtssr nvhpedssml slagdagaaa vvapmqgsdl
      181 cyhiesfgem adyllvargg yrapriadet glslhrdnyv vmdgmgvmnf tidevpnnir
      241 allnfatldi aaidrailhq anamivrtla akigmaeecv pfmsgrignt ssasipvcla
      301 emarlgtyeg grfllsgfgv gmsiasllmd fsraqvletn ai
//
LOCUS       WP_009754785             292 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Streptococcus sp.
            oral taxon 056].
ACCESSION   WP_009754785
VERSION     WP_009754785.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sp. oral taxon 056
  ORGANISM  Streptococcus sp. oral taxon 056
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 292)
  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   2  (residues 1 to 292)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptococcus sp. oral taxon 056"
                     /db_xref="taxon:712620"
     Protein         1..292
                     /product="aminoglycoside 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=34361
     Region          8..227
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mefiskiain kgwsddkkyc vtnqnqqkyl lrvsdkekld skkiefdmme kvaslgvrms
       61 kpikfelcgd evhsiyewid grdaidsilt ysekqqytyg ieagrilrki htipttevce
      121 dweiffnrki ddkiskykec piqyesgqvf idflnenrel lknrpqvfqh gdyhignfmi
      181 gedpeiyvid fdrfdfgdpw eefnrivwsa qispafssgm idgyfddkvp dlfwkllaiy
      241 ilsnivgalp waisygeeev svmqnqakei lewyddmnrl vpswymnknn tk
//
LOCUS       WP_009753048             241 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Selenomonas sp. oral taxon 149].
ACCESSION   WP_009753048
VERSION     WP_009753048.1
KEYWORDS    RefSeq.
SOURCE      Selenomonas sp. oral taxon 149
  ORGANISM  Selenomonas sp. oral taxon 149
            Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
            Selenomonadaceae; Selenomonas.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  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   3  (residues 1 to 241)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Selenomonas sp. oral taxon 149"
                     /db_xref="taxon:712535"
     Protein         1..241
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26826
     Region          <78..229
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mtlegeklta llkhdasihi idpetdidyy gslelseeeq eagapegals vrlnipvgkf
       61 vntpetghlf pchltgpgcv yhftvayrsa sqlpdtiwyl dlpesaeriq lrdfvrvpip
      121 msievklagd hgslknfrem hlidisgggl cfvheeelle nasvvvrvpd lphigtlete
      181 gairrstpie tnlgityhig vefttltpre rehlvqsiyq lqqsylrkgl kvpqidhtkr
      241 g
//
LOCUS       WP_009756386             649 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Nitratireductor indicus].
ACCESSION   WP_009756386
VERSION     WP_009756386.1
KEYWORDS    RefSeq.
SOURCE      Nitratireductor indicus
  ORGANISM  Nitratireductor indicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Nitratireductor.
REFERENCE   1  (residues 1 to 649)
  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 649)
  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 649)
  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 649)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Nitratireductor indicus"
                     /db_xref="taxon:721133"
     Protein         1..649
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=69034
     Region          17..635
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mvtskldtmr eskpfdlskl amvvglllva fqiytagfgp fpplvqrsgh tglalimvyl
       61 tldklggpfs dflstrtgam vrlvlavvvg gtcfyivtqd trlvesfavf atpfeiacal
      121 vlmilvafva ysstgvalpl lavatllytl fgnhiagrwg hsgfdlqytv eylylgtegi
      181 wgqvtglsag liaifiifga vllstgaaqs fmdiallvag rrpggaakva tassafmgml
      241 ngsavanvat tgnfsipamk rlgyrprfaa aveatassgg qitppimgag afimaellgv
      301 pytmiayaai ipavlffacv wfsidiearr egmkpfpvee mphwkevfal rrflplaltl
      361 vvtlgamftg rtpslaafyg ivtnvtlfll lgeyswssfk srfcsllegv nsaasgivsi
      421 lallvcaqit lsligltgvg vkltetimmi nennfqllav vfamivalvl gmgmpttaay
      481 llsaavaapa lirlgidpis ahffvfysal lsaltppvct avftaaviar ehwwpicida
      541 mrlatmkyll pfffiyregv llkgtwyeia ssavmglvaa mllaiatgrf yrqpvhwyvs
      601 ailalagvsv vanhvvtdli allalatvvv rqwlavssga agqavaerr
//
LOCUS       WP_009758005             332 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Ahrensia sp. R2A130].
ACCESSION   WP_009758005
VERSION     WP_009758005.1
KEYWORDS    RefSeq.
SOURCE      Ahrensia sp. R2A130
  ORGANISM  Ahrensia sp. R2A130
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Ahrensiaceae; Ahrensia.
REFERENCE   1  (residues 1 to 332)
  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 332)
  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 332)
  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 332)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Ahrensia sp. R2A130"
                     /db_xref="taxon:744979"
     Protein         1..332
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=36096
     Region          1..331
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mlrrsaltlf clfasigaaf ancadgekkl rlgvtkliag sdlqrgsatv kervdrnlqg
       61 rfcldvledd nsfasdvams glqegaaemv lvdlgqlgrf vtvaqayrlp fafrheralt
      121 kfqtasnpal nevlksngaf vlanlvqpsv hfgarkplfe psdmagakvr tpeagnlsrp
      181 rlrpldavpq apsdagived lkagrvdive aswselqkla dakmithale shhlaggyal
      241 lvsnkwwegq sdelrkelsa lfkeavqqas frianadrna rnialaagld vriltdgqrn
      301 rwiarmsdlw gdfrasnppa vvdalesanr df
//
LOCUS       WP_009758024             158 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Ahrensia sp. R2A130].
ACCESSION   WP_009758024
VERSION     WP_009758024.1
KEYWORDS    RefSeq.
SOURCE      Ahrensia sp. R2A130
  ORGANISM  Ahrensia sp. R2A130
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Ahrensiaceae; Ahrensia.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Ahrensia sp. R2A130"
                     /db_xref="taxon:744979"
     Protein         1..158
                     /product="TRAP transporter small permease subunit"
                     /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=16942
     Region          32..153
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 merepafqpg iwvkalhgva alallaacll qvsvvglraa gigllwgqel vaalcavail
       61 tgsastlaqn rlvridvwsa grseklwrvl ekvgtvlfll pfslcliwfg wtyateswli
      121 gegsaeisgl pgryaikfli plfavsllla glakwrrs
//
LOCUS       WP_009758417             270 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Ahrensia sp. R2A130].
ACCESSION   WP_009758417
VERSION     WP_009758417.1
KEYWORDS    RefSeq.
SOURCE      Ahrensia sp. R2A130
  ORGANISM  Ahrensia sp. R2A130
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Ahrensiaceae; Ahrensia.
REFERENCE   1  (residues 1 to 270)
  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 270)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 270)
  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   4  (residues 1 to 270)
  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   5  (residues 1 to 270)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Ahrensia sp. R2A130"
                     /db_xref="taxon:744979"
     Protein         1..270
                     /product="TRAP transporter small permease subunit"
                     /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=30072
     Region          10..160
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mqehrhtgpv drltwtfsri amwgpafivs iifyevfmry vlskptlwvn emslwvggmi
       61 yvtaglyamq qrshirifvi ydlaplwlrr vfdiistlcv vifaiavvwg gfgealakfw
      121 rweafgtawd ppipatnkpl illtvvvlam qatsnlirdw pasklvrrif diactlgvia
      181 lsvmalpalf satdgdgmlk aplhwrvfls clivfsvglm vyglvkdfnd epqtldefee
      241 dhgipdqvls gnpppvdsaa grvaakdnag
//
LOCUS       WP_009758082             571 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Ahrensia sp. R2A130].
ACCESSION   WP_009758082
VERSION     WP_009758082.1
KEYWORDS    RefSeq.
SOURCE      Ahrensia sp. R2A130
  ORGANISM  Ahrensia sp. R2A130
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Ahrensiaceae; Ahrensia.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 571)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Ahrensia sp. R2A130"
                     /db_xref="taxon:744979"
     Protein         1..571
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=57860
     Region          60..310
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mttkiqnvyt nepsqsapda vtisksntpp apivpddmna kvtvtvaesg gpgedifgtd
       61 sddvltgkeg ddgfletkgn dtvdggagrn qidylgssse yaitrdgdtl tvvklnggtd
      121 tvtnvsgvyf fgddvwkats efsaatddsg ddsddcvgdd sgsddhpvdd gddttggdat
      181 ggdngfggkd ffgtddndvl tggegndgfl gsagndtidg gegynqidya gsssdysvtl
      241 dgdtltvvkp ngegtdtvsn vsgvyffgdd twkaveefga dgddgddsad nvdsydhpvd
      301 dvtdggsdda gdmtggdngf ggqdffgtdg ddvltggdgn dgflgyagnd vidggegynq
      361 vdytgsstdy qagiaadgsv tvikpngegt dtlvnvdgiy fagddvwkqv selgpidage
      421 eqpvdggdgn pvdgggeepv detpvvdcpv dgggeqaety gtdgfdilse dgssavygyg
      481 sadlifagsg davldggegf dvmhangast dytfnansdg svtassdvdg tdtmvdmeav
      541 yfagddqfam vssltgggea evemdaelsc f
//
LOCUS       WP_009759176             424 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Roseibium sp.
            TrichSKD4].
ACCESSION   WP_009759176
VERSION     WP_009759176.1
KEYWORDS    RefSeq.
SOURCE      Roseibium sp. TrichSKD4
  ORGANISM  Roseibium sp. TrichSKD4
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 424)
  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 424)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Roseibium sp. TrichSKD4"
                     /db_xref="taxon:744980"
     Protein         1..424
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46297
     Region          19..71
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mnsprlsiip araatdtslk prdlqvlcvl grhtddcgwc rrsqvkmane mgcarstvqa
       61 aidrlikagy lerhiqeten grdsahmfrv ildpvhpdmg aipgpendlg agegdafssv
      121 klpcrsvgtp agisappads gsapmlttpl ndpierkrer egerasagas geavpetatr
      181 ktwkarlrrv hagwpthadd sevtaerawf dlseadrdaa akavpaylah mkeigrkhcv
      241 afskylserr werlpeqaas asaapstakp fgkewgavrf adlmrspygr isgftrlqaa
      301 mieagtldre telrrkqaag gwpsvntmhe rairrrlgvp vqaalaglae gftqvkvgge
      361 vwqawkrlhe ergwpwlgad relpewvymp alpdghadvr aavaaalaif eanyhqlnae
      421 eaaq
//
LOCUS       WP_009760263             485 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Roseibium sp. TrichSKD4].
ACCESSION   WP_009760263
VERSION     WP_009760263.1
KEYWORDS    RefSeq.
SOURCE      Roseibium sp. TrichSKD4
  ORGANISM  Roseibium sp. TrichSKD4
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 485)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Roseibium sp. TrichSKD4"
                     /db_xref="taxon:744980"
     Protein         1..485
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=53391
     Region          11..472
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 midplemqvs vwaiytacfl lvclsvfvit lvwhsrrlna dclekdeaih tvrnldletg
       61 ipnqqafisq vdlkcgqsng tgttalfvig csspvnsvhe gvcqadrfls avspillpll
      121 rrwdnaplia rgrtgcflcl lhlhpnhqig svsedilsei kdyvgmkyed smlrpaigia
      181 lceqdggdps elisraqlaf eeavdvrhed ysvfhpslvt pqirretiak nighavehkl
      241 irphfqpcfd arsgrvfgle afarwhhpkl gwitppeflp cvrtsmlhad ldisvldqac
      301 admcrlsqqv pvtinlsket ilnddlaliv ervlsvyglk pqqlvfdige gaieaagsrs
      361 iqtlrglqgl gtklcldgfg wggarsfrnl svidwdmvkf dpelisqale diptrtlvng
      421 lmkatsdigi tplaknveta eqrdfllevg vfhaqgflyc gplafeeldk ifdeldalgg
      481 vaala
//
LOCUS       WP_009762670             428 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Microvirga lotononidis].
ACCESSION   WP_009762670
VERSION     WP_009762670.1
KEYWORDS    RefSeq.
SOURCE      Microvirga lotononidis
  ORGANISM  Microvirga lotononidis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Microvirga.
REFERENCE   1  (residues 1 to 428)
  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 428)
  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
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 428)
  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   5  (residues 1 to 428)
  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   6  (residues 1 to 428)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 428)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 428)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Microvirga lotononidis"
                     /db_xref="taxon:864069"
     Protein         1..428
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45476
     Region          <25..69
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          78..374
                     /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 mthvgnnhav sarrnrrlaf eliwregpis rtdlvartgl raqtisnivr elqdrglile
       61 sgrseggrga pqtylkinpg agssvglhld rdrlscvvyd lagqplafre dviewtdpaa
      121 avatmaaavk ltaeqceaad lwgvgvampt lqdaefdeyv gspgwqawsg fpiadrlqal
      181 tglpavvend ataaglgeli tgagrglsnf vyvfvgnglg agiiadglpf qgawnnagei
      241 gllswpenld ehpsgktpfs ldeladmlec svtaladpay lavlyekrna slmrwlelng
      301 rrlrllasii enlldpqtii vggllpssvc sslvdraypl qaspaarrdr kmprlqvgsl
      361 drkaaavgaa mlpfivngsp efrrlslgrg rgqpidaesl fdhvtgsggt kpqdeapsgr
      421 payapaap
//
LOCUS       WP_009762936             143 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Microvirga lotononidis].
ACCESSION   WP_009762936
VERSION     WP_009762936.1
KEYWORDS    RefSeq.
SOURCE      Microvirga lotononidis
  ORGANISM  Microvirga lotononidis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Microvirga.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Microvirga lotononidis"
                     /db_xref="taxon:864069"
     Protein         1..143
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=15668
     Region          35..111
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mptqlpnerq lrepgsmeld psgegiaiee trrliasskv egtpvfnqsg eqlgavynfm
       61 vdkisgqvay vvmsfggflg igesyhplpw raltydprlg gyvvdidrdr lveapqysag
      121 edpftdneyg arvdayyktt pta
//
LOCUS       WP_009763503             194 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Microvirga lotononidis].
ACCESSION   WP_009763503
VERSION     WP_009763503.1
KEYWORDS    RefSeq.
SOURCE      Microvirga lotononidis
  ORGANISM  Microvirga lotononidis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Microvirga.
REFERENCE   1  (residues 1 to 194)
  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 194)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 194)
  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   4  (residues 1 to 194)
  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   5  (residues 1 to 194)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Microvirga lotononidis"
                     /db_xref="taxon:864069"
     Protein         1..194
                     /product="TRAP transporter small permease subunit"
                     /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=22053
     Region          1..169
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mrfaylidri ntfigkavaw sivaltfavc yevfsryvlr sptewafdas ymlygllfmv
       61 agpyalarnn hvrgdflyrn wpprrqagld lvlyvlfffp gilafiyagl pftqmswmmn
      121 ehsmnspngp piypfkalip ivgvlmafqg laelirciac lrngdwpprl hdveetekli
      181 leqaeqeglt kgtv
//
LOCUS       WP_009764503             187 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Microvirga lotononidis].
ACCESSION   WP_009764503
VERSION     WP_009764503.1
KEYWORDS    RefSeq.
SOURCE      Microvirga lotononidis
  ORGANISM  Microvirga lotononidis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Microvirga.
REFERENCE   1  (residues 1 to 187)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Microvirga lotononidis"
                     /db_xref="taxon:864069"
     Protein         1..187
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=19898
     Region          27..139
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mrewitslcl lvgtisaaas aevsvsvnkt tqrmtvsvdg veryswpvst gttdystptg
       61 aftpsrlare hysrewddap mphsifftda ghaihgsrat gllgspashg cvrlspvnar
      121 ilfdlvqteg pantrieitg fdpigtavqg gngtplvysr ltsfdplrdg imaggpparr
      181 tdvrkqp
//
LOCUS       WP_009769760             380 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Paraburkholderia].
ACCESSION   WP_009769760
VERSION     WP_009769760.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 380)
  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 380)
  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   3  (residues 1 to 380)
  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   4  (residues 1 to 380)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 380)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 380)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..380
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39753
     Region          31..367
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(107..109,130..131,180,232,256)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkpmktamaf iacaaavlgl aggaaaqevv kigvagpltg saaqsgkdde rgvrlaveel
       61 naktfmvagk pvrfelvsmd dqgdpkvgvn vaqklvdggv aavighynsg vsipaariyn
      121 eahvvmmtga ssnpqlthlg fpyvfrlatn dnvmggrmal ysakvlgaqr aaviddrtay
      181 gtgvadvfve sakkagleiv areystdktt dfkailtqik srnpqvvfyg gyyaqaatla
      241 rqmgelgina tivggdgics pefdklsagv adkrmfcaqg gapldtlpdg kafrarfrsa
      301 fnadvdtyap afyaatlvva damqktgstk pevfvkalrd qaftsilgpv rfdangdwid
      361 apvtvyrlng gsltaiaqkd
//
LOCUS       WP_009770442             353 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Paraburkholderia hospita].
ACCESSION   WP_009770442
VERSION     WP_009770442.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia hospita
  ORGANISM  Paraburkholderia hospita
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 353)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Paraburkholderia hospita"
                     /db_xref="taxon:169430"
     Protein         1..353
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=38501
     Region          18..256
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 msrsistesg aaprpvhrrw admlredalc mhyqplldlr agrvtkveal arlrdgdvli
       61 apgqflpslg sddhlvlymr glaqvltqrn awrrvgidvv vsvnlppaal cdsryfdatr
      121 tafdefgcea geltleiles galpqgvald kqiagyktlg vdfaqddlgt ghsslsrlre
      181 lpfdcvkidr siadlqdhda advlpfihhl trlgqalgka vvvegvedpa lldalrifgv
      241 dlaqgygiar pmpgeqlpdw iaqtrfepqf tarasrcarl ahlmvweerm ladahlrtrs
      301 aagqhgsqad idtwfpddgp saqardglld aarnsgvhsg ayraarqrli aam
//
LOCUS       WP_009770469             269 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Paraburkholderia hospita].
ACCESSION   WP_009770469
VERSION     WP_009770469.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia hospita
  ORGANISM  Paraburkholderia hospita
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Paraburkholderia hospita"
                     /db_xref="taxon:169430"
     Protein         1..269
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=30794
     Region          12..>57
                     /region_name="YrrD"
                     /note="Uncharacterized conserved protein YrrD, contains
                     PRC-barrel domain [Function unknown]; COG3881"
                     /db_xref="CDD:443089"
ORIGIN      
        1 mlrsirdlhg civsaldgdi gsvrqayfdd eawavrylvv etgnwlkdrq vlvspysvqh
       61 tdpgssvvhv nlsrqqvrds pvldthkpvs rqheieylry ysyptywdgp nlwgmgaypa
      121 ydptdvpada lldtplqpdv dtnepeadvh lrstdevkgy rlktadgsig hvsdfiyddt
      181 dwafrylvvd thnwwpggka vliaihwidk vdwfestvst altrelikks payddsmpig
      241 rhyevvlhrf ydkhgywsdt dtyervasq
//
LOCUS       WP_009770479             257 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Paraburkholderia hospita].
ACCESSION   WP_009770479
VERSION     WP_009770479.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia hospita
  ORGANISM  Paraburkholderia hospita
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Paraburkholderia hospita"
                     /db_xref="taxon:169430"
     Protein         1..257
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=29126
     Region          4..70
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mlrsikslhg ctvaardgdi gsvdevyfdd eawgvrylvv dtgnwmherq vlispysvkh
       61 mdresgtvhv hltrqevrds pnidthkpvs rqheteylly ygyptywggp nlwgmgaypa
      121 fdvkdvspdp asealprpdl dadqvpadvh lhstnavegy hievadgsig hvsgfifddv
      181 awairyltvd trnwwpggke vlvatrwidl idwvgstvst rlsrdaikns peyddsvpfs
      241 rdyekrlhei hgrdgyw
//
LOCUS       WP_009771270             856 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Paraburkholderia
            hospita].
ACCESSION   WP_009771270
VERSION     WP_009771270.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia hospita
  ORGANISM  Paraburkholderia hospita
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 856)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 856)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..856
                     /organism="Paraburkholderia hospita"
                     /db_xref="taxon:169430"
     Protein         1..856
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=96879
     Region          231..790
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mtrkpeissd vlgslgaied wmpkfghpvt khvqhlegnr fmvtlvkrgv pfevhenvai
       61 ermfdrdtdt ysklgrdlgg rlgyhatftr rlvsfdrnyr fnprfmqwfs reyvgrfned
      121 rfyenryyls lilkyddfdd glkeieslaq qsllhlvdye aeqlevyerq hmngtkmlfs
      181 kqygfvsdlv natwtdvpva aepgtdvips swlhfgyntv airgpgvtps rqyatchdlr
      241 gfpdkpgwgq lnplltlpme ftitqsfncm tgfeanrtvd sainklesag dkakhqvkem
      301 reaqgyvntg elsfgeyhga aviygetake aiangdlfvs rslnecgvew mtatgsapft
      361 yfsqvpgakv kprpkvqssr nfaamhachd ystgkaegnp igdgsaiipf rtsaanvfnf
      421 nfhatrlgdi nvaeklaghf eakgttgtgk ttliaaaigm llrfepllyv ldkgrgwevf
      481 vramggvyvy lekgkptgwa pfeladapen reflyglvel cgrrngvdhq gkqiridlsa
      541 aekmqcrnav davmdiedvr lrrfslllds ipdegddclh arlsiwckse ggrfwwvfdn
      601 ppnlslnmsg qrcigfdvet flvenyepse paftwlfhlk tlmrrdgllm atiieeywlp
      661 irfrtireqi eetlasgrke gefiglvtqq peqaqkaadl ypalrsliat kiyladpaae
      721 eapylrdgmt rkefqefrkl taqsrrflik qgnqsafasf dlsglddaia vfsgdrenvl
      781 mldevraemg ddpnawlpvy llrvferrqr trltakhgad eqlwaeelhd algrkrlela
      841 aiyltanvem teeplv
//
LOCUS       WP_009774993             520 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Janibacter sp. HTCC2649].
ACCESSION   WP_009774993
VERSION     WP_009774993.1
KEYWORDS    RefSeq.
SOURCE      Janibacter sp. HTCC2649
  ORGANISM  Janibacter sp. HTCC2649
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Intrasporangiaceae; Janibacter.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 520)
  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 520)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Janibacter sp. HTCC2649"
                     /db_xref="taxon:313589"
     Protein         1..520
                     /product="M4 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=53626
     Region          30..520
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mkklsagfaf giavatavaa plavaqaaps aptanagqsp aakaeqakva daaktlglgs
       61 gqqlsvksvv tdpngtkhvr yertfkglrv iggdlvvera angatksvrw natkavevat
      121 tpklspgqar saakaagqdv sslvvfagea gprlaydvvv esvradqtps rlhtivdaqs
      181 gatldryddi vegtgnsqys gtvslgttls ggsyqlkdaf gnyttdlngg tsgtgtqftd
      241 addvwgngsv ssrqtaavda hygaektfdy yknvqgrngi wdtgvgarsr vhygnayvna
      301 fwdgtqmtyg dganntqplt aidvaghems hgvtentagl ayrgdaggln eatsdifgta
      361 vefyansaad pgdyligeki nirgngtplr ymdkpskdga skdcwstslk nldphyssgp
      421 lnhwfflase gsgartvngv aynspvcgta aavtgagran iekvwyrtls tkltsrsdyk
      481 aaregaitsa kelygagspt cvavksafda iavpagsatc
//
LOCUS       WP_009776331             330 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Janibacter sp.
            HTCC2649].
ACCESSION   WP_009776331
VERSION     WP_009776331.1
KEYWORDS    RefSeq.
SOURCE      Janibacter sp. HTCC2649
  ORGANISM  Janibacter sp. HTCC2649
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Intrasporangiaceae; Janibacter.
REFERENCE   1  (residues 1 to 330)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Janibacter sp. HTCC2649"
                     /db_xref="taxon:313589"
     Protein         1..330
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=35028
     Region          113..198
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
     Region          215..302
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mfrksapepe rsplplraas aagdlarrgv dmtrdtvhke lleraksqea lsddqiwrry
       61 qfrhlaafit ipalllgtas iaaaygtglm rgeqpkvvcq plvvlapaig sfkvtvlnss
      121 gqngaghtvg rdlsrrgfav gdvssaprtl yvkapariyh gkagldqall vaqtidgael
      181 endgragtgv tvvvgadftk mlpapppkpp dqksykvnvy natwrsglak atlteltarg
      241 fspgkqgndp dksflpndva vilhgpeadl aaaqvqshik gavlkevprd nmtidvilgn
      301 lyngvipaae mppkqavrkd ppptvsrpce
//
LOCUS       WP_009776716             420 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Janibacter sp.
            HTCC2649].
ACCESSION   WP_009776716
VERSION     WP_009776716.1
KEYWORDS    RefSeq.
SOURCE      Janibacter sp. HTCC2649
  ORGANISM  Janibacter sp. HTCC2649
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Intrasporangiaceae; Janibacter.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 420)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 420)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Janibacter sp. HTCC2649"
                     /db_xref="taxon:313589"
     Protein         1..420
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=45555
     Region          5..413
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mngvevwvsi ggvdvragtl yphrrrggta egasftyfde yianphaysl epglpleaga
       61 hqstvghsmf gafgdcapdr wgralikrre aaearaegre trslgevdhl lgvrddlrqg
      121 alrfrhgdgp feameergvp altdlpellt laeraetdsa dlpdlqrlir vgsslggarp
      181 kahvrdadgn laiakfpsaa hdtwnvmawe kvalelaara gitvptssll nladrtvlvv
      241 drfdrtread ggpagrvgyv samtmlqatd geqgsyleia eaiemrssrt tadlrqlwrr
      301 iifsivvsnt ddhlrnhgfl hedgdtwqls pafdinpnpe pgpkhlstai dlgddtasve
      361 lalsvadyfr lnaeeanevi aevqtavshw apvarqhgls sqeiaamswa feahsarask
//
LOCUS       WP_009777113             280 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Janibacter sp.
            HTCC2649].
ACCESSION   WP_009777113
VERSION     WP_009777113.1
KEYWORDS    RefSeq.
SOURCE      Janibacter sp. HTCC2649
  ORGANISM  Janibacter sp. HTCC2649
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Intrasporangiaceae; Janibacter.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Janibacter sp. HTCC2649"
                     /db_xref="taxon:313589"
     Protein         1..280
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30782
     Region          8..113
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          <75..263
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkyvgrvpap pldryiddly cmdgvpqhrr mdvpplpsah lianlgepvr lfdslpgvep
       61 tvitdgcfmg vwtrrfrief pspvrvvgvh fkpwgmapfi dvpssdlrdl cvpadavwgs
      121 awsgvherla aaasteelld vldgelrsrl aetpsrgldl vhhtasrlet swgdvsvsdl
      181 tgdagvsgnh latqftshvg vtpkrvariy rfarlilnld atqpvdwagl aheagyfdqa
      241 hlskefkdft gytptgylel rrrfpaeqgf ppdsgpmpak
//
LOCUS       WP_009778160             634 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Janibacter sp. HTCC2649].
ACCESSION   WP_009778160
VERSION     WP_009778160.1
KEYWORDS    RefSeq.
SOURCE      Janibacter sp. HTCC2649
  ORGANISM  Janibacter sp. HTCC2649
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Intrasporangiaceae; Janibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Janibacter sp. HTCC2649"
                     /db_xref="taxon:313589"
     Protein         1..634
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=68000
     Region          258..409
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 marrfsrfga galaatlaaa gltlsstsva satdwgtcla gpddtqsaft rasrvsgvpe
       61 dvllavgylg grwshhggqp svsggygvmh ltdapvapvs apekgdtnqg lpsragtlqv
      121 arqqtglsae qlrtdpvani cgaaavlasy qpgtttkapa gwskavarya gtadrqealh
      181 yaglvfdvlr agatettdlg dtvrlasnps aaldtsavad drllqpgvqe lecpatiecd
      241 vveaqyrstg pavtqyvnyd ladrekdlsi dylvvhntec tydvctklik geaepnrfvs
      301 whytvrsndg hvdqhvatrn vaahagnwyl nmhsvgvehe gkagepgtwy tealyrssae
      361 lvtylaaqkg ieldrahivg heefmssnyk wdpgpywdwe hymallgapi rpdrrgpsqv
      421 ftvkpgftdn arsldgcfat etqpgrpcps fgtnyvdvrt apsdsaplaw gssdlvsdrd
      481 aravaghkfy vmgrqgdwlk vwwdgsaawi kspkgdqanv vpsqgevvep vrpsvpvyar
      541 aypeasayag tpvpyqgqpt vtapdgsvlt lqpgqryvia drtvptdyyy aksfdnslpg
      601 dktvvtgtee yvqvwvghrf gyvkaadvrv lsgr
//
LOCUS       WP_009778221             336 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Janibacter
            sp. HTCC2649].
ACCESSION   WP_009778221
VERSION     WP_009778221.1
KEYWORDS    RefSeq.
SOURCE      Janibacter sp. HTCC2649
  ORGANISM  Janibacter sp. HTCC2649
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Intrasporangiaceae; Janibacter.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Janibacter sp. HTCC2649"
                     /db_xref="taxon:313589"
     Protein         1..336
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=36201
     Region          2..320
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 misvtgarkn ygdftalddv sleipagslt allgpsgsgk stllraiagl esldggrivi
       61 ngtdvtgipp qkrgigfvfq hyaafkhmtv rdnvafglti rkrpkaeikr kvddlleivg
      121 ldgfqhrypa qlsggqrqrm alaralavdp evllldepfg aldakvradl rqwlrrlhde
      181 vhvttvlvth dqeealdvad riavlnkgqi eqigdpisly drpandfvms flgsvarlgg
      241 qlvrphdial hrtleravql darvggspgv ieavvervvr lgfevrvdlr atsgerfaaq
      301 ltraeadala laagdtvfah tvnvvnpaet epalai
//
LOCUS       WP_009779318             538 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [Leeuwenhoekiella].
ACCESSION   WP_009779318
VERSION     WP_009779318.1
KEYWORDS    RefSeq.
SOURCE      Leeuwenhoekiella
  ORGANISM  Leeuwenhoekiella
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Leeuwenhoekiella"
                     /db_xref="taxon:283735"
     Protein         1..538
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=57624
     Region          4..538
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mksklikvhp ddnvavalvd lfagdvvefe gqslkiltds kakhkialvn lkaddpifmy
       61 gvlvgkalsa idvgglltte nvkheansvs qktettswta pdiskwkdrt fmgyhredgq
      121 vgtqnvwlff plvfcenrni ellkdvfeke lsfhkaskqr qllrnlinga pedtavaeie
      181 eeqaifdnie vkfithqggc ggirqdsvsl skllagyvnn pnvagatvls lgcqnlqidi
      241 fknalaeksa aikkpvliye qqqegtvdem lakiikdsfe gikkanqikr qpapisklkm
      301 glecggsdgf sgisanpalg yasdilaavg gspilsefpe lcgveqelvn rcvsdedaer
      361 fmhlmkayek savdagsgfd mnpspgnikd glitdamksa gaakkggtsp iqaildygey
      421 vtkpglnllc tpgndvestt amvgsgasvv vfttglgtpt gnpiapvlkv asnstlarrm
      481 pdiididsga virgektiee mgeeilehvi qvasgevqsk adalgqddfi pwkrgvsl
//
LOCUS       WP_009780213             281 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Leeuwenhoekiella
            blandensis].
ACCESSION   WP_009780213
VERSION     WP_009780213.1
KEYWORDS    RefSeq.
SOURCE      Leeuwenhoekiella blandensis
  ORGANISM  Leeuwenhoekiella blandensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Leeuwenhoekiella.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Leeuwenhoekiella blandensis"
                     /db_xref="taxon:360293"
     Protein         1..281
                     /product="formate/nitrite transporter family protein"
                     /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=30862
     Region          25..280
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mseeekkqqn idqelekset seesqakshg eilkeqiceg kkiytlskss vlissltagl
       61 elgfsymmlc svffhfsdsf sedtlfklia lvyplgfilv vlgqsilfte qtslltlpvl
      121 nrkhslmsll riwglvilgn liggwliglv lfwigpqlgi feaetvvtig ehvahfslpv
      181 ilvsailagw mmgllswlvt sskdtvsrii iiflitatma fvglhhsiig nievfgayll
      241 gtdislgryl wvqstalign aiggaffval lkyrafvnnv n
//
LOCUS       WP_009781630             128 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Leeuwenhoekiella blandensis].
ACCESSION   WP_009781630
VERSION     WP_009781630.1
KEYWORDS    RefSeq.
SOURCE      Leeuwenhoekiella blandensis
  ORGANISM  Leeuwenhoekiella blandensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Leeuwenhoekiella.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Leeuwenhoekiella blandensis"
                     /db_xref="taxon:360293"
     Protein         1..128
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14846
     Region          56..125
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mkrtllssif fctfagifsn valaqsaqaq vvqdsripel lklksqmtvn deladrykiq
       61 lfygqitean kvqdeyksky kqwepkivye spnykvwvgn frnrleadra llkikenfps
      121 afvmkper
//
LOCUS       WP_009783251             736 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Lyngbya sp. PCC 8106].
ACCESSION   WP_009783251
VERSION     WP_009783251.1
KEYWORDS    RefSeq.
SOURCE      Lyngbya sp. PCC 8106
  ORGANISM  Lyngbya sp. PCC 8106
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae; Lyngbya.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Lyngbya sp. PCC 8106"
                     /db_xref="taxon:313612"
     Protein         1..736
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=81791
     Region          1..715
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mteptktlcp ycgvgcgldv lppalpgkat nrdkqgnptw qvrgdrnhps sqgkvcvkga
       61 tvsealdkdr lthpmmresl depfrqvswd eafdrivnqi qtvrvtqgps gicmygsgqf
      121 qtedyyiaqk llkgclgtnn fdansrlcms savsgyiqsf gtdgppccyd dleqtdcafl
      181 igtntaechp iifnrlrvyh kknksvkmiv vdprctqtae aadlhlaikp gtdidllngi
      241 ahllmkwgff dslfiddctk gfsdyaevir hyqpglvark cgirlddlet aarwwgesnr
      301 vlslwsmgmn qssegtakvr tlinlhlmtg nigkpgagpf sltgqpnamg greagglahi
      361 lpgyrvvknp qhraeveefw glkpgsisph pglaawdmil gleqnkvgll wiaatnpavs
      421 mpdlertkaa yrkspftvyq dayyptetaa fahvvlpaaq wgektgtmtn sermvtlcqa
      481 frsplgvaka dweifaevgr rlgfaeqfdf adsaavrref iqltrnqpce msgitheals
      541 qfgpiqwpca enspdvavhn krlytdfrfn tpdgrakfga yhsrglaepp dpnypfvltt
      601 grlygqwhtq trtgriekiv kmhpepfiei hprdamklsl qegeivevrs rrgmarfpak
      661 itknitpgtv fvpmhwgslw aelaevnnlt hpescpdslq pelkacavql ipvkeirqtd
      721 fesnnlvnqk lfaire
//
LOCUS       WP_009783421             483 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Lyngbya sp. PCC 8106].
ACCESSION   WP_009783421
VERSION     WP_009783421.1
KEYWORDS    RefSeq.
SOURCE      Lyngbya sp. PCC 8106
  ORGANISM  Lyngbya sp. PCC 8106
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae; Lyngbya.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Lyngbya sp. PCC 8106"
                     /db_xref="taxon:313612"
     Protein         1..483
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=49275
     Region          67..317
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mallngdngn niingtwlad rirglngndq lfgnagndev fgglgadtie gnsgndrllg
       61 dsegsqfggp gnitlglntt sqnttvnnsf tpvvaefspt lnvrfddftf ltnndlirgg
      121 tgkdtilgeq gndrlygdsg ddrifggtgd dsvyggvgnd vlvgnsgdde ifggdgddni
      181 sgvsgndnif agdgndiadg gsgddvvrge agydllsggl gsdflsggen ndrllgqqdn
      241 dtldggsgnd ellggegdds isggigndsl sgdlgndtle gdwgddfltg degndslngg
      301 dgddslnggd gedllngsvg ddfldggddd dllnggdgsd iltggsgydi lngglgndsl
      361 iagggsdris ftfsemnqea efesfgndti dsflrgsnii dlsdvplgvf vddqlrtnfd
      421 aldtndndil ddgdfnvsvs ssgitinvlg avdpsqgefl ggseatifvk dvmeldgndf
      481 dfv
//
LOCUS       WP_009783625             324 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Lyngbya sp. PCC 8106].
ACCESSION   WP_009783625
VERSION     WP_009783625.1
KEYWORDS    RefSeq.
SOURCE      Lyngbya sp. PCC 8106
  ORGANISM  Lyngbya sp. PCC 8106
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae; Lyngbya.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Lyngbya sp. PCC 8106"
                     /db_xref="taxon:313612"
     Protein         1..324
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33284
     Region          3..246
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mltiislpng eiqnpdgtls lfppdgvqgv grsvelrgsg vfigtasidt ifsfdegski
       61 vfgledsdef tgfglgttlf yggsgddnft ggfgddtvyg gvgvealrgg dgndllfgqt
      121 agdsidgqmg ndtilggegd dfirdeslpl einllyggqg ddnltagagn dsiwgdqgnd
      181 nlqagagvdv ltggsgfdvl iggdlgippe ggapsfpgdd tpdefvlevq sdisfdlisd
      241 fedgidkfml pegisfddla iaelstdadi lnqiselpwi naptdvgirl aqtgqllavl
      301 ngnigdnpai pvlasnqida edfv
//
LOCUS       WP_009783852             522 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Lyngbya sp. PCC 8106].
ACCESSION   WP_009783852
VERSION     WP_009783852.1
KEYWORDS    RefSeq.
SOURCE      Lyngbya sp. PCC 8106
  ORGANISM  Lyngbya sp. PCC 8106
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae; Lyngbya.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Lyngbya sp. PCC 8106"
                     /db_xref="taxon:313612"
     Protein         1..522
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=54067
     Region          157..408
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mpepdrivni etvigatgqd naidgstgis gqtsfdvdls qqrltvenlp glgdqtfeii
       61 nfanvtgtsg addivgddne nelkggegad dlvggggddr iignqgsdrl tgvdpssakp
      121 gegevdvlng gdggdtfilg didnifysfs gngdfadiln fqsgqdtiql sgnfddyifk
      181 senteifsan nndliakftn gafdttdlmf lhtgnditgt pdndsltgtn rddsikglag
      241 ddtikglggd dtiegnkged niegnegndq ldggkdedti dgnqgddhle gkkdedvlng
      301 gegndqldgg kdedilngsd gedtlqgeka ddlleggegn dlleggkded tlnggggndt
      361 lmgekgddll dggegddlld ggdredtitg gtgndtlngg dnddvligvd ptasqpgmge
      421 vdtltgdepg dedddifvlg desqayyddg yeadyalitd fddkdviqls gsagdyelgt
      481 sptglpggta iflttggfde ligiventsd ldlsddkvfn fv
//
LOCUS       WP_009784548             186 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Lyngbya sp. PCC 8106].
ACCESSION   WP_009784548
VERSION     WP_009784548.1
KEYWORDS    RefSeq.
SOURCE      Lyngbya sp. PCC 8106
  ORGANISM  Lyngbya sp. PCC 8106
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae; Lyngbya.
REFERENCE   1  (residues 1 to 186)
  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 186)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 186)
  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   4  (residues 1 to 186)
  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   5  (residues 1 to 186)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Lyngbya sp. PCC 8106"
                     /db_xref="taxon:313612"
     Protein         1..186
                     /product="TRAP transporter small permease subunit"
                     /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=21027
     Region          4..171
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mqvllqisrl idqfnefigr ivywfallmi gvgtwnvvgr yigrsvgqnl ssnalietqw
       61 yifdvifllg aaytlkhneh vrvdviqsrl ntkykalvdf lgsvlflipf svmvifyswg
      121 tisnswkile tspdpgglpr ypiksliivs fvlliiqgis eaiknfaifk gilspetedp
      181 nrraie
//
LOCUS       WP_009784692             127 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Lyngbya sp. PCC 8106].
ACCESSION   WP_009784692
VERSION     WP_009784692.1
KEYWORDS    RefSeq.
SOURCE      Lyngbya sp. PCC 8106
  ORGANISM  Lyngbya sp. PCC 8106
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae; Lyngbya.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Lyngbya sp. PCC 8106"
                     /db_xref="taxon:313612"
     Protein         1..127
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14711
     Region          25..113
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 msnhiqywre rqakqkaqnq rmvmqarsql vdivnvlvdk fkvtkvivfg slvkdkftae
       61 sdidiavegi rkqdfftals evnrqtnrwv dlkpiedlep hfrqrvfetg eciyeadfsk
      121 snsgtdn
//
LOCUS       WP_009785656             243 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Lyngbya sp. PCC 8106].
ACCESSION   WP_009785656
VERSION     WP_009785656.1
KEYWORDS    RefSeq.
SOURCE      Lyngbya sp. PCC 8106
  ORGANISM  Lyngbya sp. PCC 8106
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae; Lyngbya.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Lyngbya sp. PCC 8106"
                     /db_xref="taxon:313612"
     Protein         1..243
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24998
     Region          <4..179
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 martingtsg ndfideyvse dltvyanggd dyvwtgwgdd liygddgndt lkgwsgddfi
       61 dggagndqvy gedgndtldg wsgndlvygg ngndfiwgwy gndslngggg ndtllgendd
      121 dvlngssgnd singgsgidt liggsgkdtl ngggggghys gfdnltggag edvfvlrnds
      181 ytviedfevg idkislgsgl sfadldffqg ynttiislps anisiaglqg vssddldsps
      241 nfv
//
LOCUS       WP_009785873             484 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Lyngbya sp. PCC 8106].
ACCESSION   WP_009785873
VERSION     WP_009785873.1
KEYWORDS    RefSeq.
SOURCE      Lyngbya sp. PCC 8106
  ORGANISM  Lyngbya sp. PCC 8106
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae; Lyngbya.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Lyngbya sp. PCC 8106"
                     /db_xref="taxon:313612"
     Protein         1..484
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51274
     Region          3..209
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mlsdiiteng ldlgiattgn dsiimsqlpp dqlayfsasp fpdaiallqg ddnllndntg
       61 rifygnqgsd tiiggggndt lfggqeddfl eagggnsilf gnfgndtlig gpgndslygg
      121 agndvviggs gnsivsgdkg ldtltgsgga nqfilassga dqdvitdfqp gidkmrlpag
      181 vtfadlevrg sganteilsn gevvailngv isssinsndf iaagqetppp pppppvsiep
      241 gntpetagdl glfsgirefd nfvgtadsdd yyrftlsevh efdldlfnle qdatvqlylg
      301 eenldgtfdl gqlietsnnw sdaeesisrs lgagtyfvrv ypryndvdtr ynlrltatpt
      361 gitdspqdgl sflnlgslng trtftdfvgt adsndyygfl ldevkdfnlv lgdleqdatv
      421 qlylgednld gtsnlgrvie tsnnwsdaee sisrslgagi yfvrvypryn dvdtrytlql
      481 tata
//
LOCUS       WP_009786131              86 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Lyngbya sp. PCC 8106].
ACCESSION   WP_009786131
VERSION     WP_009786131.1
KEYWORDS    RefSeq.
SOURCE      Lyngbya sp. PCC 8106
  ORGANISM  Lyngbya sp. PCC 8106
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae; Lyngbya.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 86)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 86)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 86)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Lyngbya sp. PCC 8106"
                     /db_xref="taxon:313612"
     Protein         1..86
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=9427
     Region          7..86
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 msslaitvtv qlfaiyqevy kvrklvltlp pqtpvsqvle hcigehpele rwrplthfgv
       61 nlqfvppetp lsngdevvli ppvsgg
//
LOCUS       WP_009786938             639 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Lyngbya sp. PCC 8106].
ACCESSION   WP_009786938
VERSION     WP_009786938.1
KEYWORDS    RefSeq.
SOURCE      Lyngbya sp. PCC 8106
  ORGANISM  Lyngbya sp. PCC 8106
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae; Lyngbya.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 639)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Lyngbya sp. PCC 8106"
                     /db_xref="taxon:313612"
     Protein         1..639
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=71503
     Region          25..639
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 midkllrtlk rkwpdatefs ivatatfvli iallgvihlg glqplelvvy dqmmrlrstl
       61 ppdprilvva iteediqtyn rfplsdqlia ellekllelq prvigldlyr dipyepgheq
      121 lvkqlqfpni iaiknlgdpd akgvpappei dpsrvgfndi pldydnvvrr nlffadstsg
      181 tsfsfslqla lhylksqgiq pqndpadpdr irlgkaifvp lktdsggyqn idakgyqill
      241 nyrsgmdgvv tvnvsevlng siepdwvknk ivligttaps gkdlfltpys pgkknsprtp
      301 gviihaqmvs qiidaatger plfqfwpqwv eiiwisswai igttlawlsr hplilvlgsp
      361 lllgilftls fmlflnaywv pvvspgfafl ltsatlisyr afqaqrqqqi mmrllgqnas
      421 peiaealwks rdrlifdgkl pgqkltatil ftdirnfsti seqmppenll ewlneylaml
      481 tqtihnhhgi inkftgdgim aafgvpmarv senqiardar aavscalems eqlqklnlvw
      541 qprglpviqm rvgiftgpiv agslggrdrl eygllgdsvn iasrlescqk erqssvcril
      601 iayqtlqyid hqfeveswgl mplkgkqqmv dvyrvirkl
//
LOCUS       WP_009787708             111 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Lyngbya sp. PCC 8106].
ACCESSION   WP_009787708
VERSION     WP_009787708.1
KEYWORDS    RefSeq.
SOURCE      Lyngbya sp. PCC 8106
  ORGANISM  Lyngbya sp. PCC 8106
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae; Lyngbya.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Lyngbya sp. PCC 8106"
                     /db_xref="taxon:313612"
     Protein         1..111
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12540
     Region          4..104
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(4,22..23,31,34,36..37,39,42..43,45,54,59,68)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(22,54..55,57,84)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mstydkiydi vrqipvgkva tygqvaelan lagkarlvgy alyrvdiqss dipwyrvina
       61 kgeishstlr qgtdyyqktr leeegivfts dgkiklsqyq wqpsyemgil n
//
LOCUS       WP_009790411             300 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Synechococcus sp.
            BL107].
ACCESSION   WP_009790411
VERSION     WP_009790411.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus sp. BL107
  ORGANISM  Synechococcus sp. BL107
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Synechococcus sp. BL107"
                     /db_xref="taxon:313625"
     Protein         1..300
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32083
     Region          20..264
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 magapeamkv rcvldaqagl aegphwwvek svliwvdiea srvgffdpvt grnrflvvps
       61 higavvpmsd gellaataqg fvrlhpdsgv vsslqdpedd qpgnrfndgk cdpwgrfwag
      121 tmaydfaaga gslwrvnpdf scirqrhglt ipnglawsqd rgtlyfidsp trqvlafplt
      181 ssgdfsgepi pcitipedwd avpdgmcida egmlwialfg ggavtrwdpa sglllerlal
      241 pcrqvtsccf ggpnldqlfv ttarqemdaa aikaeplagg lfqadvgvkg ltadcfqlaa
//
LOCUS       WP_009792923             549 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: M4 family metallopeptidase [Bacillus].
ACCESSION   WP_009792923
VERSION     WP_009792923.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 549)
  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 549)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..549
                     /product="M4 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=59698
     Region          60..548
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mtkklatlvl gtslalsaaf paatayglsp sekllnqmel qqkleqkekh apkflagkls
       61 knkakndddi kkflkdnkdl fkvdpfkeli llnaeiddlg mkhykfsqsi ngvpvegaif
      121 kvhtdknsdv taatgqlyad asekitdtka aiskkeavdl awkninltee dtkgsdqavp
      181 adlekagkks evknthvknd lvihekdgey tlaykvqlqf iepyganwqi fvdaknghiv
      241 eaynavadaa atgtgtgvtg gsktlntyss ggtyylydvt kpmngvietf tanngsslpg
      301 srsadsnnaw tatnqradvd ahyyagkvyd yfknthnrns fdnngatirs tvhygsrynn
      361 afwngsqmvy gdgdgsqfts lsgaldvvah eithavtert anlqyqyqsg alnesfsdvf
      421 gyfldpgdfl mgedvytpgr sgdalrsmsn ptlygqpehm nqyvntssdn ggvhinsgip
      481 nkaayytiss igkaqaekiy yraltvyltp tsnfsyaraa llqsaadlyg sgssaynavr
      541 tawdnvgvy
//
LOCUS       WP_009793498             295 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Bacillaceae].
ACCESSION   WP_009793498
VERSION     WP_009793498.1
KEYWORDS    RefSeq.
SOURCE      Bacillaceae
  ORGANISM  Bacillaceae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales.
REFERENCE   1  (residues 1 to 295)
  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 295)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 295)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 295)
  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   5  (residues 1 to 295)
  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   6  (residues 1 to 295)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Bacillaceae"
                     /db_xref="taxon:186817"
     Protein         1..295
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33482
     Region          21..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..287
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mdllkqlnea iayieenltg didyreaakk afcsefhfkr mfvflsgvsi seyvrkrrlt
       61 maaleladek ikvidaavky gysspdsfsr affqmhgitp searktgyrl kafppmsfql
      121 tikggnemnf rleekgpfyi vglkkrvriq fngvngeiae mwrsltpdki qelkalsdqe
      181 pgglisasvh fsegrmkekg eldhyigaat gepgparyes lkiessswav feakgpfpet
      241 lqniwgriya ewfpssgyeq tegpeilwne skdtsspqfk seiwipvikr ktpfk
//
LOCUS       WP_009793863             109 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Bacillus].
ACCESSION   WP_009793863
VERSION     WP_009793863.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..109
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12373
     Region          1..102
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(4..5,23..24,32,35,37..38,40,43..44,46,54,59,67)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(23,54..55,57,82)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mqpftqrtik iikeipagkv mtygqiaala gsprearqvv rilhslsrqe klpwhrvisk
       61 mgeismkdpm lreeqrflle aegitvdvkg iirlenflhe pkkgldnnt
//
LOCUS       WP_009794158             653 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter permease [Bacillus].
ACCESSION   WP_009794158
VERSION     WP_009794158.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 653)
  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 653)
  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 653)
  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 653)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..653
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..653
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=69784
     Region          9..643
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 msnkgetltq eqqqelleky dpeagtrklk gvlgwivflg llsfslfqly tgifgvltaq
       61 lqrsihlgfa lalifllfpa rkkdrgkkhk vawydlilai aavavgaywp lmideivmrv
      121 grltdldfyi gltaiilvle atrravglpi tiiaalflay alygpympgf lahrgldlqr
      181 lvqtmfftte gilgtplgvs atfiflfllf gsflvktgvg qyfndlavsi agkrtggpak
      241 vaifssalqg tisgssvanv vtsgsftipm mkklgykkef agaveaaast ggqlmppimg
      301 aaaflmvefi gggitywdia kaaaipally ftgiwimthf eakriglrgl kkeempnrkk
      361 vlskiylllp ilavvvllms gmsviraalw silitiavsa ikketrinfk daidalvdga
      421 rtalgvaaat aaagiivgvv tktglglkla nglldlagga liptlmltml aaivlgmgsp
      481 ttanyvitst iaapaiillg vpdlsahlfv fyfgiiadit ppvalaafaa agvsggepik
      541 tgvnsaklai aafiipymfv lspellmidt twyylvwvvf talagmmaig sgvigywfrr
      601 lwwferiigi vgglcliype tltdiiglvs faaliilqfv ikrddslkpq tag
//
LOCUS       WP_009794231             307 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Bacillus].
ACCESSION   WP_009794231
VERSION     WP_009794231.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 307)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..307
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=34573
     Region          63..295
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mqkqeswika pyqsldelet kleaicrqlg dsakklkagi sqygtkpaql lnaselfsrv
       61 shremvhtiq hgefhsyqqp iinlkegdri ygyesllrta gskqippgil fktaeetglm
      121 smldqkarea aikarkniip pgiksfinfl pstiynpdfc lqhtfqivek yeidpadlvf
      181 evvetekisd idhlkkvlnt ykkrgmkval ddvgagfstl emlealqpdy lkidrsfidr
      241 cdqrpesqqf lskvmniadg lgiivlaegi erkeelefcr sigadlaqgy yigrpakeie
      301 salqvns
//
LOCUS       WP_009794306             170 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase family protein [Bacillus].
ACCESSION   WP_009794306
VERSION     WP_009794306.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 170)
  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 18888537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..170
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=18482
     Region          6..51
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
     Region          64..168
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mewlliyhtv rqgetltsis mdyrrpiaql laanpqisnp nqiyqgqrvm ipglpepsai
       61 pysisitlst rrlsllkngi lqktypvgig kmltqtppgd yvivnrepnp ggpfgimwls
      121 lskagygihg tnnpasigka vskgcvrmnn qdvlelsgiv pngtrvmirn
//
LOCUS       WP_009794484             291 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Bacillus].
ACCESSION   WP_009794484
VERSION     WP_009794484.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..291
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31926
     Region          14..257
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mgeaelvlda katlgegpcw daekqllywv dikekkvnif npasgenrei qldqnigtiv
       61 prnaeeaava ledglyllnl etekltlike lesdipsnrf ndgkcdpagr fwagtmdqqg
      121 agaegalycl dtdqqvekkl dqlgisngla wspdnrfmyf idtptkkisr fdfdlgtgai
      181 enrtevisfp egdgapdgmt idgegmlwia hygggkvsrw nphtgkklse ikvpaknvtc
      241 ctfggedlkd lyittardgl neeqqkeypl sgglfrvktd vkgspaysyk g
//
LOCUS       WP_009795880             674 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Bacillus].
ACCESSION   WP_009795880
VERSION     WP_009795880.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 674)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 674)
  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   3  (residues 1 to 674)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..674
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..674
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=74416
     Region          1..674
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          174..252
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 memsqylevf ieesrehlqa inehllelek npadlkiine ifrsahtlkg msatmgyedl
       61 arlthqmenv ldairnqkig vtpelldtvf lavddleamv lsiseggdgk rdvstavkql
      121 eliengqtpl mesrqeaaaa aaaeaevpae lrsdydefer tvlsqskeqg fdvfeisisl
      181 redcllkaar vfmvfevlek sgeiiksnpp vdvleeeqfd saftvtlvtk epkeeiqaki
      241 mkvseiekae iinidlmpas paeeepapap giiqpveepk eesrngapak qassktirvn
      301 ierldilmnl feelvidrgr leqiskelnn qelhetverm srisgdlqni ilnmrmvpve
      361 tvfnrfprmv rqlardlnkk inleivgaet eldrtvidei gdplvhlirn aldhgvetpe
      421 vrkangknee gtvvlkayhs gnhvfielid dgaginrdkv lqkavkngii teqagasltd
      481 kqvyelifas gfstadkisd vsgrgvgldv vkstieslgg tvtidsqegk gstfsiqlpl
      541 tlsiisvmli evqkekyaip lssiietaii kkedimnahn qkvidfrgkv vpllflkdvf
      601 avpvhleedg yysvvivrkg dkmaglvvds figqqeivlk slggylndif aisgatilgd
      661 gqvalivdcn alin
//
LOCUS       WP_009796603             168 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: endonuclease domain-containing protein [unclassified
            Nitrobacter].
ACCESSION   WP_009796603
VERSION     WP_009796603.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nitrobacter
  ORGANISM  unclassified Nitrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Nitrobacter.
REFERENCE   1  (residues 1 to 168)
  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 168)
  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   3  (residues 1 to 168)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="unclassified Nitrobacter"
                     /db_xref="taxon:2620411"
     Protein         1..168
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18146
     Region          17..114
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mphaavstlq rsrakqlrrt mtpaetllwr hlkanrtdgl sfrgqapfgr yivdfvclsa
       61 kliveldgys hdfgvqqkdd kvrdaffvae gfrvlrfsnh dvtsnlegvv etirltasac
      121 ascsppslpl phkgggnrks acqtsasssv sdqtsseiaa tsirgpqp
//
LOCUS       WP_009796724             117 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Nitrobacter sp. Nb-311A].
ACCESSION   WP_009796724
VERSION     WP_009796724.1
KEYWORDS    RefSeq.
SOURCE      Nitrobacter sp. Nb-311A
  ORGANISM  Nitrobacter sp. Nb-311A
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Nitrobacter.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Nitrobacter sp. Nb-311A"
                     /db_xref="taxon:314253"
     Protein         1..117
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=12827
     Region          16..74
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mdgrtenlis sdkhsgkavy gaedkkigsi ecvminkssg epayavlsvg gflgmgddhy
       61 pvpwkllryd seldgyrsdi sgnrlkgapk hgselfdwta rraelddyyn devirpg
//
LOCUS       WP_009797701             345 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Nitrobacter].
ACCESSION   WP_009797701
VERSION     WP_009797701.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nitrobacter
  ORGANISM  unclassified Nitrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Nitrobacter.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 345)
  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   6  (residues 1 to 345)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="unclassified Nitrobacter"
                     /db_xref="taxon:2620411"
     Protein         1..345
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38855
     Region          26..211
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          134..344
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mnpstkdkiy svakiativd llrdegipak ealadislsp eqlrspatkv saaqvlqsyr
       61 naiklsthpr fayhaglksc vstygiygla ilsctdfrnt mafaaayhql atpmmeicfk
      121 eegstavwiv tpthdldidd rlyrfivefq mavhlslhrn imgpafkpal idyalrrphd
      181 dgsgtaffdc pilydkpenr ftfdaawldr rpdygnelty aelrqlcdgl lkqlklgagv
      241 agevrglila nlsmpiefkr iakylnmser slrrrlqeeg tsfrqladel kaqiaikyir
      301 dtdlsveeia falgfgdaas frhafrrwtn atpqdyrksg irret
//
LOCUS       WP_009797830             832 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [unclassified
            Nitrobacter].
ACCESSION   WP_009797830
VERSION     WP_009797830.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nitrobacter
  ORGANISM  unclassified Nitrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Nitrobacter.
REFERENCE   1  (residues 1 to 832)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 832)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 832)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..832
                     /organism="unclassified Nitrobacter"
                     /db_xref="taxon:2620411"
     Protein         1..832
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90530
     Region          77..125
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          104..832
                     /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 msgaedngcg kgagaahkiv llgsaaalmv vvsgaivgsa saqtiplqqs apqtiafnip
       61 aqdlggalna fadraglrll fpsnlvaglr saglagsltr nqaltrllag sgltyrftsa
      121 ntvtiadsaa asagaapaga isldtidvqg asssdpgkte gtgsytpsvt asstrlqltp
      181 retpqsisii trqqiddfkl ltvndvmtqt pgistvtyen erveyyargf airnfqddgm
      241 pgfyasgypa gqslsdmamy drvevlkgan glmtgtgdpg atvnlirkkp tsvfqghttl
      301 tggswdtyrg eldlsgpfnk egtvrgrfva thqdrgsymn yfknrsslvy gvleadltpd
      361 tlftvgahyq ynipkgtsfg giplfdsngd fnqmprsfnp garwssweqy vysafttleh
      421 hfdndwrvkl qlkrqvngyd trlgsasdgn pnpldgsgvs iwtgaflgqt qldvaeayat
      481 gpvhlfgrkh dlvlggiisk rhwrnsissa dpaydptvpn fydwngnipq pawvldgvgn
      541 evmrnraaya tfrfnahdkl kliagtrilr yewmqrpywd psveersnrs vvvpyfgaif
      601 dinehlsiyg shtgifqpqy erteqgitlp pqegvsnevg lksaffngrl nssaayfeiq
      661 qnnypvptgg lapdgnpayq avdgvvtkgf eleisgqlsp qwqiqtgfth kisrrdsikv
      721 stltpenqft lyttykldga ldgltvggga rwqditwsdq vwngvigadv tstapsywva
      781 dlmanykfne nlsatfnvrn lfdkkyysiy nwyssytwga prsfllsmty kf
//
LOCUS       WP_009798166             120 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Nitrobacter sp. Nb-311A].
ACCESSION   WP_009798166
VERSION     WP_009798166.1
KEYWORDS    RefSeq.
SOURCE      Nitrobacter sp. Nb-311A
  ORGANISM  Nitrobacter sp. Nb-311A
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Nitrobacter.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Nitrobacter sp. Nb-311A"
                     /db_xref="taxon:314253"
     Protein         1..120
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=13083
     Region          14..78
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mavkrktshl rpsrklsgka vygakgakig sikhvlvdek kgktayavlg iggflglgda
       61 hymvpwkvlr ydadrgayss disenrlkgr pkhgvetifd lnaryatlhp rnnefvvhpg
//
LOCUS       WP_009799033             349 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [unclassified Nitrobacter].
ACCESSION   WP_009799033
VERSION     WP_009799033.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nitrobacter
  ORGANISM  unclassified Nitrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Nitrobacter.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="unclassified Nitrobacter"
                     /db_xref="taxon:2620411"
     Protein         1..349
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38366
     Region          1..345
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msielknivk rfgafsalnn vdltiadgel lallgpsgsg kttllriiag ldwpdsgsvs
       61 fdgenalarg agerqvgfvf qhyalfrhmt vfenvafglr vqprairkde asirarvkel
      121 ldlvqldwla drypsqlsgg qrqrialara lateprilll depfgaldak vrkelrrwlr
      181 slheeihvts vfvthdqeea levanrvvvm dkgrieqigk pgevydspat afvhgfiges
      241 ivlpvdiqdg virlggtpln iaaecgaagp sklfvrrhdm qisppgwggl egtvrrvrsf
      301 gpiqradial sdgqgetiie idaprdrelr sgevvglqpr ryrifadrt
//
LOCUS       WP_009800251             163 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Nitrobacter sp. Nb-311A].
ACCESSION   WP_009800251
VERSION     WP_009800251.1
KEYWORDS    RefSeq.
SOURCE      Nitrobacter sp. Nb-311A
  ORGANISM  Nitrobacter sp. Nb-311A
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Nitrobacter.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Nitrobacter sp. Nb-311A"
                     /db_xref="taxon:314253"
     Protein         1..163
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=17417
     Region          44..102
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mtdpetrpsv gkdvhqdpag dspppapdnt rpssnlvssd kyngkavyga edkkvgaies
       61 vmvdkssgep ayavlsiggi lgmgaehypv pwrllrfdse ldgyrsdisg nrlkgypksv
      121 fgssgselfd wtaeraelds yyanidtvtt kegeenpltr stg
//
LOCUS       WP_009799383             140 aa            linear   BCT 20-JAN-2025
DEFINITION  transcription termination/antitermination protein NusG [Nitrobacter
            sp. Nb-311A].
ACCESSION   WP_009799383
VERSION     WP_009799383.1
KEYWORDS    RefSeq.
SOURCE      Nitrobacter sp. Nb-311A
  ORGANISM  Nitrobacter sp. Nb-311A
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Nitrobacter.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Kang,J.Y., Mooney,R.A., Nedialkov,Y., Saba,J., Mishanina,T.V.,
            Artsimovitch,I., Landick,R. and Darst,S.A.
  TITLE     Structural Basis for Transcript Elongation Control by NusG Family
            Universal Regulators
  JOURNAL   Cell 173 (7), 1650-1662 (2018)
   PUBMED   29887376
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Liu,B. and Steitz,T.A.
  TITLE     Structural insights into NusG regulating transcription elongation
  JOURNAL   Nucleic Acids Res 45 (2), 968-974 (2017)
   PUBMED   27899640
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Steiner,T., Kaiser,J.T., Marinkovic,S., Huber,R. and Wahl,M.C.
  TITLE     Crystal structures of transcription factor NusG in light of its
            nucleic acid- and protein-binding activities
  JOURNAL   EMBO J 21 (17), 4641-4653 (2002)
   PUBMED   12198166
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415705
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Nitrobacter sp. Nb-311A"
                     /db_xref="taxon:314253"
     gene            1..140
                     /gene="nusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
     Protein         1..140
                     /product="transcription termination/antitermination
                     protein NusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
                     /calculated_mol_wt=15621
     Region          6..>96
                     /region_name="NusG"
                     /note="Transcription termination/antitermination protein
                     NusG [Transcription]; COG0250"
                     /db_xref="CDD:440020"
ORIGIN      
        1 maeqfwaacr tftgrehvvr akieeldrga flptyvrswv sggrlssser aavpgyvffr
       61 ssrddwppvq gvdgvigvll dgdramrisn demarlvldh aagahnrfdg cvseasrsgr
      121 rksrkprrsk rarmrsltvq
//
LOCUS       WP_009800776             373 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [unclassified Oceanicaulis].
ACCESSION   WP_009800776
VERSION     WP_009800776.1
KEYWORDS    RefSeq.
SOURCE      unclassified Oceanicaulis
  ORGANISM  unclassified Oceanicaulis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Maricaulaceae; Oceanicaulis.
REFERENCE   1  (residues 1 to 373)
  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 373)
  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 373)
  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 373)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Oceanicaulis"
                     /db_xref="taxon:2632123"
     Protein         1..373
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40435
     Region          1..365
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mdrrtflsga avvaagaasa csqengaqsa paapavnrnr trrlrmvttw ptgfpglgsa
       61 aertaqfite msggaldvev ygageivgaf evfdavsngv admyhgaeyy wqgrspafnf
      121 ycavpmgmta heimgwveyg ggqelweels gqfgliafqa gnsghqmggw fkrevntled
      181 frglrmripg lggsvlrelg gaavalsgge iyqslqsgai datewvgpwn dlafgfyrea
      241 pyyygpgfhe pgsalavgln rgvwdslpad qqaivraaar aannqslaef tyqnglalrt
      301 ltgehgvqlr qfseeiwrev griseqvvad tanadplsrr vyesyrearr lgrdwanvse
      361 apyyqnrelv lgr
//
LOCUS       WP_009801014             246 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Oceanicaulis sp. HTCC2633].
ACCESSION   WP_009801014
VERSION     WP_009801014.1
KEYWORDS    RefSeq.
SOURCE      Oceanicaulis sp. HTCC2633
  ORGANISM  Oceanicaulis sp. HTCC2633
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Maricaulaceae; Oceanicaulis.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Oceanicaulis sp. HTCC2633"
                     /db_xref="taxon:314254"
     Protein         1..246
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=25718
     Region          143..>204
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mlnklmltts ialisttala taqaqdagmq aemetsaeat mssdmvkasd ivgadleyad
       61 gasaitdirm ndagdpealv isrggflglf deevavstva asiahdaege lvvtasltda
      121 qledaeaiqd spfvvsiedq redgdlfysd ltgaailnda getiahledv kftlsgetey
      181 aiirdggflg lggevglvdf nelelaysae tgwtvtsdit gddvrvmeet pintgayldg
      241 rqfprg
//
LOCUS       WP_009801495             245 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [unclassified
            Oceanicaulis].
ACCESSION   WP_009801495
VERSION     WP_009801495.1
KEYWORDS    RefSeq.
SOURCE      unclassified Oceanicaulis
  ORGANISM  unclassified Oceanicaulis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Maricaulaceae; Oceanicaulis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="unclassified Oceanicaulis"
                     /db_xref="taxon:2632123"
     Protein         1..245
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=26435
     Region          2..153
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
     Region          <150..>213
                     /region_name="YcbB"
                     /note="Murein L,D-transpeptidase YcbB/YkuD [Cell
                     wall/membrane/envelope biogenesis]; COG2989"
                     /db_xref="CDD:442228"
ORIGIN      
        1 mqvikhaspn fnerrlplsm lvlhytgmet geaaierlad sdagvsahyv veetgriiqm
       61 vaedkrawha gkgvwrgced vnsasigiei vngghdfglp dypeaqivav lalsrailsr
      121 hpiaacdvig hsdlapdrkq dpgekfpwkr laengvglwp dpapagfaps apgddgeave
      181 alrqslfeig ygvartgayd dalksvvlaf qrrfrpdlls gnadeetcvl ieglrrkvts
      241 vtskr
//
LOCUS       WP_009801015             267 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Oceanicaulis sp.
            HTCC2633].
ACCESSION   WP_009801015
VERSION     WP_009801015.1
KEYWORDS    RefSeq.
SOURCE      Oceanicaulis sp. HTCC2633
  ORGANISM  Oceanicaulis sp. HTCC2633
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Maricaulaceae; Oceanicaulis.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Oceanicaulis sp. HTCC2633"
                     /db_xref="taxon:314254"
     Protein         1..267
                     /product="formate/nitrite transporter family protein"
                     /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=27854
     Region          25..267
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mskktdhelr akrlaarsei asktlysvia etgkeellrp sssllysalt aglamgasvl
       61 lmgaiekavg daswsslaia vgypagflli amarmqlfte ntltavlpvt knrrwrsvrl
      121 lgrlwaivlf gnlvgavaig avlshvtepd lfeamvsass hithrdalgn fisalpagfl
      181 iglmawslpg lpyeklgavf ivtylvgagg fphivagtve ttvlivagvw gageglafil
      241 pvlvgntlgg aalfaglayg qvheeid
//
LOCUS       WP_009803197             387 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Oceanicaulis sp. HTCC2633].
ACCESSION   WP_009803197
VERSION     WP_009803197.1
KEYWORDS    RefSeq.
SOURCE      Oceanicaulis sp. HTCC2633
  ORGANISM  Oceanicaulis sp. HTCC2633
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Maricaulaceae; Oceanicaulis.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Oceanicaulis sp. HTCC2633"
                     /db_xref="taxon:314254"
     Protein         1..387
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=41029
     Region          123..365
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mtdptalrpy rdavsaagal aveinfldhd ltlggevtal glgalgaagd vrhlrerlap
       61 adqprldllq ragpcdvrlr llgddhevry vrligqgdgl hwrglmlpag gsaggradmd
      121 letaladslk sgdvcayyqp vvdlktkrla gfealarwdr pgvgvlgade fmplaqahgy
      181 veavgesvrs mavqdlsawl aarngpldlf vtanatatev sapdfadrll qavqasglpr
      241 gafklevnet dvmvdpeaae rtlnavrdqg vpivlddfgt gysslarldr fafdvvkldq
      301 yfiraaltdg sarsiissvv riaesygmsv vaegveseaa qtlclelgcd ygqgyhfapa
      361 lspqdaarav tqgmatrfga aqmqerg
//
LOCUS       WP_009803708             727 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Pseudooceanicola batsensis].
ACCESSION   WP_009803708
VERSION     WP_009803708.1
KEYWORDS    RefSeq.
SOURCE      Pseudooceanicola batsensis
  ORGANISM  Pseudooceanicola batsensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudooceanicola.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 727)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Pseudooceanicola batsensis"
                     /db_xref="taxon:314255"
     Protein         1..727
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=75143
     Region          21..722
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mtllkplspe agvalsatgw ealvaprsia ligasgrass vsftsrlvat nealgfggsl
       61 yminpkrdei fglkawdnva elaeapdvta inlpgemvld aardaiaagt kalmihsggf
      121 gergadgear eaelkalcae agvaalgpnc lgimsltrka svssfkagkl gqgplalisq
      181 sgsvasilmq iaqpfgaslv astgneavtt aedlmhhaie dpdtriivgf vealrrpeql
      241 fglawkaraa gkpiillkag ltakggevsr ghtgalagsg evyrqalaqa givmaedfee
      301 laqmvelfat lkvyptggrl gmlstsggel gnvtdlceaa gvdlpplsea tlatlqerla
      361 lpedvlprnp vdvgtgfafa gtyeermsga idavasdpsv divtfvqgvh rdsedmslsl
      421 nheickaaak eagrqskpmv flptqvtppd etiaallrga gipilrgirp glaalralna
      481 ymataeapes adtlavstet lspwpdgtvp qarlfpalaa aglpvtrslr atdptlseaa
      541 vadlgravmk idtpravhks diggvalnvt qdiaaetyqr lcaaltppvg tepgegvfva
      601 eqldggtefy vgakrdatfg tvvvcgmggr mlelmertal lvcpfteada laaidrsgag
      661 rfldgfrgdp vsdrealarl ivtvgriasg fgarletldl npvivthdrp ggciadarli
      721 ltgdtdt
//
LOCUS       WP_009803757             645 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Pseudooceanicola batsensis].
ACCESSION   WP_009803757
VERSION     WP_009803757.1
KEYWORDS    RefSeq.
SOURCE      Pseudooceanicola batsensis
  ORGANISM  Pseudooceanicola batsensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudooceanicola.
REFERENCE   1  (residues 1 to 645)
  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 645)
  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 645)
  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 645)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..645
                     /organism="Pseudooceanicola batsensis"
                     /db_xref="taxon:314255"
     Protein         1..645
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=67821
     Region          10..637
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mdnsparhlf qviarvlafl vplvaviwvl aipqrmgfli ypeqvaalml gaalcvafsr
       61 daatssgpkl lidavlaila lsvgayvyvr fpvlsegshl ypteafilgl lvallvlegl
      121 rrvvgwtlvi itltmfcyal wghlvpgplr grgqefadvm rfigtdsagt wgsalqiaaf
      181 vvvifvlfgg vllavgggdf ftqiatrfag rgpgntakia vvasglfgsi sgsavsnvms
      241 tgvmtipmmr rsgfrpdqag aiesvastgg qlappvmgaa aflmaellqm pyksillaai
      301 lpaviyylsl yvqidfiarr ddhrsadwie hrpmrqviad gwlplaafvv llgsifawnt
      361 raevaaiwal glivvvalgf wvlrvvnvsw gpavspkela agitktggqv cdvllicaaa
      421 gmiigllatt glgfslslfl iqfggqnlfg llvvtaivgi vlglglpttg vylllatmta
      481 palvqlgips lsahmfvfyy gmlsmitppi alaayaaasi sgapqirtgv qafrfgwiay
      541 flpflfiykp gllmsgpwyd iayvfassva alalvsaali ghalgriplp arigaavlgi
      601 amiaplrqig paalefgvsa lgiaviaiyv lrmrsgpgtm talrd
//
LOCUS       WP_009803958             188 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Pseudooceanicola
            batsensis].
ACCESSION   WP_009803958
VERSION     WP_009803958.1
KEYWORDS    RefSeq.
SOURCE      Pseudooceanicola batsensis
  ORGANISM  Pseudooceanicola batsensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudooceanicola.
REFERENCE   1  (residues 1 to 188)
  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 188)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 188)
  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   4  (residues 1 to 188)
  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   5  (residues 1 to 188)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Pseudooceanicola batsensis"
                     /db_xref="taxon:314255"
     Protein         1..188
                     /product="TRAP transporter small permease subunit"
                     /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=19574
     Region          20..182
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mthpdiepng gdprrhslpa rlwggvvnal aalgtaliag lmliicadiv arngmgaslp
       61 lvselgalll vmivclqfaa tvradrlara glfidplrrt rpragaalev vfslvgaamv
      121 glmawatldv lstdwsrgef igtpglgtlp twpfrlfilv gltaaalefi araivsarat
      181 agigetir
//
LOCUS       WP_009804729             319 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Pseudooceanicola batsensis].
ACCESSION   WP_009804729
VERSION     WP_009804729.1
KEYWORDS    RefSeq.
SOURCE      Pseudooceanicola batsensis
  ORGANISM  Pseudooceanicola batsensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudooceanicola.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pseudooceanicola batsensis"
                     /db_xref="taxon:314255"
     Protein         1..319
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33621
     Region          236..309
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 maeiqvesgq edpslsmatl inltgglvsi allvgvgvwg yrtlmrdvsd vpvvraaadp
       61 mriapedpgg tlagnvglav nkvaaeglae kpadrlilap apvrlefede spkriaarre
      121 aeaeaaaaea raeaeradpi aaltarvlkd aaplsgetve pvttddtiar allkaeqaae
      181 atetkaallm dgtggpnltl rprmrpvvla ttapqapiaa paplqpavdv dpasipagtr
      241 lvqlgaydsv etarkewdrf nsrfrdymdd kqrviqkass ggrtfyrlrv mnfadlsatr
      301 hfcaalvaen adcipvvak
//
LOCUS       WP_009804793            1210 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Pseudooceanicola batsensis].
ACCESSION   WP_009804793
VERSION     WP_009804793.1
KEYWORDS    RefSeq.
SOURCE      Pseudooceanicola batsensis
  ORGANISM  Pseudooceanicola batsensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudooceanicola.
REFERENCE   1  (residues 1 to 1210)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 1210)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 1210)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1210
                     /organism="Pseudooceanicola batsensis"
                     /db_xref="taxon:314255"
     Protein         1..1210
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=125957
     Region          <15..183
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          <978..1151
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mllfllfpal lgliaigfdd tppdsgsedp dqpggsgddl ltepdrhgat pgddaiggts
       61 gadeidalsg ddtiaglrga drvdggagrd aldggsgddl lsgggeadrl fggvgddtmd
      121 ggsgddlfdd iagadsfsgg tghdvifaie peqgapdeie ggsgddrfwg ddgdtmtggd
      181 gadrfmvatg rpgaepvvir dldfsrpehg gqpdqviftd aegaiyprsa fydgtlnagi
      241 gdlpdgsgav vvfgsqevai ieghtaeelf hqtiwignlq vhepnliqpg darngtaedd
      301 hlvggsgddt lggnggedwl ngrdgddlid grdpagtagg dvllggagwd tiraddgdfv
      361 agfegrdsye lvygradaaa itifgyevls egglpepvtl idetgaplsa aetragltle
      421 aqaegdgtdl lfdgqriahl sgvapaelae msawltnlag pvpppapppe dgaeegddvd
      481 pgdtgivtpg ldksatlisa tatgavattg hfggnavftv nttdgqptgn ftsatdalgi
      541 ehlrfpagqg dpqagledge dwldvtlmvp ddsgqpdlrp elkrmldwag dndaqvtlvv
      601 ttrlmsvddy advvadrltp faekvmrdyg evveafeign eywatmnett ygqkadlaai
      661 glrngmlaag lseaqqadil vqmatptgas dfvgskdsrg yiarledana aiidelgtet
      721 raaidgvveh yyynktelay tdadseqnyi drdyavwdaa fsgdldlhit ewnvrttdyd
      781 evgirsasti qeqfenmled gvdrahvwpv qhntdsdlvg spretavlde agrvtnsvrg
      841 amfdlmsesl pglelmatef egddgsfein ayrsddrtvv yvssrslevl dldvdltglv
      901 gtgatgtgvq igidqsaqss dgfhwrhdtg htpsssveid grayyydehd vrasltdhaf
      961 dgpevalrlk pfevieitft aaadpgvgpd dpavsgevin gtgnvddlsg tpgddtiggf
     1021 grddtlhggd gddlinghgg ddslvggrgn ddmrgspgnd tlrgwggddt lrgfndddll
     1081 tgqhgddvlv gnrgndlllg negndslngg ighdtligge gadtvtgwaw gdvfgfdegd
     1141 iapgdtitdf tpgqdviqla lpgisglsdm tfqprpggle iglgrhgtlf legdltvaai
     1201 aqsgnfdfap
//
LOCUS       WP_009804848             168 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Pseudooceanicola batsensis].
ACCESSION   WP_009804848
VERSION     WP_009804848.1
KEYWORDS    RefSeq.
SOURCE      Pseudooceanicola batsensis
  ORGANISM  Pseudooceanicola batsensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudooceanicola.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Pseudooceanicola batsensis"
                     /db_xref="taxon:314255"
     Protein         1..168
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=18229
     Region          89..156
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mkpiltgfaa lmltaaplma qtqvtgddtq ettaeemhtd tnvgtyesda agsmdyagai
       61 rtrditggei ystagmggew sadtrfdrvd tqwtdvgeie divlnrdgrl tgvvaevggf
      121 ldiadkhvil niermrlvpv ddrsyaivtd mteeelesle avdegfwn
//
LOCUS       WP_009805368             190 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Pseudooceanicola
            batsensis].
ACCESSION   WP_009805368
VERSION     WP_009805368.1
KEYWORDS    RefSeq.
SOURCE      Pseudooceanicola batsensis
  ORGANISM  Pseudooceanicola batsensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudooceanicola.
REFERENCE   1  (residues 1 to 190)
  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 190)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 190)
  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   4  (residues 1 to 190)
  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   5  (residues 1 to 190)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Pseudooceanicola batsensis"
                     /db_xref="taxon:314255"
     Protein         1..190
                     /product="TRAP transporter small permease subunit"
                     /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=20953
     Region          1..168
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mlqiaggitr lnrfigkwls lavliifafl ladvvmrylv gqptiwtael atlifgvyai
       61 lgggfllaer ghvnvdiiyg sfsprrkall diltyplfll fvgvllwqgw diawesfvdk
      121 eqtnsiwkpy lwptkafipv aavllllqgf vrlwsdirvl qgkpvpedvf gvpapsdsha
      181 naaaageaqe
//
LOCUS       WP_009805608             651 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Pseudooceanicola batsensis].
ACCESSION   WP_009805608
VERSION     WP_009805608.1
KEYWORDS    RefSeq.
SOURCE      Pseudooceanicola batsensis
  ORGANISM  Pseudooceanicola batsensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudooceanicola.
REFERENCE   1  (residues 1 to 651)
  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 651)
  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 651)
  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 651)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Pseudooceanicola batsensis"
                     /db_xref="taxon:314255"
     Protein         1..651
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=68797
     Region          65..647
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mphtpdhpaq gaepqasrds aqqsevtrlg eafsvrsivf vvlcacglam glayafgipi
       61 agnrllegqy ywvfigifsa aafialpavk gqtalpiydi vaaaaalgis lwfsthawdi
      121 vqagwvnipa givlwllmle marrsggipf llvvlllgly piiadrfpgl lmgipydfdr
      181 mieahvfrte gmmgittkiv aeiilgflvf agvliatgag effidlanag fgkyrggpak
      241 vsivasgffg slsgsifsni agtgsitipt mkkvgypphy agaieacast ggvvmppvmg
      301 aiafvmaiti gvdyatvmva ailpsllfyf glmlqvdaya arkgltgmaa etlpsarkvl
      361 lrgwpflsvl vflvwgllym rweyyapwya cglmialsfl rkdtmmtprr lydtlrqigv
      421 lvtqtaaiil piafvvsalt itgvtgsvts glvalggdnv fliialgvla cfimgmagla
      481 ivayiflavt lapaiirigg lnevavhffi iyyamlsvit ppvgaaafla atiagakpmr
      541 tsftavrlgv viyfvplffl fqpalvfqgd ltpliyvlps iiagiillsg glegyllgig
      601 lvrpvlrlpl aaagfafsfp glmttligga vsaalvaliw ldsrrnsvpa e
//
LOCUS       WP_009805889             336 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudooceanicola batsensis].
ACCESSION   WP_009805889
VERSION     WP_009805889.1
KEYWORDS    RefSeq.
SOURCE      Pseudooceanicola batsensis
  ORGANISM  Pseudooceanicola batsensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudooceanicola.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 336)
  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   6  (residues 1 to 336)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Pseudooceanicola batsensis"
                     /db_xref="taxon:314255"
     Protein         1..336
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37230
     Region          22..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <149..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mpdqtmaagf aaaflayavv egaprdglla acalteddlt dqdrripvas yealiaagik
       61 atgdtslllr hvlesqletm sivgqivhas asfphslvql nryarlmadv pipggrdrfe
      121 lvregeavwl vdhrpsdgtw mateasfarf isefrrsape hpfeqalevt yappphanry
      181 pelfgvpvsf rttrnalrin pvwldetfdg gkdyvfgvft rhadslmedl atndtvrsav
      241 eahiladlhe gtlsmdriar dlgmsrqtly rrlkdegvsf aqvhddlrrr mamdylnark
      301 vsvgetayll gfseasafvr afrrwtgvsp tawlgn
//
LOCUS       WP_009806023             180 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Pseudooceanicola
            batsensis].
ACCESSION   WP_009806023
VERSION     WP_009806023.1
KEYWORDS    RefSeq.
SOURCE      Pseudooceanicola batsensis
  ORGANISM  Pseudooceanicola batsensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudooceanicola.
REFERENCE   1  (residues 1 to 180)
  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 180)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 180)
  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   4  (residues 1 to 180)
  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   5  (residues 1 to 180)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Pseudooceanicola batsensis"
                     /db_xref="taxon:314255"
     Protein         1..180
                     /product="TRAP transporter small permease subunit"
                     /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=20553
     Region          3..171
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mkamrryval vdgfnhrlgr limygifalm gvllwstfsk valspslwtl emaqflmvgy
       61 yilggpyaiq mgsnvrmdlf ygdfsprrka wfdvftvffl lvylgvllwg giestqyafq
      121 yggersssvw rpylwpikvi mcigivlmll qavselfkdv lflktgepwr edqkgpadal
//
LOCUS       WP_009807124             400 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Pseudooceanicola
            batsensis].
ACCESSION   WP_009807124
VERSION     WP_009807124.1
KEYWORDS    RefSeq.
SOURCE      Pseudooceanicola batsensis
  ORGANISM  Pseudooceanicola batsensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudooceanicola.
REFERENCE   1  (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   2  (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
REFERENCE   3  (residues 1 to 400)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Pseudooceanicola batsensis"
                     /db_xref="taxon:314255"
     Protein         1..400
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45637
     Region          1..397
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 marpvldnqa arrlflhkhl lgdppagpgr grdllevira lgfvqvdsvs tvarahhmil
       61 farrpayrpk slahllerer slfehwthda aiiptefypy wslpfrrtra rlsekwrtwq
      121 geaymdeier vkahvaragp vrssdllgee drgrsggwwn whpskaalef lwrtgslsis
      181 krqgfqkfyd lpervhpdas arpapdteea vewfcrgald rlgfatsgei aafwahvspa
      241 eardwtargl aegrleeidv icqdgrarks vawpgtaera atlppapnrv rvlspfdpal
      301 rdrnraerlf gflyrieifv paekrkygyy vfpilegerl igridmkadr aarllevskl
      361 wlepgvrpak grlakleael drmarfadcd gvriapdwlq
//
LOCUS       WP_009806839             462 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Pseudooceanicola batsensis].
ACCESSION   WP_009806839
VERSION     WP_009806839.1
KEYWORDS    RefSeq.
SOURCE      Pseudooceanicola batsensis
  ORGANISM  Pseudooceanicola batsensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudooceanicola.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Pseudooceanicola batsensis"
                     /db_xref="taxon:314255"
     Protein         1..462
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47099
     Region          112..365
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 matgrvirgl ggpagfgeaa larsddgsfa ldaravfpgg ltyfgrhhag dairvgtngi
       61 vsfgagvevy pavgsplpva dmiapfwadv dtridgegre sgqiwvdldp egghltvtwa
      121 dvgsyrrqad etnlfqlrlt drgagdfdir fayeridwts gtasddagam vllngvrlpe
      181 awiaagdaga lasqagntgi agtwqfemrd gilpgltpvs gatltgtdaa ntltggadgd
      241 ilrgyegtdv lrghggadwl fggdgadtln ggsgddvieg gtsaadlrdv vyggdgadri
      301 daghgndlvy ggagddvieg gfgvdeligq qgddtlsgaa wsdlifggdg adflnggfgy
      361 drlngggggd rffhlgifdh gsdwvqdysa aegdalvwgr gpataadfqi nwadtagaga
      421 agvaeafvih rgtgqiiwal vdgaaqeeit llvsgtgydl lg
//
LOCUS       WP_009807562             325 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Roseobacter sp.
            MED193].
ACCESSION   WP_009807562
VERSION     WP_009807562.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. MED193
  ORGANISM  Roseobacter sp. MED193
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 325)
  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 325)
  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 325)
  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 325)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Roseobacter sp. MED193"
                     /db_xref="taxon:314262"
     Protein         1..325
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=34706
     Region          20..323
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mkhalfaaaa tlltaaplwa eeikiavgcp pvnacsdyvy aedlaaglre qgleasvfag
       61 galgkdpevv dqlsqglvqf gmtnfvmike vdprilgfia pymfddmehf fratqdtqsd
      121 lleeikasme gqgvkiaglp glggtmgvfn vktpvakved madlrlraid atqielfknw
      181 gvqgavvdmp efagavqqgv vdgyynppvv alifrhtefl khytdigagt pfrsalmsad
      241 wygdlddadr akvdqavdqa naknrvwtak aaagelaglq ksgvtistms pealadlkar
      301 seeawaglmp adsveafral aaktr
//
LOCUS       WP_009807666             361 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Roseobacter sp.
            MED193].
ACCESSION   WP_009807666
VERSION     WP_009807666.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. MED193
  ORGANISM  Roseobacter sp. MED193
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 361)
  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 361)
  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 361)
  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 361)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Roseobacter sp. MED193"
                     /db_xref="taxon:314262"
     Protein         1..361
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=38917
     Region          1..354
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkrrdfikig aagaaassla apataqgirq wnmvtawpkn lpgpgvaaqm ladrittlsg
       61 grievklhaa gelvpgrgvf davsegtael yhavpaywgs kskgmllfgs qpfglradeq
      121 fgwlyhgggq alydeiygrf nlkpflcgns gpqwqgwfrd eihslddlkg lkfrttglas
      181 emcskigmav qamgprdmfq alqtgaldag efigpwtdsa vgfyqvakny ywpgvgepss
      241 aeecavnata yaelpddlkq avsfacesly npvwteyttk haqalkqmve negvqvkmlp
      301 ddvvaamaaa aaevmaelae dedelvrrit asftayrdsv gsymsyadng qmnarakalg
      361 y
//
LOCUS       WP_009808364             192 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Roseobacter sp. MED193].
ACCESSION   WP_009808364
VERSION     WP_009808364.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. MED193
  ORGANISM  Roseobacter sp. MED193
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Roseobacter sp. MED193"
                     /db_xref="taxon:314262"
     Protein         1..192
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21145
     Region          1..163
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlrrlydrtm sladhrhalw wlaavsfves sffpippdvl mipmilarps rawiiasval
       61 iasvaggmlg yaigamfyes lgqpileamg kgaaieefnn kfndfgfwav lgagitpfpy
      121 kvitimsgwt gmpvmtflat svlaralrff ivagllrafg apirdfieqr lglvftvfiv
      181 llfggflvlr yl
//
LOCUS       WP_009810455             151 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Roseobacter sp. MED193].
ACCESSION   WP_009810455
VERSION     WP_009810455.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. MED193
  ORGANISM  Roseobacter sp. MED193
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 151)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Roseobacter sp. MED193"
                     /db_xref="taxon:314262"
     Protein         1..151
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16003
     Region          2..150
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 maadyktlak tiaalteged davalmatla celhhsddrf dwtgfyrvva pellkigpyq
       61 gghgclqipf srgvcgaaar sgeaqlvadv dsfpghiaca sstrselvlp vwnsagqlia
      121 vldidsdlpn afteedqeql sailqqvfgr p
//
LOCUS       WP_009810493             404 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Roseobacter sp.
            MED193].
ACCESSION   WP_009810493
VERSION     WP_009810493.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. MED193
  ORGANISM  Roseobacter sp. MED193
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 404)
  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 404)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Roseobacter sp. MED193"
                     /db_xref="taxon:314262"
     Protein         1..404
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45998
     Region          1..398
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 malprlenaq arrlfmdrha llqppsggsk gadllqlisq lgfvqldsin tvarahdmil
       61 yarrpsyrak hltnlyhggg alfehwthda amiplayypq whlrfqrdee llrkrwrnwr
      121 rdgfeqqfet vlkhirdhgp vsssdlgkde kkssggwwdw hpsktaleyl wrtgaltvig
      181 rsgfqkrydl tervieehlh apanqldpaq tvdwlcnnal drlgfatpge laafwdtasn
      241 aearswcqea kargeieeie vaaadgslrk syarpgvieq aaelgpapgr mrvlspfdpm
      301 lrdrkraerl fgfhyrievf tpapkriygy yvfpliegqk mvgridmkad raadclrvta
      361 lwpergvkfs aartkrleae ldrvarfagl aavgfadgwl rqpv
//
LOCUS       WP_009810969             341 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Roseobacter sp. MED193].
ACCESSION   WP_009810969
VERSION     WP_009810969.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. MED193
  ORGANISM  Roseobacter sp. MED193
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 341)
  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 341)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Roseobacter sp. MED193"
                     /db_xref="taxon:314262"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38381
     Region          21..202
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          251..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtavsiiyar kqiehaewlp dkaalwelig ltpesaadps vmvpveayhd lmeviaesef
       61 pdlkfhmktc rsmrcdefgv fglafkaapt lrqgfqriwr yvrlhnraad fsagqegdry
      121 cwsmqapnvg rlgnylsrea amgttltlcr etttqdltar hvqfvhereg sidslvehfg
      181 cvpefgaqsd alhfdvehvd rpctigdtai wsfllshldq evekqcdpek nfetqvveei
      241 tkllsggvpq lsdvsksmgl ggrtlqrrls ergqsfqslt dearrqlaqq lirsstysfs
      301 eiafltgfse qsafsrafkr wsgqtpkayr galrervave t
//
LOCUS       WP_009811779             247 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Roseobacter sp. MED193].
ACCESSION   WP_009811779
VERSION     WP_009811779.1
KEYWORDS    RefSeq.
SOURCE      Roseobacter sp. MED193
  ORGANISM  Roseobacter sp. MED193
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Roseobacter sp. MED193"
                     /db_xref="taxon:314262"
     Protein         1..247
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=26539
     Region          23..173
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 msqgqagqqg tkggrpdtda pldaiwspsp nqsarrdglr psmvvlhyta mqgaeaalar
       61 lcdpaaevsa hyligrdgrl wqmvpesqra whagagewrg qgdinsrsig ieldntgghp
      121 fsepqmavle vllaqilrrw silpeavigh sdmapgrkcd pgprfdwarl aglglaravp
      181 avsgsslqes daeledlfcr yardlgytaa vdtatllaav rlryrpwaag plvaedlipl
      241 aqsdlwl
//
LOCUS       WP_009812202             291 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Roseovarius nubinhibens].
ACCESSION   WP_009812202
VERSION     WP_009812202.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius nubinhibens
  ORGANISM  Roseovarius nubinhibens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseovarius.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Roseovarius nubinhibens"
                     /db_xref="taxon:314263"
     Protein         1..291
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29355
     Region          219..290
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mltsvaalal agcqglgens pfkkrpdaaa esgaastssv rlverdveap evfqvtdegl
       61 wdgrpslggv wvahpdvkep erviirhagn gkfvigalfr reranpgprl qvssdaaaal
      121 gmlagspqkl nvtalrreaa peagaaadpa aaglaadtve ttaldpiaga aaaidkaeaa
      181 agdsaitpaa apapkpvaap apaaapkpas ggsklskpyl qigifsvedn anntatamrq
      241 agmvptvleq sskgktfwrv ivgpastese raallkkiqg igfddayavs n
//
LOCUS       WP_009812625             326 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [Roseovarius].
ACCESSION   WP_009812625
VERSION     WP_009812625.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius
  ORGANISM  Roseovarius
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 326)
  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 326)
  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 326)
  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 326)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Roseovarius"
                     /db_xref="taxon:74030"
     Protein         1..326
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=35055
     Region          2..326
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mkllntltai gltmmtvapl qaaeikiamn svddptvsge aafaqgfaaa legtdftvem
       61 ypsntlgkek erldqvaqgl levnlaaast vysmspllkg vilpfyfasd aemdatieag
      121 klmdefnkpl vesgirlvgl nyigtamgih nskmpistmd qmaelrfral npeqiklqea
      181 igssgtviaw aevanaiqtg vadgyfnpps sairnghtsf lkyytpadlw pssraivise
      241 dwyqtlsdee ktqidaavda glaanrdwva ewstsvtekq velgvtitpl aegerdkiia
      301 vakplwsetl taeqlalwdq akaaaq
//
LOCUS       WP_009813663             678 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Roseovarius nubinhibens].
ACCESSION   WP_009813663
VERSION     WP_009813663.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius nubinhibens
  ORGANISM  Roseovarius nubinhibens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseovarius.
REFERENCE   1  (residues 1 to 678)
  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 678)
  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 678)
  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 678)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..678
                     /organism="Roseovarius nubinhibens"
                     /db_xref="taxon:314263"
     Protein         1..678
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=71961
     Region          15..671
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mtadttpelt peqlaeierk ydpetafrpt gkmlglviat alvamsvyhf yasgfglvre
       61 llhrgihisf vlglvfllfg mrkgdatlpp rawyrfdgvp ildiifalla vaaamylpll
      121 spaalaqrvg npsttdifmg tallvltlea trrsvgptlp iiglifiafa yfgpwmpgal
      181 khggsswlai inhlymtnqg iygiaigvma qyvflfilfg vlatriglgq lfidlamvia
      241 grysggpakv aifssafmgt isgssiantv ttgaltipam krvgypahfs gaveatastg
      301 gqitppilga aafimveyle iplrdvlaaa lfpallhyfg ifimvhleak klglrglrae
      361 elpkmglvlk dhwlslipli ilvylilsgk tpdfaavygi iacvvvgfln pthrlslrdl
      421 wdglasgakn tlavgaaaat vgvvvgvvtl tgvgfrlgyv vvqtatdigt mlstlpilgy
      481 ftvtqwalft sliliaiaci imgagiptta tyiilvavaa palaqlqvep lvahffvfyy
      541 gvladitppv alaayaaagi agsnpfktgn tafrlgiaka lvpfvfvysp alllvadgft
      601 wwaftvtllg amlgiaslgv afsgyliagl ktwerwwval vsflfiapgl mtmglglalm
      661 lpilliqlrr rnattvea
//
LOCUS       WP_009813836             258 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Roseovarius nubinhibens].
ACCESSION   WP_009813836
VERSION     WP_009813836.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius nubinhibens
  ORGANISM  Roseovarius nubinhibens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseovarius.
REFERENCE   1  (residues 1 to 258)
  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 258)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Roseovarius nubinhibens"
                     /db_xref="taxon:314263"
     Protein         1..258
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27170
     Region          1..258
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mprfaanlsl lftecapldr fkaaraagfq gcellfpydh aaadlaqaae aaalpvvlin
       61 tpggnwagge rgvaaipgce arfrdefdqa lamagalgag llhvlaglae gaaaratyvd
      121 nlrwaaaraa asnpalrlti epinghdmpg yflqdfaeaq aslaeiaapn lglqfdayha
      181 qritgdaraa wdnldkmplh vqvagvpgrh epqsgdidfp afftqldtgg yagwvsgeyh
      241 pkrstteglg wlreasrs
//
LOCUS       WP_009814071             189 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Roseovarius nubinhibens].
ACCESSION   WP_009814071
VERSION     WP_009814071.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius nubinhibens
  ORGANISM  Roseovarius nubinhibens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseovarius.
REFERENCE   1  (residues 1 to 189)
  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 189)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 189)
  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   4  (residues 1 to 189)
  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   5  (residues 1 to 189)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Roseovarius nubinhibens"
                     /db_xref="taxon:314263"
     Protein         1..189
                     /product="TRAP transporter small permease subunit"
                     /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=20682
     Region          1..170
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mqmilklvdr isslldyaaq amvliliasm lyevaarylf gaptlwafdi aymstgtlfi
       61 lgcaqtlred ahvrvdllss rmparlrdmi dgvafllvla pimgwlskia geralrayvh
      121 gevehvspwa plmwpfytvl algmagltlq laaegwrafa gqrkppaphd appldlpkfd
      181 tatspksea
//
LOCUS       WP_009814248             210 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Roseovarius nubinhibens].
ACCESSION   WP_009814248
VERSION     WP_009814248.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius nubinhibens
  ORGANISM  Roseovarius nubinhibens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseovarius.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Roseovarius nubinhibens"
                     /db_xref="taxon:314263"
     Protein         1..210
                     /product="TRAP transporter small permease subunit"
                     /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=22801
     Region          14..185
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 magggtvlsd dstlsrvdrq fyriervlal vsglavfamm llavgsvsgr nffdqplpgy
       61 vdwieqampl iafmgisyvq rdgghirmdl vvgnlkgrvl wlvemittlv vlglmvllvw
      121 gtwahfqrsf dfgaplwsrd ssmdialplw pakllapvaf gvlclrlvlq vigygrafle
      181 naekpvavpl vvdaatqaae earhvsdgng
//
LOCUS       WP_009814629             177 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Roseovarius].
ACCESSION   WP_009814629
VERSION     WP_009814629.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius
  ORGANISM  Roseovarius
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Roseovarius"
                     /db_xref="taxon:74030"
     Protein         1..177
                     /product="TRAP transporter small permease subunit"
                     /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=18691
     Region          1..166
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mtqllillgr vnerlalaag lllllsvsvt lfdvvarplg lslggtdels gyamaiatsw
       61 gmsyaltnlt hvridlvrar gsapvrawfd avsilslaav avtigyrgwp vlaksikngs
      121 tanttletpl wipqslwmag wlwfalsgvv lavvvcvfla ggkhaeidef agtrgei
//
LOCUS       WP_009816560             262 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Roseovarius sp. 217].
ACCESSION   WP_009816560
VERSION     WP_009816560.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius sp. 217
  ORGANISM  Roseovarius sp. 217
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseovarius.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Roseovarius sp. 217"
                     /db_xref="taxon:314264"
     Protein         1..262
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25774
     Region          2..235
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 maadslaghg gndtlrgdag ddrlaggagd dlieggagqd niggglgadr lrgqggddtm
       61 gggdgddvls ggdgqdvmsg gpgndllegg agddrlagsf drdtvrggdg ddvigggpgr
      121 dlldggagnd qfgggegddt llggsgddfl agggrndlmd ggtgrdtlng gaghdtlrgg
      181 aeadvfvfnd lvagerdvva dfqigedqir lsgvagpglm grflaldlfd tvdgavvrya
      241 dheilledva tsslsvedfi fl
//
LOCUS       WP_009817592             151 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Roseovarius sp. 217].
ACCESSION   WP_009817592
VERSION     WP_009817592.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius sp. 217
  ORGANISM  Roseovarius sp. 217
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseovarius.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 151)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Roseovarius sp. 217"
                     /db_xref="taxon:314264"
     Protein         1..151
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16158
     Region          4..151
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mridydhiar tiaalteges devalmatvv cevhhaddrf dwtgfyrvta pemlkigpyq
       61 gghgclsipf srgvcgaaar mgtvhlvpdv eafpdhiaca sstrseivlp vrdgagrlia
      121 vfdidsdqqa afteedaarl geilaavfgr i
//
LOCUS       WP_009818007             677 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Roseovarius sp. 217].
ACCESSION   WP_009818007
VERSION     WP_009818007.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius sp. 217
  ORGANISM  Roseovarius sp. 217
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseovarius.
REFERENCE   1  (residues 1 to 677)
  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 677)
  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 677)
  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 677)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Roseovarius sp. 217"
                     /db_xref="taxon:314264"
     Protein         1..677
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=71765
     Region          7..670
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 madpeltaee lheierkydp elafrptgrs iailvsiclv amsayhfyas gfglvrellh
       61 rgihlsfvlg lvfllfswrr ststnlppat wyrlsgvpil dlvfaslava aamylpllpp
      121 aavsvrvgnp sdldvlmgsa lflltleatr rsvgptlpii alifvafaif gpyapgalkh
      181 ggasweglin hlymtnqgiy giaigvmaqy vflfilfgvl atriglgqlf idlamviagr
      241 yaggpakvai fssafmgtis gssiantvtt galtipamkr vgypahfaga veatastggq
      301 itppilgaaa fimveyleip lrdilaaalf pallhyfgif imvhlearkl glrglradel
      361 pkaglvlrqh wlsiiplgil vylilsgktp dfaavygiia cvvvgflnpv nrltlrdlwq
      421 aladgarntl avgaaaatvg vvvgvvtltg vgfrlgyvvv qtatdmgaml seiwllsyft
      481 lqqwalfvsl iliavsciim gagipttaty iilvavaapa laqlqvepiv ahffvfyygv
      541 laditppval aayaaagiag anpfrtgnta frlgiakalv pfvfvyspal llvtdgftws
      601 afsitlagam lgigglgaaf sgyllapmrg werwavglts llfiapglit maiglllwsp
      661 ilflqwrkar lggalpr
//
LOCUS       WP_009819631             721 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Roseovarius sp. 217].
ACCESSION   WP_009819631
VERSION     WP_009819631.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius sp. 217
  ORGANISM  Roseovarius sp. 217
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseovarius.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 721)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Roseovarius sp. 217"
                     /db_xref="taxon:314264"
     Protein         1..721
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=77142
     Region          24..719
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mqessnlynv navvsetaph vvhphlldpl lrptsvafig asnrpqtlgn imvstaavdg
       61 ypgalypvnp kesmisglpc fpdiasipgq vehvviglad qrieqalhea iekgvraati
      121 ftgcdmsdqg ddkllyrlsd mareaglhic gpnsmgllnp tiglrlngya spiplkpgni
      181 alilqsgsaf salaynhprl rfsfcvstgr elatrsedym lwaleqpetk viglfqetar
      241 dparfitale rarqrsipvv vlkvgktels ahfasshsga iagdaaayea vfrsygvvat
      301 stldefgacl qifskvdaar lpdgllagvh dsggeremvv dlaeregvfy adiskatkak
      361 lsanldsglk penpldvwgs gheferkven cmkaliddpa tgalalfqdi rdgsyvatgf
      421 lsalrrvsks snkpaiivsn yagvrhgtia leaveaglpv iegsqeglka irelfafrdr
      481 qkvsrgslpa tspeivsrwr trlsepndls eaealaliad ygiatprvve vdtlealrna
      541 vpevglplvl ktaapgikhk sdvagvflgl tdmasielay reiavrlgpq aileemlpsg
      601 ielafglvqd etfgpfvima aggiwieale drvvalppfd qaeargmide lrirrqlggg
      661 rgvppadlda iaqafsrfsq laadlgdlif emdvnplfar adgiravdal lsvcatrtpn
      721 i
//
LOCUS       WP_009819611             818 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Roseovarius sp. 217].
ACCESSION   WP_009819611
VERSION     WP_009819611.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius sp. 217
  ORGANISM  Roseovarius sp. 217
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseovarius.
REFERENCE   1  (residues 1 to 818)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 818)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 818)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..818
                     /organism="Roseovarius sp. 217"
                     /db_xref="taxon:314264"
     Protein         1..818
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=86093
     Region          550..787
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mlrvydqtde nsetvivedm fganltittd lslmqelgar fqglglhair fpggsvtewy
       61 fdisdiaggs hdrtissfed avvelipffk flnfaatlek svtlviptik gfsqtaseal
      121 lsgdfgnrlv tetylenvad fvamavltsq qqgvtidafe ignefmasgr mtaseygqla
      181 aavaavvert ldslaiarpa qadivvqtls aagtyspngt tilyvdeatg fiyelhemgg
      241 anvpevsdlt evvvpsqgta rqqniaiisa feqdrvtiqs angkqitfdt snavgaidgv
      301 tehyfldggf davdadeqfg fnqlelwrqs llmrdaslpe ldfyitewnv rrngdvdean
      361 nrglqqaatn vamfyemvth dvttayfwps ifdqsssvtl ihqnrehlti ageafaqltn
      421 tigmipfldf ldqgnvdihg fenetdafvi lsersgtenr mqlnltevld svrysvswie
      481 lwdggsggqd etadpviqtt eivdlvtpke lesflvtmqs wsilymkiev vstgepqrae
      541 apsgdaarri vtgseahdnl hgglgndtlr gldgddqldg gegndsiggg lgndtidggd
      601 gddiigggfg adsitgsign dvvaggagnd tleggdgnds msgsfgneli nagggtddvg
      661 ggtgrdtida gagndrvggg egddlisgga gsdflagggr ndtidggtgn dtlnggagnd
      721 vmtggagadq fvfsaffdge adviadfedg idrffirivn pdtgetnisn gnnglqgfva
      781 algivdtaag aqlnvngnti lvegtaaasl tvddfsfl
//
LOCUS       WP_009819670             181 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Roseovarius sp. 217].
ACCESSION   WP_009819670
VERSION     WP_009819670.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius sp. 217
  ORGANISM  Roseovarius sp. 217
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseovarius.
REFERENCE   1  (residues 1 to 181)
  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 181)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 181)
  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   4  (residues 1 to 181)
  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   5  (residues 1 to 181)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Roseovarius sp. 217"
                     /db_xref="taxon:314264"
     Protein         1..181
                     /product="TRAP transporter small permease subunit"
                     /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=19624
     Region          5..164
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 madsvlhlmr tlnrgvayli gimllacaaf vladivlrqf gtsfggtddi sgyvmaiata
       61 wgmgfallel shvridllrq kanplgrslf difsmivmta vvlviayhcw pvlersitns
      121 stantpletp liwvqgpwfa gwvwfgivst lttlsalali lqgrfaeseq aigafgeadm
      181 r
//
LOCUS       WP_009819979             243 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Roseovarius sp. 217].
ACCESSION   WP_009819979
VERSION     WP_009819979.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius sp. 217
  ORGANISM  Roseovarius sp. 217
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseovarius.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Roseovarius sp. 217"
                     /db_xref="taxon:314264"
     Protein         1..243
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26329
     Region          146..218
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mpsssdltaa pfylefappa gaeaqvetly vfrdagvlsr rgrglfatdl fdlsvsvlna
       61 cdtgphvsla pprpgfvprr asfcgivagl rlssrpqhmp paetfdslas ilrrvrvgdd
      121 ampelvtald glaedlsfaa ipqafsdrtg rrriraetgm srrrlaairr frrlvdelac
      181 qtlplsdlal dagfydqphm ssacrafagm spgalrgqaa rqplghflqd erlktrvkhi
      241 ing
//
LOCUS       WP_009825283             239 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Sulfitobacter sp. SK025].
ACCESSION   WP_009825283
VERSION     WP_009825283.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter sp. SK025
  ORGANISM  Sulfitobacter sp. SK025
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 239)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Sulfitobacter sp. SK025"
                     /db_xref="taxon:1389011"
     Protein         1..239
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=25842
     Region          <41..222
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mitgfsavpt chtsmntdma aplnaseiae detpfshfsn lthalhrakt lqrashfpii
       61 itcslsteqv ddaqlaakle weldrldvkt atlrlalpqh lcqhtpshpl istcrdlrtl
      121 gcgialngfg sgphcveiiq kcgvdlaiid psltndvdkh pnrrrilsav vamahdlgve
      181 tlacdirtag ehsllsqlgc dhvqgdgiap pmqiyeattw mhthsqkltr lpsvvggir
//
LOCUS       WP_009825823             401 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Sulfitobacter].
ACCESSION   WP_009825823
VERSION     WP_009825823.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter
  ORGANISM  Sulfitobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
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   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 401)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Sulfitobacter"
                     /db_xref="taxon:60136"
     Protein         1..401
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45423
     Region          1..398
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mtlplignrd arriflhrhl lsdapqgpas gddllqliqg lgfvqldsin tvarahdlil
       61 fsrrqryrpq alktlyerdg alfehwthda avipmgyyph welrrqrdaq mlrqryknwh
      121 qhdfegrfqs vldqiraqgp vsssdvgqde prsnggwwdw hpsktaleyl wragalcvvg
      181 rdgfqkrydl tervidaalc dpsqapdaaq sidwccngal drlgfatpge laafwahisp
      241 aeakawvqre qaagrvepvq iagadgtvhr sfarpglasd paidmaptar lrvlspfdpa
      301 lrdrkraerl fgfryriemf vpapkrvygy yvfpilqgds iiarvdmkah rdrdtlvvra
      361 lwpepgsrwg kgkqaafeae lariirlagv sqiafedgwl r
//
LOCUS       WP_009825829             456 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Sulfitobacter].
ACCESSION   WP_009825829
VERSION     WP_009825829.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter
  ORGANISM  Sulfitobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 456)
  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 456)
  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 456)
  AUTHORS   ter Beek,J., 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 456)
  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 456)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Sulfitobacter"
                     /db_xref="taxon:60136"
     Protein         1..456
                     /product="CmpA/NrtA family 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=49933
     Region          25..303
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mkntfallla stslmataas aemlalekee ltfgfikltd maplavayel gyfedeglfv
       61 rleaqanwkv lldgvidgql dgahmlagqp laatigygtk ahiitpfsmd lngnaitvsn
      121 diwdemkpnv ptmddgrpqh pisasalapv vegykdrgep fnmgmvfpvs thnyeirywl
      181 aagglkpgyy saqdisgqid advllsvtpp pqmpatmeag tisgyavgep wnqqavfkgi
      241 gvpvitdydm wknnpekvfg itaefaednp nttlaltkal iraamwldan dnanreeave
      301 mlsrseyvga dadviansmt gffefekgdv rpapdfnvff rynatypfys daiwyltqmr
      361 rwgqidetkp dewyfetaad vyrpdiylqa arllvdegma deaafpwdsd gfkaptpaad
      421 iidgisydgr apnayidslp iglksgqtvv dskveg
//
LOCUS       WP_009825911             185 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Sulfitobacter].
ACCESSION   WP_009825911
VERSION     WP_009825911.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter
  ORGANISM  Sulfitobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Sulfitobacter"
                     /db_xref="taxon:60136"
     Protein         1..185
                     /product="TRAP transporter small permease subunit"
                     /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=20370
     Region          1..168
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mfklarfitq lnrmigywis fcvliifall ladvvmryli gqpaiwtael atlifgvyai
       61 igggyllter ghvnvdiiyg qfspkrkalv divtwplfli fvgvllwqgy diaseaiadm
      121 ersnsvwkap lwptkslipv aalllllqgf vrlwadvrtl mglpndpaif gqpatgdtqa
      181 aggqs
//
LOCUS       WP_009826482             222 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Sulfitobacter].
ACCESSION   WP_009826482
VERSION     WP_009826482.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter
  ORGANISM  Sulfitobacter
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Sulfitobacter"
                     /db_xref="taxon:60136"
     Protein         1..222
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=23984
     Region          1..160
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 madapdryls pnhgprrngl rpslivlhyt amdsaeaaca rlcdpaaevs ahylitgkge
       61 tvplvpedqr awhagaggwq grddinsrsi gieldnrgnh pfsepqmatl etllrgimqr
      121 wsippegvig hsdmapgrki dpgprfdwpr larqnlagkg sryaendpgs dptpaafiaa
      181 ahaagytatd didlllhstr lryapwrkgp lcaadmtlgh dl
//
LOCUS       WP_009826988             262 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Sulfitobacter].
ACCESSION   WP_009826988
VERSION     WP_009826988.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter
  ORGANISM  Sulfitobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 262)
  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 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   3  (residues 1 to 262)
  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   4  (residues 1 to 262)
  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 262)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Sulfitobacter"
                     /db_xref="taxon:60136"
     Protein         1..262
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29139
     Region          26..262
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          181..259
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mtentiellt laqlsqgqdw rvqlchdrpv hmliwitrgq gllqldgqrr glgahnavfi
       61 paralfaldm grqgigqavv ipdgtelrlp qmprhlrird vqaqteltgl ieaaqreqqa
      121 krplyhdale ghaalmsvwl rrqimqdehv pnrrnaaarl sarfcqmvce ryssgapmaq
      181 yaeslevtpt hlsravksat gktaadilte rvvhearhll gttehsaqdi arhlgfgsaa
      241 yftrfmqqht gltpsrlrat aa
//
LOCUS       WP_009826199             664 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter permease [Sulfitobacter].
ACCESSION   WP_009826199
VERSION     WP_009826199.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter
  ORGANISM  Sulfitobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 664)
  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 664)
  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 664)
  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 664)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Sulfitobacter"
                     /db_xref="taxon:60136"
     Protein         1..664
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=69959
     Region          19..634
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mtdpdtsrtp qpkfeevaid gatpaerisg varwvvvitt llslvlvvnq lfnlqlfgiv
       61 lidgrylyil ggmflaltfl ifqarggkgg eptlldwvlf aasvgttgyl aqtaqqnlsq
      121 gweyaapeta qyvsvifffl ileatrragg lvlflivtlf afyptfaghv pdpfsgfqst
      181 flqtvpyhiy saessfgipm kafggvvigf ilfgavlqrt gggqffndla lglvggyrgg
      241 aakvsifasg fmgsmsgsvi snvlttgavs ipamrktgfs aktaaateac astggvlmpp
      301 imgatafvma sflsrpyvei alaaaipsil fywglfaqid aysakrglrg lpkpdlprlr
      361 qvmiegwpyi fvfalllymm iglrqessap fyatalllvv nqfrashrln lsrlgnmivg
      421 vgmglselta illgvglivg sfsatglagt lvnelvflag dstlilllmg aitafifgmg
      481 mtvtacyifl avvlapalea gglnqlavhl filywgmvsy itppvalgaf aastmagsnp
      541 iatgfeamrl ggviyiapff fvlnpaligq apawevvval scamigvtli saalqgyisl
      601 vgpiegrgal pmrvalffgg vliampqndl aglgyslsfl iggalcalpm lrawqatsaa
      661 rvtp
//
LOCUS       WP_009826933             414 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Sulfitobacter].
ACCESSION   WP_009826933
VERSION     WP_009826933.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter
  ORGANISM  Sulfitobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 414)
  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 414)
  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 414)
  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 12807598
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Sulfitobacter"
                     /db_xref="taxon:60136"
     Protein         1..414
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43955
     Region          25..89
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          28..366
                     /region_name="PRK10856"
                     /note="cytoskeleton protein RodZ"
                     /db_xref="CDD:236776"
     Region          305..372
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 migrwssksa dneqveakgf dafdlrlgdl mrgeratlgk slldvqrelr ikasyiaaie
       61 nadpeafdtp gfiagyvrsy arylnmdpdk afaafcaesg favahgmssk asvvkkptre
      121 ermtrngesd ifarpatpft pvgdsllari epgalgsllv lvaliggigy ggwsvlqevq
      181 rvqvspvdet pvvlsdldpl qgalasapet tedpdaptam avprsdaldr lyrpaaldvp
      241 vlvardapis sidprsigsf astspspsvg dalrtaentv vqrdtpevlp gavpqvvegp
      301 apqlrmvaay pswvrvraad gkvifegimn kgdswdipat eepptlrtge sgalyfamdg
      361 qyfgpvgdrg avtsnlplhr qalaelyepa vleensalat mvaelknaat spte
//
LOCUS       WP_009827553             823 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Planktotalea sp.].
ACCESSION   WP_009827553
VERSION     WP_009827553.1
KEYWORDS    RefSeq.
SOURCE      Planktotalea sp.
  ORGANISM  Planktotalea sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Planktotalea.
REFERENCE   1  (residues 1 to 823)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 823)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 823)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..823
                     /organism="Planktotalea sp."
                     /db_xref="taxon:2029877"
     Protein         1..823
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=90156
     Region          9..822
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mvmifrwtlr ltggaiiaal lmavlayfla arslpeytkt lkvegitasv eivrnnanvp
       61 hifgetdtdv ffglgyahaq drlwqmtmlr rtaqgrlsev fgkrtlsvdt llrrldiyrl
      121 asvsvasqda rtsdalsaya agvnmritei nnrslgrgap emflfgapis pwrpadslav
      181 tklmalqlsg hlqdevlrar tslvlpdear lsdilpdmpg tgvaalpkya tlfdqplpqy
      241 aeastqrnpl hpvpprglgg asnawaaaps rsasggtila ndphlgftap aiwylarlel
      301 aaggviggti pgmpvvlagr satigwgits sylddqdlfi eqlnpenpee yrtpngfkpf
      361 etrksiinik daepvtltlr wsdngpvlsg sdfslstitp qghvaalawt alsprdtsls
      421 aamgimqsad vhsalistea yiapsqnltl vdkdkialkl igampqrnan hqskgrmpsp
      481 gwiadnrwqg lfpaptnprf ldpeggilgn tnnklvqrsf pahvsyewgd sqriqrwqrl
      541 mqnrqvhtrd sfieaqldtv svtartllpl igadlwftge papngtperk rqialellan
      601 wtgemnehlp epliysawlh alqgrliqde lgplskefkh veplfiervf rningaaewc
      661 dilqsspket ctdvarisld eailwleeny tidlvslrwg dahqathdha vlgevpvlry
      721 fvnirqstsg gdntlmrgrt kggegteafl nvhgagyrgv ydftdpdssl fvistgqsgh
      781 lfsrhyddlg tlwrrgeyip msldeglara aavgittlip egn
//
LOCUS       WP_009827761             259 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Planktotalea sp.].
ACCESSION   WP_009827761
VERSION     WP_009827761.1
KEYWORDS    RefSeq.
SOURCE      Planktotalea sp.
  ORGANISM  Planktotalea sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Planktotalea.
REFERENCE   1  (residues 1 to 259)
  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 259)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Planktotalea sp."
                     /db_xref="taxon:2029877"
     Protein         1..259
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27889
     Region          1..250
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mkfsanlgfl wtdrslpdai raakeagfda vechwpydtp atetlaalhe tglqmlglnt
       61 rrgdvaggen glaalpdrtt daraaideai ayannlecka vhvmagfvsg gdahatfvgn
      121 lnyacaqaaa ngitiliepl nkydapgyfl sttnqaleii kevgapnlkl mfdcyhvqlm
      181 egdlshklsd llpkighiqf asvpdrgppe sgevnfehif dviaslgysa plgaeykpqa
      241 ptdetldwlr lrqsrllph
//
LOCUS       WP_009828290             361 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Planktotalea sp.].
ACCESSION   WP_009828290
VERSION     WP_009828290.1
KEYWORDS    RefSeq.
SOURCE      Planktotalea sp.
  ORGANISM  Planktotalea sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Planktotalea.
REFERENCE   1  (residues 1 to 361)
  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 361)
  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 361)
  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 361)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Planktotalea sp."
                     /db_xref="taxon:2029877"
     Protein         1..361
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=38287
     Region          1..351
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mdrrsflkts alggsaaaaa tlaapayaqg krvltmvqsw prgfavldda atylqdmvga
       61 msdgqltidk kapgelvgal evfdavssgq admyhsadyy figqhpayay ftavpfggta
      121 qeltnwyhhg gghelhnelg eifnlksfla gnsgsqsggw frkeigsaad fnglkfrmpg
      181 lggkvlgklg asvqnipgge lyqalssgal dglewvgpma deragfqeva kvyyaagfhe
      241 pgsglacgmn ldvyndlspa hqaiisnsca atthlqlsqt lasngaalar lqsqgvkvlq
      301 fsddvwdafg kasaevmden mgdeifaktr ksfeesmaas sswidksdgy yvkqrnrvlg
      361 n
//
LOCUS       WP_009830263             696 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Planktotalea sp.].
ACCESSION   WP_009830263
VERSION     WP_009830263.1
KEYWORDS    RefSeq.
SOURCE      Planktotalea sp.
  ORGANISM  Planktotalea sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Planktotalea.
REFERENCE   1  (residues 1 to 696)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 696)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Planktotalea sp."
                     /db_xref="taxon:2029877"
     Protein         1..696
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73048
     Region          1..691
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mtpersanfq rllkprniaf vggrdaliav rearrrgfdg qmwavnpkra dldgvpcvps
       61 iadlpqvpda vylaipadgi vaalselaai gvggvvcfsa gfketgdaaa eqalieaagd
      121 maligpncyg linyidnval wsfehggwsp gygaaiitqs gmfssditms arslplaymv
      181 sagnqavlgl edfldvfadd asvraiglhi eglqdiqafe raalkaierg iavvalktgs
      241 saigaaltvs htgslsgsde lyealfarsg visvtspaqf ietlkylcvv kapkapsvtg
      301 ftcsgggatm ladhaekigl sfpkvsaegh arlqdllpdi atvsnpldyt tpiwgqaeht
      361 ypvfaktmet vgaeaavlvq dypaegldas kvyyqndaga faraakehgi pasicatlpe
      421 nldkatrrhl islgvapmqg ihealnamrd aaiwsnrrqr iladwpagll pseaaetlsm
      481 ltedagkawl sargvrvpng rtvaavdadd aatkigypva lkmmsldlah kteagavalg
      541 indkealgia ltrmtrsvaq hdvnalsdsf lieamsplpl aelivtlrsd pqfgpalvlg
      601 sggiltelvg davtlllpat padiaealgs lrvarllngf rgrvvadlee iatalhqlcd
      661 ayleerakva eieinpmfvy adhivavdal vhmvas
//
LOCUS       WP_009832272             704 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Marinomonas sp. MED121].
ACCESSION   WP_009832272
VERSION     WP_009832272.1
KEYWORDS    RefSeq.
SOURCE      Marinomonas sp. MED121
  ORGANISM  Marinomonas sp. MED121
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinomonas.
REFERENCE   1  (residues 1 to 704)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 704)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..704
                     /organism="Marinomonas sp. MED121"
                     /db_xref="taxon:314277"
     Protein         1..704
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76496
     Region          1..703
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mtlsnthyld rllkpetial vgvspregtv gndmlkvlls ggykgqvflv nprydeiegh
       61 kcfaslsdip vaidmavlsv ashrmeplfd eaislniggv tifdycklee easptllerl
      121 sykakqanmp icggncmgyy nfdndayisf qspgerkagh isliahsgsi fvlptsndrr
      181 frfnlvvsag qeiatsldey mdfaleqest rvlaifmeai rnpenfvkvl ekakrkgipv
      241 vvtkvgrtev saqlaathsg aiagnntaye alfkkygvia tdslddlmtc aqilsqggdl
      301 gagdlgyigd sgglrelfvd taeehdltfa nltddtmnkl kqrlplglea vnpldaagpf
      361 tpdyaevfrd svryimedpn vavgvfefea rdefiympef ieiakevkqy snkpfivlnt
      421 fslalnagia edlmdhdipl vngvenavka ianlfanrdq qadshtpaen isnparkekw
      481 harlatglpm setdslnlla dygigianpq eahtqedtlk avetmtfpvv lktaephihh
      541 ksdvggvkln lnsstevsea yddlanrlgy rvtiepmvgq gtelafgmvn dpqfgpmvmv
      601 gsggiyievl kdrvfslapf deieamamid slrtrpllag vrgakaadln qlakqlanfs
      661 hlaadlgddi seidvnpiiv ndkgsiavda lviakevdae qsaa
//
LOCUS       WP_009832978             237 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Marinomonas sp. MED121].
ACCESSION   WP_009832978
VERSION     WP_009832978.1
KEYWORDS    RefSeq.
SOURCE      Marinomonas sp. MED121
  ORGANISM  Marinomonas sp. MED121
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinomonas.
REFERENCE   1  (residues 1 to 237)
  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 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   3  (residues 1 to 237)
  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   4  (residues 1 to 237)
  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 237)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Marinomonas sp. MED121"
                     /db_xref="taxon:314277"
     Protein         1..237
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26769
     Region          3..220
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          143..220
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mshitdvwsa hshsngsili lpdgcrdlii kthqvnnrth pslwfvsplf ehtqavqtqa
       61 nthtlgfrlk pgvkieqekl vkymplfkld neaishdeka isqdqkaisq ledmlnevts
      121 ikpcveealt slasdlfnvt qaakqlgmst rslqrmlire tdkspsywlq lararkaakh
      181 lgqtktmadt avlygysdqs hmcrefqhwf klsptqllnn pmlmaqldst gygfdlf
//
LOCUS       WP_009833735             417 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Marinomonas sp. MED121].
ACCESSION   WP_009833735
VERSION     WP_009833735.1
KEYWORDS    RefSeq.
SOURCE      Marinomonas sp. MED121
  ORGANISM  Marinomonas sp. MED121
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinomonas.
REFERENCE   1  (residues 1 to 417)
  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 417)
  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
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 417)
  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   5  (residues 1 to 417)
  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   6  (residues 1 to 417)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 417)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 417)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Marinomonas sp. MED121"
                     /db_xref="taxon:314277"
     Protein         1..417
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45021
     Region          19..69
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          78..385
                     /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 mkhsgstseq srlyneriil qavreqpgis raqiaelagl saqtisvits yliekelvci
       61 tgkvkgkrgq psikleinaq gayglginid rdhisaalvd fngaclllrq chvhfptete
      121 akqialglie evrdnlgddw nkvqgvgltm pdymaewles lvlkadeald lmhlrnamty
      181 wasddfklwl arhtektvic endanasain elllsggeis aqdffyifvg aacgggivsk
      241 gecvqgaagk agnfglipta kgelgawile alstvslkrf faqqevtyps ndnawqvknv
      301 qalvtnwcek vaaditpali siialqdpkr illggrlpss vlkvlinvlt lsvresapkv
      361 ldlppidvav tgatssivga ailplyqtfs pyhslllvtd epfkrqaiqg vngleks
//
LOCUS       WP_009834260             240 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Marinomonas sp. MED121].
ACCESSION   WP_009834260
VERSION     WP_009834260.1
KEYWORDS    RefSeq.
SOURCE      Marinomonas sp. MED121
  ORGANISM  Marinomonas sp. MED121
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinomonas.
REFERENCE   1  (residues 1 to 240)
  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 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   3  (residues 1 to 240)
  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   4  (residues 1 to 240)
  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 240)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Marinomonas sp. MED121"
                     /db_xref="taxon:314277"
     Protein         1..240
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27361
     Region          5..236
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <134..235
                     /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 mlgkitirty nphsrahshd fhqiliptqg fidlkldgie skassghcvv ikagcfhefk
       61 aheefrfivi dvsemppelm qletsrvsln eaaihyiqfi ekqlqnplep dfekslikll
      121 fdlliqqdfr ekidervqac lnflaqdiar phsieelani aclsptqfkh vfsknmkmpp
      181 lqylaklrie kaktllqntd lpisqiaqev gfanqssftr sftqslgqtp klyrqntsla
//
LOCUS       WP_009834642             835 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Marinomonas sp. MED121].
ACCESSION   WP_009834642
VERSION     WP_009834642.1
KEYWORDS    RefSeq.
SOURCE      Marinomonas sp. MED121
  ORGANISM  Marinomonas sp. MED121
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinomonas.
REFERENCE   1  (residues 1 to 835)
  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 835)
  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 835)
  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   4  (residues 1 to 835)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Marinomonas sp. MED121"
                     /db_xref="taxon:314277"
     Protein         1..835
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=92357
     Region          84..789
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mskivsplpl sslsakvpde hlsfsslkel dalsgilgqe raieaiqfgv amrrpgynvy
       61 amgesgtgrs syvsnylkse akrqpapkew tyvnnfsdnr sakalsfepg eakvfeqair
      121 hfidglmatf paafehpnyq qqksaidrdf nelyeaaitk veraalrmgv amfrdansvs
      181 fapmrdgkal edaefaslsd eerdafqdgv selekllnde llslpqwkrt tyenirqlnl
      241 atveesvetl iqplfesyqe neavtaflka mredldktli dqmvddkate nrdevsrrqv
      301 yeelylpniv vthtldggtp vvyeahptyr nlfgqveyss eqgllitsyr lirsgslhaa
      361 nggylildad klmadhylwe alkralktkt lkieqpyadm glmntttlvp eevplqvkvi
      421 ligsreiyyl lqdldpdfqd mfrvlvdfdd slkrnadtey afarllkdri akegyadvsr
      481 dgvaslieys srlaehqkem vakigdvfel lgeadfvrem ardeittseh ikralkakmh
      541 rtgrvsekii eeilegtvll dsegtaigki naltvmqigd ssfgaparis ttvypggkgi
      601 vdieresnlg qnihskgvli lsgylgskya qkypldisas iameqsygyv dgdsastael
      661 ccllsamvql plrqdlaitg slnqygevqa iggvnekieg ffnvchargl tgtqgviipk
      721 snvnnlmlnd evrdavtqgk fsvyaidtad ealhiltgve pgvadaegvy pegsinamvi
      781 dklealsklg dddeeeesed sdknssdkks sdnkssdnks sdnkssdnks sdkds
//
LOCUS       WP_009835283             121 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Marinomonas sp. MED121].
ACCESSION   WP_009835283
VERSION     WP_009835283.1
KEYWORDS    RefSeq.
SOURCE      Marinomonas sp. MED121
  ORGANISM  Marinomonas sp. MED121
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinomonas.
REFERENCE   1  (residues 1 to 121)
  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   2  (residues 1 to 121)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Marinomonas sp. MED121"
                     /db_xref="taxon:314277"
     Protein         1..121
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13014
     Region          40..104
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mysailnnpr nlnktlpsll kvffvlvlvs llclsnvsma akpldvnlat aeqlaavmvg
       61 vgqkkaqaii eyretngafn aldelifvkg igpsllkknr vylsigpgee fkgeklteip
      121 l
//
LOCUS       WP_009836148             179 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Marinomonas sp. MED121].
ACCESSION   WP_009836148
VERSION     WP_009836148.1
KEYWORDS    RefSeq.
SOURCE      Marinomonas sp. MED121
  ORGANISM  Marinomonas sp. MED121
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinomonas.
REFERENCE   1  (residues 1 to 179)
  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 179)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 179)
  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   4  (residues 1 to 179)
  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   5  (residues 1 to 179)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Marinomonas sp. MED121"
                     /db_xref="taxon:314277"
     Protein         1..179
                     /product="TRAP transporter small permease subunit"
                     /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=19941
     Region          2..166
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mfllnlervi srysillgkl sallfillll nvfydvlmry vfndvsigmq elewhlyaai
       61 fllgipygla tgghvrvdlf yerlsikgka widlfgcilf lipfavlvay ygvgfateaf
      121 klgetsgdpg glpyrwiika vipfaffsia isgigmllrc inairglska gfdhepiqh
//
LOCUS       WP_009836673             110 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Pseudoalteromonas tunicata].
ACCESSION   WP_009836673
VERSION     WP_009836673.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas tunicata
  ORGANISM  Pseudoalteromonas tunicata
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Pseudoalteromonas tunicata"
                     /db_xref="taxon:314281"
     Protein         1..110
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12494
     Region          15..109
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(32,63..64,66,92)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(32..33,41,44,46..47,49,52..53,55,63,68,74)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mvlqknardi efkkqqiwtv vsaipygcva sygqiatmag lpnyarfvgs clknlpkdtl
       61 lpwhriinsq gkisfpldsa rffrqkelle kehvlvsngr vslkkyqwnv
//
LOCUS       WP_009836850             715 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Pseudoalteromonas tunicata].
ACCESSION   WP_009836850
VERSION     WP_009836850.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas tunicata
  ORGANISM  Pseudoalteromonas tunicata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 715)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Pseudoalteromonas tunicata"
                     /db_xref="taxon:314281"
     Protein         1..715
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=80593
     Region          12..663
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mlavhtsghv nwsiiskven ylydlrllmt meqsiddkii iidideksla negqwpwprd
       61 klaqlinrlf ddyqirsigf davfaeaqan nslntlsylf kkglfdetqy qnlrleldhd
      121 qrfsealiar davlgivfkh siydqqtnge lpaplaslei lnevkndlyy gtgyaanlai
      181 lqqasgfggf fdyirddetl rkvpliqyyn nqiypslafe larislnqpa iefqlsgnqq
      241 stlrslefik lgdykipvdq tgsvyvpfrg kqgsftyisa tdvlnqalpi dalsgkiall
      301 gtsasglldl ratpvgksyi gvevhanivs aileqrfkha pgyrlgielf slfilamlms
      361 fifpflqsig aavfiislts vycalnlyfw hwqnmiftla tplffifisg flhlnynffv
      421 eqkkkrrlsk vfsqyiphel vtdfdsnqae mslagenrim svlftdvrnf tnmsekmtpt
      481 eltvlmnefl tpithcihqq qgtidkymgd avmafwgapi ndeqhashai saalniiiqm
      541 dkltrafkak nwpeikvgig iasgemsvgn mgsefriayt vmgdtvnlgs rlegitkmyg
      601 vdiivsentk ilasefiyrt vdkvkvkgkd lpvtifeplg lfeqlnettl anlaayeaal
      661 qlywqsefaa aleqfetlns tspcllftiy ierctlyrit ppalpwdgsf thtsk
//
LOCUS       WP_009837392             726 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Pseudoalteromonas tunicata].
ACCESSION   WP_009837392
VERSION     WP_009837392.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas tunicata
  ORGANISM  Pseudoalteromonas tunicata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 726)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 726)
  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   3  (residues 1 to 726)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..726
                     /organism="Pseudoalteromonas tunicata"
                     /db_xref="taxon:314281"
     Protein         1..726
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=77554
     Region          6..725
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msfevdedil qdflveagei lellseqlve lennpentdl lnaifrgfht vkggagflsm
       61 telvdachga enifdvlrqg krsvtpelmd vilqaldtin emfakiqnre qpdpaspell
      121 etlhklskpa sdndfvvaps apvieepvas epaqdefddi ffgadpvdep evasdssggi
      181 dditedefes lldelhgsgk gpavvekqsa snndditdde feslldelhg sgsfgavsad
      241 apkatpapvs hskassqsde eitedefesl ldelhgagaa pkavastpaa npkvetkpqp
      301 aakpapvpas kapepvakap vaaakapapk paapqaettv rvdtkrldqi mnmvgelvlv
      361 rnrlvslgat vssesmskai snldvvtadl qgavmktrmq pikkvfgrfp rvvrdlarsl
      421 rkdinlllvg eetdldknlv ealadplvhl vrnsvdhgie mpdvreasgk srtgtvtlsa
      481 sqegdhillk ivddgagmdp eklksiavgk gvidadvaar lsdteaynli fapgfstkee
      541 isdisgrgvg mdvvktkitq lngsikiesq kgvgttleik vpltlailpt lmvmvgqqtf
      601 alplagvsei fhldltktnl vdgqltiivr kkaiplfyle rwlirnyvhd erkrsqghvv
      661 ivqlgtqqvg fvvdsligqe evvikpldal lqgtpgmaga titsdggial ildvpsmlkh
      721 yagktk
//
LOCUS       WP_009837551             369 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Pseudoalteromonas
            tunicata].
ACCESSION   WP_009837551
VERSION     WP_009837551.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas tunicata
  ORGANISM  Pseudoalteromonas tunicata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 369)
  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 369)
  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 369)
  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 369)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Pseudoalteromonas tunicata"
                     /db_xref="taxon:314281"
     Protein         1..369
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40606
     Region          35..366
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mknklipwca iffgfilsgc gdktpaeqnq vtthsavyee papikwklvt swpknypglg
       61 taperfaknv elmsngrlki kvygagemvp gfevfdtvsa gtaqmghsaa yywkgkipaa
      121 qfftaipfgm naqevngwlh hggglklwqd lyapfnlipa aggntgvqla gwfkkeinsv
      181 ddlqglkmri pglggevlkk lggipvsltg gdlftalqtg aidatewvgp yndlafglnk
      241 aaefyyysgw hepganlefl inkdafnalp kdlqaivtaa mrvantdmld eytarnneal
      301 eqlknkyhvd irplppevma alkqataqvm qeqiaadpkm neiwqsydaf lqqvisyhti
      361 sekayylnr
//
LOCUS       WP_009837781             211 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Pseudoalteromonas tunicata].
ACCESSION   WP_009837781
VERSION     WP_009837781.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas tunicata
  ORGANISM  Pseudoalteromonas tunicata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 211)
  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 211)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 211)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Pseudoalteromonas tunicata"
                     /db_xref="taxon:314281"
     Protein         1..211
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22653
     Region          1..204
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 meiysteeqq aeaikrffre ngtalvigvv lglgglygwk aynqnqvesa eaasdayekl
       61 vkadaqnktn alagadefik nnkdssyavl aafvaakeav ekadfnlake kltwitqnnk
      121 npelnaians riarielelk nydaalkvls vtmpeafkas vaelkgdvyr aqgdlgqars
      181 ayqaaadagg ltnnatlqmk lddlavdtpa l
//
LOCUS       WP_009838736             101 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Pseudoalteromonas tunicata].
ACCESSION   WP_009838736
VERSION     WP_009838736.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas tunicata
  ORGANISM  Pseudoalteromonas tunicata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 101)
  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   2  (residues 1 to 101)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Pseudoalteromonas tunicata"
                     /db_xref="taxon:314281"
     Protein         1..101
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10780
     Region          40..100
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkfitlisfv lsllltlpam tfanepaqpe nmpvkmvsdl inintadlkt lqslpglgkt
       61 kaaaiiayre qfgefaslad lknvkgigdk viakldgkis f
//
LOCUS       WP_009838761             738 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Pseudoalteromonas
            tunicata].
ACCESSION   WP_009838761
VERSION     WP_009838761.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas tunicata
  ORGANISM  Pseudoalteromonas tunicata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Pseudoalteromonas tunicata"
                     /db_xref="taxon:314281"
     Protein         1..738
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=82580
     Region          26..738
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mkktvlavai aavvtplhan eqskkqptnl ehiqiishhd rlrtesgsat lltevelekf
       61 eyddihrils svpgvniree dgyglrpnig frgvtpersk kitiledgvl igpapysapa
      121 ayyfpvttrm tavevfkgpa aikfgpqtva gtlnmvtrqv pdlqeggidi atgqdgyqkm
      181 hgyygnafdd vsflvegvhl aadgfkdldg ggntgfdknd llakvryqfn gagfeqnvql
      241 klsyadetsh etylgltdsd fsdnpyrrya atqpalmete hqqimlshni hnsafslttr
      301 lyrndyerdw lklnalgntn aslsailaep qtyqaeyavi tgernsvvsg etshnlvmgt
      361 nareyysqgl qldgtwqfnl fdfdhklsfg aryhqdeidr shfeeifvmq dgvaeqivgs
      421 kydtshnier tdalavyied aitldkltlt agvrgefmdm hyhnkanlnd wqdkkariwl
      481 pgisgfyqfs dsagmlfgvh qgfvpsspqq gndieleksv nyefggrfnd gitqfemvsf
      541 fndysnlkes csqsncgddt lldtefngga vhvyglesqf aqryplnmql evpysvvyty
      601 tksefqqeif sdfvqwghvk kgdelpylpt hqatfnigln sdnwrvnvaf kyvssmkeaa
      661 grswqsdagq qvdvplagik tdsasvidvs asydigqfgr iyakidnitd evniisrrpy
      721 garpskarqf sigykyqf
//
LOCUS       WP_009839470             641 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Pseudoalteromonas tunicata].
ACCESSION   WP_009839470
VERSION     WP_009839470.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas tunicata
  ORGANISM  Pseudoalteromonas tunicata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 641)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 641)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 641)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Pseudoalteromonas tunicata"
                     /db_xref="taxon:314281"
     Protein         1..641
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=72698
     Region          <215..639
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 magltrflli qifffittls iasytfisql qslasqqqlv aqksidyyik synptddtpl
       61 grkvaitfnl nslivrdneg kiqesiqgdf dylplfakli qnsspfirpq fvvntesnlk
      121 leftikleee assihtqfii lliiifilsf lpllsvksii kraqenignn mslmvdnfie
      181 kndkniqlds siaatsvssi fpsivrlnay lrkkqqeieq salsikqkaf kdsvtalgnr
      241 nlfveyyedh vesaenqfgs limvrcselq linqtrgyyh gdeyikevaq lllkstgtya
      301 gatcyrlnss dfavllpnip lkeaerfgqd lqskfteyqr saelssvgns givsyssakp
      361 lgellsqvdt alslaqskqt nawhvlkdsd lmdnvsanfg nqnwrevidd vlnnsrvqll
      421 iqtimptnrs akvyseilar fktaedqilp tasflamaek leqiyhvdkm iveaaltsik
      481 tmnlggqffg initarsahd eqfmiwlerr llkdsnistk lifeisefgl qqnikaskrf
      541 idmihrvgar itverfgvgl tsfkffrdlk pdfikmdasy trgleedknn qyfmrlivdl
      601 ahrigvtvla egvesqeeky iieqlcldga qgyyierpre i
//
LOCUS       WP_009840619             699 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Pseudoalteromonas tunicata].
ACCESSION   WP_009840619
VERSION     WP_009840619.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas tunicata
  ORGANISM  Pseudoalteromonas tunicata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 699)
  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   3  (residues 1 to 699)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Pseudoalteromonas tunicata"
                     /db_xref="taxon:314281"
     Protein         1..699
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76358
     Region          20..690
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msidlsqffe vffeesfegl dtmesellnl qpgdldseti ntifraahsi kggsgtfgfs
       61 svadfthvle tlldqirdgr rtlepehvnl llqsvdclrl llsglqaeqd pdltqsvalr
      121 keferildns sgavvakpaa vqviadspvs idtlqisfkp fhhlfktgne plfmiselse
      181 lgsldvtani edlpnihdmq pddcylswtf fletteseqr vkevfewved daelaitvcg
      241 glfelddepa ilpvlevkse ggsfdkttke ppsslpkves easssknsap akaaestsir
      301 vsidkvdsli nmvgelvitq amltqlgege itdnkimalq eglaqlahnt rdlqesvmri
      361 rmlpisfvfs rfprlvrdts qklgkqvelk llgeqteldk tvmekisdpm vhlvrnsldh
      421 gletpdvrik agknpvgkvt lnsfhqggni vieimddgng lntqkirska lqsglinetd
      481 eltddqinel ifmpgfstad evsdisgrgv gmdvvrrnil slngsievts eqgvgstfti
      541 rlpltlaild gqlvtigqht yiiplisive slqvdtskvn svgggldvlr lrdeyvpilr
      601 lyqifnhtga ieeldkgllv vvesdnqkvg llvddllaqq qvvikslean yqkvegvsga
      661 tilgdgrvsl ivditglikl aglkkagrqe laidalgvn
//
LOCUS       WP_009840744             144 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Pseudoalteromonas tunicata].
ACCESSION   WP_009840744
VERSION     WP_009840744.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas tunicata
  ORGANISM  Pseudoalteromonas tunicata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Pseudoalteromonas tunicata"
                     /db_xref="taxon:314281"
     Protein         1..144
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15955
     Region          1..143
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 maylslffta fvaatilpsa sevlltgllt qgynlwllfl aatvgnvlgs cvnwwlgref
       61 lrfkdkkwfp isedtlekaq drfnrygtys lllawvpiig dpltivagtm kvrfdlflll
      121 vtigkafrya aviatvlgig qlin
//
LOCUS       WP_009840868             785 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Vibrio sp. AND4].
ACCESSION   WP_009840868
VERSION     WP_009840868.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. AND4
  ORGANISM  Vibrio sp. AND4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 785)
  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 785)
  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 785)
  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   4  (residues 1 to 785)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..785
                     /organism="Vibrio sp. AND4"
                     /db_xref="taxon:314289"
     Protein         1..785
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=87831
     Region          79..785
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mavqrleakq lysvaelenm pckstkelpp ideivgqera qkavefamsi kekgyniyai
       61 gqnglgkrtm ilrylnrhqh dvelfdwcyv anfedtrtpk vlklpcgign klrvdieklm
      121 gkllnalpla fdnemyysra drlknqlank qqseldiisk eakdkgislt itaqgdyqfv
      181 amngeelhte esfdelskke qeyfgsside levslrnmvr eltewedsfs ekikklnddv
      241 tldvithfik qlkvdyaeys eiktyltdlq kdivenaeif leqsgeqgei atasldkklp
      301 rrykvnvlvn rkdcefpivv eenpnyhslf gsietatfkg tvftdfslir agslhkangg
      361 vllmdaqkvl eqpyvwdglk ralrsrqlsf tslekevtlt gavsldpepi pldikiilfg
      421 dyrtyqllqh ydpefgelfr vtadfedemk rtpdselqya rfissvvndn nmlhcdkkai
      481 ariieyssrl sgdqtklslh sanianllre snyvarqans nmirvghvee alsnqemrvs
      541 rlqdsvmetf tngttlihtd gsavgqvnal svlstsdhmf gapnritatt cygdgevidi
      601 ersvdlggsi hskgvmilsa ylssvfgkta rvpltttitf eqsyggvdgd sasmaefcav
      661 vsafskqpnr qdiaitgsmn qfgesqpigg vnekiegfyd vceikgrhag qgviiprsnv
      721 hnlmlrpdiv kavekgdfqi waidhvteav elftgkaage atdegtypid tifglaqakl
      781 nalrk
//
LOCUS       WP_009840908             193 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Vibrio sp. AND4].
ACCESSION   WP_009840908
VERSION     WP_009840908.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. AND4
  ORGANISM  Vibrio sp. AND4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Vibrio sp. AND4"
                     /db_xref="taxon:314289"
     Protein         1..193
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19549
     Region          <4..172
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mirndthlgn rgsdeiadfd ggndvfvgfg gndvfvgggg ddlmvggsgd drltggagdd
       61 ilmagtgndy lgggtgndll lgllgdnkln ggvgedvlva gsgdnilvvg sgadkfiftd
      121 kfkghgeakv vdftigedsl hiisdavtsf sdltfsydak gnavftdgvd ltvkligvtq
      181 adintygsel fii
//
LOCUS       WP_009842542             737 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Vibrio sp. AND4].
ACCESSION   WP_009842542
VERSION     WP_009842542.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. AND4
  ORGANISM  Vibrio sp. AND4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 737)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 737)
  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   3  (residues 1 to 737)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Vibrio sp. AND4"
                     /db_xref="taxon:314289"
     Protein         1..737
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=78698
     Region          6..736
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msydldedil qdflieagei lellseqlve lennpedkdl lnaifrgfht vkggagflsl
       61 aelvdtchga envfdvlrng qrsvtpslmd tmlkaldtvn hqfqavqdre saeaadpall
      121 eelhrlcrpe sedqvvaeve apivtpepai pepiieqpaa pvepdsdpss vgsvdqited
      181 efeklldelh gkgsspckqa svsesapant psvesgditd deferlldel hgvgksptvs
      241 dvdpvappka pepeasslpa ssggdlmtda efekllddlh gsgkgpslee ldlatkpase
      301 nvapapapap epaaavpspa papkpqakpv akkeeakapa vkkpqaeatv rvdtstldti
      361 mnmvgelvlv rnrllslgln sndeemskav snldvvtadl qgavmktrmq pikkvfgrfp
      421 rvvrdlarnl nkdivlemrg eetdldknlv ealadplihl vrnsvdhgie mpddrvkagk
      481 prtgnvvlsa sqegdhiela ivddgggmdp nklrgiavkr gmmdedaaar lsdkecfnli
      541 fapgfsskek isdisgrgvg mdvvktaina lngsididse ltkgtkitik vpltlailpt
      601 lmvgvgghpf alplasvnei fhldlgrtnv vdgqltiivr eksiplfylq nwlastpssv
      661 rertghghvv ivqigsqrvg fvvdtligqe evvikpldnl lqgtpgmaga titsdghial
      721 ildvpdllkq yaaasri
//
LOCUS       WP_009844076             138 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Vibrio sp. AND4].
ACCESSION   WP_009844076
VERSION     WP_009844076.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. AND4
  ORGANISM  Vibrio sp. AND4
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Vibrio sp. AND4"
                     /db_xref="taxon:314289"
     Protein         1..138
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14079
     Region          4..129
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mqtnkqqgft lielmivvai igvlagvaip ayknyvkkse aaagmvtvra lltnidvyiq
       61 engsfpatdk ladlgasagm ntlgtialaq dgsaseagsv afnfgtgaal nstnitytrs
      121 asgwscnhtt gltikscn
//
LOCUS       WP_009843139             204 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Vibrio sp. AND4].
ACCESSION   WP_009843139
VERSION     WP_009843139.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. AND4
  ORGANISM  Vibrio sp. AND4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 204)
  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 204)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 204)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Vibrio sp. AND4"
                     /db_xref="taxon:314289"
     Protein         1..204
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22128
     Region          1..202
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 melydteeqq veaikdwwke ngkaviigav vglgglfgwr yyqdsvtqas eaasqsyttv
       61 mstlqtkgad aqadiqafid snevkeysvl aalqlakvqv eakdlsaale qlkwaqsntk
      121 davlaplisy riarieaemn nfdaanaela lvtdaawtgr iaelrgdial rqndkaaaya
      181 ayteaqqatd asptlqmkld dlak
//
LOCUS       WP_009844436             495 aa            linear   BCT 20-JAN-2025
DEFINITION  AAA family ATPase, partial [Vibrio sp. AND4].
ACCESSION   WP_009844436
VERSION     WP_009844436.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. AND4
  ORGANISM  Vibrio sp. AND4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Liu,Y., Sung,S., Kim,Y., Li,F., Gwon,G., Jo,A., Kim,A.K., Kim,T.,
            Song,O.K., Lee,S.E. and Cho,Y.
  TITLE     ATP-dependent DNA binding, unwinding, and resection by the
            Mre11/Rad50 complex
  JOURNAL   EMBO J 35 (7), 743-758 (2016)
   PUBMED   26717941
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Chen,Z., Luong,T.T. and Lee,C.Y.
  TITLE     The sbcDC locus mediates repression of type 5 capsule production as
            part of the SOS response in Staphylococcus aureus
  JOURNAL   J Bacteriol 189 (20), 7343-7350 (2007)
   PUBMED   17704228
REFERENCE   3  (residues 1 to 495)
  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   4  (residues 1 to 495)
  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
REFERENCE   5  (residues 1 to 495)
  AUTHORS   Hopfner,K.P., Karcher,A., Craig,L., Woo,T.T., Carney,J.P. and
            Tainer,J.A.
  TITLE     Structural biochemistry and interaction architecture of the DNA
            double-strand break repair Mre11 nuclease and Rad50-ATPase
  JOURNAL   Cell 105 (4), 473-485 (2001)
   PUBMED   11371344
REFERENCE   6  (residues 1 to 495)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Vibrio sp. AND4"
                     /db_xref="taxon:314289"
     Protein         1..>495
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          1..>481
                     /region_name="sbcc"
                     /note="exonuclease SbcC; TIGR00618"
                     /db_xref="CDD:129705"
     Region          1..>164
                     /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            35..42
                     /site_type="other"
                     /note="Walker A/P-loop"
                     /db_xref="CDD:213179"
     Site            154..157
                     /site_type="other"
                     /note="Q-loop/lid"
                     /db_xref="CDD:213179"
ORIGIN      
        1 mkpikltmqa fgpfaqietv efdklgtnpl flingptgsg ktsildaicf alygettgne
       61 rqgiqmrcdt aaptlltevt lefslhgkvy rvirspeqea pkargegttv rkhtaalyei
      121 tdeeklitsk ttqvrvevtn iiglnetqfr qvmvlpqgkf relllatske redifgqlfq
      181 tdiykkieya lkdkasaisk akgefdnqir galqvagvss eteltdqrea lstqfetaqk
      241 qehdslaqln tikvdlqkaq tlsnefkkhe qaelalkqhm aqsevvssrq iqldnakkas
      301 kielpyvtlq navkqthele qkvatlskdl akadeavkak egalytakeq aaqlpklteq
      361 qfqlesmkgk lvekseleka inkgithkse fettlkkyis lkekltleaq qgqktldqar
      421 vdiasigsve aeikqqqrlm qdlqkltgln qelakldalt qskqasveqa kakfvelqrf
      481 adslelswhg aqaav
//
LOCUS       WP_009844437             379 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Vibrio sp. AND4].
ACCESSION   WP_009844437
VERSION     WP_009844437.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. AND4
  ORGANISM  Vibrio sp. AND4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Vibrio sp. AND4"
                     /db_xref="taxon:314289"
     Protein         1..379
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42780
     Region          1..270
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          267..353
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkfihtsdwh lgrqfhnvsl lddqqavleq liqyiknnpv davivagdvy drsvpptvai
       61 ellnktvkri cgelntpmil isgnhdgaer lgfgseqmkn aglhiisnfe dmltpvviet
      121 esagqvafyg mpyndpeqvr fayqepisth dqahkllaek iteqcqpeqr kvlvshcfvd
      181 gamesdserp lsiggsdrvs hehfldfdyv alghlhqpqk kgeeyirysg slmkysfgeq
      241 nqkkgftlvt idqngfvsae hvdltaphem riiegeleqv ieqgktdpkn edyllvrlmd
      301 rhailnpmek lravypnvlh lekpgmligv eqemakakla rseidmfrdf ftqaqdgqls
      361 qqqdqaisdi iqqlspqaq
//
LOCUS       WP_009846168             248 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Vibrio].
ACCESSION   WP_009846168
VERSION     WP_009846168.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  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   3  (residues 1 to 248)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..248
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27684
     Region          43..227
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mnaplkkple hnqalqdprn rtvstlnstd alamiehgse ltlnvstpvg tkflattkfi
       61 gthsdncivv evpdvsnddl sfffqegfwm tarayslrge galihfksqi hhrigdpfpi
      121 lvlstpssmq vtqlrketry evnlasriif ndqranceir dlsksgcrfv tsptsraiqi
      181 adrvsievtp enyngplipp lkgiicnlqk sthyarygve fddigrsnak hllaklkfdg
      241 tklclrnr
//
LOCUS       WP_009846943             344 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio sp. MED222].
ACCESSION   WP_009846943
VERSION     WP_009846943.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. MED222
  ORGANISM  Vibrio sp. MED222
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 344)
  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 344)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 344)
  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   4  (residues 1 to 344)
  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 344)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Vibrio sp. MED222"
                     /db_xref="taxon:314290"
     Protein         1..344
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38611
     Region          32..215
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          259..340
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 meiiaeykpt ghrhqlgtld ialllntieq rgidierlln dvglpnmdwr dpngkltyad
       61 klalfsaanq sfphdglglw lgehaslshf gvlgyalsts qnvgeaiksg fkylrlngpi
      121 fsvkllldse haviqientl evgellpfcs eyflssivsl fkeltgheld ihtlalpyak
      181 pnytklyder fqcpvifeqn hcelrfdasv lsqtllthda atlkrylasc qsivetldse
      241 hlltnqikti fyqtagsfln ieqladefgc ssrtlrrelv thkssyqlll tevrvelake
      301 lllgttmsid digerlgysd panfrrafkg wlnktpaqfr dgls
//
LOCUS       WP_009847138             364 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein [Vibrio].
ACCESSION   WP_009847138
VERSION     WP_009847138.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 364)
  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 364)
  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 364)
  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 364)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..364
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40648
     Region          10..360
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mslisnsltr vfknvavtaa aclalvatga taadkvyrlk laetwgpnfp vfgdatknma
       61 amaekmsngr lqiridsank hkaplgvfdm vksgqydmgh sgsyywkgkv pntlyftsmp
      121 fgmtpaeqya wfyhgggmel meqvysphnl msfpggntdi qmggwfqkei nsvedlqglk
      181 mripgfagei laelgakptn iapgelytsl errtidalew vgpsldlrmg fhkiapyyyt
      241 gwhepgselq flvnkrtwnk lpedlqeilr vamrtaaydm ytqathesgk nwvsmkteyp
      301 dvqvkdfppe vmsalkeand rllakhaekd alakeiqasq asyleqvrsw tdishrayln
      361 sqak
//
LOCUS       WP_009847280              99 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Vibrio].
ACCESSION   WP_009847280
VERSION     WP_009847280.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 99)
  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   2  (residues 1 to 99)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..99
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10651
     Region          38..98
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mrtiystlfl tflillspaa yadsptkael ydgieitvni ntataeelsa llvgvgdkka
       61 qeivdyrdqn gafttaddlv svkgigeatv nknreriql
//
LOCUS       WP_009849854             136 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Mariprofundus ferrooxydans].
ACCESSION   WP_009849854
VERSION     WP_009849854.1
KEYWORDS    RefSeq.
SOURCE      Mariprofundus ferrooxydans
  ORGANISM  Mariprofundus ferrooxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Candidatius
            Mariprofundia; Mariprofundales; Mariprofundaceae; Mariprofundus.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Mariprofundus ferrooxydans"
                     /db_xref="taxon:314344"
     Protein         1..136
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14588
     Region          3..135
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdwplffsal isstlfpggs ealllyrlne ggnavtlvli atvgnvlgsl ityamgrlgn
       61 aamhkkwlri seaqseraer wfaaygkpal lfawlpvvgd plclvagllr cgivpflilv
      121 tigklaryav lalpfi
//
LOCUS       WP_009851245             392 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Mariprofundus ferrooxydans].
ACCESSION   WP_009851245
VERSION     WP_009851245.1
KEYWORDS    RefSeq.
SOURCE      Mariprofundus ferrooxydans
  ORGANISM  Mariprofundus ferrooxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Candidatius
            Mariprofundia; Mariprofundales; Mariprofundaceae; Mariprofundus.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Mariprofundus ferrooxydans"
                     /db_xref="taxon:314344"
     Protein         1..392
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=44312
     Region          65..>389
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mtmekitpdh sqaqsanlia enietlkslf pelitegpeg lsvnvdvlka lvgdqtvtdc
       61 dekyglnwfg krrarqlalt pstgtlrpap eesenwdttq nlfiegdnle vlkllqksya
      121 gkvkliyidp pyntgkdfvy kddfrdnikn ykkltgqvde agsplttnte asgrfhtdwl
      181 nmmyprlkla rnllredgli fisiddaevs nlksilneiy geenfeghih wrrrhnqpnd
      241 knkmlalvae hilcyaknke aykaagvgkv evtgnfsnpd ndprgewask pwkvgsgqsg
      301 srykittptg kvydeewmgd egtfqkllkd nriifpnggn gaprkkyfrm ereaegqcat
      361 nwwphdrfgh nqaatslvet lfgekkvfea vn
//
LOCUS       WP_009856337             104 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Rubrivivax benzoatilyticus].
ACCESSION   WP_009856337
VERSION     WP_009856337.1
KEYWORDS    RefSeq.
SOURCE      Rubrivivax benzoatilyticus
  ORGANISM  Rubrivivax benzoatilyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Rubrivivax.
REFERENCE   1  (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   2  (residues 1 to 104)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Rubrivivax benzoatilyticus"
                     /db_xref="taxon:316997"
     Protein         1..104
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10456
     Region          24..77
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkrflrpaaa llfaafafna haavdanqas qaeletvkgi gpglsakile armagafksw
       61 admvdrvpgi gagnaarfsq agltvagagw sggdakdtkp akak
//
LOCUS       WP_009857209             235 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Rubrivivax benzoatilyticus].
ACCESSION   WP_009857209
VERSION     WP_009857209.1
KEYWORDS    RefSeq.
SOURCE      Rubrivivax benzoatilyticus
  ORGANISM  Rubrivivax benzoatilyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Rubrivivax.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 235)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Rubrivivax benzoatilyticus"
                     /db_xref="taxon:316997"
     Protein         1..235
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=25063
     Region          6..222
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 matppfsyaf qpiidaverr vvsyealvrg pggepaaevl grvpeaqlaa fdrlsrahal
       61 alaaqlglpc llnlnllphg lladgdaida tlraardagl pperlvfeit esdaiadraa
      121 faalvnrhks dglllaiddf gagqsglnll adfqpdmikv drhlihgvda hgprqailrg
      181 llltcellgi dvvaegvesa adyrwlrarg vrlfqgylfa rpgfetlpqp tlpeg
//
LOCUS       WP_009857418             292 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Rubrivivax
            benzoatilyticus].
ACCESSION   WP_009857418
VERSION     WP_009857418.1
KEYWORDS    RefSeq.
SOURCE      Rubrivivax benzoatilyticus
  ORGANISM  Rubrivivax benzoatilyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Rubrivivax.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Rubrivivax benzoatilyticus"
                     /db_xref="taxon:316997"
     Protein         1..292
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31756
     Region          14..262
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mqvdalpvap cgtgespfww peqgalywcd ipgrrvhrwr ardgahdswd qpedvgciap
       61 rldgglmlar rdglfrldlt tgatqrlapp pydrtsqrfn dgkadpqgrf wvgticeprl
      121 ppraalyrwa dgaldpqldt astsnglaws pdgatmywcd tqahrieafd fdasdgslsr
      181 rrvfhqfppk padgslagyg grpdgaavdv eggywvamye garllrlapd grvladlalp
      241 vrcptmpcfg gadlrtlyvt sampkgdagp ldgrvlalrv dvpglpvnfv ha
//
LOCUS       WP_009857445             430 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA, partial [Rubrivivax benzoatilyticus].
ACCESSION   WP_009857445
VERSION     WP_009857445.1
KEYWORDS    RefSeq.
SOURCE      Rubrivivax benzoatilyticus
  ORGANISM  Rubrivivax benzoatilyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Rubrivivax.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 430)
  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   3  (residues 1 to 430)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Rubrivivax benzoatilyticus"
                     /db_xref="taxon:316997"
     Protein         <1..430
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <12..430
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 rpapaagldg tpaaepgetv aaaagrraag plaaagedag qkvlkvsqdk idrlmdlige
       61 mvvaknalpy laqraeevfq qrelareikt qysvinriae dmqhavlqvr mlpvgtifqr
      121 fgrlvrdisk klgkdvqlvv egedteadkn viesladpli hilrnsldhg lelpaarlaa
      181 gkpaqgtlrv aarqegdrvl ldisddgagi dtarvrakav erglipadra dslseheaaq
      241 lvflpgfsta dtisdlsgrg vgmdvvrsav eringsvtlt sergrgttir lalplsmavt
      301 nvmmievggr rfgvpmdliv etvrvpaddi hhfkraktav lrgrivplrp lhellaldea
      361 prlnaedeha vlvvrlggep iglvvddfhg tsdiilkple gvlagitgfa gtalmgdgsv
      421 lmilnpkeli
//
LOCUS       WP_009857449             628 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Rubrivivax].
ACCESSION   WP_009857449
VERSION     WP_009857449.1
KEYWORDS    RefSeq.
SOURCE      Rubrivivax
  ORGANISM  Rubrivivax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae.
REFERENCE   1  (residues 1 to 628)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 628)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 628)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 628)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 628)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 628)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..628
                     /organism="Rubrivivax"
                     /db_xref="taxon:28067"
     Protein         1..628
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=67868
     Region          24..628
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mtphpptprt paalaaltlg algvvygdig tsplyalkev fhaghvpmsr enilgvlsli
       61 fwtmtiivsl kyvllilrad nrgeggliam lalattavae kprlrrglla lgmfgtaify
      121 gdgvitpavs vlsaveglev aapqlehwvv pitlivltgl ftvqrfgtgg igrafgpvtl
      181 vwfatlialg apqiaehpgv liamlptyal hfivdqplia fialgsvvlv vtggealyad
      241 lghfgklpir iawyglvapa lvinyfgqga llledptave npffllapgw arlplvllat
      301 aatviasqal itaafsvtkq aiqlgllprl rvvhtsvrdt gqiyvpfvnw glyacivlav
      361 glfgssskla aaygitvtld mtittimtff virhgwkypl wlalgatgff faiditffas
      421 nvlkllaggw fplvigiamf tlmrtwvdgr rlvaerlrde aidlksflea vfvspptrvp
      481 gtaiflsgea gltpnalmhn lkhnkvlhdf nvfvtvqhhe vpwigfdkrl eveplghrcw
      541 qvrlhfgfmn dpdvpealkl lqgrgvplde metsyflsrd aiipslgsgm amwreklfas
      601 mhrnaaaagd flnlpanriv elgakvei
//
LOCUS       WP_009858000             311 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Rubrivivax
            benzoatilyticus].
ACCESSION   WP_009858000
VERSION     WP_009858000.1
KEYWORDS    RefSeq.
SOURCE      Rubrivivax benzoatilyticus
  ORGANISM  Rubrivivax benzoatilyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Rubrivivax.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Rubrivivax benzoatilyticus"
                     /db_xref="taxon:316997"
     Protein         1..311
                     /product="formate/nitrite transporter family protein"
                     /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=32613
     Region          30..300
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mldrtnpryl lnedeplpay gaaaprslfd plapdavaca aeemgvkkak agaaqqfgla
       61 vlggafvalg amfatiaiag aehmlpwgvm rllmgaafsm glmlvvvaga qlftsdalmv
      121 mawasgrldt rrmlrvwtiv wfgnlvgalg tativflggq ygfghgevga salylaaska
      181 slppfkafsl ailcnvlvcl atwlslaars vtdkivamfl pitafvaagf ehcvanmyfv
      241 pyglmvkwfa paafwaepaa qakaateipv aqylvnlgvv tlgnwvggal lvagaywwlf
      301 rrgaraaaka a
//
LOCUS       WP_009858025             707 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Rubrivivax benzoatilyticus].
ACCESSION   WP_009858025
VERSION     WP_009858025.1
KEYWORDS    RefSeq.
SOURCE      Rubrivivax benzoatilyticus
  ORGANISM  Rubrivivax benzoatilyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Rubrivivax.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 707)
  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   3  (residues 1 to 707)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Rubrivivax benzoatilyticus"
                     /db_xref="taxon:316997"
     Protein         1..707
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=75789
     Region          1..699
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mddalktffs earelladme tallgadvap gaavdvnaif raahtikgsa glfgldgvvr
       61 fthvlesvld evrsgtvaiq gpltplllrc cdhvgawvda leagvelddg hlaaedtlla
      121 rlraylgaea aapepaadet aqptegqwhl sirfgadvlr ngmdplafvr ylstigrier
      181 ivtlpdavpa leeldpescc lgfeialvts adratiesvf efviddcelr lvpprsrvae
      241 yveliralpe qperigeilv rcgsiterel edalgrqres dppprlgall teqgqvapev
      301 veaaldrqrq vretrtaess tirvdankld rlitlvgelv iaaagaqqas rrvrdlelqe
      361 ahatlsalvq dvrdsalnlr mvrigatfsr fkrvvhdvaa elgkdielrv ggedteldkt
      421 vveklgdplm hlvrnaidhg idspeqraar gkpargvvgl nayhdsgaiv ievsddgggl
      481 nrerilakar ergivdadhv padheidqli feagfstaeq vtnlsgrgvg mdvvkqnita
      541 lrgsvelasr pgegttvtvr lpltlaiing fqvavgrsmf vvpmemvdec vayscadghd
      601 ytdlrnsvlp lvrlrelfgl ggeppvrqni vvvqcagarc glvvdallge sqtvikplsr
      661 mfqqvrgisg ssllgsggva lildvpalla vaghgryspp ercaiva
//
LOCUS       WP_009858520             465 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Rubrivivax benzoatilyticus].
ACCESSION   WP_009858520
VERSION     WP_009858520.1
KEYWORDS    RefSeq.
SOURCE      Rubrivivax benzoatilyticus
  ORGANISM  Rubrivivax benzoatilyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Rubrivivax.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Rubrivivax benzoatilyticus"
                     /db_xref="taxon:316997"
     Protein         1..465
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=50191
     Region          20..424
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mrpddvdvse prsafvpphs deaeqsvlaa vlvepacfds vagllrpesf ysgrhaaiws
       61 amtalraega gldavslvea lrargtlvfa gdreyiaals vavpsashar rhaeivaaka
      121 aqreliaaag ealdiareps sdlgekldri garlaavqrt qmrrapirla eavqrvldqc
      181 damqrgegee vgwatgigpl ddalagglrp gelygiaarp gigkssvart iayriaragt
      241 ptlvlsmemp irqvagalia qfgrvdsmri rsarlesedw nrmldfaevs qdaplwidde
      301 pgltlaaiag karhvkglkv lvvdylqlaa stlkgattnd qvaelskglk riamelgiav
      361 vvlsqlnrqv eqrgdkepvm adlrdsgaie qdldvavllw evvktadaqn rpigwkvdkn
      421 rhgpkprwlt yfdgaryefq haaetieqvr arcalpaagt rrryd
//
LOCUS       WP_009858790             225 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Rubrivivax].
ACCESSION   WP_009858790
VERSION     WP_009858790.1
KEYWORDS    RefSeq.
SOURCE      Rubrivivax
  ORGANISM  Rubrivivax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae.
REFERENCE   1  (residues 1 to 225)
  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 225)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 225)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Rubrivivax"
                     /db_xref="taxon:28067"
     Protein         1..225
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23792
     Region          5..209
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 matqldlqeq eqldalkafw krygnlvtwl liaalaayag wngwnywqrd qalkasamyd
       61 eldraaaagd adktarifgd lkdrypgtay aeqgglaaak vqfekgqvda akasltwvaa
      121 naaedeyrtv arlrlaavla aakqfdqala eldaakaagf ealvadrrgd vlaaagreae
      181 araayeaayk amddsvdykr lieakltalg aapapaapaa sgaas
//
LOCUS       WP_009859983             399 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Parabacteroides].
ACCESSION   WP_009859983
VERSION     WP_009859983.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..399
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43445
     Region          1..398
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkilvlncgs ssvkyklfnm dthevlaqgg veklglpgsf lkftqpdgkk vilekempeh
       61 naaiefilsv ltddkygcik sfneidavgh rvvhggeafs ssveitpevi gkmvecidla
      121 plhnppnlkg iramsalipg irqvgvfdta fhqtmpdyay myglpyslyk kygirrygfh
      181 gtshryvskr acdilgvpye eqriitahvg nggsiaavkn gksidtsmgl tpvegllmgt
      241 rcgdvdagal tfimdkekld akglsdlink qsgvqglsgi ssdmreieaa vaegdkraim
      301 alniynyrik kyigayaaam ggcdilvwtg gvgenqwatr rvvcenmefm gmkidvekne
      361 gmrgeemvis tpdskvtiiv vptdeeymia sdtmdilgk
//
LOCUS       WP_009860767             495 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [Parabacteroides].
ACCESSION   WP_009860767
VERSION     WP_009860767.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..495
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54021
     Region          2..495
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mkkqiqinpa dnvvvavdtl sagdhitvgt ttvtvreeip aghkvalqdf ktgesiikyg
       61 fpigharkdi stgslvnekn iktnleglqd yiwqpqdttl dipdkgltfn gyrrrngdvg
      121 irneiwiipt vgcvngivnq laetlrqets gkevdaivaf phnygcsqlg ndhentrkil
      181 rdmvkhpnag avlvvglgce nnqpdafref lgeydterir fmvcqqvkde heegmnilre
      241 lytiastdkr taipmnelrv glkcggsdgf sgitanpllg vfsdflvaqg gttvltevpe
      301 mfgaetllmn rcateelfnk tvrlindfka yflenkqpvy enpspgnkag gistleeksl
      361 gctqksgksk vkdvlmygdr lttrglnlls apgndlvast alaasgchmv lfttgrgtpf
      421 gtfiptvkis tntalsenkp gwidfnagtl vegesmetls eqfirfilev aggrfvnnek
      481 kgyreiaifk sgvtl
//
LOCUS       WP_009868430             397 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Paramagnetospirillum
            magnetotacticum].
ACCESSION   WP_009868430
VERSION     WP_009868430.1
KEYWORDS    RefSeq.
SOURCE      Paramagnetospirillum magnetotacticum
  ORGANISM  Paramagnetospirillum magnetotacticum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Magnetospirillaceae; Paramagnetospirillum.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Paramagnetospirillum magnetotacticum"
                     /db_xref="taxon:188"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43073
     Region          5..393
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mregilvina gsssikfsly issgdekpll sckgqvegin vaphfiakap hggvlneqrw
       61 pdqpnmshea lfkymidwie aqlgdaelka aghrvvhggs qysqpllvtd elmdeldklv
      121 plaplhqphn lapiraltkv hpnltqvacf dtafhrsnpw taqsfalprk itgegvkryg
      181 fhglsyeyia rqlhqlspaa argkvvvchl gsgasmcaie ggksvastmg ftaldglpmg
      241 trtgtldagv vlyllqqkgm tpkeiedlly kqsgllgvsg vsndmrille ssephaaeav
      301 elfvyrisre lgslaaamgg vdalvftagi gershqirer vcahaewlgv emdqeanqrd
      361 sllisavesp vsvwviptde emmiakhtre vlkslrd
//
LOCUS       WP_009864761             108 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Methylobacteriaceae].
ACCESSION   WP_009864761
VERSION     WP_009864761.1
KEYWORDS    RefSeq.
SOURCE      Methylobacteriaceae
  ORGANISM  Methylobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 108)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Methylobacteriaceae"
                     /db_xref="taxon:119045"
     Protein         1..108
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=10991
     Region          <19..88
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mgtrqarpkv dqpqttknrk fpldrikidr sfveavdepg taaivgaiag lgaslgaavt
       61 aegveterql galrlsgcge aqgylfgkpa paaeaaaflr rgagtraa
//
LOCUS       WP_009868661             260 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Paramagnetospirillum
            magnetotacticum].
ACCESSION   WP_009868661
VERSION     WP_009868661.1
KEYWORDS    RefSeq.
SOURCE      Paramagnetospirillum magnetotacticum
  ORGANISM  Paramagnetospirillum magnetotacticum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Magnetospirillaceae; Paramagnetospirillum.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Paramagnetospirillum magnetotacticum"
                     /db_xref="taxon:188"
     Protein         1..260
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27665
     Region          22..124
                     /region_name="COG3942"
                     /note="Surface antigen [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443142"
ORIGIN      
        1 mrnaiillaa alflalpfea satlqcvtya revtglnlkg dawkwweaae gvyergripk
       61 vgsvlvfkrq gsmshghvav vqgaansrll fvdhanwaph rtagrgkvtk svpvmdvsan
      121 ndwsevrvwy qptreygskt yktqgfvyrp gnsvipaalr teapstmaaa pvempeesva
      181 aamaetaapa aieapkaeia vqpkaetvaq pkaiqapkvi eapkviearm paapaipsaa
      241 qpaadsdlgk fdarawaeqa
//
LOCUS       WP_009870966             431 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Paramagnetospirillum magnetotacticum].
ACCESSION   WP_009870966
VERSION     WP_009870966.1
KEYWORDS    RefSeq.
SOURCE      Paramagnetospirillum magnetotacticum
  ORGANISM  Paramagnetospirillum magnetotacticum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Magnetospirillaceae; Paramagnetospirillum.
REFERENCE   1  (residues 1 to 431)
  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 431)
  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 431)
  AUTHORS   ter Beek,J., 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 431)
  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 431)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Paramagnetospirillum magnetotacticum"
                     /db_xref="taxon:188"
     Protein         1..431
                     /product="CmpA/NrtA family 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=46600
     Region          42..299
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mtsnststkg isrrsvlasa avlaaaraal pggawaaagd apevkgatfg fialtdaspl
       61 iiakekgfft kygmpdvqvl kqaswgttrd nlelgsgggg idgahiltpm pylmaagrvt
      121 knntkvpmni larlntngqc isvsnaykdl klttearafg palakgraag keikvamtfp
      181 ggthdmwlry wlaangidpd kdvstivvpp pqmvanmkvg tmeafcvgep wndqlahqgi
      241 gfsavttgel wkdhpeksla mrgdwveknp kaakavtmav meaaqwcean ieemckivsg
      301 rewfkvpved ivarasgfin ygdgrlveks phvmkfwkdf asypfqshdl wfltenqrwg
      361 yqpmdldtka linqvnredi wraaakdlai paaqiptsts rgiekffdgk sfdpanptay
      421 lkslaikraa v
//
LOCUS       WP_009871228             255 aa            linear   BCT 20-JAN-2025
DEFINITION  3-deoxy-manno-octulosonate cytidylyltransferase
            [Paramagnetospirillum magnetotacticum].
ACCESSION   WP_009871228
VERSION     WP_009871228.1
KEYWORDS    RefSeq.
SOURCE      Paramagnetospirillum magnetotacticum
  ORGANISM  Paramagnetospirillum magnetotacticum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Magnetospirillaceae; Paramagnetospirillum.
REFERENCE   1  (residues 1 to 255)
  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 255)
  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 10118537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Paramagnetospirillum magnetotacticum"
                     /db_xref="taxon:188"
     Protein         1..255
                     /product="3-deoxy-manno-octulosonate cytidylyltransferase"
                     /EC_number="2.7.7.38"
                     /GO_function="GO:0008690 - 3-deoxy-manno-octulosonate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0033468 -
                     CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28264
     Region          3..244
                     /region_name="CMP-KDO-Synthetase"
                     /note="CMP-KDO synthetase catalyzes the activation of KDO
                     which is an essential component of the lipopolysaccharide;
                     cd02517"
                     /db_xref="CDD:133010"
     Site            order(9..11,50,77,102,104)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133010"
     Site            order(127,144,150..152,158..159,161..167,176,201..202,
                     205..207,214..217)
                     /site_type="active"
                     /note="oligomer interface [active]"
                     /db_xref="CDD:133010"
ORIGIN      
        1 mtrivglvpa rmaasrfpgk plfplcgrpm lehcflrgrm fphwdalavc tcdaeirdfa
       61 vskgwpviwt kdthtraldr vaeaagkcgi eladddivvc vqgdepmlhp dmikavvapf
      121 sqepevkgtm lgvhitdeam wrnpdivkii sdlkgnvlyt srapipyakt fspelgarrv
      181 ggifafrwaa lrwftetpes plekkescds nripdngwfq rlapypavty ysvdspadag
      241 lveaamkadp lwgky
//
LOCUS       WP_009871302             261 aa            linear   BCT 20-JAN-2025
DEFINITION  3-deoxy-manno-octulosonate cytidylyltransferase
            [Paramagnetospirillum magnetotacticum].
ACCESSION   WP_009871302
VERSION     WP_009871302.1
KEYWORDS    RefSeq.
SOURCE      Paramagnetospirillum magnetotacticum
  ORGANISM  Paramagnetospirillum magnetotacticum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Magnetospirillaceae; Paramagnetospirillum.
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   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 10118537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Paramagnetospirillum magnetotacticum"
                     /db_xref="taxon:188"
     Protein         1..261
                     /product="3-deoxy-manno-octulosonate cytidylyltransferase"
                     /EC_number="2.7.7.38"
                     /GO_function="GO:0008690 - 3-deoxy-manno-octulosonate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0033468 -
                     CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28754
     Region          4..245
                     /region_name="CMP-KDO-Synthetase"
                     /note="CMP-KDO synthetase catalyzes the activation of KDO
                     which is an essential component of the lipopolysaccharide;
                     cd02517"
                     /db_xref="CDD:133010"
     Site            order(10..12,51,77,102,104)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133010"
     Site            order(127,144,150..151,153,159..160,162..168,178,203..204,
                     207..209,216..219)
                     /site_type="active"
                     /note="oligomer interface [active]"
                     /db_xref="CDD:133010"
ORIGIN      
        1 mtlrtiaivp armnsgrfpg kplktidgms mvghctlrtr lcktltkvvv atpneevaad
       61 irslggevvv tpefdmcndr iawayeevak tdgpydlvin vqgdqplvhp dmldqiiaah
      121 aadpglesst lvepltliee fhdlnrvkvl frdsdggliy msrapipspk khgvlpervy
      181 khtaiiafkp aflkeflafg mtyneevegi dynrviemgr smkvlvtpiv sdtvdnaedl
      241 arvtktmatd plwnakaygr s
//
LOCUS       WP_009874950             356 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Actinobacillus pleuropneumoniae].
ACCESSION   WP_009874950
VERSION     WP_009874950.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus pleuropneumoniae
  ORGANISM  Actinobacillus pleuropneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Actinobacillus pleuropneumoniae"
                     /db_xref="taxon:715"
     Protein         1..356
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=40119
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 maisvkqink rfgqfqalnn idfsiqngel tallgpsgcg kttllriiag lematsgqil
       61 fddcdvtqls akerdigfvf qhyalfrhmt iadniafglr mkpkqerlse aeiqtkvknl
      121 laliqlehig grypdqlsgg qrqrvalara iatepkvlll depfgaldak vrkdlrrwlr
      181 dfhheinlts ifvthdqdea levadkiilm nkgqieqigt peqvykqprs afvanflgdv
      241 nilhgyildg alhidtfkkp ieqcyatddv vvyvrpnema itknkientl kgvisrvhta
      301 gptvflevlh knhepieisv syaqfgqeqf cigdevyfqp lllnffvqne liefmi
//
LOCUS       WP_009876821             721 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor family protein [Pseudomonas].
ACCESSION   WP_009876821
VERSION     WP_009876821.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..721
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=79255
     Region          13..721
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mssvsslsrl avaialgvsm qaaqaeeeak elgtvtvvgd wlgeadqavv qnhpgarsvv
       61 rrremlesga qnvrdvlrkv pgvqvqdnng tggsdislnv gvrgltsrls prstvmidgv
      121 paavapygqp qlsmmplsig nlesidvvrg agsvrygpqn vggvinfvtr aipekfsgei
      181 gttiehaghg gwkklnqafl ggtadnglgv allysgvkga dyrdgnndnd iddvllkthw
      241 qltdsdqlaa nfhyydayad mpggltqaqy dddpfqsvrd wdnfrgrrkd fslkytrqvd
      301 dltqfevlty ysdsfrgssi aarnlrtits yprdyhvfav eprvsriffa gpttqevgig
      361 yrylkeamne rasqlalvdn vptvrpgsdg htyqdrtggt easafyiddk idvgnwtitp
      421 girfekidsd wrdrpvlgln gkpvqekkrs kdyneplpal slmyhlsdew klfanysesf
      481 gslqyfqlgq ggsgndtaag lepekaktye lgtrydngsw ggeitlfyid fddelqyvsn
      541 dvgwtnlgat khqgietsgh ydfaaldprl dglsvygslt ytratyegdi psfkgrdlpl
      601 ysrqvatagv ryevdrwtyn ldafaqsmqr apglstdsqg nfthnyitep sadgqygdip
      661 gyvtwnarvg ydfgpqasnl klglgvknlf dkqyftrssd nnsgiylgqp rtlfmqasvg
      721 f
//
LOCUS       WP_009877306             674 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter permease [Pseudomonas].
ACCESSION   WP_009877306
VERSION     WP_009877306.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 674)
  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 674)
  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 674)
  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 674)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..674
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..674
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=71975
     Region          15..671
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 msdhqnglhl eaenwpralf avalafsvfq vvtaafplis tqvlramhvg llllvvyisy
       61 pafgigrpwq plawllgmag lgtavyqwvf egdliqrsge ltqadmvvgv vlivlvfeaa
      121 rrvmgialpi icalflaygl fgehlpgdla hrgygfdqiv nqlsfgtegl ygtptyvsat
      181 yiylfilfga fleqagmirl ftdfamglfg hrvggpakvs vfssalmgti tgsgvanvvt
      241 tgqftiplmk rfgykpafag gveatasmgs qlmppvmgav afimaetinv pyveiakaal
      301 ipallyfgsv ywmvhlearr adlkglpreq cpsawgavre rwfllipllv liallfsgrt
      361 plfsgtigla ltaivilgsa iilrvsslgl riafwvalgl lcagffrlgi gvifvviaal
      421 alacwfvrgg retlricvra laegarhaip vgiactlvgv iigvisltgi attfasyvld
      481 lgrenlllsl vltmvtclvl gmgiptipny iitssiaapa llelgvpliv shmfvfyfgi
      541 ladltppval acfaaapiak erglkisfwa vrialagfvv pfmavyspal mlqeggwgat
      601 lyvtckavla vglwgmasig ylqgplawwe rlvafaagas lvlalpisde lgfvlgalvi
      661 gwhlwrqrar eava
//
LOCUS       WP_009877634             293 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein, partial [Pseudomonas
            aeruginosa].
ACCESSION   WP_009877634
VERSION     WP_009877634.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         <1..293
                     /product="formate/nitrite transporter family protein"
                     /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          42..292
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 ghaaegarkp rargeerkek padgrsatal tanerreidd kqppraavlh evirvqgehe
       61 lqrtlaalww savaagltig lslmgmglfr aalpeqewai ivssfgypmg flavilarqq
      121 lftentltav lpvmteptle kawqllrlws vvlfgnivgt llfawavlhl pifneaadaa
      181 fleigrevmh ndlaqmfakg ivsgwmiatm vwlipaaega kvwiiamvty lmalgsfthi
      241 vvgsaevgyl afageidwse fllkfalptl ggnivggsli falishaqir seg
//
LOCUS       WP_009881039             242 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Streptococcus pyogenes].
ACCESSION   WP_009881039
VERSION     WP_009881039.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus pyogenes
  ORGANISM  Streptococcus pyogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
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
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptococcus pyogenes"
                     /db_xref="taxon:1314"
     Protein         1..242
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=27166
     Region          1..>240
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mirfnnvskt fgqtkvlqeq tfqindreff vlvgpsgsgk ttllkmincl iepssgdill
       61 nnvpqteldl remrlsigyv lqqialfpnl tvaeniaiip emkqwsaeei rqkteelldk
      121 vglpakdyld rypsdlsgge qqrigivrai ishpkillmd epfsaldpis rkqlqelmls
      181 lhkefdmtiv fvthdideai klgdrvailn egeivqldrp emikthpana fvanlfggde
      241 ha
//
LOCUS       WP_009883447             406 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase [Brevibacterium].
ACCESSION   WP_009883447
VERSION     WP_009883447.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium
  ORGANISM  Brevibacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Brevibacterium"
                     /db_xref="taxon:1696"
     Protein         1..406
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=44340
     Region          5..>390
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mstalnwtgk daafalgrrl istdasghlg egphflregd tyvptidenm lvvgdnlpal
       61 trllathrgr ikvvyidppy ntgnalaykd hghdhaswln fmtprlmlar elmredgvif
      121 ihlddgesaw aqllgheifg ednslgtlih qrakgggnsp sfvrghdyvh vwakvadqag
      181 afltekkapa kleiidgkrm lvetdvlrag fgryargqer rlmyedilev kgpkklaevd
      241 aklgtgeyvl rpwgpagkha vvrvtpaeka ssklysiika lggqndledl glggifsypk
      301 pvelvktlva sqtffdpgai vldffagsgt taqavmaane rdagsrtfil iqtpeplqtk
      361 narslvgads edgfpeisrl taerirraak rhdpelhfte iavaeq
//
LOCUS       WP_009884243             295 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Brevibacterium
            aurantiacum].
ACCESSION   WP_009884243
VERSION     WP_009884243.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium aurantiacum
  ORGANISM  Brevibacterium aurantiacum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Brevibacterium aurantiacum"
                     /db_xref="taxon:273384"
     Protein         1..295
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32355
     Region          12..287
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mfpqthevfs htaqqaaaav isnystsfgl atrllgltyr hhirniyalv riadeivdgl
       61 asdagldage qrqlldnfaa atrsalhfgi sdnliihafa qtarttgitf dliepffasm
      121 radlsapsap vrglpadehr dyvygsaevv glmclkvfls dqnrtpteve tlefgarqlg
      181 aafqninflr dladdsvrlh rsylttesrl sdsdktawvi iirqqladaq atfsllpkda
      241 raavrsaaal faalndrial tpvdrlyqer vripnvvkmr lasrailsta regrp
//
LOCUS       WP_009888659             198 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Burkholderia thailandensis].
ACCESSION   WP_009888659
VERSION     WP_009888659.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia thailandensis
  ORGANISM  Burkholderia thailandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia thailandensis"
                     /db_xref="taxon:57975"
     Protein         1..198
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21263
     Region          8..195
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 meprpapprr livaitgatg aiygvrmldm lrasggveth llissagwln iqhelqlskd
       61 dvlaradvvh svrdvgasia sgsfatdgmi vapcsmrtla siahglsdnl itraadvalk
      121 errrlvllvr etpfnlvhlr nmtavtemgg vifpplpafy ampktigemv dhtvarvldm
      181 falgvprtap wqglrehg
//
LOCUS       WP_009890045             382 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Burkholderia thailandensis].
ACCESSION   WP_009890045
VERSION     WP_009890045.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia thailandensis
  ORGANISM  Burkholderia thailandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 382)
  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 382)
  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   3  (residues 1 to 382)
  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   4  (residues 1 to 382)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 382)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 382)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia thailandensis"
                     /db_xref="taxon:57975"
     Protein         1..382
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39934
     Region          33..369
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(109..111,132..133,182,234,258)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mrlrsslssl alaaafacga tgaaraaddt pvrigfaapl tgvnagygkd lqngvqlald
       61 daraqnvkig gkparfelvv eddqadprig vqaaqslvdk kvsvvvghfn sgttipasvv
      121 ydkagipvid paatnpvits rglanvfmvi atdgqnagna gryavdvtka kriaivddrt
      181 afgqgeadef dkavkaagsa ivareytnnq avdfraqits lksknvdlif fggldslaan
      241 fikqmkqlgl naqfvggggv kdaefikiag paaegamawe ygrpldqlpq gkdfearfkk
      301 rfgvdvlsya qfgydatwaa iramqaagst dpngyrpalk kidfegitgr isfggdgslk
      361 sgmstlyqvk ngawqtivtk gg
//
LOCUS       WP_009890410             258 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Clostridioides
            difficile].
ACCESSION   WP_009890410
VERSION     WP_009890410.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..258
                     /product="formate/nitrite transporter family protein"
                     /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=27100
     Region          3..256
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mhketldklt naainkinll ntskvkylvs safaglyvgi gilliftigg lltdagspmt
       61 kivmglsfai alslvimtgt elftgnnmvm sagmlnkgvs ikdtskiway swvgnligal
      121 vlglifvgtg lvdkgpvaef fantaaskas mpftalffrg ilcnilvcvs vlcsfrtnsd
      181 takiimiflc lfafitsgfe hsvanmtiys vslfsptist vtiggaiynl vavtlgnivg
      241 galfmglgty ilgkekln
//
LOCUS       WP_009890729             272 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Clostridioides
            difficile].
ACCESSION   WP_009890729
VERSION     WP_009890729.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..272
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32164
     Region          14..113
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          <67..256
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mlsvtrysik nvrlkpwvkf iwyfetksni llnnkllptd sidiilnlsd vmeykienqd
       61 ytasnmhfng irdkhgfiiq hgnirvigis fypfglypfl kipisefnrq ivdleavsel
      121 fakkleesln ptqsvekivl yleemllsil eedlisnksv kllnsfiydn rysnikafcd
      181 ntniniktle riclkytgyt pkilkriyrf kmassqliyn ykdnelfdfi yeneyydqah
      241 fikefkkfsg tspikfigen ktikenikyn yl
//
LOCUS       WP_009890769             199 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Burkholderia thailandensis].
ACCESSION   WP_009890769
VERSION     WP_009890769.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia thailandensis
  ORGANISM  Burkholderia thailandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 199)
  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   2  (residues 1 to 199)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Burkholderia thailandensis"
                     /db_xref="taxon:57975"
     Protein         1..199
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18970
     Region          24..80
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mlkkllmlvv alslsltaal aaavevntad qaalesvkgl gpvkskaiid erakngpfkd
       61 addlanrvkg lgaksvanle aagltiggst tpptgakakt satkpaatat papapattpa
      121 kpapstatpa paaatpstaa sapaakktrs skkkdkaaaa asaaaqasap aaasstktkg
      181 skksrknkaa tpasaasga
//
LOCUS       WP_009891111             312 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia thailandensis].
ACCESSION   WP_009891111
VERSION     WP_009891111.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia thailandensis
  ORGANISM  Burkholderia thailandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
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
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia thailandensis"
                     /db_xref="taxon:57975"
     Protein         1..312
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=32925
     Region          1..309
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mieiervsrl fgdiaavddv slavargtvt alvgasgsgk stllrminrl iaptsgtirv
       61 dgvdtasvpa etlrrgigyv iqghglfphw tvarniatvp rllgwraari darvrellal
      121 feldydtyar klphqlsggq qqrvgvaral aaepaillmd epfgaldpii rgkaqddlaa
      181 lqrrlgitiv ivthdideal rlgdqiavmd agrilqagpp aeilgrpqpg vverlvagld
      241 rplrllaltr vdalaepgaa pgepisgalt lrdaisellw rgasalpvss adgaaarrit
      301 ldaivaqakr pa
//
LOCUS       WP_009891312             351 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Burkholderia
            thailandensis].
ACCESSION   WP_009891312
VERSION     WP_009891312.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia thailandensis
  ORGANISM  Burkholderia thailandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Burkholderia thailandensis"
                     /db_xref="taxon:57975"
     Protein         1..351
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38092
     Region          1..350
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mgitvrnlhk rfgdftaldd vtldfpagel vallgpsgcg kttllrviag lehadsgqvv
       61 lqgldvasvg arerqvgfvf qhyalfrhmt vfenvafglr vkprrerpge aairakvhel
      121 lslvqldwla qrypselsgg qrqrialara lavepkvlll depfgaldak vrkelrgwlr
      181 rlhddlhist ifvthdqeea levadrivvl dhgrveqvgs pqdvydhprs afvyeflgaa
      241 nrldgtvsgq gfvahgaaqa iavdadfagp arayvrphdl elaapharad giaadvrrvv
      301 plggsvrvel aarsggvlea eldrnawral aldvgdaltv vpravrvfpa r
//
LOCUS       WP_009892108             347 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia thailandensis].
ACCESSION   WP_009892108
VERSION     WP_009892108.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia thailandensis
  ORGANISM  Burkholderia thailandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 347)
  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 347)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 347)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 347)
  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   5  (residues 1 to 347)
  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   6  (residues 1 to 347)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Burkholderia thailandensis"
                     /db_xref="taxon:57975"
     Protein         1..347
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38595
     Region          33..220
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <182..347
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mamsvpdptr qlnkasvssa yalfmlmlae ergiagadll antgvtrskl eepdaritpl
       61 qqaaivfnll gmtndpsiai eiglrssltk sgligfglms catlgeaiql girylptrvp
      121 ffsvrltele htvqidilea fplgrlrqfa venfmvetai lfnslltpsh dktmkanael
      181 cfewpeppyf aryrdrlprc hfgapanqir ceaalldepi rtanahtaqm ivqqceaela
      241 rlgyaesive rvrnllirgn ngypsldala relhlsertl krklsdygat ysalldeirl
      301 rdalrllegt hltveeiaar vgytdranfs rafrrwtgts pssrrra
//
LOCUS       WP_009894043             278 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Clostridioides difficile].
ACCESSION   WP_009894043
VERSION     WP_009894043.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..278
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31271
     Region          1..248
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mltelhchts isdnnfttee iikkaaekni nilaitnhdt lsgldealvl gehygitiip
       61 gieisaydyk nrkrvhilgy nidlnsqeik nlcnpmvcdr hkasvkmvnk iidlgykisl
      121 edvkkysskt gifkqhimka lidkgytdni ysslykelfh rgngkvyvsl kyvdyrdaik
      181 aiknsggicv lahpgqmdnf saieemvkvg ldgievyhps hnkelekesl syakkynlvv
      241 tggsdyhgfy sqhnyelgsk slnkedlfkf rlalggvl
//
LOCUS       WP_009894180             393 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Burkholderia thailandensis].
ACCESSION   WP_009894180
VERSION     WP_009894180.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia thailandensis
  ORGANISM  Burkholderia thailandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 393)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Burkholderia thailandensis"
                     /db_xref="taxon:57975"
     Protein         1..393
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=41980
     Region          213..316
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(284..285,293,309..312,314)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mcaaaisfgm pdrprqlfmn hrcatgprll pyarllcvaa gaslagisaf vpqtaraesa
       61 aaaasnafap agaasskfas aaqsrdassr igseasapas pasaasapph asnaqasapr
      121 alaaprlppl teaeaadvtr ralalrtafa qevtrrlnvp aaerraygvr lqqtldandv
      181 gelareyvvl vdrapnvqaa fiyfrttrdn awrmigaspv atglpgqydh fvtplgvfeh
      241 tpenmdfrae gtinengirg ygqrdmriyd fgwtdatrgw gkggvsqmrf qmhatdpdyl
      301 epllgirhsk gcvripasln vfldqhgild aeyearaaag dppwvlrvhr qvtpwagryl
      361 vvvdsqrktr pawspapgkk araklpkggd tad
//
LOCUS       WP_009895576             344 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Burkholderia thailandensis].
ACCESSION   WP_009895576
VERSION     WP_009895576.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia thailandensis
  ORGANISM  Burkholderia thailandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Burkholderia thailandensis"
                     /db_xref="taxon:57975"
     Protein         1..344
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=37407
     Region          58..225
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 maeeqqakii negrrgflar ssawpvgmlm lplagcgdgd gvvpsahaqd apqppgagya
       61 idrsiqspnq dsrvrtlvlh ytaqtladsi asltspqrqv sshylvpdap dggerfkvfe
      121 lvpearrawh agvsywqgdr mlnagsvgie ivnlgfpped enlplmnrrw ypypdaqvav
      181 fgalaaevva rhqvlphkvv ghsdvapgrk tdpgplfpwk klydqykiga wpeteavdyy
      241 rtnrpfagdv aslqskllay gydapqtgtl dvqtvnvvsa fqmhfrpsry dgvpdvetva
      301 ildallekyf nrgrsinkqa lpgatapage kgsdvwplap aspr
//
LOCUS       WP_009895906             358 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Clostridioides difficile].
ACCESSION   WP_009895906
VERSION     WP_009895906.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..358
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=41379
     Region          1..348
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mslyvdiekd lssfklkvei kqekgtlgfl gesgsgksmt lkciaglekp trgkivlndr
       61 vlfdsekkin lstqdrkvgf lfqnyalfph mtvsqnielg llklsksekk eivaryldil
      121 klngfegryp wqlsggqqqr valaralats pdillldepf saldhhlrsn mekelmnmlk
      181 dykgdilfvt hdieeayrvc ddiivynkge glpkrpkkel fespkyliea kitgcknisk
      241 lnrldkntiy atdwgceltl nreigdniey vgirehhikv ldsnedlnek lcfelinive
      301 npftytiyvr ktdlsnecvp iqielekskm rfkkgdriyl nfpqeylfcf rynynkke
//
LOCUS       WP_009897686              52 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Clostridioides difficile].
ACCESSION   WP_009897686
VERSION     WP_009897686.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 52)
  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   2  (residues 1 to 52)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..52
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..52
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=5630
     Region          <2..50
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mdslpgvgea tankilqhre engqfssiee iknvngigdk kyenikdlic vd
//
LOCUS       WP_009897357             699 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Clostridioides difficile].
ACCESSION   WP_009897357
VERSION     WP_009897357.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 699)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..699
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76737
     Region          2..696
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 msleklirpk siaivgvtdk lgfgrsaals ivksketdrv yyvnpkreel fgrkcyktiq
       61 evpevvdcvv vctprnvvps vlkdsgelgt kavvvyasgf aeegteegtd lenqlieisn
      121 tydmkilgpn cmgllncidk vnlwaggskw dldtkkpgig ivgqsgfita eivssdyfni
      181 sygfstgngn ivtledavdf lvdddyasvi aiyleglknp qkfidalkra aqkrkpviil
      241 ksgrsekgai saashtgnla gsskafesif ekygvisven leqfmclaqa fsvldgnlpa
      301 nsnfaainfs ggenticadl aeengvelae issetkeemk kylpgfatpk npldattalf
      361 hekdmivgll htfekddsvg ftmvganird eenemhetlc kavseareqg lkkpvfavpt
      421 legnryldyr trlednqvpi mssvgttftc fnkmakfidy dyskrtlefk avkkresnnv
      481 valseldski emkkygvpvp gqgnakside ldeilkyiky pvvlkinsse ilhksdvggv
      541 kigiknrdea vdayneiltn vkkakpdani dgilvqemve sgieiiigit nddqfgpmll
      601 vglggvfvev fkdttlyplp inhdeaimml kklksfklln gyrgsepcdi daladmmvkl
      661 gkyayenkde vkeidlnpvf vypkgkgvca vdalivkyk
//
LOCUS       WP_009897800             153 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Burkholderia
            thailandensis].
ACCESSION   WP_009897800
VERSION     WP_009897800.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia thailandensis
  ORGANISM  Burkholderia thailandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (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   2  (residues 1 to 153)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 153)
  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 153)
  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 153)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Burkholderia thailandensis"
                     /db_xref="taxon:57975"
     Protein         1..153
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17181
     Region          11..100
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(30,49..50,68,71,79..80,92,97)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mdckylyidn ikinfvrrvi eidgeaislt prefdvvefl ldnmnkvvsr qaiqeavwgr
       61 elavssrtld thvsrirskl gldfdknmri ipiysigyrl vlfgaattrv eqhdeqhavh
      121 adaprlaada avpaaplarp saaphverfa eyh
//
LOCUS       WP_009898135             386 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Clostridioides difficile].
ACCESSION   WP_009898135
VERSION     WP_009898135.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 386)
  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 386)
  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
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 386)
  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   5  (residues 1 to 386)
  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   6  (residues 1 to 386)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 386)
  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 20283052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..386
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42537
     Region          15..>56
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          81..375
                     /region_name="ASKHA_ATPase_ROK_SaXylR-like"
                     /note="ATPase-like domain of Staphylococcus aureus xylose
                     repressor (XylR) and similar proteins; cd24077"
                     /db_xref="CDD:466927"
ORIGIN      
        1 mvtdkytire mnerlvleqi ikngpisras iastiglnka tisaitkkli deslvheigi
       61 gnsthsggrk pillvfnkca gislsmdvgy dyifsslsyl dgtiinskkl tdiqvskdnv
      121 iqlideiins yniskidtpy kvigltlaih gitcenkvlf tpyynlneid lysilskkyd
      181 fpihienean ltalaentfs tvhnsllsls ihsgfgsgii innklysgrn gmsgeighti
      241 impngklcpc gnrgcleqyc sekkvfeqls slenipkids divkqlyyed nqnakkvihe
      301 fcsyltiain naittyapei iylnsqiisd ipeilqitkd mlvssfnkgi nieisslgse
      361 aslyggsavn iksflniqnl tlinei
//
LOCUS       WP_009899063             640 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Clostridioides
            difficile].
ACCESSION   WP_009899063
VERSION     WP_009899063.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 640)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 640)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..640
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=73128
     Region          51..639
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mffkkkkeks takiidfnkd dilnetnlld kgipslkeli spssfevdad yikigkkyvr
       61 sfimqgfpaq vyvgwldsif nyegetdtti hidptddkia leeytrkitq feaqlmseqe
      121 kgnirnitrl rdkiqelyme rsklerntdk lfqvqiacnl ysdsldelnk etqkidnklr
      181 grkmymmpty lrqddtyktv spygksyved mfrnfnsgal tscfpfynsd irhekgvfcg
      241 inlstcspil idfydrsklk nsnitvigqp gtgktffvsl ltmrsalrgi rtviidpese
      301 ygrltealgg sriylatdsk ecinpfdiee edeldenflp tgiklvdvkg kiadllnlia
      361 vmagglsgaq tstvaqllqe lyesfgitkn pkslyvtepy fdkntkefih egrkktmpif
      421 sdfynslsey aeknsdievm dlvrvlkmfk kggvydlfdc ytssnisnfk nspivtfdvs
      481 kleenilrpi gmyvalswtw ekfgkkdpyi nkrivcdeaw mlvsknmags eysakfleta
      541 srrirkrmgg llvasqkfte fvestqgqav ltsaetkifl gqdttdidsi qnmfklsege
      601 klfllradkg emlvriqges tvvkvlafdf ekkliekrta
//
LOCUS       WP_009899139             255 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia thailandensis].
ACCESSION   WP_009899139
VERSION     WP_009899139.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia thailandensis
  ORGANISM  Burkholderia thailandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 255)
  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 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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (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   5  (residues 1 to 255)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Burkholderia thailandensis"
                     /db_xref="taxon:57975"
     Protein         1..255
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27837
     Region          1..251
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <154..251
                     /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 mtrlasptls lrrygvvres dvhdfhqivl gvdgamtmtv dgvderidrr aawlipagsr
       61 hdyagladns qlvldlppgs lavperlfer aktmsidpgl tmlvgelasr iargphadaa
      121 sarrlhwqaa arlcdalvge lggapaqsaa gldfaridrw lrahlaqplr iadlaahcgf
      181 gmrrfhqlfc eafgetphry lqrlrldaav vllgnpkhsl adiasevgfa dqsafthaft
      241 krfglapgrw rsdrh
//
LOCUS       WP_009900523             310 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Burkholderia
            thailandensis].
ACCESSION   WP_009900523
VERSION     WP_009900523.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia thailandensis
  ORGANISM  Burkholderia thailandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia thailandensis"
                     /db_xref="taxon:57975"
     Protein         1..310
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32802
     Region          26..272
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 messsrpart gaasaatlrv dcrnalgega twcdatraly wvdiegarlw rwraagaqgg
       61 aatdswempe rigcfaltdd pdvllvglas rlaffdarrr aftpivdvep dlptrlndgr
      121 cdragafvfg mkdegggspr avggyyrlnp dlslqrlalp paaiangiaf spdgsamyfc
      181 dsptreiqvc dyrpggdvdr irpfvrladd cgepdgstvd adggvwsaqw ggarivryda
      241 qgveteriav ptpqpscval ddggrlyvts arvglddgal arspgaggvf vadtrhagla
      301 tsrfalarna
//
LOCUS       WP_009900901             375 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia thailandensis].
ACCESSION   WP_009900901
VERSION     WP_009900901.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia thailandensis
  ORGANISM  Burkholderia thailandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 375)
  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 375)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 375)
  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   4  (residues 1 to 375)
  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 375)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Burkholderia thailandensis"
                     /db_xref="taxon:57975"
     Protein         1..375
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41504
     Region          47..229
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          274..354
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mlaplnytyr fchtaprhap amkheekkgt vsielvessl alsrrrgvdd apllaqsgia
       61 aallaqrnar vsarqygalw naiaraldde ffgqdshpmr cgsfiamsqa alsarnglra
      121 laravnfmhc vlddlhaeid anaervrlrf vhrnsanppe mfayatyfii vygltcwlig
      181 rripllhasf rcgepravhe yqlmfcddmr fgesesyvdf dpafaalpvv qtaktlkpfl
      241 rdapasfivk yrnphalggr vraalralpp aawptarala arlhvaeatl rrklkqeghs
      301 yqtikdalrl dlacealadp artvadvaaa tgfaepsafy rafrkwrgms padyrdaala
      361 araaasrfrr kpptl
//
LOCUS       WP_009901237             302 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia thailandensis].
ACCESSION   WP_009901237
VERSION     WP_009901237.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia thailandensis
  ORGANISM  Burkholderia thailandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 302)
  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 302)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 302)
  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   4  (residues 1 to 302)
  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 302)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia thailandensis"
                     /db_xref="taxon:57975"
     Protein         1..302
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32429
     Region          58..297
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <195..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 mmtllavppe klsaasavst sagstsaast aasvngasas pppatsasaq laahggddgd
       61 gfaamlahfa qlepvfdalp dvaffvkdah aryalvnrtl aqrcgykdkr dlygkaadev
      121 fprrfgrsyv eqdlaiiagg rqltdqlelh lysgrqpgwc ltckeplrna hgkivgiagl
      181 srdlrahess hpaysriadv vryihahyvq plnlkhlagm agmsvaqler yfhkvfhltp
      241 rqmllkarld aatallvthd kvtdvaalcg ytdhsaftrq fkatvgvtpt eyrmmlqegr
      301 ga
//
LOCUS       WP_009902819             398 aa            linear   BCT 20-JAN-2025
DEFINITION  RHS repeat-associated core domain-containing protein, partial
            [Burkholderia thailandensis].
ACCESSION   WP_009902819
VERSION     WP_009902819.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia thailandensis
  ORGANISM  Burkholderia thailandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 398)
  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 12859901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Burkholderia thailandensis"
                     /db_xref="taxon:57975"
     Protein         <1..398
                     /product="RHS repeat-associated core domain-containing
                     protein"
     Region          <13..145
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
     Region          <13..66
                     /region_name="Rhs_assc_core"
                     /note="RHS repeat-associated core domain; TIGR03696"
                     /db_xref="CDD:274730"
ORIGIN      
        1 gvaavalalg aadatglvch glrwydprvg qfispdpvvt svytvgawnp yvyclgnpil
       61 ladpngcsfl svleiigvai laaacvvgai ftggatlval gvlsaniggw llagvalgsl
      121 ggaiagelaa qkaggnlwag aflgaflgga tsliggalgg aaaagidtli ggtktflsfv
      181 aagaiqgtla gagtglaigy aggkgnaesm liamakgaaw gavlgtllga gigaiagtgi
      241 sgaakpdnfl nigafgqkfa dftststain sadnaagvte sltqlsmpng fnagnmlgll
      301 pnlvttneqa agwfsipigw lgpgvlndag faglvdtsma ldqagfsyah qislllgaap
      361 yfidyaatma qivdasgvnn femafnnafg sgspsntg
//
LOCUS       WP_009903080             699 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Clostridioides difficile].
ACCESSION   WP_009903080
VERSION     WP_009903080.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 699)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..699
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76739
     Region          2..696
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 msleklirpk siaivgvtdk lgfgrsaals ivksketdrv yyvnpkreel fgrkcyktiq
       61 evpevvdcvv vctprnvvps vlkdsgelgt kaavvyasgf aeegteegtd lenqlieisn
      121 tydmkilgpn cmgllncidk vnlwaggskw dldtkkpgig ivgqsgfita eivssdyfni
      181 sygfstgngn ivtledavdf lvdndyasvi aiyleglknp qkfidalkra aqkrkpviil
      241 ksgrsekgai saashtgnla gsskafesif ekygvisven leqfmclaqa fsvldgnlpt
      301 nsnfaainfs ggenticadl aeengvelae issetkeemk kylpgfatpk npldattalf
      361 hekdmivgll htfekddsvg ftmvganird eenemhetlc kavseareqg lkkpvfavpt
      421 legnryldyr trlednqvpi mssvgttftc fnkmakfidy dyskrtlefk avkkresnnv
      481 valseldski emkkygvpvp gqgnakside ldeilkyiky pvvlkinsse ilhksdvggv
      541 kigienrdea vdayneiltn vkkakpdani dgilvqemve sgieiiigit nddqfgpmll
      601 vglggvfvev fkdttlyplp inhdeaimml kklksfklln gyrgsepcdi daladmmvkl
      661 gkyayenkde vkeidlnpvf vypkgkgvca vdalivkyk
//
LOCUS       WP_009904483             170 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Burkholderia thailandensis].
ACCESSION   WP_009904483
VERSION     WP_009904483.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia thailandensis
  ORGANISM  Burkholderia thailandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 170)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Burkholderia thailandensis"
                     /db_xref="taxon:57975"
     Protein         1..170
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17949
     Region          9..159
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfalsealps skpalyetla aqaralveae tdivanaanf aslvyhsldg lnwagfyffd
       61 grelvvgpfq gkpacvripl gkgvcgtaaq trgtqvvhdv hafaghiacd sasqseivvp
      121 liardgalig vwdvdsplig rfdaedatgm ealcrvfvev awenatrrge
//
LOCUS       WP_009904892             167 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Clostridioides
            difficile].
ACCESSION   WP_009904892
VERSION     WP_009904892.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 167)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 167)
  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 167)
  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 167)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..167
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19034
     Region          74..163
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(93,112..113,131,134,142..143,155,160)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mkknisyipm dsaleiwlle kllrdppdsd yakdllsgiq emirgevssl llgsseesdc
       61 pvgtlsdril agdleiyprg rkvlikgsev nltpkefdil yflvqnkgev ftkeqiyrav
      121 weedylldns nimafirklr kkiepapdsp tyiltiwgig ykfndqi
//
LOCUS       WP_009905601             351 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Burkholderia
            thailandensis].
ACCESSION   WP_009905601
VERSION     WP_009905601.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia thailandensis
  ORGANISM  Burkholderia thailandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Burkholderia thailandensis"
                     /db_xref="taxon:57975"
     Protein         1..351
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38120
     Region          1..350
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mgitvrnlhk rfgdftaldd vtldfpagel vallgpsgcg kttllrviag lehadsgrvv
       61 lqgldvasvg arerqvgfvf qhyalfrhmt vfenvafglr vkprrerpge aairakvhel
      121 lslvqldwla qrypselsgg qrqrialara lavepkvlll depfgaldak vrkelrgwlr
      181 rlhddlhist ifvthdqeea levadrivvl dhgrveqvgs pqdvydhprs afvyeflgaa
      241 nrldgtvsgq gfvahgaaqa iavdadfagp arayvrphdl elaapharad giaadvrrvv
      301 plggsvrvel aarsggvlea eldrnawral aldvgdaltv vpravrvfpa r
//
LOCUS       WP_009906309             198 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Burkholderia thailandensis].
ACCESSION   WP_009906309
VERSION     WP_009906309.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia thailandensis
  ORGANISM  Burkholderia thailandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia thailandensis"
                     /db_xref="taxon:57975"
     Protein         1..198
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21235
     Region          8..195
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 meprpapprr livaitgatg aiygvrmldm lrasggveth llissagwln iqhelqlskd
       61 dvlaradvvh svrdvgasia sgsfatdgmi vapcsmrtla siahglsdnl itraadvalk
      121 errrlvllvr etpfnlahlr nmtavtemgg vifpplpafy ampktigemv dhtvarvldm
      181 falgvprtap wqglrehg
//
LOCUS       WP_009908049             294 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia thailandensis].
ACCESSION   WP_009908049
VERSION     WP_009908049.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia thailandensis
  ORGANISM  Burkholderia thailandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 294)
  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 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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia thailandensis"
                     /db_xref="taxon:57975"
     Protein         1..294
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31705
     Region          49..289
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <187..285
                     /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 mmtllavppe klsaasavsa aavstaapvn aasaspspaa sasaqlaahg gdgfaamlah
       61 faqlepvfda lpdvaffvkd aharyalvnr tlaqrcgykd krdlygkaad evfprrfgrs
      121 yveqdlaiia ggrqltdqle lhlysgrqpg wcltckeplr nahgkivgia glsrdlrahe
      181 sshpaysria dvvryihahy vqplnlkhla gmagmsvaql eryfhkvfhl tprqmllkar
      241 ldaatallvt hdkvtdvaal cgytdhsaft rqfkatvgvt pteyrmmlqe grga
//
LOCUS       WP_009908264             676 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Burkholderia thailandensis].
ACCESSION   WP_009908264
VERSION     WP_009908264.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia thailandensis
  ORGANISM  Burkholderia thailandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Burkholderia thailandensis"
                     /db_xref="taxon:57975"
     Protein         1..676
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=73595
     Region          66..>486
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mmqkldaasp eaqsadlvsa nverlralfp dvvtegpdga svnldalaam vgasaaavad
       61 adekyglnwh gkrrarrlal tpstgtlrpc presvgwast rnlmiegenl evlkllqksy
      121 agraklvyid ppyntgkdfv ysdnftdslr hyleltgqtt dgkrisshtd asgrfhtdwl
      181 nmiyprlkla rdlladdgvi avhideheqh alvlvmreif gednelgvav wdkrnpkgda
      241 rgiayqhesi vlfardaqll feraplkrpk rnaqrmldaa rgaiagaati adanaayraw
      301 vksqttlsgg eamydrisad grvyrlvsma wpnkkkapdd yfvplvhpvt gkpcpvperg
      361 wrnppatmqa lidkglvefg adettqpqri yfldenmyen vpsvlpfggs ddalmkslgi
      421 pfdqpkpvef aasiigwctd gddlivdffg gsgttghavm alnaadggnr ryvlvqlpep
      481 ldagskdqka aadfcaaqrv plnlaeltke rlrraaarva aehpgtradl gfrvfrldst
      541 nvsewdprgd diqqslfaav ehikpnrsee dllyelmlkl gldlcapida rtiagkavyv
      601 idgaivacfd ahidrastda lgegivelia eaaaagaaha rdvtcvfrds gfaddvakvn
      661 lsaileqhgv krirsl
//
LOCUS       WP_009910620              86 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Burkholderia
            thailandensis].
ACCESSION   WP_009910620
VERSION     WP_009910620.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia thailandensis
  ORGANISM  Burkholderia thailandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   3  (residues 1 to 86)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Burkholderia thailandensis"
                     /db_xref="taxon:57975"
     Protein         1..86
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9321
     Region          15..66
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msfehlnram reqfpptakv ipiflarlad eqgncdpsid aiaefagvtr vtvsstlrtl
       61 eeagalritr rpghpsayrl tlgras
//
LOCUS       WP_009914010             379 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Burkholderia].
ACCESSION   WP_009914010
VERSION     WP_009914010.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 379)
  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 379)
  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   3  (residues 1 to 379)
  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   4  (residues 1 to 379)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 379)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 379)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 379)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..379
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39928
     Region          29..365
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(105..107,127..128,177,229,253)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mqhtmkklag atfvavmsla gtahaddvki gfaapmtgaq ahygkdmqng ivlaiedina
       61 tkptiggkpv kfvldtqddq adprtgttva qklvddgikg mlghfnsgtt ipasriyana
      121 gipqiamata peyttqgykt tfrmmtsdtq qgsvagtfav kdlgmkkiai vddrtaygqg
      181 ladqfekaak asgativdre ftndkavdfk ailtklkask pdlvyyggad sqaapmakqm
      241 kslgvtaplm ggemvhtptf lkiagdaaeg siaslaglpl aempggktya dkykkrfged
      301 vqtyspyayd gamamfnamk kanstdpaky lpllaktdma gvtsthiayd akgdlknggi
      361 tmykvekgew kplksiggk
//
LOCUS       WP_009914589             129 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein, partial
            [Burkholderia humptydooensis].
ACCESSION   WP_009914589
VERSION     WP_009914589.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia humptydooensis
  ORGANISM  Burkholderia humptydooensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (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   2  (residues 1 to 129)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 129)
  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 129)
  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 129)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Burkholderia humptydooensis"
                     /db_xref="taxon:430531"
     Protein         1..>129
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          11..100
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(30,49..50,68,71,79..80,92,97)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mdckylyidn ikinfvrrii eidgepvslt prefdvvefl ldnmnkvvsr qaiqeavwgr
       61 elavssrtld thvsrirskl gldfdknmri ipvysigyrl vlfgtattrv ephdeqhaah
      121 aaaplarpa
//
LOCUS       WP_009919607             347 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia pseudomallei].
ACCESSION   WP_009919607
VERSION     WP_009919607.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 347)
  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 347)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 347)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 347)
  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   5  (residues 1 to 347)
  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   6  (residues 1 to 347)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..347
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38747
     Region          33..220
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <182..346
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 matsvpdptr qlnkatvssa yalfmlmlae ergiadadll ahtgvtrtkl eepnaritpl
       61 qqaaivfnll gmtndpsiai eiglrssltk sgligfglms catlgeaiql girylptrvp
      121 ffsvrftefe htvqidilea fplgrlrqfa venfmvetai lfnslltpsh dktmkanael
      181 cfewleppyf aryrdrlprc hfgapanqir ceaalldepi ktanahtaqm ivqqceaela
      241 rlgyaesive rvrnllirgs hgypsldala relhlsertl krklsdygtt ysalldeirl
      301 rdalrllegt altveeiaar vgytdranfs rafrrwtgts psdrrrt
//
LOCUS       WP_009923395             289 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia pseudomallei].
ACCESSION   WP_009923395
VERSION     WP_009923395.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 289)
  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 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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..289
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31451
     Region          33..280
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <182..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 mmtllavppe klpaasaast aagptpaagn garaspplsg aapedddgfa amlahfaqle
       61 pvfdalpdva ffvkdvrary alvnrtlaqr cgykdkrdly gkaadevfpr rfgrsyveqd
      121 ltiiaggrql tdqlelhlys grqpgwcltc keplrnaqgr ivgiaglsrd lrahesshpa
      181 ysriadvvry ihahyvqpln lkhlagmagm svaqleryfh kvfhltprqm llkarldaat
      241 allvthdkvt dvaalcgytd hsaftrqfka tvgvtpteyr lmlqegrga
//
LOCUS       WP_009925287             353 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Burkholderia pseudomallei].
ACCESSION   WP_009925287
VERSION     WP_009925287.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 353)
  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 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   3  (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   4  (residues 1 to 353)
  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 353)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..353
                     /product="CmpA/NrtA family 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=37771
     Region          14..260
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mntarikaaa admperarlr igfvalsdaa plvaaqrlel garygltlel crqpswasir
       61 dkllsgelda ahalyglvyg vqlgiggpra dlavpmvlnr ngqaitfsnr ladayrasge
      121 lkaalatlgr rpvfaqtfpt gthamwlyhw lashgvdplr dvrsvvippp emvdalaage
      181 ldglcvgepw navaeargag rtvaatsevw pdhpekalac rrefvalypn tarllvrtll
      241 dacewlddad hrmkaaawla epdaigvpig qiaprllgdy gagpfaqppa pikfyehgtv
      301 nrpaasdgmw flsqyrrwgm lsgdvddaai angvahtaly deavalggar rge
//
LOCUS       WP_009926601             328 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Listeria monocytogenes].
ACCESSION   WP_009926601
VERSION     WP_009926601.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
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   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   4  (residues 1 to 328)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..328
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=36646
     Region          1..318
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mirfdnvskk ysddktaavn nvtldikdge ffvfigpsgc gktttlkmin rliplttgti
       61 yinekrisdy dihelrwdig yvlqqialfp hmtieeniai vpelkkwske kihdritell
      121 dsvgldpesy rhrkpaelsg geqqrvgvvr alaadpgiil mdepfsaldp isrqrlqqdi
      181 salqkkikkt ivfvthdmqe alalgdricv mqggeivqva tpqeimknpe ndfvkdflas
      241 ghafntpile anftvndlie adlfysyqts dgtlgisste pvenlvrria eeqsipvtde
      301 agnyigtvsn khvmqflarh lessgelv
//
LOCUS       WP_009926990             343 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Listeria monocytogenes].
ACCESSION   WP_009926990
VERSION     WP_009926990.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..343
                     /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=40260
     Region          4..276
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mtqsalkres yfdnakfili flvvfghflq tfiadyagvr vlyiyiytfh mpafvlisgf
       61 faksfgkpgy lkktmkklil pyvffqliys ifyyfllskd nlsiqlldpe wslwfllslf
      121 fwnvmlsifa kikpwksisi alfvglvagy fdiiggylsl srtlvffpff lvgyflkkeh
      181 fyylkthfvm ilggifivll lsfitfhpnl ndkwflgskp yanfvevksl glfiralvyl
      241 isfgsiaaff sfiprkrlff tkwgkntlyv yllhgffikf fregsqtdfq yspstflllf
      301 vvtfvltvll ssrlvkifvq pvielrvsml rdvfsrltkr esy
//
LOCUS       WP_009929344             571 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Listeria
            monocytogenes].
ACCESSION   WP_009929344
VERSION     WP_009929344.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 571)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..571
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=63883
     Region          2..552
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 midkrlfqlv ekkslvllil frvlslglmi glwlvfaqql thyleaqsvd wlwligtvlv
       61 vlvgkailtk laekqiyqas aelrlsmrra vmekafrlgn negqlpastl tqlavdgieq
      121 leiyysrflp qlfycliasl mifgslvgfa wqpaivllic mpmipivima vmkiakrils
      181 gywsdytnlg tkfhenlsgl silkayeqdk ykqeeivsda erfrkatmsl lsmqlnsiti
      241 mdiisysgaa lgigmslimf tngnismtgm lmflllsaef fipmrqlgsl fhvamngisa
      301 csklfaylel keqvygsvel akplekmevr hltytyeegk akalqdisvn fnkgsfsalv
      361 gksgsgkstf vrvllnqlpg yqgeivwndv plaslsgeti rkqavlvdnh gylyansire
      421 nllignpaan dsdlwnvleq vsladfvrkl peqlnenlee ngsnlsggqr qrlllarall
      481 cqaevfvfde itsgvdlese kiillvlqkl akekivlfis hrlynvldad qvlvfdagkl
      541 vevasperlq qesnyfknyf leeeallkgg a
//
LOCUS       WP_009930007             297 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Listeria
            monocytogenes].
ACCESSION   WP_009930007
VERSION     WP_009930007.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
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
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..297
                     /product="aminoglycoside 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=34434
     Region          14..232
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mdvtqlkmlh nakviseink gfsvdrkyqv detylvrvfp idllqereqe fkiiqaldsq
       61 tpfvpkaydf gfieregymi isylrgedae igmtrlshse qlkagfsage ilrevhkipl
      121 aipkmnwldf qtvkferkvk elkeleitas fltdtekfvn eniarlnnrp iclqhgdfhp
      181 aniilnnkkf vglidfnrle fgdplfdlak igffttevsi pfargnilgy idkeevtdfw
      241 nlyalytamh itsavnwaak nesrnfkklm dyaaktvash dnfqrivpnw mneeefk
//
LOCUS       WP_009932194             171 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding
            protein, partial [Burkholderia pseudomallei].
ACCESSION   WP_009932194
VERSION     WP_009932194.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 171)
  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 171)
  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   3  (residues 1 to 171)
  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   4  (residues 1 to 171)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 171)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 171)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 171)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..>171
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          32..>171
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mnikmqkllp isaaamllaa aatnaaadqv vkighvaplt ggiahlgkdn engarlavee
       61 inakgltigg qkvtlqldaq ddaadprtat qvaqklvddk vvavvghlns gtsipaskiy
      121 sdagivqisp satnpaytqq gfkttyrvva tdaqqgpala nyarskgvks v
//
LOCUS       WP_009932812             397 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Listeria monocytogenes].
ACCESSION   WP_009932812
VERSION     WP_009932812.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43002
     Region          3..388
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mhkimainag ssslkfqift mpgeevlvkg lieriglpda ifnmsfqnek iketraindh
       61 gkaveilleq lkahqvindl seitgvghrv ahggedfvts cvvtdevvkg ieavtnlapl
      121 hnpaniigik tfrellpnav svavfdtafh qtipqenfly alpyelyekh hirkygfhgt
      181 shkyvagkaa evlekplekl kiischlgng asvcaieagk svntsmgftp naglmmgtrs
      241 gtidatiipy lvdelgysld evmhmmsnes gvlgvsgiss dfrdieiaak egnsralltl
      301 rmftgqicny igayasamng cdallftagv gensplirqm vteqlsylgv tchvtknnag
      361 dmiisndnea vkvciiptne elmiardvek yakqtig
//
LOCUS       WP_009933455             311 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Burkholderia
            pseudomallei].
ACCESSION   WP_009933455
VERSION     WP_009933455.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..311
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32949
     Region          26..273
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 messnrpart heasaatllv dcrnalgega twcdaahaly wvdiegarlw rwraagahgg
       61 ercdswempe riaccaltgd pdvllvglas rlaffdtrrr altpivdvep drptrlndgr
      121 cdragafvfg tkdesggasp raiggyyrln adlslqrlal ppatiangia fspdgsamyf
      181 cdsptreiqv cdyrpggdvd rvrsfvrlad ahgepdgstv dasggvwnaq wggarvvryd
      241 aqgvetdria vptpqpscvt ldaagrlyvt sarvglddga lagnsgaggv fvahtrhpgg
      301 atprfalarh a
//
LOCUS       WP_009935055             350 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia pseudomallei].
ACCESSION   WP_009935055
VERSION     WP_009935055.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 350)
  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 350)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 350)
  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   4  (residues 1 to 350)
  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 350)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..350
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39147
     Region          33..216
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          264..342
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtrrstkdnl glrrptipva ylrhlltvfe ergidardar agtglrddvl gepdariaps
       61 qwgrlvlnai rlsgdegigf elglrlrmsv hgflgyaalt aadlrasllv naryfrmrnr
      121 qyrlhyaerd dgatlslhgv qaspvlqhha mfeivltgia qnvgtvagra dppielqfaw
      181 pepdyyaryr drlppvrfgc aanavwvsrd aldwplplad dvahrqalaq vereyadvrh
      241 eegdlvarvr aeltltahgy pgpdalarhl lmstrtlrrr lldagcgyra lvdearlrda
      301 rrllrasdld lktiaarlqf ndpanftraf rkwtgltpsa yreagggder
//
LOCUS       WP_009935270             318 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 5'-3' exonuclease [Mycobacterium].
ACCESSION   WP_009935270
VERSION     WP_009935270.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium
  ORGANISM  Mycobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Mycobacterium"
                     /db_xref="taxon:1763"
     Protein         1..318
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33892
     Region          1..309
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mrsplvlldg asmwfrsffg vpssitapdg rpvnavrgfi dsmavvitqq rpnrlavcld
       61 ldwrpqfrvd lipsykahrv aepepngqpd veevpdeltp qvdmimelld afgiamagap
      121 gfeaddvlgt latrerrdpv ivvsgdrdll qvvaddpvpv rvlylgrgla katlfgpaev
      181 aeryglpahr agaayaelal lrgdpsdglp gvpgvgekta atllarhgsl dqimaaaddr
      241 kttmakglrt kllaasayik aadrvvrvat dapvtlstpt drfplvaadp ertaelatrf
      301 gvessiarlq kaldtlpg
//
LOCUS       WP_009943065             393 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein, partial
            [Saccharopolyspora erythraea].
ACCESSION   WP_009943065
VERSION     WP_009943065.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora erythraea
  ORGANISM  Saccharopolyspora erythraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
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   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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Saccharopolyspora erythraea"
                     /db_xref="taxon:1836"
     Protein         <1..393
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          1..386
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 aqgfadsrpa gevnrrhlqr algrtkllql dsvnvavrah ympvysrlga ypadlvddaa
       61 wshrtrrprl lveywaheas lipvedwpll rwrmreygga wrrkfrtlle rapqlvddvl
      121 aavkdlgpig agalerelgg gqkqgtgpww nrtdtkhace llfamgeltt garrgferly
      181 dlpervlpad vlaadpeddv airglversa qalgvgtesd lrdyyrlspa qskqavaelv
      241 edgvlepvtv rgwrqpayrh aearvprkvt grallcpfdp liwersrter lfgfryriei
      301 yvpepkrqyg yyvfpflldg rlvarvdlka drtagvlrvp gafaepgadl asvvpelaga
      361 lgdmaswlgl ggvavgergd latalrtttr gdg
//
LOCUS       WP_009955164             237 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease family protein [Mycobacterium avium
            complex (MAC)].
ACCESSION   WP_009955164
VERSION     WP_009955164.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium avium complex (MAC)
  ORGANISM  Mycobacterium avium complex (MAC)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Mycobacterium avium complex (MAC)"
                     /db_xref="taxon:120793"
     Protein         1..237
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=25128
     Region          89..230
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mnrkvllwla aaaalavvva yqtvgtsasr hsaeyaarad vptvlpgvdv lagiavvpvr
       61 lhrydylraa fgdawdddnd aplghngcdt rddilnrdlv dktyvsikrc pdavatgtlh
      121 dpytnktiaf argpkvgesv qidhivplay awdmgaygwp aperlrfand panllavdgp
      181 anqdkgdspp gqwmppngaf acqyamqfia vlrgyalpvd aastgvlrqa aascpag
//
LOCUS       WP_009953981             246 aa            linear   BCT 20-JAN-2025
DEFINITION  AAA family ATPase, partial [Mycobacterium intracellulare].
ACCESSION   WP_009953981
VERSION     WP_009953981.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium intracellulare
  ORGANISM  Mycobacterium intracellulare
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Liu,Y., Sung,S., Kim,Y., Li,F., Gwon,G., Jo,A., Kim,A.K., Kim,T.,
            Song,O.K., Lee,S.E. and Cho,Y.
  TITLE     ATP-dependent DNA binding, unwinding, and resection by the
            Mre11/Rad50 complex
  JOURNAL   EMBO J 35 (7), 743-758 (2016)
   PUBMED   26717941
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Chen,Z., Luong,T.T. and Lee,C.Y.
  TITLE     The sbcDC locus mediates repression of type 5 capsule production as
            part of the SOS response in Staphylococcus aureus
  JOURNAL   J Bacteriol 189 (20), 7343-7350 (2007)
   PUBMED   17704228
REFERENCE   3  (residues 1 to 246)
  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   4  (residues 1 to 246)
  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
REFERENCE   5  (residues 1 to 246)
  AUTHORS   Hopfner,K.P., Karcher,A., Craig,L., Woo,T.T., Carney,J.P. and
            Tainer,J.A.
  TITLE     Structural biochemistry and interaction architecture of the DNA
            double-strand break repair Mre11 nuclease and Rad50-ATPase
  JOURNAL   Cell 105 (4), 473-485 (2001)
   PUBMED   11371344
REFERENCE   6  (residues 1 to 246)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Mycobacterium intracellulare"
                     /db_xref="taxon:1767"
     Protein         1..>246
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          2..>143
                     /region_name="SbcC"
                     /note="DNA repair exonuclease SbcCD ATPase subunit
                     [Replication, recombination and repair]; COG0419"
                     /db_xref="CDD:440188"
ORIGIN      
        1 mklhrliltn yrgishreie fpdhgvvvvc ganeigkssm iealdllles rdrstkkevk
       61 qvkpthsdvg sevsaeiscg pyrfvyrkrf hkkcetelti itpcreqltg deahervram
      121 laetvdsdlw haqrvlqsas taavdlsgcd alsraldvaa gdsgglcgte pllieridte
      181 yaryftptgr ptgqwaaaia rladaeaava ecaaavaevd drvarhavlt eqvadfsqrr
      241 iaagpr
//
LOCUS       WP_009955237             403 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Mycobacterium
            intracellulare].
ACCESSION   WP_009955237
VERSION     WP_009955237.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium intracellulare
  ORGANISM  Mycobacterium intracellulare
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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 403)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Mycobacterium intracellulare"
                     /db_xref="taxon:1767"
     Protein         1..403
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44428
     Region          1..401
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mstrrlsaaq arriavaaqg fteprpggei trahlkrlis riqvlqldsv svavrahyap
       61 vfsrlgpydr dvldraawgp rssrllaeyw aheaalmave dwpllrwrmr qyrhgrwgth
      121 ivkanprlae kvvaavaelg pstagqieeh laagprgprg swwgsrsdtk wvaealfsag
      181 vlttatrvgf arhydlverv lpaavlarev dddealrelt lraatalgvg teadirdyfr
      241 lsaaqvkpai aqllaagdie rvdvdgwsap aylragrtvp radrgtallc pfdpliffrp
      301 rverlfefhy rieiytpaak rqygyyvwpl lmdgrlvarv dlkadrpadr lrvvgafaep
      361 dtpkarvaaa lagelrsmas wlglggfsvs grgdlaadlr ais
//
LOCUS       WP_009956135             367 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Mycobacterium intracellulare].
ACCESSION   WP_009956135
VERSION     WP_009956135.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium intracellulare
  ORGANISM  Mycobacterium intracellulare
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Mycobacterium intracellulare"
                     /db_xref="taxon:1767"
     Protein         1..367
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38571
     Region          5..362
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mselqlravv adrqvdvefs vsagevlavl gpngagkstv lhviagllrp dhgtvrlgdr
       61 vltdtaagid vpthdrrvgl llqdallfph mtvaanvafg phsrraslrp aratqkatas
      121 rwlrevdaer ladrkprqls ggqaqrvaia ralaaepdvl lldeplagld vaaaaairav
      181 lrevvtrsgc aailvthdll dvftladrvl vlesgkvaei gpvpdvltap rshfaariag
      241 vnlvngtvdr dgslvavggd rwyaapperg elvsheqhai avfaptvvav yrdrphgspr
      301 navevtvaem dvrgsavlvr gaqqpdgapg laaeitadaa aelrlapgdr vwfsvkahev
      361 tlypaah
//
LOCUS       WP_009954521             304 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Mycobacterium
            intracellulare].
ACCESSION   WP_009954521
VERSION     WP_009954521.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium intracellulare
  ORGANISM  Mycobacterium intracellulare
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Mycobacterium intracellulare"
                     /db_xref="taxon:1767"
     Protein         1..304
                     /product="formate/nitrite transporter family protein"
                     /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=31349
     Region          38..298
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mtinapaqpl pssatagtvt alptgvvttd rapedpfepl tvgamvdrva amavekaahp
       61 waflmrslvg gvmvafgall alvvstgvkt pgvasllmgl afgmsfvlil vsgmslitad
      121 maagflavlk rtlsvgnyal lvtvgligni agalifvtic aaaggpylga faeraatvgt
      181 lkagqpfwta lllavvctwf lqtsmcmffk arsdvarmtf afygpfafvi ggtqhvianv
      241 gflglpllln lfhptaprga igwgfgahgl ltnigittvg nliggtvfva lpfwiiarlq
      301 hrqi
//
LOCUS       WP_009956298             837 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Burkholderia pseudomallei].
ACCESSION   WP_009956298
VERSION     WP_009956298.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 837)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 837)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 837)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..837
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=92042
     Region          52..835
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 msirhatrsv alcsmlalas tlgctsgahd apaahaprta qtahatavaa giaglrepvr
       61 ivrdsvgvsh iyarnthdlf faqgynaard rlwqldlwrr qgegkmaeqf gprfaaqdra
      121 arlflyrgdl eaeyasyhpe akqilqafad ginayvreak adpakmppef rltgaepgew
      181 rpessliriy gitrnvtgev alarqvaavg lskalslnaf eppvrqtaip agvdvglidk
      241 riladyllar nglpfraedf prsplgaaqr dalaarlnaa rltladdsan plapryesnn
      301 wvvagartas gkpllandph rrigmpslry mvhlhapgwn vigagepalp gvsvghndrv
      361 afgltifafg deedlyvydt rpghpdeyry rgrwekmriv eetvavrgqa nrverlaftr
      421 hgpvlyedaa hrkayalraa ylefpgtaay laslrldqar dwpsfvagmr rhyvpgenmv
      481 yadvdgnigw fggalapirr eadwsgalpv pgdgryewag ltegealphv lnpaagyiat
      541 anaydlpdgy ryvdrsahvw aepfrqrrld evlrgasglt vadmqrlqyd drslpaqaml
      601 gfasqlkade pgtrdalarl arwsgdmaid svpatiyefw mrevmrrvrd vevpaaarda
      661 fpklevrqvl rylrqpdgaf gadpvagrda lllaalrdgl anaraklgen vdawrwgrlh
      721 haqfdhqlag vlpefgafgt eryavggndd tvhrgtyrps dfrqtsgasy rqvidvadwd
      781 rsmiqntpgq sgdprspfha nllkgwasge ywpmafsdra vdalahdtli lepapaq
//
LOCUS       WP_009956730             364 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Mycobacterium intracellulare].
ACCESSION   WP_009956730
VERSION     WP_009956730.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium intracellulare
  ORGANISM  Mycobacterium intracellulare
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Wilkens,S.
  TITLE     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   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   4  (residues 1 to 364)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Mycobacterium intracellulare"
                     /db_xref="taxon:1767"
     Protein         1..364
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=38551
     Region          1..299
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
     Region          <243..361
                     /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 mitfdevskv fgdgttavdr lnlevpsgkl tvfvgssgsg kttalrminr mieptsgtia
       61 idgvdvatrd pvklrlgigy viqhaglmph qrvidnvatv pvlrgqsrra arkagyevle
      121 rvgldvklar rypaqlsgge qqrvgvaral aadppillmd epfsavdpvv rhelqneilr
      181 lqsdlhktiv fvthdideal rlgervavfk ggslqqydep arllsrpand fvsrfiglgr
      241 gyrwlqrlda aglplhdvar itpetlsgag lsdgwavvvd gggaplgwid aegarrhrdg
      301 aplsdcmsga gslfrprgnl sqaldaalss psgvgiavdd ggkviggvla advlaavesq
      361 rgsr
//
LOCUS       WP_009959870             555 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Verrucomicrobium spinosum].
ACCESSION   WP_009959870
VERSION     WP_009959870.1
KEYWORDS    RefSeq.
SOURCE      Verrucomicrobium spinosum
  ORGANISM  Verrucomicrobium spinosum
            Bacteria; Pseudomonadati; Verrucomicrobiota; Verrucomicrobiia;
            Verrucomicrobiales; Verrucomicrobiaceae; Verrucomicrobium.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Verrucomicrobium spinosum"
                     /db_xref="taxon:2736"
     Protein         1..555
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=58852
     Region          10..555
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mttaatapsi lrihpaddli valrplqage qvsldgqswi lrhkvgakhk faardfakda
       61 lvtlygvtvg rakvaiaage lvhthnlqha tagfsgkqrd tawtpptlsn wsrttfngyk
      121 rpgtragtan cwlviplvfc enrnlafmke alqkalgygr tgpyehyare lvglhqrgaa
      181 rqeieestla lgtrphtpvp lfphldgvkf lehdmgcggt rldaealcnl lagyvahpnv
      241 agatvlslgc qhaqvslleq alekfhpgys rplhifeqqk alseqdmmar aikttflgmr
      301 danelrrepc pvsdlvvgve cggsdgfsgi sanpaighta dllvalgasv alsefpelcg
      361 ieqelsdrcv naaladrfvh lmrtyeraaq acgsgfdanp spgnirdgli tdaiksagaa
      421 kkggtspitd vldyaepitk pglslvctpg ndvesttaia gagctvilfs tglgtptgnp
      481 icptlkiatn telaqrmgdv idfdtgpiir geksvltmge ellaltldta sgitvpkavs
      541 lgqddfipwk rgvsl
//
LOCUS       WP_009959549             726 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Verrucomicrobium spinosum].
ACCESSION   WP_009959549
VERSION     WP_009959549.1
KEYWORDS    RefSeq.
SOURCE      Verrucomicrobium spinosum
  ORGANISM  Verrucomicrobium spinosum
            Bacteria; Pseudomonadati; Verrucomicrobiota; Verrucomicrobiia;
            Verrucomicrobiales; Verrucomicrobiaceae; Verrucomicrobium.
REFERENCE   1  (residues 1 to 726)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..726
                     /organism="Verrucomicrobium spinosum"
                     /db_xref="taxon:2736"
     Protein         1..726
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=80107
     Region          35..726
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mkhqtilava smgilplgaq qpstpppapt atlpevtvtg tkespsltvp sveaarenla
       61 rtpgntsvvd aeeyrigrss sfedvfksvp gvyapargsd gdevklsirg sgldlgyhlr
      121 gikilqdgvp vsladgfgdf qsidplslry veiwrgsnal rygsttlgga vnfvsptgyd
      181 adpfrvrfea gsfnyynaql sgggvsgpld yyvsgsfmsr egfqehsqmd nerfygnfgy
      241 risddletrf fltyvrsrsd lpgnltksei enspraadpd aiafdqgrdv dwfrianktt
      301 lkldethrle gslyythfel dhplfwnpyf lnglgvrigt ydsfggelry lseedwlgrk
      361 nrftlgftpa vtflhderle ndfgrhgphv adgdftavny dlyaeeqhyl tdklsvlvgs
      421 sftysvrnfd dnfnsdpngd qsrdqdyygf spklgllyev spqsqffanv srsfepptav
      481 etvglggpsg dvltrdidaq tattvevgtr geagrfkwel ayyyswlnde lltvndaagn
      541 plgtvngpdt hhqgvelgld ailwqsspap vvtsakspka vapvqlqggd kltlkqvfnw
      601 ndfrfddsda ygdnhlagap effyraelll elsngiyfgp nfqwvsrvpa dyanslyads
      661 yailgvrlgy rsskgwtifa earnltdeny assaepiada rtafgparvf hpgepvsfyg
      721 gfewkf
//
LOCUS       WP_009956440             137 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein [Mycobacterium].
ACCESSION   WP_009956440
VERSION     WP_009956440.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium
  ORGANISM  Mycobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Mycobacterium"
                     /db_xref="taxon:1763"
     Protein         1..137
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=15243
     Region          25..>77
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
     Site            51..52
                     /site_type="other"
                     /note="putative proton transfer pathway, P2"
                     /db_xref="CDD:238138"
ORIGIN      
        1 mtteahttli kltgtvvkvk natddmrgrq vkdndhkhfg rvhdvfvddr erkprfllvd
       61 hggllgvgek kslvpvdvit attsddvfvg dahdhicgap ayeaelvndr dyqsrvcgyy
      121 gclpywssgy vypsfnr
//
LOCUS       WP_009960795             625 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Verrucomicrobium spinosum].
ACCESSION   WP_009960795
VERSION     WP_009960795.1
KEYWORDS    RefSeq.
SOURCE      Verrucomicrobium spinosum
  ORGANISM  Verrucomicrobium spinosum
            Bacteria; Pseudomonadati; Verrucomicrobiota; Verrucomicrobiia;
            Verrucomicrobiales; Verrucomicrobiaceae; Verrucomicrobium.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 625)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Verrucomicrobium spinosum"
                     /db_xref="taxon:2736"
     Protein         1..625
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68392
     Region          2..625
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mqhndtsksw plalaalgvv ygdigtsply alreclgegr flstdpvtvl gpvslmlwsf
       61 ilivsvkyll mltratnqge ggvfallsil kqpvaglssk aiswlglfai lgaalmygdg
      121 vitpaisvls aveglkeidp hfeqyivpva vvillgvffv qrhgthriga sfgpvmvvwf
      181 lvlagtgmvn vvehpaalka lsphygvryi lehghhgvgi mgsvllcvtg cealyadigh
      241 fgatamrrsw fllagpalsl nymgqaglvl anpeahgnpf yrmvpggwlv pmvilatmat
      301 iiasqamitg vfsltqqavq lgylprlkik htnpdlrgqi ympqintllc vaclalvvgf
      361 essgalaaay glsvsanmvl stilfyavav rvwkwslwka lvpvvaflll ecsyvagslt
      421 klfhgawmpv latvvlwivm ktwqdgrail wrlvkqgqlp tehliaelen nritrvkgtg
      481 vfmsgtadgl plvllhhlkh nkalhervvl ltiqfheepy vkeekrvsai elapkfhrvv
      541 lhygfvespd vmrdlchalq fkkihemsni sfyqarelll ptgrgkmaew rkklfvslsr
      601 aarpatgyfd lpsrqvielg iqmel
//
LOCUS       WP_009961899             730 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Verrucomicrobium spinosum].
ACCESSION   WP_009961899
VERSION     WP_009961899.1
KEYWORDS    RefSeq.
SOURCE      Verrucomicrobium spinosum
  ORGANISM  Verrucomicrobium spinosum
            Bacteria; Pseudomonadati; Verrucomicrobiota; Verrucomicrobiia;
            Verrucomicrobiales; Verrucomicrobiaceae; Verrucomicrobium.
REFERENCE   1  (residues 1 to 730)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Verrucomicrobium spinosum"
                     /db_xref="taxon:2736"
     Protein         1..730
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=80731
     Region          24..730
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mkhtpsllll lagvlpsqls hgqtpatsvr tttelptvtv tatpesltvp tiaqaeqela
       61 lvtggasvvn aedykkgrav tlkdaldfat gvftqprfgt eearisvrgs giqrtfhgrg
      121 lkvlqdgvpi nladggfdmq sieplaadyi evyrganalr ygsttlggai nfvsptgyta
      181 pafqgrfeyg sfntfrgqls aadvlgnldy yatvthyste gfrdhsdqnt qrffsnvgyk
      241 fsedvetrff ltyvhtdsel pgnltkeelr nhpdraqrna fakqfdyids dwqrnfelfr
      301 ianrttwnlg edqqlsfssf yaykdldhpi lfvidqvshd fgfdlnylnn adlgghknhf
      361 iagisptfgl lddvrfanvl gergakfaqn yqqstnvdfy iedlyyltdr favsvggqis
      421 yarrdnedrf pvsatnpdns dvqdwwgysp kvgllyelte saqlffnasr sfeppsfgel
      481 snsalggagl veleaqtatt leigtrgksa nnrvkwdiay yfswiddeml elsvapglnq
      541 tinagrtihq gvelgldvtl legifargtv apapalasak gakavqplaa papqdrlvfr
      601 qnylyngfrf dndkefgdnq lagvpehyyr aelvyehpsg fylgpnlewv fndypvdfag
      661 tlsadsyail gfkvgyrtak glsiyvdarn ltdehyaatt gvinragafn qaqflpgdgr
      721 sfffgveykf
//
LOCUS       WP_009963439             240 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Verrucomicrobium spinosum].
ACCESSION   WP_009963439
VERSION     WP_009963439.1
KEYWORDS    RefSeq.
SOURCE      Verrucomicrobium spinosum
  ORGANISM  Verrucomicrobium spinosum
            Bacteria; Pseudomonadati; Verrucomicrobiota; Verrucomicrobiia;
            Verrucomicrobiales; Verrucomicrobiaceae; Verrucomicrobium.
REFERENCE   1  (residues 1 to 240)
  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 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   3  (residues 1 to 240)
  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   4  (residues 1 to 240)
  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 240)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Verrucomicrobium spinosum"
                     /db_xref="taxon:2736"
     Protein         1..240
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28121
     Region          1..239
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <135..240
                     /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 mrqispdsaf hrlfdhmpev sffakdrefr fiaasrrfye rfgfteerqi ighndfdifp
       61 trlaenfrkd devvistgqp klnimelfft qqgipdwfvt nklplfnreg qpigimgsvq
      121 syegrkqvmq pylqldkavn yirqhfrtgv tiselaelvh lsprqlhrkf vetfgsspqa
      181 fimklriqaa cealqhedrq isevamemgf cdqssftqqf qkhvgltpmr yqrqfrlrag
//
LOCUS       WP_009962785             351 aa            linear   BCT 20-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein
            [Verrucomicrobium spinosum].
ACCESSION   WP_009962785
VERSION     WP_009962785.1
KEYWORDS    RefSeq.
SOURCE      Verrucomicrobium spinosum
  ORGANISM  Verrucomicrobium spinosum
            Bacteria; Pseudomonadati; Verrucomicrobiota; Verrucomicrobiia;
            Verrucomicrobiales; Verrucomicrobiaceae; Verrucomicrobium.
REFERENCE   1  (residues 1 to 351)
  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 351)
  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 10478448
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Verrucomicrobium spinosum"
                     /db_xref="taxon:2736"
     Protein         1..351
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=36656
     Region          23..151
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          108..151
                     /region_name="LysM"
                     /note="LysM domain; pfam01476"
                     /db_xref="CDD:396179"
     Region          205..351
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          304..348
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
ORIGIN      
        1 mndksnlspt rrlfasesfr rhyvsaveng dqadwtereq sgnlgrvfvf llllhvflig
       61 aivlynivsd rpkvsvaasm gkaapalpgd ttetstgslv krselseyqv rsgdtvqsia
      121 datgatteei irlnqldqng elyvsrrlql plrkevadev papaaavalt sgqtsrettv
      181 aaakevsgka gkgqpesfka avvgesagtk sksgeshpap tlikakpvtl qdappadarv
      241 akledsppag kagsggstqk atpvspvklq eappkekpap katpvvaata kekpaptaat
      301 gggrsyeikg gdtfysiark nginvndlik anpgtnpsrl kkgmmikipa k
//
LOCUS       WP_009963461             381 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Verrucomicrobium
            spinosum].
ACCESSION   WP_009963461
VERSION     WP_009963461.1
KEYWORDS    RefSeq.
SOURCE      Verrucomicrobium spinosum
  ORGANISM  Verrucomicrobium spinosum
            Bacteria; Pseudomonadati; Verrucomicrobiota; Verrucomicrobiia;
            Verrucomicrobiales; Verrucomicrobiaceae; Verrucomicrobium.
REFERENCE   1  (residues 1 to 381)
  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   2  (residues 1 to 381)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Verrucomicrobium spinosum"
                     /db_xref="taxon:2736"
     Protein         1..381
                     /product="aminoglycoside 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=42132
     Region          72..319
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mnattitssa ppanaadlvs pshrrttyyw kcdrpaafhg ttgrtdagtl qsalkqalqe
       61 kfpsarlsle pghgqgnhit fiatvdearr fvrvedgpek dnylivesrv lhevrtlglp
      121 aprvhavdas resvpfawqm ldlvdapdln hfqkkgeldl prmageigaa iarwqcaepa
      181 gygpfdpaqv metntlcgfh asyedyfflh ferhlrylth qqllssreaa eiesevllhr
      241 pllalnqgcl vhkdlalwni lgtpegvaaf idwddaisgd amddlsllac fhdgpvlara
      301 legyqmlrpl ptehrrrfwl hllrnmivka virvgagyfe ksdgffligs gssgqnlqtf
      361 ttqriasalq glrgdlpvas l
//
LOCUS       WP_009964154             227 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Verrucomicrobium spinosum].
ACCESSION   WP_009964154
VERSION     WP_009964154.1
KEYWORDS    RefSeq.
SOURCE      Verrucomicrobium spinosum
  ORGANISM  Verrucomicrobium spinosum
            Bacteria; Pseudomonadati; Verrucomicrobiota; Verrucomicrobiia;
            Verrucomicrobiales; Verrucomicrobiaceae; Verrucomicrobium.
REFERENCE   1  (residues 1 to 227)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Verrucomicrobium spinosum"
                     /db_xref="taxon:2736"
     Protein         1..227
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24624
     Region          51..179
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(139..140,143,153..156,158)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mslpsqlpkf vilafaglsa lglsscktlq vakqddydsp ayrpqslsnv rvkvslnkqm
       61 vyvmegdkpl lvtatcvgtp snptpkgnft vykkiekkrs msygfavqgn aitpvkatsm
      121 rggryvgypm pywvefspay gfhqgyvwnv prshgclrlh knvapkffal trlgtpvnia
      181 nsqpedstlg asatrpgpeh ylapdppnsv liteaafkap dkplfan
//
LOCUS       WP_009968524             353 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Burkholderia pseudomallei].
ACCESSION   WP_009968524
VERSION     WP_009968524.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 353)
  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 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   3  (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   4  (residues 1 to 353)
  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 353)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..353
                     /product="CmpA/NrtA family 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=37716
     Region          14..260
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mntarikaaa admperarlr igfvalsdaa plvaaqrlel garygltlel crqpswasir
       61 dkllsgelda ahalyglvyg vqlgiggpra dlavpmvlnr ngqaitfsnr ladayrasge
      121 lkaalatlgr rpvfaqtfpt gthamwlyhw lashgvdplh dvrsvvippp emvdalaage
      181 ldglcvgepw navaeargag rtvaatsevw pdhpekalac rrefvalypn aarllvrtll
      241 dacawlddpa hrmqaarwla qpdtigvpve qiaprllgdy gagpfaqppa pirfhahgta
      301 nrpaasdglw flsqyrrwgm lsgdvddaai angvahtaly deavalggar rge
//
LOCUS       WP_009970543             282 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein, partial [Burkholderia
            pseudomallei].
ACCESSION   WP_009970543
VERSION     WP_009970543.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
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
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..>282
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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]"
ORIGIN      
        1 mieiervsrl fgdlaavddv slavargtvt alvgasgsgk stllrminrl iaptsgtirv
       61 dgvdtasvpa etlrrgigyv iqghglfphw tvarnvatvp rllgwraarv darvrellel
      121 feldydtyar klphqlsggq qqrvgvaral aaepaillmd epfgaldpii rgkaqddlva
      181 lqrrlgitvv ivthdideal rlgdqiavmd agrilqagsp aeilgrpqpg vverlvagld
      241 rplrllaltr vdalaepgaa pgepisgalt lrdaisellw rg
//
LOCUS       WP_009971079             263 aa            linear   BCT 20-JAN-2025
DEFINITION  MJ0042-type zinc finger domain-containing protein, partial
            [Burkholderia pseudomallei].
ACCESSION   WP_009971079
VERSION     WP_009971079.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 263)
  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 10020205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..>263
                     /product="MJ0042-type zinc finger domain-containing
                     protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
ORIGIN      
        1 mllatrcphc etvfrlqreq lalhdglvrc ghcqqvfdaa ralvptepea aaaqaaprap
       61 eqpaarrlfd atspdrrple aghrdftpga wdmrgpwldg aidpklqmts asvstaagga
      121 vaahaaahet rnaaadtpaq easkasdals vseasqasra sdtsthdtlp vpetpetpag
      181 gtpapgerpa hawpeanaga pairpsdadl phagarefap pprptldldl drsatakhkp
      241 dtarasaspp gdavepmlas haa
//
LOCUS       WP_009974921             837 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Burkholderia pseudomallei].
ACCESSION   WP_009974921
VERSION     WP_009974921.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 837)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 837)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 837)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..837
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=92031
     Region          52..835
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 msirhatrsv alcsmlalas tlgctsgahd apaahaprta qtahatavaa giaglrepvr
       61 ivrdsvgvsh iyarnthdlf faqgynaard rlwqldlwrr qgegkmaeqf gprfaaqdra
      121 arlflyrgdl eaeyasyhpe akqilqafad ginayvreak adpakmppef rltgaepgew
      181 rpessliriy gitrnvtgev alarqvaavg lskalslnaf eppvrqtaip agvdvglidk
      241 riladyllar nglpfraedf prsplgaaqr dalaarlnaa rltladdsan plapryesnn
      301 wvvagartas gkpllandph rrigmpslry mvhlhapgwn vigageptlp gvsvghndrv
      361 afgltifafg deedlyvydt rpghpdeyry rgrwekmriv eetvavrgqa drverlaftr
      421 hgpvlyedaa hrkayalraa yleypgtaay laslrldqar dwpsfvagmr rhyvpgenmv
      481 yadvdgnigw fggalapirr eadwsgalpv pgdgryewag ltegealphv lnpaagyiat
      541 anaydlpdgy ryvdrsahvw aepfrqrrld evlrgasglt vadmqrlqyd drslpaqaml
      601 gfasqlkade pgtrdalarl arwsgdmaid svpatiyefw mrevmrrvrd vevpaaarda
      661 fpklevrqvl rylqqpdgaf gadpvagrda lllaalrdgl anaraklgen vdawrwgrlh
      721 haqfdhqlag vlpafgafgt eryavggndd tvhrgtyrps dfrqtsgasy rqvidvadwd
      781 rsmiqntpgq sgdprspfha nllkgwasge ywpmafsdra vdalahdtli lepapar
//
LOCUS       WP_009975423             215 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Mycobacterium avium].
ACCESSION   WP_009975423
VERSION     WP_009975423.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium avium
  ORGANISM  Mycobacterium avium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Mycobacterium avium"
                     /db_xref="taxon:1764"
     Protein         1..215
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23948
     Region          19..205
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mnveylltat psarksldld apvepgdire clriglqaan gsnaqswrwl vvsdpalrar
       61 iaelyrdayl rrvggrllag lmpagtpesr imsstewlve nlarvpmlvi pcyepylpri
      121 dgdesfhlat lygsifppvw nfqlalhtrg ygtcittlhl hhedqvaqll gipptyvqgc
      181 llpvgrlrag rtfrparrrp iqeviacdrw dgppl
//
LOCUS       WP_009978006             412 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Mycobacterium
            avium].
ACCESSION   WP_009978006
VERSION     WP_009978006.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium avium
  ORGANISM  Mycobacterium avium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 412)
  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 412)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Mycobacterium avium"
                     /db_xref="taxon:1764"
     Protein         1..412
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45188
     Region          12..411
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mspgggivga vstrrlsvaq arriavaaqg fteprpagav trahlnrlis kiqvlqldsv
       61 svtvrahyap vfsrlgpydr evldraawgp rssrllveyw aheaalmave dwpllrwrmr
      121 qyrhgrwgth ivqanprlad avvaavaelg pstagqieah laaeprrrkg awwnrsdtkw
      181 vaealfaagv lttatrvgfa rhydlvervl padvlarrvd ddeaireltl raagalgvgt
      241 eadirdyfrl saaqvkpaia elvaagdler vevagwpapa ylragravpr tdrgtallcp
      301 fdpliffrpr verlfefhyr ieiytpaakr rygyyvwpll mdgrlaarvd lkadraegtl
      361 rvlgafaepq aprprvaaal agelwsmasw lglgglsvad rgdlapalra va
//
LOCUS       WP_009979609             314 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia pseudomallei].
ACCESSION   WP_009979609
VERSION     WP_009979609.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 314)
  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 314)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 314)
  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   4  (residues 1 to 314)
  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 314)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..314
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34009
     Region          35..186
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          214..295
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msfeplfadg garlqrrila lfgqlapneg ythaaidgvr firsnrpvpr mpvlydssiv
       61 vvcqgrkrgy vgersfvyda qqylvlsvpl pfecetfatp depflaisir idlaviaela
      121 illdethgas vseprgiyst pldapladav lrllealasp adtrvlgpai mreigyrvlt
      181 gaqgdairaa laqqhhfgrv aralrrihad lsgeldvetl aseagmslav fhaqfksvta
      241 tspmqyvkat rlhharlmmv qdglnagaaa arvgyasasq fsrefkrlfg rspsdevrwv
      301 qaggrqpval eage
//
LOCUS       WP_009981038             392 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Burkholderia pseudomallei].
ACCESSION   WP_009981038
VERSION     WP_009981038.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..392
                     /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=40979
     Region          2..320
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mrdsyldtar gagiilvvyg hvlrglfsag lvpagwpsal laatdytiyt fhmplfflls
       61 glhvpkslrr agdvflltkl rtivypyfvw sllqgavqia lsargtnhaf tpndllaigw
      121 rpfgqfwfly alficmliaw avsaitlrar thggasgang enggtevsge ngepsgapca
      181 vpampivlvl laigglaava fvagsatrwg ivsmtfayfp ffvlgmlige rlpaflervs
      241 sgpalvavaa afaasvafah rfgesdsiwa lpaalsgsal vllvahraar rgdaarhapr
      301 aswleylgfa smpiylahil ataatrialv tlgivdvgaq lalgtfagvl gptllyalal
      361 ragtarlagf pplpagyamt pdkgrigrad aa
//
LOCUS       WP_009980459             790 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Burkholderia pseudomallei].
ACCESSION   WP_009980459
VERSION     WP_009980459.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 790)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 790)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 790)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..790
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=84848
     Region          33..790
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 masrtnrlpr wlkilpgvil lgallvaaga alflraslpr ldgdvraptl ggpmtierda
       61 agvptvaard rfdaaygigy lhaqdrffqm dylrrtgage laellgpaal dfdrehrlfr
      121 fraraaaafa qlppderrll erytqgvndg laalrarpfe yallgeppar wrpedsllvi
      181 wamyfqvqgt lasrdiarnw ltahatqqqr afllpsssgf dapldaprid eapaplpdaa
      241 pdwfraagdg aakrasldfr ssvgsnnwai agsrsargaa ivgddmhlvl glpntwyraa
      301 fiypggaapv rravgvtlag lpaivagsng hvawgltvgy adcldlvple rdgddsrafr
      361 msgarqvarr yvesirvrgg asvsltvlet tvgpvreigg rpyavhwvaq lpgavnlgla
      421 rladavdvdg amrvantlgi paenivvgdr agrigwtiag alpdrraprg gegaawrsll
      481 ppdayprvvd psggqlwtan srqlagdayr ligdggtdlg aratqlrdgl talgrtdeqa
      541 ayridfddra lfiaqwrdra lrvlddaala ghpsraefrr llehgwtgra svdsvgytla
      601 rgflyrlydv tfdglnarlk qvdagadyel anlrwpavva rlldaqppgw lpagasswrd
      661 vqliaidrti aaltadgapl araswgarnt lriahpfags lpllggwlta paaqmpgdsh
      721 mprvaapdfg qsermvvspg heefgifnmp ggqsghplsp fflaghdawv raeptpflpg
      781 varhtlrfap
//
LOCUS       WP_009981076             338 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia pseudomallei].
ACCESSION   WP_009981076
VERSION     WP_009981076.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 338)
  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   5  (residues 1 to 338)
  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   6  (residues 1 to 338)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37294
     Region          33..216
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          107..332
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mmpvanvfsr taaqrpaplh tvvialnvmk emgvpaevll rgtgispeei eqanamvtha
       61 qemvlfanal eatgnsaigl higssipvta yglrghamlv sptlgdamrl ayeyplmais
      121 yfqitlavna drarvtvggy tyradllvln tdmclaavrr eivdligrvp tfrrlglafp
      181 ppahasvysd ifdcevifdt eenflefdad lldirlplah siefeisrra cekrefelsh
      241 wvpadlvgrl fgimydnptc qdvvkltgkl gmsprslqrk lkemgtsfsa lhdlvrrdia
      301 srylsenkst keiaarlgyk ntsafsramk rwsklagd
//
LOCUS       WP_009981229             289 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia pseudomallei].
ACCESSION   WP_009981229
VERSION     WP_009981229.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 289)
  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 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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..289
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31372
     Region          44..280
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <182..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 mmtllavppe klpaasaast aagptpaagn gacasppssg aapedddgfa amlahfaqle
       61 pvfdalpdva ffvkdvrary alvnrtlaqr cgykdkrdly gkaadevfpr rfgrsyveqd
      121 ltiiaggrql tdqlelhlys grqpgwcltc keplrnaqgr ivgiaglsrd lrahesshpa
      181 ysriadvvry ihahyvqpln lkhlagmagm svaqleryfh kvfhltprqm llkarldaat
      241 allvthdkvt dvaalcgytd hsaftrqfka tvgvtpteyr lmlqegrga
//
LOCUS       WP_009999784             348 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Leuconostoc lactis].
ACCESSION   WP_009999784
VERSION     WP_009999784.1
KEYWORDS    RefSeq.
SOURCE      Leuconostoc lactis
  ORGANISM  Leuconostoc lactis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Leuconostoc.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Leuconostoc lactis"
                     /db_xref="taxon:1246"
     Protein         1..348
                     /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=39441
     Region          2..277
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 maskriawld fakgvtiflv vivhvvegly ktgqfpaqqn istnimgvlf tvvmpvffal
       61 sgyvytppqn grqyiigigk klvnlgmpyv lfsvlyvclq hgsqavhhls swqdlahiya
      121 lpvgylwyly vlffvygvvg lltllrlsll iqgviyslfl wlavthttal pyalvgvlmw
      181 tssfyigyvf kryptwlthw ltvslsgflf vgglawqmqq ghdwfatdmm tttdvwakla
      241 svplflflyq knrggfvsry fttygrysli iylvhapmas igrvlllklg vnhyalllvl
      301 lvafawgtsl iviygtkkwp llnavfnpva yirqiaspkq rlderlkf
//
LOCUS       WP_010001061             323 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Leuconostoc lactis].
ACCESSION   WP_010001061
VERSION     WP_010001061.1
KEYWORDS    RefSeq.
SOURCE      Leuconostoc lactis
  ORGANISM  Leuconostoc lactis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Leuconostoc.
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   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   4  (residues 1 to 323)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Leuconostoc lactis"
                     /db_xref="taxon:1246"
     Protein         1..323
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=35686
     Region          5..317
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mttaiefqhv qkdfngqtvi pdlnltidqg elfilvgtsg sgkttslkmi nclepltagk
       61 ilvngtdttt ipvrslrwqm gyvlqqialf ptmtvsqnia vipemkgtak keinqtidel
      121 laevgldpke yrdrmpsels ggeqqrigil raiaaqpdiv lmdepfsald pisrqqlqdl
      181 vlrlharyhn tivfvthdmn ealklgdrig vmqhgqliqv dtpaalaqhp vndfvrnffg
      241 asraknvydv yvgrvgliqg yltekpsvas griqsldvqa tlrtaftalt dhdyvavtee
      301 nrvvgyldsq rivaylsqhe evs
//
LOCUS       WP_010002066             159 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Leuconostoc lactis].
ACCESSION   WP_010002066
VERSION     WP_010002066.1
KEYWORDS    RefSeq.
SOURCE      Leuconostoc lactis
  ORGANISM  Leuconostoc lactis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Leuconostoc.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Leuconostoc lactis"
                     /db_xref="taxon:1246"
     Protein         1..159
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17107
     Region          10..158
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 msavqspapl isqlldtwiq gegsqdfpma nyanaaaily qnvadinwvg fylyddaqnh
       61 lvvgpflgkp avaliapeag vvghafsvqe tvvvddvntf anhivcdpns naeivipltt
      121 adgrrlgvld idsptrqrfs aqdradlehf vqtllayvk
//
LOCUS       WP_010007608             129 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Leuconostoc fallax].
ACCESSION   WP_010007608
VERSION     WP_010007608.1
KEYWORDS    RefSeq.
SOURCE      Leuconostoc fallax
  ORGANISM  Leuconostoc fallax
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Leuconostoc.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 129)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Leuconostoc fallax"
                     /db_xref="taxon:1251"
     Protein         1..129
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=14573
     Region          2..121
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(7..10,41..43,46,69,106,120)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mirlycdaar qqhsgvstag aivivnkqqq qfkttlgplp dnhaaeftal lwilqqlslq
       61 damltiyvds kivadslnkq yakhyqayvd diwlilnqvk fvsiewisek enlgahhlal
      121 qmlhqknks
//
LOCUS       WP_010008010             202 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Leuconostoc fallax].
ACCESSION   WP_010008010
VERSION     WP_010008010.1
KEYWORDS    RefSeq.
SOURCE      Leuconostoc fallax
  ORGANISM  Leuconostoc fallax
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Leuconostoc.
REFERENCE   1  (residues 1 to 202)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Leuconostoc fallax"
                     /db_xref="taxon:1251"
     Protein         1..202
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=22756
     Region          81..202
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(146..147,151,175..178,180)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkkwtilvls migigivigg yhslvtshts sasaqhlsvk kshpnhvqqk ssmrpmtgdy
       61 ylkssekkpy vdlkkyqhvn vlvsiakqrv yirsnqkvly tmysstgknd ttprgqyhiq
      121 gergqhfyna ssdeganywv swkdhgiylf hsvpvdhtgh yiaaegqqlg kkaashgcvr
      181 lsvsdakwfy enipentevt ir
//
LOCUS       WP_010008889             323 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein
            [Lactobacillaceae].
ACCESSION   WP_010008889
VERSION     WP_010008889.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillaceae
  ORGANISM  Lactobacillaceae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales.
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   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   4  (residues 1 to 323)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Lactobacillaceae"
                     /db_xref="taxon:33958"
     Protein         1..323
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=35656
     Region          5..317
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mttaiefqhv qkdfngqtvi pdlnltidqg elfvlvgtsg sgkttslkmi nclepltagk
       61 ilvngtdttt ipvrslrwqm gyvlqqialf ptmtvaqnia vipemkgtak keinqtidel
      121 laevgldpke yrdrmpsels ggeqqrigil raiaaqpdiv lmdepfsald pisrqqlqdl
      181 vlrlharyhn tivfvthdmn ealklgdrig vmqhgqliqv dtpaalaqhp vndfvrnffg
      241 asraknvydv yvgrvgliqg yltekpsvas griqsldvqa tlrtaftalt dhdyvavtee
      301 nrvvgyldsq rivaylsqhe evs
//
LOCUS       WP_010010576             391 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein, partial [Loigolactobacillus
            coryniformis].
ACCESSION   WP_010010576
VERSION     WP_010010576.1
KEYWORDS    RefSeq.
SOURCE      Loigolactobacillus coryniformis
  ORGANISM  Loigolactobacillus coryniformis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Loigolactobacillus.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Loigolactobacillus coryniformis"
                     /db_xref="taxon:1610"
     Protein         <1..391
                     /product="HNH endonuclease family protein"
     Region          106..245
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 ikdqrvksll irlghlnndi lvpyllqvfa ktrdgalsad qlvevlrvll aylarrlfig
       61 vpttglnllf aaldrqvehy vdqakvdyve glklvltqiv kenkrfptdk slkdalvekd
      121 yyhmssmslw fildelnnas geeqdlfdaa qsgkysiehi mpqvvnsswq kalgtdwrpv
      181 hnvwlnrlan ltltgfngqm snrpyiekrd madgyrksgi klnqwvaqfd kwdeatlqer
      241 qadlltralt vwprpnvstq latddpnswd tldmileanp tgtkpvafsf vddqvvqiks
      301 wtdlynqlid llwdadpsnf famansdesl vkhvnevead qryrqlgdsd vavyaggdsa
      361 wsrvqhikrl lagsdhdlse vnvktrkvnh s
//
LOCUS       WP_010011867             234 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Loigolactobacillus coryniformis].
ACCESSION   WP_010011867
VERSION     WP_010011867.1
KEYWORDS    RefSeq.
SOURCE      Loigolactobacillus coryniformis
  ORGANISM  Loigolactobacillus coryniformis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Loigolactobacillus.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 234)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Loigolactobacillus coryniformis"
                     /db_xref="taxon:1610"
     Protein         1..234
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=26916
     Region          <2..214
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mirffgqpky standtlgye ffirqyhqgn wvfpqnfnqf saqqirdlai asikalpknv
       61 alvsinldqi qfirpdfiag mtqvqkacyp vevvielter pqkvplsdli daarqyqanq
      121 lwvclddvgt gdntirlana ldpyvteykf alqnfrqytd fssiispllq fwrqyaqihh
      181 kffaiegfet kaelsigshy hadvmqgyyl grpqlisigc tqtqkktdkv nkfh
//
LOCUS       WP_010012229             205 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Loigolactobacillus coryniformis].
ACCESSION   WP_010012229
VERSION     WP_010012229.1
KEYWORDS    RefSeq.
SOURCE      Loigolactobacillus coryniformis
  ORGANISM  Loigolactobacillus coryniformis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Loigolactobacillus.
REFERENCE   1  (residues 1 to 205)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Loigolactobacillus coryniformis"
                     /db_xref="taxon:1610"
     Protein         1..205
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=22742
     Region          83..204
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(149..150,154,177..180,182)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkrfikmqql aiivvlavil lglsyhhivs akqtmapqvt ststtkskpk stqkatvqkk
       61 tidwrapsen kaypdlkqhp hvwldvsqgk qrvyvkdgnt vlytmyastg mnnttpngtf
      121 tieaergksf fnkslnegan ywtswsghgv ylfhsvptda agnynvteae klghkashgc
      181 vrltiadaqw intyipygtk vvvhn
//
LOCUS       WP_010012711             267 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Lactobacillaceae].
ACCESSION   WP_010012711
VERSION     WP_010012711.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillaceae
  ORGANISM  Lactobacillaceae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales.
REFERENCE   1  (residues 1 to 267)
  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 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   3  (residues 1 to 267)
  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   4  (residues 1 to 267)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Lactobacillaceae"
                     /db_xref="taxon:33958"
     Protein         1..267
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30978
     Region          53..265
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          186..265
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mriafnkpve tmplycdsvg ydwdqppihr lngyyayhwl qtqsgsgvit idhqsislep
       61 qqgillrprv aheyhptggs pwkvsfltfn gtlcrsladf lklgdylvin qvspelttfi
      121 pevlnefnns hpialldqsv qiykfimllk qnnllnnhry qdsaittpil kyianhyaep
      181 isneklakvt sysvtyqnrv fkrlytmtpl eyltdyrmrk akellltnpt leirevaakv
      241 gfhnpshfid qfkkfyrttp shfrkfi
//
LOCUS       WP_009979600             426 aa            linear   BCT 20-JAN-2025
DEFINITION  DNA polymerase domain-containing protein [Mycobacterium avium].
ACCESSION   WP_009979600
VERSION     WP_009979600.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium avium
  ORGANISM  Mycobacterium avium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Zhu,H., Nandakumar,J., Aniukwu,J., Wang,L.K., Glickman,M.S.,
            Lima,C.D. and Shuman,S.
  TITLE     Atomic structure and nonhomologous end-joining function of the
            polymerase component of bacterial DNA ligase D
  JOURNAL   Proc Natl Acad Sci U S A 103 (6), 1711-1716 (2006)
   PUBMED   16446439
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Zhu,H. and Shuman,S.
  TITLE     A primer-dependent polymerase function of pseudomonas aeruginosa
            ATP-dependent DNA ligase (LigD)
  JOURNAL   J Biol Chem 280 (1), 418-427 (2005)
   PUBMED   15520014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Mycobacterium avium"
                     /db_xref="taxon:1764"
     Protein         1..426
                     /product="DNA polymerase domain-containing protein"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=47175
     Region          4..312
                     /region_name="LigD"
                     /note="Eukaryotic-type DNA primase [Replication,
                     recombination and repair]; COG3285"
                     /db_xref="CDD:442515"
ORIGIN      
        1 mnhmtrpvsl evagrrvtit hpdkvvfpra gggettgsaa gpytkldlvr yylsvadgal
       61 rgvagrpmil krfvkgitqe avfqkrapan rpdwvdvael ryargtsaae avihdaagla
      121 wvinlgcvdl nphpvladdl dhpdelrvdl dpmpgvswrr ivdvalvare vledygltpw
      181 pktsgsrgfh iyariarrwe frqvrlaaqt vareverrap eaatsrwwke eregvfvdfn
      241 qnakdrtvas aysvratpda rvstplrwde vagcrpeaft idtvparlae igdpwagmdd
      301 avgdldrllv laeelgpper apkgagtrsg grrrssmpli evartktrdg amaaldvwrd
      361 rhpeaaarlq padvlvdgmr gpssiwyrir inlqrvpedq rppqeeliad yspwqgyggr
      421 qkpsrg
//
LOCUS       WP_010013689             273 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Loigolactobacillus
            coryniformis].
ACCESSION   WP_010013689
VERSION     WP_010013689.1
KEYWORDS    RefSeq.
SOURCE      Loigolactobacillus coryniformis
  ORGANISM  Loigolactobacillus coryniformis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Loigolactobacillus.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Loigolactobacillus coryniformis"
                     /db_xref="taxon:1610"
     Protein         1..273
                     /product="formate/nitrite transporter family protein"
                     /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=28312
     Region          33..254
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mnslkanqvi emfslkaktk sqlglgelll lgmmagafia igylafvrva gtvpkswgsf
       61 stflgaclfp igliaitflg gelvtgnmmi ltfgflkkql tlvaviknwv lvllanclgg
      121 alfgllfghl vgltegdfaa ktiaiatakl adspsamiis gvgcnilvgm aiflaamsqd
      181 ffgkvigvwf pimifvvcgf qhvvanafil taavlagghf sasalvlnil lvfignaigg
      241 alglavpvyy anresavvst tspesikqvi ane
//
LOCUS       WP_010014933             332 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Loigolactobacillus coryniformis].
ACCESSION   WP_010014933
VERSION     WP_010014933.1
KEYWORDS    RefSeq.
SOURCE      Loigolactobacillus coryniformis
  ORGANISM  Loigolactobacillus coryniformis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Loigolactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Loigolactobacillus coryniformis"
                     /db_xref="taxon:1610"
     Protein         1..332
                     /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=37783
     Region          2..281
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 msgkrriawi diakaigiia vvvghaypeh dtfynvlyww hmplffmigg fflrplqvgq
       61 fktfaqhklv pllreyfgfg lfltlvsawv tpekwqglaq glsdllyggt hlngvlsafw
      121 ymtvyllavt lltviisfvp qnwlrwlivt aaflvgtays nagdlfgfal pgdadvtlca
      181 lfymyagrel fryqrqrlrs nwwlsvival ssagimaqql gvidlhlymk sheitsqsla
      241 lilplilcsa ifmlaywlqf tpfvngltfv gkhtmiimyl hklvfaifer laggswllla
      301 vaglmipimm mvsferlkes qqrlfwltpr lq
//
LOCUS       WP_010017872             158 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein, partial [Fructobacillus
            fructosus].
ACCESSION   WP_010017872
VERSION     WP_010017872.1
KEYWORDS    RefSeq.
SOURCE      Fructobacillus fructosus
  ORGANISM  Fructobacillus fructosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructobacillus.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 158)
  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 158)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Fructobacillus fructosus"
                     /db_xref="taxon:1631"
     Protein         1..>158
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          19..72
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mantrffsqi pawvdeldnv sdfqvrllgf iytvsntgnq afpsnsflak kyhksastvq
       61 halsdlyqkg llkstpkyvd gtnriekryl eivephyhdl ngmaenggts enghtptpns
      121 dippsrkrty pmseigtdnr llnkspnksv ytdrdesv
//
LOCUS       WP_010018905             254 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Companilactobacillus
            farciminis].
ACCESSION   WP_010018905
VERSION     WP_010018905.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus farciminis
  ORGANISM  Companilactobacillus farciminis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Companilactobacillus farciminis"
                     /db_xref="taxon:1612"
     Protein         1..254
                     /product="formate/nitrite transporter family protein"
                     /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=27057
     Region          1..254
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mftpeeilqk sinagtnklk ktllakmilg figgamislg flayvrvtas ipkdlasvka
       61 lvggavfpig livillagge latgnmmavg tslfdkkahl ldylknllvi tlfnfigaif
      121 vayffghvvg ltharpfqqa visiasaktd asfwsalisg igcnwlvgla vwlsfgakda
      181 agkilgiwfp imifvavgfq hsiancfiip aaifeggstw glflqnfipv ylgniiggli
      241 fvagfyyysy adkk
//
LOCUS       WP_010019586             232 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Companilactobacillus farciminis].
ACCESSION   WP_010019586
VERSION     WP_010019586.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus farciminis
  ORGANISM  Companilactobacillus farciminis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 232)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Companilactobacillus farciminis"
                     /db_xref="taxon:1612"
     Protein         1..232
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=26634
     Region          <6..218
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mdkiyryfvq pqidiktdti fgyellikql tpegwrlprs fseistetts klliattkil
       61 glkvdycsvn vnreqlldtr medaiiqsql qlfptkvvve lteeegpkky sdafliphlr
      121 kfmehgmqis lddvgtgdns ldaircflpm aselkfalqn fnsqnedpdl qkklimwqgi
      181 sqeygqrlil egieddedak mssnlginlr qgyyygkpel lslpgdeqyy kk
//
LOCUS       WP_010021414             221 aa            linear   BCT 20-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein
            [Fructilactobacillus fructivorans].
ACCESSION   WP_010021414
VERSION     WP_010021414.1
KEYWORDS    RefSeq.
SOURCE      Fructilactobacillus fructivorans
  ORGANISM  Fructilactobacillus fructivorans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Fructilactobacillus.
REFERENCE   1  (residues 1 to 221)
  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 221)
  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 11443421
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Fructilactobacillus fructivorans"
                     /db_xref="taxon:1614"
     Protein         1..221
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=23555
     Region          82..221
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          177..220
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
ORIGIN      
        1 mkddkhednk kkdpwddsfs ddtdpdgnls rteyrkhhrs nslvvimlvs iivvialval
       61 vfglskerav gtgstsqkaq sskvshskak sskpdrrakk sssssnsqdd attnsdttdd
      121 dagsssatpn tqgntstnes ttpssansdn stsdskqptq kssqttdnnd nsesndyvkv
      181 qkgqgvyrva tnagismqql lklnglssss qihpgqslrv k
//
LOCUS       WP_010024477             227 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Sporolactobacillus inulinus].
ACCESSION   WP_010024477
VERSION     WP_010024477.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus inulinus
  ORGANISM  Sporolactobacillus inulinus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  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   3  (residues 1 to 227)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Sporolactobacillus inulinus"
                     /db_xref="taxon:2078"
     Protein         1..227
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26119
     Region          18..219
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mqmkvgstli lehrnnqnei nryrcklaei rdhmllidyp idektgrtsl llngtnfmav
       61 yliddhvfrf pttllhrsag kvpllamsfs gedqmqsiqr rnyvrvacnv diaihstegm
      121 frpftsltsd lggggalvll pdkcegvhed mmirswlslp rasgsyyylv irsqvtrift
      181 dkrtngqras iqflpdseke rqpiirycfe kqlearkkqi dlemrrs
//
LOCUS       WP_010031124             393 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Rhizobium sp. M1].
ACCESSION   WP_010031124
VERSION     WP_010031124.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. M1
  ORGANISM  Rhizobium sp. M1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 393)
  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 393)
  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
REFERENCE   3  (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   4  (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   5  (residues 1 to 393)
  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   6  (residues 1 to 393)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (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 12210646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Rhizobium sp. M1"
                     /db_xref="taxon:2035453"
     Protein         1..393
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40779
     Region          31..66
                     /region_name="HTH_CRP"
                     /note="helix_turn_helix, cAMP Regulatory protein;
                     smart00419"
                     /db_xref="CDD:128696"
     Region          80..379
                     /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 mtmtspvaqt piarkistna virtvlanrs isradiaklt glskqtisev vrdledegwl
       61 kpvgrtdgrp grnaviyein araglavsid lggtkiaaai cdllgnvvae tkvatdrrgg
      121 mhlvnqfsdl ivelasaagt tadklrlvvl gtpgvldpvt ghinvapnip gvdamdlrqv
      181 fssrmglpvi vendvnlaaq gerwrghgve vdnfafvalg tgvgmgiian gallrgarga
      241 ageiaylpig gdafdpggft lgtlesavgs vamlrryigf ggrnastvad lfaafnages
      301 savaaieeta rlaavaiaai gatldpelvi tggsigarpe lvnairrflp rctpypprie
      361 isrfgnraal mggmgiaver mhddlfgvkl rea
//
LOCUS       WP_010032272             118 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein [Streptomyces].
ACCESSION   WP_010032272
VERSION     WP_010032272.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            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="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=13130
     Region          1..77
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mirsadirew rdhdvvdpkq hkigmleavy vdtatdqpam atvrtglpsr rrlvfvpldd
       61 avlgpgyvqv pyargqvrka psigtddvlp aereeeifqh ygmtyqagag gerrlarr
//
LOCUS       WP_010034497             177 aa            linear   BCT 20-JAN-2025
DEFINITION  transcription termination/antitermination protein NusG [Gemmata
            obscuriglobus].
ACCESSION   WP_010034497
VERSION     WP_010034497.1
KEYWORDS    RefSeq.
SOURCE      Gemmata obscuriglobus
  ORGANISM  Gemmata obscuriglobus
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Gemmatales; Gemmataceae; Gemmata.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Kang,J.Y., Mooney,R.A., Nedialkov,Y., Saba,J., Mishanina,T.V.,
            Artsimovitch,I., Landick,R. and Darst,S.A.
  TITLE     Structural Basis for Transcript Elongation Control by NusG Family
            Universal Regulators
  JOURNAL   Cell 173 (7), 1650-1662 (2018)
   PUBMED   29887376
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Liu,B. and Steitz,T.A.
  TITLE     Structural insights into NusG regulating transcription elongation
  JOURNAL   Nucleic Acids Res 45 (2), 968-974 (2017)
   PUBMED   27899640
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Steiner,T., Kaiser,J.T., Marinkovic,S., Huber,R. and Wahl,M.C.
  TITLE     Crystal structures of transcription factor NusG in light of its
            nucleic acid- and protein-binding activities
  JOURNAL   EMBO J 21 (17), 4641-4653 (2002)
   PUBMED   12198166
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415705
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Gemmata obscuriglobus"
                     /db_xref="taxon:114"
     gene            1..177
                     /gene="nusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
     Protein         1..177
                     /product="transcription termination/antitermination
                     protein NusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
                     /calculated_mol_wt=19407
     Region          8..173
                     /region_name="NusG"
                     /note="Transcription termination/antitermination protein
                     NusG [Transcription]; COG0250"
                     /db_xref="CDD:440020"
ORIGIN      
        1 mdestiidev grwaalrtaa rwekavteql aaagvpvflp lltrvsrtks ktqtaqlpvf
       61 pgyvfcgere yrdstrvpps crkliaqllr apdpdqlkde lrsvadllan rqllqervyg
      121 vigdtvrivg gplagslgti lrlkpgtrrv lievsflgar meatveerll ekavsia
//
LOCUS       WP_010035376             947 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: penicillin acylase family protein [Streptomyces].
ACCESSION   WP_010035376
VERSION     WP_010035376.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 947)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 947)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 947)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..947
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..947
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=103067
     Region          39..947
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mppnttastg qqpgksgrrk grkarlivlv lvlaliggla fgaywsistv rasfpqtkgs
       61 ltlkglsgpv evkrdnygip qiyassdadl fmaqgyvqaq drfyemdvrr hmaagrlsem
      121 fgksqvdnde flrtlgwerv akeeydtkls aatkkylqay aqgvnaylqg kdgkdisley
      181 aalgftndyk pqkwtpvdsi swlkamawdl rsnmqdeidr alltsrlgpk qiaelypqyp
      241 ysrnkaivqe gqydeltgaf eqggtsgtsg tgtggtsgtg gtatgtagta sgtsgtasgt
      301 sgtasgtsgt asgtsgldsq ltglsdalsd lppavgvngd gigsnswvvs gehtitgkpl
      361 landphlsps lpsvwyqmgl hcrsvssacq ydvsgytfag mpgviighnq diawgmtnsg
      421 vdvtdlylek itgdgylydg kvkpfetree tikvaggspk tivvretnng pllsdraeel
      481 vkvgkkatvd taapdrgdgy gvalrwtalq pgttmdavfa mdraknwtdf rkaaalfdvp
      541 sqnliyadte dnigytlpgr iptrsqdddg svpapgwdpk yrwtgyieqd alpyeynppr
      601 gyivtanqav idpdkypytl tedwsygtrs qritdliqsk iknggkistd dmrqmqldns
      661 seiarllvpt llkidpgskd vreaqklleg wdytqdtdsa aaayfnavwr nilklafgnk
      721 lpkelrvkgq clwvepvntt gpadeagkvr ecgerdpdqa qpdggdrwfe vvrklmdqpd
      781 sdwwktpkag trpaadnrdq lfkramidar weltaklgkd idtwtwgrlh rlflknqtlg
      841 tegpgfvqya lnrgpwelsg geatvnatgw naaggygvvw vpsmrmvvnl gdldksrwin
      901 lsgasghays ahyvdqtdkw adgellpwsf sdravedgtt dklvlkp
//
LOCUS       WP_010035720             742 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate--CoA ligase family protein [Streptomyces].
ACCESSION   WP_010035720
VERSION     WP_010035720.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 742)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..742
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=78539
     Region          49..737
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mlgsthgtlt tdsrrtraia cgersgpvvh grpaqtgdld vsgrplhagv pdldrffrpr
       61 svavigasda egrpntgitr qladwaervg arlypvhpsr psvfgtpcsp svaglpepvd
      121 lavvlvgdpl pvveelaeak arfavvfasg faetgaegea aqrrltaave rsgmrllgpn
      181 tnlnaferfr ddlqgpaial itqsghqgrp vfalqelgir lshwaptgne adletadfls
      241 yfaeqpevga iacyleglkd grsfllaadr aarrgvpvva vkvgrtetga rtaashtgkl
      301 tgadavvdaa lrqygvirvd gldelqdtaa llararppra dgvvvysisg gtgahvadla
      361 tgaglrlpvl searqaelhq wipeylsvan pvdngghpvg dwrgrkiida ilddpevgvl
      421 vcpvtgpfpp lsdrlvrdlv aaaeqtdklv cvvwgspvgt epayrevllg ssrvatfrtv
      481 gncltavray lghhrfttgy hspfddaprt pspsyrkaqa lmrpgeqlse haakqllray
      541 girvpreqlv tsaaaavraa glvgypvvmk asgariahkt elglvkiglt sasqvrdayr
      601 eltdiaryed vpldgvlvcq mvehgvemvv gvthddlfgp tvtvglggvl vevlrdtavg
      661 vppfgeerar dmlaglrgra lldgvrgrpp adldalvevv lrvqrmalel gdqlaeldin
      721 plmvlpqgqg avaldalavc sr
//
LOCUS       WP_010036631             212 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Gemmata obscuriglobus].
ACCESSION   WP_010036631
VERSION     WP_010036631.1
KEYWORDS    RefSeq.
SOURCE      Gemmata obscuriglobus
  ORGANISM  Gemmata obscuriglobus
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Gemmatales; Gemmataceae; Gemmata.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 212)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Gemmata obscuriglobus"
                     /db_xref="taxon:114"
     Protein         1..212
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=22637
     Region          6..131
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(10..13,44..46,49,73,113,127)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 msdtatmhid gasrgnpgaa ayavvlarpg lpvveeadti gtasnnvaey talveglgla
       61 aelgvkqlqv fsdselmvkq magaykvkne dlrtlyeeac rlrkqfesvt ithvrreqnk
      121 radaigneal dgrprkrgqv pppvhtprpe dgagghpspa sdapvrtdav rcltdaanhw
      181 aakglkglpp eavweqlwsl leesgvlkkk ak
//
LOCUS       WP_010039993             158 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Gemmata obscuriglobus].
ACCESSION   WP_010039993
VERSION     WP_010039993.1
KEYWORDS    RefSeq.
SOURCE      Gemmata obscuriglobus
  ORGANISM  Gemmata obscuriglobus
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Gemmatales; Gemmataceae; Gemmata.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 158)
  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 158)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Gemmata obscuriglobus"
                     /db_xref="taxon:114"
     Protein         1..158
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17342
     Region          55..110
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msttarkssv papkpqeeaa pkpkwgpfte kfggtvrdag vtavprvllt glaalklkpm
       61 ecvvllqlis cwgdaktcph pkrktlrewl gcdkrtldra iaglvkkkll tktmrarrgr
      121 rrsneydlsg lveqlkplgr raldekkkya alraaaal
//
LOCUS       WP_010040989             402 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Streptomyces].
ACCESSION   WP_010040989
VERSION     WP_010040989.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 402)
  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 402)
  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
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 402)
  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   5  (residues 1 to 402)
  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   6  (residues 1 to 402)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 402)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 402)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..402
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41309
     Region          30..81
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          96..389
                     /region_name="ASKHA_ATPase_ROK_BsXylR-like"
                     /note="ATPase-like domain of Bacillus subtilis xylose
                     repressor (XylR) and similar proteins; cd24076"
                     /db_xref="CDD:466926"
ORIGIN      
        1 mtaplhedrp agpgralpdt qqgmrrrnla rvlhavraeg plsraavasr igltraavst
       61 lvdelirsgl leelgperpg rvgrpgsala lsgrgpagig aeigvdhlav cavdlrgttr
      121 srairqganr grspgpvlae ltelirrvva eaegeglwpa glavavpglv ardartvvra
      181 pnldwheadl gdllpadfpl tvdneanfga laelwlgdgt prdflhvsae igigaavvvd
      241 ggllrgtrgf agelghvpvq pdgpecacgg rgcleqyage eavlraagle pdedrvglla
      301 graaegdedv rralrdagta lgvaltgavn lldpqsvvlg gelsglapwl lpslrdelar
      361 rtagpacpvs vsrlgpqgpl lgaahsvvra vlddpatvae ra
//
LOCUS       WP_010041540             163 aa            linear   BCT 20-JAN-2025
DEFINITION  3-hydroxyacyl-ACP dehydratase FabZ family protein [Gemmata
            obscuriglobus].
ACCESSION   WP_010041540
VERSION     WP_010041540.1
KEYWORDS    RefSeq.
SOURCE      Gemmata obscuriglobus
  ORGANISM  Gemmata obscuriglobus
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Gemmatales; Gemmataceae; Gemmata.
REFERENCE   1  (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 10101294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Gemmata obscuriglobus"
                     /db_xref="taxon:114"
     Protein         1..163
                     /product="3-hydroxyacyl-ACP dehydratase FabZ family
                     protein"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=17344
     Region          5..123
                     /region_name="FabZ"
                     /note="FabZ is a 17kD beta-hydroxyacyl-acyl carrier
                     protein (ACP) dehydratase that primarily catalyzes the
                     dehydration of beta-hydroxyacyl-ACP to trans-2-acyl-ACP,
                     the third step in the elongation phase of the bacterial/
                     plastid, type II, fatty-acid...; cd01288"
                     /db_xref="CDD:238615"
ORIGIN      
        1 mrwtwidrfv afesgksata vknlslaedh fadhfpgfpv mpaplilegl aqtggilvge
       61 arqyrenvvl akmsnmkfhr dalageqlty tttlidlndt garvaatars gadlvvegei
      121 lfahanpsql ppglpdtkfv fngelthllr maaavskpaa agg
//
LOCUS       WP_010041799             221 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Streptomyces].
ACCESSION   WP_010041799
VERSION     WP_010041799.1
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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..221
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=24636
     Region          76..216
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mgarraskdt drrigrrali vggaaaaags avlardelgr lwwrvpgvek prkegevdya
       61 garwvaasda nwrradrpdd ygidmvvvhv tqgsfdsavk afqdpahkaa shyivrkdgh
      121 iaqmireldv ayhagnrdyn ersvgiehag fvdrpqdftd emyeasarlt aricarydip
      181 vdrehiighv evpgtdhtdp gphwdwdrym rlvraarttp a
//
LOCUS       WP_010042228             738 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: molybdopterin oxidoreductase family protein
            [Streptomyces].
ACCESSION   WP_010042228
VERSION     WP_010042228.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 738)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 738)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..738
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=78452
     Region          3..738
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mqttatpthc pycalqcgmn ltpapdgtve vsertdfpvn rgalcgkgrt apavlasnvr
       61 ltsplvreqg alvpaswdea ldriaeglrr traeygpdgv gvfggggltn ekaytlgkfa
      121 rvvlgtsqid yngrfcmssa aaagikafgl drglpfpled iprtgcvilv gsnlaetmpp
      181 slrfltelke nggtlividp rrtrtaeqad lhlaprpgtd lalalgllhl viaegrvdee
      241 yvqertvgwe daraaamahw peyveritgv svpelretvr mfcepesamv ltargpeqqs
      301 kgtdtvgawi nlclatgrag rplsgygclt gqgngqggre hgqkadqlpg yrklddpaar
      361 rhvaevwgvd pdslpgpgrs ayelldalgt dvrslllmas npvvsapraa hieeriksld
      421 flavcdvvls etaaladvvl pvtqwaeetg tttnlegrvl lrrqaitppd gvrsdlevlh
      481 elaarlgvek gfptdpeeif eelrrasagg padysgityr rlveengvfw pcpavepegl
      541 tgaedgaggp gaqgsapgrp astddrpaat gdtpaatgdt adpahpgtpr lfldrfatpd
      601 grarfvpvsh raiaeepdde ypvllttgrv vaqyqsgaqt rrvaelnaaa pgpfvelhpr
      661 laarlgaaeg dpvavvsrrg ravaparitn tirpdtvfmp fhwpgegran sltnpaldpt
      721 srmpefkaca vrleavrp
//
LOCUS       WP_010046374             457 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Streptomyces].
ACCESSION   WP_010046374
VERSION     WP_010046374.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 457)
  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 457)
  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
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 457)
  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   5  (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   6  (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
REFERENCE   7  (residues 1 to 457)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 457)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..457
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=46765
     Site            order(9..10,14..16,27..29,38..41,43..44,47..48,50..51,
                     64..66,71..73)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Region          11..55
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Site            order(27,30,80)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
     Region          76..440
                     /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 mpaspstara indrlalnll qregpltagr lkqltglsrp tvadlverlt aagliavvge
       61 ageqrrgpna kvygivadra hlaaldvrte gvavavadlv grvlaeesvp iggdmgtgpa
      121 veqavalver vvkeagadrl htvgigapgl idpasgelrd ssglpewhrr lvaalqerlp
      181 earvsvenet nlaalaeqrd gvardrdtfv llwlghgtga avvldgalrr gasggtgeig
      241 flpvpgtaal psstdceggf hslaaadavv dlaarwgvpa epgqepsvvg vvraaagmvr
      301 savrqvrepg agagafrsvn eggesrsvsd gdvprsrsdr eeeprpaggs eassspgavp
      361 aarfldalad rlavgvasvv aildpgcvvl ggevgraggd elaarvqdri armtplptev
      421 rtttlgggav lrgalltard raqdelftpg erpvqrw
//
LOCUS       WP_010046959             793 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Gemmata obscuriglobus].
ACCESSION   WP_010046959
VERSION     WP_010046959.1
KEYWORDS    RefSeq.
SOURCE      Gemmata obscuriglobus
  ORGANISM  Gemmata obscuriglobus
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Gemmatales; Gemmataceae; Gemmata.
REFERENCE   1  (residues 1 to 793)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 793)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 793)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Gemmata obscuriglobus"
                     /db_xref="taxon:114"
     Protein         1..793
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=84728
     Region          17..791
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 msisrfllrl algrrlpqta gelrvtgvaa pvtirrdrwg vphidaasea dayfalgfcq
       61 gqdragqlev lwrlargala ewvgavalpa drmsrhigfr raaeaqlpvl saeargafea
      121 faagvcagtt tglpqkphef aivggapsaw dgadvlavlk lqsfllpsnw dvelarlrvl
      181 ladgpdavre ldpvsvppvv dpvmgapgea glldrlaadl aalqvylprg ggsnnwcisg
      241 trtesgkpil asdphlaptt pppwylahvr tpawevagag lagapgfpig hngfaawgvt
      301 agltdnsdlf ietlssdgrs vrqpdgtfvp cdvvrevvrv rgaadvveev lvtprgpllt
      361 tvlpdtklav slsavwlqpr pvegflkspt arsfeefrkp fahwpalpln vlyadangti
      421 gwqlvgevpe ragsagllpk padapgsawt gtvpfdampf qenppsgfla tandppnewa
      481 qasflpnsss gqrgageelg hdfvdpyrar rirellaard sgwtlagasa iqldvqslpw
      541 rearevvlal aptdpdarda lallhewngr vetdssaaav felfvaemcv rvarakapks
      601 watavgegal gvatynlfsd rrvghlvhll rtqpdgwfgs wagemeqala gavrtlrraa
      661 gpgprfwawg hlrqlllehp lfgkhrwlgp afnrgpfpwg gdsntvsqag arpaeptaft
      721 hnmanlrtaf dladlskstf vlcggqsgnp lsphhadqla lwlqgesfil pwdqadvira
      781 avdtlrlmpg ers
//
LOCUS       WP_010046997             393 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Streptomyces].
ACCESSION   WP_010046997
VERSION     WP_010046997.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 393)
  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 393)
  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
REFERENCE   3  (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   4  (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   5  (residues 1 to 393)
  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   6  (residues 1 to 393)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (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 12122468
            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="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41882
     Region          12..54
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          77..365
                     /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 mtnptsrdyn kasvldvvls hapltrnqli eltglskatv sraveelrad gfvvdggvde
       61 itgrgrrsty ldlpgttghv agvsfgaqtt gvlvtdlrgr eiqhvtvpta dhqevedaar
      121 wlvdlieraa rsaqgplrqi vaavpgrvrn gteifgpaes mkifagsglh ravenlveap
      181 vlldsdanas llgiltddat irnaalfsvs tilnfasctd helargstpt fgdigvlssg
      241 agdenldell strgllrfar krgldlerie dlwlqphtea ppneaphaev lqafttaivt
      301 avsvvavtld pesvyfvgrl rplvdvvlpq vrerldqnlp avpeirtgph qiglstaqga
      361 vyacltiaqe rlrdavlsar rrsqaagqaa paf
//
LOCUS       WP_010047237             710 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Gemmata
            obscuriglobus].
ACCESSION   WP_010047237
VERSION     WP_010047237.1
KEYWORDS    RefSeq.
SOURCE      Gemmata obscuriglobus
  ORGANISM  Gemmata obscuriglobus
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Gemmatales; Gemmataceae; Gemmata.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 710)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Gemmata obscuriglobus"
                     /db_xref="taxon:114"
     Protein         1..710
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=77372
     Region          13..706
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mtalppipla tlsqpelavr thcpycafqc gilmgedlgg drprisgdph fpvnngqlcv
       61 kgwssaallg hpqrvtvpql rdgrgrwrpa ewdealdfva aklasirerc gadangvfgs
      121 galtnekayl lgkfarvalg tanidyngrf cmasaagaqn rafgidrglp fpvadverae
      181 vvllvganta dtlppmmqwf drqranggrl vvadprrtpt arradlflqv tpgtdlalan
      241 gllyiaieeh ivdgryiadr tngfaaarav vlqyhparve rltgvsesql rqavrwlata
      301 rssmvltgrg teqhskgvds vhawinlmla lgkvgkphsg fgtltgqgng qggrehgqka
      361 dqlpgyrlie vdahreavas vwgvdaaslp rkgksayell dvlsgevksl fvmgsnvava
      421 apnlarilpk lqalellvvc dafhnetseh ahvflpvyqw aeeegtltnl egrvirrrtv
      481 arpptgprsd lrvlydlalr lgvgdkfafr saehvfdelk ratagapady sgisyakier
      541 qdgvfwpcrs eddpgtprmf terfhhpdgr anffavehre ageepsaefp lffttgryke
      601 hynsgaqtrg vgklanaqll prleihprla rrhrvstgsr vtvesrrakv efvaevtadi
      661 rpdtlfapfh wggrqaanll tsgvldptsr mpefklaavr iasvrdgaqg
//
LOCUS       WP_010051164             328 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Carnobacterium].
ACCESSION   WP_010051164
VERSION     WP_010051164.1
KEYWORDS    RefSeq.
SOURCE      Carnobacterium
  ORGANISM  Carnobacterium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Carnobacteriaceae.
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   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   4  (residues 1 to 328)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Carnobacterium"
                     /db_xref="taxon:2747"
     Protein         1..328
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=36005
     Region          1..>243
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mikfenvtke yqadtpvvss lnleikagef fvligpsgsg ktttlkminr liplttgtir
       61 iqgkpiseyn lnelrwnigy vlqqialfpn mtieenitiv pemkkwpkdq lanrvtdlln
      121 svgldaesyr hrkpaelsgg eqqrvgvlra laadpdiilm depfsaldpi srkklqedva
      181 klqkkvqktv vfvthdmqea lalgdricim rdglveqigt paelaaqpkn efvreflqsg
      241 hipieeagtv qdlldancya clttdllndl dsnflvpsds idslvlkltn aseisiknpe
      301 sslligtita ehlvaflask lqtggapl
//
LOCUS       WP_010053060             383 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: exonuclease SbcCD subunit D [Carnobacterium].
ACCESSION   WP_010053060
VERSION     WP_010053060.1
KEYWORDS    RefSeq.
SOURCE      Carnobacterium
  ORGANISM  Carnobacterium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Carnobacteriaceae.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Carnobacterium"
                     /db_xref="taxon:2747"
     Protein         1..383
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43753
     Region          1..266
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          262..354
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkfihtadwh igkkihgfql lkeqrevfeq mlevaireev daivvagdly dravppseav
       61 allnqlfvel nienrfpila isgnhdsptr letggpwyqt lnfhlhtkis qslkpivign
      121 tqffllpyfe pidarlyfkd etlvthelaa krvveemekq fnseynqvlv ahlfvagslr
      181 tesetevmvg gldqvsasif nafdyvalgh lhdpnatrha klqysgtllk fsiseanqqk
      241 gfklielsde geltnqffpv spekelrvle gffadliept yyeaqkrddf iyvqlkdtkm
      301 ipdamnrlre iypnvlgmer ldrsglmatm nlttreklkt kdpselfkdy yeevmgeals
      361 skqetllnel lqnldvtnkg grn
//
LOCUS       WP_010054235             294 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Carnobacterium].
ACCESSION   WP_010054235
VERSION     WP_010054235.1
KEYWORDS    RefSeq.
SOURCE      Carnobacterium
  ORGANISM  Carnobacterium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Carnobacteriaceae.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 294)
  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 294)
  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 294)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Carnobacterium"
                     /db_xref="taxon:2747"
     Protein         1..294
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31325
     Region          1..69
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          216..279
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mneigeklqe arkakgytld dlqqmtkiqk ryliaieegn fdvmpgkfya rafikqyadt
       61 vglngdqlle qytdavpqth deeyvekvnt nqtrsenhvt nelvekiknm lptilivllv
      121 faiiggiwya atktgnkddg siiskdadsv sitstseske ssqekesqss sskepekepe
      181 kpkqavavas stgatteytv tnatepgtit ltaqggaswv gvevngapad qktmqsgesl
      241 evplpagtts vsvrignaaa tsitlngeav afapeaagvi tqsltftitp vvaq
//
LOCUS       WP_010054532             252 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Carnobacterium].
ACCESSION   WP_010054532
VERSION     WP_010054532.1
KEYWORDS    RefSeq.
SOURCE      Carnobacterium
  ORGANISM  Carnobacterium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Carnobacteriaceae.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 252)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Carnobacterium"
                     /db_xref="taxon:2747"
     Protein         1..252
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=29178
     Region          4..239
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mkeadirvai taqnyelyyq pkfesvekkl igaealmrlk vngkvlgpdd fmpivnemeq
       61 metmqnflih evvtklnsee lvnydfsisl nmnssefvhk ehmdevllff knelinpnkl
      121 eieiterref pdfdlavsyl eklketgikv slddfgrgfn slaylrmlpi dvlkidrafm
      181 nevltdkkvq mivkaviqla hdldilvlae gmetkqqvef mdqmgcdtyq gfyfgspvpy
      241 avfqetwlpf lq
//
LOCUS       WP_010054653              68 aa            linear   BCT 20-JAN-2025
DEFINITION  zinc ribbon domain-containing protein [Carnobacterium
            maltaromaticum].
ACCESSION   WP_010054653
VERSION     WP_010054653.1
KEYWORDS    RefSeq.
SOURCE      Carnobacterium maltaromaticum
  ORGANISM  Carnobacterium maltaromaticum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Carnobacteriaceae; Carnobacterium.
REFERENCE   1  (residues 1 to 68)
  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 10577258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Carnobacterium maltaromaticum"
                     /db_xref="taxon:2751"
     Protein         1..68
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7724
     Region          7..>66
                     /region_name="Zn_ribbon_2"
                     /note="Putative zinc ribbon domain; pfam12674"
                     /db_xref="CDD:463667"
ORIGIN      
        1 maktnlcqsc gmplkdetdf gtekdgtlst kycekcyqdg ewtktdldfd gmyaynlkkf
       61 qesdmnki
//
LOCUS       WP_010057155             302 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Streptomyces globisporus].
ACCESSION   WP_010057155
VERSION     WP_010057155.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..302
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32638
     Region          1..296
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mlldtaslyf rayfgvpdsv rapdgtpvna vrglldfigr lvhdhrpdel vacwdndwrp
       61 qwrvdlipty kahrvaeetp agqtdeeeip dtlspqvpii edvlaalgia rvgvtpyead
      121 diigtltara kgpvdivtgd rdlyqlvdda rqvrvlyplk gvgtlqltde awlrekygvd
      181 gagyvdlall rgdpsdglpg vpgigektaa klldaygdld gimaavddpr akltpsqrkr
      241 ldesrayvav apkvvrvagd vplpdfdpal pgepldpaal ealaeqwgls gaiqrlltvl
      301 qr
//
LOCUS       WP_010059618             775 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: molybdopterin oxidoreductase family protein
            [Streptomyces].
ACCESSION   WP_010059618
VERSION     WP_010059618.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 775)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 775)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 775)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..775
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..775
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=85177
     Region          45..734
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mtadpraaad rrtfipldps lappgtrafr daggipadqw hadqngetlv pthccfcgvq
       61 cgmylrvdrg gkvfgveprn hdinrmrlcp kginayqqvn hpdrltaplm rrsrdeefre
      121 vsweealdft vseikriqqt ygndafgllg gaslfsekty lvgkfarval ksrhvdyngr
      181 lcmvsaagan klafgidrag npfsdilltd clliagsnvg ecfpvmtqyv wgardrgasl
      241 ivvdpretai artadihval kpgtdsafft svlnvvieeg ltdenfladh atgweelkak
      301 aaeyppsraa aicgipaeqi vqvarafara pkamawharg iehhsqgven clsvinlcaa
      361 tghigkpgag ygtitgqgng qggrehgqks dllpggrsim neehrrqice iwgieeselp
      421 pagtsmmemv wqmqrreirg ligicnnpfv slpnyrvvke gydttefhaq fdfflsetaa
      481 nahvvfpvtt waedegvman aearvvkhnk aqdpppgvrt dtwvicelar rlgagdkfdf
      541 pdsrsvfdel rvasagtvnd yygityerle etggiawpcp ttdhpgtprl fedgktyhpd
      601 grihlqvvew hppmdpydde hpmslttgrt vahflsgnqt rrlgalveqt prpwaeihps
      661 hgfrngepvr vvtrrgsevf palvteairp dtvfvpyhwp vptaanalti daldprskip
      721 eykvcacrie haeridevpa ppvapghvay petqvsrtdp lpptapqgrg tsers
//
LOCUS       WP_010061610             288 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Streptomyces].
ACCESSION   WP_010061610
VERSION     WP_010061610.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..288
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30193
     Region          1..254
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mridlhthst asdgtdtpae lvanaaaagl dvvaltdhdt vgghqqaida lpegltlvtg
       61 aelscrvdgv gmhllaylfd padaelerar elvrddrvpr aqemvrklra ldvpitweqv
      121 ariagdgsvg rphvaaalve lgvvptvsda ftpdwlgngg rayaekhefd pfeavrlvka
      181 aggvavfahp gaakrgavvp estiaalaea gldgievdhm dhdeptrarl rglarelgll
      241 ttgssdyhgs rktvelgayt tdpeiygeit rratgafpvp gaggavrr
//
LOCUS       WP_010062629             117 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein [Streptomyces].
ACCESSION   WP_010062629
VERSION     WP_010062629.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..117
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=12953
     Region          18..86
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 msenlwgyqp taghtvgtdl igykveatdg sigkvdkhsd dvtssylvvd tgvwifgkhv
       61 llpagtvsrv dnddkkiyvd ltkdqikdsp efdkdkhvgd adfhrttgey ygrhrrv
//
LOCUS       WP_010062967             388 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Streptomyces globisporus].
ACCESSION   WP_010062967
VERSION     WP_010062967.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..388
                     /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=43086
     Region          53..323
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mfhapsvfqr aplppatres eprhaqtlta taprpapgts apdaaapapa aakkrdpyfd
       61 nvkylaivlv avahawepvm dgsratraly mvvymfhmpa filisgyfsr sfdmtapkvk
      121 rlltsvvvpy lvfetayslf kryaddspdm aislvdpffl twflialfiw rvttpiwqai
      181 rhplpvalai amlasvspdi gddldlqrvl qflpffvlgl lvkpehfqlv rrrevrllsl
      241 plfagallfa ywaaprmqlg wfyransaqe mgapwwsgav mtlamfgcal vltvgflawv
      301 pgrerwftvl gagticgyll hgflikgaey aglfdrytwl sdpvglvvvs lvaavavtlm
      361 caplvgralk watepdmnwa frkvsarr
//
LOCUS       WP_010063805             116 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein [Streptomyces].
ACCESSION   WP_010063805
VERSION     WP_010063805.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..116
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=12739
     Region          2..>63
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mfeaenirdw rdhdvvdaeg skigslesvy vdtatdqpaf agviiglptr kritfvplnk
       61 avvapsylkv awpkqlvkda psidtdgell aeeeqavfah ykleygsgpg rrlarr
//
LOCUS       WP_010071454             200 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LytR C-terminal domain-containing protein
            [Streptomyces].
ACCESSION   WP_010071454
VERSION     WP_010071454.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 200)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..200
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=20609
     Region          84..173
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mggkyritgd typrmrrprh rrrlvlagig avvvlglagw gtlqlievft ggdksasaag
       61 hkrdcptakp svapakalpk paaikvnvyn attrtglaka aaeelkkrgf tigevgnask
      121 eydkkvpgtg vllgapaakn gsftvlgtql agtvqktdtr ktgevdlilg akfkafstpk
      181 eataamtalt kpapapspsc
//
LOCUS       WP_010072512             399 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Streptomyces].
ACCESSION   WP_010072512
VERSION     WP_010072512.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 399)
  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   5  (residues 1 to 399)
  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   6  (residues 1 to 399)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 399)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..399
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40609
     Region          14..77
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          77..379
                     /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 metpgsqtsl hranlervvr avrmagsltq aeiarstgls aatvsnivre lkdggtvevt
       61 ptsaggrrar svslsgdagi vigvdfghth lrvavgnlah qvlaeesepl dvdassaegf
      121 draevlvkrl ieatgigpdk vigvglgvpg pidvesgtlg stsilpgwtg inpseelsgr
      181 lgvpvyvdnd anlgalgelv wgsgrgvkdl ayikvasgvg aglvidgtiy rgpggtagei
      241 ghitldesgp vcrcgnrgcl etftaaryvl pllqpshgpg ltmervvqla regdpgcrrv
      301 igdvgrhigs gvanlcnlln psrvvlggsl aeagelvlgp irdsvsryai psaarqlsvl
      361 pgalggraev lgalalvlse mgdstllest lpvatpaft
//
LOCUS       WP_010074282              82 aa            linear   BCT 20-JAN-2025
DEFINITION  zinc ribbon domain-containing protein [Clostridium cellulovorans].
ACCESSION   WP_010074282
VERSION     WP_010074282.1
KEYWORDS    RefSeq.
SOURCE      Clostridium cellulovorans
  ORGANISM  Clostridium cellulovorans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
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 10577258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Clostridium cellulovorans"
                     /db_xref="taxon:1493"
     Protein         1..82
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=9269
     Region          3..81
                     /region_name="Zn_ribbon_2"
                     /note="Putative zinc ribbon domain; pfam12674"
                     /db_xref="CDD:463667"
ORIGIN      
        1 mnicqscgmp menqelngkn kdgsvnteyc vycypngefn kpdetleemv etcvpflvre
       61 gfteegakkh lestlkslkr wv
//
LOCUS       WP_010074677             428 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Clostridium cellulovorans].
ACCESSION   WP_010074677
VERSION     WP_010074677.1
KEYWORDS    RefSeq.
SOURCE      Clostridium cellulovorans
  ORGANISM  Clostridium cellulovorans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Clostridium cellulovorans"
                     /db_xref="taxon:1493"
     Protein         1..428
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=48568
     Region          9..427
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 meninipkni naeieilaii fnknnaisei eldtndfykp vhqqiytami elykeeqpis
       61 ivsvyskige fikenggisy ltniqntfkd sqikyyaklv kecsnkrkii kfakemmeka
      121 clgkekvgdi lssfsdkamk isdnnnkkpk hiseviietv geieeaynag gkitgmasgi
      181 knldrflngf qkgelvtiga rpsmgktafa leiaqglake nkglyfqfem rdtdmvkrli
      241 arntlidgyy inrgklndsd wskishsann lsqrnlwine dtnltifeif niakqqkmkq
      301 gldflvidhl llvkktnene rlaiaeitrq cklmakslni cvillsqlsr gvelridkrp
      361 llsdlkesgs ieedsdkvil lyrdeyynpd seekgvlead taknrngrvg alrlafnaky
      421 qfisdlei
//
LOCUS       WP_010074927             352 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Clostridium
            cellulovorans].
ACCESSION   WP_010074927
VERSION     WP_010074927.1
KEYWORDS    RefSeq.
SOURCE      Clostridium cellulovorans
  ORGANISM  Clostridium cellulovorans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Clostridium cellulovorans"
                     /db_xref="taxon:1493"
     Protein         1..352
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39413
     Region          1..331
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 myvelknikk tfkdfkasdd vsfgiekgkl igllgpsgsg kttilrmiag letpdsgdii
       61 idgvrvndie agkrgigfvf qsyalfrhmt vfdniafgln vqkqdkkkik arveelikli
      121 glegmekryp hqlsggqrqr vafaralapn phlllldepf aaidakvrqe lrtwlkktis
      181 elnitsifvt hdqdeaieva deiivtnkgr ieqkgtpmei yknpktpfva qfigesavie
      241 dysklkgfgd skftkaivrp efiqlaknka elkyihpvee givedvafrg ssiqitfkvg
      301 ditltayrsl ehdpikvgdk vfalifrlyv fndteayile nnamtdpmpv fi
//
LOCUS       WP_010075035             148 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Clostridium cellulovorans].
ACCESSION   WP_010075035
VERSION     WP_010075035.1
KEYWORDS    RefSeq.
SOURCE      Clostridium cellulovorans
  ORGANISM  Clostridium cellulovorans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 148)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Clostridium cellulovorans"
                     /db_xref="taxon:1493"
     Protein         1..148
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16051
     Region          3..148
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mdkllvkqme alitkedwli tnlsnasall wselqdinwa gfylirdgel vlgpfqgkva
       61 cthialgkgv cgtaavedst krienvhdfp ghiacdsasn seivipihss kgtvvgvldi
      121 dsplfgrfsv edqeilediv kivekafd
//
LOCUS       WP_010075268             289 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Clostridium cellulovorans].
ACCESSION   WP_010075268
VERSION     WP_010075268.1
KEYWORDS    RefSeq.
SOURCE      Clostridium cellulovorans
  ORGANISM  Clostridium cellulovorans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 289)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 289)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Clostridium cellulovorans"
                     /db_xref="taxon:1493"
     Protein         1..289
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33373
     Region          21..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..286
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mdwvkqlnes inyieenlag eisyeaiski agcsiynfqr mfsyiadkpl seyirnrrlt
       61 maafdllnst eriidislky gyesqdsftr afknfhgvlp ssvrnetvql kscpkrsfqi
      121 tikgenhmny qieqwpafrv mgisqkmkts tafemvpkvw enawkdgtmn rfiekfpdyr
      181 pagflgiaqg gqwgeseeme yiiavtnyvd vpscehvpal egmkefaype atwaifeang
      241 elpeaiqkvy kqfygewlpn sgyeladlpv iecymqdnhq evwiavikk
//
LOCUS       WP_010075653             182 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Clostridium
            cellulovorans].
ACCESSION   WP_010075653
VERSION     WP_010075653.1
KEYWORDS    RefSeq.
SOURCE      Clostridium cellulovorans
  ORGANISM  Clostridium cellulovorans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 182)
  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 182)
  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   3  (residues 1 to 182)
  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   4  (residues 1 to 182)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 182)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 182)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Clostridium cellulovorans"
                     /db_xref="taxon:1493"
     Protein         1..182
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=20553
     Region          1..173
                     /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"
ORIGIN      
        1 mkriiiafpr eqncngvvsi fkkigindiq icdsgikvle lvegstkgli icsyrlkdmf
       61 ssklinqipe gysmlmlvan pslcesidsr isvltlpink gnflatinml lnknkfkksl
      121 steenliiqk akdllikern fteqqahryl qvnsmnngrk mietskrile gsdnneeirn
      181 cn
//
LOCUS       WP_010075752             150 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Clostridium cellulovorans].
ACCESSION   WP_010075752
VERSION     WP_010075752.1
KEYWORDS    RefSeq.
SOURCE      Clostridium cellulovorans
  ORGANISM  Clostridium cellulovorans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Clostridium cellulovorans"
                     /db_xref="taxon:1493"
     Protein         1..150
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15984
     Region          1..>50
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mqgktgkerk gftlieliiv lavmaiiasi aipnfvsvrd nskrkadaqs cetikrmmis
       61 evvegsindg dtftylpsgp tltdtnntls tnteallake lkdvkkpqfk npiedtngdg
      121 eytevtgagv saptvytiii ssgnvqvkts
//
LOCUS       WP_010076174             194 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Clostridium cellulovorans].
ACCESSION   WP_010076174
VERSION     WP_010076174.1
KEYWORDS    RefSeq.
SOURCE      Clostridium cellulovorans
  ORGANISM  Clostridium cellulovorans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Clostridium cellulovorans"
                     /db_xref="taxon:1493"
     Protein         1..194
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21688
     Region          4..184
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdiiienilt rrstrkfkvd qirdedlsti leaakhapsg gnsqcwhftv iqnqeilkkl
       61 nylvreafak vvvdentyks irtgkaaaqn enycfyynap tliivsnein ygnamadsac
      121 aienmllaan alslgscyin qirwfyedea mrkvlteigi penhqvcgsv algyndglip
      181 atkkikegtv tfir
//
LOCUS       WP_010076429             235 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Clostridium cellulovorans].
ACCESSION   WP_010076429
VERSION     WP_010076429.1
KEYWORDS    RefSeq.
SOURCE      Clostridium cellulovorans
  ORGANISM  Clostridium cellulovorans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Clostridium cellulovorans"
                     /db_xref="taxon:1493"
     Protein         1..235
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26477
     Region          4..195
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mftrgdfhih ttasdgylnp rqvvmfaksr gidtiaisdh nsidgiyeas eagkefgvsv
       61 ipaielstrf ddesihvlgy fkddrynsld fhrilrlvka reaykvtgil dcyrkhhank
      121 hlstvdgifl lktcgasvvl ahpvrisekn lpwllnmpfd gieakysrst dyqirsfisv
      181 atekfsyyta gsdfhtneps drkhsligep fldsteiqkf leksealvlg ntsdy
//
LOCUS       WP_010076503             328 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Clostridium
            cellulovorans].
ACCESSION   WP_010076503
VERSION     WP_010076503.1
KEYWORDS    RefSeq.
SOURCE      Clostridium cellulovorans
  ORGANISM  Clostridium cellulovorans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 328)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Clostridium cellulovorans"
                     /db_xref="taxon:1493"
     Protein         1..328
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37265
     Region          3..328
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 menvkireie vyhgknivdn eyyiehfkkq gkdikkffee tmgrrnryei nrdtenaltm
       61 aiqssqavle kskltgkdid mivysgmlae yvsptsalfi hnaikgkeec fchdmngnci
      121 gmtyaldlvf rymssnpqin rlllvgsdyl tpqvspenee cygqygdvac alilertded
      181 cklidtkisv ntdfidyvrf pkcgfshiyd tpkedvyvdw ksfgtwwidg aveninsmld
      241 ksnlaindis mfcfsqiayk nvatlreklg igtekalyva dtygytgtts pflvfyegik
      301 ngqvkrgdyv vfctvaagst hislllky
//
LOCUS       WP_010077679             406 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Liquorilactobacillus mali].
ACCESSION   WP_010077679
VERSION     WP_010077679.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus mali
  ORGANISM  Liquorilactobacillus mali
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Liquorilactobacillus mali"
                     /db_xref="taxon:1618"
     Protein         1..406
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44560
     Region          2..391
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mskiiainag ssslkfklfe mnteqvlaqg lfdriglaqg aikikygade efktneeikd
       61 hsyavkrllg lmlnleiihe fseikgvghr vvaggeyfkr svainskvir kinslaeyap
      121 ihnpanlmgi kafkkilpta tavavfdtsf hqtmpkenyi fsvpyewyqk ygvrrygahg
      181 tshryvadva asmlkrplke lklischlga gasicaikng ksfdtsmgft pltgitmatr
      241 sgdtdvamia fmmqkldmhs mpeaiydlnk ksgllgisgv ssdmrdvmee sttnsraqla
      301 vdifvkdivk yigsytaemg gvdgiiftag igensaeirs avlkrlsymg ievdeeknll
      361 rgenivists sskvkalvip tdeelmiard vdkimkkknv ksaklv
//
LOCUS       WP_010077808             187 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Liquorilactobacillus mali].
ACCESSION   WP_010077808
VERSION     WP_010077808.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus mali
  ORGANISM  Liquorilactobacillus mali
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Liquorilactobacillus mali"
                     /db_xref="taxon:1618"
     Protein         1..187
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20445
     Region          1..187
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mkrlivgvtg asgsiyaidl lkklqqiptv evhlvlsmwa qkniaietdy klsdiqklae
       61 fnykaqdlga aiasgsfltd gmivvpasmk tvagiasgys ddlimraadv tlkeqrklvl
      121 vpretplspi hlenltklar lgvqiippip afyggpttiq dlldhqsmkl ldafqiennf
      181 rkrwsgd
//
LOCUS       WP_010078752             198 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Micrococcus].
ACCESSION   WP_010078752
VERSION     WP_010078752.1
KEYWORDS    RefSeq.
SOURCE      Micrococcus
  ORGANISM  Micrococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 198)
  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 198)
  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   3  (residues 1 to 198)
  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   4  (residues 1 to 198)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 198)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Micrococcus"
                     /db_xref="taxon:1269"
     Protein         1..198
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21741
     Region          11..196
                     /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"
ORIGIN      
        1 mstltppeet glravvaede tlirldlvev ltgagyrvva eagdgraave avrehrpdiv
       61 vmdvkmpvmd giaaageiag erlapvvmlt afsqrelver artagamayv vkpfteadlv
      121 paielavarf delrsleaev rdlgdrletr kivdrakall qermrlteae sfrwiqktsm
      181 drrltmreva qavidqvg
//
LOCUS       WP_010079485             262 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Micrococcus
            luteus].
ACCESSION   WP_010079485
VERSION     WP_010079485.1
KEYWORDS    RefSeq.
SOURCE      Micrococcus luteus
  ORGANISM  Micrococcus luteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Micrococcus.
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   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 262)
  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 262)
  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 262)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Micrococcus luteus"
                     /db_xref="taxon:1270"
     Protein         1..262
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28223
     Region          159..246
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(178,197..198,217,220,228..229,238,243)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mgqsagyvhi svrnaqrrad gmsrrgqara glrlaggtda pdsqtaptpv lapngipgpq
       61 avarenearg fvvyvgmdel aasaagtslt rlanelrhyv eslvpgaesh aavalapaga
      121 egrdlevvrq vlgdptvqgg arpdlaqapa pvstrqpgvl idlsrrevql dgeslnltfk
      181 efellnylve ngertvgree lldalwrnad evpnertidv hirrlraklg rlantvrtvr
      241 gqgyrfyrhp evvvwaapey si
//
LOCUS       WP_010079994             298 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phytoene/squalene synthase family protein
            [Micrococcus].
ACCESSION   WP_010079994
VERSION     WP_010079994.1
KEYWORDS    RefSeq.
SOURCE      Micrococcus
  ORGANISM  Micrococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Micrococcus"
                     /db_xref="taxon:1269"
     Protein         1..298
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31769
     Region          13..290
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 maaptpspaa lytrtahtaa aqvirrysts fswacrtlpr qarqdvatiy amvrvadevv
       61 dgvavaagld eagvraaldd yeraceaama sgfatdpvlh afadvarrhg itpeltrpff
      121 asmradlgir ehgaeslday ihgsaevvgl mclqvflslp gtrartpgqr qelraqasrl
      181 gaafqkvnfl rdlaadhhel grtylpgaap gvltearkae lvaevradld aalpgirvld
      241 pgagravala hglfaalvdr ieatpaaela hrrvrvpdhq kariaarvla rgrrggrr
//
LOCUS       WP_010080517             335 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Actinomycetes].
ACCESSION   WP_010080517
VERSION     WP_010080517.1
KEYWORDS    RefSeq.
SOURCE      Actinomycetes (high G+C Gram-positive bacteria)
  ORGANISM  Actinomycetes
            Bacteria; Bacillati; Actinomycetota.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 335)
  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   4  (residues 1 to 335)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Actinomycetes"
                     /db_xref="taxon:1760"
     Protein         1..335
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=35900
     Region          11..327
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mstdrdagae irlesltkly pgqdrpavda ldliipaget vvfvgpsgcg kttslkminr
       61 lieptsgril iggeditrrd ptrlrrqigy vvqgggmmph lsvaenvglv prllkwdrrr
      121 iadrvdelld lvgldpaiyr drfprelsgg qqqrvgvarg laadppvllm depfgavdpl
      181 trkrlqqeml diqarvgkti vmvthdvdea vllgdrilvl epgahvaqya tpeevlarpa
      241 tefvadfvgs gaglkrlglr svdslplrpi ahhptgtlpg gpvldaatpi sealaalvta
      301 pteeiavvrd gtviglldyp tlrahvragg eqarp
//
LOCUS       WP_010080580             136 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Micrococcus luteus].
ACCESSION   WP_010080580
VERSION     WP_010080580.1
KEYWORDS    RefSeq.
SOURCE      Micrococcus luteus
  ORGANISM  Micrococcus luteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Micrococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Micrococcus luteus"
                     /db_xref="taxon:1270"
     Protein         1..136
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=14150
     Region          26..112
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(39..40,47,50,52..53,55,58..59,61,67,72,79)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(39,67..68,70)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mtdhpvlpga rhrddgpltl geglealarl vppghavsyg glagllgagg prqagramae
       61 sspgtpwwrv vradgslppe laaraavehe reatprtpag rvdlrrarwe pddgaarair
      121 aiadrivsgp garmrp
//
LOCUS       WP_010089113             233 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Burkholderia
            ubonensis].
ACCESSION   WP_010089113
VERSION     WP_010089113.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ubonensis
  ORGANISM  Burkholderia ubonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Burkholderia ubonensis"
                     /db_xref="taxon:101571"
     Protein         1..233
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=25273
     Region          1..>219
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mslvvdirkt yasaerrfal dvsfaatsqr vvlfgpsgag ksltlqaiag lltpdagtia
       61 ldgeplfdaa rgidvptrar rvaylfqdya lfphlnvrqn iafgltpglr nprakalppe
      121 vaywlrafel ealasqypaq lsggqkqrva laraliaqpr illldepfaa ldgamrqrmr
      181 helaelqarl dipmvlithd pddvaafgdq vvqlsdgrvr tasahaawpt rvv
//
LOCUS       WP_010087871             221 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [endosymbiont of Riftia pachyptila].
ACCESSION   WP_010087871
VERSION     WP_010087871.1
KEYWORDS    RefSeq.
SOURCE      endosymbiont of Riftia pachyptila
  ORGANISM  endosymbiont of Riftia pachyptila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            sulfur-oxidizing symbionts.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 221)
  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   3  (residues 1 to 221)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="endosymbiont of Riftia pachyptila"
                     /db_xref="taxon:54396"
     Protein         1..221
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24242
     Region          22..213
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 msdiirtlqi gdtlqlqhap psdipdrygv kligylpnes lvittprkqg kailvregqn
       61 ftvrvlqgsn vfgfvsrvmh aaarpyphlh laypedvasa vvrnaprvst tldtkvrntn
      121 vadtpenhla akiadlsnsg arlitkkpig sigdmiqiql nidvcngsds mqimgeiknl
      181 refelegqgs qfvhgvqfkg vnrfqqlllc ayvlsqitte r
//
LOCUS       WP_010089949             388 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Burkholderia ubonensis].
ACCESSION   WP_010089949
VERSION     WP_010089949.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ubonensis
  ORGANISM  Burkholderia ubonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 388)
  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 388)
  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   3  (residues 1 to 388)
  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   4  (residues 1 to 388)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 388)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 388)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 388)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Burkholderia ubonensis"
                     /db_xref="taxon:101571"
     Protein         1..388
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39828
     Region          34..369
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(109..111,132..133,182,234,258)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkisfvpasl awsaaalias tsavaqsapq tiliglaapl tgpsarigkd lqngaqlaid
       61 danakhpsig gkpvvyklva addqsdprta vavaqqlvdk hvvgvvghwn tgcsvpasrv
      121 yrdagiaqia pastghqytq qgyatafrim ghddaggnft gayavktlka kriaviddrt
      181 sfgagladqf ikgveasgga ivdrqyvndk ttdfsgvlta ikgkradlvf fggldaqaap
      241 larrmrqlgv napllgaggf vsqtflslag kdgegvtale pglplarmpg gsafdaqyqs
      301 ryhapielha pfaydaaatl iaatqkagtt qpaklvaavr aidrpgvtgr iafdgagnln
      361 npaftiyqvr ggkwtvvdvl ggaraask
//
LOCUS       WP_010090335             325 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia ubonensis].
ACCESSION   WP_010090335
VERSION     WP_010090335.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ubonensis
  ORGANISM  Burkholderia ubonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 325)
  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 325)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 325)
  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   4  (residues 1 to 325)
  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 325)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia ubonensis"
                     /db_xref="taxon:101571"
     Protein         1..325
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35588
     Region          37..186
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          214..295
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msfqplfada gdrvqrrmid llarlapneg ftqadmegvr firanrpvpr mpvlyepsiv
       61 vvcqgrkhgy lgdqsfiyda qqylvlsvpl pfecetfane depfltisir vdlaviaela
      121 illdetrgva vseprgvyst pldapladav lrllealasp hdtrvlgpsi mreiayrvlt
      181 gargdairaa lvqqhqfgri akalrrihad ltgdldvdtl areagmsvav fhaqfksvta
      241 tspmqyvktt rlhqarlmmv qdgigagaaa arvgyasasq fsrefkrlfg rspgdevrwm
      301 retggrtigg gavidywtde ravga
//
LOCUS       WP_010090556             441 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Burkholderia
            ubonensis].
ACCESSION   WP_010090556
VERSION     WP_010090556.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ubonensis
  ORGANISM  Burkholderia ubonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 441)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia ubonensis"
                     /db_xref="taxon:101571"
     Protein         1..441
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=49157
     Region          16..420
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mngkaikpdv sealdlhvgt aglpvgqlly vsqgrrelsq fvydeawlah pdrfeispdl
       61 plqsgyqtrr apravdsvfh faladtepda wgrrvidrah aklrrtqpdl rplneldylc
      121 avddfsrvga lrlcragryl rteedgrrtt ppfieleria datraieagt dtaedlrylq
      181 gkgtslggmr pkctvldehg rlaigkfpsi gdtisvtrae vlalrlaraa gidaagarcv
      241 kvggtpvali erfdrtddgr ripylsaasm lqasreeeha yteivdvmqq rgarplddar
      301 qlwrrlvfnl litntddhlq nlgflydgdg rwrlapafdv npmpgklhes ktwlsedtgp
      361 idsidmllda cgyfsltreq alavtgevfd avqgwrrigq saeigmtare lddlddafeh
      421 aqtewarall grpmrrtahe r
//
LOCUS       WP_010091751             117 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Burkholderia ubonensis].
ACCESSION   WP_010091751
VERSION     WP_010091751.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ubonensis
  ORGANISM  Burkholderia ubonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 117)
  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   2  (residues 1 to 117)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Burkholderia ubonensis"
                     /db_xref="taxon:101571"
     Protein         1..117
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11414
     Region          20..78
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mikqwfaaaa llgaiasawa avdvntaged aligikgigp arakailder sahgpfknad
       61 dlaarvkgmg ghtverlqre gltvgaagag aapaaakpaa apattpakpa aartaqk
//
LOCUS       WP_010092265             611 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup, partial [Burkholderia ubonensis].
ACCESSION   WP_010092265
VERSION     WP_010092265.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ubonensis
  ORGANISM  Burkholderia ubonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 611)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 611)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 611)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 611)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 611)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 611)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..611
                     /organism="Burkholderia ubonensis"
                     /db_xref="taxon:101571"
     Protein         <1..611
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
     Region          1..611
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 aaigvvfgdi gtsplyslke afspahgipl tegsilgvis llfwaiilvv gvkyllfvmr
       61 adnngeggvl almalslrpl nsksrvtgal malgifgacm fygdavitpa isvmsavegl
      121 eiatphlshl vlpitivili alfwiqrhgt atvgklfgpi mvlwfvaiaa lgvyhivrvp
      181 givaainpyy avsfmsdhll qayvvlgsvv lvltgaealy admghfgakp iriaayglvm
      241 pslvlnyfgq galliqnpka ienpffllap dwallplvvl stvatviasq avisgayslt
      301 sqaiqlgyvp rmkvlhtsel aigqiyvpvv nwlllfvilc ivigfkssdn laaaygiavt
      361 atmvittvla avvmvkvwnw nrllvgaiia vflavdlgff ganllkvaqg gwlplgigal
      421 lffllmtwyk grhivkerta adgiplepfl qgllahpphr vsgtaiyltg ndklvpvsll
      481 hnlkhnkvlh ertifltfvt rdipyvrddk rlaardaggg lymvtaeygf netpdvkavl
      541 eefgrthdmt felmdtsffl aretvvptql pgmsiwrerv fawmhqnaak ptdffaipan
      601 rvvelgtkie i
//
LOCUS       WP_010093399             677 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Ornithinibacillus scapharcae].
ACCESSION   WP_010093399
VERSION     WP_010093399.1
KEYWORDS    RefSeq.
SOURCE      Ornithinibacillus scapharcae
  ORGANISM  Ornithinibacillus scapharcae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Ornithinibacillus.
REFERENCE   1  (residues 1 to 677)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 677)
  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   3  (residues 1 to 677)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Ornithinibacillus scapharcae"
                     /db_xref="taxon:1147159"
     Protein         1..677
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=75369
     Region          1..677
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          172..249
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 mdttqyldvf idesnehiev lykkllelek dptekaiiee ifraahtlkg msatmgyndl
       61 aklthtlenv fdairydkvq vqsemidllv etvdhlnamv ediasggngs qditdvanql
      121 eaiekgevvv pkekietvqe vvtaqnssvf tkldefelsi lnesnergfq nfevsvqlre
      181 dcllkgarvf mvfevleqlg eviksnpsvt dledenfdys fsvilvssak eneiaekikk
      241 vseiekvtvd afsvnnyldr ketelttpvt nevntvedkk veknestdse ntksshnkti
      301 rvnidkldvl mnlfeeliid rgrleqiste lrntelqesv ermsrvssdl qniiltmrmv
      361 piehvfsrfp rmirklardl dkqvdleiig adteldrtvi deigdpivhl lrnaidhgve
      421 tpevrlqkgk pekgtiklka fhsgnhvfie iaddgagink ekvlkkaien givsendkdt
      481 ltdqqiygli mesgfstadk isdisgrgvg ldvvknties lggsitidse ynkgsvfsiq
      541 lpltltiisv llvelnkeky aiplssiiet aivskeqils ahhkkvidfr gkvvplvnlk
      601 eifdvpnadh deeytsiviv kkgekmaalv vdsfigqqev vlkslgayls stfaisgati
      661 lgdgqvaliv dsnavik
//
LOCUS       WP_010092760             426 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Burkholderia ubonensis].
ACCESSION   WP_010092760
VERSION     WP_010092760.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ubonensis
  ORGANISM  Burkholderia ubonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 426)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Burkholderia ubonensis"
                     /db_xref="taxon:101571"
     Protein         1..426
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=46813
     Region          32..255
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mpqtrglsle sllerltptp sgwvtdyrgv tlrsvfqpvl sithkrvvgy eallratdan
       61 getlspgalf dkaqgdadal lldrlarclh tanfvaqgig dgwlflnvtp rvldsglvqr
      121 efvellckhf alppnrvvle vveqpsrdea alartidmiq hrdfliaidd fgtgfsnfdr
      181 vwrakpdivk ldrslverat wsaedrrimh hlvsmlhqag amvlaegves ddalqalmea
      241 didfvqgfqf grpdpsiara saaapallda awkrfiarrh aqtsaaqpgf daierlvlag
      301 aaafaasgdl rnaaqrvlvm psarrvfvtn eigeqflpsi saqpdernpa ttrlaplfpe
      361 thsnwsrrpy fqraiaapgr valmgphfsl tegrdcytaa vatrvhdrlv vfcvdfvlds
      421 agtimr
//
LOCUS       WP_010093087             379 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Burkholderia ubonensis].
ACCESSION   WP_010093087
VERSION     WP_010093087.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ubonensis
  ORGANISM  Burkholderia ubonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   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 379)
  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   3  (residues 1 to 379)
  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   4  (residues 1 to 379)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 379)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 379)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 379)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia ubonensis"
                     /db_xref="taxon:101571"
     Protein         1..379
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40029
     Region          29..365
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(105..107,127..128,177,229,253)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mqhtmkklag atfvavmsla gtahaddvkv gyagpmtgaq ahygkdmqng ivlaiedfna
       61 tkpviggkpv kfvldtqddq adprtgttva qklvddgikg mlghfnsgtt ipasriyana
      121 gipqiamata peytqqgykt tfrmmtsdtq qgsvagtfva kdlglkkiai vddrtaygqg
      181 ladqfekaak aagativlre ftndkavdfk ailtklkaaq pdivyyggad sqaapmvkqm
      241 kalgfkaplm ggemvktptf lkiagdaadg tiaslaglpl dempggksya dkykkrfged
      301 vqtyspysyd gamalfnamk kanstdpaky lpllaktdma gvtsthlayd akgdlknggi
      361 tmykvekgew kplksiggk
//
LOCUS       WP_010094507             165 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein, partial [Burkholderia ubonensis].
ACCESSION   WP_010094507
VERSION     WP_010094507.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ubonensis
  ORGANISM  Burkholderia ubonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 165)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Burkholderia ubonensis"
                     /db_xref="taxon:101571"
     Protein         <1..165
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <21..146
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 lghgtiapav aaalagaglt pdrleievte tallhdegka vadlralram gvrvalddfg
       61 tgfsslahlr afpfdkikid gsfvrdavtr pdcaavvcav adlgkrlgvt tvaegvetee
      121 qlacitqagc revqgfllgr pepgerdapa vqwieraala akkra
//
LOCUS       WP_010094956             247 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Ornithinibacillus scapharcae].
ACCESSION   WP_010094956
VERSION     WP_010094956.1
KEYWORDS    RefSeq.
SOURCE      Ornithinibacillus scapharcae
  ORGANISM  Ornithinibacillus scapharcae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Ornithinibacillus.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 247)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Ornithinibacillus scapharcae"
                     /db_xref="taxon:1147159"
     Protein         1..247
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=28267
     Region          <20..234
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 minqyrnnim ddldiyhviq piidldrnnv fgyemllrsr efnnpelllk kaeesnqlye
       61 ldmhsirkaf etinnkantl nglyifinil pstignpasf kkieqlkssl klttgsvvle
      121 lteerkeael emcvrmvdei knkgfliald digkgestlp yvielepniv kldqyfsrdl
      181 anspkkqkai ellfhlidee timilegien eadlqaakkl gvryaqgyhl gkpqvlnyyl
      241 anseqvv
//
LOCUS       WP_010095633             281 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Ornithinibacillus
            scapharcae].
ACCESSION   WP_010095633
VERSION     WP_010095633.1
KEYWORDS    RefSeq.
SOURCE      Ornithinibacillus scapharcae
  ORGANISM  Ornithinibacillus scapharcae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Ornithinibacillus.
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
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Ornithinibacillus scapharcae"
                     /db_xref="taxon:1147159"
     Protein         1..281
                     /product="aminoglycoside 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=32281
     Region          5..195
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mkigkklgeg anaevfewed ntkviklaks ninrtdlere fnnsltvwnl glavpkpyem
       61 idyhdrpgiv yerifgktlr erffenlipq nhvdsnldwn darlsarila kvhntlshke
      121 ipsqqrdflk rqilsvnyls efekeavldi lnslpakdni chgdanpnnl lfsneqpili
      181 dwmnasngnp eadlaefiim iryailppet psnalklfds nrekiiaefm eeytnltgtt
      241 ynevdpwivp iaarklstdg ifedeklllv neirirlenk n
//
LOCUS       WP_010095821             339 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia ubonensis].
ACCESSION   WP_010095821
VERSION     WP_010095821.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ubonensis
  ORGANISM  Burkholderia ubonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 339)
  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 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 339)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 339)
  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   5  (residues 1 to 339)
  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   6  (residues 1 to 339)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia ubonensis"
                     /db_xref="taxon:101571"
     Protein         1..339
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38071
     Region          33..218
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          107..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkpvadvshr taaqrpaplh tifitldfmk rmgvpvdvll rgtgispsdi erpnamvtha
       61 qemvlfanal eatgnsaigl hignaipvts yglrahamlv sptlgdalrl gfehpllgis
      121 yfrmrittkg dvaritvggy tyradllvln tdmvftairr emrdligryp eflrigftfp
      181 epphfesyea yfdcpiefns sesfiefdrs ileielplah piefelakka cskrefelah
      241 wvpsdligrl lglmyeypac qdvaefsrql gislrslqrk lqemgtsfsa mhnlvrqdlt
      301 sqylakkeys ikeiaarlgy kntsafsram krwskgsae
//
LOCUS       WP_010095939             220 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Ornithinibacillus scapharcae].
ACCESSION   WP_010095939
VERSION     WP_010095939.1
KEYWORDS    RefSeq.
SOURCE      Ornithinibacillus scapharcae
  ORGANISM  Ornithinibacillus scapharcae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Ornithinibacillus.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 220)
  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   3  (residues 1 to 220)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Ornithinibacillus scapharcae"
                     /db_xref="taxon:1147159"
     Protein         1..220
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25417
     Region          9..218
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mkigvfltie ayseehkqne kyrckvvdkd nkylyidypv hlkmkrtsas frvgtrmkae
       61 ylgddqsvyr fktevkkrnk gkiptlalei pesdkieriq rreyvrieta vdvalhsvyd
      121 nfapfatvsv dlsggglsvv vpkdihindg eeimvhlvlp mqsgeyhyle lkgeiirlih
      181 nvnsantasi klksldeldk qiiirfcfek qrearqkemh
//
LOCUS       WP_010095940             383 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Burkholderia ubonensis].
ACCESSION   WP_010095940
VERSION     WP_010095940.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ubonensis
  ORGANISM  Burkholderia ubonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 383)
  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 383)
  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   3  (residues 1 to 383)
  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   4  (residues 1 to 383)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 383)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 383)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 383)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Burkholderia ubonensis"
                     /db_xref="taxon:101571"
     Protein         1..383
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39979
     Region          33..369
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(109..111,132..133,182,234,258)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkfrirslsg aalaaatlvl pagaalaqet vvkvgvagpl tgggaaygkd iengvrmavd
       61 eanaarptig gkpvkfvvas qddqsdprag vqaaqqltda qvavvighfn sgttlpaski
      121 yakagipmit psatnpeitr aglgtvyrvi atdtqnagna gayaasvtka kriailddrt
      181 afgqgeadef ekavkanggt ivtreftndk avdfsaqltk iksvnadlvf fggldaqaam
      241 lvkrmrqlgi kaqflagggv mnanfirlag gaaegasvwe ygqplarlek grtfetkfrq
      301 kygvdmlaya pfaydatwia ikamenanst kpadfngalk rtrydgitgt iaftdtgdlk
      361 npsstlyevk naawqpvttk san
//
LOCUS       WP_010096419             795 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Ornithinibacillus scapharcae].
ACCESSION   WP_010096419
VERSION     WP_010096419.1
KEYWORDS    RefSeq.
SOURCE      Ornithinibacillus scapharcae
  ORGANISM  Ornithinibacillus scapharcae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Ornithinibacillus.
REFERENCE   1  (residues 1 to 795)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 795)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 795)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..795
                     /organism="Ornithinibacillus scapharcae"
                     /db_xref="taxon:1147159"
     Protein         1..795
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=89936
     Region          25..795
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 msepslaenl sekklqnwkk iiflivgvll ailligvffv nayinkslpq vegtieipgl
       61 qdevivttde hgvphiqasn dhdlymaqgy mqaqnrifqm elsrrqasgt lsevvgesti
      121 nqdkyfrtlg lrraaeksyq iysdeskqil qwfadgvnty inqakesnsl pieftligse
      181 paewtpidsl tigkfmafdl gghwerqafn yyvlnefnee kayelfpvyp etkptiiqed
      241 eivdvassfe kaviphpfng snnwvvsgek tqsgmpllad dphlglatps iwmqmhlqtd
      301 elnvsgvifa gvpgiilghn dyiawgvtnt gpdvqqlyle kqnpdnpney lfdeeweeat
      361 iieepikvkd getidyqvve trhgpivsef aensgkntvm slrwtaldat teleailemn
      421 qaknwkefek glekflvpaq nfvfaskdgt iaykangkip iyensedali plpgwdptyi
      481 lneyipfdel pkvvnpkkgy iatannkvag neypyhisnv waqpyryeri aevleandtl
      541 tkedmmalqm dqtnlqaref vpmfldmlkd sklskyeaqa lslltewdyv dnvdavqpli
      601 fhhwinsied ilynelpdgv mdlfnsrgqt tdellrkaas gegsiwvden gglesvlhvs
      661 lqqtieklte sygedmdtwk wgdyhqvqfh hplsavhpvl ayffnngdpv pvggsnvtpm
      721 aaafetetge vdhgaswrfv idmedpttgy hivgpgqegh frsdwyhnqi ddwvegiyhe
      781 tklipengkv lhlvp
//
LOCUS       WP_010097103             249 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Ornithinibacillus
            scapharcae].
ACCESSION   WP_010097103
VERSION     WP_010097103.1
KEYWORDS    RefSeq.
SOURCE      Ornithinibacillus scapharcae
  ORGANISM  Ornithinibacillus scapharcae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Ornithinibacillus.
REFERENCE   1  (residues 1 to 249)
  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   2  (residues 1 to 249)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Ornithinibacillus scapharcae"
                     /db_xref="taxon:1147159"
     Protein         1..249
                     /product="aminoglycoside 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=28283
     Region          6..>87
                     /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"
     Region          <49..219
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mnpdtligkg ntaniylvgn qiqkvfhdrf tvaeatyeak kqiiafdngl tvprvldvtt
       61 ienkaviime yikgrtlgel lledidnaey ylniavdihm qihsiettsl enmkdrlesk
      121 iegapilqps hkrilmkhle qmplrtklch gdfhpfniim gkegstvidw vdassgdkha
      181 dvfrtyllys qhsielaeqy vaiyceksgl lkeeifewap iiaaarlsdk astedierll
      241 rivndfynm
//
LOCUS       WP_010097285             220 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Ornithinibacillus scapharcae].
ACCESSION   WP_010097285
VERSION     WP_010097285.1
KEYWORDS    RefSeq.
SOURCE      Ornithinibacillus scapharcae
  ORGANISM  Ornithinibacillus scapharcae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Ornithinibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Ornithinibacillus scapharcae"
                     /db_xref="taxon:1147159"
     Protein         1..220
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=25268
     Region          46..218
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkivihsail yliilivips prisakeiyh sghdllvhqm ylpidnsepr neevttivih
       61 sisnvlanpd spyritdvyq llkeyglsth yiidrsgeif qlvpdyrvay hagrssfpyl
      121 pffphnmnqf sigielmgig tkdemlsivp ealydaldkn ligyteeqyq slswllaqlh
      181 qkypsigrdr fhvigheeya pgrksdpgkl fhwekifetk
//
LOCUS       WP_010098155             251 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Burkholderia ubonensis].
ACCESSION   WP_010098155
VERSION     WP_010098155.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ubonensis
  ORGANISM  Burkholderia ubonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  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   3  (residues 1 to 251)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Burkholderia ubonensis"
                     /db_xref="taxon:101571"
     Protein         1..251
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27735
     Region          42..249
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mnielsmdps qdaghsgpdy arrnpleigv qlrnlvnrgd fltveypggq lvtrllevdv
       61 gartftfdwg alaeqnsgil aaahckfsas pegvrvefgt gapretryeg lpafeadfpd
      121 vlyciqrrey frvdapiidp ylcrgklpdg esflfevhnl slggvglrta dervaalelg
      181 tvlpdvelel nghgklsldl qlvsqrstev pngtrryqlg frfmslpgsa entlqrlitq
      241 lemkrrqlar a
//
LOCUS       WP_010098471             301 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Burkholderia
            ubonensis].
ACCESSION   WP_010098471
VERSION     WP_010098471.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ubonensis
  ORGANISM  Burkholderia ubonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia ubonensis"
                     /db_xref="taxon:101571"
     Protein         1..301
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32361
     Region          20..261
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mqqqiqaara tllvdsrntl gegatwcdat dtlywvdier arlwrcradg tgaaswpmpe
       61 rlacfaltde pdvllvglat hlaffdlrte tftrivdvep glptrlndgr cdphgafvfg
      121 mkdeggeppr avggfyrlna dlalerlvlp paaiansiaf spdgskmyfc dslvreilvc
      181 dygragtsgv rsfarltdad gdpdgstidr dgglwnaqwg grrvvrygpd gveteriavp
      241 taqpscaald dagrlyvtsa rvglsdaala sdahaggvfv aqtrhaglpt trfplkrtmr
      301 g
//
LOCUS       WP_010100934             296 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Burkholderia
            oklahomensis].
ACCESSION   WP_010100934
VERSION     WP_010100934.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia oklahomensis
  ORGANISM  Burkholderia oklahomensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Burkholderia oklahomensis"
                     /db_xref="taxon:342113"
     Protein         1..296
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31845
     Region          17..269
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mhastsveri gdmrcgvges pvwhageaal ywtditgral wrwesetnra hawalpemag
       61 siamiadggi alamqtgvyr vprpapgapl pepvllagva haadgmrfnd grcdrqgrfw
      121 agtmacdtsl arasgrlyrl dsnaralaae cdalivpngl afspdgrtmy lsdshptrri
      181 vwafdydvda grphgrrvfv dmnahagrpd gaavdedgcy wicgidsgyv hrftpdgrld
      241 rsiavpvakp smcafggarc dtlfvtsirt dddplsgatf aldprarglp epamrl
//
LOCUS       WP_010102562             345 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia oklahomensis].
ACCESSION   WP_010102562
VERSION     WP_010102562.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia oklahomensis
  ORGANISM  Burkholderia oklahomensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 345)
  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 345)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Burkholderia oklahomensis"
                     /db_xref="taxon:342113"
     Protein         1..345
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38450
     Region          33..220
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          264..342
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 matsvpdptr qlnkatvssa yalfmlmlae ergiadadil antgvtrakl eepdaritpl
       61 qqaaivfnll gktndpsiai eiglrssltk sgmigfglms catlgeaiql girylptrvp
      121 ffsirltele htvqidvlea fplgrlrqfa venfmvetai lfnslltpsh drtmkanael
      181 cfewpeppyf aryrdrlprc hfdapanqir ceaalldepi ktanaqtaqm ivqqceaela
      241 rlgyaesive rvrnllirgs dgypsldala relhlsertl krklsdygtt ysalldeirl
      301 rdalrllegt qltveeiavr vgytdranfs rafrrwtgas pssrr
//
LOCUS       WP_010102826             340 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia oklahomensis].
ACCESSION   WP_010102826
VERSION     WP_010102826.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia oklahomensis
  ORGANISM  Burkholderia oklahomensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 340)
  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 340)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 340)
  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   4  (residues 1 to 340)
  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 340)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Burkholderia oklahomensis"
                     /db_xref="taxon:342113"
     Protein         1..340
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37576
     Region          28..212
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          255..337
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtvklarwdf vrpvnttrvl vdvgveqglg vcqcldgsgv apelldrpea avaaaqelri
       61 vrnlmrllgp dfplgietgr ryhataygiw gfallssatf adavsvglry lqltstfcdi
      121 rptvrgedat lviddhdlpg dvrdvlveit vaalitlqvd ldaanlpvkr lafkmeapsy
      181 adrfrtlfaa spefgaaena ltvdvrcldl klpqrnsltr rlcedecrrv lerrrrsegw
      241 agrvrrhlag dsarrptmaa laaelgvsar tlrrrlageg tdyetvvdei retlaeella
      301 tttltvaeis erlgysepsa farafrrwka mspseyrwsa
//
LOCUS       WP_010103270             630 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Burkholderia oklahomensis].
ACCESSION   WP_010103270
VERSION     WP_010103270.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia oklahomensis
  ORGANISM  Burkholderia oklahomensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 630)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 630)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 630)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 630)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 630)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Burkholderia oklahomensis"
                     /db_xref="taxon:342113"
     Protein         1..630
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68481
     Region          1..630
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mtdtnhsstr qhslqslaia aigvvfgdig tsplyslkea fspahgiplt qssilgvisl
       61 lfwaiilvvg ikyvlfvmra dnngeggvla lmalslrpln pksritglmm algifgacmf
      121 ygdavitpai svmsavegle vaapqlshlv lpitivilia lfwiqrhgta mvgklfgpim
      181 vlwfvtiavl gvyhiarapm vvaainpyya fsfmsehvll ayvvlgsvvl vltgaealya
      241 dmghfgakpi rlaayvlvmp slvinyfgqg alllldpkai enpffllapq waalplvvls
      301 tvatviasqa visgayslts qaiqlgyvpr mkilhtsdla igqiyvpvvn wlllfvilci
      361 vigfkssdnl aaaygiavta tmvittilaa vvmvkvwnwn kllvsliigv flvvdlgffg
      421 anllkveqgg wlplgigaml ffllmtwykg rhivkertaa dgiplapflq gllahpphrv
      481 sgtaiyltgn dklvpvsllh nlkhnkvlhe rtlfltfvtr dipyvkdder vtiqdagegl
      541 yivkaeygfn etpdvkavle evarqrgitf elmdtsffla retvvpthlp gmsiwrervf
      601 awmhqnaakp tdffsipanr vvelgtkiei
//
LOCUS       WP_010103882             283 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein, partial
            [Burkholderia oklahomensis].
ACCESSION   WP_010103882
VERSION     WP_010103882.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia oklahomensis
  ORGANISM  Burkholderia oklahomensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Burkholderia oklahomensis"
                     /db_xref="taxon:342113"
     Protein         1..>283
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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]"
     Region          1..>283
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mgitvrnlhk rfgdftaldd vtldfpagel vallgpsgcg kttllrviag lehadsgqvv
       61 lqgldvasvg arerqvgfvf qhyalfrhmt vyenvafglr vkprrerpse aairdkvhel
      121 lslvqldwla qrypselsgg qrqrialara lavepkvlll depfgaldak vrkelrswlr
      181 rlhddlhist ifvthdqeea levadrivvl dhgrveqvgs pqdvydhprs afvyeflgaa
      241 nrldgtvngt gfvangaaga iavdadfagp arayvrphdl alv
//
LOCUS       WP_010104830             843 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Verminephrobacter
            aporrectodeae].
ACCESSION   WP_010104830
VERSION     WP_010104830.1
KEYWORDS    RefSeq.
SOURCE      Verminephrobacter aporrectodeae
  ORGANISM  Verminephrobacter aporrectodeae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Verminephrobacter.
REFERENCE   1  (residues 1 to 843)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 843)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 843)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..843
                     /organism="Verminephrobacter aporrectodeae"
                     /db_xref="taxon:1110389"
     Protein         1..843
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=92490
     Region          6..836
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 maswikwvvv glgvaillag savavyvqrs favldgrlav vglrqavqvq rddadvthir
       61 aqtpqdawfa mgyvhaqers wqlefnrrvm hgelsevfgg atletdklmr aldiignarr
      121 qyqglppyar qalqsysqgi qafhrhrsqa lppefhllgv epggwepeds vgwalmmale
      181 mggnwgheft rlsvastldt erlwqlmppy pgerpatsvd latlyrqlgv yraadqgaap
      241 qgaapkhqaq qegllsrqis aglrawaeal trtagshegr gsnnwalags rtvsgkplla
      301 ndphldlsap siwylaalqa pagraadgtp iapidvigat mpglpfvvlg rtghvawgft
      361 ntdpdvqdly leqinpadat qyrtpegwap ftvrsetirv kgeadqvirl rstrhgpvls
      421 daqeshagtl nldkyvlalr wsaldadnqt vlaglqtnqv qtvdelfqal ssyhspmqnv
      481 vaaddrgqir fqavgrvpir aaandirgva papgwearyd wqgwiapgkt prddgakgwl
      541 atanqrvtap dypyyltqdw tlpyryqria qliearekhd vasmqamqgd vtslavrrll
      601 pylrqvrsah plaaaaqaql adfdgvmdag qaapllfsaw vdelvrglia priglerfaa
      661 tyggerdyra avegilernd gwwcqplsca gqsaaafdra ldrlqmaygp dparwrwgva
      721 hpalsvhrpm gsvpvlahff nvrhaspggp ytvnvgqynp gdakglfvnh haaslravyd
      781 ladleqsrfi cqtgqsglvf ssryrdmnsp wanmgyrllq rqpahwahel tlvpggdrsf
      841 tpd
//
LOCUS       WP_010104567             376 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Verminephrobacter aporrectodeae].
ACCESSION   WP_010104567
VERSION     WP_010104567.1
KEYWORDS    RefSeq.
SOURCE      Verminephrobacter aporrectodeae
  ORGANISM  Verminephrobacter aporrectodeae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Verminephrobacter.
REFERENCE   1  (residues 1 to 376)
  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 376)
  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   3  (residues 1 to 376)
  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   4  (residues 1 to 376)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 376)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 376)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Verminephrobacter aporrectodeae"
                     /db_xref="taxon:1110389"
     Protein         1..376
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39475
     Region          29..368
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(105..107,128..129,178,230,255)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mqlklkltvl avvaaagggv acaqeqvvki ghvaplsgpq ahygkdneng armaieelna
       61 qgitiggkki rfelqaedda adpkqgaava qklcdskvag vvghlnsgtt ipaskiyhdc
      121 aipmvtgaat npnltkpgyk ttfriiasds algaglatya adtlklrtva iiddrtaygq
      181 gvaevfkkta iakgikvvde qfttdkatdf mailtavkak spdavfyggm dpqagpmlrq
      241 meqlgmgnmk ffsgdgscta eiaklsggak tlsnmicgeg aaslakmpgg aawkakydak
      301 ypgqfqlysp ytydatqllv damkransvd pkvyvnelak snyrgvtaei vfepngdlkn
      361 paitlyvykd gkktpm
//
LOCUS       WP_010107173             369 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Burkholderia oklahomensis].
ACCESSION   WP_010107173
VERSION     WP_010107173.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia oklahomensis
  ORGANISM  Burkholderia oklahomensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Burkholderia oklahomensis"
                     /db_xref="taxon:342113"
     Protein         1..369
                     /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=38692
     Region          2..297
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mrdsyldtar gagivlvvyg halrglfaag lvpagwpstl laatdytiyt fhmplfflls
       61 glhvpkslqr agdgfllakl rtivypyfvw sllqgavqla lssrgmnhaf tpndllaigw
      121 rpfgqfwfly alficmliaw gwsivapgir ahgraapgra haslaalaig glavvalaag
      181 sstqwgimsm tltylpffvl gmligdklpa lverasngla laavavtfaa avafahrfge
      241 pdsvsavpaa lagcalvlll ahramrrgda aprlaprptw lehigfasmp iylahilata
      301 atrialvklg vvdvgvqlal gtlagvacpm llyglvlrsg tarlvgfppl pagyadarek
      361 grigsadaa
//
LOCUS       WP_010105140             119 aa            linear   BCT 20-JAN-2025
DEFINITION  PilZ domain-containing protein [Verminephrobacter aporrectodeae].
ACCESSION   WP_010105140
VERSION     WP_010105140.1
KEYWORDS    RefSeq.
SOURCE      Verminephrobacter aporrectodeae
  ORGANISM  Verminephrobacter aporrectodeae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Verminephrobacter.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 119)
  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   3  (residues 1 to 119)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 119)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Verminephrobacter aporrectodeae"
                     /db_xref="taxon:1110389"
     Protein         1..119
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12871
     Region          1..119
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mnspstaprp sviqlaikek aalyaayipf fteggifvpt hreyklgddv yvllmlpddt
       61 qrypvagrva wvtparaagn rsqgvgihfp kdeksralki kiegmlgtal gtdratqtl
//
LOCUS       WP_010107619             276 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Verminephrobacter
            aporrectodeae].
ACCESSION   WP_010107619
VERSION     WP_010107619.1
KEYWORDS    RefSeq.
SOURCE      Verminephrobacter aporrectodeae
  ORGANISM  Verminephrobacter aporrectodeae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Verminephrobacter.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 276)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 276)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Verminephrobacter aporrectodeae"
                     /db_xref="taxon:1110389"
     Protein         1..276
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=29966
     Region          <4..217
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mavakftsry dthaveraev ltlklaricg ldvpkariem sdglpvaiiq rfdrsdkgri
       61 pfisaqtmld aptatggtyv sladtirqht aspheemhal frrvgfsilv snvddhlknh
      121 gflyagngkw rlspafdvnp aperfrelkt aiadpadpss siallmdhsf cfeidpdkaa
      181 qivgsmakti qmnwrvlahe agmsraevgd yrlafeheea kyaaravapt vvapglepqa
      241 adtakgsmqr qprkdiaaat pqaqsdnvad gfdpsp
//
LOCUS       WP_010108277              96 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Verminephrobacter
            aporrectodeae].
ACCESSION   WP_010108277
VERSION     WP_010108277.1
KEYWORDS    RefSeq.
SOURCE      Verminephrobacter aporrectodeae
  ORGANISM  Verminephrobacter aporrectodeae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Verminephrobacter.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Verminephrobacter aporrectodeae"
                     /db_xref="taxon:1110389"
     Protein         1..96
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10255
     Region          1..96
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mrpsvvldik rsavreavsr frtanprvfg svlhgtdrdg sdldllvdal pgatlldlgd
       61 ledelklllg vdvdlltpgd lppkfrakil aeaqpl
//
LOCUS       WP_010108433             126 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein, partial
            [Burkholderia oklahomensis].
ACCESSION   WP_010108433
VERSION     WP_010108433.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia oklahomensis
  ORGANISM  Burkholderia oklahomensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (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   2  (residues 1 to 126)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 126)
  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 126)
  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 126)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Burkholderia oklahomensis"
                     /db_xref="taxon:342113"
     Protein         1..>126
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          11..100
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(30,49..50,68,71,79..80,92,97)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mdckylyidn ikinfvrrai eidgepvslt prefdvvefl ldnmnkvvsr qaiqetvwgr
       61 elavssrtld thvsrirskl gldydknmri ipiysigyrl vlfgaattrv ephdapqaar
      121 vgeprv
//
LOCUS       WP_010108692             431 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Burkholderia oklahomensis].
ACCESSION   WP_010108692
VERSION     WP_010108692.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia oklahomensis
  ORGANISM  Burkholderia oklahomensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 431)
  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 431)
  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   3  (residues 1 to 431)
  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   4  (residues 1 to 431)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 431)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 431)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 431)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Burkholderia oklahomensis"
                     /db_xref="taxon:342113"
     Protein         1..431
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44074
     Region          60..394
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(135..137,158..159,208,260,284)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkfpatlslg aalsvaavfa apaaqaqtpa rtaafaqsaq saqfeqsaqs aqsaprtvli
       61 glaapltgps arigkdlqng aqlalddans rhpalggkpv vyklvavddq sdprtavtva
      121 qqlverrvig vvghwntgcs vpasriyrda giaqiapast grqytrqgya tafrivghdd
      181 aggayagayv vktlhakria viddrtafga gladqfvkgv eanggaivdr qyvndkatdf
      241 savltavkar radvvffggl daqaaplarr mrqlklsatl vgaggfvtqt flslagpdgd
      301 gvtalepglp lagmpggaaf daryraryra pielhapfay daaatliaaa eranstapar
      361 lpavlhtlkr qgvtgaiafd aegnlqdpaf tiyragggkw tavdvlggga aagtrvesht
      421 stastastas k
//
LOCUS       WP_010109112             353 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Burkholderia oklahomensis].
ACCESSION   WP_010109112
VERSION     WP_010109112.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia oklahomensis
  ORGANISM  Burkholderia oklahomensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 353)
  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 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   3  (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   4  (residues 1 to 353)
  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 353)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Burkholderia oklahomensis"
                     /db_xref="taxon:342113"
     Protein         1..353
                     /product="CmpA/NrtA family 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=37774
     Region          12..260
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mntarmntat ldaperrhlr igfvalsdaa plvaaqrlgl garygltlel crqpswasir
       61 dkllsgelda ahalyglvyg vqlgiggpra dmavpmvlnr ngqaitfsnr ladayrasgd
      121 lkaalatlgr rpvfaqtfpt gthamwlyhw lasrgvdplr dirsvvippp emvgalaage
      181 ldglcvgepw naaaeacgag rtvaatsevw pdhpekalac rrefvalypn tarllvrtll
      241 dacewlddad hrmkaaawla epdaigvpvg qiaprllgdy gagpfaqppa pikfyehgtv
      301 nrpaasdgmw flsqyrrwgm lsgdaddaav ardvaqtaiy deaaalagar rdd
//
LOCUS       WP_010111556             336 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia oklahomensis].
ACCESSION   WP_010111556
VERSION     WP_010111556.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia oklahomensis
  ORGANISM  Burkholderia oklahomensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 336)
  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 336)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Burkholderia oklahomensis"
                     /db_xref="taxon:342113"
     Protein         1..336
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37723
     Region          25..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          252..333
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mfdsdrpsip tayadlmldi ldergvakav alkraeidaa rlrnvdgris asewarlsrc
       61 amtlaedegl gieyglrqlp tahgtlgyav itsatlrdll dtsakysrsr lsvyaiylke
      121 dgvsatltvr ekvplgnlrn fffecvlvgi aatvkflfpd lfeqielgft wpqpdyfery
      181 rdrlpkvnfr asdnqlrlps sslarkspla naaahsqair qldremalln ldasdlvdrv
      241 raglmlsedg ypslarlass lflsertlkr rlrehgtsyr emlekaryrd acallretdl
      301 sladvsaklg yqnpptftra frrwsgiaps ryrdtl
//
LOCUS       WP_010111570             357 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia oklahomensis].
ACCESSION   WP_010111570
VERSION     WP_010111570.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia oklahomensis
  ORGANISM  Burkholderia oklahomensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 357)
  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 357)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 357)
  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   4  (residues 1 to 357)
  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 357)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Burkholderia oklahomensis"
                     /db_xref="taxon:342113"
     Protein         1..357
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38540
     Region          25..212
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          256..338
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msvwdftrsp asvrlmvdfg aeralaeaql lagaglsvaq lddpnvkvta aqelrvasnl
       61 lrllrhpagl glqvglryhf sayglwgygl iasatagdal alalrflplt yaftaityhh
      121 dgdlgvltfg epelademkr fvverdmaaa avllheiggd afaltrfslk sdrgalesal
      181 aaeirralgv apaysarsns lafeqallsr plpqanpitv smceqmcqrl ieerrlrlgt
      241 aamirhymsa vpgivpstld dmarlmntsp rtlkrrlqde gttfrallag argamasell
      301 tdtdlplsei aerlgfsdls sfsqafkrwq gmapsvfrsr aaangsgdad rrgeskr
//
LOCUS       WP_010112706             233 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Acinetobacter sp. P8-3-8].
ACCESSION   WP_010112706
VERSION     WP_010112706.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. P8-3-8
  ORGANISM  Acinetobacter sp. P8-3-8
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 233)
  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 233)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 233)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Acinetobacter sp. P8-3-8"
                     /db_xref="taxon:1029823"
     Protein         1..233
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=25640
     Region          5..211
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 msaisdeeql dslksffkky gsamvtgvli aliaffgwey wqkktlaenq netakvqqlm
       61 ddakavgsdp kasaalvtsa dkivkdnpds vqaiqaqivm aklafdkndy ataerelkkv
      121 ensklkdagl lqvvklklad tqlaqkkfde alktlsvvde pafkasaeel kgdiyvaknd
      181 idnakksyqa awnavverkq erqilqikle svgvlvddpe lespilktqv des
//
LOCUS       WP_010113290             731 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Acinetobacter sp. P8-3-8].
ACCESSION   WP_010113290
VERSION     WP_010113290.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. P8-3-8
  ORGANISM  Acinetobacter sp. P8-3-8
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Acinetobacter sp. P8-3-8"
                     /db_xref="taxon:1029823"
     Protein         1..731
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=80043
     Region          18..731
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mlqslkfkps tlsyaiglsf lsvtsvsyae nedntqtqtl apivvqakgn wlenanaekv
       61 hnhagartii drkkmdasav tsirdalkqv pgvqvqdsng tggsdvslnl gvrgltsrls
      121 prstvlmdgv plsfapygqp qlsmaplsmg niesvdvvrg agsvrfgpqn vggiinfttr
      181 aipeyfsgsv glttefatgt dqikyspnlf iggtmenglg lallysgtkg dgyreannki
      241 diddvmlkts yqftdhdqva vnlhhyegrg empegltaaq yaenpyqsnq trnyfagrrs
      301 disvkyshkd dvnnfevlgy yvdsfrtsdl esaientpns risnsprdyk yfgieprysr
      361 aytwgkmnne vtvgyrylee dssefsgrta pyntltgtpg trvpnttsdg gtkahavyid
      421 nrfgigawti tpgvrfesie thndftayqg gianntvhpk iksdeflpni aiqyafndqw
      481 nvfanagvsf gpqqynqlvt trtinsknta vttldglhpe ksnnyeigtk ylgnglnael
      541 tvfyldfdke lllerpdnig tgiwtnlgat shkgveagls ydfgslsdsl kglkaysnyt
      601 ftkavseagk fdgkdlpyys rhvanlgmgy tvnkwsvnad mfaqskqhap gsgdvyqtee
      661 tvdgrigdip gystfavrtg ynfgkdfygl kvaggiknlf dtqyftrssd stggkyigqp
      721 rtfylqtsvd f
//
LOCUS       WP_010112829             322 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Acinetobacter sp.
            P8-3-8].
ACCESSION   WP_010112829
VERSION     WP_010112829.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. P8-3-8
  ORGANISM  Acinetobacter sp. P8-3-8
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 322)
  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 322)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Acinetobacter sp. P8-3-8"
                     /db_xref="taxon:1029823"
     Protein         1..322
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=36689
     Region          15..68
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msnfnfvkav rqismppttk lvaitlatya dyetgecyps iqtlmddtgl snravglhik
       61 hienlgilvv drsngrrsyy rfdvesltka vtqghssdne ssdsdnntsd sddsepvtft
      121 qqpvtlvqka vtqghtnyqe qpieqpiers sntheekisq ppvqfvqyhn fdlakisvie
      181 lgqkystlks dfielskprh pdldqhdlen lfdefgdwfa spndygkqsf ktaqkwavaf
      241 ltwvnnnkhk linrkeknnv teqsgrnkpi qtpsayqakq envnrwlryg qkvreeqhqe
      301 ssfidvvpep pknflieevg ha
//
LOCUS       WP_010113303             296 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Burkholderia
            oklahomensis].
ACCESSION   WP_010113303
VERSION     WP_010113303.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia oklahomensis
  ORGANISM  Burkholderia oklahomensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Burkholderia oklahomensis"
                     /db_xref="taxon:342113"
     Protein         1..296
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31889
     Region          17..269
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mrastsveri gdmrcgvges pvwhageaal ywtditgral wrwesetnra hawvlpemag
       61 siamiadggi alamqtgvyr vprpapgapl pepvllagva haadgmrfnd grcdrqgrfw
      121 agtmacdtsl arasgrlyrl dsnaralaae cdalivpngl afspdgrtmy lsdshptrri
      181 vwafdydvda grphgrrvfv dmnahagrpd gaavdedgcy wicgidsgyv hrftpdgrld
      241 rsiavpvakp smcafggary dtlfvtsirt dddplsgatf aldpracglp esamrl
//
LOCUS       WP_010113684             344 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter sp. P8-3-8].
ACCESSION   WP_010113684
VERSION     WP_010113684.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. P8-3-8
  ORGANISM  Acinetobacter sp. P8-3-8
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 344)
  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 344)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 344)
  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   4  (residues 1 to 344)
  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 344)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Acinetobacter sp. P8-3-8"
                     /db_xref="taxon:1029823"
     Protein         1..344
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39982
     Region          55..207
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          257..332
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqelqipngy fhlwqmylse rgidvltaef lqddrvhlqt ilalpidtqs syfffqqmie
       61 ktkhaldcpq iifemaeyvr pehfgvlgym asrsttvaea lqnilrfsrl vidgdhilpm
      121 qmelkgqqvh viwpfhheky tlmneltnal mmhlarkivp anqfllqcvn fahppqmavy
      181 hyqkfygchv tfnkpeysfv lgleglnvki qqadpslmql lvkqaedaia skprhetlpq
      241 hlhfiiaeyl rlkeqapkie disqelnist rtlqrqlndf dtsfkkivei ermkrcelll
      301 gnnlqfteia mrlgysdqsa laraykafsg qtllqkkvql knkq
//
LOCUS       WP_010113691             347 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Acinetobacter sp. P8-3-8].
ACCESSION   WP_010113691
VERSION     WP_010113691.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. P8-3-8
  ORGANISM  Acinetobacter sp. P8-3-8
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Acinetobacter sp. P8-3-8"
                     /db_xref="taxon:1029823"
     Protein         1..347
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38413
     Region          <28..>280
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          269..339
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 msmnnkqrwm ggvvllsggv llaalllkgk eeihqkqvet qpveqvqqnk nasageaiql
       61 qpltvdvate krlleeqkrs rekavaeqea kaaeflrmqq qaeadaarka aeeyaamnar
      121 rgaaaqegtd ippelvqdek tkaqqkaadq kqleqqnaql kqkadaekkl aeqkrqatad
      181 aekkaaedkk rqldaekkaa dekkrkveeq lkieeqrkae aekkaaadkk aeaerkaeve
      241 kkrkaqedak kkaeaekard llengdkqwm vqvalaanea nadavaaklr akgykvtksp
      301 tskgirimvg pakdretada arkkintdas lgmksawvie wvpldrr
//
LOCUS       WP_010113805             141 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Acinetobacter sp. P8-3-8].
ACCESSION   WP_010113805
VERSION     WP_010113805.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. P8-3-8
  ORGANISM  Acinetobacter sp. P8-3-8
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Acinetobacter sp. P8-3-8"
                     /db_xref="taxon:1029823"
     Protein         1..141
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16100
     Region          1..136
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 maylllflsa fgaatllplq seavllglla qaqyltylli lvatignvlg scvnwylglk
       61 ieqykhkkwf piskksmlka ekiyqkygfw sllfswtpvi gdpitlvagl mrenfwrfll
      121 ivtfakggry lfvywiylgi f
//
LOCUS       WP_010114271             424 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Burkholderia oklahomensis].
ACCESSION   WP_010114271
VERSION     WP_010114271.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia oklahomensis
  ORGANISM  Burkholderia oklahomensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 424)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia oklahomensis"
                     /db_xref="taxon:342113"
     Protein         1..424
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=46247
     Region          35..254
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 msmididpps fqsprpiagd dgnrrtvlyg dytvfsvfqp vfsvshrrai gyhaslrahd
       61 shgnqvpshe vftqaarrgd llelgrlaes lhlgnfhtfd shdewlflsl hpaalmdtvy
      121 gdallanlkt lglppqrvvl evpeqagget prfaaivdgl rkagflialg gfgakhsnid
      181 rvwhlhpdiv tldrgilaqa sehshlervl pglvsllhes gqlvlmggit terealiale
      241 cdvdfvqgqy fagpsvepvq pqvaagimdt lsaalrlrva eraraqdarl apyvaallqa
      301 sallragrdl tdaskellel qeaarcflld asgrqigdnv lprvhasqra krfspllhse
      361 gaswerrpyf ieamrvpgrv hftppylsin eahlcvtasi atpaaqgmqv lcvdinweaa
      421 ahrd
//
LOCUS       WP_010114988             336 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Acinetobacter sp. P8-3-8].
ACCESSION   WP_010114988
VERSION     WP_010114988.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. P8-3-8
  ORGANISM  Acinetobacter sp. P8-3-8
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 336)
  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   6  (residues 1 to 336)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Acinetobacter sp. P8-3-8"
                     /db_xref="taxon:1029823"
     Protein         1..336
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38649
     Region          42..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          82..336
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mqqfkdyags vygglgqllf afseanglki spklqqvqnl erfdfniwre llddiqaqtq
       61 spalgleiaa hvqpkhlgii ayiaqscdtm gealsryfdy hrlifdgspl kiesfhdgyl
      121 gihwttlpsh lttqitdeia ialmvqflrh flstkdiqlh qinfthvkps nlkiyekffd
      181 cpvrfnqpla elifplhvmt vplshgdqtl qkllmqqaqa llndlpnssq iderlqqiil
      241 lglqknlyqi geiakqlnis irqlqrhlqn qgttyqqrvq evrkllavqy lqdpylglhe
      301 ialllsyseq safqrafkqw tgitpqqwri rnrssk
//
LOCUS       WP_010115625             351 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Burkholderia
            oklahomensis].
ACCESSION   WP_010115625
VERSION     WP_010115625.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia oklahomensis
  ORGANISM  Burkholderia oklahomensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Burkholderia oklahomensis"
                     /db_xref="taxon:342113"
     Protein         1..351
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37988
     Region          1..350
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mgiivrnlhk rfgdftaldd vtldfpagel vallgpsgcg kttllrviag lehadsgqvv
       61 lqgldvasvg arerqvgfvf qhyalfrhmt vfenvafglr vkprrerpse aairdkvhel
      121 lslvqldwla qrypselsgg qrqrialara lavepkvlll depfgaldak vrkelrswlr
      181 rlhddlhist ifvthdqeea levadrivvl dhgrveqvgs pqdvydhprs afvyeflgaa
      241 nrldgtvngt gfvangaaga iavdadfagp arayvrphdl alvapgarad giaadvrrvv
      301 plggsvrvel avraggvlea eldrnawral aldvgdalta vpravrvfpa r
//
LOCUS       WP_010115801             252 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Acinetobacter sp. P8-3-8].
ACCESSION   WP_010115801
VERSION     WP_010115801.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. P8-3-8
  ORGANISM  Acinetobacter sp. P8-3-8
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Acinetobacter sp. P8-3-8"
                     /db_xref="taxon:1029823"
     Protein         1..252
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28820
     Region          24..249
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 msqdaqpkkr yyeaapqdid venfrkvves rrsvrkftdk lipaetldac ldlallapns
       61 snlqpwtfyv vqsqpkkkrl vkaclnqfaa rtaaelivcv artdridema qnninefpfp
      121 eipplvkryy rfipynyktg ylnalgnfkk vafkvarqfd kqlpvtaytp adaklwatkt
      181 talacenlvl alraygfdsc mmegfdepmv rkilnlnade ypvmvvaage raedgvfypq
      241 yrfdrnlfiq kv
//
LOCUS       WP_010116262             127 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Acinetobacter sp. P8-3-8].
ACCESSION   WP_010116262
VERSION     WP_010116262.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. P8-3-8
  ORGANISM  Acinetobacter sp. P8-3-8
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 127)
  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 127)
  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   3  (residues 1 to 127)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Acinetobacter sp. P8-3-8"
                     /db_xref="taxon:1029823"
     Protein         1..127
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14734
     Region          15..118
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mkpynknlkq psrdlrnnmt daelllwrrl rskqihglqf yrqkpilnyi vdfycpsanl
       61 viecdggqhy tedgleadrv rdealvglgl mvlrfdnlqi lneidgvveq iycvveqrle
      121 liklesp
//
LOCUS       WP_010117230             118 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acinetobacter sp. P8-3-8].
ACCESSION   WP_010117230
VERSION     WP_010117230.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. P8-3-8
  ORGANISM  Acinetobacter sp. P8-3-8
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Acinetobacter sp. P8-3-8"
                     /db_xref="taxon:1029823"
     Protein         1..118
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=12766
ORIGIN      
        1 mkknngftli elmivvtiig llaaiavpsy lnytknadrk aclletksyv ndtyylifdq
       61 ssetnprapa isacesitda sswnetttnl iieaksknsa iinikcdlsk ganctiip
//
LOCUS       WP_010117379             380 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Burkholderia oklahomensis].
ACCESSION   WP_010117379
VERSION     WP_010117379.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia oklahomensis
  ORGANISM  Burkholderia oklahomensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 380)
  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 380)
  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   3  (residues 1 to 380)
  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   4  (residues 1 to 380)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 380)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 380)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Burkholderia oklahomensis"
                     /db_xref="taxon:342113"
     Protein         1..380
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39696
     Region          32..365
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(108..110,131..132,180,232,256)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mnikmqkllp isaaamllaa aatnaaadqv vkighvaplt ggiahlgkdn engarlavee
       61 inakgltigg qkitlqldaq ddaadprtat qvaqklvddk vaavvghlns gtsipaskiy
      121 sdagivqisp satnpaytqq gfkttyrvva tdaqqgpala nyarskgiks vavvddstay
      181 gqglanefek kakalglkvv shdatndkav dfrailtkik genpdavmyg gmdatggpfa
      241 kqakqlglra kilagdgvct eklsdlagda tdnvvcseag aslekmpgga afkakyekrf
      301 gqpiqiyapf tydavyiivd amkranstdp akivavmpkt nytgvigttt fdskgdlqhg
      361 vislydykng kktfldevkm
//
LOCUS       WP_010117622             454 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Acinetobacter sp. P8-3-8].
ACCESSION   WP_010117622
VERSION     WP_010117622.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. P8-3-8
  ORGANISM  Acinetobacter sp. P8-3-8
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Acinetobacter sp. P8-3-8"
                     /db_xref="taxon:1029823"
     Protein         1..454
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=50227
     Region          6..442
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mielfsipve qailstvigt eqgmdeyieq iqasdfyaaq hqiiwthvks qfvkgegydq
       61 vmlweliran aievnavdek filnlmgcyc phsllpthlk klkdfavrrk iqdvskqigt
      121 valdmvsyts etalnraqal vsgletgsvd nrlkhahefs kdaikefler htalhnntpf
      181 dggirtgfve ldnklgevgk gdlviigarp smgkttlaqn faadmminqn lpvlfvsiem
      241 sgkqiaqrmi sgigqielrk vlsgkaqied cgkintaami lekaplmidd narsttstir
      301 rsarkvqaey gkvgaifvdy iqrvtpltkn nygrsdkdig eisgelkkia rdfecpvfal
      361 aqlnrnlenr pnkrpvnadl kesgdleqda diimfiyrde vynkeskevg taeiiigkar
      421 ngstgtvkla tdlarstfad lspeyyammq gggv
//
LOCUS       WP_010118953             198 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Burkholderia
            oklahomensis].
ACCESSION   WP_010118953
VERSION     WP_010118953.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia oklahomensis
  ORGANISM  Burkholderia oklahomensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 198)
  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 198)
  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   3  (residues 1 to 198)
  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   4  (residues 1 to 198)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 198)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia oklahomensis"
                     /db_xref="taxon:342113"
     Protein         1..198
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21908
     Region          9..196
                     /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"
ORIGIN      
        1 mgstdqpskl rvllvtdtdk pigelrdtla rlgyemldev atparlpaav eeqrpdvvii
       61 dtespsrdtl eqlavmnata prpvlmfshd adqqliraav gagvsaylie glsaerlapi
      121 levalarfsh deqlrqrlae veseladrkl idrakrmlmd rrklseqday atlrrsamdq
      181 giriveaarr lltahtqs
//
LOCUS       WP_010119199             385 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Corynebacterium nuruki].
ACCESSION   WP_010119199
VERSION     WP_010119199.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium nuruki
  ORGANISM  Corynebacterium nuruki
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 385)
  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 385)
  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   3  (residues 1 to 385)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Corynebacterium nuruki"
                     /db_xref="taxon:1032851"
     Protein         1..385
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42407
     Region          255..366
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mgenntnpaw elpqdiidal negrytpgwg pwyctrilpv mmprrrkdll aggvtrrtld
       61 rdyvtltrgi vvpaaeipds gedrgvygac gvlrarafhv lypdrivagw qaaalhglpy
      121 wadsapvlml sltaapsgsh rttvaaehpy rvavrrppen fdvdrdtvtp dpvcpamrvv
      181 tvpvalaqcv rsvlsghhiw qvpevpgltd reiravqlid afvqcttvta gefayaakgl
      241 vsrrqvrklt glacrgaesp retllrlyvr allpagyrwr tqvavryrdi rsdgserirt
      301 tyldlgcpel kvglyydggh hagagqtdrd faqlqdlrde qwtvvridkd lmknvrkmlt
      361 qvstvigmav qagdrgagda gdgte
//
LOCUS       WP_010119890             328 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Corynebacterium nuruki].
ACCESSION   WP_010119890
VERSION     WP_010119890.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium nuruki
  ORGANISM  Corynebacterium nuruki
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Corynebacterium nuruki"
                     /db_xref="taxon:1032851"
     Protein         1..328
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=35372
     Region          1..323
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mtisvshavk tygdfhaldd vsidipegsl tallgpsgsg kstllrtiag leqpdsgqvv
       61 idgrdvtrls pqdrgigfvf qhyaafkhmt vrdnvafglt vrkrpkkeid arvdelleiv
      121 glagyqtryp sqlsggqrqr malaralaps pgvllldepf galdakvred lrtwlrhmhe
      181 eftvttvlvt hdqeealdva driavlsagr ieqigapsel ydspetpfvq aflghvteld
      241 gktvrphdir lgrnaspevh gneipatevr eavvervvvl gfevrvelkd aatgapftaq
      301 itrgdanalg lsgasvgeti yaratela
//
LOCUS       WP_010121396             340 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia oklahomensis].
ACCESSION   WP_010121396
VERSION     WP_010121396.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia oklahomensis
  ORGANISM  Burkholderia oklahomensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 340)
  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 340)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 340)
  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   4  (residues 1 to 340)
  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 340)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Burkholderia oklahomensis"
                     /db_xref="taxon:342113"
     Protein         1..340
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37643
     Region          28..212
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          255..337
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtvklarwdf vrpvnttrvl vdvgveqglg vrqcldgsgv apelldrpea tvaaaqelri
       61 vrnlmrllgp dfplgieigr ryhataygiw gfallssatf adavsvglry lqltstfcdi
      121 rptargedat lviddhdlpg dvrdvlveit vaalitlqvd ldaanlpvkr lafkmeapsy
      181 adrfrtlfaa spefgaaena ltvdvrcldl klpqrnsltr rlcedecrrv lerrrrsegw
      241 agrvrrhlag dsarrptmaa laaelgvsar tlrrrlageg tdyetvvdei retlaeella
      301 tttltvaeis erlgysepsa farafrrwka mspseyrwsa
//
LOCUS       WP_010123456             193 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Sphingomonas sp. KC8].
ACCESSION   WP_010123456
VERSION     WP_010123456.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. KC8
  ORGANISM  Sphingomonas sp. KC8
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 193)
  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 193)
  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   3  (residues 1 to 193)
  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   4  (residues 1 to 193)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 193)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Sphingomonas sp. KC8"
                     /db_xref="taxon:1030157"
     Protein         1..193
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=20784
     Region          1..191
                     /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"
ORIGIN      
        1 mriaivdesg lratileegl resgfddihv vpptgafvar ierlapdvvl mdlgtpsrds
       61 leemlvvsra larpiamfvd qsdeamigaa idagvsayvv dglrkervkp ilelairrfn
      121 afatlrtele dartaladrr kidrakailm dsrgvgeaea yallrstamn qgrkiadvad
      181 alitatellg gpk
//
LOCUS       WP_010123481             333 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Sphingomonas sp. KC8].
ACCESSION   WP_010123481
VERSION     WP_010123481.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. KC8
  ORGANISM  Sphingomonas sp. KC8
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 333)
  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 333)
  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 11677403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Sphingomonas sp. KC8"
                     /db_xref="taxon:1030157"
     Protein         1..333
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36805
     Region          12..200
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          114..330
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          251..328
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mivlldtlae iggdvrgvlr rsglgliega ardgramlip raafaqlaad cvlalhaesc
       61 rknrlqpfpv rnhrilllam lgcttlreav vvmtdfyaml gersaqwavt knghavrfal
      121 drrtrevsla eflislfsla syhrilgwvi geevplidvt laypdmlqea glndlfsihp
      181 rfeerqdsfs faehyldwpi arkptevdgl falfpfdllp pdygtetlaq rlkaamrgal
      241 smgeavpntv alarmfgltp atlrrrlare gaslvsvrtq crrelaltml agtsltvrev
      301 asrlqyadva tfrrafmgwt gmtpsawraa dgk
//
LOCUS       WP_010121721             252 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Corynebacterium nuruki].
ACCESSION   WP_010121721
VERSION     WP_010121721.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium nuruki
  ORGANISM  Corynebacterium nuruki
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 252)
  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   2  (residues 1 to 252)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Corynebacterium nuruki"
                     /db_xref="taxon:1032851"
     Protein         1..252
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=24327
     Region          95..150
                     /region_name="SLBB"
                     /note="SLBB domain; pfam10531"
                     /db_xref="CDD:463136"
     Region          180..251
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 maarvealtq qvpgheladv rferravvap ksaralvtva avvvavvvgv mlvgkfsggg
       61 dgagepaavg lspvgettat apttvaagqa dpspvvsvqg mvtrpglvtv eaatrlgqla
      121 dlaggalpga rldglnlaek vvdglqlvvd dagsrvvypg gagaaatggg epgnagappa
      181 gtgeaagqgt avnlntadat algglpgvgp ktaeaiiawr dahgpfssve qlmevkgigp
      241 akfealrdgv tv
//
LOCUS       WP_010123768             698 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein, partial [Sphingomonas sp. KC8].
ACCESSION   WP_010123768
VERSION     WP_010123768.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. KC8
  ORGANISM  Sphingomonas sp. KC8
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 698)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 698)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 698)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..698
                     /organism="Sphingomonas sp. KC8"
                     /db_xref="taxon:1030157"
     Protein         <1..698
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
     Region          126..382
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          347..598
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 dpggetpggg dpgpadpgge tpgggdpdpg dpggetpddg dpgpgpgtgd ngshagpdgt
       61 rnppgrtlpd vapdvgtgah ihgaqiigad tserfdlalp gmpgnargga gddvilgrqd
      121 rnqlegndgd dliigyasgi ggegdrligg ggddtligdd ftgatastla gadrpgddad
      181 wisggegndl awggggddvl tggagddvlf ggtgndalsg gdghdalhgg egvdtllgga
      241 gddllagdgg ddllhgeagd drldggdgrd slyggaghdr lwggagddml rggdgddsll
      301 ggagadslfg ddgadtldgg dgmdrldggl gddllrgggd addlrgdaga dtidggdgad
      361 ylqggagddv ltggadddil vgadgadrld ggagndwlgg yadddvllgg agddtldggd
      421 gtdlldggdg ddwlsgggdd dvvaggagnd alfgnggddr ieagagddva sggdgadlll
      481 ggigsdwlyg qdgadtldgg agddslsggn ddddlsggag nddlygddga dwlmggdddd
      541 lldggaghdg leggagadgl yggtgndsly gdagddallg eagddwlegn agddtltgga
      601 grdlftfdvt tdghdvitdf sladrdqiai yisdpflfdi erlrivddgt dlhlvmgdas
      661 itlaslgggg favlgidsid dlnalsqgva gydmvvfa
//
LOCUS       WP_010125773             718 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Sphingomonas sp. KC8].
ACCESSION   WP_010125773
VERSION     WP_010125773.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. KC8
  ORGANISM  Sphingomonas sp. KC8
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 718)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 718)
  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   3  (residues 1 to 718)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..718
                     /organism="Sphingomonas sp. KC8"
                     /db_xref="taxon:1030157"
     Protein         1..718
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=75564
     Region          6..704
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mstgndelde iqgiffeeca eglvvaeqgl samaggdvsa dviagvfrav hsikggsgaf
       61 ghaallafsh rfenvldevr agkipptaev trvmlnafdi lsdhvaaaqg gtappaheam
      121 lvaldailes kgagggdvpa apepvavepa ddefgfvpvq agveefdpfg fepvaidldd
      181 ltppaaqpwv vrfgpsraam angseplfiv relegmggqi vavdssalpg lrdldpedsy
      241 lvwtlslpgt veeqdirecf dfvapdsiie maratveaep vtavaaveqi vapvaapvaa
      301 pmpaappapp taavaegrta epaaqtirvd lskldqllnl vgelvihgsi lsdrlspvdq
      361 ervelpelsr ltrqiqdnvm slraqpirqa fsrvprmlrd lmtetgkkvi lettgettev
      421 dkgviekigd plthmirnav dhgiespeqr iaagkpaegt irlsaeqkga rivvrvsddg
      481 rgidrvrvra kaiekgiisa davmsdeeid slicapgfst aetisnisgr gvgmdvvrsn
      541 vealggrvei hstpgegttf tmalpltlai ldgmivrlgq qrfvlplgnv ietvqpepgq
      601 vkptspnsev ielrgsylpv krvgqmfgig andlrtpees lviivesdaa ghvglmvdti
      661 enrrevviks lednlhpirg lggatilgdg tiglildida lvaatntpsk yalkgmaa
//
LOCUS       WP_010127912             689 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Sphingomonas sp. KC8].
ACCESSION   WP_010127912
VERSION     WP_010127912.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. KC8
  ORGANISM  Sphingomonas sp. KC8
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 689)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 689)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..689
                     /organism="Sphingomonas sp. KC8"
                     /db_xref="taxon:1030157"
     Protein         1..689
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70773
     Region          2..689
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 maadlarmlr arrvavigas ernpfaasvi rnldhfgfrg dvqlvnprge pvagratlrr
       61 agalegpida afvcvpsdqv iptveeaada gvtgfvvvss gfaetgadga raqeqlrala
      121 grtgvtllgp nalgfanyvd gvalcalere nrrgsfgias vsgsvggyla kvahlrgvgl
      181 shmvlagnea gttisdvvdf lvddpdtrsi gvflesiydp hlfasaaera mrahkpivml
      241 kagasentar lamahtgalv gddrvfdava relgicrvts yedmiataml lektgprasa
      301 gvamltisgg sgeiasdlae pagvsfppfs dairpeldai vsgfgqthnp ldvtgaalrd
      361 tglwerllkt iakdeaiglp lciwdvptga eaawmaetla siargyagya cvppvistvs
      421 etvsdygiqa laeagipgai cglhpamaal aaharwserv ldmrpvqlfa asdampaslp
      481 rgeralldwl avrgvpvtpg viagnadaam faadaigypv alklaaadva hkseiggvrl
      541 glgdgaavra gfdailnavp ngvavdgvvv spmrdhqiel ivsisrdpvw glmlalglgg
      601 iwvellgdsv llplpvdgar vvaalhrlka aplfagargr ppvdldavat avvaianaal
      661 algpgltale inplaifadr aeamdallv
//
LOCUS       WP_010130737             148 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Microbulbifer
            agarilyticus].
ACCESSION   WP_010130737
VERSION     WP_010130737.1
KEYWORDS    RefSeq.
SOURCE      Microbulbifer agarilyticus
  ORGANISM  Microbulbifer agarilyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Microbulbiferaceae; Microbulbifer.
REFERENCE   1  (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   2  (residues 1 to 148)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Microbulbifer agarilyticus"
                     /db_xref="taxon:260552"
     Protein         1..148
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16641
     Region          65..143
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mnhiqpdqas lsedkplqqa rlsgdpnild qllappeats fgiaarvidv leqrigkasl
       61 airpvasdls mstrtlqrrl qehnlsfasl rdhvrfrhav hflkdtalsv dgisrildfs
      121 drtsftsafk rwtgmsptgy rrqvrqry
//
LOCUS       WP_010131562             458 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Microbulbifer agarilyticus].
ACCESSION   WP_010131562
VERSION     WP_010131562.1
KEYWORDS    RefSeq.
SOURCE      Microbulbifer agarilyticus
  ORGANISM  Microbulbifer agarilyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Microbulbiferaceae; Microbulbifer.
REFERENCE   1  (residues 1 to 458)
  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 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   3  (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   4  (residues 1 to 458)
  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 458)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Microbulbifer agarilyticus"
                     /db_xref="taxon:260552"
     Protein         1..458
                     /product="CmpA/NrtA family 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=51222
     Region          31..312
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mtwnkplktl aaslalavsf sivpataeel gypekeeltf gfikltdmap iaiayekgyf
       61 edeglyvtie aqanwkvlld gvidgrldga hmlagqpiaa tmgfgtkaei itpfsmdlng
      121 ngitvsntiw eemkpnipkr adgkpvhpik adalkpvvek ykeegkpfnm gmvfpvsthn
      181 yelrywlaag gihpgyyaph kgdisgqida dallsvtppp qmpatleagt iygycvgepw
      241 nqqavfkgig vpvvtdyeiw kdnpekvfgi tkefaekypn ttvrvtrali raamwldenn
      301 nanrpeavki lsqsnyvgad ydviansmtg tfeyekgdkr evpdfnvffr ynatypyysd
      361 aiwyltqmrr wgqisedkpd ewykelaakv yrpdiyqaaa kslideklat aeqfpdfete
      421 dgfrnpqthf idgivyngke pnayiekfdi glksgqkl
//
LOCUS       WP_010131612             196 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Microbulbifer
            agarilyticus].
ACCESSION   WP_010131612
VERSION     WP_010131612.1
KEYWORDS    RefSeq.
SOURCE      Microbulbifer agarilyticus
  ORGANISM  Microbulbifer agarilyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Microbulbiferaceae; Microbulbifer.
REFERENCE   1  (residues 1 to 196)
  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 196)
  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   3  (residues 1 to 196)
  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   4  (residues 1 to 196)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 196)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Microbulbifer agarilyticus"
                     /db_xref="taxon:260552"
     Protein         1..196
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21356
     Region          5..196
                     /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"
ORIGIN      
        1 mtstpisill vddqteraam vsgqltaagy nllaqlssae gllfqvekhr pdivlidies
       61 pdrdilesls vinqhnptpv amfsarggad fissavdagv saymaeglsa ervapaieia
      121 maqfrsyqql rqslertqqq lderkiiera kgllmarkni seqaahqtlr tlamnsnstm
      181 rnvaeqiish lqtpar
//
LOCUS       WP_010131753             800 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Microbulbifer agarilyticus].
ACCESSION   WP_010131753
VERSION     WP_010131753.1
KEYWORDS    RefSeq.
SOURCE      Microbulbifer agarilyticus
  ORGANISM  Microbulbifer agarilyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Microbulbiferaceae; Microbulbifer.
REFERENCE   1  (residues 1 to 800)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 800)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 800)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..800
                     /organism="Microbulbifer agarilyticus"
                     /db_xref="taxon:260552"
     Protein         1..800
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=87834
     Region          8..796
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mprwlkqlaa avfilvlalg tfltftlras lptldgeiav ssglnapatl arddkgiavi
       61 taanrldaay amgfahgqdr ffqmdlasrl asgelaelfg sialdadkky rvhqlrrran
      121 ealaqipaee raildiyaeg vnaglaslgs kpfeyhllrv epkpwsptes mlvsmsmfiq
      181 mtgklaqsdy ardlllragg etllefiqpq gtqwdtaidg tryatpaips eatfaingas
      241 apsetnelag vspepgpmng snswaisgak tshggallsn dphlgmaiph iwyrvqlnyt
      301 spagnavhmn gvsfpgmpam aigtngkvaw smtnsagdwa dyivlehdet hyeapqgrqp
      361 fdrqtetirv kgeksvtlei dntiwgpavt lqdgqraayr wlvqyaealn plpflnldda
      421 vtaaeaadia hrsgispfnf vvadsageil wtilgriper gsvpserlvp wqqvddtwrg
      481 wlqpadypmi tskqldyiwt annrivgdkm rdqigrgtya lgtrgwlieq dliateqfde
      541 lrmtemlqnn raetvsgwrd hlldwmeplt dlsadehsal taltdwtara avddvgytva
      601 reyqreftra mnralqetlv nnevisaehd evwlfnsnse galakirdqq pthwlpqgfd
      661 nwlafqrvvl qsvladlvek hgalaqanwg khnalqmhhp lasalpgflg erlnmpaseq
      721 agdsymplaq rpkhgqsmrf vvspgkeqdg flimpggqsg hplsdfysag hadwvnaent
      781 pllpgaviht ltlspqyspq
//
LOCUS       WP_010131838             684 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Microbulbifer agarilyticus].
ACCESSION   WP_010131838
VERSION     WP_010131838.1
KEYWORDS    RefSeq.
SOURCE      Microbulbifer agarilyticus
  ORGANISM  Microbulbifer agarilyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Microbulbiferaceae; Microbulbifer.
REFERENCE   1  (residues 1 to 684)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Microbulbifer agarilyticus"
                     /db_xref="taxon:260552"
     Protein         1..684
                     /product="amidohydrolase family protein"
                     /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=74207
     Region          256..662
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mrtlttflll lalfgcskpa ddvqdtkesk teetfsvmfg gttvgdmtvv rtgnqlqidf
       61 gfsnngrgas sqealvlgeg gvptewkitg kttfgnavde eyvrtgdtar wrsasgegqa
      121 dvsanpiyia qnaspyalfl ytravldatg drypalpagd lvvtpkrelq ltgedkqlsa
      181 imyavggidm dpqylvldtq qelvaivspr aafirqgleg eekhlrelaa slnaarfeei
      241 asrvthqyeq pvrvnnvrif dpsalaltqp vsvlvkdgvi saidgvqagp npaevtidga
      301 ggtlvaglye mhghmsdnda llnviagvts vrdmgnesdv lesliekids gqligpriik
      361 sgfiegvsey snstgelapt kedalqlvrd yaakggytqi kiyssmngew ipdiakeahk
      421 lglrvaghvp afytadqmie agyneithin qlmlgwvltp eedtrtlfri tgmkrfvdld
      481 ltsdkvartl emmvandial dpttvihelg mtsrngvtrq galdyienmp vsvqrrakva
      541 mlnvadeaed qaykaayqki idtlalmhqk gillvpgtdl ggafeqhrel elfqefgmsa
      601 aealkrgtyd maeylghadt lgsievgkqa dfflvpgdpt qdlkaiktis mvttngkffy
      661 ptevypefgv mpfteapavq easl
//
LOCUS       WP_010132132             138 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Microbulbifer agarilyticus].
ACCESSION   WP_010132132
VERSION     WP_010132132.1
KEYWORDS    RefSeq.
SOURCE      Microbulbifer agarilyticus
  ORGANISM  Microbulbifer agarilyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Microbulbiferaceae; Microbulbifer.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Microbulbifer agarilyticus"
                     /db_xref="taxon:260552"
     Protein         1..138
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14248
ORIGIN      
        1 mhkqtgftli emmivvaiig iisaiaypsy mesvrksnra dakatlndva hrlqrcftty
       61 saydnancsv attlsgggti tsaegmysvt aaitattytl taapvagtsq aadtkcgslt
      121 ltnagvrnat gsygaecw
//
LOCUS       WP_010132831             366 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Microbulbifer agarilyticus].
ACCESSION   WP_010132831
VERSION     WP_010132831.1
KEYWORDS    RefSeq.
SOURCE      Microbulbifer agarilyticus
  ORGANISM  Microbulbifer agarilyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Microbulbiferaceae; Microbulbifer.
REFERENCE   1  (residues 1 to 366)
  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 366)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 366)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 366)
  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   5  (residues 1 to 366)
  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   6  (residues 1 to 366)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Microbulbifer agarilyticus"
                     /db_xref="taxon:260552"
     Protein         1..366
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40836
     Region          38..230
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <278..362
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mgsdsqslva gtghsqgddi ripiayvqrl leeaanrgcd raellaavgi serdledtaa
       61 fsavtygrly qrvmwlaqde wfgmlsggrv rsgsfrllcl tvvncatvrq aitlsaefme
      121 icrgfrvkpv lsqegdrdkv viegisslqp gefetliadt spsvirttla vwhrfycwlv
      181 greiplaklh fsfpcpeefq tlaqseagel lfdqpgnale yesryldypv vqspqtvedf
      241 irtapyhlvi sdgnansikt kvktilnrdv sesmppaeav aerlnmsvtt lrrklqqent
      301 syqklkdecr meaafhylsc pdlsntqiae mlgfdeasaf frafkkwtgv tpgeyrkspr
      361 tsiveg
//
LOCUS       WP_010133283             372 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Microbulbifer
            agarilyticus].
ACCESSION   WP_010133283
VERSION     WP_010133283.1
KEYWORDS    RefSeq.
SOURCE      Microbulbifer agarilyticus
  ORGANISM  Microbulbifer agarilyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Microbulbiferaceae; Microbulbifer.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 372)
  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 372)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Microbulbifer agarilyticus"
                     /db_xref="taxon:260552"
     Protein         1..372
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=42889
     Region          8..367
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mkaytkappl pvdraralvl arqfvqqpwp gdiagliahl galqldaiqv itrahlhqlh
       61 vrlpkpdetr liqmldsaer errvfeywsh aaaylpmqsy rfarvrmdri regqkhwfek
      121 naklcrfvld riraegplka sdfvrtkggw wswseekkal eqlfhegelm vshregfqkv
      181 fdlperllps qvettaasea eygrhlvrsf lnaqgigrat emsylrkhdk plindavvqm
      241 krtgellevg telmlaeeld ceppvvprkv rllspfdplv lqrkrlkrlf dfdyqlecyv
      301 paakrrygyf clpilyrdgf agvvdlkadr svgrlrikal hwreqpragl lsgfnkalad
      361 farfhglvse gl
//
LOCUS       WP_010136188              79 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Ochrovirga pacifica].
ACCESSION   WP_010136188
VERSION     WP_010136188.1
KEYWORDS    RefSeq.
SOURCE      Ochrovirga pacifica
  ORGANISM  Ochrovirga pacifica
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Ochrovirga.
REFERENCE   1  (residues 1 to 79)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 79)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 79)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 79)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Ochrovirga pacifica"
                     /db_xref="taxon:1042376"
     Protein         1..79
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8720
     Region          2..79
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mkitvkyfgm lleqtqsete vlhctegsti asvekivlek ypslqnfsyn iahnrtlkkk
       61 qqsvtdgdel aflppfagg
//
LOCUS       WP_010137318             223 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Oceanicola sp. S124].
ACCESSION   WP_010137318
VERSION     WP_010137318.1
KEYWORDS    RefSeq.
SOURCE      Oceanicola sp. S124
  ORGANISM  Oceanicola sp. S124
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceanicola.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Oceanicola sp. S124"
                     /db_xref="taxon:1042378"
     Protein         1..223
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=22486
     Region          109..>137
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mktliastsr tallalalaa pvvapihava qdaqvegeag tdpllvpegg dtgaemttdp
       61 maptdgdvae apgtpdpmad pmategtdva eaeeapkpve gqitmqdkds ilaadligap
      121 vyngqdekvg dindliialg gnvegvvigv ggflglgekd vaiemaqldv atsegdvqrl
      181 vtsasradle sapefvtaqe qareaealqm qsdttggati pve
//
LOCUS       WP_010137960             197 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Oceanicola sp. S124].
ACCESSION   WP_010137960
VERSION     WP_010137960.1
KEYWORDS    RefSeq.
SOURCE      Oceanicola sp. S124
  ORGANISM  Oceanicola sp. S124
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceanicola.
REFERENCE   1  (residues 1 to 197)
  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 197)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 197)
  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   4  (residues 1 to 197)
  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   5  (residues 1 to 197)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Oceanicola sp. S124"
                     /db_xref="taxon:1042378"
     Protein         1..197
                     /product="TRAP transporter small permease subunit"
                     /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=22078
     Region          3..196
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mklmrgyiaw idgmnrligr itmfglfilm gillwssisk tfflpslwtl emaqfvmvay
       61 yilggpysiq lgsnvrmdli yaelsdrrka wldaftvffl ifylgvmiyg glaslayslg
      121 nfmgsplaff gkligafftg gpaaagevmg yietsrsswg pvmwpiklit clglflmllq
      181 vlseffkdll rlrgeei
//
LOCUS       WP_010138116             747 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Oceanicola sp. S124].
ACCESSION   WP_010138116
VERSION     WP_010138116.1
KEYWORDS    RefSeq.
SOURCE      Oceanicola sp. S124
  ORGANISM  Oceanicola sp. S124
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceanicola.
REFERENCE   1  (residues 1 to 747)
  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 747)
  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 747)
  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 747)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Oceanicola sp. S124"
                     /db_xref="taxon:1042378"
     Protein         1..747
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=80010
     Region          36..735
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mtqdsppkad nrghtaadgd heftadevea lvreydsesn frnlvgptai fvtiasvvls
       61 lfhvytagfg llnevmhrti hltfvmglif lvfprkrarp nrklwiesgi faafylyllw
      121 silpslpega tkyvfiavvl vltgltlpin rrnadpekia lrdwifaaag agfsaylsif
      181 fhyifienvg nppqpvymmg liaimmtlea trrtmgptla yigigcliya lfgpylpgif
      241 ahrgysitri inhlfigteg iygvavgvva tyvfhfvlfg ilaqmsglgq lfidlatiia
      301 grasggsakv svvssgffgm isgspiantv ttgaftiplm kksgfsgrfs gaveasascg
      361 gqitppimga safvmtemlg ipynelilia ivpaafhyia illmvhleak klgltgmtke
      421 nipqfgkvla kswhlfiplg vmvamllmqy tpflaafwgi iltivcsyvp limrqfgntt
      481 mdtstvltpp rlvrgfedga kfalaigaac acvgfllgmt tltglgfkfs aavvelahdl
      541 agwvtmidft gllseqgmal ffglifvaia ciimgagipt tptyiilasi aapaltefgv
      601 pliathffvf yfgvladvtp pvalaayaaa glarsepmtt gttafrlsmg kalvpfmfiy
      661 apsllfveft wlefitalls gltgvlalsa ayigwfrrsl vlwekivltl aglllistnf
      721 iaitigalvv laillrptgs gsspaaa
//
LOCUS       WP_010138493             681 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Oceanicola sp. S124].
ACCESSION   WP_010138493
VERSION     WP_010138493.1
KEYWORDS    RefSeq.
SOURCE      Oceanicola sp. S124
  ORGANISM  Oceanicola sp. S124
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceanicola.
REFERENCE   1  (residues 1 to 681)
  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 681)
  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 681)
  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 681)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..681
                     /organism="Oceanicola sp. S124"
                     /db_xref="taxon:1042378"
     Protein         1..681
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=72204
     Region          21..676
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mdkmqeqpsg araeaqagag spadeqgtai gepgprnltg igkwavrlaa vlmlmlavnq
       61 tfnlgflvgy tlvdmrfyya ilalalavgf lvypatgqsa sgriawydwl lsastlvvca
      121 yfftnamnit lrgwemappe tavwfsyalw ilvleagrra gglplalivg vmslyplyte
      181 mlptaisgfg ssapyaaayh amgsesilgi plrtfaglii gfivfgaalq qtgagaffmn
      241 lsfallgrvr ggpakvaifs sglmgsmsgs vitnvlttgv mtipamrrtg fkgtfaagve
      301 tcastggtlm ppvmgatafv masfmnvpyg tvalaaiips alyffglfvq idamagkedi
      361 kgmpaeelps irqtlkegwy yifvfalliy mllvmrreal apyyatplli llnqvlsrkt
      421 rwgwkelgef idslgmlfan lvailaavgm ivgalsmtgv aatlvndllr ladgsaifll
      481 vmgaltglil gvgmtstaay iflaillapa lvqvglnpma vhmfifywgm lsfitppval
      541 gafaaasiak tppmqtgfea mrigsviyfi pfffafqpal vlqgtamqvv istslavvgi
      601 alfacsvqgy vplvgrlfqg rayafplrll lflsavlial pasiipgwsd fdlvlvamvv
      661 alpilalatw qnrqpaqagi h
//
LOCUS       WP_010139198             635 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein, partial [Oceanicola
            sp. S124].
ACCESSION   WP_010139198
VERSION     WP_010139198.1
KEYWORDS    RefSeq.
SOURCE      Oceanicola sp. S124
  ORGANISM  Oceanicola sp. S124
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceanicola.
REFERENCE   1  (residues 1 to 635)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 635)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..635
                     /organism="Oceanicola sp. S124"
                     /db_xref="taxon:1042378"
     Protein         <1..635
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
     Region          84..604
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 aadttrrlrk ldevvgflls sfdelkprll aastgellgf lgslntgeeh plfprsrlgv
       61 iaedvantrv tfrgttials dgavgdklga ifavknypak tdslmldeln lpvdmvvths
      121 fvpinanima grikrqlrlm qaandgavsl aqelelaqdd leskrlifge hhmtvavyar
      181 tqtalddiaa eirnisatsg inliseafga rahfmaqhpg ntgarsrkaa itnhnfgdla
      241 tfhrtplgkt grevpwgvpi tlfptpersg frfnfheqga pdreptgght lilgrpgsgk
      301 svlaaflmtm arradarvfv fdyragmema vralggsyst vragrptgln plqteidmrg
      361 qawladwlas llerrdrplt pvqtnrlqev vrqnasagha glrnwsdfas llvstddegd
      421 lfermqewta egrygwifga naedsfsidg dvagfdltgi ldsesererm avlsylfrrv
      481 erviedrkpt iivideawka ldnayfaerl snwlvtarkq navvvmmtqy asqlertrtg
      541 ktiveavptq vllpnirasa adyamlglse keldvllgvg stsrlalvrd drgsvvidad
      601 lsalgplvti lggmekgeal vgpnyrdrpd fwrvt
//
LOCUS       WP_010138509             416 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Oceanicola sp. S124].
ACCESSION   WP_010138509
VERSION     WP_010138509.1
KEYWORDS    RefSeq.
SOURCE      Oceanicola sp. S124
  ORGANISM  Oceanicola sp. S124
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceanicola.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Oceanicola sp. S124"
                     /db_xref="taxon:1042378"
     Protein         1..416
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41000
     Region          <26..>125
                     /region_name="PHA03169"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:223003"
     Region          87..336
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 myllagllgm vmvgatafia fddlpdsgee pedddsgddv dswgnlldei fdeegegspa
       61 agpvdpvgde lpggeladde laddeqvgge tpaddlsgdd tfdlppegdt segestagap
      121 adaddmqail arlaeeiats enmitagspg ddlltgdlgd dqlggysged tlaggagddt
      181 llgmgdddal lgqsgndslg ggsgddtlfg gagedalfgm mgddqlsgga gndlmhggag
      241 ddlltggsgd daasggigad rltgglgadt lfgasgddwi sglvaslgdg sapegdvdsd
      301 ldtgdylngg sgddtlvaga gdtvtvgage driilgdwia sdedaaqild fetgqdllvv
      361 syaddgpape isfevtgdvt rvladgtcva tlsgsdavsi ediallpqse altfaa
//
LOCUS       WP_010139989             665 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Oceanicola sp. S124].
ACCESSION   WP_010139989
VERSION     WP_010139989.1
KEYWORDS    RefSeq.
SOURCE      Oceanicola sp. S124
  ORGANISM  Oceanicola sp. S124
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceanicola.
REFERENCE   1  (residues 1 to 665)
  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 665)
  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 665)
  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 665)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Oceanicola sp. S124"
                     /db_xref="taxon:1042378"
     Protein         1..665
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=70278
     Region          1..627
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mqsisklrpa graiavlgwl gavglalagv wiagfgsase tllrigsftl aavvllltri
       61 gsrldvdkpw pvlidlvlla alavamqrya sigealeigl yffqtsdili gvagvvvlle
      121 ltrrafgmpl vvvcllavay alfgrylpwi fqhggyslqq vmqviwysfd gvfgrplsvv
      181 ttlilvfivf gavleavgag pvllrfafva tgrmrggpah aaiaasgvfg tmsgsvsgnv
      241 vgtgvmtipm iikrgfpary aggveaaass ggqfmppimg avafimsdvt gipylticla
      301 allpalfyya slfvavhlea vardirpipr relpvltrhd wlmslcfvvp lvlmlavmis
      361 grspamagfw avlcavvlgf vlnpevrrap qvileglrqg glaaaqilia vaaigivigv
      421 mnmtglglrf agviqdisgd slflslvmmm lgslvlgmgm ptvpaylivi lvmgpaiqmm
      481 gvpvviahlf vvyfgvlssi tppvaiaafa aapiaranpv aigidacria ligfiipfvm
      541 vynpslslvt gftwvglawv clrlsltiwl fstgfsgyas srlgagqrgl rfalglgvlv
      601 pmiwvevact llalalvwsd wrnrsreded spatphhhrd rggrgalapa agpythlksi
      661 redkt
//
LOCUS       WP_010140047             292 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Oceanicola sp. S124].
ACCESSION   WP_010140047
VERSION     WP_010140047.1
KEYWORDS    RefSeq.
SOURCE      Oceanicola sp. S124
  ORGANISM  Oceanicola sp. S124
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceanicola.
REFERENCE   1  (residues 1 to 292)
  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 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 292)
  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   4  (residues 1 to 292)
  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 292)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Oceanicola sp. S124"
                     /db_xref="taxon:1042378"
     Protein         1..292
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31755
     Region          29..158
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          205..285
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mrtlenlsra tealalrkha glrptptgvp glsamrstap slldhdlfgp vfclvlsgak
       61 ttrfdageva fhagqavcis ldlpavsqvv raspaepyla lglqldmael relapqvpag
      121 ddatpqplas aeatpelvda marllsledr adlalmaply lrelhllllq splgamlrrl
      181 arpeteetqi aralsqlrra pgahlriddl arasgmspsl fhrrfreitg ttplqfhkrl
      241 rllearrllq qeghgvtqaa fevgyespsh fsrdyrrlfg lsprqdlstt ga
//
LOCUS       WP_010140326             294 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Oceanicola sp. S124].
ACCESSION   WP_010140326
VERSION     WP_010140326.1
KEYWORDS    RefSeq.
SOURCE      Oceanicola sp. S124
  ORGANISM  Oceanicola sp. S124
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceanicola.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Oceanicola sp. S124"
                     /db_xref="taxon:1042378"
     Protein         1..294
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31746
     Region          16..259
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 msdrnvelvq kvdaqlgetp lwdatrgllw widieqptlw qldpasgaae aeahpgtylg
       61 siamtrsggl laardltlvh rraqtrdwrp fasvpgeamp atrlndgrvd angslwigtm
      121 dnglsqglgg lyrvdpdgtm trmlddvivs ngiafapdgr smyftdtrrh vtwrlgldet
      181 greitsrevl adysssgirp dgacvdaegc lwqaffaggq vvrytpdgrl drqialpvtn
      241 ptclcfggrd lttlfvtsaf kflspaqlad eplagsvfai egvgqgvpen lfai
//
LOCUS       WP_010140939             254 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein, partial [Oceanicola sp. S124].
ACCESSION   WP_010140939
VERSION     WP_010140939.1
KEYWORDS    RefSeq.
SOURCE      Oceanicola sp. S124
  ORGANISM  Oceanicola sp. S124
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceanicola.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 254)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Oceanicola sp. S124"
                     /db_xref="taxon:1042378"
     Protein         <1..254
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          1..208
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 rwdnprhglm apdsfesvft dpelanrltr hmareafrif gsargqmdpg tklslnltyf
       61 dlmdrefvfd lqvllaehql dwsdlvvevq etvvmggdng qifrsltelr hrgaeialdd
      121 fgtgygalkh lrtwpvdmlk idrsfvqmic lnsrdraivg silqlsqdlg frvvaegves
      181 eeqaqllfem gcdlgqgygf grprrgehll edlprgwlag eddcpdeega aveadeaggd
      241 mpscarasfg aevr
//
LOCUS       WP_010141370             730 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Oceanicola sp. S124].
ACCESSION   WP_010141370
VERSION     WP_010141370.1
KEYWORDS    RefSeq.
SOURCE      Oceanicola sp. S124
  ORGANISM  Oceanicola sp. S124
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceanicola.
REFERENCE   1  (residues 1 to 730)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 730)
  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   3  (residues 1 to 730)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Oceanicola sp. S124"
                     /db_xref="taxon:1042378"
     Protein         1..730
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=78666
     Region          8..721
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msdqndpmae irasffiece elmealqdgl qeledgsedp etinvvfrav hsikggagaf
       61 glealvrfah ryetvldevr ngslhpdsda mklfflaadh lsdlirgcrd eseideatsd
      121 elltrldall gedsvseeve petfevqgvs ldldldlgee pddsatvytv rfkpeqdlfa
      181 tgnepsmllr nlcdlgeatv rcnfadlpsl qdlapetpyv ewivelktea aepeirdife
      241 fvdglcelei iggaapatld tsgpaeapsa eealpppatg tadlisddaa paestsakvv
      301 pmgakpappe askdgegerk anttaaksvv rvdlerierl vnlvgelvin qamlsqslde
      361 aglsphsdam ngleefqrlt rdiqdsvmmi raqpvkslfq rmsrivress aavekevrlv
      421 tigeatevdk tvierladpl thmirnavdh gleatekrqe lgkpragtvt ltaahrsgrv
      481 iievaddggg inrkrvheia vtkglvpaea qlsdgeidnl lflpgfstak qvsnlsgrgv
      541 gmdvvktsiq slggritins epgkgttfsi slpltlavld gmvvnvanet lvlplnvvve
      601 tlslgkddvq mlrpghyvvr wrggfvplyd lgvmlgyrhh rqtdpgsivl livledgsra
      661 alvidgiqdq rqvvikgldd sfyrapgiaa atilgdgqia lildpadvis gmghirgtdl
      721 mlserkiane
//
LOCUS       WP_010141567             455 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Oceanicola sp. S124].
ACCESSION   WP_010141567
VERSION     WP_010141567.1
KEYWORDS    RefSeq.
SOURCE      Oceanicola sp. S124
  ORGANISM  Oceanicola sp. S124
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceanicola.
REFERENCE   1  (residues 1 to 455)
  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 455)
  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 455)
  AUTHORS   ter Beek,J., 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 455)
  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 455)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Oceanicola sp. S124"
                     /db_xref="taxon:1042378"
     Protein         1..455
                     /product="CmpA/NrtA family 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=49618
     Region          26..302
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mkrlllslaa ttamvapasa emldlekdvl tfgfikltdm aplavayeqg ffddeglfvt
       61 leaqanwkvl ldgvisgtld gahmlagqpl aatigygtea hiitpfsmdl ngngitvsne
      121 vwemmkpgle tdadgkiahp isashlkpvi esfnaqgkpf nmgmvfpvst hnyelrywla
      181 aggiepgyys penvtgqiga eaflsvtppp qmpatleagt isgycvgepw nqqavfkgig
      241 vpvitdyelw knnpekvfgi saafaeenpn ttlavtkali raaqwldend nanrpeavei
      301 lsrpeyvgad yeviansmtg tfeyekgdtr evpdfnvffr ynatypfysd avwyltqmrr
      361 wgqipeakpd swydevaksv ykpeiyleaa rllveeglan eadfpwdsdg ykaptpasdv
      421 idgigydgka pnayleslpi glkgeqvvvg nevqg
//
LOCUS       WP_010141569             194 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Oceanicola sp. S124].
ACCESSION   WP_010141569
VERSION     WP_010141569.1
KEYWORDS    RefSeq.
SOURCE      Oceanicola sp. S124
  ORGANISM  Oceanicola sp. S124
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceanicola.
REFERENCE   1  (residues 1 to 194)
  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 194)
  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   3  (residues 1 to 194)
  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   4  (residues 1 to 194)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 194)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 194)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Oceanicola sp. S124"
                     /db_xref="taxon:1042378"
     Protein         1..194
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21011
     Region          3..194
                     /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"
ORIGIN      
        1 msdklsiivv epdrdramli vdslaeagdy dihviaevtg larrvkahnp dmvlvdianp
       61 srdmleeltl asgplerpva mfvdqsddgl traaieagvs ayvvaglqpd rvkpvmdaav
      121 arfnmfqrmr nelaatkral eerkvidrak gllmkargmg edeayallrk tamdqnrrva
      181 dvaqalvtaa gllg
//
LOCUS       WP_010142342             709 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Oceanicola sp. S124].
ACCESSION   WP_010142342
VERSION     WP_010142342.1
KEYWORDS    RefSeq.
SOURCE      Oceanicola sp. S124
  ORGANISM  Oceanicola sp. S124
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Oceanicola.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Oceanicola sp. S124"
                     /db_xref="taxon:1042378"
     Protein         1..709
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=71549
     Region          1..706
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mtrptgltai fqpgsiavig assnptktgg rpvhmlikhg yagqiwpvnp kadeiqglpa
       61 faaldalpgv pdlilvavpg asavavleqa aamgvpaaiv lsagfaesgp eglalqhrvt
      121 eiaaasgmri vgpnclgaig vrnraigtfs ialeqqmprs ggisivsqsg nigsaalrll
      181 gesgagvarf iatgneadvq aadaidwlag ddetkvilcc letcrdagrl taaldraraa
      241 gkpvialkig vseagqqaal shtgglagsd rvydavfarh gavrvhslee lvqvgaaaea
      301 kgarrigtrp svaviaasgg fgvmmadaaa angiavnplg eaararinra lplasaanpi
      361 dataqmsadp dilgelldav medkanstlc lmlalsmeip rlrsvftaal aevtrrhpdr
      421 tlvacvsgpa davqelsalg vvcfptidaa magiaalgrl eaiagqsqaa lpviaaakla
      481 pgacrneata ratlaaaglp faqeitatta eeaaaaattl ggamalkils pdiqhksdig
      541 gvelgvsgpe aaraaferii aaaaqhapea vidgvlispm tsggtelilg tttdptfgpv
      601 vmvglggifa eifedtalrl apvsrveaaq mlrelrafpl lngargrapa dlevleqaiv
      661 dlsvfaarha advaeidinp llarpqgqga ialdaliips vtprqeaae
//
LOCUS       WP_010145456             132 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Citricoccus sp. CH26A].
ACCESSION   WP_010145456
VERSION     WP_010145456.1
KEYWORDS    RefSeq.
SOURCE      Citricoccus sp. CH26A
  ORGANISM  Citricoccus sp. CH26A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Citricoccus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Citricoccus sp. CH26A"
                     /db_xref="taxon:1045009"
     Protein         1..132
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=13161
     Region          26..116
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(35..36,43,46,48..49,51,54..55,57,63,68)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(35,63..64,66)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mehtagpgwp egpyelseal vlaaglvppg raisygglag llgaggprqa gramsmaphg
       61 tpwwrivrad gtlpaslsar aaprylaegt plkgtggpdd gagprvdlaa arwvpdtaal
      121 allarlragl gp
//
LOCUS       WP_010145966             353 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Serinicoccus profundi].
ACCESSION   WP_010145966
VERSION     WP_010145966.1
KEYWORDS    RefSeq.
SOURCE      Serinicoccus profundi
  ORGANISM  Serinicoccus profundi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Ornithinimicrobiaceae; Serinicoccus.
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   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   4  (residues 1 to 353)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Serinicoccus profundi"
                     /db_xref="taxon:1078471"
     Protein         1..353
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=37804
     Region          1..290
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mirfesvtkr ypdgttavdd lslevprgdi tvfvgpsgcg kttslrminr mveptegril
       61 indedvaqrk paqlrrsigy viqhaglfph rtvlanvmtv ptligwdkgr artaameaie
      121 kvgltadqas rypaqlsggq qqrvgvaral asdpevvlmd epfsavdplv rtdlqnevrr
      181 lqrelgitvv lvthdideai slgdhvavmr qgghlaqlat pgelltepad dfvasfvgkd
      241 rgyrklgfte ariqpgpeat vtlgedvaag rgwvlvvdea qeplgwvdrd gsggpvrqee
      301 lhrmgsladv gdsarvflda alsapsgrgv vveggrvvgt vraqqvleal gra
//
LOCUS       WP_010146937             219 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Serinicoccus profundi].
ACCESSION   WP_010146937
VERSION     WP_010146937.1
KEYWORDS    RefSeq.
SOURCE      Serinicoccus profundi
  ORGANISM  Serinicoccus profundi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Ornithinimicrobiaceae; Serinicoccus.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Serinicoccus profundi"
                     /db_xref="taxon:1078471"
     Protein         1..219
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24289
     Region          19..198
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mefgevvrrr rmvraydpdr pvpeevvtra lehatrspsa gfsqgwdfvv ltteqererf
       61 wsaatsaear ermdpwlrgv rsapclvvcl sdkeaylery aepdkgradr deahwpvpyw
      121 dvdtgmaall mlltavdegl gglffgvpve hgaqtvaalg apagrrivgv vamgyaasdr
      181 drrspslrrg rrpvsevahr gaygrpwvgg evrreveqg
//
LOCUS       WP_010147162             224 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Serinicoccus
            profundi].
ACCESSION   WP_010147162
VERSION     WP_010147162.1
KEYWORDS    RefSeq.
SOURCE      Serinicoccus profundi
  ORGANISM  Serinicoccus profundi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Ornithinimicrobiaceae; Serinicoccus.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 224)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 224)
  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 224)
  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 224)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Serinicoccus profundi"
                     /db_xref="taxon:1078471"
     Protein         1..224
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24158
     Region          136..222
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(155,174..175,191,194,202..203,214,219)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 maqtfwitpl daappdvava kraceesrft ctivplpalr dllggerpta aillggrpsp
       61 plieaqrwla darvptlill ptltddleai lldrgaqdvl rlplstrrlg arlrllgrap
      121 vqvheesdei rvdgnvtlsp gsrtvcvgns pvtltksefd llltialrrg svvdnhdlsr
      181 alghntlsnr alqthasrvr sklraagapd vissvrgigy rlre
//
LOCUS       WP_010148402             308 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Serinicoccus profundi].
ACCESSION   WP_010148402
VERSION     WP_010148402.1
KEYWORDS    RefSeq.
SOURCE      Serinicoccus profundi
  ORGANISM  Serinicoccus profundi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Ornithinimicrobiaceae; Serinicoccus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Serinicoccus profundi"
                     /db_xref="taxon:1078471"
     Protein         1..308
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34258
     Region          13..276
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mhdavsraad pllsqgysrc reltrrhgtt yywgarllpp eqrrdvyavy alcrladdiv
       61 depetvqvpv padadpgvrl rgfqalftta ladggstdpv maavvdsvrr rgtdpecfdr
      121 fframeldlt retwatweel rdgymegsaa vigemmlpvl epvnpaakgp arslglafql
      181 tnflrdvged ldrgrvylpq adlarhgadp htrtvtpawr avmaeqikrn relyrdasrg
      241 vamlpprsar cvatalrmya lildrieaad ydvfserrrv prrvkvaivs dvlargplrr
      301 lpgpvdgg
//
LOCUS       WP_010149390             405 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Serinicoccus profundi].
ACCESSION   WP_010149390
VERSION     WP_010149390.1
KEYWORDS    RefSeq.
SOURCE      Serinicoccus profundi
  ORGANISM  Serinicoccus profundi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Ornithinimicrobiaceae; Serinicoccus.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 405)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Serinicoccus profundi"
                     /db_xref="taxon:1078471"
     Protein         1..405
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42022
     Region          17..402
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mssgvgepgg gvvlvvnags ssvkyelldp vpgvshakgl ierigladga vhhtvdgvth
       61 devldvpdhe talrlatraf eqhgpsldtv nllavghrvv hggadfadpt litpevvaav
      121 erlvplaplh npgnlagiaa tqaafpdvpq vavfdtafhq gmpeaaatya vprswrqehl
      181 vrrygfhgts hayvsrraad llgrpleevr sivlhlgnga satavdggrs idtsmgmtpl
      241 eglvmgtrpg dldpgvaghl arvaglsmtd lelalskesg llgltgsadf rqvmqrraeg
      301 deaarlafdv vvhrllhyvg ayaavlgrld alvftagvge nnadlrasvl drlagfgvrl
      361 dasandaang etlittaesa vagyviptae eleiarqaaa lvtrp
//
LOCUS       WP_010154740             654 aa            linear   BCT 20-JAN-2025
DEFINITION  type I restriction-modification system subunit M [Leucobacter
            chromiiresistens].
ACCESSION   WP_010154740
VERSION     WP_010154740.1
KEYWORDS    RefSeq.
SOURCE      Leucobacter chromiiresistens
  ORGANISM  Leucobacter chromiiresistens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leucobacter.
REFERENCE   1  (residues 1 to 654)
  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   2  (residues 1 to 654)
  AUTHORS   Youell,J. and Firman,K.
  TITLE     Mechanistic insight into Type I restriction endonucleases
  JOURNAL   Front Biosci (Landmark Ed) 17 (6), 2122-2139 (2012)
   PUBMED   22652768
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 654)
  AUTHORS   Sistla,S. and Rao,D.N.
  TITLE     S-Adenosyl-L-methionine-dependent restriction enzymes
  JOURNAL   Crit Rev Biochem Mol Biol 39 (1), 1-19 (2004)
   PUBMED   15121719
REFERENCE   4  (residues 1 to 654)
  AUTHORS   Murray,N.E.
  TITLE     Type I restriction systems: sophisticated molecular machines (a
            legacy of Bertani and Weigle)
  JOURNAL   Microbiol Mol Biol Rev 64 (2), 412-434 (2000)
   PUBMED   10839821
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114514
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..654
                     /organism="Leucobacter chromiiresistens"
                     /db_xref="taxon:1079994"
     Protein         1..654
                     /product="type I restriction-modification system subunit
                     M"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=72556
     Region          16..151
                     /region_name="HsdM_N"
                     /note="HsdM N-terminal domain; pfam12161"
                     /db_xref="CDD:463478"
     Region          165..426
                     /region_name="HsdM"
                     /note="Type I restriction-modification system, DNA
                     methylase subunit [Defense mechanisms]; COG0286"
                     /db_xref="CDD:440055"
ORIGIN      
        1 mtittppqtq rvattenvvw atadkflrnv veeteygdyi lpftvlrrle clltatktdl
       61 itvvngliek dtpvrfidae vkrrfglsfy ntsplsleai aatddhveas vldyvagfsh
      121 niadiwtsfe fprlvkklad antlhqvvrh fstldlsaes vsntamgdlf envmyrafdk
      181 kgkaagafyt prdaiklmvd llfasdeetl tgqnttrsiy dptagsggml lvgkehltel
      241 npdievnlfg qelmdsafal gkadlliqgg lpdairqgdt llrdeyadrq fdyvlsnppf
      301 ggdwekqyks vveqskvpgs rfshglpsks dgqmlflvhc asklapagka ghggraavvs
      361 nasplfnsdk gpnairqwlf dedlidtiia lptqmfygtg iatyvwildt nkpaerqgki
      421 qlidgsglwd pmrkamgdkr rrmgkakrql vhdaykqfed adpaisrvlt kedfmfrdvt
      481 vfkqarratv fteealetia ehknytdaha diirgldgia wnslpvlfsq rcksaglkap
      541 iglvdavaqa lgvqddtapl aidrkgnpvl ldgwkiterv pmsedldehm qrevlpfaeg
      601 aawdekkakp gneipftrif yvpeeprple eidadvsrlm gelaemfeav hrda
//
LOCUS       WP_010155224             288 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Leucobacter
            chromiiresistens].
ACCESSION   WP_010155224
VERSION     WP_010155224.1
KEYWORDS    RefSeq.
SOURCE      Leucobacter chromiiresistens
  ORGANISM  Leucobacter chromiiresistens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leucobacter.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Leucobacter chromiiresistens"
                     /db_xref="taxon:1079994"
     Protein         1..288
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31592
     Region          1..282
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mrasavvirs ystsfgaatr llgrrhrghv rnvyalvrva delvdgvteg agltpaeqad
       61 alerleaeva rairsgyssd livhafaqta raaridatli apffasmrad lpprdasega
      121 daaglrgfda eqhgayvygs aevvglmclr iftrhrslda leqhrlerga rslgaafqnv
      181 nflrdladdt drlgrsylgt qqrltdadri dwvrrieael adaravlpll pkdarsavrc
      241 alnlfaeltr risrttvddl yarrvrvpdw rkagiiarsi artaaear
//
LOCUS       WP_010155887             395 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Leucobacter
            chromiiresistens].
ACCESSION   WP_010155887
VERSION     WP_010155887.1
KEYWORDS    RefSeq.
SOURCE      Leucobacter chromiiresistens
  ORGANISM  Leucobacter chromiiresistens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leucobacter.
REFERENCE   1  (residues 1 to 395)
  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 395)
  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
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 395)
  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   5  (residues 1 to 395)
  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   6  (residues 1 to 395)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 395)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 395)
  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 15726307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Leucobacter chromiiresistens"
                     /db_xref="taxon:1079994"
     Protein         1..395
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39885
     Region          1..>88
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          77..381
                     /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 mtaiiapsep passaggllq lfrdgaprtr ahlaqvtgls rptvaqridq lielgliapv
       61 adaastggrp saqlafnpra rvvlaadlga lharvavtdl rgellaeist preissgpea
      121 aiswildsae ellpglgydl shvagvgigv pgpvefstgr pinppimpgw drfdipsair
      181 sridapvlvd ndvnimalge latawngvtd lifvkvasgi gagivsggsl rrgangaagd
      241 ighialaraa dtpcpcgnrg cleavasgra laralstpea plhrpsavva lakagdvhai
      301 qlirqagrdi gevltacvsi mnpsaivigg tmaqaaehlv agvrevvyar siplsteqlt
      361 iapslaagna aiygaaqlai daalaperia aalgg
//
LOCUS       WP_010155945             231 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Leucobacter
            chromiiresistens].
ACCESSION   WP_010155945
VERSION     WP_010155945.1
KEYWORDS    RefSeq.
SOURCE      Leucobacter chromiiresistens
  ORGANISM  Leucobacter chromiiresistens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leucobacter.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 231)
  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 231)
  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 231)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Leucobacter chromiiresistens"
                     /db_xref="taxon:1079994"
     Protein         1..231
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25132
     Region          123..212
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(142,161..162,183,186,194..195,204,209)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mnattqtlra arpdlaadla pqsaperrvp egtevrgfal yvgladdkia dgdpklgaiv
       61 trikqlvael apaaetyaav alapeqtggr dvdvvrlalg dpaavarqkq heaeeqdhaa
      121 sgvildlsrk rvlldnvtaa ltfrefellq ylvlregrti sreeliaalw segsdeevps
      181 ertidvhirr lrvklaqyqd ivrtvrgtgy rfdrhadvai lhtaapspda f
//
LOCUS       WP_010156551              82 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Leucobacter chromiiresistens].
ACCESSION   WP_010156551
VERSION     WP_010156551.1
KEYWORDS    RefSeq.
SOURCE      Leucobacter chromiiresistens
  ORGANISM  Leucobacter chromiiresistens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leucobacter.
REFERENCE   1  (residues 1 to 82)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 82)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 82)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 82)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Leucobacter chromiiresistens"
                     /db_xref="taxon:1079994"
     Protein         1..82
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8564
     Region          3..82
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 maritvryfa aaadaaglee eaweldapat laalraelve qygetmhrvi rsgsflvdgt
       61 vrrddgaitg dvvdvlpafa gg
//
LOCUS       WP_010157317             203 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Leucobacter
            chromiiresistens].
ACCESSION   WP_010157317
VERSION     WP_010157317.1
KEYWORDS    RefSeq.
SOURCE      Leucobacter chromiiresistens
  ORGANISM  Leucobacter chromiiresistens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leucobacter.
REFERENCE   1  (residues 1 to 203)
  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 203)
  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   3  (residues 1 to 203)
  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   4  (residues 1 to 203)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 203)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 203)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Leucobacter chromiiresistens"
                     /db_xref="taxon:1079994"
     Protein         1..203
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22289
     Region          12..203
                     /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"
ORIGIN      
        1 mvndqstaps aprrvvvaed eslirldive tlrdngfevv geagdgetav klveelrpdl
       61 vvmdvkmpql dgisaaerin kthlapvvll tafsqrelve raseagalay vvkpftpadl
      121 ipaieialsr fqqivalese vadlaerfet rklvdrakgi lndkmglsep eafrwiqkas
      181 mdrrltmqdv aktiidqlgp kkd
//
LOCUS       WP_010157567             266 aa            linear   BCT 20-JAN-2025
DEFINITION  YaaA family protein [Leucobacter chromiiresistens].
ACCESSION   WP_010157567
VERSION     WP_010157567.1
KEYWORDS    RefSeq.
SOURCE      Leucobacter chromiiresistens
  ORGANISM  Leucobacter chromiiresistens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leucobacter.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Prahlad,J., Yuan,Y., Lin,J., Chang,C.W., Iwata-Reuyl,D., Liu,Y., de
            Crecy-Lagard,V. and Wilson,M.A.
  TITLE     The DUF328 family member YaaA is a DNA-binding protein with a novel
            fold
  JOURNAL   J Biol Chem 295 (41), 14236-14247 (2020)
   PUBMED   32796037
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Liu,Y., Bauer,S.C. and Imlay,J.A.
  TITLE     The YaaA protein of the Escherichia coli OxyR regulon lessens
            hydrogen peroxide toxicity by diminishing the amount of
            intracellular unincorporated iron
  JOURNAL   J Bacteriol 193 (9), 2186-2196 (2011)
   PUBMED   21378183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006857
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Leucobacter chromiiresistens"
                     /db_xref="taxon:1079994"
     Protein         1..266
                     /product="YaaA family protein"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=27720
     Region          2..219
                     /region_name="YaaA"
                     /note="DNA-binding protein YaaA associated with the
                     oxidative stress response [Replication, recombination and
                     repair]; COG3022"
                     /db_xref="CDD:442258"
ORIGIN      
        1 mlillppset krpggsgafd parlrfaael segrtrvrqa lealsgdeaa aakalklgvk
       61 nrgelahnlr lgdsgvlpai erytgvlyda ldvasldaaa rdwldahvav qsalfgtiga
      121 gdeipayrls assrlpelga plkrvwsaah taipwaegrg ivldlrskdy aalaplpaga
      181 gwfvnvaqrs adgrvralnh fnkaakgdlv rrlaqaqaef cdvdallawg aaaglelhvd
      241 pdaeaitlvt elgapgdats rpsdag
//
LOCUS       WP_010161157             334 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Sphingomonas sp. PAMC 26617].
ACCESSION   WP_010161157
VERSION     WP_010161157.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. PAMC 26617
  ORGANISM  Sphingomonas sp. PAMC 26617
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Sphingomonas sp. PAMC 26617"
                     /db_xref="taxon:1112216"
     Protein         1..334
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=34206
     Region          5..334
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mthtiltlng gsssvkygvy vqegnavret asgdvehaga dtalfetiga ivpdaighri
       61 vhggaalfap vvidpaviaq lrhaaafapl hgpaalamit laqarfpdav qvacfdtgfh
      121 admpeiattl pipaafradg vrrygfhgls cesilaqlge avpdrliiah lgngasvtav
      181 dggrsvdtsm gltpaggvvm gtrtgdidpg vllylmrehg mdadavetlv drhsgllgls
      241 glsadlrvlh aadapaaala irifcrsvak qiagmlvtlg gadlivftgg igehdalvrd
      301 ailgalrwag dvpmrvlpsq enaqiarhva allg
//
LOCUS       WP_010162625             655 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Sphingomonas sp. PAMC 26617].
ACCESSION   WP_010162625
VERSION     WP_010162625.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. PAMC 26617
  ORGANISM  Sphingomonas sp. PAMC 26617
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 655)
  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   3  (residues 1 to 655)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Sphingomonas sp. PAMC 26617"
                     /db_xref="taxon:1112216"
     Protein         1..655
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=69934
     Region          1..653
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mtgqdpiaaf rveagelleq ieqglldlgh rlddrdlvde vfrglhtlkg sgamfgfdal
       61 agfthhceta fdrvrkglap athalvaail sakdhmrali dgdgagleat saailarlqa
      121 aiddgadgai avpapveagw slsfrlpada mangtnplml ldelralgdc rivartdaip
      181 pladliptec higwdvelrg dvsrgdiddv fifvmddmal kieplvsvav adatppagpv
      241 tnapaplsep tpatvarvav apgesvrvpa erldelmdrv gelvivqsrl sqvaksggsa
      301 ddlvlrsise eierlaselr etmmvlrmvp vatlfgrfrr lvhdlaretg ktielatege
      361 ateidktvie rladpmihli rnacdhglet paqriaagkp atgqvrlsay qaggevviti
      421 rddgrgidcd rvrakaetqg lvqpgqtmte qetlqlifhp gfstaaqitn lsgrgvgmdv
      481 vkrtieslrg gidvtsvvgq gstvvlripl tlaiidglli rvgtgryvip laaveeciel
      541 sleedlrsrs rsfvtlrdrl vpflrlremf dtgtrpdphq kivviatgte rvglvvdqii
      601 gshqtvikpm sqlhrdvttf agatilgdgg valildagql valgqqqeer lraaa
//
LOCUS       WP_010164208             229 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Sphingomonas sp. PAMC 26617].
ACCESSION   WP_010164208
VERSION     WP_010164208.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. PAMC 26617
  ORGANISM  Sphingomonas sp. PAMC 26617
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Sphingomonas sp. PAMC 26617"
                     /db_xref="taxon:1112216"
     Protein         1..229
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=25345
     Region          7..154
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mdiietpspn fderslpvsm ivlhytgmqt aqaaidrlrd peakvsahyl vaedgqvlrm
       61 vaesqrawha gkscwrgied insasvgiei vnpghelgyr pfmeqqidsv vrlvgditkr
      121 hgitrgnvvg hsdiaptrkq dpgelfpwnr laklrlalpr ptkglmdpmw adagflvale
      181 rfgydvtdkl aavvafqrrf rpelidgvid gecrsillal llpkptgdd
//
LOCUS       WP_010165929             467 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Candidatus Epulonipiscium
            viviparus].
ACCESSION   WP_010165929
VERSION     WP_010165929.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Epulonipiscium viviparus
  ORGANISM  Candidatus Epulonipiscium viviparus
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Candidatus Epulonipiscium.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Candidatus Epulonipiscium viviparus"
                     /db_xref="taxon:420336"
     Protein         1..467
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51030
     Region          11..>467
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 meivsareyv innlqyafnp ksiaivgasr yytkvgykvi ealntwgyrg kiypvnprat
       61 kvfglmaypt vkdipneidl vfiatpahiv ksvledcvak gvkivviats afkeigrgdl
      121 qdkltqycrd nqlpligpnl iglgspylnf ncgfipylpv kgavamisqs ganllaslga
      181 sqkdrfgisf fvglgnkadv dfcefieyan rdahtkcisl yiegidcpea fiktcqnatk
      241 pivaikaggs aigkkaafah tasenlqtsn eyydalfkea kvirvatwqe fldvslglgm
      301 mpplksssiv mitngggsgl lscdhfercg lpmrelqdis aelaqrvkay mpmfgsslnp
      361 vdisgtatpt qykgaftqal rdprvdgvlg sicptavtkv eeiidividl hktykhlnkp
      421 fimecqggee cqraiyklre ngipaygtpe qavnamialy kyynikr
//
LOCUS       WP_010169338             181 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Candidatus Epulonipiscium
            viviparus].
ACCESSION   WP_010169338
VERSION     WP_010169338.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Epulonipiscium viviparus
  ORGANISM  Candidatus Epulonipiscium viviparus
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Candidatus Epulonipiscium.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Candidatus Epulonipiscium viviparus"
                     /db_xref="taxon:420336"
     Protein         1..181
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19475
     Region          6..178
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 meavaaiter rsvrxfanne vsrdlireiv dvarfypswk nsqsarfyiv ddkdkkaxia
       61 teatlglrhn ekiisgcsal lvltikkgls gtgangeyvt skneswevfd sgiaaqtfcl
      121 aavdkgigtv ilgvfkeevv aqicdipdde qvsalialgy peddakksgv rkdvneilff
      181 i
//
LOCUS       WP_010171825             237 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Pseudomonas].
ACCESSION   WP_010171825
VERSION     WP_010171825.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 237)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..237
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=26061
     Region          41..208
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mltfccrlgl iistfaslst valadtgkph tlysslahaa pelnpavlks altamqcavg
       61 ngleqsdrla vidysqpsta rrlwifdlrk ktlvlrdlva hgqksgenfa tqfsnregsy
      121 qssiglfrtq esyegahgys lrmdglepgf ndrardraiv ihaaeyvspl wskregrigr
      181 sqgcpavrpq varqvvdklk dgqfmfswyp dqrwlkssay lnckprqmas agtvkgg
//
LOCUS       WP_010173744             163 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Bacillus coahuilensis].
ACCESSION   WP_010173744
VERSION     WP_010173744.1
KEYWORDS    RefSeq.
SOURCE      Bacillus coahuilensis
  ORGANISM  Bacillus coahuilensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 163)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Bacillus coahuilensis"
                     /db_xref="taxon:408580"
     Protein         1..163
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=18272
     Region          <5..153
                     /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 mktknldqlv hdilketevs plhleleite svglfencev vgqlenirdl gvrvtlddfg
       61 tgfsslaylh tfplngikva rdfimnienn ekslnvtkai ismgnhlhlr vlaegveske
      121 qmdslvqmgc hyfqgyyfnk pmpsgavttl lenlhqqkls qlq
//
LOCUS       WP_010174472             311 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Bacillus coahuilensis].
ACCESSION   WP_010174472
VERSION     WP_010174472.1
KEYWORDS    RefSeq.
SOURCE      Bacillus coahuilensis
  ORGANISM  Bacillus coahuilensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 311)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Bacillus coahuilensis"
                     /db_xref="taxon:408580"
     Protein         1..311
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=35689
     Region          <73..310
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mgeykqndhn riltkesqst iayqsisqlk diikvaldqn ietvtiqkhr nesphtystk
       61 qlalyiqhfe elqmiqseel vsyiqpiltl etnklfgyes llrsnnpais fnpgrlfeva
      121 ntlglnsfld kkarelaika rmnqipkgvk sfinflpsti ynpefclmht fqvvekyqvd
      181 pndlvfevve tenikdidhl klvldtyrre gmkvalddvg sgfstiemlt llqpdivkvd
      241 rhyishcdkd dnkqqflkqv ieranllgit tlaegierke evevlkqlgf hlgqgyffgk
      301 psptveyfql a
//
LOCUS       WP_010175464             116 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Bacillus coahuilensis].
ACCESSION   WP_010175464
VERSION     WP_010175464.1
KEYWORDS    RefSeq.
SOURCE      Bacillus coahuilensis
  ORGANISM  Bacillus coahuilensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Bacillus coahuilensis"
                     /db_xref="taxon:408580"
     Protein         1..116
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=12505
     Region          3..>53
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mlrylknerg ltliellaav ailgvlsaia vvsyfgiken terdvcdanl lqlekdygrh
       61 lvleeldhsd glfgqflvgy deicpiggvv syvdghvecs ehgeseeddg ggvpil
//
LOCUS       WP_010177684              63 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein, partial [Glaciecola sp. HTCC2999].
ACCESSION   WP_010177684
VERSION     WP_010177684.1
KEYWORDS    RefSeq.
SOURCE      Glaciecola sp. HTCC2999
  ORGANISM  Glaciecola sp. HTCC2999
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Glaciecola.
REFERENCE   1  (residues 1 to 63)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 63)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..63
                     /organism="Glaciecola sp. HTCC2999"
                     /db_xref="taxon:455436"
     Protein         1..>63
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          1..>57
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mtnyqtlqqq vlallgdesd vianlaniss ilfmeleqin wagfylhknd elvlgpfken
       61 qlh
//
LOCUS       WP_010177934             286 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Glaciecola sp. HTCC2999].
ACCESSION   WP_010177934
VERSION     WP_010177934.1
KEYWORDS    RefSeq.
SOURCE      Glaciecola sp. HTCC2999
  ORGANISM  Glaciecola sp. HTCC2999
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Glaciecola.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Glaciecola sp. HTCC2999"
                     /db_xref="taxon:455436"
     Protein         1..286
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32378
     Region          1..275
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mkidlhshty ysdghlspae lvlrahqmql dvlaitdhdt tqalaearha qaqekrhlei
       61 isgielttrw hgfdihilgl hfdehdeqlq qrlleqtrtr vdrarqicvk lakcgienvf
      121 ddamvkvgqg qitrahiaqv llergevssf qgaftkylgk dkrafvsaqw idiataiqwi
      181 heaggvaaia hpasydmktk wlkrllsefk slggdgmevt hpnmqptkke llaklaleyd
      241 lkavvgsdfh fpsrwselgk rldisakltp lwqdwpclas fnkeyl
//
LOCUS       WP_010179203             118 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Glaciecola sp. HTCC2999].
ACCESSION   WP_010179203
VERSION     WP_010179203.1
KEYWORDS    RefSeq.
SOURCE      Glaciecola sp. HTCC2999
  ORGANISM  Glaciecola sp. HTCC2999
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Glaciecola.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Glaciecola sp. HTCC2999"
                     /db_xref="taxon:455436"
     Protein         1..118
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12935
     Region          7..110
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(13,31..32,40,43,45..46,48,51..52,54,62,67)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(31,62..63,65)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 myliedatpa ekykailgvv krvpkgcvat ysqiadiagl pgrarmvgka lgatfassei
       61 pwfrvlradg riafgadthi gkeqamhlsn etievknmrv nlklyqwrpe slwgdstd
//
LOCUS       WP_010179621             122 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Aquimarina agarilytica].
ACCESSION   WP_010179621
VERSION     WP_010179621.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarilytica
  ORGANISM  Aquimarina agarilytica
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 122)
  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 122)
  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   3  (residues 1 to 122)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Aquimarina agarilytica"
                     /db_xref="taxon:1087449"
     Protein         1..122
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14604
     Region          20..121
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mtnkkqihnr kyietyrknl rnnctsaeaf lwkylkksql rgrkfrrqhs ignyitdfyc
       61 pkekliield gaihnlpeii ekdeirtqyl eglgfkvirf enkmvfdhlg qvlkeieshf
      121 kt
//
LOCUS       WP_010179924             460 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Aquimarina agarilytica].
ACCESSION   WP_010179924
VERSION     WP_010179924.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarilytica
  ORGANISM  Aquimarina agarilytica
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 460)
  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 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   3  (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   4  (residues 1 to 460)
  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 460)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Aquimarina agarilytica"
                     /db_xref="taxon:1087449"
     Protein         1..460
                     /product="CmpA/NrtA family 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=50682
     Region          46..320
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mkktylhiaa vsltailasc ggekkkaatt vatpepesks tqlviekpql kfgfikltdm
       61 aplaiakekg ffedeglfvs veaqsnwkni ldrvidgqld gshmlagqpi aaqagfgrqa
      121 alvtpysmdl ngngitvsnd vwakmkpnvk kgadgkpvhp isaeslkpvi seykksgkaf
      181 kmgmvfpvst hnyeirywla aaginpgmyt aeniqgqvda evllsvtppp qmpatlesgt
      241 iygycvgepw nqqavfkgig vpvttnydiw knnpekvfvm tkeftekypn ttvaitkali
      301 ragkwldtpg nrpeaveils rpeyvgapvk vlansmtgtf efekgdkrem pdfnvfyryn
      361 atypfysdav wfltqmrrwg qipeakpadw ysskakdiyk peiwkkaael lvaegkipas
      421 dipqtdgykp attefidgnk fdgkdpigyi nsfkignkdq
//
LOCUS       WP_010182188             433 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Aquimarina
            agarilytica].
ACCESSION   WP_010182188
VERSION     WP_010182188.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarilytica
  ORGANISM  Aquimarina agarilytica
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 433)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 433)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Aquimarina agarilytica"
                     /db_xref="taxon:1087449"
     Protein         1..433
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48971
     Region          3..429
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 minsaivkiw gitagavlwn edtqlasfey tpdfalkgyd laplkmplra gtiynfpels
       61 sknetlestf hglpglladv lpdrygnrll nswlaqqgrp ensmnpiekl cfigsrgmga
      121 iefepstnsk qnafdvemeg lvnvathmln krekfttnik qnelkamqdi ltigtsagga
      181 rakaiiaynk ktgvvksgqa napegfehyl lkldgvddaq fgttkgygrv emayylmavd
      241 cgiemmpsll leendrahfm tkrfdrengs tkhhiqtlca mqhynfnevg aysyeqlfqt
      301 mrllrlpypq aeqmfrrmvf nviarncddh tknfafrlkq dsewelspay dichayrpds
      361 iwvskhalsv ngkregitkq dlltvaksmn ikkseliike inacvqkwkf yaqkvnvner
      421 lttkinesil nis
//
LOCUS       WP_010182602             385 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Aquimarina agarilytica].
ACCESSION   WP_010182602
VERSION     WP_010182602.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarilytica
  ORGANISM  Aquimarina agarilytica
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 385)
  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 385)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 385)
  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   4  (residues 1 to 385)
  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 385)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Aquimarina agarilytica"
                     /db_xref="taxon:1087449"
     Protein         1..385
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44893
     Region          <42..151
                     /region_name="ATPase-IID_K-Na"
                     /note="potassium and/or sodium efflux P-type ATPase,
                     fungal-type; TIGR01523"
                     /db_xref="CDD:130586"
     Region          173..378
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          297..378
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mtlildfiln lgiivnilil yilgknerka yhykvlfiif lfilvtqfcf lgyafknkml
       61 ffsmfifqda ipitigpllf lyvkfillps htiweknwih fllpflyvlf asfptlykmq
      121 snpnvfnhlr tgwenayafs ivyslvycif alkilkkgqy lieefysnkd kidlgwlkkl
      181 iyatllvitv disitiyelt isdfegavfp vailvvflii ylayhgimqt evlipefflk
      241 khglqkqtei svvesavist kkfeydreem ieiqekleve mlnnkwfldp dlslgilaek
      301 lsitdkklsy llnqhmtasf ytyinqlrvn takakltdlk lknytiiaia eesgfkakst
      361 fntifkrftg mtpsqyrkit kntkv
//
LOCUS       WP_010183180             644 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Sphingomonas sp. PAMC 26605].
ACCESSION   WP_010183180
VERSION     WP_010183180.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. PAMC 26605
  ORGANISM  Sphingomonas sp. PAMC 26605
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 644)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 644)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 644)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 644)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Sphingomonas sp. PAMC 26605"
                     /db_xref="taxon:1112214"
     Protein         1..644
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68936
     Region          1..644
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mtsatdsiva katphpalva ltigaigvvf gdigtsplya frealnltak dgldpseilg
       61 vlslaiwsli lvvtvkyvif lmradnqgeg gvlaltalar ralgrrslia lvlgaagasl
      121 fygdaiitpa lsvlsavegl ktipglggmf tdsvilgvti vilvalffiq srgtasvsal
      181 fgpvcivwfl aigalglwhi tdepsilrvi sphygaifla thgvtglfvl gavfltvtga
      241 ealtadmghf gilpirigwf vlvfpcliln ylgqgayaln aleaaaaagk pfvnqdwffl
      301 mapegvrpwl iglammatvi asqavitgay sltqqaiqlg llprlrirqt satqagqiyl
      361 psinwlllvg vlvlviqfrt ssamaaaygi avtgtmvvtt llayivvrhr wnwgrplala
      421 vilpfltldl iffganilrv ieggwvplvv aavigliiyt wnrgrgivre felrqsvpla
      481 dlaaalakrp pervegtavf ltanpdsapg allhnlkhnk vlheknlivs irtadrpsve
      541 qderaeirpv danftiivlt ygfmespdvp rdlgleavsh kkslnpakts yfigrntikp
      601 aadqgmplwq drifmflqrn asdptdflri ppgkvlelge qvtv
//
LOCUS       WP_010184092             498 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Sphingomonas sp. PAMC 26605].
ACCESSION   WP_010184092
VERSION     WP_010184092.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. PAMC 26605
  ORGANISM  Sphingomonas sp. PAMC 26605
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Sphingomonas sp. PAMC 26605"
                     /db_xref="taxon:1112214"
     Protein         1..498
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=50869
     Region          1..498
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mpkallidpt dsvatlvepa hagdtllfgv hpvialsdvp sghkvavvpi mrgtpvlkfg
       61 fpigtatadi avgahvhshn lataldgtld yrftpgavaa ppggsdratf egypradgrv
      121 atrneiwvlp tvgcvartat riaaladaal aretgdgmvd gvhafthpfg csqlgddldg
      181 trsilaalac hpnaggvliv glgcesnqia alleeipatr rpmvrtlvtq lagdeidegv
      241 akvaklvtla ragrstvgld rlvlgvkcgg sdglsgltan plvgriserv vaaggsvvlt
      301 eipemfgaer llmdratdet vfdgivtmvn gfkryfldhn epvsenpspg nvaggittle
      361 ekslgavqka graavsqvla yggrvsatgl tlleapgnda vsctalaaag atailfttgr
      421 gtplgfpvpt lkiasnsdla mrkpgwidfd agavlehgfa pvaedlagtl caiasgaata
      481 aerngereia iwkrgvtl
//
LOCUS       WP_010184303             236 aa            linear   BCT 20-JAN-2025
DEFINITION  MJ0042-type zinc finger domain-containing protein [Sphingomonas sp.
            PAMC 26605].
ACCESSION   WP_010184303
VERSION     WP_010184303.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. PAMC 26605
  ORGANISM  Sphingomonas sp. PAMC 26605
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 236)
  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 10020205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Sphingomonas sp. PAMC 26605"
                     /db_xref="taxon:1112214"
     Protein         1..236
                     /product="MJ0042-type zinc finger domain-containing
                     protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25115
     Region          1..35
                     /region_name="MJ0042_CXXC"
                     /note="MJ0042 family finger-like domain; TIGR02098"
                     /db_xref="CDD:131153"
ORIGIN      
        1 milectecht rylvpdsaig pdgrtvrcas ckhswfqegv tadetldrdd asateaavsp
       61 pipdapppve haapteaaap sqsgydafah appfrarrnp akrwtiaala agvvmiaafg
      121 givysgapgl asdlfqrnag tplkivskpi dqhvfngnei favsgtvlnp tdspqpvpdi
      181 radlrdaqrr ivfswmirpe antlaprgkl dfnsakldvp vnakelvlsf sgeppr
//
LOCUS       WP_010184551             269 aa            linear   BCT 20-JAN-2025
DEFINITION  3-deoxy-manno-octulosonate cytidylyltransferase [Sphingomonas sp.
            PAMC 26605].
ACCESSION   WP_010184551
VERSION     WP_010184551.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. PAMC 26605
  ORGANISM  Sphingomonas sp. PAMC 26605
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (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   2  (residues 1 to 269)
  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 10787365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Sphingomonas sp. PAMC 26605"
                     /db_xref="taxon:1112214"
     Protein         1..269
                     /product="3-deoxy-manno-octulosonate cytidylyltransferase"
                     /EC_number="2.7.7.38"
                     /GO_function="GO:0008690 - 3-deoxy-manno-octulosonate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0033468 -
                     CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28812
     Region          1..257
                     /region_name="KdsB"
                     /note="CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell
                     wall/membrane/envelope biogenesis]; COG1212"
                     /db_xref="CDD:440825"
ORIGIN      
        1 mpdlivvpar fgsqrlpgkp liaiagqtll srvvavareg arragqvdvv vatddarild
       61 haralgcdav ltdgaitsgs grawaaardr apaivvnlqg dapfvdpamv aaligalrds
      121 asavatpvvr ldwaaldamr ahkttspfsg ttcvrdatgr alwfskavlp airdearlre
      181 tealspvfrh iglyayrfea lrafeatppt pyeqfegleq lrflesgvei rtvevapprh
      241 amsgidtpad vvmaerliaq fgepertwr
//
LOCUS       WP_010185741             320 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Sphingomonas sp. PAMC
            26605].
ACCESSION   WP_010185741
VERSION     WP_010185741.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. PAMC 26605
  ORGANISM  Sphingomonas sp. PAMC 26605
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 320)
  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 320)
  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 320)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Sphingomonas sp. PAMC 26605"
                     /db_xref="taxon:1112214"
     Protein         1..320
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32500
     Region          15..82
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          175..241
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mtepipadep klfpksagdt lreareaqgl slaevaartr ipvrqleave egnyaalpsi
       61 tysvgfakay aravgvdeva iarevrgasd qpsarrtqye ayeidepsrv pprglaittl
      121 liavvvviga alffgtslfr gdgepaptps saigntmqea patapspsap tgavvltasd
      181 dvwlrvydka gktlhlgtmk pgesyavpad avgpminvgr pdklqvtvgg tavaplgdgk
      241 raikdvplda asltarstpa aaatgspgva pttarreetr asrtrstsse paaaaplnia
      301 apatvapepa apggaatpap
//
LOCUS       WP_010185951             140 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Sphingomonas sp. PAMC
            26605].
ACCESSION   WP_010185951
VERSION     WP_010185951.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. PAMC 26605
  ORGANISM  Sphingomonas sp. PAMC 26605
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 140)
  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 140)
  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   3  (residues 1 to 140)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Sphingomonas sp. PAMC 26605"
                     /db_xref="taxon:1112214"
     Protein         1..140
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15522
     Region          19..117
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mtksrytvgd gsierarelr rnataaetkl wsvlrgsald ghkfrrqqrl gpfyadfvcq
       61 aarlvveidg ethvgneerd arrtaflere gyrvlrfsna dvmqnvegvt qvirsaigas
      121 pshlampggp lplprgerrs
//
LOCUS       WP_010186573             396 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Sphingomonas sp. PAMC 26605].
ACCESSION   WP_010186573
VERSION     WP_010186573.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. PAMC 26605
  ORGANISM  Sphingomonas sp. PAMC 26605
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Sphingomonas sp. PAMC 26605"
                     /db_xref="taxon:1112214"
     Protein         1..396
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=40383
     Region          12..394
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msasrvpagt tiltfnggss slkfglfdva galaeplltg eietagggav rlhaadpagr
       61 vrvdhslgta apdswtrhvv dlldrtalpa pavighrlvh ggpellapvr idaavlgqiq
      121 aaarfaplhi ptalatirat qqhfpncpqv acfdtgfhat mpavastlpl paalraqglr
      181 rygfhglsce sivrqlghdv perliiahlg ngasvtavra grsvdtsmgl tptgglimgr
      241 rtgdldpgvl lhllrscgyt petlatlvdr esgllgvsgi dsdlrrlnaa aatqpaaala
      301 iamfchalvk tiaamagslg gvdmivftgg igehdpgvra tacaalgwmg valdptrnra
      361 gaatisgdas rvavrvlpar edreialhsa avvgag
//
LOCUS       WP_010186903             793 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Sphingomonas sp. PAMC 26605].
ACCESSION   WP_010186903
VERSION     WP_010186903.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. PAMC 26605
  ORGANISM  Sphingomonas sp. PAMC 26605
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 793)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 793)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 793)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Sphingomonas sp. PAMC 26605"
                     /db_xref="taxon:1112214"
     Protein         1..793
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=85156
     Region          35..790
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 minrrsfllr saaaaaiasg pacraadpag rqtnvrgaaa pieivddvyg iphiraqsip
       61 daffgqgyvv ardrlfqidf ehrrelgrma eafgpefvrh daqarlfhyr gdldaelrri
      121 paevlacara yiaginarid avtadptllp leyrilgvap irwdihdmvl argaaagntd
      181 devrrarlaa lglleldavi aplmpahplt vpdgldvaqv snddlgvlti grlpfgpntp
      241 vvdpdersgr leranagsna wtiaaarsat grpilandph lgiggfgprh vahlsapgld
      301 vigggapglp gimqghterf afgrtnfhid qedlfvlelh phdperyrha ggwkrftrve
      361 isvpvkgaap htevlryaaq gpvvsydpak hrataiasia mqpggggsfa miainlakdw
      421 aglqeafklh psptnlhyad vagntgwqai gfmpvrkrga glmpvpgdgr ydwtgmrdhr
      481 alpsaynpak gwfasanqdn lppdwptdri pafdfrdpyr yeriadvlsh qtshsladsv
      541 alqhdtlstp arqlvallpt assegarpav tllrgwncrl daasgaaalf emlwrelshr
      601 mlaaivpera kaivtsigps vllgllarpd arlgqdptaa rdalfdaali aawtnakaql
      661 gpdpanwrwg alhrlriqhp laripaiaaa fpaievgptg gdsytvqahw lgngpgwsag
      721 ggasylqvid vgawdnslvl nlpgqsndpr sphyqdqvat wsvgqmqpml ysraaveaha
      781 iarltltpqg arp
//
LOCUS       WP_010188284              99 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Corynebacterium aurimucosum].
ACCESSION   WP_010188284
VERSION     WP_010188284.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium aurimucosum
  ORGANISM  Corynebacterium aurimucosum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Corynebacterium aurimucosum"
                     /db_xref="taxon:169292"
     Protein         1..99
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10539
     Region          10..91
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(26,52..53,55,74)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mppknpsssr vtevvlripp gnvstygeia kvvgvgaryv gwvmsksagl pwwrvvnstg
       61 rahtsaaqvh weeegvphrg drvvlsecgl daadlqhla
//
LOCUS       WP_010191930             290 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Bacillus sp. m3-13].
ACCESSION   WP_010191930
VERSION     WP_010191930.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. m3-13
  ORGANISM  Bacillus sp. m3-13
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 290)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 290)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Bacillus sp. m3-13"
                     /db_xref="taxon:406124"
     Protein         1..290
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33050
     Region          21..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..287
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mdllkdmnta mkyieenlts eidfkvvart ahcseyhfkr mfsflagitl seyirrrrls
       61 laalelhnsk vkvidvaiky gynspdsftr affnlhgitp searengqql kayplmtfql
      121 sirggnemnf rieqkeafni vgikkrvpiv fqgenpeiae mwksldadki shlqklsnve
      181 pkgmiqastn fsegrmeekg eldqyigvat tqenpenfsk lkvpastwai festgpfpqt
      241 lqetwgriys ewflssnyqv tagpemlsik nrdlsapsvk ceiwipvlkk
//
LOCUS       WP_010192101             277 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phytoene/squalene synthase family protein
            [Bacillaceae].
ACCESSION   WP_010192101
VERSION     WP_010192101.1
KEYWORDS    RefSeq.
SOURCE      Bacillaceae
  ORGANISM  Bacillaceae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Bacillaceae"
                     /db_xref="taxon:186817"
     Protein         1..277
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32111
     Region          7..274
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mndlmkayhh cesiikehsk tfykafmllp kekkqavwav yafcrqvddi vddgmnpkee
       61 lfafkamfad flegklpsed pmwlalqdvf nryemdvqsf hdmivgqemd lykklynsee
      121 evlhysyhva stvglmllpi laptnkdilr edaialgqam qitnilrdig edlerdriyi
      181 piemlekagy slddlnkhiv nnkfisvwee mankaeslye qalstihlyp mhsrtpvkga
      241 aylyrailgs irkkgysvfk tkhyvtseek qqiisqm
//
LOCUS       WP_010193909             323 aa            linear   BCT 20-JAN-2025
DEFINITION  GerAB/ArcD/ProY family transporter [Bacillus sp. m3-13].
ACCESSION   WP_010193909
VERSION     WP_010193909.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. m3-13
  ORGANISM  Bacillus sp. m3-13
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Bacillus sp. m3-13"
                     /db_xref="taxon:406124"
     Protein         1..323
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=36810
     Region          2..302
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 mrnketislw qlfilmlife mgsatvvgig geakqnvwma islagligvg yiyvlhfmlg
       61 rkkgynlfal iefclgkwvg gavsflyimy fiyissrvlr dfgelivsti fiytpieiis
      121 itimltivym lnsgievmar tseiffpyvf lftflvgifi lmsgeiqfen lrpfldegik
      181 pifqaifpsl ltfpygelia favvlplvtk ykkakgfama siilstsvlv yssviqvmtl
      241 ghemkersnf pllsaareis lldfvervdi avvfvvmfgi ivkigvflfw cikgfrtylq
      301 krvpqisfsc wfhnlfvfyh hnr
//
LOCUS       WP_010195811             182 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Psychrobacter sp. PAMC 21119].
ACCESSION   WP_010195811
VERSION     WP_010195811.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter sp. PAMC 21119
  ORGANISM  Psychrobacter sp. PAMC 21119
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Psychrobacter sp. PAMC 21119"
                     /db_xref="taxon:1112209"
     Protein         1..182
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=19750
ORIGIN      
        1 mnmkalkqql gftlielmvv imivailaai aipsyrqyiv rnaesqaqas mqqldielnr
       61 wrasaltykg fipkkqasdg tfsyaydatd nktiyvprgs ngtnydylim lvdgstgntl
      121 aptgtgysta gsswrmfaqp ntslknsnaq ilmtsstgvk ckskdrtita astncgtgqe
      181 dw
//
LOCUS       WP_010195949             410 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Psychrobacter sp. PAMC 21119].
ACCESSION   WP_010195949
VERSION     WP_010195949.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter sp. PAMC 21119
  ORGANISM  Psychrobacter sp. PAMC 21119
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Psychrobacter sp. PAMC 21119"
                     /db_xref="taxon:1112209"
     Protein         1..410
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44651
     Region          24..408
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msasltttfd dknsdtstlt sptlvlncgs ssikyalisd dnstritgla enlgldtari
       61 khttlngekl eisipggrhk lalqkilell eqyhfiavgh rvvhggreys eavrvddhal
      121 aevkrlkila plhnpanalg ieavqaiypd mpqvvvfdta fhqtmppvaf ryalpkylye
      181 ehkirrygfh gtshayvser tsqiteskgp hgwltahlgn gcsvaavydg ksldtsmglt
      241 pleglmmgtr sgdvdpslhm hlkrqlgmsl eetdkmlnsd sgllgisgls ndlrtieqaa
      301 seghkdaqla iemfcyragk ylaslscalp eftgivftgg igensvttra silavmrhfg
      361 ikidadknad lsrgkegsfh addssielwv vptdeeyria qetrqalnlv
//
LOCUS       WP_010196230             580 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA, partial [Pseudomonas amygdali].
ACCESSION   WP_010196230
VERSION     WP_010196230.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas amygdali
  ORGANISM  Pseudomonas amygdali
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 580)
  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   3  (residues 1 to 580)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Pseudomonas amygdali"
                     /db_xref="taxon:47877"
     Protein         1..>580
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          3..>579
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msinldqaqq tfivearell qameesllql esepgdqdai gavfrathti kgsaglfglt
       61 pivsfthive dvldrlregs vsvdagliav llksgdhmle lidvvasrgq tlqppalere
      121 aalrqalqvy qapgnaqpad eaqapsvide qpaevlwhis lrfgvdvfrn gmdplsflry
      181 lntlgqmvqv ttvtdsipal eawdpeschl gfeidfrssa ghaainevfd fvredcavei
      241 tlmsetanhv dptgtdlvsq tgqspavasg ellgdqravp rapaaatale rpssaseqkn
      301 kdgryvrvna dkldelinlv gelviasaga sllarscdnd plqeasstvs glveqildga
      361 lhlrmipigd tfnrfrrvvr dvsqelgkdi dliingaete ldktvvekig dplmhllrns
      421 mdhgiesaea rraagkpakg hlslnayhds gsivieiadd gaglnreril dkaqqrglva
      481 agasltdqei ynlifepgfs taeavtnlsg rgvgmdvvkr nitllrgtvd ldsqpgqgtt
      541 vrirlpltla iingflvgid qstyvipldm vqecielder
//
LOCUS       WP_010198155             633 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA, partial [Pseudomonas amygdali].
ACCESSION   WP_010198155
VERSION     WP_010198155.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas amygdali
  ORGANISM  Pseudomonas amygdali
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 633)
  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   3  (residues 1 to 633)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Pseudomonas amygdali"
                     /db_xref="taxon:47877"
     Protein         <1..633
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          164..632
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 raepqsadev aapepepvve aeapapvaeq aasdditdde feqlldslhg tspvsaapsa
       61 apavapagde itdqefesll dqlhgkgkfa adavaapapa paaqskgaap agdeitddef
      121 ealldqlhgk gsfdgaiaat aapapapapa avaakapsaa aasdeitdhe feslldelhg
      181 kgkfepdavv akapapaaai aaapppaakp aaapvpaaka epakpapapa rapaptgekp
      241 vateaettvr vdtarldeim nmvgelvlvr nrlvrlglns gdeamskavs nldvvtadlq
      301 tavmktrmqp ikkvfgrfpr lvrdlarqlk keinlelvge etdldknlve aladplvhlv
      361 rnavdhgiet peereasgks rggkvilsae qegdhillsi sddgkgmdpn vlrsiavkrg
      421 vmdkdaadrl sdtdcynlif apgfstktei sdvsgrgvgm dvvktkisql ngsiniystk
      481 gqgskivikv pltlaimptl mvmlgnqafa fplvnvneif hlnlsttnvv dgqevvivrd
      541 kalplfylkr wlvssaahee qreghvvilt vgtqrigfvv dqlvgqeevv ikplgkmlqg
      601 tpgmsgatit gdgrialild vpsmlkryaa rri
//
LOCUS       WP_010198204             115 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [unclassified
            Psychrobacter].
ACCESSION   WP_010198204
VERSION     WP_010198204.1
KEYWORDS    RefSeq.
SOURCE      unclassified Psychrobacter
  ORGANISM  unclassified Psychrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 115)
  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   3  (residues 1 to 115)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="unclassified Psychrobacter"
                     /db_xref="taxon:196806"
     Protein         1..115
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12453
     Region          2..115
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mampgrggil tchmedietl yasylsfvnn galfissdrv qklgdevfia vtlpnsserl
       61 pmngkvvwin ykaqsgrpag favqigtdia gqriknever llagkidslq stytm
//
LOCUS       WP_010199558             434 aa            linear   BCT 20-JAN-2025
DEFINITION  TerD family protein [Psychrobacter sp. PAMC 21119].
ACCESSION   WP_010199558
VERSION     WP_010199558.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter sp. PAMC 21119
  ORGANISM  Psychrobacter sp. PAMC 21119
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Psychrobacter sp. PAMC 21119"
                     /db_xref="taxon:1112209"
     Protein         1..434
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=47319
     Region          7..434
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 msqnqpqkli aganaplptd sisirilsqn aidcaayrlt tdgkvrgdgd mifygqtrsd
       61 dgnvsfrghd sdgffdinla aqpadidkia lafssaqala qigdvdiqvl qgsqvlmtcq
      121 lssagrneka iilaecyrrq gswkfrfiaq gfegglkpls ehfgveiade apaqsssqnn
      181 nqaqnqnqsq gqsqpintqr pintqkvgsa tqastpppip aspsinlski tltknqssin
      241 lkkrddfgki svnlnwnqrp dmdkqapkkg llgdlfkqhk aggidldvga mihlkngekt
      301 liqalgnrfg slqsapyvcl raddrtgqvs ggewldingq qwsqieevfi fafiyegapn
      361 waktdgvvti hvpdqspiet rltegtgnlp mcaiarlvnq qgsinverin qyfkghqemd
      421 kafnwgfswk rgsk
//
LOCUS       WP_010199939             327 aa            linear   BCT 20-JAN-2025
DEFINITION  formate dehydrogenase accessory sulfurtransferase FdhD
            [Psychrobacter sp. PAMC 21119].
ACCESSION   WP_010199939
VERSION     WP_010199939.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter sp. PAMC 21119
  ORGANISM  Psychrobacter sp. PAMC 21119
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Psychrobacter sp. PAMC 21119"
                     /db_xref="taxon:1112209"
     Protein         1..327
                     /product="formate dehydrogenase accessory
                     sulfurtransferase FdhD"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0097163 - sulfur carrier activity
                     [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36208
     Region          49..324
                     /region_name="FdhD"
                     /note="Formate dehydrogenase assembly factor FdhD, a
                     sulfurtransferase [Energy production and conversion];
                     COG1526"
                     /db_xref="CDD:441135"
ORIGIN      
        1 maklntqaaa idmpeataes tvtplsrahl vqkhyyapte ssgsqqtyie dqsanlvvea
       61 aisiiingih yavlmaspyq leylaigflf segliqhshd lldwevtqlt dvasyqrftq
      121 hsdeddtags fgqtlaqlqd ydiyvveltl nqrshqriqa qrrqlagrtg cgmcgitglt
      181 qalpdlsiyr qdkkrikvdt pslgdlleir qkvdamqhth qltgavhaaa tmqgqhlhlf
      241 edvgrhnald kligwqlqhk adincvvmts rlsielvqks irshipwlig msaptstavr
      301 vaeryglgla gflrdsrvty ysnhsng
//
LOCUS       WP_010201374             293 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Psychrobacter sp. PAMC 21119].
ACCESSION   WP_010201374
VERSION     WP_010201374.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter sp. PAMC 21119
  ORGANISM  Psychrobacter sp. PAMC 21119
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Psychrobacter sp. PAMC 21119"
                     /db_xref="taxon:1112209"
     Protein         1..293
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32001
     Region          1..289
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mkidlhchst csdgtyapte vvqrahaagv dvlaltdhdt llgiddarat atacgmtlin
       61 gveiscehtl sggygknkst nkiihvlgld ftdrekmhat lqqlqdsrat rgqritekls
      121 elldinydel wqavldkasg npqavgrahi gqvlfergev ktvqkafdky ladnkpayva
      181 iealtmqhgi elihacggka vlahptryql satrvrklie efaqlggdac elpansepis
      241 trrmvdrsia ehelvtsigs dfhgsnmpwr rigdvptlhp eqqgiwqsft alt
//
LOCUS       WP_010203537             340 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Salinibacterium sp. PAMC
            21357].
ACCESSION   WP_010203537
VERSION     WP_010203537.1
KEYWORDS    RefSeq.
SOURCE      Salinibacterium sp. PAMC 21357
  ORGANISM  Salinibacterium sp. PAMC 21357
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Salinibacterium.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 340)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Salinibacterium sp. PAMC 21357"
                     /db_xref="taxon:1112215"
     Protein         1..340
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35999
     Region          6..340
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mnhvtarias tgtylperir ttaetekqlr sqnptvklat glihrltgve svhlrpdgwq
       61 tsdlavaaar talehspgpi dliifssasq dliepatshi vaakleidcp vmdvknacns
      121 vlngmqvgaa liatgqyrrv liasgetpsl gvrwdldshq qfirsfpgyt msdggaavil
      181 eaveldpadd apagildslf vaasknwsvg tlsiggsmnp rnaelsyfdi dgaalqqafl
      241 dlgpqpvhdi ldrngltwdd idlvaihqva lpylpavfer lgvvedktvi tvadhgnlas
      301 vtlplqleva ratgqvkpgs lvlmiglagg islglmlvrl
//
LOCUS       WP_010203680             377 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Salinibacterium sp. PAMC
            21357].
ACCESSION   WP_010203680
VERSION     WP_010203680.1
KEYWORDS    RefSeq.
SOURCE      Salinibacterium sp. PAMC 21357
  ORGANISM  Salinibacterium sp. PAMC 21357
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Salinibacterium.
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
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 377)
  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   5  (residues 1 to 377)
  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   6  (residues 1 to 377)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 377)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Salinibacterium sp. PAMC 21357"
                     /db_xref="taxon:1112215"
     Protein         1..377
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38860
     Region          27..77
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          88..371
                     /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 mgftngkalr ptakvlpeha rnhnrslviq tlyrqgelsr adiaretglt rvtisdlvae
       61 livdglvvet gqregsrpgk patmlelnae afdlvgvdls dystfrgavm dlhgairyrh
      121 eialadssga datakvialv eallanvtrp vlgvgigspg vvdlagvvls apnlgwtdvp
      181 lqsmlterfe lpvvvandan vaalaehsfg saasdmmlik vghgvgagll lggiplfgss
      241 faageighvv vgtdggleca cgktgcletw latprldaai aaasdddarn tvlteagqrl
      301 gialapvvga lnlseivlsg ptsllegalk hatietlrar tmakfhgdlt vrmtalgedi
      361 vmrgaavmvl saqlgvs
//
LOCUS       WP_010202590             201 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Salinibacterium sp.
            PAMC 21357].
ACCESSION   WP_010202590
VERSION     WP_010202590.1
KEYWORDS    RefSeq.
SOURCE      Salinibacterium sp. PAMC 21357
  ORGANISM  Salinibacterium sp. PAMC 21357
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Salinibacterium.
REFERENCE   1  (residues 1 to 201)
  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 201)
  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   3  (residues 1 to 201)
  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   4  (residues 1 to 201)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 201)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 201)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Salinibacterium sp. PAMC 21357"
                     /db_xref="taxon:1112215"
     Protein         1..201
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22054
     Region          11..201
                     /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"
ORIGIN      
        1 mtdqntnkta prrvvvaede slirmdivei lrdagyevvg eagdgetava latelrpdlv
       61 imdvkmpqld gisaaerlsa nhiapvvllt afsqkelver aseagalayv vkpftpndll
      121 paieialsry aqiitleaev sdlverfetr klvdrakgll nekmglsepd afrwiqkasm
      181 drrltmhdvs qaiidqlsak k
//
LOCUS       WP_010204396             288 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Salinibacterium sp. PAMC
            21357].
ACCESSION   WP_010204396
VERSION     WP_010204396.1
KEYWORDS    RefSeq.
SOURCE      Salinibacterium sp. PAMC 21357
  ORGANISM  Salinibacterium sp. PAMC 21357
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Salinibacterium.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Salinibacterium sp. PAMC 21357"
                     /db_xref="taxon:1112215"
     Protein         1..288
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31379
     Region          9..283
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mssrlklydr vaedaasivi rsystsfsaa srllgvevrq hveniyalvr iadeivdgga
       61 eeagldliat trqlnelere tenamehgfs snlvvhafal tarevsfgae ltapffesmr
      121 mdlsqkvhdq asferyvygs aevvglmclc aflhghdvgd eqraklehga ralgaafqkv
      181 nflrdladdf etlgrsyfpg idvatfteee kvrllddlda dlrdaaigse lpasskkava
      241 lahalfaqls kriratpase lvrtrvrvpn vvklrlaaaa aigvgpre
//
LOCUS       WP_010204851             336 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Salinibacterium sp. PAMC
            21357].
ACCESSION   WP_010204851
VERSION     WP_010204851.1
KEYWORDS    RefSeq.
SOURCE      Salinibacterium sp. PAMC 21357
  ORGANISM  Salinibacterium sp. PAMC 21357
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Salinibacterium.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 336)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Salinibacterium sp. PAMC 21357"
                     /db_xref="taxon:1112215"
     Protein         1..336
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36505
     Region          1..336
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mkarvqavey ylpenvltnl dlatefpews vdkisaktgi errhiaapdq fsshlaiaag
       61 erlfkqknid rstieylivc tqspdyylpt taclvqdglg lrteigatdi tlgcsgyiya
      121 lglakglies gqvtnvlvit adtyskfinp kdksvrtifg dgsaatlitg sdddedhftg
      181 itygtngaga knlivpnggl rpgtdispka aiserniees qydifmdgpe ifnftldivp
      241 ssvdsilska slelddidlf vfhqanafml ehlrkklgvp kekffvalee sgntvsstip
      301 ialveaerrg alkpemrvmi lgfgvglswg gmivkw
//
LOCUS       WP_010205514             412 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Salinibacterium
            sp. PAMC 21357].
ACCESSION   WP_010205514
VERSION     WP_010205514.1
KEYWORDS    RefSeq.
SOURCE      Salinibacterium sp. PAMC 21357
  ORGANISM  Salinibacterium sp. PAMC 21357
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Salinibacterium.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 412)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 412)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Salinibacterium sp. PAMC 21357"
                     /db_xref="taxon:1112215"
     Protein         1..412
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44897
     Region          4..397
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 madlrvelyg elvghlvggd rrtfdfiatp eaiaawglgs tilsesvpld lvanrsragr
       61 rrnffaeilp egralenlaa eirvsaddvi pllarfgrdv agaiqiydpe apgeprtpar
      121 aavssaeigr mltntqaapl gnrpqsgrts lagvqdkivl aredgqwfqv vegypsthiv
      181 kppssrypti tfdeeygyra akaagltsle akienfdgiq glvierydrs pdapqgrihq
      241 edmnqalgas rnekyqefgg kvtlkrisdv lgrdgdresv eqllrlltvs qavgnldmhg
      301 knismlhlhd gttritpayd vvpqthldsd gkmalavsrk yahsaitidd lvaeaetwkv
      361 rsaraiisst ldsvdvflra eapvaqaypg lhddisrftr nlldgrqtgy vs
//
LOCUS       WP_010205605             373 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Salinibacterium sp. PAMC 21357].
ACCESSION   WP_010205605
VERSION     WP_010205605.1
KEYWORDS    RefSeq.
SOURCE      Salinibacterium sp. PAMC 21357
  ORGANISM  Salinibacterium sp. PAMC 21357
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Salinibacterium.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Salinibacterium sp. PAMC 21357"
                     /db_xref="taxon:1112215"
     Protein         1..373
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=38869
     Region          4..371
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mttvfvvnsg sssikwelld aesgsvysgg iverigepgg gatdhddgmq qilaelggeh
       61 pavvghrvvh ggaeftqatv itdavaqrle eisvlaplhn panlkgiraa ratfstvphv
      121 aifdtafhgt lppaaytyai dtelaqthgi rrygfhgtsy ryvadraaam lgkdladlkl
      181 ivfhlgngas vcaidggrsi dtsmgmtple glvmgtrsgd idpgalfhlg ragmdlpgld
      241 hllnresgll gmtgtgdmrd vqsaadggda raqaalavyy hrlrhylgay lialagadav
      301 vftagvgenn antrlatvag letfgiemdv aanaaanrse rvvsaaasrv tvlviptnee
      361 lqiaresvea ltr
//
LOCUS       WP_010206749             250 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: hydroxypyruvate isomerase family protein
            [Pseudomonas].
ACCESSION   WP_010206749
VERSION     WP_010206749.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 250)
  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 250)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..250
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27400
     Region          1..250
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mlkfnahlgf qfnelpflqr ieaaaaagfr avefpspyef daslladhla qynlpliqfa
       61 apagvtkgia alqgkeqefr dglreaarya kalncsdvhi msgvttpqde sapayvsnle
      121 yavkyledqg lralievicp qampgyymsd fskaqqvlet ftsvglildl yhaqlltgda
      181 agvlaqfydr tvhvqiadnp grhepgtgtm dfaalfaale qrgyrgwigc eyrpsgttve
      241 slewlkplra
//
LOCUS       WP_010206878             397 aa            linear   BCT 20-JAN-2025
DEFINITION  TerD family protein [Pseudomonas syringae group genomosp. 3].
ACCESSION   WP_010206878
VERSION     WP_010206878.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group genomosp. 3
  ORGANISM  Pseudomonas syringae group genomosp. 3
            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 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Pseudomonas syringae group genomosp. 3"
                     /db_xref="taxon:251701"
     Protein         1..397
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=42130
     Region          3..397
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mtqlvpgana pvaagpltve iiyspladad idvsafllts sgkvrgdqdm cfygqksvng
       61 gavqqteasa gravfsldts rldpviekva ltatiyenka sfgsvsrlal nitggieadi
      121 ptngmketal ilgefylrqg awkfrcvaqg faggleplak nfgvevsapq dqpapapapa
      181 pvpapvpapa akptvnlski tldktrasis lekssagfge mrvnlnwnrr ndtkgggffs
      241 mkkstaidld vgclfelqdg fkgavqalgd sfgslnaepf iklmgddrtg sisdgewlhi
      301 ngahwnkirr ilvyafiydg apnwketdgv vtihapgqpp ievrlneegg rqgmcaiall
      361 endngsvkvt rcvdfhnghs nmdkaygwgm rwaagsk
//
LOCUS       WP_010207915             213 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Pseudomonas].
ACCESSION   WP_010207915
VERSION     WP_010207915.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 213)
  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 213)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 213)
  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 11459477
            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="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22576
     Region          3..208
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 msstddeqla efkdwwqrng kplvtgglla lvvvfgwqaw tkyqanqsqg asivyqqlle
       61 ttltpdgkpd paqvadlagk lknefggsty aqygslfvak vavdtgkldd aaaelkaiad
      121 kptnptlgei arqrlaqvla aqnkadealk lldgdadkaf vatreelkgd llvqlgrtde
      181 anaayqkaka alsdeaavgg lqiklddlak gda
//
LOCUS       WP_010208338             249 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Pseudomonas].
ACCESSION   WP_010208338
VERSION     WP_010208338.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  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   3  (residues 1 to 249)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            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="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28376
     Region          37..242
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mfnalnaeda pqppkvlttp leiastlrml qdshdpliit fhersqrfqs ylvdvnrdsg
       61 tlaldemipr dgerylenge pfriegfheg vrvawesngs lsisekdghr iytgnmpdev
      121 vyhqrrnafr aalklaqlvn ielggeklka pisgklldis atgcklrfeg diserlqlgq
      181 vydrfiaalp fgsmttavel rylhfeekin ttfagvrfhn msglvqrqve rfvyqlqrea
      241 rrfdkdddf
//
LOCUS       WP_010208362             332 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010208362
VERSION     WP_010208362.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 332)
  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 332)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 332)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 332)
  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   5  (residues 1 to 332)
  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   6  (residues 1 to 332)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..332
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37909
     Region          22..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          79..330
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mrertiashy araalggarr agydysgllq qvgitpellt eprariapeq ftrllqmlwl
       61 alddeylgfa dgpskrgtfa mmchalihcr tlekalergl lfyslfpqgp rwqltregem
      121 arlslddsql wdpehflsec llviwhrlgs wligqrirlh qatfsypqpa haseydllfp
      181 caqvfgapns slvfparyln lpllqdertl khflerspad llsrpdegds lssqlrrlls
      241 rdrspwpdle avaqhlhisp qtlrrhlree gtsfqalkde lrrdiaiyhl gradlslqei
      301 aeqlgfseps afhrafkkwt gltpgayraq es
//
LOCUS       WP_010208773             735 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Pseudomonas].
ACCESSION   WP_010208773
VERSION     WP_010208773.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 735)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 735)
  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   3  (residues 1 to 735)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..735
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..735
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=77880
     Region          6..734
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msfgadeeil qdflveagei leqlseqlve lesrpddanl lnaifrgfht vkggagflql
       61 helvecchia envfdilrkg erhvdselmd vilealdavn gmfsevrera pitaatpell
      121 aalaryaepa dlsaapvaea apepvaeaep dvtdsefeql lnslsavkae aeapaaavaa
      181 ptseditdae feslldqlhg kgqfaadavt paavseapaa ptanantdit ddefealldq
      241 lhgkgtfvad alpevaataa apaaasaapa gdglisdhef eslldelhgk gkfsevapaa
      301 tvataapvaa kaaapapapa akpapaaapa paraaaapva dkpaseaett vrvdtarldd
      361 imnmvgelvl vrnrlvrlgl ssgdeamqka vsnldvvtad lqtavmktrm qpikkvfgrf
      421 prlvrdlarq lkkeinlelv geetdldknl vealadplvh lvrnavdhgv etpeereasg
      481 ksrngkvila aeqegdhill sitddgkgmd pailrniavk rgvmdkdaad rltdsecynl
      541 ifapgfstkt eisdvsgrgv gmdvvktkis qlngsiniys tkgqgskivi kvpltlaimp
      601 tlmvmlgnqa fafplvnvne ifhldlsrtn vvdgqevviv rdkalplfyl krwlvasakh
      661 eeqreghvvi lsvgtqrigf vvdqlvgqee vvikplgkml qgtpgmsgat itgdgriali
      721 ldvpsmlkry aarri
//
LOCUS       WP_010209769             820 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [Pseudomonas].
ACCESSION   WP_010209769
VERSION     WP_010209769.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 820)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 820)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 820)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..820
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..820
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89740
     Region          63..109
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          88..820
                     /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 msqparfalc plalatslfc lgapmvhaad spssqeaarp yriaagslvs vlnnfaeqsg
       61 ifiaghnsla agktspglng nytpaaglqr llqgsglqal sqgnngyvld pipantgale
      121 lgattvsgqd lgattedtrs yttgsmasat glplsmretp qsvtvitrqq mddqgtnsia
      181 dtlrrapgvs vqnydserwe fssrglpitn fqydgvnsty dgvydygtts tdmavydhle
      241 iikgsaglls gagdpsatvn lirkkptaaf qasvtqtfgs wdnyrtegdi sgpltesgnv
      301 rgrfvgvyqd rqsyldhyqn tkdiaygile adltpdtllt fgidqqdtrs rgaswtgfpm
      361 yfsdgsrtnf srsfnpaadw srrdfnnqtl fasvqqklan dwslkvsldr krsqhdtlla
      421 sasggnpdpv sgenmymfmg kykgdqvqnt ldvnlsgpfs llgrehelim gfmttrskqd
      481 vpvygsvypp vggsifdwhg eyakpdiprs gqndivqrqt gaylatrlkp tddlsvilgt
      541 rvsnfsgtdn tdfydptkad nrtryhqsgv vtpyagivyd lndtwsvyts ytqiyrpqns
      601 kdadrklldp iegdtyeagi kaafyegrln asfaafrieq dnvaehvsgf etdsvyrpia
      661 gattkgfeae lsgevldgwn vsagytyqht rdanngyvys svlqtttpqq vvrlfstyrl
      721 pgalenvtvg ggvnwqseff gnvfqpnpnd tvnfgqyari tqdsyylvdl maryrfnehl
      781 sttlnvknlf dkkyytglgn fgtgfygepr slqlatkwdf
//
LOCUS       WP_010211546             827 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas sp. R81].
ACCESSION   WP_010211546
VERSION     WP_010211546.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. R81
  ORGANISM  Pseudomonas sp. R81
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 827)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 827)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 827)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..827
                     /organism="Pseudomonas sp. R81"
                     /db_xref="taxon:1144885"
     Protein         1..827
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90376
     Region          66..117
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          95..827
                     /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 mqafpsprsp lkravqaall gvclssalpv avmaetpasd tqardwniaa galataldqf
       61 arqagislsy datsvagkts pglsgrfdsq qaleqllrgq glqaqrqgns twmllpqvad
      121 tgslnlgatl ingerlgatt dgtgsyttga vtigkgehsl retpqsvsvm trqfmddqnv
      181 ttiddvmert pgittyespm ggkyfysrgf kmlgqyqyds vpldmgkdyv qadsfsanma
      241 iydrvevlkg aagmlkgagt asgavnfvrk rpqakpttsl slsagtwdny radvdtggpl
      301 ndsgtlrgra avsqqtrgsy mdiakrqdqa fygaldfdlt pdttlgvgas yedvdatpcw
      361 gglpryadgk sanlsrstcl gqswndwqsr rttffadvth hfnddwklkv aavhsrnlqd
      421 tkyaasegti nygnpaptan syaalmdydh kdfgldayvd gkfeafgleh elilgangsr
      481 gtqddvyaiq nlpkrqsiyq pdhhfpepdd ntfwpnmyrg gtvketatqy gtyatlrlrl
      541 aeplmfivgs rvswyenrrq snnlawgewa vqdartketg evtpfaaliy dldehlsvya
      601 syadifqpqs syatvdgaal kpkigdnyel gikgewfdgr lnssvalfra iekngaesdy
      661 ttmcptsadg ycytdtgkvr aqgveteisg ellerlqlfg gytytqtksl knidsqvegg
      721 ssntyvprhm lrlwgdyqld galakwsvga gvnaqssnyr vqtikleqag yatwsarmay
      781 riddtwtval ngnnlfdksy yntvgtaswg nfygeprnft vslkgnf
//
LOCUS       WP_010211925             110 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Pseudomonas].
ACCESSION   WP_010211925
VERSION     WP_010211925.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (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   2  (residues 1 to 110)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..110
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11648
     Region          36..107
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mqntyicali fafltsisat ttaapsikpe aptpiatqms kaeqsakvnl naadaetlrr
       61 dlfgigaaka raivayresn gpftavdell evkgigkall eknrerlvin
//
LOCUS       WP_010214256             817 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [Pseudomonas].
ACCESSION   WP_010214256
VERSION     WP_010214256.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 817)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 817)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 817)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..817
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89132
     Region          64..108
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          93..817
                     /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 mphhpiqpla ralrrglfvs llatvpmvpt lgyaeesaea qrsynipagn ldqalnrfas
       61 asgillsvda tltegkrsag lqgrygvesg lerllmgsgl mamqsqggws lqavsnggpl
      121 qlgatqisgq qtqesawgpv dgivatrsas gsktdsslve ipqtinvita aeikargaqs
      181 vtqallytpg mtaggfadrv klfdeptsrg fsptplyldg lhlpygggst ggalqiepys
      241 lerievlkgp asvlygqnqp ggivnmvskr psetaihqvv leagtyehkg aaidlsgpld
      301 eqgqflyrlt glandgqdei nyvenkrqfi apsltwrpsd etsvtvfaqy qkdkgvpeaq
      361 glpasgtlwd npngkikrdv figepgvnqy nreqyalgye ishrlndtwt lkqnaryaev
      421 ddrytaplhg yrfvanpvsg vqdqrylqrf gvdwaqnnkv fgvdsiaqae fdtgalshtm
      481 ifgldyyhsn slfhglydrn ppiidlfkpv ygqrlnfgqp yrwdrtitqt glymqdqikl
      541 dkwalvlggr ydwanvvnke pltdtrfask dqaftgragl vylfdngvap fvsytesflp
      601 lagtdanqkp fkpstgnqye vgvkyqppgq ksfvqvsvyq ldqenvlttn pvdttfstqs
      661 gamrsrgvel eakavlsdaw divasasrnd ikytkdndgr egrhpagisp ltasmwvnys
      721 vlgdtplagl gaglgvryar qslgdyyega fsvpsysvyd aslsydlsrs plklkgvkla
      781 mnvqnltnkt yvsqctsnld cyygegrtvv ssltydw
//
LOCUS       WP_010215382             215 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Sphingomonas sp. PAMC 26621].
ACCESSION   WP_010215382
VERSION     WP_010215382.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. PAMC 26621
  ORGANISM  Sphingomonas sp. PAMC 26621
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 215)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Sphingomonas sp. PAMC 26621"
                     /db_xref="taxon:1112213"
     Protein         1..215
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=22874
     Region          48..212
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mlsrrafggs alallgasti vparaqapvf argpapatiq plassrvvrp ellrkalaal
       61 qqhgssiprh driaiadfsl pssqprfymv dmangmattl lvthgsgsdp shtgylqrfs
      121 nsegsnasse gafvtgdyyv gkhgrsqrlm gldetnyral qralvvhsaw yadpdmvkth
      181 gqlgrsqgcf avsegdldqv farlgagrmi ysaki
//
LOCUS       WP_010215671             166 aa            linear   BCT 20-JAN-2025
DEFINITION  division/cell wall cluster transcriptional repressor MraZ
            [Sphingomonas sp. PAMC 26621].
ACCESSION   WP_010215671
VERSION     WP_010215671.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. PAMC 26621
  ORGANISM  Sphingomonas sp. PAMC 26621
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Chen,S., Jancrick,J., Yokota,H., Kim,R. and Kim,S.H.
  TITLE     Crystal structure of a protein associated with cell division from
            Mycoplasma pneumoniae (GI: 13508053): a novel fold with a conserved
            sequence motif
  JOURNAL   Proteins 55 (4), 785-791 (2004)
   PUBMED   15146477
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449500
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Sphingomonas sp. PAMC 26621"
                     /db_xref="taxon:1112213"
     Protein         1..166
                     /product="division/cell wall cluster transcriptional
                     repressor MraZ"
                     /GO_function="GO:0000976 - transcription cis-regulatory
                     region 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=17993
     Region          15..146
                     /region_name="MraZ"
                     /note="DNA-binding transcriptional regulator and inhibitor
                     of RsmH methyltransferase activity [Translation, ribosomal
                     structure and biogenesis]; COG2001"
                     /db_xref="CDD:441604"
ORIGIN      
        1 mdergdyqgd glglvddkgr vaipaslrat laanaprpdg kdggtvivgv hpkhkclray
       61 dpayvrilra qldareaaht sadgepnynf krrgasgepv pfdgsgrfim pgfprdyagi
      121 gehaffwgtl dwieiwdpkt lldaedvdpv mqaacryhck tkgval
//
LOCUS       WP_010216262             131 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Sphingomonas sp. PAMC
            26621].
ACCESSION   WP_010216262
VERSION     WP_010216262.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. PAMC 26621
  ORGANISM  Sphingomonas sp. PAMC 26621
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 131)
  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 131)
  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   3  (residues 1 to 131)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Sphingomonas sp. PAMC 26621"
                     /db_xref="taxon:1112213"
     Protein         1..131
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14834
     Region          16..117
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mirgtteafh rsrasrrklt lpevllwqql rkrgtghkwr rqqpagvysl dfychaarlc
       61 ievdgeahsr gdrpqrdarr dawvqaqgiv tlripavdil rdldavvrgi vahaterapl
      121 hspsrdepge e
//
LOCUS       WP_010217429             333 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas
            syringae group].
ACCESSION   WP_010217429
VERSION     WP_010217429.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 333)
  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   6  (residues 1 to 333)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..333
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36837
     Region          5..191
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <154..320
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mqdaglatap vlrraqlpgd lftrqnvrld sahffklwea ieaeaasina dlpaplqiar
       61 vmssdwfdpe lfaalcsanm adaleriaky vrliapmvir vvptkahttv tmdfldacep
      121 ptvflafklv ffvqlarlat rspvqplqvn wpspstpgpd lqayqayfgi pvthapqasl
      181 vfaaadverp fltenhkmwl ffepglrqrl sdldrtsgmv ervrsalles lpagavsmqq
      241 isrklgvstr tlqrrlqdeg ttfqqtldtl rdslarhylr stamssaqis fllgfedans
      301 farafqswtg stpgkvraem dnsrhpstar sge
//
LOCUS       WP_010218010             648 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Sphingomonas sp. PAMC 26621].
ACCESSION   WP_010218010
VERSION     WP_010218010.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. PAMC 26621
  ORGANISM  Sphingomonas sp. PAMC 26621
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 648)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 648)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 648)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 648)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Sphingomonas sp. PAMC 26621"
                     /db_xref="taxon:1112213"
     Protein         1..648
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=69519
     Region          12..648
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msvatattta anphgttphp alfaltigai gvvfgdigts plyafreale ltgkdgldpg
       61 eilgvlslai wslilvvtvk yviflmrmdn qgeggvlalt alarralgkr slialvlgsa
      121 gaslfygdai itpalsvlsa veglktipgm etviseqvil smtivilial faiqsrgtas
      181 vsrlfgpvcl vwflvlgalg lwhiadepsi lrvisphyga fflldhgvtg lfvlgavflt
      241 vtgaealtad mghfgrlpir igwfalvfpc licnylgqga falnaleaak aagqpfhnqd
      301 wfflmapagl rpwlivlama atviasqavi tgaysltqqa iqlgllprlr irqtsatqag
      361 qiylpsinwl llfgvlvlvv qfrtssamaa aygiavtgtm vvttllayiv vrhrwswsrp
      421 valavilpfl tldliffgan ilrvieggwv plvvaggigl viytwnrgrg ivrafearqs
      481 vpltdlaaal akrpperveg tavfltanpd sapgallhnl khnkvlhekn livsirtadr
      541 psvapeerae irqvdpnfti vvlhygfmes pdvprdlgle atshkktlnp aktsyfigrn
      601 tikpaadqgm plwqdrifmf lqrnasdptd flkippgkvl elgeqvtv
//
LOCUS       WP_010218720             122 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Sphingomonas sp. PAMC 26621].
ACCESSION   WP_010218720
VERSION     WP_010218720.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. PAMC 26621
  ORGANISM  Sphingomonas sp. PAMC 26621
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Sphingomonas sp. PAMC 26621"
                     /db_xref="taxon:1112213"
     Protein         1..122
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=13317
     Region          19..87
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 msqteptqll lqsnksdamq vrsrdgdkig svltlmvnkr tgqtiyavlt iggflgmgka
       61 yypipfsllq fdpvndtyiv tidrrvlegg pswasnaptf dqayadrvsk yydvasedls
      121 va
//
LOCUS       WP_010219030             269 aa            linear   BCT 20-JAN-2025
DEFINITION  3-deoxy-manno-octulosonate cytidylyltransferase [Sphingomonas sp.
            PAMC 26621].
ACCESSION   WP_010219030
VERSION     WP_010219030.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. PAMC 26621
  ORGANISM  Sphingomonas sp. PAMC 26621
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (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   2  (residues 1 to 269)
  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 10787365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Sphingomonas sp. PAMC 26621"
                     /db_xref="taxon:1112213"
     Protein         1..269
                     /product="3-deoxy-manno-octulosonate cytidylyltransferase"
                     /EC_number="2.7.7.38"
                     /GO_function="GO:0008690 - 3-deoxy-manno-octulosonate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0033468 -
                     CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28623
     Region          1..259
                     /region_name="KdsB"
                     /note="CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell
                     wall/membrane/envelope biogenesis]; COG1212"
                     /db_xref="CDD:440825"
ORIGIN      
        1 mtdlivipar fgstrlpgkp lrriagysll ervvrvaraa aeiasdcdvv vatddsriad
       61 haealgcpva mtareissgs gracaaattr svrpdivvnl qgdapflpaa ivaalisaar
      121 dtaaacvtpv vhldwpalda mrahkltsps sgttcvraan glahwfskti lpairdeaal
      181 raegpvspvf rhlglyayri ealeqfeatp pspyerlegl eqlrflemgl tihtilvepp
      241 lhamsgidta vdvalaedli rrfgdphtr
//
LOCUS       WP_010218726             273 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Sphingomonas sp. PAMC
            26621].
ACCESSION   WP_010218726
VERSION     WP_010218726.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. PAMC 26621
  ORGANISM  Sphingomonas sp. PAMC 26621
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Sphingomonas sp. PAMC 26621"
                     /db_xref="taxon:1112213"
     Protein         1..273
                     /product="formate/nitrite transporter family protein"
                     /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=28156
     Region          26..273
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 madttsqddn teagtgtvee lkaanakelh ravreegqee lerpvsalfw sgvaaglavt
       61 asliaegaia shvppgptrp llialgypig fvmvilgrmq lftestvtam iplvttpswd
      121 algrtlrlwa vvllancigt alatgafagl glgdssldag mievsikite haaletffna
      181 vpagfliaiv awslpnareq affvifgivy vvaiggfshs vvgsseafll lwtgkigigg
      241 alsflvpavl gnlfggaglf avlahaqvre ega
//
LOCUS       WP_010219191             238 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Sphingomonas sp. PAMC 26621].
ACCESSION   WP_010219191
VERSION     WP_010219191.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. PAMC 26621
  ORGANISM  Sphingomonas sp. PAMC 26621
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 238)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Sphingomonas sp. PAMC 26621"
                     /db_xref="taxon:1112213"
     Protein         1..238
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=25413
     Region          3..222
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 maitmafqpi vdietgsvfa yealvrgadg qsagevlsgi ehdmiykfdq acrvkaiela
       61 galfipdgda klsinfmpna vyepdacira slaaarrvaf npgrlmfeft enermldtth
      121 vqqiieayqa rgfitaiddf gagyaglgll adlrpdmlkl dmalirgids saarrtivan
      181 vvrmadelgi gciaegieta aelqtlraig lrlcqgylia rpaiealpss aiaasanr
//
LOCUS       WP_010222947             823 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas donghuensis].
ACCESSION   WP_010222947
VERSION     WP_010222947.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas donghuensis
  ORGANISM  Pseudomonas donghuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 823)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 823)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 823)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..823
                     /organism="Pseudomonas donghuensis"
                     /db_xref="taxon:1163398"
     Protein         1..823
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89804
     Region          67..118
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          94..823
                     /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 mtptcprapr plvravhlal fgltlaplpl lallpakama qsastqfqia pgplgtalsl
       61 fatranitls fdarqtqgqq saglqgdysv eeglarllsg tglqaqrqsn ggyvlvpass
      121 gavmelgats inaqglgett egthsyttaa trtatklpls iretpqtitv vtrqqmddqg
      181 aqsisdvlrn tpgvsaqtyd sdrtefssrg lvitnyqydg vntvydgvyg egtahvdmai
      241 ydrvevlkga tglmtgsgdp satvnlirkk ptaqfqsslt gsagswdnyr gevdvsgpin
      301 ssasvrgrfv saqqdkkgyq dhyqqskevy ygileaditp dtlltvgidq qtttprgssw
      361 tgnpvyytdg grtdfsrsfn pgadwsrrdf qnrtyfasle qalandwslk ltvnqlqsdh
      421 dtrlasasgg apdrngdgms ffwgrweghr vqnsadlnls gpftlfgrqh dlvvgldtnh
      481 srqtgatwdt sefamvpgsi fdwdghiavp afpkngkyeq nksqngayla trlhpsddls
      541 vilgtrvstf kysdqydydg lnptfqnnqs gykqhgvvtp yagivydldd tysvyasyts
      601 iyqpqsnkds ngatldpveg dsyetglkaa yfdgklnasl alfrieqdnv aesigtnpat
      661 negiykatsg attqgielev agelqegwnl sagytyarsr dadeqhiygf pmstskpehl
      721 vrlfttyrlp gvpdkvtvgg ginwqsafyg kiynrsvndy tfikqggytl vdlmtryqyn
      781 eqlsftvnan nvfdkryltg lgnydttyyg dprnvmlttr wef
//
LOCUS       WP_010223325             191 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Pseudomonas].
ACCESSION   WP_010223325
VERSION     WP_010223325.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 191)
  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 191)
  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   3  (residues 1 to 191)
  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   4  (residues 1 to 191)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 191)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            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="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21258
     Region          1..191
                     /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"
ORIGIN      
        1 mlrilliddt akkvgrlkaa lvqagfevie esgltidlpa rvetvhpdvv lidtespgrd
       61 vmeqvvlvsr drprpivmft dehdpgvmrq aiqagvsayi vegiqatrlq pildvamarf
      121 esdqalkaql qardqqlaer krielakgll mkmkdcneeq aytlmrrqam skqqkliqva
      181 eqiiamsdll g
//
LOCUS       WP_010223436             520 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein, partial [Pseudomonas
            donghuensis].
ACCESSION   WP_010223436
VERSION     WP_010223436.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas donghuensis
  ORGANISM  Pseudomonas donghuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Pseudomonas donghuensis"
                     /db_xref="taxon:1163398"
     Protein         <1..520
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
     Region          <7..520
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 apadnglgaa llysgvngng yrssnndndi ddvllkthwa vtdsdefwln fhyydakadm
       61 pggltqaqfd ddpyqsdrdy dtfsgrrkdv sfkylrqidd vtqfevqtyy tdsfrgssia
      121 ardqktlssy prsyhtfaie prvsriffag pttqevsvgy rylkeamheq strlalinnv
      181 ptvtptsdgh vfqdrtggte asayyiddki dvgnwtitpg irfehintdw herpvrgtng
      241 vpvqeknrsv tsneplpals vmyhlsdewk lfanyetsfg slqyfqlgqg gsgdqtangl
      301 qaekaktyev gtrynngtwg geltafyidf ddelqyisnd igwtnlgatk hqgieasmhy
      361 dlsgldprlq glsanagfty tratyegeip gfkgrdlpfy srqivnaglr yeinrwtwnl
      421 dayaqskqra pgtgmnadgs fngnyiteps adgqygdipg yvtwaarggy dfgkelsnlk
      481 laagvknifd kqyytrssdn nagiylgepr tfyvqasvgf
//
LOCUS       WP_010224334             343 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010224334
VERSION     WP_010224334.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 343)
  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 343)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 343)
  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   4  (residues 1 to 343)
  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 343)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..343
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38513
     Region          23..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          255..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtekdtismq lvreallqsy apgapsqall grvgidpgql headarvpas ayaqlwrlla
       61 rrchdeffcm dprglrtgsl aflcrssmaq ptlgaalesa laflglmleh lqpvlvrqqs
      121 laeivvgepl deprraftyf tfwmivhgva cwlagrripi laielrcaep pfcddyrvmf
      181 senlqfgrpr trmifaadcl dlplkrtpee lqrflaeapa nilvkyrdpa slarriketl
      241 rqlpagewpe tetqaqqlci sastlrrrla eegttyqglk dsvrkelsia wlaeaqvsfa
      301 eiaerlgfad sssfykafrk wygcnpghyr tligqgethp par
//
LOCUS       WP_010225028             744 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Pseudomonas donghuensis].
ACCESSION   WP_010225028
VERSION     WP_010225028.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas donghuensis
  ORGANISM  Pseudomonas donghuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 744)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 744)
  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   3  (residues 1 to 744)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Pseudomonas donghuensis"
                     /db_xref="taxon:1163398"
     Protein         1..744
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=78557
     Region          6..743
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msfgadeeil qdflveagei leqlseqlve lesrpddadl lnaifrgfht vkggagflql
       61 nelvecchia envfdilrkg arrvdaelmd vvlealdtvn smfgqvrert ditpatpell
      121 aalsrlaepa gedevavpaa epevveapaa eaeaditdte feqlldslna vkaeaeaqva
      181 epgsdeisda efeslldqlh gkgqfaadnl gagapapaaa pagsdasgdi tddefealld
      241 qlhgkgtfav dalpgaaaap apaaapaadg ehisehefea lldelhgkgk fapdavaaaa
      301 paataapaka aakpapaava kaaapapaak aaapapapap arqaapaaek hpasetettv
      361 rvdtarldei mnmvgelvlv rnrlvrlgln sgdeamskav snldvvtadl qtavmktrmq
      421 pikkvfgrfp rlvrdlarql kkeinlelvg eetdldknlv ealadplvhl vrnavdhgve
      481 tpeereasgk srggkvvlsa eqegdhills isddgkgmda dvlraiavkr gvmdkdaadr
      541 lsetecynli fapgfstkte isdvsgrgvg mdvvktkisq lngsiniyst kglgskivik
      601 vpltlaimpt lmvmlgnqaf afplvnvnei fhldlsrtnv vdgqevvivr dkalplfylk
      661 rwlvssaahe eqreghvvil svgtqrigfv vdqlvgqeev vikplgkmlq gtpgmsgati
      721 tgdgrialil dvpsmlkrya arri
//
LOCUS       WP_010225146             365 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas donghuensis].
ACCESSION   WP_010225146
VERSION     WP_010225146.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas donghuensis
  ORGANISM  Pseudomonas donghuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 365)
  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 365)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 365)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 365)
  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   5  (residues 1 to 365)
  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   6  (residues 1 to 365)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Pseudomonas donghuensis"
                     /db_xref="taxon:1163398"
     Protein         1..365
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40431
     Region          35..218
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <174..344
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkavsdaase hrtttgsfir alalskftef asneglrpta mlrlvalpvd veqfpqqila
       61 yqrycglldl caqqaehalf glrfgmhqgl aifgdmlylv gstqsvgeal lelkdnyavf
      121 ngavsmelip areqvclefs tpqqygpgqf qaaelmcava lkllramigd ewqpdhvaft
      181 haplgseldy rsilgsrpif ssaftglvfp rdvlslplna kdttlhqlle thigrmerls
      241 saalpgsikq llrhllpsgr atvekaaswm vlnprslqrq lfaegtsfqq lldevrqesa
      301 qhylkdpais mnrlakllgy adssgfsraf hrwfgltplq wqrktglakq prllrgrkny
      361 ngpae
//
LOCUS       WP_010226065             633 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Pseudomonas].
ACCESSION   WP_010226065
VERSION     WP_010226065.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 633)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 633)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 633)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..633
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68307
     Region          5..633
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msqaatsana hspvktssls lliaaagvvy gdigtsplyt lkevfaghyg vqanhdgvlg
       61 ilslvfwsli wvvtikyvlf vlradnqgeg gimaltalar raaapyprls rvlvllglfg
      121 aalfygdsmi tpaisvlsav eglqlafdgi dhwvvplavv vlvalfliqk hgtarigiif
      181 gpvmvlwfsv lgalgvygiv qrpevllamn pawavnffiv hpgmgvailg avvlaltgae
      241 alyadmghfg rkpiarawil lvlpglvlny fgqgalilgn peavrnpfyl lapdwalvpm
      301 ialatlatii asqavisgaf sltrqaiqlg yvprmfiqht ssqeqgqiyi gtvnwalmvg
      361 vvllvigfes sgalaaaygv avtgtmlitt llssavvlll wkaprwlavp lllgfllvds
      421 lyfaanapki fqggafpvia gtalfilmtt wkrgrkiive rldesalplp lfissiaaqp
      481 phrvrgtavf ltaradavph allhnllhnq vlhervvllt vvsqdrprvp aaqrfevqgf
      541 gegfyrvnln fgfieepdvp aalqlchlee ldfspmvtty flsretvipt krigmarwre
      601 alfafllkna nsnlkyfnlp lnrvielgtq vem
//
LOCUS       WP_010226087             338 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas donghuensis].
ACCESSION   WP_010226087
VERSION     WP_010226087.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas donghuensis
  ORGANISM  Pseudomonas donghuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 338)
  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   5  (residues 1 to 338)
  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   6  (residues 1 to 338)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Pseudomonas donghuensis"
                     /db_xref="taxon:1163398"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37325
     Region          21..202
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          84..334
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtalvraasl tnylevsrhl glnphallah vglsaalldd pnqriavssv vtlleesarv
       61 sgcetfglrm aelrqlsdfg eislllshqr tlrdalqviv qyrhllndal aihieeagkt
      121 viireevvtd lpqrgrqate laigvmlrlc aallgahwhp isanfthaap adlaihrrif
      181 gctlvfgsef ngivcpaadl dtanplanea marlaqryld tlqaggklsl elemrktidl
      241 llpmgratie qvaqtqgmnv rtlqrrleec gvtfsdlvng vrrdlviryl enpsyslgri
      301 admlgysmps sftrwfiaqf gmppaswraq hdrrhsqh
//
LOCUS       WP_010226300             413 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Pseudomonas
            donghuensis].
ACCESSION   WP_010226300
VERSION     WP_010226300.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas donghuensis
  ORGANISM  Pseudomonas donghuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 413)
  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 413)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Pseudomonas donghuensis"
                     /db_xref="taxon:1163398"
     Protein         1..413
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46034
     Region          2..404
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mpttqslsla qarrlalsaq gfntrqtsas mgaaqlqrmi erlgvvqids vnalvrshyl
       61 plfsrlgsyp qalldqlawg rnrqrklfey wgheasllpl slypllrwrm drarqgqgif
      121 qqlarfgreq qatiarvlaa vteqgalgag slstrqerag pwwdwsaekh alewlfaagl
      181 vnvagrrgfe rlydlpervl paalleqppm neadaqrgll lhaagalgva tekdlrdyfr
      241 lapgdsrarl aelveegalq acavqgwtqa ayclgsprvp rkvsssalls pfdslvwere
      301 rterlfdfry rleiytpahk rvygyyvlpf lhneriaarv dlraerandc lavhavheeq
      361 agldeagmqa laeslqrmaa wlglaevqln cprasaarlr ealarsdlsd vpa
//
LOCUS       WP_010226964             174 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Pseudomonas].
ACCESSION   WP_010226964
VERSION     WP_010226964.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 174)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..174
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=19169
     Region          9..162
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cl49639"
                     /db_xref="CDD:483979"
     Site            order(104,118,121,134..137,139)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 masldflhis ladqclygfa qgqlrlrldv starngagel kgsgctprgr hqvrakigag
       61 lpqgavlrgr rwtgeiwspa lhehfpgrdw iltrilwlsg cepgvnrlgp vdtfhryiyl
      121 hgtpdsepmg vplshgcvrl rnadllnlfd qvpvhcpvqi deaacpqwah irvn
//
LOCUS       WP_010231405             341 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Pseudonocardia].
ACCESSION   WP_010231405
VERSION     WP_010231405.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudonocardia
  ORGANISM  unclassified Pseudonocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 341)
  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 341)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="unclassified Pseudonocardia"
                     /db_xref="taxon:2619320"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36606
     Region          23..209
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          250..332
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mgtgsltrar alrglpglvd elggdgaaml drfhipaeav dgadpdalvp travalvlet
       61 aaaeldcsdl glrlaerqgp eilgplavav qnsptlgaal dcaskylyvh spalriaavp
      121 dpehvagvtg veygsterlp phvadlgvgv lhriigllsg ggyglrsvhl phpalaserr
      181 yreffgaevr fdrptavlrv padlprrpld gdqavrdiai eylethfdrp drrvtdrvrt
      241 avdrslgtgp vrigavarll rvhprtlqrh laaedttfeq ivddarrdta erlvtrsdlp
      301 ftqiaamvgl aeqsaltras rrwfgvpprt lrkagpvlpg r
//
LOCUS       WP_010231762             113 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Gillisia marina].
ACCESSION   WP_010231762
VERSION     WP_010231762.1
KEYWORDS    RefSeq.
SOURCE      Gillisia marina
  ORGANISM  Gillisia marina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Gillisia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Gillisia marina"
                     /db_xref="taxon:1167637"
     Protein         1..113
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12636
     Region          4..105
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(7..8,26..27,35,38,40..41,43,46..47,49,57,62,69)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(26,57..58,60,86)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 malepnffer vyevvklips grvtsygaia ryigaaksar mvgwamnkah dleevpaqrv
       61 vnrlglltgk hhfggtnamq qllesegvvv rdnqiqnfek vfwdpnkelv kpr
//
LOCUS       WP_010227707             333 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Pseudonocardia].
ACCESSION   WP_010227707
VERSION     WP_010227707.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudonocardia
  ORGANISM  unclassified Pseudonocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 333)
  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   6  (residues 1 to 333)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="unclassified Pseudonocardia"
                     /db_xref="taxon:2619320"
     Protein         1..333
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37037
     Region          23..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          103..331
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 masgslarya alnnfielsr slgldpagmi revgldpgsl smqdrwipav avaqllelaa
       61 aasgredfgl rlaelrrfsn lgplslvvre epdvrgalal liryehmyne alharvhehn
      121 giatlgield vhetgtrqsv elavgvlhql mqgflgatwr pltvafthge phrktihhrv
      181 lgpsvkfrqs ynglsvyaad ldapnamsdp llreytrhfl dsletskqtt tssrvrelve
      241 mllptgqcsv eqvarslgvd rrtvhrklkq egetfsgvld atrrglaehm vlnrnrpltd
      301 vaqmlafssh snftrwfrgq fgcsptewrr rst
//
LOCUS       WP_010232401             269 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Gillisia marina].
ACCESSION   WP_010232401
VERSION     WP_010232401.1
KEYWORDS    RefSeq.
SOURCE      Gillisia marina
  ORGANISM  Gillisia marina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Gillisia.
REFERENCE   1  (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   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Gillisia marina"
                     /db_xref="taxon:1167637"
     Protein         1..269
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31198
     Region          11..112
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          <182..255
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mdkiyshkaa sstlsaiiks fwliedeist kkiekiipdg ypelifhygd lykidingfw
       61 klqgrnliag qiknhfflen tgkrkvfgik fqpwaltnlf dlnmgyltdk vvavpdevlk
      121 sikpikelsv sqlsfqekve kiedwlaafi aqqrftnhsg qkaiemiids qgkvnlktih
      181 nelgisertl eryfkkhvgl spkyfsriir fsnifkivqg dvwdwadiff kagfydqshf
      241 iknfkeftge dpskygfsee nlanfflkk
//
LOCUS       WP_010233251             128 aa            linear   BCT 20-JAN-2025
DEFINITION  zinc ribbon domain-containing protein [Clostridium arbusti].
ACCESSION   WP_010233251
VERSION     WP_010233251.1
KEYWORDS    RefSeq.
SOURCE      Clostridium arbusti
  ORGANISM  Clostridium arbusti
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 128)
  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 12181465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Clostridium arbusti"
                     /db_xref="taxon:1137848"
     Protein         1..128
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14766
     Region          22..123
                     /region_name="zinc_ribbon_15"
                     /note="zinc-ribbon family; pfam17032"
                     /db_xref="CDD:465334"
ORIGIN      
        1 mffigifgag krheeiriin nmvckscerm tayklikmyn yfqiffipif kwreeyylis
       61 kccgsifgls keqgedlerg edsvlsnlni tilednrsqc gklicdncgk evdenfdfcp
      121 hcgtklsd
//
LOCUS       WP_010233226             280 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Clostridium].
ACCESSION   WP_010233226
VERSION     WP_010233226.1
KEYWORDS    RefSeq.
SOURCE      Clostridium
  ORGANISM  Clostridium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Clostridium"
                     /db_xref="taxon:1485"
     Protein         1..280
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31431
     Region          1..247
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mkadlhnhsf lsdgvlsvqd iigyskkvgl nciaitdhdt magvlpaytf gekigmsiip
       61 gveistvnye tnrsvhmlcy fpkdifklqg flnkilinre nakrqmakml msecpitmeh
      121 ieryscksqs myethimqav adlgytnvvi gklykellsk kgkyyvqity psvyealemi
      181 kevggiavma hpgqfdsiel leelarkglv qgaeynhprn seevkkqikd iaerynlimt
      241 ggtdfhgyys nsphpigsft cpegevekli tlghkayenk
//
LOCUS       WP_010233701             186 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Clostridium arbusti].
ACCESSION   WP_010233701
VERSION     WP_010233701.1
KEYWORDS    RefSeq.
SOURCE      Clostridium arbusti
  ORGANISM  Clostridium arbusti
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Clostridium arbusti"
                     /db_xref="taxon:1137848"
     Protein         1..186
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20408
     Region          4..178
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 msealrnlle rrsvrafkse qikdeelqqi leagkyapsa anqqswhftv iqnkevlqki
       61 ndvtkavfgk sgnkiyeert kakdfsafyh aptyiivsad ekaiapvads alalgnlfla
      121 aealgigsvw ihavnflytt eegkalfkel gipdgyipyg sgafgynage kpkaaprrqe
      181 tvniik
//
LOCUS       WP_010234582             307 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Clostridium
            arbusti].
ACCESSION   WP_010234582
VERSION     WP_010234582.1
KEYWORDS    RefSeq.
SOURCE      Clostridium arbusti
  ORGANISM  Clostridium arbusti
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 307)
  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   2  (residues 1 to 307)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Clostridium arbusti"
                     /db_xref="taxon:1137848"
     Protein         1..307
                     /product="aminoglycoside 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=36234
     Region          16..243
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mdynfnditn snmwtkirki eygwssdeky yiednkniky llrisssdty eqkkkefqvi
       61 kkfnaldfqm sraiefgffn ehknvymlls wvdgnsleer lnsipkieqy nlgiyagkvl
      121 rkihsiqvdv qdvpyvnkis kkllqlqkye nsavripnde naiafvrsni eiicktppvy
      181 ehgdfhvgnl iyttnkkigv idfnrwecgd ryeefykiqs fdvehsvafs vgqihgyfdg
      241 tpptefwriq avyvahasly sikwaekfgn keiigmtkrc leafdhydnf nlivpkwysq
      301 nkdkyil
//
LOCUS       WP_010235849             466 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: amidohydrolase family protein [Citromicrobium].
ACCESSION   WP_010235849
VERSION     WP_010235849.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium
  ORGANISM  Citromicrobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 466)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Citromicrobium"
                     /db_xref="taxon:72173"
     Protein         1..466
                     /product="amidohydrolase family protein"
                     /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=49330
     Region          30..451
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mlrclaflam ialataplaa sppapaaage tlvienvtvi pmtkeggvlp nrtvvieggr
       61 ivsiadaada gdppdanrid gtgkwlvpgf sdmhvhigne rmlrllarsp vpedgaanmq
      121 daftpyivng vlqvfdlaam petvgqriai esgrvlgphv amatmidsnd pvlpfgiths
      181 agspaqgrqa vkdaaadgfd fvkvyghldl ptftaiveea rarnirvvgh ipqrgegite
      241 affqpgydlv vhaeefaqqt rspdvavips yvemarkngt alvttltand riaqiardpg
      301 slasredlyv lppqfydlsv nsnpyaaqss egyiayaqsi vdfngslvra faqagipvlt
      361 gtdagipgva pgfslhdefe alaqagldnr lilegstrla aeflgvegdr gtvavgkrad
      421 lvlldadple diantreiaa virdgryldr edldalladl iarnrk
//
LOCUS       WP_010238180             491 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Clostridium arbusti].
ACCESSION   WP_010238180
VERSION     WP_010238180.1
KEYWORDS    RefSeq.
SOURCE      Clostridium arbusti
  ORGANISM  Clostridium arbusti
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Clostridium arbusti"
                     /db_xref="taxon:1137848"
     Protein         1..491
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54356
     Region          4..491
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mknffkinek dnvvvaltdl nkadiieidn kkitiedsik rghkiavdni kkgdniikyg
       61 fpighateni kvgqlvhshn lktnldgikd ydynkkdlki dfehrnltfn gyvrengkvg
      121 irneiwivpt vgcvngiada iarkfqeetn vevqvfkhny gcsqlgddhf ntmtilgdiv
      181 khpnaggilv lglgcenntm gdfikslevy dknrirflis qevedeveeg ikllkevyen
      241 akkdkrvavp lselniglkc ggsdgfsgit anpllgkfsd fltsqggttv ltevpemfga
      301 etllmnrakd kevfnktvnl indfkkyfmg ydqpvyenps pgnkaggitt ledkslgctq
      361 ksgssqvvdv lkygqtlnkk glnllsapgn dlvastalas agchmvlftt grgtpfgtfv
      421 ptikvstnsq iyekkkrwid fnagdlikdk tmdelmeefi nyiiniange lanneknhir
      481 eiaifkngvt l
//
LOCUS       WP_010238746             399 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Clostridium].
ACCESSION   WP_010238746
VERSION     WP_010238746.1
KEYWORDS    RefSeq.
SOURCE      Clostridium
  ORGANISM  Clostridium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Clostridium"
                     /db_xref="taxon:1485"
     Protein         1..399
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43476
     Region          1..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkvlvincgs sslkyqlidm kdetvlakgl veriaiegsi ltqkvngeky iieqpmndhk
       61 eaiklvldal vdtthgvikd mseisavghr vvhggekyad svlidddvme siqecvklap
      121 lhntpniigi nackdlmpnt pmvavfdtaf hqtlpdyaym yplpydlytk ygirkygfhg
      181 tshkyvskat aeflkkdlss lkiitchlgn gaslaavkgg ksvdtsmgft plagvamgtr
      241 sgdidpaivt flikelklts devnnllnkk sgiygiygks sdmrdikkag lqekdekatl
      301 alnvfhykvk qfigsyaasm ngvdavvftg gigenspenr egicenmdfl gikidkkkne
      361 qtigndadis aadsktkvlv iptneelmia rdtrdivtk
//
LOCUS       WP_010239179             288 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Clostridium arbusti].
ACCESSION   WP_010239179
VERSION     WP_010239179.1
KEYWORDS    RefSeq.
SOURCE      Clostridium arbusti
  ORGANISM  Clostridium arbusti
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 288)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Clostridium arbusti"
                     /db_xref="taxon:1137848"
     Protein         1..288
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=32860
     Region          151..287
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(226..227,230,260..263,265)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mrlkclgrfi lsclictimt sifiiipsff fasvpnqdka ietsvkvide naikdtlkkd
       61 mqnklkdsia vfslndcfkk tyyishdgvk mykkigdens lircldnnde ivaykeengy
      121 iycennsgdk gwirksdndl kpmifnvtry vidvnltkqn iniyengkni rknimcstgi
      181 lgnsdtetps gifkiktkls ypngftvndg dgtketvmyp vqffsnylih svpinqiqhn
      241 nrieqeenkv eksklgnpas hgcirvamdd akwiynntsk dtevyihy
//
LOCUS       WP_010241846             249 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Fannyhessea vaginae].
ACCESSION   WP_010241846
VERSION     WP_010241846.1
KEYWORDS    RefSeq.
SOURCE      Fannyhessea vaginae
  ORGANISM  Fannyhessea vaginae
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Coriobacteriales; Atopobiaceae; Fannyhessea.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Fannyhessea vaginae"
                     /db_xref="taxon:82135"
     Protein         1..249
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=27477
     Region          31..172
                     /region_name="YrrD"
                     /note="Uncharacterized conserved protein YrrD, contains
                     PRC-barrel domain [Function unknown]; COG3881"
                     /db_xref="CDD:443089"
ORIGIN      
        1 msierisqcv nkkayiirtk tsngvtvehk kplgkvhftl ftpagdrlvg flikrpdmlw
       61 mfkrkdifvp ldvchlqgse lhihasmrql gksalsrlal dwdsciiwqg mdvvsqdkqm
      121 ighvsdvaln assgavlafi iddgkiasrl vghikipfss yescekgrvl vntqgistel
      181 skglaadagk kyaeakyagk klaqrvnnki devsssqeyt naaksvgrqi kksrsmfgdf
      241 ldeykkask
//
LOCUS       WP_010239408             393 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Citromicrobium
            bathyomarinum].
ACCESSION   WP_010239408
VERSION     WP_010239408.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium bathyomarinum
  ORGANISM  Citromicrobium bathyomarinum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 393)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Citromicrobium bathyomarinum"
                     /db_xref="taxon:72174"
     Protein         1..393
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43235
     Region          6..387
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mtdeprnqfa tfaygrryle radriavdpv alplheagts rtfrteegfa vfggirdaap
       61 dgwgqylmyk amgdrlpsei dlilasgehr vgalafgpts aqperitpwg ggpapgeeft
      121 laelaeaaer aqhvdelden lrallaagss lggarpkaat kigdqpwiak fqkrgdsfpe
      181 crvelatmrl asecgldvpp ldfrcvldrd iylierfdri phgnwlerrp fasgltmlga
      241 hesevssfsy adlagairqf gtevrqdlhe lfrrmllnil vtndddhlrn hgflfdgegw
      301 rlsplydvvp kpqlglerrl vlgvgpegrn atienalaga avfdlshdda kaiaenmsrt
      361 vatrweqlft eagisaadrk rfatcfrlaa pas
//
LOCUS       WP_010242128             193 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Peptoniphilus].
ACCESSION   WP_010242128
VERSION     WP_010242128.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus
  ORGANISM  Peptoniphilus
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Peptoniphilus"
                     /db_xref="taxon:162289"
     Protein         1..193
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22248
     Region          3..155
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mevknllnwr rsyrkfdesk kiskkdkdei ldsikfasca nnrqtlrfis veseekvlei
       61 fentkwaasl sneigrpkig erpvyfiavl tnedkklkfn gideglvisn ltliaaekgi
      121 gsciigsvnd nkmrkilnye nnfscevvia fgypkiksti keintkedqs yyldedknyi
      181 vpkykvediv rrm
//
LOCUS       WP_010242731             649 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-oxoacyl-ACP synthase III family protein
            [unclassified Pseudonocardia].
ACCESSION   WP_010242731
VERSION     WP_010242731.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudonocardia
  ORGANISM  unclassified Pseudonocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 649)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 649)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 649)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 649)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 649)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="unclassified Pseudonocardia"
                     /db_xref="taxon:2619320"
     Protein         1..649
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=70932
     Region          293..612
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mkpfvvnshd rlvfpanflg eldfsviddl eqftaivgrd feakaptgtd ilervttgay
       61 rsrfallrdm sqnlfwvnry tltmfekrpt rwrdlprhrg dvflptltpw rdgdkkvrav
      121 qeafavlpst wddgveekif dllfdvygnr rhhatelpav kptveqfltt pgartfvvph
      181 hdpdypvfsw seildahaer pelealtrwa mvlhnqypwd raatelrtad eigdddhvia
      241 fhprnrdvaa fldratgarp arrgriatqa epveperplp pvrvreafav qpkvealavv
      301 rgehvcsndd vvrnsafsws pmsaeeistk tgidqrryte ldiedlawaa avralehsgr
      361 drseigavlv atctserlip slstwlsgql gllqthcsad ivaacaglpy glaeavrqlq
      421 evrrpvllvc vekfsdkign vrtsrmifgd gaaamvvapa aegergdvdl lqtyasgpvs
      481 qvnsiiwpnp efdnditvyg pevkalvary lsqmigelte qagpdgtgtm ldavdlivph
      541 qanktmilql aakaglsaeq lyfnigsmgn vsaasipial hdactdgavt grtrvfapgf
      601 gagavggyav levdpavmap evvldpaaap eaaavaapts ddvriafge
//
LOCUS       WP_010242752             458 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Peptoniphilus rhinitidis].
ACCESSION   WP_010242752
VERSION     WP_010242752.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus rhinitidis
  ORGANISM  Peptoniphilus rhinitidis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 458)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Peptoniphilus rhinitidis"
                     /db_xref="taxon:1175452"
     Protein         1..458
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=52570
     Region          209..311
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          332..451
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(402..403,406,424..427,429)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkktfkifft iliiliifiy aaglyffkdr fmprtyvngr dfgltkisef eknyndlskn
       61 fvleviskdk ennekitase inyednigsg fvdqtpfywp vaslvpknye iehemhyddn
      121 alsnrindlk vvknekvhsa dakviyngrd feieeevygd fvkrnelrns ilnhfadkdd
      181 klnledenly iepkitsdsd yiknllnsyk evykkkiiyd fddrkeevtg qniiamyskt
      241 ddgnlvvdee kvakfvgnls skydtfktsr vfnatgignv kvdggiygwl tdrvktkeel
      301 iaaldkdsev ilkpvyrqda isrsaddigk tyievdlarq klwyynngvm eletnivsgn
      361 pnrgngtptg tdrvwsrerd ryltgetyrs kvnywvpinw sgiglhdatw rsnfggniyl
      421 sngshgcinv ppsvmgnlyg ktfngmpviv ydsatqki
//
LOCUS       WP_010243855             216 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [unclassified
            Pseudonocardia].
ACCESSION   WP_010243855
VERSION     WP_010243855.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudonocardia
  ORGANISM  unclassified Pseudonocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="unclassified Pseudonocardia"
                     /db_xref="taxon:2619320"
     Protein         1..216
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23700
     Region          10..211
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mtdvldlgpd elltttrsvr krldldrpvp mdvvreslev alqapsgsnq qgwhwlvitd
       61 pekrkavgey yrqafmayrn ssayptnrts gdadrdatqn rvadsalyla ermsdvpvlv
      121 igalkasadl pasnqaglwg sllpaawslq ialrarglgs awttlhlqye keisellgvp
      181 advrqgvllp vayytgdtfk pakrqpldtv lhvdgw
//
LOCUS       WP_010244384              79 aa            linear   BCT 20-JAN-2025
DEFINITION  zinc ribbon domain-containing protein [Acetivibrio cellulolyticus].
ACCESSION   WP_010244384
VERSION     WP_010244384.1
KEYWORDS    RefSeq.
SOURCE      Acetivibrio cellulolyticus
  ORGANISM  Acetivibrio cellulolyticus
            Bacteria; Bacillati; Bacillota; Clostridia; Acetivibrionales;
            Acetivibrionaceae; Acetivibrio.
REFERENCE   1  (residues 1 to 79)
  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 10577258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Acetivibrio cellulolyticus"
                     /db_xref="taxon:35830"
     Protein         1..79
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=8668
     Region          3..77
                     /region_name="Zn_ribbon_2"
                     /note="Putative zinc ribbon domain; pfam12674"
                     /db_xref="CDD:463667"
ORIGIN      
        1 mktciacgmp mktkedfamg deskeyckyc tkpdgtmqny deklkgmtgf iiktqgldek
       61 aaqkaaigmm aklpawkdc
//
LOCUS       WP_010245096             195 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Peptoniphilus rhinitidis].
ACCESSION   WP_010245096
VERSION     WP_010245096.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus rhinitidis
  ORGANISM  Peptoniphilus rhinitidis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Peptoniphilus rhinitidis"
                     /db_xref="taxon:1175452"
     Protein         1..195
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=22971
     Region          8..195
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mnilkeyiqe nlvitnkeae elgytrhnls eltkigqler lrpglyqlkg kviddfvlis
       61 snsnriifsh qtalylhdls drtpnvfhis vpqgynashi kkryedlqvh yvkkdlyelg
      121 kaeikspqgn lipvydidrt icdiiverek idkqifteal kryfkstnkn lrrlikysrl
      181 fkieneirky mevll
//
LOCUS       WP_010245814             416 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Pantoea].
ACCESSION   WP_010245814
VERSION     WP_010245814.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 416)
  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 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   3  (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   4  (residues 1 to 416)
  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 416)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..416
                     /product="CmpA/NrtA family 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=45216
     Region          39..290
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 msktpfsltr rqalisgaal gaawivpglr navwaagsda pekaqvrvgf ipltdcapvv
       61 masvkgfdkk ygltlqvske aswaavrdkl tsgeldaahv lygmiyalql gvagpqhdma
      121 nlmtlnhngq aitlsnqlka sgvtdaaslk kaidgsakgs ftfahtfpts thamwlyywl
      181 anagihpfdd vrtvvvpppq mvmnmkignm sgfcvgepwn qraisdnigf taatsqqiwp
      241 ehpekvlgtr aewvkenpnt araltaavle aarwidasdd nrretaqvla grawintkve
      301 tlqgrmlgqy qnglgqswqd ahpmrffdng nvsfpwlsdg mwfltqmkrw gllasdpdyl
      361 avarqinrid iykqaasavg qvalpasemr sstfidgkvw dgsdpaayaa sfaikr
//
LOCUS       WP_010246463             110 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Acetivibrio cellulolyticus].
ACCESSION   WP_010246463
VERSION     WP_010246463.1
KEYWORDS    RefSeq.
SOURCE      Acetivibrio cellulolyticus
  ORGANISM  Acetivibrio cellulolyticus
            Bacteria; Bacillati; Bacillota; Clostridia; Acetivibrionales;
            Acetivibrionaceae; Acetivibrio.
REFERENCE   1  (residues 1 to 110)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Acetivibrio cellulolyticus"
                     /db_xref="taxon:35830"
     Protein         1..110
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=12184
     Region          3..110
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(66..67,70,83..86,88)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 myrieidtqk rvltlfndnn lvkrypvavg kpstptppgn wtiikkglwg aqfgghfmql
       61 svpwgiygih gtdkpwsisq avshgcvrmy spdagelynm vpigtpvhiy
//
LOCUS       WP_010246728             806 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Acetivibrio cellulolyticus].
ACCESSION   WP_010246728
VERSION     WP_010246728.1
KEYWORDS    RefSeq.
SOURCE      Acetivibrio cellulolyticus
  ORGANISM  Acetivibrio cellulolyticus
            Bacteria; Bacillati; Bacillota; Clostridia; Acetivibrionales;
            Acetivibrionaceae; Acetivibrio.
REFERENCE   1  (residues 1 to 806)
  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 806)
  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 806)
  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   4  (residues 1 to 806)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..806
                     /organism="Acetivibrio cellulolyticus"
                     /db_xref="taxon:35830"
     Protein         1..806
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=90867
     Region          1..805
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mprikglpyk mlrkecdpns fkfndtseld alediigqer atkalqfglk iktrgynifm
       61 sgstgtgkts yaqnyvkkia qkaktpddwc yvynfnnpnq psalnlpagl gkifqgdmed
      121 fvkvlqleis rafdsedyer ektsiakeyq trrndllerl nedaekqgfk vkttnagiyf
      181 lpvvegktis eeeygdldek lkheiteksn ivqletidii rkikaiekea eekvsewenk
      241 ialfavgmhi ndlkekyqdy kkvtdyleni qedilknldd freedygddq qqllipwirs
      301 segsptdkyr vnllvdnskl kgepvivdfn ptffnllgkl eyenefgtmt tdytmikggl
      361 fhqanggyli lqakdvlsnv qswellkrvl rtkqiaienm keqmglvavs tlkpepipve
      421 ikvilvgsey lyqalyefde dfkklfkika dfdaemdrnk estkklarfi nsfcnregtl
      481 hydktgvakv veyssrlved qtklstkfnd iveilsesca wadiegcslv gaehvkkaia
      541 ekifrsnkyd kkilesledg tiildtegev vgqingltil dmgdysfgkp sritantfmg
      601 ergivniere vemsgtshsk gvfilsgyig qkfaqeiplt ltaslcfeql yggvdgdsas
      661 saelyavlss ladvpikqyi avtgsvnqkg eiqpiggaie kiegffelck lrglngkhgv
      721 iipyqniknl vlndevieav kegmfsiyav ktidegieil tgikagekkk dgtypagtin
      781 ylvyeklkky aqtaagfykd ekksgk
//
LOCUS       WP_010246921             572 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Peptoniphilus
            rhinitidis].
ACCESSION   WP_010246921
VERSION     WP_010246921.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus rhinitidis
  ORGANISM  Peptoniphilus rhinitidis
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Peptoniphilus rhinitidis"
                     /db_xref="taxon:1175452"
     Protein         1..572
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=65707
     Region          2..550
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mfnrklfnei kdekvlilkl lvikifqllt qiamifiigk flenlykinl eiskfvmamf
       61 fimainiilt kyyskisykv syrvknnlre kllkkvfsfk meysskvtis evinlgvegi
      121 eqlnlfysel lpqllfalia plilflilsy lnfkialiml lliplipiai ilvqkiakkv
      181 vktywksytn lsdvfidfly gittlevfsa deeynkllne kaedfrvktm kllsvqlnni
      241 tvldlisylg salgitlsif yfskgdlnif safsfvllsq efflplrklg slfhvamngi
      301 ssanslfdil eikdskdfkk iiedenidin ikdlnfsygd keilinlnme fkygnitaiv
      361 gksgcgksti akliagflkd yngkiyynkl ievskdslne nimlvdntpy ffneslkynl
      421 kcanknande mlidalkkvg lynyfankdg ldskvessgn nlsggqkqrl qiarvilrkp
      481 kilildesis nidkeseeli lgliqelkek mtiiiithrl ntvvnadyiy yienknvaee
      541 gtfesilkke kfskiynhqk dlemwglnec nn
//
LOCUS       WP_010248454             244 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Peptoniphilus].
ACCESSION   WP_010248454
VERSION     WP_010248454.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus
  ORGANISM  Peptoniphilus
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae.
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   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   4  (residues 1 to 244)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Peptoniphilus"
                     /db_xref="taxon:162289"
     Protein         1..244
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=27707
     Region          1..>237
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mityknvsms ypdsgkvldn lnfdikdgef fvivgpsgsg ktttlklinr lieqtegdii
       61 fkdkkikdyp lrelrlrigy vlqeialfpn ltvaeniaii pemkkmdkka inkktkrlle
      121 qvgldpkkyi nrlpkdlsgg erqrigilra iaadpeillm depfsaldpi skaqlqdlik
      181 klhddykitt vfvthdmnea lkladricvm regkiiqide pkeimdnpen kfvseffnne
      241 sgvi
//
LOCUS       WP_010248820             262 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Acetivibrio cellulolyticus].
ACCESSION   WP_010248820
VERSION     WP_010248820.1
KEYWORDS    RefSeq.
SOURCE      Acetivibrio cellulolyticus
  ORGANISM  Acetivibrio cellulolyticus
            Bacteria; Bacillati; Bacillota; Clostridia; Acetivibrionales;
            Acetivibrionaceae; Acetivibrio.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Acetivibrio cellulolyticus"
                     /db_xref="taxon:35830"
     Protein         1..262
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29151
     Region          1..244
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mradlhihst vsdgsktihe iidmatnngl dfiaitdhdt mahakllpks paikviagie
       61 isaidkktgt kahvlgykin nadyvenltl pllkkrhens lrqieilqkd gieidinkln
      121 kedgkyiykq himeylvetk qviemfgsfy ktvfksggic dfdieyidvy davnviksag
      181 glavlahpgq qknfylidki pfdgiefnhl ansegdkkii reyaskynlf ltggsdyhgk
      241 yeavpvdigd fiseesgvna lc
//
LOCUS       WP_010249021             302 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pantoea].
ACCESSION   WP_010249021
VERSION     WP_010249021.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 302)
  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 302)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 302)
  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   4  (residues 1 to 302)
  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 302)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..302
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33605
     Region          27..179
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          207..288
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mahdalchrl aqqvvtlmth ghdrlcpven vsliyanqyr prtpmmyqpg ivilfqgskt
       61 gylgstvfqy daskylmltv plpvecetwa spevpiaglc lnvdtaslqd llieigdddq
      121 fqpqpqtsgi hsawltepml caaerlldvm tqprdarvlg phivreiiyy vltgpiggal
      181 lslvsrqtqf sliaralrri enhyaenlsv dalaaevnms vsafhhnfka vtqtsplqyl
      241 kryrlhqarl lmlhdglkas aaavrvgyes psqfsrefkr yfgvtpgeev nrvrqtvadp
      301 sa
//
LOCUS       WP_010249081             363 aa            linear   BCT 20-JAN-2025
DEFINITION  GerAB/ArcD/ProY family transporter [Acetivibrio cellulolyticus].
ACCESSION   WP_010249081
VERSION     WP_010249081.1
KEYWORDS    RefSeq.
SOURCE      Acetivibrio cellulolyticus
  ORGANISM  Acetivibrio cellulolyticus
            Bacteria; Bacillati; Bacillota; Clostridia; Acetivibrionales;
            Acetivibrionaceae; Acetivibrio.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Acetivibrio cellulolyticus"
                     /db_xref="taxon:35830"
     Protein         1..363
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=40364
     Region          5..362
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 mlaskekisi rqamiillcv tysptmrfva fsgveiakqa awispiisfv ivipivlmlh
       61 siykkhenqs ftevmedilg saagkivtvf yavfltflfs ttsyinadkl vatvypnqni
      121 mifiaivlft aafitrkggi vviariseii fmllvsiflf ilvlalkdin isrltpisyl
      181 diypafkani eilgvwsylp liflfsnyin nkekikkact ltllsltllt ilmfvvaigl
      241 lgasilelsp vpyvtavkqi svfqvlerle aaeiglwila dfilsaillf talnvfkslf
      301 klsdirplag iysviiflla lmtgrnvfev qflgyniisl istlfgfiip givfsvgkvr
      361 rki
//
LOCUS       WP_010249125             154 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Myroides injenensis].
ACCESSION   WP_010249125
VERSION     WP_010249125.1
KEYWORDS    RefSeq.
SOURCE      Myroides injenensis
  ORGANISM  Myroides injenensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Myroides.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 154)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Myroides injenensis"
                     /db_xref="taxon:1183151"
     Protein         1..154
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17160
     Region          2..152
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mesdynailk raklilsrsd ldnddklkev cellydsivy ydwvgfyfak eetrtlhlgp
       61 yvgeatehtv ipfgkgicgq vavsnetfvv ddvlaqdnyi acsitvksei vvplfvngvn
      121 igqididsht knaftnedkl flealnievs klya
//
LOCUS       WP_010249136             696 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Acetivibrio cellulolyticus].
ACCESSION   WP_010249136
VERSION     WP_010249136.1
KEYWORDS    RefSeq.
SOURCE      Acetivibrio cellulolyticus
  ORGANISM  Acetivibrio cellulolyticus
            Bacteria; Bacillati; Bacillota; Clostridia; Acetivibrionales;
            Acetivibrionaceae; Acetivibrio.
REFERENCE   1  (residues 1 to 696)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 696)
  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   3  (residues 1 to 696)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Acetivibrio cellulolyticus"
                     /db_xref="taxon:35830"
     Protein         1..696
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=77297
     Region          1..695
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdmsqyleif idetkehlqg lnqsllqleq npqdistlne ifrvahtlkg magtmgfnkm
       61 aklthdmenv lhalrsneik vtpnlvdilf kcldalenyt enivntggeg nneyndiise
      121 lgnavnkkav eptaqkaatv hktenteqea einthataqf klnqyeqnva ykakemgmnv
      181 lkitvvlnkg cvlksarsfi ifqtlerhse iikseprved iedekfdfef tvvcvtkeep
      241 dvfvkdinsi aeideviint lgstdfqpsp mqeecsvsnq tdscesntns eadcsaetkq
      301 dtnaqgasah ktktgktvrv didrldvlmn lvseliiikt rleglegger sqsyseavey
      361 lerittnlhd avmkvrmvpv emvfnrfprm irdvarelkk eivlnmsgee teldrtvide
      421 igdplihllr nsadhgiesi ekrkeigkpa sgqinlrayq dgnnvvieve ddgqginlek
      481 vkkkaiekgl vkkdiantls qkdiidflfk psfstqdqit dlsgrgvgld vvktkieqlg
      541 gvvevetesg kgskfiirlp ltlaiiqall vtigeekyai plnstkeilk vspdqimmvq
      601 kqevimirnt viplvrldki levpkndtks akqltvvivk kgerlsgfvv dsligqqeiv
      661 ikslgkllyg ikciagatil gdgnvamild vnslai
//
LOCUS       WP_010251915             126 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Myroides injenensis].
ACCESSION   WP_010251915
VERSION     WP_010251915.1
KEYWORDS    RefSeq.
SOURCE      Myroides injenensis
  ORGANISM  Myroides injenensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Myroides.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Myroides injenensis"
                     /db_xref="taxon:1183151"
     Protein         1..126
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14572
     Region          51..123
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mrilrvlllf stilfsfsti qaqekktivn epntitelmn mkktynssit andkfriqvf
       61 ygknseakea lqnfkslype inatiiyntp tykvfvgnfk trleaernlr iikkdfpnsl
      121 lirpsk
//
LOCUS       WP_010252817             109 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Myroides injenensis].
ACCESSION   WP_010252817
VERSION     WP_010252817.1
KEYWORDS    RefSeq.
SOURCE      Myroides injenensis
  ORGANISM  Myroides injenensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Myroides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Myroides injenensis"
                     /db_xref="taxon:1183151"
     Protein         1..109
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12069
     Region          2..106
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(7..8,26..27,35,38,40..41,43,46..47,49,57,62,69)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(26,57..58,60,86)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mssstnffer vyevarqipy grvttygaia kaigaarsar mvgyamnash yddtvpahrv
       61 vnrngllsgk hhfdgtnlmq qllesegisv idnqvqnfne llwlpevqk
//
LOCUS       WP_010255107             714 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Borreliella burgdorferi].
ACCESSION   WP_010255107
VERSION     WP_010255107.1
KEYWORDS    RefSeq.
SOURCE      Borreliella burgdorferi (Borrelia burgdorferi)
  ORGANISM  Borreliella burgdorferi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Borreliaceae; Borreliella.
REFERENCE   1  (residues 1 to 714)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 714)
  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   3  (residues 1 to 714)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..714
                     /organism="Borreliella burgdorferi"
                     /db_xref="taxon:139"
     Protein         1..714
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79375
     Region          1..713
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdssdvidkf knsfkeesie nisdieqall nlevssdqdi insifrnlht ikgssgmfgf
       61 nftaslvhei etvldvvkng kaafnqaaid atlmsvdfir eliegdevis eidfdkrkqf
      121 lvneirkvld isndvkgafq ealendfsks dnssvleesv kvnsenkfdd ealqsefksy
      181 kilfspakgi lfhghkpinl lsklinlgng yvrakvdnip dlelispdnv yvdweirlnt
      241 eesresiedi ftfldsqski diqeldkcle anegdnvesk nfnllhldrn skdltnssfe
      301 ksefvgksff ngdknrsniq ddtarskvni asikvdskkl dhlvnlvgel vtiqsklske
      361 aenrnsniln sisaefslli nelrdyttgl rtvpieilfv kfqrivkdls tslgksilyh
      421 asggdtvldk siieklnepl vhlirnsidh giesaqeres lgkdpkgiik lsacqsgdsv
      481 iviieddgrg ldknkilkka ierniisdsv aktlseidvy nlifepgfst assvtdisgr
      541 gvgmdvvkkq veslrghvvl esefgkytri klifpltlai iegwlvrvkd ehfivplsnv
      601 esclesnkli sqmdgietks nvmnyrgsmi syirlreffq vssekslseq vvvvntnsgk
      661 mgivvdevlg qhqtvikalg kiysrvegvs gatilgdgsl alvvdidait klik
//
LOCUS       WP_010257542             205 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Pseudomonadota].
ACCESSION   WP_010257542
VERSION     WP_010257542.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonadota (proteobacteria)
  ORGANISM  Pseudomonadota
            Bacteria; Pseudomonadati.
REFERENCE   1  (residues 1 to 205)
  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 205)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 205)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Pseudomonadota"
                     /db_xref="taxon:1224"
     Protein         1..205
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=21979
     Region          1..204
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 mevysneneq tdalrnffan ngkalaigvv igiaalggwr ywsshqddta ktvsaqyqql
       61 tsamqagkpe tleavnrfas ensntygala amdlakqyvd agqldkaatl lqnglkdtkd
      121 anlqavinlr lariqlqqnq adaalktldg vkgdgwtaiv adirgeallt kgdkqgarda
      181 wskgvesdas palkqmmqmk mnnls
//
LOCUS       WP_010257904             311 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Pantoea agglomerans].
ACCESSION   WP_010257904
VERSION     WP_010257904.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..311
                     /product="formate/nitrite transporter family protein"
                     /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=33892
     Region          33..284
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mkpssgneqg pndveseekd kgtdievdee alpsraaaih eeirqdgeke lerdgmallw
       61 saiaaglsmg aslmakgifq vhldgvpgaf llenlgytfg fvivimarqq lftentvtav
      121 lpvmhkptws ngalllrlwg ivllgnligt algalafnem pifdeatrqa ftnismkvme
      181 ntpgemfana visgwiiatm vwmfpsagga kllvivmmtw lvalgdlahi vvgsvevlyl
      241 vfngsiswye ffwpfalptl lgnitggtli falishaqir ndmseaavak akaekkkqek
      301 rhqreeqeka e
//
LOCUS       WP_010257982             259 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pantoea].
ACCESSION   WP_010257982
VERSION     WP_010257982.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 259)
  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 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   3  (residues 1 to 259)
  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   4  (residues 1 to 259)
  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 259)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..259
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29604
     Region          8..258
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          179..257
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mtlkviyqpp ldapqlryfm ryeqanarte ylphahawgq limvkshvle mqvegerllt
       61 padipvwipp gqlhssynhr qaqfrtfnla aplcadlprr aclllvdpia haimdefaeq
      121 qieqpetdaq wrlcevlrdr lqlaqvqesy lptsddkfla pvlhaleahp gdnttlagwa
      181 arvfttertl arrcqqqlhm tfgewrqrlr flraivlleq gesvqsiahe lgyssasali
      241 vmfqqqagtt peryrarlg
//
LOCUS       WP_010259089             286 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein [Pantoea].
ACCESSION   WP_010259089
VERSION     WP_010259089.1
KEYWORDS    RefSeq.
SOURCE      Pantoea
  ORGANISM  Pantoea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Pantoea"
                     /db_xref="taxon:53335"
     Protein         1..286
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30771
     Region          12..252
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mfsiaaevrn tlgecplwce rtrrlywtdi easellaiee gndavmrwsl perlgsfalt
       61 eksnillmgf asglafydln sslitpvaas pgdigtrigd grcdragnfv fgtmddgypv
      121 kvigkfhrln aatltvetla lpdvaipnsi cfspdggtly ycdsmqgrim ccdypllqnq
      181 rvfaeiegsg apdgscvddm gylwnaewgg nrvvryrpvg ttdailtspg iqstcptlgg
      241 egftrlyctt atvgltalse ydgallkaes dvspglpenr faahtv
//
LOCUS       WP_010259700             618 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Treponema primitia].
ACCESSION   WP_010259700
VERSION     WP_010259700.1
KEYWORDS    RefSeq.
SOURCE      Treponema primitia
  ORGANISM  Treponema primitia
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 618)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..618
                     /organism="Treponema primitia"
                     /db_xref="taxon:88058"
     Protein         1..618
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=70596
     Region          66..583
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mtkserlklq tpdrtdrnfa alaalfpnav tetvdengav iraidadvlr qeinthvveg
       61 keeryqftwp dkrksvllan apiaatlrpc ceesvnfdit eniyiegdnl dvlkllqety
      121 lnrvkmiyid ppyntgndfv yeddfagean dfliqdgqyd ddgnrmvrnl dsngrfhtdw
      181 lnmiyprlrl ardlltddgv ifisiddnev enlkkicnev fgaenfvani vwkhtqqskn
      241 derhfsrqyn ynvvyaknia nlsnfffert eednknysnp dddpkglwrs gdvrspnyrr
      301 tlcfdiiapn gniikapeig wrwsedtlke klasgeivfk ndfsgiirki ylceqngrtp
      361 enlwdgdkfs ttrraaamik qlfdgkqifd tpkpvelvkc mlqlvtgegd vildffsgsa
      421 ttahavmqln aeddgkrkfi mvqlpevcap dseaakagyk niceigkeri rragakiksd
      481 spltttdldi gfrvlkldst nmkdiyytpq eivqrdldgf vdniksdrtp edllfqvmld
      541 lgvplsakie krgtvfyvnd nylvacfepv dealvmeiah akpyyavfrd ssfkndstlv
      601 nfeqifktys pttirkvl
//
LOCUS       WP_010259945             213 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Alistipes timonensis].
ACCESSION   WP_010259945
VERSION     WP_010259945.1
KEYWORDS    RefSeq.
SOURCE      Alistipes timonensis
  ORGANISM  Alistipes timonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Rikenellaceae; Alistipes.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Alistipes timonensis"
                     /db_xref="taxon:1465754"
     Protein         1..213
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23873
     Region          32..179
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 madnylerkm eeyrarttag qgsrrplatl grlllknrsh rgydanfivr edqlrriiav
       61 nakipsarnq qvlrfrpvls geaqkvlehi rlggalphlh lplpgtepna fiiicstaae
      121 dryvdidlgi saqsmllqaa eiglngicig afdkerirqe fgleweplli laigrgieki
      181 elvpigadge rayyrendth yvpkvrpedl tik
//
LOCUS       WP_010260532             259 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Alistipes timonensis].
ACCESSION   WP_010260532
VERSION     WP_010260532.1
KEYWORDS    RefSeq.
SOURCE      Alistipes timonensis
  ORGANISM  Alistipes timonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Rikenellaceae; Alistipes.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Alistipes timonensis"
                     /db_xref="taxon:1465754"
     Protein         1..259
                     /product="formate/nitrite transporter family protein"
                     /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=27572
     Region          6..259
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mtlintpkev lalagrsaad klrnpvsktl ilaflagayi aigglfslia gfgfpgaaea
       61 pgfqrllsga vfplglilvv ftgaelftgn navlvpgalg rqygwsrvlr nwglvyignf
      121 agalfftwfl vvvpgvlsse lwqkaaygia qakvsmpwmt vflrgvganw lvclavwlgl
      181 sandvpgrmm glffpimcfv aigyehcian mffiplgmml gapvtcgeff idnlipstlg
      241 nivggglfvg glywhlnrk
//
LOCUS       WP_010261237             408 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Streptomyces].
ACCESSION   WP_010261237
VERSION     WP_010261237.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 408)
  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 408)
  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   3  (residues 1 to 408)
  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   4  (residues 1 to 408)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 408)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 408)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 408)
  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 10156937
            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="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42957
     Region          41..393
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(115..117,138..139,198,250,274)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mlilttvltt galtlsacgs rdddsgddkg gssggkkttv vigvdapitg dlsalglgir
       61 nsaelatkia nkqdlvpgfq fkiqalddqa qptigqqnat kfignkdvlg vvgplnsnvs
      121 qsmqkpfnda kltqvspant gteltqgdnw ksgdkkrpfa sffrtattdq iqgsfaakyl
      181 hdtakinkvy liddqktyga glaasfkdtf tklggkivga dhinpddrdf nsvvakvkkt
      241 gakavyygge ypaagplsqq lkdsgakipl mggdgiyaad fiklnkkaqg dlatsvgapv
      301 eqldsakkfi sdydaagykd gyeaygggty daawsiieav kkvaadndgk lpsdarakvl
      361 eamstvkfsg vtgdisfdey gdttntmmta yqveggkwvp rksevykp
//
LOCUS       WP_010262336              98 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Alistipes timonensis].
ACCESSION   WP_010262336
VERSION     WP_010262336.1
KEYWORDS    RefSeq.
SOURCE      Alistipes timonensis
  ORGANISM  Alistipes timonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Rikenellaceae; Alistipes.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Alistipes timonensis"
                     /db_xref="taxon:1465754"
     Protein         1..98
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10393
     Region          4..91
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(7..8,26..27,35,38,40..41,43,46..47,49,55,60)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(26,55..56,58,79)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mhlpadfdae iwdivaqipa griatygqla rlagmpgyar rvgramaaap agipchrvvn
       61 aagrtapgwt aqrelleaeg vrfrrngcad lthlidgf
//
LOCUS       WP_010262487             408 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Streptomyces].
ACCESSION   WP_010262487
VERSION     WP_010262487.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 408)
  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 408)
  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 10007089
            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="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45211
     Region          5..394
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mttqplplsa dearrialra qgllgapdrr agargvlrhl gavqldtisv larshelvpy
       61 arlgaigrqa vesaywappe apahafeyws haacvlpvee wphfafrrra yrdrplwghe
      121 mppgayekvl aqlrdegplt atelggakng gewwdwsgsk vaveraltyg dvvcvrrtgw
      181 rrvydlpera ipaellhddl ddlecvrrli rlaarslgvg trsdladyhr lkteqfdavi
      241 edcglvrvrv egwgkpawad pqalessprg rhrttllspf dsliwerara erlfgfshrl
      301 eayvpkpkrv hgyfampvls ggrliarvdp aregttlvar qitlggdvpg tatprkaveg
      361 takalaeaat wvgctrvrvd rvdppelrep lereatralt arlegaev
//
LOCUS       WP_010265735             400 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Alistipes timonensis].
ACCESSION   WP_010265735
VERSION     WP_010265735.1
KEYWORDS    RefSeq.
SOURCE      Alistipes timonensis
  ORGANISM  Alistipes timonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Rikenellaceae; Alistipes.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Alistipes timonensis"
                     /db_xref="taxon:1465754"
     Protein         1..400
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43195
     Region          1..400
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mvilvlncgs ssikyqvidm epssskllak giveriglpe gdlvhkpvgk enfelhqpip
       61 dhttgiklvl daltdpahgv iasldevkav ghrvahggef fpescivted akekirslfe
      121 iaplhnpanl egvlsiekvl pgvpqvtvfd tsfhqtipav nymyalphay ydkyrvrkyg
      181 fhgtshkyva qvgaelagld fhnskiitch igngasvtai lngksfdtsm gfspldglvm
      241 gtrcgsvdas aitfigekeg mtyaqlndmm nkksgvlgis dissdmrdid raydegnpra
      301 ilardmhygr irkfvgeyaa emggvdmiif tggvgensce mreevcrgle fmgvkfdpaa
      361 nkgargvnki lsaadskvkv atiatneelv iatdtynlvk
//
LOCUS       WP_010266589             399 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Alistipes timonensis].
ACCESSION   WP_010266589
VERSION     WP_010266589.1
KEYWORDS    RefSeq.
SOURCE      Alistipes timonensis
  ORGANISM  Alistipes timonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Rikenellaceae; Alistipes.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 399)
  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   5  (residues 1 to 399)
  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   6  (residues 1 to 399)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 399)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Alistipes timonensis"
                     /db_xref="taxon:1465754"
     Protein         1..399
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43574
     Region          17..61
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          81..394
                     /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 mkqsflklat egnknailkq hiirhfifeg dssiadlska vnlsvptvtk llgelieeef
       61 vhnfgeqqta ggrkpniygl npytgliiga dikkdsvimg amnfkgnlih revvdfnleg
      121 pqalddlcnv ilgfikrhki dptkilavgv nisgrvnsrt gysysyffve eqplsvllee
      181 rlgytvfien dtraaaygey mnnesyaqqt llyinaswgl gigiiidgkl fyghsgfsge
      241 yghfpfndee iicrcgkrgc letvasgsal yrmfleklea gsvsvlsdkf ksgakitmdd
      301 ilaaianedv laieiletvg hnlgkaiagl inifnpeqiv iggslstake yimlpvrnav
      361 nkyslmlvnk dtriclselg enagvtgacl larnkligl
//
LOCUS       WP_010269514             689 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Paenibacillus senegalensis].
ACCESSION   WP_010269514
VERSION     WP_010269514.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus senegalensis
  ORGANISM  Paenibacillus senegalensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 689)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 689)
  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   3  (residues 1 to 689)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..689
                     /organism="Paenibacillus senegalensis"
                     /db_xref="taxon:1465766"
     Protein         1..689
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=75409
     Region          1..689
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          161..238
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 mdvnqylsvf idesrehlqa mndqlleleq qpedisivqt ifrsahtlkg msatmgfedi
       61 aslthemenv ldmirnekls mneaifevlf qaadaleamv ediveggsgt sdvqsliavl
      121 qqivgggepv aakgevhqtl sldefqlsvm qqsiaagmkv yqievtlred cvlkaarcfm
      181 vfgilensge vvgsepsved ieqekfeqkf tvylvserda aelrseianv seveqvilvs
      241 vteemliqvk egrreaaaan aaaavqseek aaagavgspa gkiqktqkde qatdrknkar
      301 narassanrt irvdierldv lmnlfselli drvrleqlaa eigraelsdt vehmarvsad
      361 lqnivlklrm vqvdtvfnrf prmirdiaks ldkkvelvit gadteldrtv ideigdplvh
      421 llrnaidhgl eatneriaag kpetgtiqls afhsgshvfi eieddgkgin rdkvlataik
      481 rnviseeqae klsdeevfrl lfasgfstae qisdlsgrgv gldvvkskie slggqvsvts
      541 rlgrgtkfsv qlpltlsiis amlvrigvek falpissive taivsrkeir kvhgnqlvpy
      601 rdhvipvifl devldipvhe vsadptlemv virkgeklaa vvvdefigqq divlkslgqy
      661 ltqlfavsga tilgdgqval ilepndlik
//
LOCUS       WP_010271087             123 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein [Streptomyces].
ACCESSION   WP_010271087
VERSION     WP_010271087.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..123
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=13396
     Region          2..75
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 metdidphal igrkavdheg arigtvdevy lddatgipew aairtglfsr dafvplepsr
       61 lvsgvlrvpf aralikdapd fgvgrhlspq qelqlyrhyg ldanppephe dvefgsiagr
      121 eda
//
LOCUS       WP_010271478             679 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: M4 family metallopeptidase [Streptomyces].
ACCESSION   WP_010271478
VERSION     WP_010271478.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 679)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 679)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 679)
  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 679)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..679
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..679
                     /product="M4 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=69606
     Region          42..652
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mrrtssrraa atggallavs alltaamqtg vataapsptg kaasaarpga lpaklspaqr
       61 aeliakaqkk saatagelsl gaqeklvvrd vikdqdgtlh tryertydgl pvlggdlvvt
      121 tnpagetgkv vrasqaklsg vkttakvpaa taqkqalgaa kaqgaakpat dqaprkvvwl
      181 aegkpvlaye tvigglqedg tpnelhvvtd aatgaklyey qgiengtant qysgtvtist
      241 tksgstynlt datrgghkty tlanktsgtg tlvsgpddvw gdgkgttpet aaadaaygaq
      301 etwdfykntf grsgirgdgv aaysrvhygn qyvnafwdds cfcmtygdga gnaapltald
      361 vaghemshgv tsetaglnys gesgglneat sdifgtgvef ysntatdpgd yligekidin
      421 gdgtplrymd kpskdgasad nwsstlgnkd vhyssgpanh ffyllsegsg aktvngvsyn
      481 sptydglpvt gigrdkvlqi wykalttqft sttnyagart gtlaaassly gatsaeykav
      541 qdawaainvg arsgggtdpg ngggtvftst tkvaipdags avtsslavtg rsgnapsnls
      601 vavdithtyr gdlvvdlvap ngtsyrlkns sssdsadnvk atytvnassv aangtwklkv
      661 qdvysgdtgs ingwsltfp
//
LOCUS       WP_010271693             383 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Streptomyces].
ACCESSION   WP_010271693
VERSION     WP_010271693.1
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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..383
                     /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=41992
     Region          52..320
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mhhdpaesgq lsavpadpaa rrllppespa rtvgpgaakg agaadtgggk ardpffdnak
       61 ylaivlvaia hswepllass rplralyltv yafhmpafii isgyfsrtft lgapqvrkli
      121 tgvavpyvif qyaytlfarl agpepvptws vidpwwlnwf lvalfvwrlt tplwrlvrwp
      181 lplalafavl gsmspeigad ldlqrvlqfl pyfvlglllr phhfallahk wpkivaapvl
      241 ltglcaawwl aprmpyawly hresaqdlga pwwsgplmtf allaaslvlt aaflalvprr
      301 ttwctrlgag tlggyllhgf likavewggw ydsafahslp gallfsagaa lvvtllctpp
      361 vrrafrwale prldwafgdt rgt
//
LOCUS       WP_010272324             384 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Streptomyces].
ACCESSION   WP_010272324
VERSION     WP_010272324.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 384)
  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 384)
  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
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 384)
  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   5  (residues 1 to 384)
  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   6  (residues 1 to 384)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 384)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 384)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..384
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40341
     Region          20..69
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          81..367
                     /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 mgrltggdps llrrinsavv ldtlrggrpr tlteiarltg lsrptvegsv ddltaaglvv
       61 eaaadsgark qgrparlyrf raeaghllgl eigphrvaat vsdlegrelg taareveesa
      121 gaddrierlr atvgellrrt gvardslrav gvgspgivea dgtirlgtal pqwtglrlge
      181 rlrrsfrcpv lvendanaaa laehwqgvar gsddvvvvla glspgagsli ggrlhrgfgg
      241 aageigalhl lgqeetpetl lsttgrplhp lderavtevf alaregddqa raavdrflar
      301 lvhdvaalvl aldpelvvig gwaagldgvl eplrqqleky clrtprvals glgeaairtg
      361 alrlaldhve kelfavestv sars
//
LOCUS       WP_010273278             182 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein, partial [Corynebacterium bovis].
ACCESSION   WP_010273278
VERSION     WP_010273278.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium bovis
  ORGANISM  Corynebacterium bovis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Corynebacterium bovis"
                     /db_xref="taxon:36808"
     Protein         <1..182
                     /product="HNH endonuclease family protein"
     Region          38..171
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 avrgllatlp vkgrapktgy treqfgpswd dvdrngcdtr ndilardlrd ivlsgrckvm
       61 sgtlddpytg ttipfvrgrq tssavqidhv valsdawqkg aqqldpvrrt elandplnll
      121 avdgpsntak gagdaatwlp pntafrcryv atqvqvkaky glwvtaaerd avdrelgrcp
      181 ag
//
LOCUS       WP_010273899             216 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Paenibacillus senegalensis].
ACCESSION   WP_010273899
VERSION     WP_010273899.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus senegalensis
  ORGANISM  Paenibacillus senegalensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 216)
  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   3  (residues 1 to 216)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Paenibacillus senegalensis"
                     /db_xref="taxon:1465766"
     Protein         1..216
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24749
     Region          17..215
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mepqiaqelk cqfstgsspg qqaqyrsrla dynsqyimid ipihcesgkl tlpyigdelr
       61 itytrngrsh sfltsvlghl qepvplivvk rprrreifld yeesyfkmdg qlelavkgpg
      121 glhfvaiteq vsgdgvtfsc estiklihhe eyhcwlllht skgnpvvvdf raelvrslpi
      181 tpngqvvqmt fteikeqhrq eivrycfekq rrtrka
//
LOCUS       WP_010276510             425 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Paenibacillus senegalensis].
ACCESSION   WP_010276510
VERSION     WP_010276510.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus senegalensis
  ORGANISM  Paenibacillus senegalensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Paenibacillus senegalensis"
                     /db_xref="taxon:1465766"
     Protein         1..425
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=48517
     Region          19..424
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mskytnnngl etsrneprae ilggflsdps lldeyrqqlt pemfaeyrwl ynlilevads
       61 egltfrgvss rcdlyqiqtl hqvkasffse rrlpdlithi kkenlslvik niarqaletd
      121 dpdealrllq qetytlsste sgtekdfdqe ldewaaevme iaddpskayg mmtglgeldr
      181 ftmgfqrtdf svigartsmg ktafvielml rlhkagykva myslemgrkq lfyrmiaslm
      241 qvdfemfksg klakthyeta mkrkeelrgl vindtrgvta dyisddmrrl krtqgldfvv
      301 vdyiqdvhep getndnsgsa isricrklrk aakisdchvm glsqvvrdve krqdkrplns
      361 dlsgstgiet sadviallyr ddyynpdtdr kgilevnftk qrngktgkve lyydrttqki
      421 sslsr
//
LOCUS       WP_010277148             293 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: class II fructose-bisphosphate aldolase
            [Streptomyces].
ACCESSION   WP_010277148
VERSION     WP_010277148.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 293)
  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 293)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            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="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29053
     Region          2..285
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 malvptgelv aeavaggrgl pafnvitleh veavvagaer aggavvlqvs enavryrlgr
       61 lgplaaaars aavaagvpvg lhldhvtdae llrqaadegf gsvmydgakl pyeanlaatc
      121 eavlwahghg lwveaelgev ggkdgaaplg phapgartdp geaaafvaas gvdglavavg
      181 sshamtsrta aldhgllgrl rdaagvplvl hgssgvpdee vraavrggit kvnvgtalnv
      241 altaavrerl gaepglvdar gylgagream aevverltrv vagagegvae grg
//
LOCUS       WP_010277713             200 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LytR C-terminal domain-containing protein
            [Streptomyces].
ACCESSION   WP_010277713
VERSION     WP_010277713.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 200)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..200
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=20371
     Region          83..172
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mggkyritgd kyphmrrprk rgrlvaviva saavlgllgw gslqlfdvfs gggtataaag
       61 pkhcarpsae parvtklpap kavkvnvlna ttrsglaket adelkkrgft igevgnapaa
      121 ydkkvktagl ligpksaads slkvlgtqfa gagtrtdark gaaldlvigd gftkltapgt
      181 aekalaalqr gpaesakpkc
//
LOCUS       WP_010278866             431 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Paenibacillus senegalensis].
ACCESSION   WP_010278866
VERSION     WP_010278866.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus senegalensis
  ORGANISM  Paenibacillus senegalensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Paenibacillus senegalensis"
                     /db_xref="taxon:1465766"
     Protein         1..431
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=48849
     Region          4..361
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mivdydvein vlagmlkdek slyeglsllt eqhfngdqhk evfreiqrls sngqvtynmv
       61 ykalretvhm dlfkalrqsi vsadsfpywy kqlheiyvkr lyfeaaqeis eiansnrpls
      121 eiteiveski mgasvqegte rivtpeeagr kaaeeferrv ksgetihgik lsrpvpsggm
      181 pvtdgfpgld dmfrglrggd liilaaktge gkttlaqniv rhasihqsyr tfyqntemke
      241 idivnrfvaq mtgksyagid sgsldsfdrt lvrqafenya ksrvfiselp mltpersrgl
      301 arqfktkygk ldllvidyvg rmeldnskgk qewqilrdia keckrlaqql dtcvilvaql
      361 neegklqgar amaneadgvl flepltreev nnapygathk lepykarrgs kdkhlwisfn
      421 kakmyitevr g
//
LOCUS       WP_010279748             831 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pectobacterium brasiliense].
ACCESSION   WP_010279748
VERSION     WP_010279748.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium brasiliense
  ORGANISM  Pectobacterium brasiliense
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 831)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 831)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 831)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..831
                     /organism="Pectobacterium brasiliense"
                     /db_xref="taxon:180957"
     Protein         1..831
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=91833
     Region          71..119
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          97..831
                     /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 malipffstq rtpsklamav hlllcgaplf vhstataaet aavaatktys isagplnqql
       61 nqfatqsgvy lvgdaqlatg ktgpslqgny svdggfsall agsglqvipq pngvwrlqri
      121 pqgdemlvva gvnrngvteg tqsyttrsmn tatqlnlspr etpqsvsvvt rqrmddqnmt
      181 sldeamkqtt ginvvnqnsy qvkyesrafv mdnikedgvn fssqnsvsnm gavqassesp
      241 dlaiydrvei lrgasglsqg ngepggtvnl vrkqpthnfq asgsigagsw dnyrseldis
      301 gplnddaslr grlvgvyqdr qsfkdyehse rkvlfgtlay dltpsttvtg ginwqktrgv
      361 pdvygipfat nksslnlprs tylgaswnri efekinpfve lehhfdndwt lktalnyihs
      421 raassyigim ngtsgvnpat gnsslnnnlr ydnkaeqwgy nlslngpfel lgrshelvvg
      481 gdyqkesfnn nhirinntst vnifnwqpns laepdwsnts lynnhyndrf nlyqrgafat
      541 arfeladdwk lilggrysay sydeyftnhf rntsslsslh asnefvpygg llwdfadnyt
      601 wylsyaeiyk pqsekdrngk llpaitgtny etgikgeffd gdlntslalf riiqanrama
      661 vadssvclig tscsqaqgev rsqgvefdit gklaegwqiq agytltnsky legsaseraa
      721 qfsprtpkhm fklytsynlp gelnqwtvga gmtaqtetqt ypnrayglhq ggytlfnani
      781 ryqhsknlsf nlvgnnltdk tyflnlnnrh lsgnnyygdp rnfmltakwn f
//
LOCUS       WP_010280775             302 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 5'-3' exonuclease [Streptomyces].
ACCESSION   WP_010280775
VERSION     WP_010280775.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..302
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32303
     Region          1..296
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mlldtaslyf rayfgvpdsv rapdgtpvna vrglldfiar lvqdhrpdal vacmdadwrp
       61 ewrvslipsy kahrvaeete tgpdeeevpd tlspqvpvie avldalgiar lgvpgyeadd
      121 vigtlatrah gpvdivtgdr dlfqlvddar gvrvlyplkg vgslqvtdea llrekygvdg
      181 pgyadlatlr gdpsdglpgv pgigektaak llaaygdldg iraaaadpas kitpaqrrrl
      241 vesapyldva pavvrvardi pvpedlderl pdeprdgevl talgerwglg gsldrvlhtl
      301 tr
//
LOCUS       WP_010283751             334 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Bacillus timonensis].
ACCESSION   WP_010283751
VERSION     WP_010283751.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 334)
  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 334)
  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
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  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   5  (residues 1 to 334)
  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   6  (residues 1 to 334)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 334)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 334)
  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 13384462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..334
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37578
     Region          18..>59
                     /region_name="MntR"
                     /note="Mn-dependent transcriptional regulator MntR, DtxR
                     family [Transcription]; COG1321"
                     /db_xref="CDD:440932"
     Region          80..331
                     /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 mdqsitfkdi kknnysliyh llyqkgklsk qdianelnls lptvtqnlvr lekenliekn
       61 glfessvgrr ataysicsha risigveilk ktvqilaidl rgetiqqtef airykneesy
      121 fkevsqavre fiaaldvsdd qilgigfavq altsidgqki tygkilnstg lgidvftkyl
      181 nypcmfvhda qcaattelwm qnevgdaiyl sigphlggai ilndklymgn egysgtvehm
      241 tvnpngpscy cgqkgcmety ssinalleen esldiffqqv rlhtpsyver wnaflnhlay
      301 sinnihlvln rdfilgghla pylekmilky fmik
//
LOCUS       WP_010286013             142 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Pectobacterium brasiliense].
ACCESSION   WP_010286013
VERSION     WP_010286013.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium brasiliense
  ORGANISM  Pectobacterium brasiliense
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Pectobacterium brasiliense"
                     /db_xref="taxon:180957"
     Protein         1..142
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15436
     Region          5..140
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 msefwavfsl fwssllsatl lpgssevllv tllladsakp ylliavatvg ntlggltnif
       61 igrllpqpkq qagysvamrw lqrygcaall fswvpvvgdl lcvlagwlrm pwmqsalfig
      121 igkalryivl tgitlqgmaw ws
//
LOCUS       WP_010286265             331 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Kurthia massiliensis].
ACCESSION   WP_010286265
VERSION     WP_010286265.1
KEYWORDS    RefSeq.
SOURCE      Kurthia massiliensis
  ORGANISM  Kurthia massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Kurthia.
REFERENCE   1  (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   2  (residues 1 to 331)
  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 331)
  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 331)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Kurthia massiliensis"
                     /db_xref="taxon:1033739"
     Protein         1..331
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35842
     Region          1..69
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          252..315
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 maelgtrlke arlakgysle dlqeitkiqk rylsaieegn fsvmpgafyv rafikqyaea
       61 vgldaneile tykseipank aaevsagtat siqqpkggsn qrssqpaqka vkhkaqttkk
      121 ksdlmpkiav avivvvviai vwflmqnras ndvtedvkqe qtaktettkt datkddskeq
      181 evvdqeaeek aaaekaakek akakakaeke kaekekaake kkkagtiskg edagdsattn
      241 ytlsntkkfk vrvemtgdnw vgitdkngan lvagkmyang dklefdakgq esirirlgaa
      301 aagkvfinnk evkllvpass rptqnivvkt k
//
LOCUS       WP_010288309             159 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Kurthia massiliensis].
ACCESSION   WP_010288309
VERSION     WP_010288309.1
KEYWORDS    RefSeq.
SOURCE      Kurthia massiliensis
  ORGANISM  Kurthia massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Kurthia.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Kurthia massiliensis"
                     /db_xref="taxon:1033739"
     Protein         1..159
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17141
     Region          8..159
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfekttyagd laaqytllsk qlaalleget dhmailsnas allnqflndv nwcgfylykn
       61 delllgpfqg lpacvhipig rgvcgtaakt metqlvkdvh afpghiacda atnseivvpl
      121 skdgalfgvl didspstgrf detdrdgiel fartlekyl
//
LOCUS       WP_010290369             343 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Kurthia massiliensis].
ACCESSION   WP_010290369
VERSION     WP_010290369.1
KEYWORDS    RefSeq.
SOURCE      Kurthia massiliensis
  ORGANISM  Kurthia massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Kurthia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Kurthia massiliensis"
                     /db_xref="taxon:1033739"
     Protein         1..343
                     /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=39914
     Region          1..280
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mseskqrifv fdnvkalliv lvvlghaady ytdqfesmrm fffyiylfhm plfiflaglf
       61 skstilkdpf riekianflv lyfileilfy fiihywlgnq synfnpfven gvpwfmfama
      121 awlcigrvir rvpayivlpv siiaalligy thvgdtlvls riitffpffi lgfyvktndl
      181 veslkapelk iiswislvli aftiyfnidg lydmrnllsg rnpydrvnle lgipasgavm
      241 rllvmvvtic msisvmalmt hkrtwftvlg trslaiyffh rpilfiyqhy hlndylkdaf
      301 phawlwiyla ffllvsivla aapfekllls iqsfvtrtmk rsv
//
LOCUS       WP_010290565             386 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: threonine synthase [Streptomyces].
ACCESSION   WP_010290565
VERSION     WP_010290565.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 386)
  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 386)
  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   3  (residues 1 to 386)
  AUTHORS   Parsot,C.
  TITLE     Evolution of biosynthetic pathways: a common ancestor for threonine
            synthase, threonine dehydratase and D-serine dehydratase
  JOURNAL   EMBO J 5 (11), 3013-3019 (1986)
   PUBMED   3098560
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10107605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..386
                     /product="threonine synthase"
                     /EC_number="4.2.3.1"
                     /GO_function="GO:0004795 - threonine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009088 - threonine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39393
     Region          57..367
                     /region_name="Thr-synth_1"
                     /note="Threonine synthase is a pyridoxal phosphate (PLP)
                     dependent enzyme that catalyses the last reaction in the
                     synthesis of threonine from aspartate. It proceeds by
                     converting O-phospho-L-homoserine (OPH) into threonine and
                     inorganic phosphate. In plants; cd01563"
                     /db_xref="CDD:107206"
     Site            order(74,79..80,95,118,134,137..138,144,160..166,168..170,
                     182..183,214,329..331,332..333,363)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:107206"
     Site            order(101,127,228..232,361)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:107206"
     Site            101
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107206"
ORIGIN      
        1 mtsaapssta lpdrlcprdg trvpladpaw ccpacagpld ldfhpvpgpp agpatslwry
       61 adilppaapg islgeggspl vpltervsak ldflmptlsf kdrgavllvg laqrlgarev
      121 ladssgnagt svaaycarag lrctvyvpes tspkkteqia ahgarvvrvp gdreataraa
      181 raaadepgvf yashvfhpyf tqgtktyahe lwdqlggrlp ealvvpvgng tlllgvalav
      241 eelhgaglip hrpalhavqa eavsplaraw reglddlggd tpaaptlaeg iaiprpprar
      301 qilaavratg gafhtvpesa iapaqadlak rglyveatgv acwaavrega lgdteavvpl
      361 cgaglktgma psaqpgpaqk tspsga
//
LOCUS       WP_010292291             403 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator, partial [Streptomyces sp.
            SA3_actF].
ACCESSION   WP_010292291
VERSION     WP_010292291.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. SA3_actF
  ORGANISM  Streptomyces sp. SA3_actF
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 403)
  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 403)
  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
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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   5  (residues 1 to 403)
  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   6  (residues 1 to 403)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 403)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Streptomyces sp. SA3_actF"
                     /db_xref="taxon:682181"
     Protein         <1..403
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          16..59
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          79..373
                     /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 rpaprafnql algsyneklv iesireagtl srveiaastg ltpqavsrit rnlltsgliv
       61 qdegrsagag kpriplrlrp dagyaagihl dpwmitavav dlcgqvvarr rmpleaprdp
      121 dwclaqmaal areaaaevpd ggpvlgygaa lpgpldrrag vlldpplfeg wdrvdvgakl
      181 sarlgspvvv ekdataaaig erwlgaaera edfvylylga gagsgaflng dvhrgatgna
      241 gelgelcapr praagdddvp rsaeecapis ttlarvraag lpvprgeday pwvcaraaeg
      301 dpavrevvdg varvlargaa glvglfdtel livggpavlp gvraryldvi taavntfpla
      361 hhvrtvrvap shlgeeaaav gaassvfhat ftpslkagrr arn
//
LOCUS       WP_010292454             803 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Clostridium senegalense].
ACCESSION   WP_010292454
VERSION     WP_010292454.1
KEYWORDS    RefSeq.
SOURCE      Clostridium senegalense
  ORGANISM  Clostridium senegalense
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 803)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 803)
  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   3  (residues 1 to 803)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="Clostridium senegalense"
                     /db_xref="taxon:1465809"
     Protein         1..803
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=90184
     Region          1..802
                     /region_name="PRK10547"
                     /note="chemotaxis protein CheA; Provisional"
                     /db_xref="CDD:236712"
     Region          <424..803
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdtsqylsmf leesmdnlqt lnesllileq epndkerlne ifrvahtikg maatmgynti
       61 aelthkmedv lskfregeln vtpkvvtvlf rcldnlenmi ntiadgeeld ydisdivhql
      121 edignkkqsd eakenaenae gksieavcdv anqlqfneyd lnvikqakds gfnaysiyvk
      181 lddgtilksa rafvimqale ehgeiiktqp iledleiedf dldinfayit ketketiknl
      241 iedisevriv evsdvktdkn keeinsdcsn ynlseydmdv ikqakqvgfn alnvniqlde
      301 gtllksarvf iimqeleahg eviksipase dleaenfdyn ieltyitkkt eketkdilfk
      361 isevksveis nisennknsi knlkpkeitd ksekikeink eiekgkdikg kkttndkhns
      421 dkhpkgrtvg qsvrvdlerl dkfmnmvsel vihrtrleqi slnhkipeln etleqvarst
      481 sdlqdlvmki rmlpldavfn rfprmirdls ielgkeidle ilgqdteldr tvieeigepl
      541 ihllrnaadh giespeerik agknpngkik liaypegtka vikveddgkg lnvdkiraka
      601 esvgittegm sendiknlif sqgfstnevv tdisgrgvgm dvvktkiaal ggtvdaisel
      661 gkgtsfiirl pltlqiiqal lvkvgsetma islgyidrvi eykkeltkkt nnkeviiynd
      721 nivnlirvne klnipeddhg kkyvvmtkvg erevgllvds llgqqeivik pfgktlknln
      781 eyigatilgd glvtlildva sli
//
LOCUS       WP_010293685             285 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Clostridium
            senegalense].
ACCESSION   WP_010293685
VERSION     WP_010293685.1
KEYWORDS    RefSeq.
SOURCE      Clostridium senegalense
  ORGANISM  Clostridium senegalense
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Clostridium senegalense"
                     /db_xref="taxon:1465809"
     Protein         1..285
                     /product="formate/nitrite transporter family protein"
                     /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=30162
     Region          4..275
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msknmlsple vteyveevgv kkaknksiqt lflgilagay ialgafgsav ashsvtnfgl
       61 qktvaglvfp vglllvlicg aelftgncll svavaqkris ikdmaknlli vfignfigtv
      121 liallvygag lldfnsgavg gyaikvatgk vnltitqalf sgilcniivc lavwgsytak
      181 disgkvlmgf ipifvfiisg fehcvanmyy ltigllakgn pvyveashqt aeklanlnvi
      241 gvihnlipvt igniiggsil igltywfiyk kseknkeivk enkva
//
LOCUS       WP_010294785             184 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Clostridium senegalense].
ACCESSION   WP_010294785
VERSION     WP_010294785.1
KEYWORDS    RefSeq.
SOURCE      Clostridium senegalense
  ORGANISM  Clostridium senegalense
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Clostridium senegalense"
                     /db_xref="taxon:1465809"
     Protein         1..184
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20680
     Region          6..173
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mtnnetlkai knrrsirkfk dnqitkeeln aivqsaiyap tghndqpwhf tiiqnkevln
       61 kisevaneam knseiewisk lgsknrplfy naptvvivsg kegtyspltd csaaiqnmli
      121 aaeslnigsl wnglvsyffe nkeeakvlnl kegykpyyav algykdceap iapernedvf
      181 tyil
//
LOCUS       WP_010295303             419 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Pectobacterium].
ACCESSION   WP_010295303
VERSION     WP_010295303.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
REFERENCE   1  (residues 1 to 419)
  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 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   3  (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   4  (residues 1 to 419)
  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 419)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..419
                     /product="CmpA/NrtA family 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=45449
     Region          1..>56
                     /region_name="DUF839"
                     /note="Bacterial protein of unknown function (DUF839);
                     cl23843"
                     /db_xref="CDD:474079"
     Region          42..293
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 msdsktksmt vsrrqfllgs aalggslmlp glmnsawaag sdapekkeir vgfipltdca
       61 svvmaavkgf dkkygitivp skeaswaavr dklvsgelda ahilygqlyg lqmglsgsqs
      121 nmaalmtlnq ngqgitlanq lraanvtdla alqkyvaasp agtytfaqtf ptgthamwly
      181 ywlasagihp lndvrtvvvp ppqmvmnmki gnmvgycvge pwnqraisen igftaatsqd
      241 iwpdhpekvl gtradwvnan pnsaraltaa ildasrwida sdenrretag vvagrayina
      301 keetivgrml gqyenglgks wkdehamrfy hdgsvnypyl sdgmwfltqh krwgllteep
      361 dylavakqvn ridiykqaad avgnvplpgs dmrssvlidg rrwdgsdpag yansfsvkk
//
LOCUS       WP_010248805             450 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Acetivibrio cellulolyticus].
ACCESSION   WP_010248805
VERSION     WP_010248805.1
KEYWORDS    RefSeq.
SOURCE      Acetivibrio cellulolyticus
  ORGANISM  Acetivibrio cellulolyticus
            Bacteria; Bacillati; Bacillota; Clostridia; Acetivibrionales;
            Acetivibrionaceae; Acetivibrio.
REFERENCE   1  (residues 1 to 450)
  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 450)
  AUTHORS   Magnet,S., Arbeloa,A., Mainardi,J.L., Hugonnet,J.E., Fourgeaud,M.,
            Dubost,L., Marie,A., Delfosse,V., Mayer,C., Rice,L.B. and Arthur,M.
  TITLE     Specificity of L,D-transpeptidases from gram-positive bacteria
            producing different peptidoglycan chemotypes
  JOURNAL   J Biol Chem 282 (18), 13151-13159 (2007)
   PUBMED   17311917
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   4  (residues 1 to 450)
  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 20588217
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Acetivibrio cellulolyticus"
                     /db_xref="taxon:35830"
     Protein         1..450
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region 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=51356
     Region          126..187
                     /region_name="SH3_3"
                     /note="Bacterial SH3 domain; pfam08239"
                     /db_xref="CDD:462405"
     Region          310..448
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mkrafvllpi illfltacdk ktdnniavrn evynevynse sehdrivtpd tnvtaeplkg
       61 eaeeknvtes dvivdqkele sgkgdlteyr eimlktfesk vpeevvinkk yskyevptdy
      121 llilsdeini rekpsssakv igkaqyfekv nlvaevqgey lekyktdkwy kiawkvdnkv
      181 qngyilsila ekrefqfdkm feavntaqne ldkntsayit nyknragtap lykgrtkdkf
      241 giqrnqaapa yyepnlgaef ryisdgalvs iiaetdsfyk ihalnfegey yvpkkyisfr
      301 esieklskvv vvdrknqneg vfelidgkwn lisytyattg enskhklptd lgyymaiqkv
      361 akftylddat kqiagyapya irfnggayih gvpvdyikkg gkrvdpgmqe ylstvgtvpr
      421 shkcvrnyts hakflynwve igksavivie
//
LOCUS       WP_010296187             127 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ribonuclease HI family protein [Leuconostoc].
ACCESSION   WP_010296187
VERSION     WP_010296187.1
KEYWORDS    RefSeq.
SOURCE      Leuconostoc
  ORGANISM  Leuconostoc
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Leuconostoc"
                     /db_xref="taxon:1243"
     Protein         1..127
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=14280
     Region          3..123
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(7..10,41..43,46,68,105,119)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mmtlyvdaar nvhtgqsavg avlivnkhqq qlksdlpqsa dnheaefmgl iwgikqlpmi
       61 dnlqiytdsk ivadaiqkky akhyqsyvdr iisllsefpl vliswipekq nhgahqlamq
      121 alkktnr
//
LOCUS       WP_010298696             378 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator, partial [Streptomyces sp.
            SA3_actF].
ACCESSION   WP_010298696
VERSION     WP_010298696.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. SA3_actF
  ORGANISM  Streptomyces sp. SA3_actF
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 378)
  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 378)
  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
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 378)
  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   5  (residues 1 to 378)
  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   6  (residues 1 to 378)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 378)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 378)
  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 15726307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Streptomyces sp. SA3_actF"
                     /db_xref="taxon:682181"
     Protein         1..>378
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          10..>124
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          69..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 mahtqasagh llrlirsgaa itrgelqeat glsrstvghr ldqlfaagwl rgssgtstgg
       61 rpsarlefdt ghavvlvadl etpharaavv dlagtvlaeh rdalviadgp dvvldqlarw
      121 faelldasgq ppervcgvgl svpgpvdwer allvqppimp gwdgyplrer freyhaahvg
      181 rppreeplpv fvdndanlma lgeqralhpd crafvfvkas tgigagvvvd galyrgidgg
      241 agdighirlh drpdvvcmcg stgclaavas ggaiaaqlte agvptasghd vrahlaagqp
      301 davrlsrrag qrigevlvtv vtllnpgvlv lggdlagtpf ltgvrellyq ramprttahl
      361 qvltselgdr agllgaai
//
LOCUS       WP_010299459             271 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein, partial [Streptomyces
            sp. SA3_actF].
ACCESSION   WP_010299459
VERSION     WP_010299459.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. SA3_actF
  ORGANISM  Streptomyces sp. SA3_actF
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 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   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 271)
  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 271)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Streptomyces sp. SA3_actF"
                     /db_xref="taxon:682181"
     Protein         1..>271
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          17..84
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          203..255
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 msignspaee rpsddgpslg etlrraraka glrvedlsas trirvplvqa ienddfsqcg
       61 gtvyarghlr alaravgldp epllarydae hdgaplptpa aplfeaerir pdrrrpnwta
      121 amvaaivavv afvgftvvsg gdepagtkrh aaegapagds aspspsasps gspspaspan
      181 paesavaavp adkvtvklsv perrswvsvk dhtgrslfdg vleqgqhktf tdaeqvdlvl
      241 gdagavrvsv ngkpiadkfr pgqvqrlsyt k
//
LOCUS       WP_010299889             246 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Pectobacterium carotovorum].
ACCESSION   WP_010299889
VERSION     WP_010299889.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium carotovorum (Erwinia carotovora)
  ORGANISM  Pectobacterium carotovorum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 246)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Pectobacterium carotovorum"
                     /db_xref="taxon:554"
     Protein         1..246
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=28060
     Region          14..239
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mntttlnidg kilrltaefq piihlphnki fryealarfy nsegvlistq qtidkieeck
       61 aidkvtdfmf dvvcqviknk ssmtisfnls hllfnnsayl etlyqkclmh evnpqnieie
      121 isekttrqql idgipflnqa kkygfmisld dfgagnlqid slslfdfdti kidrsiidgi
      181 gkeetksqkl kvllnklipl gvniicegve katdlnrlnk yhpigiqgyi fyrpltfsql
      241 rllegf
//
LOCUS       WP_010300047             831 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pectobacterium carotovorum].
ACCESSION   WP_010300047
VERSION     WP_010300047.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium carotovorum (Erwinia carotovora)
  ORGANISM  Pectobacterium carotovorum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 831)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 831)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 831)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..831
                     /organism="Pectobacterium carotovorum"
                     /db_xref="taxon:554"
     Protein         1..831
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=91828
     Region          71..119
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          97..831
                     /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 malipffstq rtpsklaiav hlllcgapll ahstaiaaet tataatktya isagplnqql
       61 nqfaaqsgvy lvgdaqlttg kagkslqgny svedgfsall agsglqvipq pnsvwrlqri
      121 pqgdemlvva ginrngvteg tqsyttrsmn tatqlnlspr etpqsvsvvt rqrmddqnmt
      181 sldeamkqtt ginvvnqnsy qvkyesrafv mdnikedgvn fssqnsvsnm gavqsssesp
      241 dlaiydrvei lrgasglsqg ngepggtvnl vrkqpthnfq asgsigagsw dnyrseldvs
      301 gplnddaslr grlvgvyqdk qsfkdyehse rkvlfgtlay dltpsttvtg ginwqktrgv
      361 pdvygipfat nksslnlprs tylgaswnri efekinpfve lehhfdndwt lktalnyihs
      421 raassyigim ngtsgvnpat gtsslnnnlr ydnkaeqwgy nlslngpfel lgrnhelvvg
      481 gdyqkenfdn nhirinntss vnifnwqpns laepdwsnts lynnhyndrf nlyqrgafat
      541 arfeladdwk lilggrysay sydeyftnhl rntsslsslh asnefvpygg llwdfadnyt
      601 wylsyaeiyk pqsekdrngk llpaitgtny etgvkgeffd gdlntslalf riiqanraia
      661 vadssvclig tscsqaqgev rsqgveldvt gklaegwqiq agytltnsky legsaseraa
      721 qfsprtpkhm fklytsynlp gelnqwtiga gmtaqtetqt ypnrayglhq ggytlfnanv
      781 ryqysknlsf nlvgnnltdk tyylnlnnrh lsgnnyygdp rnfmltakwn f
//
LOCUS       WP_010301338             317 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Kurthia senegalensis].
ACCESSION   WP_010301338
VERSION     WP_010301338.1
KEYWORDS    RefSeq.
SOURCE      Kurthia senegalensis
  ORGANISM  Kurthia senegalensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Kurthia.
REFERENCE   1  (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   2  (residues 1 to 317)
  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 317)
  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 317)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Kurthia senegalensis"
                     /db_xref="taxon:1033740"
     Protein         1..317
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34322
     Region          1..69
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          242..307
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 maelgnrlke armakgysle dlqeitkiqk rylsaieegn fsvmpgafyv rafikqyaea
       61 vgldateile tykneipenr akeatsasta iqqpkggtnr rtnanqpsst ikttstssrk
      121 msdlmpkiav avivvaviai vwflfvhsas nedttpkvkq eqtqdqtttt tnkavdeqek
      181 aqkaadekaa adkaakekaa aekakkakaa gtlsegqdag dgatttytlt dtknfkvrvd
      241 mtgdnwvgit dqnggnlstg kmyakgdkle ydakdqsyir irlgaasygk vyvngkevkl
      301 avpasqrvtq niviktk
//
LOCUS       WP_010302619             168 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Pectobacterium carotovorum].
ACCESSION   WP_010302619
VERSION     WP_010302619.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium carotovorum (Erwinia carotovora)
  ORGANISM  Pectobacterium carotovorum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 168)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Pectobacterium carotovorum"
                     /db_xref="taxon:554"
     Protein         1..168
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18250
     Region          1..153
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mnkqefyqdl irdmssliad enrfitilsn ssallferld gvnwagfyll dndtlflgpf
       61 qgkvacvrip vgkgvcgtai aenriqrvdd vhafpghiac daasnaeivl plvvngqpig
      121 vldidstlyq rfdaddeegl kavvsvlcaq leasdvmtfi nsltlrqg
//
LOCUS       WP_010303791             159 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Kurthia senegalensis].
ACCESSION   WP_010303791
VERSION     WP_010303791.1
KEYWORDS    RefSeq.
SOURCE      Kurthia senegalensis
  ORGANISM  Kurthia senegalensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Kurthia.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Kurthia senegalensis"
                     /db_xref="taxon:1033740"
     Protein         1..159
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17266
     Region          8..159
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfeqttyegd laskytllsk qldalmtget delailsnas sllnqflsdv nwcgfylykn
       61 eelllgpfqg lpacvhiaig rgvcgtaaqt metqlvadvh afpghiacdg atnaeivvpl
      121 qkdgqlygvl didsptkdrf setdrvgiel fartlekfl
//
LOCUS       WP_010304238             118 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Synechococcus sp. CB0101].
ACCESSION   WP_010304238
VERSION     WP_010304238.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus sp. CB0101
  ORGANISM  Synechococcus sp. CB0101
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Synechococcus sp. CB0101"
                     /db_xref="taxon:232348"
     Protein         1..118
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12959
     Region          1..105
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(5..6,24..25,33,36,38..39,41,44..45,47,55,60,69)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(24,55..56,58,85)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 meptfdervq qvvaqippgq latygqigef igaygcarqv gwalrrlvlp sevpwhrvvn
       61 aqgrismsls regsdwmqre lllaegipvd eqgrlplsry rwlppgascv atsdalpc
//
LOCUS       WP_010305993             751 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Synechococcus sp.
            CB0101].
ACCESSION   WP_010305993
VERSION     WP_010305993.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus sp. CB0101
  ORGANISM  Synechococcus sp. CB0101
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 751)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 751)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 751)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..751
                     /organism="Synechococcus sp. CB0101"
                     /db_xref="taxon:232348"
     Protein         1..751
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=81098
     Region          8..708
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 malsstgsvr sqcpycgvgc glelmppaqp gqavkrdaeg npvwtargdr qhpssqgqvc
       61 ikgatvgdtl argrlseply rssldqdfqp iswdqafdll egrirstlaa kgpqaiamyg
      121 sgqfhtedyy laqkllkgal gsnnfdansr lcmssavagy trslgsdgpp ccyedldhcs
      181 vafligtnta echpvlfqrl lkrkkrtpkd vtvvvvdpra tdttkaadlh laikpgsdla
      241 llhgiahlvi aaggldadfi eeategladf aqlvasatpe rtaelcgise qqlrdvaalw
      301 arndrilslw smgvnqrreg tavvcglinl hlltgqigkq gagpfsltgq pnamggreag
      361 glahllpgyr lvanaehrae leaawrlepg siaaspglaa wqqveamerg eldlwwvvat
      421 nplvsmpnle rvkaamarcp lvvvsdayad tetahyahll lpasqwseka gamtnserrv
      481 tycpayrprh gqsrpdwevf aelgrrlgye qqftynssae vyaefaalta grvcdvsgls
      541 halldqegpq qwpfpqgsia ssdskrlyan gcfptpsgra rfvadpvlgl aeppcavypl
      601 vltvgrylgq whtmtrtakv drlqtmhpep lleihpndak rfgvvdgela avssrrgsvt
      661 akvlvsdrir pgsvflpmhw gfsqdqacea nvlmhdqacp iskqpelkat avvvapavsv
      721 vkpleqsegr lqrlrrlflq astsekaasr l
//
LOCUS       WP_010306411             275 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Pectobacterium carotovorum].
ACCESSION   WP_010306411
VERSION     WP_010306411.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium carotovorum (Erwinia carotovora)
  ORGANISM  Pectobacterium carotovorum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Pectobacterium carotovorum"
                     /db_xref="taxon:554"
     Protein         1..275
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=30631
     Region          36..188
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mlkwmvcial gllagcqsas slkeqnnyvl etavqsraqe srirflvihy taedfatsln
       61 iltdehvsah yliparpplq rgkplawqlv pesqsawhag asswrgfsrl nnssigieie
      121 nagyqrtltg ytwepftasq iqlvtaiacd ivdryqiapq nvvahsdiap qrkqdpgplf
      181 pwqalaqagi gawpdaqrva fylngrptmq pvdeavllek lgrygysvqd mmtarekrqv
      241 iaafqmhfrp enyqgqpdaq seaivdalle kygsr
//
LOCUS       WP_010310499             305 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Saccharopolyspora spinosa].
ACCESSION   WP_010310499
VERSION     WP_010310499.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            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="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32477
     Region          1..299
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mlvdsaglwf rsyyalpdsl tapdgtpvns vrgfcdmlak litdrrpsrl vacldndwrp
       61 qfrvdalpsy kahrvaeddp aaeevpdtls pqipvilevl daagiataea egyeaddvig
      121 aladredrdp vevvtgdrdl fqlvrtqpta vrvvyvgagl akaqdygpae laekyalsad
      181 ragddyaema vlrgdpsdgl pgvagigekt aaklitqfgs leallaaaes adsrltprir
      241 gklaeaadyl aaapsvvrva rdapvvqdrp dalpqspvdt drlrelqraw glgasidrli
      301 aamtp
//
LOCUS       WP_010315122             127 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Synechococcaceae].
ACCESSION   WP_010315122
VERSION     WP_010315122.1
KEYWORDS    RefSeq.
SOURCE      Synechococcaceae
  ORGANISM  Synechococcaceae
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales.
REFERENCE   1  (residues 1 to 127)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Synechococcaceae"
                     /db_xref="taxon:1890426"
     Protein         1..127
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=13916
     Region          8..126
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(78..79,82,99..102,104)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mveliasivv dlsdqklyvy nqqqelvrtv lvstgkgstp tpmgvgqvyd kyrsvtmrgr
       61 gyvapnvpwa mcitqngmic mhgapwqeqa neafgvprsh gciripspha rwlfentpkg
      121 tpvsiqa
//
LOCUS       WP_010317452              99 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Vibrio ordalii].
ACCESSION   WP_010317452
VERSION     WP_010317452.1
KEYWORDS    RefSeq.
SOURCE      Vibrio ordalii
  ORGANISM  Vibrio ordalii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 99)
  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   2  (residues 1 to 99)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Vibrio ordalii"
                     /db_xref="taxon:28174"
     Protein         1..99
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10646
     Region          38..98
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mklktklgll llsivlplsp elaeekvvet hqgieitvni nqdsaeeiat llkgiglkka
       61 qaiveyrqqn gafktkedls lvkgigaatv kqnaeriil
//
LOCUS       WP_010319440             416 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Vibrio ordalii].
ACCESSION   WP_010319440
VERSION     WP_010319440.1
KEYWORDS    RefSeq.
SOURCE      Vibrio ordalii
  ORGANISM  Vibrio ordalii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 416)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 416)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Vibrio ordalii"
                     /db_xref="taxon:28174"
     Protein         1..416
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47186
     Region          2..415
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 msreivevya dwqpieapll igllsysdss rggvfsfayd kafltsayrl qidpilslhs
       61 gelyndeadk nfrafldssp drwgrilmqr raaiearkgi ratsrlneld yllgvhdsyr
      121 mgwirfkrvg sdaflddnse faappmaslr elehaamqie kddnidsdey yrwlkmlisp
      181 gsslggarpk acvtdeqghl wiakfpnlnd thdvgawemv cyelalaagv dmypseikqf
      241 ssqhhtfltk rfdrdgekrl hfssamtqlq yydgeqsqga syleiaefis nsgaqteadl
      301 aqlwrrivfn iavsntddhl rnhgflltkn gwklspaydl npivgkhglh lnitdadntl
      361 dyqlafdvkd lfrlsqtqat qiydevliav kqwqtvakrl gisraeqamk qsafnv
//
LOCUS       WP_010319678             152 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase, partial [Vibrio ordalii].
ACCESSION   WP_010319678
VERSION     WP_010319678.1
KEYWORDS    RefSeq.
SOURCE      Vibrio ordalii
  ORGANISM  Vibrio ordalii
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Vibrio ordalii"
                     /db_xref="taxon:28174"
     Protein         <1..152
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
     Region          <1..65
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 gvtttfspyh pqqiaalksl ainilqrypd vsptniighs dvspgrksdp galfpwkely
       61 lsgigawyde etktkyckkf qtnlpnkndi leklktygyg ttktedaqvy qqlirafqlh
      121 frpenysgkv dietvailys lvdkyksspr st
//
LOCUS       WP_010322901             403 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Marinobacterium
            stanieri].
ACCESSION   WP_010322901
VERSION     WP_010322901.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium stanieri
  ORGANISM  Marinobacterium stanieri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 403)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 403)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Marinobacterium stanieri"
                     /db_xref="taxon:49186"
     Protein         1..403
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44687
     Region          7..396
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mtnlvstlnv llhgepvgti tnvghdrtlf aftdgyinde srpvlglgfk dslgglltdf
       61 kptqtrllpf fsnllpeerm rhylaeragv npareffllw algqdlpgai tvepangeal
      121 ppnyhnetqg dpkreapmrf slagvqlkfs avqqakgglt ipatgqggsw ivklpssrfe
      181 avpeneysmm elarmlgmdv petqllpinq ianipegigq fgesafvikr fdradgraih
      241 iedfaqvfgv yphdkyqkas mrniaqvlgi egqdediaef trrlvfntli gnadmhlknw
      301 sviykdkhta siapaydfvs tvpyipddsa alkvsrskkf sdftldelsh laakamlpek
      361 wvleiaketv agfnevwake kahlpltqsm ieaierhqrs ipi
//
LOCUS       WP_010323275             342 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Marinobacterium
            stanieri].
ACCESSION   WP_010323275
VERSION     WP_010323275.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium stanieri
  ORGANISM  Marinobacterium stanieri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 342)
  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 342)
  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 342)
  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 342)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Marinobacterium stanieri"
                     /db_xref="taxon:49186"
     Protein         1..342
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=37025
     Region          1..337
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkmrvlsvav ttaiwaagvq aakvsmdvqs awpltlpasg qnaahfaeri netgagslkv
       61 klysagklvp plqifdavqq gsldagytsp lyvagrfpav qlfggvpfgp damdylgwly
      121 ngggleiwre iyakqgvvpv pcglmdseag gwytfeintp adlkgkkirf aglagevmkk
      181 agasvvllsg gdiypnlerg vidgtefsmp aidaamgfek atkyyylpgw hqpaaineli
      241 inkrkwdamd daqrgliedt crethiwsit sttvpnaeai akfkaagtei rsfpdevmtv
      301 frkaadevma eqaaedadfk rawdslqayr dktalwsthk ad
//
LOCUS       WP_010323313             138 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Marinobacterium stanieri].
ACCESSION   WP_010323313
VERSION     WP_010323313.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium stanieri
  ORGANISM  Marinobacterium stanieri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Marinobacterium stanieri"
                     /db_xref="taxon:49186"
     Protein         1..138
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14592
     Region          1..138
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mnilhrskgf tlveimvava ivgimaaial payfqyvtda rrsdgranll qlaqfmeryy
       61 tangryvdag gnapalpfte aprdgadkfy dlalgvitaq tytltatpkn alagdacgtl
      121 tlnqagvrga ggnidecw
//
LOCUS       WP_010323881             141 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Marinobacterium stanieri].
ACCESSION   WP_010323881
VERSION     WP_010323881.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium stanieri
  ORGANISM  Marinobacterium stanieri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Marinobacterium stanieri"
                     /db_xref="taxon:49186"
     Protein         1..141
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15472
     Region          7..140
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 miealpaplt lffsalvsst llpggseall awllnqnqys awtlwlaats gnvlgslltw
       61 gmgywiarry plktldkpgh qrardwlqky gpaslllawl plvgdplclv agwlrfnfll
      121 slvmitlgka lryalivglf s
//
LOCUS       WP_010324560             183 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Marinobacterium stanieri].
ACCESSION   WP_010324560
VERSION     WP_010324560.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium stanieri
  ORGANISM  Marinobacterium stanieri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 183)
  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 183)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 183)
  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   4  (residues 1 to 183)
  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   5  (residues 1 to 183)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Marinobacterium stanieri"
                     /db_xref="taxon:49186"
     Protein         1..183
                     /product="TRAP transporter small permease subunit"
                     /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=20615
     Region          7..175
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 msqphpvtgl irfldgfsew tgrliawltl lmvistfvvv vmryvfeqgn ialqesvvym
       61 hsfvfllgaa ytlkhdghvr vdiiyrplse kgkawinlfg tlflllpvci flfwisweyv
      121 atswelkegs qeagglayry ilktallamp ammilqaiae llrslmvlag kshlppaeee
      181 hal
//
LOCUS       WP_010325077             263 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Marinobacterium stanieri].
ACCESSION   WP_010325077
VERSION     WP_010325077.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium stanieri
  ORGANISM  Marinobacterium stanieri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Marinobacterium stanieri"
                     /db_xref="taxon:49186"
     Protein         1..263
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=28746
     Region          18..230
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mydispaill dflggigigv eyqpivsttd rrvlgheala rfrvngggrl ppdrvfralh
       61 dsplslfqme yrikqlqlqh apdsenlfln idqdafevfl nepvhpmval lehragtvve
      121 iienssvsda qvsiamqqaf ggaglplald dvgaqdslvs fdllagveyv klardwlcrl
      181 tgqgadalfa alisfarasg ktvilegven eqqfararel gvdavqgflf rddfiqawqp
      241 dagandrldg rqleawlkpc rsa
//
LOCUS       WP_010325185             232 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Marinobacterium stanieri].
ACCESSION   WP_010325185
VERSION     WP_010325185.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium stanieri
  ORGANISM  Marinobacterium stanieri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 232)
  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   3  (residues 1 to 232)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 232)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Marinobacterium stanieri"
                     /db_xref="taxon:49186"
     Protein         1..232
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25476
     Region          26..226
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mtdlsrilgn eltslaelap avgesirldv rapnqklsar llgyrepgsl mvsapklapg
       61 gaivhegtrm sarmmignyl ctfetrlvqv qsrpfgywhl eyparvesrr lrketripin
      121 lsvrveqdel slgasavsav crdislqgan lessralaqp eeqlfitlrv svagmdhlll
      181 lpalvrnvqq letgpvpvfs qgvefvdlee dtrlilagfv yeqqlqnagl ie
//
LOCUS       WP_010325923             264 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: hydroxypyruvate isomerase family protein
            [Acinetobacter].
ACCESSION   WP_010325923
VERSION     WP_010325923.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..264
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29398
     Region          1..257
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 msklavnlsm iftevpller falaqavgfk hveiqfpyel sieqiqtqlt lhdlslclin
       61 vpagdlmtgg nglagvpgke lefhhalqla vqyasalkvp svnilagkqp ldadllpcln
      121 tlsknlklac hmfsehdiqp vfemingtdm prflvqniaq aqemleavqh palkmqydcy
      181 hmammgedvl qglqeniqdi ghiqfadcpg rhepdtaqim yanifewlqh ssydgfiaae
      241 yrpktvstqs fawkakyfat hpqs
//
LOCUS       WP_010325336             704 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Marinobacterium stanieri].
ACCESSION   WP_010325336
VERSION     WP_010325336.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium stanieri
  ORGANISM  Marinobacterium stanieri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 704)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 704)
  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   3  (residues 1 to 704)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..704
                     /organism="Marinobacterium stanieri"
                     /db_xref="taxon:49186"
     Protein         1..704
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=74951
     Region          6..703
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msldvdqeil edflveagei leqlseqlvd leqrpddkdl lnaifrgfht vkggagflql
       61 damvecchka enlfdllrng elavsanlmd vvlqaldsvn amfesvrsgd epehaspqll
      121 qalkdyaegk ggevppvaap asapaapppa papqapaeaa ssnpntpsde femllgdlag
      181 shaeggdaps ggddelited efeslldelh gpgkgpvhtp easgdapaag stgedlitdd
      241 efealldelq ssgqgafahl phdeaasaaa papapvapep qpapvepvaa aapvvaepek
      301 pkdtaskaaa kankppaesn vrvdtrlldk imnmvgelvl vrnrlvrlgn tredeemaka
      361 lgtldmvtad lqtsvmktrm qpvkkvfgrf prlirdlsrs lkkevrlelr geetdldknl
      421 vealadplih lvrnavdhgi edpdqrassg kpreghvlls aeqegdhill iiqddgagmd
      481 peklrnlavk rgmmdaeaar rltdqecfnl ifqagfstkt eisdvsgrgv gmdvvktkit
      541 qlngtlsids ilgqgtriai qvpltlaimp tlmvvlegqa falplvnvne ifnldltktn
      601 ivdgqqviiv rdqalplfhl krwlvkgqsg aelpdqghvv ivsvgttrvg fivdqlvgqe
      661 evvikplgsi lhgtpglsga titgdgrial iidipnllky yast
//
LOCUS       WP_010327277             107 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Acinetobacter].
ACCESSION   WP_010327277
VERSION     WP_010327277.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..107
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11803
     Region          12..106
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(28,59..60,62,89)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(28..29,37,40,42..43,45,48..49,51,59,64,70)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 maesivkela pmifqviaqi pygrvasygq iarlagipkh arlvgyvlkh mdadsslpwy
       61 rvinsqgkis lsklndqgqn iqaqlllaeg ilvigdkvkm kefqwni
//
LOCUS       WP_010331847             292 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Bacillus].
ACCESSION   WP_010331847
VERSION     WP_010331847.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..292
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33015
     Region          14..256
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mdavleadtr avigegplwd eengrlywvd ilgselhifd pkekinrsvk ftsfvtalak
       61 yskdelimtm kdgfylyhlh ddslekikqp kdmheslrfn dakcdpygrl wagttsmege
      121 qkqaslyrld adgslvkmkd qvstsngldw drernlmyyi dtptqeivcy qydpesgnvs
      181 npetvyrfek sdglpdgmti dqngmlwval fggsrvvhid pfqkkeidsi svpakyvtcc
      241 afggqdmktl yittateqmt eteryeqpha gglfsarlet ggyqpvpfag el
//
LOCUS       WP_010333994             340 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Bacillus].
ACCESSION   WP_010333994
VERSION     WP_010333994.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..340
                     /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=39256
     Region          3..272
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mnksrdsyfd nakflliflv vfghilrsfi hdnnfmlyly kfiytfhmpa filvsgyfak
       61 gfkragyvkk lavkliipyl ifqsiysvfy yiiqdesmtn mnpidpqwsl wflvslffwn
      121 illypfskls kqwalfvscg iavligyldf vsstlslsrt fvflpmflvg fylnkhhfdl
      181 lrskrgkqia lgvlaavfvi cwgvdfdysw lfgskpyssf gdvtlasgls riswyvlafa
      241 atfsflalvp qkryfftkwg trtfyvyllh gfiiktlrqv gledgltdyq nlvillllta
      301 altsilssnf vktvaqpfie lrmtgllqlv rgnsknaylk
//
LOCUS       WP_010334113             521 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Bacillus mojavensis].
ACCESSION   WP_010334113
VERSION     WP_010334113.1
KEYWORDS    RefSeq.
SOURCE      Bacillus mojavensis
  ORGANISM  Bacillus mojavensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 521)
  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 521)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Bacillus mojavensis"
                     /db_xref="taxon:72360"
     Protein         1..521
                     /product="M4 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=56649
     Region          44..520
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mglgkklsvv vaasfmslsi glpgvqaaen yqlkenqtnf lpksaiaqte lsapndkavk
       61 qflkknskvf kgdpakrlkl vesttdvlgy khfryvpvin gvpikdsqvi vhvdksdkvy
      121 aingelhnqs asktnnskkv ssdkalalaf kaigkspdav sngsaknsdk aelkaveted
      181 gsyrlaydvt iryiepepan wevlvdaetg silkqqnkve haaatgsgtt lkgatvplni
      241 syesgkyvlr dlskptgtqi itydlqnrqs rlpgtlvsst tnkfttssqr aavdahynlg
      301 kvydyfystf krnsydnkgs kivssvhygs qynnaawtgd qmiygdgdgs ffsplsgsld
      361 vtahemthgv tqetanlvye nqpgalnesf sdvfgyftdt edwdigedit vsqpalrsls
      421 nptkydqpdn yadyqnlpnt degdyggvhi nsgipnkaay ntitklgisk sqqiyyralt
      481 tyltpystfk dakaaliqsa rdlygstdaa kveaawnavg l
//
LOCUS       WP_010335312             162 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Bacillus].
ACCESSION   WP_010335312
VERSION     WP_010335312.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 162)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Bacillus"
                     /db_xref="taxon:1386"
     Protein         1..162
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17613
     Region          7..162
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfhveqqsgd kekdyqlllk qleaitedet dqianyanas allyhslpev nwagfyfake
       61 gegqlvlgpf qglpacvrip fgkgvcgtay angkvervad vnafpghiac daasqseivl
      121 pihvdgnlvg vldidspvkn rfdeidekyl sqfvktleka la
//
LOCUS       WP_010335672             559 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Sphingobium
            yanoikuyae].
ACCESSION   WP_010335672
VERSION     WP_010335672.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium yanoikuyae (Sphingomonas yanoikuyae)
  ORGANISM  Sphingobium yanoikuyae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 559)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Sphingobium yanoikuyae"
                     /db_xref="taxon:13690"
     Protein         1..559
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=59764
     Region          1..543
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mavirtlcgr cgvgcglrai tgedrdlmve gdrmhpanag rlcgrgleia eevglegrll
       61 qpmidgrpqr wekaiaqvar rlsavigqhg pdsvalhvgg glltedyyva nklmkgfigs
      121 ahvdagwaan dgaalaqhaa ygedvmpaay edieraelil migadlaqdh pvlnariaaa
      181 raeqgvells lappgegtsv eadlridvpr egmaawiagl lrhchdtgat dgdylarsvs
      241 vpddfwaqlr trhdlwsvar gcglspvelr alydriaavp rivtlfggad eglaravidf
      301 hlatgrigrp gaapfamtaa angmggrevg cnatglaahr gftaeamaqv grfwsaeama
      361 tgpgldgaql aeavrggrir alwsisgdgi dpawlraald avplairstp wadperdgrg
      421 ialpsaswve kdgtltgadr lisrqrrlfp lpgdakpdww ivtqvaramg wqaafhyewa
      481 aeiyrehvrl taygnegarl lnlrrhapis npayeeltpw rwgelpfdeg rfptpdgkar
      541 llppvlggrs pgdgaptrq
//
LOCUS       WP_010336121             563 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: amidohydrolase family protein [Sphingobium].
ACCESSION   WP_010336121
VERSION     WP_010336121.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 563)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..563
                     /product="amidohydrolase family protein"
                     /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=62057
     Region          63..531
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mknkmlirss laalalmtva sashahdpde wyvggaagiv ngkkptfvpa pargsadnvg
       61 pfrklvirga tlidgtgapp rgpydivveg nkitaitqag wpglpqakgr aptdadyeid
      121 atgmyvmpgf ndmhvhtpas dkapdmsyay klwlahgvtt vrgvpladpv vasseknrsa
      181 aneiaaprif nyqtlgagwd ggpidspdka rawvkwaaah nidgikffnr peetpqiiaa
      241 aideahknkm gttahlsqtg vanfnaydaa eagldtvthy yghfesllkd gtiqrfpsdy
      301 dynneqhrfg evaeiwnqtv epeserwwdy lkhqkekhvt fdptmniyaa srdlmrarna
      361 dwqnlyttpq lwayfqstrd nhgsyfydwg tenefawkkf ynnyfklvnd ykniggrvtv
      421 gtdsgfiykv ygfayieele llreagfspl eimrsatmwg sqtlyepkgm apptgvlrvg
      481 mladmvitke nplanlktly gtghsrlnpe tnkqemvggv sytikdgivy dakkllaeva
      541 emvkaekart gqagagpanp nam
//
LOCUS       WP_010338091             286 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Sphingobium
            yanoikuyae].
ACCESSION   WP_010338091
VERSION     WP_010338091.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium yanoikuyae (Sphingomonas yanoikuyae)
  ORGANISM  Sphingobium yanoikuyae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Sphingobium yanoikuyae"
                     /db_xref="taxon:13690"
     Protein         1..286
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31350
     Region          16..257
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mtawrkierg eirdtlgegt lwsarenavy wvdilapaln rlsldegqvs rwampeplgw
       61 vaeraqggfi ggfqsgfasf tldplaitpi hdpephlpgn rmndgkadkd griwcgtmdm
      121 aegqdvgaly rldpdgsvtv mddgyrvpng pafsacgeyl yhsdtgrrim yrfrrgpdgt
      181 ihdrqpfitf teadghpdgm tvdaegylwv ahwggsrisr fspegkldra ielpakqvtn
      241 itfagpdldr mfvssaaigl pesdydgaff evecgvkglp tnlyag
//
LOCUS       WP_010336144             413 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Sphingobium
            yanoikuyae].
ACCESSION   WP_010336144
VERSION     WP_010336144.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium yanoikuyae (Sphingomonas yanoikuyae)
  ORGANISM  Sphingobium yanoikuyae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 413)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 413)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Sphingobium yanoikuyae"
                     /db_xref="taxon:13690"
     Protein         1..413
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44260
     Region          9..405
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mtaartaeti taldvflnsa kvgtivrtpg dfnafsldpa yratggipvl slslraasgg
       61 lrkdprpvag slppffanll pedrlreame khhagnvrpg ndfdllaalg adlpgavrvl
      121 psdgqpgiga apsqgrpkar fslagvqmkl svmkntgkgg gltlplgdde gqyiakfpst
      181 afpgvsenef anlalaeaig mdvperelvs rdqfegipee fetlaeglvl lvrrfdrgtd
      241 gqrihiedfa qvfglypark ydgaashdia svlnvaispf aalefvrrlt fsvimgngdm
      301 hlknwsliyp gdgdrpalap iydmlstvpy ipadglalsl ggerafkgla parwkafanr
      361 arlpepavlk avvetvkrid akwwtlperk vvpplvleri dahvktmipi ltg
//
LOCUS       WP_010338097             632 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Sphingobium yanoikuyae].
ACCESSION   WP_010338097
VERSION     WP_010338097.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium yanoikuyae (Sphingomonas yanoikuyae)
  ORGANISM  Sphingobium yanoikuyae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 632)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 632)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 632)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 632)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Sphingobium yanoikuyae"
                     /db_xref="taxon:13690"
     Protein         1..632
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68015
     Region          8..632
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mteqgdpaag qdrtphgrpa alalgalgvv fgdigtsply alkesfvghh pltvdplhiy
       61 gvlslifwtm tlivtvkyvf ivmradndge ggsmallali grrlgetrwt paiamlgvla
      121 talfygdaii tpaisvlsav egltivqasl admvlpiaiv ilialfliqr fgtamvgmaf
      181 gpimaiyfvt laalgianiv qhpeiigivn plwairffai dprlaflalg svvlavtgae
      241 alyadmghfg rkaisiawly aafpclmlny lgqgallldn paaaqnpffl mapdwarlpl
      301 vilatmatii asqavisgaf svtqqavqlg flprlrilht sasaagqiyv plinwlllif
      361 villvlgfgn ssnlaaaygi avtgtmvita cmlgvltfsv wrwplpaaag vtglfliidg
      421 ayfasnvtki pdggwfpllv aavvftvltt watgrrimrh ylregameld lfvrstlasl
      481 krvpgtaifl ssttdgvppa llhnvkhnkv lherviiltv rtqgvphlpl qgrttvedhg
      541 sgfyrlilrh gfmedvdipa amksvhdcgg pisvkdtsyf lsrqtlipse rpgmamwrek
      601 lfawmirnae spmaffnlpt nrvvelgsqi ei
//
LOCUS       WP_010338189             291 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Sphingobium].
ACCESSION   WP_010338189
VERSION     WP_010338189.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..291
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29511
     Region          3..246
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mliaylgtgd dyvllgprea iiragdgrdr liggamhddf rgdggddvlf grgggdsldg
       61 gagtdlilgg agaddivgad gadrlyggdd rdtlsggngd drihgdagdd ilyggsdadi
      121 mfgddgadil wgewgddrlh ggsgndqldg gegrdivdgg agddavagga gndriygglg
      181 adrllggagk drfvwrdlae ggdtvrdfeq gvdrlvvagr avgglssvdd snfssnangv
      241 aidandrfly aqdsrmlffd pdgsgaapat liaqiqfsvg iqlyasdivi g
//
LOCUS       WP_010339088             331 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Sphingobium].
ACCESSION   WP_010339088
VERSION     WP_010339088.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 331)
  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 331)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..331
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37314
     Region          24..200
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          243..324
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mdeqrdafea inahmlrflp elvaelggda pdsgdaspsy rqtialieda ahrlacpdfg
       61 mrlalrqrgv dlfgplgdam rnaptfgaai dyvcshnyah slaaavwlrr fpsvrhvfvg
      121 hdillegvpn raqamehill vghlfamelt ggrararrvh frhqpispar iyrryfgcpv
      181 hfgqnedgis fserdmaspv idrdaaifaa vtayierefp hrhpplhaqv rgivmqwlwt
      241 ahcsndrvaa elglhprtlh rrlategtsf qkikdevrrd ilryyleqtd mdfahvsekl
      301 gfseqsvmtr scnhwfgasp trlrarlhap a
//
LOCUS       WP_010339119             440 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Sphingobium yanoikuyae].
ACCESSION   WP_010339119
VERSION     WP_010339119.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium yanoikuyae (Sphingomonas yanoikuyae)
  ORGANISM  Sphingobium yanoikuyae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 440)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Sphingobium yanoikuyae"
                     /db_xref="taxon:13690"
     Protein         1..440
                     /product="amidohydrolase family protein"
                     /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=47656
     Region          2..392
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mlvadgriaa igaklkapas arqvdgrgry llpgfidsnv hatvygnpar rdtssryadr
       61 neelalefaq rqlragvttm rdsygvlppl lavrdriasg qaigarmlva gnilgwggpf
      121 sltysltgdr dltlfqeqwn dmlaqgmgee lmdmtpeqlr aavsayldrg vdflkyggts
      181 hfmmpsligf sprqqaviva eahkrgkmae thatsseglr laveagidli qhpeilsrdy
      241 pddlialils kgtlcamrsn mvtgavrqkq iarraravad iaqmppalts telrrraamr
      301 gddaeierrn aerlvaagcp vtiatdnylg dapefrrspk speqepgegs llaieglvel
      361 gmtpmqaiva atrngaraag rlqdlgtvep gkiadlllld adpladihni rrlgrlfvag
      421 qeidlqtlpq thlfmvadkr
//
LOCUS       WP_010340168             266 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Xanthomonas sacchari].
ACCESSION   WP_010340168
VERSION     WP_010340168.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas sacchari
  ORGANISM  Xanthomonas sacchari
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Xanthomonas sacchari"
                     /db_xref="taxon:56458"
     Protein         1..266
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=29197
     Region          37..184
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mtrvpvpsls avrrllllgt lallgacaha pqrnplatwv pspnydarrp ilivihytdq
       61 hsvqqsldtl rshnskgkvs ahyligrdgt ryqlvadqdr awhggagrwg titdinsasi
      121 gieldndgkt pfaqeqiasl lvlledlctr lriprtqvvg hedfapsrkv dpgplfpwkr
      181 laeagfgrwp aadtppappg fdpwqalali gypvddraat lrafhhhyrg ndatdfdaed
      241 lrilyaltqp llarpqpvpa mepdas
//
LOCUS       WP_010341206             411 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA, partial [Xanthomonas sacchari].
ACCESSION   WP_010341206
VERSION     WP_010341206.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas sacchari
  ORGANISM  Xanthomonas sacchari
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 411)
  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   3  (residues 1 to 411)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Xanthomonas sacchari"
                     /db_xref="taxon:56458"
     Protein         <1..411
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          <28..411
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 paaastpaaa attaasagpa kaagargegg sirvdadkld rmidlvgeli iavastgana
       61 qrtgdaqlle stsilaglve evresalqlr mvkiggtfsr fhrvvhdvar elgkdialvv
      121 ngedteldks vvekiadplt hlvrnamdhg iepaevrqar gkpvrgtvrl nafhdsgsiv
      181 iqisddgggl nrdrilakal ergliepgrq lsdrevfali fepgfstaek vtnlsgrgvg
      241 mdvvkrniaa lrgsvdissq qdvgttisvr lpltlaiing fqvgvgksvf vvpldvveec
      301 vefapnyqse yidlrgnvlp yvrlrslfai agapparesi vvirqgaqrf glvvdtllge
      361 wqtvikplsk vfaqvkgisg ssilgsggva lildvpsllg qlqpgaesla a
//
LOCUS       WP_010341427             645 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Xanthomonas sacchari].
ACCESSION   WP_010341427
VERSION     WP_010341427.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas sacchari
  ORGANISM  Xanthomonas sacchari
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 645)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 645)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 645)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..645
                     /organism="Xanthomonas sacchari"
                     /db_xref="taxon:56458"
     Protein         1..645
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=69377
     Region          103..630
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mpandtapls predtrarhv raetppphyw rrwvgdaara tpadvasaag iadpastaat
       61 adatppagne hddgaadana aafvvanata dssaqaaaaa pyrvlivedd raqalfaqsv
      121 lhgagmhaqv qmqaegvqqa iadyrpdlil mdlhmpgldg mrltalirqq pqhqllpivf
      181 lsgdadpele yevldsgadd fltkpirprh liaavsnrir rarqqaqhgh aeaaplnnpe
      241 tglptrahvl qlldttlrah rpgslyfiei asalglrery gyaaferlmv qagrrlagvt
      301 apqplarlnd nsflllaeda eadaqlqcaq rlrdalsgha fplredealh lrcaigyadf
      361 ghgfedagsa leavertalq arlqpqgiaa yvppradedl qriamlegql epayqpivav
      421 aggdiaqyqv llrlrqrdgs llsagqvlpa aeaggriadl dqqvldhalg llhlyqhatp
      481 plrlfvsqss rtlartafae wlidtigrrg vtgtslvidl rlddalvhta tlqqfcarlm
      541 plgvqfcvsq fepgaeaeal lahlplgylr lsarfagaha dpelrdqlra tidlahragl
      601 liigqqieqa qaaaamwmgg vdfiqgnlvq svgdqlnfdf qnavl
//
LOCUS       WP_010341527             204 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Xanthomonas].
ACCESSION   WP_010341527
VERSION     WP_010341527.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..204
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22337
     Region          3..171
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mkifgplyer aigwsrhrra palltglsfa eaivfpvppe vmlapmslaq prralwfatl
       61 sllgslagal igyllghfaf aavqpliewl gwtqkidaqv shlreviaes pwrafwllvl
      121 agftpiplki ftwasgivgv pllpflasml vgrgkrvylv agairlggpr aeaalrrwie
      181 plgwvasail allvvwviwr akfg
//
LOCUS       WP_010343482             382 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Xanthomonas
            sacchari].
ACCESSION   WP_010343482
VERSION     WP_010343482.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas sacchari
  ORGANISM  Xanthomonas sacchari
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 382)
  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 382)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Xanthomonas sacchari"
                     /db_xref="taxon:56458"
     Protein         1..382
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43266
     Region          6..380
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mrtpvasvpi apdraralwl haqrlttpap fgsgaeavrq atahlgyvqi dtihviarsh
       61 hhvlytripe yrerdleqaq sqdkslfeyw thalayvpva dyrmyvaqma rrraqadarg
      121 avdaqdyarl lrrirsegpl sirdidddvl vekthpwgsr kpsraalqyg ffsgdlvisq
      181 rsgmlktyel aarhfgwrqr prpvsdaqya ryllqralra qgivgvesic ygetaakpav
      241 raliaaevar krlipvhlqg qegvalwaep elldsvpppp dptralllsp fdplviqrkr
      301 lqqffsythr feayvpapqr vlgyfalpvl vgdrivaald lkmdrragrl liqqwtwlvp
      361 rraalqatid aalqrferfh la
//
LOCUS       WP_010343825             160 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Xanthomonas sacchari].
ACCESSION   WP_010343825
VERSION     WP_010343825.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas sacchari
  ORGANISM  Xanthomonas sacchari
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Xanthomonas sacchari"
                     /db_xref="taxon:56458"
     Protein         1..160
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16963
     Region          8..160
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfasssltgs kpeqyaqlld qaralvagep drianaanla alvyhalprl nwvgfylydg
       61 kelvvgpfqg lpacvriplh kgvcgaaast gqtqriddve afpghiacda asrselvvpl
      121 lrdsalvgvf dldspdlarf daddqrglea iaqvfvdslr
//
LOCUS       WP_010344016             456 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein, partial [Xanthomonas sacchari].
ACCESSION   WP_010344016
VERSION     WP_010344016.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas sacchari
  ORGANISM  Xanthomonas sacchari
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Xanthomonas sacchari"
                     /db_xref="taxon:56458"
     Protein         1..>456
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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]"
     Region          16..>456
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mrgrwkrlll gtlllavaiv lgvwlllrgs latldgkapl qglqapvsiq rdalgtvtie
       61 aadeadamra lgyvhaqerf femdllrraa agelselvgp halgvdkarr aqrlrarsna
      121 qlaafagtha aalqaysagv nqglhalrvr pwpylllfaa prdwqpvdsa lagqamyfdl
      181 qgkqldrkle lyrlqqrlpa plyallrhdg sswdaaldgs avgdavlpda gqvdlrrlpd
      241 gaaqanadav apaapgsnnw aiagsrtadg raivandmhl alrapslwfr vrlryadaqa
      301 pggrvdvsgf slpglpaviv gsnghiawgf tnsyadtadw yrltpcaatp qpgctpvtvh
      361 nerirvsgap dtvlqvedta ygpilqhepd gsalalrwaa qlpgalnlgl adfaratslp
      421 dafaraqria tpaqnlvlad rdghigwrvl gplplr
//
LOCUS       WP_010345256              82 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Paenibacillus peoriae].
ACCESSION   WP_010345256
VERSION     WP_010345256.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus peoriae
  ORGANISM  Paenibacillus peoriae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 82)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 82)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 82)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 82)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Paenibacillus peoriae"
                     /db_xref="taxon:59893"
     Protein         1..82
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8689
     Region          4..82
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mkyhiqvfag laehmggpmi tvpteqeamt itelkgllse rfpeaaaqlq safvaknqvy
       61 aapeelvsih deiaiippvs gg
//
LOCUS       WP_010345766             220 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Paenibacillus peoriae].
ACCESSION   WP_010345766
VERSION     WP_010345766.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus peoriae
  ORGANISM  Paenibacillus peoriae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Paenibacillus peoriae"
                     /db_xref="taxon:59893"
     Protein         1..220
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=24094
     Region          12..207
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mnsnqvsshq gkrivigitg asgsiygvrl vetlldlqyt vhlivsnagw rvlkeelgwn
       61 vtdregalne qfggrpgslv yhpftdigas iasgsylvda miimpcsmgt lsavahgssd
      121 nlmaraadvm mkegrplilv pretplhaih lenmlklarl gvkmipampa fyfhpktldd
      181 ivlflvgkvl dslriehqlf trwgdsdant gqqddhyrkn
//
LOCUS       WP_010345813             398 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Paenibacillus].
ACCESSION   WP_010345813
VERSION     WP_010345813.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..398
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43536
     Region          1..398
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkilvinags sslkyqlydm tdesvlakgl verigmdssi lthkptgkee ytevseileh
       61 ttavrkvlna ltdaehgvis svseieavgh rvvhggeifk qsalitpeak seirrlfdla
      121 plhnppsmmg iraaeanmpn vpqtvifdts fhqtmpekay myaiprvlyn kykvrrygah
      181 gtshdfvske aakflgrple dlkiitchig nggsitavkg glsvdtsmgm tpleglmmgt
      241 rsgdldpaiv pyvmnkeelt vnevnsmlnk hsgllaisgi ssdmrevteg mekgdanstl
      301 afemyeyrlr kyigsyaaam ngvdvivfta gvgensavlr krvleqltfl gielddslna
      361 irsgeprrit tanskvevlv iptneelvia rdtfrlvq
//
LOCUS       WP_010345349             394 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Paenibacillus peoriae].
ACCESSION   WP_010345349
VERSION     WP_010345349.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus peoriae
  ORGANISM  Paenibacillus peoriae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Paenibacillus peoriae"
                     /db_xref="taxon:59893"
     Protein         1..394
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43325
     Region          1..277
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          274..363
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrilhtgdwh lgrtlegrsr lkeqeaflee lakmaddqqa dlimmagdvy dsvnpsaaae
       61 qlfyeasarl taggrplvvi agnhdqperv ssvtplvsgr gitllglpsg qavrvhtprt
      121 gemaciaalp ypsesrlnel lsedgdetvl reaysrrvgl lmaqlgtafq pdtvnlsmsh
      181 iyvlgglesd serpiqvgga ytvdpsalsi gaqytalghl hrpqyvkgdg lmrysgspla
      241 ysfseagqak svtlidvvas kpaqveelyi tsgrplvrwr arggleevyr wldegldmda
      301 fidleitlde amsmgdiqrl rksregiihi rplypemaaa qlehqrselp vhelfrafyq
      361 rqtggaqpdd glvqlflelv eqdnardhae eedv
//
LOCUS       WP_010347452             417 aa            linear   BCT 20-JAN-2025
DEFINITION  TerD family protein [Paenibacillus peoriae].
ACCESSION   WP_010347452
VERSION     WP_010347452.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus peoriae
  ORGANISM  Paenibacillus peoriae
            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 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Paenibacillus peoriae"
                     /db_xref="taxon:59893"
     Protein         1..417
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=45259
     Region          32..417
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mavivvkgqk adltktnpgl thvnvgigwe spaaleldts afllgpggkv sgdedlifyn
       61 npttpfitys dgqqsgdkkq fsldltkips hiekiaftlt iydadqkrqn fgqvqggsir
      121 fahpvsgevl rfnldsgftv etaivigely rhngewkfna igagfsggld alcgnfgiev
      181 enspapvptp ppvpqptppp appapkpepp atpvnlnlrk ielkkkgdti nlkkgssggl
      241 geilinlnwn qvqqskgffs rgskgvdldl gclyemkngd kgvvqalgev fgslnrfpyi
      301 aldgddrtgs vktgenlrin gakiseikri lvftfiyegv tnwsqadgvv tlyqkdgpdi
      361 ivhlnehdnr kgmcaiamiq nvndetfsie rlvqfygghr eldrahnwgm rwsqgsk
//
LOCUS       WP_010347444             262 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Paenibacillus peoriae].
ACCESSION   WP_010347444
VERSION     WP_010347444.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus peoriae
  ORGANISM  Paenibacillus peoriae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Paenibacillus peoriae"
                     /db_xref="taxon:59893"
     Protein         1..262
                     /product="formate/nitrite transporter family protein"
                     /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=29146
     Region          9..254
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 meteglrnve qlamkkykiy kqsllrylar smlasmfigf gvivafktgn ffymehspft
       61 ypmaavtfga aiiliayggg dlftgntfyy tyaalrkklr wgqvlrlwia syggnllgag
      121 vfalliyltg lfdsssvnsf llnvvehkme apamqlffra ilcnwlvcla ffvpmfmken
      181 gakmfammlf vfcffisgye hsianmcafa ialvldhpgt vsvagvihnl vpvtlgnlvg
      241 gvllmgvmyy svnlpfldee eh
//
LOCUS       WP_010347899             593 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Paenibacillus peoriae].
ACCESSION   WP_010347899
VERSION     WP_010347899.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus peoriae
  ORGANISM  Paenibacillus peoriae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 593)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 593)
  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 593)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Paenibacillus peoriae"
                     /db_xref="taxon:59893"
     Protein         1..593
                     /product="M4 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=63645
     Region          35..>574
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mkkvwvsllg gamllgsvas gasaaessvs gpaqltptfh aeqwkapssv sgddivwsyl
       61 nrqkktllgt dstsvrdqfr ivdrtsdksg vshyrlkqyv ngipvygaeq tihvgksgev
      121 tsylgavite dqqeeatqgt tpkisaseav htayqeaatr vqalptsddt iskdaeepss
      181 vskdtyseaa nngktssiek dklslekaad lkdskieave aepnsiakia nlqpevapka
      241 elyfyakgda lqlvyvtevn ilepaplrtr yiidandgki vsqydiinea tgtgkgvlgd
      301 tksftttasg ssyqlrdttr gngivtytas nrqsipgtil tdadnvwndp agvdahayaa
      361 ktydyykekf nrnsidgrgl qlrstvhygn rynnafwngs qmtygdgdgt tfiafsgdpd
      421 vvghelthgv teytsnleyy gesgalnesf sdiigndiqr knwlvgddiy tpriagdalr
      481 smsnptlydq pdhysnlyrg ssdnggvhtn sgiinkayyl laqggtfhgv tvngigrdaa
      541 vqiyysaftn yltsssdfsn ardavvqaak dlygassaqa taaakafdav gvn
//
LOCUS       WP_010349393             353 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Paenibacillus peoriae].
ACCESSION   WP_010349393
VERSION     WP_010349393.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus peoriae
  ORGANISM  Paenibacillus peoriae
            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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Paenibacillus peoriae"
                     /db_xref="taxon:59893"
     Protein         1..353
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39552
     Region          1..332
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mhvevrglnk hfgnfhavkd vsfdiqtghl igllgpsggg ktsilrilag leqpdageih
       61 fhgkrvndla pqergigfvf qnyalfkhms vydniafglk vkkssethik ervtelvelt
      121 glkgfehryp hqlsggqrqr vafaralape pqlllldepf aaidakirqe lrswlrelie
      181 rvgitsifvt hdqdeaieva deimvinqgr leqkgtpwdi ykkpgtpfva sfigestvie
      241 qasslkgfee aagagvrali rpeyidvgps eefallsate egivkhlhfr gsewmvevqv
      301 gdqrlmtyrs lekstlepgq qvrvlvhray lyndqsswmv enrlkkdpmp ivi
//
LOCUS       WP_010350282             308 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Streptomyces acidiscabies].
ACCESSION   WP_010350282
VERSION     WP_010350282.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces acidiscabies
  ORGANISM  Streptomyces acidiscabies
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Streptomyces acidiscabies"
                     /db_xref="taxon:42234"
     Protein         1..308
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32687
     Region          1..291
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mtgrlmlldt aslyfrayfg vpesvkapdg tpvnavrgll efidrlvkdh hpdelvacmd
       61 adwrpqwrvd lipsykahrv aeerpagpda eeipdtlspq vpiieavlda vgiarvgveg
      121 yeaddvigtf tarakgpvdi vtgdrdlyql vddvrgvrvl ypikgvgtlq itdeavlrek
      181 ygvdgrgyad lallrgdpsd glpgvpgige ktaakllaef gdlagimaav ddpaskltps
      241 qrkrldesrp yvavapkvvq vagdvplpev etalprgard gglaaalgar wglggslgrl
      301 lgtlegtr
//
LOCUS       WP_010351963             214 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Streptomyces acidiscabies].
ACCESSION   WP_010351963
VERSION     WP_010351963.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces acidiscabies
  ORGANISM  Streptomyces acidiscabies
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Streptomyces acidiscabies"
                     /db_xref="taxon:42234"
     Protein         1..214
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=22968
     Region          <116..208
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mrkfyargrl silaaltgli asvgvlngpt asaalptpvs gatarsylsq ltvatenrtg
       61 ydrdlfphwi tisgtcntre tvlkrdgsgv vtdsacasts gswyspydga twtaasdldi
      121 dhlvplaeaw dsgasawtta qrqafandlt rpqliavtdn vnqaksdqdp atwmpsvtsy
      181 rctyvrawvq vkyyydlsvd taeksaltsy lasc
//
LOCUS       WP_010352626             298 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Streptomyces
            acidiscabies].
ACCESSION   WP_010352626
VERSION     WP_010352626.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces acidiscabies
  ORGANISM  Streptomyces acidiscabies
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 298)
  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   2  (residues 1 to 298)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Streptomyces acidiscabies"
                     /db_xref="taxon:42234"
     Protein         1..298
                     /product="aminoglycoside 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=33024
     Region          49..252
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 msvmtrsvqp viippsplsp letwiesvlg pvelypvldh yswhairpdg rryivkrats
       61 lrsfqreiya hscvlgalda asvpclvaas hprltlitta lpgipvtrtr llpdtyihty
      121 rsagtllasl hhalqpapra laaartalre tadradrilt lmqpsplspd erafaadria
      181 hlreaevnei gfihgafhed swvrstttrr laltdfsasr fapvvydlih iacrwinhgh
      241 lrtaffqgyg rrlstcerrt lvslvtlhca tqlalnptgr aaraehrvlt rlsdgahl
//
LOCUS       WP_010352934             384 aa            linear   BCT 20-JAN-2025
DEFINITION  TerD family protein [Streptomyces acidiscabies].
ACCESSION   WP_010352934
VERSION     WP_010352934.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces acidiscabies
  ORGANISM  Streptomyces acidiscabies
            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 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Streptomyces acidiscabies"
                     /db_xref="taxon:42234"
     Protein         1..384
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=40582
     Region          10..384
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mpmpslskga nvpvpttalr iecgrrsgrg vpdvdasall lvggkvrsdd dfvfynqpah
       61 asgtvrhegk qtsgdlvtdt lvvdlarvep dvdtvllaas adggpfgrvp glyvevrdaa
      121 rgtvvarfdp agasvetafv lgelyrrqga wkfravgqgy dsgleglatd ygitvdepqh
      181 tappvrltkv tltksapsvs ltkqggtsga lrvnlnwqsr sgsahtgldl dlcalyelad
      241 grkgvvqalg nafgalerpp yihldgddrt gavaagenlt vnldhaadlr rvlvfvtiya
      301 garsfadlha tvtlrpqhga pvdfsldect vastvcalal itntggdlvv rrearylvpe
      361 rgvspqrtvd raygwgmnwt pgrk
//
LOCUS       WP_010353631             320 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase LdtC [Escherichia].
ACCESSION   WP_010353631
VERSION     WP_010353631.1
KEYWORDS    RefSeq.
SOURCE      Escherichia
  ORGANISM  Escherichia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Magnet,S., Dubost,L., Marie,A., Arthur,M. and Gutmann,L.
  TITLE     Identification of the L,D-transpeptidases for peptidoglycan
            cross-linking in Escherichia coli
  JOURNAL   J Bacteriol 190 (13), 4782-4785 (2008)
   PUBMED   18456808
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Magnet,S., Bellais,S., Dubost,L., Fourgeaud,M., Mainardi,J.L.,
            Petit-Frere,S., Marie,A., Mengin-Lecreulx,D., Arthur,M. and
            Gutmann,L.
  TITLE     Identification of the L,D-transpeptidases responsible for
            attachment of the Braun lipoprotein to Escherichia coli
            peptidoglycan
  JOURNAL   J Bacteriol 189 (10), 3927-3931 (2007)
   PUBMED   17369299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: BlastRule
            Evidence Accession :: NBR008111
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Escherichia"
                     /db_xref="taxon:561"
     gene            1..320
                     /gene="ldtC"
     Protein         1..320
                     /product="L,D-transpeptidase LdtC"
                     /calculated_mol_wt=34662
     Region          30..308
                     /region_name="PRK10260"
                     /note="L,D-transpeptidase; Provisional"
                     /db_xref="CDD:182341"
ORIGIN      
        1 mmiktrfsrw ltfftfaaav alalpakant wplppagsrl vgenkfhvve ndggsleaia
       61 kkynvgflal lqanpgidpy vpragsvlti plqtllpdap regiviniae lrlyyyppgk
      121 nsvtvypigi gqlggdtltp tmvttvsdkr anptwtptan irarykaqgi elppvvpagp
      181 dnpmghhair laayggvyll hgtnadfgig mrvssgcirl rdddiktlfs qvnpgtkvni
      241 intpikvste pngarlvevh qplsekiddd pqllpitlns tmqafknaaq tdaevmqrvm
      301 dvrsgmpvdv rrhqvnqqtl
//
LOCUS       WP_010354750             280 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Streptomyces
            acidiscabies].
ACCESSION   WP_010354750
VERSION     WP_010354750.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces acidiscabies
  ORGANISM  Streptomyces acidiscabies
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Streptomyces acidiscabies"
                     /db_xref="taxon:42234"
     Protein         1..280
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29572
     Region          13..250
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mgyevavrae atlgegptwd adagrllwld ilgsrvysyd pssgrqtlrt tdqhvgaakp
       61 raggglvlnl rdgvglldpd dtfrwlhrev vpgrrandaa vapdgtlwag tmrydeapgg
      121 gtlarfgptg lletvlddva vsngtgwspd gtlmyyvdsp trrvdvfdyd gervsgrref
      181 vtiedgagfp dgltvdadgc vwvalwdgga vrrytpegkl drvislptpr vtacafggpd
      241 lsdlyittar igltdphpva gsllvvpgag kglelpafag
//
LOCUS       WP_010354804             548 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Streptomyces acidiscabies].
ACCESSION   WP_010354804
VERSION     WP_010354804.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces acidiscabies
  ORGANISM  Streptomyces acidiscabies
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 548)
  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 548)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Streptomyces acidiscabies"
                     /db_xref="taxon:42234"
     Protein         1..548
                     /product="M4 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=57255
     Region          29..548
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mspfrqhvrg srlaaagiaa ttatlmaavl spvadaadrp traqaidnaa savadraasl
       61 ginsaqgtsv rdvvvdkdgt qhvrydrtyr qlpvlggdfv vhlapdgayr nadratrnai
      121 alatitpavp apeaadkavn alraahlgag vrqakakpql vvdalhgtpk lawktdavgl
      181 daqgnpvart vvtdartgaq idawdaieta agdgqslygg tvplettlsg ttyqlkdpsr
      241 gntytgdaen ktdlcifgic ivrapatlft dadnhwgtgt tasrataavd aqygtdvtwd
      301 yyknvhgrng igndgkgsyn rvhygngynn afwddscfcm tygdgdgtql gplvaldvag
      361 hemshgvtsk tanltysges gglneatsdi fgtlvefhaa nsndpgdyli gekivrsgfg
      421 rdalrymdrp srdansadyw sssvggldvh yssgvanhfa yllaegsgtk tingvtynsp
      481 tsngstltgi graklgaiwy raltvymtss tnyagartat lnaardlygn gsaeynavaa
      541 twsavnvn
//
LOCUS       WP_010355857             352 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Streptomyces acidiscabies].
ACCESSION   WP_010355857
VERSION     WP_010355857.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces acidiscabies
  ORGANISM  Streptomyces acidiscabies
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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   4  (residues 1 to 352)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Streptomyces acidiscabies"
                     /db_xref="taxon:42234"
     Protein         1..352
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=37505
     Region          1..334
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 miqfdavhkr fpngttavhd ltldmpeggv tvlvgssgcg ktttlrminr mveptsgtie
       61 vagkdvtrqd aadlrrsigy viqqsglfph rtvldniatv plllghgrrk araragdlle
      121 tvgltpevgk ryphqlsggq qqrvgvaral aadppvllmd epfgavdpvv rtqlqdellr
      181 lqkelsktiv fvthdideav rlgdkiavfr tgghlvqcas paellaqpad dfvagflgae
      241 rglkllslkn ladvpqgqap eggdwrlvld aarrpqhwks gdaelpvrpl rdtdsllaal
      301 deslasptgl varvdadgvl tgvssrddih draghahaea rtaththegg aa
//
LOCUS       WP_010356027             264 aa            linear   BCT 20-JAN-2025
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            acidiscabies].
ACCESSION   WP_010356027
VERSION     WP_010356027.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces acidiscabies
  ORGANISM  Streptomyces acidiscabies
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Streptomyces acidiscabies"
                     /db_xref="taxon:42234"
     Protein         1..264
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=29661
     Region          1..252
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mryeilgplr ivddnkysti narkveivls vlliradqvv sldqlmlelw gedlprrata
       61 glhvyisqlr kllrsrcsgd shvetrapgy vlrtghdeid ahlfpqlvdr grsllreerl
      121 draaaqfeta lglwrgpalg hggsgpaang piidgfttwl aevrlecqem laecrlrlgr
      181 hreavgmlya ltaenpmres fyrqlmlaly rserqadalk vyqsvrktln delglepgrp
      241 lqdlqraila gdrrlmatpv vsgr
//
LOCUS       WP_010356344             355 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces acidiscabies].
ACCESSION   WP_010356344
VERSION     WP_010356344.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces acidiscabies
  ORGANISM  Streptomyces acidiscabies
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 355)
  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 355)
  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
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 355)
  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   5  (residues 1 to 355)
  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   6  (residues 1 to 355)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 355)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 355)
  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 20283677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Streptomyces acidiscabies"
                     /db_xref="taxon:42234"
     Protein         1..355
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36431
     Region          23..73
                     /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(37,39..41,50)
                     /site_type="other"
                     /note="non-specific DNA interactions [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            50..56
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238044"
     Site            order(51..52,56)
                     /site_type="other"
                     /note="sequence specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238044"
     Site            51..52
                     /site_type="other"
                     /note="putative cAMP binding site [chemical binding]"
                     /db_xref="CDD:238044"
     Region          87..348
                     /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 mnrtndpgrt tgtnllavrg hntalvldll rtagadgisr lelaertglt pqavskitar
       61 lreeglaaea grrastggkp rtvlrlvpea ghavgvhldr delrvvlvrl dgrvvaerrt
      121 pldlgagtse vvdglvrevr gllaegvvgl lgvgaalpgp ldhtygvlgr vtgfpdwdgf
      181 plrdvlarel gvpvvvdkdt naaalglava geggsfaylh lgtglgaglv iagtvhrgar
      241 tgagefghqv illdgppcpc gksgcvealc laaldrenpe eaarvlgvga anlvglldid
      301 qvllggrrie qtpevfvrgv stevgevpvr vadggvwgva vgaaqlwlge vfgrg
//
LOCUS       WP_010357692             640 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Streptomyces acidiscabies].
ACCESSION   WP_010357692
VERSION     WP_010357692.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces acidiscabies
  ORGANISM  Streptomyces acidiscabies
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Streptomyces acidiscabies"
                     /db_xref="taxon:42234"
     Protein         1..640
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=68631
     Region          248..421
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mprripqava saalllplla aapphesgas rlalqrafda aaaeygvprs vllgvsylqs
       61 rwddhagaps vtggygpmhl tdagtalaga shhsegeedp rgdsarpvlr paavlaqsvd
      121 aprlhtlara aaltglapet lrtdpaanie ggaallaaaq ralgeplstd paewyaavar
      181 fsgaddtata aayaddvydv lragqerttd agqlvaldaq prlapderql araglrqpvt
      241 agtecprdvs cewipapyke fgdkdygnhd lanrpasqpv ryivvhdteg swegvlnmvq
      301 dptyvswhyt lrstdghiaq hvktkdvawh agnwyintas vgiehegfla qpdawyteam
      361 yrasarlvry lahrygvpld rqhilghdnv pgpttanvpg mhtdpgpywd wrhyfellka
      421 pikataqghg glvtirpsyg anrptymdcv akgqpcadhg ssevrlytgp getyplvkdi
      481 grgtepttgv ndlssrvstg qqyavagrsg dwtaiwylgq kawfknprkh atavhaaglv
      541 arakagrasv pvygraypea saypkgvpvq avsplsytlp agqsyvvgge vpgeyyyavt
      601 fatdshrvvv gkdmyyeiqy ghrvayvraa dvdvvpslrg
//
LOCUS       WP_010357123             292 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptomyces acidiscabies].
ACCESSION   WP_010357123
VERSION     WP_010357123.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces acidiscabies
  ORGANISM  Streptomyces acidiscabies
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 292)
  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 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 292)
  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   4  (residues 1 to 292)
  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 292)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptomyces acidiscabies"
                     /db_xref="taxon:42234"
     Protein         1..292
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31804
     Region          31..292
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          210..288
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mmlpagdaip rlgfnppdpr vpgfeiigla dlhhrlrhgv hrvdfhtltl vtggsgehtv
       61 dfvtypcrpg tllrvrpgqv qrytlpgtad glhvlfapaf pppftgagrl ldegdepvcr
      121 qlgaspeyav latllgqlra eyertgavgd sygrtpsvei lrhllatvll qvdrlprpdg
      181 gdpyaggevy arfraelers yattrraady ahrlgytvkt ltractaatg rpvkhvidar
      241 valeaqrlla htdepaatia rrlgfpeptn fgkfftrhtg ltpgafreth ra
//
LOCUS       WP_010359729             175 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Neisseria gonorrhoeae].
ACCESSION   WP_010359729
VERSION     WP_010359729.1
KEYWORDS    RefSeq.
SOURCE      Neisseria gonorrhoeae
  ORGANISM  Neisseria gonorrhoeae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 175)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Neisseria gonorrhoeae"
                     /db_xref="taxon:485"
     Protein         1..175
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18997
     Region          15..170
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 myanmgdmmh alhfsasdka alyrevlpqi esvvadeadw vanlantaav lkeafgwlwv
       61 gfylvdtrsd elvlapfqgp lactripfgr gvcgqawakg etvvvkdvna hpdhiacssl
      121 srseivvplf sdgrcigvld adsehlaqfd eadalylgel akilerrfea srqaa
//
LOCUS       WP_010360059             197 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Streptomyces acidiscabies].
ACCESSION   WP_010360059
VERSION     WP_010360059.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces acidiscabies
  ORGANISM  Streptomyces acidiscabies
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Streptomyces acidiscabies"
                     /db_xref="taxon:42234"
     Protein         1..197
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18743
     Region          <52..183
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mptshsapaa lhtlcrlgaa avlvwgatla asppahadpv pvcdgkaati vsdapvvsgt
       61 dgddvivtgd gnhdvlaggg ndtvctgagd dtlsggdgdd elfggdgrds lhgqagddvv
      121 rgeggddfav dggpgtdlvd agpgadgarg gpgddelrgg pgddrldggp gtdvidggdd
      181 tdvcvngetv sncestg
//
LOCUS       WP_010360119             320 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase LdtC [Escherichia].
ACCESSION   WP_010360119
VERSION     WP_010360119.1
KEYWORDS    RefSeq.
SOURCE      Escherichia
  ORGANISM  Escherichia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Magnet,S., Dubost,L., Marie,A., Arthur,M. and Gutmann,L.
  TITLE     Identification of the L,D-transpeptidases for peptidoglycan
            cross-linking in Escherichia coli
  JOURNAL   J Bacteriol 190 (13), 4782-4785 (2008)
   PUBMED   18456808
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Magnet,S., Bellais,S., Dubost,L., Fourgeaud,M., Mainardi,J.L.,
            Petit-Frere,S., Marie,A., Mengin-Lecreulx,D., Arthur,M. and
            Gutmann,L.
  TITLE     Identification of the L,D-transpeptidases responsible for
            attachment of the Braun lipoprotein to Escherichia coli
            peptidoglycan
  JOURNAL   J Bacteriol 189 (10), 3927-3931 (2007)
   PUBMED   17369299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: BlastRule
            Evidence Accession :: NBR008111
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Escherichia"
                     /db_xref="taxon:561"
     gene            1..320
                     /gene="ldtC"
     Protein         1..320
                     /product="L,D-transpeptidase LdtC"
                     /calculated_mol_wt=34517
     Region          28..308
                     /region_name="PRK10260"
                     /note="L,D-transpeptidase; Provisional"
                     /db_xref="CDD:182341"
ORIGIN      
        1 mmiktrfsrw ltfftfaaav alalpvkant wplppagsrl vgenkfhvve ndggsleaia
       61 kkynvgflal lqanpgvdpy vpragsvlti plqtllpdap regiviniae lrlyyyppgk
      121 nsvtvypigi gqlggdtltp tmvttvsdkr anptwtptan irarykaqgi elpavvpagp
      181 dnpmghhair laayggvyll hgtnadfgig mrvssgcirl rdddiktlfs qvtpgtkvni
      241 intpikvsae pngarlvevh qplsekiddd pqllpitlns amqsfkdaaq tdaevmqhvm
      301 dvrsgmpvdv rrhqvspqtl
//
LOCUS       WP_010360422             389 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Streptomyces acidiscabies].
ACCESSION   WP_010360422
VERSION     WP_010360422.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces acidiscabies
  ORGANISM  Streptomyces acidiscabies
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 389)
  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 389)
  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
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 389)
  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   5  (residues 1 to 389)
  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   6  (residues 1 to 389)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 389)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 389)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Streptomyces acidiscabies"
                     /db_xref="taxon:42234"
     Protein         1..389
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40529
     Region          20..65
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          84..368
                     /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 mgrliggdps llrrinsavv lhalraaera tltevtrvtg lsrptvegvv edligaglvv
       61 eeaadvtvvr rqgrparrfr fraeagyllg ldigahrvsa vvadldgrvl gaqdrgvaes
      121 asaeerlera rtvvaellrr agvprsalra vgvgtpgive tdgtvrlcaa lpewtglrlg
      181 erlsrsfkcp vlvendanaa avaehwkgaa vdsddvvlvl aglspgagsl iggrlhrgyg
      241 gaageigalh llgrevtpet llsttdvplp pldhqaaiev ftragdgdpg acaavdrffr
      301 rlvhdvaala laldpelvvi ggatagladl lgplrnelar yclrpprvtl sslgeaavam
      361 galrlaldhv dqqlfavegt vtgrqglgw
//
LOCUS       WP_010361889             101 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Pseudoalteromonas citrea].
ACCESSION   WP_010361889
VERSION     WP_010361889.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas citrea
  ORGANISM  Pseudoalteromonas citrea
            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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Pseudoalteromonas citrea"
                     /db_xref="taxon:43655"
     Protein         1..101
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11350
     Region          1..100
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(24,55..56,58,84)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(24..25,33,36,38..39,41,44..45,47,55,60,66)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mqdehkqrlf tliggipagk vaaygqladl aglprqarav grllkelpks stlpwyrvvn
       61 sqgkisfpyg sqkyteqktr lqmegvifik dkinmrvyqw a
//
LOCUS       WP_010362238             103 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Pseudoalteromonas citrea].
ACCESSION   WP_010362238
VERSION     WP_010362238.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas citrea
  ORGANISM  Pseudoalteromonas citrea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 103)
  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   2  (residues 1 to 103)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Pseudoalteromonas citrea"
                     /db_xref="taxon:43655"
     Protein         1..103
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11080
     Region          43..102
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mhiksmllvt slffctssft aekvpslltp tsqtdnieha raininlahl eelavlpgig
       61 kkkaqaiidy rtkhgnffdl aslsqvkgig qgiigklegk vtf
//
LOCUS       WP_010362316             251 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Pseudoalteromonas citrea].
ACCESSION   WP_010362316
VERSION     WP_010362316.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas citrea
  ORGANISM  Pseudoalteromonas citrea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 251)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Pseudoalteromonas citrea"
                     /db_xref="taxon:43655"
     Protein         1..251
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=28250
     Region          21..238
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mkgrelvsca ncvqlegldi dftmafqpiv haqskrifgy ealarglnne paysvlsqvn
       61 dknryafdqm crvkaielaa kldlssylsi nflpnaiyqp qrcirttlaa aekhgfpver
      121 imfeftevek isdsghikrv veyyrtlgfk tatddfgsgy sglnlladfq tdiikfdmgl
      181 irdihidkvr qvilrhcisl chklqittla egvetsgefk wlqsegvdli qgyfiakpgf
      241 eclpsvdfsq l
//
LOCUS       WP_010363056             417 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Pseudoalteromonas
            citrea].
ACCESSION   WP_010363056
VERSION     WP_010363056.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas citrea
  ORGANISM  Pseudoalteromonas citrea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 417)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Pseudoalteromonas citrea"
                     /db_xref="taxon:43655"
     Protein         1..417
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47286
     Region          5..416
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mslvtaevya swfpikeptl aghllfqets rggvfsfeyd rdflkspfrm qldpslalts
       61 gehyndrsak nfsvfldscp drwgellmkr raaldfkngh ratarmtamd yllgvhdsyr
      121 mgglrfktap egnflddnae yaaspmaslk qleyasmmie ndenidsdey yrwlsmliap
      181 gsslggarpk acvhddnndl wiakfpnsnd itdvgawemv chklalgagi dmypcdiqkf
      241 nsthhtfitk rfdrdkgqri hfssamtqlq yydgrdeted asylelaefl tvngsqtqkd
      301 laqlwrrivf niavsntddh lrnhgflltk kgwalspayd ltpsidmtgl qlniddisne
      361 ldydlafsva dyfnlkesea kkiyddvmls vknweviasg igisrqeqlg mqkafrv
//
LOCUS       WP_010363534             358 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Xanthomonas vasicola].
ACCESSION   WP_010363534
VERSION     WP_010363534.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas vasicola
  ORGANISM  Xanthomonas vasicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Xanthomonas vasicola"
                     /db_xref="taxon:56459"
     Protein         1..358
                     /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=38718
     Region          22..301
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mtselspsfv arahspadar ptrdwqidaa kalaialvvl ghasgmpsay klfaysfhvp
       61 lffvlsgwvg erfgqraltg atvaklartl lvpylaffmv ayalwlltav ldghsghpqt
      121 rplwhpltgl lwangsrlyv lpalwflpal fvttlayial rarltaaava avslplalaw
      181 agwfpslqlr lplaldvlpv alffiaiggw lsrfadalrl lgaqvwalal lplaagwwwl
      241 agwngqvdvn nlqfgqsaav fllvsllgtv mtfcvayfir gvrwvqwigt ntllilctht
      301 lvflvatsvv artgliarsa igtpawalgl safaiatsvp mravlvrvap wmlglkrk
//
LOCUS       WP_010363792             141 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Xanthomonas vasicola].
ACCESSION   WP_010363792
VERSION     WP_010363792.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas vasicola
  ORGANISM  Xanthomonas vasicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Xanthomonas vasicola"
                     /db_xref="taxon:56459"
     Protein         1..141
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14298
     Region          2..137
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkkqqgftli elmivvaiia ilaaialpay qdyttrakls ealtmsapak lavtetassl
       61 gglanvtsan sgyafpgatk yvsgititna tgqvavtstv pnatgtillt pvdvgggqlk
      121 wtcssaintk ylpaecrnsg t
//
LOCUS       WP_010364167             239 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudoalteromonas citrea].
ACCESSION   WP_010364167
VERSION     WP_010364167.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas citrea
  ORGANISM  Pseudoalteromonas citrea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 239)
  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 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   3  (residues 1 to 239)
  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   4  (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   5  (residues 1 to 239)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Pseudoalteromonas citrea"
                     /db_xref="taxon:43655"
     Protein         1..239
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26602
     Region          16..239
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          157..228
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mptviiepgi lavqthvldt tshqhtlqqi tlpigsvhln vttaqgiqsy nntaiiikes
       61 vphqltmhag wvilieptsq vglqvsamla gqeayllnip hapdefshlp tllglcnlrf
      121 qqqthqydpr isqllkhldq clagtcikpa hwlakdiaqq lnlsqsrflh lfkenmglaw
      181 rpyllwrrli caitalqadh tatqaaymag fsdsahlsrt fkkqfgitlq kllsqnksq
//
LOCUS       WP_010364178             206 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Pseudoalteromonas citrea].
ACCESSION   WP_010364178
VERSION     WP_010364178.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas citrea
  ORGANISM  Pseudoalteromonas citrea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 206)
  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 206)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 206)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Pseudoalteromonas citrea"
                     /db_xref="taxon:43655"
     Protein         1..206
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22004
     Region          1..199
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 meiysteeqq aeaikqffrd ngvslalgiv lglgglygwk aynqsqitsa eaasnaysdi
       61 vegeevlasa esfianngds nyavlaafva akeavdkqqy svateklrfa adtvknpelk
      121 ataltrlari qltekkldea latlnttmpa sfnaqvseik gdvylekgdk qsarthyqaa
      181 vsasedannt llqnklddla taqpaa
//
LOCUS       WP_010365596             137 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Pseudoalteromonas citrea].
ACCESSION   WP_010365596
VERSION     WP_010365596.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas citrea
  ORGANISM  Pseudoalteromonas citrea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Pseudoalteromonas citrea"
                     /db_xref="taxon:43655"
     Protein         1..137
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14967
     Region          1..137
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mqirslkgft ltellisvli vavlgslalp syfqyvqesr rseaqqkmlq iaaileriys
       61 rnggypdsgi fpisqtadgy dfvyehknkh ddsgetnsle fslsakpkag gpqatdkcgt
      121 ltlnhqgikg pvdndcw
//
LOCUS       WP_010365761             291 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein, partial [Xanthomonas
            vasicola].
ACCESSION   WP_010365761
VERSION     WP_010365761.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas vasicola
  ORGANISM  Xanthomonas vasicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Xanthomonas vasicola"
                     /db_xref="taxon:56459"
     Protein         <1..291
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          8..256
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 ppsrcthgeg vlwctqreal ywvdisekrl wrhhpgtaht rywtlpdrpg ciglmddgrv
       61 lialakaigi vdpdnveedv lpfekladve adnpltrsnd gradrngnfv fgtmdehdtk
      121 targamyqfs lkhglralpl pgvsipnsic fspdgrtlyy cdsvrpqilc cdydaqtaqt
      181 sntrvfttld rddaepdgsi idaeghlwna qwrawrvvry rpdgsveriv qlpvkhptcs
      241 afggaaldrl hvissrldhs aeelartpea gglylcdlpv aglpeslvas a
//
LOCUS       WP_010366199             805 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Xanthomonas vasicola].
ACCESSION   WP_010366199
VERSION     WP_010366199.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas vasicola
  ORGANISM  Xanthomonas vasicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 805)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 805)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 805)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..805
                     /organism="Xanthomonas vasicola"
                     /db_xref="taxon:56459"
     Protein         1..805
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=86746
     Region          27..805
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mrkwlgrlll aivllaltag lalyllmrgs lpqldgdaal sglaapvsvq rdqlgvvtid
       61 atnqldvmra lgyvhaqery femdlmrrap agelselfgp kavdldkrnr vhrlrarvha
      121 nldiaagsqh aalqaytdgv naglaalrvr pwpylllrqt prawtlddsi ltglamyadl
      181 qdnsnqtela aariravvpp alaallghqg sswdaplfgp pqgdaslpda atldlrrlph
      241 pataphaetp tpgsnnfavd gsltadgrai vaddmhlglr apniwfrarl ryadsnapng
      301 kvdvtgftlp glpavvvgsn ghvawaftns yidtadfari paptpghrqa lttnvetirv
      361 agaapmrfev reaawgpvlh tnadgsvlal rwaaqlpgai rldfaqmsta gdlqaafava
      421 drsgiptqnl lladrsgria wrligarper nagcspsgia elatsapvpn aatsapadta
      481 atpsmpgicl pwslrsdaap alidppshrl wtansrivda qqlatlgsag ydlgaraqqi
      541 rddlfakqrf nerdllaiql ddravlltrw whllrrvvdh skdpalqqia pvtrdwdgha
      601 stqsasyriv refrtktida veagllapah aalgedfltp rraqlegivw pllqqrpanl
      661 lppafaswdq llsdaarnaq sdviaedaqs ehrgqhtwgq rntaaichpi aralpalakr
      721 wlcmppdqlp gdrdmprvqg pafgasermv vspgheqdgi vhmpggqsgh plspfwgagh
      781 ddwvhgrptp flptaarytl qlrpq
//
LOCUS       WP_010367004             767 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pseudoalteromonas citrea].
ACCESSION   WP_010367004
VERSION     WP_010367004.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas citrea
  ORGANISM  Pseudoalteromonas citrea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 767)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 767)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 767)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..767
                     /organism="Pseudoalteromonas citrea"
                     /db_xref="taxon:43655"
     Protein         1..767
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=84495
     Region          6..763
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mliwlkriia glvllalatt atlygvlsls lpsldgtgts ngitaattve rdalgqavit
       61 aqsrkdaayg lgfahgqdrf fqmdllrrna agelselfgs aaikldknmr fhqlrkrsqa
      121 ivaslpmdqq qvlqaytqgv negrvqagfq sfeyllsgat ikawrsedsi ltifsmyldl
      181 qsanferdka liylehifgn amrefilqps ihqaaldgsr lpirralipe lptlsvqadi
      241 hdigsvnlyg snnwavtgal tesgkamlsd dmhlglavps iwyraqlnyq sqnspvtvtg
      301 vslpgapaiv vgtndhiawg ftngyldtad wielssddet wqekehiqlp ndevhtysll
      361 mseygpvqqf ndksyalswv ghqpyavnln llametaltv ddalalaptv gipvqnmivv
      421 dqhgdagwgl mgaipartnp sdiamesiny skqwqdndss ravlknpeng klwtansrvv
      481 saqahtrygd ggyalgarav qirdrllake tfneddfnql qhdndalflt pwhqhltall
      541 shneaskarf kidlqhlaqw qacacadsvg ytlvkrfrts finsafapve aqmkesgvgl
      601 ryikrylepa lwqlleqqpq swlnqhgswq ilqlsayeaa kqklsaefgp nmaswqwgev
      661 nalkvkhpfs kqipilsqfl dmpktsafgd tfmpsvqgrd fgasqrfiaq pgalsnaimt
      721 vaggqsghpl spfyragfhd yaqgnatpll pgqvihalti rpkdqpe
//
LOCUS       WP_010367575             670 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Pseudoalteromonas citrea].
ACCESSION   WP_010367575
VERSION     WP_010367575.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas citrea
  ORGANISM  Pseudoalteromonas citrea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 670)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..670
                     /organism="Pseudoalteromonas citrea"
                     /db_xref="taxon:43655"
     Protein         1..670
                     /product="amidohydrolase family protein"
                     /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=74085
     Region          243..651
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mkkqkklnhy tfllcsallv aqasattiin nvytekglag smsqtqvdkn tytsktqfgw
       61 nnrrvniset mslgengipv sftthgtsaf gapisekfdy nkgiatwqdt dgkgsikddt
      121 vnfyvaknss ltlenarlry liktgktqad vypqgqvqvr klltrklqne dihlyvtsgl
      181 altpdfawyd nngnyfaqsw gggmyvlrkg vpqsefatlr klqkeqeqty ledlsaslth
      241 thqsllikdv avldvdqgvv tsgqhvllrd gkikrisnep lklngiatvn gsgktlipgl
      301 wdmhghlske ngilniangv tsvrdmgneh knimeieslf dtnrvlgtrv yragfmdkls
      361 ensaglsvet leealktvdf fadngyvqik lyssidpkwv kpiadrahnr glrlsghvpa
      421 fmtaeqaina gydeiqhinm lflnflagqd vdtrttkrfs ligeqasqlp ldtdemsafi
      481 klladkkivv datvstfrsl lmaenekvnp eyahlidhmp isfvrqmkga vmhvddihki
      541 nyqrsgeamq nmlkklydag vnivpgtdnv agftlirele lyalagipta dvlkmatins
      601 aklmgvahkt gsisenktad lilvdgdple ditalrktsl iikgeqvfkp eqiynaigvk
      661 pftpaskith
//
LOCUS       WP_010368791             671 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: amidohydrolase family protein [Pseudoalteromonas].
ACCESSION   WP_010368791
VERSION     WP_010368791.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 671)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..671
                     /product="amidohydrolase family protein"
                     /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=74266
     Region          246..646
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mtkiitkrsa lstlvaallt tqswavfadt itnnvysekg lagtltqeki deqnykakie
       61 fgwnnrrili detlklnekg lpinfslkgr safgsaidet fsynrgiaqw ksvnesgika
      121 datldfyvps nnrlaldnat mryvlknnky eldvypqgkm liekmktmkl geqtvhllvt
      181 sglsltpnfa wydddgnyfa qswgsmyvlr dgytksqfee leaiqkqaeq qylenlaskl
      241 thdvpallie nvavfdgeqk kllknhdvli kngkiveitk hikkqngvas ldgkgktlip
      301 glwdmhghls kdngilnian gvtsvrdmgn dhdnimeiea lfntnqvlgs rvyragfmdk
      361 ysensaglsv ksleealetv dffadngyvq vklyssidpn wvkpiserah srglrlsghv
      421 pafmtaeqai angydeiqhi nmlflnflag eevdtrtqkr fslmgeqasg lsldspqmna
      481 fikllsdkri vvdptvstfr sllmaedqki npeyaaiseh mpiafarglk gaemhvdeqf
      541 klsyqesgea mqqmlkklyd agvpmvpgtd niagftlire lalyvdagip aadvlnmatl
      601 esaklmgvah qtgsiakgkv adlvlidgdp lkditalqka tlvikgeqaf kpaeiyqaig
      661 vkpfttspsl k
//
LOCUS       WP_010369721             118 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Xanthomonas vasicola].
ACCESSION   WP_010369721
VERSION     WP_010369721.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas vasicola
  ORGANISM  Xanthomonas vasicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Xanthomonas vasicola"
                     /db_xref="taxon:56459"
     Protein         1..118
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12547
     Region          <30..111
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 msdvdapapg ggaaahwqcm gvvfaqcvtv eevclygsra rgtnrpnsdi dlcvtsstld
       61 figlarlgea ladlglpwki dltlrrtrtp pvtaqpafnl ahqiaryavp vfvraper
//
LOCUS       WP_010370486             303 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Weissella].
ACCESSION   WP_010370486
VERSION     WP_010370486.1
KEYWORDS    RefSeq.
SOURCE      Weissella
  ORGANISM  Weissella
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 303)
  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 303)
  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 303)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Weissella"
                     /db_xref="taxon:46255"
     Protein         1..303
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31823
     Region          9..74
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          226..294
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mneernsvig qelqnarldk glslddiqqs tkiqkrylaa iengqfdqlp gafyerafvr
       61 qyasavgldv tefmqnhdiq tqtvepdlsg arvdsdnvtr agmhhveest aektrqmlpk
      121 iligvavvai igiiwalvas fagsakqent tssvsvttsk vsssassdae ksstdaskes
      181 aaksssasse kkdkdavdlg agqatgntvn ygtvkapank eltlnlkttg aswiqvsdas
      241 gavlwngtlq angnqdvkip atvpgvrvsi gnaaatavsl dgksvdlman natvwnlamt
      301 far
//
LOCUS       WP_010370665             369 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Pseudoalteromonas
            piscicida].
ACCESSION   WP_010370665
VERSION     WP_010370665.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas piscicida
  ORGANISM  Pseudoalteromonas piscicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 369)
  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 369)
  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 369)
  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 369)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Pseudoalteromonas piscicida"
                     /db_xref="taxon:43662"
     Protein         1..369
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=41110
     Region          5..333
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 msksrrqfle aslaaclsas fpvsqvlaln lfsedereqe makrsaalhi lrlaspypad
       61 qsdfiphmhq vlkenvesmt rgkiyvdvhh sgalgsgrel maavtrghvg aalisvsnls
      121 ralpvldiln ipfwassnra flnlicspqw qslvikpise qgklnilmhh lvggrtltst
      181 kqfnrlinlp eklkgvvlrv paskvlshfy smtsanvidv pwaqvakmar tehievidps
      241 vvglfsgpdl lkneigqial lesvpdawvt vanqhwldgl plrlkgeied agkqtfhthi
      301 aqieqlqkhc erelmalgak lhplsvdekr ewqlrfghhn aqwnkvkrel lgstrafqql
      361 vnatekefi
//
LOCUS       WP_010371100             221 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Pseudoalteromonas piscicida].
ACCESSION   WP_010371100
VERSION     WP_010371100.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas piscicida
  ORGANISM  Pseudoalteromonas piscicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 221)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Pseudoalteromonas piscicida"
                     /db_xref="taxon:43662"
     Protein         1..221
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=24133
     Region          80..219
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 makmsdyisl selsisrell llqleklday ieqnsspavw syqipelgeg gacslfgylq
       61 eapfllsdyv ekntanarsl tklqtivsav veftavdwfg iyqaratneg kqllklaysg
      121 apsrplfpit dafaatsnni qtvlsakarv indipqyvas ggeyytcdpk vkaetclplf
      181 ddaqncigii daeafsesff neeilallaa actripeylp k
//
LOCUS       WP_010371108             102 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Pseudoalteromonas].
ACCESSION   WP_010371108
VERSION     WP_010371108.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (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   2  (residues 1 to 102)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..102
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10696
     Region          32..101
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mfnkptilsi llalglscss vlakpaeqak svsqtqqqsa vldinsadas alsslpgigi
       61 rkaeaiveyr kkmgrfkttt ellevkgigk gilaklegki rv
//
LOCUS       WP_010371658             397 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Weissella].
ACCESSION   WP_010371658
VERSION     WP_010371658.1
KEYWORDS    RefSeq.
SOURCE      Weissella
  ORGANISM  Weissella
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Weissella"
                     /db_xref="taxon:46255"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43569
     Region          3..391
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 maktlainag ssslkfqlld mpaetviakg qveriglpes vftmkfngek teivrdiadh
       61 kaaieemleq frtqnvadks eitgvghrvv aggewfnksv ivddevlhki hrladyaplh
      121 npanatgiev fqellpdavs vavfdtafhq tlprenylyp lpyeyytkyg arkygahgts
      181 hryvaeraad mmgkplselk litlhlgaga sitaikdgks fdtsmgftpl aglmmatrsg
      241 dvdpsliyyi qereglsnae mlrilnnksg llgvstlssd mrdleevadt nehaklaldm
      301 flnrvvrylg qytfemggvd givftagige naanvredii arlkflgiem dkeannvrgv
      361 eriistpess atvllvptne eleiardver lkaqagk
//
LOCUS       WP_010372009             809 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: Lon protease family protein [Pseudoalteromonas].
ACCESSION   WP_010372009
VERSION     WP_010372009.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 809)
  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 809)
  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 809)
  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   4  (residues 1 to 809)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..809
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..809
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89047
     Region          73..805
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mtksklscek alpasqlaps vslthienci qnpypealpf igqqraqtal dfalgmelpg
       61 ynvyvmgeaa lgrftmvkdk leahsktkpt pkewlyvnny ddhrepialf mqageskqle
      121 adidafidei ldtfpaafdn pgyqrkkksl dkefeqkyda aitaveqqam nmsvaliedt
      181 gtvgfapvvd gkqlsdtefs aldehvqahf ltaietleda lieslielpr wkresserlr
      241 nlkkttieva tkpllkaleh kyaahigvlr ylkdlkveiv davldwlddd ssnsdenkdd
      301 fdskgmltdf fapnilvefk eddpapvvye pnptfgnifg kveyatsqgn litsyrsiqa
      361 galhranggy limdaekvma naqvwdglkl slkthqiknd lpyqdnsvgs sftlkpqlip
      421 ldvkiillgs rdlyytigey deefaelfrv ladfdyylps sdkmqyqfit kvmeycndtl
      481 kielssaala rmlkfsyrqa ehhsklsarf advlelvaea sfyakqdgvn qiaanhidea
      541 iagkeyrtgq lsenmlsdiq eghtliateg taigkvnglt vlhigdtafg tparitstvy
      601 agadgvidve revdlgksih skgvmlltgy lgnkyaqdfs ltlsaniaie qnygfidgds
      661 aslaelcall savtqlpvdq slaltgsinq hgevqaiggv nekiegffkl ckmrgltgkq
      721 gvivpesnkv nlvlddevia avekglfhvy avatvdeals llmdrpagal sdegypensi
      781 navamakler iakvvngddd kgeeshddn
//
LOCUS       WP_010372807             658 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Pseudoalteromonas piscicida].
ACCESSION   WP_010372807
VERSION     WP_010372807.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas piscicida
  ORGANISM  Pseudoalteromonas piscicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 658)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 658)
  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   3  (residues 1 to 658)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Pseudoalteromonas piscicida"
                     /db_xref="taxon:43662"
     Protein         1..658
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=72743
     Region          3..653
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mvdlseiqav fieeakelvl qfeesllame silpnsddei ineafraaht ikgsagvvgy
       61 dhivdfthfv eatmellrdh alnpcerlis tllecndhin alikclesne dfpqaltdae
      121 aglleslksy sglqdqasse qtvvenqeat qsfrvsaqfy kacmvdgfdp lsiiryiesk
      181 gstvevdwli devpalnavt adelelchfr mqleihhstr edideafefi aaesnieiap
      241 ieddkptptl vkadkqptkn nkvkpknper mmkipaqkld elvnelgelv ivsaaledht
      301 ktirdsalte ivehiqqlvs dvqsstlqlr mvqigetfnr fsrvvrdtsk elekqvslei
      361 mgaeteldks mvekivdplt hlvrnaidhg meppaqrads gkpeygtlsl kafhdsgsiv
      421 ieisddgrgl dkekikekai qrnlispdte ltdkeianli fepgfstaek isnisgrgvg
      481 mdvvrkniea vrgtvsvesv ehqgtcfqlr lpltmaiidg fmvsvadakf vipldmvtec
      541 ielplgngat rqtdyinlrg tvlpfihlsr ifdlptnpki rpsivvvkyg qlragivvdq
      601 llgefqtvik plgalfekms gisgssilgs gdialildvp klihdfahep esrklans
//
LOCUS       WP_010373538             286 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Xanthomonas vasicola].
ACCESSION   WP_010373538
VERSION     WP_010373538.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas vasicola
  ORGANISM  Xanthomonas vasicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
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   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 286)
  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 286)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Xanthomonas vasicola"
                     /db_xref="taxon:56459"
     Protein         1..286
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30056
     Region          11..81
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          203..269
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 misdsnpnlf eqekgcgqhl reareaagls vddvagklrm pghvvrsleq edwprlgapv
       61 fvrgqlrsya rllqvdlepl lqqatiapie pvklvshtht prarrilest arkamyvvit
      121 gvfavpvwya trshldgkap stvsldsmpe atksaapgap aaqpapapre qpapyiasmt
      181 pvpratadaq apaaaaapgg slslnfsgds wvqilapdgs avekalirag errtyspgqv
      241 grivlgnasa vqvqqggsiv dvkpfqranv arfavssdgs vvpase
//
LOCUS       WP_010374326             144 aa            linear   BCT 20-JAN-2025
DEFINITION  AAA family ATPase [Pseudoalteromonas piscicida].
ACCESSION   WP_010374326
VERSION     WP_010374326.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas piscicida
  ORGANISM  Pseudoalteromonas piscicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Liu,Y., Sung,S., Kim,Y., Li,F., Gwon,G., Jo,A., Kim,A.K., Kim,T.,
            Song,O.K., Lee,S.E. and Cho,Y.
  TITLE     ATP-dependent DNA binding, unwinding, and resection by the
            Mre11/Rad50 complex
  JOURNAL   EMBO J 35 (7), 743-758 (2016)
   PUBMED   26717941
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Chen,Z., Luong,T.T. and Lee,C.Y.
  TITLE     The sbcDC locus mediates repression of type 5 capsule production as
            part of the SOS response in Staphylococcus aureus
  JOURNAL   J Bacteriol 189 (20), 7343-7350 (2007)
   PUBMED   17704228
REFERENCE   3  (residues 1 to 144)
  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   4  (residues 1 to 144)
  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
REFERENCE   5  (residues 1 to 144)
  AUTHORS   Hopfner,K.P., Karcher,A., Craig,L., Woo,T.T., Carney,J.P. and
            Tainer,J.A.
  TITLE     Structural biochemistry and interaction architecture of the DNA
            double-strand break repair Mre11 nuclease and Rad50-ATPase
  JOURNAL   Cell 105 (4), 473-485 (2001)
   PUBMED   11371344
REFERENCE   6  (residues 1 to 144)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Pseudoalteromonas piscicida"
                     /db_xref="taxon:43662"
     Protein         1..144
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15454
     Region          7..>97
                     /region_name="SbcC"
                     /note="DNA repair exonuclease SbcCD ATPase subunit
                     [Replication, recombination and repair]; COG0419"
                     /db_xref="CDD:440188"
ORIGIN      
        1 mtsklnlkkl tisglrgvsn pltlnfektf tlifghngtg ktsicdaidf langdcsslg
       61 dnslgsarhk fwpfvgkkss dvavdlslsd gsswratilg tktsvsvssk relpvvkvwr
      121 rkqmmdlila kplcnstqfs tais
//
LOCUS       WP_010375900             192 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Pseudoalteromonas].
ACCESSION   WP_010375900
VERSION     WP_010375900.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..192
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=20914
     Region          13..165
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 maltaelkqk tkrlvesknm lkgitvasfl estivpiple avmvplmqar reklwlialm
       61 atvgcvigal fgyalgyylf davgdsviel lsspsqfeqv kaqmqsqgfw fvltlgiapv
      121 pfqiamlaag atkfsllqfl iatciarslr yfglaavvyf agnqaeklik khkikavilt
      181 taivllawwi as
//
LOCUS       WP_010378101             142 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Pseudoalteromonas].
ACCESSION   WP_010378101
VERSION     WP_010378101.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..142
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15677
     Region          3..140
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 miylslfgla fiaatllpas selalsglvv kqqgelvwlw laattgnllg scvnyylgwf
       61 iakwrdkrwf pvsqqqydka cglfnrygkf sllfawlpiv gdpltvvags lrtsfgwffv
      121 lvalgkgary alviylalqv is
//
LOCUS       WP_010382387              97 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Pseudoalteromonas rubra].
ACCESSION   WP_010382387
VERSION     WP_010382387.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas rubra
  ORGANISM  Pseudoalteromonas rubra
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 97)
  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   2  (residues 1 to 97)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Pseudoalteromonas rubra"
                     /db_xref="taxon:43658"
     Protein         1..97
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10139
     Region          25..96
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mniktllatl alsaalpima qpeqasattq qvadavvnvn hasaeeltrl pgigmkkaqa
       61 ivrsreeagd fqdmdallrv ngigvnilak lkgrvsf
//
LOCUS       WP_010382264             742 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Pseudoalteromonas rubra].
ACCESSION   WP_010382264
VERSION     WP_010382264.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas rubra
  ORGANISM  Pseudoalteromonas rubra
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Pseudoalteromonas rubra"
                     /db_xref="taxon:43658"
     Protein         1..742
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=82268
     Region          19..742
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mkrsvlamav alaapqvlan sdannddmeh iqilshydkl rteagsatll teeqlaefey
       61 ddihrilasv pgvnireedg yglrpnigfr gvtperskki timedgvlig papysapaay
      121 yfpvttrmta vevfkgpaai khgpqsvaga lnlvtravpe fsegsidlam gsdgytkaha
      181 yfgsvvnnvg fllegvnlqa dgfkdldgga dtgfekndll akfnyklqqg efehtfglkl
      241 syadelsnet ylgltdadfd atpyrryaas qpdnmdtkhs qvmfshhlky qdvsltsrvy
      301 rndyerawlk ldgltntdat lpeilanped eqyqrlyqvi sgtadsiads grpnylsmgt
      361 ndreyfsqgi qvdgsakfkl agydntlsfg vrfhedeier khfnetygmr dgsafnlgld
      421 kvytsqnten tkawsvyled kvtidaltlg lgirgelmdm ayqstvnadd wqdkttriwl
      481 pgmsgfyqls edsgilfgvh qgfspaspqq svdieiekst nyefggrfnd gvtqlevvsf
      541 fndysnlkes cgqsncgale vgkefnggea hvygleaqfs qryplnlqid ipygfvytyt
      601 kgefkndryt nfaqwghvks gdelpylpeh qasfniglsa pdwrvslavk yvgsmseaag
      661 rswdsstdsn apngsydlvl egkevsaitt vdlsavyelg kygqvyakvd nlldetkivs
      721 rrpygarpgk prqftlgyky sf
//
LOCUS       WP_010382392             219 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Pseudoalteromonas rubra].
ACCESSION   WP_010382392
VERSION     WP_010382392.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas rubra
  ORGANISM  Pseudoalteromonas rubra
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 219)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Pseudoalteromonas rubra"
                     /db_xref="taxon:43658"
     Protein         1..219
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=24019
     Region          73..217
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mistylshcn lsiseavvag qlaeldayld thslsatwsy qipelgeggs cslfgnlqea
       61 pfllsdfvsr nseserqlsr lqtiaeyvkt atgvdwfgiy qarpaegiqq llklayygap
      121 srplfpitea faatsnniqt ymseqarvin nipdyvaqgg eyytcdpkvq aevclpllnq
      181 qgeclgiida eafeqecfde yklavlvaac iraieylps
//
LOCUS       WP_010382894              82 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyl carrier protein [Leuconostoc].
ACCESSION   WP_010382894
VERSION     WP_010382894.1
KEYWORDS    RefSeq.
SOURCE      Leuconostoc
  ORGANISM  Leuconostoc
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
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   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 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   4  (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 10011594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Leuconostoc"
                     /db_xref="taxon:1243"
     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=9285
     Region          5..81
                     /region_name="acpP"
                     /note="acyl carrier protein; Provisional; PRK00982"
                     /db_xref="CDD:179197"
ORIGIN      
        1 mamekeaiyn mmadeiaerf nikrsavtpd lnfltdidad sidfvelile vedmfnisis
       61 dedsenlitl qqtvdyivah qi
//
LOCUS       WP_010383931             247 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Pseudoalteromonas rubra].
ACCESSION   WP_010383931
VERSION     WP_010383931.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas rubra
  ORGANISM  Pseudoalteromonas rubra
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 247)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Pseudoalteromonas rubra"
                     /db_xref="taxon:43658"
     Protein         1..247
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=27531
     Region          22..234
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 magcktcrch tdyrmditma mqpivdlrnr qvyayealvr gtqgqsagqv lsqvtkdsky
       61 yfdqlcrtta iemmaklsdt aklsinflpn aiydpqtclr ktleaadqfn lakeriifev
      121 seqehltdpd klidiantyn kngfkvaldd fgagyagiev lhrfqpdiik ldialingia
      181 qdpvkqaivd gvclmarrln idlvvegvet eddyrclcdl gvylmqgylf akpvvatlpq
      241 psfptsp
//
LOCUS       WP_010384388             337 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudoalteromonas rubra].
ACCESSION   WP_010384388
VERSION     WP_010384388.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas rubra
  ORGANISM  Pseudoalteromonas rubra
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 337)
  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   6  (residues 1 to 337)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Pseudoalteromonas rubra"
                     /db_xref="taxon:43658"
     Protein         1..337
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38580
     Region          32..212
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <161..334
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mslkfaylhd krmpahflit ilelaehyqi kpqhlirgsq lfledlaypg aqvapvnvli
       61 ilkklkrela eqpqlamelg qriatghghv lfdlwryapd lhsaltawar vqkgfetliq
      121 fnverhqgkl yirltesasl stqqrmvfei vlsacrlllk eqlgaqtwiq ielpwsqpgq
      181 dfhypvylge hvrfnaprca ivlsdevmyq pfkeasalrf aqakrsasqv shppqllqah
      241 lrrlfrknlg qawsleytan ylgmspatlk rrlkqdgtnf kllvdevrgq ealhlmdlnq
      301 wnnsqlastm afadvhsfrr afkrwtgavp safrcgs
//
LOCUS       WP_010384480             284 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudoalteromonas rubra].
ACCESSION   WP_010384480
VERSION     WP_010384480.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas rubra
  ORGANISM  Pseudoalteromonas rubra
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 284)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 284)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Pseudoalteromonas rubra"
                     /db_xref="taxon:43658"
     Protein         1..284
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32793
     Region          18..101
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          129..280
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mdrffksidy ieahlhekis vheiaaashy styhysrifk alvgdtpkey lrkrrltlaa
       61 krlltedvsi ltlamdcqfd sqeaftrafk alfdmtpaqy rkinepfrll ykkpfspddl
      121 aflqnnisme peiieqpamk ivgianvyed gdlslpklws gfrpyrdkip nrvgdhffgi
      181 yenyqedgdt trfvyicsaq venfddvpdg litrelaaqt yarfthtgpi anleetlryi
      241 wgswlpksry eyadkpdfel lpggfndadp nnkvylnipv tlka
//
LOCUS       WP_010386265             139 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Pseudoalteromonas rubra].
ACCESSION   WP_010386265
VERSION     WP_010386265.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas rubra
  ORGANISM  Pseudoalteromonas rubra
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Pseudoalteromonas rubra"
                     /db_xref="taxon:43658"
     Protein         1..139
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15289
     Region          1..139
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mlktsrmrgf tlielliaia ivailasval pnygeyvres rrldaqhlll qtsatleriy
       61 srnggypnta tfeglpaaey ytfsyearnk pqgasgdfrn mgyilratpv adesqnrdvc
      121 gvltldhlgn qggnlndcw
//
LOCUS       WP_010387603             194 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Pseudoalteromonas].
ACCESSION   WP_010387603
VERSION     WP_010387603.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..194
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21322
     Region          5..165
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 maiqkklkqk trqfiesknm lggitiasfl estivpiple avlvplmqar reklwqialm
       61 atlgcivgal fgyalgyylf diigdwvint fsspeqfenv kqkmqaqgfw fvlslgivpi
      121 pfqiamlaag atkyslalfl lasaiarsir yfglaivvyy agnqaeriis khktktmigl
      181 tilvaigwgv stli
//
LOCUS       WP_010387934             738 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Pseudoalteromonas undina].
ACCESSION   WP_010387934
VERSION     WP_010387934.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas undina
  ORGANISM  Pseudoalteromonas undina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 738)
  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   3  (residues 1 to 738)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Pseudoalteromonas undina"
                     /db_xref="taxon:43660"
     Protein         1..738
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=78804
     Region          6..738
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msfevdedil qdflveagei lellseqlve lennpddtel lnaifrgfht vkggagflam
       61 telvdachga envfdllrqg vrtvnselmd vilqaldtin emfatiknrd qpepadpell
      121 avlhklgqpp taeelagdsv vediapvetp svepepvaeq psndaeedpf afdelfsgpd
      181 ssssdsqide itedefesll delhgkgqap qekqssssgn dvsgditdde fdslldelhg
      241 vgsfgevsqa tastpqqtps apvappsneq ssgddeisdd efealldelh gkgapksiet
      301 papvskpepv aakkpepvaa akpqpkpepa kpapaaqaak aappkkaapp paettvrvdt
      361 krldqimnmv gelvlvrnrl vslatnsdse amgkaisnld vvtadiqgav mqtrmqpikk
      421 vfgrfprvvr dlartlkkdi nlllvgedtd ldknlveala dplvhlvrns vdhgiempdi
      481 reaagkprtg tvtlsasqqg dhilltiqdd gagmdaeklk kiaiskgvld hdqasrlsdt
      541 eaynlifapg fstkeeisdi sgrgvgmdvv ktkitqlngs vniksemgvg ttleikvplt
      601 lailptlmvv vgeqtfalpl agvseifhld ltktnvvdgq ltiivrkksi plfylehwli
      661 kgadrgqrka qghvvivqig tqkvgfvvds ligqeevvik pldallqgtp gmagatitsd
      721 ggialildvp smlkhyag
//
LOCUS       WP_010392588             146 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Pseudoalteromonas].
ACCESSION   WP_010392588
VERSION     WP_010392588.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..146
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16078
     Region          3..144
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlyitlffta fisatllpss sevlmggmim qgntnlwliw faatlgnvlg scvnywlgtq
       61 alrfkdkkwf pvsekglkka qkqfnkygvy sllfawlpiv gdpltviggv fkvrfsmflv
      121 lvtlgkglry lavialavgl fvpvqs
//
LOCUS       WP_010393217             397 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Paracoccus sp. TRP].
ACCESSION   WP_010393217
VERSION     WP_010393217.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 397)
  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 397)
  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
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 397)
  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   5  (residues 1 to 397)
  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   6  (residues 1 to 397)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 397)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 397)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..397
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42022
     Region          17..61
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          83..364
                     /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 mpttmpagst pqgvrgqner lilwlirrng pmpraalaqa mglsaqavsn itreliaagl
       61 ldaggerrrg kvgqpllpla lapegalflg lkvgrrlael vlvdfsgqir qmrvlphafp
      121 hpdairdfai asadeilagl teaqrarlsg mgiaspfylw dwaremepwr grdlraelae
      181 vldmpvwlen dgscacgaem mfgtaelpen flyfyiahfa gggvvldgrl rlgpsrnaga
      241 mgsfpvpggr qvldvasvsv leatlghdlp lddaawdlpp dilcewldks aqvlshaalg
      301 avaaldfplv vidgampdkl raalveatsa slarmrhhgv tlpevragtl grsaralgaa
      361 alplgagfmp ggtfsaprpg rigqetqgap lrspddr
//
LOCUS       WP_010394743             214 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Paracoccus].
ACCESSION   WP_010394743
VERSION     WP_010394743.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
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   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   3  (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   4  (residues 1 to 214)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 214)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..214
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=23578
     Region          22..206
                     /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"
ORIGIN      
        1 mtgapvdrsr rpaarrlldd lrqarvlvlh phdedravlt ehlkrlgcav talwplpaal
       61 ppetdtifvq vddlpgealp allqdrtpai iaimtyetpt alqaitdlna hgviskplrp
      121 fgilaqfvla ryrrgyegrl tgkiqkleet mksrrlvdra vklmaelrgi pddeayrllr
      181 dqatarrtsl tsiaegllaa eatlrsiglt iaek
//
LOCUS       WP_010395387             238 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Paracoccus sp. TRP].
ACCESSION   WP_010395387
VERSION     WP_010395387.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..238
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24715
     Region          <5..192
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mvrkigtsls erltgtkygd wlsglggndk lygldgndtm fggdgndtme ggngrdslsg
       61 gngndllrgg ndndtlyggn gddrlsggng nddlnggrga dylhggagrd eleggagndt
      121 lvagagndel egddgndrly ggdgndkleg grgndvlngg agadifefer gdgrdiitdf
      181 qngvdrldfd dfsraqvqav iknaqqvgdd lvlrlsadtt vtirdmqlgq ldmsdfif
//
LOCUS       WP_010396116             562 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein, partial [Paracoccus sp. TRP].
ACCESSION   WP_010396116
VERSION     WP_010396116.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..>562
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
     Region          14..>554
                     /region_name="COG4625"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal beta-barrel porin domain [Function unknown]"
                     /db_xref="CDD:443664"
     Region          209..460
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mpyslsltsf wnlaqgpttd qpgsdftlat sydprlndtr iifptpdqtl ddiaggsdtp
       61 pgptsdhqye nsagqpisld evqtatviqa gityenvril igpktdadws vtgggdvsal
      121 naagfqilav waeltpgnwq iigytsrgms iedatrlvpg adasssldad dglaatafqq
      181 asngivegtd dddsidenyt gdpegdmvdg gntppphgpy ddviygfggn dtihggdgnd
      241 tidggdgndi ifggrdddsi lggmgddsiy gnegndyidg glgsdtidgg egndiilggd
      301 gpdsligglg ndviiagsgn dtidggdgnd tihgeegddt iyggdgndfi nagkgndfve
      361 ggagddfilg gedndtidgg dgedlifgde gddsifggag ndilqgglgn dtiyggeddd
      421 ylfgedgdds lvggtgndti yggdgndfid agkgndfveg gsgndsiyad yndagnatly
      481 ggegddflqg gdgdhlygea gndtlinvrg natldggegn dslivyggna tltggdgfdr
      541 fsfvdlsgdl gsvlitdfnt gt
//
LOCUS       WP_010397255             266 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: 3-deoxy-manno-octulosonate cytidylyltransferase
            [Paracoccus].
ACCESSION   WP_010397255
VERSION     WP_010397255.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 266)
  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 266)
  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 10787365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..266
                     /product="3-deoxy-manno-octulosonate cytidylyltransferase"
                     /EC_number="2.7.7.38"
                     /GO_function="GO:0008690 - 3-deoxy-manno-octulosonate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0033468 -
                     CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28880
     Region          1..259
                     /region_name="KdsB"
                     /note="CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell
                     wall/membrane/envelope biogenesis]; COG1212"
                     /db_xref="CDD:440825"
ORIGIN      
        1 msvviiipar hastrypgkp lvelrgatge gqslirrswe aaravqgtdr vivatdderi
       61 rdhaegfgae vamtstsarn gtercaeava rlglspeivv nlqgdapltp awfveelvag
      121 lradpgadva tpvlrcsgam rseliadrva grvggttavf ghdrralyfs kevipyaaad
      181 fgpgdptpvy hhvgvyayrp ealaeyptwd egrlealegl eqlrflergr rilcvevear
      241 grefwelnnp sdvakleamm qrmgia
//
LOCUS       WP_010396870             428 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Paracoccus].
ACCESSION   WP_010396870
VERSION     WP_010396870.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 428)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..428
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=46190
     Region          <19..411
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mgygiaaate wptwpvwgqa sgqgvqrfal vlrvtnpeyl pggagsalsr qirdqlrsrl
       61 vaelglslhs scddgdeicg lvadpgpqag qglllrlrai cseriylpgv slypmvqgvi
      121 vadpfgches talyahgrvv ldgssphtls shirlvdmeg qegraypvla gddqislqfq
      181 pqiccttgsv lalkvlprih lvrevgqgrn ltgilprldd nrqlrittal lreacaslrg
      241 wdrmgryvpc lslalpdril aspsvvevil aqlerhdlsp hrleieviep vgkgatqavv
      301 aanlqelrra gcqlglgefg tgmtrpdnlr hhgfhrvrvg rsfvagcdhr gdqqrtllai
      361 talarhlglq viadgvstrd ersflsqigv dgvqgpavfl plsaeevddl llhrgfaacf
      421 spkvwgra
//
LOCUS       WP_010397529             199 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Paracoccus sp. TRP].
ACCESSION   WP_010397529
VERSION     WP_010397529.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. TRP
  ORGANISM  Paracoccus sp. TRP
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Paracoccus sp. TRP"
                     /db_xref="taxon:412597"
     Protein         1..199
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20228
     Region          1..187
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mrvvlgvsga sgaalaldca raltrvgadv dlvvspmakr tlatevgtga ladlcamaar
       61 vhaqgdpgae iasgscpvag mivapcsmrs laaiahgldd glltraagvq lkerrplill
      121 areapltlah ldnmqaatrm gavilppvpa fylrpqslae vtaqiaarav dllrlgppla
      181 rawspanppv npcegdthd
//
LOCUS       WP_010397583             186 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ribonuclease HI family protein [unclassified
            Janthinobacterium].
ACCESSION   WP_010397583
VERSION     WP_010397583.1
KEYWORDS    RefSeq.
SOURCE      unclassified Janthinobacterium
  ORGANISM  unclassified Janthinobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 186)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 186)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="unclassified Janthinobacterium"
                     /db_xref="taxon:2610881"
     Protein         1..186
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=19535
     Region          36..163
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(41..44,76..78,80,106,146,160)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mtteaqarka rkqakmqarr aqlvlhrqdh ggalawrgwf dgsahpnpgk lgigalllgp
       61 hgerievsqa agygsssdae yaaltallqa algvhpppvq lllygdsqvv indvlgttpr
      121 gakglelhra svvallqqft dvslhwlprh rngeadrlsq laiasftpea svpgpspqgt
      181 tpaitg
//
LOCUS       WP_010398239             275 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Paracoccus].
ACCESSION   WP_010398239
VERSION     WP_010398239.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 275)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..275
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=30431
     Region          28..259
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mtdntdslqk adspldfivn eqsrvtmasv rravsrgdgv lafqpvvrad spdraafheg
       61 liriidetgr ivplrdfmpl aettelgrqi dclslslglk slaqepslrl sinmsarsig
      121 yspwlrilqq glagndsige rlileitess amglpepvdr fmhelqshgv sfalddfgag
      181 ytsfrylrdf cfdmikidgq firdiaqtrd nqvlaralqs iarhfdmftv aesvetaeda
      241 afliemgvdc lqgyyfgapt ivppwkspgt qahrk
//
LOCUS       WP_010398348             207 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit [Paracoccus].
ACCESSION   WP_010398348
VERSION     WP_010398348.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 207)
  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 207)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 207)
  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   4  (residues 1 to 207)
  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   5  (residues 1 to 207)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..207
                     /product="TRAP transporter small permease subunit"
                     /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=23267
     Region          3..171
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mgallglsrg idrinsiigr gmswmilvav lvsagnavvr kvlntssnaw lelqwylfga
       61 aflgaaaytl kenehiridi iygmwsrrrq hwidlighvl flmpfvtlmi wylypwvmrs
      121 yargevsnna gglvlwpakm mlliafimlf fqgiseiikk iavmrgvied ptpfvsahea
      181 aavesemmar emqavleqdt edgdsrk
//
LOCUS       WP_010400701             298 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [unclassified Janthinobacterium].
ACCESSION   WP_010400701
VERSION     WP_010400701.1
KEYWORDS    RefSeq.
SOURCE      unclassified Janthinobacterium
  ORGANISM  unclassified Janthinobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="unclassified Janthinobacterium"
                     /db_xref="taxon:2610881"
     Protein         1..298
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32016
     Region          16..264
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mniyeikavs dkpmqvgecp lwhgkeaaly wvdidgravh rlhpasgqqa qwsmptepsa
       61 lainagggli valrsgfahl dtktgslaqi apapfdvatt rfndgkvdps grfwvgtife
      121 prsaaaaemf vlekgqvrkv wsggmtvsng lgfspdgrtm yhsdttthri drfdfdaatg
      181 aiseaqpfqr fstdkkaady ggrpdgaavd segnywsamf eggkilrfap dghllgeitv
      241 pvrcptmvtf ggpdlrtlyi tsashnrsat eladypltgh vlsvrvdvag qpetpyqa
//
LOCUS       WP_010402224             383 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Sphingomonas echinoides].
ACCESSION   WP_010402224
VERSION     WP_010402224.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 383)
  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 383)
  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
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 383)
  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   5  (residues 1 to 383)
  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   6  (residues 1 to 383)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 383)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 383)
  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 20170230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..383
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39989
     Region          <29..>69
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          88..378
                     /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 mnhgfagqfa paflredgrr tatdnervvm allhrtgtas radlaratgl taqsitrlvd
       61 pliergllve gtpqiagrgk psaklrlvad aafavgvsvm tdavslvlmd ltgairarad
      121 apllsvdfar aaaqiaslid atvtkaaldp arrigigvgv tgyfigdgar lnppaqlepw
      181 alipidtmla erlggpvwvd ndgnvaalge amlgagrttg dfaylyfaag fgggviagga
      241 qlrgshgnag efasilpegw pqpnlenlrl ylanhgqpyd dlhtmlaafd padplidgwl
      301 dlctpsfnlv asvisaaldp dlivlggrlp pvlaeriiar irftnperrg hyrptpsiap
      361 saigpdaaai gaamlplrta fft
//
LOCUS       WP_010402347             645 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Sphingomonas echinoides].
ACCESSION   WP_010402347
VERSION     WP_010402347.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 645)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..645
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..645
                     /product="amidohydrolase family protein"
                     /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=68617
     Region          19..426
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mkwvaaflam sslsavcaaa spddtilirg arvfdgsgap atvgdvlvrg drivavgphl
       61 rkprgarsvd argltlipgl hdlhthlrsp gydapddlgk ayagyllagv tsvndysvsg
      121 emiapirqmv asgavaaphl elavrvgvpg ghgteygwga fftlqaatpa aahvamatal
      181 pyqpslikvf adgwrygrds dlnsmnvptl saivadahka glpvithtvt vqgdrvaama
      241 gvdavghgag dalidddlia lmkthhtayi ptlvvyepqq trrfepdeqr altppeaafe
      301 ashaaqsskp vaaydakrwa imqdnvrrlk aagvrigvgt dagiegvyhg pgtlreiwwl
      361 tklgftpaea lvaatatsad ilgrsadngr iapgqradlv liagrpderi tdlwkvarvf
      421 vsgrevalap lralvnraap tplplhvmpg pidtgaradg rtdldtlpve stdsgvdhsh
      481 ldfvrpgsdd pkspdrpvfl iahmgakprp faqlvlpltq gavqladarg ftgvafdarg
      541 sgrydllfds yaindddwfr tgfeagevrr tfhipfsafa srepkaqldl aklralivrl
      601 egkpggkawl qldnihfyre rasddraapl papgarnpqh ysetn
//
LOCUS       WP_010405881             240 aa            linear   BCT 20-JAN-2025
DEFINITION  MJ0042-type zinc finger domain-containing protein [Sphingomonas
            echinoides].
ACCESSION   WP_010405881
VERSION     WP_010405881.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 240)
  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 10020205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..240
                     /product="MJ0042-type zinc finger domain-containing
                     protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25464
     Region          1..35
                     /region_name="MJ0042_CXXC"
                     /note="MJ0042 family finger-like domain; TIGR02098"
                     /db_xref="CDD:131153"
ORIGIN      
        1 milectecht rylvpdsaig adgrtvrcas ckhswfqaga pvldlvarae aapiapppva
       61 arteaavetp pepvsapaas aatasyddyd afaheppfrp rrnparrwtv aaiaagiaml
      121 aaaalvfysd lpglagqlfr patgtplkiv skpvdqhtfn gneifavsgi vlnptdtrqp
      181 ipdiradlrd aqkrivfswi irpeattlpp kgqvqfnsaq vnvpvnaqel vlsfsgeaah
//
LOCUS       WP_010402928             762 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Sphingomonas echinoides].
ACCESSION   WP_010402928
VERSION     WP_010402928.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 762)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 762)
  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   3  (residues 1 to 762)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..762
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..762
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=81425
     Region          1..520
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mddllqefia etretleals geivawesap ddrdrldaif rfvhtvkgsc gfldlprlar
       61 lshaaedvla avrsgerapd trlvnavlai vdrigeivea idaghaldds gedlliaald
      121 tgaemaapqa vsaprspsrs vrlnvdlldr mmsgmsdmvl arnelarrvr dggadpvvea
      181 alerlsltva emrdtvtrtr mqkidalfsa lprmvrdtat elgksvtlhi egsdveldre
      241 miemmrdplv hiirnsidhg ieapalrral gkrengwlnv aarqsgnqiv ieisddgqgv
      301 dtdrlvakva naglrsdaql rsmseqakld lifepglstk dmataisgrg vgmdvvranv
      361 eqiggrielh napgkglris ihvpltlsim stigvgvrdq rfaisrqvie eivrvggdmi
      421 ridrigdtls atvrdrrmpl idlgdllgfg prspvmlaiv sasggsyala vdsvldheel
      481 vikpaapaim atgvyagqtl pdsglpmlml dcagiahvag lvfgreamve eieaeavvpg
      541 vqallfddld gvrrvlplsv idrvepvsas airfsagrlr lsveggiipl valgewapqs
      601 tvsvvrlrdg sveigyaige aidivelpet vvpahdagpi agvvaidgdq ievidlhwlf
      661 ashadagtvs daplclfdgp etawmttflk pvlegagyrv atmlrpgetp rvvvrmsddp
      721 tgsaatvpvv rlrrdadgdd gsifrydrpa llaavarstg gr
//
LOCUS       WP_010407442             122 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Sphingomonas echinoides].
ACCESSION   WP_010407442
VERSION     WP_010407442.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            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="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=13444
     Region          19..87
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 msqteptqll lqsnktdtmq vrsrdgdkig svyammvnkr tghtlyavlt iggflgmgra
       61 yyplpfsllq fdpvndtyiv tidrrvlegg pswaanppef dqayadrvsk yydvagedls
      121 lg
//
LOCUS       WP_010406928             336 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Sphingomonas echinoides].
ACCESSION   WP_010406928
VERSION     WP_010406928.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..336
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=34448
ORIGIN      
        1 mdavstrvlt lnggsssvky gvyavgeavv elsageveha dvdaavfaei gggqpdaigh
       61 rivhggidlf apvridagvl arlqaatafa plhgpaslrm ialaqarypg vpqiacfdtg
      121 fharlpaiaa tlpipkalrd agvrrygfhg lscesilaql gdavphrlii ahlgngasvt
      181 avldghsvdt smgltpsggv vmgtragdid pglllylmre rrldaaqiet lidrqsgllg
      241 lsgrssdlrv lhasgdaaat lalaifcrsv akqiagmlvv lggadlivft ggigehdaav
      301 raaisadlaf arpiaqrvlp sqenaqiarh taqllg
//
LOCUS       WP_010407598             426 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Sphingomonas echinoides].
ACCESSION   WP_010407598
VERSION     WP_010407598.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas echinoides
  ORGANISM  Sphingomonas echinoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 426)
  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 426)
  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
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 426)
  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   5  (residues 1 to 426)
  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   6  (residues 1 to 426)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 426)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 426)
  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 15726307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Sphingomonas echinoides"
                     /db_xref="taxon:59803"
     Protein         1..426
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45943
     Region          56..>175
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          118..413
                     /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 msgerrsssn ggasartsrh lfpfrsdrap astgidaaad spapyltldi danhnqrvvf
       61 qeirthkrvt rselatitgl tiptivnvsr hllqaglive akrpargrgq pawelelnpd
      121 gafsaglnid rdhltlvvld lsgqirgrvs aeigfaspdd arrffaqswr elvtkahisp
      181 drvvglgial pdelgtlafp gkpltydawa rtdaadlfrd tfagptfven davaaaigea
      241 qfghgleaps fvyvlisvll gggividrty frgengrsge fgfmrvktpt gaictlqdvv
      301 slgalsewlk irgvaitgpe dlkrldaagt aaveqwleea sgyltsifsq iqrfidpdsi
      361 llggrlpehl ldrlavlcqq rqadaqpres gdirraklss dapaigaail pfqtllfpsl
      421 emlgrf
//
LOCUS       WP_010410043             680 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Citromicrobium sp. JLT1363].
ACCESSION   WP_010410043
VERSION     WP_010410043.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 680)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..680
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=75949
     Region          62..>535
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mtiekldass pdltqqnier lldlfpecrt egpredapmv dfdllrqals dhlvegpaer
       61 yrldwpgkrq alltantpid ktlrpmrees vdfdttrnlf iegdnldalk llqetylgkv
      121 kmiyidppyn tgndfvyhdn fvqsqtnydi esgqaddqkg rlvanpetng rfhsnwlnmi
      181 yprlklaknm lgddgiifis igddevfnlq evcdeifgid nflgnacris kkannqgdyw
      241 spnfdyvlty akskehcpvf fggvnykayk evdaegprag ekyqlvrlym tsldplrgct
      301 nqryfieapd gtllippgtv fpeekkdgak vapersedkv wrwsqqayle kkdeiyvkav
      361 rssnlvdqng devfwnvftk tylndviaks sskpnsliee hinqnsshel kalgipfpha
      421 kpsslieflc eiskvgendi vmdffagsgs sahgvfrhnl ksgskarsis vqlpevldpe
      481 dkdqkagwhl ceelglkktv asisrerirr agrkiadegg kptgkldtgf rafridsgnf
      541 vdtsvtpkea tqealagmvs hikdhrseed llfgallrwg vditlpieqr evagrevwlv
      601 dappnddgdg tgkgaaliac fakpassgkg gidteladai aelaplralf rddgfaddat
      661 kenvhsrfkq lapdtqvrvl
//
LOCUS       WP_010410934             367 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Leptospira inadai].
ACCESSION   WP_010410934
VERSION     WP_010410934.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 367)
  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 367)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 367)
  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   4  (residues 1 to 367)
  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 367)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..367
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42394
     Region          110..365
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          280..360
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mansflsffl lfsallslly aigeifsfsr gnrrivlfgi flslsyflfh aylvssrnil
       61 lfpylflthl pcsailgall erylllawgn paekperfll kilpalgiai wltpfyfqnr
      121 eskihlleki avsgtdwhvk ipvlftmcif lyfllsvlvr lfrtvrfsvv krdinlativ
      181 flssfailst figsysvlsg gkdplgmiga wlgifllfiy vyrqrypeff lavrkvveee
      241 krvrasqlgk fdltdikskl kdlfendriy reeeltlstl agrlglsshq lseylnneek
      301 ksffqllney rvgeakekir sspkdtllti ayssgfrsks tfndvfrret gltpseyrkr
      361 ilkrkek
//
LOCUS       WP_010411571             803 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Leptospira inadai].
ACCESSION   WP_010411571
VERSION     WP_010411571.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 803)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="Leptospira inadai"
                     /db_xref="taxon:29506"
     Protein         1..803
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=89251
     Region          66..802
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 maykshlrtl ilclflllpi aailsqpngn ngeekskdgt etkeqpskee edinekrrrf
       61 lesgqinvig skdedlkkip gsanvigkki lketspidsm ealrrvpgat iryqdavglt
      121 pniafrgvsn eesrktlile dgvftslspy gqpesyfiph idrmervevv kgsgsilfgp
      181 ttlggivnfv trkppekptl nlkliggtng yasnlvqygg tvqntntayd vsylhtqgng
      241 yrnyqgfnvn dfnvklmqki gdkdtvflky qvyqqdsqat ylgltqglyw kdpkinparf
      301 drkhierqaa vighdhafse nwklitrsyw tnvgfdfkqe sysynsanel glptpptgnv
      361 favyapapig nrpgdviyml nttpnrhqff rtggleskle gkfvtfgleh eisvgarahy
      421 etvnaaynqf pyptmnqglt tqqqtrnaka yatyvqdsik lterlkiipg vryeyisqgv
      481 ythrkfattt dvayglattv gqnilvnqan esytkvvlpg fgitydlmek fmwfagahta
      541 fappsfstil npslglgykl naersnnyet gvrgnitkyf ytqvstyalf fsnqivntne
      601 agssigavpi nagksvnrgv esnfvfdfgk faesrweipl eiaysythai sttyvpvgti
      661 qnsdgtvsvt nqplfsvnss gnvikvntsg nylpyvpmqt vitaigfksp rgfyarveyq
      721 hfdkqysdlq ntknqsadgs qgvvpaygiw nadfgyelpg grwsifvngk nledrvyisg
      781 rlpvgiqqgp yrqinigatl kld
//
LOCUS       WP_010413726              99 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Leptospira inadai].
ACCESSION   WP_010413726
VERSION     WP_010413726.1
KEYWORDS    RefSeq.
SOURCE      Leptospira inadai
  ORGANISM  Leptospira inadai
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            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="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11192
     Region          3..97
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mitssqiqev lyshkeelfk lgvqklflfg siarrentkd sdvdilvrfn sgqknfdnfm
       61 dlsfrledil kvhvdllted sisgsvrdsi laeavdiei
//
LOCUS       WP_010414926             228 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Citromicrobium sp. JLT1363].
ACCESSION   WP_010414926
VERSION     WP_010414926.1
KEYWORDS    RefSeq.
SOURCE      Citromicrobium sp. JLT1363
  ORGANISM  Citromicrobium sp. JLT1363
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Citromicrobium.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Citromicrobium sp. JLT1363"
                     /db_xref="taxon:517722"
     Protein         1..228
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24919
     Region          13..111
                     /region_name="COG3942"
                     /note="Surface antigen [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443142"
ORIGIN      
        1 manaatsgqe lpaylqcvpy ardvtgidiy gdahtwwqqa agrygrgntp rvgsvmafap
       61 tskmtlghva avarvidsrt vlldhanwsp idgrrgqier nvkavdvspn ndwsqvrvwy
      121 hplqalgtta wpvhgfiypd gkaqprqrfa qaqtqrsapq ptreepsraf laafsntper
      181 asperrapra aasrpaprla yatarplapr gnndradavv eravalye
//
LOCUS       WP_010416477             195 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Anaerophaga thermohalophila].
ACCESSION   WP_010416477
VERSION     WP_010416477.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..195
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21962
     Region          4..157
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mtnlkdlvrr nrsyrrfyed itipeyvles lvdlarlsps arneqplkyf iscdaktnel
       61 ifphlswagy lkdwdgpapg erpsayivil ndvnisdtyf cddgiaaqsi rlgaaeqglg
      121 gciigsvdrl klqkalklpg hlkiievial gkpreevvie dvkdgnikyw rdenqvhhvp
      181 krsleeiivk csgke
//
LOCUS       WP_010418233             147 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Anaerophaga thermohalophila].
ACCESSION   WP_010418233
VERSION     WP_010418233.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..147
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16221
     Region          5..141
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mwidlgylgl flasflaati ipfssefvls gilaaggnpa lslvtatlgn wlggltsywi
       61 gwlgkyewie kylripkvkl ekwhkkvegk ewwialfcwl pgvgdiiavv lgllksnfwf
      121 aatgmlagka lrylvwgmlt leiisgl
//
LOCUS       WP_010419356             154 aa            linear   BCT 20-JAN-2025
DEFINITION  division/cell wall cluster transcriptional repressor MraZ
            [Anaerophaga thermohalophila].
ACCESSION   WP_010419356
VERSION     WP_010419356.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Chen,S., Jancrick,J., Yokota,H., Kim,R. and Kim,S.H.
  TITLE     Crystal structure of a protein associated with cell division from
            Mycoplasma pneumoniae (GI: 13508053): a novel fold with a conserved
            sequence motif
  JOURNAL   Proteins 55 (4), 785-791 (2004)
   PUBMED   15146477
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449500
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..154
                     /product="division/cell wall cluster transcriptional
                     repressor MraZ"
                     /GO_function="GO:0000976 - transcription cis-regulatory
                     region 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=17676
     Region          4..127
                     /region_name="MraZ"
                     /note="DNA-binding transcriptional regulator and inhibitor
                     of RsmH methyltransferase activity [Translation, ribosomal
                     structure and biogenesis]; COG2001"
                     /db_xref="CDD:441604"
ORIGIN      
        1 mftfigdfec ktdakgrivf psafkkvlge gdlrmivrkd lfepclvlyp fsvweeelar
       61 irtglnpynr ehnrflrhff rgsaeisldg ngrflipkrl leqagierev vllgvdryie
      121 iwdkgsymdg slshkelgnl aekilgdthp eedn
//
LOCUS       WP_010419958             695 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Anaerophaga thermohalophila].
ACCESSION   WP_010419958
VERSION     WP_010419958.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 695)
  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   3  (residues 1 to 695)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..695
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=77551
     Region          2..685
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 midkfkakfv eesldnvndl eealfalend mqskdlieri framhslkgg gamfgfnhls
       61 dfthhlenif dkvrngkikv tpdlisltfs avdeikylle kgdltarddl deynlmmgei
      121 qnflqgggtg nqenssvsgd dasaanseek tylisfipge dllqngtnpl fllddlhalg
      181 kghsivythk ipsfdniepe nnyclwqiil staesvneik dvfifvedec dlsieevgkg
      241 gfemnpavek lienarnsnt likvsdlkvl lnknetegkk teqeqentet eqgrkksqlk
      301 dhkissirva sskidelvnl vselvtiqaq lsvyaekkgd ndilelaenv qklsrqlrdn
      361 afeislipmq telmrfqrlv rdlskelgke iefvieggdi eldkniiehl tdpllhilrn
      421 svdhgiekpd ervavgkspk gniyfkayha gasvlievtd dgrgidvdsi rakavskgmi
      481 eeneelshke ilnlifqsgf strdtvsgvs grgvgmdvvr kkiseirgev tvdsvvgqgt
      541 tvtlrlpltl siidgllvki genqyvvpis siekifaldk rqlkdsfnrv viidneqlpy
      601 vdmreifkee iketethqmv lvrhedrrlg lvvdevlgeh qavvkplgry ltshevvsga
      661 silgdgsisl vidtnrilql tssgkfrgkt ktste
//
LOCUS       WP_010420480             224 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Rickettsia helvetica].
ACCESSION   WP_010420480
VERSION     WP_010420480.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia helvetica
  ORGANISM  Rickettsia helvetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; spotted
            fever group.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Rickettsia helvetica"
                     /db_xref="taxon:35789"
     Protein         1..224
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25239
     Region          143..215
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 minnifikif lvclicisai yfgyqyyqns kpvitiypde lptkikpsii ennqiaavhs
       61 tiyenliakd tniktvkllp dpekpmsids rnqsqsdesf deisnliali epnnnsknet
      121 dlniiklekg skdksnnpkn cknnesykvq lgsvkseaea mkegerikkk fpkilknvvi
      181 ttkkvkyddg kffylilagd ygslsqakav ckklaynkqs cvlk
//
LOCUS       WP_010421224             280 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Anaerophaga
            thermohalophila].
ACCESSION   WP_010421224
VERSION     WP_010421224.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..280
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32655
     Region          11..274
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mksidlynin alscsrnttk hystsfslgi kllapeirea vysiygfvrf adeivdtfhn
       61 hdkaklleny rkdtylaike gisanpilhs fqrvankyqi dhelidafft smsmdlnqke
      121 ydhqnfktyi ygsaevvglm clkvfykddp egyealkypa rklgeafqkv nflrdvqadl
      181 kergrtyfpn vdllnftite kekiekeiee dfraaykgiv klkkearlgv yvayvyylkl
      241 fqkikkmqpa aimreririn nwvkmgllfq glvkhetgrv
//
LOCUS       WP_010421426             333 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas syringae].
ACCESSION   WP_010421426
VERSION     WP_010421426.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 333)
  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   6  (residues 1 to 333)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..333
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36729
     Region          5..191
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <206..320
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mqdaglatap vlrraqlpgd lftrqnvrld sanffmlwra ieaeaksina evpaplqiar
       61 vmssdwfdpe lfaalcsanl sgaldriaky vrliapmvir vvptkahttv tmdfldaaep
      121 pavflafklv ffvqlarlat rsavqplqvn wpspstlgad leayqayfgv avthapqasv
      181 vfaaadvgrp fltenhkmwl ffepglrqrl sdldrtsgmv ervrsalles lpagavsmqe
      241 islklgvstr tlqrrlqdeg ttfqqtldtl reslarhylr stamssaeis fllgfedans
      301 farafqswtg stprkvraem dnsrhpstah see
//
LOCUS       WP_010421961             360 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Anaerophaga
            thermohalophila].
ACCESSION   WP_010421961
VERSION     WP_010421961.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 360)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            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="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40306
     Region          5..359
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 meyqiysvit gtgsyipsrv vknedfmqnk ffspsgepvk kdnreiiekf keiteieerr
       61 yvedeyvasd igtfaaqqal easgvdpetl dqiivahnfg dvsketlqtd ilpslaskvk
      121 yklriqnpfc vaydilfgcp gwiqaliqad fhiksgaarr vlvigtetls rvsdphdvds
      181 miysdgagav vleareserp vgiishitrt dtfdnawllh mgpsynpdve kskqflkmng
      241 rkvyeyalqt vpptvrkvie dagidisdvk kvlihqanak mdrailerlf klfglrnvpd
      301 ytmpltisnf gnnsvatvpv lfdlvikkel qnhrlhsgdh fiftsvgagm ninaivyrma
//
LOCUS       WP_010423764              96 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Prolixibacter sp. SD074].
ACCESSION   WP_010423764
VERSION     WP_010423764.1
KEYWORDS    RefSeq.
SOURCE      Prolixibacter sp. SD074
  ORGANISM  Prolixibacter sp. SD074
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Prolixibacter.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Prolixibacter sp. SD074"
                     /db_xref="taxon:2652391"
     Protein         1..96
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11266
     Region          3..96
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mitkndilnr lkdlkpilyr dysvkqiglf gsfsddsytd dsdidllvef erpigwkyfs
       61 leiylenifg rkidlvtkna lkeqikdril nqvkyv
//
LOCUS       WP_010424885             129 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Anaerophaga
            thermohalophila].
ACCESSION   WP_010424885
VERSION     WP_010424885.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 129)
  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 129)
  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   3  (residues 1 to 129)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..129
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15013
     Region          24..>104
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mpiddqvnmf fnakpaifek akdlrknmtp aelklwehik dnkilglrfr rqhpigifia
       61 dfychkiklv ieldgrihnn penkgydenr taelerlgik virfkneevl enveeviskl
      121 nkacgdllk
//
LOCUS       WP_010427670             755 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Pseudomonas].
ACCESSION   WP_010427670
VERSION     WP_010427670.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 755)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 755)
  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   3  (residues 1 to 755)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..755
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..755
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79891
     Region          6..754
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msfgadeeil qdflveagei leqlseqlve lesrpddadl lnaifrgfht vkggagflql
       61 helvecchia envfdilrkg errvdselmd vvlealdtvn smfgqvrert dvtpatpell
      121 aalarlaepq sadevaapep epepvvevqa aavavpaagd eitddefeql ldslhgsspv
      181 saapapasap aaapagdeit dqefeslldq lhgkgkfaad aatapapapv aqgsaepagd
      241 eitddefeal ldqlhgkgsf daavaapvaa aavavaakap gaaasdeitd hefenlldel
      301 hgkgkfepea ivakapapaa aaaapappva kpapapaaka epakpaaapa parapvpsge
      361 kpvateaett vrvdtarlde imnmvgelvl vrnrlvrlgl nsgdeamska vsnldvvtad
      421 lqtavmktrm qpikkvfgrf prlvrdlarq lkkeinlelv geetdldknl vealadplvh
      481 lvrnavdhgi etpeereatg ksrggrvils aeqegdhill sisddgkgmd pnvlrsiavk
      541 rgvmdkdaad rlsdtdcynl ifapgfstkt eisdvsgrgv gmdvvktkis qlngsiniys
      601 tkgqgskivi kvpltlaimp tlmvmlgnqa fafplvnvne ifhlnlsttn vvdgqevviv
      661 rdkalplfyl krwlvssaah eeqreghvvi ltvgtqrigf vvdqlvgqee vvikplgkml
      721 qgtpgmsgat itgdgriali ldvpsmlkry aarri
//
LOCUS       WP_010427811             378 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Pseudomonas].
ACCESSION   WP_010427811
VERSION     WP_010427811.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 378)
  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 378)
  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   3  (residues 1 to 378)
  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   4  (residues 1 to 378)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 378)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 378)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..378
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39728
     Region          30..365
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(104..106,127..128,177,229,254)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mshtfyrkgf laiavatalg vssfaqadvk igvagpmtga nasfgqqymk gaqaaadain
       61 kaggvngeki vlvagddace pkqavavanr lvdqekvigv vghfcsssti paseiygdag
      121 viaitpgstn pavterglke mfrmcgrddq qgivagdyiv dvlkgkkiav indkdtygkg
      181 ladatakqlt argvkpilee gltrgekdfs alvtkirsvg advvyfgglh peagplvrqm
      241 reqglkdvkf msddgvvtde lvttaggaqy vdgvymtfga dpralpdska vvdefrkagy
      301 epegytlyay asvqalaagf ngaksnkgda aatwlkanpv ktvmgekawd akgdlkvsdy
      361 vvyqwdaagk ykqlekqk
//
LOCUS       WP_010428902             271 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Pseudomonas congelans].
ACCESSION   WP_010428902
VERSION     WP_010428902.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..271
                     /product="formate/nitrite transporter family protein"
                     /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=28301
     Region          5..251
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mslntpqqia eiavesgvkk ahmglsslmi lgflagafia lgflldihvs tmiphewasl
       61 gnllgavvfp vglilvvlag gelltgnmms lpmalfagri glgqlvrnwl lvtlanliga
      121 lfvaycfghv vgltegafma ktvaianakv gasfeqafis gigcnwlvcl avwlsyaskd
      181 vigkvvgmwf pvmafvaigf qhivanmfvi paaifagals waqfgdnfvp vflgnavgga
      241 vfvglayhla ffnaatrpae lsrtngaqtp e
//
LOCUS       WP_010429099             276 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Enterobacter mori].
ACCESSION   WP_010429099
VERSION     WP_010429099.1
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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Enterobacter mori"
                     /db_xref="taxon:539813"
     Protein         1..276
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=30590
     Region          24..192
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkrslstlll alllagcate kgvidkgaye ldtrhqaqaa yprikvlvih ytaddfdssl
       61 atltdknvss hylipaippa pdgkpriwql vpeselawha gisfwrgtnr indtsvgiel
      121 enrgwqktsg vkhftpfepa qiaalvplak diitrynirp envvahsdia pqrkddpgpl
      181 fpwrqlalqg igawpdagrv afymngrppy qvvdtaalld llarygyevp dnstpaqqkr
      241 iimvfqmhfr pqlwngvadv etmaiaeall ekygqg
//
LOCUS       WP_010429906             290 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Pseudomonas congelans].
ACCESSION   WP_010429906
VERSION     WP_010429906.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            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="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31356
     Region          13..261
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mnwlpvsehr fklaegafwd aaeqalywad isgflvcrlv agqirqwrmp epvsafipte
       61 qgdalvtlas gvyrldlesd ktsllpfcva dptpgnrane arcdarghlw lgsmqnnida
      121 eggdvplvrr sgglfrvepd arvtrlldgq givntllwne egsvlysadt lddviyhypv
      181 ladgalgprk vwaakhdrgs pdgsamdaeg yvwnarwggn clirfapdgs vdrvielpvs
      241 hptscvfggp dlqtlyvtsa apadangrfd gallmaqvgv kgtpcrrfag
//
LOCUS       WP_010432248             631 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Pseudomonas congelans].
ACCESSION   WP_010432248
VERSION     WP_010432248.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 631)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 631)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 631)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 631)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 631)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 631)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..631
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68210
     Region          1..631
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msqanshaea ggaakpigll iaavgvvygd igtsplytlk evfqggygvd vthdailgvl
       61 slifwsliwv vsfkymafvl radnqgeggi malmalarra sakhprlqmm mvvfglfgaa
      121 lfygdsmitp avsvlsameg lelafdgldh wivpmalivl vglfliqrhg tarigvlfgp
      181 vmvtwflvlg algvygimqs pevlkavnpa wgvnffiihp gigvailgav vlaltgaeal
      241 yadmghfgrk pisrawfilv lpalllnyfg qgalvlgnpe avrnpfylla pgwallplig
      301 lstmatiias qavisgafsm tlqaiqlgyi prmhiqhtss daqgqiyiga vnwalmagvi
      361 llvigfessg alasaygvav tgtmlcttil vstvmlmlwk wppllavpll iclllvdglf
      421 faanvpkifq ggafpvlaga vlfilmttwk rgkqllaeri degglplpif igsirvqpph
      481 rvqgtavflt arsdavphal lhnmlhnqvl heqvvlltvv yedsprvpsa qrfevesyge
      541 gfyrvilhfg fidepdvpaa lalchlpeld fspmrttyfl sretvipskm dgmarwreal
      601 fafmlknang nlrffklpfn rvielgtqve m
//
LOCUS       WP_010432130             274 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio cyclitrophicus].
ACCESSION   WP_010432130
VERSION     WP_010432130.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 274)
  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 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   3  (residues 1 to 274)
  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   4  (residues 1 to 274)
  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 274)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..274
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30138
     Region          20..272
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <154..270
                     /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 mpkplpfpnl dlsplgltgp rpaeiitlps hmdchehhys qvviglkgqa efevrgkgnl
       61 vgpgqgcvvt assdhafggv vgqsdilvln mpvptdddpl mlekinqles snvyfqldaq
      121 iqklihmlvq emqsspddll lsracndtvi almqrhisaf etpikdsrfd lealdryieq
      181 hlankisvaq lagsvflges qfhmlfkdqm gitphqyvlg kridrsrhli eqgnlslgqv
      241 aelagfsgqs sfthtfsrlq gmspsqykkk isvk
//
LOCUS       WP_010437247             289 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Ruegeria conchae].
ACCESSION   WP_010437247
VERSION     WP_010437247.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..289
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31311
     Region          14..255
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mraelvvdck nqhgegifwn padglvwwtd iegcalwsfd aatsetashe mpervccfap
       61 rasgglivay adrvvlfdsl nseetlvarf epnnpetrln dgrtdrqgrl ivggmnevsg
      121 kadssvilvd kdlsvrtiie gvscanstcf tsdgetmffa dtpdreivaf dydtrngtvs
      181 nrrrhasfnd epglpdgscv daeggvwnae weghrvvrva pdgtidrvie vpvwkptcca
      241 fggpdldtlf ittsrlmsde aaltkepesg glfavkpgvr gvidapfkg
//
LOCUS       WP_010437483             412 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Ruegeria conchae].
ACCESSION   WP_010437483
VERSION     WP_010437483.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 412)
  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 412)
  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 412)
  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 412)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..412
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=45505
     Region          24..392
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 meigkklsgi srrdffrvag rygmsstlla aggfggamsl anlaqaaest yekrfskepk
       61 htlkfgasgf ntrnlliera gaiefardle ertdgeirie figdnqicgq lscvektqqg
      121 ivdiyaastq nsaggapyln vldyaymfps raaqyhffys pasqrilrdp lekrhglkfl
      181 fthcelrglq mgstfadkpt vtkleelfgt knrvtgtqlg riamqllnln pvpvaweetl
      241 dalktglidg aetwasavay anmapvvsqs vnlkffcgte htsmsakvfd slggelqdav
      301 messyftqal iqganeaall ntvgfsepql pdtifaengv rpafladdqi klaeemcapn
      361 ynpepwaqwr erlnkwaggi dtyqeiydia reipantlpe nveprrwwkg ea
//
LOCUS       WP_010437586             330 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010437586
VERSION     WP_010437586.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 330)
  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 330)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..330
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36811
     Region          22..196
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          243..325
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpepsslasw tpalrkqlta lgmdsdalcq sagidlnrls epdaqfspdv tatlwqravq
       61 asldpalglr vsrfvsptaf halgytlvas gslrevferi vryrsmaeds leldfrtvge
      121 ryefrfgtpp scqspvhell dafaaiyvrt crnrlgrgya plavhlqrpa pkdprpwydl
      181 frspvmfaaq enllefggdq fdshlddgpv qlngqesqgd plpsliweqr vrsaietllp
      241 dgeptvksia ealhlstrsl qrhladegcc ydlllnqcrq nlallhmndq qsslneiayl
      301 lgfsdtdcls rafkrwtglt peqyrsavvr
//
LOCUS       WP_010438392             251 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Ruegeria conchae].
ACCESSION   WP_010438392
VERSION     WP_010438392.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 251)
  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 251)
  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 11466508
            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="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27963
     Region          1..250
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mpkfaanlsl lftelpyldr fsaaaqsgft aveilfpydl aaketrrall angldlvlin
       61 apppnytgge pgyaavpggt arfqsdirrv lryakvlmpq yihvmagyas geealacfve
      121 nlrwaadfap dqmftiepln pvsqphyfln dyelaaevld hverpnvglq ydsfhaqmih
      181 gdaltiwdrf kaqivhaqig aapdrsepgr gemdfaalfk amdqsdyqgw vsaeytpttr
      241 rtqdtliwlr q
//
LOCUS       WP_010438324             276 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Ruegeria conchae].
ACCESSION   WP_010438324
VERSION     WP_010438324.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 276)
  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 276)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785082
            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="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=28979
     Region          2..276
                     /region_name="Fba"
                     /note="Fructose/tagatose bisphosphate aldolase
                     [Carbohydrate transport and metabolism]; COG0191"
                     /db_xref="CDD:439961"
ORIGIN      
        1 mslvtlsdal qpalrggyav aglvtlgwed mrayvaaaea egvpiilqag pscrehtplp
       61 vlgkmfrhla egasvpvvah ldhgythedc riaidsgfts vmfdgsrkpl eqniaetaai
      121 aemahsagvs cegeigfvgy sggegsdgtd pdeaaqfahe tgvdamaisv gnvhlqqnke
      181 ggldegrira ieavtevplv ihggsgvpvt qrsalargsk ickfnigtel rmafgnalrt
      241 avnadpdrfd rvqilkethe pvveatrrvl qafkga
//
LOCUS       WP_010440734             257 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Ruegeria
            conchae].
ACCESSION   WP_010440734
VERSION     WP_010440734.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 257)
  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   2  (residues 1 to 257)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            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="aminoglycoside 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=28851
     Region          4..211
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mlyggrtnqv wkvlsdhsda vlklyrapfq nplfrndarl eanclralns tgfvpnlrat
       61 gsfekaswvy ydhapgnpwr egvenvavll rrlhslsinl dlptgcngse dlrchaeqil
      121 rscqnaetqq lialkprgqi ppfaerclih gdpvagnilq ssagltlidw qcpasgdpce
      181 dlaiflspam qqlyrgtpls evevtnflta ydrhqvtary lslrswygwr maayclwrve
      241 ngspeyvraf eleiqal
//
LOCUS       WP_010440756             163 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Vibrio].
ACCESSION   WP_010440756
VERSION     WP_010440756.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            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="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17740
     Region          2..157
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mkiehyqrlt kqavaliese tdltanlani ssllfmelde lnwagfylik qdqakekdel
       61 vlgpfqgqpa cvripvgrgv cgtavatntv qrihdvhefe ghiacdaasn seivipfsid
      121 gkvagvldid spnvgrfsqi dedgltffma evekllnsha nka
//
LOCUS       WP_010441217             344 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio cyclitrophicus].
ACCESSION   WP_010441217
VERSION     WP_010441217.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 344)
  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 344)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 344)
  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   4  (residues 1 to 344)
  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 344)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..344
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38694
     Region          33..215
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          259..340
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 meiiaeykpt ahrhqlgtld ialllntleq rvidiekllm dvgleamdwr dpngkltyad
       61 klalfsaanq sfphdglglw lgehaslshf gvlgyalsts qnvgeaiksg fkylrlngpi
      121 fsvklfldse qaviqientl evgdllpfcs eyflssivsl fkeltgheld ihtlalpyar
      181 pnytklydnr fqcpvifeqn ycelrfdvsv lsqtllthda atlkrylasc qsivetldse
      241 hlltnqikti fyqtagsfpn ieqladefgc ssrtlrrelv thdssyqill tevrvelake
      301 lllgttmsid digerlgysd panfrrafkg wlnktpaqfr dgls
//
LOCUS       WP_010441543             671 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Ruegeria conchae].
ACCESSION   WP_010441543
VERSION     WP_010441543.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..671
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70120
     Region          1..669
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mskdisrllr pksiaviggg awcqqviqqs qlmgyagdiw pihpkaaela ghkayarled
       61 lpsapdaafv ginrhatiea vqilsemgsg gavcfasgfs eavaeddtgg dlqselikaa
      121 gsmpilgpnc ygfinaldga llwpdqhgaf pvergvailt qssnisinlt mqrralpiay
      181 mvtcgnmaqt sqaeiaaali ddprvtavgl hvegfkdvre wealaakafe ksvplialkv
      241 gaseqaqaat vshtaslags dvgaqallnr lgiprlkslp efletlkllh cygpltgani
      301 asiscsggea sliadmavgt glgfpklsed ketrlrdalg pmvalnnpld yhtyvwrdea
      361 amasawagmt gddidltisi vdypttdltd wacatnaalk vreetgarfa vaatlpellp
      421 edvaqtlmag gvvpfmglse tlaatraagq icapshepic lpgdleakrt lteadakqal
      481 tghglrvpqn rsvrsaeeaq cathemtapf avkgvglahk sehaavrlgv qasdvpkvaa
      541 eigtdeilie emisgtvael lvgvvrdpah gfvltlgagg vmteilrdta sllipttpdd
      601 irgaldalki apllagyrgq paadmdeiia avlavqsyvv hnadtlgeve inpllctptr
      661 avavdalvrk a
//
LOCUS       WP_010442401             399 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Ruegeria conchae].
ACCESSION   WP_010442401
VERSION     WP_010442401.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 399)
  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   5  (residues 1 to 399)
  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   6  (residues 1 to 399)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 399)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..399
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43529
     Region          20..>67
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          85..381
                     /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 merealkilt ggvsqsgvrd hnerliltvl qrhgpaagae iarltglspq tvsiilrkle
       61 kdeilkrgtp lrgkvgkpst pmelnpegil svgmkigrrs adlllidftg kprhqistty
      121 dyplpeavfg flekgleell vhepqklrdr vcgigigtpf elwkwhdlsg laakkfrswk
      181 nvnffsevak fsdlpvfvvn dataachaeh lygrgaeyrd yfyffigsmi gggvalngtv
      241 fegnqgnaga lgamrttgpl gesqqlidta slflledrli eagvdpqilw tkpqdwssis
      301 ryvepwigtt aqelakaals icavidfeai fidgafpsev reelvarvrr yllnqdkrgl
      361 ippvveaaav gdnargigaa sspifrqfll ntnaglsgm
//
LOCUS       WP_010443052             404 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Ruegeria
            conchae].
ACCESSION   WP_010443052
VERSION     WP_010443052.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 404)
  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 404)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..404
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47102
     Region          1..397
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mtlqrlnnrq artmfmdrha lleqpaggsk gedllrlihr lgfvqldsin tvarahdmil
       61 yarrpsyrpr nlkrlyerdr alfehwthda avipmdfyrh whlrflrdad mlkarwknwr
      121 rdgfeqrfes vlqhirdhgp vgssdvgkde kkgsggwwdw hpsktaleyl wrsgaltvig
      181 regfqkrydl tervidtqlc pgsiacdvda tvdwlcnaal drlgfatsge laafwdtvsa
      241 geakawcdqa ltkgiiaevf vecadgndrk vfarpeiseq vaalpeapgr irvlspfdpm
      301 lrdrkraerl fgfhyrievf vpepkriygy yvfplmersr migridmkah rnhgnlhvra
      361 mwpeqsvlws dartrrleae ldrvrrfadl dtiefarnwl kdpk
//
LOCUS       WP_010443189             336 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Ruegeria conchae].
ACCESSION   WP_010443189
VERSION     WP_010443189.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 336)
  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   6  (residues 1 to 336)
  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 11677366
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37005
     Region          58..201
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <167..336
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 masvtyafar amanaagmtl nddgalisng avvlrlpeaq dgqladdayf dlidwiraqq
       61 adeaalveay anaiatddlg vlglavktap tlrqslqrie ryfrlvtdta vyrldetgdp
      121 vlwifegqts hraalelrne calaafarnm hrfvgdglsl ayvtfqhpcr qeperyaeyf
      181 gcpvrfgsah naiamrpaml esenrlgdpg lsdfmtkhld eefnsrdedt slsqaivhrl
      241 tpalsngapq aahvaqemgm sertlyrrla eegltyrdvl gqaqvalard llrdgkasia
      301 eiafmtgfse qstfsrafkr wvgqaparfr qqatsd
//
LOCUS       WP_010443567             760 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Ruegeria conchae].
ACCESSION   WP_010443567
VERSION     WP_010443567.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 760)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 760)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..760
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..760
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=81756
     Region          36..695
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mktsqayfsp sakeanvagk ikarigrrlg frlaglaliv lgcfirildp ypvrmsrliy
       61 fdvlqrispr eynpelpvkv ldideqslan wgqwpwprtl laqmvqnlge ngaaaiafdm
      121 lfaepdrysp arllndpala gvltverhaq kadydvmfgl evarwpvvlg taartsqegs
      181 qisskagive igenptaglv svpywtpiap pldrsaagig gvnvspiggm gvvrrvpalw
      241 ggpdgalpgl giealrvald apyilvegss keegivlave igdfrlptte dgevwvryrk
      301 dqpdlylsad aimqnpddpa lrseieghii lvgtsaaglf dmhqtalges vpgvsihaqi
      361 ieqilvgdll srsdvtaale lvafvilgiv vtvvmsnfga vasfvtggva amvviliswl
      421 sfqnqsvlfd atfplaggma nfgllagylf isterekrvi rqtfshyvap eildemeang
      481 hqlqlggetq eitvmfsdir gftplsesvs atdlvallna lfseigdqil vergtidkfi
      541 gdavmafwna plpvddhpcr aalaalkmrv alenfnsssi mrdrppiala tgcatgaacv
      601 gnigsrrrfn ytvigdvvnv aarieqncrh vdydilvshs iqqatnsdla lleagfvdlk
      661 gksepepvyv lvgdrqlags aefkaleaah frlleavrsr asqfdvanls kecaalaati
      721 epgltsfygt lpgrtadfrs emvhaqpvfs hhnglresat
//
LOCUS       WP_010443827             696 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Ruegeria conchae].
ACCESSION   WP_010443827
VERSION     WP_010443827.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 696)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 696)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..696
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73936
     Region          6..693
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mtparrenle rllkprhiaf iggrdatiav rearrrgfqg qmwavnpkra dldgvgcvps
       61 isdlpeppda vylaipaagv tdalreleqm gaggvvcfsa gfketgdiqs erdlievagd
      121 maligpncyg minyidnaal wsfehggwsp gygaaiitqs gmfssditms arslpmaymv
      181 sagnqavlgi eefldafaed pavraiglhi eglrdiaafe raalkaldrg vpvvalktgn
      241 saigatltvs htgslsgsse lyqalfdrtg vidvtspsqf letlkylcva gapqgrrvag
      301 ftcsgggatm ladhserigv cfpkvgsagq esltsllpei atvsnpldyt tpiwgqgdkt
      361 ypvfatalsa lnadlavlvq dypaegldas kiyyqndaaa faqaaqehsv paaicatlpe
      421 nldrgtrrhl ielgvapmqg ihetlnamrd aiwwsearar tridrpaalr pgatiqnpmv
      481 ltedkgkswl rqmavavpng hvcnaaeaag vaqdigypva lkmmspslph kteagavalg
      541 ikdaeglssa ikamtasvaa ydraavtdrf lieamspkpl aelivtlrad pqfgpslvig
      601 sggvltelvr dartvllpas kdeieralcs lrvarllegy rgsrqadipr iadalhrlct
      661 eflkargeva eieinpmfvy pdhivavdal iqvprs
//
LOCUS       WP_010443653             277 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Ruegeria conchae].
ACCESSION   WP_010443653
VERSION     WP_010443653.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria conchae
  ORGANISM  Ruegeria conchae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 277)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Ruegeria conchae"
                     /db_xref="taxon:981384"
     Protein         1..277
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=30478
     Region          <18..261
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mgnrkradlp egsdnplsaa vtsrdqsvvq mateavkhkq crlafqpviq ahppqgiafy
       61 egfirvldet grviparefm pqventpigr dldcialdmg lrtlirnpgi rlsinmsars
      121 igysnwsrvl drflkkdasl gerlileise asamqvpelv vdfmdqqqar giafalddfg
      181 asnfsfrhfr eflfdaakid gqfirgvskn sdnqalvral iavarefeil vtaesveiae
      241 daaflvengv dclqgflyga psvsppwvke kssktgs
//
LOCUS       WP_010447628             179 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit [Vibrio].
ACCESSION   WP_010447628
VERSION     WP_010447628.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 179)
  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 179)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 179)
  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   4  (residues 1 to 179)
  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   5  (residues 1 to 179)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..179
                     /product="TRAP transporter small permease subunit"
                     /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=20142
     Region          4..169
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mrsliyieri fnrfgdflgw lssilfilll anvvydvvmr yvfndvsiaf qemewhlfsa
       61 vfllgvpyai ksgghvrvdi fyerlsykaq siidilgtll flfpfcllva wfgidfakes
      121 yalgetsgdp gglpyrwiik gmiplsflfm avsgvglllh sinkivnphl iyagnngks
//
LOCUS       WP_010450926             732 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Vibrio rotiferianus].
ACCESSION   WP_010450926
VERSION     WP_010450926.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 732)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 732)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 732)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..732
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=81817
     Region          183..716
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 msintskygv fsyvilslsi vsmifvsfgl sslfvleqdn fqiisivgat alvsflryrs
       61 kaipsvvlgl ffyywltgrg vqfsatysll lpiipfvtaw lfhtyndral dkpastrlsv
      121 ffltagcfyp lantlmmliv sgvigsnyfd thflvyatlg gyltqllvtp tlyvatcllt
      181 gtdqqrfial drslrhssnt dkrylfwlfg sigllslaay apssfllntv sfclilivis
      241 glsrhgiiqp lvigsfatll iiydaihafn agphnqekll glmiivsvlv tlayllagys
      301 ikyyemsqkq iqaeridpyt elyniaqlke dlftqsqsvl iyldltstls mltglghegk
      361 sqlikqlsdy lssrneginr cyrppfstgv isftemsedi hgelyevsrh lakfqfywqg
      421 tsvslvnpvl hcariyptmd iekvasvlcd qragydetih wvklnsahsd rvdklnyiqq
      481 ifkndqfely cqpyktlspt antptsfevl lrvinsdgsi lapadffpli nqfgletqld
      541 rwvidhtflm ldahvedwtq idycsinlta ktlgvpnlae qiiskaaqlk iplekvcfei
      601 iessalsneq qaietlttlr eagckvaidd fgtgyasfey lrrlpldvlk idgafvknlp
      661 ynetdrlivs sictvaremk lqtvaefves eahiqilsel ginyaqgygv akpmplvacl
      721 kgmakkgvkt va
//
LOCUS       WP_010451002             247 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Vibrio].
ACCESSION   WP_010451002
VERSION     WP_010451002.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 247)
  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   3  (residues 1 to 247)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..247
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27617
     Region          45..224
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mrnttasgrd nrsalheksv qqrqastlns tdamgmvehg sevtlnvttp vgtkfittsl
       61 figchsnnsa lieipnisdd dlkfyfqegf wvnvkalshr gegaiipfra qikhrleepf
      121 pvlvltlpnt mqvyqlrkev ryevnlqakv hlndyktdce irdlsksgcr fitspmsrqi
      181 qvgemvslni vlgergpmla plkgkvcnlq ksthyarygv qfddfgkana knllgqlkfn
      241 gtklmlk
//
LOCUS       WP_010451096             197 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Vibrio rotiferianus].
ACCESSION   WP_010451096
VERSION     WP_010451096.1
KEYWORDS    RefSeq.
SOURCE      Vibrio rotiferianus
  ORGANISM  Vibrio rotiferianus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..197
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20527
     Region          <13..142
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 msdpnkyedk eqgtnsndvi ksydnsssvi vgldgsdkiy agakddlvig gdgndlivgg
       61 kgndvlkggh gndtmrggtg ddvllashgd nrmhggadnd rliigsgknv vsggsgedkf
      121 vftdkfgghg nstvldfnad edilmfsses vqslsdleis ydargnavls ngedftvkvk
      181 gltqeeveah gsdlfvf
//
LOCUS       WP_010452022             337 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Vibrio rotiferianus].
ACCESSION   WP_010452022
VERSION     WP_010452022.1
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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Vibrio rotiferianus"
                     /db_xref="taxon:190895"
     Protein         1..337
                     /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=37907
     Region          1..273
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mgrtpffdna kfilvflvvf ghlieplien spiikivyls iysfhmpafv iisgmlsrsd
       61 gssdavakav rnilipfvaf tiayeafnyl ttgsisnytk nvqpywmlwf lyslflwklm
      121 lpsiqkfkyp iamtlliavs agyieligyd lgisrtlyfl pffvighkft pdtfmsvrik
      181 ycgrslkaam vgvvvlnval fsyyngmphq wlygsfsysr lgvgdisagl irlglmlisl
      241 ltafavllli pvgsnkilsq gknslyvyaw hgffikafii lgvpmlltsy svltclfflf
      301 vfsviltltl sqefianktk qlvlnplhhi lqsrkis
//
LOCUS       WP_010455102             297 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Pseudomonas mandelii].
ACCESSION   WP_010455102
VERSION     WP_010455102.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..297
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32132
     Region          13..264
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mqaelivdar navgespvwv peenalywvd ipagglqrws adsghvnawk apqmlaciar
       61 hrdggwvagm esgffhlqph ndgsldsell ahvdharvdm rlndgrcdrq grfwagsmvl
      121 nmganaadgt lyrysagqrg pleaqlggfi vpnglgfspd grtmylsdsh plvqqiwafd
      181 ydidsgtpsn rrlfvdmnqf pgrpdgaavd aeggywican daglihrftp dgrldrslav
      241 pvkkptmcaf ggsrldtlfv tsirpgdddd pqslaggvfa lnpgvkglpe plfndll
//
LOCUS       WP_010456104             234 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Pseudomonas].
ACCESSION   WP_010456104
VERSION     WP_010456104.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 234)
  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 10614777
            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="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=25295
     Region          37..204
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 maplrfgylf sallltamsv psayadslaa alikaapkan anvinlavra sqcsiaqgka
       61 pvqrlavidy slpsteqrlw vfdlkkrkll fhelvahgrn sgenmavnfs nqnesfatsl
      121 glyrtqqsyv gqngyslrme glepgfndna fdraivihga pyvspvlara ngrigrslgc
      181 pavrpavarr lidsmkggql lfsyypdqrw lksssyincg sgtvadtsap kkhl
//
LOCUS       WP_010456937             743 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Pseudomonas].
ACCESSION   WP_010456937
VERSION     WP_010456937.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 743)
  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   3  (residues 1 to 743)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..743
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=78858
     Region          6..742
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msfgadeeil qdflveagei leqlseqlve lesrpddadl lnaifrgfht vkggagflql
       61 nelvecchia envfdilrkg errvdselmd vvlealdavn smftevrers pitaatpell
      121 aalarlaepq tadesapvae vveapaaees gditdnefeq lldslnavka qaeapavapv
      181 aaadsaagde itdaefesll dqlhgkgqfa vdavapptap aapkaagdss ditddefeal
      241 ldqlhgkgnf avdalesaia avpasaapta kaaggdlisd hefeslldel hgkgkftevg
      301 tgaavaapaa kaaapkpvak apepkaeapk paaaaapapa rapsapppek paseaettvr
      361 vdtarldeim nmvgelvlvr nrlvrlglns gdeamskavs nldvvtadlq tavmktrmqp
      421 ikkvfgrfpr lvrdlarqlk keinlelvge etdldknlve aladplvhlv rnsvdhgiee
      481 paereamgkp rsgkvilsae qegdhillsi sddgkgmdad vlrgiavkkg lmdkdaadrl
      541 sesdcfnlif apgfstktei sdvsgrgvgm dvvktkiaql ngtiniystk gkgskivikv
      601 pltlaimptl mvmlgnqafa fplvnvneif hldlsrtnvv dgqevvivrd kalplfylkr
      661 wlvssaahee qreghvvils vgtqrigfvv dqlvgqeevv ikplgkmlqg tpgmsgatit
      721 gdgrialild vpsmlkryaa rri
//
LOCUS       WP_010458330              96 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [Pseudomonas].
ACCESSION   WP_010458330
VERSION     WP_010458330.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..96
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10197
     Region          1..96
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mkpstaldlk raavrevvgr frtsnprvfg sallgtdkeg sdldllvdal pgatlfdlgg
       61 lqveledllg vsvdlltpgd lplkfrqqvl eqarpv
//
LOCUS       WP_010458793             375 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Acidovorax].
ACCESSION   WP_010458793
VERSION     WP_010458793.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 375)
  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 375)
  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   3  (residues 1 to 375)
  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   4  (residues 1 to 375)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 375)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..375
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39371
     Region          28..367
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(104..106,127..128,177,229,254)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mqlklkltvv aaiaavagva saqeqvvkig hvapvsgaqa hygkdnenga rmaieelnaq
       61 gvtiggkkik felqaeddaa dpkqgtaaaq klcdskvagv vghlnsgtti paskvyndcg
      121 ipmvtgaatn pnltkpgykt tfriiandna lgaglafyav dtlklktvai iddrtaygqg
      181 vadvfkktav akgmkvvdeq fttdkatdfm ailtaikskn pdavfyggmd pqagpmlrqm
      241 eqlgmgnvky fggdgvctse iaklaagakt lanvicaegg sslakmpggt awkakydaky
      301 pnqfqvyspy tydatfllvd amkransvdp kvyvnelaka nfkgvtsaia fepngemknp
      361 sitlyvykdg kktpl
//
LOCUS       WP_010459821             360 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [Acidovorax].
ACCESSION   WP_010459821
VERSION     WP_010459821.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 360)
  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 360)
  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 360)
  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 360)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..360
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39221
     Region          1..354
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mdrrsiikha giagvlaagv apavhaqaav rwrlassfpk pldtiyggae vfanavkams
       61 ggkfeisvha ggelmpamgv adgvqqgsve mchtvpyyfy gknpafalgs aipfgmnsrq
      121 mnawmmhgng rklmdefyag ygmlsfaggn tgtqmggwyr keiksvadlk glkmrlgggl
      181 vgevmqkmgv vpqslpggei yqalekgtid aaewvgpydd qklgfnkvap hyyypgwweg
      241 gpevdffinq kafdalspen kaiiqaassh aavdmlakyd arnpvalkql igakikllpf
      301 tkdvldasfk asqevyaend akspewkkiy adfrnfqrdq vawfrvaegr fdsymqtvkl
//
LOCUS       WP_010459157             172 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein, partial [Acidovorax radicis].
ACCESSION   WP_010459157
VERSION     WP_010459157.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 172)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         <1..172
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <1..152
                     /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 arqfrqtglr grsaadlksh nadprklkle lteslllgdi edtiarmvql ksegvgfald
       61 dfgtgyssls ylkrlpldqv kidqsfvrdv lsdpndaaiv rtilalaksl dlevvaegve
      121 ttgqlsflrl hgcegfqgfl fgrpvpidvf arehqlglfa qpavalpegr kp
//
LOCUS       WP_010459918             180 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein, partial [Acidovorax radicis].
ACCESSION   WP_010459918
VERSION     WP_010459918.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 180)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         <1..180
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <1..176
                     /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 eqlqrwgqhe atahlsisvn vsarqfrqpg fvaevlqtlk shnadprklk lelteslllg
       61 diedtiarmv qlksegvgfa lddfgtgyss lsylkrlpld qvkidqsfvr dvlsdpndaa
      121 ivrtilalak sldlevvaeg vettgqlsfl rlhgcegfqg flfgrpgpvg didallyptr
//
LOCUS       WP_010460330             345 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010460330
VERSION     WP_010460330.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 345)
  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 345)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..345
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38366
     Region          20..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          250..332
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mykmssgyas vlvntlsaqg ldvaslcrea gldidladqp gafcerkaiy rlwelaaeas
       61 gdqdiglray gsfhpgsfqi igytmmssln lknalerlvr fspligtgfs lfftaeqqhy
      121 rlsgldhqqq gsvkprqytd aglasllgfc rklaggnapq plsveftype pedttehrrl
      181 fgcnlqfnap ydsilfdgqe lmrplsmane tlavlhdsfa eaqldllfgf civgrirali
      241 terlsqgqgq cdmesiaaal niskrtlqra lekegtqfkd vlsavrrqla dfylrhshfn
      301 mkhvayllgf hdhssfnkac srwfgmtpgq yrsdesfeiq eaapv
//
LOCUS       WP_010460041             414 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Acidovorax].
ACCESSION   WP_010460041
VERSION     WP_010460041.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 414)
  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 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   3  (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   4  (residues 1 to 414)
  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 414)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..414
                     /product="CmpA/NrtA family 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=45191
     Region          39..289
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mtdllktsln rrtvlqaatv gavgvspalr alvhaqgsda pekkevkigf ipltdcasvv
       61 masvlgidkk ygvtiiptke aswagvrdkl vngeldfahv lyglvygvhl glagpkkdma
      121 vlmnlnqngq aitlskklad kgavngagla klmasekrey tfaqtfptgt hamwlyywla
      181 ahgidpmkda kvitvpppqm vanmrvgnmd gfcvgepwnh raimdgigvt atttqdiwkd
      241 hpekvlgtts efvqkypnta ravtaailea skwideglan knkmaetiag kayvntgvda
      301 inqrilgryq dgmgktwddp nhmkffnegt vnfpyltdgm wfltqhkrwg lmkdhpdylg
      361 vakavnridv ykqaataskt plpktemrss kfmdgvvwdg kdpakyadsf kika
//
LOCUS       WP_010460688             144 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Pseudomonas mandelii].
ACCESSION   WP_010460688
VERSION     WP_010460688.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            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="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16047
     Region          4..142
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mggayiglff aafgaatllp lqsealfvgl llseqywlwl llavatlgnv lgsvvnwwlg
       61 crierfrdrr wfpvsprhle qarkhyqryg hwslllswvp iigdpltlva gvmreplgrf
      121 llivtlakga rygvlalatl gwig
//
LOCUS       WP_010460521             830 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Acidovorax radicis].
ACCESSION   WP_010460521
VERSION     WP_010460521.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 830)
  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 830)
  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 830)
  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   4  (residues 1 to 830)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..830
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..830
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89948
     Region          68..816
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mpafalaphq lrltidpatl gfastaelqd lplpwigqer aqaaaqfglg lhqpdyhlfv
       61 lgevgsgras llrqamqaaa sqravppdlc ylhnfdtpdr pralrlpagq grqlrqglad
      121 maknlqadip kslaaadfka eaerieknwq tqeaeafaal dafaearqfr ltrdggqmvf
      181 tltgpkgqpl tesearalpr erraeidaae qevrteiarf leaarplera rddalaalrr
      241 qtikplveha lhdirqglrk qikdtvklth wldqveqavl gdidlfepld terggdqgtd
      301 aeddrkdald dllarcqvnl vvdnhgrtaa pvvvednptq rtlfgsiehg sdadtvqadh
      361 tgihagsllk ahggfillhl hdlaaeeglw qrlrrflrcg rlqieegggg pghgpggava
      421 lqpepvdvdv kivligsvde yyalqdadpd aarrfrvkvd fsdhfaatpa thhatailva
      481 qvckkrglpp fgpdavalll eqthreaddq rrqsarfaht ealaiesasl ckarggplvq
      541 agdvltalaa rtqrhnqpee elhdsitege rlislagsit gqinamtqid lgdyrfgfpv
      601 ritartfagq egllnierev dmsgpihdkg vlilhsylta lfshvaplal nasivfeqey
      661 sgvegdsasc aelyallssl sglplrqgia vtgalnqhge vlpvgginek iegwfracst
      721 agldgtqgvl iparnqrhlm ldrsvldave rglfhvytmg hvsegiallt geasgmspae
      781 llqaqadela draaavedtv mqraeltlra yrracqiags trrgrgalgr
//
LOCUS       WP_010461655             111 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Pseudomonas].
ACCESSION   WP_010461655
VERSION     WP_010461655.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (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   2  (residues 1 to 111)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..111
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11532
     Region          41..108
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mrtgyiyslv falltsgsia aiaaptvtsd patpslvqdv aqptqtgkvd lnsadatilq
       61 relagvgeak akaivayrds ngsfasldel levkgigkai lernreklev n
//
LOCUS       WP_010461299             409 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Pseudomonas].
ACCESSION   WP_010461299
VERSION     WP_010461299.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 409)
  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 409)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..409
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46336
     Region          2..404
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mpatlsfsnk qarrlalaaq gfngrqppaa ikpvqlnrli erlgilqids vnalvrshyl
       61 plfsrlgnys pdlldqaaws qgrrrtlfey wgheasllpm smyplmrwrm qratrgediy
      121 qqlarfgreq qdtirrvlas vqelgalgag slstrqerag pwwdwsaekh alewlfaage
      181 vtvagrrgfe rlydlpervi psavlqqpll seaeaqrgll lhaatalgvg tekdlrdyfr
      241 lnpadsrprl aelietgell acevqgwrqp afclpepkvp rkvessalls pfdsliwers
      301 rterlfdfry rleiytpqdk rvygyyvlpf lhneriaarv dlraeralgr lavhavheee
      361 pgldeagmla lavnlrqmad wlgleqvqln cprasaarlr valaqiqvg
//
LOCUS       WP_010462682             633 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Pseudomonas].
ACCESSION   WP_010462682
VERSION     WP_010462682.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 633)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 633)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 633)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..633
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68072
     Region          5..633
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mgqassqaag aehsaakpig mlvaavgvvy gdigtsplyt lkevfsggyg vpvnhdgvlg
       61 ilalifwsli wvvsikymmf vlradnqgeg gimaltalar raaaghpklr allvvcglig
      121 aalfygdsmi tpaisvlsai eglglafegi dhwvvplslv vlvalfliqs hgtarigilf
      181 gpimvtwfvv lgalgvhgil qhpevlqaln pvwgvrfftq hpgmgvailg avvlaltgae
      241 alyadmghfg rkpiarawfi lvlpalvlny fgqgalllgd peaarnpfyl lapswallpl
      301 vglstmatvi asqavisgaf sltrqaiqlg yiprmhirht ssaeqgqiyi gavnwalmvg
      361 villvlgfes sgalasaygv avtgtmlmtt ilvsavilll wkwppvlavp lllgfllvdg
      421 lyfaanvpki iqggafpvia gialfvlmtt wkrgkqllve rmdegglplp ifissiavqp
      481 phrvqgtavf ltarpdavph allhnllhnq vlheqvvllt vvyediprvp ssrrfevdsy
      541 gegffrvilh fgfvdepdvp qalklchldd ldfspmrtty flsretvias klegmarwre
      601 alfafmlrna ngnlrffnlp lnrvielgtq vem
//
LOCUS       WP_010464833             198 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Acidovorax radicis].
ACCESSION   WP_010464833
VERSION     WP_010464833.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            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="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21237
     Region          7..194
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 madsahtrri ivaisgasga vygarllqvl qglpgiethl vvshagwrnl qheldmdrpa
       61 vealahrvhd vanvgaaias gsfqchamvv apcsmrtlaa iahgladnll traadvalke
      121 rrrlvlmvre splhlthlrn mvavtemggi icpplpafyl rpqtvgevvd ysvarvldli
      181 dvphdlaprw vglelnal
//
LOCUS       WP_010464846             329 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Pseudomonas].
ACCESSION   WP_010464846
VERSION     WP_010464846.1
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 11438136
            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="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=36966
     Region          1..321
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msievrnvsk nfnafkaldn isldiqsgel vallgpsgcg kttllriiag letpdqgniv
       61 fhgedvsghd vrdrnvgfvf qhyalfrhmt vfdnvafglr mkpknqrpse sqiavkvhel
      121 lnmvqldwls drypeqlsgg qrqrialara lavepkvlll depfgaldak vrkelrrwla
      181 rlhedinlts vfvthdqeea mevadrivvm nkgvieqigs pgdvyenpas dfvyhflgds
      241 nrlhlgednh vlfrphevsl srheledhha aqvrdirplg attrvtlkve gqselieaev
      301 vkdhdslidl akgdtlffkp kvwqklani
//
LOCUS       WP_010464898             165 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease P protein component [Acidovorax radicis].
ACCESSION   WP_010464898
VERSION     WP_010464898.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Reiter,N.J., Osterman,A., Torres-Larios,A., Swinger,K.K., Pan,T.
            and Mondragon,A.
  TITLE     Structure of a bacterial ribonuclease P holoenzyme in complex with
            tRNA
  JOURNAL   Nature 468 (7325), 784-789 (2010)
   PUBMED   21076397
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Harris,M.E. and Christian,E.L.
  TITLE     Recent insights into the structure and function of the
            ribonucleoprotein enzyme ribonuclease P
  JOURNAL   Curr Opin Struct Biol 13 (3), 325-333 (2003)
   PUBMED   12831883
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Pace,N.R. and Smith,D.
  TITLE     Ribonuclease P: function and variation
  JOURNAL   J Biol Chem 265 (7), 3587-3590 (1990)
   PUBMED   1689306
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..165
                     /product="ribonuclease P protein component"
                     /EC_number="3.1.26.5"
                     /GO_component="GO:0030677 - ribonuclease P complex
                     [Evidence IEA]"
                     /GO_function="GO:0000049 - tRNA binding [Evidence IEA]"
                     /GO_function="GO:0004526 - ribonuclease P activity
                     [Evidence IEA]"
                     /GO_function="GO:0042781 - 3'-tRNA processing
                     endoribonuclease activity [Evidence IEA]"
                     /GO_process="GO:0001682 - tRNA 5'-leader removal [Evidence
                     IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
                     /calculated_mol_wt=17412
     Region          4..140
                     /region_name="RnpA"
                     /note="RNase P protein component [Translation, ribosomal
                     structure and biogenesis]; COG0594"
                     /db_xref="CDD:440359"
ORIGIN      
        1 mqrlktrpqf qaamaggtvs rtahfalhrl vldtggstpa gqanaptgpg slpstqgpqa
       61 lfavqgvwlg amvpkrwarr avtrntikrq iytvgatfea rlpqaahvvr lrtafdrkqf
      121 vsatsdqlkq avraellqlf gyaarrsgga vsapvsplaa eavap
//
LOCUS       WP_010465578             297 aa            linear   BCT 20-JAN-2025
DEFINITION  RHS repeat-associated core domain-containing protein [Acidovorax
            radicis].
ACCESSION   WP_010465578
VERSION     WP_010465578.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 297)
  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 10264210
            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="RHS repeat-associated core domain-containing
                     protein"
                     /calculated_mol_wt=31905
     Region          37..68
                     /region_name="RHS"
                     /note="RHS protein; pfam03527"
                     /db_xref="CDD:427349"
     Region          64..145
                     /region_name="Rhs_assc_core"
                     /note="RHS repeat-associated core domain; TIGR03696"
                     /db_xref="CDD:274730"
ORIGIN      
        1 misistlhsf wlrllarlal llafgafaas agaqttitff hndilgspai atdadgavvw
       61 kenylpyghr lqapaagann klwfagkpyd qtnwitymga ryyipligrf tsvdpqgivp
      121 enphsfnrya yannnpykyv dpdgrsatwa lkvlvtaavl vgaanhltpe qrarmeqaga
      181 llqqrtsell drasglvfne gadtskgqvd tavngltegl knetdakgrp tkgqyvkpgg
      241 daqkdldslp gtagdngqki lpdgsvagih tstttgldtl hvhrpsgsrd ikirypq
//
LOCUS       WP_010466278             441 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [Pseudomonas].
ACCESSION   WP_010466278
VERSION     WP_010466278.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 441)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            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="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=49677
     Region          2..434
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 makvaevwmw etrvgvvlwd enqipatgtf efdpefceig leiapltmra epdevyafpg
       61 lnpvafkglp pclsdslpda fgnavidawl aqkgrdprsf spverllyvg qrgmgalefr
      121 paldraidkv eqlqleslvd lagrileerq tqfddlhlei kseeedqalk hlfqvgssag
      181 gqrpkaiiai neetgaicsg qieapegyty wlfkfdvsng astlgdpagf grveyayhlm
      241 tlaagvkmte crlhiegpra hfmtkrfdrl ddgdkvhiqt lcamdsadyt lpgaysyeqa
      301 lqvcrdlglp redqvelfrr avfnvvarnq ddhtknigfq lwrdgvwrlt paydmcwsyr
      361 pdspwvsqhq mslngkrdnf elkdllavak litnldgrkv vkevveavrr wrefadvagm
      421 tddnlieqie sthrlylgdg l
//
LOCUS       WP_010466670             413 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Acidovorax radicis].
ACCESSION   WP_010466670
VERSION     WP_010466670.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax radicis
  ORGANISM  Acidovorax radicis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 413)
  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 413)
  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
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 413)
  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   5  (residues 1 to 413)
  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   6  (residues 1 to 413)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 413)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 413)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Acidovorax radicis"
                     /db_xref="taxon:758826"
     Protein         1..413
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44246
     Region          39..>105
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          98..400
                     /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 mldtdasplp vdnaaaspal lrqrgsnhvg lrqfnervvl qalrthgsla kaemarvtgl
       61 taqtiglita rldedqllrr eapvrgrvgq psvpiglnpd gafaigikig rrsadwllvd
      121 ftghvrervv ldyafpdidv llpairkhlh qlldglgplr srvvgvgvaa pfqlggwhrm
      181 lglteaqsea wnsidlaeqv qqmtelpvsf akdtsaacva ellqgrgrdi psflylfmdt
      241 fvggglvins hlhrglhgna gavaslplsp alpgqapaql isqaslwele qrfrehgldp
      301 maaydkrvlq apwlehsrgw iaraaaglah civsatafld ldavvvdgaa apellqalce
      361 garhaladyn weglhqpprl elgtmgsdar alggallplh acfapdtdif lka
//
LOCUS       WP_010466922             295 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Pseudomonas].
ACCESSION   WP_010466922
VERSION     WP_010466922.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            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="formate/nitrite transporter family protein"
                     /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=32245
     Region          24..274
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mdikqdgktp nlspeeqhdv dknqppraav lheiirtqgd qelersvaal wwsalaaglt
       61 mglslmamgl lnsrlpdgeg fkviasfgyc agflavilar qqlftentlt avlpimtkpt
      121 lnnfgrllrl wsvvlvgnlc gtllvayvml nlpifdsktd lafldigrki mendasqmfa
      181 kgivsgwmia tmvwmipsme sakmwiiili tylmalgdft hivvgsaevs ylvfagelpw
      241 kdfwlvfagp tlagniiggs fifalishaq irsesgppkk ttdqasepdp qkskk
//
LOCUS       WP_010467585             135 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: pilin [Pseudomonas].
ACCESSION   WP_010467585
VERSION     WP_010467585.1
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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..135
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=13640
     Region          2..133
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mntqkgftli ellivvaiig ilatfalpay skyqarakvt aglaeitalk vpfedlmnsg
       61 tnpdltkvgg tattsncttt aagvatdgtg tigctilnap gpvlsktitl trsltgwtca
      121 ttvaqeyapk gctgv
//
LOCUS       WP_010468095             328 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phytoene/squalene synthase family protein
            [Streptomyces].
ACCESSION   WP_010468095
VERSION     WP_010468095.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..328
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36097
     Region          16..283
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mtrreldaag vadprlraay twcrrlnarh grtyflatrl lpverrpavh alygfarwad
       61 divddlarrl apeerdrrlr aleddladgl rgtgggdpvv ravadtadry aidhrlfadf
      121 masmrsdlsv tdyptyadlr aymhgsaavi glqmlpvlgt vvpreeaaph aaalgvafql
      181 tnflrdvged ldrgrvylpa dllaahgvdr pllewsrrtg rrdpriraal vaaehlarda
      241 yreaepgiam ldprvrpcig vartlyggil davaddgyav lhhrsavprr rraavaavgl
      301 ahvlgarvra ravrpapagt terkehvr
//
LOCUS       WP_010468625             262 aa            linear   BCT 20-JAN-2025
DEFINITION  phosphonate ABC transporter ATP-binding protein [Acaryochloris sp.
            CCMEE 5410].
ACCESSION   WP_010468625
VERSION     WP_010468625.1
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   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
REFERENCE   2  (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   3  (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   4  (residues 1 to 262)
  AUTHORS   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            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="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=28834
     Region          16..257
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mlklkrlaak sarsnsilal rqvshqfgtv maladvsfai ypgqivalig ssgagkstll
       61 qllngtlqpt agevwamgql wqarsarriq rqigtiyqql hlvpslrvih nvnaghlgrw
      121 pfwkaaaslv wplevetaqt alaqvgipdk lyartdrlsg gqqqrvaiar vlvqdpaiml
      181 adepiasldp ershdimrll srlvrergkt lvvslhgvey aqrycdriig lkqgqvqfdl
      241 paqdvtpeql hhlyqldnpp ss
//
LOCUS       WP_010468971             842 aa            linear   BCT 20-JAN-2025
DEFINITION  AAA family ATPase, partial [Streptomyces somaliensis].
ACCESSION   WP_010468971
VERSION     WP_010468971.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces somaliensis
  ORGANISM  Streptomyces somaliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 842)
  AUTHORS   Liu,Y., Sung,S., Kim,Y., Li,F., Gwon,G., Jo,A., Kim,A.K., Kim,T.,
            Song,O.K., Lee,S.E. and Cho,Y.
  TITLE     ATP-dependent DNA binding, unwinding, and resection by the
            Mre11/Rad50 complex
  JOURNAL   EMBO J 35 (7), 743-758 (2016)
   PUBMED   26717941
REFERENCE   2  (residues 1 to 842)
  AUTHORS   Chen,Z., Luong,T.T. and Lee,C.Y.
  TITLE     The sbcDC locus mediates repression of type 5 capsule production as
            part of the SOS response in Staphylococcus aureus
  JOURNAL   J Bacteriol 189 (20), 7343-7350 (2007)
   PUBMED   17704228
REFERENCE   3  (residues 1 to 842)
  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   4  (residues 1 to 842)
  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
REFERENCE   5  (residues 1 to 842)
  AUTHORS   Hopfner,K.P., Karcher,A., Craig,L., Woo,T.T., Carney,J.P. and
            Tainer,J.A.
  TITLE     Structural biochemistry and interaction architecture of the DNA
            double-strand break repair Mre11 nuclease and Rad50-ATPase
  JOURNAL   Cell 105 (4), 473-485 (2001)
   PUBMED   11371344
REFERENCE   6  (residues 1 to 842)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..842
                     /organism="Streptomyces somaliensis"
                     /db_xref="taxon:78355"
     Protein         1..>842
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          2..>219
                     /region_name="SbcC"
                     /note="DNA repair exonuclease SbcCD ATPase subunit
                     [Replication, recombination and repair]; COG0419"
                     /db_xref="CDD:440188"
     Region          <150..682
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          <685..>759
                     /region_name="COG4913"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal ATPase domain [Function unknown]"
                     /db_xref="CDD:443941"
ORIGIN      
        1 mrlhrlrvag fgpfgtaqei dfdalcsagl fllhgptgag ktsvldavcf alygsvpgar
       61 qspgaslrsd happgtvtev vldltvagrr levtrrpaql rpkkrgkgst tekaqswlre
      121 hdpatgtwng lsrshqeige eiaqlvgmsr dqfcqvvllp qgdfsrflra daeargkllg
      181 rlfgtrrfaa veerlaelrr aaerrvrdgd qrllalahrm aqaagdaagd wpapggepgd
      241 pglaeavlsw aavarsgare aldtaglala aaeqrqaaar rtlderrala alreryddar
      301 rraaaleerr aehearqarl dasrtaerva gplalrdeae rdhraadaar dralaalpdp
      361 lpgslpgspa dagadalarl aqtrrrelad ldsarraeqr laqiaherad ldrqaraddr
      421 alrdtadwla gwettrrtll arvdatreaa traehllgrl aparrrrdaa rrrdalaqda
      481 aaararltaa reraatahet wldlrerrlr giaaelaarl edgapcavcg saehpapaqp
      541 tadhvdraae daayaahtra aealtaaerd laavrealaa aaaeaaeqps pgargtevre
      601 aghgdagsrd pgrddagerg pnggsaegrh sgrdgaggrs pdhggagdha pyrdgagdhd
      661 pdrdgagdyd pyrdgaggps vavledlvar lerehaeahd laadgqaare aleraereha
      721 rrteehrqte vraaalasrr ealdqeqaar eadlaralgd gggtvarraa alereaaald
      781 aaadavraae aaarrlkead grladaayra gfatpaaaaa allddaarrd lqhrvdawha
      841 ea
//
LOCUS       WP_010469080             277 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Streptomyces].
ACCESSION   WP_010469080
VERSION     WP_010469080.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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   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 277)
  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 277)
  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 18568702
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..277
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30872
     Region          19..76
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          97..275
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mtqvpeqvgg qrgqdpadel lrsfgrqiki lrqraghtqa algellgyse aqiaaieqgr
       61 rvprpdtidr ldhlleaegm llamkrpval trypaffrda arieetavef hqyaplivpg
      121 mlqteeyart mftvwrprrs eteieqmvsa rlerhrlfdr kpapvlsfvl eeavlqrpig
      181 gvdvlrgqle hlllagqnpn veiqvmptqv tdhacvdgpf tlmvpeggeq vayvesqgsg
      241 rvltcretvr giaarygiir aqalppaksq nliekll
//
LOCUS       WP_010470491             401 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Streptomyces].
ACCESSION   WP_010470491
VERSION     WP_010470491.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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
REFERENCE   3  (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   4  (residues 1 to 401)
  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   5  (residues 1 to 401)
  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   6  (residues 1 to 401)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 401)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 401)
  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 18624027
            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="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40390
     Region          14..77
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          77..379
                     /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 metpgsqtsl hranlervvr avrmagsltq aeiaratgls aatvsnivre lkdggtvevt
       61 ptsaggrrar svslsgdaga vvgvdlghth lrvavgtlah rvlteesepl dpgtscaegl
      121 draerlvrrl igeagvspgk vigvglglpg pigaapgapg aapvppgraa adpgrelsar
      181 lgapvyvddd arlgalgelv wgagrgvrdl ayvrvadgvg aglvidgriy rgpggtagei
      241 ghitldesgp vcrcgnrgcl etftaaryvl pllrpghgpd ltmagvvrla regdpgcrrv
      301 ladvgrhigs gvaslcnlln psrvvlggdl aeagelvlap lresvsryai psaarhltvv
      361 sgalggraev lgalalvlne mgdstllggt rraggrapas v
//
LOCUS       WP_010471147             679 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: M4 family metallopeptidase [Streptomyces].
ACCESSION   WP_010471147
VERSION     WP_010471147.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 679)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 679)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 679)
  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 679)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..679
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..679
                     /product="M4 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=70564
     Region          81..664
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mrstpsrrat atgalvaaaa vlavgvqtgs ataddawgts apkrqaaaqa dpgslpadlt
       61 paqraalira adadkaakak elglgaqekl vvrdvvqdrd gtthtryert yaglpvlggd
      121 llvtenpaga tervakasra elrnvdttad vapaaaerqa laaartegak apeaqqaprk
      181 vvwlaegrpv layetvvggl qhdgtpnelh vvtdattgek lyewqavhng tgntmysgqv
      241 nlgsaqsgss ytltdtargg hktynlnrgs sgtgtlfsga ddtwgdgtpa nletagadah
      301 ygaaltwdyy knvhgrsgir gdgvaaysrv hygnnyvnaf wqdscfcmty gdgennakpl
      361 tsidvaahem thgltsatak lvysgesggl neatsdilaa avefhanntk dvgdyligek
      421 idirgngtpl rhmdkpskdg sskdywysgi gsvdvhyssg panhwfylls egsgakting
      481 vaydsptsdg lpvtgigrdk aaliwfkalt tkftsttnya garagtvava telygagsae
      541 vkavenawag vnvgarpggg dpvgkvfent advsipdggt avtssvnvtg itgnapsalk
      601 vgvdivhtwr gdlvvdlvap dgtayrlkna ssgdsadnvk etytvdasse langtwklrv
      661 qdtarydsgy insfkltfp
//
LOCUS       WP_010471205              83 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase, partial [Streptomyces
            somaliensis].
ACCESSION   WP_010471205
VERSION     WP_010471205.1
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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Streptomyces somaliensis"
                     /db_xref="taxon:78355"
     Protein         <1..83
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
     Region          <3..59
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 pkdftpamya asarltagic arygipvdre hvighveveg tdhtdpgphw dwdrymelvr
       61 raaaapsasp sapaaraggg ras
//
LOCUS       WP_010472867             158 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010472867
VERSION     WP_010472867.1
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   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            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="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=16485
     Region          11..119
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mshyhsrlls klmkhnnsqg ftliellvti vivailagva lpsmlgqank srqsaaksqi
       61 gavnraqqvy rlesatfsnn mnllgigipl ttddysysfg ttnstlaefr atptnetlta
      121 itgctnanvv lgslattsvt leeqpapggg tiatppsc
//
LOCUS       WP_010472869             154 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010472869
VERSION     WP_010472869.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            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="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15643
     Region          14..>104
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mktnlqakli qhfankkgnk gftliellvv viiigilaav alpsmlnqan rarqsaaqsq
       61 vgavnraqqa yrleapqfap ayadlqiada stedytiaia vstaiagett avpidtgsgl
      121 sayrgcvsvd aatgttdsei aenpgnaaap aagc
//
LOCUS       WP_010473140              73 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Streptomyces].
ACCESSION   WP_010473140
VERSION     WP_010473140.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 73)
  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 73)
  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 73)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 73)
  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   5  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10164212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..73
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..73
                     /product="winged 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=7893
     Region          8..72
                     /region_name="WHTH_GntR"
                     /note="Winged helix-turn-helix (WHTH) DNA-binding domain
                     of the GntR family of transcriptional regulators; cd07377"
                     /db_xref="CDD:153418"
     Site            order(8,10,33,35..36,44..48,50..51,54,64..65,67..70)
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:153418"
ORIGIN      
        1 meldrsipfa gqvaddlrrr ldagewksgd kfpgtvaiaa eydisqstav ravgvlvseg
       61 rlrkviprgf fvm
//
LOCUS       WP_010473517             414 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Streptomyces].
ACCESSION   WP_010473517
VERSION     WP_010473517.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 414)
  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 414)
  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 414)
  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 18568580
            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="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44613
     Region          <3..56
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          <16..403
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mglaerrral gysqerlaqa vgvdrttvgr wesgritpqp aqrrrlattl dlslreldvl
       61 lsppragqga agrqvdavps agdldemirr eflrlltlsg alaalsddea qaltseflqa
      121 apsdftqmna hlwqvyrlar tkatlrpvir dqlaalgraa sgshprpllh aaadllqlag
      181 evafdanrht eaaasyalaa sagkdtrayd lwacalvrha yvdmaehrhr qavqlldmar
      241 klaergdtal ptrhwaasvq aqayaglgdl aaceraldha eqvrelppgs anggwlrfdg
      301 srlaeergar yvrlgrldla ekalgealrq aalapgrsfr rrgavladla avgvrrgdpe
      361 qavayggeav elaeasasgy varrlqelch elaplgrdpr vaelkariva ldtp
//
LOCUS       WP_010480193             229 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010480193
VERSION     WP_010480193.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 229)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..229
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=25752
     Region          1..215
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mafqpivnla dgnifaqeal vrgmnnesai sileqvtden lyrfdqacrv qaiqlaaeld
       61 iqsilsinfl pnavyhpefc lhttletaeq cnfpisrilf eltevekvid yahvqsiikh
      121 yqklgfrtal ddfgagysgf nfladfrpdf ikidmalirn idkdkarqai vrgivqvcrd
      181 laiepiaegi etgleldvlr elglqlfqgy yfakpsfrsv itdlslars
//
LOCUS       WP_010480530             703 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Stenotrophomonas
            geniculata].
ACCESSION   WP_010480530
VERSION     WP_010480530.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..703
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=76669
     Region          34..702
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mslspyrptp sllflavslg lastaaaapq attldavqvt aaadasaqar ealkrvpgas
       61 nvidvakads rlsssadvla sqpgisaqsp gnegtkisir gsginrgpga hasgiavsid
      121 glpltgpggt pyelleplwl srvevlrgan gfergalalg gaidyvsrsg rdsagvqlhy
      181 eagsrgyqkh giswggvngd vdyflaytdt efdgyqrhar gdgkgamani gwqitpdlqt
      241 rffvryretn hetpgrltrd qirndphaan asnlaidarr pqpgstwvgn vttlqideds
      301 slqaglvyht ypmdlnesly rqqldyanln atldyrrrhr lfgldsettv glrvthdlda
      361 dvreslrfas ngyaagtrtr dfrhhgtdst lhvgntltfn drlrmqtgla listrrdvqv
      421 twpssggrlr dhdwdyaprl gftwqhsaqt qwfgnlsrsv eaphpwsmiw gsnqyfgpgn
      481 gpstgrqrap vpmqnqtatt lelgargdaa lgrweltgyy ahvnhellsv elqpvpnlfi
      541 aennasptvh rgieagldst lwqaapgrls lrqaytfsdf gyrhdarfgs nrlpglprhs
      601 yqaelrfdha sglyaalnte yasriavdya nsywadshvi fgsrigyeap ggrwqawaem
      661 rnignrhyaa tvtpgyddag kdvarstpge grgvyagvrw rfd
//
LOCUS       WP_010481033              86 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Acaryochloris sp. CCMEE 5410].
ACCESSION   WP_010481033
VERSION     WP_010481033.1
KEYWORDS    RefSeq.
SOURCE      Acaryochloris sp. CCMEE 5410
  ORGANISM  Acaryochloris sp. CCMEE 5410
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Acaryochloridaceae; Acaryochloris.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 86)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 86)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 86)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Acaryochloris sp. CCMEE 5410"
                     /db_xref="taxon:310037"
     Protein         1..86
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=9126
     Region          7..86
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 msapnikvtv klfaayqevv gspelelefp ngstvahvgq yfweqypela slksvthfgv
       61 nldfvpgdtp lqpgdevvli ppvsgg
//
LOCUS       WP_010482841             249 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Pseudomonas].
ACCESSION   WP_010482841
VERSION     WP_010482841.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  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   3  (residues 1 to 249)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            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="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28197
     Region          37..244
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 msspfaeedg pqpprvlkap meiaatlrql qqnhdplvis fhernqrfqs flievdpdkg
       61 rlifdelvpn dgerflknae pfsvessreg vrvawqcdds aqisehdglr cyfcampsev
      121 lyhqrrsafr atlklgelva islkgeklak plsgqmldis atgckiriag dvsqslkpgm
      181 iyeelvaqlp fgamtapiel rhvhynekld tsmlgvrfyr msglvqrqve rfvyqlqrea
      241 krlesdtfl
//
LOCUS       WP_010483027             347 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010483027
VERSION     WP_010483027.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 347)
  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 347)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 347)
  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   4  (residues 1 to 347)
  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 347)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..347
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38955
     Region          29..214
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          258..340
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mavtsprirl gdlsvgfvds laeamrscgq dplalldsyg ldparlatpr arlsiprymr
       61 lghaaieqtg qpdlglimgk lsrlgqlgla gvtaaqaptv rqaarslirf eplyasnyrg
      121 hasfaedhqg gwlrfysisp ynaynrfvid svlagwtrql eqvaqqpitp erahiefpap
      181 hysdayepal acpvefaaeh nqlrlsqatl nlrnpqhcps twlhlqelce heleqltrtr
      241 slreriiqll gpllhgrepd lqevaarlqm ptwtlrrkla eegtqfrail netrhdlava
      301 yirdtelafg eiayllgfas aeafqrafkr wnqqtpgefr raqrlgs
//
LOCUS       WP_010483488             301 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Stenotrophomonas
            geniculata].
ACCESSION   WP_010483488
VERSION     WP_010483488.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 301)
  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 301)
  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 11466508
            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="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32501
     Region          52..301
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 msvhsirpap ptgltrrdal riavagsigl gaatiagtlp asaataplkg nlkhsvarwt
       61 fpqlsvtqlc atvkdigfaa idlvgpedwp tlkahgvyss mcngaelglt kgfagrqfhd
      121 qlverytrhi dlvadagyrn licfsgnrng mdpaegmana eaglkrilgh aekrgvvlvm
      181 ellnsrvdhh dylcdhsawg velcqrlgsd nfgllydiyh mqimegdiia tigkhhacfk
      241 hyhtagvpgr neigdqqelh ypaicraird tgfkgylaqe ftpaapdpva slreairlcd
      301 v
//
LOCUS       WP_010483599             241 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Stenotrophomonas].
ACCESSION   WP_010483599
VERSION     WP_010483599.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 241)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..241
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=25770
     Region          46..215
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mtasrlcrla afgllatsas apalaqtpal atsaddlaal lsrsapkadr hvlqlaaham
       61 rcalqrpelg ingdrlsvid ysrpsteprl wvfdlahqrl lfeewvahgr nsgenrtehf
      121 snrdgsfmss lgaftaqety mggngyslrl aglepgfndr ardraivihg apyvnpataq
      181 lqgrlgrslg cpavrlsvak plidalrggt mvfayypdqd wlkhsqllag gcggqgtlat
      241 r
//
LOCUS       WP_010485090             485 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Stenotrophomonas geniculata].
ACCESSION   WP_010485090
VERSION     WP_010485090.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 485)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..485
                     /product="amidohydrolase family protein"
                     /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=51890
     Region          19..461
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mfrsrplsla illvvaplsa saaeradlli rnatvvdveh astlagqsvv irgddivavg
       61 pdaqlrsqws atrqidakgk ylipglwdmh vhfgggpali eenkallply iahgittvrd
      121 csgdlpeqvl qwrgeiakgt lfgprllssg akiegikpvw kgtievgsea dadkaiarlq
      181 hdkvdfvkit dstlkpelfl ysasaarkag fkasghipma ltveqavdag lasiehldya
      241 fkagskdeaq iaadfgagri draeanrrld asfdrdtamr ayrdfakrgv fvtptlnggr
      301 ildfldqddh andpylayig pglratyqwr vdraakatpa qiearhaqyh qvaavlpllq
      361 eagvtiiagt dagflnsfnf pgialhqelq lfvkeglsap qalsaatrsg pawfgqmdry
      421 ggvaqgkaad lvlltanplq diaatekids vilrgnvydr aaldgmladt kakvaawnae
      481 aakan
//
LOCUS       WP_010486193             188 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Pseudomonadota].
ACCESSION   WP_010486193
VERSION     WP_010486193.1
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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Pseudomonadota"
                     /db_xref="taxon:1224"
     Protein         1..188
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=20861
     Region          16..182
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mpnpllpdlq lqplpyqdrl plrdpatlem vvihctelpd lamareyger vlydsgagns
       61 ghfyidrdgs vvqyvaperv ahhvrgmnah tlgielvntg rypdwfdsrh qamdeaytea
      121 qlaalealll alvarypslr riaghdqldl eqvpasddpt ltvarkrdpg plfpwarvla
      181 kvplqpvg
//
LOCUS       WP_010485164             693 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Stenotrophomonas
            geniculata].
ACCESSION   WP_010485164
VERSION     WP_010485164.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 693)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..693
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..693
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=75322
     Region          24..693
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mpilalqpar lplaaalalc llpttrafaq dgattldsiq vsgswlgtgl hdsvkrfaga
       61 rtvvdrqrie asgaaslgda mrripgvqvt dnsgtagssv slnigvrglt grysprstvl
      121 ldgvplavap ygqpqlsfap tslsniesid vvrgggavry gpqnvggiin fstraiptea
      181 glhgeagvry taydhgggds tqynaflggt gdndlgaall ysgqdgrgwr qgsddrfndl
      241 alkfayaide qqelraklsy ydvrsltpgg ltraqyeadp fqstrptdfw kghrtgidlg
      301 ytntlsanse fevlayynes trasslinaa ntqltvqprd yrvlgiepry tqrlhwgsav
      361 hditagyrfl rergndrsyt varrtgaasa ttrfdnatda hafyiddria igqwritpgv
      421 rmewidmdrr qaggtatfsr rndkalpsin iaylltpqlt vfgnyttsfg pvqniqlnsq
      481 tasnplnpev akttelgarw qdgalraevt vfkmrfdnqi lqvpgitppt fqnigatdhk
      541 gvesaleyhf aedsalagle lyanytwtka iqqsgdnrgl dvpfysrdtd sigaryalag
      601 wtfnvssthq sgqfsdtant waesadarvg rvpgvrlwna qvawqvpglg dseialgvnn
      661 ladkrwytrn vdgnagrmva aprtfyvqgr yrf
//
LOCUS       WP_010486584              82 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Pseudomonas].
ACCESSION   WP_010486584
VERSION     WP_010486584.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 82)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 82)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 82)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 82)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..82
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=9003
     Region          1..82
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mirvqyfary realgldgeq lsnsedfstl ndvrefllar ggawqvlaeq nlmcarnqel
       61 csldeavaeg devaffptvt gg
//
LOCUS       WP_010486988             282 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Stenotrophomonas geniculata].
ACCESSION   WP_010486988
VERSION     WP_010486988.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas geniculata
  ORGANISM  Stenotrophomonas geniculata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Stenotrophomonas geniculata"
                     /db_xref="taxon:86188"
     Protein         1..282
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28885
     Region          169..236
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mltralivvl ailnlgvacw wllrdapqpp apppqpagva elrwvpggvd aaeaadataa
       61 apvaplmdre paektavaat papaaparpe iakpqvaeat pvaaaakpvt ppapvpapek
      121 patrpvaaep arcvalgpfa draaatsaqg kagnvisqvr lreqpaasgs aryrvmlpaa
      181 anrddaqatv krivaaglsd yyiisqgeda navalgqyrn regaerrmaa vqaagfqprl
      241 vasgdagqww legqlaagtq paqaqqrsga aqsrslecar lr
//
LOCUS       WP_010487766             364 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Pseudomonas sp. S9].
ACCESSION   WP_010487766
VERSION     WP_010487766.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 364)
  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 364)
  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 364)
  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 364)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..364
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39696
     Region          37..362
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mnlrnllgaa vallatmgla gckeeakatt aetskpaqsv hwkmvtawpk nypglgtaae
       61 rlaervstms ngrlsikvya agelvpalev fdavsrgtae lghgaayywk ekvpaaqfft
      121 avpfglsase mnawlskgdg qklwdeayap ygvkpmvvgn tgmqmggwyn keinslddlk
      181 glkirmpglg gevlsrlgat tvnlpggevf taletgaida tdwvspyndl afglnksaky
      241 yyfpgwqepq avlellvnqk aldslpqdlr ailteatlaa nqdmmddyvy hnatalvelk
      301 kqgtelkrfp devlaamkqq ssavldelag qselntriwn smkafqeqvt pmhevsekel
      361 ynwr
//
LOCUS       WP_010488281             132 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Lacticaseibacillus zeae].
ACCESSION   WP_010488281
VERSION     WP_010488281.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 132)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 132)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..132
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=14268
     Region          2..126
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(7..10,40..42,45,71,108,122)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mlklytdgat kgnpgptgig ilvsglpqqi qrhaalppmt nheaefaaai agfnllieae
       61 lttvpvafys dsklvvqaie krytkhypal taellalidr fplvlpnwlp drqnrgahtl
      121 aqqglreaet ks
//
LOCUS       WP_010489650             835 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Pseudomonas sp. S9].
ACCESSION   WP_010489650
VERSION     WP_010489650.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 835)
  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 835)
  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 835)
  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   4  (residues 1 to 835)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..835
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=91766
     Region          65..799
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mpdsvatqlr lapdaltrpf apeqfnfttt ddlepfrgil gqeravealq fgvamprpgy
       61 nvfvmgepgt grfsfvqryl kaegkrmdtp adhvyvnhfd epreprvlel sagsagefia
      121 dinllidnll atfpavfehp syqqkksaid rafnkrydqa ldvierlsle kgialyrdss
      181 niaftpmleg kaldeaefaq lpeadrerfh ldiamleerl neelaslpqw kressnqlrq
      241 lneetitval qpllsplsek yaenaeicay lqavqvnllk tvveqlvdve kvdaqtrkll
      301 eeqycpslvv ghhvdggapv vfephptydn lfgrieynnd qgalytsyrq lrpgalhran
      361 ggflileaek mlgepfvwda lkralqsrql kmesplgdlg riatvslnpq viplqikvii
      421 igarqlyyal qdhdpdfqem frvlvdfded ipladesleq faqlmktrts eegmapltaa
      481 avarlatfsa rlaehqgrls arigdlfqlv seadfirqla setvtdvghi eralkakatr
      541 tgrvsariid dmlagiilid tsgaavgkcn gltvlqvgds afgvparisa tvypggsgiv
      601 dierevnlgq pihskgvmil tgylgsryaq efpleisasi aleqsygyvd gdsaslgevc
      661 tlisalsrtp lkqcfaitgs inqfgevqav ggvnekiegf frlcearglt geqgaiipqs
      721 nvttlmlddr vlqavrdgqf hiyavrhvde alsllvgedv gspndkgqfp tgsvnarvve
      781 rlreiaeidm geedkepeal aekvakavpt psdkkppakk pvpakpavsk tekpe
//
LOCUS       WP_010490021             351 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas sp. S9].
ACCESSION   WP_010490021
VERSION     WP_010490021.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   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 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   3  (residues 1 to 351)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 351)
  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   5  (residues 1 to 351)
  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   6  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12117664
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39669
     Region          24..208
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          86..341
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mqsdkgtisi rlvteavlel qgrgqdsgpl ltragiapal lakpyarvtc eqyarlwldl
       61 arqmddeffg lnarrmkvgs fafmartask etslepalhg alrflglife dfsprllrag
      121 gmaeiaidqs pnsqatrpra fadftlwmmv hglacwlvgr ripiiaidvq rpqpdyledy
      181 rvmfsdnlrf grpysrllfn aqwldlpirr sadelkqflq aapqgilvry rdpqshaari
      241 kaylrgikpe rwpdieaisa hffmapstlr rklsqegqfy qsfkdhvrrd lalnrlnqge
      301 vnfnelafel gfadasafyk afkkwtgstp gqyqammqpq ggvtvktaqt g
//
LOCUS       WP_010490183             156 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Pseudomonas].
ACCESSION   WP_010490183
VERSION     WP_010490183.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 156)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            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="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16806
     Region          7..155
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfelegaeey pllvaqlesl laderdfian aaqfsaflfq qmpalnwagf ylardnelvl
       61 gpfqgkvacv ripfgrgvcg aaaqslqtqr vedvhafagh iacdsasnse lvvpllksgk
      121 ligvldldsp qvgrfsaedq agveqmvevf lrltdc
//
LOCUS       WP_010490488             267 aa            linear   BCT 20-JAN-2025
DEFINITION  phosphonate ABC transporter ATP-binding protein [Pseudomonas sp.
            S9].
ACCESSION   WP_010490488
VERSION     WP_010490488.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S9
  ORGANISM  Pseudomonas sp. S9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
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   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Pseudomonas sp. S9"
                     /db_xref="taxon:686578"
     Protein         1..267
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=28381
     Region          3..246
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mtvtlqgvgl thangqvals didltinaae riaiigpsga gkttllrlla tslqpstgsi
       61 slleqqpwal sasqrqrlra riglihqapp lpprqrvvta ilagklgaws llksvlnlfy
      121 pvditgaqaa larldladkl fercdqlsgg qlqrvgiarv lyqgpqlila depvsamdpv
      181 laghtlnvln neaaargvtl laslhavdla mahfprvigv ragrimfdlp sdqispeqld
      241 tlyaneklqp tpevitpppl vvqiprc
//
LOCUS       WP_010491274             685 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Paenibacillus elgii].
ACCESSION   WP_010491274
VERSION     WP_010491274.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 685)
  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   3  (residues 1 to 685)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..685
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=74759
     Region          1..685
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          170..248
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 memnqylsmf idesrdhlqa mneqilsles spediaivqn ifrsahtlkg msatmgfedl
       61 aslthemenv ldlvrnhklk mdsfifdclf ksldslesmv ediiqggtgq advteivaal
      121 ksivsgdytk ggaaggttak aaqatvagge ldefqysilq qsieagipvl rlevtvrqdc
      181 vlkaaraymv fnvleqngev iksnpsvedi eqerfdqsfv vyyisqidtd elhkqvasvs
      241 eidkvdvivl dqakltelms ppsgssaaaa qaqaqaetaa astqeapkqe akkapaagga
      301 pvagrtirvd ierldtlmnl fsellidrvr leqlaseirr seltetvehm srvssdlqni
      361 vlklrmvpid tvfnrfprmi rdvaktldkk vdliitgadt eldrtvidei gdplvhllrn
      421 avdhgvepsa ervalgkset gtihlrayhs gnhvfieiee dgrginrdkv lkkalennvl
      481 tkeqaaritd devnqlifas gfstadkisd isgrgvgldv vktkiqslgg qvqldsawgk
      541 gskfsvqlpl tlsiisamli rlnnekyaip lssivetmav rqeqirsvhg nrmveyrtgv
      601 iplvsladlf dvpggtnise netqvviirk gdkmaalvvd efigqqeivl ktlgkyltkl
      661 faisgatilg dgqvaliidt nalik
//
LOCUS       WP_010492221             198 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Lacticaseibacillus zeae].
ACCESSION   WP_010492221
VERSION     WP_010492221.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..198
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=22809
     Region          25..197
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mgknkgldsl ladyhtfisg tatqygvsss mltnairegr isreargvyv engytwddfa
       61 ilsqrysrgv faldtalfly gltdqipdrf imafprgyrn prlsehwivp iyyvpsrysp
      121 gittvetpnm nfvrtysver tlldvwerpd vapytrneaf knyfdeygqn nasferllkl
      181 keqlyphsdl tkllevlv
//
LOCUS       WP_010493501             374 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Lacticaseibacillus zeae].
ACCESSION   WP_010493501
VERSION     WP_010493501.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus zeae
  ORGANISM  Lacticaseibacillus zeae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Lacticaseibacillus zeae"
                     /db_xref="taxon:57037"
     Protein         1..374
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42013
     Region          1..265
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          260..347
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrflhtadwh igkklndfdl ladqqavfdq lvavakaqkv daiviagdly dralpseaav
       61 avldqmlvkl nrdlhypllv isgnhdsavr lrtgrswfsa tqmyvntqla eaftpiemdg
      121 vqffllpyfe pfavreyfqd qtitnvaqai rpivtkmktl fkpdmrhilv shffaagsdh
      181 sasetkvnvg gldavpiddl aafdyvalgh lhnhnalhge pkiqysgall kyavgeakqe
      241 kgvyivdtet mqrkfvslkp qhdllelkas yadltdpayy qkqdrdayig vdltdtqvip
      301 nvmaqlrqiy priislrren gvqavkplqq rqrdldpvsl lkafyeelmq tdltadqlkw
      361 akaglaaaes eqkq
//
LOCUS       WP_010494755             282 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Ligilactobacillus
            acidipiscis].
ACCESSION   WP_010494755
VERSION     WP_010494755.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 282)
  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   2  (residues 1 to 282)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            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="aminoglycoside 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=33032
     Region          <80..225
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mesvlidfln eyykanlkki hdvagnqhla gysqyyktdl fvkifkqqem fyaeqhvdqv
       61 ycpdifigtv ifgenyvvvl kdrqlkeveq kdlneeqayi ygrllaefhr nltgkvsvpq
      121 tneslsqqik fkfdslkdek hqqkakrvlk viekdlpaad qefaklkkvv lhgdfsirni
      181 miyqgnyvli dferthigcq yedfikfffy evkdkkmrqs fiagyqslle feipqkscqq
      241 allfytaldi ysfhesheqe kfgdmadqml atvsdgvpvl ei
//
LOCUS       WP_010495659              85 aa            linear   BCT 20-JAN-2025
DEFINITION  zinc ribbon domain-containing protein [Paenibacillus elgii].
ACCESSION   WP_010495659
VERSION     WP_010495659.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 85)
  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 10577258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..85
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=9397
     Region          5..84
                     /region_name="Zn_ribbon_2"
                     /note="Putative zinc ribbon domain; pfam12674"
                     /db_xref="CDD:463667"
ORIGIN      
        1 mdkqfcqscs mplntaedfg tnadgsrnee yctycyqgga ftspdatvqs mieecvphvv
       61 kgqgmseqqa remlnhvips lkrwl
//
LOCUS       WP_010496189             367 aa            linear   BCT 20-JAN-2025
DEFINITION  GerAB/ArcD/ProY family transporter [Paenibacillus elgii].
ACCESSION   WP_010496189
VERSION     WP_010496189.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            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="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=42416
     Region          5..364
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 mktnkrtkpl nayvlffiis gtqlgdpaqs fqrnvyiaag hdawvcmiln gllvsvalya
       61 mvktmgvype kdlyqihqel fgrwlgklfn lafvlyffif cftvlhsysq vvhtwlfpdm
      121 nswlfntlms llflygvtgg vqviagfavv sfilwlwvfl lyyfpwkyaq vdqllplfet
      181 gpgqivkgir aatypmlgye lvyflypfir dkhnvqkysq lavaftvfty ctllinaivf
      241 yageqlkhti watyswykia qfpflerfei vgaafwmilv lpnnlvllwa strgmrsvfk
      301 lkqkyalyac clifvlssel lfthedvewi snllgeigvf lvwlypfalf alvrwksgra
      361 kkkgaea
//
LOCUS       WP_010496233             293 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010496233
VERSION     WP_010496233.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 293)
  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 293)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 293)
  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   4  (residues 1 to 293)
  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 293)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..293
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33325
     Region          33..286
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <184..292
                     /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 mrsdliirel pivkqvfpyk vlpqkspsqf yshyhddvfe illvqqgsae friggqrlta
       61 vpgdifline geiheggtld dgaeycaflf drtriahshv ahsdyaaslt eplsvpvhls
      121 psdahyesva allrhiadey drketgfevv iqsyitvlit vltrlyaspg rsdqgeaask
      181 rkleklkevl tfvethyrek ltieraaqva nmsnhhfcrv fraavgrtfm eyvhllrink
      241 aeelirdtdw smttiaeevg icdvnyfgrl frkykrcspa qlrkhryagq ppg
//
LOCUS       WP_010496447             227 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Paenibacillus elgii].
ACCESSION   WP_010496447
VERSION     WP_010496447.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  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   3  (residues 1 to 227)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            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="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25203
     Region          <69..220
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mnwtlalane tvvfprscsl ivvgetkegs pfcyednftl lkasaeeltv tldaasihpl
       61 eklhhvcfie fsfreqgily yalvdllhle tkrnvctltl taplelkqsq krryprialp
      121 trtpvtsriv gvreqishqn vaftgqildl ssggmafmts trvfcplele lsfvlpgiaq
      181 kitvygeivr vahfssdayr vavrfhrvpd statlmeeyc sasgads
//
LOCUS       WP_010497219             169 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Ligilactobacillus acidipiscis].
ACCESSION   WP_010497219
VERSION     WP_010497219.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         1..169
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17837
     Region          3..168
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdimqtiyqr qavrdfsdeq vptkdlqdim dagqagpvgm geyekfhftl ltnsgtikqv
       61 eadsvsnpyy gapaviiisa qkqdssvgsm ecvsagamve nmalaatgkn lascvimgal
      121 iplskdddll sklqipagfa pvislavgyp aesiskptkg rhevtqtii
//
LOCUS       WP_010497981             457 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Paenibacillus elgii].
ACCESSION   WP_010497981
VERSION     WP_010497981.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 457)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     Protein         1..457
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=52134
     Region          <12..431
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mtfsfasgew kerirmllrl pypsralrff ppeftfrnpv lslvrryrsq gkscglilly
       61 ledfhhmfst ysesrlcalq drirqtilel lpscfrdkdv igvrqfaldd ygifvkeqav
      121 cgfdelqrka qelqkevsrr lrmhadvdaq apvslqsgcy iigpdlents agiqaayhya
      181 rciatrklpp hfcptrehll dilkqenifv laqpilnlas gelygweilt rgpqnspfht
      241 paelfdmayq adllssfefl vikkafmeis sraiqeqvfi nvtpvslghp lflhqlletl
      301 kqfpaisasq vvleiterha irdfqyigav mnacrahgvr favddagagy sslqsiselv
      361 pdiikidrsv iaeidrmsvk qsllkallhf adnmncqvia egverpeels mlcemqvhmv
      421 qgfyfarpqp lvpdqervrq lqlvkekivg hrhmhpa
//
LOCUS       WP_010498464             392 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Paenibacillus elgii].
ACCESSION   WP_010498464
VERSION     WP_010498464.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 392)
  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 392)
  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
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 392)
  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   5  (residues 1 to 392)
  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   6  (residues 1 to 392)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 392)
  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 12122468
            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="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41939
     Region          21..60
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          86..382
                     /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 migrgqtgna klvkhinreg ilhqlkenpr vsradlaklt elsrpcvsal vdemivegli
       61 sevgfgeskg grkpilleyn fqaygvigav fegstlqlai anlkgellvq rttclphpmn
      121 gemaiqsieq glaallnesg fdkarllgmg lglpgitqrs egtvsyapst gwmglpvrke
      181 ieaalglpvv iendvnlmtl gefhkgigvg hsnlmymyag tgigagimid gqlyrgakea
      241 sgeigymvig pvgnqtkgey gvfernysvr airekakavl psldegesiv kqivdqakgg
      301 veaaqtlldd icrhwtygia nltsvmdpal lilsgemlhi gdegvhkiqq wltdwvpsvp
      361 riemaslgdq agligaihca leafpstskl qr
//
LOCUS       WP_010498555             213 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase, partial [Ligilactobacillus acidipiscis].
ACCESSION   WP_010498555
VERSION     WP_010498555.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus acidipiscis
  ORGANISM  Ligilactobacillus acidipiscis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 213)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Ligilactobacillus acidipiscis"
                     /db_xref="taxon:89059"
     Protein         <1..213
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
     Region          63..200
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 ansvkmakqa sidkkrdqki akqkkdqkqr arkpvdwskp sltgeypdlt pyrhikkkkd
       61 kvwldvsvrk qrvyvmqgry ilytmyasig knydghtqdy qrtpvgdfrl qkehgpeyyd
      121 atkkygakyw tsfsghgvyr fesvpfdkng kviekqagrl gsqkvtkkhn iknygsirlt
      181 vpdakwlqen ikphtrvvvh gkksdkefld fly
//
LOCUS       WP_010499891             197 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Paenibacillus elgii].
ACCESSION   WP_010499891
VERSION     WP_010499891.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 197)
  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 197)
  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   3  (residues 1 to 197)
  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   4  (residues 1 to 197)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 197)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 197)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            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="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21841
     Region          1..188
                     /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"
ORIGIN      
        1 mknsivvvdd dpiirmdire mleeegyava geakngeeai elvaalkpdl vimdvkmpvm
       61 ngikasriir slhdtetsvl lltaysqkel vqdarsagva aylvkpvsee dlipaveial
      121 sqkeridslk kdlehlkqsi eerkriekak givmktfald eeeayrkmra asmaesipli
      181 kladgilkdg pqrwfgp
//
LOCUS       WP_010500170             296 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Paenibacillus elgii].
ACCESSION   WP_010500170
VERSION     WP_010500170.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            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="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32194
     Region          18..262
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mepwqltael ildekaalge gpvwdhrsgr llwvdiegmr ihhydpvqgt nrsiqldqrv
       61 gaavpragge slvlalehgf hlldlateql tkltdpeagq penrfndgkc deagrfwagt
      121 mnrkssgptg tlyclepngt lrkaidgvic snglgwspdg rtmyyidspt kqvvaydyep
      181 aagaisnrrt vvtipegegi pdgmtvdcdg mlwvaqwggw rvsrwnpqtg erlgfvrvpa
      241 aqttscafgg pdwdelyitt artglseeql aqqphagglf rvkpgvkgsp arfygg
//
LOCUS       WP_010500460             227 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Paenibacillus elgii].
ACCESSION   WP_010500460
VERSION     WP_010500460.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  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   3  (residues 1 to 227)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            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="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25475
     Region          15..218
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mntpavsrnf nnskerhrss gtvmlnsriv vekekfvstg tltyvegdil eiemseykaf
       61 elgdavklti yspggfypfe stvvakdqga vmviippqhl srfaekrehp rvevnqkgal
      121 vsyrnedgsw qvpegqiplt vknislsgig fiieepveld rdalvqlhld lgfsmhcrae
      181 iirtepvefg cyygahfdel aadkanslra filkkqveth faqkree
//
LOCUS       WP_010505566             303 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Gluconobacter].
ACCESSION   WP_010505566
VERSION     WP_010505566.1
KEYWORDS    RefSeq.
SOURCE      unclassified Gluconobacter
  ORGANISM  unclassified Gluconobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 303)
  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 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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="unclassified Gluconobacter"
                     /db_xref="taxon:2644261"
     Protein         1..303
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33494
     Region          28..178
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          207..288
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mnyqsdtssl lalaaelapr sgynatslpn vrilrsetil edvpvlyrpg avfvlqgfkq
       61 gflngeiyry daehylavsv pvpfrmasqa spdqpllaiy fdfdlhlaae iattlngqag
      121 hdekmparsl vssrmaptmt dvlqrllhal hhpqelailg pgllrelhyr ilvgpqggsl
      181 maalrrngtt drivqsltli rerykeglsv selavtagms vpsyhvgfks ltgntpiqyl
      241 kalrlhearl miarrqgtla tiaaevgyas paqfsrdfkr hfhrtpseea kwmrehlgep
      301 iqa
//
LOCUS       WP_010507290             439 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Komagataeibacter europaeus].
ACCESSION   WP_010507290
VERSION     WP_010507290.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..439
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=48375
     Region          3..>437
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 matlewegkh avtaclermr agvlqvdshl crgaaegqdm iilgdnlaal dalmpdhagr
       61 vdmvlidppy ntgrrdwlyd dsastpaalh wleaalgpgq agrlsrqdrw lclmyprllq
      121 lrqlmaengv iacciddrey prlrllmeev fgpanflatf vwvntgnidn hsriktnhey
      181 vvvfardarr fvpgrvlapq vgarsklrrp virntiikng prnpvsdlvl pvgfparved
      241 gaipvptdpg fwprfdvpiv irdgrlaqav tlrsgwssrr qcaafiaagf ddiidrqglk
      301 trfyltssga vfmekdrlaq pshiltvleg mgtvqqaate laqcgvrfdy pkplslvtyl
      361 lralcpdpaa vvldafggsg ttgqavmdln aedggtrrfi vmemdehiat tvtqprlahv
      421 larharpgtg frfcrlgms
//
LOCUS       WP_010508827             470 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Komagataeibacter europaeus].
ACCESSION   WP_010508827
VERSION     WP_010508827.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Komagataeibacter europaeus"
                     /db_xref="taxon:33995"
     Protein         1..470
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47412
     Region          210..460
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mgvtvtgatg ltlginpdks diilglhrvs evaalqslgn vssaevsalq qaygndisal
       61 avrmfgvagi dtvmeqsggv nqqittagth tvtgteveig sttstplnsr iilkgathaa
      121 tvidgdmgtv dfvaqsgdvn yyaaggntdf vsgkgndtih vlggadtiyg adgrptvtgd
      181 wnapgstada arfnggdvnl rvidgvmvqd vshstisgyg dddyfgehnp acytntidgg
      241 vsdsiygsnn lvvdsvsdst irgnealtvs ggsndtisas ysthlddvna stisvsvngs
      301 ltfidgsngi sdtvtgnhat iygtagldlt antkttatyy assgnetldg glstgnlyav
      361 ggsgndtlig gsghdtlqag tgddllmags aktefefikg kaggndiiqd fgksagnvvt
      421 lagydatsss iqamldnati sggnttvslt ddtritfvgv tdlkvqnfks
//
LOCUS       WP_010512130             430 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Komagataeibacter
            europaeus].
ACCESSION   WP_010512130
VERSION     WP_010512130.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter europaeus
  ORGANISM  Komagataeibacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 430)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 430)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            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="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47691
     Region          11..410
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mtsekdaglp svkeafvwiw lpgavapvva grieregnah iftygrsylk regaipiyap
       61 elnlqrgaip pelplnmagc lrdgapdawg rrviinrltg lqgdaaadvd fdeltfmlns
      121 gsdrigaldf qrsadiyepr eqdnatleel qdaaghverg epippgleka lfhgssigga
      181 rpkaliedcg tkyiakfsas ndtyavvkse fvamrlaqrv glnvasvvrt qangkdvllv
      241 erfdrgtiey gwtrkaivsa ltmlgltelq ahyasyidla qivrvrfvqp retlrelfar
      301 mvfnvlvgnt ddharnhaaf wdgevlaltp aydicpqprn greanqamav heqdrrslle
      361 ncrlsassfl lrdkdareii srqaseiiag waevcdeael teidrdflwr rqflndyafe
      421 nfvdglpngl
//
LOCUS       WP_010514818             164 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Komagataeibacter oboediens].
ACCESSION   WP_010514818
VERSION     WP_010514818.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..164
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17463
     Region          44..123
                     /region_name="COG3942"
                     /note="Surface antigen [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443142"
ORIGIN      
        1 mkrertraal artvltrvva aggllslaac agggsghgwh gavqcapyar qvthvqlsga
       61 aaswwgqaqg ryprthaprt gavlvfratg rlpdghvsvv ravrsprevl vdqanwvpgr
      121 vgrgepvvdv sarndwsrvk vwwspihdmg ktvypaygfi lpag
//
LOCUS       WP_010515784             501 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Komagataeibacter oboediens].
ACCESSION   WP_010515784
VERSION     WP_010515784.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            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="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=55038
     Region          19..491
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mngiifppna eimpdapvni qaemgvlggi lmnnrgyelv cdflekrhfa nsvngwlyge
       61 iekviqsgve atpvtlkarv enaieldavg gfsyltqilm sqpgwmacrd fghairdawl
      121 rrelldigam aksramsaeg sapeeiiddl eqalltlgkd rgdqrltslt samdqameea
      181 saaaargdgi igmrtgfqkl deetsglapg cfyllagrps mgktgmgvgi avraakisrk
      241 pilywsgemd aksisariis ahsrlplrwv ltgtkpgprn pdgsegqrip lhrrewdrif
      301 aarkeaeqvp vvvddrpait vaqlygrarr marskaglgm ivvdyvglmr gtpttrkqgk
      361 yaevseissd llalakslnv pvlglqqlnr gvegrddkhp tmadlrdsgn leqdasgifl
      421 lyrdhyyaqr dpeptkrpae nmdtfsqrvd awherirase gkaeiiiakn rqgdcgtvpm
      481 lfngpttwfr dvregedsva w
//
LOCUS       WP_010516032             351 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Komagataeibacter oboediens].
ACCESSION   WP_010516032
VERSION     WP_010516032.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..351
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37944
     Region          1..299
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msvqldhitr ilpqggrpiv edinllvpdg sftalvgpsg agktsllrii agldphqdgh
       61 vmidgacvdm qdararnigf vfqhyalfah mtvaanigfg lsirprrtrp dkadiaarvt
      121 dlldlmqlpr mgaryphels ggqrqrvala ralatgprvl lldepfgald plvrqqirgw
      181 lrdlherlgl ttilvthdrq eaaeladtvv lmrnghvvqs gparqlednp adpfvmtftg
      241 dvvritghva hgvfmpalpd iqpvatpatd gpaeilirpa dirlrpgsgs arahlrhrrg
      301 lvgiyettia httfavetvt tpeparvipd caldiaagrl argdawlert a
//
LOCUS       WP_010515715             192 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Komagataeibacter oboediens].
ACCESSION   WP_010515715
VERSION     WP_010515715.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..192
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=20883
     Region          1..163
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mldrlyarii alaasrhaii wlaviafaea svfplppdim lvpmvlacra rafrlaaict
       61 aasvcgavlg wtigsflldy iampivrfyh aqntllilqe rfrewgvwii likgltpipf
      121 kfvtiasgaa hlplapflla cavtrgarff llaallrrfg apiqafierr lplvaglfal
      181 alvggivalk yi
//
LOCUS       WP_010515092             666 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Komagataeibacter].
ACCESSION   WP_010515092
VERSION     WP_010515092.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 666)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 666)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 666)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 666)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..666
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=72261
     Region          42..666
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mtqptgpsap gsptppdgag hpataadkat tapkiteyga dqhehaanpv gfaallgvlg
       61 vvfgdigtsp iyalrstimv vsqhhriapw evlgvlslii wslllivtvk yvilimradh
      121 ngeggiislm slaqrvapsn rlrialgmvg iggaclffgd gmitpaisvl saveglevsf
      181 paardlvipi almvliglfs vqcygtgkvg tvfgpimlvw fsllgilggl qilhhpavll
      241 aisptyavqf ivyhgwlsfi algsvvlsvt gaealyadmg hfgrqpirya wlfcvlpcla
      301 lnylgqgali iadpaalanp ffllgphwlq vpmiilstfa tviasqagis ggfslcrqii
      361 qlgylprmrv thtnaeeegq iylpefnrfl mvgalllvla frssdalasa ygiavtgtfm
      421 ctcvlamvvf rrlyhwsrpa aiatfggffl ldatffasna lkipqggwvp vllgivltlm
      481 mttwkkgrql imnrqkqdsm pmnsflarlp qsriirvpgt avymtgnpdf vpacllhnlk
      541 hnkvlhdhvl fvtvqtldqp eadhghrval qelapdiyri ilrygfmemp nlpraledlk
      601 asgldfdalq asyftsrell vrssvpklsr wrmslflfma rnatpateff rippdrvvel
      661 gvrlai
//
LOCUS       WP_010516076             459 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Komagataeibacter oboediens].
ACCESSION   WP_010516076
VERSION     WP_010516076.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter oboediens
  ORGANISM  Komagataeibacter oboediens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Komagataeibacter.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Komagataeibacter oboediens"
                     /db_xref="taxon:65958"
     Protein         1..459
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=50534
     Region          3..>436
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 matlewegkh avtvylermr rgvlqvdpal srgaaqggdr iilgdnlaal dalvpdhagr
       61 vdmvltdppy ntgrrawlyd dsastpaglh wldaalgpav aralsrqdrw lclmyprlly
      121 lrrlmaehgv iacciddrey prlrllmeev fgaenflatf vwvntgnidn hsriktnhey
      181 vvvfardarr fvpgrvlapq vgarsklrrp virntivkng prnpvrdlvl pagfpasfdh
      241 gvipvpvdpa fwprftapme vragrlvhpv tlrsgwssrr qcaafiaagf kditdrqglk
      301 trfyltasga vfmekdrqdq pshiltvlqg mgtvqqasaa larcgvrfdy pkplplvtyl
      361 lralcpdpga lvldafggsg ttaqavmdln aadggtrrfv vmemderiat tvtqprlahv
      421 larharagtg frfcrvvmpp saqdaemaip vgheaahen
//
LOCUS       WP_010516126              80 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Komagataeibacter].
ACCESSION   WP_010516126
VERSION     WP_010516126.1
KEYWORDS    RefSeq.
SOURCE      Komagataeibacter
  ORGANISM  Komagataeibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 80)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 80)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 80)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Komagataeibacter"
                     /db_xref="taxon:1434011"
     Protein         1..80
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8563
     Region          3..80
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mpnielqyfa qlqdevgrah errhtsapta aalydelraa ygfalapacm rvainaafap
       61 weqplgegdh vvfippvtgg
//
LOCUS       WP_010516589             798 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Croceivirga radicis].
ACCESSION   WP_010516589
VERSION     WP_010516589.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 798)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 798)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..798
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=91072
     Region          21..798
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkklrkvlws vlgllllflf avfifvntlt psyegskein glaekvtvyf dpygiphiya
       61 nneedayrsl gyvhaqdrlw qmelmrriak gelsevfgkd lvdtdkfmls lgidehtkkt
      121 vgqldinsem vrlaqayldg inqfleegpt piefyltgid krpftledvy ntvgymaftf
      181 aqahktdpll thikdklgpe ylknlpidtn tvteiiknyd idkdpvssql sgiaynalek
      241 lpvplfegsn swvlapektk ngkvifandp higfaqpsvw yeahlvtpty ekygyhlagv
      301 pfpllghdrk iaygltmfqn ddldfyyetn npenpnqykt esgwqdykti tktirvkdea
      361 dieftykvsr hgpvlngiak qiedktpvam swmytkketn evldglfgmi ksknitdfra
      421 alpkihapgl nvmygdaegn vawwataqly tmpdsvqtkf ildgtlgkae pigfiefkdn
      481 phainppwny vysannqpds vngklypgyy lpenrakriv alldnkedwt lsdtqkmild
      541 vtsslnpqii neslrfvgis nyspeqleml dllnswegdy plnsvaatff hrsvyyvlkn
      601 sfedelgpek feqflgthlm krhvatgtrf ktgiwwddvr tkdkietked ivarsladay
      661 kslvrdfgpd ytkwtwdrvh tiefehpigq vealrsffnv gpfpvegsre vinnmsfpyd
      721 stgfyrvasg pstrrvidfs dienstsilp tgqsgnplsk hykdqveqyv kgefrkmmmn
      781 qqeiesvskd vlvlepkk
//
LOCUS       WP_010517718             392 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Croceivirga radicis].
ACCESSION   WP_010517718
VERSION     WP_010517718.1
KEYWORDS    RefSeq.
SOURCE      Croceivirga radicis
  ORGANISM  Croceivirga radicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Croceivirga.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..392
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42600
     Region          1..389
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mrilvlnsgs sslkfqliql peqsvlaiga ieeigkeksi vtfssdakeg vqkemaipnf
       61 evgltvvaqw lmegtiklie qptdlfavgh rvvhggeilk ksmlatpevk aeikklfgla
      121 plhnpanlkg ievaeqifkg vkqyavfdts fyadlpakay rypvpkewyt dygvrvygfh
      181 gtshkyvank gvdflglvek ykvisihlgn gcsmaaikdg vcidttmglg plpglmmgtr
      241 sgdldpsvlf ylhekgftvs dlkesvnkks gllgiagdnd lrtvlqkrkd gdkdaalala
      301 iytyrikkyi gayiaalggi daliftagvg ensddvrwes cegldcfnin ldaelnnkrl
      361 antrniakes svpvlivptn eelaialevn tl
//
LOCUS       WP_010518124             108 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Croceivirga radicis].
ACCESSION   WP_010518124
VERSION     WP_010518124.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Croceivirga radicis"
                     /db_xref="taxon:1929488"
     Protein         1..108
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12108
     Region          1..104
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(6..7,25..26,34,37,39..40,42,45,47,55,60,67)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(25,55..56,58,84)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 meevsffdkv yevarlipyg rvtsygaiak ylgaarsarm vgwamnnshg kdvpahrvvn
       61 rvgvltgkhh fegtnlmqql lenegvkvrd nqvvdfktlf wdpmaelk
//
LOCUS       WP_010521682             203 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Aquimarina agarivorans].
ACCESSION   WP_010521682
VERSION     WP_010521682.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..203
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23213
     Region          127..188
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mphideieln nlkhklentl efneilkkhr ttlgiicgil lvlligctty fsltsitnsn
       61 leekgltlis skeyqdlidf khgvaeqkll deekkeeatn qeasnddlyd nqennakqps
      121 indeliyavq igaldekais lytdtfpqfk efhvdefyky tvgafeslee aqtfrmevva
      181 mgfedafigs ykngrririe dpf
//
LOCUS       WP_010521612             351 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Aquimarina agarivorans].
ACCESSION   WP_010521612
VERSION     WP_010521612.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 351)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..351
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38611
     Region          1..350
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 msikitglgs yipnkviane dfenhsflni dgsnfkqnnk tiikkfvait gieerryase
       61 nlntsdmayv aaqraienas cdpesidyii vshnfgdvky gdgqadmips lasrvkqklq
      121 iknpscvayd lifgcpgwve gviqanafik agiakkclvi gaeslsrvid phdrdsmiya
      181 dgagasiies tteiggiish etasftlnea nfifngksyn atadntyfik mhgrkiyefa
      241 ltnvplamkk cldeskfniq dinkilihqa nekmdeaivk rfyqlfdmet ppqimpmcin
      301 klgnssvatv ptlydlilkg nlhpheinkg dvlllasvga gmninaivyq h
//
LOCUS       WP_010524686             326 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Nesterenkonia sp. F].
ACCESSION   WP_010524686
VERSION     WP_010524686.1
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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..326
                     /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=35691
     Region          1..267
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mssrdhrldr akgilivlvv lghlltrasg wdaealravq ttiysfhmpa fvflagitak
       61 strlaerttf flvllvtaip ayygwmalld ldvgfdgvtp iwltwflmam vwwmlsvpli
      121 ernprtmltv slivglvggi ipslgdefav artltfwpff vvgklygari lswagergla
      181 graaltgaav vpvalfilgd ldrmwlfgsr siewfdvgva eglgmraava lsaalttlvl
      241 ltwtarrddv vatvgrrsla iyllhgfavr lvedplhlvs gmlpprrrwr sawcwrpasp
      301 gssrsrpstp asgttarasp ascwpr
//
LOCUS       WP_010524760             104 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Nesterenkonia sp. F].
ACCESSION   WP_010524760
VERSION     WP_010524760.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 104)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..104
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=10556
     Region          5..104
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mspgitlrff aaaaeaagve slrlpledai slpalrdelp rllaertere avaapssdap
       61 sletvlprcs flvdgvragt tegagatvlr ggetvdvlpp fagg
//
LOCUS       WP_010525382             211 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Nesterenkonia sp. F].
ACCESSION   WP_010525382
VERSION     WP_010525382.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
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   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   3  (residues 1 to 211)
  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   4  (residues 1 to 211)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 211)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 211)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Nesterenkonia sp. F"
                     /db_xref="taxon:795955"
     Protein         1..211
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=22985
     Region          23..211
                     /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"
ORIGIN      
        1 mteeqnsasa eaasdaasda eaptrrvlva edetlirldi veilsgagye vvaqaddgeq
       61 avelarehdp dlvvmdvkmp vmdgitaatt iaeeqiapvv mltafsqrdl vesareagam
      121 ayvvkpften dlipaievav arfdeirale qevaslndkf etrklvdrak sllttkmgls
      181 epeafrwiqk tsmdrrlsmr evaetvvdqm g
//
LOCUS       WP_010525462             309 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Nesterenkonia sp. F].
ACCESSION   WP_010525462
VERSION     WP_010525462.1
KEYWORDS    RefSeq.
SOURCE      Nesterenkonia sp. F
  ORGANISM  Nesterenkonia sp. F
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Nesterenkonia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   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 309)
  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   3  (residues 1 to 309)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            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="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33673
     Region          205..290
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 myalpqelag raftasaaaa hdvsrdrltr sdvvalgsgv haprafaerl ddvallraka
       61 aaliaerpda wvshvsaarl hglwlppalr ddsrlhlsrp agpdtwtrrr gvcghrmqvr
      121 dgdlvsvggv passparawl dvagrcgehq liimgdqlir tpylryegrs tpfatvpglr
      181 emlddargap grrrclaale rmrigadsvq etrlrlalvd aglpepalqv pavpgdrfsp
      241 radlgypelk iaiqyegemh fdpeqqradq rrdnvfhgeg wtvlrvnved hrdgfaaiva
      301 qvaallaar
//
LOCUS       WP_010526344             687 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Thermophagus xiamenensis].
ACCESSION   WP_010526344
VERSION     WP_010526344.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 687)
  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   3  (residues 1 to 687)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..687
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=77024
     Region          2..684
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 midkfkakfv eesldnvndl eealfalend mqskelieri framhslkgg gamfgfnhls
       61 efthhlenif dqirnnklev tndlisltfs avdeikylld kgdlteeedl eefnslmeki
      121 qaflhddgap svshktsssn avddnsdski ylisfipren llqngtnplf llddlhalgd
      181 ghsivfthkv ppfdalvpdy nycfwqiils tsepvneikd vfifvedecd lsieevgkgs
      241 fkltppiekl iesarqansl iksselkill nkvdkkednk ssqkaksgtn kqktqlkehk
      301 issirvaskk idelvnlvse lvttqaqlsv yaekkgdsdi ltlaenvqkl srqlrdnafe
      361 islipmqsel mrfqrlvrdl skelgketef vieggdield kniiehltdp llhilrncvd
      421 hgietpeerv aagkspkgni yfkayyegan vmievtddgk gidvnaikak aikrglihet
      481 deltqkeimd lvftsgfstr dtvsdvsgrg vgmdvvrkki aeirgevtid sqvgqgttit
      541 lrlpltlsii dglllkvgfn kyvvpissie kiyslakeql rdsfnrvvvi dntqipyvdl
      601 rdvfkeekqe ttniqmvlir henkrlgllv devlgehqtv vkpmgrylqr hevisgasvl
      661 gdgsialvvd tnrifqfsgg nnsgknn
//
LOCUS       WP_010527335             192 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Thermophagus xiamenensis].
ACCESSION   WP_010527335
VERSION     WP_010527335.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..192
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21743
     Region          4..157
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mnslkdlvrr nrsyrrfyqd vsipeyvleg lvdlarlsps arnaqtlkyf iscmpqtnek
       61 ifphlswagy lkdwdgpapg erpaayiiil ndttisdtyf cddgiaaqsi llgaveqglg
      121 gciigsvnrl klqkalnipe hlkiievial gkpreqvvie dmkngdykyw rdenqvhhvp
      181 krsleeiiik ck
//
LOCUS       WP_010527989             597 aa            linear   BCT 20-JAN-2025
DEFINITION  type I restriction-modification system subunit M [Thermophagus
            xiamenensis].
ACCESSION   WP_010527989
VERSION     WP_010527989.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 597)
  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   2  (residues 1 to 597)
  AUTHORS   Youell,J. and Firman,K.
  TITLE     Mechanistic insight into Type I restriction endonucleases
  JOURNAL   Front Biosci (Landmark Ed) 17 (6), 2122-2139 (2012)
   PUBMED   22652768
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 597)
  AUTHORS   Sistla,S. and Rao,D.N.
  TITLE     S-Adenosyl-L-methionine-dependent restriction enzymes
  JOURNAL   Crit Rev Biochem Mol Biol 39 (1), 1-19 (2004)
   PUBMED   15121719
REFERENCE   4  (residues 1 to 597)
  AUTHORS   Murray,N.E.
  TITLE     Type I restriction systems: sophisticated molecular machines (a
            legacy of Bertani and Weigle)
  JOURNAL   Microbiol Mol Biol Rev 64 (2), 412-434 (2000)
   PUBMED   10839821
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114514
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..597
                     /product="type I restriction-modification system subunit
                     M"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=68353
     Region          16..149
                     /region_name="HsdM_N"
                     /note="HsdM N-terminal domain; pfam12161"
                     /db_xref="CDD:463478"
     Region          162..425
                     /region_name="HsdM"
                     /note="Type I restriction-modification system, DNA
                     methylase subunit [Defense mechanisms]; COG0286"
                     /db_xref="CDD:440055"
ORIGIN      
        1 msnevnnnns kvevgfiwqi tndvlwnafk kneigdvllp fvvirrldci leavnekvrk
       61 ayndfhdkva edkldpilrk aagglkfynt skhtlislkd dpqnieinfn nylngfnpdv
      121 reildyfqfd kivarliknk llyemidaic kvnlntdkid nhgmgyifee lirisneqsn
      181 etagehftpr dvialmnaii fapekeelsq pgiirtiydp acgtggmlnl gkkyikevll
      241 adspnkptik tygqeineqs faiakseali tgedannikh gnsfsedqfv gkhfhymman
      301 ppygvswkkd qkfiqnealn pagrfyaglp rtsdgqllfv qhmiskmerd gsrigvvtng
      361 splftgdags geseirkwii endwleciia lpkdlfyntg intyiwfitn kkrpkrkgkv
      421 qlinaaahie kgtngskkve yifanpmkks lgnkrniiee qfiakiaeiy nnfeegeyck
      481 ifdndhfgyy qltieqplld engnivtnkk gepkpdpkkr dkekvpltad ieeyfekevk
      541 phvpdawidf dktrigyein ftryfykykd lessetikae iaeleqeisk llkells
//
LOCUS       WP_010528362             151 aa            linear   BCT 20-JAN-2025
DEFINITION  division/cell wall cluster transcriptional repressor MraZ
            [Thermophagus xiamenensis].
ACCESSION   WP_010528362
VERSION     WP_010528362.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Chen,S., Jancrick,J., Yokota,H., Kim,R. and Kim,S.H.
  TITLE     Crystal structure of a protein associated with cell division from
            Mycoplasma pneumoniae (GI: 13508053): a novel fold with a conserved
            sequence motif
  JOURNAL   Proteins 55 (4), 785-791 (2004)
   PUBMED   15146477
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449500
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..151
                     /product="division/cell wall cluster transcriptional
                     repressor MraZ"
                     /GO_function="GO:0000976 - transcription cis-regulatory
                     region 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=17492
     Region          4..144
                     /region_name="MraZ"
                     /note="DNA-binding transcriptional regulator and inhibitor
                     of RsmH methyltransferase activity [Translation, ribosomal
                     structure and biogenesis]; COG2001"
                     /db_xref="CDD:441604"
ORIGIN      
        1 mytfigdfec rtdakgrivf psafkkalge rdarlvvrkd lfeaclvlyp ysvweeelar
       61 irsglnpynr ehnrflrlff rgsaeivldg ngrflvpkrl meqaeigrdv vllgvdryie
      121 lwdrekyvnr satedelgdl aekilgnknn e
//
LOCUS       WP_010528524             685 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Thermophagus xiamenensis].
ACCESSION   WP_010528524
VERSION     WP_010528524.1
KEYWORDS    RefSeq.
SOURCE      Thermophagus xiamenensis
  ORGANISM  Thermophagus xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Thermophagus.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 685)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Thermophagus xiamenensis"
                     /db_xref="taxon:385682"
     Protein         1..685
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73766
     Region          4..685
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 minesllkpk sivvvgased itkpggkllk nileggyqgn lyvinprhdt vqgiasyksv
       61 adlpqipdla ilaipaqlcv svteeltqkg trafivisag fsedgpegkk leealtkain
      121 kvdgtligpn cigvltptys giftspvprl dpkgcdfvsg sgstavfile salpkgltfa
      181 slisvgnsaq lgieevlehw dhtyvpgrss dikliyvehi qnpdkllkha sslvrkgcri
      241 aaiksgitea gkratashtg amasadsave alfrkagivr cfgreelttv asvfnyprle
      301 gknlaiitha ggagvmltda lsqgglaipp iegkdrdhll sllnpgasas npidilatgt
      361 aeqlgqviey cdqkmdnihg mivifgstgl srvfdayqti hekmkqcrkp vfpilpsiss
      421 areeveffls hghinfpdev mlgralttih qtplpadeei fkegidleei rtiikaapeg
      481 fldpgtindl lqaagipvvq egvatsrkel lalarqfeyp valkvvgpvh ksdvggviln
      541 iksdehliae ykrmrkikgv ksvliqkmqt gtelfigaky eptfghvilc glggifveal
      601 gdhssglapl tfnearsmvr slksypiirg irgqegined qfveiivrls tllrfateik
      661 emdlnplign sneirvvdar mriek
//
LOCUS       WP_010529075             642 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Lentibacillus
            jeotgali].
ACCESSION   WP_010529075
VERSION     WP_010529075.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 642)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..642
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=73464
     Region          36..640
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mpmqmkpsgk pkppqldkdf ltaiqpqggi rfqdkyikkg dgyetcihvf eypssvdvlw
       61 ldkimamydv tvvtdvatmn qdetvsaink smveqdvrfr sskhesermd aqrgyqemed
      121 lyrqisemge vikllhirlf vasptiwele kkvertmskl qsfgfkgqif lnetywewqs
      181 lflpyeqqla fpnkregkgm paltlasglp yhfselndrt gsylgtsftg gnvlfdlfhk
      241 dkmrrffnav vvgkmgagks ttlkkllmdn eargnfirgf dvtgefktlv qsvnghtisl
      301 dgsdgvinpl qifrtednsn pekneeisfm qhiskvatfy mflagnpsse eieefkkvlr
      361 lfydslgftd kihttgitsl anedypifsd flrfirdqly dntekriirs elsstrvkrl
      421 ekielvidnl vnsfsylfng httipditne qviffsirnl tgleksvfna qmfnalnliw
      481 dnliqigssq kqlmyddesf dideatrflv mideahrlvn senmlavkfl tdfarearky
      541 fgglilasqs irdfvpdhsd tdtvtkirtl feltqykfvm qqdsnsldtl rtvfegqltd
      601 selehvpqlq qgecllsisg vgnlmlsiea sdeelhlfeg gl
//
LOCUS       WP_010530072             336 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Lentibacillus
            jeotgali].
ACCESSION   WP_010530072
VERSION     WP_010530072.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 336)
  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 336)
  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 336)
  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 336)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..336
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=37470
     Region          1..335
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mktkisllgv clitvmfvvg cnaetsgsek etheiimthe lpesffkhdy mkqfkdlvee
       61 rsdgrldvti hpsgqlytda eavqnlgtgs vhmvwpvsvh letlaeeygv vnlpfalkde
      121 imlndpqyrk dltnlldsfv edngikvlgl mrtaegiils nqeiskmsdl sgmkirsvgg
      181 hvandmlgaf gatatsmpat eittslsqgv idgvntspdg wanvvgsaas hgfvvpemqi
      241 ftysiatdka wfenlpedlq siiqetidel ivdqwkesie ldkqhleeit ndfgevnrvs
      301 eskldkwkeq teevrkkfee rhpeamrkfk elnegd
//
LOCUS       WP_010532021             719 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Lentibacillus jeotgali].
ACCESSION   WP_010532021
VERSION     WP_010532021.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 719)
  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 719)
  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 719)
  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 719)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..719
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..719
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=76607
     Region          1..702
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mdkdkktnve dydresnirt nypksigifi tvaggalglf hlytsyagsl vdikqrsihl
       61 yalillgfll yplmkkgnkn kipfydyiia glaagaglym lftanriies ggqinqvdly
      121 vgfavlilll eitrrvtgwg ltllalgfli ygfyvklsvy peltapvvln vsegiishli
      181 yitegilgta igvsasyiil filfgaflsk sgmgqmfndl amavaghtkg gpakvavlss
      241 gflgsingsa ianvvttgaf tiplmkkigy hknfsgaves assvggqilp pimgaaafim
      301 aenlgipytt iilagiipal lfyigillqv hirasklglk glnrnelpsv tevlkkrghl
      361 lipmvillyl lfsgktpfya afwaiiatvi itgtgrmllv saavsmflif epqvrailsg
      421 tsipgvrdnw lelglvvaip fivnlvrkka gvkaeeisvr sfvgsledgv rttipvaiac
      481 gavgiivgia sltgvaleia stivslgevi dsplvqllit lvltmvasii lgmglpsipt
      541 yiitstmaap illqlpyfre magsgetavf vahmfvfyfg ifanitppva laafagsgis
      601 ggdpmrtgfq amklaiagfi vpfmfvfshe mlmidatagn vlliattslm gvfllsvaae
      661 ghfkvplrwy lriiaivgal fliypgiwtd iagliafalv ianrftkkie qepasiaeq
//
LOCUS       WP_010532376             160 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Lentibacillus jeotgali].
ACCESSION   WP_010532376
VERSION     WP_010532376.1
KEYWORDS    RefSeq.
SOURCE      Lentibacillus jeotgali
  ORGANISM  Lentibacillus jeotgali
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lentibacillus.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Lentibacillus jeotgali"
                     /db_xref="taxon:558169"
     Protein         1..160
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17802
     Region          8..159
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfqatayssn kakdyerlik qltalseeet datailsnas allnqfldev nwvgfylwkd
       61 delvlgpfqg lpacirieyg kgvcgtaike wktqlvadvs afpghiacds asqseivvpl
      121 skdhdiygvl didspiksrf detdkiylek fareletflk
//
LOCUS       WP_010532757             113 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Brachybacterium squillarum].
ACCESSION   WP_010532757
VERSION     WP_010532757.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..113
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12121
     Region          1..84
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(24,51..52,54,76)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(24..25,33,34,36..37,39,42..43,45,51,56)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mddltvervl rtveaippgr vanygqvgav agvgarlvgr imstwgsgvp wwrvvaadgr
       61 iapplrarar ehweaegipl aphgegcair rvradpaelr eraraawadl pes
//
LOCUS       WP_010532844             386 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Brachybacterium squillarum].
ACCESSION   WP_010532844
VERSION     WP_010532844.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..386
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41945
     Region          1..276
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          272..359
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkilhtsdwh lgrtlhgael eehqaafhdw llqqvrehgv dvvvipgdvy dravppiqav
       61 rllgrtlaal aelatvvitp gnhdsadrlg fgrelmrpgi hlltdlpaid hpvsvddehg
      121 evlffglpyl dpdryrhrla adgeeplars heavtraald rvraraaehp garvvvlaht
      181 fvtggegsds erdlsvggvd svpagvlggi dylalghlhg cqdlsrtvga pawysgspla
      241 fsfsershrk avllvelgap gevtverlpa pvpraltelr gpleeilara pehgedwlka
      301 vvtdtarpah lqerlresfp qlletvyape grrpaeatpe vrreadplav mddfvqyvta
      361 aeptaaehrv lqdalgavrg rreeas
//
LOCUS       WP_010533007             274 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brachybacterium squillarum].
ACCESSION   WP_010533007
VERSION     WP_010533007.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
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   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   4  (residues 1 to 274)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..274
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=29202
     Region          1..268
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 miafesvgkt ypdgtvavad fdleiashes vvlvgtsgsg kttlmrmvnr mvdptqgrvt
       61 idgedvaatd pvalrrsvgy vmqasgllph rtvldniatv pvlrgtgkaq aheraaelme
      121 vvgleesmas rypsqlsggq qqrvgvaral aadpnillmd epfgavdpiv raelqtellr
      181 lqrelrktiv fvthdideaf lvgdrvvilk pgghiaqigt peqilaepad dfvrsfvgad
      241 raerrlhlqq vagrevvvda sgraagvleq ggtp
//
LOCUS       WP_010533455             250 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Brachybacterium
            squillarum].
ACCESSION   WP_010533455
VERSION     WP_010533455.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
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   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 250)
  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 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   5  (residues 1 to 250)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            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="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26496
     Region          153..240
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(172,191..192,211,214,222..223,232,237)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mtitldrptt arsataragg palravprsa aeegvtitlt vtlppgtgdv eaaliadelr
       61 thaqrravsr qgrtavavss pqafrattpg sarslppraq asapvsplrp rrtgvvspns
      121 parrdieaar rralaatavs paspsaagad salvidlygr rvridgadvd ftykefella
      181 hlarharstv sreqlmesvw sespaetger tvdvhvrrvr sklaryrrli stvrgagyrl
      241 dpgsdvsilg
//
LOCUS       WP_010533997             514 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Brachybacterium squillarum].
ACCESSION   WP_010533997
VERSION     WP_010533997.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium squillarum
  ORGANISM  Brachybacterium squillarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 514)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Brachybacterium squillarum"
                     /db_xref="taxon:661979"
     Protein         1..514
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=54774
     Region          15..>226
                     /region_name="YoaR"
                     /note="Vancomycin resistance protein YoaR (function
                     unknown), contains peptidoglycan-binding and VanW domains
                     [Defense mechanisms]; COG2720"
                     /db_xref="CDD:442033"
     Region          217..337
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          391..511
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(469..470,473,486..489,491)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mtnvtdpata ggpsgasrgg rrrvtlvlla ivavlavilt ggalayakqf egkalpgttv
       61 lgqdvsgqtp aqissmvaer aegvtvsvta ddevhevsla dlgasvdada taaaavered
      121 dfgavisstw sgehpvdpvv svdeqavsdf asslvpedrt dpvnasvsyd edadewsvse
      181 atpglgvdpt elvetvtaqa atlsdfsveq pieeiapait teeaeetlas iasvleqsmt
      241 vtdpegdtle isserrsswm svaesedgks lelsvdedav rewvseraak stveakdgie
      301 qvdadgevve vvaektdgle vtntdavadq liealkgtta leatfesrtv eadveqvaap
      361 eeedeateee sseeeatted eeeatptgek widvnlsdks vtayvgdtpv wgprsmvdgg
      421 egyetvtgty eiylrydmqd mtnasryded deeyyytedv pwvqyfhggy gfhgapwrss
      481 fgysgshgci nlpvsdakwl ydwagigvrv eshy
//
LOCUS       WP_010538635             281 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Bacteroides faecis].
ACCESSION   WP_010538635
VERSION     WP_010538635.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides faecis
  ORGANISM  Bacteroides faecis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Bacteroides faecis"
                     /db_xref="taxon:674529"
     Protein         1..281
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32319
     Region          5..108
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          <75..250
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 meniqviqpt kllapyikqy wflriddvkq gfqrsipagc valvfhkgnk iissfhkgtq
       61 pqsyisgqis tysdiefsfl dmviilfqpi gcriffpypm eeftnqnigi dlldntclve
      121 leekineasd nyqivrliee yllnrlceni scnanrmmat ihninegegn isvlsqtacl
      181 gykqfkrifa eyvglnpkdf iqitrfrkaf nilqptpqis iskvaydcgy ydkshlikef
      241 kmftgytpkq lleicdtyte nlsvfnsvfi ndnkelnnia l
//
LOCUS       WP_010537711             402 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Bacteroides].
ACCESSION   WP_010537711
VERSION     WP_010537711.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 402)
  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 402)
  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
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 402)
  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   5  (residues 1 to 402)
  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   6  (residues 1 to 402)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 402)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 402)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..402
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=44317
     Region          19..61
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          81..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 mnqqflkeie mgsknalvkk riithyiyng sstipdlske ldlsvptitk figemcedgy
       61 indygklets ggrhpnlygl npesgyfigv dikrfavnig linfkgdmve lkmnipykfe
      121 nsiegmnelc klilnfikkl pinkekilni nvnvsgrvnp esgysfsqfn feerpladvl
      181 seklghkvti dndtramtyg eymqgcvkge kdiifvnvsw gvgigiiidg kvytgksgfs
      241 gefghvnayd neiichcgkk gcleteasgs alhrilleri qsgessilst risgeedpit
      301 ldeiitavnk edllcieive eigqklgkqi aglinifnpe lviiggtvsl tgdyitqpik
      361 tavrkyslnl vnkdsaiits klkdkagivg acmlarsrmf es
//
LOCUS       WP_010540688             389 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Dietzia alimentaria].
ACCESSION   WP_010540688
VERSION     WP_010540688.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
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   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   4  (residues 1 to 389)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..389
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=41935
     Region          12..320
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mtnndslsgv pivlddvtki ypgqerpavd rvslelpagq ttvlvgpsgc gktttmrmin
       61 rlieptsgti tidgednrrl dadtlrrsig yaiqasglfp hmtvaqnvat vprllkwkrd
      121 girervdqml dlvgldpsdy rdrypaqlsg gqqqrvgvar alaadppvll mdepfgavdp
      181 itraslqdel lrlqselhkt ivfvthdfne avrlgdriav lgpgssvlqf dtpeavltsp
      241 adetvagfig ddaalktltl rrvgdvqlge attmtarasd dpaefasrlr gssdewavvl
      301 ddaghplrwv rgdqvaqmte lgsgdqpmns tvtvdstlqe aldgllstas attvvvnrdg
      361 syrgtlgidd lvdelrrihh rhsddeapa
//
LOCUS       WP_010540855             403 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Dietzia alimentaria].
ACCESSION   WP_010540855
VERSION     WP_010540855.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..403
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43416
     Region          4..400
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mtrvlvinsg ssslklqild taleselawa lverigdalg tvtvrrsdlp gapgdqrtve
       61 esfpdhtaal srvleltrel hvhptelgvq aighrvvhgg pafhdpvevt peveadieel
      121 ellaplhnpa nlrgirvard llpglphvav fdtgffhtlp aaahtyaidl etarkwdlrr
      181 ygfhgtshef vsrrtadvlg qpyeqlnqiv lhlgngasas aidcgravdt smgltplegl
      241 vmgtrpgdvd pgllihlird rgmtpqdvst llnrksgleg mcgardfrel ltrvddhddd
      301 ailaydvvih rlrryiggyw ailgrvdait ftagvgenva rlradalstl agwgveldad
      361 anengsgeri isspgssvkv lvvptdeela iaracddvlg lks
//
LOCUS       WP_010541099             293 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Dietzia alimentaria].
ACCESSION   WP_010541099
VERSION     WP_010541099.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..293
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31949
     Region          11..279
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mtvksphqef teaarkcsev ilrrystsfa lacrllapdt rphvaaiyaw arvgdevvdg
       61 amndpaaare liaearrrth raieqgldpd pvthafadta rrfgidarlv dpfydsmead
      121 lditehtees lrryihgsae vigemclrtf aggglgddde taagaralgs afqkvnflrd
      181 vredfmdlgr nylpgrdpra lterdvrela ddvdtdlrla rvaiasipgr drlavaaahd
      241 lfaelndrlr aagavrvsag rvrvpdpvki avigraaagr grtsqhngkv atr
//
LOCUS       WP_010541439             133 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Dietzia alimentaria].
ACCESSION   WP_010541439
VERSION     WP_010541439.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..133
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=14172
     Region          <17..125
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mdrsaagcev stgilvdpyt grlvdagvtg vrgihvdhiy plaaawdlga wrwrperraa
       61 fandvdrnll avigsvnsak gdatpedwmp pdvarhcfya aryltaaiay glpvtnadhq
      121 vlakavsrcp vgd
//
LOCUS       WP_010542389             405 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Dietzia alimentaria].
ACCESSION   WP_010542389
VERSION     WP_010542389.1
KEYWORDS    RefSeq.
SOURCE      Dietzia alimentaria
  ORGANISM  Dietzia alimentaria
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Dietzia alimentaria"
                     /db_xref="taxon:665550"
     Protein         1..405
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=45071
     Region          58..>402
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mtspdltvek ivkigelfps vitesvdadg nlvravdfdl lrqelsdhvv egpqeryqld
       61 wpgkrasafa anapiaktlr pvreesvnfd atknlfvegd nldalkllqe sylgkvkliy
      121 idppyntgnd fvysdrfast ssdylresgq hdvdgarlva npeangrfhs dwlsmmyprl
      181 rlarnllsnd gflvvsiddg evanlrslcs eifgeanfvc timwrrkret sndsknvaiq
      241 geylvvfsrs pesafflepl seayvesayr dptaqfpdgk wrgvpitvsk glrgggyeyv
      301 vtsptgnsvt rtwayppagf erlaesgriy wgmdgsavpq rvmyahesqg qpttnywhst
      361 ssnkegkkvi idlfgeavfd takplaliqr ilrlatgpdd lvvri
//
LOCUS       WP_010543625             749 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Sphingomonas elodea].
ACCESSION   WP_010543625
VERSION     WP_010543625.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 749)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..749
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=80289
     Region          42..749
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mhrisnstar rraawvltas maalmiggqa ladplsddpk pakdpavkad dgqqergeiv
       61 vtgarvidea kkkleqvagg valvdngale rqavftnadf lnlqpgvyaq tasgsdgiki
      121 sirgsavnrg anffrsgilf lfdglpvtgp ggtpyelfep lglarteilr ganafsygss
      181 tlggainyvt rtgrdapifg arveggsygy ykvqgesggv igpadyyvsi trggrdeyqt
      241 qsvgnnfgin anvgfqlapn vetrffvryr etfnetpgfl tkaeieanpr qarplntkdp
      301 sgtltaarqn trriqpgslw ianrtdvtla desalsvgfv yhdypinieg gvnqaiwgys
      361 dlsgvlryqr tdqlfgrdah ltvgglvtfh pndgyqntkv riptgatagl avgtvirray
      421 yggldgnfff eheseplanl hvllgtaair verstgvtap vipglttpfk rsdwyaapra
      481 gfrwdandki qvfgnvsrsv ephndwsnlt tppsipagyp asglaargld lndqkattye
      541 lgvrgtlpil gnltlsayra dvrdellsve vvpasattaa itaesnaspt lhqgvelglt
      601 tplwtspgnp sigatltqsy tyndfrfknd rqfgknrlpg ipehtysaql nlngpagfyg
      661 sltttvaskn wldyansvaa nsfqvfgasl gwerpggkfr ifvdfdnitd ehygavvspv
      721 ynlrgsdatn prltpgdgft viggiavrf
//
LOCUS       WP_010544213             501 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Sphingomonas elodea].
ACCESSION   WP_010544213
VERSION     WP_010544213.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..501
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=55070
     Region          3..392
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mtreadvraa agvpyrlleg vpaldggdaa agnmliqgdn ldalkallpy ykgavkciyi
       61 dppyntrsaf dhyddnlehs qwlamiyprl vllrdllaen gsiwvsiddn eghylkvvmd
      121 evfgrrnfit nviwhkmfsv knsaqyfsed hdyitvyakn adawrpnela rsekqdsmyk
      181 npdndprgpw tsgdfsarnf ygagtypvtt psgrvipgpp pgmywrfsat kleelkadnr
      241 iwwgkdgngv prlkrflsev kggrvpqtiw qhadvghtqe akkevvalns edvfgtpkpe
      301 rlmqrvlhia snpgdlvlds flgsgttaav ahkmgrrwig iemgdhaeth ckprldkvia
      361 geqggiseav gwtggggyrf yrlgapvfda dghitdgirf ttlaahvwfs etgapftgaa
      421 dtpilgvhdg maycllyngi lgdrsvsggn vltaallakl radsgwvgpm tiygewcklg
      481 aarlaeagvt fkqtpydvra r
//
LOCUS       WP_010544765             233 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Sphingomonas elodea].
ACCESSION   WP_010544765
VERSION     WP_010544765.1
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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..233
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=25752
     Region          11..158
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mtsgleilda pspnfgerls pvsmivlhyt gmesgeaala rlrdpeaqvs ahylieedgr
       61 ifrlvdegkr awhagrshwr gnddvnsasi gieivnpghe fgyrpftaeq mssliplvad
      121 ikerhgitrg nvvghsdvap arkqdpgelf nwhalarlrl alprptrnlv dpgwpdggfm
      181 lalerfgydv tdpvaavtaf qrrfrpelid geidmecrci llalllpkpq gdd
//
LOCUS       WP_010546111             395 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Sphingomonas
            elodea].
ACCESSION   WP_010546111
VERSION     WP_010546111.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas elodea
  ORGANISM  Sphingomonas elodea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 395)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 395)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Sphingomonas elodea"
                     /db_xref="taxon:179878"
     Protein         1..395
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43745
     Region          9..371
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mesavipnrh aivtykgkra gllseigpdt rfvydagwtq diactlpstt rehfwrngli
       61 pffehlgpeg wlrghqarag gtpdqddfgl llnygadcig avgilpedgt hvhpipdadp
      121 veaaatapgr tlsgvqkkwl vyrneqrfep siragdpath iakfnrvdqp tlvqnedlsl
      181 rlarevlgke evtaaaigtv rgedgvaliv erfdrlgevr lrledfaqil grprgrefdg
      241 kynasyeeaa avitrhsara lidlgrffrl vafnlvigna dahlknfsll erdgglrlsp
      301 aydllntivy phyerhtala idgekrafed lhrdlvvalg vsiglprrav dgalqqlakr
      361 fanaraldvp pyaqpndfrv ryrdvvldna erilk
//
LOCUS       WP_010551378             511 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010551378
VERSION     WP_010551378.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Magnet,S., Arbeloa,A., Mainardi,J.L., Hugonnet,J.E., Fourgeaud,M.,
            Dubost,L., Marie,A., Delfosse,V., Mayer,C., Rice,L.B. and Arthur,M.
  TITLE     Specificity of L,D-transpeptidases from gram-positive bacteria
            producing different peptidoglycan chemotypes
  JOURNAL   J Biol Chem 282 (18), 13151-13159 (2007)
   PUBMED   17311917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19799648
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..511
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=55030
     Region          6..>226
                     /region_name="YoaR"
                     /note="Vancomycin resistance protein YoaR (function
                     unknown), contains peptidoglycan-binding and VanW domains
                     [Defense mechanisms]; COG2720"
                     /db_xref="CDD:442033"
     Region          389..509
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mtnvtdtapg grsrrrvali lvaivavlav iltggalaya kqfegralpg tmvlgqdvsg
       61 ksseeiaalv tehgesvkvs vtagdqqlev pladlgvsvd saataaaale rddslpavis
      121 stwsgehsve pvvevdeaav aefanglvpe dmttpvdaqv vfdeeaqawn vepgrngqgv
      181 dpqtlveavk tkapalesfs veqpieeiap aitteeaeev vgtisslleq pmsisgadge
      241 thevsaerrs dwisvtpdes genltiavde davrewvatr adkdavepen gieqvdeage
      301 vvkvvsekkd gleitntdav adelitalkg ttpleaafet kkleaevdkv dapkdeeekd
      361 eekssddekk deetkdeepa aeptgekwid vdltnktvta yvgdtpvwgp rsmvdgkegn
      421 etptgtyeiy lrydrqdmtn aayydeghpk yyytpdvpwv qyfhhgygfh gapwrssfgy
      481 sgshgcinlp vsdakwlydw asmgtktvvh r
//
LOCUS       WP_010551148             363 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Brachybacterium
            paraconglomeratum].
ACCESSION   WP_010551148
VERSION     WP_010551148.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium paraconglomeratum
  ORGANISM  Brachybacterium paraconglomeratum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 363)
  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 363)
  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
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 363)
  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   5  (residues 1 to 363)
  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   6  (residues 1 to 363)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 363)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 363)
  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 15726307
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Brachybacterium paraconglomeratum"
                     /db_xref="taxon:173362"
     Protein         1..363
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38597
     Region          1..>135
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
     Region          77..>280
                     /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 mrpttpldrm agahdaavla varrgdpvsr sglaqelqvt pqaiskilar lmerglveea
       61 gtvtsgpgkp ttlyeivpgs rraiglhltr srlhsvvvdl tgeilerrel eigrlqpvpe
      121 lvatladetr alqdvgpgil lgvgvgmpgp vdgeegvyrg tsdpdpwrga pirrllaeel
      181 gmpvlldhds raalvgeaws qpgllrnaal llvedglgaa lclddqivrg ahshageigh
      241 tvvrmdgipc pcgrrgcaqr ehraalerge delaarilae vvvnlvrlvd vdrvvlggrt
      301 vheqheasmd airealtagl sdepwvhvev mlstrgtdli avgaacevle heyglpqvlv
      361 gpe
//
LOCUS       WP_010553673             647 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Pseudoalteromonas arctica].
ACCESSION   WP_010553673
VERSION     WP_010553673.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 647)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..647
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=72898
     Region          116..644
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 magfkklifi qiiswllcva agsyfisisf dtavsdaqks aqitvtkyin dlslddisaq
       61 nlkqsiadgn tfssftlrdy qgaeifsinp ptqlpmfadf vlsnfnsvrp qfavndasdi
      121 kvefvlnieh lasqlqtslf ivilisailv iipiilmqsi fyrlnknist tvadiidiyi
      181 nqnqvdndle taldstrlkk lgkdlvpsfn rlshflksks ediqsaalsi kheaykdvit
      241 slgnrnmfve yyekniente qstfgslamv rcselqainq srgyqkgdey vkgvadiikh
      301 isgtytdsqv frlnssdfav vlphtplkea erfgenlqsr ftqyqqnqel ssvantgivg
      361 yekgkplgel lsvvdnamsm aqskqvnawh vqretdlvnn vsagfgnqnw rkvinevies
      421 krvhlvmqni mplgksikay aeiqvrfkte dnqvlptasf lamaeklgma ieidrliids
      481 slekvksrnl sekffglnvt assahndqfv iwlerrllkd thiasklvfe vsefglqqni
      541 kaskrfidmv hrvgarvtve rfgvgltsfk ffrdlkpdfi kmdasytrgl eddknnqyfm
      601 rlmvdlahri gvsvfaegve sqeekhiiet lcldgvqgyy iekpkdi
//
LOCUS       WP_010552141             272 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator
            [Brachybacterium].
ACCESSION   WP_010552141
VERSION     WP_010552141.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 272)
  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 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   3  (residues 1 to 272)
  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   4  (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
REFERENCE   5  (residues 1 to 272)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     Protein         1..272
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29671
     Region          24..270
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          190..268
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 masrasddie rahlrdpadr sftihrrlpp aslrpwlrry wipvwdvpeg eraeqrvlqf
       61 pvclmittpa ysrfvgpnpg lsttvlegcs wgfgvmfapa agavlhgggl relagghrel
      121 egvaalaglt aplrelmaqg pdedevhaac calveeriag lgppreedll idaiveeven
      181 dpalcevgql csrfglgera lqrltgrrlg ltpawlirrr rlheaadglr gdedlaalaa
      241 rlgyadqshf thdvrtatgs tpgelarrwr eg
//
LOCUS       WP_010553781             587 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Pseudoalteromonas arctica].
ACCESSION   WP_010553781
VERSION     WP_010553781.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 587)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..587
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=67334
     Region          <298..578
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mfklslslvl mqilnntlvn nltseyamqq sklwflkqfk giyftfiacv llsfnfllnd
       61 alhqkihasg qqlvkqvhel nlaplinnev llalaksegf mleaqpsssh fmhlvsvere
      121 vfsyktlsls lyhypawvmq sylflllnli iigtagwsfr wwsllkisre tintptvstk
      181 kakqkqqktm fikqvkncel sslygvnpat hhlfllvscs cnfdqnidiq asfnvlvakt
      241 fselrgrsvn vvdsnylait lrgvpvteld cyvarlhkcv fvlcqnnqkg itrknikiga
      301 cdyklgadei mvnqfarsal tlsqssllqh chrlplhhsq eralsseqvi enieknkfil
      361 ffqplfelss gdilqhevli rvrhskhgll aaryfinqiy sdqdtlildk avinqvkrli
      421 qsessaltvs vnlhpnswfn defwhwlsgq ltqlkfnakl qfeireedff tqrkkitnal
      481 niikknrsqv iidnvqnsek italinhnev calklsyelv rlvheknhnq iqikkiveaa
      541 kllnlpvyav gvetqkelfm leklgivgaq gfyfseplqe ftktvfh
//
LOCUS       WP_010554538             157 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: pilin [Pseudoalteromonas].
ACCESSION   WP_010554538
VERSION     WP_010554538.1
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 11471942
            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="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=16699
     Region          1..133
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mrtkgftlie lmvvvsiigi laavalpqys kyiqraelvd plamaaaire dvtvyylenr
       61 rfpasneqag vpaskflign rvtgitvdng aihislgnka sqllqntvlt frpavvtgsp
      121 tspiawlcgf depvtgmqav genkttvpke ilpsaci
//
LOCUS       WP_010554635             219 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Pseudoalteromonas arctica].
ACCESSION   WP_010554635
VERSION     WP_010554635.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas arctica
  ORGANISM  Pseudoalteromonas arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 219)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Pseudoalteromonas arctica"
                     /db_xref="taxon:394751"
     Protein         1..219
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=24170
     Region          79..214
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 missylkqaq lsanpalist elekldlhla ntalpdvcwe yqipelgegg acslfgylqd
       61 epfkltdyik ndeqtqfkla tlqsivsyie qqtgvdwygi yqstntpegn qllklayhga
      121 psrplfpltq afaagsnnvq valshkgrii nnveaylsqg geyytcdpkv ksetclplfn
      181 aqnecvgivd aeafkndffd ektlavliac cikithflv
//
LOCUS       WP_010555294             290 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Pseudoalteromonas].
ACCESSION   WP_010555294
VERSION     WP_010555294.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            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="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32372
     Region          16..258
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mfdpsvtife stqnqlgesp lwhpilntff wvdinkklll sknthnesql kivnmpdtls
       61 aiawideqhl llctstglyk yhinsntrhl ilnientlln rrsndgradp wggfwfstmh
      121 vnakkgdgki yryykrqlka vvsdlsipng lcfdkarlcg yycdsltsci yvldldeqtg
      181 epcseprvfy qfnntdvdpd gcvtdqlgnl wlavwgmgcv mclspggeli ktiklcaikp
      241 tctafggena elllvtsafd eainntvteq gavfqisgik ngqfeppvll
//
LOCUS       WP_010555347             258 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_010555347
VERSION     WP_010555347.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 258)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..258
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=29179
     Region          25..242
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 msekskdcek vtcsncadan dlefdfsmaf qpiincktnl iygyealvrg lngesaysii
       61 skvnednrya fdqlcrikai qlasklgits mlsinflpna iykpercirt tleaakkynf
      121 piqnimfeft evekiedtah ikrivdyyqs lgfktatddf gagysglnll adfqtdiikl
      181 dmalirdisn dkkrqlivth clnmfrdlni tplaegietv qeytwlknag velmqgylfa
      241 kpsfenlpev nfedigad
//
LOCUS       WP_010555572             741 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Pseudoalteromonas marina].
ACCESSION   WP_010555572
VERSION     WP_010555572.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 741)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..741
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=81498
     Region          16..663
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mtinllkkit skhfyigvli tlliasieff stgavaklln rvegiiydsr lqltladtpr
       61 kvnesvviid ideksmqeqg rfpwsrskva dlvtkltdag viviafdiff sepevnpvtk
      121 imdelpdfsa kyasplstik qqvdadtkla kalaknditl gfllindels ehnapakssv
      181 iwqegehtns qindypgaii nipklqnaaa ghgfinahsd edgfirkaal vnrvgntlyp
      241 slaleaarly tlantietrs ttsngitlfe gvkfhnkwiq tdeygqilip ykggarsfay
      301 ysatdvltqk vglkelegsv afigtsavgl adlrstpvgl qypgvevhan ifeglmnpql
      361 lpskpswslg aslviiiitg lalsffsigk tarfilafsi ivasvnvain fymwsaqkvn
      421 lplfmtlllt tllasyyiiv gsiaemkhsk kiktmfdqyv pperinqlie qggnlvqnse
      481 rrnmtvlfad irgftslses msahqlseyl nqylsaitki ifdntgtidk yvgdmvmafw
      541 naplldkdha qhgveaalam teglaeintl fakqnlpais igvglssgdm nvgdmgsmyr
      601 kaytvlgdav nlgarveslt kfygvailvt edtmqacsgi sfrlidkvqv vgkttsvaly
      661 epinytnkls kiqlneidns lkaitlfhnk ewesalslfk qlksnavlna dvyriyieri
      721 qstdiqtlak dwngafvhtk k
//
LOCUS       WP_010556179            2103 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Pseudoalteromonas marina].
ACCESSION   WP_010556179
VERSION     WP_010556179.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 2103)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 2103)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 2103)
  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 2103)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..2103
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..2103
                     /product="M4 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=230474
     Region          1..566
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
     Region          744..>862
                     /region_name="gliding_CglD"
                     /note="adventurous gliding motility lipoprotein CglD;
                     NF033765"
                     /db_xref="CDD:468178"
     Region          <1855..2075
                     /region_name="myxo_dep_M36"
                     /note="myxosortase-dependent M36 family metallopeptidase;
                     NF038112"
                     /db_xref="CDD:468355"
ORIGIN      
        1 myktlssgli afcflntlss qaavslrink sstqevkqll nqnasiannp sassyfvele
       61 qpqlslsqqv nasskkmqqy fsgvpvwgqq irvqsnsehi sgffakninf tslnktastt
      121 fdqskavksl ltksklddsl eseiinnkry iyihdgkayy vrlielkvte ngiekmpigl
      181 isestyqife lwdniqsvdg tgpggnqkig qyeygtdkda fnvtqvgetc flendkvktv
      241 tmesgsepse afsftcdrnt hkeingafsp lndahafgta vfdmyqqwyn tapltfqllm
      301 rvhsgdnwen atwngqamtf gdgadrfypl vsldivshev shgftsqnsn liysnqsggi
      361 nesfsdmage taeyflrget dwlsgadisk vdpalryfet psldgvsidk asdfypgmdv
      421 hfssgvfnra ffllsntegw dpqkafeiml kanqnywvns sgfidgacga insaidlnyn
      481 asdvisafne vevicdnikf vdtdsdlmdd ywellygldp sdaddanldl dqdglsnlee
      541 ylantlpnsv dtdadslsdy delnvymtmp nnadsdsdrm pdgwevtfaf npldaadael
      601 dfdadswanl ieyygnsdpt dpnsepsvfp ettynfddai vpeflvssnp qapwfitdyd
      661 ghdslvlsss ditdsqqtst efqflsdehr fvnfnyllet etnydffkvy indtlvldes
      721 gltdwkvasf pvpagfntvk fvytkdftvs egldavfidn lyigpnfpds dgdgmsdmwe
      781 lsygldintd dsaldldndg lsnlleflnn glpnnsdtdg dlmpdgweyn nslnltdaad
      841 asqdtdndgf tnlteyqant dpqsdasypv alnittsfes dtlptwmies vdssapwfit
      901 ndfatqgsqs irsgdisdsq fsgftvtglf eegvlafdyk idsesccdff mvtidgqevi
      961 gfaergdlea peptsflvni segvhkiefk ytkdgsvstd adavwldnfa mlpvgdqtdt
     1021 dndqmpdywe llnglnrfda sdaqsdndvd slsaldeynl gtnpnsadtd sdelsdgyev
     1081 nngllpldps dasldfdadg ytniqefygq svandatstv qsfsqlnesf eegllpamft
     1141 elaehttqwq lntnwstdgt sslslntspa gsisgfaiag lfeagfinld yfsnsnssfq
     1201 isvngtqyni khyrsrllip vndgfnivki kyespylagm pfsvdniswt aeldvvsdfd
     1261 gdgipdywea qnglnaldsy dasndpdydg lsnlneyqms snplstdtdg dgvldsedsh
     1321 ptdsslgeni apvfvsslep itleatsqnt nvinvfvpea tdnghlepyv yaasgsylpl
     1381 gehqitwvar dfvgnettai qtvtlvdttp pviqdyysvd vygssidhik aalfnsnaiy
     1441 dsvsdvaiid idsnfvfrtg dilipvsavd gagntstgev narvfpkvsi qpttyvyqdg
     1501 navidlfisg kspygsvsfd lignntskyi stnlhglvkv elereffena snirintrss
     1561 sftdrndtsq lvflnetakp efitnlyqdg kvisnvvqrd ssdfivdvha vnlpsaaadn
     1621 sielqlssqg dyfvnkighs kwnitftpql ltdsdnldia ftikqnseav atdkislrvi
     1681 davtfndpel dtdgdgipda eegvsdgdkd givdyldsss ithsavldsg dmvrsidefn
     1741 hlsvgnikqa tvtqmiadms ileqdlstyf dslditephf qaksdivnih itlsnssgta
     1801 eiaipeyvns ilssemqirl lsntgwqsva kltgnvyeqi csgcftfavt dgsefdldge
     1861 vngvielvak laeeslnqap vldvtipati eelsttelda sgttdpdgdl lsfewsidhp
     1921 qlslapletd skasltvgel eetfttditl lisdgyeqft evftvtfmhv nqlpavdlss
     1981 sslsvdegkd vsvtatatdk esseltyswv qtqgievaie dansntlsft apsvsvtsel
     2041 gfklsvsdge geteqsvivt vndvpvalpt pkegdksggg slsffllllt alfvyrraql
     2101 fhk
//
LOCUS       WP_010556413             152 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_010556413
VERSION     WP_010556413.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..152
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16159
     Region          1..152
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mqkhdfyqsl vkqtesliag esnvianman isallftsld dvnwagfyfi dspselvlgp
       61 fqgnpaciri pvgkgvcgta aatlqtqlie dvhafdghia cdaasnseiv vpimkhgkif
      121 avldidspsi srfdtddkag lealvkcfea sl
//
LOCUS       WP_010556787             290 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Pseudoalteromonas
            marina].
ACCESSION   WP_010556787
VERSION     WP_010556787.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            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="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32305
     Region          16..258
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 msdfkitlfn ntqnqlgesp lwhpmletlf wvdinkkllf ccslgkpana ysvempfivt
       61 aiawqdkehl ilgtesgiyr ynikrkipql itelesgdtn rrsndgradp wggfwlstmd
      121 mtaekgqgki yryynkkldc ivtdltipng lcfdkarsrg yycdsftsci yfldldvntg
      181 evagtakvfy qfnntdvdpd gcvidsignl wlavwgmgci mclspdaevi htikvnnlnp
      241 tctafggkqg ellfvtsavc esnkdlqniq gttiqisgik ngqleppvil
//
LOCUS       WP_010557758             695 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Pseudoalteromonas marina].
ACCESSION   WP_010557758
VERSION     WP_010557758.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 695)
  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   3  (residues 1 to 695)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..695
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76583
     Region          20..683
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msidlsqffe vffeesfegl dtmeaellnl vpgeedleti ntifraahsi kggsgtfgfs
       61 svsdfthvle tlldqirqge rtlttehvnl llkavdclrs llaglqaeqe pdlteadtlr
      121 aqfeevlgin sttqesniqt sdsqsdsdty qidfkphhhl fktgneplim iseleqlgel
      181 dttvfydevp eitnlssdec flhwrfflnt shgesaikev fewveddadi tielcgglft
      241 delptpdtds stvnqepsiq epvpkqaeqa kpikptsant nkksttpest sirvgidkvd
      301 slinmvgelv itqamlnqls eqditpatit alqeglaqla hntrdlqenv mrirmlpinf
      361 vfsrfprlvr diaqklnkqv elkligeqte ldktvmekis dpmvhlvrns ldhgletvek
      421 rlqagkdpvg tvtlnafhqg gnivieimdd gqglntkkiq ekaianglis adnhlsneei
      481 nelifmpgfs tmdevsdlsg rgvgmdvvkr niqslngsve vtsapgvgst ftirlpltla
      541 ildgqlvkva qhtyiiplis iveslqidia kvsrvgknld vlrlrdeyip ilrlydifnh
      601 dnaiesldkt llvvvetdnq kvgllvddll sqqqvviksl eanyqkvdgi sgatilgdgr
      661 vslivdisgl iklsglkkpg sqelsiesqa aleas
//
LOCUS       WP_010557979             553 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Pseudoalteromonas marina].
ACCESSION   WP_010557979
VERSION     WP_010557979.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas marina
  ORGANISM  Pseudoalteromonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 553)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Pseudoalteromonas marina"
                     /db_xref="taxon:267375"
     Protein         1..553
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=61632
     Region          <145..546
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mamittlfsv kntnikfsyl ctgvvglail stgeawlsil lafgfcfhlw qsfernnwsm
       61 iitssaagll fvvlfsahll ldvplfwvvl aillcavvgl lndesdepkv smapkqvdda
      121 fveesplsvf askkelrqgy yvwcddtqve avliiirleg feqvnqhigr gfgdillaqs
      181 anriqeqles eevitlvgne klahlgglnf aficslanhk hlheqiidti lgatlkpfnv
      241 anctvevkar asyvacneqd tnfddlisya ylaldsqptq kvvpyhqqmm ieqleqqarl
      301 kelanidfas elelyfqpvi cnkngqiefl elllrwqhpk qgilsanrfi ddiriaglgy
      361 plakfviera aelamalrie giaiplsinv fgpemlneef vefvdnvite hnlqmgdliv
      421 ecplhiftgl ddkgramiar lnniglklcv dglgdnpvll sklpslavey ikvapsltad
      481 fsnqnnirsl vggmvemhnq qktkvifegv etleqlkfvk slnayaaqgy yfghplssig
      541 lmswlkewqq aqg
//
LOCUS       WP_010558580             368 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_010558580
VERSION     WP_010558580.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 368)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..368
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=41370
     Region          <112..346
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mfcadcerid nylfpettfw lflptfesvn kaivfcgngd ypatqvdshc irvkvtkrqv
       61 nrfllglfge fepnelnask itttdgreps fadigrlvpa svlinrlnse wiinaiegdn
      121 yethfqpife ldkhgevtpf ayeglfrird efnnivppah afklaegsdl lfsldlvarr
      181 savghfkksg lngklfinfn pssiydpsyc lratasainv lgiqpqdvvf eitettsatd
      241 esvmrgilnf yrnagfgval ddigsgwsgl nmlhkyrpdy vkidmdlvrg lhedpykqti
      301 vkhliqiahd ngskviaegi ehqqelailr eykadyyqgf llgkpmlqqs kltveaqtqi
      361 dntlkgin
//
LOCUS       WP_010559216             101 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Pseudoalteromonas spongiae].
ACCESSION   WP_010559216
VERSION     WP_010559216.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..101
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11087
     Region          1..101
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(25,56..57,59,85)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(25..26,34,37,39..40,42,45..46,48,56,61,67)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mtqeekvqai llvvgsipsg kvctygkvae maslngharl vgtvmkklpt gsripwfrvi
       61 nsqgkisfpe nsekfhqqks lleqegivfk gtkvnlkvcm w
//
LOCUS       WP_010558828             397 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_010558828
VERSION     WP_010558828.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 397)
  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 397)
  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
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 397)
  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   5  (residues 1 to 397)
  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   6  (residues 1 to 397)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 397)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 397)
  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 20282815
            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="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43329
     Region          16..>57
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          77..332
                     /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 mkgsnakqnk alnlrlalsq ivalgpisrv eiarntnltk qtitnmvetl lehdlvsevg
       61 ikkaegagkp skmlcfneka aysiairime nelfvgmfkl ngdcinsltt lfspnelvsk
      121 atylvntlvn ienidsskvl avglamqdsn nfaldahkva ketqvalaes lnlpvalest
      181 asacaayqml fgeaqtlqsf vyvhignrve ssvvynrdil lgqngltgal gdifvtpetd
      241 ndtgelgrln dfsslnslka alnidnqkhd dflanltadn klleswvnra eepmriaiht
      301 iesifnsqti ilggdinewl ldtlikqlrp yipsiaqyge rqvirliktp evsqitqkgi
      361 atlplyaalg fenhhilycp talqatplqa liyalda
//
LOCUS       WP_010559479             374 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Pseudoalteromonas
            spongiae].
ACCESSION   WP_010559479
VERSION     WP_010559479.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 374)
  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 374)
  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 374)
  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 374)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..374
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=41531
     Region          48..335
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mpisrryfik sssalvassl fqvgylnaat tlpnaddlaq dneikqrseh tlvfaspyht
       61 sdasfvphlh iefkrniqsl sqgkiyvdiq gqgamgigtd lmaavsrgri daalisvanl
      121 sralplldil nipfwagddq allnlisspy wqqnviekia kqgklailyh yitggrtlst
      181 tkrtntvikv ptdlknkvlr ipaskvlkhf ysmtdahive vnwanvaama rvgkfhvldp
      241 givglyagpn nlrdeiatit qlnsvpdtwv nvvsqkwlnt lprtlrlavn daaektflsq
      301 lsnvshiesn ceqefikrgc tvfkpdqpti alwqdqfghh rhewrdikks llgssnefsr
      361 lldatktpsk hslt
//
LOCUS       WP_010559963             108 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_010559963
VERSION     WP_010559963.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (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   3  (residues 1 to 108)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..108
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12051
     Region          2..108
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mqellvdfed trelyksymp ylktgglfvr tnmqfemsqp lalrislpda leedvitgev
       61 vwitpqgsqn snppgvgvsf iddksqvrdk iekmlggmln ssdptytm
//
LOCUS       WP_010560009             151 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_010560009
VERSION     WP_010560009.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 151)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            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="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16314
     Region          1..151
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mnkeslyqsl nnqvvalied etnlianlan vsallnlsle dinwvgfyll endtlvlgpf
       61 qgnpacvrip vgkgvcgtaf aekqtqridn vhdfeghiac daasnseivi plikdgnyig
      121 vldidspsls rfdsddqtgl erimaslaeh l
//
LOCUS       WP_010560668             106 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Pseudoalteromonas].
ACCESSION   WP_010560668
VERSION     WP_010560668.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 106)
  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   2  (residues 1 to 106)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            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="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11391
     Region          38..105
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkllslpvlg alllgitsit fsvnaesqat kptksnveev vklelvnvnt anaeqlatlp
       61 gigesralri inyreqngki ksleelneik gfgersiakl kgrvtf
//
LOCUS       WP_010560566             737 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Pseudoalteromonas spongiae].
ACCESSION   WP_010560566
VERSION     WP_010560566.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 737)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 737)
  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   3  (residues 1 to 737)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..737
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=78341
     Region          6..734
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msfdvdedil qdflveagei lellseqlve lennpedadl lnaifrgfht vkggagflsm
       61 telvdachga enifdvlrqg qrrvtpelmd vilqaldtin emfahiqnra qpdpadpqll
      121 aelhrlsqpe sadeapvaea paeeivepea veedpfvdil fdadapsdea qssgdsvddi
      181 teeefeslld elhgsgngpa snaapeases sdsdeitdde feslldelhg agsfggaset
      241 sapesaapaa ssgddedite defealldel hgkgsapsta eksfnteava akpatptppp
      301 aakptpakpq asapkpvadk paapsaakpa aapskapakp aappaettvr vdtkrldqim
      361 nmvgelvlvr nrlvslganv snesmgkais nldvvtadlq gavmktrmqp ikkvfgrfpr
      421 vvrdlarslk keinlqlvge etdldknlve aladplvhlv rnsvdhgiem pddreaagkp
      481 rtgtvtlsas qegdhillti eddgagmdae klksiaigkg vidadqaarl snneaynlif
      541 apgfstkeei sdisgrgvgm dvvktkitql ngtvniesek gkgtvleikv pltlailptl
      601 mvvvgqqtfa lplagvseif hldltktnlv dgqltiivrd kaiplfylek wllrnprseq
      661 krsqghvviv qlgtqqmgfv vdsligqeev vikpldallq gtpgmagati tsdggialil
      721 dvpsllkhya gqgrnkk
//
LOCUS       WP_010561506             698 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Pseudoalteromonas spongiae].
ACCESSION   WP_010561506
VERSION     WP_010561506.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas spongiae
  ORGANISM  Pseudoalteromonas spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 698)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 698)
  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   3  (residues 1 to 698)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..698
                     /organism="Pseudoalteromonas spongiae"
                     /db_xref="taxon:298657"
     Protein         1..698
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76051
     Region          3..684
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msidlsqffe vffeeslegl dvmesellnl tpgdvdneti ntifraahsi kggsgtfgft
       61 hvsdfthvle tlldqiregs relaaehvnl llqsvdclre mlgdlqnnqe tdlttatqlk
      121 ekfeailage sqpastpvat nsssdnppve hgaldtyevi fkpqhhlfkt gnepiyliee
      181 laelgqldvt anlddvpdih nlaadecflt wcfyletdkg eeaikevfew veddaeitit
      241 lcgglfgddp iesepegvse qateeastpt aesksdkpap aakaaaksgs testsirvsi
      301 dkvdslinmv gelvitqaml tqlgegeite nklmalqegl aqlahntrdl qesvmrirml
      361 pisfvfsrfp rlvrdtsqkl gkevelkllg eqteldktvm ekisdpmvhl vrnsldhgle
      421 tpeqreeagk prvgtvtlna fhqggnivie imddgaglnt qkikqkaiqn glisdsddls
      481 ddeinelifm pgfstadevs disgrgvgmd vvrrniqsln gsievtseqg igstftirlp
      541 ltlaildgql vtvaqhtyii plisiveslq idlkmvncvg gglnvlrlrd eyipilrlhk
      601 ifnhsgaied ldkgllvive sdnqkvgllv ddllaqqqvv iksleanyqk vegvsgatil
      661 gdgrvsliid itgliklagl kkagtselai epieseea
//
LOCUS       WP_010561916             624 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_010561916
VERSION     WP_010561916.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 624)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 624)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 624)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..624
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..624
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=70953
     Region          138..610
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 myysnqgirw lffagvlfla slggyvyyvy shtyndilkd vdakllnaaq svkfilgdey
       61 hdnitdpdhi deksyllksk qlsefaskle leyvyamike gdqvyfsass ytnediknnk
      121 ltyfydlype atqlnvkafy steplfehse dqwghfrtif lpfqakdgrt yltgaditik
      181 dlneqlaasv tqavitasff ffiatlvgsa yiyllkqnlt rdpvtgyanh ialerklqsh
      241 splhmqlaiv lisnleding fygshigdev mqkllarlnk lkstechlyr lssnkialls
      301 pnldsnaclk lvenlnknap llydpfiyvt lcagiatgnk tllienaria veqakrsrel
      361 vvfysdamni iknqyqhnlk iakdvreafk ngqveahfqp iltidgnetl kyeglariki
      421 ndalyepdyf lsvvnrsrmd gqltrmvfld cvkrfrqtnl cwsmnltaqd mldpslaqfl
      481 ddelkryptp hhisfeliet eaianlteik gfvemvrrhg akvfiddfgt gysnisnilk
      541 levdglkidr slvsqitkdd evflfiqhia nfakevnltl iaegvenklv adklakagik
      601 yvqgfyyakp arelahisqt akas
//
LOCUS       WP_010562243             764 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: penicillin acylase family protein
            [Pseudoalteromonas].
ACCESSION   WP_010562243
VERSION     WP_010562243.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..764
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=85466
     Region          6..754
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mtkiikwlsl fliiaalvat atvygiltls lpelsgktqv sdisnntsle rdalghavvn
       61 aksrkdaaft lgyahgqdrf fqmdllrrna agelselfgk aavgldkkmr fhqfrkrske
      121 ilkslpteht eilkryaqgv nlaqshtpys sfeylltgas rkpwlpedsl lvifsmyldl
      181 qsktfnrdlt ltyiaeqfgs emvgfltqps qyqaaldgse felveyaips inkslftnvt
      241 heihepkdig snnwavtgrl tesgnallad dmhlglavpi iwyrtqlnyv endknyqitg
      301 vslpgapavv vgtnghvawg ftnayidtad wialdetqet ktiherivtp dkeymyslek
      361 sefgpvkhia gkkyalkwva hqdyavdmel mnleratnve ealsiaktig ipvqnmlvtd
      421 slgnaawqat gaiparttpt eiaikpevfd tnwqydavdv pfmvnpennr lwsgnsrvvs
      481 veqdkrygng gyalgarakq iqqrlfekeq fsehdfyqiq ldnqaiflkp wqalllkvln
      541 lspekyaqdi klvenwgeca cadsvgytlv rryrsalink lfspietqlr aegltlapik
      601 ndlepaawql insftdqwlp psvaswpell sttyinmksd llnkhtgsds gslnqltwga
      661 vnelniqhpf seqipllskl ldmpktpafg dsfmpavqgt sfgasqrlfv qpgleqkail
      721 tlpggqsghp lspyyragyn dyieqkntpl lpgeivhrid fekr
//
LOCUS       WP_010562920             186 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Pseudomonas].
ACCESSION   WP_010562920
VERSION     WP_010562920.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            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="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20099
     Region          3..181
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mnlnkaisgr rstrdytaap vdekvilrli daatqapsam nqqpwtftvi rdqalleris
       61 reakacmlat tpvgshsshf qsllsddsfq ifyhapvlvl isgnassqwm vedcalaaqn
      121 lmlaayaegl gtcwigfaqg flntpqgkhm lglpaewmpv apiivghpls tpvpvahkap
      181 eihwig
//
LOCUS       WP_010563352             378 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Pseudomonas].
ACCESSION   WP_010563352
VERSION     WP_010563352.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 378)
  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 378)
  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   3  (residues 1 to 378)
  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   4  (residues 1 to 378)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 378)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 378)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..378
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39932
     Region          30..365
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(104..106,127..128,177,229,254)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 msqtfykkgf lalavaaalg vsafvqadvk igvagpmtga naafgeqymk gaqaaadvin
       61 kaggingeki vlvagddace pkqavavanr ladqdkvigv vghfcssnti pasevydeag
      121 iiaitpgstn pqvterglga mfrmcgrddq qgivagdyiv dvlkgkkvav indkdtygkg
      181 ladatsaqlk krgvtpvlee gltrgekdfs alvtkirslg advvyfgglh peagplvrqi
      241 reagmkdvkf msddgvvtde laktaggnqy vdgvymtfga dprllpdska vvdafrkagy
      301 epegytlyay asvqalaagf ngaksnkged aakwlkahpv qtvmgkkewd gkgdlkisdy
      361 vvyqwdkdgk yhqlekqk
//
LOCUS       WP_010563553             813 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pseudomonas extremaustralis].
ACCESSION   WP_010563553
VERSION     WP_010563553.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 813)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 813)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 813)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..813
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..813
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=88288
     Region          39..813
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 maspalshfl prfgvaaava salslagcql qstqdtllpv agvqpikgla qnvsirrnaq
       61 gmpliesntf hdalfslgyv hasdritqmv tlrllaqgrl aemsgpdvld vdrfmravnl
      121 kksagelyna ssprlkrffe vyargvnayl fryrdklppd lartgykpey wkpedsallf
      181 cllnfsesan lqeelaslvl aqkvgvdkla wltpsapdep ipqaeadklk gvnlgqitgl
      241 agldaasqql sslnslavtt ssnwaigpqr srsgksllan dlaaqpqaps pwsyvqirap
      301 kyqavgasia glptllsgfn gkvawsmsav kgdtqdlfle kvkrqgnaly yenngkwlpa
      361 gvrnetffvk gqrsirevvy etrhgallns sqalttglgl alqtadfkdd ksldaffdls
      421 raqsvakasd atreiraial nmvfadatni gwqvtgrfpn rregegllps pgwdtrfdwd
      481 gyadamlhpy dqdpaqgwig tanqrtaprg ygmqlsnswd aperserlaq lanagkhdsr
      541 sviamqydqt ttfaaklktm fkapgmaqpl kqaidalpta eqakarealn rlmafdgrlv
      601 atsadaalye lflqestrqi fldelgpens aswkafvsna glsyaaqadh llgredspfw
      661 ddvrtaqked kpailarsla aaisagdsql gadhkawqwg klhsttwknt qgqairgpla
      721 sggdhntlnp apyswgrdfn ttqvpalrmi idfgqpepmm gqggigqsgn paspnyangi
      781 dpslkaqyls fpmqpqnfdk vygkarltlt pgk
//
LOCUS       WP_010564564             237 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Pseudomonas].
ACCESSION   WP_010564564
VERSION     WP_010564564.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 237)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..237
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=26171
     Region          41..208
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mlnficrfgv iavslaalsp valaadgqsp slysslarqa pelnptvlks alnavqcavn
       61 ngeerserla vidytqpsta rrlwifdlrk ktlvlrdlva hgaksgenfa tqfsnregsh
      121 qsslglfrtq esylgthgys lrmdglepgf ndqardralv ihaadyvnpl wskregrigr
      181 sqgcpavrpq varqvvdklk dgqfmfswyp dqrwlkssty lnckpqqvas srtirgg
//
LOCUS       WP_010564792             833 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas extremaustralis].
ACCESSION   WP_010564792
VERSION     WP_010564792.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 833)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 833)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 833)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..833
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..833
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90695
     Region          62..112
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          89..833
                     /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 msrlarplhp lalsvamafa avpllnvqta faedsssalr rfqipagdln qalnslaeqa
       61 glvlafdasl trgkhsngvs gqyatdvalt qllagsglqa lkisaeryrl eaipeqgaam
      121 elqattisaa yqaesptgpv sgyvasrsls gtktdtalie tpqsisivtk dqmraqnaes
      181 lnqilrysaa vipetrgata srldqltirg fapatyldgl rmpssrdalp qkdafdlerv
      241 evlrgpasvl ygqgtpsgvi nmvskrpldt pfhevgveyg tfnkkrttfd lsgpiddqgv
      301 yayrvaglfd dadgqvehte trrqslssaf twrpdedtsl tllghlqkdp kgasygsvpa
      361 wgsvlhsptg rkidvdfydg ekdfeksdre hysigwafeh hindvwtvrq narylrsegq
      421 yrslynnylq tdyrtirrst iatdvdmday tldnqaqakf etgplqhtll mgldyqntrt
      481 ntlsgsgtyt agptldifdp vygaavpvpa yttdgtsrse qtgvylqeqm kwdkwvlllg
      541 grydwastds strtlstgak sqsaldskaf tgrvgvvylf dnglapyasy aesfnpqsgt
      601 gyggsvfkpt egkqyeigik yqppgsnsfi taaifdlrqt nvlttdpdpt hlcgsgrcqs
      661 qdgevqsrgf elegkaslnd nlditaayay ldnrisqsnn tvryapvsdi gvgsalsaeg
      721 tttyavprht asawadytfr dgnlkgfgmg agaryvgssw gdtantlkvp gyilfdaavh
      781 ydipniarlk dnlrlalnat nlankeyvas cysyswcwyg sqrtvqasat yrw
//
LOCUS       WP_010564912             344 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010564912
VERSION     WP_010564912.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 344)
  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 344)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 344)
  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   4  (residues 1 to 344)
  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 344)
  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 12117701
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38702
     Region          25..210
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          255..337
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkpvrlgdls vgfvqtlada vhshgldpqp lllqygldpa rlaeagarls iprymrlghg
       61 aiqltgdpgl glrmgqfsrl sqaglagvta aqapnvreaa rtltrfealy gsnyrgqssl
      121 hedaegawlr fysispynay nrfvvdsiia gwlhqlsnla qqtvqaqrid iefdapeyse
      181 rysilsdspv hfgaevnqlr lsqqtlalrn pqhcpstwql mlqlcerele qltrtrslre
      241 ritrllgpml nggrepdlee vaarlklptw tlrrklaeeg tqfrailndt rrdlamtyir
      301 dtelafgeia yllgfasaqa fqrafrrwnn qtpgefrrsq rhsa
//
LOCUS       WP_010565240             213 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Pseudomonas].
ACCESSION   WP_010565240
VERSION     WP_010565240.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 213)
  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 213)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 213)
  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 11459477
            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="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22663
     Region          3..208
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 msstddeqla efkdwwqrng kplvtgglla lvvvfgwqaw tkyqanqsqg asivyqqlle
       61 ttltpdgkpd parvadlask lknefggsty aqygslfvak vavdtgkldd aaaelkaivd
      121 kptnptlgei arqrlaqvla aqnkadealk lldgdadkaf vatreelkgd llvqlgrtde
      181 anaayqkaka alsdeaavgg lqiklddlak gda
//
LOCUS       WP_010565435             339 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas
            extremaustralis].
ACCESSION   WP_010565435
VERSION     WP_010565435.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 339)
  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 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 339)
  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   4  (residues 1 to 339)
  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 339)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..339
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38202
     Region          29..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          252..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msekdtislh lvreallqsc apgeatvevl skvgidpall qtpsarvpat ayarlwrlla
       61 rrmddeffgm dprklrsgsl aflcraslaq ptlaasldta laflslmler mpaqlvrqqs
      121 laeivllepe peprraftyf tywmivhgva cwlvgrripi laielrgprp dfcddyqvmf
      181 sdnlrfdrpr trmifsadcl dlpikrspee lkrflahapa nilvkyrdpd slaarikhdl
      241 rqmpadtwpe teglaaslci sastlrrrla qegqtyqglk dsvrkelaiv wlaepqisfa
      301 qiaerlgfad tssfykafrk wagsnpghyr slildeisp
//
LOCUS       WP_010565918             284 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Pseudomonas
            extremaustralis].
ACCESSION   WP_010565918
VERSION     WP_010565918.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            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="formate/nitrite transporter family protein"
                     /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=31096
     Region          24..276
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mathedgktp nlsreeqkdv ddnqppraav lheiirtqgd qelersvaal wwsalaaglt
       61 mglslmamgl lnsrlpdgea fkviasfgyc agflavilar qqlftentlt avlpvmskpt
      121 wanvgrllrl wsvvlvgnlc gtllvayvml hlpifdtktd hafleigrki menspgqmfa
      181 kgivsgwmia tmvwmipsme sakmwiiili tylmalgdft hivvgsaevs ylvfagelpw
      241 kdfwlvfagp tlagnivggs fifalishaq irsesslpid sdkr
//
LOCUS       WP_010567867             328 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas
            extremaustralis].
ACCESSION   WP_010567867
VERSION     WP_010567867.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas extremaustralis
  ORGANISM  Pseudomonas extremaustralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 328)
  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 328)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 328)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 328)
  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   5  (residues 1 to 328)
  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   6  (residues 1 to 328)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Pseudomonas extremaustralis"
                     /db_xref="taxon:359110"
     Protein         1..328
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36427
     Region          24..205
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <217..321
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtnatpaikl stlrqiapyl smrgvlplef frrfgisphv fqnpeawvpr aacfhianem
       61 aaaaqdpfgg atvghltdvr stgvwgelil gstnlaqaca aaavhtdllh qgsevkiite
      121 grktkliqhf tgqhevdpkq vifgtlavlr kvpllsgepg airvhlknpr ergdealeey
      181 lgpnlamnae ynmiefdrel leiplqpvrd vawkttqaln stseaadvla rqiadqeqsk
      241 lvtisrkigl svrtlqrrle hcgidfealr detrrheafq llasgkytat eiaymvgysd
      301 pahftrafkr wtgsppsryr aillkqdr
//
LOCUS       WP_010569658             212 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Leptospira broomii].
ACCESSION   WP_010569658
VERSION     WP_010569658.1
KEYWORDS    RefSeq.
SOURCE      Leptospira broomii
  ORGANISM  Leptospira broomii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Leptospira broomii"
                     /db_xref="taxon:301541"
     Protein         1..212
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=23788
     Region          10..208
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 melnphtntk livamagasg siyatrfira lmelegeswf vaspaairvf qeeyetkvss
       61 skeildfiee cwkptvrhnf kirnhkdvga diasgsntwd gmvivpcsmk tvasirsgit
      121 dnlieraadv slkerrklil vpretpynri hlqnmidlhd agaillpasp gfyqipktld
      181 dlgdfmatri frllginmdl yprwnpnpdi es
//
LOCUS       WP_010572879              80 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Leptospira kmetyi].
ACCESSION   WP_010572879
VERSION     WP_010572879.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 80)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 80)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 80)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..80
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8676
     Region          2..80
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mnvtvktfgi lkdhfqsdfi lnletpvrvl dvveemrksk patsgildvs lwavqdkmvg
       61 adriveegei vlilpplsgg
//
LOCUS       WP_010574720             374 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Leptospira kmetyi].
ACCESSION   WP_010574720
VERSION     WP_010574720.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..374
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42907
     Region          61..230
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mvfkkrihpr vwsrllggia flgvthllts filksdlevr knspfqgdqi hspysqtehr
       61 wlklafhlhs drdgfspfrs ppeeiqerys eknydligit dylkisgies gnskffpgye
      121 wgrdfnrkhi lalgsetpir dffplfasig niqwtidqmq ksgsfvavsh pglegsisys
      181 ilenlrgvda vevfspygnt fsdwvrlldl gipilavsgd dlhyfpgesi ralklplyqr
      241 ifheltfsdq negeafvryv llntnsvdrk eivrnlklgn yvsvvkatdy mddpkitelk
      301 leknrivaef petfvklefi gkngkvlqek iqmqkaeytf rkedeyaivr avfpsgviys
      361 npfyriseik segk
//
LOCUS       WP_010575046             358 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Leptospira kmetyi].
ACCESSION   WP_010575046
VERSION     WP_010575046.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 358)
  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 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   3  (residues 1 to 358)
  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   4  (residues 1 to 358)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..358
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40179
     Region          92..346
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          263..343
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mflgqivlpn kvrlnyllgv lflgmsilqg ssisilsfsa sflswlillh ipalysvgpv
       61 lygiykvstg esflesaker ilhailpltg aflyfgilff pgnvpetirr sfsekifpsp
      121 ldwvllpavi giafyvflvl kssrdlwrwe vwkaeptari lsflaatslf hltlgafffi
      181 tkipdflilt sggmglalca aylighrnpr ffqklqevtq atrekyarsl lvgidratlk
      241 enlihlmekd flyreedlgl gdladelals thqvseflnq elgknfsvfv ndyrvaears
      301 lltsepdksi ldiaysvgfr tkssfnrafq khtgitpsey ransaqfids vagprrnr
//
LOCUS       WP_010575874             301 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Leptospira kmetyi].
ACCESSION   WP_010575874
VERSION     WP_010575874.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 301)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            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="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=34779
     Region          79..294
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mkeimdfspn tdlvlsesfl neglvrnlft lnakhetake iiseletdpa fsvppkkset
       61 sahaqidgvd llktlsvilq tknfhteyep ilsldtgkif gyealarfyi egqrispefv
      121 fqelhkdadl ffefetnlkr fqienrpkgk nlflnldphv cknetqansw nellgkkkni
      181 vceiientds twieetrfcl nalknsnvpi alddmggkrn lfcfdfleys kfikfdkhwl
      241 hlfktkesyk niawgfldfa resniqcile gietqedlli aaemrfplvq gflfrsknil
      301 v
//
LOCUS       WP_010578540             356 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Leptospira
            alexanderi].
ACCESSION   WP_010578540
VERSION     WP_010578540.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..356
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=40045
     Region          1..352
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mgievknlvk rfenftaidr lslevpagel vallgpsgsg kttllriiag ledadegqvi
       61 feglevskkn akdrgvgfvf qhyalfrhmt ifeniafgle vrkrserpsk eairdkvmsl
      121 lklvqlenfh nrypselsgg qrqrialara laieprflll depfgaldak vrkelrnwlr
      181 rlhdeihits vfvthdqeea levsdkvvil nsgkieqvgt pdevynhpin sfvfhflgdv
      241 nlfhgrvqgg qtqlgeikvd tpehseiesa savgyvrpyd veilrapiea qtipaeiqyi
      301 hstgrtvkid lkrldtgsil esqlnssefq slnllpgetv hirfkkvkvy vedyti
//
LOCUS       WP_010579772             461 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Liquorilactobacillus vini].
ACCESSION   WP_010579772
VERSION     WP_010579772.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 461)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..461
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=51855
     Region          203..309
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          337..461
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(412..413,416,434..437,439)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mrvikrkkli giiliiligm lggigyyryn hfnqkiiing invgglnakq tlkrlqqksa
       61 sqkiylknkl iyqyqrsgsd ftkkdlpqik qlikrqwtff psskqqsflv epsevtkhed
      121 nktaatlktk ltqenlhrqa pkdayavlta gkiktvqaqa gnkynlqall kqyhqqeflp
      181 kveltavylq plkaksrqvq hekqkleels krsveyrvqn nkykfstksn lqrvtytngk
      241 ykidstnltd eiakinqqda tlqkgisfkt hdgntvqiad ggsygwalks eravehieqa
      301 lltgkkslda kqdiygvgyl tygtgyglsn ngignsyaev sisqqhlwiy kngqevvstn
      361 vvtgkhntge dtpkglwyim ykqspsvlkg sevgnanysv nvkywaqftn sgcgfhdasw
      421 rtnwssdayl nngsggcvnt pssvmadvyn nlsqkeavvi y
//
LOCUS       WP_010580529             693 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Liquorilactobacillus vini].
ACCESSION   WP_010580529
VERSION     WP_010580529.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 693)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 693)
  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   3  (residues 1 to 693)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..693
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..693
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=77202
     Region          2..684
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          178..257
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 mddnsayrel ffeesednlq klndnvlele kepdnkdlin eifraahtlk gssatmgydv
       61 mtklthrmed ifdlfktdkl kvngdhisli fkcldkltel lndlqddkel sedqiselit
      121 elnkvetsat gkavedtpte ssqeakkpqv kldtvfasle epdldvvkqa kssghnvfai
      181 airldqgtll kgprvflimq kldeegdvvh teptadllen gnfdtdfkli fvtnssldev
      241 ksiinsssei dqviiedfdg ekamkaqeer kknpptpqka pakpkaaasa ksvakkaksg
      301 apkhetahhp rnqsirvdlg rldrflnlvs elvvyrnqme dsshrndldg ikdsleqvsr
      361 ltselqdlvl rirmqqvslv fsrfprmird lsrdlhkemd lviigedtel dktvvtelge
      421 plihllrnsa dhgiedpetr eklgkprkgt itlsayqegn qviitleddg kgidpqvikk
      481 saeekginte gmsedelrll ifhpgfstak kitnisgrgv gldavktkit glggsiemrs
      541 qvnvgskfii klpltlsiiq almvkignen faipldvvek vvmldeseii staenevyry
      601 qggiipiirt nellkiksta edkkfaiivk sdqqyfgila dqligqkeiv ikkidpvlqk
      661 inryqgatif nngsialild vnalcqgkgk vks
//
LOCUS       WP_010585916             711 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Schlesneria paludicola].
ACCESSION   WP_010585916
VERSION     WP_010585916.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 711)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 711)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..711
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=79770
     Region          27..704
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mrffrlflsi itfysltsnf ahaadrkvtv hrdkwgvphv yaetasegay glgyaqaedr
       61 lhdiytsirt gtgtmaeafg snyleqdyim rlcrnndiaq nslktmpani rtlvenftag
      121 iqayvdehpe avpefavkle pwkiltigra milrwplgti ddeknqvpns krppmgsnew
      181 avapsrsadh vpillsdphl twegmsvlye arvhagemhm ngffligspi laighnqrvg
      241 walttggpdt advyemtira npdkkqleye ydgewkpvsq qlfsipvkgg atvekpalyt
      301 hlgpvlsapd lkqgtalvga apllemsgmm eqgyqmvmsk ncqeffqavg kgefnpqnim
      361 fadikgdigf vrcgvtpirp egydwkrpvp gntsktawkg ihpvedlvhi fnppqgymqn
      421 cnisplnmmk dspftadkyr dyiyhvswdt enprslrirs lleadhavtr ekaiaytmdi
      481 fdvhaqrwqt elklaidavg kqkmqnpqfa aavkaildwn gyftseatat slykfwrlkv
      541 gteanieqlq dgghfdatqq evvlnvlqkt iddmqtkygk wdvawgdihq vgrdeqlfpa
      601 agadfqsgpk elnfsetlfd vrskdnpthp gkfiansgsm avilmffhpd giqsltctpw
      661 gqsgnpksph yadqaeklys klqmkptwwt ekelvqnles trtlaikava k
//
LOCUS       WP_010584043             713 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Schlesneria paludicola].
ACCESSION   WP_010584043
VERSION     WP_010584043.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 713)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Schlesneria paludicola"
                     /db_xref="taxon:360056"
     Protein         1..713
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76016
     Region          1..712
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mrddglqaif apksiavvga sdkpgsvgga lfanlkatgy qgelfainsk hllvqgeray
       61 eslaklprvp dlvvvctpas tvpclvqecg rlgtrgmivi sagfreagad grrieselva
      121 aarefpllrf igpnclgvlr pvhklnasfs pvmphpgria flsqsgalct aildwsaere
      181 lgfsacvsvg nmtnvgmgdl idyfaedqqt daillylegl dqashflsaa rkcarhkpvi
      241 vcksgrfaes alaavshtga iasadavcdi afrhagierv dtieelfdca slliahgape
      301 gdrlaivtna ggpgvmasda wlalghplsr lseesiesln rvlpscwshr npvdvlgdag
      361 carfqaaiqi vaqdpnvdal lviltpqtmt dperiaesiv varangtkpi vvafiggaav
      421 ttgrtilrra gvpnydfpee avralshvta lrrkqcaats fdsvntsatp eslrrlgrav
      481 tseqiafwra elaekqglld erksksllad fgiqvvqgrl aasadaaeei aeqtgypvvl
      541 kvlspdishk tdvggvmlni pnaqsvreaf atmmkvvrer spsariegvs vqpmvsiarg
      601 velilgmtrd pqlgpvvvig aggitaelqr dtamelppcd eqtadrmlrs lrlypilegy
      661 rqrpgvdlvq lkltmkrffq lvedlpelsm veinpllata ttcialdgrm svg
//
LOCUS       WP_010581256             230 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Liquorilactobacillus vini].
ACCESSION   WP_010581256
VERSION     WP_010581256.1
KEYWORDS    RefSeq.
SOURCE      Liquorilactobacillus vini
  ORGANISM  Liquorilactobacillus vini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Liquorilactobacillus.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 230)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Liquorilactobacillus vini"
                     /db_xref="taxon:238015"
     Protein         1..230
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=26542
     Region          14..223
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mkaekdlsqk lakftliaqp ifdatkreas dfelllhskd sdqfpvaefs yfiknnanne
       61 illnwftcql ktkfkkkpqe kfainlepqq lffqstlncl kelkiyhnrl sleiterppk
      121 lctnvqslvq klqqikalgf eltlddvgtg mntssfvlen akffkrikfs liksnkrswt
      181 scleqwfkla qsrqiefvie gidnpekaqf alskgiylqq gflwnalaae
//
LOCUS       WP_010587393             163 aa            linear   BCT 20-JAN-2025
DEFINITION  3-hydroxyacyl-ACP dehydratase FabZ family protein [Schlesneria
            paludicola].
ACCESSION   WP_010587393
VERSION     WP_010587393.1
KEYWORDS    RefSeq.
SOURCE      Schlesneria paludicola
  ORGANISM  Schlesneria paludicola
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Planctomycetales; Planctomycetaceae; Schlesneria.
REFERENCE   1  (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 10101294
            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="3-hydroxyacyl-ACP dehydratase FabZ family
                     protein"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=17686
     Region          1..123
                     /region_name="FabZ"
                     /note="FabZ is a 17kD beta-hydroxyacyl-acyl carrier
                     protein (ACP) dehydratase that primarily catalyzes the
                     dehydration of beta-hydroxyacyl-ACP to trans-2-acyl-ACP,
                     the third step in the elongation phase of the bacterial/
                     plastid, type II, fatty-acid...; cd01288"
                     /db_xref="CDD:238615"
ORIGIN      
        1 mrwiwidrfv efvngshaka iknvtlsedh lhdhfpgfpv mpqslmlegm aqtggillgk
       61 vnefnhvvil akvpkmtfhs waipgdtlty taklidarpe ggmveveahv gerlvangei
      121 vfahvdekaa gggkidqknf vfsmrllgvm dvgkagdglt ptp
//
LOCUS       WP_010592248             289 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: endonuclease domain-containing protein [Rhodococcus].
ACCESSION   WP_010592248
VERSION     WP_010592248.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 289)
  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 289)
  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   3  (residues 1 to 289)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..289
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31342
     Region          177..276
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mhsfdapfrg teaiasgalt ayelrhgfvr lhravyvrrg vaptarnrvr aawlwsagrg
       61 tlaglsaaal hgtkwidgsa paellraghv rapsgivvrq gipdddelcr vdgmtvtspa
      121 rtgfdlgrta kgdravelld alchatgvkp aeirelacrh agargvsalr qvlefvdgga
      181 esppetrtrl llvrgglpvp etqihvraad grllaradlg wrswrvlvey dgghhwtdpa
      241 qrtrdidrya llesagrrvv rvdarllaer pdvvlervra alraagarw
//
LOCUS       WP_010592411             285 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Rhodococcus].
ACCESSION   WP_010592411
VERSION     WP_010592411.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 285)
  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 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   3  (residues 1 to 285)
  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   4  (residues 1 to 285)
  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 285)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..285
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30668
     Region          36..265
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          186..265
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mtgisdgarr rpapplcpyv rsydgyrltg fapgthlglp spdltvvlti gapvelaraa
       61 apgqgpgrfg alasglatta vtiahdgnqh giqlaltpag arvllgvpag algawvvdle
      121 dvlgaaarel geriaaaagw esrfrvldev larrlaaehg eidphlrhvw rrlqdprtpg
      181 vriadladei gwsrrylnar ftaefgvgpk eaarvvrfdr srrllrrpgp hvladvaars
      241 gfydqahlar ewraiagvpp shwlrdeqfp ivqdgdpaad ehwqp
//
LOCUS       WP_010592425             284 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PHP domain-containing protein [Rhodococcus].
ACCESSION   WP_010592425
VERSION     WP_010592425.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..284
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29821
     Region          1..257
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mridlhthsl asdgtdtpag lvraaveagl dvvaltdhdt tagwdaaada lpaglrlirg
       61 memsctgrge dgrpvavhll aylfdprnea favererlrg ervgrirama ermaadglpv
      121 dperivtaag pvagrphlar alveagvvps ieaafadlls srgryyvtka dtplseavrm
      181 vadsggvtvv ahararsrgr llaldhieel aelglgglea dhpdhapada qlmrdmaakl
      241 dlfvtgssdy hggnkavplg ryttdaeafe altaratgve vleg
//
LOCUS       WP_010593504             243 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease family protein [Rhodococcus].
ACCESSION   WP_010593504
VERSION     WP_010593504.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..243
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=25997
     Region          99..239
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 maaanstgrr rwlwllayvl afvafvvlqq tyggdeagpg gstsapvpap ssaaaaeave
       61 llkslavrep dpsggydral fgpawtddvt vaggrngcdt rndvlkrdlv niklapvtke
      121 ctveagtlyd pytgreiyfr rgvdtssavq idhvvalsda wekgarllda qarknlandp
      181 rnllavdgpt nqgkgdkdaa qwlppnpeyr ctyvsrqiev kaeyglwitp dekdamagvl
      241 atc
//
LOCUS       WP_010595414             352 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Rhodococcus].
ACCESSION   WP_010595414
VERSION     WP_010595414.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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 11438136
            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="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=35881
     Region          13..346
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mtglqlrarv esrdvdlava aesgsvlavl gpngagksta lnviagllqp ddgrvevdgr
       61 vltdtatgva vpphrraval laqqpllfph lsvldnvafa prsagrgrsa araaawrhla
      121 avgatdladr kprqlsggqa qrvaiarala adprllllde pmaaldvtaa pavrsllrtv
      181 lkdagrtalv vthdpldala ladravvvdg griveagtvr dvlsrprsaf aariaglnll
      241 agtltadgvd tvvgrvrgvp dddcapgdsa vavfapaava vypdephgsp rnsfavvvge
      301 levrgatvlv raaesgmtae vttsaaadla lapgaavwfv vkatevriha ar
//
LOCUS       WP_010594821             396 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Rhodococcus].
ACCESSION   WP_010594821
VERSION     WP_010594821.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 396)
  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   4  (residues 1 to 396)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..396
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=42534
     Region          16..321
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
     Region          329..>368
                     /region_name="CBS"
                     /note="CBS domain [Signal transduction mechanisms];
                     COG0517"
                     /db_xref="CDD:440283"
ORIGIN      
        1 mntpppsaaq isgtdidlid vvktfpgqar pavdglslhi pageivmfvg psgcgkttsl
       61 kminrlvept sgtiriggdd irsadvddlr rrigyviqgg slfphmtvaq nisivprllg
      121 wdrrrtadrv tellelvnld pdryrdrypr elsggqqqrv gvarglaadp pvvlmdepfg
      181 avdpitrlrl qdellrihdd lrktivcvth dideavklgs rilimqeggh vaqydtpeti
      241 lsapaspfve kfvgagstlk qlslsrvaev elaepttaev gssaeeavar arargddtvv
      301 vldrrrrpva wlwvrelqgs gtvpdgdpdd lvtldrhatl ndaldtmlas ahgaaivtgr
      361 hgefqglinf esvtgrirgg esqsaaagpg etgqht
//
LOCUS       WP_010596234             170 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Rhodococcus].
ACCESSION   WP_010596234
VERSION     WP_010596234.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 170)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 170)
  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 170)
  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 170)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            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="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18470
     Region          66..153
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(85,104..105,124,127,135..136,145,150)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 meilatrndv vtaagaelvl vlrlpdigth ssrdlaalad alreaahdlv pgvsthtvls
       61 ptpipliidl pardvlldgr rvllshsefe ilaylvrnpr tvvsravlrd lgtgvrevds
      121 rgrnvdvhvs rirtklqqfg siistvrgsg yrfdphpavh itelltrrca
//
LOCUS       WP_010601689             161 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Pedobacter agri].
ACCESSION   WP_010601689
VERSION     WP_010601689.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..161
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=18054
     Region          26..100
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
     Site            53..54
                     /site_type="other"
                     /note="putative proton transfer pathway, P2"
                     /db_xref="CDD:238138"
ORIGIN      
        1 menqgntysq llelansdyk ltageadikg wtvqneagas igkvrdllfd pqnnavryli
       61 idlddlgvdl eskgvlipig lahlhdhddi vilpnihtdq fkalpyyvsg evdqstedei
      121 rdaigspaal rmeetiiemd qnsfynhhhf drakfyrrgn k
//
LOCUS       WP_010601943             383 aa            linear   BCT 20-JAN-2025
DEFINITION  prolipoprotein diacylglyceryl transferase [Pedobacter agri].
ACCESSION   WP_010601943
VERSION     WP_010601943.1
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 10002130
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Pedobacter agri"
                     /db_xref="taxon:454586"
     Protein         1..383
                     /product="prolipoprotein diacylglyceryl transferase"
                     /EC_number="2.5.1.145"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008961 -
                     phosphatidylglycerol-prolipoprotein diacylglyceryl
                     transferase activity [Evidence IEA]"
                     /GO_process="GO:0009249 - protein lipoylation [Evidence
                     IEA]"
                     /GO_process="GO:0042158 - lipoprotein biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42595
     Region          144..382
                     /region_name="Lgt"
                     /note="Prolipoprotein diacylglyceryltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0682"
                     /db_xref="CDD:440446"
ORIGIN      
        1 mfptvshfle ylfginlplp fntfgvfvai afvagywaft kelkrkealg vlhpikktiv
       61 igkpattsei imnalfgfii gyklvyalln yslfvsdaqs ilmstkgnll gglffaglfa
      121 ywdykekdkn kldkpketqv tvhpyqimsn livwaaiwgf lgakffdnle ywddfvqnpi
      181 erllsfsglt fygglicgga avliiakrng ikplhmldvg gpgmmlayav grigchlsgd
      241 gdwgivnsnp kpfswlpdwl wsykypnnvv gegipipgct gkfcnelaqg vyptpiyevi
      301 iclllfaflw sirdkikapg lmfgiymiln gierfcieli rvnskyhvfg lsftqaemis
      361 tflviggial sayalrnknt las
//
LOCUS       WP_010603042             296 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Pedobacter agri].
ACCESSION   WP_010603042
VERSION     WP_010603042.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter agri
  ORGANISM  Pedobacter agri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 296)
  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 296)
  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 11466508
            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="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32657
     Region          48..296
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mpsnlnrrna lkniiagtaa igvssglatf amdqsnkknt aslkgnvnhs vcrwcfstly
       61 vetlcteakk igikgidlvg pkdwpilkkh glestmcnga einlvdgfnd ekfhetlikn
      121 ysemiplvaa agyknlicfs gnrrgkddet glnncvkglk qlmplaekhg vilvmellns
      181 kinhkdyqcd ktawgvelck rlgsenfkll ydiyhmqide gdvihtiken hqyiahyhta
      241 gvpgrneidd sqelnypaim kaivgtgfkg fvaqefipkn anklaslkqa isicdi
//
LOCUS       WP_010604213             761 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pseudoalteromonas maricaloris].
ACCESSION   WP_010604213
VERSION     WP_010604213.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 761)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 761)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..761
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=83640
     Region          19..761
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mltwikrivv vllllvllgt atiygllals lpaldgkgsa ttientvtva rdamgqavvs
       61 adsradasyg lgfahgqdrf fqmdllrrna agelselfgs aaigldermr fhqfrkrael
      121 ivrslpsayr ltlerytrgv ndgraqsgft sfeylllgsk pkpwqpedsl lvifsmyldl
      181 qtanyerdea lialkqqygq gmldfilqps hhqaaldgsv itaptaaipi lephlaqiqp
      241 qhiedvplyg snnwavtgal tktgaamlsd dmhlglsvps iwyraqlnyq eqgkevqvtg
      301 vslpgapaiv vgsnnhiawg ftngyldaad wielnsdtkt qqiaeeimlp sgevhtyqle
      361 msafgpvkql gdkklalswv ahqpyavnle liqlelfsev geatahaknv gipiqnlvvv
      421 dsqgsaawtp igaiparkfa hdtavkqeey esswqnnesi rpvvqdpesg klwtanarvv
      481 svadnqrfgd ggyapgaraa qirdgliskq vfteadfyql qldnqakflt pwherlvtll
      541 qtqdpssfdk dlkllkdwqg cacadsvgyt lvkayrnali dtlyapleqy lqtqslslks
      601 vkgyfepglw qllteqpnsw lgsysnwnel elaayqlakq klserygsnm aawrwgdvna
      661 lkvqhpfskq ipmlsglldm pttqafgdtf mpavqgkafg asqrfiaqpg hlenailtva
      721 ggqsghplsp fyrtgfndyt eggntpllpg kithqivisp k
//
LOCUS       WP_010603933             349 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Pseudoalteromonas].
ACCESSION   WP_010603933
VERSION     WP_010603933.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
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 11438136
            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="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39230
     Region          1..349
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msievknlfk hfgnftalnd vsvvfpeggl vallgpsgcg ktsllrviag letpdsgqvy
       61 lngedveskg irerqvgfvf qhyalfkhms vfenvafglr akprsqrvse seiqkrvmql
      121 lelvqldwla drypaqlsgg qrqrvalara laiepqylll depfgaldak vrkelrrwlr
      181 klhdelhits lfvthdqeea levadkvvlm negrieqigt peevydkpas efvyrflgss
      241 nrfnatalkg ltdaggkpiv ssifdqenmq tvyarpheit llthcledns lsakiersls
      301 igpltrleir ipqldeliev elprheyqlk glksgdqvwl elplltsfp
//
LOCUS       WP_010604624             152 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Pseudoalteromonas].
ACCESSION   WP_010604624
VERSION     WP_010604624.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..152
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16283
     Region          1..152
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mqkqdfyqtl vkqaqglisg ehnvianman lsallfttle dinwagfylm dsaeelvlgp
       61 fqgnpaciri pvgkgvcgta aatcetqlve dvhafaghia cdaasnseiv ipvfkdnkvi
      121 avldidspsl arfdeqdkig lealvkvfee tl
//
LOCUS       WP_010605594             399 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: exonuclease SbcCD subunit D [Pseudoalteromonas].
ACCESSION   WP_010605594
VERSION     WP_010605594.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            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="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44414
     Region          1..277
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          272..374
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkvlhtsdwh lgqsfyehdr seehqlfldw lcdalveqqi dvllisgdif htatppasae
       61 kqlytfiqka sqlcpqlhii liagnhdsan rietakpllt lfnthvigrf nkqapeqvvi
      121 dlpiaaqhmh vvampflrsa dlpkplddef dyqtgvqlay qhalstieev kgpivlmghl
      181 hakggtised sernlniggf davsagvfge qfdyvalghl hkaqtvakqs airycgtplp
      241 msfsernykh qvllaefneq glvdvnplyv prfkdvlyip edgakrlael ceaiaaqdfs
      301 kfdsapyvrl klsaaetnsr fraeidealk gkdikfcgie rvskgaaase wlfedlgkve
      361 slspntlldi ayreiepeqe kapatlhekl aeviasmee
//
LOCUS       WP_010606249             322 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010606249
VERSION     WP_010606249.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 322)
  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 322)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 322)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 322)
  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   5  (residues 1 to 322)
  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   6  (residues 1 to 322)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         1..322
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36118
     Region          31..198
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <145..322
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mhstsfvyfy sawvylhdhf tddkrlqgef aelvasrper vtlveyerll evgrelsgdp
       61 ligfelgkai qlhdygalgy lvetskdlqq aitsllhyda ivadiglavf tsdsdnaklt
      121 wqpktplgkq ailrnmtawv saarqllrst lspnqlqlsf svcdlelqrl qswfgcpvsq
      181 ncpenalsfp ldfltmpvat vdslmhehie qavaksvsal cdnhdlktrv anllaakhsl
      241 tgvnqasmak alnmsvrsmq rklkaqhtsf rtlldqerkh rfeqlidntr lldivdalgf
      301 teqsalnkvc ikwygkppsk lk
//
LOCUS       WP_010607810             146 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein, partial [Pseudoalteromonas
            maricaloris].
ACCESSION   WP_010607810
VERSION     WP_010607810.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas maricaloris
  ORGANISM  Pseudoalteromonas maricaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 146)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Pseudoalteromonas maricaloris"
                     /db_xref="taxon:184924"
     Protein         <1..146
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
     Region          <7..130
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 envamkqikl eltesammae enmligpleq lhqagfgiyi ddfgtgyssl arlnhlpvdg
       61 ikidrafmsg ieldgkatql ieaicaiahs fnlvvtaegi etaaqldtls rlychqtqgy
      121 fmskpllvae akrlalpnkk vhqlfa
//
LOCUS       WP_010614780              88 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein, partial [Actinomyces oris].
ACCESSION   WP_010614780
VERSION     WP_010614780.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oris
  ORGANISM  Actinomyces oris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Actinomyces oris"
                     /db_xref="taxon:544580"
     Protein         <1..88
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          <2..61
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 srqrrlvpde tfaqmaeagl aalemnhrdq gpeqreqvrl laqrlglgls gasdyhgtgk
       61 pnrlgenlmp pelleqilde galdlvrp
//
LOCUS       WP_010619303             372 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Secundilactobacillus malefermentans].
ACCESSION   WP_010619303
VERSION     WP_010619303.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..372
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42074
     Region          1..263
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          259..348
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrflhtadwh igkklhefdl vdeqqdayqq iaeiakeekv daiviagdly drkvpseesi
       61 nqldamildl nltrkfpila vsgnhdsapr lgsgshwyea thfylhttia qaltpiemad
      121 tqffllpyfe pfqvrhffed dsiqnvqqam nrlvaemqkn fdatkqhvlv ahffaagsqh
      181 vdsettvevg gldaiavdsm atfdyvalgh lhgkdalhae tvkysgspvk fslseakqqk
      241 gvwivdtapy nakfvpikpk kdieiltesf atlinpayye kvnrsnfiai sltdvdvitd
      301 vmarlrkiyp yiinldrkyg iqdvesqkri dpnldpmtll tdfynqatds qmskdqqkwa
      361 aqaltvaked de
//
LOCUS       WP_010620672             155 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Secundilactobacillus
            malefermentans].
ACCESSION   WP_010620672
VERSION     WP_010620672.1
KEYWORDS    RefSeq.
SOURCE      Secundilactobacillus malefermentans
  ORGANISM  Secundilactobacillus malefermentans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Secundilactobacillus.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 155)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Secundilactobacillus malefermentans"
                     /db_xref="taxon:176292"
     Protein         1..155
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16497
     Region          3..153
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mtetdfsivn eqidalltge tnpvanlsna sallfdtitd inwagfylyn eetealdlgp
       61 fqgkvacmhi nngsgvcgta fktntvtrvk nvhefpghia cdsdsnaelv vplevsgkli
      121 gvmdidsksl drfsdddqag ltkfasvlas hldia
//
LOCUS       WP_010621177             311 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paucilactobacillus suebicus].
ACCESSION   WP_010621177
VERSION     WP_010621177.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
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
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..311
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=34881
     Region          1..292
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 miefkdvtkk ydgqtalnnl nltihdgelf vlvgpsgsgk ttllrminql vkqttgtiki
       61 ddqdvtkvdi melrhqigyv lqagalfpnm tveqnagiql eqfnwdvrek hdricelldk
      121 vgldsktfln rmpselsgge aqrvgivral asqpkfilmd epfsaldpls rrqlqelvvk
      181 lhkelsttiv fvthdmqeai kladrlavih ngdllqlgrp reilanpand fvaeffddst
      241 trslflsqvt ktgfgrlqed gdepvtldds ktifdwadll nqhprqmiiv ddlilepqdl
      301 vaymaqigqv d
//
LOCUS       WP_010621769             220 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Paucilactobacillus suebicus].
ACCESSION   WP_010621769
VERSION     WP_010621769.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 220)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..220
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=25174
     Region          <4..215
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mykffvqqlv dkfqhslvgy ellmrrrdgd qwvlpvdfat ipvedvvnal leasellkgk
       61 vpiialnlnr dqllnidlln aivdckdkiv plklvieite eessqkidde lildrvkffw
      121 nndiqialdd vsngenhfdg ivnlipfase ikfalqndhl dfsapevqrl isnwqdianq
      181 hhirfvlegi etstddvtad rlgiayrqgy yygkpylvds
//
LOCUS       WP_010621860             374 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Paucilactobacillus suebicus].
ACCESSION   WP_010621860
VERSION     WP_010621860.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..374
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42249
     Region          1..262
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          259..346
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrllhtadwh igrrlhgfdl tdvqedafkq ieqiaidekv dgillagdly drgmpsensv
       61 sllnkmiqkl nledrlpiya isgnhdsair lstgapwfea tkfymatsie qafqpitvgn
      121 sqifllpyfe pfaaqqyfen ekithldqav kavvekiktl fdpakkhilv ahffvagssv
      181 tdsetqlsvg glaevplsvl sdfdyvalgh lhgrqalqad naaysgspvk fslseadqek
      241 gvyildtenm ertfkalqpl rdvtrlhdsf ekltnpiyye kigrkdyfgi tltdtkpipn
      301 vlarlreiyp nivsldrekg yqpsinprsl nvknqnpmel ldqfyesiak edlteqqkkw
      361 aenalgkanr evqk
//
LOCUS       WP_010622165             129 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Paucilactobacillus suebicus].
ACCESSION   WP_010622165
VERSION     WP_010622165.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 129)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..129
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=14296
     Region          2..126
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(7..10,40..42,45,71,108,122)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mikiytdaat kgnpgptglg flivqnqvai qktetlklat nhegefaaai asfsylkehy
       61 ganetvlfyt dsrllsdaig knytkhyksq ladlsklfeh fnlvitrwip ekenngahnl
      121 anqalkrld
//
LOCUS       WP_010622792             322 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Paucilactobacillus
            suebicus].
ACCESSION   WP_010622792
VERSION     WP_010622792.1
KEYWORDS    RefSeq.
SOURCE      Paucilactobacillus suebicus
  ORGANISM  Paucilactobacillus suebicus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Paucilactobacillus.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 322)
  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 322)
  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 322)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Paucilactobacillus suebicus"
                     /db_xref="taxon:152335"
     Protein         1..322
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34489
     Region          9..75
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          216..275
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 maeenskiei gkklrnarvs mgytlddlqk atkiqkryli aiedenfnel pgdfyvrafv
       61 kqyadtvqln gdellrdydd elpkskstey sehmsraiet ragqtrkntd sldrvrqylp
      121 tiiiavvilv ilgviwltal hgrssssdnn nidsssvsvs gessqksskt ssknssstke
      181 stssksskls lnatsqtssa avftvkgass sdlklkitpt krawisvttd gtpqlsqtls
      241 anesqtvkis ssakkvvisl gnaqyttlkl ngktinatkd neypnvskvt lnlngstsst
      301 tssssssass ssagsssstq sn
//
LOCUS       WP_010625767             182 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Halomonas sp. KM-1].
ACCESSION   WP_010625767
VERSION     WP_010625767.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 182)
  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 182)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 182)
  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   4  (residues 1 to 182)
  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   5  (residues 1 to 182)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..182
                     /product="TRAP transporter small permease subunit"
                     /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=20389
     Region          10..172
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mptanrdpvl lawldgftev vgrsiawlvi immavqfaiv vmryvfsihs ivmqesvmym
       61 hamvfmlgaa wtlrhdghvr vdifyrklsv rgrawidlgg tlfllfpvvl fiawssygyv
      121 rsswailers pdggipgvyl lktlilvmma lllvqgvaqv mrqililrgk apgntpdhde
      181 vv
//
LOCUS       WP_010625837             219 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Halomonadaceae].
ACCESSION   WP_010625837
VERSION     WP_010625837.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 219)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..219
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24179
     Region          59..217
                     /region_name="YafK"
                     /note="Murein L,D-transpeptidase YafK [Cell
                     wall/membrane/envelope biogenesis]; COG3034"
                     /db_xref="CDD:442269"
ORIGIN      
        1 mnraffqaaa mtagffafgp taqanipess htlngvmpel ptlwqvldav aqpegltade
       61 vwlsidlrnr rvrvmrgere ikriehlafg aggaaplrar gssmtpigef rvdrinrasr
      121 fglffgfdyp naqvaeealr sgkitmqeyw hienyrarhg raphttalgg ligihglgqg
      181 dpeihrsfdw tegcvavsne eiraldpwlr igtrvvikg
//
LOCUS       WP_010625867             547 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [unclassified Halomonas].
ACCESSION   WP_010625867
VERSION     WP_010625867.1
KEYWORDS    RefSeq.
SOURCE      unclassified Halomonas
  ORGANISM  unclassified Halomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 547)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="unclassified Halomonas"
                     /db_xref="taxon:2609666"
     Protein         1..547
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=58005
     Region          15..547
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mttqtiasdh ghldslrvhh adnvrvalkd lpaghavedg drhlrlaeai rhkhkfalrd
       61 lavgdavvmy gvtvgratrp ipagaaittd ntahstatse pqarrgqwqa pdvsafagat
      121 fegyhrpngq vgtanvwlvv plvfcenrni evlrqcvada lgedpyrdyk rmarellhgs
      181 sgtapaepsg erlfpnvdgv rflthtlgcg gtdddaqalc qllagyichp nvagatvlsl
      241 gcqkaqieml qnavaerdpr glrpvhyleq qasiseeali realttifdg lseanrtprt
      301 paplsaltlg vecggsdgfs glsanplvga vvdrlvalgg sgilsefpel cgveheliar
      361 crddavaerf aklmeayqrh aarvgadfsm npspgnirdg litdamksag aakkggdspv
      421 vdvldyteph traglsllct pgndvestta lagsganlil fttglgtptg npvtpvlkis
      481 snselaarmg dvidfdagpi irgetsidel aerllrlcld tasgrylpra velaqydfip
      541 wkrgvsl
//
LOCUS       WP_010626436             720 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter permease [Halomonadaceae].
ACCESSION   WP_010626436
VERSION     WP_010626436.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 720)
  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 720)
  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 720)
  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 720)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..720
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..720
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=75847
     Region          99..708
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mthetqpeqa askigtegvs dipiahnerv lsgllgqtvf aacvlftamh lyalnvspie
       61 twafriihva gglavgfait aaytldrspg erhiakvewl amipaiaaiv yaafaigyaw
      121 firetqgtpp agwvlvhmsw altiatgiam isswiwrsss rsvhwadavl ivasiivaay
      181 llfvlqrwrm aagtpfagqt eflvsavgva limeltrrva glalilitav flvyafagpy
      241 lpgllehrgy spqrfftyly tdngilgatt avsstyiilf itfaaflqas rvgdyfvnfa
      301 faaagrargg pakvavfasg lmgmingtsa gnvvatgslt iplmkkvgyh prsaggieaa
      361 astggqivpp imgagafima eitgipytei aiaalipaal yflsiylmvd learrggmqg
      421 lpkdqlpvfr kmvkqvylfl piiiligtlf mgysviragt lamvsaavvs wftphwmgpk
      481 allnalslga rmaipliavc acagiivgvi altgvgarfa smllgiadas hllalffamc
      541 isillgmgmp ttaayavaas vvapglqqig ipplvahffv fyyavlsait ppvalagyaa
      601 aaisgtdplk tavtsfkfgl aafivpfmff yspallmdgt wmqilrvalt agvgiyllaa
      661 svqgwflngg vnfvqrvmll aaalsmiagg wmtdllgvgi gglvfmwqaa alkakpkalt
//
LOCUS       WP_010626345             338 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Halomonas sp. KM-1].
ACCESSION   WP_010626345
VERSION     WP_010626345.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 338)
  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   5  (residues 1 to 338)
  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   6  (residues 1 to 338)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38165
     Region          28..203
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          95..335
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtvtvsmhfv nelfrgvpes eaaregylvr agispfllsa phgrvtveqf atlyrllvna
       61 cddetpgffa rplrsgtlkl lclsvleapt lkvalhrytl ffrivlddfg yeyrvedgla
      121 rvalvehrpp tgsrilvhel mlklfhgics wliaskippv mmecayaqpp hsadylyfyp
      181 gkvsfereqt aiyfdaalle lpirqtkkhl gaflrrapad wfyvsfedrv vshrvrehla
      241 rhlatsgsvh dvaralhmsv rtlsrrlaae gthfqavkde frrdfaiqal trserpllai
      301 adelgfqdla cfsrafkgwt gnspaayrra strlpqsa
//
LOCUS       WP_010626637             214 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Halomonas sp. KM-1].
ACCESSION   WP_010626637
VERSION     WP_010626637.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 214)
  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 214)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 214)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..214
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23084
     Region          1..207
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 maelrteeeq leaikrwwke ngtaliagva iaiagvvgwn awqnhqenqs asasmryqhl
       61 vnltdsgeid earslvaeit dnhgrtlyad larlidarla veagdldaar avlegviess
      121 nrdyvqglar lrlarlqvaa gdaeaaldtl ardipaalaa qqadvrgdal hsvgrtdear
      181 qawqealava eqrnqpiygv qlklddlgae eatl
//
LOCUS       WP_010627400             715 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Halomonas sp. KM-1].
ACCESSION   WP_010627400
VERSION     WP_010627400.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 715)
  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 715)
  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 715)
  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 715)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..715
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=76062
     Region          1..706
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mnatptpevr deaaseaper lehpwlgrvl falaivvals hlyfntlgtl sevwvsalhf
       61 gmfgllcals vpmlkarsvg garlvlavdi llglaalgca fyligfedal yargvrfsta
      121 dwvvsivalg lvlefarrtt gwfipllclv altyvawwgr hvggvfgfpg lswetvlfrs
      181 ylggdgmlgs iariswsyvf mfilfgaflv rsgagdfiie larcaagrfi ggpgfvavfs
      241 sglmgsvsgs svantvstgv itiplmrkag fpprfaagve aaastggqlm ppvmgagafi
      301 masytqvsyl tiigvaalpa llyflsvamf vrieakrsga qhveteeapr flevlkggwh
      361 fllplvvlva aliygftpty aagiailsvv vaswlsrnpm tptvvmealv lgtrnmitta
      421 illltvgliv nvvsttgign tfslmitdwa ggsllitivl iaiaslvlgm glpvtaayiv
      481 lgtlsapaly glmahgqlme llmagqlpeq akaifmltap eslealsapm daasarella
      541 lvpddfrrql yeqalsphtl tlllvaahmv ifwlsqdsnv tppvcltafa aaaiartppm
      601 rtgftawkia kglyiipllf vwsplitgsp aemltvfafa lfgiyaiiag legflehelp
      661 wwlrlvmfpm galmlwphdq laldflglal flatlawsar agrtsatalp apgha
//
LOCUS       WP_010627451             198 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Halomonadaceae].
ACCESSION   WP_010627451
VERSION     WP_010627451.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 198)
  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 198)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 198)
  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   4  (residues 1 to 198)
  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   5  (residues 1 to 198)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..198
                     /product="TRAP transporter small permease subunit"
                     /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=22173
     Region          22..184
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 msiplpdapp ddtplrpelp tnrvshvidt aiavlgklls wlwlvtlavv ltnvfsrfil
       61 grgsialeel swhffgatmi ltlayavvtd dhvrvdvlrd kfslrfqawv ellcivllvl
      121 pvlyfmvdgl teyaqrsfar gersqapsgl pyrfiikstl pigmaliaia lssralrcct
      181 ylfgfprqlp lrrpvdhr
//
LOCUS       WP_010628491             313 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Halomonas sp. KM-1].
ACCESSION   WP_010628491
VERSION     WP_010628491.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 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
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..313
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=34541
     Region          1..310
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mielfdvtkr fgdetavdgi slrvergelc alvgtsgcgk sttlrminrl iehdggeihl
       61 dgqpvrafde valrrrigyv iqstglfphw tvarniglvp rllkwpkskv rerveelmql
      121 lglpvaefad kyprqlsggq aqrvgvaral aadpdillmd epfgaldpit ratlqgemre
      181 lqarlhktvv fvthdmdeal aladrlvvmh qgrivqqgsp vdllrepanp fvesllggmd
      241 rglkeaaliq vsehmlplgp rllaseripy gaslsqalsv mlwhrvdrlt vvdeedipig
      301 elslrrllga kvp
//
LOCUS       WP_010629391             431 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Halomonas sp. KM-1].
ACCESSION   WP_010629391
VERSION     WP_010629391.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..431
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=47589
     Region          3..300
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          296..397
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mlklihtadw hlgqtfhgqe rhaehrlfld wlldtlvare adallvagdv fdvvnpslaa
       61 qallydfivs aherlpaldi vliagnhdsg nrielpaplm rrlrthalgr vcwlddgsld
      121 aerllvpltd ahgetrawcl alpflrpaev tghglapaea negeplsdkp rndyvagisr
      181 vheqlidaar krrvsgqalv amshahlhga avseaserpi viggeesisa glfptdiayv
      241 alghlhraqq vgeahirysg splpldfsev nyphqvvaav legeslaqve aiavprpvam
      301 qrvgpgelde vlaelealph dpalprewwp wlevrvslta pvpdlrarve aaldgkavrl
      361 lrlerrlpqq atgdkpervd lqqlgprklf qrtwekqwge ppddnvladf dqllqdvldt
      421 heeprsgerr p
//
LOCUS       WP_010629443             241 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Halomonadaceae].
ACCESSION   WP_010629443
VERSION     WP_010629443.1
KEYWORDS    RefSeq.
SOURCE      Halomonadaceae
  ORGANISM  Halomonadaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales.
REFERENCE   1  (residues 1 to 241)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Halomonadaceae"
                     /db_xref="taxon:28256"
     Protein         1..241
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=26471
     Region          53..216
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mrflptlrlp lstlaasllv tlptahagnf lsqaglsyps paplsrtlan lapdanpvvl
       61 klaakavaca epdarrlavi dfsrpstepr lwvfdlaqqr lmfeelvshg rgsgdaeatv
      121 fsntpesyqs slglfrtmns yygrngyslr leglepgvnd layqraivih gadyvseafi
      181 rqtgrlgrsh gcpavrqevt yplidsiked hylfayfpdp ewlensafls cerdatqlam
      241 y
//
LOCUS       WP_010629792             369 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Halomonas sp. KM-1].
ACCESSION   WP_010629792
VERSION     WP_010629792.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. KM-1
  ORGANISM  Halomonas sp. KM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 369)
  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 369)
  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 369)
  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 369)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Halomonas sp. KM-1"
                     /db_xref="taxon:590061"
     Protein         1..369
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40309
     Region          4..359
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 msvnrrnflk yggaaavgtv mapsivkaqe tfnwrmttsw psgfpffqsg pgsatdfarr
       61 veemsggrik irvygageli pafdgfdavs rgqqvqlnha csyywagesf aaqyfttvpf
      121 gmtfqgfnaw lahgggyelw ketyepynli plavgctgaq pvgwfrepvt svadfrglni
      181 rmpglagdvy naiganarll pggeifsale rgaidaaewv gpyldralgl hnaakhyyss
      241 gwhepsttte vivnkdayds lpsdlqavlh naaaacnits htwieaqngd alddlvnnhg
      301 vafetlpddv iralfeatrd ilateadkdp lvkrindsfw afkkkhdgwh tnseavfant
      361 isrygqgmi
//
LOCUS       WP_010630602             353 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Sporolactobacillus vineae].
ACCESSION   WP_010630602
VERSION     WP_010630602.1
KEYWORDS    RefSeq.
SOURCE      Sporolactobacillus vineae
  ORGANISM  Sporolactobacillus vineae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Sporolactobacillaceae; Sporolactobacillus.
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 11438136
            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="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39695
     Region          1..350
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msielrhisk sygpyqilkd inltiqtgel vallgpsgsg ktsllrvlag leyadeglil
       61 fhgedltnap ikkrkagfvf qhyalfdtmt irdniaygln vkrrkdrpsk qqirervdql
      121 lhlvrlepyg drypsqlsgg qrqrvalara laiqphilll depfgaldak vrkelrqwlr
      181 hlhqqvkmts llvthdqeea fevadrviii nkgqieqigt psevyenpvn sfvydfignv
      241 nqvrgtisdg lftngsfrvp vdnteqadgv afirpdqfai rtpddiqeag rtlaatvthi
      301 hpsgsiikle ligqdedqnl evevtrrefd alalsknqqv flearkvkvf tvn
//
LOCUS       WP_010634289             216 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Aeromonas].
ACCESSION   WP_010634289
VERSION     WP_010634289.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 216)
  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 216)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 216)
  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 11459477
            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="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22898
     Region          1..203
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 mevytteeqq veviknwwke ngtsviagtv iglvglfgwr yynehqqttq eaasqaynem
       61 saqlakgdaa gfeqaqsfis ahkgdsyael aalqlaaaav kadkldlaae qltqvatsgd
      121 esirpiaalr larvlndqgk adealaqlgk inndafkaqv aevrgdilqk qgkseearda
      181 yqaaadaggl qssaelklkm ddlalpavtt geapda
//
LOCUS       WP_010635013             193 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Aeromonas].
ACCESSION   WP_010635013
VERSION     WP_010635013.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            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="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22002
     Region          3..165
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mklfsrlyvl vmqwarhkya pwylaitafi esvfwpipvd vmlapmalgk prrawhyaal
       61 atlfsvlgal vgyllgyalw epvvqplvas vgyedkiava eqwfqqwgiw vifiasftpi
      121 pykvftvtag llqmallpfi vtsligrgmr fflvaglmrw ggekmerklm hyvdvlgwlc
      181 iglavvayfw fsr
//
LOCUS       WP_010635216             250 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Aeromonas dhakensis].
ACCESSION   WP_010635216
VERSION     WP_010635216.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 250)
  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 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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (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   5  (residues 1 to 250)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     Protein         1..250
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27470
     Region          1..246
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <139..245
                     /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 mtrplaassl sapfslrryq sdvcshshdh aqlvipldgp ieievqgqgr rlapgfacii
       61 apgerhdyaa dpalsflvqe shwlpgelge rpfieldeaq rhylaflhrm vaegrhvagm
      121 eqvwlgllae aqqagsrgra rlaprigkvq rhieahlaep lsnerlaaia clgqsqfkha
      181 fqqqvgmsvs hyirarrmal artllahtal pvgeiasrcg yqnqgafaer flaetgvtps
      241 lwrqqngclp
//
LOCUS       WP_010638901             395 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Acidithiobacillus thiooxidans].
ACCESSION   WP_010638901
VERSION     WP_010638901.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..395
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42155
     Region          7..391
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 maditqilsi nsgsssikfa lfafgaglee qqldgaveri gqsmgriwle qagqrvldrq
       61 qafvdqsaal qavvavlsel githpdaigh rivsggphqq ahvcidatvl kdlrdalafa
      121 plhlpaeiaa ieslqkiwpe kpqvacldta fhhsmpemaa rlplprnlwq egvrkygfhg
      181 lsyeyivsql pdqgkaptii ahlgngasma avadgrcldt tmgltptggl vmgtrsgdld
      241 pgillylmae kgysapqler llnhlsgllg isacsgdmqv llrqrennph aaeaiaqfay
      301 sarkhigslm avlgsvqrli ftggigehaa avrwaicrpl ealgfhldpe anaavaqear
      361 risapespve vlvvptdedl miarhtlrll gtgtp
//
LOCUS       WP_010638967             427 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Acidithiobacillus
            thiooxidans].
ACCESSION   WP_010638967
VERSION     WP_010638967.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus thiooxidans
  ORGANISM  Acidithiobacillus thiooxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 427)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 427)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Acidithiobacillus thiooxidans"
                     /db_xref="taxon:930"
     Protein         1..427
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47711
     Region          23..415
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 msrtdnaplf yvyvcpdatq rylagiltyh esaaistfqy vrsyrerddl ppiapmpawr
       61 kdgppiltqt mnrglpgpir dalpdywgtl vyaknlgiav esvqfsdllq advqdrpgfl
      121 afsrdlesap vipapvnrtd dvpdlsaivq avesleqegp ssyplqplad flvqrtsmgg
      181 arpklsvyhq gqmwlaklpa yrdsydvgll eqatmilarr agittpntel yplqdgrhvf
      241 lsqrfdrvgt penrrhlamv sglsllnfde senrlgsypd lanhlrmfgd lsgatelfrr
      301 mifnwlvrnt ddhlrnhavi lgvdgtwqls paydinpths rpglhtqfdl sialgkegrq
      361 atlqnalsmv eafgldrsea thivheccea lqgwravlqd lglsqkdinf wehsfsdqsk
      421 nvlssns
//
LOCUS       WP_010643503              97 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Streptomyces].
ACCESSION   WP_010643503
VERSION     WP_010643503.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..97
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10187
     Region          4..97
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(22,51..52,54,76)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(22..23,31,32,34..35,37,40..41,43,51,56,63)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mtwvdevrea vltipagsva sygeigrhlg tgprqvgram sllgeetglp wwrvvhadgt
       61 patchgglap allagegtpm rggrvdlera rhrwgpp
//
LOCUS       WP_010644247             379 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Vibrio campbellii].
ACCESSION   WP_010644247
VERSION     WP_010644247.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..379
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42804
     Region          1..270
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          267..353
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkfihtsdwh lgrqfhnvsl lddqqavldq liqyvednpv davvvagdiy drsvpptiai
       61 ellnkvvkrv cgelntpmil isgnhdgaer lgfgseqmkn aglhiisnfe dmltpvviet
      121 esagqvafyg mpyndpeqir fayqepvsth dqahkllaek iteqfhpeqr nvlvshcfvd
      181 gaieseserp lsiggsdrvs hehflnfdyv alghlhqpqk kgeeyirysg slmkysfgeq
      241 nqkkgftlve idqngfvsae hidlaaphem rivegeleqv ieqgktdpkn edyllvrlmd
      301 khailnpmek lrtvypnvlh lekpgmligv eqemaqakla rseidmfrdf fseaqdgqls
      361 qeqdqaisdi ikqlsqqaq
//
LOCUS       WP_010642839             413 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Streptomyces].
ACCESSION   WP_010642839
VERSION     WP_010642839.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 413)
  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 413)
  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 10007089
            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="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44836
     Region          16..394
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mtslpsaadt lavhrpvasl sadearrial raqgflgapd rragvrgvlr atgavqldti
       61 svlarshelv pyarlgavgr paveaaywss dadgsphafe ywshaacilp veewphfafr
      121 rrayrdrphw hhdlpqaayd kviaqltaeg pltaselgga knggewwdws etkiaveral
      181 mygevvctsr rgwkrvydla eraipapllh dalddqaclr elvgqagral gvgtrsdlad
      241 yhrikgesfd sviadtglvp vevegwakpa wadpealstp prgrhrttll spfdsliwer
      301 arterifrft hrleaytpka krlygyfamp vlaggklvgr vdparsgdtl varhvalggd
      361 lpgspgpaks vaatavalae aarwvgctev rvehmtqpel rpaltaelaa aln
//
LOCUS       WP_010644713             117 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein [Streptomyces].
ACCESSION   WP_010644713
VERSION     WP_010644713.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..117
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=12719
     Region          16..86
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 msdgiwgyqp taghtagtdl igykveatdg tigkvdkhsd evgssylvvd tgvwifgkhv
       61 llpagtvrtv dgaerkihve ltkeqiknsp efdkdrhvgd reyhdklggy ygghrpl
//
LOCUS       WP_010646692             283 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio campbellii].
ACCESSION   WP_010646692
VERSION     WP_010646692.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 283)
  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 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   3  (residues 1 to 283)
  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   4  (residues 1 to 283)
  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 283)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..283
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32828
     Region          18..281
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          198..277
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 msnitlpipk lqlilgepfr alefsgiqea pfiephrhey weivwcldns gtqsidfvey
       61 qnrlgrlfti spgqvhhsel mgksvrmlif ssgfaetnpr stqlvntvfs tidrppyldc
      121 neegfpyles iytllqeece reacdwdlie sllnsflryv lrfskkpsqk geqkdarivq
      181 lielielhyr eqkncqfysd alaltskrln elvkadrgkt vtqlihdrii leanrelvfs
      241 tktvktiafe lgfddpayfs rfyrkqkget pakfrhrcsd sti
//
LOCUS       WP_010647514             678 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Oceanobacillus massiliensis].
ACCESSION   WP_010647514
VERSION     WP_010647514.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 678)
  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 678)
  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 678)
  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 678)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..678
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..678
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=72621
     Region          31..667
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mtrkhndqtg khtasevdnn vdtqvileky daesrvrqlk srnivifisi iaifysafhl
       61 fvtynpipal lqrsvhmsvg maliflifpt fkkqdrakip vydwflflls iisslylive
      121 ynaivttrgg ipnaidilfa iltvllvlea arrvtglilp vlaliflayp fisymdwlpt
      181 mlmtrpfdlg difgqlylkt eglfstaiga svqfiflfil fgafltrsgm gqlfndlama
      241 lagskqggpa kvavissgfm gsingaavan vvgtgaftip lmkkigyskn fagaveasas
      301 iggqilppim gasafimaet tgiaygtial aalipavlyf lgvimqvhfr agrrnlkgip
      361 kadlprvkev lkerghlllp iaglvvmlym gipvgfsafy tiiltvivaa frktsrmgik
      421 dilgamedga rqslsvmiac avvgiiigvv nltsfgtvmt saitnigdgs lfltlfltmi
      481 asiilgmglp sipayiitat mtapalaefg ipilvahlfv fyfgifanit ppvalaafag
      541 agisggdpmr tgftalrlal agfiipylfv ynpamllvdt tglpvnatef pfppllavam
      601 iittsvigii glgaalegyf kthlnviyri ilgvgsimmi vpetttdiig liivigifal
      661 nylknkkdns iiesktas
//
LOCUS       WP_010647689             675 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Oceanobacillus massiliensis].
ACCESSION   WP_010647689
VERSION     WP_010647689.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 675)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 675)
  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   3  (residues 1 to 675)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..675
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..675
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=74473
     Region          1..675
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 metdqylevf ldesrehlqa vndnilelek qpedlnlvne ifrsahtlkg maatmgyedi
       61 aslthkmenv ldlmrnhklk vsteiidvif laieyledmv nsisegndgk kdvsglvqrl
      121 dqiekgnpvq dstetridaq dqvvnsddlg ldefqitive qakeqgffpf qitveltddc
      181 ilkgaraymv fealedygev irtnpsveei eegnfaqsfs miflsgkest eiktiiekvs
      241 evkqvqignl vtisnainpa ehesveniae taakeetaat teqssqtsvk ssgsktirvn
      301 lekiddllnl feevvidrsr leviaeniss hdltetvehm srvstdmqsl ilamrmvpie
      361 qvfnrfprmi rglardlnkq isleiygadt eldrtvidei gdplvhlirn svdhgielpe
      421 vrqqsgkqae grlilrafhs gnhvfieied dgaginrekv qekaiengii srdeaevltd
      481 dqiagfimss gfstadkvsd isgrgvgldv vknkieslgg qisietkagk gsifsiqlpl
      541 tlsiiatllv kvqketyavp lssiietvil nkeqimyahg kkvmdfrgkv vpivslaavf
      601 dipeaeaheg neysviivkk gdkltglivd sfigqkevvl kslgnylgdv faisgatilg
      661 dgevaliidp nalik
//
LOCUS       WP_010647922             351 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Oceanobacillus
            massiliensis].
ACCESSION   WP_010647922
VERSION     WP_010647922.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 351)
  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 351)
  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 351)
  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 351)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..351
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39725
     Region          12..344
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mtlkkiftpi imaiifvsli llgnmtlssn agnkesgtvq lrlgqakaat hpvsqgidrf
       61 aklvkeksng eivvetfhdg ligndrevie saqmgslama ssstpnmtsf tnyftawdlp
      121 yifenkeevy taidgepgei vrkemeeygf kviffpdygy rqivnnvrpv evpedlagmk
      181 vrttnsrieq adfnmyganp tpvawsevft alqqgtvege gnsysllwds khqevldyat
      241 evnynyssdi vvmnldryeg lseyhqkiim eageeatkwq revanereae akqqfidygi
      301 eiyepteeem kqwkqavepv wdqfvvegls dpeyvevile tlgktkedif e
//
LOCUS       WP_010648506             667 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Oceanobacillus massiliensis].
ACCESSION   WP_010648506
VERSION     WP_010648506.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 667)
  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 667)
  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 667)
  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 667)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..667
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=71452
     Region          11..653
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 msenkeqhel taeeqqqlle kydtesntrd vggiigkvif fgliafslfq iytgifgqyt
       61 ayvqrtvhlg falslifllf parrktkkss ipwydfilvl lsiivcgywp vfydtlvqqi
      121 ggidlaqvii gglaillvle aarravglpi tiiailflvy alfgpsmpgm lahrglsldq
      181 lidsmfftte gilgtplqvs styiflfllf gaflvqtgvg qyfndlaisi agkqtggpak
      241 vaifssalng tisgssvant vttgsytipm mkklgyhrnf agaveaaast ggqimppimg
      301 aaaflmiefa gesywniaka atipailyfa giwimthlea krigllglpd edipskksvl
      361 kkihlllpil aivyflfvgv sveraalygi latvivslfr kdtritpgkf ivalqsgakt
      421 algvaaatac agiivgvvtk tglglkmgng lvsiagnlan spetqllltl fftmiasiil
      481 gmgspttany iitstialpa ilalndqlev aipvlaahmf vfyfgivadi tppvalaafa
      541 atgisggepi rtgfnaskla iaafiipymf vlnptllmie gtfldiawal italvgmlai
      601 gacmigfwyk klnwleriit latgllllyp eghtdiigli ifivllvyql ikredkqdsl
      661 pktsgeg
//
LOCUS       WP_010649175             393 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Oceanobacillus massiliensis].
ACCESSION   WP_010649175
VERSION     WP_010649175.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 393)
  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 393)
  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
REFERENCE   3  (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   4  (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   5  (residues 1 to 393)
  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   6  (residues 1 to 393)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..393
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42637
     Region          17..57
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          76..383
                     /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 mqrgtfqlmk svnksnilnk irtaepisra qiakeieltp ptvssivkel ieqelvress
       61 lgksqggrkp tmlhinneaf yvigvdagpe tveciltdlk geicerahnk lkkpitnnef
      121 ltilketiwk ilhsstvnqe kilgigvamh gvvdvetgts viapnlnlin ipikteleqe
      181 fnltikvend aramalgesw fggygdedsm vavnigrgvg sglvingkly hgehdiagev
      241 ghmtvdmnge tcecgnvgcl qtfvsgeaia krasnqapdr qhregltgkd vfelaqngdd
      301 fyrnilqetg kiigigltnl ihlinpskii lgggvmkgek yilpaiqqti eqralilkak
      361 qtkvsisklg edatllgavs lllvelfdpv eks
//
LOCUS       WP_010649309             262 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Vibrio campbellii].
ACCESSION   WP_010649309
VERSION     WP_010649309.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 262)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            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="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=29762
     Region          28..255
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mmsitqllgc iskqldgqyi ahykqltlrs vfqpiyqkdl siiglealvr isnqggqmir
       61 pdqffqsnti pvkdqinver lsrlihisnf gqskfsnkkl flnvlpkaae mlakdmsysn
      121 llkqaiiead lrreqivmel veldasdenc lykatkelsd ngymlaiddy gvdastverv
      181 ksvrpniiki drslllryes gdftclmeal slakdirskt viegietehq lnlmkklgfd
      241 myqgyllamp qtleayqefk ta
//
LOCUS       WP_010649525             179 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Vibrio campbellii].
ACCESSION   WP_010649525
VERSION     WP_010649525.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 179)
  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 179)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 179)
  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   4  (residues 1 to 179)
  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   5  (residues 1 to 179)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..179
                     /product="TRAP transporter small permease subunit"
                     /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=20091
     Region          31..169
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mrsliyiert fnrfgdylgg lssilfilll anvvydvvmr yvfndvsiaf qemewhlfsa
       61 vfllgvpyai ksgghvrvdi fyerlsykaq siidilgtll flfpfcllva wfgidfakes
      121 yalgetsgdp gglpyrwiik gmiplsflfm avsgvglllh sinkivnphl iyagnkgkf
//
LOCUS       WP_010649720             673 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Vibrio campbellii].
ACCESSION   WP_010649720
VERSION     WP_010649720.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 673)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 673)
  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 673)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..673
                     /product="M4 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=74300
     Region          1..608
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mrnvtllslv pfafasqaaq ivehsqtdis ealnivgkss ytpastelsy qninrveigq
       61 qtlvrkqqlh ygvpvyghsv vadlsakgfa qsidgnvvvg idndldstlp misanqaiei
      121 atgteqgfas nespendara elmvwldeqn tahliykvda vkivnlrpsr pitlvdaksg
      181 eimdqwegla fleaegpggn qksgryyfgp ntkfggfqvd qycqmnsdnv etinmnnqqw
      241 ggqvhrfncn vnnyreinga yapmndahyf gqrvfdmyre wlgarpiqqk ltmrvhygsn
      301 ygnafwdgrq mtfgdgnssm yplatwdvia hevshgfteq nsgleyrgms ggmnesfsdv
      361 aaaalsqyvh gsfnwkmgeh vmkyspamry finpshdgas idhvnqyyrg idvhhssgif
      421 nkafyhlats sgwsikkafm ayatanqlyw tpnstfqqga egvckaaqkl gyessavtsa
      481 fsqvgvqvmn cesgqpnpnp npgpdtgmne lslnmpvaiq snaageqqfv lrktssddvw
      541 vqtyngfgnv elyvaidrpa tpsdydcsst nmgneeacgf ggiqgsdiyv tvtntqsasd
      601 aylavsetyg tpqpnpepqd qcaslqewsp ynyypagssv kywgnrfvat qdnwgadpfq
      661 nywfwtfegs cnd
//
LOCUS       WP_010650182             243 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Oceanobacillus massiliensis].
ACCESSION   WP_010650182
VERSION     WP_010650182.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            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="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=28389
     Region          2..77
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mffytsqlkd fnihatdgem gkikdlyfne dkwdvryaiv dtrkwlpgrk vlltpstfkt
       61 inkdeefvev eydkekirns ppvpeednls aeqennlidy fgwnsyrdna lagvergplg
      121 tfeenglvre nipqkpdlfr deyevsdvnk mrsedetigf kvhakdgkig kladmiydte
      181 qmqikyivvk ssdnliedef yiyrteqiet vdwyendlyi ndsvkgiaen npfldkedii
      241 psl
//
LOCUS       WP_010651048             289 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Oceanobacillus massiliensis].
ACCESSION   WP_010651048
VERSION     WP_010651048.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..289
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31673
     Region          1..288
                     /region_name="SpoIIB"
                     /note="Stage II sporulation protein SpoIIB (spatial and
                     temporal regulation of the dissolution of septal
                     peptidoglycan during engulfment) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5816"
                     /db_xref="CDD:444518"
ORIGIN      
        1 mdkhkailve engkqlkykl hdnirpitae kesaaavdes eesipvltgl hkskkglqkk
       61 rqgkfnyfkp ilfalgsavi igsllgisml rlfvdveaem taptvnnnaa tavqdneaat
      121 avslfnpepl hafvlqagif sekgnaeewa geyaekgvpa miwerdqqyf liagaadtke
      181 gakaiadglq kggnveiyvk ewstaagevn vtateqdwla kfknlweasl vswseqnsis
      241 megwegllae speqsdglsp lttaiteage qvtqihllqw myyyeqlsh
//
LOCUS       WP_010651381             249 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Oceanobacillus
            massiliensis].
ACCESSION   WP_010651381
VERSION     WP_010651381.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 249)
  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   2  (residues 1 to 249)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            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="aminoglycoside 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=28221
     Region          3..>85
                     /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"
     Region          <49..219
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mnlgspiaig ntakiylhne miikvfrddl plteaqyead kqkiaysygl qvpkvldvtl
       61 iagrqaiime yvpgktigdi lsqnkdqtay ymnlsidvqq kihqiipdsl epmrekirrq
      121 iesvncldar hktcliqkme sitfetklch gdfhlfnlll snekvtiidw vdssagdira
      181 dvyrtyllys qfskaladly vhvyceksgi akddifqwap iisgarlset vssentkrll
      241 giinhycsl
//
LOCUS       WP_010651546             290 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Oceanobacillus
            massiliensis].
ACCESSION   WP_010651546
VERSION     WP_010651546.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 290)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 290)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..290
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33277
     Region          19..100
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          125..285
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mlksmneald yieshldgei dyseleritg tsvyhfrrmf sflsgmtlge yvrnrklsna
       61 tfdllhegms vtetafkysy esvdgfsraf rewsginpse vkkknmlkaf pklsfqltiq
      121 gginmdyrie kkqafkivgl kkrvpiqfeg enqeiiklak sitpeqrkrl hsyanmepnq
      181 vvnasynldd gwkeekgsld hmigflttke kdfdgfevve apaltwaifs skgefpkvmq
      241 etwakiasew lpssdyelve apnisftgdl sdsnnvysei wfavkkkrev
//
LOCUS       WP_010652045             653 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Oceanobacillus
            massiliensis].
ACCESSION   WP_010652045
VERSION     WP_010652045.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus massiliensis
  ORGANISM  Oceanobacillus massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 653)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 653)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..653
                     /organism="Oceanobacillus massiliensis"
                     /db_xref="taxon:1465765"
     Protein         1..653
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=75001
     Region          40..651
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mkqhtntfie eeknskkpkl dkafltkiqp qggmtfkdky iqkgdgyeac vhvwdypsnv
       61 nllwldkvma mydvtvvadv ttmdqdetis sinksmvehd vrfrsakqes drmdaqrsyk
      121 emedlyqqis emgevikllh irlfvatpti welerkveqt isklnsigfk gqiflnetyy
      181 ewqslflpye qqirfpnkre gkgmpaitla sglpyhfsel ndrtgsflgt sftggnvlfd
      241 lfhkdklrrf ynavvvgkmg agksttlkkl lmdneargnf irgfdvtgef ktlvgalggq
      301 sisldgsdgi inplqiyrad dksnyneeqv sfeqyekqcf mqhiskvaif yeflagspst
      361 eeieefkkil rmfyeslgfm kktkttgvtt lgnkeypifs dlleyireql ydnsekrtir
      421 nelsisrvdr lekielvvdn lvnsyaslfn ghttiqditd eqviffsirn ltkleknvfq
      481 aqmyntlnli wdnliqvgar qmkqmyqset fdpddavrfl imideahrlv naenmlavsf
      541 ltdfareark yfggmilasq sirdfvpdnk dtatvtkirt lfeltqykfv mqqdsntlds
      601 lrtifegqlt eselehvpql qqgdcllsis gvgnimlsie aseeelklft ggl
//
LOCUS       WP_010652138             549 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Fluoribacter dumoffii].
ACCESSION   WP_010652138
VERSION     WP_010652138.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 549)
  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 549)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..549
                     /product="M4 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=61833
     Region          3..543
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mikkllgisl vfitydafav teldlyqapl sslkqfslkk ttkmtapfaa iskeekntlr
       61 qinqtqehak timryqqmyr gipvvgaqim vtkedaqvng hllndiqlni qpalspnqai
      121 elakkswfsf nspmpvyeel gelqiranqn elklvyqvsf ktnqgdnkpa lpifiidaht
      181 gdileqwnni knyldagpgg nekvheywyg kdglpflevf qqgsqcimnt skvklvnlef
      241 awdwndllst pfqypcsnnv eeningafsp tndayyfgqt ivdmykdwyg inalqnpdgt
      301 smqlvmrvhf gqhydnafwd gqfmsfgdge dfyplvsldv aghevthgft eqhsgleyhd
      361 esgalnesls dmagqaaray llekfpqlyn klylepdtvt wgigetivrd sfgkalrfmd
      421 fpssdgssad cldknlaqsh gaycaisype lvayaksrip npqerqsfiv htasgifnka
      481 fyllaknigi kqayqmmiia nskywtpttn fikgacgvly aakdlnvnhk mvksvfdqvg
      541 vdthscrmi
//
LOCUS       WP_010654457             116 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Fluoribacter dumoffii].
ACCESSION   WP_010654457
VERSION     WP_010654457.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..116
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=12682
     Region          11..78
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 menrgivksg eltgtkvins anenlgeiae vvidkasgtv nylvldfggf lgfgnkffav
       61 pwnlflydnk ddcfilnvek qhlknapgfd kshwpnfsap efkttitgfy tggkea
//
LOCUS       WP_010654509             140 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Fluoribacter dumoffii].
ACCESSION   WP_010654509
VERSION     WP_010654509.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            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="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14934
     Region          1..137
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mmhtrskgft lielmiavli mgilatlayp fyvnfllkar rsdalatlaq dqiilercys
       61 qnfsysaacg slpsfpqtsa qgfysitltn lgsttytlta tpigsqtedt tcasmtvdqa
      121 ntktavdtsg taqticwgss
//
LOCUS       WP_010654523             424 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Fluoribacter dumoffii].
ACCESSION   WP_010654523
VERSION     WP_010654523.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   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 10614777
            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="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=47129
     Region          66..233
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mgsfllllla vtsnyfpqls lgvskapani ndnshsiset aqyssslqin eqalndmklm
       61 liheapnlnp lvinkvltsl kcaieynvdh nniltlidys lpsnkkrlwv fdlnakkllf
      121 htyvshgiks gtlltnyfsn kfnskassig vyqtqeayyg rdglslrldg ldrnfndnas
      181 gravvmhsgw yveerfikky grpgrswgcp alplqnsnai intikdksll viyypsdawf
      241 akskflncdk dssdqyttns tiqiplsppd ehrepilfvg sgykggkhae tkpvavisad
      301 tyqrvfhtta plsrmlrrqi nnaeyialda keldylahqn pagaaaaneg insilfvipv
      361 lkvvrggyye tqmqivnlgk ikeikandgl arenspassf tvyfegkspv nlnackdfir
      421 wvgl
//
LOCUS       WP_010655197             764 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Fluoribacter dumoffii].
ACCESSION   WP_010655197
VERSION     WP_010655197.1
KEYWORDS    RefSeq.
SOURCE      Fluoribacter dumoffii (Legionella dumoffii)
  ORGANISM  Fluoribacter dumoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Fluoribacter.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 764)
  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   3  (residues 1 to 764)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Fluoribacter dumoffii"
                     /db_xref="taxon:463"
     Protein         1..764
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=86196
     Region          161..756
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mtpddnllkq lletfgtele sllkvisdnl nkiergasgd dldhimeeis ragrnikvsa
       61 lsvgmddlgk maeyieklfa saqreaspdr mnlasraveg mqelfhnfid knprptalde
      121 lfrqlqqsla hkdkeethln enfagsappe ttsptldnef ikkivetfka elqenlitit
      181 dgllkleket lsdqdfqkvl eeifrvahni kgssrgvgan dvgeiahhie tlfaaiqkks
      241 lpvspelinl clqsidfmne amqcysaqkp lsfdlknhll qleyyfespt hkissppqlp
      301 eehkaepqki skpalpakan efetlrvslq nldnvsfyme eiqtikiaie eyfcrlnkmn
      361 fkigdllqsw kknraylknl ahdkieaids lfsdnlhelt einstirfmq remnmslnef
      421 sllinalqde irtlrlvpvt tqlrylprlv rdlahelnkq vnleinsndv kidkiildgl
      481 kdplvhllrn aidhgienvg vrkaagktae gnilinvnqe dnqivfriid dgrgiktedl
      541 irvalqknii tqtelenmke kdiydlifrp gfstreiatd isgrgvgldv vrsnllrlkg
      601 qvsvnsqpgk gtifflkvpl tlaterglii scseqifvll tssiesvmlv krqeiknveg
      661 spavlvkeqp vllcslskll hlkekkqntn envsvvvikk dadriallvd eilgereivl
      721 kplqeplthi paiigatltg snqinfvlns selmkrmllv nyyp
//
LOCUS       WP_010657252             145 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Pseudomonas].
ACCESSION   WP_010657252
VERSION     WP_010657252.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            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="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15951
     Region          2..144
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mfeitsylgl flaafgaasl lpmqseavlv amllsgkyla stlllvatlg nvlgsvlnwl
       61 lgrsverlrh kpwfpvseqk ldkarqfylr ygrwslllsw vpiigdpltm iagvmgeplw
      121 rfvlivtlak garylalaal tlgwt
//
LOCUS       WP_010658633             219 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Brucella/Ochrobactrum
            group].
ACCESSION   WP_010658633
VERSION     WP_010658633.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..219
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22037
     Region          <1..195
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 matleggayd dvlfgsrfdd firahggddl vfggdgndtv fggngsdilf ggtgndtlfg
       61 engndilfgn egndvlsggn gsdvlyggng ddilqggngs dllfggahnd ilyggngsdi
      121 ldggagndvl iggngsdtfl fnggggndvi ldfnpgedil qiqkgingld iasaddladr
      181 vtqvggnvvv dlgngdsvtl vntnaddvqa hpdqyftvh
//
LOCUS       WP_010658267             182 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Brucella/Ochrobactrum group].
ACCESSION   WP_010658267
VERSION     WP_010658267.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 182)
  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 182)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 182)
  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   4  (residues 1 to 182)
  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   5  (residues 1 to 182)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..182
                     /product="TRAP transporter small permease subunit"
                     /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=19961
     Region          4..171
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 msvllalsra idaannfigk svswlilvav lisainavsr klfnvssnaw leaqwylfsa
       61 vfliaagytl lhsehvkvdl lysrysrrtq llveifgtlf fllpfcliti ylswpiveak
      121 iasgetsnnt gglvlwpvwv lipigfglla lqgiselikr iailqgripd tvaledaeaq
      181 tl
//
LOCUS       WP_010659063             183 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Brucella/Ochrobactrum group].
ACCESSION   WP_010659063
VERSION     WP_010659063.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 183)
  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 183)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 183)
  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   4  (residues 1 to 183)
  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   5  (residues 1 to 183)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..183
                     /product="TRAP transporter small permease subunit"
                     /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=20654
     Region          5..171
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mpkpirlfvk yvdavnyyvg rfamylffvl gacllystfs rvvlgvpvnw vlemsqflls
       61 ayyllggaya mqqgahvrmd lffdrlsprr kmitdmitil fiifylgvmv aggisstnya
      121 ivysqknyta wapllwpikl imtvgillll lqcvsnffkd waslrgqpis tiagpaieeg
      181 hhi
//
LOCUS       WP_010661253             277 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phytoene/squalene synthase family protein [Brucella].
ACCESSION   WP_010661253
VERSION     WP_010661253.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..277
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30797
     Region          1..275
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mneneahcla llrqadrdry lsvlyapedr rgglaalyaf naevarirdl vheplpgevr
       61 lqwwrdling eargsaeahp vaaalintie kyelprtafd nycearifdl yddpmpsrnd
      121 legycgetas aiiqlagfil drdaaqaqte itghagvaqa vtgllrlmpi hrrrgqlyvp
      181 admlqavgvt retfiagedk aavermisim lafarehlai feknksqlpk slvpaflpla
      241 lvpaylraie rlgaqaaekv adisairkqw lmfranf
//
LOCUS       WP_010661751             192 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Brucella].
ACCESSION   WP_010661751
VERSION     WP_010661751.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..192
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20335
     Region          1..187
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mkrvvvgisg asgaliplkl leqlsalsdv ethlvvsdaa qhtlrhelgp dgyallhrla
       61 hrsysvsdig aliasgsvat agmivapcsm rtlaaiatgh sdslltraad vhlkerrrlv
      121 liaretplhl vhlrnmctvt emgaivmppv pafyfkpqsv devadqiaar aidligigek
      181 qseswagipg nr
//
LOCUS       WP_010662398             365 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Marinilabilia salmonicolor].
ACCESSION   WP_010662398
VERSION     WP_010662398.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..365
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40503
     Region          189..358
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mgkqlqnilq kagllghark aylkwmdlre vaellvvlpi lkksgllrrf yfaffsstfs
       61 aemrqyihgr yfylkrsrgp vfnesllrrn vhrlekglma eerkpvfgld figqtvqqfs
      121 asvaeagpsd lndwafdiln eyfkivgesp vihdacqyfs svvytkslpg qsklpfvklp
      181 pdadafthfq kllnirksvr sfvpgsnpsr dqiqqgvrma atapsscnrq pfrfivledr
      241 esvvavskla ggarsfaegi pslavvvgst svspspgdrh lmyidgslas mnfmlalesm
      301 gvsscpinwp dnktpekalr kivalekfer pvmliamgqa agtglvacsv rkgvpellef
      361 hqpke
//
LOCUS       WP_010662591             429 aa            linear   BCT 20-JAN-2025
DEFINITION  galactokinase [Marinilabilia salmonicolor].
ACCESSION   WP_010662591
VERSION     WP_010662591.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   McAuley,M., Kristiansson,H., Huang,M., Pey,A.L. and Timson,D.J.
  TITLE     Galactokinase promiscuity: a question of flexibility?
  JOURNAL   Biochem Soc Trans 44 (1), 116-122 (2016)
   PUBMED   26862196
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Holden,H.M., Thoden,J.B., Timson,D.J. and Reece,R.J.
  TITLE     Galactokinase: structure, function and role in type II galactosemia
  JOURNAL   Cell Mol Life Sci 61 (19-20), 2471-2484 (2004)
   PUBMED   15526155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..429
                     /product="galactokinase"
                     /EC_number="2.7.1.6"
                     /GO_function="GO:0004335 - galactokinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0005534 - galactose binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0046835 - carbohydrate phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=46624
     Region          36..412
                     /region_name="GalK"
                     /note="Galactokinase [Carbohydrate transport and
                     metabolism]; COG0153"
                     /db_xref="CDD:439923"
ORIGIN      
        1 makieslvqr inngdnkafq rlygtdagel ktqaerytql meefrslfgq ddvelfsspg
       61 rteiggnhtd hnhgrvlaga vnldniavaa pngtdivrik sagypefqvd lsnlepdeke
      121 hytstalvrg ivakmkangy kaggfdacie grvpkgsgls ssasfevlig aivnhlfndg
      181 kmdavenaii gqwaennffg kpcglmdqta csvgglitid fkdpaepivk pidfdfvssg
      241 yslvitdvgg ghddpasqqe yaslptemks varelgagvl revsleqive kipeirdktg
      301 drailraihf qgdnqrvadq vealenndfq aflkmvvesg qssymynqni ydithkeeqv
      361 vslglalsem vlkgkgawrv hgggfggtiq afvpqeslqe yvatlehvyg qgkchtmfir
      421 pegsikvel
//
LOCUS       WP_010662683             417 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Marinilabilia
            salmonicolor].
ACCESSION   WP_010662683
VERSION     WP_010662683.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 417)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..417
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47720
     Region          3..416
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mesnvvkvkl wnldagylsw dqsahvanfe ydpeflnqnl diapltmsiy sprsqrqipw
       61 pgnsdklyqg lppmiadslp dkwgnslfna wlrdnqlsqk kvtpvdhlsf ignramgalt
      121 yepahklgdq kafsvdvqkl yefarqvlne rettilnqen svlwqdliki ssspggkrpk
      181 aivalnektg kiisgqgkip edyqhfilky ddnsaypfgk leyiyyrmal dagikmmpsq
      241 lktfgnithf ltrrfdrvhn erihiqtlaa mdpdsnsyed ifsvirklkl pyedleqqyi
      301 rmvfnvlsrn vddhsknfaf cmhkdgswkl spaydltfsv dlaapayvnr hslsvngkye
      361 nitradleii gqnndiqnyk slidkvgnai sgfdtyaree klnagliddi rkefiei
//
LOCUS       WP_010663472             129 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Marinilabilia
            salmonicolor].
ACCESSION   WP_010663472
VERSION     WP_010663472.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 129)
  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 129)
  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   3  (residues 1 to 129)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..129
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15369
     Region          24..127
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mpidnqvnmf fnakphifek akdlrknmtp aelklwkyik nnqilglrfr rqhpidifia
       61 dfychqiklv ieldgevhnn nenheydvnr taelerlgit virfnnheim dniekvveql
      121 kkicedllr
//
LOCUS       WP_010664797             147 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Marinilabilia salmonicolor].
ACCESSION   WP_010664797
VERSION     WP_010664797.1
KEYWORDS    RefSeq.
SOURCE      Marinilabilia salmonicolor
  ORGANISM  Marinilabilia salmonicolor
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Marinilabilia.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Marinilabilia salmonicolor"
                     /db_xref="taxon:989"
     Protein         1..147
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16344
     Region          5..147
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mwidlgylgl flasflaati lpfssefvls gllaaggdpv lslatatlgn wlggltsfwi
       61 gwigkfewie kylriprdkl etwhrkvagk ewwislfcwl pgvgdiiavi lgllksnfwv
      121 saigmfvgka lryvvwglit levierl
//
LOCUS       WP_010666661              87 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Acetobacter aceti].
ACCESSION   WP_010666661
VERSION     WP_010666661.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 87)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 87)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 87)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 87)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..87
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=9272
     Region          4..87
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mngsvtvlyf aglreqvgrg setvalapdi qtvkdflavl rqqdaafdav flqfprmrva
       61 vnkvmgdlst avhngdeiaf fppmtgg
//
LOCUS       WP_010667034             663 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Acetobacter aceti].
ACCESSION   WP_010667034
VERSION     WP_010667034.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter aceti
  ORGANISM  Acetobacter aceti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter; Acetobacter subgen.
            Acetobacter.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 663)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 663)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 663)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 663)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 663)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Acetobacter aceti"
                     /db_xref="taxon:435"
     Protein         1..663
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=72053
     Region          39..663
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mtghetsags ngappaaadk gagaaahqdp kvtefgadqp qheappvgfa allgvlgvvy
       61 gdigtsplya lrstievvsg hhpvqntevl gieslifwtl iivvtvnyvl lvmradhnge
      121 ggilaltsla qrvtadgrmr milgligivg aclffgdgii tpaisvlsai egvevsfpaa
      181 qefiipmaia viiglfsvqw igtgkvgaif gpvmllwfgs lgmmglfeil hhpgvlfais
      241 plyalqfiih hgtlsfmalg svvlcvtgae alyadmghfg rqpiryawlf fvlpmlvlny
      301 fgqgalvman psalanpffm laphsmqvpl vilstfatvi asqagisggf qvcrqliqlg
      361 ylprmrivht naeeegqiyl pdfnrflmvg aillvvafrs sdalaaaygi avtgtfictt
      421 vlcfivfrkh fhwsaqavyc tfipfllidm tffsanalki pdggwvplml gcvltlmmtt
      481 wkrgrsliia rqgqdslpmg sfiarlpqsr tirvpgmavf ltatpdfvpp cllhnlkhnk
      541 vlhdhvlfvt iqnldqpead rghrvmveel ahdiyrvilr ygfmetpnip raleelkang
      601 idfdpslasy fisreliars svpkmarwrm avfmfmarna tpateffrip mdrvvelgvk
      661 vai
//
LOCUS       WP_010670936             340 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Pantoea
            agglomerans].
ACCESSION   WP_010670936
VERSION     WP_010670936.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 340)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 340)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..340
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=38404
     Region          <55..330
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mnserclitl krlkeselkt gystkgirhl lgslnvalsl pftrsqfiqe lperqkgmsi
       61 sgyqpklslr lakgelvvvs ndgtyilkps peeyphlaen ehatmcvmqr lkfdvppfgl
      121 mpfrhddnrp eelafvikry drtasdnarl hqeqldgamg lgdkygridn hkaicyekaa
      181 kflntrvnss lkskrdlflr ivyayvlgnn dfhlrnigii lppqgspwla pvydfisvvp
      241 ypaafgeyla lpllereend agnapginse ygeylgadfi llaqgmdinp tlarkwlsev
      301 vshhqliidt yneshmpesq reavldyvar ritllavtei
//
LOCUS       WP_010671380             291 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Pantoea agglomerans].
ACCESSION   WP_010671380
VERSION     WP_010671380.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Pantoea agglomerans"
                     /db_xref="taxon:549"
     Protein         1..291
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32119
     Region          15..257
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mvhdvknila lqaelgecpl wsveeqvlyc vdilapaihr fdpvsgelqt fpqaeevgci
       61 glreqgglia alrggvwlld aqgkperkia enpgvaaqsr fndgrvdpwg nfwcgslwep
      121 qdknggllcr vtpdlklevk ardikisngl afspdrrwmy hsdtpnealy ryplnaqgep
      181 gertlfrrfd akgglpdgaa vdsegfywsa qfdggrvvri dpqsseivde illpvkwptm
      241 vafggadlkt lfitssredr teeelarypq sgdifavdvs vagmaeprfr g
//
LOCUS       WP_010672397             254 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Aeromonas].
ACCESSION   WP_010672397
VERSION     WP_010672397.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 254)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..254
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=28834
     Region          24..241
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mdipsapaqs icqqcheqvd ldfdftmafq pivdcsqrtl fgyealvrgl nnesaqsvid
       61 rvnddnryrf dqlcrikaia laarldmrgm lsinflpnav yrpercirtt lqaarehlfp
      121 ieqimfefte veqvqdnrhi rgivdhyqal gfktaiddfg agysglslla dfrpdiikld
      181 mhllrgidqd pirqaivrhc lalftelqit plaegvetre emaclremgv slmqgylfar
      241 pgfetlpevd fasl
//
LOCUS       WP_010672489             267 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Aeromonas].
ACCESSION   WP_010672489
VERSION     WP_010672489.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 267)
  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 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   3  (residues 1 to 267)
  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   4  (residues 1 to 267)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12820790
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30536
     Region          8..267
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <151..263
                     /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 mnapqsrihy wqsrllpgve lshshhrefs ygrhvhldyh iglvqrggqk fihkgnshnl
       61 vrgelstvnp demhdglsll pegyevrvfs iapeqlarwl pehpepffhq glqsrpdlyq
      121 gfarlhmhld gpapdgllae sqllallgel frlaperhal adpqlrflrd hllarlderh
      181 tledlaalfg ldrfaflrqf kkktgmtpya wlkrlrleqg krllgsglpv sevalavgff
      241 dqshfhhgfr qafgltpaey rqqmlpa
//
LOCUS       WP_010673936             718 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Aeromonas].
ACCESSION   WP_010673936
VERSION     WP_010673936.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 718)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 718)
  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   3  (residues 1 to 718)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..718
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..718
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76654
     Region          6..717
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mafevdedil qdflveasei leqlseqlvd lekrpddknl lnaifrgfht vkggagflsl
       61 telvdvchga enlfdmlrng krtlsaelmd vilqaldain vmfaqvqnre eispaspdll
      121 hdlhelckpe gqeqlrtasv aaqpepepep epapepevia evapvavngg gsideisade
      181 ferlldelhg vgkaptvsaa pvlsgsgdit ddefealldq lhgqgqhgga pdlaplqsvq
      241 kevdeliddd eferlldelh grgqapqhsl asapapapep kapapaapaa pvtppkapva
      301 akpapaeppa pakaapakqa apaessavqs dttvrvdtkt ldvimnmvge lvlvrnrlvs
      361 lgiasndeem skavanldvv tadlqgavmk trmqpikkvf grfprvvrdl artlkkeiel
      421 vmvgedtdld knlvealadp lvhlvrnscd hgvempdvre kagkprqgti tlsasqqgdh
      481 illcieddga gmdpeklksi aisrgvldad saarmsdnda ynlifapgfs tkseisdisg
      541 rgvgmdvvkt sivslngsvh idstwgkgtr leikvpltla ilptlmvevg qqtfalplgc
      601 vneifhldlk kanvvdgqlt iivrdkaipl fylhkwlvrg agktarqdqg hvvivqigtq
      661 qvgfvvdnli gqeevvikpl dnllqgtpgm agatitsdgg ialildvpsl lkayarrh
//
LOCUS       WP_010677382             389 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Bacillus timonensis].
ACCESSION   WP_010677382
VERSION     WP_010677382.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..389
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=41105
     Region          <7..389
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mdnqqyfmgy rrpdgkvgvr nhvlilptit catqaaqqvt qlvhgtvsfi hqhgctqvgv
       61 dydqtfrtyv gvglnpnvyg vivlglgcet hqarsvaeei aksgkpvetv siqenggtlq
      121 tianaakiaa kmvqdasaim repchvseli vgtecggsda csglsanpav gyvsdllvka
      181 ggtailaett eligaehlla nravddrtve rvyekikqae gralmmgidi rtgnptpgni
      241 agglssleek slgaatksgt splqelidya etptkkglvw mdtpgqdieq ltgmvaggaq
      301 vvlfttgrgt ptgspiapvi kistntpmfn smrenmdlna gtiiegretv qsvgqsifee
      361 iksvssgklt kseilkqndf giwrigptf
//
LOCUS       WP_010678440             159 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Bacillus timonensis].
ACCESSION   WP_010678440
VERSION     WP_010678440.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..159
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17623
     Region          8..159
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfhveqyegn kakdynlvtk qlqalledep dqianlanas allnqflkni nwvgfyirkg
       61 delilgpfqg lpacvripmg rgvcgtaaqn vktervadvh lfpghiacds asqseivvpi
      121 mkngevfgvl didspikerf devdqqclee fvkvlekhi
//
LOCUS       WP_010677627             291 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Bacillus timonensis].
ACCESSION   WP_010677627
VERSION     WP_010677627.1
KEYWORDS    RefSeq.
SOURCE      Bacillus timonensis
  ORGANISM  Bacillus timonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 291)
  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 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   3  (residues 1 to 291)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 291)
  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   5  (residues 1 to 291)
  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   6  (residues 1 to 291)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Bacillus timonensis"
                     /db_xref="taxon:1033734"
     Protein         1..291
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33017
     Region          21..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..288
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mdsiknmnea idyieenltg einfhkvakl alcseyhfkr mfsflagvtl seyirrrrlt
       61 lagfelansn lriidiaiky gyssadsftr afqtlhgvnp searmngnnl kayprmtfql
      121 sikggtemny rieekegfni vgimkrvpiv fqdenphinr mwkslnmdli selkslsnve
      181 pegiiqastn fsegrmeekg elnhyigvat sneypnkfse levpastwav fesegpfpst
      241 lqgtwgriya ewfpssnyql tegpeilsik tkdltspavk seiwipvrkg k
//
LOCUS       WP_010679583             372 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Leptospira interrogans].
ACCESSION   WP_010679583
VERSION     WP_010679583.1
KEYWORDS    RefSeq.
SOURCE      Leptospira interrogans
  ORGANISM  Leptospira interrogans
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Leptospira interrogans"
                     /db_xref="taxon:173"
     Protein         1..372
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43621
     Region          61..230
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mvfkrrihpr vlykvlgaft ffviihllts filtkdlrli knspfkgnri yspysetkhr
       61 wlkmafhlhs drdgfspfrs speeiqekyl ekkydlisit dylkisgtes kdpkyfpgye
      121 wgrdfnrkhi lalgteslir dffplyaske niqwtidqmq ksgafivish pglegsisyk
      181 ilerlqgvda vevfstygdt fenwirlldq gipmfatsgd dlhyfpgeli ramklplyqr
      241 ifheltfsdq negeafvryi llntdsterd eiirnlkkgn yvsvikiady medpkitelk
      301 ltkdrifaef pdkflkivfi gkngkilked qlefrssyqf qnedeyvivk vtfssgyiys
      361 npfyrtsnsd tk
//
LOCUS       WP_010679879             400 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Fusobacterium gonidiaformans].
ACCESSION   WP_010679879
VERSION     WP_010679879.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..400
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43474
     Region          1..398
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkvlvincgs sslkyqlinp dskevfakgl cerigiegsk feyevpakdf eiklqspmpt
       61 hqealklvvd nlvdkkhgvi asveevdaig hrvvhggetf assvliteev mkaiednndl
      121 aplhnpanlm gihtcmklmp gkpnvavfdt afhqtmpaks fmyplpyedy telkvrkygf
      181 hgtshlyvsq tmreimgnpe hskiivchlg ngssmsavld gksvdtsmgl tplqglmmgt
      241 rcgdidpaav mfikdkrgls dkeidnrlnk qsgflgifgk ssdcrdvedg vaagderail
      301 addmfcyrik syigayaaam ggvdaicfag gigenaagir ekvleglefl gvkldkevns
      361 vrkkgnvkls tedskvlvyk iptneelvia rdtfaivsgk
//
LOCUS       WP_010680350             191 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Fusobacterium gonidiaformans].
ACCESSION   WP_010680350
VERSION     WP_010680350.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..191
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21605
     Region          2..152
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mlekikknrs hrsfeqvnip tedlhrilta vsysasarna qenrfmftns fkqckqifkq
       61 tkwagaiswn pteeegptay illcnpsekp tamsfvdmgi alqsmtlvaq dlgysccilg
      121 aynkkeveki fglpdgyfsf lllaigkatd tvevvmthdl svkyqreeen hhtvfklpme
      181 dvlltniden n
//
LOCUS       WP_010680579             238 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Fusobacterium gonidiaformans].
ACCESSION   WP_010680579
VERSION     WP_010680579.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium gonidiaformans
  ORGANISM  Fusobacterium gonidiaformans
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 238)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Fusobacterium gonidiaformans"
                     /db_xref="taxon:849"
     Protein         1..238
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=27351
     Region          41..204
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mnykkplycl ifilisfsll ahsfteekie slykdmnlek ritfpafkqg iqgmerirnr
       61 nnniltivdf tkpsteerly iidldkeqvl vssyvahgmr tgdlyakyfs nrkgtlkssd
      121 gffltgesyk gkngfslrly glehgrnnna yertlvihaa ryaeqsfinr ygrlgrsrgc
      181 lavprsengk iieyiqggsv cyvhseglky edyaflnftv adthkkpedv eeiekles
//
LOCUS       WP_010680959             512 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Acetivibrio cellulolyticus].
ACCESSION   WP_010680959
VERSION     WP_010680959.1
KEYWORDS    RefSeq.
SOURCE      Acetivibrio cellulolyticus
  ORGANISM  Acetivibrio cellulolyticus
            Bacteria; Bacillati; Bacillota; Clostridia; Acetivibrionales;
            Acetivibrionaceae; Acetivibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Acetivibrio cellulolyticus"
                     /db_xref="taxon:35830"
     Protein         1..512
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=58972
     Region          66..>510
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mdkiamksdn lkqinieria qffpnvitev rddsgklkra idfdllkqel tseivdgene
       61 ryqvswpgkk eairlsnips dkvlrpiked svdwentqnl yiegdnlevl kllqesymnk
      121 ikciyidppy ntgkdfiykd dfsmgttqyf akcrqdencn rlsedsevhg rfhsgwltmm
      181 yprlklarnl lqddgvifvs idnnelynlq wmmneifges nyvetfiwtk tctppslsnk
      241 srktaeyvlc yekninniky ygdkldngda pllntgnpir vlnfpkgtik ftfcrdgsfk
      301 agnydkvevl ndfdvrdgvn ysevslkgaf kwtdefllne ikngtyfiik sskfsirfqr
      361 vdtegryktp tnmldvelnk ingigtnesa vkelehlgmg rcfdypkpvs likkiinmiv
      421 kdekeaivld ffsgsattah avmeinayda grrkyimvqk peqvpadsia ykagyrdicq
      481 igkericraa kklkeesgid idygfrvyrl ds
//
LOCUS       WP_010682225             507 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Methylobacterium mesophilicum].
ACCESSION   WP_010682225
VERSION     WP_010682225.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..507
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=53581
     Region          1..506
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mssypvitlr pddgvvvarg aiesgtavtd gvtvaeripa ghkvavrshr vgepvtkygq
       61 iigfakadia agqhvhvhnl gmgdfardya fgvdarptrl vappatfqgi rrpdgrvatr
      121 nyvgiltsvn csahvadlia dafrrhpilg ldplaeypnv dgvvalthkt gcgmamgepl
      181 rllrrtlagy arhvnfshiv miglgcevnq igafleeqgl gdrirsmniq slggtrrtve
      241 agiafvkgil aeanvvhrep vpaselival qcggsdgysg vsanpalgva sdlvvrnggt
      301 vilsettety gaehlftrra vspevgqklv dlmhwweeyt rkegseidan pspgnkaggl
      361 ttilekslga makagstnlv dvvryadpvt akgfvfmdtp gydpvsatgq vagganlvcf
      421 ttgrgsvfgc kpspsikiat nsamykrlee dmdvncgtil egaetveqag qrifdlilrv
      481 aggertkseq fdfgssefap wqigatv
//
LOCUS       WP_010682366             434 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Methylobacterium mesophilicum].
ACCESSION   WP_010682366
VERSION     WP_010682366.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..434
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=46167
     Region          6..394
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mtpvllvlna gssslkfqvf asddaagpcr lfrglfeglg gsahliirdg tgsvvaearf
       61 drggafghee allhvsawlg eqsggfrlia aghrivhggt tysepvrvdt qvlealerlv
      121 plaplhqphn lepirilqrr lpdlpqiacf dtafhagqpe iarlfavpha miergvrryg
      181 fhglsyayia svlaeydpal aagrvivahl gsgaslcaln rgasvattmg fsaldglpmg
      241 trcgsldagv vfymlremkl gpdeaermly tqsgllgvsg isndmrtlrs vavtdpdarr
      301 aidlfvyrig relgslvaal ggidalifta gigendaatr aevlrgaawa gftldeaana
      361 sgsprvtrgs gpsawviptd eelmiargtr avlaqhessr prptlratgd rhgsveneaa
      421 drsrtrrrnl hvgr
//
LOCUS       WP_010682644             356 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Methylobacterium
            mesophilicum].
ACCESSION   WP_010682644
VERSION     WP_010682644.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            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="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37548
     Region          10..287
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mpalppefaa aadrsacraa iragsrsffa agqllpgdvr eaayglyafc rlsddlvdea
       61 agsadrhdav arltdrigra yagqpvdapa drafaevvtt haipealpra liegfawdad
      121 grryadleal qayaarvags vgammalimg arsadalara cdlgaamqlt niardvgeda
      181 rmgrlylpln wmaeadldpe tfladprpsp alaalvarll aeadrlyasa nagiealppr
      241 crpairaasl iyaeigriva angfdsvsgr arvtagrkla liaratrphr vgsdlgapal
      301 paaaflieav tsephgglrp raalrpwwdl ggrvvhvldl iermrereaf grsaps
//
LOCUS       WP_010684732             699 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Methylobacterium mesophilicum].
ACCESSION   WP_010684732
VERSION     WP_010684732.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 699)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..699
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=71292
     Region          12..699
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 marelshdlg pslfrperva vvgasddvsk ttarplrflr rsgfagavyp vnprretvlg
       61 erawpsiesl petpdhafvl aptegvpeav aacvargvpl vsvlaggfge vgeagrarea
      121 eltailagsr trllgpnsig ivnvntglvl tanaafaept lprgglfvas hsgsmigail
      181 srglakgigf agfvstgael dlslgeicaa tlddplidty alflesiahg rairsfalaa
      241 aargkaviay klgrsaqgae lsqshtgaia gedgiadafl kdcgicrvet legliegpam
      301 lrragpaaps gagatrrpqv avvtttggga amvvdqfglr dvavmspsae tmaalaargv
      361 aaapgrivdl tlagtrpavm raaletllaa pefdvvvava gssarfqpel lvpgiveaaa
      421 garkplvafv apeapealar lagagipcfr tpeacgdvva avlgrrpakp mteartspar
      481 prqldeaegy avldrlgipv aphavvapda ttspigypaa vkllsadvlh ktelggvvlg
      541 vrdddglrea lvriardvpr aapevaverl lvqemaqgvg evllslrrdp eagpvvmlaa
      601 ggilaeihrd rslrlapvdr aealamigev raigalagyr grprgdldal adavvaisra
      661 gpeiveaein plivrraghg vvavdavvrc asaqggaga
//
LOCUS       WP_010685099             426 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Methylobacterium mesophilicum].
ACCESSION   WP_010685099
VERSION     WP_010685099.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            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="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=45812
     Region          9..426
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mfkeaaqleh eiatpfvgga pdqfatqala tkrasenyts atfmgwrren grvgvrnhvv
       61 llplddlsna aceavannvk gtmalphayg rlqfgedldl hfrtligigs npnvaavvvi
      121 giedqwtnrv vegiaktgkp vvgfgieghg diaivakasy qakrfvqwat elqreecpia
      181 dlwvstkcge sdtttglasc ptvgnmydkl iphgiygvfg etseitgaeh lcreraispe
      241 isdkwytmwk ayqddvieah ktddlsdsqp tkgniagglt tieekalgnl ekighecrfi
      301 dalqpaeapa kgpglyfmdt ssaaaecvtl maaagyvvht fptgqgnvig npivpvikit
      361 gnprtvrtmg ehidvdvsgv ltremtipqa gdalidmvvr tangrltaae slghrefvmt
      421 klyrsa
//
LOCUS       WP_010684971             667 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Methylobacterium mesophilicum].
ACCESSION   WP_010684971
VERSION     WP_010684971.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 667)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 667)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 667)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 667)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 667)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 667)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..667
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=71478
     Region          47..667
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msqifapgva aqpasdards aptsdadgqg plqgpatsgt ldapekaetq hghagfwtll
       61 vgsvgvvygd igtsplyafr ealgpartdg illpeevigt vslilwalfm ivtvkyvail
      121 lrmdnngegg ilslmalark alggsrivfm lgllgaslfy gdavitpais vlsaveglkl
      181 vtpalddyvl pitvviival flvqnrgtgk vaaffgpmti vwflamalaa lphialhpev
      241 frainpvhav vyllghgtga lvalgavfla vtgaealfad lghfgrkpiq vawiglvfpa
      301 lalnylgqaa lvlekpdtad pffqlvpawg llpmvllatl atvvasqavi tgafslsrqa
      361 iqlgllprle irhtseshag qiylpqinsl lmigvvllav lfktssslas aygiavtgtm
      421 lltasltflv mwrmwkwspv aaaavmlpfi vleflfllsn likvveggyv plllagglii
      481 lmwtwvrgvt ilfnktrktd vplvelvgml ekspphhvrg tavfltsdpe iapaallhnl
      541 khnkvlhekn viltvetvdt prsneadkvr iepvgphfyk vvmkfgymet pnipktlvll
      601 rrqgfkfdim atsfflsrrs irpaahsgmp lwqdrifitl aknandatdf fqiptgrvve
      661 vgtqvtv
//
LOCUS       WP_010685909             645 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Methylobacterium mesophilicum].
ACCESSION   WP_010685909
VERSION     WP_010685909.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium mesophilicum
  ORGANISM  Methylobacterium mesophilicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 645)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 645)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 645)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 645)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 645)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 645)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..645
                     /organism="Methylobacterium mesophilicum"
                     /db_xref="taxon:39956"
     Protein         1..645
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68337
     Region          14..645
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 msqsiapaan ppveagetep ahgrlkagli lgalgvvygd igtsplyafk eavkaatsgg
       61 asvpaaatga vslilwslil ivslkyavli lradnrgegg ivamlallga rqarpgtwka
      121 lllvvglvga allygdgait paisvlsaie glkvdapalg pyvvpitlvi liglflvqhk
      181 gvaaigrvfg pvmlvwfvvl allgvggivg spgilaaanp lravdfmlha gvhvsfamlg
      241 aaflavtgge amyadlghfg alpiraawfa lvlpalvlny fgqgalllae pdalenpffh
      301 lcpdwahlpl ialatlatii asqaiisgvf sltqqsvqlg flpamrivqt areergqiyv
      361 pmvnwllaaa tlvavvmfgs sdalagaygi avsmlmgitt llaalialrw gynpvlvvav
      421 ngvflmidav flaansvkil eggwfplvla glvalmmltw kkgnelveea rvalrlsedv
      481 flsglqhrdl lrlpgtaafl saaehgiplh lsrfvernha lmeriliita lyeetpsvpr
      541 errahvtila pdfyrvilry gfmeeasipe glsravesrh lpphvlddmt vfvghetiip
      601 kkdkrgmapw renlfafmqr naertgaffg vptrqvvevg teiei
//
LOCUS       WP_010687889             124 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Leuconostoc gelidum].
ACCESSION   WP_010687889
VERSION     WP_010687889.1
KEYWORDS    RefSeq.
SOURCE      Leuconostoc gelidum
  ORGANISM  Leuconostoc gelidum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Leuconostoc; Leuconostoc gelidum group.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 124)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 124)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Leuconostoc gelidum"
                     /db_xref="taxon:1244"
     Protein         1..124
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=13974
     Region          2..124
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(7..10,41..43,46,69,106,120)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mikifvdaar niqtgqstag aviitnnkqr qlksdlphtq nnqeaeflal iwalktldnt
       61 tdmiqlysds qilidaihkk yakhyqiyvd eistlvschk lflsqwlpek enlgahnlal
      121 qalk
//
LOCUS       WP_010688099             370 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: exonuclease SbcCD subunit D [Ligilactobacillus].
ACCESSION   WP_010688099
VERSION     WP_010688099.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus
  ORGANISM  Ligilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Ligilactobacillus"
                     /db_xref="taxon:2767887"
     Protein         1..370
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42016
     Region          1..259
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          259..342
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkflhtadwh igkrlheypl vkeqqdaldq iaqiaqkeqv davvvagdly drslpseeav
       61 tlvnqalknl nlkadlplla isgnhdsavr latgqewfkq tklylhtkla eaftpiefad
      121 tqffllpyfe lqearnyfad eslsdltsam klivaklktk fdptkkqvlv ahffaagslr
      181 sdsetkievg gldsvppelf sdfdhvalgh lhdkraldlp tvkysgsllk ysvaeansqk
      241 gvwivetepf sckwipldpl ndirrleasy aelttklyqt vaeddyvaie ltdeheiidv
      301 mnklrkyypr ivelkrkkrl vhtkqaekie sktplelftd ffvqatgqep tqlqqkwake
      361 sllalkkege
//
LOCUS       WP_010688387             398 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Ligilactobacillus animalis].
ACCESSION   WP_010688387
VERSION     WP_010688387.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..398
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43790
     Region          3..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mekimiinsg ssslkfklfn nethetlasg iierigihgs kikvkygdgq kyeldheitn
       61 hlqgiellln vlkelnliad lseikgighr vvaggeyfsq pvvvdndvia kikelaelap
      121 lhnpanlngi kafrkylpna lsvavfdtaf hqtlpqenym ystpyewyek ygvrrygahg
      181 isheyvarka aelmgrpfed lklitchlga gasitavkhg rsfdtsmgft plsgiqmatr
      241 agdvdislan yimkklnvqs msdmvyllne ksgflgvsgv sadmrdveda aaagnkrael
      301 aiklfynsil ryvgqyitem ggvdgivftg gigenspets eeimkrlaym gvtineaenk
      361 krgaetiisg pdstvtvmri ptdeeymiaq hvwellge
//
LOCUS       WP_010688433             213 aa            linear   BCT 20-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein
            [Ligilactobacillus animalis].
ACCESSION   WP_010688433
VERSION     WP_010688433.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 213)
  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 213)
  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 11443421
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..213
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=22468
     Region          69..213
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          167..211
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
ORIGIN      
        1 mfkseqfkhg ytrkdeprmr keffvergnd pvqrekatqt dkpakrvnsk vilallalvv
       61 lvfggvfwyq ktqasnatka kgnsasiakv ssqkkaasls esktkalsak easqkaases
      121 aqkaaeesqr kqaaassesa akassesaak assesaasls saqadaqtin vadgdtlesl
      181 aakyattvek iqelnnlgss vdltagetly vpk
//
LOCUS       WP_010688498             391 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Ligilactobacillus animalis].
ACCESSION   WP_010688498
VERSION     WP_010688498.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus animalis
  ORGANISM  Ligilactobacillus animalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..391
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42971
     Region          3..388
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mpkillmnag sssvkwklfe ltdesvvakg lvermlapgs kfeikygdqt yqeiqdnlsy
       61 ekaaemiiek iqeleitsla dikcvghrvv aggtkftqat kmdqaaikev lalsdhaplh
      121 npmeakyiel mqqvmpdtpq yavfdsqfft qmpeenaifs lpyeltqkyg irrygehgis
      181 heylaqktad llekpladlk litlhlgsgs svsavkdgka fassmgftpl tgltmgtrag
      241 dvdpsivlfl mkkldktade vlelfnqksg llglsgysdd mrdikanqad qrcklaldvy
      301 lnkivsyvgs yfaqlggadv lvfaggigen npwlradvcq rlaclgvqld qelneanheg
      361 vistetskvk vmlvptneel amvqqikaql d
//
LOCUS       WP_010688591              81 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyl carrier protein [Ligilactobacillus].
ACCESSION   WP_010688591
VERSION     WP_010688591.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus
  ORGANISM  Ligilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
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   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 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   4  (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 10011594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Ligilactobacillus"
                     /db_xref="taxon:2767887"
     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=9011
     Region          3..78
                     /region_name="acpP"
                     /note="acyl carrier protein; Provisional; PRK00982"
                     /db_xref="CDD:179197"
ORIGIN      
        1 mtkeeilnkv qeivseqldv daadivltad ikedleadsl dvfeimnele deldiqlead
       61 esiktiqdvv dhvakqlean d
//
LOCUS       WP_010690218             350 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Ligilactobacillus animalis].
ACCESSION   WP_010690218
VERSION     WP_010690218.1
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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Ligilactobacillus animalis"
                     /db_xref="taxon:1605"
     Protein         1..350
                     /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=39360
     Region          1..285
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mkkridwidi vravgmflii mghtlevyty sivgklifav hvpvffvlsg ylykekpfkk
       61 vfkggnvnll lpylatliiv viitrfnfif pnwiydldmr nfwvsalygs gttlnpfwdk
      121 sltinaigai wfllamyfgn iifdliikss rgnlyivgim vtiitfsgfy lsdtgillpw
      181 slnaalasql fyyggylirr fdligkygml gciiggvlwi isaqsgflyl niahadspil
      241 avlggiggsl tlmylakllc etkvnlkavk yygqmslivl cvhlidlnsf aisgkiygtl
      301 aqttgnqifa vsmeilyrff ltvvgiiiip klpivrsfyl nrtypffvrk
//
LOCUS       WP_010692319             397 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Treponema denticola].
ACCESSION   WP_010692319
VERSION     WP_010692319.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            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="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43332
     Region          1..397
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkilvincgs sslkyqlidm tnedvlvkgl verigiegsr ikhekkgmda vlieekmndh
       61 kkaiqlvlea lidknhgvvk smdeitavgh rvvhggeefn ksvllddrvm agikecidla
      121 plhnpanimg ieackalmpk tpmvavfdta fhqtmpaeny iyalpyeyye kykirrygfh
      181 gtshrfvsek asetlknnsa dfkvitchlg ngsslaaikg gkcvdtsmgl tpleglvmgt
      241 rsgdldpail pfimnkekls addmsnvlnk ksgvlgisgv ssdfrdieta akegnkraql
      301 aldvfcnrvr kyiasyaaql ggvdalvfta gigensielr ekichglefl gveldseknk
      361 vrgkltdask asskvkvlii ptneelmiak dtmalvk
//
LOCUS       WP_010692371             606 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Treponema denticola].
ACCESSION   WP_010692371
VERSION     WP_010692371.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 606)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..606
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=67235
     Region          2..586
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mihkrltgsv pkskkwills alsswisllc ntaitfvtvr fifglynfsl dkktvfvlls
       61 aasaaliirv iavrkrsyfs yragtevkrt lrsmlydkfi slklnysqyi smaevtqigt
      121 dgieqldsyf gaylpqfffs maapvtlfii lapinffaal vlfvcvplip lsiaaiqtva
      181 krilkryldv ytglgdsfld slrglitlka ysddeaqhre lnaeaenfrr itmrvltmql
      241 nsifvmdtva yggtalgtiv slyqlragnl siegallfil lcaefflplr algsffhiam
      301 ngitaanrlf elmdvksdsa svlsgdelee takkikraqp vsqpdslqgn lpslevknln
      361 fnynasryav knasleflkp gfygiagesg sgkstaaall mglqknysge illsgieakk
      421 lpdefrakym nlvstesflf gasvrenlli anpsasdeel msvlkkvlld efilnrnssg
      481 dgnsgldfyi esggknlsgg qvqrfalara llhdadiyif deavsnidve seelilstly
      541 elsktkiiif ishrlanien adhiyvfekg eikeegthsn liekngiyar mylqqqnlek
      601 irmgvk
//
LOCUS       WP_010692681             133 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Saccharopolyspora spinosa].
ACCESSION   WP_010692681
VERSION     WP_010692681.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..133
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=14786
     Region          <38..128
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mlardgqnvr snnaceptsg twtsayngqq ltdpsaidid hmvplanawr sgankwddqr
       61 reqfandmql pqlvavdass nrskgdqdps qwkperanwc syatswitvk hsydltitep
      121 eqkalqemla tcg
//
LOCUS       WP_010692721             187 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein
            [Saccharopolyspora spinosa].
ACCESSION   WP_010692721
VERSION     WP_010692721.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
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   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
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   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..187
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20859
     Region          92..172
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(105,124..125,143,146,154..155,164,169)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mtleaafrep vgpespearp ledgavievt arfvvpqrdl atlerdfark lrsladvpdq
       61 stveiqarpe aprlrslpap teaalrilva prrvvradgt nidftrlefd lllflcenpg
      121 rvhrrgslln avwhlnstps trtvdvhvrr irsklgpdld littvrgvgy rmdrttdvhi
      181 epdpyas
//
LOCUS       WP_010693239             354 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Saccharopolyspora spinosa].
ACCESSION   WP_010693239
VERSION     WP_010693239.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..354
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37423
     Region          241..328
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 mdvddiasrf aselfthqgk legkvgevqr aqaalesaan aiqhqreahq kaadkllsnw
       61 eseatdgfqk katkfdqdlt atadasakga kivaevtkal dgrhsavgsl vedfitkagq
      121 viqagvavag vaapaglmra vaevadlagg yikqsggelk dardemaeaa rklralleev
      181 dsdgvadpek qlrkpgedga eggedgpgkg kgsskadeil hnagkhigyh egpnnqnkwg
      241 psgqpwcayf atsmwreagv dipkygytgd vykwgeqhgt aygqhdllkn aqpgdallfg
      301 tgpghgqseh igliekvegn kittiegnsg dqvarrtytl pkdadrfygg vhpk
//
LOCUS       WP_010693598             699 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Treponema denticola].
ACCESSION   WP_010693598
VERSION     WP_010693598.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 699)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..699
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=77776
     Region          8..626
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mkkirrlffi sipvffivlf fiylgvfkqa eyffyddrmn rtasyfspsd eivlvlvdqk
       61 slnyaaserg wtwpwpreay aeivdffsgg gaksvafdml ftesssygda ddkkfadask
      121 esgiviqtvf fdrvqgntqs wpdsapkpep idetslskng lgpakelpgi fpideiassa
      181 klignvnslp dsdgtirrar lfyswknyki ptlgiasyfv ggdedealpe elnlrftksi
      241 ddylpysagd ilkaqadira greselrped fedmyvffgl yapglfdicq tpvsasypgv
      301 gihitlldni lsgnrivktg flinaliili ciilaglpei fsekiksraa sisinavsfl
      361 vfvalylfia yylfrlgiai paasvlagmv lsfvaslavs ymvegkqrry lknafkqyls
      421 pavieqliad psqlklgger keisiffsdl qgftsisesl spealtelln dylsdmskii
      481 ldsggtidky egdaiiafwn aparvehhar saveaawacq kkleerradf ekraqgrpfk
      541 mriglntgfa ivgnmgsvsr fdytmlgdsv nlaarlegln kqfgsytmca eaakkqaees
      601 gtilkfrela raavvgksep vvvyevmdek tynekkalld sfdrglkefy agnfkealni
      661 faqteeadpp skhyaekckt lisqkpegew lgiwkadtk
//
LOCUS       WP_010693693             428 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Treponema denticola].
ACCESSION   WP_010693693
VERSION     WP_010693693.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..428
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=49613
     Region          4..>420
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mgvftwegkd ralselnlll knqnkfsfte nkvksfnsey aknlyieadn lyallflqkd
       61 ykdkikiiyi dppyntgkkf tyadnfqskt ewmnylyvrl slaktlltdd glifisiddk
      121 acphlriild eilgtenfis tlvwnnstgg glrkkhints heyiilyakd ktkvksmtap
      181 mtekakkmyk yrdadgrffr yqqfawknkt dakrqkypik tpdgnfiipk agyiyrfvek
      241 sffnlleknl iefkksdksv ftdikgrptk wtiyvktyle kkeetvpksl lpaeyvktni
      301 qsvyeqkvlf gakifdyakp vsllkylfkl vpnsddavvl dffsgsatta havmelnael
      361 nenrkfilvq rgepcpedsp alkagfktia elgreriira saliqkrftq ktfgfkylel
      421 sgeqdlif
//
LOCUS       WP_010693979              95 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Saccharopolyspora spinosa].
ACCESSION   WP_010693979
VERSION     WP_010693979.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Saccharopolyspora spinosa"
                     /db_xref="taxon:60894"
     Protein         1..95
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10310
     Region          1..93
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(24,52..53,55)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mdeeaveqvr avvasippgs vlsygdvael aglrsarlvg rilaedggdl pwhrvlrsng
       61 tvadhlrrrq lellraegvl adgaridmrh yrwga
//
LOCUS       WP_010695381             286 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Saccharopolyspora
            spinosa].
ACCESSION   WP_010695381
VERSION     WP_010695381.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora spinosa
  ORGANISM  Saccharopolyspora spinosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            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="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30947
     Region          15..250
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 msedfellvd rqalcgtgll wmsalncvhw vdllrrelht yhrdsgvdev rvlpgavtal
       61 gatrhgqlia aagngfarvy lgraalepvv qvrngdrmsv gacdpagrfv agtlthardl
      121 rasalyvldg drarllvegv tgvgglawsp dgtrmylvdt rtiwvydydv dgaravsgrq
      181 wvvcaesegs pegiavdaeg cvwvamhwtg rihryapsgd letvlwaptr ritslafggs
      241 rleemyvtsa cfgydelglr ddpyagallr fkpgtagvql ppwqgi
//
LOCUS       WP_010696468             801 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Treponema denticola].
ACCESSION   WP_010696468
VERSION     WP_010696468.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 801)
  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 801)
  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 801)
  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   4  (residues 1 to 801)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..801
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..801
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=90153
     Region          71..795
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mmngsaekln ldelefsfpe skirelknng adstivgqdr alkaielglg iegegynifv
       61 mgapgtgrrt vissllqnyk pnfakiqdia yaynfsrpie pialffpage grlfrktikk
      121 avghihtqtl allksegfla eqkkivtktd neenillmef eskmlhagfk vlqikdennq
      181 sldlipiikg keisfselqs kaarkkfseq elaalrekyy asldemself silrdkriem
      241 deklikhqkd svmpiikeal dplrklvdsy ttksdnpkqi ednkkillfl kkaeddlisr
      301 mniyssefks srikknffgr ylinlicenn kdknyvinen lpsftnlfgt ieshsdsdap
      361 einghlrire gavhrafggy livrlhdlle eddswsylkr vlqsgkievq ippsgnhtps
      421 vfkpealpan fkiiiiggey tydilyqedp dfyklfkvca efdsvmqknd kniaslihlt
      481 eylckekkal nfddsgysrl isyaselags rhlltaqftk isdliieadf nakqqkkdti
      541 caavlngtie krrylhslpe ekfaemvhlg eilidvsgrk lakinglave ergyhsfgvp
      601 vsvtaqaspg tggiiniere aglsgeiydk ahliitsllr ekfskdipls isasicfeqs
      661 ysyidgdsas caeflalisa iggfemrqdi avtgslnqhg mvqpvggite kiegffntck
      721 ilgftgtqgv mipvsnknnl flskevkeav kegkfniwti ktidegikll sglqeevytw
      781 misqrleefy kkvneislrk d
//
LOCUS       WP_010697523             102 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [Treponema].
ACCESSION   WP_010697523
VERSION     WP_010697523.1
KEYWORDS    RefSeq.
SOURCE      Treponema
  ORGANISM  Treponema
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Treponema"
                     /db_xref="taxon:157"
     Protein         1..102
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11948
     Region          6..99
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mkpkekkeif nfleynknil qsygvkkigl fgsyihnqqn knsdidilve fhankknynn
       61 finlvyyled nlntkidllt ieslspyigq rilneveyvs iq
//
LOCUS       WP_010698293             428 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Treponema denticola].
ACCESSION   WP_010698293
VERSION     WP_010698293.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..428
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=49505
     Region          4..>420
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mgvftwegkd kalselnlll knqskfsfte nkvksfnsed aknlyiesdn lyallflqkd
       61 ykdkikiiyi dppyntgkkf tyadnfqtkt ewmnylyvrl slaknlltdd glifisiddk
      121 acpylriild eifgtenfis tlvwnnstgg glrkkhints heyivlyakd ktkvkpmtap
      181 mpekakkmyk ykdadgrffr yqqfawknkt dakrqkypik tpdgnfivpk agyiyrfvek
      241 sfinlleknl iefkksdksv ftdikgrptk wtiyvktyle kkeetvpksl lpaeyvktni
      301 qsvyeqkvlf gakifdyakp vsllkylfkl vpnsddavvl dffsgsatta havmelnael
      361 nenrkfilvq rgepcpkdsp arkagfktia elgreriira saliqkrfsq ttfgfkylef
      421 sgeqglif
//
LOCUS       WP_010701519             259 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Bartonella bovis].
ACCESSION   WP_010701519
VERSION     WP_010701519.1
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 11459553
            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="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=29803
     Region          1..169
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mykidynsyr aiqsfnhrir flvmhytavn fetsialltg plvsahylvp dpseetylea
       61 gfkdmrifnl vdenkrawha gisswsehnn lndtsigiei vnlattenev fifppynqiq
      121 idaikelsln ilqrypditp tnvvghsdia igrkndpgas fpwkqlykag igawyddelk
      181 nyyqkefhnc icfekakkqv vaklkqygyd tsdaetecgy knlirafqlh frqenydgil
      241 daettaiiya lvdkyfppe
//
LOCUS       WP_010700469             122 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein, partial [Acinetobacter baumannii].
ACCESSION   WP_010700469
VERSION     WP_010700469.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         <1..>122
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
     Region          <13..>122
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 svsadeiilk qasadriitf ndstatihfg egqlssivfd dgtvwnkaqi eaniigrllg
       61 tdgddhlqad anysviygld gndtiqggvq ndylyggngd dtlisnggsd slyggsgndt
      121 li
//
LOCUS       WP_010701683             200 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Bartonella bovis].
ACCESSION   WP_010701683
VERSION     WP_010701683.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..200
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22796
     Region          2..165
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 milnklkawv vslaqrrtap hwlgliaffe ssffpvpada lcipmalvrp qkayhyalig
       61 tvcstlggvf gwiigfyayd tiakpilefy gkyesfqtfq ndatlkflii llitsglfhf
      121 ppiklvtlls glmgvslplf iiicllargt rfyffawfiq rfgqktldll frhftwfvpi
      181 glilvlltyn lliyklysaf
//
LOCUS       WP_010702705             145 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Bartonella bovis].
ACCESSION   WP_010702705
VERSION     WP_010702705.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..145
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=16004
     Region          57..128
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mkkiaitalt silmvssaya qfslpsehek vlaegivrvk admvagdatp lttdfvvsnl
       61 igvnvynien eeigevkdii lrqnkidgiv isiggffgmg ehyvaispek lqmkrddgkw
      121 klmvnvtkna lkeapkfkye dylir
//
LOCUS       WP_010702941             200 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Bartonella bovis].
ACCESSION   WP_010702941
VERSION     WP_010702941.1
KEYWORDS    RefSeq.
SOURCE      Bartonella bovis
  ORGANISM  Bartonella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Bartonella bovis"
                     /db_xref="taxon:155194"
     Protein         1..200
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22864
     Region          2..166
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 milnklkawv vslaqrrtap hwlgliaffe ssffpvpadi lcipmalvrp qkayhyalig
       61 tlcstlggmf gwiigfytyd tiakpilefy gkyesfqtfq ndatlkflii llitsglfhf
      121 ppiklvtlls glmgvslplf tiicllargt rfylfawfir hfgqkavdfl lrhftwfvpi
      181 glillllayn llvyklyfaf
//
LOCUS       WP_010703590             286 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Bartonella
            schoenbuchensis].
ACCESSION   WP_010703590
VERSION     WP_010703590.1
KEYWORDS    RefSeq.
SOURCE      Bartonella schoenbuchensis
  ORGANISM  Bartonella schoenbuchensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Bartonella schoenbuchensis"
                     /db_xref="taxon:165694"
     Protein         1..286
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32799
     Region          5..278
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mtnflpycld ilratdrdry isvlfapknk rralaalyaf naeiarires vhdpfigeir
       61 lrwwydsian geiknnkhnp ilddllttia lfnlpktafl rycdarvfdl yndpmatihd
      121 leaycsktas tilqlacqil dfdsaqnftk ayehggiaqa lsgilrllsl mqsryqgyfp
      181 sdmlkamgme reelefnhin neqkheiika mvalskdhyl kfyehsitlp ktlkpaflpl
      241 sitpaslqrt mqlgakvfqe natlsqlhry wlitkaamsg rfpkll
//
LOCUS       WP_010705485             146 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Bartonella vinsonii].
ACCESSION   WP_010705485
VERSION     WP_010705485.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..146
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=15783
     Region          58..132
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mkkivcttlm svliassaya qsfpapsape mvsstgivqv rsdvsvryvt platdfvass
       61 liganiynve nenigevkdi ilrenniagf vvavggflgi gesyvvispe tiqmindygk
      121 wklitnatrd slkeaptfky egrwtr
//
LOCUS       WP_010705541             317 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Bartonella vinsonii].
ACCESSION   WP_010705541
VERSION     WP_010705541.1
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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     Protein         1..317
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=36010
     Region          1..225
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 myqidynsyr svksfnrrir flvmhytsln fkesvmaltg ekvsahylvp dpseqtylea
       61 gfkdmrifnl vdeserawha gisswaghsn lndtsigiei vnlatghsvs sdktyvetsl
      121 kdvrilnpvp kdenelqags wtekrhvssp vlplekdhff tcqnegvifp pynptqidav
      181 kelalnilqr ypditptdvv ghsdiaigrk idpgaafpwk elymagigaw ydderkhhyq
      241 eqfcksfpsk edvlaqlkcy gydisiacse igyknliraf qlhfrqenyd gildvetaai
      301 lyalvdkyfp sdlssls
//
LOCUS       WP_010707384             395 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Enterococcus faecalis].
ACCESSION   WP_010707384
VERSION     WP_010707384.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..395
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43263
     Region          2..394
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msktiainag ssslkwqlyq mpneeviakg iveriglkds iftikygegq kyevivdidn
       61 hevavkmlld qlidlnilgs ydeitgvghr vvaggeefkd svvitdevle kiealselap
      121 lhnpanamgi kafkhilpei isvavfdtsf httmpehnyl ysvpreyyek faarkygahg
      181 tshryvsqra aemlgrpied lkiitchlgn gasitavdgg ksvdtsmgft plagvtmgtr
      241 sgdvdasllp ylmtklgltd vqdmvdilnk nsgllgltng lssdmrdiqs nldkpevqta
      301 ynifidrirk yigsyvtvmn gvdaivftag igenavgvrk diidgmtwfg ceidddknnv
      361 hgeeavistd dskiklllvp tdeelmiard verlk
//
LOCUS       WP_010708812             285 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Enterococcus].
ACCESSION   WP_010708812
VERSION     WP_010708812.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
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   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 285)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..285
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34011
     Region          19..73
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
     Region          <227..281
                     /region_name="DnaB2"
                     /note="Replication initiation and membrane attachment
                     protein DnaB [Replication, recombination and repair];
                     COG3611"
                     /db_xref="CDD:442829"
ORIGIN      
        1 mnehrgyyai ipaivrydnh lngnakllyg eltalanekg ycwatnqyfa nlynvskrti
       61 iswlkqleer nyikmqifyk pnskmvdrrh iyilpyptdt efytpseenf itygknhqeg
      121 deenfttpse enftenntli nntknntkni ysveqsstms elfekvwkty pkktnkkkak
      181 eqflkkiksd egferfktgy kaylkyikln dwyhpqelfr wirderfnde ydlsetttqa
      241 rytnppvrqe qlpdwvnepk qeeeklspee qaalkrqiqe lsgge
//
LOCUS       WP_010714303             199 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein, partial [Enterococcus faecalis].
ACCESSION   WP_010714303
VERSION     WP_010714303.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..>199
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
     Region          35..161
                     /region_name="COG3942"
                     /note="Surface antigen [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443142"
ORIGIN      
        1 mkrkslksfi yvsallvfls gfvgvslfvk sevveattig ddypvkwknl plggaiddwr
       61 mytryctsfv ayrlstannf elpsgfgnad rwgteamarg ykvdknpkvg svawwtsthv
      121 awvaevsgdn vkveeynygf dgkyntrwin knsangyihf kdmpqtpvgw ynnghydyyy
      181 yadgtkaigl twvgtkryn
//
LOCUS       WP_010714639             491 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein, partial
            [Enterococcus faecalis].
ACCESSION   WP_010714639
VERSION     WP_010714639.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..>491
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
     Region          47..>491
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 maflkkkkqe qvtnkihnes fqkltevldt dsvdsiypfs wiekkshiet genyiknllv
       61 vdypqsvkga ylsnllkkng niqitkfirp aniermidhl nnsiknktae qmrttdpkrn
      121 atikreiess kkqldkflde ktgfmymymy itlngdsyek iqalekdvkr tltrlrlkth
      181 tptnamresf htvlplnrnf lsaftqqnmd tataghffmf ddseiidltp ntsvfginkn
      241 tdslvavdfn nkektlnknm tiigtsgvgk stlnmrmild nikksirqfi idpedefsyi
      301 tkyyggtvvn istssnikin pfeifseevf ekedetdnet tsdvltenne hesqidtlvr
      361 skigklktff rvlkdeisqt eisvlsstlr qlyqdkgfkg naklsdfkse dyptltelyn
      421 klkdldpeky evlkdltlii edytmehgtt tifdgytnik ldneivtfnl kplqtekdvq
      481 saaylnifsf l
//
LOCUS       WP_010715159             274 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Enterococcus].
ACCESSION   WP_010715159
VERSION     WP_010715159.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            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="formate/nitrite transporter family protein"
                     /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=29346
     Region          2..259
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mdffsseeiv aslgdkaemk gklsfvrlci lgimagfcia lgylafirit gtaptewgsf
       61 nnflggalfp vglialtfvg gelatgnmmv mtlgvlqkkv rvgalcynwi vvlltnclgg
      121 flvaylfghi vgltegafld ktvavaqaki adpplvafvs gigcnifvcl avylgalaks
      181 ylgkmfglwf pvmvfvvcgf qhvvanafii paaifsqsta iswwdylqnt lwvflgnavg
      241 gslfmavpli fmtkpatvkp rvektiqtee lygn
//
LOCUS       WP_010720779             197 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Enterococcus hirae].
ACCESSION   WP_010720779
VERSION     WP_010720779.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..197
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=23347
     Region          16..196
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mqdklkella irdgnlsmke arkfgiaatt vqrfvnkgkl ikvdrgyyve dghgiddlfw
       61 lqqrfsrgif shettldiyq lstnmpkfih ltfphgynvd rsitkeqqlq fhfvkkevye
      121 lgkvegtsfq gnpitmydke rtlcdiwnpr yeieyemkla alkeymedpl rdpsklrdym
      181 tklhvekemk yhmqsly
//
LOCUS       WP_010720891             394 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Enterococcus hirae].
ACCESSION   WP_010720891
VERSION     WP_010720891.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..394
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43867
     Region          2..392
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msktiainag ssslkwqlyq mpeetviakg iverigleds iftikygedq kfekimdidd
       61 hevavkmlld qlialqilss ydeitgvghr vvhggetyad svivdeavmd rieelaefap
      121 lhnpanlmgi kafkkilpdi qsvavfdtsf hatmpkssyl yslpvsyydd fkvrkygfhg
      181 tshryvaera akmlekpiee lklitchlgn gvsitavdgg ksvdtsmgft plagvtmgtr
      241 sgdidpavlp ylmekleidi demvnilnkk sgllgltgls sdmrdlekny eqehihlayd
      301 ifvdrirkyi ggyvttmngv daivftagig endghvrsei ikgmtwfgce idpemnkkrg
      361 eeldistkds kvkvlviptd eelmiardve rlrk
//
LOCUS       WP_010721690             466 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Enterococcus faecium].
ACCESSION   WP_010721690
VERSION     WP_010721690.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 466)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..466
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=51969
     Region          <139..>240
                     /region_name="YoaR"
                     /note="Vancomycin resistance protein YoaR (function
                     unknown), contains peptidoglycan-binding and VanW domains
                     [Defense mechanisms]; COG2720"
                     /db_xref="CDD:442033"
     Region          207..325
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          344..466
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(417..418,421,439..442,444)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mtrsshrkks khvallsalg vllvlisfyt yrstyytkhf lpnteingin vsnltvekan
       61 eklkeaysdk klaikedgkv wqevpkselg ykddftsels pilneqngwt wgmtyvsaae
      121 kqeidpvsqn hqkldttvqt lttkltdlnk drtpttdati ekagdsfvik pevngntidv
      181 daavkqlksa vnsgkdtiel tefkekpkvt sedsslkeql asmnaianvk atysingetf
      241 qipssdimsw ltyndgkvdl dteqvrqyvt dlgtkyntst ndtkfkstkr gevtvpvgty
      301 swtiqtdset ealkkailag qdftrspivq ggttadhpli edtyievdle nqhmwyykde
      361 kvaletdivs gkpttptpag vfyvwnkeed atlkgtnddg tpyespvnyw mpidwtgvgi
      421 hdsdwqpeyg gdlwktrgsh gcintppsvm kelfgmvekg tpvlvf
//
LOCUS       WP_010723342             254 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Enterococcus faecium].
ACCESSION   WP_010723342
VERSION     WP_010723342.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
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
REFERENCE   2  (residues 1 to 254)
  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 254)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..254
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29881
     Region          19..73
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 menkpnfyai lpatvryder lnaiqklfya eisalstkek rcwatnkyfe dvfgvststv
       61 tralngliel gylkrvivyk dgtkeverry lyicetantp iiknditpii kndeenntre
      121 eqykkeqyig esqddcadsr vtkekqlked feklwklypn kkgkelafka ykraikdgtt
      181 nkeiqtgiva ykkqiainht ekqymlhggt ffnqrrwede dlkeivtthk qqetndnfsd
      241 idpmnmqdmf knrf
//
LOCUS       WP_010722400             394 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Enterococcus faecium].
ACCESSION   WP_010722400
VERSION     WP_010722400.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..394
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43845
     Region          2..392
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msktiainag ssslkwqlyq mpeetvvakg iveriglqds iftikygdnq kfeqimdien
       61 hevavkmlld qlielqilss ydeitgvghr vvhggetygd svvidekvmd riaelaefap
      121 lhnpanlmgi kafkkilpdi lsvavfdtsf hstmpkqnyl yslpvsyyed fkvrkygfhg
      181 tshryvsera akllnkpiee lkiitchlgn gvsitavdgg ksmdtsmgft plagvtmgtr
      241 sgdidpavlp ylmekleidi deminvlnkk sgllgltgls sdmrdlekny ekehirlayd
      301 ifvdrirkyi ggyvttmngv daivftagig endghvrsei ikgmswfgce idpalnelrg
      361 eevdistkes kvrvlviptd eeliiardve rlrg
//
LOCUS       WP_010723612             499 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Enterococcus faecium].
ACCESSION   WP_010723612
VERSION     WP_010723612.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..499
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54581
     Region          6..499
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mletlqptmk lnqrdsvvva ltlipkqtql tidqqtittl edipqghkia lgdlkagdnv
       61 ikygypighv ttdvtagqwl hthnvktnls geldyryekd vhpshypfen rtfqgylrkn
      121 gkvgirndlf lvptvgcvng iaelivkqfk ekhpdlgqfd hitilkhpyg csqlgkdhqn
      181 treiladavn hpnaggvlvf glgcenntvp efkkilgeyd eervkflvaq dvydeieqgv
      241 alleelltaa endqrisvpf sklnvglkcg gsdglsgiia npllgafsdy liaqggstil
      301 tevpemfgae qvlmaraene evfdsivdli ndfkqyflsy gepvyenpsp gnktggittl
      361 edkslgctqk sgsspvvdvl qygekirkpg lsllqapgnd lvaasalass dcqlvlfttg
      421 rgtpfgsyvp tvkvstnttl ferkghwmdf nagvlleqpm evilesfvqk iiavasgeet
      481 kneqndvrei aifkngvtl
//
LOCUS       WP_010727322             499 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Enterococcus faecium].
ACCESSION   WP_010727322
VERSION     WP_010727322.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..499
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54571
     Region          6..499
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mletlqptmk lnrrdsvvva ltpipkqtql tidqqtittl edipqghkia lgdlkagdnv
       61 ikygypighv ttdvtagqwl hthnvktnls geldyryekd vhpshypfen rtfqgylrkn
      121 gkvgirndlf lvptvgcvng iaelivkqfk ekhpdlgqfd hitilkhpyg csqlgkdhqn
      181 treiladavn hpnaggvlvf glgcenntvp efkkilgeyd eervkflvaq dvydeieqgv
      241 alleelltaa endqripvpl sklnvglkcg gsdglsgita npllgafsdy liaqggstil
      301 tevpemfgae qvlmaraene evfdsivdli ndfkqyflsy gepvyenpsp gnktggittl
      361 edkslgctqk sgsspvidvl qygekirkpg lsllqapgnd lvaasalass dcqlvlfttg
      421 rgtpfgsyvp tvkvstnttl ferkghwmdf nagvlleqpm evilesfvqk iiavasgeet
      481 kneqndvrei aifkngvtl
//
LOCUS       WP_010727566             271 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Enterococcus faecium].
ACCESSION   WP_010727566
VERSION     WP_010727566.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            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="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30996
     Region          1..248
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mkadlhvhsc ysngffhpke llslataqei nhlaivdhht fagieavkev ffespvnlie
       61 gieisafdlk rqkhvrilgy nlsnrsyikq lcrpllhfqt nqtlfklkkl qaegyhlkee
      121 elwkeaekat alypchlyrl lkkrgygtkm dhtfyqklmt aeevsdnrkk invydaieai
      181 kygggltvla cpgkfdnydl ipelasfgid glekyhpahr irdlkilsdl iktyhfscfg
      241 gsdfhgirgt tgfgrtlitd arefpdqlly n
//
LOCUS       WP_010728271             271 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Enterococcus faecium].
ACCESSION   WP_010728271
VERSION     WP_010728271.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            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="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31044
     Region          1..248
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mkadlhvhsc ysngffhpke llslataqei nhlaivdhht fagieavkev ffespvnlie
       61 gieisafdlk rqkhvrilgy nlsnrsyikq lcrpllhfqt nqtlfklkkl qaegyhlkee
      121 elwkeaekat alypchlyrl lkkrgygtqm dhtfyqklmt aeevsdnrkk invydaieai
      181 kygggltvla cpgkfdnydl ipelasfgid glekyhpahr irdlkiltdf iktyhfscfg
      241 gsdfhgirgt tgfgrtlitd arefpdqlly n
//
LOCUS       WP_010730322             197 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Lactobacillales].
ACCESSION   WP_010730322
VERSION     WP_010730322.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillales
  ORGANISM  Lactobacillales
            Bacteria; Bacillati; Bacillota; Bacilli.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Lactobacillales"
                     /db_xref="taxon:186826"
     Protein         1..197
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=22826
     Region          13..196
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mdllekpvyn yikknhgvit frdieelnfs yqqlnqlvsk gkvesiergi yhlpdtyidd
       61 ffslqyrfpk giysletalw lhglsltvpf epvmtfpfgt ntrlmkeagv kpivarnhhe
      121 igiiklerqa gqfisvydme rtlveclrta yhvdvqviap afqayfkkgt vnyakmyhya
      181 klfnvteklq syvevls
//
LOCUS       WP_010732757             321 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus faecium].
ACCESSION   WP_010732757
VERSION     WP_010732757.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
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
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            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="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=36583
     Region          5..312
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mtkliefkhv qkkydgkyvi ddltlaineg eifvlvgpsg sgktttlkmi nglskpsagd
       61 iyfkgkslne ynlqkmrwnm gyvlqqialf ptmtvkqnie vipemlgwek qkradrvdel
      121 lqkvglspdi yrdrmprels ggeqqrigii raiaaspdvi lmdepfsald pisrnslqel
      181 vlslheelgt tivfvthnme eaiklgdria fmkdgeiiqc dtpeqllmnp kneyvrhffd
      241 epkqtkewrv edlvvngyfl kevpknshqq vcldtplkev ysllsvypni vivekgknig
      301 sltskevftf lsreeeenen i
//
LOCUS       WP_010732827             253 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Enterococcus].
ACCESSION   WP_010732827
VERSION     WP_010732827.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            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="formate/nitrite transporter family protein"
                     /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=27305
     Region          1..252
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mhtpeeimei sihlgakkiq kpilaklilg figgamislg ylayvrvsas ipesmaslts
       61 lvgasvfpig llvillggge litgnmmava iafmdkkvtf lqlvknwsvi tfaniigaif
      121 vayffghfvg lthsgvyldq vihiadhkia vswwqalgsg igcnwfvgla lwlsygakda
      181 agkvltiwfp vmifvaigfq hsvancfvip aaifegqatw leflsnfipv yigniiggai
      241 fvsgfyyvsy khh
//
LOCUS       WP_010734034             298 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Enterococcus mundtii].
ACCESSION   WP_010734034
VERSION     WP_010734034.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..298
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34156
     Region          13..282
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 miktnqelfe khaddfayce tmikkysksf yaafsqlpee kaksvyaiya fcrladdtvd
       61 lahseeella lkhqldafsm gkipdepiwr alsvvfsvyp mtlspfydmi agqkqdlvft
      121 qpetladled ycyyvagsvg lmllpllsdq aekiqsqakr lgeamqltni lrdigednkm
      181 griylpkemm rahgvtetml qadkpakpli dlweaianea ekkyetsftm lpfidrncql
      241 altaaamiyr eqlsvirenn yfmldrknyv sqirkiqllr kakkyvetli nspqqstl
//
LOCUS       WP_010734171             501 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Enterococcus mundtii].
ACCESSION   WP_010734171
VERSION     WP_010734171.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..501
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54819
     Region          9..501
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mtdpdfstri iqlhpqdsvv vatttiptnt tlrfddvtlt nfeeiplghk ialsdlstga
       61 dvikygypig hlltdvkagq wihthniktn lsgeesyqyq pksrpivypq enrtfqgylr
      121 edgqagirnd lfiiptvgcv ngiaeliiqe fkkrhaddnp fdhltilkhp ygcsqlgkdh
      181 entkkilada ihhpnaggvl vfglgcennt iqelkaslnk ynkqrvkflt aqdvtdeiah
      241 gvslleelae iarrdfrvpv pldkltiglk cggsdglsgi tanpllgafs dylisqggst
      301 iltevpemfg aeqvlmarae nqevfesivr lindfkqyfl synepvyenp spgnkaggis
      361 tledkslgct qkagnstvvd vlaygdkvrk tglslleapg ndlvaasala sadcqlvlft
      421 tgrgtpfgsy vptlkvstnt plferkqhwm dfdagelltq smaevlplfi dkiirvasge
      481 etkneandvr elaifkngvt l
//
LOCUS       WP_010734689             278 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Enterococcus mundtii].
ACCESSION   WP_010734689
VERSION     WP_010734689.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..278
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31662
     Region          1..251
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mkadlhvhsy fsdgssspee llklalnhhm nilsvvdqdt saglahirqv fapspinfie
       61 gievtaydfk rrqqvhilgy nllnyqyieq lceplraart rntlrqlrri qtegfrikee
      121 qvrqfakqat alykqhimsa likagydtsi dghlyrklfk yndfgqeeae midvyeviqa
      181 iklcggmsvv ahpgkldsfe lipelasfgi dgiekyhpeh slkdqrkvqe lvdrfnihcf
      241 ggsdfkgkng pdyfgecama nvrefpdell ldahmkan
//
LOCUS       WP_010734237             372 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Enterococcus mundtii].
ACCESSION   WP_010734237
VERSION     WP_010734237.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..372
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42859
     Region          1..258
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          260..348
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrflhtadwh igkklqgydl lkeqehvlse iltiakkekv daiviagdly drsipaveav
       61 eifnrlmidw nlnekfpifa isgnhdssvr lsagtewfsq tkfflhtrfa eafqpidyqn
      121 tqffllpyfe pisarsyfed dtirtvqqam ekvvdqmqla fdpekkqvlv shffvtgskk
      181 sdsetkievg gldaipgsll epfdyvalgh lhnqaalqqe narysgsplk fslseinqkk
      241 gvwivdltdt lvldfqeitp lydiaevtas fkelldpsfy htinrenylq iylkdravip
      301 nmmnqlraiy prilgvervn grhcstskrq tleikqpkkl aetfftemvd epmteqqmsw
      361 leetlqelte te
//
LOCUS       WP_010735877              74 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyl carrier protein [Enterococcus].
ACCESSION   WP_010735877
VERSION     WP_010735877.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 74)
  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 74)
  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 74)
  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   4  (residues 1 to 74)
  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 10011594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..74
                     /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=8417
     Region          1..74
                     /region_name="acpP"
                     /note="acyl carrier protein; Provisional; PRK00982"
                     /db_xref="CDD:179197"
ORIGIN      
        1 mvfekiqeii aeelgkdtee iklttniqed leadsldlfq iineiedefd vkietedgik
       61 tvqdlvtyve kqta
//
LOCUS       WP_010737077             394 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Enterococcus].
ACCESSION   WP_010737077
VERSION     WP_010737077.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            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="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43881
     Region          2..392
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msktiainag ssslkwqlyq mpeetviakg iverigleds iftikygedq kfekimdidd
       61 hevavkmlld qlialqilss ydeitgvghr vvhggetyad svivdeavmd rieelaefap
      121 lhnpanlmgi kafkkilpdi qsvavfdtsf hatmpkssyl yslpvsyyed fkvrkygfhg
      181 tshryvaera akmlekpiee lklitchlgn gvsitavdgg ksvdtsmgft plagvtmgtr
      241 sgdidpavlp ylmekleidi demvnilnkk sgllgltgls sdmrdlekny eqehihlayd
      301 ifvdrirkyi ggyvttmngv daivftagig endghvrsei ikgmtwfgce idpemnkkrg
      361 eeldistkds kvkvlviptd eelmiardve rlrk
//
LOCUS       WP_010737250             289 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phytoene/squalene synthase family protein
            [Enterococcus].
ACCESSION   WP_010737250
VERSION     WP_010737250.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            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="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33569
     Region          15..279
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mitinndpfq eyqkdfayce siikknsksf ylafsqlpkr kaqsvyavya fcrraddlid
       61 rdnnqaglrq lerqlldfne gkvpndpvwr alsvvfdnfp mvtapffdml tgqrkdadfk
      121 qpetrkdlee ycyyvagsvg lmllpllter padivvpakk lgeamqltni lrdvgedyqm
      181 griyltkedm trfgvattml kekqaqtqlv alweslakqa enlyeesfem fplitedcrq
      241 alasaafiyr eqlnivrkqh yslfdnknkv shyrkvqllk evksylksy
//
LOCUS       WP_010738882             612 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Enterococcus faecium].
ACCESSION   WP_010738882
VERSION     WP_010738882.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..612
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=69605
     Region          39..>481
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mssqpekvkv pklevdaell nelqelfkka ddqkerydft wngkakaffe aatpstktlr
       61 pqpeesvnfe ntenlfitgd nlealkllqe sylgkidfiy idppyntgkd fvyhdnfsks
      121 vkeadeaegn vdedgnrlvk nersagrfhs dwlsmmyprl klarnlladd avifisiden
      181 evanltllmd eifgesnfvt nfvwekkkkp sflnanignk feyilcyakd rsnskafsve
      241 tttkgkkypf nnagnspqel ifpphsvkft smgdqlvsaq dmsagnikte llndfsivng
      301 tneqeihlyg ewrysqqkln elvnegseit issipfrpnl tksggeikkm hnlltkeqyd
      361 vgmnedatde ftklmggnyf dyakptklik tliksytydn dnavvldffv gsgttaesvm
      421 qlnnedggsr kyivatldea isddnpakqd gydsidqiar erirrasdll edksgfrvlk
      481 idnlgirddv fkpaddtiqa nimdlignyr ddrtdydlly dvlvdgaley nrqisketie
      541 nqeiikydyf gelsgvicyf gkeltdeltr eiakmrplia vfkestfsks sqkvnvleqf
      601 rinspdtkvk vi
//
LOCUS       WP_010739199             128 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ribonuclease HI family protein [Enterococcus].
ACCESSION   WP_010739199
VERSION     WP_010739199.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 128)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 128)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..128
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=14204
     Region          2..125
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(7..10,37..39,42,68,107,121)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mlkvytdaat naeksgggil iiaekqkqla islpetdnhq aelavilyal tyliehqlnd
       61 qtillysdsk taikildqgq tknklfqpyl sefnelapqf pllvlqwipe gknkgadnla
      121 rqglrkkl
//
LOCUS       WP_010741198             336 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Enterococcus].
ACCESSION   WP_010741198
VERSION     WP_010741198.1
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 10007593
            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="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=38952
     Region          5..274
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mstitkpnre ylydnirgil illvvlghal eyfrldnkvg eflyvfiylf hmpvfifisg
       61 yfsknlakgr stavetflvp ylllnmilsl imlaigkine fmilspgwtl wylycmfiwr
      121 lllpdlvkvr rililsfivg ifsgfltefg tymamartlg flpyflagyf mdrsmlekih
      181 rlrwrkfisf giilaglgva yfwvqtalpp eilwrdrsfl lfklplyqnv lnnvllylvg
      241 fafvfvflsl aapkphffts wgqktlaiyl lhvylvsplv eftqyvkdpl lhlillvagt
      301 llilyllsrp kvtttlqkti arilhfimpn kngdss
//
LOCUS       WP_010742004             283 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Enterococcus].
ACCESSION   WP_010742004
VERSION     WP_010742004.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 283)
  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 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   3  (residues 1 to 283)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 283)
  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   5  (residues 1 to 283)
  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   6  (residues 1 to 283)
  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 12204073
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31866
     Region          21..101
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          127..281
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mewldhlnts iayveenltg kieleraaql aqcssyhyqr mfsyiadvtl geyirrrkms
       61 lagvdlqrge kvvdvagkyg ydsptsfnrv fksihgmtpk eakqsgaklt sypmltfklt
      121 vkgvqameyq lidkdafqvt gfglklaqdm eaaqkripef wnevsssgql eqliphmdqn
      181 npgvmgislm tsevqdawey vigvasndtt eefaqyeipa akwavfsgtg pmpgaiqelq
      241 qqvftewlpt sgfeyaelpd ielylnmepe naqfqvwlpv rak
//
LOCUS       WP_010743128             469 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Enterococcus malodoratus].
ACCESSION   WP_010743128
VERSION     WP_010743128.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 469)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..469
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=53013
     Region          63..168
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          315..448
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(396..397,400,421..424,426)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkeyesqrvl rivgvvagam affllvyayf gshfyfgstv anvdvgglsv aaaekkirqe
       61 tkqveielkg enqtiklqla spytlqkgyl krnirrgevs lplkkgakdd lidainrasf
      121 lggkeakrak ivyandrfki epekkgtvid svkirkelck didegtlqte yaladfyrep
      181 evtakklqkq kilqkleevq nrgiklkmtn ksvplteqml aasvdeqgnf dqdlilswva
      241 elerehstiy ksvdftnihg qhlryknign ygwfidikes akkitkklke petqiiqlvl
      301 rgetkkqplh itknyievdl dnqkmycfnq gkkvvetdvi tgrydkgtat vpgfhtimdk
      361 rrnvdlsgvl stgdgtynvp vdywlpllsy gqtiteiglh dtdhklqyfg qpgayqtdlg
      421 sygcvntpka qvaqiydnsf igmpvfiygh iyddapgefd kpveygtei
//
LOCUS       WP_010742058             258 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Enterococcus
            malodoratus].
ACCESSION   WP_010742058
VERSION     WP_010742058.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus malodoratus
  ORGANISM  Enterococcus malodoratus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Enterococcus malodoratus"
                     /db_xref="taxon:71451"
     Protein         1..258
                     /product="formate/nitrite transporter family protein"
                     /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=28153
     Region          9..248
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mddyslllqv gqnkftffqk tpmkffvksi lagiylgvam slslalggii atinpnlaki
       61 afamffgltf vliiflngel ftgnclttif piynkkqsls sllkmwgncl lgnavgisiy
      121 svlfirsral stiiipylan lveakqhftl eslliksilc nfivciatyv alkikedlak
      181 tfimlvvimt fvvcgfdhci aniglflmqa msggtalsgs lvfqnilfsi vgnvlggsvm
      241 maaplyfvlc ptnlnmrr
//
LOCUS       WP_010743654             189 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Enterococcus].
ACCESSION   WP_010743654
VERSION     WP_010743654.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            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="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20519
     Region          2..189
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mkkrivigvs gasgiiyaid likrlkadst iethgiisdw akqnlklese vslkelegml
       61 dyhysnrdlg aavasgsflt dgmvivpasm ktvagismgf gdslisraad vslkeqrkli
      121 lvpretplna ihlenltkla rlgvqiippi pafysqpkti edivahqsmk lmdalgienh
      181 vsgrwkdnd
//
LOCUS       WP_010744909              86 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein, partial [Enterococcus
            raffinosus].
ACCESSION   WP_010744909
VERSION     WP_010744909.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus raffinosus
  ORGANISM  Enterococcus raffinosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 86)
  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   2  (residues 1 to 86)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Enterococcus raffinosus"
                     /db_xref="taxon:71452"
     Protein         <1..86
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          22..85
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 geeiprlkea tvesdgsigg esqekinint adatelqkls gigekkatdi ikyreengsf
       61 naiddltkvs gigektlenl kdsiti
//
LOCUS       WP_010745158             576 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein/permease
            [Enterococcus].
ACCESSION   WP_010745158
VERSION     WP_010745158.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 576)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..576
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=64594
     Region          2..553
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 midrrlfaia kkktlilqvv irciglglsl yiwrtlalll sqvmqglsle lsrpfglill
       61 alagklilir lsanltdqas aelrvalrkq vmekafrlgn tsrqlpattl aqlagdgieq
      121 lemyyahflp qlfycllasl mlfaylvsla wqpavamlic vpfipltima vmkiakrils
      181 kywddytnlg trfheslsal svlkaydqdd akqrelaada qkfrkatmsl lsmqlnsiti
      241 mdifsysgaa lgiglaliaf qqqyltvygv llfilvgaef flpmrqlgsl fhvamngiss
      301 cgkifdylal pekndgtike wtesldtvtv kqltftyekq qsqainavsi tlkkgtftaf
      361 vgksgsgkst faqlllnqld dyqgrihwnq telkdlnrst vlekamlvnt kdflyadsir
      421 enlllakssl tdtelwqlle qvkladfvrq lpeqldtvle engknlsggq rqrlilaral
      481 atsaelyifd eitsgvdies eeiilhtlkk laqqaivifv shrlynvlea drvyvfkegt
      541 vveagtpqel eqtsdyfkay fieetrqmkg vteneg
//
LOCUS       WP_010745245             336 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Enterococcus].
ACCESSION   WP_010745245
VERSION     WP_010745245.1
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 10007593
            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="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=38835
     Region          5..274
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mstitkpnre ylydnirgil illvvlghal eyfrldnkvg efiyvfiylf hmpvfifisg
       61 yfsknlkkgr stavetflvp ylllnliltl imlaigkidq fmilspgwtl wylycmfiwr
      121 lllpdlvkvr rililsfiig ifsgfltefg tymamartlg flpyflagyf ttpelvsrvr
      181 ktpfrkiisi giilfglvta ffwtknnlpp ellwrdraya ffpvpllqnl ltiiflygig
      241 fafifvflal vnnkphffta wgqrtlaiyl lhvylvaplv eftqfednav lhlillvags
      301 gfityllshp kvteilrktl srilhfimpn kngdss
//
LOCUS       WP_010746155             158 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Enterococcus].
ACCESSION   WP_010746155
VERSION     WP_010746155.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 158)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..158
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17390
     Region          5..157
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mtwknqeake eaykllllqq kallegetdl ianlanssal lnqtlqdtvf agyylfknde
       61 lilgpfqgnv scvhiamgkg vcgeaaeknq tlivdnvleh knyiacdsaa rseivvpmkk
      121 gnsligvldl dsseigmydq idrfyleqyv slllenig
//
LOCUS       WP_010746835             469 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Enterococcus].
ACCESSION   WP_010746835
VERSION     WP_010746835.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 469)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..469
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=53102
     Region          <124..>196
                     /region_name="YoaR"
                     /note="Vancomycin resistance protein YoaR (function
                     unknown), contains peptidoglycan-binding and VanW domains
                     [Defense mechanisms]; COG2720"
                     /db_xref="CDD:442033"
     Region          315..448
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(396..397,400,421..424,426)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mgehenrvvl rivgvvagam tvlmlifvyf gshfyfgstv anvavgglsi nkaekkirqe
       61 tkqveirltg enqtvklqit spyriqkeyl kknirkgefs lpykkeakee liqavnaasf
      121 lggkeakdak iiykdkkfqi ipeksgtvvd svrirkelsk afdegnlqaa ydladfyrep
      181 eltakdlkrk kipqkletvk drgimlklnk kkiplteqml ansiddqgnf dqalitewva
      241 dlereystiy ksvdftnihg qhlqyknvgn ygwfidikes tkkitkalkk sdtktiplvl
      301 kgdtkkqplh itknyievdl dnqkmycfnk gklvvetdvi tgrynkgtat vpgfhtimdk
      361 rrnvdlsgvl ttgdgtynvp vdywmpllsy gqtiteiglh dtdhklqyfg qpgayqtdlg
      421 sygcvntpka kvaeiyeysy igmpvfiygh iyddapgefd kpveygtei
//
LOCUS       WP_010751033             133 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Enterococcus villorum].
ACCESSION   WP_010751033
VERSION     WP_010751033.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 133)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 133)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 133)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..133
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=14837
     Region          2..128
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(7..10,40..42,45,71,110,124)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mlkvyidast kgnpgpsggg ilivhenkqe qlsiplskgs nhqaefevfl ktleflkekg
       61 lnnetilcys dskvlvstvd knhtenssff cylekikqll pnfhllilqw ipenknkgad
      121 nlarqalqkq lka
//
LOCUS       WP_010751213             321 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus villorum].
ACCESSION   WP_010751213
VERSION     WP_010751213.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus villorum
  ORGANISM  Enterococcus villorum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
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
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Enterococcus villorum"
                     /db_xref="taxon:112904"
     Protein         1..321
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=36742
     Region          5..312
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mnrliefkqi qkkygekyai kelslsideg eifvlvgpsg sgkttslkmi nglsqpsvge
       61 iffkgkslke ynlqkmrwqm gyvlqqialf ptmsvkqnie vipemigwer kkreqvvdql
      121 lekvgldpki yrnrmpqels ggeqqrigil ralaaspevi lmdepfsald plsrsslqdl
      181 vlslhqelgt tivfvthnmd eaiklgdria vmkdgeliqc dtpeqllasp knnfvrsffd
      241 etiqqkqqtv kdlvlakcys qnqhhsnqpf vylstplnev ykllsqheii tiqennewig
      301 evtrkdilty lsrkerenek i
//
LOCUS       WP_010753201             156 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Enterococcus asini].
ACCESSION   WP_010753201
VERSION     WP_010753201.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 156)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..156
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16911
     Region          4..152
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mswdeaekka ayellllqqa glleaednwl anlanssall nqtlketvfa gyylfngeel
       61 ilgpfqgkvs ctrikmgkgv cgesaakeet livpnvkeha nyiscdgtam seivvpmikd
      121 gkligvldid agvtamydei dqeylekyva lllgsn
//
LOCUS       WP_010753879             138 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Enterococcus asini].
ACCESSION   WP_010753879
VERSION     WP_010753879.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 138)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 138)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            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="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=15271
     Region          2..128
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(7..10,40..42,45,71,110,124)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mikayidast kgnpgpsggg illvdgqaqq qlhfplpilt nhqaefavle qllthlieae
       61 qtaetimvys dskvlvstid knhtnnsdfq ayliriqsll ahfpllilqw ipekqnkgad
      121 hlarqglqka lllqnrrq
//
LOCUS       WP_010754680             265 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Enterococcus asini].
ACCESSION   WP_010754680
VERSION     WP_010754680.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..265
                     /product="formate/nitrite transporter family protein"
                     /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=28736
     Region          9..257
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mnpvsplfek idtsiekkvd lieksyprya lraifacmfl glgtavafgi gmkadhiapg
       61 lgkmlyafmf swslvmilym naelgtsnml ymtvgvyrkr igvplalkil fscilfnlig
      121 gvlfgfliah tgpfqglead nffftsiaak ldkssiqilv egmfanivvn tavlvsmrmk
      181 ddagkvaaii fiififaflg yehvianfpa ftmafvasgg tiegmtvasv lhnlffalig
      241 nyiggglvmg lgfawlnnsk ssyvd
//
LOCUS       WP_010754893             468 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Enterococcus asini].
ACCESSION   WP_010754893
VERSION     WP_010754893.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus asini
  ORGANISM  Enterococcus asini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 468)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..468
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=51275
     Region          <8..>68
                     /region_name="PknB_PASTA_kin"
                     /note="Stk1 family PASTA domain-containing Ser/Thr kinase;
                     NF033483"
                     /db_xref="CDD:468045"
     Region          <129..>219
                     /region_name="YoaR"
                     /note="Vancomycin resistance protein YoaR (function
                     unknown), contains peptidoglycan-binding and VanW domains
                     [Defense mechanisms]; COG2720"
                     /db_xref="CDD:442033"
     Region          224..327
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          346..468
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(419..420,423,441..444,446)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 msrtsrhkks gkkkyvliai lvvlaalttg ygvnasnyse rflpntkinh tdisdltvae
       61 ankklkaatd dtkftitdng qewksislsd lgmktdfsge lknlledqnq wgwgmayvft
      121 ndssdvnglt ldkdelnaaa atiqgelntl nesrtkttna tltkgdsgft itpevngnsv
      181 nvdnvikdlk dfvskdksgl elmdytekpt vlstdeslqt emnklnqiaq iqanytinge
      241 tfqiptesis swlqytdgei tldrdqvkay vaslgdkynt stnptkfkst krgevsvpag
      301 tlswtiqvdt etdalveail ageaftrtpv tkgsstaaep migntyievd menqhmwyyk
      361 dgavaletdv vtgkpttatp agvnyiwekk tnetlkgkne dgsdyatpvd ywlpidwsgv
      421 gihdsswqaa yggdryltyg shgcvntppd vmktlyetve egtpvlvf
//
LOCUS       WP_010754922             334 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Enterococcus asini].
ACCESSION   WP_010754922
VERSION     WP_010754922.1
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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Enterococcus asini"
                     /db_xref="taxon:57732"
     Protein         1..334
                     /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=38845
     Region          5..274
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 msiiskqsrd lafdnirgll iflvvfghal eyfrlsfpfa qflyvfiyff hmpvfifisg
       61 yfsknvqrgr eqavrqfllp ylllnlilsl imlaigkidq ililnpgwtl wylycmfgwr
      121 lllpdlirvr hvfilslivg alsgfltefg tymamartfg flpfflagyy ctpahiekir
      181 hfpyrrllsi lvlviglita ffwvksgtpa eilwgdraya llelplwqtl padiylyals
      241 fafifvfltl gqakhrfytt wgqrtlsvyl lhvylvaplv eftekitnpv lhlsllfggs
      301 llilwllsrp vvtkqlqlvl qrvthfimpn kekr
//
LOCUS       WP_010756028             158 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Enterococcus pallens].
ACCESSION   WP_010756028
VERSION     WP_010756028.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 158)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..158
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17303
     Region          9..158
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mswnsqeeke aayqlmleqq kallegetdl ianlanssal lnltlkdtvf agyylfkege
       61 lilgpfqggv scvhiplgkg vcgeaaeknq tlivedvtkh pnyiacdska kseivvpmkk
      121 gdqligvldl dsseigmydq idqfyleqyv alllqnvd
//
LOCUS       WP_010757036             290 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Enterococcus pallens].
ACCESSION   WP_010757036
VERSION     WP_010757036.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus pallens
  ORGANISM  Enterococcus pallens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            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="formate/nitrite transporter family protein"
                     /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=31944
     Region          29..287
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mksnltmeid eeamensksn apsqtvvkyf plmsqldksi kkkkelldns fpryavrsmf
       61 aclflalgta iafyiairtq eaipglekms yafmfswslv milfmnaelg tsnmlymtvg
      121 vyrkkisvsf aakllftcil fnliggvlcg yllsltapfs hleagnymft giasklakpt
      181 vqilvegmfa nivvntavlv smrmkddagk vmaiifiifi faflgyehvi anfpafslay
      241 fashgtiegm naasvlhnlf ftlignfigg glvmglgyaw lnktetsyvd
//
LOCUS       WP_010758286             336 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Enterococcus pallens].
ACCESSION   WP_010758286
VERSION     WP_010758286.1
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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Enterococcus pallens"
                     /db_xref="taxon:160454"
     Protein         1..336
                     /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=38834
     Region          5..274
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mstitkpnre ylfdnirgil illvvlghal eyfrlenkvg qflyvfiylf hmpvfifisg
       61 yfsknlekgr rtavetflip ylllnvflsv imlalgkiee isilspgwtl wflycmfiwr
      121 lmlpdlvkir yvlllsfivg ifsgfltefg tymamartlg ffpfflvgyy adqkliknlr
      181 ripyskvisi giiifavita ylwtrnnlpp ellwrdrayn afsvpllqnl ltiiflygmg
      241 fafvfvfitl annkphlfsa wgqrtlaiyl lhiylvaplv qgteyienpv iqlivlvcgs
      301 llilyllsrp kvaatlqktl arilhfimpe kkddsp
//
LOCUS       WP_010761973             249 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010761973
VERSION     WP_010761973.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            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   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 249)
  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 249)
  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 249)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..249
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28655
     Region          143..230
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(160,179..180,199,203,211..212,222,227)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mnntigllhi rddseqsnhi ellikrdlne qqyslikite keqigtldgl vihlekasgy
       61 vkafqwlidi qedhslfiwi lcgekgselp klypllskns vieiiesdqg iealgikikn
      121 alnyknhlln reepkkisdh hfldpaklsl vvhdkiialt rkefkiiell yenldnvvty
      181 dqindaiygt stgealekyr vanfifhirs klkkqsyfei eiirtrgyll tsakngrfll
      241 kgrsdkvlq
//
LOCUS       WP_010762303             241 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010762303
VERSION     WP_010762303.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            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   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 241)
  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 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   5  (residues 1 to 241)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..241
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27663
     Region          141..235
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(160,179..180,196,206,214..215,227,232)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mynigiipve elknstyteq fsktryrlyp ltkaeictka sqmdaliiee splvglkstc
       61 elilelrrna kaliwvvska vtktskivyl qlgadgvvdt etekeefllq fsnilsrftn
      121 eqetenktfs yavqesfqrq lklipsnlsi vvegkeislt qlefqtiall lenigravty
      181 eeifaavwqd kyadnqlenk qyrisnlifh lrkkmeidig hpnyiktvrs kgymlmntkn
      241 a
//
LOCUS       WP_010762517             229 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010762517
VERSION     WP_010762517.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 229)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 229)
  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 229)
  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 229)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Enterococcus haemoperoxidus"
                     /db_xref="taxon:155618"
     Protein         1..229
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26645
     Region          138..227
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(157,176..177,195,198,206..207,219,224)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mynigfvlld nedeqkyids lkstqlnvyp inkneiteki ghydgiilne qnaqnigvic
       61 elllllkkkq dpfiwvisqq snkmnhivyl qlgadgiidq ecdpeeckll mfnafdrynr
      121 aypiaeeptd kmvdtqkiql rpcnysvlln geeinltkle fktiefletk kgvavsyeei
      181 ykkvwenegn dkqyrvsnli fhlrqkieed aahpkyiktv rskgykltv
//
LOCUS       WP_010763126             269 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Enterococcus
            haemoperoxidus].
ACCESSION   WP_010763126
VERSION     WP_010763126.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus haemoperoxidus
  ORGANISM  Enterococcus haemoperoxidus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            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="formate/nitrite transporter family protein"
                     /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=28885
     Region          2..259
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mdfessqevv tslgdkalak sqlsffrvsv lgimagffia lgylsfiris gtmpkswggf
       61 stflggclfp iglvaltfvg gelatgnmmv mtlgvlqkki rtkaliynwl vvlvtncigg
      121 clvayffghv vgltegafle ktlsvaqaki ddtmlvafvs gigcnifvcl avylgamgks
      181 ylgkmfglwf pvmvfvvcgf qhvvanafii paaifsnash iqwpdyllnt ivvflgnavg
      241 gslffavplm fvnaekkeas epdglyeky
//
LOCUS       WP_010763743             572 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Enterococcus
            moraviensis].
ACCESSION   WP_010763743
VERSION     WP_010763743.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..572
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=64365
     Region          2..552
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 midkrlfrlt dktnlfklvi arllnlvlsi fmwltiakql anylnsgkvd dkrlvvvlig
       61 vllfkilltk wmeqltyqas selrlamrka vmekafrlgn gqgqlsaasl aqlsvdgieq
      121 leiyyarflp qlfyclfasl liflslvgfa wqpalillvc mpliplvims vmkiakrils
      181 gywnqytdlg akfhenlsgl stlkaydqde ikqveaanda ekfrnvtmsl lsmqlnsiti
      241 mdivsycgaa vgiglalfay qqeqltlvgm lmfillsaef fipmrqlgsl fhvamngisa
      301 ckklftylel peqeygevtl sssldqlkie hvdfryagse alalndvsll ikrgeftafv
      361 gqsgsgksti vrlllhqlsq yegriywnqd elktlsqeti qqtaslvdnh gylypttike
      421 nlllgnkkas ddelwqvlek vqladfvqql pkklseplne nganlsggqr qrlllarall
      481 kdaqlyvfde itsgidlase qiilsclqel aktnsvifis hrlynvlead qvivfedgrv
      541 iesgspaqlq resvyfknyf kqeqamingg eq
//
LOCUS       WP_010765599             379 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Enterococcus moraviensis].
ACCESSION   WP_010765599
VERSION     WP_010765599.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus moraviensis
  ORGANISM  Enterococcus moraviensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Enterococcus moraviensis"
                     /db_xref="taxon:155617"
     Protein         1..379
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=43389
     Region          1..264
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          261..353
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrflhtadwh igkklhgydl leeqvdafqq ilaiakneev daivvagdly drsvpsveai
       61 evfnqmivem nlqekfpvla isgnhdsstr letggpwfvq sdfhlntrld qafqpvemgn
      121 tqffllpyfe pisarlffdn eeirtieqam qevikkmkeq fkpdmahvlv shffvagsek
      181 sdsetklmvg gldtvplsll esfdyvalgh lhgknalqae narysgsplk fslsemnqkk
      241 gvwivdtqps ettfefkelt plrdvkqieg gfkeltsqtf ydsinrenyl hiqltdravi
      301 pnmmnqlrki yprvigverl fgreerqkqt etkkevktla pvelvdqffs evtgesltqq
      361 qqrwieenlg aihqaergk
//
LOCUS       WP_010768017             265 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Enterococcus
            phoeniculicola].
ACCESSION   WP_010768017
VERSION     WP_010768017.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..265
                     /product="formate/nitrite transporter family protein"
                     /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=28850
     Region          9..257
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mnpvsplfek idssiekkvn liensyirya vramlaclfl tlgtaiafai amkgesmvhg
       61 lgkilyafmf swslvmilym naelgtsnml ymtvgvyrkk iklpmalkil ftcilfnlig
      121 gvifgylvsl tapfqnlpvd nymfegitak lekstvqilv eamfanivvn tavlvsmrmk
      181 ddagkvaaii fiififaflg yehvianfpa ftlayaasng glaamtagsv ahnlifalig
      241 nyiggglvmg lgyawlnnsk snyvd
//
LOCUS       WP_010769925             253 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Enterococcus
            phoeniculicola].
ACCESSION   WP_010769925
VERSION     WP_010769925.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..253
                     /product="formate/nitrite transporter family protein"
                     /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=26994
     Region          1..250
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mlnpgeilqq sikmgsqkie kpllaklilg figgamislg ylayirvsas isvelpsias
       61 lvgasvfpig livillagge litgnmmavs saffakkvtl meliknwlvi tlanivgaif
      121 vayffghfvg lthtgafqaq visvaqhkve ssflqafvsg igcnwfvgla lwlcygakds
      181 agkilgiwfp vmvfvaigfq hsvanafvip aaifeggstw mdfiqnfipv ylgnivggav
      241 fvsgfyylsy nhh
//
LOCUS       WP_010770643             220 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Enterococcus
            caccae].
ACCESSION   WP_010770643
VERSION     WP_010770643.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 220)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 220)
  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 220)
  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 220)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..220
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25311
     Region          134..218
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(150,169..170,188,191,199..200,210,215)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mhkigvvtle kensqaihql lnesnyiavk isdksqikdl dgiildvgkd ncfsqvcewl
       61 ihcqiapqvf iwvilpnini reinmylhlg mngcmleene tnelplmlkn tfsrifsgyp
      121 eeekkkregi vlndtnmcav inggkeiplt rseyqilqil ykqkgstvsy qtiyetlwnk
      181 qanddlyrva nlifhlrkkl gmqgeqyiqt vrtkgyrlig
//
LOCUS       WP_010771498             333 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Enterococcus
            caccae].
ACCESSION   WP_010771498
VERSION     WP_010771498.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..333
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37485
     Region          1..294
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mklfvdiqkk lrdhqlkvkf eiesttfgil gasgcgksml lkciagietp dsgriylgdr
       61 vlfdkekkid lppqqrkvgl lfqqyalfph ltvyknlssv tknhalilel laifhlenvk
      121 dsyprqlsgg qkqrvalari lasdpellll depfsaldts lkeelqlevq krlsnfkgnv
      181 livshsldel yrlcpllgim tesglvkget tdlfkqpqtv eaarltgckn ifpikridsh
      241 tvqvygvktp livtaevpva cryigirahd mlvndsgvnr ldvkfvssqk tpfeqnawfv
      301 wneldlwwkg skqieantik hfslspeaim vlk
//
LOCUS       WP_010772386             131 aa            linear   BCT 20-JAN-2025
DEFINITION  ribonuclease HI family protein [Enterococcus caccae].
ACCESSION   WP_010772386
VERSION     WP_010772386.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus caccae
  ORGANISM  Enterococcus caccae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 131)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 131)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 131)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Enterococcus caccae"
                     /db_xref="taxon:317735"
     Protein         1..131
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=14621
     Region          2..128
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(7..10,40..42,45,71,110,124)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 mlriyvdaat kgnpgpsggg ivlvgdhlhe qihvplgecs nheaefkvfi kalqltiekk
       61 lnnqtvvihs dskivvqtie kqhaknllfq pylktfqqle qnfalllvkw lpenqnkgad
      121 slarqalqky q
//
LOCUS       WP_010776766             499 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Enterococcus faecium].
ACCESSION   WP_010776766
VERSION     WP_010776766.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..499
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54577
     Region          6..499
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mletlqptmk lnrrdsvvva ltpipkqtql tidqqtittl edipqghkia lgdlkagdnv
       61 ikygypighv ttdvtagqwl hthnvktnls geldyryekd vhpshypfen rtfqgylrkn
      121 gkvgirndlf lvptvgcvng iaelivkqfk ekhpdlgqfd hitilkhpyg csqlgkdhqn
      181 treiladavn hpnaggvlvf glgcenntvp efkkilgeyd eervkflvaq dvydeieqgv
      241 alleelltaa endqripvpl sklnvglkcg gsdglsgita npllgafsdy liaqggstil
      301 tevpemfgae qvlmaraene evfdsivdli ndfkqyflsy gepvyentsp gnktggittl
      361 edkslgctqk sgsspvvdvl qygekirkpg lsllqapgnd lvaasalass dcqlvlfttg
      421 rgtpfgsyvp tvkvstnttl ferkghwmdf nagvlleqpm evilesfvqk iisvasgeet
      481 kneqndvrei aifkngvtl
//
LOCUS       WP_010773846             300 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Enterococcus faecalis].
ACCESSION   WP_010773846
VERSION     WP_010773846.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            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   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 300)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..300
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33633
     Region          33..87
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mstkqnelqd klavegvnan gygvmpklvm qdkrltieak siyayivsfa gagstafpsl
       61 rkiledlqis ekrfykhrkl lidcnyisvt qirnekkeii knlytlisnp kieeevqdeg
      121 irqndcdpip qfngypisqn drhksnslki nnikddddin nacegkltne nfssyskqks
      181 vdcpltvrer lttvlkgkdy laplavslla agvsdadcle iiqfivtlpv ineevsdlvn
      241 aqiranetea ktngltsyka yfitglkqkl enadifvqet nivnpdtikp lptvtmhnwv
//
LOCUS       WP_010778974              92 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: zinc ribbon domain-containing protein [Enterococcus].
ACCESSION   WP_010778974
VERSION     WP_010778974.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 92)
  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 10577258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..92
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10433
     Region          6..89
                     /region_name="Zn_ribbon_2"
                     /note="Putative zinc ribbon domain; pfam12674"
                     /db_xref="CDD:463667"
ORIGIN      
        1 meemtycqsc gmpltsgthg tehdgsqnke yclycykhga fvddhtmeem iaislthmke
       61 agileeqgkt eeealafmnd ffpelkrwkk ss
//
LOCUS       WP_010780496             158 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Enterococcus].
ACCESSION   WP_010780496
VERSION     WP_010780496.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 158)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..158
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17427
     Region          5..158
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mswknqeake eayklllmqq kallegetdl ianlanssal lnqtlqetvf agyylfkege
       61 lilgpfqgnv scvhiamgkg vcgesaeknq tlivenvmth knyiacdsaa rseivvpmkk
      121 gdqligvldl dssevgmydq idqfyleqyv alllenve
//
LOCUS       WP_010779309             285 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Enterococcus gilvus].
ACCESSION   WP_010779309
VERSION     WP_010779309.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..285
                     /product="formate/nitrite transporter family protein"
                     /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=31388
     Region          31..277
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mksdlfmeie etpasenekh vkphsdlmaq leysiskkmd lfnsslprya vrsmlaclfl
       61 algtaiafyi airmqeaipg lekmayafmf swslvmilfm naelgtsnml yttigvykkm
      121 msvsfavkll ftcilfnlig gvlcgyllsl tapfghlepd nymftgiask ltkstgqilv
      181 egmfanivvn tavlvslrmk ddaakvmaii fiififaflg fehvianfpa fslayfashg
      241 tiaemtagnv ahnlfftlig nfiggglvmg lgyawlnnte skyvd
//
LOCUS       WP_010781745             462 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Enterococcus gilvus].
ACCESSION   WP_010781745
VERSION     WP_010781745.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus gilvus
  ORGANISM  Enterococcus gilvus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 462)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Enterococcus gilvus"
                     /db_xref="taxon:160453"
     Protein         1..462
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=51751
     Region          62..150
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          <116..>188
                     /region_name="YoaR"
                     /note="Vancomycin resistance protein YoaR (function
                     unknown), contains peptidoglycan-binding and VanW domains
                     [Defense mechanisms]; COG2720"
                     /db_xref="CDD:442033"
     Region          307..440
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(388..389,392,413..416,418)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mvrivgvvag amaffimiyl yfgshfyfgs kvanvevggl sipaaaekir ketevveikl
       61 kgdhqtvqlq leapydiqkd ylkknvrrgd vrlpfkkgar knlvmalnsa sflggkeakd
      121 atviytnkqf kiqpekvgta vdsprlikel casfdkgelq tsydltdfyk qpaitkgdle
      181 kqkvtqrleg irkrgiklkl nkqtipltee mlsasvdeqg aidlgavtew vaelerkyst
      241 iykpveftnv hgqrlryknv gnygwfidik qsakkivhel kdpeaqtial vlrgntktqp
      301 lrvtknyvev dldnqkmycf dkgklvvetd vitgrydkgt atvpgfhtim dkrrnvdlsg
      361 vlttgdgtyn vpvdywlpll sygqtiteig lhdtdhklqy fgqpgafmtd lgsygcvntp
      421 kanvaqiydy sfigmpvfiy ghiydeapge wdkpveygta vg
//
LOCUS       WP_010770196             490 aa            linear   BCT 20-JAN-2025
DEFINITION  response regulator transcription factor [Enterococcus
            phoeniculicola].
ACCESSION   WP_010770196
VERSION     WP_010770196.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus phoeniculicola
  ORGANISM  Enterococcus phoeniculicola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 490)
  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 490)
  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   3  (residues 1 to 490)
  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   4  (residues 1 to 490)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 490)
  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   6  (residues 1 to 490)
  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   7  (residues 1 to 490)
  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 14435958
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Enterococcus phoeniculicola"
                     /db_xref="taxon:154621"
     Protein         1..490
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=57782
     Region          4..124
                     /region_name="REC_YesN-like"
                     /note="phosphoacceptor receiver (REC) domain of YesN and
                     related helix-turn-helix containing response regulators;
                     cd17536"
                     /db_xref="CDD:381091"
     Site            order(9..12,15..17,20,106..107)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381091"
     Region          395..478
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mykvllvdde ymilmglski ipwkdygfei aataenakda lailekesid lvitdvtmpe
       61 msglefieaa qnqrytfefm ilsgyqefdy lksglqlgai nylmkpvnkt eliesllrvk
      121 erleerieqk nqqeiyrefl lsqwvneeld egeeqevftf lgestgpwrv ilgqfkreyr
      181 kqfsewlnrk nqpfyyfrnl gelvyfvivy qegesiepft rftqelflet nwvmsisqpt
      241 neveeipeiy rfirqtyqlh qfygmqtthi llpqeesgqd slidlsefnr lvtlnkpaal
      301 keavqkvfqe vltlgtsped vrhiafllfm diyrqvgqld desylatiqt inkamtvnel
      361 eklllklide qkepvaysen vqkvlaiiee qyqeeltlkr isdelhlnvm ylgqlfkket
      421 krsfsqflnq hrmekaqsml lhsekninei adeigynnst yfskmfkkmy gvspkeyres
      481 iergtldkke
//
LOCUS       WP_010783032             267 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Enterococcus faecalis].
ACCESSION   WP_010783032
VERSION     WP_010783032.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            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="formate/nitrite transporter family protein"
                     /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=29244
     Region          9..242
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mksgsplfeq idksidkkvn lfsnsfsrya vramlaclfl tlgtavafai aikgegishg
       61 lgkmlyafmf swslvmilym naelgtsnml ymtvgvyrkk vnfslaakil ftcilfnlig
      121 gvlfgflvsl tvpfqdlpkd sffftsiagk lekttlqilv eamfanivvn tavlvsmrmk
      181 ddagkvaaii fiififaflg fehvianfpa lslayfasng aieaftagnv vhnlfwafig
      241 nfiggglimg lgyawldkdn knltyfd
//
LOCUS       WP_010784184             446 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein, partial [Enterococcus faecalis].
ACCESSION   WP_010784184
VERSION     WP_010784184.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..>446
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
     Region          52..135
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 mrknkkiwaf lgillvvmsf sfksgvvnae dkvigddypa kwknlplgat tddwgmatry
       61 ctsfvanrls venkfdirrd gldwnanqwg nnarrqgykv dmiprrgsva ywnsmyhvaw
      121 vaavdgdrvl ieeynygytg rynsrwiskn svdgyihfkd issspekqai nkyititkdg
      181 qdffeniect tkkaktvrgr iyyvkiaykl sngqllysvy edekgtawig ylrqgsseft
      241 qletfnrkkv sltnnattlw kdlnyqgklg msvagnaytv nrvfynstnn asyhelyrgn
      301 tfcgyvnsga vkdittqtvn kystiteanq difgnielts tkgktergri yyttigynlg
      361 dgsvlyslyk detaaewvgy vkenvfeytp ietfdkkqvi ltnstttlwk dlnyqgklgm
      421 svagnaytvn rvfynstnna syhely
//
LOCUS       WP_010784469             300 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Enterococcus faecalis].
ACCESSION   WP_010784469
VERSION     WP_010784469.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            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   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 300)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..300
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33707
     Region          33..87
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mstnqnelqd klavegvnan gygvmpklvm qdkrltieak siyayivsfa gagstafpsl
       61 rkiledlqis ekrfykhrkl lidcnyisvt qirnekkeii knlytlisnp kieeevqdec
      121 irqndcdpip qfdgypisqn drhkinsfki nnikddddin nacesklthe nfssysnqng
      181 vdcpltvrer lttvlkgkdh laplavslla agvsdadcle iiqfivtlpv ineevsdlvn
      241 aqiraneiea ktngltsyka yfitglkqkl enadifvqet nivnpdtikp lptvtmhnwv
//
LOCUS       WP_010786389             123 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Glaesserella parasuis].
ACCESSION   WP_010786389
VERSION     WP_010786389.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 123)
  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 123)
  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   3  (residues 1 to 123)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..123
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14561
     Region          15..117
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mqpysrdlkp lsqklrstqt eaerklwqri nrdqllgfrf nrqkpllsyi vdfyclkakl
       61 vieldgsqhy epdyqekdrl rdaelnslgf tvmrfdnhsv mtnidgvvea iyqylseikv
      121 eek
//
LOCUS       WP_010786564             194 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Glaesserella parasuis].
ACCESSION   WP_010786564
VERSION     WP_010786564.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..194
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21681
     Region          3..163
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mklfgtiydk tmewskhrfa agwlsfvsfi eatffpippd vmlipmsmsk pqmatryaiy
       61 ttlasvlggi igyfiglyaf dwvkgiitdw gmqasfdqam dwfetwgvai vflagfspip
      121 fkvfticagv lqmsflpfil taaisrfarf ilvaklsawg gekyadkirr sieligwgtv
      181 viavaayviy tllk
//
LOCUS       WP_010787815             352 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Bacillus atrophaeus].
ACCESSION   WP_010787815
VERSION     WP_010787815.1
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 10007593
            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="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=39861
     Region          1..275
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mkgrvewidi skgigiilvv lghaptddal ksfifsfhmp mffflsgavy rdtglgffqf
       61 alkkargllv pyavfsvity lfwllverhf qflgsadvdp avplkgivys ipdhymlthn
      121 palwfltclf lvdivffllk kacrgkwlil iagsclvsvv nvyvlhisll wnaevaaaal
      181 gfytigfvvr nklkelsyrr tifavvvcfs ltallqment rvdmraneyg nmlifyltaa
      241 lgtggvvfas fklrklaflq flgrnsliil vlhypilrtm eavvyyvlni pvsstyqagw
      301 gilytaatlt alvpfifffk rypvlfgkpl akrrvygirg lfpgkyreyr sy
//
LOCUS       WP_010789904             292 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Bacillus atrophaeus].
ACCESSION   WP_010789904
VERSION     WP_010789904.1
KEYWORDS    RefSeq.
SOURCE      Bacillus atrophaeus
  ORGANISM  Bacillus atrophaeus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Bacillus atrophaeus"
                     /db_xref="taxon:1452"
     Protein         1..292
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32785
     Region          14..256
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 meavleadtr avigegplwd eekkclywvd ilgsrlhvfd paekenhtvs fksfvtslak
       61 yssdelimtm kdgfylyhlr enkltpikqp edmdkslrfn dgkcdpsgrl wagttsmegk
      121 qetasfyrle adgglvkikd nvstsngldw drkrqlmyyi dtptqeivcy qydpdsgdvs
      181 npetvyrfqk sdgspdgmti drdgmlwval fgggrvakid pfqkkwidsi mvpakyvtcc
      241 afggedlktl yittateqmt eterynqpha gglfsvrltt ggyvpapfsg tl
//
LOCUS       WP_010786486             286 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Glaesserella parasuis].
ACCESSION   WP_010786486
VERSION     WP_010786486.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
REFERENCE   1  (residues 1 to 286)
  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 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   3  (residues 1 to 286)
  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   4  (residues 1 to 286)
  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 286)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     Protein         1..286
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33350
     Region          34..286
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          202..281
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 makigntqai ptpqsaleic lfsefnqsnl hadeltreml aeqhrfdfyv wlwvtegecq
       61 hlldfqsvtq rtgewllirp qqvhhfqtme gwdgwglsfp aewvsadlas iwqqlpqkqs
      121 vtaeqapllq lalqqlkqyr yfewqgqnyq pllqtqlhtf ltllntlyaa nqpqedhqnq
      181 rwqgfsqlle qhfctqhqvq fyaeqlgcte ktlgstclah tglpakmvin qrllleakrl
      241 lvhtqksvkh ialqlgfeea thfnkffkky erctpkgfre sylaek
//
LOCUS       WP_010792540             247 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Pseudomonas].
ACCESSION   WP_010792540
VERSION     WP_010792540.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 247)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            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="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=26873
     Region          20..243
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mmisrprsia vgacagpgle lalvvqpvmh lgsrhpsaia yecllrvveg tqlaaparli
       61 asaeadgsiv dldrwvvsqa ariagafpnv hlwvnasqis vsdirfieha isefdrhgvt
      121 srmtfeites adgdackivk glerlnlkam pvmlddmrdg fakrqllmnr avtgcklsrr
      181 ttrdiaespa vrgeveklvr dcraagkrvv legiedaael eiaraleief cqgfyfgrpa
      241 lpeylfg
//
LOCUS       WP_010792992             296 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010792992
VERSION     WP_010792992.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 296)
  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 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 296)
  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   4  (residues 1 to 296)
  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 296)
  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 12071874
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32509
     Region          25..178
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          209..289
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msttstdmas liatlqdepg fdatripgvr lmraeqaypr spvfyepric ilaqgqkigf
       61 lggetyryda erylvmsvpl pfecethasa aepllgvsvd vdigtlkell lqmeeapgsd
      121 ddnelapsap masvpldagm adavmrllgc lpspldshil gpqlvreiif ralrseqgna
      181 lravagrhsg ygrmaralrr ihtdyasald idtlareanm svstfhhnfk amtftsplqy
      241 lksvrlykaw slmvqdglna staanqvgye spsqfsrefk ryfgrtpsee vqaarr
//
LOCUS       WP_010793450             802 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [Pseudomonas].
ACCESSION   WP_010793450
VERSION     WP_010793450.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 802)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 802)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 802)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..802
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..802
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87344
     Region          51..94
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          74..801
                     /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 mkhvvssall lglsslslaa qaapialdlp aqplaasleq lqgasglrir fdraavadrr
       61 apalrgklep sealqrllag sglsgevrgg dawveaaatg agiapgdsvd lgalsvvatq
      121 dpattaited sgsyttramr tstklamsir etpqsvsvvt rqrmddqgmr dlndavkgvt
      181 gltvqqygpa rvkyaargfd vdnimydglp tsistytqdv isaadlamfd rvevvrgatg
      241 lmqgagnpaa ainmvrkrpt qdfraslqgs vgtwdryrse advsgplnse gtlrgravva
      301 yqkgnsfqdh vssergvfyg iaeadlspdt tfaigasnqn dnrndnwvgl psplggrhld
      361 lkrssyygad wsywdtdtth lfsdlthrfa ngwqmklaad klwarinmlg lyndcyystt
      421 gcasmtqnpg dysytddhds ydayangpfq llgrehelvv gasyrqerfd ghggwgslfn
      481 kdgtptgpmd ptqwdpsstl kprlntslwg mkldqeqkga ylttrlnlad plkvilggrl
      541 dwykadadtd sykvtrnvtr yagviydlnq tysvyasytd ifkpqsnfda ggglldpitg
      601 knyeiglkge hfggalnsqi alfqidqenr atedvggpsp cpfsptsryc srasgkvrsq
      661 gvdlelsgal sddwqmmagy tyvdakykhd snkanegkpf daakprhlfk latsytlpge
      721 lhkwrvggdl atqsktedss tgfqqggytv vnamlgykvn eridtrlnfn nlfdkyyysg
      781 idfgnlnyge prnlmftvky sl
//
LOCUS       WP_010793071             361 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010793071
VERSION     WP_010793071.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 361)
  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 361)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 361)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 361)
  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   5  (residues 1 to 361)
  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   6  (residues 1 to 361)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..361
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40512
     Region          31..212
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          87..344
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkndgetqas tkgtisvrlv gealvewrrq ggeegevlqa agidpqllgk pyarvtshay
       61 srlwldlarr mddeffgmda rrlksgsfaf msrcaiheqt lepaltgilr flclqfddfq
      121 prlqrrggla eivldeapgr ygralsyftl wmithglacw lvgrripila idlrcpqpdy
      181 iedyrvmfsd nlrfsrplsr llfnadclal pvrrdkrelr rfllgapani lvryrdpqsl
      241 aarikaylrs lrpgrwpdad alaghffmap stlrrklsle gqsyqalkdq vrrdlaiarl
      301 dagaanfael alelgfadgs afhkafkkwt gstpgqyrtq vaaetasaes sgvlsetlgr
      361 r
//
LOCUS       WP_010793170             402 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Pseudomonas].
ACCESSION   WP_010793170
VERSION     WP_010793170.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 402)
  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 402)
  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 10007089
            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="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45668
     Region          33..401
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mslslslaea rrlalaaqgf dgrrtrrsvq rrhlremlar lgllqidsvn alvrshylpl
       61 fsrlgpysmt lldeaawsvg rhrqlfeywg heasllpleh yplmrwrmrq aadgqgiyqq
      121 larfgreqqp lirqvlqavr eqgalgagsl strqeragpw wdwsaekhal ewlfaagelt
      181 vagrrgferl ydlpervfpa ellarpelse aqaqrellrm aasalgvate kdlrdyyrls
      241 paqsrarlae lveagellpv rvegwsqpay cpgepqvprr lgasallspf dslvwerara
      301 erlfdfryrl eiytpkekrv ygyyvlpfly ngrlvgrvdl raerarerla vhalhaeang
      361 mddaalhela eqlrsmaawl glatvaiegr gelaarlrgv ll
//
LOCUS       WP_010794061             809 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: penicillin acylase family protein [Pseudomonas].
ACCESSION   WP_010794061
VERSION     WP_010794061.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 809)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 809)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 809)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..809
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..809
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=89539
     Region          37..799
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 msknaryawr lslgglllgl lacavyllav plgfkygeiq vghglehegr iawdaagvph
       61 iraqsledgy fllgyshard rlwqmefarr yaggtlsevf gaktlpmdrf artlgfrrta
      121 egiyanldap trvllqrysd ginaylelap aalplefslv rherpgpwgp vdslslhlly
      181 swtlsanlgm qlqrlalaeh ldlarinevf apypgelppa trdyaslyrs lhgtpdagkl
      241 lgqlpgsnve gigsnnwvvs asrsatgkpl landphlrlt npaafylasl kipglsltga
      301 nfagaplfvi ghnqriawgy tntgshiqda ylervdpqdp rryltpdgyr pfetrleria
      361 vrdgetvsle vrstrhgpvi sdiyeparlp qaqrdrlvia lawtgldrhd ktfpsllain
      421 raegweqfld aaadfgvppq nmvyadvegn igyvsagrvp lrgadddlhg lapspgwesr
      481 ydwvgyvpes akprslnpre gfiatanqri vppdnafdfg hdwvlpyryd rirewlggpg
      541 qrtledslel qndefssvma sllpemleqv sdpelrasea fallqgwnhq aaadlaapli
      601 agywvraftr ellqprigtq llasgwnqrn ydgflrlild gqadlrfwcg qeqgcdlkln
      661 qslrraldel raahgsapsg wkwgeahaal aehvpfhktp lralfdlknn kggdnfsvnv
      721 grfdysdpan pfntriaatl rmvidladfd nsryalstrn sglpfdgatd lnelwargay
      781 iriaddapda tdrqlvlrps asssgeprp
//
LOCUS       WP_010794130             344 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010794130
VERSION     WP_010794130.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 344)
  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 344)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 344)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 344)
  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   5  (residues 1 to 344)
  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   6  (residues 1 to 344)
  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 12117664
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38313
     Region          26..210
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          90..339
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mptppwsprr saisahlliq fgidrglgle qclagsgldi rllgdpsgei daaqelsvvr
       61 nlvrhlgdac apglaaglry hlnaygiwgf allssptfls aaqlglryld ltfafhgirl
      121 evhddeahlv lddagipedl rifllerdag gvlriqrdlt gqrlpilrag frrpppadpa
      181 pyvrelglcp afgqadnrvv ferrfldlpl pganpevara ceeqcralla rrqvrgglag
      241 rirdrllrtp ghlpdmqtla melhltvrtl rrrlddegss yrllldevrl alaeellatg
      301 airleeiaer lgygevsnfi hafrrwkgmt prqyrqrrrl dams
//
LOCUS       WP_010783181             493 aa            linear   BCT 20-JAN-2025
DEFINITION  response regulator transcription factor [Enterococcus faecalis].
ACCESSION   WP_010783181
VERSION     WP_010783181.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 493)
  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 493)
  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   3  (residues 1 to 493)
  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   4  (residues 1 to 493)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   5  (residues 1 to 493)
  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   6  (residues 1 to 493)
  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   7  (residues 1 to 493)
  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 14435958
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..493
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     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:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=57776
     Region          4..124
                     /region_name="REC_YesN-like"
                     /note="phosphoacceptor receiver (REC) domain of YesN and
                     related helix-turn-helix containing response regulators;
                     cd17536"
                     /db_xref="CDD:381091"
     Site            order(9..12,15..17,20,106..107)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381091"
     Region          398..481
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 myrvmfvdde ymileglkwi ipwqklgfei vktarsaqea lafletesid vlltditmpe
       61 msgielieqa kkkghqfisl ilsgyqefdy vkkgmalqvq dyllkpvnkq ellaniqrik
      121 teldqqkksh arvrlyleng lmrwlndeis egeyeelmqq fttikpgdft vllveaempf
      181 letikelfmk kgqllfiesw mstyhqllli ykgarqeafl fireieaila gqgqifvges
      241 vnewetvyes yekvkqlqai etfyqeflpn nqkeqmnrsa edftflafnq almigdmqti
      301 qreldaifnq lsqqhatpey vryvvfllfs disrqyptvl eenyekivee irasnnlntl
      361 yalmqqvlae vknkpkikky sesvsqaver ieqgyleeln lktvadelhl npsylgqifk
      421 ketkrsfsqy lnqvrtkhaq klllytddti neisekvgfn ntnyfskmfk klngitpkef
      481 reqyqsnyag vee
//
LOCUS       WP_010794143             285 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Pseudomonas].
ACCESSION   WP_010794143
VERSION     WP_010794143.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 285)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            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="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=31780
     Region          28..263
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mngspqarqh ehppavaasl agdlrlarrf qaalargrvr ldwqavrhag hpeweplyre
       61 tllrvtaasg epplptqeli lalerlglir lldrcvlgtv ldrlnaeptl rlacnlsrqs
      121 aamdawweav crwlaarpqv arrltlelte tavgervatr efirrlrehg vriaiddfga
      181 ahnnldfvld arpdvikidc rytrearrsa kgaevlrhll alcrelapcv vlegleedda
      241 farlptgdvy lqgnaiappm rvepplsvrr pksrarieal asrqg
//
LOCUS       WP_010794507             396 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TerD family protein [Pseudomonas].
ACCESSION   WP_010794507
VERSION     WP_010794507.1
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 10790521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..396
                     /product="TerD family protein"
                     /GO_process="GO:0046690 - response to tellurium ion
                     [Evidence IEA]"
                     /calculated_mol_wt=42050
     Region          4..396
                     /region_name="TerA"
                     /note="Tellurium resistance protein TerA/TerD [Defense
                     mechanisms]; COG4110"
                     /db_xref="CDD:443286"
ORIGIN      
        1 mttlvpggna pvatgqlrvd isytpipgad ldisafaltn tgkvrgdgdm cfygqtsils
       61 gavqltassa graeftvdls rvdpavdkva ltatiyenka tfdrvstlal altggieaqi
      121 ptrgmnetal ilgefylrqg awkfrcvaqg faggleplak hfgvdiaaps gnqaqntaqp
      181 apapapvppa apkstislsk vtldksrssi slektsagfg eikvnlnwnq ggtgllsgll
      241 gkrnaidldl gclfemqdgy kgavqalgkr fgdlreepyi qlmgddrtgs vaggewlhin
      301 gqhwsevkri lvfafiydga pnwkatdgvv tifvpgqpei evrmneeggr hgmcaialle
      361 nvngavkvsr rvdfhpghee mdraygwgmr wkagsk
//
LOCUS       WP_010794798             819 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [Pseudomonas].
ACCESSION   WP_010794798
VERSION     WP_010794798.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 819)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 819)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 819)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..819
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89409
     Region          73..123
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          101..819
                     /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 mdsrrsyqaf fkrsplrqav haaalaipms lalvplagna aeaaaaaqav rsydipagpl
       61 stalsrfage anvmlsadga ltegkqspgl kgqysveegf aallkgsglq ivstgngsys
      121 laagtasvgs dvselsattv tdfalgnalg tmegynaths qiatktsksi letsqsvsvv
      181 trdqiddqgs qtvsqalryt pgvmtnpyga thrydyvamr gfndgsvdni yldglktmgd
      241 sgtyssmqvd pyfleridil kgpssvlygr snpgglvalt skkplyepyh eiqatvgtqg
      301 qrgmgfdfsg pvnedqtiay rlvgladksd tqfdhneekr yaiaptvaid fdenttltlq
      361 aymqhdpegg yhgglpadgt lyrhngqyis khffegdsdf dkfertqqmv gyqfehrfnd
      421 vwsarqnfry ldgkvdmrqa yaagwasigs nelaratteg kerlhawivd nmaqaefntg
      481 sakhtllmgl dyqrrkakvd yaggsasnid afdpvygnpg vtetwqtsdl rrmeqtglym
      541 qdlidldkwr fslglrkdwv etssedelyg agkntykenk vtprvgglyl fdngiapyis
      601 ysesfnpnsf tdqngdplka tegkqweagi kyqppgtdni ftasvfhitq enlatklane
      661 qyyrpvgkvr sqgveleahm qvtdsfrvlg sytfadveyi ksddgtegnt pnvaprhmas
      721 vwgdysfkeg slqglslgag vravskswad pantervpgy tlfdasvgyd lsnvglkgvd
      781 vrvnannltd kkyvaacnsl lycyygeern vtatvsykf
//
LOCUS       WP_010794985             191 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Pseudomonas].
ACCESSION   WP_010794985
VERSION     WP_010794985.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 191)
  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 191)
  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   3  (residues 1 to 191)
  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   4  (residues 1 to 191)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 191)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            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="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21656
     Region          1..190
                     /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"
ORIGIN      
        1 mrilliddtp kkvgrlkaal leagfdviee sgltidlpar ieairpdvil fdtqspsrdv
       61 mdqvclvtrd rprpivmftd ehdpdvmrqa iqsgvsayiv egihaqrlqp ildvamarfe
      121 tdqalraqlq areqqlaerk rielakgmlm kmrdcneeqa ytlmrrqams kqqklvqvae
      181 qiismnellg m
//
LOCUS       WP_010796785             492 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type I restriction-modification system subunit M
            [Pseudomonas].
ACCESSION   WP_010796785
VERSION     WP_010796785.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 492)
  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   2  (residues 1 to 492)
  AUTHORS   Youell,J. and Firman,K.
  TITLE     Mechanistic insight into Type I restriction endonucleases
  JOURNAL   Front Biosci (Landmark Ed) 17 (6), 2122-2139 (2012)
   PUBMED   22652768
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Sistla,S. and Rao,D.N.
  TITLE     S-Adenosyl-L-methionine-dependent restriction enzymes
  JOURNAL   Crit Rev Biochem Mol Biol 39 (1), 1-19 (2004)
   PUBMED   15121719
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Murray,N.E.
  TITLE     Type I restriction systems: sophisticated molecular machines (a
            legacy of Bertani and Weigle)
  JOURNAL   Microbiol Mol Biol Rev 64 (2), 412-434 (2000)
   PUBMED   10839821
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114514
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..492
                     /product="type I restriction-modification system subunit
                     M"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=55728
     Region          3..147
                     /region_name="HsdM_N"
                     /note="HsdM N-terminal domain; pfam12161"
                     /db_xref="CDD:463478"
     Region          161..402
                     /region_name="HsdM"
                     /note="Type I restriction-modification system, DNA
                     methylase subunit [Defense mechanisms]; COG0286"
                     /db_xref="CDD:440055"
ORIGIN      
        1 mslqqkidri tdilrrddgi sgamhyteqt swvlflkfld dyesekedea vfsgknyqpv
       61 lddehrwsnw acpkttdgkl dlaraktgdd ltdyvnkqlf pylksfsnaa atgadpksft
      121 ykigaifqyl dnkvasghtl revldivdsl sfqsesdlfe lslvyegllq nmgdaggyag
      181 efytprpvvr amvqavdpkp gktiydaaag scgflveafe hlkrkkkqls teqwefiqrd
      241 tffgyektsl ayvmgmmnmi lhgiespnlf rgntltqnir diqekdrydi ilanppfggk
      301 eksqiqqnfp iqsnatellf lqhfmktlks ggkaavvvpe gvlfqtnsaf kqvkqellen
      361 fnlhtilslp agvflpysgv ktnvlffers ggtsdvwyye cepeqkltkn kpitdqhlke
      421 fvelyisrev tdrswivsas klaedydlsv knptkqkdae hlapsdilkr irikeelvsg
      481 llneiedlla ek
//
LOCUS       WP_010798397             144 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Pseudomonas].
ACCESSION   WP_010798397
VERSION     WP_010798397.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            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="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15301
     Region          3..137
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mhkhidtrrs ggftlieili vvaivgilaa iavpsyssyv trsqiktaqg dlvalglnme
       61 nvrqrtlkys sapvtattaa tealfngkwq paqgadfeym itqvtdtayt vsargksakl
      121 stctltltsk nertatgcpg vtsw
//
LOCUS       WP_010799153             207 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Pseudomonas].
ACCESSION   WP_010799153
VERSION     WP_010799153.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            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="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=22600
     Region          9..195
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 msahsnsrpe rlivgisgas gavygmrlle llrdtpieth lvvsksalit lahetdmsws
       61 riktladvsy vnqdigaaia sgsfktmgmi iapcsirsls eiasgvtstl ltraadvvlk
      121 errrlvlmvr etplhrnhlr smtelaelga viappvpafy tkptsledmv dhtvgrvldm
      181 fdielgivrr wreqpervat ldevvdg
//
LOCUS       WP_010800248             209 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Parabacteroides].
ACCESSION   WP_010800248
VERSION     WP_010800248.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..209
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23691
     Region          3..191
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdfyqilekr rtirdfsdke vtdevlkkvl saafkaptnd hlrqfefvvv rgqeniarlv
       61 spvaqntkni qqtglnaaag vmdkdehamf tdalpkqqrm lmqsnclvlp ffrqkdyplc
      121 qpadqsslny fasawaaven mllaataegl acafripign epehvkqlvk apdgyeftcy
      181 laigypaena hickqkeiri edrihdnrw
//
LOCUS       WP_010801024             388 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [Parabacteroides].
ACCESSION   WP_010801024
VERSION     WP_010801024.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 388)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 388)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..388
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43797
     Region          22..384
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 msgkkksetr kirslekirq inkvsvfygd kkvgelamtp tqrcafeydk ewlksgfsia
       61 prqldlkegl fiapiepfyg nfgifedslp dgygryllnr ilqkegiddt sltpvqrlsi
      121 vgasgmgals yvpelyigep kglpeldymq nlalevlaek tdkdvdvlyf nsgnsggcrp
      181 kslykdeegd wilkfrhind pkdmgkmeyq ynkaarasgi nvpdfklien kyfatkrfdi
      241 edgqrlhtat agallnqsih ypaltyenll altgvitqdp vqveemfrrm vfnilaenkd
      301 dhaknfsfyy rnaqwelapa ydltrcsggy ngehattang sgnptiedml vvgegirisr
      361 kkgqeiigql kevckeilad rfkersnk
//
LOCUS       WP_010802181             589 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Parabacteroides].
ACCESSION   WP_010802181
VERSION     WP_010802181.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 589)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..589
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=67767
     Region          131..384
                     /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          506..583
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mkyktsliti lwgsllnlal pvlaqnnlqh qkdslrqvie hsegidklrs ynrlyylyms
       61 eiaddqkmdt llmllnrvea eaikqgnaem qgmvygnaii ahinrsehdk viekapayld
      121 fyienglwkf yyqihmqlit aynlkgeyes aveegekmya rakerkdkag matalyatgi
      181 iynsqdrwke eekcfrecig llwevsgydn iltqsyaflc mvlraqnryd dllqlvpeye
      241 kaiarfekas graqpeargn lyialmntyi direydkaep ylakieglin ndisrfellr
      301 aralilqshg dygkalaaid samtrtpesd fnrnslrrik mqilarmgry readgllnei
      361 iatndtlknv evnarfdelr tqyevekhia ekernfhyll falaiclvla lllagafyyn
      421 rtialknrkl yerikeqdrl adelsrlena rqsesspkds gkkagatelf assgeqqnlv
      481 irlqeyllsd dnlsntdinr ddiisalgtn knaltdavks vtgkspmeym rtlkveearr
      541 kldshpelti eaiafscgfn ipstfyrlfr kqygisptey rkmatskek
//
LOCUS       WP_010803721              91 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: zinc ribbon domain-containing protein
            [Parabacteroides].
ACCESSION   WP_010803721
VERSION     WP_010803721.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 91)
  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 10577258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..91
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10485
     Region          5..89
                     /region_name="Zn_ribbon_2"
                     /note="Putative zinc ribbon domain; pfam12674"
                     /db_xref="CDD:463667"
ORIGIN      
        1 mdpiycqscg mplvsdtdyg tnqdgsknne ycafcfkdgk ftqdvtmeem iqiclqysds
       61 fkhengesyt keealagmqy yfpqlkrwkk d
//
LOCUS       WP_010804335             248 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Pandoraea].
ACCESSION   WP_010804335
VERSION     WP_010804335.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 248)
  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   2  (residues 1 to 248)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..248
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=23584
     Region          11..79
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mlrklllavv afftlcglam aavdintadq tqlealkgig pvkskaiiee rnahgpykda
       61 advakrvkgl gaksvstlqs egltingqgg aaapaapaas aksapatapa apakpvpqat
      121 qtpaapaapa kpataaptap vpptatqkap vptpaagpam kpastgatat qakpgttvpa
      181 aasaagapdt kaakskkske akeakaakad tapsaasapa aagagsapak sskskkakap
      241 spasapkl
//
LOCUS       WP_010804608             327 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Pandoraea].
ACCESSION   WP_010804608
VERSION     WP_010804608.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea
  ORGANISM  Pandoraea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  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   3  (residues 1 to 327)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Pandoraea"
                     /db_xref="taxon:93217"
     Protein         1..327
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35277
     Region          111..317
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mhstciasgy pgfvavnrre ldahvplswp lfdadgtpll aagerlpsea dldwlftmfa
       61 phrplpdgat tgeaagrtea ansasplgag astvylhglp vplpigawiq vrvapeaqtt
      121 rvrarligra pngmliitpp tagemrlpvt agdrlalwtf pgdnlyeftc dvhsvhhgpf
      181 dyllvsrpsq vretpvrrtp rvdtrlvarl spldettras ftrmladpqd tpewlvmvrd
      241 isadgagila kaplpdgchh valqfrvpig advvpilgma avrgvegplv dgtwayglef
      301 mqmdtrnkaa ircfvyesrl tdpragq
//
LOCUS       WP_010805402             343 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pandoraea sp. SD6-2].
ACCESSION   WP_010805402
VERSION     WP_010805402.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 343)
  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 343)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 343)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 343)
  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   5  (residues 1 to 343)
  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   6  (residues 1 to 343)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..343
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38107
     Region          21..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          86..334
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mhslsatvpi slvrgfldgv gappdvvrqy leaagisdal ltepgarvte sqfstlyral
       61 aiefddempg ifarplrngt lkylclslld apnletamhr fgqfmhlild dfrfassrvg
      121 pvaeialrag pagvsalgqq lmlklahgvg swligqkipl lqvefaferp phavdylylf
      181 pgpaqfdckq trmrfsasyf dmrvrqrkad lrkflarape dwifvafdeq ltshrvrdcl
      241 asrlpdmpsi ddvaqvlncs vrtlcrrlsa egsafqtlkn elrrdiairr ltetqdaiaa
      301 iaadvgfddp tafhrafrqw tgstpgeyrh aahrpvaarp pra
//
LOCUS       WP_010806344             336 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pandoraea sp. SD6-2].
ACCESSION   WP_010806344
VERSION     WP_010806344.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 336)
  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 336)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..336
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37930
     Region          22..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          252..330
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mekgsisiyf vinalahver lggdptallr aadiapslla hpqarvsadr yahlwrlisl
       61 alddeffgqd srrmkvgsfa mlcysvigcr tleqalqraa rfmalllddl emhlvrdgal
      121 arlevherad aqaprifghe tllilfyalt cwliarrvtl stayfafpep aysdeyrtmy
      181 sprlvfhaah taiefdaacl dlpvvqnevs vkeflraapa niilkykntk gmvarvrrrl
      241 ktmptdgwpa fevlagefht tpstlrrrle degqsyqsik dqlrrdlaih alchtskpmm
      301 eialslgfad psaffrafrk wtgvrpgdyr rqavea
//
LOCUS       WP_010806877             375 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Pandoraea sp. SD6-2].
ACCESSION   WP_010806877
VERSION     WP_010806877.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 375)
  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 375)
  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   3  (residues 1 to 375)
  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   4  (residues 1 to 375)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 375)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..375
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39615
     Region          25..359
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(101..103,124..125,174,226,250)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mplkhltata ialcalaaha qtivtigyag altgaqahfg kdsergirla mdeinaqhpv
       61 iagkpvqfal daqddaadpr tattvaqrfa dnhvsavigh qnsgtsiava riyaqqhiae
      121 ltpsatnpef trlgfgttfr mlanddflgv alsqyvssql harriavidd rtaygqgiae
      181 vfarqaekag ativarefst dkafdfaavl trikrenpda iffggmdaqg gpmlkqmrqy
      241 siraplvggd glctaemirl agaaldgnlf cadggrslak mpggqafaak fkakygepvq
      301 lyapyaydam maiyraalaa qstdaakisd alhrvsfggv tgqiafdehg dlrepaatis
      361 tykggkkmal tevsk
//
LOCUS       WP_010807558              90 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Pandoraea sp. SD6-2].
ACCESSION   WP_010807558
VERSION     WP_010807558.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 90)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 90)
  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 90)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..90
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9601
     Region          13..67
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msfhrvnqaw gvelrhteki vllalshhav mstgesspkv srlardcgms esavresika
       61 leaaghiatv pvrrgvtlfr vlgaqngsra
//
LOCUS       WP_010808686             812 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pandoraea sp. SD6-2].
ACCESSION   WP_010808686
VERSION     WP_010808686.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea sp. SD6-2
  ORGANISM  Pandoraea sp. SD6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 812)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 812)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 812)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..812
                     /organism="Pandoraea sp. SD6-2"
                     /db_xref="taxon:1286093"
     Protein         1..812
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=89152
     Region          9..810
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mqrpnavhaa svlafavttw saslhaadga aatpsqtltv aglsqpadil idhngvphif
       61 aanerdgffv qgfnaardrl fqidlwrrrg lgqlsevfgr ayvaqddaar rfvyrgdmat
      121 ewrrygpdak paaeafaagv nayigwlash pdqmpyefrk vgywpakwsa edivrirshg
      181 ltrnlkseva rakvvcrasl dadgvrvglq ptwktqvpdg ldpclpddll kvfdlatqgv
      241 kitkdslqqa dadivqladn gpydvstesa egsnnwvisp qksatgraim andphrayaa
      301 pslryivqvs tptlnligag epaipgvaig hngtiafglt ifnidqedly vyalnpanpd
      361 qyryrgkwvp mrtvretiev rdgtpvqtdl kftkhgpviy vdadkhraya vrtawlepgm
      421 spyfdamrym raktyaefqt alntwgaptv nqvyadtagn igwvpsgmap irpnwdglmp
      481 vpgdgryewa gfwrgdqlps aynpaagyft tsnemnlpag ypyaerklgf ewtngsrhar
      541 idevlkakdk vsiedserlq ndivsiparr lmallaplss ndpqtdaalk llkgwnadmq
      601 adsaqaalee vwfsrhlgra yknavlpkaa aesfgapdpa amlvaleqpa arfgenanak
      661 rdavlltslg eawgemvklq gsdpgawqwg klqtnlnahp ladavdadmr aklnvgplpk
      721 ggspftpnqs tyrvsdfrqt ngpsfrivvd vgnwdntram nlpgesgnpd sphyrdlaqk
      781 wldgeyfklp ysraaveadt esrlhlvpee sr
//
LOCUS       WP_010809533             820 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Cupriavidus sp. GA3-3].
ACCESSION   WP_010809533
VERSION     WP_010809533.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 820)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 820)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 820)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..820
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..820
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=90652
     Region          28..818
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mrwfgrltrf aagllvlava gaaaalvwyr haaqppasgq ealaglrgqv tvvrdghgvp
       61 hiraaskada wfalgyvhaq drlwqmqmnk rvvagrlaei lgpsaldtdk flrtlgvrrn
      121 aeailaqasp etraalqaya dgvnawidhr kgplppefll lraqperwep adtlgwqtmm
      181 awdlggnwtq etlrmrlaqv lpvarisell apypgeqpvr tmdyghlyqq laplanamas
      241 vgdkappgyv egmgsnnwvv sgahtqsgkp mlandphlgl qapalwyfar mtapgldvtg
      301 atlpgmplvv lghndriawg ltntapdvqd lyierlrpgn dtqyqtpdgw aafetrteti
      361 rvkgapdvvl kvratrhgpv isdvaeplsa aagplgaqyv vafqwtalrp ddrtfqaglr
      421 mneardwagf taalrdfhsp qqnivyadvd gnigfyapgr vplrradndl kglapapgwd
      481 arydwtgfip fealphrynp adgvivtanq rivapdypyf itsewtvpyr fdrikallad
      541 tprhsfdsfa aiqkdvvsla vrdalpllla apvsrdaarp ereralleal rkwdgnmdpg
      601 raeplvvtaw lrelsrrlfe ekageaifvr lwdqrnvqqp mlnilrdprt lgafwcdrqh
      661 traaetcdda iadawtrama dlsrrygdds arwrwgeaht arsehkpfgk vaylsplfnl
      721 rvptggdtyt vnvgrhnlrd dkapfentha asvralydla dleasrfmds tgqsgnallp
      781 ryrdwagkwa aveyvtippv pslpqqdapd alilvpaatk
//
LOCUS       WP_010809784             439 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [Cupriavidus].
ACCESSION   WP_010809784
VERSION     WP_010809784.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 439)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 439)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 439)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..439
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47342
     Region          8..427
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 msyelhprfl evrlydqlcg ylceasgnvr fvpseafrgd trrptlslsi svpteagrka
       61 taevldnpfh pavystghel ppyfagllpe gelrkrleat rsnpddkddf gilasagndl
      121 pgavvivpad igalpeyart ygvtggadnl eiavvegatq gaasvsgvqn klalstvlqd
      181 krytlpakgr lsdiiaklpa rnddsqvfne sismqlaaaa gvhvaptrvl pvstievegl
      241 veslgenlhy lavdrfdrtp agrvhaedgc qmlgrmpakk yagiesyiql vaalyrlsps
      301 gveharqffl rqavntlign sdahlknfsv tyhngvlpel spaydivcva alpgfatygq
      361 nvaidrrqre etlatyetia ekagvprria taavkeaval ahanwprmld dldapqairn
      421 ivaerlqtlp laraarpar
//
LOCUS       WP_010810001             130 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PilZ domain-containing protein [Cupriavidus].
ACCESSION   WP_010810001
VERSION     WP_010810001.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 130)
  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   3  (residues 1 to 130)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 130)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            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="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13693
     Region          16..130
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mntavagapp aaptgsgaas rpnvlslsik dqaglyaaym pflarggifv psnrpfrlge
       61 qvflvlslld rpqkyqiagh vawitpagtp mktpgvgvhf pdddngrnlr raveeilgkm
      121 lesgrptqtl
//
LOCUS       WP_010810775             810 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Cupriavidus sp. GA3-3].
ACCESSION   WP_010810775
VERSION     WP_010810775.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 810)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 810)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..810
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=89594
     Region          27..810
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mlrtprrlaa alallattip aamaeapvrn nvlavpglek pasvlvdrwg vphiyagtly
       61 daffvqgfma ardrlwqidl wrkrglgema rdfgpayadg drmaravlfr gdmyrewlay
      121 gsdakrvaea fvagvnayva lteqkpellp pefrklnykp arwraddivr irhhgltlnf
      181 tgeveraqly cqakqdapra dwlrreldpq ieprlspgid pctvpaaelr rayelataaa
      241 rfpkeawgna qaasipldql yalvdpnsda grslgsnnwv iggkrtttgr qilandphrs
      301 hgapslryis hlnapgmsvi gagepflpgi sighngtiaf gltrfymdqe dlygyelnpa
      361 npheykykgr wepmesitee ivvkgesapr kvtidftrhg pvlvadagra qawalraawl
      421 dygmapyfgs mdymrarnwd qfraamnrwg apgenqvyad ssgnigwipg gltvkrpnwd
      481 gltpvagdgr yewagyrnmd elpwaynpap gyivtanenn ippehpaakl gvgyewsdss
      541 rarrlkavvg anarssvqds mawqndtvsl paqrvvallr dvrsddpqla rgldllrgwd
      601 gneradsaaa alfevwfskh lrqavvraal tpeaarlvga gdaarvvavl eqpgpwmpve
      661 rrnavmlesl kaamaeaegk lgpdprawrw gklhtavfth pmdpilsdae rqqfnvnagp
      721 iggsaftpmn tsyrntdfrl tagasfrmvl dvgnwdasrv intpgqsgnp asphyrdlap
      781 lwakgeyfpl vytrkaveka srerlelvpq
//
LOCUS       WP_010810984             254 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Cupriavidus sp. GA3-3].
ACCESSION   WP_010810984
VERSION     WP_010810984.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 254)
  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 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   3  (residues 1 to 254)
  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   4  (residues 1 to 254)
  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 254)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..254
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27612
     Region          1..253
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <157..254
                     /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 mpkpaepqas plvehrryrp qpdghqhgyh qllfglagat eleidghvyr vddrtglivp
       61 agshheflgl dgnlqlvadf parsvalpar lmtrprtfpl dgafgsrvra laawraaaaa
      121 rgpqtdwhla atlaaaladc lgmpgdeqvf plmavdaylr anlaapllva evaghfgwsv
      181 rrfqtlfaea fgdtphryqt rlrldralql ltqstlplae ialasgypdq ttftrsfarr
      241 fgqppgawra aarg
//
LOCUS       WP_010811365             357 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Cupriavidus sp. GA3-3].
ACCESSION   WP_010811365
VERSION     WP_010811365.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 357)
  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 357)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 357)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 357)
  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   5  (residues 1 to 357)
  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   6  (residues 1 to 357)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..357
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38376
     Region          39..223
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          140..357
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mpranlpdgg asgmqagtal gtvslaylra vldhgarqgi apadqlravg vspellhvtg
       61 aqtatripga aylalldwle qvtgdpdvgl ragaafaprh yaemgyvvlt tptvrdailq
      121 giryevland iggtrlietp haacmtwear hgplsrhahe lhmatwvvfa rwligeqhva
      181 tqvefphpap adtrlhaevf gcpvvfnaar hamhierall dlpslqadag mqaqmtriad
      241 tqlqqiapag adalaqaray isgrlpqgel piadvaahls lpvrtlqrrl qaqgisysql
      301 vdnvrralae qyladpgisl aqcamrlgys eqsafthafk rwtgetphgw rrkgqaa
//
LOCUS       WP_010812281             198 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Cupriavidus].
ACCESSION   WP_010812281
VERSION     WP_010812281.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..198
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21307
     Region          4..192
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mtrkqrlvva itgasgavyg vrvlqalsal dgwethlvcs psglltahhe lglqrpqlea
       61 madvvhnvrd igatiasgsf rcdgmvvapc smrtlaaiat gladnlvtra advmlkerrr
      121 lvllaretpf hlvhlrnmtt vtemgaivvp pvpafythpq svddivnhtv grvldlfdvp
      181 hdglverwqg lrpnvata
//
LOCUS       WP_010812306             203 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Cupriavidus sp. GA3-3].
ACCESSION   WP_010812306
VERSION     WP_010812306.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. GA3-3
  ORGANISM  Cupriavidus sp. GA3-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 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
REFERENCE   2  (residues 1 to 203)
  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 203)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Cupriavidus sp. GA3-3"
                     /db_xref="taxon:1229514"
     Protein         1..203
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=22370
     Region          32..87
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msaiaptada sfraettwfh vfrsmfssrd aarmgpyavt vylvikahan fntgnsfpsi
       61 dvivdetgis ksqvirvlkv letfgylkrt kagrkneyrl rekvsirdgr gqqaavatwd
      121 ylpttvqaam adlknlmlsg dfsgsrvvhi erlqinvtha grdvitlnaa dfdelpiatq
      181 eallslrgkl psrdvievih sse
//
LOCUS       WP_010814223             347 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [Cupriavidus].
ACCESSION   WP_010814223
VERSION     WP_010814223.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 347)
  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 347)
  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 347)
  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 347)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..347
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=38441
     Region          1..335
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mgfpaivkaq gpvtmrwqst wptkdifhef agdfvtkvnn msggdlkiel lpagavvkaf
       61 dlidavskgt ldgghgviay wygknsalal wgsgpawgmd pnmllawhky gggkelqqei
      121 yrslnldvvs flygpmptqp lgwfkkpitk pedfkglkfr tvglsidift glgaavnalp
      181 gaeivpamdr glldaaefnn assdralgfq dvskvcmlrs fhqpseqfei lfnrkrydal
      241 paklkalian aveaasadms ikaidryskd yqalqkqgvk fyatpnsvlq aqlkvwdeiv
      301 arkekenpmf kkvndsmkaf aeratrwqnd tnvdfrlats hyfskrt
//
LOCUS       WP_010814461             270 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Cupriavidus].
ACCESSION   WP_010814461
VERSION     WP_010814461.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (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   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..270
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29512
     Region          3..>50
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          <91..249
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          175..249
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mfqviapcaa lapyvngywf vedlagvyag rrivtcpypg svlsinfgrp nameggptvp
       61 qvsllgfqst srqwrswpdt yfvmamlsga glarlfpgig pdckdqlldl agylgdgath
      121 alsadlsaaw tparvacqld awllrrmtai rpaaelatir aahallrqgr qvqevaslta
      181 vnrrqlnrwf erhlgvgpkq lmdlerlqss iqavqrgagd alsgysdqph qirswrrrla
      241 qtpgdyarng psplaeyfgr lpddapafyl
//
LOCUS       WP_010814804             436 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Cupriavidus].
ACCESSION   WP_010814804
VERSION     WP_010814804.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 436)
  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 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   3  (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   4  (residues 1 to 436)
  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 436)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..436
                     /product="CmpA/NrtA family 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=47084
     Region          61..311
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mpsrlriakp lhaavhvpda aadavpassg rrralatiag asvmtlvdpl vragawaags
       61 dapektdvri gfipltdcas vvmaatlgld kkygikitpt keaswagvrd klvngeldaa
      121 hvlygliygv qlgiggpkkd mavlmnlnhn gqaitlsskl aekgvkdgas lkalmmkekr
      181 dytfaqtfpt gthamwlyyw laanginpmq dakaitvppp qmvanmrvgn mdgfcvgepw
      241 garaiadkig ftaettqaiw kghpektlgt taefvqkypn taramvaavl easkfidasa
      301 snrrktaeti aaksyvntdm diildrmlgr ytnglgktwd dpdamkfyqd gaanypylsd
      361 gmwfltqhkr wgllkehpdy lavarqvnri dvykqaaaaa qvplpksdmr saklidgvvw
      421 dgkdpkayad gfkika
//
LOCUS       WP_010815691             268 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Enterococcus faecalis].
ACCESSION   WP_010815691
VERSION     WP_010815691.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            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="formate/nitrite transporter family protein"
                     /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=29406
     Region          9..243
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mksgsplfeq idksidkkvn lfsnsfsrya vramlaclfl tlgtavafai aikgegishg
       61 lgkmlyafmf swslvmilym naelgtsnml ymtvgvyrkk vnfslaakil ftcilfnlig
      121 gvlfgflvsl tvpfqdlpkd sffftsiagk lekttlqilv eamfanivvn ntavlvsmrm
      181 kddagkvaai ifiififafl gfehvianfp afslayfasn gaieaftagn vihnlfwafi
      241 gnfiggglim glgyawldkd nknltyfd
//
LOCUS       WP_010815726             300 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Enterococcus faecalis].
ACCESSION   WP_010815726
VERSION     WP_010815726.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            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   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 300)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..300
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33744
     Region          33..87
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mgtnqnelqd klavegvnan gyglmpklvm qdkrltieak siyayivsfa gsgstafpsl
       61 rkiledlqis ekrfykhrkl lidcnyisvt qirnekkeii knlytlisnp kieeevqdeg
      121 irqndcdpip hfdgypisqn drhksnsfki nnikddddin nacksklthe nfssysnqkg
      181 vdcpltvrer lttvlkekdy laplavslla agvsdadcle iiqfivtlpv ideevsdlvn
      241 aqiranetea ktngltsyka yfitglkqkl enadifvqet nivnpdtikp lptvtmhnwv
//
LOCUS       WP_010816173             481 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Enterococcus faecalis].
ACCESSION   WP_010816173
VERSION     WP_010816173.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 481)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..481
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=53447
     Region          61..>199
                     /region_name="YoaR"
                     /note="Vancomycin resistance protein YoaR (function
                     unknown), contains peptidoglycan-binding and VanW domains
                     [Defense mechanisms]; COG2720"
                     /db_xref="CDD:442033"
     Region          208..307
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          328..460
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(408..409,412,433..436,438)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkkeemqmrn tcrqksgknn kkkviitslv glalvaggsy vyfqshflpt tkvngvsvgw
       61 lnvnaaeekl aqvnqteevv vqtgtkeeki qlpkkyqldq kflkdhlhss kvklplneaf
      121 kkeleaklat lsfpegkpsk nasirrgngt feivpeeqgt vvdtqrlnqq iiadveagkg
      181 nyqynakdfy kapeitkedq tlkatlttln nklnktitvd ingekvafdk tqiqnvlndd
      241 gtinkekltt wvtqlettyg sanqpvlftd vhgttrrfkn ngsygwsidg aktqdllvna
      301 lnsqeqtnai tvplvgdtke nskiannyie idlkdqkmyc fidgkkivtt diitgrynkg
      361 tatvpgfhti lyrttdvnle gqmldgsrys vpvkywmpll sqggvvtqig ihdsdhkldk
      421 ygdkeafktd agsngcintp gtevskifdv sydgmpviiy ghiyddapge fdkpvdygee
      481 v
//
LOCUS       WP_010816321             339 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Enterococcus].
ACCESSION   WP_010816321
VERSION     WP_010816321.1
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 10007593
            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="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=39309
     Region          5..274
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mendkriykw dnvklflifl vifghildre aspsrlmeti nfwiysfhmp afifvsglfs
       61 khaikqrkyl rllsfvwlyl lakllitlan fafankmnfd llnetgvpwy llslasfyli
      121 tiflqrvqpk imlpiivvig casgylpveg flslgrtlgf fpffycgylm diqklqtfld
      181 hrkvkwaaig vilssflfvn sqwslatkfw gfltgwasya eispafeyss fiqlffyvaa
      241 alvslswfal lpkrklplsa lgkdtlypyl lhmpliille sglqldtlfk ewftfrilal
      301 fflalfilai tnmpvvkrga dylfnpiayv lpkqwlkvk
//
LOCUS       WP_010816742             481 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Enterococcus faecalis].
ACCESSION   WP_010816742
VERSION     WP_010816742.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 481)
  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 13100268
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..481
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=53438
     Region          61..>199
                     /region_name="YoaR"
                     /note="Vancomycin resistance protein YoaR (function
                     unknown), contains peptidoglycan-binding and VanW domains
                     [Defense mechanisms]; COG2720"
                     /db_xref="CDD:442033"
     Region          208..307
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          328..460
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(408..409,412,433..436,438)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkkeemqvrn trrqksgknn kkkviitslv glalvvggsy vyfqshflpt tkvngvsvgw
       61 lnvnaaeekl aqvnqteevv vqtgakeeki qlpkkyqldq kflkdhlhss kvklplneaf
      121 kkeleaklat lsfpegkpsk nasirrgngt feivpeeqgt vvdtqrlnqq iiadveagkg
      181 nyqynakdfy kapeitkedq tlkatlttln nklnktitvd ingekvafdk tqiqnvlndd
      241 gtinkekltt wvtqlettyg sanqpvlftd vhgttrrfkn ngsygwsidg aktqellvna
      301 lnsqeqtnai taplvgdtke nskiannyie idlkdqkmyc fidgkkivtt dvitgrynkg
      361 tatvpgfhti lyrttdvnle gqmldgsrys vpvkywmpll sqggvvtqig ihdsdhkldk
      421 ygdkeafktd agsngcintp gtevskifdv sydgmpviiy ghiyddapge fdkpvdygee
      481 v
//
LOCUS       WP_010819041             677 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Enterococcus faecalis].
ACCESSION   WP_010819041
VERSION     WP_010819041.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 677)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 677)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..677
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=77376
     Region          52..135
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 mrknkkiwaf lgillvvmsf sfksgvvnae dkvigddypa kwknlplgat tddwgmatry
       61 ctsfvanrls venkfdirrd gldwnanqwg nnarrqgykv dmiprrgsva ywnsmyhvaw
      121 vaavdgdrvl ieeynygytg rynsrwiskn svdgyihfkd issspekqai nkyititkdg
      181 qdffeniect tkkaktvrgr iyyvkiaykl sngqllysvy edekgtawig ylrqgsseft
      241 qletfnrkkv sltnnattlw kdlnyqgklg msvagnaytv nrvfynstnn asyhelyrgn
      301 tfcgyvnsga vkdittqtvn kystiteanq difgnielts tkgktergri yyttigynlg
      361 dgsvlyslyk detaaewvgy vkenvfeytp ietfdkkqvi ltnstttlwk dlnyqgklgm
      421 svagnaytvn rvfynstnna syhelyrgnt fygyvnsgav kdivsesikk yvtvtednqe
      481 ifgnyeqtni rgktergriy ysnvsydlgn gtilhslyrd etmsewvgyv kenvfeytpi
      541 etfdkkqvil tnstttlwkd lnyqgklgms vagnaytvnr vfynstnnas yhelyqgntf
      601 cgyvnsgavk divseskfke nsdmnqtdvl ktqdsmdefi dfdndgkenk eslkeditek
      661 nlsskeesnk eqteisy
//
LOCUS       WP_010819750             317 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Enterococcus].
ACCESSION   WP_010819750
VERSION     WP_010819750.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
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
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            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="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=35751
     Region          1..309
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mikfqnvskv yrenavlsdv nltiqqgeff vlvgpsgsgk tttlkminrl iepttgeval
       61 neqavtnypl relrlkigyv lqqialfpnl tvaenielip emkkwpkeqr rertiellkk
      121 vqldpeeylh rkpaalsgge qqrigilrai aaepevilmd epfsaldpis rhhlqrlvke
      181 lhqelastiv fvthdmneal llgericimd agkiiqvdtp eaiqkhpknn fvgqffkqss
      241 pelanycgad ltafleaade tiepvptvfm etnlkeivql inaqekanlv ekqqvlgcit
      301 sktitrfmeq lleseeq
//
LOCUS       WP_010821707             287 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010821707
VERSION     WP_010821707.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 287)
  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 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   3  (residues 1 to 287)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 287)
  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   5  (residues 1 to 287)
  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   6  (residues 1 to 287)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..287
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32431
     Region          19..99
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          124..283
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mlanlnqamd yieehlteev sfdelakktg isvyhfkrtf sfvagmslae yikkrrlaea
       61 nlallagkkv tdvafkygyq siegfsrafr dwtgqapsev mktqiqktfp kfsfyidikg
      121 gqsmdvklie kpafqivgvs qkvplqyqge nqaimelaqr itpqqraemh tfddvyphqv
      181 vnasfdfqeg rtteggemth migfatsqen tyenleqlsv pahtwavfpn egpfpqtlqe
      241 twarifsewl pssgyqvvaa peisftqyqg paeakyseiw lavtatk
//
LOCUS       WP_010823942             481 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase family protein [Enterococcus].
ACCESSION   WP_010823942
VERSION     WP_010823942.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 481)
  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 13100268
            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="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=53484
     Region          61..>199
                     /region_name="YoaR"
                     /note="Vancomycin resistance protein YoaR (function
                     unknown), contains peptidoglycan-binding and VanW domains
                     [Defense mechanisms]; COG2720"
                     /db_xref="CDD:442033"
     Region          208..307
                     /region_name="PG_binding_4"
                     /note="Putative peptidoglycan binding domain; pfam12229"
                     /db_xref="CDD:403443"
     Region          328..460
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(408..409,412,433..436,438)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkkeemqmrn trrqksgknn kkkviitslv glalvaggsy vyfqshflpt tkvngvsvgw
       61 lnvnaaeekl aqvnqteevv vqtgtkeeki qlpkkyqldq kflkdhlhss kvklplneaf
      121 kkeleaklat lsfpegkpsk nasirrgngi feivpeeqgt vvdtqrlnqq iiadveagkg
      181 nyqynakdfy kapeitkedq tlkatlttln nklnktitvd ingekvafdk tqiqnvlndd
      241 gtinkekltt wvtqlettyg sanqpvlftd vhgttrrfkn ngsygwsidg aktqellvna
      301 lnsqeqtnai taplvgdtke nskiannyie idlkdqkmyc fidgkkivtt dvitgrynkg
      361 tatvpgfhti lyrttdvnle gqmldgsrys vpvkywmpll sqggvvtqig ihdsdhkldk
      421 ygdkeafktd agsngcintp gtevskifdv sydgmpviiy ghiyddapge fdkpvdygee
      481 v
//
LOCUS       WP_010825355             287 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Enterococcus faecalis].
ACCESSION   WP_010825355
VERSION     WP_010825355.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 287)
  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 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   3  (residues 1 to 287)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 287)
  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   5  (residues 1 to 287)
  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   6  (residues 1 to 287)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..287
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32463
     Region          19..99
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          124..283
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mlanlnqamd yieehlteev sfdelakktg isvyhfkrtf sfisgmslae yikkrrlaea
       61 nlallagekv tdvafkygyq siegfsrafr dwsgqapsev mktqiqktfp kfsfyidikg
      121 gqsmdvklie kpafqivgvs qkvplqyqge nqaimelaqr itpqqraemh tfddiyphqv
      181 vnasfdfqeg rtteggemth migfatsqen tyedleqlsv pahtwavfpn egpfpqtlqe
      241 twarifsewl pssgyqvvaa peisftqyqg paeakyseiw lavtatk
//
LOCUS       WP_010825928             339 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Enterococcus faecalis].
ACCESSION   WP_010825928
VERSION     WP_010825928.1
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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..339
                     /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=39351
     Region          5..274
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mendkriykw dnvklflifl vifghildre aspsrlmeti nfwiysfhmp afifvsglfs
       61 khaikqrkyl rllsfvwlyl lakllitlan fafankmnfd llnetgvpwy llslasfyli
      121 tiflqrvqpk imlpiiivig casgylpveg flslgrtlgf fpffycgylm diqklqtfld
      181 hrkvkwavig vilssflfvn sqwslatkfw gfltgwasya eispafeyss fiqlffyvaa
      241 alvslswfal lpkrklplsa lgkdtlypyl lhmpliille sglqldtlfk ewftfrilal
      301 fflalfilai tnmpvvkrga dylfnpiayv lpkqwlkvk
//
LOCUS       WP_010827150             317 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Enterococcus faecalis].
ACCESSION   WP_010827150
VERSION     WP_010827150.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
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
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..317
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=35606
     Region          1..309
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mikfqnvskv yqenavlsdv nltiqqgeff vlvgpsgsgk tttlkminrl iepttgeval
       61 neqavtnypl relrlkigyv lqqialfpnl tvaenielip emkkwpkeqr rertiellkk
      121 vqldpeeylh rkpaalsgge qqrigilrai aaepevilmd epfsaldpis rhhlqrlvke
      181 lhqelastiv fvthdmteal llgericimd agkiiqvdtp eaiqkhpknn fvgqffkqss
      241 pelanycgad ltafleaade tiepvptvfv etnlkeivql inaqekanlv ekqqvlgcit
      301 sktitrfmeq llesegq
//
LOCUS       WP_010829306             665 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Enterococcus
            faecalis].
ACCESSION   WP_010829306
VERSION     WP_010829306.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 665)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 665)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..665
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=75803
     Region          64..663
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 msvlqtvnrv ltpktkrsvv npleqlneyq lsvlekegyd lefleaiqpr ggvqflengy
       61 mtadghvrtl kvygyakdad lfwlaylmnn qdtvatldia taekdevink intklneled
      121 rsvserkatd rndsvhdyre laeyaanltk ngeiakkill qihvyaptle kldercdelm
      181 kdikgtgykv yprmfqskyd yqslftnfsq qshnpnfqrg htlpslvlgk giplhhqalk
      241 dpqgaeygyt ktggtfiwdv vqlnstrlss nlvmfgtmga gkstilkmia enmlaagnyv
      301 wgfekakdfl plirsrdgri vrldgsegmi nplevfatkt ddsglqvnek gsfishldkv
      361 thqlslinpe lkgtlrsdfr iylrhfyirk glipksfkee avssepfkit glspeayptl
      421 selwafiksi klekgttpak larkeqletm iqelcetygd mfdghstitn lsnepfvffd
      481 iesidgldrg vfqaqlymam tliwnqalie grrqkylyen gqlkeedmrq fcalidechn
      541 vvnahnietv eymtnfqrem rkvkaltlla tqspqemvpe nanhehldql kkvfelstqk
      601 iflkmddsql qhiknlvgms ltqselqsit sqkkgeaiit fgdretyrvh itpnqrqlkl
      661 fsggk
//
LOCUS       WP_010829391             265 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Enterococcus faecalis].
ACCESSION   WP_010829391
VERSION     WP_010829391.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            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   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 265)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..265
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31381
     Region          19..71
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 merafkgiwi pknvwlddel swiekflive idsldnengc fasneyfsnf fglskdrvsk
       61 lisglkekgy idvsyqyksg tksierrvvk itdryrrkql egigennyrg igenakdnnt
      121 llnntenntk nkknsvepss tmpelfekvw ktypkktnkk kareqflkkf kteedlesfk
      181 kgykdylayi klndwyhpqe lfrwirddry ndeydlsqtn kqptyskaqv rqeqlpnwtg
      241 mqedvplsae elaelerqkq ellge
//
LOCUS       WP_010830091             179 aa            linear   BCT 20-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein, partial
            [Enterococcus faecalis].
ACCESSION   WP_010830091
VERSION     WP_010830091.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 179)
  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 179)
  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 11443421
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         <1..179
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
     Region          8..177
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          84..128
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
ORIGIN      
        1 dageeiekip nsdvkvgdtv kvkfsvdawa tgeaipdwvk gnsykvqeat gsrvllegil
       61 swiskgdiel lpdatvvpdk qpetthivqh getlssiayq ygtdyqtlas lnglanpnli
      121 ypgqvlkvng satsnvytvq lgdnlssiaa klgttyqtla alnelanpnl iypgqtlny
//
LOCUS       WP_010830296             300 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Enterococcus faecalis].
ACCESSION   WP_010830296
VERSION     WP_010830296.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            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   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 300)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..300
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33682
     Region          33..87
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 mstkqnelqd klavegvnan gygvmpklvm qdkrltieak siyayivsfa gagstafpsl
       61 rkiledlqis ekrfykhrkl lidcnyisvt qirnekkeii knlytlisnp kieeevqdeg
      121 irqndcdpip qfngypisqn drhksnslki nnikydddin nacegkltne nfssyskqks
      181 vdcpltvrer lttvlkgkdy laplavslla agvsdadcle iiqfivtlpv ineevsdlvn
      241 aqiranetea ktngltsyka yfitglkqkl enadifvqet nivnpdtikp lptvtmhnwv
//
LOCUS       WP_010831204             167 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Nocardioides sp. CF8].
ACCESSION   WP_010831204
VERSION     WP_010831204.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 167)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..167
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=17367
     Region          58..141
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mtaslksalt llalgallvi aavwgwhavt kpfpsteppp lctdvtvntg tevfrdqvav
       61 svfngsnrng lagatmaqle ergfvgadsd naptkvagvq iwtdqprnaa vrlvarqfka
      121 akivsgdelg rgivvvvges fkalrkkeve svtavetstf cspsagq
//
LOCUS       WP_010831314             473 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Nocardioides sp. CF8].
ACCESSION   WP_010831314
VERSION     WP_010831314.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..473
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47372
     Region          248..462
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mrrtttltal llgatllapt gganavgetc rgeaativga knqtvtgtdg rdvivtnaaa
       61 kvdagagddl icvtapsmse gayidaavda gpgndvvdas gagstrlkav lgagadeflg
      121 gpsydvvygg llaadgyagg idierdvidt agdidaitsg tpapagqvtt tpnpdvvvgg
      181 egddslgvhg pltaegridg gggrdnagle vdaatwqvst atgatrdgva hsrwtglesv
      241 girsvqpgar ltvvggsged avsiygaaaa tyavdlaagd dllelsvaps tgssvalgdg
      301 hdrltthter avvdlsegvf sldgsapssl tgvedvfaeg readltgddg dnrliggpcs
      361 vkldgrggnd mlyrfpfegt ppdcvdepvr lkggagkdfl rasnnddrlf ggpgrdklda
      421 rggddllrgg pgrdrldass gndrifgdag rdigigskgr dlcrtevrks cer
//
LOCUS       WP_010831732             230 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease family protein [Nocardioides].
ACCESSION   WP_010831732
VERSION     WP_010831732.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..230
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=25719
     Region          92..220
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mralsgsrap qpraasgrli laalalactp latpvhaadd srvdrllaav evvdtapyhp
       61 gydrdcdpga cvfgepwtdd hdgpfahngc ttredvllrq mrdiemrwgs rcriydarlr
      121 dpytgrrltw rtdgyyiaid hvyplaeawh ggawawsqrr rvafandvrr ellavsasan
      181 ddkvasspse wlpprrayhc tyvrkylrva vawglpitsa deatirrldc
//
LOCUS       WP_010832185             406 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Nocardioides].
ACCESSION   WP_010832185
VERSION     WP_010832185.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 406)
  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 406)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..406
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45032
     Region          1..387
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mesisnlqar rialaaqgfa drahatptla tlqrtlgrtg vlqvdsvnvl qrahymplys
       61 rmgaydvdll rraassqgrr prrmveywah vqafmpvelw pvmqhrmery rgergkwgft
      121 adpalepril aavrergpvt argldeefsr prlkenwgwn wsdarrvldy lflvgdvaia
      181 grtsqfevly dvpervlpad vlalatptka eahvelvrra arshgvgtvr cfadyyrmav
      241 adakvavetl veagelsavr vegwrkpafl haearlprri garallspfd pvvwerdrae
      301 alfgffyrie iyvpaakrvh gyyvlpfllg eaivarvdlk adrgtgrllv kgayaeagap
      361 setaeelaae lirlagwlgl saieveprgd lapalaaasa aagwrg
//
LOCUS       WP_010832261             380 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Nocardioides sp. CF8].
ACCESSION   WP_010832261
VERSION     WP_010832261.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. CF8
  ORGANISM  Nocardioides sp. CF8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 380)
  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 380)
  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
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 380)
  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   5  (residues 1 to 380)
  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   6  (residues 1 to 380)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 380)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 380)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Nocardioides sp. CF8"
                     /db_xref="taxon:110319"
     Protein         1..380
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38248
     Region          14..>57
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          76..373
                     /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 msspgstasl rsanqqrvvd vlraggtvsq adiarqtgla patvsnivre lagaglvate
       61 pgsgrrgttv alartaglva gidfghshva valgdltgql laeerrpids ghayadglae
      121 aesildslla aeglardkvr tlgmglpapm tdgvvrtsai lpgwvgvnaq daarealgav
      181 vhtendanlg alaehrqgva rghdtsvfvk vssgvgagiv lndqlfhgag gtageighlt
      241 ldengpvcrc gsrgcleayt stvalqammg lqlpgatvdd ivgaardgnv salraledag
      301 lhlgwalasv vnllnpalvv vggdmarage lllesarigl rrhaldavas tpvvaselge
      361 raslvgavll aaertslltd
//
LOCUS       WP_010834042             360 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: DNA polymerase domain-containing protein
            [Nocardioides].
ACCESSION   WP_010834042
VERSION     WP_010834042.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides
  ORGANISM  Nocardioides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Zhu,H., Nandakumar,J., Aniukwu,J., Wang,L.K., Glickman,M.S.,
            Lima,C.D. and Shuman,S.
  TITLE     Atomic structure and nonhomologous end-joining function of the
            polymerase component of bacterial DNA ligase D
  JOURNAL   Proc Natl Acad Sci U S A 103 (6), 1711-1716 (2006)
   PUBMED   16446439
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Zhu,H. and Shuman,S.
  TITLE     A primer-dependent polymerase function of pseudomonas aeruginosa
            ATP-dependent DNA ligase (LigD)
  JOURNAL   J Biol Chem 280 (1), 418-427 (2005)
   PUBMED   15520014
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Nocardioides"
                     /db_xref="taxon:1839"
     Protein         1..360
                     /product="DNA polymerase domain-containing protein"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=40052
     Region          3..318
                     /region_name="LigD"
                     /note="Eukaryotic-type DNA primase [Replication,
                     recombination and repair]; COG3285"
                     /db_xref="CDD:442515"
ORIGIN      
        1 maaakpvmvq agdrevrvss pdrviyeatd mtpevtkvmv aeyftsvqeg lmralrdrpt
       61 alerwtsgvr pgmklatgpm dkdadafyqk rvpkgapdyl esveitfpsg rtaeeicpte
      121 iavpvwcahm gtltfhpwpv rrddvdhpde lridldpqpg tdfadavrva gaarelladl
      181 gmtgyaktsg nrgihvyvri eprwefsavr haaiafgrel ekrdsgvtta wwkeergeri
      241 fvdfnqntrd rtiasayslr plpgapvstp vswdelatlt spsglnlftv psrlandgdp
      301 wetiddehfs lqplldlwda npvelnyppd hpkmpgeppr vqpskkvaah wdedgnriad
//
LOCUS       WP_010835726             462 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: replicative DNA helicase [Salmonella].
ACCESSION   WP_010835726
VERSION     WP_010835726.1
KEYWORDS    RefSeq.
SOURCE      Salmonella
  ORGANISM  Salmonella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Salmonella"
                     /db_xref="taxon:590"
     Protein         1..462
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=50499
     Region          5..415
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mspqeleacv lagllnggas pdafdviast peesfsigfy rrtfseikkq altsgmidml
       61 fisealggss lanlseisri patvpnlkgy arkmvkawrs ralakllqdg adgirnaanq
      121 dqrdqivena vaqlldmtad sgdvqpvhin ellpaymdtv qkrmdgdest rnlltgivdl
      181 dnatgginpq dlivvagrpg mgktefalrv vegvtskggg alifsmemaa aqiverslag
      241 agnlsvsrlr npqdmydedw arltaaigel tdrdiwivda tdltveqira iaethkrrhp
      301 hlamimvdyl glikkpkaer ndlavahisr nlktmamrlh tptfalsqls ravdarpaaq
      361 rrpvmsdlrd sgsieqdads ilflyrddvy npespaagva evilgkcrfa aagtviyqef
      421 knghflpidq hvgkektriq leaakprkph rkysekyntd af
//
LOCUS       WP_010835725             326 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Salmonella].
ACCESSION   WP_010835725
VERSION     WP_010835725.1
KEYWORDS    RefSeq.
SOURCE      Salmonella
  ORGANISM  Salmonella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (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   2  (residues 1 to 326)
  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 326)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Salmonella"
                     /db_xref="taxon:590"
     Protein         1..326
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=36221
     Region          3..103
                     /region_name="DnaT"
                     /note="DnaT DNA-binding domain; cl46275"
                     /db_xref="CDD:480615"
     Region          20..65
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msmtlmaram aiktgnpirk lvlikladna ndngecwpsy qhiadhcecs rsavrshida
       61 ligmgvltke nrmginngkg ntsnvyylnl dnpmppksta pvpskitgmp lentppmpcg
      121 gtrtshsfep vnepndppnp qkgegdewll adakkalefy neqtgtrcrd ikpfvlmltp
      181 tktreaytla elqlvirwvl atwrrrgsgl pkpanicrvn rfdgyladae awatteadvd
      241 pdavmngyne ifadtlpaae ldadrrgmii rlaahmknqt tgaflgyfek fradapdfyf
      301 gasgwrasfd ylmkpetlrk treeal
//
LOCUS       WP_010835961             271 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Salmonella enterica].
ACCESSION   WP_010835961
VERSION     WP_010835961.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 271)
  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 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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..271
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31328
     Region          23..267
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <166..268
                     /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 mlelsitlpi kvqngglfis rgigrhparr lqsweiifve kgclkiqeee cvfcveages
       61 lllwphrrhi gveefpadlk fywlhfevka pdsdprwlth lsvpqhtqva dpqalialfr
      121 qfmneqekhq rspalefivl lilqqltvda rqnenaeaag vslawkvqql irthyhlpls
      181 ssvlakelhc nvdylgrvyr gvfhltltea ihrqrvreae kllisdarsl kevaercgfn
      241 dvgyfrqifr khtgltptaw krryskehvn s
//
LOCUS       WP_010836738             397 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Rhodococcus rhodnii].
ACCESSION   WP_010836738
VERSION     WP_010836738.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=41714
     Region          5..394
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mngtvlvins gsssikfqlv dpepgdvlak glverigede grlsctagge trerteriad
       61 hsagfalala eltdsgvldp dtltaighrv vhggavfgep vliddhvvse ihrlsalapl
      121 hnpanavgie ilrstlpgvp evavfdtaff hdlpaaaatf aidrdvaren rvrrygfhgt
      181 shqyvserva dvlgrplgel rqivfhlgng asasaisggr aqdttmgmtp ldglvmgtrs
      241 gdidagvlfq lhrqagmkvd elddllnrrs glkglagvnd fraltelieq gdadaqlawd
      301 vyvhrarkyl gaylvllggv daitftagvg envpalraai lqglepfgiv vdpdrnasgs
      361 gerhigadgs atallviptd eelaiaraaa tlvrgsr
//
LOCUS       WP_010837084             267 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Rhodococcus rhodnii].
ACCESSION   WP_010837084
VERSION     WP_010837084.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..267
                     /product="formate/nitrite transporter family protein"
                     /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=27909
     Region          16..259
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mervyddtld dlgdqaeskr gllraslpay llgavlagay vgigsialas vggpldrads
       61 pflipatgav fgialavvlw agselftgnn liftvaalrr rvrwrdtaai wfwsylgnla
      121 gslalaalvv wsgvlsvggs deylaslasd kmndpvlelf lrgivcnwlv claiwtslra
      181 kgdaaklvfv fglilvfvaa gmehsvanms mltmalfdga ggdvtwggfv hnlvpvtlgn
      241 viggavfvgg ayvlvarard tavtekn
//
LOCUS       WP_010837395             380 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Rhodococcus rhodnii].
ACCESSION   WP_010837395
VERSION     WP_010837395.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
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   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   4  (residues 1 to 380)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..380
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=39784
     Region          1..301
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
     Region          <276..>348
                     /region_name="PRK07807"
                     /note="GuaB1 family IMP dehydrogenase-related protein"
                     /db_xref="CDD:181127"
ORIGIN      
        1 misfehatke fdggvvavdd ltldipaesf tvfvgpsggg kttamrminr mvtptsgtvr
       61 vdgrdvagld atrlrlgmgy viqnggllph rtvldnvatv pvlsgdsrrs arrtalgvle
      121 rvglgaslan rypaqlsggq qqrvgvaral aadppillmd epfsavdpvv reelqtemrr
      181 lqselrktiv fvthdideav tlgdriavfg pggrlrqyda pdvvlaspad dfvaefvgrd
      241 rgyrglsfrs asdvpiheir tvttesvgea tlgesgwalv vsddgrplgw vdaagvakvr
      301 ggsavsaaia aggslfplga dlrqaldaai sspsgigvav dadgvvrggv lgtevlagls
      361 dqrrsedatr ertefgeaer
//
LOCUS       WP_010837458             341 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Rhodococcus rhodnii].
ACCESSION   WP_010837458
VERSION     WP_010837458.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus rhodnii
  ORGANISM  Rhodococcus rhodnii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 341)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Rhodococcus rhodnii"
                     /db_xref="taxon:38312"
     Protein         1..341
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35928
     Region          3..325
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mnrpthilat gtalpgdpid naalceviga qpewidlfvg trtrhfavdl dtgrqthslt
       61 dmatdaarqa msradvtaad igflvlgtat pdhlmpttan lvadalgldr iptfqlqsgc
      121 sgaiaafdlg irmldderql glvigadvca khlridrdas tamspselin fvlfgdgaga
      181 avlshdddga qltmrslinr faglgrapaq qiewfgladr hldgpalded ykaieqwvps
      241 lsrdvlgdvv aaaglaaddv eyllppqlsg rmttrvvqqm apaagtreis vvadtgnngn
      301 alpflqidal aneirpgera avvtiesskw ieggmvlega s
//
LOCUS       WP_010840912             212 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Gordonia].
ACCESSION   WP_010840912
VERSION     WP_010840912.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..212
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23390
     Region          3..201
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mdlseamrtt gtcryfserp veddvlyraf ddarfgpqgg nrqpvrwvvv rdevtkkala
       61 dlylpfwegy yaavvegskk vgavpktves anyfahhlae vpalivvcae meglhptdhe
      121 lgrlsvvgga siypsvqnlt lalrqqgvat alttllcaae nevkdllgip egyltaahia
      181 vgyprddfpr kltrtpveei tfldrfdnrm fa
//
LOCUS       WP_010841686             269 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease family protein [Gordonia].
ACCESSION   WP_010841686
VERSION     WP_010841686.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..269
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=28127
     Region          128..265
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 msahrvtggt vgascndsev rrraawlsvv iaavsvavga salfvtgtgi dtapgsgppt
       61 ptspaigssa spspqpqtsa paadraltdl asldvkgrap ktgyartrfg rawddaadvq
      121 fgrngcrtre dilrrdltgi tfhadgcrvl agtladpytg ttipftrgqe tsalvqvdhv
      181 valsdawqkg aaswaagkri afandprnlq avsgtvnqqk sdgdaatwlp pnkayrctyv
      241 grqievkksy glwvtpaerd amrrvlasc
//
LOCUS       WP_010843132             313 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Gordonia terrae].
ACCESSION   WP_010843132
VERSION     WP_010843132.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..313
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33972
     Region          18..281
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mmhipghtev vpphrrydev aeasaalvik sysssfglas rllpprirrd iqniyalvrv
       61 adeivdaprp eqglvdrsne ldqleaqtsv alvtgsssnl vvhafaqtar rvgidldlvg
      121 pffdsmrsdl tqvqhdfdsl atyiygsaev iglmclrafv adeaksaary dhlapgaqrl
      181 gaafqkinfl rdfgedsdgl grrylvgldp ddpaesawal wlddidldls aaaaaiphlp
      241 vgsrvavcta hdlfaeltar lressaaear rsrvripnpg kariaaaava rrgmprtasr
      301 aeavdvrrrk ina
//
LOCUS       WP_010843940             100 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Gordonia terrae].
ACCESSION   WP_010843940
VERSION     WP_010843940.1
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 10790320
            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="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=10887
     Region          5..99
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(27,55..56,58,80)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(27..28,36,38,40..41,43,46..47,55,60,65)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 maaiteeqve qirtlvsaip agrvstygdl aaaaglsspr ivgwimrtdt adlpwhrvvp
       61 asgrpaphla hrqlerlrae gvpitdgrir lrecrwdisv
//
LOCUS       WP_010844025             161 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Gordonia terrae].
ACCESSION   WP_010844025
VERSION     WP_010844025.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 161)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..161
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=16327
     Region          72..>138
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mnadrepnrl plragammlf avavvfiglg whsaatagnd sptteaattv tptptstsps
       61 tsaastgkrl cvinagqvag lasdvtellq akgyqmaepg nytaggfsen tifheddtdk
      121 sqadevaaal ggevaveerp ttftrcrggi pvivvtavsg a
//
LOCUS       WP_010844311             270 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phosphonate ABC transporter ATP-binding protein
            [Gordonia].
ACCESSION   WP_010844311
VERSION     WP_010844311.1
KEYWORDS    RefSeq.
SOURCE      Gordonia
  ORGANISM  Gordonia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
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   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Gordonia"
                     /db_xref="taxon:2053"
     Protein         1..270
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=28421
     Region          18..258
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mstaalaptt dgvrkglplv tvrglrvayd drpvldgvdl dllpgemval lgasgsgkst
       61 lmrsltgfap isggsvrvag hdvtnlarge lrtlrsevgq vfqqfnlipq msvltnvltg
      121 tlhgagainl vggfsgahrr ralelldrvg iahkakepar slsggqqqrv aiaralmqqp
      181 kiiladepva sldpklagsv lrllreiatq dgipvlvslh vlplalahss rivglrhgem
      241 lvsartcdld taelavlyde egddddeldf
//
LOCUS       WP_010844656             291 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Gordonia terrae].
ACCESSION   WP_010844656
VERSION     WP_010844656.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 291)
  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 291)
  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   3  (residues 1 to 291)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..291
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32410
     Region          175..271
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mtsdrgvftl neltalgwta edikqarrte tltplgygwv raadadsqav aavtaggals
       61 cvsalrfhqk hghpgiwips ghnethvrrs khkknaprps gpfrwcqgfg qplpvrtavd
      121 piplaigcaa rclpaeewia ivdsilstte wtipdlqadm grvarsvsam fercdprsqs
      181 gtesiarlrl vaagfsvqvq psiggrerad lrtgslliec dgqsyhadak afandrrrdr
      241 mtmldrwmtm rltyddvlyg wdqvleeira vtrqdrhrir rrddprrgiv e
//
LOCUS       WP_010844839             400 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Gordonia terrae].
ACCESSION   WP_010844839
VERSION     WP_010844839.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            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="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42108
     Region          7..399
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msgasgavlv fnagssslky qlvqpadgtv vaegiaerig dagssmtheq ngetvtetlq
       61 lddhlaavrr aerffayngt dlakaglsav ghrvvhggrs fyeptvvtpe viseierisp
      121 laplhnpanl vgilaaqell pdvpsvavfd taffhglpds satyaidrav adehairryg
      181 fhgtsheyva grvaefldrd paslnqivlh lgngasasai aggqpidtsm gmtpleglvm
      241 gtrsgdidpg lvlhlnrvan lsvgeidtll nkrsglrglc gendfrtite lmdsgddaar
      301 rafdvyihrl rrylgayafa lgrvdaitft agvgensavv rsralagleg fgivldeern
      361 alrgkatrri saddsavdvl vvptneelai arqsaavvgg
//
LOCUS       WP_010845049             130 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Xenorhabdus nematophila].
ACCESSION   WP_010845049
VERSION     WP_010845049.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus nematophila
  ORGANISM  Xenorhabdus nematophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 130)
  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   2  (residues 1 to 130)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Xenorhabdus nematophila"
                     /db_xref="taxon:628"
     Protein         1..130
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14166
     Region          64..129
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkglrvlfns livalcinmp lshaittnes tdktakqpss qhtatvensi skeggkqipd
       61 qkiskkgtln inianaeela kelngigvkk aqaiieyrek ygpftaieql qevqgigptf
      121 ieknrnklty
//
LOCUS       WP_010845907             223 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Xenorhabdus nematophila].
ACCESSION   WP_010845907
VERSION     WP_010845907.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus nematophila
  ORGANISM  Xenorhabdus nematophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 223)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Xenorhabdus nematophila"
                     /db_xref="taxon:628"
     Protein         1..223
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=25374
     Region          3..209
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mifapafkpi kdvgtgsfva aevlarwyde grvltpssls sqlhwglvdm evarfiqdnl
       61 hhcldqyptl flnvseqtly sdvifkawtr virdiaknhs srivieiteg iqdaslalrw
      121 nvlvetgvel alddygdknp slerlscydw ryckfdarrl csledypail hcrrkgiqli
      181 aeqvetfplg esakllglsw qqgfyhgkpa vmdkhlnyek alp
//
LOCUS       WP_010852530             306 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Lunatimonas lonarensis].
ACCESSION   WP_010852530
VERSION     WP_010852530.1
KEYWORDS    RefSeq.
SOURCE      Lunatimonas lonarensis
  ORGANISM  Lunatimonas lonarensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae.
REFERENCE   1  (residues 1 to 306)
  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 306)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Lunatimonas lonarensis"
                     /db_xref="taxon:1232681"
     Protein         1..306
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33710
     Region          41..302
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mkrrnfiknv slgtaagfag asglqagvld snptaestfn lnyaphfgmf rnhagedlia
       61 qldfmyergf rsledngmmg rpvdvqekig nhlaklgmdm gvfvldkggn gantfasglk
      121 ehtdiflngc rravevakrv nakwitvvpg dfdrrlpidi qtanvidtlr lgaeilephg
      181 lvmvleplsd tpnlflrtsa qtymicravn spackilydv yhmqkneghl itmmnhcwde
      241 iayiqigdnp grkepgtgei nylnvfkhih ekgyrgimgm ehgnahpgkd gesaliaayr
      301 kadsfl
//
LOCUS       WP_010851811              92 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Phycicoccus elongatus].
ACCESSION   WP_010851811
VERSION     WP_010851811.1
KEYWORDS    RefSeq.
SOURCE      Phycicoccus elongatus
  ORGANISM  Phycicoccus elongatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Intrasporangiaceae; Phycicoccus.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 92)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 92)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Phycicoccus elongatus"
                     /db_xref="taxon:101689"
     Protein         1..92
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=9302
     Region          16..92
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mseamrvgvr pgdpgtltvr fwagaraaag tdrvsmpvgt vkcvraella wqpdlapvle
       61 vsslladglv vgddaeldag stlevlppfa gg
//
LOCUS       WP_010855804             809 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Lunatimonas lonarensis].
ACCESSION   WP_010855804
VERSION     WP_010855804.1
KEYWORDS    RefSeq.
SOURCE      Lunatimonas lonarensis
  ORGANISM  Lunatimonas lonarensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae.
REFERENCE   1  (residues 1 to 809)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 809)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 809)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..809
                     /organism="Lunatimonas lonarensis"
                     /db_xref="taxon:1232681"
     Protein         1..809
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=91676
     Region          53..809
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkyvgfiisl fvtlalvmgl sldlggvppi sdlldpfrgf wqnqysedqr areslpvsgl
       61 qeevlvryds hliphifaqn efdlyraqgy vtaqhrlwqm efqilaaagk iseivgpqal
      121 efdrlqrrkg lafgaeaglr fledndpetl qklqayaegv neyidqlpfs klpieykllg
      181 yrpspwdagk tvlllkymad mlvgdfdiey tnlrlmlged wmnklfpdfp dvvdpvidts
      241 hvwtfsggqp qvpddlsypd sllwlktlnk pepgtgsnnw avsgrktesg npmlandphl
      301 slnmpslwya vqlstpeftt kgvslpgalg visgfneyia wgvtnatrdv rdsylinfrd
      361 dsrleylynd qwipsvvrve rikikgepdf ldsviythhg pvvydrdfsg rhqlvnvalk
      421 wtahegsneq ktflllnrgr thsdyleald hftspaqnfv fasksgdiai kvqgkfpvkw
      481 neqgkylmdg sdprfdwggy ipfdenpssl npargfvssa nqhstdstyp yymfdhtfeh
      541 yrnrrinsql srmdqisisd mkalqldeyh lhaseilpvl lqylrdqsed eplsnrvldy
      601 mgiledwdys aganqlgatv ftvwwdqlke mvfakwtrdg lptvqpsnfq fsrlisgepa
      661 selfdlpets iresavelam isfqkavdrl eeiktekgsl ewhvykntqi shlvpnfgsf
      721 gfqgiktggg kgivnatdsr hgaswrmvve mgsevqafgv ypggqsgnpg srfygnlipi
      781 wasgdyvdfg lmkrvdakpf lfetrldpr
//
LOCUS       WP_010858673             287 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Lysinibacillus sphaericus].
ACCESSION   WP_010858673
VERSION     WP_010858673.1
KEYWORDS    RefSeq.
SOURCE      Lysinibacillus sphaericus
  ORGANISM  Lysinibacillus sphaericus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lysinibacillus.
REFERENCE   1  (residues 1 to 287)
  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 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   3  (residues 1 to 287)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 287)
  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   5  (residues 1 to 287)
  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   6  (residues 1 to 287)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Lysinibacillus sphaericus"
                     /db_xref="taxon:1421"
     Protein         1..287
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33067
     Region          21..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..287
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mswiesiqka inymeenlln dltmeqiaqe vnssvfhfqr ifsiltdmsi adyirrrrlt
       61 laaqellnte hkiidlayky gydspeaftk afrkqhnvtp searkqqgpl qsynrliiqv
      121 slkgaepmky kivekekfqv vgvkrtyncq ngentqgipl fwdemnnkgm ddalfklnng
      181 eikgvlgvcv pdknykensl mdywiatdht gdvpedlltm evpaskwvvf evhgpmptam
      241 qntwkqiyse wfpsnpyept gsaelevytd edpsspdlys eiwipik
//
LOCUS       WP_010860462             282 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Lysinibacillus sphaericus].
ACCESSION   WP_010860462
VERSION     WP_010860462.1
KEYWORDS    RefSeq.
SOURCE      Lysinibacillus sphaericus
  ORGANISM  Lysinibacillus sphaericus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lysinibacillus.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 282)
  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   6  (residues 1 to 282)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Lysinibacillus sphaericus"
                     /db_xref="taxon:1421"
     Protein         1..282
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31971
     Region          20..103
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          127..282
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mwlqsiqqai eyienhlted iqiedianva hsssfhfqrg failtgmtvg eymrgrrltl
       61 aaqeiassdc kiidiaykyg yetpeafaka frkqhgmkps dvrkavgmih synklvihvq
      121 lkgaepmkyk iiekesfqli gvkrtfsckd geqtkeitkf wqdvyvdgtn aqlfplntge
      181 ihgvmgvcdm iehdimnywi atnhagddsh gfetfmvpaa kwvvfevtga mptaittmwe
      241 kiyqewlpsn afeltggsel evysngdass dhyyseiwlp ik
//
LOCUS       WP_010860819             317 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Lysinibacillus sphaericus].
ACCESSION   WP_010860819
VERSION     WP_010860819.1
KEYWORDS    RefSeq.
SOURCE      Lysinibacillus sphaericus
  ORGANISM  Lysinibacillus sphaericus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lysinibacillus.
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
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Lysinibacillus sphaericus"
                     /db_xref="taxon:1421"
     Protein         1..317
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=35694
     Region          1..306
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mitfdnvskk ydndqvavka inleikkgef fviigpsgcg kttllkminr liyltegtir
       61 ingqrisdyn ihelrwnigy vlqqialfph mtieeniaiv pelkkwrqqq iqqrvralle
      121 mvglepdkys qrkpkelsgg eqqrvgvvra laadpeiilm depfsaldpm srtklqddll
      181 elqraiqkti vfvshdmqea lklgdricvm kdgeivqvgt pqevmenpin dfvkefigvk
      241 ehsfndfnie qvlepmtnge lqhvvsckds lpvilsklaq haclavendg tiigvitrqs
      301 mlqflakdgs qrgeang
//
LOCUS       WP_010860954             359 aa            linear   BCT 20-JAN-2025
DEFINITION  GerAB/ArcD/ProY family transporter [Lysinibacillus sphaericus].
ACCESSION   WP_010860954
VERSION     WP_010860954.1
KEYWORDS    RefSeq.
SOURCE      Lysinibacillus sphaericus
  ORGANISM  Lysinibacillus sphaericus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lysinibacillus.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Lysinibacillus sphaericus"
                     /db_xref="taxon:1421"
     Protein         1..359
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=41411
     Region          4..356
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 mntynqkiln kyhvvflaqs vmigtgllsl pqklsplgys qtffpfimgi iasftlwpmi
       61 wlcskfpnen lfrineillg kwfgkclnil fvlqfvvfta giitdymnli estalpeqti
      121 tipvllilll llyivkggik svanfciltf fitlilvfft rwaiekgdis hflpifnftg
      181 heffdalkng yfsllgyeli mfyfpfiinq kkaykhafig iwisillyfv atavsvmyfs
      241 ewqlenvkfs ilnlfkagef sfieridifg mtlwifhilc aisgyvwcak qgmesliskn
      301 akyylvilsi iiffivnmpf sqefqkklfl gsnyagyaii vspiflslvy virkkkvqq
//
LOCUS       WP_010861428             304 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Lysinibacillus
            sphaericus].
ACCESSION   WP_010861428
VERSION     WP_010861428.1
KEYWORDS    RefSeq.
SOURCE      Lysinibacillus sphaericus
  ORGANISM  Lysinibacillus sphaericus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lysinibacillus.
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
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Lysinibacillus sphaericus"
                     /db_xref="taxon:1421"
     Protein         1..304
                     /product="aminoglycoside 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=35395
     Region          18..243
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mliedvidhi aslkgyssik kiekgyspde kyivsvgqnh yfirlsdiqy hekrtiefsl
       61 lqalekqgvq thkaiectll seanlsvmvl syiegypade iilnlsdvgq fnlglaagke
      121 lrkihqlhah vpqtmhweea qrkkfsfyln dykkgsyqvp kehkilnfie nnfhllkdrp
      181 itllhddfhl ghiivqnntf ngvidfnsyd fgdpyhdfyn lslfsrrhsi pfcigqingy
      241 ftappddtfw riyalyaamn ivstivwtkk ydepsfddal erihliladh dyfnvdqplw
      301 yktl
//
LOCUS       WP_010862283             238 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Plesiomonas].
ACCESSION   WP_010862283
VERSION     WP_010862283.1
KEYWORDS    RefSeq.
SOURCE      Plesiomonas
  ORGANISM  Plesiomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 238)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Plesiomonas"
                     /db_xref="taxon:702"
     Protein         1..238
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=27035
     Region          <15..218
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mlnnvlfkyk yremefgvia qpiienrtkk vssfellsrs iaidcvdsff gtlsasdvtk
       61 vsciqmnqia dllsvsnkgd nlrvhvnihy ktlfnadfik lakkikwvkf afeingfecd
      121 aeqliklkna fkiiqsfghe iwlddhgvnn atvsllldlp wdgvkidkei vwrssqeqlc
      181 alvhcckcya gkvtlegved eylqdlsvya gsdfsqgfnw rllnkgffmq esplllea
//
LOCUS       WP_010863299             275 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Plesiomonas
            shigelloides].
ACCESSION   WP_010863299
VERSION     WP_010863299.1
KEYWORDS    RefSeq.
SOURCE      Plesiomonas shigelloides
  ORGANISM  Plesiomonas shigelloides
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Plesiomonas.
REFERENCE   1  (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   2  (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   3  (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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Plesiomonas shigelloides"
                     /db_xref="taxon:703"
     Protein         1..275
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30442
     Region          20..67
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msmtlmakam nikvgnplrk lvlikladna ndkgecwpsy qniadhcecs rsavrahida
       61 lmdmglltke nrignnngkg nrsnvyylil dtpmpsngtp lchqmtppmp ldgtpcatrw
      121 hqnqsiepvi episvtsens dessddhsgg vslpddgkai qsgtkwgtad dlaaaewmfg
      181 qvlaiapkak kpnyaawane irlmrerdgk qhremcelfr wacqdsfwsg nilcpvslrr
      241 kwdqleikrn kqlagtansa slnfdntdwa kgllv
//
LOCUS       WP_010864346             147 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Plesiomonas shigelloides].
ACCESSION   WP_010864346
VERSION     WP_010864346.1
KEYWORDS    RefSeq.
SOURCE      Plesiomonas shigelloides
  ORGANISM  Plesiomonas shigelloides
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Plesiomonas.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Plesiomonas shigelloides"
                     /db_xref="taxon:703"
     Protein         1..147
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16281
     Region          2..141
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mlsaawenyg lwgllassfl satilpgnse vvlvwmlrqa qwpqwqllaa avvgntlgsl
       61 csvwmgrgla ilkpqrgldt atrwierygv wslwfswlpl igdilcllag wfrlpwasst
      121 lfillgktlr ylviilifng asgilfg
//
LOCUS       WP_010864110             374 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Plesiomonas
            shigelloides].
ACCESSION   WP_010864110
VERSION     WP_010864110.1
KEYWORDS    RefSeq.
SOURCE      Plesiomonas shigelloides
  ORGANISM  Plesiomonas shigelloides
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Plesiomonas.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Plesiomonas shigelloides"
                     /db_xref="taxon:703"
     Protein         1..374
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=41288
     Region          1..354
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msvevrhiqk afngfatlhd inltfpsgel aallgpsgcg kttllriiag leqedsgqil
       61 lngqdvsalt ardrqvgfvf qhyalfrhms vfenvafglr vkprklrpde atirrkvntl
      121 lelvhlghla grypnelsgg qrqrvalart lavepqvlll depfgaldaq vrkelrrwlr
      181 qlhdelhvts lfvthdqeea levadrivvm nkglveqigs peevyetpat pfvhqflgtv
      241 nllpaqiqgq qihfdghvlp assaldyafg sqavafvrph dievlpadvn vgtparvsrl
      301 lrlgavtrve fitevtdrrq avievemnrd qlsrlglasg srvrlcpqrv hiypdsnaqd
      361 vsrsatgtqg ekaa
//
LOCUS       WP_010864446             123 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Plesiomonas shigelloides].
ACCESSION   WP_010864446
VERSION     WP_010864446.1
KEYWORDS    RefSeq.
SOURCE      Plesiomonas shigelloides
  ORGANISM  Plesiomonas shigelloides
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Plesiomonas.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Plesiomonas shigelloides"
                     /db_xref="taxon:703"
     Protein         1..123
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=13640
     Region          1..123
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkrgftliel mivvavlgil aaiavpayqk hvtksrrsda itqllqgqlk qeqlwltksp
       61 raysnqisel gftnnsyyqy siksssnnsy tlqataqnsq lrdsgcttlt idhsnnktpp
      121 dcw
//
LOCUS       WP_010871597             756 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CHASE2 domain-containing protein [unclassified
            Synechocystis].
ACCESSION   WP_010871597
VERSION     WP_010871597.1
KEYWORDS    RefSeq.
SOURCE      unclassified Synechocystis
  ORGANISM  unclassified Synechocystis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Merismopediaceae; Synechocystis.
REFERENCE   1  (residues 1 to 756)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 756)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..756
                     /organism="unclassified Synechocystis"
                     /db_xref="taxon:2640012"
     Protein         1..756
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=82184
     Region          20..649
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mgwtipsawk rfvwqsrgiw iatpavtamv illrftgllq vlewqsydag vrllprhedd
       61 rivivgideq dvtylntpii ddqllakilt klkaqqpaai gldlyrdlpm ppgtdelaav
      121 ftstpnlvgi ekvagkpgie tvnpppllke nnqvgandli idadnivrrg fiylvrdgep
      181 hysfglhlal hfldslkiyp epvregsddf rlnqvtfspl qsdsggyira ddggfqllid
      241 yqstfpkvsl tdvledklpa dwgkgkiill gkvgesfkdl yftpnsstfg lsravpgvei
      301 hgniisqiln agmegqpllk swsepvewlw vglwsffgav itwqlryatr rsggqwlpia
      361 aivgslgall aisygallag wwlpvippml gllgsgvfiv twmaragvqv rntfgryltd
      421 qvvatllenp eglkmggdrr pitiltsdlr gftstsegln peevvkvlni yfgkmadvit
      481 hhggtidefm gdgilvlfga ptsqqddalr avacgvemql alrevnqqvt glglqplemg
      541 igintgevvv gnigsekrtk ygvvgaqvnl tyriesyttg gqifissttl eaagdrvhvn
      601 gnrtvqpkgv kdpvviwdva gvgepynlsl aveeqkyvpi pqplsleyic legkhitdav
      661 ipgtlqqisa kggfiqispn hncpegltni kinlredgep gktpalyakv ldlapgeshg
      721 fyvhfsampt diaqrfyqly qgalaqpaai asaqgg
//
LOCUS       WP_010872118             714 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: molybdopterin oxidoreductase family protein
            [unclassified Synechocystis].
ACCESSION   WP_010872118
VERSION     WP_010872118.1
KEYWORDS    RefSeq.
SOURCE      unclassified Synechocystis
  ORGANISM  unclassified Synechocystis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Merismopediaceae; Synechocystis.
REFERENCE   1  (residues 1 to 714)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 714)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 714)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..714
                     /organism="unclassified Synechocystis"
                     /db_xref="taxon:2640012"
     Protein         1..714
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=79501
     Region          9..714
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mdspailptt rtlcpycgvg cgleavaspq ksvvdaghah kirgdrqhps sqgmvcvkga
       61 tvmesmdkqr llypmfrssl dqpwqqiswe aaleivvdki qqvkqtlgvs glcmyasgqm
      121 qtedyyvaqk lfkgclgtnn fdtnsrlcms savsayslsf gsdgppccye dleitdcafl
      181 igtntadchp iifnrlrkhh kqnphvkliv vdprctatae vadlhlainp gsditllhgi
      241 ayllkkwnli dqkfidnhtq dfeqycqvid hyppekvtqi cgisleqlet aahywgnakt
      301 vlslwsmgmn qsfqgtakgr clinlhlltg qigkpgsgpf sltgqpnamg greagglshl
      361 lpgyrsiknp qhrqeveqlw qispgrinpe pglsawemfm glenqqvgfl wivatnpvvs
      421 mpdlervkka lqqstftihq daysptetae yahlllpaaq wsektgtmtn serrvtlspa
      481 frsppgearp dweifaevgr rlgfenqfnf vdsaavhrey vqltaerlcd qsgvsyeklq
      541 klgplqwpcr qsdqesqlls tkrlytdykf ctengranfc ldhsrglaep vdpnypfvlt
      601 ngrlyghwht qtrtghieki kkmhpkpile mhpkdaeklg iksqdlvaik srrgsaqlev
      661 lvtraiapgt vfmpmhwgfl wddnaevnsl thatacpisk qpelkacavn itpv
//
LOCUS       WP_010872122             446 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [unclassified Synechocystis].
ACCESSION   WP_010872122
VERSION     WP_010872122.1
KEYWORDS    RefSeq.
SOURCE      unclassified Synechocystis
  ORGANISM  unclassified Synechocystis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Merismopediaceae; Synechocystis.
REFERENCE   1  (residues 1 to 446)
  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 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   3  (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   4  (residues 1 to 446)
  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 446)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="unclassified Synechocystis"
                     /db_xref="taxon:2640012"
     Protein         1..446
                     /product="CmpA/NrtA family 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=48836
     Region          58..313
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 msnfsrstrr kfmftagaaa iggvvlhgct sptttstgtg tgsstdqais plvegenape
       61 vttaklgfia ltdaapliia kekgfyakyg mpdvevlkqa swgttrdnlv lgsasggidg
      121 ahiltpmpyl itmgtvtdgk ptpmyilarl nvngqgiqlg nnykdlkvgt daaplkeafa
      181 kvtdpkvamt fpggthdmwi rywlaaggme pgkdfstivv ppaqmvanvk vnamesfcvg
      241 epwplqtvnq gvgyqalttg qlwkdhpeka fgmradwvdq npkaakallm avmeaqqwcd
      301 qaenkeemcq ilskrewfkv pfediidrsk giynfgngqe tfedqeimqk ywvdnasypy
      361 kshdqwflte nirwgylpas tdtkaivdkv nredlwreaa qalevpadqi psspsrgiet
      421 ffdgitfdpe npqayldslk iksika
//
LOCUS       WP_010872380             170 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [unclassified Synechocystis].
ACCESSION   WP_010872380
VERSION     WP_010872380.1
KEYWORDS    RefSeq.
SOURCE      unclassified Synechocystis
  ORGANISM  unclassified Synechocystis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Merismopediaceae; Synechocystis.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="unclassified Synechocystis"
                     /db_xref="taxon:2640012"
     Protein         1..170
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=18347
     Region          14..115
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkaqfsigss sncrhfngtr qrgftllell vvviilgvlg amtlpnlfsq igkareaeak
       61 qilsaigqaq qsyffekasf aesnqaleis fqsnyydise pqligtdvak ssatatngvq
      121 qnarnfamgv yyenqtyrvv lcqspvpaet nsteapnnss gdcvngiklf
//
LOCUS       WP_010854052             592 aa            linear   BCT 20-JAN-2025
DEFINITION  type I restriction-modification system subunit M [Lunatimonas
            lonarensis].
ACCESSION   WP_010854052
VERSION     WP_010854052.1
KEYWORDS    RefSeq.
SOURCE      Lunatimonas lonarensis
  ORGANISM  Lunatimonas lonarensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae.
REFERENCE   1  (residues 1 to 592)
  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   2  (residues 1 to 592)
  AUTHORS   Youell,J. and Firman,K.
  TITLE     Mechanistic insight into Type I restriction endonucleases
  JOURNAL   Front Biosci (Landmark Ed) 17 (6), 2122-2139 (2012)
   PUBMED   22652768
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 592)
  AUTHORS   Sistla,S. and Rao,D.N.
  TITLE     S-Adenosyl-L-methionine-dependent restriction enzymes
  JOURNAL   Crit Rev Biochem Mol Biol 39 (1), 1-19 (2004)
   PUBMED   15121719
REFERENCE   4  (residues 1 to 592)
  AUTHORS   Murray,N.E.
  TITLE     Type I restriction systems: sophisticated molecular machines (a
            legacy of Bertani and Weigle)
  JOURNAL   Microbiol Mol Biol Rev 64 (2), 412-434 (2000)
   PUBMED   10839821
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114514
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Lunatimonas lonarensis"
                     /db_xref="taxon:1232681"
     Protein         1..592
                     /product="type I restriction-modification system subunit
                     M"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=68336
     Region          10..143
                     /region_name="HsdM_N"
                     /note="HsdM N-terminal domain; pfam12161"
                     /db_xref="CDD:463478"
     Region          156..419
                     /region_name="HsdM"
                     /note="Type I restriction-modification system, DNA
                     methylase subunit [Defense mechanisms]; COG0286"
                     /db_xref="CDD:440055"
ORIGIN      
        1 msnrkvdvgf ifqitdkvlw nvfkkneigd vllpfvvlrr ldcildpvnq kvrdaynnfk
       61 dkvtedkldp ilrkaagglq fynisrhtle slrenpktie idfnnylygf nkevreiiec
      121 fqfdkvlgrl lknrilyqmi daickvdlht dkvdnhdmgy vfeelirisn eqsnetageh
      181 ftprdviqlm ievmfsteke vfsqpgiirt iydpamgtgg miniaknyvv dvlsanqtnk
      241 ptirtygqei neqsyaiaks ealitgenid nirhgntftk drftdkkfhy mlanppygvt
      301 wskdadyiin esanpagrfy aglpaksdgq llflqhmisk meyegskiav vtngsplfsg
      361 gagsgesdir kwiissdwle civalpkdlf yntgintfiw fltnnkpshr rgkvqlinav
      421 eaedkinekt gfcrpekrsl gnkrnkiedy hiqrivdlyt rfeegryski fdneyfgyyq
      481 vtieqpelde ngkpkegrng ewkadskkrd keniplsedi eiyfekevlp higkgwidyd
      541 ktrigyeinf skyfaefkpl rptqeikaei qelefgnknd kgimellkel lg
//
LOCUS       WP_010879993             338 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Aquifex aeolicus].
ACCESSION   WP_010879993
VERSION     WP_010879993.1
KEYWORDS    RefSeq.
SOURCE      Aquifex aeolicus
  ORGANISM  Aquifex aeolicus
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Aquificaceae; Aquifex.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 338)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Aquifex aeolicus"
                     /db_xref="taxon:63363"
     Protein         1..338
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=38653
     Region          107..317
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 meeilflfkd eekarefees lhstgaktrr tgtavitagl kdeeilylls emdentlkdl
       61 kvyqgevgnd cenivkaisk aepvtnlidk viyhslgnif idtktlfhpi vdvkekrvka
      121 fealcrppik ivdlinmgks tsefsenfcr ymalknarkf lkedmwlfln fhprflrepl
      181 kvfgdfistl ymhdvsprqv vvelteyeel eisavkslis flksegvkia lddvgsgysg
      241 lfylselgpd iikidmelir dihkhsmkkv ivnylirlah ennikvvseg vetleelktv
      301 lymgtdfvqg fifskplenp nleelnekie kiisqslt
//
LOCUS       WP_010881465             857 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Treponema pallidum].
ACCESSION   WP_010881465
VERSION     WP_010881465.1
KEYWORDS    RefSeq.
SOURCE      Treponema pallidum
  ORGANISM  Treponema pallidum
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
REFERENCE   1  (residues 1 to 857)
  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 857)
  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 857)
  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   4  (residues 1 to 857)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..857
                     /organism="Treponema pallidum"
                     /db_xref="taxon:160"
     Protein         1..857
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=95671
     Region          99..131
                     /region_name="LonC_helical"
                     /note="Lon-like LonC helical domain; pfam20437"
                     /db_xref="CDD:466586"
     Region          141..857
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mlgnlmlgpy crsslwrels wqevtgivap dtiaylkara qdhpfllahe racaairlgm
       61 rmygdgynic vigasgtgkr ttlqyllkdf vprpeqmwdi ayaynfvhph epqvlqfpag
      121 egmpfatalr rsvnailnta qdivksdafl rerrtlladi etrecaelsr ieaelytrgf
      181 rvrwhrkrgt ysfdlvpllk gkdssfealh dlasraklsr cvvhelhary rlscdevssl
      241 lhtlrtarra arrrlaqyyr arlrliileq macikkrvac yapvfspppv scaaeqtere
      301 ktsssrliev phefeemrar iisyieriqt dvqvrvqclm smrisalvkk rffdrytlnf
      361 vcvhtehagy vftehqpnla nlcgsieskg negdtlengh lriragalhr ahagvlivql
      421 edllaeeeaw thlkralrtk qvllpagssq sqgmlrpegv pltcklvlvg epcsferlsq
      481 edssfrelfk vcaefdtsmp nsdknqvali ayldrvvary gtfsldssay arllayaeel
      541 aeshtrlsts fvqiadlvle shavavdmhp dvsvitahvv qealnrrqyv csrarerfqr
      601 miacgellve vqgyrigrin alaieehcgh sfgivislta qasagkegvm niereaglsg
      661 eiydkahlii tsllrekcls afadaafdpa vddlgkgqds fplclsaalc feqsyhgidg
      721 dsasaaeflv llsaigrfpl rqdraitgsv nqlgqvqaig gvsekisgfy dvcalngltg
      781 mqgvlipkss caqlflperv qdavragtfh vwavctidda lelmvpddlk eqgsaqlyqc
      841 vrarlrdfyv tvkghce
//
LOCUS       WP_010880309             189 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Aquifex aeolicus].
ACCESSION   WP_010880309
VERSION     WP_010880309.1
KEYWORDS    RefSeq.
SOURCE      Aquifex aeolicus
  ORGANISM  Aquifex aeolicus
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Aquificaceae; Aquifex.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Aquifex aeolicus"
                     /db_xref="taxon:63363"
     Protein         1..189
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21125
     Region          1..189
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mqkialcitg asgviygikl lqvleeldfs vdlvisrnak vvlkeehslt feevlkglkn
       61 vriheendft splasgsrlv hyrgvyvvpc stntlscian ginknlihrv gevalkervp
      121 lvllvreapy neihlenmlk itrmggvvvp aspafyhkpq siddminfvv gklldvlrie
      181 hnlykrwrg
//
LOCUS       WP_010882624             649 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Helicobacter pylori].
ACCESSION   WP_010882624
VERSION     WP_010882624.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 649)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     Protein         1..649
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=75747
     Region          231..649
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mksetiykdf cfelegilfn fdtslleskk ynekvdlifd lksivkdkdt ktntlnfsvt
       61 lsskgtqtkt neilkecsnq gvkldeeilk kafvkfkkqg smdyfihkna qgflkeqldl
      121 ylfeylfkem tafdhkrlng intikevale vialvsefen elckiwnkpr lvlnshfivs
      181 ldklkaknyd lskitnhpny pkqvkewqdl nleiadnllg neflpldtly fkdleeevks
      241 lfneneingt liksenyqal nslknrykea idciyidppf ntgsdfayid rfqdstwlsl
      301 mhnrlqlayd flspqgnfyl hldyranylg rmllndifsk enfrneiiwh frtyqgqiqs
      361 nfprkhdsll wyskncnvnn ffkitysdny kdtvdyrrwr efivdnnkiv ypnypkadsr
      421 fdgylkrylq stkepkngdi iatingyvid dvwtdiqaid pkkaderlqg tltqkpekll
      481 eriikassne nsivcdffag sgttcavahk lkrkyigvem gehfesvilp rlkkviggfk
      541 sgalkefngg gvikvyeles yeeilrkiky edndkplaye eqysdlverk nesytlniea
      601 lenmgvdike tlenlhgvgv effnekvvkf kgndkevsil kalkealiw
//
LOCUS       WP_010882645             641 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Helicobacter pylori].
ACCESSION   WP_010882645
VERSION     WP_010882645.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 641)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     Protein         1..641
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=72817
     Region          59..542
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mqnkeiggek svneknvevf nryfpgclsi endnkltldt gklkallgdf seikeegygl
       61 dfvgkkialn qafkknhkil kplnestskh ilikgdnlda lkilkqsyse kikmiyidpp
      121 yntkndnfiy gddfsqsnee vlktldyske kldyiknlfg skchsgwlsf myprlllakd
      181 llkqdgvifi siddnecaql kllcdeifge gnfietflwn ktqtppsasn ktrkthefil
      241 cyqknkdnkk miakfsdggd aplwnetnse riltfpanyv fsnlkngiyk kgirdkievl
      301 ddievyngki insfrlkghf rwkqetlnee iinnvflvvk sdkfsirycr egerivmptn
      361 eiskkdnvgt netaskelfk lfdnnkifnf nkpvslikyl isicsnntne gdiildffag
      421 sgttahavle snksdyqkls eggglfngln avfkerrfil vqldekiekn ksaydfclnt
      481 lkstspsifd iteerikrag akikeacahl dvgfrafeii ddethtndkn lgeahqkdlf
      541 aysnldrmet qtilikllgc eglelttpii clienalyla lntafivgdi emsevlenlk
      601 dkgvekisvy mpaisndrlc lelgsnlldl klesgdlkir g
//
LOCUS       WP_010886853             123 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Deinococcus radiodurans].
ACCESSION   WP_010886853
VERSION     WP_010886853.1
KEYWORDS    RefSeq.
SOURCE      Deinococcus radiodurans
  ORGANISM  Deinococcus radiodurans
            Bacteria; Thermotogati; Deinococcota; Deinococci; Deinococcales;
            Deinococcaceae; Deinococcus.
REFERENCE   1  (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   2  (residues 1 to 123)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Deinococcus radiodurans"
                     /db_xref="taxon:1299"
     Protein         1..123
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12602
     Region          <21..>74
                     /region_name="PRK10856"
                     /note="cytoskeleton protein RodZ"
                     /db_xref="CDD:236776"
     Region          55..121
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mtktllsala alllstaafa qtaptpvhaa ptqtassqta pttsthtpka rtatprttap
       61 lptapvnvnt ataaqlmtlp gvsnkiaaei ikdrpyknaa elvkkvkgig knnvkpmtpy
      121 laf
//
LOCUS       WP_010887191             125 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Deinococcus radiodurans].
ACCESSION   WP_010887191
VERSION     WP_010887191.1
KEYWORDS    RefSeq.
SOURCE      Deinococcus radiodurans
  ORGANISM  Deinococcus radiodurans
            Bacteria; Thermotogati; Deinococcota; Deinococci; Deinococcales;
            Deinococcaceae; Deinococcus.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Deinococcus radiodurans"
                     /db_xref="taxon:1299"
     Protein         1..125
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=12977
     Region          1..122
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mqkateaftl iellvvmtii ailisvlvps lagarskayd sattsylrhc asaleisrdd
       61 lgvlpspppt scedpalgvn aqskpasvkq sqvtvtssgt aytisalsqs gktftydqgg
      121 freip
//
LOCUS       WP_010887583             395 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Deinococcus radiodurans].
ACCESSION   WP_010887583
VERSION     WP_010887583.1
KEYWORDS    RefSeq.
SOURCE      Deinococcus radiodurans
  ORGANISM  Deinococcus radiodurans
            Bacteria; Thermotogati; Deinococcota; Deinococci; Deinococcales;
            Deinococcaceae; Deinococcus.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Deinococcus radiodurans"
                     /db_xref="taxon:1299"
     Protein         1..395
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39872
     Region          213..275
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
     Region          326..>371
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mtrartpspg rpsprrprrp agprrwpelv aatlvlalgv glgslllger rapaepvgap
       61 qpttsipvsp gavvadgspq taapaqaqtt agkippapaa ppapkipppv lpeprrmpap
      121 ptpprpveet ttaaspitqp pvtqapatqt ptpqtpaaqa patqppatpa pepaapaepa
      181 pattpepatp tepaapapgt pavapsaqrt plrsdyrvml gtfgseaalr satagvsalg
      241 ytvyaidlgn qfvaqvgpfa deasgqqaaa dirrayarae lypprgqtlr npapaaaaea
      301 patpepasep aptpaetpta apapagpvyv qvgafnnveg aqrfveqlra qgfspsvnap
      361 etgkvtvllg pltgsdltst egrldaagld hfrlr
//
LOCUS       WP_010888203             278 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Deinococcus
            radiodurans].
ACCESSION   WP_010888203
VERSION     WP_010888203.1
KEYWORDS    RefSeq.
SOURCE      Deinococcus radiodurans
  ORGANISM  Deinococcus radiodurans
            Bacteria; Thermotogati; Deinococcota; Deinococci; Deinococcales;
            Deinococcaceae; Deinococcus.
REFERENCE   1  (residues 1 to 278)
  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   2  (residues 1 to 278)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Deinococcus radiodurans"
                     /db_xref="taxon:1299"
     Protein         1..278
                     /product="aminoglycoside 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=31340
     Region          26..202
                     /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(27..30,33,35,44,46,69,85..88,167,171..172,174,
                     185..186)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Region          115..260
                     /region_name="CotS"
                     /note="Thiamine kinase or a related kinase [Coenzyme
                     transport and metabolism]; COG0510"
                     /db_xref="CDD:440276"
ORIGIN      
        1 mrgsnfssaa pahfpvlear ygpltpmdsg mqsrvystpg geavvkvyrn hqgehrteaa
       61 nmrraglgew vvdateadgi ealvlrrfsg rpltredvtr alpalrtqla alhqhregrv
      121 dlrrvqerlr rfrsslsgyg lsdlfeavev pldqglfdqp aafchldlwh dnilmnresg
      181 evliidwtka apddplrdla llktgtldll padeslsaal tflpdqqpat lrryrayvam
      241 ttlhdlywfl mnepyefdsq rekkiprarh vlarlpge
//
LOCUS       WP_010888490             126 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Deinococcus radiodurans].
ACCESSION   WP_010888490
VERSION     WP_010888490.1
KEYWORDS    RefSeq.
SOURCE      Deinococcus radiodurans
  ORGANISM  Deinococcus radiodurans
            Bacteria; Thermotogati; Deinococcota; Deinococci; Deinococcales;
            Deinococcaceae; Deinococcus.
REFERENCE   1  (residues 1 to 126)
  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   2  (residues 1 to 126)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Deinococcus radiodurans"
                     /db_xref="taxon:1299"
     Protein         1..126
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13224
     Region          60..125
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mlpherlwqv alaagallvg gltlgpallp rpqlptvtrt alppvqadan aeprtyptta
       61 svtplisgrv nlntasqeql ealpkvgpam akkiiagrpy hsladldrvk gvgeatlrtl
      121 tplvkw
//
LOCUS       WP_010889227             195 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Deinococcus radiodurans].
ACCESSION   WP_010889227
VERSION     WP_010889227.1
KEYWORDS    RefSeq.
SOURCE      Deinococcus radiodurans
  ORGANISM  Deinococcus radiodurans
            Bacteria; Thermotogati; Deinococcota; Deinococci; Deinococcales;
            Deinococcaceae; Deinococcus.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Deinococcus radiodurans"
                     /db_xref="taxon:1299"
     Protein         1..195
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20286
     Region          8..194
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 msdapsgppr lvvgvsggsg ipyaldilra lrgldvethl vvssgakrvm saeggpqlad
       61 ltalasvvhd drdlaaavas gsyrtggmli vpcsagtlak vahgfadnli sraahvtlke
      121 rrplvlvvre dpmprpmlqn mlaahdagat vmsaspgfyh apeslgellg fvtarvldqf
      181 glnapgfrrw redea
//
LOCUS       WP_010889397             309 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Deinococcus radiodurans].
ACCESSION   WP_010889397
VERSION     WP_010889397.1
KEYWORDS    RefSeq.
SOURCE      Deinococcus radiodurans
  ORGANISM  Deinococcus radiodurans
            Bacteria; Thermotogati; Deinococcota; Deinococci; Deinococcales;
            Deinococcaceae; Deinococcus.
REFERENCE   1  (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   2  (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   3  (residues 1 to 309)
  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   4  (residues 1 to 309)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Deinococcus radiodurans"
                     /db_xref="taxon:1299"
     Protein         1..309
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=32690
     Region          1..305
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 miefqnviks fggpavlqdi sltvptgelv iligpsgcgk stllrlvnrl leptsgdirv
       61 ggvsvleqdp valrrrlgyv iqsvglfphl tvqenvelvp sisgvgretr aaralellsl
      121 mglepgqyag ryprqlsggq qqrvgiaral aadpeyllmd epfsaldpit rarlqeqflt
      181 lkreigktiv fvthdvdeav rlgdricvlg ngtvqqyaap eeilrhpand fvasfvgegr
      241 elrslslrpv salmrpgagd gqalgtvaad lpadqalsrl lgagnrtlnv vdsggavvgt
      301 lsladfgaa
//
LOCUS       WP_010889767             714 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Borreliella burgdorferi].
ACCESSION   WP_010889767
VERSION     WP_010889767.1
KEYWORDS    RefSeq.
SOURCE      Borreliella burgdorferi (Borrelia burgdorferi)
  ORGANISM  Borreliella burgdorferi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Borreliaceae; Borreliella.
REFERENCE   1  (residues 1 to 714)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 714)
  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   3  (residues 1 to 714)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..714
                     /organism="Borreliella burgdorferi"
                     /db_xref="taxon:139"
     Protein         1..714
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79259
     Region          1..713
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdssdvidkf knsfkeesie nisdieqall nlevssdqdi vnsifrnlht ikgssgmfgf
       61 nftaslvhei etvldvvkng kaafnqaaid atlmsvdfir eliegdevis eidfdkrkqf
      121 lvneirkvld isndvkgafq ealendfsks dnssvleesv kvnsenkfdd ealqsefksy
      181 kilfspakgi lfhghkpinl lsklinlgsg yvrakvdnip dlelispdnv yvdweirldt
      241 eesresiedi ftfldsqski diqeldkcle anegdnvesk nfnllhldrn skdltnssfe
      301 ksafvgksff ngdknrsniq ddtarskvni asikvdskkl dhlvnlvgel vtiqsklske
      361 aenrnsniln sisaefslli nelrdyttgl rtvpieilfv kfqrivkdls tslgksilyh
      421 asggdtvldk siieklnepl vhlirnsidh giesaqeres lgkdpkgiik lsacqsgdsv
      481 iviieddgrg ldknkilkka ierniisdsv aktlseidvy nlifepgfst assvtdisgr
      541 gvgmdvvkkq veslrghvvl esefgkytri klifpltlai iegwlvrvkd ehfivplsnv
      601 esclesnkli sqidgietks nvmnyrgsmi syirlreffq vssekslseq vvvvntnsgk
      661 mgivvdevlg qhqtvikalg kiysrvegvs gatilgdgsl alvvdidait klik
//
LOCUS       WP_010894263             208 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Xylella fastidiosa].
ACCESSION   WP_010894263
VERSION     WP_010894263.1
KEYWORDS    RefSeq.
SOURCE      Xylella fastidiosa
  ORGANISM  Xylella fastidiosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xylella.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Xylella fastidiosa"
                     /db_xref="taxon:2371"
     Protein         1..208
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22431
     Region          <24..163
                     /region_name="DamX"
                     /note="Cell division protein DamX, binds to the septal
                     ring, contains C-terminal SPOR domain [Cell cycle control,
                     cell division, chromosome partitioning]; COG3266"
                     /db_xref="CDD:442497"
ORIGIN      
        1 mlvralilvl vvlnfgvalw wrnqsapkvp vpvaasspvg vpqlellpmi qvekpksldt
       61 pihkvstycy nvgpftsead artvlatlgk dvdkgmiral qsgdsnnyrv vmsasdhasa
      121 qalakrivga gfrdyyvlgn evilgqyrnr egakrmradl aaagfqanvl sgdvsgweih
      181 lrsaiefaal qvrlngyhig sldcatlr
//
LOCUS       WP_010895452             597 aa            linear   BCT 20-JAN-2025
DEFINITION  sensor histidine kinase [Vibrio cholerae].
ACCESSION   WP_010895452
VERSION     WP_010895452.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cholerae
  ORGANISM  Vibrio cholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 597)
  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 597)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20493667
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Vibrio cholerae"
                     /db_xref="taxon:666"
     Protein         1..597
                     /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=67972
     Region          30..242
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          270..590
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mpsirrlslm lwvmfivlvs msthlywrfq yqallnehqs qldrfsshiv atldkyahip
       61 hliskdkelv dallsaqnsa qiditnryle qvneviqaad tylidrfgnt iassnwnldr
      121 sfigrnfawr pyfylsiagq ksqyfalgst sgqrgyyyay pviyaaeilg vivvkmdlsa
      181 ieqgwqnkss yfvatddhqv vfmssqpawl fhsvadlspa qlndirqsqq yldspipslg
      241 wqgdlqaeqs ewrkpekhwl qddyivssrp lpelaltirv lspkielfws afglviilcm
      301 lfaivylgfq lwhhrqlrqr qieqlqqetk qklefevmer taklhaeiae riktehalrq
      361 tqdeliqaak lavlgqmsas ishelnnpla airsfadngr rflatnkper aeenlsrisa
      421 ltermakise qlksfarkst sneqqdvqly plilsakelm tgqfkaqmtl lelcdletpv
      481 wvrvnpiqle qvlinlltna lqalegqaer vvqirlqtse qqialfvddn gpgvgietlp
      541 hlfepfhttk knglglglsi sqqilhsmqg tlsvatsplg garftitlpr ftplnmd
//
LOCUS       WP_010895557             321 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010895557
VERSION     WP_010895557.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 321)
  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 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 12071874
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35312
     Region          37..188
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          216..295
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msaslpdsea irsadrqrmv allenlapqe gynltgldcv rllrsdrpla rtpvlydpgi
       61 vivcqgrkrg yfgeqiylyd eqhylavavp vpftmetdat perpllaiyl hldfplaagl
      121 aveidrqral aqveaprslm sspmdaplra svlrflealg dpletailap allrelyfrv
      181 ltgpqggamr aalamrgrfg niaralrrih aqyaeplela qlageagmsv psfhshfkai
      241 tqtspmqylk ctrlhqarll mvrqgmsaqa achavgyasa sqfnrefkrl fgrsplaear
      301 rlragfslpp aqgeaeyvss h
//
LOCUS       WP_010897630             170 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Halalkalibacterium halodurans].
ACCESSION   WP_010897630
VERSION     WP_010897630.1
KEYWORDS    RefSeq.
SOURCE      Halalkalibacterium halodurans
  ORGANISM  Halalkalibacterium halodurans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Halalkalibacterium (ex Joshi et al. 2022).
REFERENCE   1  (residues 1 to 170)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Halalkalibacterium halodurans"
                     /db_xref="taxon:86665"
     Protein         1..170
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=18549
     Region          30..153
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(109..110,113,126..129,131)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mrqllivflv astlsplwpi gpnptvgdpf livniatnrl ayvdegkiqk ivpiatgkps
       61 dktpvglfti tvkaeqpyyr kkniaggdpk nplgtrwlgf dakdtegrty gihgtnrpes
      121 igryvtagci rlqnkeveel yaniplgtki livdyvvsfe alakehgame
//
LOCUS       WP_010898011             156 aa            linear   BCT 20-JAN-2025
DEFINITION  3-hydroxyacyl-ACP dehydratase FabZ family protein
            [Halalkalibacterium halodurans].
ACCESSION   WP_010898011
VERSION     WP_010898011.1
KEYWORDS    RefSeq.
SOURCE      Halalkalibacterium halodurans
  ORGANISM  Halalkalibacterium halodurans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Halalkalibacterium (ex Joshi et al. 2022).
REFERENCE   1  (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 10101294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Halalkalibacterium halodurans"
                     /db_xref="taxon:86665"
     Protein         1..156
                     /product="3-hydroxyacyl-ACP dehydratase FabZ family
                     protein"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=17743
     Region          19..149
                     /region_name="FabZ"
                     /note="FabZ is a 17kD beta-hydroxyacyl-acyl carrier
                     protein (ACP) dehydratase that primarily catalyzes the
                     dehydration of beta-hydroxyacyl-ACP to trans-2-acyl-ACP,
                     the third step in the elongation phase of the bacterial/
                     plastid, type II, fatty-acid...; cd01288"
                     /db_xref="CDD:238615"
ORIGIN      
        1 mvsvldkinv telrpgnmll qqppflfvdr ilefdeetit cskylshnep ffsghfptqp
       61 impgvliief aaqasllltm lqlneleplm gylvktenft fhalaepgte leakvkmlkk
      121 mgnyyttqvt vrrsdnkkkv akgqlvfyld eegker
//
LOCUS       WP_010898439             290 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Halalkalibacterium halodurans].
ACCESSION   WP_010898439
VERSION     WP_010898439.1
KEYWORDS    RefSeq.
SOURCE      Halalkalibacterium halodurans
  ORGANISM  Halalkalibacterium halodurans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Halalkalibacterium (ex Joshi et al. 2022).
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Halalkalibacterium halodurans"
                     /db_xref="taxon:86665"
     Protein         1..290
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32694
     Region          6..264
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mslsrnsdlh mhstasdggy sptelmekch qanlkfvalt dhdtvngiee akqtahrlgf
       61 ilipgielst kasgqsvhml gygidwkndt lkrrldrqqd irkqrleqil lklkaagvpl
      121 eqdavlryad ggaigrphva kalmdkgyvr svqeafehyl aegrpcyvkr qeyisveqai
      181 awihqaggva ivahpgyydl ddqligwvre ygldgievyh rdhsrevvah yeqlckrmea
      241 etgrrllrtg gsdfhhesyg rtaaplgttr ipdqltyell hdlerkktra
//
LOCUS       WP_010897796             225 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Halalkalibacterium halodurans].
ACCESSION   WP_010897796
VERSION     WP_010897796.1
KEYWORDS    RefSeq.
SOURCE      Halalkalibacterium halodurans
  ORGANISM  Halalkalibacterium halodurans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Halalkalibacterium (ex Joshi et al. 2022).
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 225)
  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   3  (residues 1 to 225)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Halalkalibacterium halodurans"
                     /db_xref="taxon:86665"
     Protein         1..225
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25748
     Region          19..221
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 miaigdtiyl ektgeqgene eaeryycrlv drlnqemvid vpiheqtkkp slfpegtpfr
       61 ahflgkdgam yifestiker rretipvlvf ndpgpeiykr iqrrqdvrvs atvdcaihpt
      121 entaftpfra ttvdisgggc aivlpngrsl pgdgeidivl alhlqssdmf fvearckivr
      181 lhkrheeals rvslqfisie erhkekiirf cferqlqdkq llfds
//
LOCUS       WP_010898117             516 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Halalkalibacterium
            halodurans].
ACCESSION   WP_010898117
VERSION     WP_010898117.1
KEYWORDS    RefSeq.
SOURCE      Halalkalibacterium halodurans
  ORGANISM  Halalkalibacterium halodurans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Halalkalibacterium (ex Joshi et al. 2022).
REFERENCE   1  (residues 1 to 516)
  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 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   3  (residues 1 to 516)
  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   4  (residues 1 to 516)
  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 516)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Halalkalibacterium halodurans"
                     /db_xref="taxon:86665"
     Protein         1..516
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=59298
     Region          256..508
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          426..506
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mihviiated atfadrlksi ivsaqnqfsr laisdsdqkm lqlvkdlfti ilidetdlpl
       61 qnnmdliqti qkqhpktqtv llrnrknfnd eimkteqssk hsapeivlkn vlhemfqeiv
      121 qkqencyetf vrslihgdlg tgvsftnshr yrhhllvlcc aglvssfdqs keipaqvfwk
      181 qsdwqerlsv qlkgiaecti vdgatpsekw lmisfyqqqk dhsvqhwiel vgnllnqgmn
      241 vtishsnlfh sfdevreltk mlrmvlikhi rlavsgcfsl adlertvadp apdpifekef
      301 afaleqrdlk lvknvlyglf vqwqetkpqq nylarqlmgi likiqqvfhc sssytldlfy
      361 adlsdamlra ldyddlyrst crmidlfaav akdivegqhh dndllaqeie ayidehfpep
      421 inhqtlsqrf glvpsylski fsrykgispa kyivklrlea tkelllenpg ltikdiayvv
      481 gfedpsylsr ifkretglsp sefrkqqkvl ptvdds
//
LOCUS       WP_010898906             386 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Halalkalibacterium
            halodurans].
ACCESSION   WP_010898906
VERSION     WP_010898906.1
KEYWORDS    RefSeq.
SOURCE      Halalkalibacterium halodurans
  ORGANISM  Halalkalibacterium halodurans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Halalkalibacterium (ex Joshi et al. 2022).
REFERENCE   1  (residues 1 to 386)
  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 386)
  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
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 386)
  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   5  (residues 1 to 386)
  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   6  (residues 1 to 386)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 386)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Halalkalibacterium halodurans"
                     /db_xref="taxon:86665"
     Protein         1..386
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41990
     Region          81..379
                     /region_name="ASKHA_ATPase_ROK_BsXylR-like"
                     /note="ATPase-like domain of Bacillus subtilis xylose
                     repressor (XylR) and similar proteins; cd24076"
                     /db_xref="CDD:466926"
ORIGIN      
        1 msvtgdqrfi kqmnkqivlq tirkeaplsr aqvslttgln kgtvsslvae liadnlvyev
       61 gpgessggrr pvmlmfqnka ayaiginiav nylsgvltdl vgnviekvew slhvkefdhv
      121 nqqmvqlieq lmkaappsty giigigvavp givneegdvl fapnlnwrei plkkqleehf
      181 qlpiavenea nagalgekvf gkgkesenmi ffsigigigs giifgnslyr gkggysgevg
      241 hmsietngpl ctcgnkgcwe lfasekavlq qgealyeevl tlddlfekar kgeqtaidlf
      301 qkigvylgtg ianminalnp elvvvgnrmv kgrpwlehsl kqtvadrals fhaeqvlvef
      361 sdlnengisl gvsyllidsf lekkhe
//
LOCUS       WP_010899091             656 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Halalkalibacterium halodurans].
ACCESSION   WP_010899091
VERSION     WP_010899091.1
KEYWORDS    RefSeq.
SOURCE      Halalkalibacterium halodurans
  ORGANISM  Halalkalibacterium halodurans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Halalkalibacterium (ex Joshi et al. 2022).
REFERENCE   1  (residues 1 to 656)
  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 656)
  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 656)
  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 656)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Halalkalibacterium halodurans"
                     /db_xref="taxon:86665"
     Protein         1..656
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=71037
     Region          13..648
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mtekqtidep klspeeqeil ekydaesrfr tfsgkklpll vsllaiglsl yhlytsyfgt
       61 pltlqhrslh vavilalvff lyppfkkanr ksvplydwlc vllalsttiy ffvdyagivh
      121 rggipntydl lfgvilvili leaarrvtgw alpllavlff iyglfgrels giwrhrgygw
      181 delinfmyvt tegvygtaig vsatyiflfi lfgaflsksg mgqffndmal aiagqtkggp
      241 akvsviasgf lgsingaaia nvvttgsfti plmkkigyhr nfagaveaaa svggqilppi
      301 mgaaafimae ilgipysqia laallpallf ylaiivqihl ratklglkgi skenlpqvmd
      361 vlkerghlli plffllymlf fsgrtiiysa fltiivtvfv amfrkttrmt irdlldaleq
      421 garnaigvav acacvgiivg vatmtgfglk langivmlgg eslfltlfft miaciilgmg
      481 lpsiptyiit atmaapalvt lgieplvahl fvfyfglfan itppvalaaf aaagisggdq
      541 mktgfismkl aiagfivpym fvyneallll nttfiegalv vvtsitgvvm lgaaaegylf
      601 tkiplflril lfggallfmn pnlvqdlmgf aiigfvllyq wwrgkkqava setvsl
//
LOCUS       WP_010905886             390 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Lactococcus lactis].
ACCESSION   WP_010905886
VERSION     WP_010905886.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus lactis
  ORGANISM  Lactococcus lactis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Lactococcus lactis"
                     /db_xref="taxon:1358"
     Protein         1..390
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44770
     Region          1..277
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          272..367
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkflhtsdwh igrtlngfsl leeqkyafeq ilslakqnqv dgiiiagdly eravpsaesv
       61 itfnqmlrem niiekfpiym isgnhdgakr lsyakdwldy nnlhlrtsle eafipvetke
      121 tqifllpffd pmdariyfsn qgldeedtkq iktiddamtl viskmksqfn nkknqvlvth
      181 favsphkeei vltsetpskv gglstlnvsq fadfdyvalg hihtrlasps dkvqysgspv
      241 kfntkeastq kgifvveike kmlnsnflpl qvktdlvvle eeweqlisrd fyerqplnka
      301 wfaitiknfd rtklvgqnlr aqlqkiygti ieldyqfekk qltrsrsqdi etldnveils
      361 sfykfttget lddvqtaiie stfnelegek
//
LOCUS       WP_010906801             636 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Pasteurella multocida].
ACCESSION   WP_010906801
VERSION     WP_010906801.1
KEYWORDS    RefSeq.
SOURCE      Pasteurella multocida
  ORGANISM  Pasteurella multocida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Pasteurella.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Pasteurella multocida"
                     /db_xref="taxon:747"
     Protein         1..636
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=72466
     Region          64..522
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mskelkmhtn nlvakniekl talfpncite tqnaegkiik cvdfdllrqe lsetiiegdk
       61 eryrldwvgk keailtanap iaktlrpcre esvnfdttqn lfiegdnlda lkllqetylg
      121 kvkmiyidpp yntgndfiyn ddfaetvddf larsnqvdee gnrlvtntes ngryhsdwls
      181 mmysrlklar nlltddgvif isiddneqan lkricdeifg eknfistipr qtsaqrpsqe
      241 kyvsithdyi lvyakvkkhn fqhvikrdlr dlkqdangly iegdtspila sstqgyssgg
      301 dydiefkgki yqpidsngnr rrwlwtkprm ekaislnlvv etkttlrvqn yinkefqvgt
      361 nilvdknpnl ilttndlisp yyvnqkatsm lnelnlnkvf dfskpvalie llvnlsalqe
      421 ndiildffag ssttahavmq fnaenggnrr fimvqlpekt eekseayksg yqtiaeiske
      481 rirragnkil adnagkegik qldigfrvlk idssnmkevy ytpdnlsqtl ldhmesnike
      541 drsaedllfq vmldwgiels lpieqksvgn silyyvggns lvacfdaltl dvineiakhq
      601 plrvvscesa iqhdqdktni kerfkqlspe tdvrfl
//
LOCUS       WP_010907253             191 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Pasteurella multocida].
ACCESSION   WP_010907253
VERSION     WP_010907253.1
KEYWORDS    RefSeq.
SOURCE      Pasteurella multocida
  ORGANISM  Pasteurella multocida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Pasteurella.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Pasteurella multocida"
                     /db_xref="taxon:747"
     Protein         1..191
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21516
     Region          3..164
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mkifgamydk tmawskhrya tfflaltsfi eaiffpippd vmlipmsisq pqralklafy
       61 tavasvlggv igyglgyyav dfvqhyvqqf gyqqhwetai swfekwgilv vfvagfspip
      121 ykvfticagv mqmlflpfvl tafisraarf ilvaklaawg gekfadklrr sieligwsvv
      181 liaviaylil r
//
LOCUS       WP_010909114             355 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Mesorhizobium japonicum].
ACCESSION   WP_010909114
VERSION     WP_010909114.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium japonicum
  ORGANISM  Mesorhizobium japonicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 355)
  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 355)
  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   3  (residues 1 to 355)
  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   4  (residues 1 to 355)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 355)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 355)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 355)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Mesorhizobium japonicum"
                     /db_xref="taxon:2066070"
     Protein         1..355
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36862
     Region          26..344
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(90..92,113..114,166,218,242)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mrpgatisaa lawlflagaa saqtltigva aplsgpsail gkqieagaal aaqadgvelk
       61 teddactadg gaaaarvfaa akvsvvigfl cteaieaamp ilkdanipvi tvgvrteslt
      121 drraktgwpv yrlgprgdde rnavastlth lwqkelfaii ddgtiygrem aetfraaaeq
      181 aalkpvfvdt frpqldnqig migrlkkaga thvfaggdgd diaimgrdaa qlqagivfag
      241 genlrtppgd vpyatgtlmi appewadvad akvlesfsvq kivpdgytlp afaaveiaka
      301 astlspgkpl tevlsghdfa taigpvrfda kgdlsqspyr vfrfdgarfv plesn
//
LOCUS       WP_010910344             346 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Mesorhizobium].
ACCESSION   WP_010910344
VERSION     WP_010910344.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium
  ORGANISM  Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Mesorhizobium"
                     /db_xref="taxon:68287"
     Protein         1..346
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38274
     Region          1..345
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mevrvanvrk eferfpalhd vsldiksgel iallgpsgsg kttllrliag lerptrgkif
       61 fgdedasqks iqernvgfvf qhyalfrhmt vadnigfglk vrhgssrppa qeirrrasel
      121 ldlvqlsgle krypaqlsgg qrqrvalara maiepkvlll depfgaldaq vrrelrrwlr
      181 eihdrtghtt vfvthdqeea leladrvvvm sqgrieqvgt addiydtpns pfvygfiges
      241 sslpvkveng eiwladrpig lsaphapege atlyfrphdv elldgcsgci agtvaasrrv
      301 agtrrvelei ggerqrveie lpvghpaaqk srvafrpgrw klfpaa
//
LOCUS       WP_010910760             165 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Mesorhizobium].
ACCESSION   WP_010910760
VERSION     WP_010910760.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium
  ORGANISM  Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Mesorhizobium"
                     /db_xref="taxon:68287"
     Protein         1..165
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17204
     Region          8..163
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfaakaidts dkaafysdla aqlkalldge sdsianaant aalifqmvpd lnwagfyfla
       61 sdeelvlgpf qgkpacvria vgkgvcgtav qlgtsmlikd vhdfpghiac dadsrselvv
      121 lleddegvfg vldldsplpg rfdkadqagi etlaaiyaaa ssfed
//
LOCUS       WP_010911793             144 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Mesorhizobium japonicum].
ACCESSION   WP_010911793
VERSION     WP_010911793.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium japonicum
  ORGANISM  Mesorhizobium japonicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Mesorhizobium japonicum"
                     /db_xref="taxon:2066070"
     Protein         1..144
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15136
     Region          5..142
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mvalygalfi saflaatvlp vsseavlagm ivsgrgdpwl lltvatignt lgsvvnwvlg
       61 rgidglrnrr wfpvtadrye qacrtfrrfg ewtllfawlp vvgdaltlaa gaarvnlavf
      121 valvatgkaa ryavivaggl wata
//
LOCUS       WP_010911875             436 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Mesorhizobium japonicum].
ACCESSION   WP_010911875
VERSION     WP_010911875.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium japonicum
  ORGANISM  Mesorhizobium japonicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Mesorhizobium japonicum"
                     /db_xref="taxon:2066070"
     Protein         1..436
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=44979
     Region          52..130
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
     Region          180..262
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
     Region          333..413
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mirtllatta latlistgaf aqstttpapa tapsvqepaa avpvpraegn ivtniigesv
       61 yngtgddaen igkvsdvvfd kdgmaksvvi gvggflgvgt knvafdydkl qwaekngdrw
      121 lvaqttkdel kahpefdskp ygsapapats tdaaapktpa atdtaqapaa apaepvkrad
      181 gnlatniigk tvyngtgdda qnigsvndiv lskegkaesl vigvggflgl gaknvtydfn
      241 kaqwaekngd rwlvaqttke alqaqpdfnr kaydpapatt asnapaatap aattapatap
      301 tgktaeapaa ttapdqtqta aidkstltam pvgeikasdl kgttvygand akvgeigdvv
      361 ltpdkktdav ivnvggflgi gtkevavgld nlkfmtdkng kkylyttftk eqleaqpayd
      421 kgsyaekrdq qrmivk
//
LOCUS       WP_010913001             369 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Mesorhizobium
            japonicum].
ACCESSION   WP_010913001
VERSION     WP_010913001.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium japonicum
  ORGANISM  Mesorhizobium japonicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 369)
  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 369)
  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 369)
  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 369)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Mesorhizobium japonicum"
                     /db_xref="taxon:2066070"
     Protein         1..369
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40104
     Region          1..359
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mdrrsfirka gvtgvgaaaa aatlaapaia qsnpkvtwrl assfpksldt iyggaevfsk
       61 mlseatdgnf qiqvfaagel vpglqaadat tagtveacht vayyywgkdp twalgaavpf
      121 slnargmnaw hyhgggidlf neflatqglf glpggntgvq mggwfrkein tvadlaglkm
      181 riggfagkvv qklgvvpqqi aggdiypale kgtidaaewv gpyddeklgf ykvapyyyyp
      241 gwweggptvh lmfnkakyde lspayksllr taaqaadadm lqkydyvnpa avkrlvagga
      301 klrpfsqeim aacfekanev yaemeasnap fkriwesikg frkehylwaq vaeynydtfm
      361 mvqqrngkl
//
LOCUS       WP_010912621             576 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Mesorhizobium japonicum].
ACCESSION   WP_010912621
VERSION     WP_010912621.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium japonicum
  ORGANISM  Mesorhizobium japonicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Mesorhizobium japonicum"
                     /db_xref="taxon:2066070"
     Protein         1..576
                     /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=63844
     Region          1..285
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 matretwlda akgvgillvv aahiagagtd pwdpffanav flfhmplffv isgyvykpae
       61 raqlfwkkva slavpyvafl lvltlavisr rtllrdfpar welgemavnd llggmrlwrd
      121 fgvfwfvtcl fftqliynei anwtkspgsp rmlgfvaffv llgyaiqfew qmnsspwava
      181 avpialccyw fghllrtyqf rpgtlwsfva avcalavaea asgaeiqfnm kysifgppvl
      241 gllialalsl allmlvrkaa aveklavpva klgeaslvim flhqffqfsl rdfgvsneav
      301 imafavsgpf aiylllrrst llspwflgtg agapghaiaw frngvgwrva kyqdqligfa
      361 kpyaaqvlia lrwplrgkgr phglpgeliv sltsypkrfp tlhltlrcll sqtiapnrvi
      421 lwltaedaaq lpasvtdlkc hgleirfckd irsykkiipt llafpsayiv tetmmsitrg
      481 ggwnslsier vkkpsfviea trlhsmmrge lsltanghlm spkpwecffp pvwvecsmap
      541 nrsrqkqwmr tssptsvpka misgcsgwag awaapt
//
LOCUS       WP_010915329             280 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Mesorhizobium japonicum].
ACCESSION   WP_010915329
VERSION     WP_010915329.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium japonicum
  ORGANISM  Mesorhizobium japonicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Mesorhizobium japonicum"
                     /db_xref="taxon:2066070"
     Protein         1..280
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=30633
     Region          155..230
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mldtrsqsek ppvgnnmkfv kvaaplalfc algvspafav cnisdaklee avlkspelrk
       61 penrylvhdl rtlrdaafvl wtyglhddce rvlanirqli aapsmaklag ndedladeql
      121 aagepkqheg gdiqgnrdap darplinldd lgpglrvdei vgsevrssdd kivgevrnvv
      181 igtkdrwdya vvasggffia gkdsivvplr ylqvneerts fylrissadv kavplmpdqk
      241 ylwladeawr akndaifqkl ipdpvrsgtp svpqantdsk
//
LOCUS       WP_010915724             388 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Mesorhizobium].
ACCESSION   WP_010915724
VERSION     WP_010915724.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium
  ORGANISM  Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae.
REFERENCE   1  (residues 1 to 388)
  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 388)
  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
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 388)
  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   5  (residues 1 to 388)
  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   6  (residues 1 to 388)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 388)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 388)
  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 12137909
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Mesorhizobium"
                     /db_xref="taxon:68287"
     Protein         1..388
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41137
     Region          16..58
                     /region_name="HTH_24"
                     /note="Winged helix-turn-helix DNA-binding; pfam13412"
                     /db_xref="CDD:404317"
     Region          78..359
                     /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 malrgtnqef grpynrrivl esirlhgpia rgeiasrvgl tvqtvstivr eleeqgyils
       61 vreeprgrgl ppatlrinpe ggyavgihit plginaalin lsgdviesty reapnatpdh
      121 afemigamvi eltglraggr vlgvglalpg pfgvesmsfv gpttmtgwqd valrerlaas
      181 tglpaffetd maaaamgerl yglgaqfsey yylyfgvglg gvmvhegsvq rgawgnagev
      241 ghipvvpgge acpcgnrgcl erylslealr rwngteadwv aevapifhna vavienlfdp
      301 etvilgglas tdllerlags tgglhnsvsa rkdriaprlm varggqhsvl rgaaalavsg
      361 vlsprfgqmf aaerergrdl ltakeiaa
//
LOCUS       WP_010918321             762 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Caulobacter vibrioides].
ACCESSION   WP_010918321
VERSION     WP_010918321.1
KEYWORDS    RefSeq.
SOURCE      Caulobacter vibrioides (Caulobacter crescentus)
  ORGANISM  Caulobacter vibrioides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Caulobacter.
REFERENCE   1  (residues 1 to 762)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 762)
  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   3  (residues 1 to 762)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..762
                     /organism="Caulobacter vibrioides"
                     /db_xref="taxon:155892"
     Protein         1..762
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=80019
     Region          1..753
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdeleaikvt ffqeceella dleggllame egagdletvn avfravhsik ggagafglep
       61 lvrfahvfet lldavragsv pntvelaavl lrasdiladh vsaarglgdv dmaasaamaa
      121 eleqwtdpna tptapapvaa ptvaeepapa paligaddda mdgddlgfvf vpqtitveaq
      181 aadaelipsn vwtvsirpks dlyrkaneta lllrelsrlg pikatlddsa lpllqnldpe
      241 aafitwsvrl etdqdetair evfefvdgdc dleitrgegs veasiaalta paepvaavep
      301 iapapepvev appiappaaa pvaevapave aakpaaaapa aaaaaapkat pvevpgpgqs
      361 virvdperid rlidlvgelv inqamlaqrv geygiapssn lamgldeleq ltreiqdsvm
      421 airaqpvksv fqrmprlvre vanmtgkqar lvmdgentev dktvierlsd pithmlrnai
      481 dhglespeer kaagknpegv vrlaalhrsg rivievsddg kginrervfg iavkkgliap
      541 dlqltdeeid nliflpgfst aekisdvsgr gvgmdvvkrs vqalggrisi ssrpgqgstf
      601 tlslpltlav ldgmvvdvag etlvvplaai veslrpkpee vrplgpvgsv lavrdsfvpl
      661 idvgltlgyr eesphptdgv vllvegedgs raalvadaih gqrqvviksl eqnyqqvegv
      721 aaatilgdgr valildvdat inlrrregga prppepslia ae
//
LOCUS       WP_010918496             430 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Caulobacter vibrioides].
ACCESSION   WP_010918496
VERSION     WP_010918496.1
KEYWORDS    RefSeq.
SOURCE      Caulobacter vibrioides (Caulobacter crescentus)
  ORGANISM  Caulobacter vibrioides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Caulobacter.
REFERENCE   1  (residues 1 to 430)
  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 430)
  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 430)
  AUTHORS   ter Beek,J., 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 430)
  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 430)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Caulobacter vibrioides"
                     /db_xref="taxon:155892"
     Protein         1..430
                     /product="CmpA/NrtA family 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=45911
     Region          44..302
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mimtktdkpt sgltrrsalm gaaatlaaak aafpggahaa gagpevakar lgfialtdss
       61 pliiakergl fakygmpdie vvkqaswaat rdnlvlgaer ggidgahilt pmpylmttgt
      121 itggaptpmy ilarlntngq gisvgndlks vkvglnsaga kakflqmkaa gniakvamtf
      181 rggthdlwir ywlaagginp dvdvstivip ppqmvanmka gtqdafcvge pwngqlvnqk
      241 vgytacltse lwmnhpekal gmraswvdry praaqaitaa vqeaqmwcdk aanlpqmcsi
      301 vsgrqyvnvp mgdilprlqg tvdygdgrtl knsphrmkfw adnasfpfks hdlwfltedi
      361 rwgvlpqktn tkalvdkvnr sdiwraaaks igqsgpagds rgverffdgk vfdpanpgay
      421 lasqpikklv
//
LOCUS       WP_010920916              96 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Caulobacter vibrioides].
ACCESSION   WP_010920916
VERSION     WP_010920916.1
KEYWORDS    RefSeq.
SOURCE      Caulobacter vibrioides (Caulobacter crescentus)
  ORGANISM  Caulobacter vibrioides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Caulobacter.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Caulobacter vibrioides"
                     /db_xref="taxon:155892"
     Protein         1..96
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10401
     Region          1..93
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mtldealtkl raakplldry gvarvgvfgs targeagpds dvdvlvefap ekhpgldffr
       61 lqddlanvla seidlvtpdg lhrlvrdrvl revaya
//
LOCUS       WP_010922059             439 aa            linear   BCT 20-JAN-2025
DEFINITION  AAA family ATPase [Streptococcus pyogenes].
ACCESSION   WP_010922059
VERSION     WP_010922059.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus pyogenes
  ORGANISM  Streptococcus pyogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Liu,Y., Sung,S., Kim,Y., Li,F., Gwon,G., Jo,A., Kim,A.K., Kim,T.,
            Song,O.K., Lee,S.E. and Cho,Y.
  TITLE     ATP-dependent DNA binding, unwinding, and resection by the
            Mre11/Rad50 complex
  JOURNAL   EMBO J 35 (7), 743-758 (2016)
   PUBMED   26717941
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Chen,Z., Luong,T.T. and Lee,C.Y.
  TITLE     The sbcDC locus mediates repression of type 5 capsule production as
            part of the SOS response in Staphylococcus aureus
  JOURNAL   J Bacteriol 189 (20), 7343-7350 (2007)
   PUBMED   17704228
REFERENCE   3  (residues 1 to 439)
  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   4  (residues 1 to 439)
  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
REFERENCE   5  (residues 1 to 439)
  AUTHORS   Hopfner,K.P., Karcher,A., Craig,L., Woo,T.T., Carney,J.P. and
            Tainer,J.A.
  TITLE     Structural biochemistry and interaction architecture of the DNA
            double-strand break repair Mre11 nuclease and Rad50-ATPase
  JOURNAL   Cell 105 (4), 473-485 (2001)
   PUBMED   11371344
REFERENCE   6  (residues 1 to 439)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Streptococcus pyogenes"
                     /db_xref="taxon:1314"
     Protein         1..439
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48856
     Region          5..>182
                     /region_name="SbcC"
                     /note="DNA repair exonuclease SbcCD ATPase subunit
                     [Replication, recombination and repair]; COG0419"
                     /db_xref="CDD:440188"
     Region          <125..>310
                     /region_name="COG4913"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal ATPase domain [Function unknown]"
                     /db_xref="CDD:443941"
ORIGIN      
        1 msitinklei envkrikavk iepsatglti iggnnnqgkt svldaiawal ggnkykpsqa
       61 mregsqvppt lkitmsngli verkgknasl kvidpngqkg gqqlldsfve elainlpkfm
      121 dstpkekadv lleiigvgdq laelelkeke iynqrhaigv iadqkekfak emtyypdapk
      181 qlvsiseliq qhqailakng enaqkrqnve rirydynqsi levdrlrkll adaeaktnkl
      241 sedlkiantd amdlhdesta eieaniadid evnrkvranf dkdkaeedak qqreqynilt
      301 ndiesirqqk rdllinadlp leglsvddgk llylgqewdn msgsqqliva taivrklkpd
      361 cgfvlidkle qmdnitleqf gkrleqeglq aiatrvsige ecaiiiedgy svenkahnfk
      421 taeggnfaet vaptwkgef
//
LOCUS       WP_010925521             297 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Mycoplasmopsis pulmonis].
ACCESSION   WP_010925521
VERSION     WP_010925521.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis pulmonis (Mycoplasma pulmonis)
  ORGANISM  Mycoplasmopsis pulmonis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Mycoplasmopsis pulmonis"
                     /db_xref="taxon:2107"
     Protein         1..297
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34624
     Region          6..278
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mtksgsksek fllidgnylv hrsyyvsfkf knnfrstiyl ffqtiikiik nlnpenifia
       61 fdeeggtwrh dlckeyksqr skmedefwni fkaireilds inlnsggfrg headdviati
      121 tskfkdenqi yifsrdkdll qlidknvyit hdnelknlis ienfyqnfql epdqivdfka
      181 iagdssdnlk giagigekga knllnnfksl ekifdslest nliskaqkqk irdgkeqalf
      241 lkkivtlnke vpmklekelf aikinineei lekldkydsr yvlkqfekal esddylw
//
LOCUS       WP_010925164             280 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Mycoplasmopsis pulmonis].
ACCESSION   WP_010925164
VERSION     WP_010925164.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasmopsis pulmonis (Mycoplasma pulmonis)
  ORGANISM  Mycoplasmopsis pulmonis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mycoplasmopsis.
REFERENCE   1  (residues 1 to 280)
  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 280)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10097223
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Mycoplasmopsis pulmonis"
                     /db_xref="taxon:2107"
     Protein         1..280
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=32157
     Region          9..277
                     /region_name="TBP_aldolase_IIB"
                     /note="Tagatose-1,6-bisphosphate (TBP) aldolase and
                     related Type B Class II aldolases. TBP aldolase is a
                     tetrameric class II aldolase that catalyzes the reversible
                     condensation of dihydroxyacetone phosphate with
                     glyceraldehyde 3-phsophate to produce tagatose 1; cd00947"
                     /db_xref="CDD:238477"
     Site            order(28..30,33,53,56..58,62,66,69..70,143,232..233,
                     235..236,239,243,246)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238477"
     Site            order(83..84,178..180,182,207..208,210,229,231..232)
                     /site_type="active"
                     /db_xref="CDD:238477"
     Site            order(84,179,207)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238477"
     Site            order(178,180,182,208,210)
                     /site_type="other"
                     /note="Na+ binding site [ion binding]"
                     /db_xref="CDD:238477"
ORIGIN      
        1 maiitkvdhf ykklkrknka ilafnvvnle tlksfieiae ekqvdlviqi sqntiknlgy
       61 dlivpslkks lenskanfvl hldhcddfnl lekalkdgfk svmfdgsfld fknnvfsslk
      121 akemakkyea fleveigqil gknshenqde nqktkledil efynlvkpds lafnfgtlhg
      181 iykenpkidf dllknveski ctvlvmhgts glskkeiika wkfgitkini gtdfnlahis
      241 aikeffeeyp nvkdirkinl yaikkikekt lyfldmfakk
//
LOCUS       WP_010925917             204 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Bordetella
            bronchiseptica].
ACCESSION   WP_010925917
VERSION     WP_010925917.1
KEYWORDS    RefSeq.
SOURCE      Bordetella bronchiseptica
  ORGANISM  Bordetella bronchiseptica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 204)
  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 204)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 204)
  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   4  (residues 1 to 204)
  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   5  (residues 1 to 204)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Bordetella bronchiseptica"
                     /db_xref="taxon:518"
     Protein         1..204
                     /product="TRAP transporter small permease subunit"
                     /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=21780
     Region          4..169
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mtrllellcg glraitnrac laagwalial svvialnvla rkifsfslqg vdeyggycla
       61 icasigfsqa aydrahiris vltdllpqrl racsdvfala lltsvaltla vkatgvayds
      121 ysmqalatsa lrtplaipqa mwaaalcwfg lvlatqllhs llllarrdwg ginrnygnps
      181 vdeevaeelr sanermagkl egah
//
LOCUS       WP_010926515             268 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Bordetella
            bronchiseptica].
ACCESSION   WP_010926515
VERSION     WP_010926515.1
KEYWORDS    RefSeq.
SOURCE      Bordetella bronchiseptica
  ORGANISM  Bordetella bronchiseptica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Bordetella bronchiseptica"
                     /db_xref="taxon:518"
     Protein         1..268
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27917
     Region          1..258
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mklaanltll ypglplaarm aaaredgfag veilfpydqp paqlaaqlre hglalalvnt
       61 plgaagekgl acvpgreadf gaaldqalal cratgcrivh amagmppapa gmdecratli
      121 gnlqraapra aqagvtltle plnradmpgy fyylpeqaad iiravdhpnv glqfdiyhnl
      181 regldphael rrvlplvrhv qfagpdgrhe pdpasppvaa tlrllaqsgy ggwvgceytp
      241 rglasaglka wrgaydaacg sggaacas
//
LOCUS       WP_010927174             710 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Bordetella bronchiseptica].
ACCESSION   WP_010927174
VERSION     WP_010927174.1
KEYWORDS    RefSeq.
SOURCE      Bordetella bronchiseptica
  ORGANISM  Bordetella bronchiseptica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Bordetella bronchiseptica"
                     /db_xref="taxon:518"
     Protein         1..710
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73036
     Region          27..706
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mtqdldmaer svaapqwega araaavlear svaivgasad pgkiagrpla ymlsrgfvgk
       61 lfpvnptraq vqgvksypsl aaigepvdla ivgtpaalve gviregiaag vrafvvfssg
      121 fsetgeagaa lqrrlgelar ahgvtilgpn clgvansatg liasfttale etpirpggfa
      181 lvsqsgalga ywmdiclrsg lgfskwittg necdmdaaaa iaylagdadt rviglyiedi
      241 rdtaafrral rvaaeagkpv iaikagrsqa gaaaaashtg alagddalyd aclrqhgalr
      301 vdslgemmda arlylfdsvp qgrrvavmsv sggagvliad eaerrglalp plagstaaal
      361 apvlpsfvqa anpldltgnv vqdtasigra leavardpgn daivlfvglm hsiasaftda
      421 iaqarqrthr piiviwigak eesvaaleqa ripvfrdipp avaavgaavr lralreaala
      481 malpaaappa apgarveala ecdgktllre lgvagvpagm lvsaaapdrl paplaypvva
      541 klqaasllhk sdiggvvlni gsdaqlreav hrlagiaqah gieargvlve pmqpfdhell
      601 lglrrdprfg atltlgrggv eveldadvas qllplsagai qamleslraa rlfkgfrgrg
      661 avdlaalssq iadlcrifla qpdlaevein plavrgdraw vldavvsrya
//
LOCUS       WP_010927609             458 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Bordetella
            parapertussis].
ACCESSION   WP_010927609
VERSION     WP_010927609.1
KEYWORDS    RefSeq.
SOURCE      Bordetella parapertussis
  ORGANISM  Bordetella parapertussis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 458)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 458)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Bordetella parapertussis"
                     /db_xref="taxon:519"
     Protein         1..458
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=49936
     Region          26..440
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 masrtldrvt ifahiaeqte prhafvpagl ldreraadgq qvlsfayglr ylkrpaafdv
       61 dpralsleqa ranpsmrwfp spelgefggi rdaapdawgr rviearlnaa pnsldeftyl
      121 leagndrvga ldvrdrldsp prhpagdlln lpyllqaaaa veagepvpak lmpylggaps
      181 aggarpkasv rdadgvlwla kfpaandayd maiveagamd laraagltvp plrillagse
      241 rillvrrfdr ywappgqppp alargydshp qpgategrip qvsaltmmgc pemdstaksy
      301 rdlaqtirer vhpsciaadt eelfarmvln ifvnndddhl rnhafsydaq lrgwrlsply
      361 dvvprpsvar errlhlsiga qgklatldna msefaafvvd kpaalavirr vwgatrnwka
      421 vfeahgarpa liaileqair plgevaspal erelrrst
//
LOCUS       WP_010927636             174 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Bordetella parapertussis].
ACCESSION   WP_010927636
VERSION     WP_010927636.1
KEYWORDS    RefSeq.
SOURCE      Bordetella parapertussis
  ORGANISM  Bordetella parapertussis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Bordetella parapertussis"
                     /db_xref="taxon:519"
     Protein         1..174
                     /product="TRAP transporter small permease subunit"
                     /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=19577
     Region          1..166
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 merliqvldl fsdrmgrlas mvmlpvllvt favvvlryvf gigliwlqds yvwltsvffi
       61 cmagntflhd rhvrvelfys rmtarkralv nalgvllllw ptlfvtvqqs wrpiarswrf
      121 lealpnaggl sfayvhkslv yvfclvlflq glslllksar tlagargvap easp
//
LOCUS       WP_010928005             268 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Bordetella
            parapertussis].
ACCESSION   WP_010928005
VERSION     WP_010928005.1
KEYWORDS    RefSeq.
SOURCE      Bordetella parapertussis
  ORGANISM  Bordetella parapertussis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Bordetella parapertussis"
                     /db_xref="taxon:519"
     Protein         1..268
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27949
     Region          1..258
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mklaanltll ypglplaarm aaaredgfag veilfpydqp paqlaaqlre hglalalvnt
       61 plgaagekgl acvpgreadf gaaldqalal cratgcrivh amagmppapa gmdecratli
      121 gnlqraapra aqagvtltle plnradmpgy fyylpeqaad iiravdhpnv glqfdiyhnl
      181 regldphael rrvlplvrhv qfagpdgrhe pdpasppvaa tlrllaqsgy ggwmgceytp
      241 rglasaglka wrgaydaacg sggaacas
//
LOCUS       WP_010928293             209 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Bordetella parapertussis].
ACCESSION   WP_010928293
VERSION     WP_010928293.1
KEYWORDS    RefSeq.
SOURCE      Bordetella parapertussis
  ORGANISM  Bordetella parapertussis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 209)
  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 209)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 209)
  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   4  (residues 1 to 209)
  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   5  (residues 1 to 209)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Bordetella parapertussis"
                     /db_xref="taxon:519"
     Protein         1..209
                     /product="TRAP transporter small permease subunit"
                     /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=23141
     Region          3..171
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mkallalsrg idalnlrvgr avtwvtllvv lvsagnavvr kvfhsssnaw lelqwymfga
       61 mflltagytl lknehvrvdi lssrlprhkq iwieifgvvf fllsacilim vlswpvfmds
      121 ylsgeqssns gglirwpvkl lipvgfallv laglshlikc igflrgqcpd ptardgsksa
      181 eellaeeiar ealereasvq eqrnnhegr
//
LOCUS       WP_010929195             814 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Bordetella parapertussis].
ACCESSION   WP_010929195
VERSION     WP_010929195.1
KEYWORDS    RefSeq.
SOURCE      Bordetella parapertussis
  ORGANISM  Bordetella parapertussis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 814)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 814)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 814)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..814
                     /organism="Bordetella parapertussis"
                     /db_xref="taxon:519"
     Protein         1..814
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89439
     Region          76..125
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          129..814
                     /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 mvitfnlfsv khsmrarpsa atralhsssr prrlipallg alaclgtgvq aapidvdipp
       61 qnlaqalhql grqanlqvly sqdlvdgqrs pavqgrmepa ealerllkgr nirysiqhnt
      121 vtltpmplta tlpaisvvga lpdsdtyvat gttagtktdt plieipqsis vvtaaqireq
      181 npqtlgdavr ytpgivvqeg fnrtddpfii rgfdvrtnpg vmfrdglkip lphysamsep
      241 yalerievvk gpasvlygqa spggivnvvs krptdsplre lqlsggshsn rqlagdfggr
      301 iddegrltyr ltglarnadt midhvpddry ylapaltwri spdtsltlla symknktinn
      361 agyplegtvk ynpngriprh rftgepdwsk wdqevanvgy qfahrfndtw qfkqnlgyaq
      421 srnrvnhayw wtwvpgsdfs taergayrrd ddahgvsidn qfeatwqsgr frhntlsgld
      481 ytetsftrkq yagynnlapi dffdpaygsd vllpakpdty tnekrsqlgl ylqdqikfdd
      541 klvvvlsgry dnadgstlnk lsgvntrtgd naftwrtgll yladnglapy isystsfqpq
      601 agttspargt tpfdptkgkq weagvkyqpn gsnlfitasv feltrtnvpt tdpanpvysv
      661 qegevrsrgl elsatanlas gwnliaayty tdaeitksns ntlgntpeav prnmaslwsd
      721 ytvpsgalag lnigagvrym gstynntnaa kvgdytvfda avrydfgars pslkgwtadl
      781 tvrnlfdkdy vasctyacfy gegrtvlgrv tykw
//
LOCUS       WP_010929814             674 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Bordetella pertussis].
ACCESSION   WP_010929814
VERSION     WP_010929814.1
KEYWORDS    RefSeq.
SOURCE      Bordetella pertussis
  ORGANISM  Bordetella pertussis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 674)
  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 674)
  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 674)
  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 674)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..674
                     /organism="Bordetella pertussis"
                     /db_xref="taxon:520"
     Protein         1..674
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=72041
     Region          5..666
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mqidhdktqq ltekydseir frpldktatw ivsillvtls ifhyytagfg llreathrgv
       61 hlafvlslif lvfgfskahy qrepkstllc pggvplydwa iaivlalsvl yipyifedla
      121 frvgnplpmd vamgtilivg llegtrramg wplpiiamvf layaafgpyf pgllqhagnn
      181 wpqivnhmyl tsqgiygvav gvvatyvfhf vlfgvlatri glgqlfldva stiagryagg
      241 pakvsvfgsa mfgmlsgssv anavtvgslt ipamirigyp rhfaagveaa sstggqitpp
      301 imgaaaflmi eflgipyqqi aiagifpafl yffgmfmqvh feakreglrg lteeemptlk
      361 asfkkrwptl lplimligvl asgrtpylaa fagitgcivv gllnpmqrlr lrdlyeafet
      421 gakyalavga aagtvglvig vvtltgvgfk isyivisaaq aiaggvgtii pdvvantqtl
      481 tliaalvmtg ivcilmgcgi pttanyiimv avaaptlvql gvqpiaahff vfyfgiladi
      541 tppvalaaya aagmagsdpf ktgntafrlg itklivpfvf vfspsllisv qgftwydfft
      601 tlvgcmvglv llsaafsrym lvemkswerw vcvvgallti lpgltsglvg laicipvflr
      661 qlaqlkleng akaa
//
LOCUS       WP_010930938             275 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Bordetella pertussis].
ACCESSION   WP_010930938
VERSION     WP_010930938.1
KEYWORDS    RefSeq.
SOURCE      Bordetella pertussis
  ORGANISM  Bordetella pertussis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Bordetella pertussis"
                     /db_xref="taxon:520"
     Protein         1..275
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=29854
     Region          41..193
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mpwitraapi acllalagca argpagldld tsitavsqss rvravvlhyt stgnenslki
       61 lserkvsahy litdtprprv yrlvdetraa whasisawyd qstmnstsig ielvnpgwtn
      121 gegnwtrggh gdtdsrhwap ysdaqietli vllrdivarh giapenivgh sdiapqrkvd
      181 pgplfpwqrl aqaglgrwyd eagaaahlar lqtegvpdia wfqgqlarlg yatpqsgvld
      241 tatrnvlaaf qmhyrparhd gqpdaetaai mlalr
//
LOCUS       WP_010930386             209 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit [Bordetella].
ACCESSION   WP_010930386
VERSION     WP_010930386.1
KEYWORDS    RefSeq.
SOURCE      Bordetella
  ORGANISM  Bordetella
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 209)
  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 209)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 209)
  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   4  (residues 1 to 209)
  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   5  (residues 1 to 209)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Bordetella"
                     /db_xref="taxon:517"
     Protein         1..209
                     /product="TRAP transporter small permease subunit"
                     /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=23153
     Region          3..171
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mkallalsrg idalnlrvgr avtwvtllvv lvsagnavvr kvfhsssnaw lelqwymfga
       61 mflltagytl lknehvrvdi lssrlprhkq iwieifgvvf fllpactlim vlswpvfmds
      121 ylsgeqssns gglirwpvkl lipvgfallv laglshlikc igflrgqcpd ptaregsksa
      181 eellaeeiar ealereasvq eqrnnhegr
//
LOCUS       WP_010932167             667 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Chlorobaculum tepidum].
ACCESSION   WP_010932167
VERSION     WP_010932167.1
KEYWORDS    RefSeq.
SOURCE      Chlorobaculum tepidum
  ORGANISM  Chlorobaculum tepidum
            Bacteria; Pseudomonadati; Chlorobiota; Chlorobiia; Chlorobiales;
            Chlorobiaceae; Chlorobaculum.
REFERENCE   1  (residues 1 to 667)
  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   2  (residues 1 to 667)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Chlorobaculum tepidum"
                     /db_xref="taxon:1097"
     Protein         1..667
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=74328
     Region          60..119
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkptyttwlr rmtasamlla svaspvpala fdsfeelldr sdsmgnadel fsdleelrrn
       61 kipvnratee qllklpllsa adaakiiewr eqrgpigsva eleavigkdt arrfaaylsf
      121 elppevkkka lpervkgsvi grvfwedppr agvtngkyag gnrhvysrfq aatphygvhl
      181 lsdsdvgepd iddflsfnvh aegigmltqa vignyrlsfg qglvfgqgry ffkgsdavdg
      241 vllfapalrp yisagednfl qgvaatlapg pfeltaftss nkvdatiknd vvtsiattgy
      301 hrtatelnkk dnltqevkgv nlryryrage lstaigatwa kyryglplsw lddgknggql
      361 gsveasavyr ntqvfgeaay atepgalswi cgvqsdlakg itgvvsmrdy afeyyspfag
      421 afaergdnas nesglylglk akvrdnltla glydrfrfpv ldkryyvyps sgyearfyat
      481 wkqnrwmtwd amyqhkekee akkqfdsnig tsryipvpki tnrvqlglvv ecspgitlks
      541 raafkslrsh fvtgaeseeg wllyqqinlk rgpftlktrl arfdtdsydv alyayeddlp
      601 lvymlnayyg rgkawfivld fepvknfnlt akyettwydd rdvyssgndl rntsspgsyh
      661 vgcmlkf
//
LOCUS       WP_010934013             276 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Corynebacterium diphtheriae].
ACCESSION   WP_010934013
VERSION     WP_010934013.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium diphtheriae
  ORGANISM  Corynebacterium diphtheriae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
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   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   4  (residues 1 to 276)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Corynebacterium diphtheriae"
                     /db_xref="taxon:1717"
     Protein         1..276
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=29784
     Region          1..269
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 miefesvskr ygkrgekava dfslfipkgk ttvlvgssgs gkttllrmin rmveptegrv
       61 ivrgkdvaet dpvqlrrsig yviqsagllp hrtviqnial vptlnkepka eierrakqal
      121 advnlepsla nrypgelsgg qqqrvgvara lasdpdillm depfgavdpi vrrslqkqli
      181 dlqsrlhktv vmvthdidea fcvgdhivvl ekggkiaqqg spahifahpa ndfvasflgs
      241 dqenrslhte lidghtvvvd tfgrplgtlg dgatcg
//
LOCUS       WP_010935417             523 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Corynebacterium
            diphtheriae].
ACCESSION   WP_010935417
VERSION     WP_010935417.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium diphtheriae
  ORGANISM  Corynebacterium diphtheriae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Corynebacterium diphtheriae"
                     /db_xref="taxon:1717"
     Protein         1..523
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=55484
     Region          1..523
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mnirfltlir partfiviaa viqvasvafv vgrglsvgfl vagtienwpd pmphvgawaa
       61 vlvisvvgvs amawmqrwws atgagpvitd vrsrtltaln atdprvvqen ssrwkvvlga
      121 gpesveglrp ylstyipaal ssgistpivl avialidvrs allaaatlvl ipifmiligt
      181 ltrdqtqqrl hraqvldrhi idllrgartl qeigdtsaaq sqvhssgrrh aaatmsvlrl
      241 aflssfalef vatlsvalva vsigvrlvds smtlhaglia lilapevynp lravgtayhs
      301 sadgmtavet aldliestpq tanvaplkta tvvsdgevsv dklsvhgrdg irphnlsfqa
      361 rpgevtalig sngcgksttl laimgminye gtiaaphnig ylparpalct gtladnlsll
      421 gprdrdtaga llrtigcdip lsrtvtyqge glssgqierl afartcsqec avylfdepta
      481 hvdpetarkm wehirslard gatvivathd lanrdyadqv ivl
//
LOCUS       WP_010935551             370 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Corynebacterium diphtheriae].
ACCESSION   WP_010935551
VERSION     WP_010935551.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium diphtheriae
  ORGANISM  Corynebacterium diphtheriae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Corynebacterium diphtheriae"
                     /db_xref="taxon:1717"
     Protein         1..370
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=41298
     Region          15..190
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mksyeateil sdlasqqwgl ftsaqakdsg vdlpslrrle krgvftrvrh gvyastttvl
       61 stelelkaqw lslqpnlmaa erisdpslva davvshttaa evweigdlwp dgihftvnrr
      121 rrsrqtdvqf hradladsdw vvhpasglpi ttvprtildl aqsghepdhl lhlvadagrk
      181 yllteqelld sfsghedsfg ldqgdrsglk elvdecfidt ktaqqtrllv eeamrplqeq
      241 leaivkpltq slswknamqa plqqhlaqli spipsamqvp emtvfselae tmkktaslpn
      301 isknmwseiy ppetlssvls tslprtqvsp pekqrestet nesnseakkd arpnrqrfee
      361 gsentqqepq
//
LOCUS       WP_010935939             139 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Dehalococcoides mccartyi].
ACCESSION   WP_010935939
VERSION     WP_010935939.1
KEYWORDS    RefSeq.
SOURCE      Dehalococcoides mccartyi
  ORGANISM  Dehalococcoides mccartyi
            Bacteria; Bacillati; Chloroflexota; Dehalococcoidia;
            Dehalococcoidales; Dehalococcoidaceae; Dehalococcoides.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Dehalococcoides mccartyi"
                     /db_xref="taxon:61435"
     Protein         1..139
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14560
     Region          1..115
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkipgnifkr ehgftlieil vvvailgvla gvvipnvvkf mhegkvesan telanvrlav
       61 lsamvdaein tlndggtvgs ghtsnvsygs psvslavhnf vmgevigiyt lnekglivsa
      121 lmpegsdwan ltfvngawq
//
LOCUS       WP_010936491             122 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: zinc ribbon domain-containing protein
            [Dehalococcoides].
ACCESSION   WP_010936491
VERSION     WP_010936491.1
KEYWORDS    RefSeq.
SOURCE      Dehalococcoides
  ORGANISM  Dehalococcoides
            Bacteria; Bacillati; Chloroflexota; Dehalococcoidia;
            Dehalococcoidales; Dehalococcoidaceae.
REFERENCE   1  (residues 1 to 122)
  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 12181465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Dehalococcoides"
                     /db_xref="taxon:61434"
     Protein         1..122
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14019
     Region          20..118
                     /region_name="zinc_ribbon_15"
                     /note="zinc-ribbon family; pfam17032"
                     /db_xref="CDD:465334"
ORIGIN      
        1 mivlfgnkay ydilgymvtt cpgckttsvm tveqqrkklt vyfiptfdfs rkqymycghc
       61 herfeidksl qstvkarlls kkqmenliqq lemetpryec ancearveag mrfcpqcgns
      121 lg
//
LOCUS       WP_010938013             376 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Nitratidesulfovibrio vulgaris].
ACCESSION   WP_010938013
VERSION     WP_010938013.1
KEYWORDS    RefSeq.
SOURCE      Nitratidesulfovibrio vulgaris
  ORGANISM  Nitratidesulfovibrio vulgaris
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Nitratidesulfovibrio.
REFERENCE   1  (residues 1 to 376)
  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 376)
  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   3  (residues 1 to 376)
  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   4  (residues 1 to 376)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 376)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 376)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Nitratidesulfovibrio vulgaris"
                     /db_xref="taxon:881"
     Protein         1..376
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40072
     Region          29..366
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(102..104,125..126,174,226,250)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkgvvrllav cmvtsllmaa tafaagpvrv glmcpltgkw asegqdmrni vellaeevnk
       61 aggingnkve liveddggdp rtaalaaqkl stsgvtavig tygsavteas qniydeagia
      121 qiatgstnvr ltekglklfl rtcprddeqg rvaakviknk gykavallhd nssyakglad
      181 etkalldkdg tkivfydalt pgerdytail tklkaanpdi ifftgyypev gmllrqkmem
      241 kwnvpmmggd aannldlvki agkaaakgyf flsppvpqdf dtaeakafla aykakhnalp
      301 nsvwsvlagd afkviveavq kggkadgagi atylktqlkn ypglsgqisf nekgdrvgdl
      361 yrvydvnaeg efvlqr
//
LOCUS       WP_010938477              74 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Nitratidesulfovibrio vulgaris].
ACCESSION   WP_010938477
VERSION     WP_010938477.1
KEYWORDS    RefSeq.
SOURCE      Nitratidesulfovibrio vulgaris
  ORGANISM  Nitratidesulfovibrio vulgaris
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Nitratidesulfovibrio.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 74)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 74)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 74)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Nitratidesulfovibrio vulgaris"
                     /db_xref="taxon:881"
     Protein         1..74
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=7503
     Region          3..74
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mdieikcfat lsrftpeggr mqldggttva gvmqalgiaa ddvkivfing ihatpetvlq
       61 sgdrlglfpa vggg
//
LOCUS       WP_010938885             708 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Nitratidesulfovibrio vulgaris].
ACCESSION   WP_010938885
VERSION     WP_010938885.1
KEYWORDS    RefSeq.
SOURCE      Nitratidesulfovibrio vulgaris
  ORGANISM  Nitratidesulfovibrio vulgaris
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Nitratidesulfovibrio.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 708)
  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   3  (residues 1 to 708)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Nitratidesulfovibrio vulgaris"
                     /db_xref="taxon:881"
     Protein         1..708
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76963
     Region          9..704
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mivqdelnrq afveeaqdll aeletallei eerpedrslv driframhti kgsgamfgfd
       61 diasfthdve svfdkvrnge melspelldl tlksrdhiay llqcatkgla vdvsmsadlt
      121 qalrallpgd dhasaspade mpssgevegp rrtyrvrfkp hpqlflsgtn plglvreiqd
      181 lgrsklfvhf gdvpaldeld peqchvwwdv llttdsdeaa irdiflfved datvdvrlid
      241 eanlleqdga ykrlgeille rgdvatedlr rvleeqrpig ellaeagivt pdqvasalae
      301 qktvrelrrs rtedgdkpae kagdagasir vsaakldylv dlvgelvivq sqiarmaheh
      361 papgmlslve alerlsddlr dttlgvrmlp igttfsrfrr lvrdlagelg ksvelvtlgg
      421 eteldktvie rlgdplvhcl rnsldhgves perrlaagks atgritlaaa haggevlvti
      481 sddgagidae riyqaalrkg iiapevdlst rqklelifaa gfstaekvts vsgrgvgmdv
      541 vkraieslrg rielestpgk gtvitirlpl tlaiidglqv rvgdesyiip lphveecaeh
      601 ntpdhvdgrq riinlrgdiv pfirlrdvfr vpgvspgmeq lvvvnalgsr fglvvdcvig
      661 ehqtvikslg kvykdipgis gatiqgdgsm aliidvpglv htaaleaa
//
LOCUS       WP_010940030             172 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Nitratidesulfovibrio vulgaris].
ACCESSION   WP_010940030
VERSION     WP_010940030.1
KEYWORDS    RefSeq.
SOURCE      Nitratidesulfovibrio vulgaris
  ORGANISM  Nitratidesulfovibrio vulgaris
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Nitratidesulfovibrio.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Nitratidesulfovibrio vulgaris"
                     /db_xref="taxon:881"
     Protein         1..172
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18807
     Region          7..168
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mtqqdvilca irerrsvrhy tgepvaretv rtildagrwa psglnnqpwr flvvfpgdpr
       61 qevlagltky arivreagal imvclerqrm ynamkdhqga gaciqnmllg ahavglgavw
      121 lgeivnrgde vltatglspe rlelmavval ghperagggd riplddmlle pf
//
LOCUS       WP_010942442             189 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Geobacter sulfurreducens].
ACCESSION   WP_010942442
VERSION     WP_010942442.1
KEYWORDS    RefSeq.
SOURCE      Geobacter sulfurreducens
  ORGANISM  Geobacter sulfurreducens
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Geobacterales; Geobacteraceae; Geobacter.
REFERENCE   1  (residues 1 to 189)
  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   2  (residues 1 to 189)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Geobacter sulfurreducens"
                     /db_xref="taxon:35554"
     Protein         1..189
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=20530
     Region          130..189
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkprtghavy ltlalavmtl pllfkghgts pleipavafv rsrsddrpvs imitgvpeks
       61 gvyrvargst cqsvinmalp nssvnylppa tvgrilcdgd vvivrnknra tsdvslgkla
      121 vsqlmlmrip ldpnrmdikd wellpgigpe larrivcdrq dngdfssfea lervpgigpk
      181 tlmslkeff
//
LOCUS       WP_010942985             631 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Geobacter sulfurreducens].
ACCESSION   WP_010942985
VERSION     WP_010942985.1
KEYWORDS    RefSeq.
SOURCE      Geobacter sulfurreducens
  ORGANISM  Geobacter sulfurreducens
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Geobacterales; Geobacteraceae; Geobacter.
REFERENCE   1  (residues 1 to 631)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 631)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 631)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 631)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 631)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 631)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Geobacter sulfurreducens"
                     /db_xref="taxon:35554"
     Protein         1..631
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68600
     Region          1..631
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mekngtvhtg tvrqslglsl aalgvvygdi gtsplyamre cfhgthphpa tpdnvlgvls
       61 livwaliliv slkylvfvlr adnrgeggil altallnpwg denrpprkvl vflglfgaal
      121 lygdgtltpa isvlsaiegl kiatplfhpy ivpitvvili llfliqhrgt arvgalfgpv
      181 mvlwftvlal lgirgimmap evlgalnplh avlffvrdgw sgfqvlgavf lvvtggealy
      241 admghfgrlp irlawfccvl palllnyfgq galllsdpse atepfyhlap pwalyplvll
      301 atlatiiasq avisgvfslt rqaiqlrlsp rmrivqtsse eigqiyipav nwalmlatit
      361 lvagfgsssg laaaygvava ttmvitallv rfvmlerwhw hplavagltv vfltvdlaff
      421 ganilkvgag gwiplaagla vftvmitwrr grelvtthll aqatplpsfl eelaakppqr
      481 vpgtavfmsg rlfpapptli hhlehnkvlh eqvviltvlt ediprvsase rielkrlgqg
      541 fyrlivrygf mqspnvpvil receplglvt dpetttfylg retliptekv sgmphwrekl
      601 fafmsrnslq atafynlppd rvvelgqqve i
//
LOCUS       WP_010943817             561 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Geobacter sulfurreducens].
ACCESSION   WP_010943817
VERSION     WP_010943817.1
KEYWORDS    RefSeq.
SOURCE      Geobacter sulfurreducens
  ORGANISM  Geobacter sulfurreducens
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Geobacterales; Geobacteraceae; Geobacter.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 561)
  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   3  (residues 1 to 561)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Geobacter sulfurreducens"
                     /db_xref="taxon:35554"
     Protein         1..561
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=59684
     Region          1..546
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdmsqyrdlf vaearehler lgeevlalek dpangerlds lfrtahsikg magsmgydgi
       61 adlshrmedl mdrvrkgrip fgrdiadlll acadqlgrmv edvtgggngs ldatdlcarl
      121 alvagqeaaa paapadaets pspqpsdqpe parrdesdga rtvrirsell drfvnitgel
      181 vtgknrimel aagleseplr daaaelsklv rdlqrevmsa rmmpfgticd rfprmvrdla
      241 rrsgkeatla idgkdqeldr gileilpdpl lhalrnavdh giespeersa agkgaggriv
      301 lsvrrekdhl dvtvtddgrg mdpaalvnaa lakgiitpee aatlsrqeal mlvcrpgfst
      361 arsvtevsgr gvgmdavqaa vsraggslsi qsergrgsri tlrlplsvai iqvllvgcgp
      421 ltmavpvnav rrtveldrrl qriedgravf dlggetlplv dlgllvgtgp taggdfspvl
      481 tadvagrtmg favdrffgqa evftkplgtp lnrarglagg ailgdgrvif ildlpnlvdg
      541 atsrrrvfmh pdgahkggtt a
//
LOCUS       WP_010945270             275 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [[Haemophilus] ducreyi].
ACCESSION   WP_010945270
VERSION     WP_010945270.1
KEYWORDS    RefSeq.
SOURCE      [Haemophilus] ducreyi
  ORGANISM  [Haemophilus] ducreyi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="[Haemophilus] ducreyi"
                     /db_xref="taxon:730"
     Protein         1..275
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30589
     Region          1..272
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 miydlhshst asdgmltpte lilraveqkv dvlaltdhdt lagiqeakia aesqpiqlis
       61 gveisalwqn knihltaldi dehhpaliel lqhhavlreq raveigekla kagipnayhg
      121 akmlangevt rahyarflvq qdyvrnieha fkkylgtgki ayvkpqwssi shvidvthqa
      181 ggviclahpl rykmtarwlr aliehfkqag gdgievascg qrpdqrqlia rwasefdlya
      241 svgsdfhypt gwielgkslt lpttckpiwq lfttq
//
LOCUS       WP_010947130             113 aa            linear   BCT 20-JAN-2025
DEFINITION  PilZ domain-containing protein [Legionella pneumophila].
ACCESSION   WP_010947130
VERSION     WP_010947130.1
KEYWORDS    RefSeq.
SOURCE      Legionella pneumophila
  ORGANISM  Legionella pneumophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 113)
  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   3  (residues 1 to 113)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 113)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Legionella pneumophila"
                     /db_xref="taxon:446"
     Protein         1..113
                     /product="PilZ domain-containing protein"
                     /function="Transport and binding"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12390
     Region          4..113
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mtekpqiinc sfpneaslym aympfvkggg lfirtqhvys lgqslelsvk llnenepylv
       61 tgkivwitpk gaqgnkppgv giqftgensr ylcnkietyl agmlkscqvt dti
//
LOCUS       WP_010947272             224 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Legionella pneumophila].
ACCESSION   WP_010947272
VERSION     WP_010947272.1
KEYWORDS    RefSeq.
SOURCE      Legionella pneumophila
  ORGANISM  Legionella pneumophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 224)
  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 224)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 224)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Legionella pneumophila"
                     /db_xref="taxon:446"
     Protein         1..224
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=25694
     Region          1..207
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Region          92..121
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(94..95,98..99,101,128,131..132,135..136,138..139,
                     161,164..165,168..169,172)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          126..155
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          160..188
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msvymteeeq leiikkwwkr ygnmitifls imlliiagyr ymnwhndkik qqasiayenm
       61 miafsnqnik svrsyaneli knynhtvyad iahmtlakiy vnknkleqar nelkavases
      121 qmtplrqiak iriarllaad kaytnalnel savedeaylp vinelkgdiy sakgqyqdam
      181 nayrlaidev rtngmgnlfl emktnelaik tqsmitddkk vkaa
//
LOCUS       WP_010947941             336 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Legionella pneumophila].
ACCESSION   WP_010947941
VERSION     WP_010947941.1
KEYWORDS    RefSeq.
SOURCE      Legionella pneumophila
  ORGANISM  Legionella pneumophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 336)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Legionella pneumophila"
                     /db_xref="taxon:446"
     Protein         1..336
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /function="Lipid Metabolism"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35910
     Region          8..320
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mnffrcekpi yikgpfvalp erimsnqdvl nwmnstqnpt vigfstgikn rhwvnedqac
       61 sdlavraaeh lfmektrekh kvnqvilati sgdypsppss plvqyrlglq nagafdigaa
      121 cagfvvglht saalaqtndg svlliaseir skflnknnfa tsvlfgdgaa accvsqdkee
      181 adfrfiasal fadgevydav stpaggsrlp aavcndheqf yitikestal fvkavhgmad
      241 sakdflkeln ltisdiqwlv phqgnknlvl svakqlgfpe ektiktveet gntsgssvgi
      301 aldrlrsdgk iksgekvllv aaggggiaac sllevv
//
LOCUS       WP_010948569             189 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Legionella].
ACCESSION   WP_010948569
VERSION     WP_010948569.1
KEYWORDS    RefSeq.
SOURCE      Legionella
  ORGANISM  Legionella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Legionella"
                     /db_xref="taxon:445"
     Protein         1..189
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /function="Metabolism of Cofactors and Vitamins"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20418
     Region          22..188
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mannprliig isgssgiiyg irllqvlqkl piethlvisk agqltrayet nisaaelkal
       61 advyhpctdl tasiasgsfk tlgmiiapcs mktlgeiahg issnlltraa dvvlkerrkl
      121 vllpretplh lvhlnnmvci tqmggiicpp vpafynhpqn iddlindtvg rvldlfdldc
      181 glvkrwget
//
LOCUS       WP_010948661             449 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Legionella pneumophila].
ACCESSION   WP_010948661
VERSION     WP_010948661.1
KEYWORDS    RefSeq.
SOURCE      Legionella pneumophila
  ORGANISM  Legionella pneumophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 449)
  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 449)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Legionella pneumophila"
                     /db_xref="taxon:446"
     Protein         1..449
                     /product="M4 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /function="Toxin production / other pathogen functions,
                     Protein fate / hydrolases / secretion"
                     /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=49878
     Region          9..445
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mnitgieqdi nstegklspn dieqktlgkv tepvkfknlk kviyidkgnk ahlayhlsyy
       61 snsekkhvna pnylidansg eilkqwnevr herigqglgg naftlpyrqg mfqhgnalpg
      121 lpslgkfdvn vedglcrven esikvmnlen hnigydffpi tifaesvlnl safsypcnet
      181 nlflnyadgr tgpvnyafsp vndtmyfaqq tldmyqkvyg vnrpigddlp iraythlgdm
      241 dnafavptis ldgvvlahqq ivigngdefl tapaqsvlgh elshnftalh sglmyegqsg
      301 ginesfsdma aialldylsk dypwywdged wtigreavks gqpirylddp akdgmsigha
      361 seytdaldvh itsgvfnkaf yllahkpgws iqkafqvmvd anmnywspia yydfaacgvi
      421 qatidkhwdk tpvieafaev gvvcpmhks
//
LOCUS       WP_010948981              93 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Mycobacterium avium].
ACCESSION   WP_010948981
VERSION     WP_010948981.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium avium
  ORGANISM  Mycobacterium avium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 93)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 93)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 93)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Mycobacterium avium"
                     /db_xref="taxon:1764"
     Protein         1..93
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=9576
     Region          12..93
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mgrvpvqang isvtvryfaa araaagaese tvvvvrpgtt vgelverlav rgsrlaevls
       61 rcsylcdgia vrdetqslrs gdtidvlppf sgg
//
LOCUS       WP_010950166             158 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Mycobacterium avium].
ACCESSION   WP_010950166
VERSION     WP_010950166.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium avium
  ORGANISM  Mycobacterium avium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 158)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Mycobacterium avium"
                     /db_xref="taxon:1764"
     Protein         1..158
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=16022
     Region          73..156
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mkervpdstg lplravvmvl lflgviflll gwqalgssgn seddsaspvs sstatssasa
       61 sptnkpaanq aevqvyniss kegvaartkd qltsagfkvt kvdnlavpdv sattvyytda
      121 ddehatadav gknlgapvep ripalsgqpp gvivlvag
//
LOCUS       WP_010951525             262 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Pseudomonas].
ACCESSION   WP_010951525
VERSION     WP_010951525.1
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 11459553
            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="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=29256
     Region          22..178
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mlstlkktli sflllsvagc stglridrsh psanqdnriq fvvlhytnas lerslallth
       61 gevsshylig dgpatvyqlv denrrawhag esqwqgrtwl nsssigieiv npgftdtpng
      121 rvwhpyseaq vqaliallkd ivkrnniepr hiighsdiap lrkldpgplf pwkrladagl
      181 giwpdanava rqqayfsvnp psvgwyqqel arfgyqieqt gvldvatrhv vaafqmrfrp
      241 qrfdgmpdaq taamlqvlnr mr
//
LOCUS       WP_010951702             810 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [Pseudomonas].
ACCESSION   WP_010951702
VERSION     WP_010951702.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 810)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 810)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..810
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88229
     Region          60..110
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          87..810
                     /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 msravdhilr pslmalaigl aapltspalf aaeqstsray nlpsaplatt lnqiasqagi
       61 alaidpalvs grtsapvsgq ydglgalqaa lsgtglqlqq ssagsyslva vpdgtlalpe
      121 ttvnatsase sawgpvegyv akrtaagtkt dtalvevprs vsvatreqmk drgvhsldda
      181 vrympgivsa sfgsdtrydw mrvrgfeptq fldglplprg vyanpkaetw nldrlallrg
      241 passiygqtp pgglldmvsr rpqaesahei elqygsdnhr qinfastgki ddegrflygv
      301 sgvirdsgtq idhidnkryn iapsltwnid edttltfltq ftrddtgats qfrpiqgtki
      361 dmpfgkishh knlgdpdyef ydrtyyalgy afehrindvw qfrqnlrytk sdlsfqtitp
      421 gsynkssppv qddgtvsrms tntdedisqf avdnnfqadf atgdidhtll igldhqrint
      481 nylsifdfnv pdsnvnnpvy glpitrpdrs tafydynqkt rqtglyvqdq malgnwrltl
      541 ggredwvhtg tkffnqgdat ntqrdkkfsg naaisyvfds gfvpylsyae sfqpssnasv
      601 sasdsfkpte gkqwelgvky qppgsntlls aavydltqkn vsvtntvggv titsqtgevk
      661 vrgleleavs dvtdnlkvia aytlaksevq dgdfkgnrlq lmpnqqasiw gdytwhsgvl
      721 dgfgiglgar ytgntygdqg ntylgkakay tvfdgsvhyd lgrlngsleg asvavtatnl
      781 lnkdylstcd syycyygder svvasatykf
//
LOCUS       WP_010952470             117 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Pseudomonas].
ACCESSION   WP_010952470
VERSION     WP_010952470.1
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 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..117
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12481
     Region          10..113
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(16,34..35,43,46,48..49,51,54..55,57,65,70,80)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(34,65..66,68,94)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 msdgyehald saegrrtaly svlgqvppgk vvsygqlael aglgraarwv grtlgqlpad
       61 trlpwhrvlg aggrlslalg tpsgdeqrar lraegvnvsn nrvdmtrhgw rpmehsg
//
LOCUS       WP_010952503             306 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010952503
VERSION     WP_010952503.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 306)
  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 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   3  (residues 1 to 306)
  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   4  (residues 1 to 306)
  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 306)
  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 12071874
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34239
     Region          35..187
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          215..294
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mttatstept lelqrlelae linrhagepf gpasaiddly lvrytenvrs vptlaqpalc
       61 ilaqgskslf lgdeqyaydp lhymvvsvtl plsavrldas penpslglrm dldpaeisql
      121 iaesgpmlvp nrpsgrglyv ertdaallda llrllrlldt prdiamlapl frreilyrll
      181 rgpqgyrlye ialansqthr vcqaitwlnn nfqqplried larevnlsts tlhhrfkavt
      241 smsplqyqkq lrlqearrlm lndgleaava ayrvgyesps qfsreysrly gappirdvar
      301 lratav
//
LOCUS       WP_010954585             362 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_010954585
VERSION     WP_010954585.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 362)
  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 362)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 362)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 362)
  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   5  (residues 1 to 362)
  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   6  (residues 1 to 362)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..362
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40119
     Region          26..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <176..333
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mresdsvavy flnamlhalr dtpaerdaql lavgiapqll dqplarvpak afaqlwlali
       61 qrlddeffgl dshgmplgsf alicrglile pnlekalrqc mggfglflrd lrgsltvrgg
      121 ravisvqsni adpltrvyae etylvlmigm lcwlagrria idrtelavsr paqeddlllw
      181 gpdlrlgsgr tevefdsayl rlpvvqdraa lktflrsapq glvirfrnqn glvaevyrhl
      241 ralrygqwpt laalaqqqgi sastfrrqle regrsyqqik devrramafe rlregalsia
      301 eiaeqagfqe psafhrafkk wtgqspgsyr arlvglrstc rsghareett avdgtgsagv
      361 rg
//
LOCUS       WP_010954771             675 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter permease [Pseudomonas].
ACCESSION   WP_010954771
VERSION     WP_010954771.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 675)
  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 675)
  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 675)
  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 675)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..675
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..675
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=71935
     Region          12..671
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 msdtaqglha stdrwpaalf avalvfsvfq iataafplis tqvlraihvg flllvvylsy
       61 sfvghrrpwq plawllglag mataayqwyf egdliqrsge lttsdlivgl lliglvfeaa
      121 rrvmgialpi icalflaygl lgqhlpgela hrgygldqiv nqlafgtegl ygtptyvsat
      181 yiylfilfga fleqagmirl ftdfamglfg hrsggpakvs vfssalmgti tgsgvanvvt
      241 tgqftiplmk rfgykpafag gveatssmgs qlmppvmgav afimaetinv pyaevakaal
      301 ipallyfgsv ywmvhlearr shlhglpreq cpsawdalrq rwfllvplmv lvallfsgrt
      361 plysgmvgla ltaivilgsa iilraqktwl raafwvalgi lcsgffrmgi gvilmviagl
      421 aiaccfvqgg ratlhacvma laegarhavp vgiacalvgv iigvisltgl attfagyild
      481 lgrdnlflsl vltmltclvl gmgiptipny iitssiaapa llelgvpliv shmfvfyfgi
      541 ladltppval acfaaapiak ekgllisfwa vrialagfvv pfmavydpal mmqgdsmgst
      601 lymvikaafa valwgcasig hlrapmpwwe rllafaagvs lilaapisde vgfalgaavl
      661 gwhywrtrpa sghla
//
LOCUS       WP_010955107             247 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Pseudomonas].
ACCESSION   WP_010955107
VERSION     WP_010955107.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 247)
  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   3  (residues 1 to 247)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            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="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28318
     Region          34..241
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mfnesdapqp pkvlstplei aanlrqlqes hdpliitfhd rshrfqsyvv hvdresntla
       61 ldemiprdge kfiengehfr vegfhdgvri awecdhalki sevdghrcys gplpqevtyh
      121 qrrnafraal klsqlvdiil dgahlkgnga mrgklldisa tgcklrfegn vedrlqlgqv
      181 yerfkagnpl glvdtmvelr hlhyeerint tfagvrfhnl sgqaqrkies fvyqlqrear
      241 rfdkddy
//
LOCUS       WP_010954910             690 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor family protein [Pseudomonas].
ACCESSION   WP_010954910
VERSION     WP_010954910.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..690
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=76316
     Region          26..689
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mrsdlplssc lgllaalaat qpalgasave lgrvlitdee qneltaager lreipgasnl
       61 vdmqrvgqgr vasnqdvlay qpgvfaqsag ndgiklsirg sglnrapgah gsgvytmfdg
      121 lpltgpggtp yelfeplwls raevlrgang fdqgslalgg ainyvthtgy dapalqvrye
      181 vgsrgyqhrh issgqvlgnl dyyvaltdse ydgyqahssg sakgiaanag yrfnpnletr
      241 fylryreten elpgrltkdq ikhhpraanp nylarddsrp qpgstwvgnk ttfyledear
      301 leaglvyhdy pmdlregpmr lkvaytdvsg tlnyfrrdtl fgreskttvg wrttkhlpns
      361 gasqftrngd vfgertrdft yqgsdtvlhv gndlelvpnl wlstglamiy trresdvtyp
      421 seggkvsmhd wdyaprlglr ydirpdlqvy gnlsrsvepp hpwsliwsap stggkqiqpi
      481 emqnqtattl elgargdsal grwdlawyys qvrhellave vvpnftsefn asatvhqgve
      541 agldstlwer agtgklslrq aytfsdfhyr dddtfgdnrl pgipmhyyqa elrydwpngf
      601 yagvntqmas kvqvdyansy hadeyallga rvgwdspkqd wqtwldlrnl tnqryaatvt
      661 payndagqdn arstpgegfg vyagvsysfr
//
LOCUS       WP_010955383             797 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [Pseudomonas].
ACCESSION   WP_010955383
VERSION     WP_010955383.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 797)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 797)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..797
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86630
     Region          68..119
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          95..797
                     /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 msftpvpqrh plsralhaal lglavstyal pslaqplnad hnnplkqwsi pagplapald
       61 rfareagisl sfdaqnvanr ntngvqgald trsalssllr gtelqiepqg pnaylvipqp
      121 kpagplelgv tedyrlapvi inakvkasad ddansvvake lwvggkvats ilntpasvsv
      181 vtnkemqqrs vstteealqy tpgvvsdyyg sddrndyfli rgfqattyrd gltlssmrgv
      241 redpyayeri eilrganstl fgpadpggsv nfvtkqprfe kfgqgyvtyg sydhaetgid
      301 vgdalndeqt lagrftakmq nsdreydhsq ddnrfvmggl twaptdftsa tvvldylktn
      361 sspnsggypl dkgydrsdfy gepgynfhdv ertslsgnit hdfdngftlr snlryseltd
      421 dfgyvylsdn asrvgttipr yvfgtdsdad qlngnlmlqy daqfehidss tlvgveylds
      481 ttkqssvysl apsidianpv ftgvpggitp ytrkkndatt kavflqqnls ffdrviatag
      541 vrndsmdlss keyiggeqte kdnfsetsyr aaltyivnde vstyvsmves vsppqvgvtp
      601 qtgkqyevgi kyspmgmdal fsaavydltq envtiavvlp sgiieqqtvg esrvrgldle
      661 akaqvtqdis vigaysymes evlrgslydg sslkgneftt apkhtaslws yydipgtdvs
      721 vglgaryvga yymdaantkk sdgttlfdaa lnykiakgtd lalnvsnlfd eqhvvgsgta
      781 nyynpgrevt akvsysw
//
LOCUS       WP_010955694             788 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: penicillin acylase family protein [Pseudomonas].
ACCESSION   WP_010955694
VERSION     WP_010955694.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 788)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 788)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 788)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..788
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..788
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=86403
     Region          17..788
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkrsltllav vvtvaagasg ywyvqgklpq regevavagl qapvsvryda rgvphlqaqs
       61 epdlyralgy vhaqdrlfqm eilrrlarge laevlgdkll ptdtlfrslr ireqaalmak
      121 rqdpqapawq alqayldgvn swqashpkpt efdllgitpr pftaedtlsi agylaysfaa
      181 afrtepalty irdqlgpdyl kifdlgwqpe galgtplaaa dwqslealar lsdealgdag
      241 ipqfegsnaw avagsrtrsg kpllagdphi sfavpavwye aelsapgfnl ygffqalnpf
      301 allghnrdfg wsltmfqndd vdliaektnp anadqvmvdg qwrtlekteq qiaikgeqpv
      361 tinlrrsphg pivnevlgat agatpiamww afletenpil egfyqlnrad tlgkmreaaa
      421 kvqapglnfv wanargdigw waaaklpirp dgvnpafild gassqadkpg fypfsvnpqq
      481 enpasgyivs anyqppavvp ipgyynladr grqldrqlan pevkwdmqns qalqldtasd
      541 ygprtlapll atlrqiaqgd eeeelveqla awrgdyplds tsatlfnqfl yelayaalhd
      601 elgdiwfpvl istraidaal prlaadaesp wwntrganqr tdrssivrea wqkslghlrd
      661 tlgkdpaswq wgkahtlthn hplgvkkpln llfnvgpfaa pgthevpnnl sakissapwp
      721 vtygpstrrl idfadagqal tinpvgqsgv pfdrhyadqa egyvqgqyqr aqmgvipaqs
      781 tlrlvppk
//
LOCUS       WP_010957041             280 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Treponema denticola].
ACCESSION   WP_010957041
VERSION     WP_010957041.1
KEYWORDS    RefSeq.
SOURCE      Treponema denticola
  ORGANISM  Treponema denticola
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales; Treponemataceae; Treponema.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 280)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 280)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Treponema denticola"
                     /db_xref="taxon:158"
     Protein         1..280
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31883
     Region          26..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          127..277
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mnsiqsfnkt idyiestldt epdekeimnl srysyplfsr ifsilvgypl neyirlrkls
       61 raaadlrngn ekvidialry gyespdsfaa afkkfygvsp sevrngksfk vfspvklslt
      121 vtggqtmeir iekkrafsia glciqsnqtt dfpkvwndlf nkasheelit mgngqsygsc
      181 yevkdcnsfn ymagydctde qkaetfglsv mhipeaeyav vqlkgpvpdc ihqgwkyvmd
      241 tffpeqgyrh agtpdvevyk egdmydknyn melwvpitke
//
LOCUS       WP_010957347             249 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Coxiella burnetii].
ACCESSION   WP_010957347
VERSION     WP_010957347.1
KEYWORDS    RefSeq.
SOURCE      Coxiella burnetii
  ORGANISM  Coxiella burnetii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Coxiella.
REFERENCE   1  (residues 1 to 249)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Coxiella burnetii"
                     /db_xref="taxon:777"
     Protein         1..249
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=27994
     Region          126..248
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(206..207,210,220..223,225)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mvrglkfrki kglisismlv llaltnsaay gqtsphhpdv nyeesryyga hlcayseftc
       61 iavkpgdtwt klfpnkrere ivkrlnrtnm alsnrhwivv ptelteveyl dlspfppnih
      121 pthqkllvvn lglhafaayd ekgqlvhwgp vsggqewcsd vgrkcntvvg nfrivrlggp
      181 ecvsnkfpve teggapmpyc mfyfrgyalh gstlpgyhas hgcirlfhdd akwlnkhfln
      241 vgtqiivtr
//
LOCUS       WP_010957958              99 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Coxiella burnetii].
ACCESSION   WP_010957958
VERSION     WP_010957958.1
KEYWORDS    RefSeq.
SOURCE      Coxiella burnetii
  ORGANISM  Coxiella burnetii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Coxiella.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Coxiella burnetii"
                     /db_xref="taxon:777"
     Protein         1..99
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10938
     Region          2..96
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 midlnlksla fikkilkkhl sgvevkafgs hvtgraktfs dldlviigdk pipiktinal
       61 kfefsnsdlp ilvdivdwnt iseefrekia edcvtliak
//
LOCUS       WP_010957994             160 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Coxiella burnetii].
ACCESSION   WP_010957994
VERSION     WP_010957994.1
KEYWORDS    RefSeq.
SOURCE      Coxiella burnetii
  ORGANISM  Coxiella burnetii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Coxiella.
REFERENCE   1  (residues 1 to 160)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Coxiella burnetii"
                     /db_xref="taxon:777"
     Protein         1..160
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=18100
     Region          7..158
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cl49639"
                     /db_xref="CDD:483979"
     Site            order(115..116,119,132..135,137)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mttyltvdip sqtltlfrdn qvikryrvst arngpgelin sektprgwhi irakvgegcp
       61 pntvfverrp tgevyspalk rrypdrdwvl trilwlsgle vgknrlgnvd tmrryvyihg
      121 sgdeiimgkp gsrgcirmhn hdiielfdev cagdrvyigg
//
LOCUS       WP_010959934             432 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Methylococcus capsulatus].
ACCESSION   WP_010959934
VERSION     WP_010959934.1
KEYWORDS    RefSeq.
SOURCE      Methylococcus capsulatus
  ORGANISM  Methylococcus capsulatus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Methylococcales; Methylococcaceae; Methylococcus.
REFERENCE   1  (residues 1 to 432)
  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 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   3  (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   4  (residues 1 to 432)
  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 432)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Methylococcus capsulatus"
                     /db_xref="taxon:414"
     Protein         1..432
                     /product="CmpA/NrtA family 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=47085
     Region          12..271
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mdnaqetavg ngiekprltl gfipltdcap lvialekgyf rrhgldvtls rqpswaaird
       61 kvatglldga hmlapmpiat tlglggvrka tiapmsldln gnavtvsnal yrrltavagv
      121 epaqrpvsar clrrlldrdg evlrfatvfp fsshnyllrh wlacagvdpd rhvgmtvipp
      181 pqmprclaag eisgycagep wnaravaqgi grvlitghei wnnspekvlg vnqdwaehhp
      241 ntlrallmal leaaqwldrp enrpeaaall anpdyvgvpa eilqmsmtgs fqyaagepav
      301 slpdfnvfhr yaatfpwrsh alwfltqmlr wgqiaepldl havaarvyrp dlyreaatal
      361 glpcpsgdyk regihaapwt ldtgtsslvm gpdlfcdgia fdpadpiayl agfglhrlrv
      421 rlddlrregn pp
//
LOCUS       WP_010960855             394 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Methylococcus capsulatus].
ACCESSION   WP_010960855
VERSION     WP_010960855.1
KEYWORDS    RefSeq.
SOURCE      Methylococcus capsulatus
  ORGANISM  Methylococcus capsulatus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Methylococcales; Methylococcaceae; Methylococcus.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Methylococcus capsulatus"
                     /db_xref="taxon:414"
     Protein         1..394
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=41735
     Region          5..385
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mgnpvavvna gsstvkfsll ngerrvfdal ldrlgstsan gacaslrdaq gaplfqgpip
       61 adnhedaliw lfdwlaragd gckpaavghr vvhggdgltr pvkvtgeiie kiealiplap
      121 lhqphnlapi rllaakfpdi pqvacfdtaf hasqsaverr falpreyeaa girrygfhgl
      181 syeyvaarla eidpcaadgr tivchlgnga slcamkngrs vattmsftal dgipmgtrcg
      241 aidpgvllhl mtrpgmdaat lsdllykrsg llglsglsgd mrdllasdrp eaaeaveyfc
      301 yriareigsl taalggldal vftagigeha apvraricel stwlgvaidp aaypilhtpd
      361 srihvlvvst deetmiarhv rrtlglpqgs prsl
//
LOCUS       WP_010962213             786 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Methylococcus capsulatus].
ACCESSION   WP_010962213
VERSION     WP_010962213.1
KEYWORDS    RefSeq.
SOURCE      Methylococcus capsulatus
  ORGANISM  Methylococcus capsulatus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Methylococcales; Methylococcaceae; Methylococcus.
REFERENCE   1  (residues 1 to 786)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 786)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 786)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..786
                     /organism="Methylococcus capsulatus"
                     /db_xref="taxon:414"
     Protein         1..786
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=86117
     Region          7..785
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkfkhilyia gfgilalaty agtrlekaaa slpatggesv lpgltrpatv efdrlgiprv
       61 maanredalr algylhardr lfqmdlmrrk aagrlaeifg erarahdraq riyafgraaa
      121 aivaalpesq rlaleayvag vnarmaeqtv pppeilvlgy tpepwraeds llvglgmfqt
      181 lnghpdeerm lsvmaetlpp evlafltpdv dayttvlagg ngsrrperpv paaalaella
      241 etrhltlgaa vdaetlpags nnwavagtrt rdgraivand mhlnlgvpni wyraelryge
      301 avmsgvtlpg lpllvagsnd riawgftnvd advldlvkle mhafepdryr tpegwatldt
      361 rtetlrvkdg vdetlvlkss rwgpvmtepl lgmpvalrwt aleaqgvdlg llemdgardl
      421 dsamavmnra gnppqnvvla draghiawtl tgrfplrrgf dgsvsrswsd gaawdgfvpp
      481 erlprvvdpp ggylatannr tlgrdypyvi ghnysnsyra yrigerlkqa qaltetelfg
      541 lqldtrseff dfyrdlvlal tanandpvlt earraveawd grmeadsrgi allvryrrnl
      601 artvfsrlls rcnqtdpgfv yawreaetpl ralissrlpd tvpdrsgswd aflrgileqs
      661 idelkrefgt aalqdltwgr vnrvevrhpf sknlplisal ldmpqvegvg cggqcirvlt
      721 phqgaserlv vspghhgdgi lhmpagqsgh plsphyrdqh dawatgqplp fepgpavetl
      781 rlkpal
//
LOCUS       WP_010962395             139 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Wolbachia].
ACCESSION   WP_010962395
VERSION     WP_010962395.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia
  ORGANISM  Wolbachia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Wolbachia"
                     /db_xref="taxon:953"
     Protein         1..139
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15790
     Region          4..138
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 menyfllftd slvsslvlpi hqgfvfntml yfrsyhtpll mlffgvlgss lggivnwylg
       61 ritisirksy rklenehktp kivknllica vtllswvpal gsviqilsgy fklnlytlap
      121 liilsnffyl lyliltfgv
//
LOCUS       WP_010963748             288 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Clostridium].
ACCESSION   WP_010963748
VERSION     WP_010963748.1
KEYWORDS    RefSeq.
SOURCE      Clostridium
  ORGANISM  Clostridium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae.
REFERENCE   1  (residues 1 to 288)
  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 288)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 288)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 288)
  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   5  (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   6  (residues 1 to 288)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Clostridium"
                     /db_xref="taxon:1485"
     Protein         1..288
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32893
     Region          26..104
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          128..284
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mnwigdmnna lryveenler niesgevana ahmskfyflr ifkiltgmtl gdyirerkls
       61 latkdivstn qkiidisyky gyetpeaftk afkrlngisp tearksknnl kaipplsfqv
      121 ivkgeenmny kietkksfki agvskristk egnnfkiipe fwdevkksgq ceiieknagk
      181 lgvmgvctnf dceyqefdyl iavegdkieg ldnyvvievp elsfavfesi gpmpdalqdv
      241 trrifsewfp atkyeeaegp eievylpgnp qdkdyraeiw vpvvekrk
//
LOCUS       WP_010965050             401 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Clostridium].
ACCESSION   WP_010965050
VERSION     WP_010965050.1
KEYWORDS    RefSeq.
SOURCE      Clostridium
  ORGANISM  Clostridium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Clostridium"
                     /db_xref="taxon:1485"
     Protein         1..401
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44211
     Region          1..398
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mknlvincgs ssikyqfidm kdetvlakgl verigikgsv ithkvngeky vtetpmedhk
       61 kaiklvldal lndeygvikn ideisavghr ivhggekyan svlidedvmk siedcvslap
      121 lhnpphiigi nackelmpnv pmvavfdtaf hqtipdyaym yaipyeyydk ykirkygfhg
      181 tshkyvsrta aefigkkved lkmvvchmgn gasitaveng ksvdtsmgft plgglamgtr
      241 sgdmdpavvt flmdklnina sevnnllnkk sgieglsgis sdmrdikkgn yvdkdpkaml
      301 aysvfnykik qfigsytavm ngldclvftg gigensfenr reicknmdyl gikiddkknd
      361 etmgipmdis aegskvrvlv iptneelmia rdtkdivgkl k
//
LOCUS       WP_010965443             222 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: flagellar brake protein [Clostridium].
ACCESSION   WP_010965443
VERSION     WP_010965443.1
KEYWORDS    RefSeq.
SOURCE      Clostridium
  ORGANISM  Clostridium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 222)
  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   3  (residues 1 to 222)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Clostridium"
                     /db_xref="taxon:1485"
     Protein         1..222
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25648
     Region          18..222
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mgdlsfiain dkcevvldne iyksniqgie ekyiaislpv angtyaimhk gdmteiwcyh
       61 dnqvysftst vierkkedai kliliskpsy enikrvqrrk nfrvdliesi kykvlnknvv
      121 kteieklkea seefsdgymi dlsggglkir ikqkpnvgds ifvnlpigdq klflistcvr
      181 airevngeyl cglefdddid erirehiiny tfnimrkhmk kr
//
LOCUS       WP_010967278             131 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Sinorhizobium meliloti].
ACCESSION   WP_010967278
VERSION     WP_010967278.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     Protein         1..131
                     /product="PRC-barrel domain-containing protein"
                     /function="Miscellaneous; Unknown"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=14080
     Region          36..117
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mrrilialaa tttivgaaaa qtaettttet fvtakptdvl synlinlnvt ntanesigei
       61 kdlvlsegql agyilsvggv lgmgeryvvv spkalkityv endkkwtavm datkdqlkaa
      121 pefkyegrwk r
//
LOCUS       WP_010967301             430 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Sinorhizobium].
ACCESSION   WP_010967301
VERSION     WP_010967301.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium
  ORGANISM  Sinorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group.
REFERENCE   1  (residues 1 to 430)
  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 430)
  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 430)
  AUTHORS   ter Beek,J., 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 430)
  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 430)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Sinorhizobium"
                     /db_xref="taxon:28105"
     Protein         1..430
                     /product="CmpA/NrtA family ABC transporter
                     substrate-binding protein"
                     /function="Cell processes; Transport of small molecules"
                     /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=46646
     Region          40..301
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mtktlfgglt rrsvlkttat aamvgaartl lpsgafaqga gpetakatlg fialtdsapl
       61 iiakekglfd kygmtevevv kqaswgttrd nlvlgsagag idgahiltpm pylistgkvt
      121 qnnqplpmai larlnldaqa isvgaayadl kvgidasvlk dafakkkagg eaakvamtfp
      181 ggthdlwiry wlaaagidpd kdvetivvpp pqmvanmkvg tmdcfcvgep wneqlvnqki
      241 gytavntaei waehpeksfa mradwveknp ravkalvmai eeaaqwcddm ankdelakiv
      301 gkrswfnvpp kdivdrlkge ydygngkive nsphfmkfwr ehasypfqsh dawfltenir
      361 wgklasdtdi kgliakvnre diwreaakdl gisdipasts rgpetffdgk vfdpanpety
      421 lkslaisria
//
LOCUS       WP_010967951             633 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Sinorhizobium meliloti].
ACCESSION   WP_010967951
VERSION     WP_010967951.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 633)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 633)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 633)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     Protein         1..633
                     /product="potassium transporter Kup"
                     /function="Cell processes; Transport of small molecules;
                     cations"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68626
     Region          1..633
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 madsldhapa qannlpqfla ltigaigvvy gdigtsplya frealrpfgp ggvgrdevig
       61 lvslvlwtlt aivtikyvlf llradndgeg gtlsllalll kkgtkypvlm ffagvlgaal
      121 figdamitpa lsvlsavegl klvapalhdy vlpisvviil llfavqsrgt gavsvffgpi
      181 tlvwflmmaa agvahigddl ailsafnpln aigflwnagl igfivlgaif ltvtgaealy
      241 adlghfgrhs iqaawfavvf palalnylgq galvlshpda isnpfflmfp nwallpmvil
      301 ataatiiasq svitgafsli rqaihlgflp rfeicytset qtgqiylplv ntilltgvla
      361 lmlmfgssea lapaygvsit gamvidtila fefvrrqwgw paltaiavll plfnlelvfl
      421 ganllkvhhg gyvpiliagt litmmwtwrk gvsvlrekta rqdiplsqfm aiverkseha
      481 pvqvpgtaif ltatpdttpa vllhnikhnh vlhqhnvimt iktarvpyvp ekdrytitkl
      541 sdrfsllelr fgfmddqnvs ralarcrkeg fkfeimstsf ylgrrkliad pqsglpqwqd
      601 klfiamadsa idpteyfhlp anrvvelgeq vii
//
LOCUS       WP_010968068              81 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Sinorhizobium].
ACCESSION   WP_010968068
VERSION     WP_010968068.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium
  ORGANISM  Sinorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group.
REFERENCE   1  (residues 1 to 81)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 81)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 81)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 81)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Sinorhizobium"
                     /db_xref="taxon:28105"
     Protein         1..81
                     /product="MoaD/ThiS family protein"
                     /function="Miscellaneous; Unknown"
                     /calculated_mol_wt=8770
     Region          1..81
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mvevtlwgsl aaaaegnskv eieaknirel farlserfpr leplmargia vaidgtiyrd
       61 twskelptga eiyllprlag g
//
LOCUS       WP_010968272             632 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Clostridium
            perfringens].
ACCESSION   WP_010968272
VERSION     WP_010968272.1
KEYWORDS    RefSeq.
SOURCE      Clostridium perfringens
  ORGANISM  Clostridium perfringens
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Clostridium perfringens"
                     /db_xref="taxon:1502"
     Protein         1..632
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=72040
     Region          34..628
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mgifkrdyny npyffnkiqp vggikfnprs ivkgdgyeac lriydfptsv defwlgklid
       61 ikdvtvtidv etedrskalq slnsaisenv dranslknni diieannats ilmglvndit
      121 srdeviklvt iryylsakte ieleekikqv ltkleglgyr gavflneqey ewkslflsag
      181 eqkylrnkrs ghpvpsislg agypfhyvel ndptgmfmgt sitggnvifd lftkneqrks
      241 ynalaigvmg sgkstllkkl snnnaivnnt lrilditgef kdlvnelegk ivaldgsngm
      301 inplqifatm inentnevqv eqsymqhmsk vsmiynflsp eatqeeiref erllhdfyii
      361 ygierekats ykaeeyptls eflnyikgvf yedeekasir knlsdfrkkr lesimltidn
      421 airnygklfd ghssiedltk eqivsfeirt ltgvdkrifn aqifnvlsml wnnaltqglp
      481 ekkafdegkk tveeskkyll lldeshriin snnilavdyl inferearky fgglifatqs
      541 irdvvpdvsn sevfekirtl feltqykfim qqdnntkgll seifsgqltd teinaipnfs
      601 tgdcilving dknirfniei sdrekylfkg ga
//
LOCUS       WP_010968846             212 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Sinorhizobium meliloti].
ACCESSION   WP_010968846
VERSION     WP_010968846.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     Protein         1..212
                     /product="PRC-barrel domain-containing protein"
                     /function="miscellaneous; hypothetical/partial homology"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=21497
     Region          85..167
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mkerlissva agallvgvav apmsfaqqtt tppatapetq tmepapapap atppaadeqa
       61 qtpdtadktt dmaagdatyl teqaenqvsa ntyigqsvyn asdesigein dliiekeggi
      121 aaavvgvggf lgigeknvav pfdkiavadq pdsddikltt tetadslkaa pefktksqlm
      181 aernadqpvd tsttsatgtt papapaepap qq
//
LOCUS       WP_010969442             362 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Sinorhizobium meliloti].
ACCESSION   WP_010969442
VERSION     WP_010969442.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 362)
  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 362)
  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   3  (residues 1 to 362)
  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   4  (residues 1 to 362)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 362)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 362)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 362)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     Protein         1..362
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /function="cell processes; transport of small molecules;
                     amino acids, amines, peptides"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37279
     Region          32..347
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(90..92,113..114,166,218,242)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mpkslvtslf vaalaltgpa faagvkvavv apeegafasl grqisagaaf qagdrgsqvi
       61 pinencdpag gqaltkalla sgaeaaigfl ctesleaalp alaeagipai tvsvrsdilm
      121 edalkkewpf yrlapsgkae aaaitdaiva nwkgrplali ddgtihsrel vesvrnglae
      181 igitpvftdt yrpsqeqqvs lvrrlaksga thvftggdrn dtaviardat aenvpiillg
      241 gdtlnaadld vplengvlam tipdparsse aaavakamra akvepegyvl pafaavslle
      301 qakdqaakdg ssladaltkg pyptvlgpig fnsahelaet pyrlmrwqdg rfvdaaatgs
      361 te
//
LOCUS       WP_010969805             687 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Sinorhizobium meliloti].
ACCESSION   WP_010969805
VERSION     WP_010969805.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 687)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     Protein         1..687
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /function="small molecule metabolism; degradation; fatty
                     acid"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=71972
     Region          1..687
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mttpprsldr lirprsiavf ggkearrvie qcdkmgfagd iwpvhpreee ilgrrcyrsv
       61 adlpeapdas fvgvnralti eiirdlatrg aggavcyasg freaanelad gndlqealva
      121 aagdmpivgp ncygfinmld gallwpdqhg mlrvergvai ltqssniacn ismqkrglpl
      181 ayvmtagnqa qtglsdiaca vledprvtav glhiegfdsi ealerlaara relrkpvvtl
      241 kvgkseaaql atvshtasla gndrvssall arlgigrvdt lpelletlkl lhlhgplpsa
      301 dissmscsgg easlvadagv rrkvnfralr eeqrqplres lgemvtianp ldyhtfvwgn
      361 rekqtaafta mmhggyalnl ivldfprldr cdaadwvttc eavidstkat gavagivasl
      421 genmpeetai slvsagvvpf fgidealgav etaaaigavw akpaappllr srpeggeivt
      481 lseaeakdel aaagvivpgg rsaatveeaa aaaeslgfpv alkglgvahk teagavrlnl
      541 tnrdevieaa rgmasvasgy lvekmiakpv aelivgaard avagpvltig aggilvelle
      601 dsailtlpvt eesirdaiag lkisrlldgy rgnpkgdiaa lirtvaaaas yvvanaskle
      661 eldinpimvl pdghgavaad alirrrk
//
LOCUS       WP_010970719             312 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Agrobacterium fabrum].
ACCESSION   WP_010970719
VERSION     WP_010970719.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium fabrum
  ORGANISM  Agrobacterium fabrum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium; Agrobacterium tumefaciens complex.
REFERENCE   1  (residues 1 to 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
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Agrobacterium fabrum"
                     /db_xref="taxon:1176649"
     Protein         1..312
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=33860
     Region          1..308
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mieidtitkr ygdttvvdqv sltvaprtvt vivgtsgsgk ttllrminrl veptsgtiri
       61 dgedisaipg fklrrqigya iqghglfphr tvaeniatvp qligwdrqri kakidalmhl
      121 fqldpalyad rfphelsggq qqrvgvaral aaepnillmd epfgaldpvi rakaqndlld
      181 iqkklgvtiv lvthdmdeaf hladriavmd kgrivqdcpp aelvlkpatd fvrtmigene
      241 ralkllsvlt vadivepgsa egapltegts qrdalsamlw agrdvlpvik ddgqpigrvr
      301 rdvllqratg ap
//
LOCUS       WP_010970135             313 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Sinorhizobium meliloti].
ACCESSION   WP_010970135
VERSION     WP_010970135.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 313)
  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 313)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     Protein         1..313
                     /product="AraC family transcriptional regulator"
                     /function="miscellaneous; not classified regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34699
     Region          31..181
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          209..289
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtesqriprq emidiiaria gedgdhptim pglsvhrhsv sakpncaayk pslaiivqga
       61 krvvlgeetl vygasdyllt sidlpvlsqi slaspeepyl smvfqidttr lpalldaigp
      121 eaakapaspr gmtvskltpd ledtalrllr lldrpddiav llplveqell yrlllgphga
      181 rlrqmattes qphqigravs wlkehysrpl riddlasrvs msvsslhhhf kaitamsplq
      241 yqkqlrlqea rrlmleerld agdaghkvgy esqsqfsrey arhfgepprr dvgrvrrsli
      301 grssgeveml seg
//
LOCUS       WP_010971082             295 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Agrobacterium fabrum].
ACCESSION   WP_010971082
VERSION     WP_010971082.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium fabrum
  ORGANISM  Agrobacterium fabrum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium; Agrobacterium tumefaciens complex.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Agrobacterium fabrum"
                     /db_xref="taxon:1176649"
     Protein         1..295
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31749
     Region          19..261
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 matvfpfagr vldetpmllg egptfdpasg tawwfniler elhelhlasg rktvhalpfm
       61 gsalakisds kqliasddgl flrdtatgvl tlhaelesdl pgnrsndgrm hpsgalwigt
      121 mgrkaetgag siyhvakgkv tklfadisip nsicfspdgt tgyfvdtkvn rlmrvpldar
      181 tglptgkaev fidstgikgg mdgsvcdaeg hiwnarwgeg avdrydtdgn hiaryevpgk
      241 qttcpafigp dasrllvtsa rehldddait anpqhgltfe lgievkgrfe plyrl
//
LOCUS       WP_010971122             398 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Agrobacterium
            fabrum].
ACCESSION   WP_010971122
VERSION     WP_010971122.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium fabrum
  ORGANISM  Agrobacterium fabrum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium; Agrobacterium tumefaciens complex.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 398)
  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 398)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Agrobacterium fabrum"
                     /db_xref="taxon:1176649"
     Protein         1..398
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46058
     Region          1..395
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mvikvsneaa rriflarqgl ssppgkalsk sdllqlitdi gfvqvdsigt verahhqiif
       61 srnqtyrrdh lttllekdra lfehwthdas ivptefypyw khrfrrrepi iqerwrkwhg
      121 egfdaafget leriaatgpv larelkeegh qsggwwnwhp sktaleylwh tgklaiagrv
      181 nfqkvydlae rvipgehhet evehaefvdw acrqalkrlg fathgeiaaf fdlvtpqear
      241 dwvkshrdel cevslfssdg etarpsfafa dftadltdvp epssrvrvls pfdpllrdrn
      301 rterlfgfyy rievfvpepk rqygyyvfpl legdrvigri dmkadrkrst ldvrrlwlep
      361 gvrasagrle kldaelvrla rftgvesvny legwrges
//
LOCUS       WP_010972826             145 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Agrobacterium fabrum].
ACCESSION   WP_010972826
VERSION     WP_010972826.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium fabrum
  ORGANISM  Agrobacterium fabrum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium; Agrobacterium tumefaciens complex.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Agrobacterium fabrum"
                     /db_xref="taxon:1176649"
     Protein         1..145
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15738
     Region          7..145
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 madlavyagl fltafiaati lpmqseaala glillksqpv wllvatasvg nvagsfanwl
       61 lgcgierfrh erwfpvgeaa lqraqnwyrr ygkwslllsw apligdpltv aagimkeplp
      121 vflllvtiak vgryvvlall tlnfl
//
LOCUS       WP_010973418             431 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Agrobacterium fabrum].
ACCESSION   WP_010973418
VERSION     WP_010973418.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium fabrum
  ORGANISM  Agrobacterium fabrum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium; Agrobacterium tumefaciens complex.
REFERENCE   1  (residues 1 to 431)
  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 431)
  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 431)
  AUTHORS   ter Beek,J., 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 431)
  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 431)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Agrobacterium fabrum"
                     /db_xref="taxon:1176649"
     Protein         1..431
                     /product="CmpA/NrtA family 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=46123
     Region          32..290
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 maapektags kgeatqmrda palvgsdrqk ilragfiplv dasvliaaae fgfadregli
       61 ldlvkdvswa nvrdrlafrq fdiahmlspm pvasmlglgs npsptitpfs lgrggnaitl
      121 strlfarmka ltglsetaga lenaralklv lddmrargea pptlgmtypf sshnyefryw
      181 laaggihpdh dvklvvvppp mtsdalaaga idgfcvgapw nivaaergvg rivaakqdlw
      241 psapekvigm rpewaesqqe tvgrlltald aaaswcdlad nhdalsgala dpryigapqs
      301 iirrvlagef sidsqgnrrv iekyftfhgd hanyprqsqs lwiysqmirw gqaelsetgv
      361 naalsayrpd iyraalgdgk apgdadirie gqdegdrfvd gfvfdpadia gyvnsfavrt
      421 svpvsapsge a
//
LOCUS       WP_010973924             274 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Agrobacterium fabrum].
ACCESSION   WP_010973924
VERSION     WP_010973924.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium fabrum
  ORGANISM  Agrobacterium fabrum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium; Agrobacterium tumefaciens complex.
REFERENCE   1  (residues 1 to 274)
  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 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   3  (residues 1 to 274)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 274)
  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   5  (residues 1 to 274)
  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   6  (residues 1 to 274)
  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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Agrobacterium fabrum"
                     /db_xref="taxon:1176649"
     Protein         1..274
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30219
     Region          18..101
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          127..272
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mpaldkliwq ietdlnkdlt ltvlsdrcai sthhmcrlfq lstglsimsy vrarrlsmaa
       61 dtiarhdgdi ltaaldagyg sheaftrafa nyfnalpstv rkarstssld lmeplkmknd
      121 mfvevqppem rradafmvvg lstpcslenn stipalwqrf nlreseveev vsgaaygvcs
      181 aadeagncty lagvkaltkt pgmdyielpa qsyavfthng hisdlprtvy tiwnkalpea
      241 glktadspdf erydqrfnpe tgrgsveiwi pvia
//
LOCUS       WP_010974199             336 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Agrobacterium fabrum].
ACCESSION   WP_010974199
VERSION     WP_010974199.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium fabrum
  ORGANISM  Agrobacterium fabrum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium; Agrobacterium tumefaciens complex.
REFERENCE   1  (residues 1 to 336)
  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 336)
  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 336)
  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 336)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Agrobacterium fabrum"
                     /db_xref="taxon:1176649"
     Protein         1..336
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=36531
     Region          5..333
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mninrrsila gagsavlata fvsrahaaqy nykyannlpa ahpmnirake aaeriaketd
       61 gqvnisifps sqlgadtdvl sqvrsggvef ftlsplilst lipnasisgi gfafpnyesv
      121 waamdgdlgk yvrgeiakqn lvamdtiwdn gfrqitsask piatpadles fkirvpvspl
      181 wtsmfkafks apasinfaev ytalqtgvvd gqenplaiis taklfevqkf csvtnhmwdg
      241 fwflankraw erlpddlrai vaknlnqsgk deradvakln asvkedlisk gmtfndtdat
      301 lfraalkeag fysewkgkyg deawaileka vgaslt
//
LOCUS       WP_010975706             392 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Sinorhizobium meliloti].
ACCESSION   WP_010975706
VERSION     WP_010975706.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     Protein         1..392
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /function="Small Molecule Metabolism; Energy transfer;
                     electron transport"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=41892
     Region          3..390
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 meallvinag ssslkfqifg iataglerqv rakldgiatq prlkataadg telinrrlda
       61 tavpdlpeal svardwlatl rgfdlraigh rvvhggpdyv rpvliettvl drlasyqdla
      121 plhqpnnlap irlamdikpd vpqvacfdta fhrgrtehtd cyalprtfye qgvrrygfhg
      181 isyeyiagrl revapevarg rvivahlgsg asmcalkdgr svettmgfta ldglpmgtrp
      241 gqldpgvvlh lltdqgmsaq avsdllyhrs glkglsgisn dmrellgsdd prasfaidhf
      301 vhrcaldagm laaalgglda fvftagigen sapirarvse glawlgaeld paandagasv
      361 iskagsrval hvmptdeelm iarhtlaiir ar
//
LOCUS       WP_010976309             621 aa            linear   BCT 20-JAN-2025
DEFINITION  sensor histidine kinase [Sinorhizobium meliloti].
ACCESSION   WP_010976309
VERSION     WP_010976309.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 621)
  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 621)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20493667
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     Protein         1..621
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /function="CELL PROCESSES; Transport of small molecules;
                     carbohydrates, organic acids, alcohols"
                     /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=67002
     Region          65..250
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          286..618
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mhhvrmvklp aeasdphalr srarrswlvf aavalvllaa glllardygr sqalaglagq
       61 sridaslkas llravverqr alplvladda airgallspd rpsldrinrk lealatsaea
      121 aviylidrsg vavaasnwqe ptsfvgndya frdyfrlavr dgmaehfamg tvsnrpglyi
      181 srrvdgpggp lgvivaklef dgveadwqas gkpayvtdrr givlitslps wrfmttkpia
      241 edrlapires lqfgdapllp lpfrkiearp dgsstldall pgdstaaflr vetmvpstnw
      301 rleqlsplka plaagareaq lltlaalvpl lalaalllrr rqvvamrsae erlarnalea
      361 sveertrdlr mardrletei adhrqttekl qavqqdlvqa nrlailgqva agvaheinqp
      421 vatirayadn artflhrgqt vtaaenmesi aeltervgai tdelrrfark ghfaagptam
      481 kevvegalml lrsrfagrmd airldlppdg lqalgnrirl eqvlinllqn aleaigdsed
      541 gaiqvrceea aggialtvad ngpgiaadvr eelftpfnts kedglglgla iskeivsdyg
      601 gtievesgps gttfavnlkk a
//
LOCUS       WP_010976905             210 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MJ0042-type zinc finger domain-containing protein
            [spotted fever group].
ACCESSION   WP_010976905
VERSION     WP_010976905.1
KEYWORDS    RefSeq.
SOURCE      spotted fever group
  ORGANISM  spotted fever group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia.
REFERENCE   1  (residues 1 to 210)
  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 10020205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="spotted fever group"
                     /db_xref="taxon:114277"
     Protein         1..210
                     /product="MJ0042-type zinc finger domain-containing
                     protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24137
     Region          1..38
                     /region_name="MJ0042_CXXC"
                     /note="MJ0042 family finger-like domain; TIGR02098"
                     /db_xref="CDD:131153"
ORIGIN      
        1 mhitcpncqt rfivtsnqig ingrrvkcsk cshlwyqkld yntstlndfk dkvntgtikt
       61 piknhynanv pvilpyippk kkynifpilw tsfiifclvi llidsfkfld kydqlkieei
      121 nlgksrhigg mkifyklsne sdylisdpii kvrvmdtnnq aldeyvsitk lqtkipakqa
      181 iylemniegi pitakyidiv ignrlgllfk
//
LOCUS       WP_010981065             170 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Neisseria meningitidis].
ACCESSION   WP_010981065
VERSION     WP_010981065.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..170
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=18003
     Region          1..128
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mntlqkgftl ielmiviaiv gilaavalpa yqdytaraqv seaillaegq ksavteyyln
       61 hgewpsnnts agvasstdik gkyvqsvevk ngvvtatmas snvnneikgk klslwakrqd
      121 gsvkwfcgqp vkrndtattn ddvkadtaan gkqidtkhlp stcrdaasag
//
LOCUS       WP_010982292             740 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: penicillin acylase family protein [Streptomyces].
ACCESSION   WP_010982292
VERSION     WP_010982292.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 740)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 740)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..740
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=78709
     Region          16..719
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mnataparlr tpdgivevas daldrpvvta pswtaaafgl gwtvarhrre qmdfmrrrsh
       61 grlaevlgpq avqadvrqrv lglahvarac wellpmsqrh tlrayadgvn aaapngpgga
      121 wtpvdciavt qgvfqalssd gqdvrmvevm rrtlpaavvd flldpqdefa vgidgtvpdv
      181 crsalpvael kalmaeppgp agplvvsdgr pigsnawavt dgdtavland mhleltspsl
      241 myaarlvvgd tgvtgvtvpg lpaivagtng riawgftrlp adtcelrelt pgstpgtyrh
      301 egrdrpftvr rervsvmggd dvevevretr wgpvvdqlrg rplvlsanlt dptaldfalv
      361 glyesanvaa aadllndcgm pplnavladt aadvawtvtg rhprraggpr gfsdserdpw
      421 ptprlaphel prlvtppsgh viscnngdaa grtaglgwnf fpgtrsrraa aalaaggphd
      481 earcgalqld vdaelyayyr dlalrytper apvplralrd evlawrgtsh hdeyglallv
      541 lfrellreel faaltrpcrr ydeaftycyn gherplrrll dalaadmvpk pwpgpaalvv
      601 gmlgsaktll tkrtgsaept rwgsvnalap tplggapvhg gppgghager gvglsgcpes
      661 lrvtqpdfga amrlvvapar pedglltipg spagtgpvdl dhiarwtqgk thplpmredt
      721 pygdgvrgpg slrtptgrtl
//
LOCUS       WP_010982462             342 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: phytoene/squalene synthase family protein
            [Streptomyces].
ACCESSION   WP_010982462
VERSION     WP_010982462.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..342
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37605
     Region          16..279
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mtdreldaag itdpslrkay thcrrlnarh gktyflatrl lpverrpavh alygfarwad
       61 divdsldttv gpavrsaalg rlqeslrtgl reghstepvv lalaetarry aidhqhfsdf
      121 mtamrsdlev tgyetyadlr gymhgsaavi glqmlpvlgt vvpreeaaph aaalgvafql
      181 tnflrdvged ldrgrvylpa dllrahgvdr dllrwsrdtg rrdrritral kavegltrgv
      241 yreaapglam ldpvarpcir tafvlyggil daiaddgyav vhrravvprr rraavaldgl
      301 vrlgvarlgs radarlptlp dpwrlpalvp rssprpahee va
//
LOCUS       WP_010982675             380 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: aminoglycoside phosphotransferase family protein
            [Streptomyces].
ACCESSION   WP_010982675
VERSION     WP_010982675.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 380)
  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   2  (residues 1 to 380)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..380
                     /product="aminoglycoside 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=41006
     Region          99..310
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mytasssvsa pprslhprqp gssgpyldpa rpaapllgag rsrrvpglgt qplsgridls
       61 gpqgaqlrta iasvhricpe ftpvqvlrrs grsvllvgtt grstavakcl ldhspiwaer
      121 irheiaayrs fvrhrppvrv prliaadpdn ctlviermpg rvaalqrhpa eappradira
      181 algalcrvna wrppagtfda plnyaerisr fhelglltdr dmgdlqklmh giahsagrqg
      241 mgqfchgdal lsnillspag pvlvdwehag wylpgydlat lwavlgdapv arrqisqlaq
      301 sagpaardaf lvnlmlvltr eirtyetavq rsmhdvtpaa pgqahpaaap sgeeqrlllr
      361 rlhddcqmar ravraavgtr
//
LOCUS       WP_010983244             432 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Streptomyces].
ACCESSION   WP_010983244
VERSION     WP_010983244.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 432)
  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 432)
  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
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 432)
  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   5  (residues 1 to 432)
  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   6  (residues 1 to 432)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 432)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 432)
  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 20282815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..432
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=45046
     Region          10..>60
                     /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...; cl46857"
                     /db_xref="CDD:481197"
     Region          79..400
                     /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 maarngrtvh dlrrenrtav lqrlyfdgpm srhslapatg lssgsisnvv aelladglve
       61 eagsvgsdgg rprtllrvvp gsghmigvdv getrvrvelf dlslaelart erplahkgrq
      121 aydvgvivgh irdgvaevla aagitagell gvgigvpgiv ersgeggavv hgqtigwdav
      181 plehmlrlsg qlpehvpyfi dngaktlgqa emwfgagrga hnavvvlfgs gvgacvvtde
      241 vehgravewg hltvrvqgrr crcgalgcle ayagaealla rwqeaggqpp ydtdeetalt
      301 amlaaayped grapdpvaaa vlaetaeylg aglsdlinlf qperilvggw aglqlgsrfl
      361 esvrthalay alrypagrvg ielgrlgpda vtvgaailpl adffahggrr apapdapvps
      421 pawrtsldgr la
//
LOCUS       WP_010983740             265 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AfsR/SARP family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_010983740
VERSION     WP_010983740.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..265
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=29219
     Region          1..249
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mlsfsilgal qirtalgpae isgdlqrtli qtllvnegqs isgeslveem wgeavpdnqa
       61 nalqahisrl rrklrslepd rttsrvtihp sgyrltines eldaaeftkt vrlaevatad
      121 dpaatarllg galamwrgpv fgdfpggtlc qlacaryeey rmramelrfd aelrlghhaa
      181 mlaelhdaht nhplrerfce qlmialyrsg rqadalnvyr rmwqhlsdel giepspalrr
      241 venailshdp alagdtpapi ilqpa
//
LOCUS       WP_010984227             554 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: M4 family metallopeptidase [Streptomyces].
ACCESSION   WP_010984227
VERSION     WP_010984227.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 554)
  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 554)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..554
                     /product="M4 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=57308
     Region          44..553
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mtslyarhkr ttlaiatava agallatgvt tgasaqtpvs dagkkatlag aplqlsaaar
       61 tslikkaeaa tpetaqqigl gtkeklvvrd vvkdadgtlh tryertyngl pvlggdlvvh
      121 qsksgttegv tkatkatikv aslkpqitsa kaekqaltva ksagsektsa draprkviwa
      181 gngkptlafe tvvgglqddg tpnqlhvitd aatgkklyey qaietgtgkt lysgtvtlnt
      241 tlsgstyqlt dgtrgshkty nkshtttssa gtlftdaddt wgtgaassst tdqtaaadaa
      301 ygaqvtwdfy kntfgrsgik nngvaaysrv hygnayvnaf wddscfcmty gdgsgnthpl
      361 tsldvaghem shgvtantag lnysgesggl neatsdifgt gvefyaanss dvgdyligek
      421 iningdgtpl rymdkpskdg gsadswsssv gnldvhyssg vanhffylls egsgskting
      481 vtynsptsng stvtgigrak alqiwykalt tyftsttkya aartgtlsaa salygstste
      541 ykavaaawsa vnvs
//
LOCUS       WP_010985106             936 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: penicillin acylase family protein [Streptomyces].
ACCESSION   WP_010985106
VERSION     WP_010985106.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 936)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 936)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 936)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..936
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..936
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=102257
     Region          25..936
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mppnttassg eqpgksgrkk grkarllviv lvlaiiggig fgaywsistv rasfpqtkgs
       61 itldglagpv dvkrdgygip qiyassdadl fmaqgyvqaq drfyemdvrr hmtsgrlsem
      121 fgkgqvkkde flrtlgwdrv akkeydtkls aatkkylray akgvnayleg kdgkdisley
      181 aalgftndyq pqkwtpvdsv swlkamawdl rgnmqeeidr slmtsrlgpk qiadlypdyp
      241 ysrnktivqe gqyneltkaf eqggstgtqs ttggtstgts gtsgtsgttg stsasgtsts
      301 asdpsalesq ltglyklldd vptavgvngn gigsnswvvs gdhtitgkpl landphlsas
      361 lpsvwyqmgl hcrsvsskcq ydvsgytfag mpgvvighnq aiawgmtnsg vdvtdlylek
      421 lsgdgylydd kvlpftshde tikvaggrsk tivvretnng pllsdrndel vkvgkkatvd
      481 taapdrgdgy gialkwtala pgnsmdavfe ldkaanwsef rkaaasfdvp sqnlvyadkd
      541 nigyqlpgki ptrakgddgs lpvpgwdsky qwtgyieqde lpyeynpdrg yivtanqavv
      601 dkdkypytlt tdwgygsrsq riadlieski kgggkistdd mrqmqldnss eiakllvpkl
      661 lkldvadkhv reaqkllegw dytqdadsaa aayfnavwrn vlklafgnkl pkelrvqgqc
      721 lyvdpaestg padqdqkvre cgqrdadqaq pdggdrwfev vrslmddenn dwwtspksrt
      781 deatdtrdel faramkdarw eltaklgknm dtwswgrlhr lflknqtlgt egpdvvkyvl
      841 nrgpwklsgg eatvnasgwn aaggygvvwv psmrmvvnlg dldkskwinl sgasghafsa
      901 hytdqtdkwa kgellpwafs ekavdgstsd slvlkp
//
LOCUS       WP_010985604             209 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Streptomyces
            avermitilis].
ACCESSION   WP_010985604
VERSION     WP_010985604.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces avermitilis
  ORGANISM  Streptomyces avermitilis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 209)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Streptomyces avermitilis"
                     /db_xref="taxon:33903"
     Protein         1..209
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=21456
     Region          89..179
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mggeyritgd kyprmrrprg rrrlvfavia saaalgligw gtlqlidvft gggdrataas
       61 skahcatgas psatpttaaa kalpepgkit vnvfnatprs glakktadel kkrgfrigdv
      121 gnatseydkk vkgvgilfgp easldtslpv lgtqladaer rtdagrkgta vdliigtgfk
      181 altskadadk alaeltgpap tstatkknc
//
LOCUS       WP_010986846             375 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Streptomyces avermitilis].
ACCESSION   WP_010986846
VERSION     WP_010986846.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces avermitilis
  ORGANISM  Streptomyces avermitilis
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Streptomyces avermitilis"
                     /db_xref="taxon:33903"
     Protein         1..375
                     /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=42578
     Region          34..304
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mpsprapqns sssqisqtsr gasqaaspes kpvkqrdaff dnakylaivf vamghawepl
       61 tdhsraaeal ymvvytfhmp afilisgyfs rsfdmrpdrl krlvtgvavp yvlfevaysl
      121 fkrwadndpg hpislldpwy ltwflvalfv wrlttplwkv vrwpvplala iavlasvspd
      181 igddldlqrv lqflpffvvg lfmkpehfql lrrrevrvls vpvfaialav aywagprmns
      241 awfyhrdsaq elgapwwagv vmtlalfgcs lvvtscffaw vprrkmwfta lgagtlygyl
      301 lhgfiakgsr fwdwydaawl qtpygeviat vfaatlitvl ctppvqrifr famepkmewa
      361 fkrdateiar eraka
//
LOCUS       WP_010986787             403 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Streptomyces].
ACCESSION   WP_010986787
VERSION     WP_010986787.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 403)
  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 403)
  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
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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   5  (residues 1 to 403)
  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   6  (residues 1 to 403)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 403)
  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 18624027
            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="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41777
     Region          1..>61
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          81..391
                     /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 magsagtpgt prvlramndr aaldlllehg plsrtrigkl tglskptasq llarleaagl
       61 vlmtgtsegr pgpnaqlyvv npgaahaagl dvtperilaa vadvtgrtvg ayelptpgrr
      121 paqpvvrqvt daldgavkaa glarddihrl vigtpgafdp ntgrlryash lpgwhsptll
      181 delaaalpmp veyendvnlv aiaeqrlgaa rghadfvllw negglgaalv lggrlhrgwt
      241 ggagevgflp vpgaplvrqv transggyqe lagsqaipel arelgiedip pgpyaevaat
      301 lveraaghdd gpyrqllrty atglatglas lvsvldpelv vlsgtslsrg geplralvqa
      361 eledlaasrp rlvvgdvheh pvlrgalesa laatrdevfd tsr
//
LOCUS       WP_010987071             531 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: M4 family metallopeptidase [Streptomyces].
ACCESSION   WP_010987071
VERSION     WP_010987071.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 531)
  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 531)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..531
                     /product="M4 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=54962
     Region          24..>519
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 matatatlla talaptagad tgpsratvid naaavlthqa arlgltaaqg tsvrdvvvda
       61 dggqhvrydr tyrhlpvlgg dfvvhlapng syrgadrstr raisladitp alsapkaadl
      121 ataalraant gellkkvtak pqlvvdalhg apklawrtnv vgqdslgnpv artvltdars
      181 gkqidawdsi etatgdgksl ysgtvalest lsgstyqlkd atrgntytgd aanktdlcil
      241 gicfsrapat lftdadnhwg tgaasdrssa avdaqygtne twdyyknvhg rngiagdgkg
      301 synrvhygsn ynnafwddsc fcmtygdgdg ttfgplvald vaghemshgv tsktaaltys
      361 gesgglneat sdvfgtlvef hannssdagd yligekivrs gfgkaalrfm dkpskdgnsa
      421 dcwsssvgnl dvhyssgvan hfayllaegs gaktvngvsy nsptcngstv tgigrdklga
      481 iwyraltvym tsstnyagar tatlsaakdl ygagsteyna vaaawsavsv g
//
LOCUS       WP_010987144             286 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Streptomyces].
ACCESSION   WP_010987144
VERSION     WP_010987144.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            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="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29810
     Region          14..256
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mtgldvavra haalgegptw dtaaqrliwv dilgsrvhty dpasgrrtvl ateqhvgaak
       61 praggglvvn lrdgvglygp egpggrdfrw lhrepvpgrr gndaavaadg slwagtmryd
      121 eapgggtlsr lapdgtartv lddvtisngv gwspdgrlmy fndtptrrid vfdvdedgrp
      181 vgrrtlatve egagfpdglt vdadgcvwva lwdggvvrry tpsgaldrvl elpvrrptac
      241 afggagltdl yittartgla aphpmsgsll vlpgagkglp qpafag
//
LOCUS       WP_010987229             214 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease family protein [Streptomyces].
ACCESSION   WP_010987229
VERSION     WP_010987229.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..214
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=23000
     Region          <116..207
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mpkvyarrrl silaaftgli alagifngpa asaalptpvs aatartylas ltvatenrtg
       61 ydrdlfptwi tisgtcntre yvlkrdgsnv vtnsactats gswysvydga twtaasdldi
      121 dhlvplaeaw dsgasawtta qrqgfandvt rpqliavtdn vnqsksdqdp aewmpplssy
      181 tctyvrawvq vkyyynlsvd saeksklssv lsgc
//
LOCUS       WP_010987396             194 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Streptomyces].
ACCESSION   WP_010987396
VERSION     WP_010987396.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 194)
  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 194)
  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 194)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            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="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21051
     Region          101..187
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(120,139..140,158,161,169..170,180,185)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mantrsfssv atvpspapsp gsarhrlrav drdevvdvad flppgatwlp apqhtlptlp
       61 gqppmigylv lvpadqqtvl pvavpdqpea sdltagdgpl irvdtvqrta evdgqpldlt
      121 ylefellahl vahphrvhtr dqlvttvwgy ghvgdgrtvd vhiarlrrkl gadhrqtiqt
      181 vrrvgykytp ptgr
//
LOCUS       WP_010988200             311 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: aminoglycoside phosphotransferase family protein
            [Streptomyces].
ACCESSION   WP_010988200
VERSION     WP_010988200.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..311
                     /product="aminoglycoside 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=32205
     Region          43..255
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mtadllpglt arvramahpe agpcgcdaag tladradgtv vrhadtvaka hapdtdpael
       61 alrleiasrl agillpplsp tpadlhgrpv tfwpygspvn pdcpraapwe aaatllarlh
      121 kapapkglpp mrgpakaara larlhaagph paaapilraw aglpawarae apmpssktlc
      181 hgdlhlgqlv rhpattgpwl lidvddlgvg epawdlarpa awyacgllpp dewtrflaay
      241 raeggpavpa dgdpwpvldv aaraltvqta avavakavta drpldeveqa vidacdrmgg
      301 vppefihgsa t
//
LOCUS       WP_010988429             181 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CHAP domain-containing protein [Streptomyces].
ACCESSION   WP_010988429
VERSION     WP_010988429.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467641
            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="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19455
     Region          46..>153
                     /region_name="COG3942"
                     /note="Surface antigen [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443142"
ORIGIN      
        1 mhrrtskkwp rvvaagvtat aflvlfgstg hatptagpvs sapapattal dptayrwkna
       61 hgtreldghg yfkrscvsfa awairadghp htespdflgd aghwrgaats svphvgdiaq
      121 wdpgvhgtgr rghvayvaav rddgrvtlye ynyrsefndq rpdvlsvraa aasdasrylr
      181 f
//
LOCUS       WP_010988574             199 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Streptomyces].
ACCESSION   WP_010988574
VERSION     WP_010988574.1
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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..199
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=22058
     Region          57..197
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 meraralpsr rqllkgaava avpyallpaa qagaepravd ypsaewtaas tsnytassrp
       61 ssypldyvvi hvtqetyptt ldifrnpqkg vsahyvvrsa dghvaqcvre rdiawhagnw
      121 dyntrsigie hegwvdqpay ftdalyeesa rltaaicaqy gipkdrahii ghyevpgtdh
      181 tdpgpnwdwv rymrlvnfa
//
LOCUS       WP_010989636             343 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Listeria monocytogenes].
ACCESSION   WP_010989636
VERSION     WP_010989636.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..343
                     /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=40317
     Region          4..276
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mtqsalkres yfdnakfili flvvfghflq tfiadyagvr vlyiyiytfh mpafvlisgf
       61 faksfgkpgy lkktmkklil pyvffqliys ifyyfllskd nlsiqlldpe wslwfllslf
      121 fwnimlfifa kikpwksici alfvglvagy fdiiggylsl srtlvffpff lvgyflkkeh
      181 fyylkthfvm ilggifivll lsfitlhpnl ndkwflgskp yanfvevksl glfiralvyl
      241 isfgsiaaff sfiprkrlff tkwgkntlyv yllhgffikf fregsqtdfq yspstflllf
      301 vvtfvltvll ssrlvkifvq pvielrvsml rdvfsrltkr esy
//
LOCUS       WP_010990790             397 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Listeria innocua].
ACCESSION   WP_010990790
VERSION     WP_010990790.1
KEYWORDS    RefSeq.
SOURCE      Listeria innocua
  ORGANISM  Listeria innocua
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Listeria innocua"
                     /db_xref="taxon:1642"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42985
     Region          3..388
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mhkimainag ssslkfqift mpgeevlvkg lieriglpda ifnmsfqnek iketrainnh
       61 geaveilleq lkthqvindl neitgvghrv ahggeafvss civtddvvkg iedvtslapl
      121 hnpaniigik tfrellpnav svavfdtafh qtipeenfly alpyelyekh hirkygfhgt
      181 shkyvagkaa evlkkplekl kiischlgng asvcaieagk svntsmgftp naglmmgtrs
      241 gtidatiipy lvdelgysld evthmmsses gvlgvsgiss dfrdieiaan egnsralltl
      301 rmftgqicny igayasamng cdallftagv gensplirkm vteqlsylgv tcnvtknnag
      361 dmiisnddea vkvciiptne elmiardvek ytkqtis
//
LOCUS       WP_010991083             284 aa            linear   BCT 20-JAN-2025
DEFINITION  class II fructose-bisphosphate aldolase [Listeria innocua].
ACCESSION   WP_010991083
VERSION     WP_010991083.1
KEYWORDS    RefSeq.
SOURCE      Listeria innocua
  ORGANISM  Listeria innocua
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 284)
  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 284)
  AUTHORS   Marsh,J.J. and Lebherz,H.G.
  TITLE     Fructose-bisphosphate aldolases: an evolutionary history
  JOURNAL   Trends Biochem Sci 17 (3), 110-113 (1992)
   PUBMED   1412694
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Perham,R.N.
  TITLE     The fructose-1,6-bisphosphate aldolases: same reaction, different
            enzymes
  JOURNAL   Biochem Soc Trans 18 (2), 185-187 (1990)
   PUBMED   2199259
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10097223
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Listeria innocua"
                     /db_xref="taxon:1642"
     Protein         1..284
                     /product="class II fructose-bisphosphate aldolase"
                     /EC_number="4.1.2.13"
                     /GO_function="GO:0004332 - fructose-bisphosphate aldolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /GO_process="GO:0030388 - fructose 1,6-bisphosphate
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=30807
     Region          5..281
                     /region_name="TBP_aldolase_IIB"
                     /note="Tagatose-1,6-bisphosphate (TBP) aldolase and
                     related Type B Class II aldolases. TBP aldolase is a
                     tetrameric class II aldolase that catalyzes the reversible
                     condensation of dihydroxyacetone phosphate with
                     glyceraldehyde 3-phsophate to produce tagatose 1; cd00947"
                     /db_xref="CDD:238477"
     Site            order(26..28,31,51,54,56..57,61,65,68..69,142,233..234,
                     236..237,240,244,247)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238477"
     Site            order(82..83,177..179,181,208..209,211,230,232..233)
                     /site_type="active"
                     /db_xref="CDD:238477"
     Site            order(83,178,208)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238477"
     Site            order(177,179,181,209,211)
                     /site_type="other"
                     /note="Na+ binding site [ion binding]"
                     /db_xref="CDD:238477"
ORIGIN      
        1 myvsmkgilk ranegryavm aincfnleta ravidaaqel rapiiidllq dhltshlgsr
       61 fltrpiikma eeasvevain ldhgqdvaiv kqcledgfss vmmdassypy eenvaitkkm
      121 vefaetynas veaevgniga vtgdnytnqa mytdpkvaid fanqtgidal aisygsshgd
      181 ypegftpafq fdivreikaa tnmplvlhgg sgcgeenile sirlginkin vgsdfmkaqv
      241 dkiktnlket ptinyvdlis dtitagkevv qyyiqlsgst gksl
//
LOCUS       WP_010991544             327 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Listeria innocua].
ACCESSION   WP_010991544
VERSION     WP_010991544.1
KEYWORDS    RefSeq.
SOURCE      Listeria innocua
  ORGANISM  Listeria innocua
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
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
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Listeria innocua"
                     /db_xref="taxon:1642"
     Protein         1..327
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=36707
     Region          1..317
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mirfdnvskk ysddktavnn vtldikdgef fvfigpsgcg ktttlkminr liplttgtiy
       61 inekrisdyd ihelrwdigy vlqqialfph mtieeniaiv pelkkwskek ihdritelld
      121 svgldaesyr hrkpaelsgg eqqrvgvvra laadpgiilm depfsaldpi srqrlqqdis
      181 tlqkkikkti vfvthdmqea lalgdricvm qdgeivqvat pqeivknpen dfvkdflasg
      241 hafntpiles sftvndliea dlfyayqasd gtmgissner venlvrriae eqsvpvkdet
      301 gqfigtitnk hvmqflarhl essgelv
//
LOCUS       WP_010991626             162 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Listeria innocua].
ACCESSION   WP_010991626
VERSION     WP_010991626.1
KEYWORDS    RefSeq.
SOURCE      Listeria innocua
  ORGANISM  Listeria innocua
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 162)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Listeria innocua"
                     /db_xref="taxon:1642"
     Protein         1..162
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17725
     Region          8..162
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mieiqkmtgt keenyalalk qvqamiagep nlianlsnvs silnqalsdi nwvgfyllek
       61 etnqlvlgpf qglpacirip lgkgvcgsaa sdqktyiven vhdfpghiac daasnseivl
      121 pivknnqlfg vldidsplfn rfdevdqlwl ekirdaitqe in
//
LOCUS       WP_010992280             664 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Bacteroides fragilis].
ACCESSION   WP_010992280
VERSION     WP_010992280.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..664
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=75749
     Region          68..641
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 meklkmesvs iaedslnkia elfpnvvtes mgkdgqlhka idfdklkfll tanqaemgvv
       61 yddderyelt wvgkkqaire vahpirktlr pcpeesrnwe qtqnlyiegd nldamkllkk
      121 syagkvdviy idppyntgkd fifndtfals qeesdekqgr yneegqrlfq nteangkfhs
      181 dwcsmmyarl mlartllndn giifisiddh elanlikign evfnasnfid vfnwaktetp
      241 enlskkskqi ieyivcyqkk kndmkfqglk kesvssngll nqpnsvgilt fpankvvtsi
      301 pdgvikagmy gtdaydvell edttvrgglf tapvklkakf kwsqanldke iqkgttikip
      361 tlklspsyek leydpevppn linykvgvet neqagnhqlq ffdkkvfnfp kpvsliqylc
      421 efidtknkdc ivmdffsgsg ttaeavmrmn mkprknkvky ilvqlpedvt etikkaktps
      481 ekeimqnaid fltenhkaln icelskerir ragdtieaec nqrkskdlpd igfrvfriad
      541 snmkdvyysa keysqsdlfy ftdnikedrt gldllygclt nlglslslph deedingytv
      601 ysvdktelma cfaeqipekv freiagrqpr rvvfrdasfr dsadrinide ifktlspgtt
      661 ieil
//
LOCUS       WP_010993213             410 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Bacteroides fragilis].
ACCESSION   WP_010993213
VERSION     WP_010993213.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..410
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=45997
     Region          2..288
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          283..388
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mirilhtadw hlgqtffgyd rtqehehfld wlagvltknk idvlivagdv fdvsnpsaas
       61 qrmfyrfihr vttenprlql vvvagnhdsa arlesplpll qemrteikgi vhkqngkidy
      121 ehllvelkna agevealcla vpflrqgdyp vvetegnpya egvkelyarl lkyalkkrtd
      181 gqalvavghl latgseiaek dhseriiigg lesvspesfp eqivytalgh ihkaqrvsgr
      241 eniryagspl pmsfaekhyh hgvvkvtlde gwaveiekle ytplvrllsi pateaaapde
      301 vldelrglel pedepmpyle vkvklsepep mlrqqveeil egkpvrlari vsfyrqaaeg
      361 sveeetltag lqemnplqiv katfensyqa empeelvnlf qeacrtinle
//
LOCUS       WP_010994303             338 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Nostocaceae].
ACCESSION   WP_010994303
VERSION     WP_010994303.1
KEYWORDS    RefSeq.
SOURCE      Nostocaceae
  ORGANISM  Nostocaceae
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Nostocaceae"
                     /db_xref="taxon:1162"
     Protein         1..338
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37436
     Region          1..333
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mgivvenvsk qfgsfravdq vnleiqsgkl vallgpsgsg kstllrliag lekpddgrii
       61 ltgkdatnqs vqernigfvf qhyalfkhlt vrqniafgle irkapankvk grveqllelv
      121 qlsglgdryp sqlsggqrqr valaralave psvllldepf galdakvrkd lrawlrrlhd
      181 evhvttvfvt hdqeeamevs devvvmnqgr veqvgtpaei ydnpatsfvm sfigpvnvlp
      241 sssrifqssq leiehpnvfl rpqdvvieks angttapatv trlihlgwei kveltlddgq
      301 vvnahltrdr ydelqlepkq kvyvkpkdak sfplyysi
//
LOCUS       WP_010995291             735 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CHASE2 domain-containing protein [Nostocaceae].
ACCESSION   WP_010995291
VERSION     WP_010995291.1
KEYWORDS    RefSeq.
SOURCE      Nostocaceae
  ORGANISM  Nostocaceae
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales.
REFERENCE   1  (residues 1 to 735)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 735)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..735
                     /organism="Nostocaceae"
                     /db_xref="taxon:1162"
     Protein         1..735
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=80625
     Region          17..649
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 miwaklkplf wqwrgvvfav psmtilvigl rltgllqlle laaldqffll rppeppdtri
       61 viveineadv rkqtqwpmsd aamasvldti kqqqpraigl diyrdlpvnp ghetlvklfa
      121 stpnligvqk lsdtrdssav naapvlkenn qigsndlpld gdgkirrgll yvnvneedvl
      181 esfalklall ylkpekitek paasnpnylq lnhgvfpife andggyvrad arsyqillny
      241 rgriqqfttv tlnqvqqkqi padlmrgkvv ligataeslk difytpyssn lftppermag
      301 vtihanlvsq ilsaaldsrp qiqtlpetge wllilvwsii gaslcwqqrs sknqkivlav
      361 gipliggvvi agsllafvag wwipivpsll afggsaiavt lyiaqsagem rknlgryltd
      421 evlaniletp sglklggerr kvtllfsdlr gfsamseqls peqvvqilnl ylgvmtdvin
      481 qykgtinefi gdgifimfga picrpddsqr aiacaiamqr amqqvnakth qmnlpqlemg
      541 igintgevva gnigsqkraq ytvigshvnl aarietytvg gqilisentr qdantdlqia
      601 gqmqiepkgi kepitiyeis giggaynlsl pedndlmvkl qspvpveyqv lqgkqavgev
      661 frgelvsvse kkallhspht leklanlklk llhkpelata diyakvmkqs dadlfvirft
      721 nippqaiasl nslhq
//
LOCUS       WP_010996033             746 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CHASE2 domain-containing protein [Nostocaceae].
ACCESSION   WP_010996033
VERSION     WP_010996033.1
KEYWORDS    RefSeq.
SOURCE      Nostocaceae
  ORGANISM  Nostocaceae
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales.
REFERENCE   1  (residues 1 to 746)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 746)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..746
                     /organism="Nostocaceae"
                     /db_xref="taxon:1162"
     Protein         1..746
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=83308
     Region          33..691
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 miigisnklr aafikdksyr dtavnnnwwq iilvtslgvt alvwgvrelk wlqswelkay
       61 dqmlrsrpae ppdsrillvt iteedlakks wtladdtinr llaklasyqp rvialnlyrp
      121 eqknlgmgle nptniisacl sssmgrseip pppnfppeni gyndvisdie sdqvvrralv
      181 fseandskca tqfsiaalaa ityleqtgih vdfkkhqfyl dktifpiltp nsgsykgvda
      241 kgyqillnyr hpdhlaqtft ltevlnnqvn pnlvkdrlvi igttassihp glytpysaak
      301 gqptrtpsvf ihtqitsqll savldrrplm wywpdwaell wlwawslvgg ilawrlkhpl
      361 lvvlvvgial tglvvicagl flqagwipli ppaltlvmsg vsvmtyrtyr tqqqtkviml
      421 qvekqqevie qlnillneat aiadttafyd qypyhdsavi tprknaddll lggrysissv
      481 lgaggfgrty laqdtqrpgn ptcvvkklmp arkdtkflqv arrlfiteae ileslgqhqq
      541 ipallayfev neefylveqy iaghtlheel ppvaglqsea fvvemlkgvl evlafvhehr
      601 vihrdvkptn iirsaednrl vlidfgavkl mqpptdqtte latvaigtrg yappeqfagh
      661 prlasdiyav gmmgiqaltg ippqelppdp etgnvmwrsh atvseelali ldkmvryhfs
      721 dryqsattvl qdlnrlssli qtssis
//
LOCUS       WP_010997177             184 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Nostocaceae].
ACCESSION   WP_010997177
VERSION     WP_010997177.1
KEYWORDS    RefSeq.
SOURCE      Nostocaceae
  ORGANISM  Nostocaceae
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Nostocaceae"
                     /db_xref="taxon:1162"
     Protein         1..184
                     /product="TRAP transporter small permease subunit"
                     /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=20942
     Region          4..177
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mekllkisri idafterigr ytswlvlvmv ilgvwnvvgr ylgrisgnnl tsnayieaqw
       61 yifdvifflg aaytlkhneh vrvdifysnw qrrrkaiadf lgtifflipf siivifvswe
      121 tivaswqige lspdpgglpr ypikamiivg fvlliiqgis qaiknlaiiq grlepqeenh
      181 dtgl
//
LOCUS       WP_010997437             290 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Nostocaceae].
ACCESSION   WP_010997437
VERSION     WP_010997437.1
KEYWORDS    RefSeq.
SOURCE      Nostocaceae
  ORGANISM  Nostocaceae
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Nostocaceae"
                     /db_xref="taxon:1162"
     Protein         1..290
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=32313
     Region          98..279
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mnfrdwatrv tliflmlaal ilallagkst qvqqntaips nsdiatwrqy pqiqiqsein
       61 qgnkaqdign fpvitnqssg ryittqtfak ykpkleiaav hpsnygeryt qdinglpikn
      121 qpiivlhets nsassavnff qtphtdetvq asyhaiikld gtvlylvppe krafgaansv
      181 fdgtdgietv qtnpnlppsv nnfayhvsle tppdgrgnnf lkshsgytpe qynslawlia
      241 qsqvpeerit thkavdrssq rvdplsfdfd kflellntyr qispvyraqk
//
LOCUS       WP_011000062             143 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Ralstonia pseudosolanacearum].
ACCESSION   WP_011000062
VERSION     WP_011000062.1
KEYWORDS    RefSeq.
SOURCE      Ralstonia pseudosolanacearum
  ORGANISM  Ralstonia pseudosolanacearum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Ralstonia; Ralstonia
            solanacearum species complex.
REFERENCE   1  (residues 1 to 143)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Ralstonia pseudosolanacearum"
                     /db_xref="taxon:1310165"
     Protein         1..143
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /function="miscellaneous; hypothetical/global homology"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=15918
     Region          23..142
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mptptkkpst ksrpkaprtl ktikvnltsq iveafdsnnr vfrfecvsgd rdhptdrgif
       61 rvrwkaeshr sraydvqmdy alfftndgka lhqyhgvapl aliraargni sewfgshgcv
      121 rlaeadakal fawasigttv qvs
//
LOCUS       WP_011000295             665 aa            linear   BCT 20-JAN-2025
DEFINITION  sensor histidine kinase [Ralstonia pseudosolanacearum].
ACCESSION   WP_011000295
VERSION     WP_011000295.1
KEYWORDS    RefSeq.
SOURCE      Ralstonia pseudosolanacearum
  ORGANISM  Ralstonia pseudosolanacearum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Ralstonia; Ralstonia
            solanacearum species complex.
REFERENCE   1  (residues 1 to 665)
  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 665)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20493667
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Ralstonia pseudosolanacearum"
                     /db_xref="taxon:1310165"
     Protein         1..665
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /function="cell processes; transport of small molecules;
                     carbohydrates, organic acids, alcohols"
                     /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=72655
     Region          72..270
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          294..654
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mrhgterlma gaapegtasp savhhppmse pdfpfssasp rrgfgwlvaa alvavmalvc
       61 attfvvtwnr glsqaqqaag arvdryaanl kstldryeyl palvalhpfi hdllahptpd
      121 nvaranhylr evndrarata tyviaptgla laasnynlpd sfvgaeylfr pyfqqaaagh
      181 vgrfygigit reepgyyisq pvmqngsvig vtvvklnlew fgrashdase pvmvadengv
      241 iflssvpawq yrtvepltpe lqaqlqatrq yfrkqitplp lqpempaflk lvgrmpdgar
      301 lvrvgdrina pryllvsrel vepdwqlmyl tpidpvmgaa rsatvaaafa fafvclllfy
      361 wrqrrlrlre mlrgrrllea aydqlerrve drtadlmatn eqlqheivdr traeaelrat
      421 qdelvqaskl aalgqmaagi thelnqplaa lrtfsdntri llergqhgaa adnlraiadl
      481 termgkitaq lklfagrsrr rladvqvrva ldhvlallrp rlaevetalh wrlpeaacvv
      541 radelkleqv linlignald aiaandlprp grididigpa dgapaqlciv vrdngpgiaa
      601 damphlfepf fttkeigqgl glglaistsi ardfggslsa anvpgggaqf tlslvraevv
      661 paatp
//
LOCUS       WP_011000672             143 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Ralstonia pseudosolanacearum].
ACCESSION   WP_011000672
VERSION     WP_011000672.1
KEYWORDS    RefSeq.
SOURCE      Ralstonia pseudosolanacearum
  ORGANISM  Ralstonia pseudosolanacearum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Ralstonia; Ralstonia
            solanacearum species complex.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Ralstonia pseudosolanacearum"
                     /db_xref="taxon:1310165"
     Protein         1..143
                     /product="type IV pilin protein"
                     /function="structural elements; cell exterior; surface
                     structures"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15312
     Region          3..142
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mlrptgftfi ellitlaiag vlalaasqaw sgaylrterm aahaalvatm aaleqhhaqt
       61 gsyalpgddt spldrwphtl ehprgyrlsa rrcaghalih cvemaaspvr pdadcgtlil
      121 rstgerfaei agarrwapas cwp
//
LOCUS       WP_011000678             161 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Ralstonia solanacearum species
            complex].
ACCESSION   WP_011000678
VERSION     WP_011000678.1
KEYWORDS    RefSeq.
SOURCE      Ralstonia solanacearum species complex
  ORGANISM  Ralstonia solanacearum species complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Ralstonia.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Ralstonia solanacearum species complex"
                     /db_xref="taxon:3116862"
     Protein         1..161
                     /product="type IV pilin protein"
                     /function="structural elements; cell exterior; surface
                     structures"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=17515
     Region          5..161
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mrthrspplp hqrgftliel mivvivvail stiaypsytq fvqksrrtqa kaalmenmql
       61 ferhfaqant yaasstdlth awngfrtysg daqtstsyqi savgcsgsan vdqcvelqaq
      121 ppnngkddpt cgtlvyrstg eklnillgks vpesptttgc w
//
LOCUS       WP_011002506             296 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Ralstonia
            solanacearum species complex].
ACCESSION   WP_011002506
VERSION     WP_011002506.1
KEYWORDS    RefSeq.
SOURCE      Ralstonia solanacearum species complex
  ORGANISM  Ralstonia solanacearum species complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Ralstonia.
REFERENCE   1  (residues 1 to 296)
  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 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 296)
  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   4  (residues 1 to 296)
  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 296)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Ralstonia solanacearum species complex"
                     /db_xref="taxon:3116862"
     Protein         1..296
                     /product="AraC family transcriptional regulator"
                     /function="miscellaneous; not classified regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32709
     Region          22..171
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          199..280
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 minldqiram amrhagrkhp qlprlftytl nhttevdpli ydpaaslvvq gtqrmfigek
       61 mfeygpgqsm vvaaeiaalg qvceaseekp fiavglfldq aqlsdlvlem aalpelpiea
      121 gygvstasas llgawgrllg lldrpneipv maqsleheim frllmgphgg llrqiagads
      181 rlmhirrama wirdhyterl dfkavaalag msvsvfydrf kavaavsplq yqkyirlhea
      241 rrrmianqtt aaeasyvvgy esasqfsrey krlfgappgq dtekarlslg qnsrsi
//
LOCUS       WP_011004838             380 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Ralstonia pseudosolanacearum].
ACCESSION   WP_011004838
VERSION     WP_011004838.1
KEYWORDS    RefSeq.
SOURCE      Ralstonia pseudosolanacearum
  ORGANISM  Ralstonia pseudosolanacearum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Ralstonia; Ralstonia
            solanacearum species complex.
REFERENCE   1  (residues 1 to 380)
  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 380)
  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   3  (residues 1 to 380)
  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   4  (residues 1 to 380)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 380)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 380)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Ralstonia pseudosolanacearum"
                     /db_xref="taxon:1310165"
     Protein         1..380
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /function="cell processes; transport of small molecules;
                     amino acids, amines"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39936
     Region          33..369
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(109..111,132,181,233,257)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mrfrckqsml qvvfivaaav pavgwaqaeq tvrignagpl tggaahwgkd nengarlave
       61 dlnrkglvig gkkvrfells eddqadprqa mvvanklvds gvkamlghfn sgaaipasai
      121 yaragipdis vatnpqltqq gfrntfriia sdddvgaals rfavttlnak kvaiiddrta
      181 ygqgaaevfe kgvkglgasv vsqqftsdka tdfmailtsi krtrpdvify ggmdaqggli
      241 arqmkqlgig akllgtdglc tgavakisag avngtlyctr ggkaldmmpn gsdfarryka
      301 rfgtevlnya pylydslmvi aaamqaadsv epprylpala kisldgttgp vafdekgnlk
      361 tpgftvftyq dgkavrvags
//
LOCUS       WP_011013729             249 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Corynebacterium glutamicum].
ACCESSION   WP_011013729
VERSION     WP_011013729.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium glutamicum
  ORGANISM  Corynebacterium glutamicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 249)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Corynebacterium glutamicum"
                     /db_xref="taxon:1718"
     Protein         1..249
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=26165
     Region          143..249
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 maknsrirys asikraaaai ltaaatsval iavpatasaq dlatgssqiq tdaregawat
       61 rntiqdqlas igpaalpvra avdnaingmf pglvdekvaa eqeaaraeae reaaaareae
      121 aarvaaeeaa rfdrgscpai advcvdidgg rtwlqengqv tygavpvssg gvgqetprgt
      181 fyinrkvkde isyefgnapm pyamyftyng hafhqgnvat tsagcvrlnt qdaiyyfnnv
      241 gigdmvyiy
//
LOCUS       WP_011015147             250 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Corynebacterium
            glutamicum].
ACCESSION   WP_011015147
VERSION     WP_011015147.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium glutamicum
  ORGANISM  Corynebacterium glutamicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 250)
  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 250)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Corynebacterium glutamicum"
                     /db_xref="taxon:1718"
     Protein         1..250
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27625
     Region          1..249
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 msrfaanlsl tfteldfldr fdaaskhafs avefqypydf dvqeikqrad saglpielfn
       61 appgdtfgla alaspedfqq sieqaityat vlkpkkmhvm agiadvtset taryvenirw
      121 aaqqldkldv vvviepinhy svpgyflhtl eqaywlidsi ahpnvkilfd tfhlqqihgn
      181 ltrrlrevhg agllghvqva svpdrhepgt gevnaayifq llselgydgv iageyhpage
      241 ttaglgwlel
//
LOCUS       WP_011015892             192 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Fusobacterium nucleatum].
ACCESSION   WP_011015892
VERSION     WP_011015892.1
KEYWORDS    RefSeq.
SOURCE      Fusobacterium nucleatum
  ORGANISM  Fusobacterium nucleatum
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Fusobacteriaceae; Fusobacterium.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Fusobacterium nucleatum"
                     /db_xref="taxon:851"
     Protein         1..192
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21551
     Region          2..151
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 miienikhar shrrftekki neeeilemle garfsastkn aqilrysyti ddenckklfs
       61 avslggllkn edkatleera rgfilisakk dittpdsrly fdvgiasqni iliadelgyg
      121 acivisynkk afeeilglpe eydskaviil geskdivklv dskdeedtky fvengihhvp
      181 klklgdlilg kk
//
LOCUS       WP_011018172             587 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Streptococcus
            pyogenes].
ACCESSION   WP_011018172
VERSION     WP_011018172.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus pyogenes
  ORGANISM  Streptococcus pyogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 587)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Streptococcus pyogenes"
                     /db_xref="taxon:1314"
     Protein         1..587
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=65741
     Region          24..569
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mmetedtisr gkrkrllkrl reriapkryl lyvsaflswl qfvmrmisfy liaktfstfi
       61 lghaialgrl aglllllnvv gfvlailgkq lqgiasqfar dslkqsffea fidldgqfda
      121 hasdadiltl asqgidsldt yygyylslsm rtkwncttim ilvfliypla glvflgvlpl
      181 iplsivamqk rskqimshyw ssymdvgnlf mddlkglntl ysyqaterye qefsgkaeqf
      241 rkatmsllgf qlqavgymda vmylgiglsg flavqalatg qlsffnflff lliatefftp
      301 ireqgygmhl vmmntkmadr ifsfldsvpa rkdnksktai nfnqidiqni slayekktvl
      361 sgvtmtltkg qltaiagvsg qgktslaqll lkrqsattgh ilfdgldsdn lsqetinqqv
      421 lyvsdqstll nrsiydnlrl aanlskkeil dwidqhglls finwlpdgld tivgengnll
      481 spgqkqqvic arallskrsl yifdeatssl daeneriidn litrlaktai vivithkmsr
      541 lkganqvlfl ntgqpaclgk pcdlyrdqpt yrhlvdtqar leasiyg
//
LOCUS       WP_011026217             179 aa            linear   BCT 20-JAN-2025
DEFINITION  transcription termination/antitermination protein NusG
            [Caldanaerobacter subterraneus].
ACCESSION   WP_011026217
VERSION     WP_011026217.1
KEYWORDS    RefSeq.
SOURCE      Caldanaerobacter subterraneus
  ORGANISM  Caldanaerobacter subterraneus
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Caldanaerobacter.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Kang,J.Y., Mooney,R.A., Nedialkov,Y., Saba,J., Mishanina,T.V.,
            Artsimovitch,I., Landick,R. and Darst,S.A.
  TITLE     Structural Basis for Transcript Elongation Control by NusG Family
            Universal Regulators
  JOURNAL   Cell 173 (7), 1650-1662 (2018)
   PUBMED   29887376
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Liu,B. and Steitz,T.A.
  TITLE     Structural insights into NusG regulating transcription elongation
  JOURNAL   Nucleic Acids Res 45 (2), 968-974 (2017)
   PUBMED   27899640
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Steiner,T., Kaiser,J.T., Marinkovic,S., Huber,R. and Wahl,M.C.
  TITLE     Crystal structures of transcription factor NusG in light of its
            nucleic acid- and protein-binding activities
  JOURNAL   EMBO J 21 (17), 4641-4653 (2002)
   PUBMED   12198166
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415705
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Caldanaerobacter subterraneus"
                     /db_xref="taxon:911092"
     gene            1..179
                     /gene="nusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
     Protein         1..179
                     /product="transcription termination/antitermination
                     protein NusG"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0006354 - DNA-templated transcription
                     elongation [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /GO_process="GO:0032784 - regulation of DNA-templated
                     transcription elongation [Evidence IEA]"
                     /calculated_mol_wt=20304
     Region          16..178
                     /region_name="NusG"
                     /note="Transcription termination/antitermination protein
                     NusG [Transcription]; COG0250"
                     /db_xref="CDD:440020"
ORIGIN      
        1 msevqeltkt kekplwyvvf tyhnaekrve ehinslakte kydgliikae vpvqkrtvsr
       61 rgkikeieek ifpgyvfvka vmtpevmaai rringvahfv gggnepvpit peevkrariq
      121 ddlseefkag dtvmitdgpf enfigkiiki egrkinials lfdremgidf speqimkiq
//
LOCUS       WP_011028354             286 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Streptomyces].
ACCESSION   WP_011028354
VERSION     WP_011028354.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            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="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30153
     Region          18..256
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mkrtgtafev avheeatlge gptwdpatgr llwldilnsr vhthdpatgr rtvrrtdqhv
       61 gavkpraggg lvlnlrdgig lldpddtfrw lhrepvpgrr gndaavapdg slwagtmryd
      121 eargggtltr ctgdgtaetv lddvtvsngt gwspdgtlmy yadtptrrid vfdvtadgrv
      181 agrrplaaie dgagfpdglc vdadgcvwva lwdggavrry tpsgeldrvi tlpvprvtac
      241 afggpdltdl ylttarvglp dphplagsll vvpdagrgva qpafag
//
LOCUS       WP_011028371             819 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: molybdopterin oxidoreductase family protein
            [Streptomyces].
ACCESSION   WP_011028371
VERSION     WP_011028371.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 819)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 819)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 819)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..819
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=85632
     Region          11..815
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mqntgtrtpa ttpthcpyca lqcgmnltpv eggtvevser tdfpvnrgal cgkgrtaaav
       61 lapgarltsp lvrsgdgalv pagwdealdr iagnlertra rygadalgvf ggggltneka
      121 yalgkfarvv lgtsqidyng rfcmssaaaa gtrafgldrg lpfpledvpr tgcvilvgsn
      181 paetmppslr yftelrengg tlivvdprrt ktaeqadlhl aprpgtdlal algmlhlvva
      241 egrvdeayve ertsgweear aaamahwpey veritgvsvp elreavrlfc apeaamvlta
      301 rgpeqqakgt dtvgawinlc latgragrpl sgygcltgqg ngqggrehgq kadqlpgyrk
      361 ltdpaarrhv aevwgvdpda lpgpgrsaye lldalgtdvr sllvmgsnpv vsapraahve
      421 grlrsldfla vcdvvlseta eladvvlpvt qwaeetgttt slegrvllrr raitppdgvr
      481 gdlevlhgla grlgvqkgfp tdpeevfeel rrasaggpad ysgidyrrla eengvfwpcp
      541 aqpaaddtht adpgtgtdtr trtgtgsgsg sgsgrdmste tgtgsgmytd tgtasgmstd
      601 tgsgstdagi grdpraatgt gsgmstdtgr vtrtatgtgs gmstdtgsds dsdssdagag
      661 lraaphpgtp rlfldrfatd dgrarfapvt hrpsaeepdd eypvllttgr vvsqyqsgaq
      721 trrvaelnaa apgpfvelhp rlaarlgaad gdplavvsrr gravaparit tgirpdtvfm
      781 pfhwpgegra ntltnpaldp tsrmpefkvc avrvetvts
//
LOCUS       WP_011029915             281 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase family protein [Streptomyces].
ACCESSION   WP_011029915
VERSION     WP_011029915.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 281)
  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 12830887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..281
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=30329
     Region          76..138
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          169..280
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mrmtgmgstg rvvavalgav lvaggctvqg tgpdgrgrap vrievtghpp kstpapdrhr
       61 pssappaapa aarvlwkrgd tgrdvrelqa rlrqvewlvd gptgtyddlt eravsgfqgk
      121 rglprtgrtd tvtwqrllgm shepgkwdly lmggqpaaap dprctsgrvl cvskssrtlr
      181 wmidgrtvst msvrfgsqyt ptregvfqvy wksrhhvstl ydsampyamf fsggqavhys
      241 ydfaargyag ashgcvnvrd eaaiadlyaq vktgdkvvvy q
//
LOCUS       WP_011030250             549 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: M4 family metallopeptidase [Streptomyces].
ACCESSION   WP_011030250
VERSION     WP_011030250.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 549)
  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 549)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..549
                     /product="M4 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=56899
     Region          47..548
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 msslfachkr ttlalatava agamlttglt agnaaadsaa psalpgapvl lsgsarsali
       61 qeqqagaagt aremglgake klvvkdvvkd rdgsvhtrye rtydglpvlg gdlvvhrses
      121 gatrgvtkat eaavkvatvt pkvkaakaeq qalsaakdag ssktaadsap rkviwaaqgk
      181 pvlayetvvg glqddgtpne lhvitdadtg aklyeyqgie tgsgkslysg tvelgttrsg
      241 ssyqlydtgr gghktynlar ktsgtgtlft daddtwgtga assdpqdqta avdaaygaqv
      301 twdfykesfg rsgikndgka aysrvhygsn yvnafwsdsc fcmtygdgtg ntnpltsldv
      361 aghemshgvt sntaglnysg esgglneats difgtgveyf anssadkgdy ligeriding
      421 dgtplrymde pskdgaskdy wdsglggvdv hyssgpanhf ffllsegsga rtvdgvdyds
      481 ptsdgstvtg igrdkalqiw ykalteymts ttdyadarta tlsaasdlyg adsteyktvg
      541 aswtainvs
//
LOCUS       WP_011031541             639 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Streptomyces].
ACCESSION   WP_011031541
VERSION     WP_011031541.1
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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..639
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=67919
     Region          253..422
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mpalataall lpllgaapsa aaptaappap drlqrafata aaeyhvpqsv llgvsylqsr
       61 wdahggapsv tggygplhlt dartalagas hhgggsedpr gddaraalhp aggattpsdd
      121 lparlttlpr aaeltgmspe alrtdpaanv aggaallaaa qrdlgeplsa dpadwyaava
      181 rfsgaedsat aaayaddvye virtgerrtt dagqrvslaa rpgvapdvsr ldgaglraas
      241 aagtecprsv scewvpapye efgdgdygnh dlgtrpasqr iryivvhdte gtwngvlnmv
      301 qdptyvswny tlrstdghia qhvkakdvaw hagnwyvnak siglehegfl aepdawytea
      361 myrssarlvk ylakkydipl drqhvlghdn vpgtttatip gmhtdpgpyw dwrhyfqllg
      421 rpiqptagkk sslvtirpdy danrpgytgc etagepcaph gssevrlysd hdvnaplird
      481 vglgttpttg vndlssrvst gqqyavadrw gdwtaiwylg qkawfhnpgk spaavpasgr
      541 vitprkglan vpvygraype kaaypagvpa qavsplpytl pagqkyvvge kvpgeyyyav
      601 tfdeashrvv tgkdqyyeiq yghrvayvra advtvsaar
//
LOCUS       WP_011036157             343 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Xanthomonas].
ACCESSION   WP_011036157
VERSION     WP_011036157.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..343
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=37630
     Region          1..343
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mgirishlrk qfasftaldd itldvrqgel lallgpsgsg kttllrimag lehadggqvl
       61 fgdedatrms vqsrrvgfvf qhyalfkhmd vfeniafglr vrrgkerwae arirarveel
      121 lalvqlqgle qryptqlsgg qrqrvalara laieprvlll depfgaldaq vrrdlrrwlr
      181 elheqtgltt vfvthdqeea leladrvail nrgrieqldt parvydtpas pfvysfvgav
      241 nripgvlahg qiqvaghalp sanpalaagp vevyvrpedl vpdadgwpat vawaqrsgar
      301 lrvraildaa gnevevelpa sagtitagqq lrlaarhygv fpa
//
LOCUS       WP_011036507             351 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Xanthomonas campestris].
ACCESSION   WP_011036507
VERSION     WP_011036507.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas campestris
  ORGANISM  Xanthomonas campestris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 351)
  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 11482063
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Xanthomonas campestris"
                     /db_xref="taxon:339"
     Protein         1..351
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=36863
     Region          1..344
                     /region_name="PRK06132"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:235709"
ORIGIN      
        1 mpmrrllpal llcallfcdq aaavpfwgar qsspaetppd qlkpgewiwg gvskgwgpma
       61 vivslteqra yayrngilig vstissgkpg hetptgvfti lqkdkdhrss iynaapmpyq
      121 qrltwdgval hagglpgype shgcvhlpse farllfdnsn mgmvvvvaqa gvdadavvhp
      181 ralspidpst gaqrpllplp sgqtyawqpe laptgpisml vsssdqqlav yrngveigra
      241 ravlhapada aplgtqafiv gqgflpgevp glpgvrmpnw mrigipgsaa aagqaldant
      301 iarlqvppaf lanllplltp gvvlvatdqh ilpettggkl qvldsdppea p
//
LOCUS       WP_011039009             261 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SPOR domain-containing protein [Xanthomonas].
ACCESSION   WP_011039009
VERSION     WP_011039009.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..261
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26303
     Region          152..217
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 myvralivvl iilnagvalw walqpaavpp aapsqpagva rlellptppt aaapavatva
       61 paaapvpppa apaaqpavaa vdntppptpa ataavtpaav aaspppavaa paerctslgp
      121 yaaraeadaa lpalrgqasr tsvredkdag vstfrvmlpn vgdraaaqal vkriaaagig
      181 dyyviaqged nsialgqyqs reraerrqas lvsagfpaql vpsgtgqsrw widvrssasv
      241 sslqrsagas rqrsldctal r
//
LOCUS       WP_011041396             672 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Colwellia psychrerythraea].
ACCESSION   WP_011041396
VERSION     WP_011041396.1
KEYWORDS    RefSeq.
SOURCE      Colwellia psychrerythraea
  ORGANISM  Colwellia psychrerythraea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Colwelliaceae; Colwellia.
REFERENCE   1  (residues 1 to 672)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Colwellia psychrerythraea"
                     /db_xref="taxon:28229"
     Protein         1..672
                     /product="amidohydrolase family protein"
                     /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=74033
     Region          239..654
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mnwsllrlll alssmvsalv fanntsitnl vysekglagk qimtkvsdtq yhgsldlrwn
       61 nrvfkvdeki klnekgqvls festglspfg aaiaesfkwq dgiaswesnk edgrvkstge
      121 rfylpvnsav vaenlmvqam lknignsiel lpsgtarlte lktvklsaes gseqvtlyai
      181 sglgftpdfs wydsqgnffa kdhsgfmkvi regftlddfd klkviqnsae qeylegvssk
      241 lshsyttlli knaqvvdvin svvlkntdvl fkngkvshva kninvpentp tidgsgktli
      301 pglwdmhghl skgdgllnia agvtnvrdvg nshdnimtie rlfntnqvig nrvfragffd
      361 qmsefsagls vkslaeahek idwfadngyi qiklyssidp twvesiakha hsrglrlsgh
      421 ipafmtaeqa vkagydeiqh inmlflnfla gtevdtrqql rftligekag dvdinskefn
      481 dfiqlladnq tvidptistf rslllkerkk idpeflavae hlppnvlrql kgaemnvsdd
      541 lkdnyqagad amsalvkkly dkgvpivpgt dniagftlqr elelyadagi pemdvlkias
      601 insarlvgaa hylgsitegk sadvllidgd pltdmsvlrk tslvikdnhf ykpeelykil
      661 gvkpftpssh lq
//
LOCUS       WP_011041915             192 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Colwellia].
ACCESSION   WP_011041915
VERSION     WP_011041915.1
KEYWORDS    RefSeq.
SOURCE      Colwellia
  ORGANISM  Colwellia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Colwelliaceae.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Colwellia"
                     /db_xref="taxon:28228"
     Protein         1..192
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21588
     Region          3..165
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mkvfsslyqw tlrwaehqfa prflvaltfa esiffpippd vllapmvlak pqkawyfagi
       61 ttiasilggs vgywlgylmf epwiqplisn fgyqarfdia igwfnewgvw vvfiagfspi
      121 pyklftvsag flhmaflpff iasaigrglr fflvaglikw ggsameqkik qwvdvlgwgi
      181 vgaivvgyfv lr
//
LOCUS       WP_011042101             354 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [Colwellia].
ACCESSION   WP_011042101
VERSION     WP_011042101.1
KEYWORDS    RefSeq.
SOURCE      Colwellia
  ORGANISM  Colwellia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Colwelliaceae.
REFERENCE   1  (residues 1 to 354)
  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 354)
  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 354)
  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 354)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Colwellia"
                     /db_xref="taxon:28228"
     Protein         1..354
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39280
     Region          1..345
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkkfplllls tliagsfsga vmaekkmllk tpiyynsvlp slgstikyvs dniqtlsgnt
       61 lkmkiyepnk lvnpkeilda vstgkvqagy atagnwggki paarlfsavp fgpeapeyla
      121 wfyhgngnkl hqelyddnnl nvkvqvcgvl apetsgwfkn einkpedlag lkmrffglga
      181 lvmeklgvst vglpggeifp aiekgvidat efsmpvvdqr igvkkllnyn yfpgwhqqat
      241 mmeliinkdt wkkmserqqs viehlcksat leaialgeai qapvmkqnie dgvinkywsp
      301 emlstfktkw devvieqsaa dpafkkihdd lakfrktydl wesnaflprp kpsl
//
LOCUS       WP_011042960             112 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Colwellia psychrerythraea].
ACCESSION   WP_011042960
VERSION     WP_011042960.1
KEYWORDS    RefSeq.
SOURCE      Colwellia psychrerythraea
  ORGANISM  Colwellia psychrerythraea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Colwelliaceae; Colwellia.
REFERENCE   1  (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   2  (residues 1 to 112)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Colwellia psychrerythraea"
                     /db_xref="taxon:28229"
     Protein         1..112
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11829
     Region          43..111
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mniqpkhlnk tlsvltlgii llvnsslgla ketnvtqaaq gqsaqsvksq vvnlnkstfe
       61 qlvtlkgvgn tkaqaiivyr qqvgafksvn eltkvsgige kivsdnkarl si
//
LOCUS       WP_011043369             344 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Colwellia].
ACCESSION   WP_011043369
VERSION     WP_011043369.1
KEYWORDS    RefSeq.
SOURCE      Colwellia
  ORGANISM  Colwellia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Colwelliaceae.
REFERENCE   1  (residues 1 to 344)
  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 344)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 344)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 344)
  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   5  (residues 1 to 344)
  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   6  (residues 1 to 344)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Colwellia"
                     /db_xref="taxon:28228"
     Protein         1..344
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38305
     Region          22..209
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <256..339
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msqttlstip rligqvlsiy dvapeaifsa aniditsdaq trvpmenmat lwklaveath
       61 nnelglvaas lfqpvylksi glawlasenl eeglkryias sqlintemqi elterdgidg
      121 eetliqyqrr ltssntikvh pcaielgigf flkmfrlaag knipatgvyf tfaieennkv
      181 yeeyfqcpvy gnqavngiaf skalltetlp thdvelvemn evvinkhlds mdngetsskv
      241 ikmindllpl gcpteeviay klhmskrtlq rklsvekqsf lalltsvrlm lakeklankr
      301 vsvteityql gysspstfar afkkhtqlsp leyrnqvssy sscs
//
LOCUS       WP_011043619             158 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Colwellia psychrerythraea].
ACCESSION   WP_011043619
VERSION     WP_011043619.1
KEYWORDS    RefSeq.
SOURCE      Colwellia psychrerythraea
  ORGANISM  Colwellia psychrerythraea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Colwelliaceae; Colwellia.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 158)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Colwellia psychrerythraea"
                     /db_xref="taxon:28229"
     Protein         1..158
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17074
     Region          2..154
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 msnqaefyhe llgqtkalin desdiianma nisallferl advnwvgfyr lidgelvlgp
       61 fqgkvaciri pvgkgvcgtc sftgevqris dvhqfdghia cdassnaelv vpvkiagkvi
      121 aildidstvf drfnledeqg ivsivqafeq nitamdna
//
LOCUS       WP_011044735             353 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Colwellia psychrerythraea].
ACCESSION   WP_011044735
VERSION     WP_011044735.1
KEYWORDS    RefSeq.
SOURCE      Colwellia psychrerythraea
  ORGANISM  Colwellia psychrerythraea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Colwelliaceae; Colwellia.
REFERENCE   1  (residues 1 to 353)
  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 353)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 353)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 353)
  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   5  (residues 1 to 353)
  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   6  (residues 1 to 353)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Colwellia psychrerythraea"
                     /db_xref="taxon:28229"
     Protein         1..353
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40167
     Region          <82..190
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <272..350
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkgyerydev ldaqqvllsl idlatqrgah pdkllkgtkl fhndlskknl aknsltcsan
       61 tlltviencs klvqgneisf llgrryfpsh lgllgqalmn crhlgdmlrl cqcfqlacfp
      121 lmnlqlkhfn nnsylifqsa vgklsknqqt fitefmlsal lgaikyrcge lpkldihldy
      181 pevqhieqyh vhlnmkanin iqfdqkicmv tiaskqlylp fndsanslka valqqisqln
      241 pkpypisfiq qlnsylsqrl snkgdlsqec caqhfgyssa tlkrklanhq lnyqglidai
      301 rsqqaifqlv icqhsnekia dalyfndvsn frkafkrwtg vtpnsmreqh cfn
//
LOCUS       WP_011046088             279 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Ruegeria pomeroyi].
ACCESSION   WP_011046088
VERSION     WP_011046088.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria pomeroyi (Silicibacter pomeroyi)
  ORGANISM  Ruegeria pomeroyi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 279)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Ruegeria pomeroyi"
                     /db_xref="taxon:89184"
     Protein         1..279
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=30864
     Region          36..263
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mrtrikklad lpegaenpls aaissrhrst vamateavrh gdcllayqpv lqtapphgia
       61 fyegfirvld etgrvipard fmpaventei greldcvale tglralvrnp tlrlsvnmsa
      121 rsigyrkwmq tlerflkrde algdrlilei nqtsamavpe lvidfmdrlq prgiafaldd
      181 fgdgpidfns frdfffdavk idgrfirqvs tdaanratvr alialarefe mliiaesvet
      241 eedaaflaen gvdclqgyly gaptvtpvwe kpetakasg
//
LOCUS       WP_011046227             259 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Ruegeria pomeroyi].
ACCESSION   WP_011046227
VERSION     WP_011046227.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria pomeroyi (Silicibacter pomeroyi)
  ORGANISM  Ruegeria pomeroyi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Ruegeria pomeroyi"
                     /db_xref="taxon:89184"
     Protein         1..259
                     /product="formate/nitrite transporter family protein"
                     /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=26116
     Region          10..259
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msdanptgld aykpaeiarl vetagvakag lgaaqtltla vlagafigfg gaaytmvmtg
       61 adtgfgparf lggvvfslgl ilvivggael ftgnalmvma avdrritlaa llrnwglvyl
      121 gnllgavgla lafaltglld glmgdtaqai argkaaldpg aafmrgvlcn amvclavwlt
      181 faartaagki lailwpisaf vllglehsva nmylipqgml agaevtpgaa lanlfwvtlg
      241 nilggaggva layrfaylr
//
LOCUS       WP_011047804             822 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Ruegeria pomeroyi].
ACCESSION   WP_011047804
VERSION     WP_011047804.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria pomeroyi (Silicibacter pomeroyi)
  ORGANISM  Ruegeria pomeroyi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 822)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 822)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 822)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..822
                     /organism="Ruegeria pomeroyi"
                     /db_xref="taxon:89184"
     Protein         1..822
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=89956
     Region          9..821
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mgllfrwllr laaglialav aavalvyyla sqslpdydqt qevagltapv eivrdthnvp
       61 hifgasdpdv ffglgyahaq drlwqmtmlr rtvqgrlsev fgprtvaidr llrrldlarl
      121 aqqsvsaqda yttaalkaya agvnarlaei ndealgrgap emflfnapva pwqpadslai
      181 iklmglqlsg hleeevlrar tslmlgdpar lvdilpdapg tgtaalpeya qlfpglprya
      241 agrdtphdpl mplprrglag asnawaaaps rsasggtlla ndphlgfaap stwylarlel
      301 anggviggti pgmpavllgr serlgwglts symddqdlfv erlnpdnpee yltpdgyktf
      361 esrpsiieik gaapitltlr wtengpvlpg svydletitp pghvmslgwt mldardtsms
      421 aalalinagt vqeairasea yvgpsqnltl adretvalkm vgavprrdpr hqsqgrlpaq
      481 gwraenrwqg rmpyasnpef vspvggilgn tnnkllerpf pnhvsfvwgd tqrvtrwqkl
      541 mqsrevhtrd gfieaqldpv spaartllpl igadlwftge aapegtperq rqialsllae
      601 wngemsehlp epliyaawvr alqkrlitde lgpladeykq veplfiervf rdidgasvwc
      661 dirqsapret cteiarlald dalvwigdry gsaleslrwg dahqathdhp vlgevpvlry
      721 fvnirqstsg gdhtlqrgrt sgedpdpfrn vhgagyrgvy dfadpdssvf vistgqsghf
      781 lsryyddqaq lwrrgeyipm sldadlaraa avgvtrllpa pe
//
LOCUS       WP_011047840             192 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Ruegeria pomeroyi].
ACCESSION   WP_011047840
VERSION     WP_011047840.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria pomeroyi (Silicibacter pomeroyi)
  ORGANISM  Ruegeria pomeroyi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Ruegeria pomeroyi"
                     /db_xref="taxon:89184"
     Protein         1..192
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=20991
     Region          1..163
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mltslyhrtm aladhrhalw alalvafles svfpippdll mipmilarps rawlialval
       61 vasvlggllg yaigaffyds igapileamg kgdameafnt rfndfgfwav ltagvtpfpy
      121 kvitimsgwt gmplatfvat silaralrff lvaallwkfg apvrdfierr lglvmtvfma
      181 lliggfflvr yl
//
LOCUS       WP_011048139             497 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Ruegeria pomeroyi].
ACCESSION   WP_011048139
VERSION     WP_011048139.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria pomeroyi (Silicibacter pomeroyi)
  ORGANISM  Ruegeria pomeroyi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Ruegeria pomeroyi"
                     /db_xref="taxon:89184"
     Protein         1..497
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=52404
     Region          1..497
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mrtvrlsdad nvvtaiaqla pgedgaaeli prghkmaara iargeavlky aqvigyaagd
       61 igpgahvhth nlefrnveae yefstnlrpv apvatldsfm gyvrpsgrvg trnyiavlts
      121 vncsataarm iaghftpdrl aaypnvdgvv afvhgtgcgm agqgsegfea lqrvmwgyar
      181 npniggvlma glgcemmqid wlieayglsp gplfqamniq dmgglrktvd kgiekietml
      241 plvnqarrtp cpaselmval qcggsdawsg vtanpavgha cdllvaqggt gvlaetpeiy
      301 gaehlltara adratgdklv dlirwwedyt arnkgsmdnn pspgnkkggl ttilekslga
      361 vakggttpln gvyryaepvt argftfmdsp gydpasvtgq iasgctlvvf ttgrgsafgs
      421 kpsptikvat nsemytrmsg dmdvdagril sggatveqvg reiyemwlrv asgeqsksea
      481 qglgdfefvp wqigavm
//
LOCUS       WP_011049363             404 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Ruegeria
            pomeroyi].
ACCESSION   WP_011049363
VERSION     WP_011049363.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria pomeroyi (Silicibacter pomeroyi)
  ORGANISM  Ruegeria pomeroyi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 404)
  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 404)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Ruegeria pomeroyi"
                     /db_xref="taxon:89184"
     Protein         1..404
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46310
     Region          1..398
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 malqrldnra aralfldrhg laeqpsgpar gvallelitr lgfvqldsin tvarahdlil
       61 fsrrpsyrpp dlkrlyeqdr alfehwthda avipmafyph whmrfqrdae mlrarwknwr
      121 rdgfegkfaa vldhirdhgp vgssdvgkde ektsggwwdw hpsktaleyl wrsgaltvig
      181 rdgfqkrydl terviedhlr pgaldhdpea tvdwlcnaal drlgfattge laafwdsssp
      241 aetrnwaaga eargevetie itcadgslrk vlarpdvldq aiavppapgr irvlspfdpa
      301 lrdrkraerl fgfhyrievf vpepkrvygy yvfpllegdr ligridmkah rdcgelrvra
      361 lwperglrws partrrleae ldrirrlagv eqvilakdwl rdpl
//
LOCUS       WP_011050327             109 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: endonuclease domain-containing protein [Xanthomonas].
ACCESSION   WP_011050327
VERSION     WP_011050327.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 109)
  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 109)
  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   3  (residues 1 to 109)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..109
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=12325
     Region          1..89
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mtdaeravwr clrskqlhgl kfrrqhpipp yiadfccier rliieldgsq hdassdqars
       61 qwlqsqgwtv lrfwnndvll sldavvetic kmvatpyphp npspggrga
//
LOCUS       WP_011050758             248 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Xanthomonas].
ACCESSION   WP_011050758
VERSION     WP_011050758.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 248)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..248
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=27189
     Region          20..237
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mttlpvcnac rdgqdfptai tmafqpivdv strsiyagea lvrgidgesa gsilaavder
       61 nryafdqacr ikaiecaaqi alpallsinf mpnavynpeh clratlsata qygwplnaii
      121 fevseqehlt dpahllgilr tyqargmkta iddfgagyag lgllaefqpd llkldialvr
      181 gidtdrsrqa ivrhvtrmce eldiaviaeg ieqpdqyral rdlgihlqqg ylfarpqige
      241 lpkvhwpe
//
LOCUS       WP_011051283             212 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Xanthomonas].
ACCESSION   WP_011051283
VERSION     WP_011051283.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 212)
  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 212)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 212)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..212
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22856
     Region          1..200
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Region          93..119
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(95..96,99..100,102,126,129..130,133..134,136..137,
                     155,158..159,162..163,166)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          124..151
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          154..181
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 maiddlldeh eqgervrswl rkngaglvgg vllglalilg wqwwqtrtnt alveangrye
       61 avvksiqakd ldkaakdiva lddgkggiya elaalrlaka qvdagkndea iktlrdvpae
      121 gelkqivqqr larlltesgk pdeaikllad aqdhasleir adalvvqgkp dearalyaka
      181 lttvdvaspq rrlletklmd vggkvpdpae qi
//
LOCUS       WP_011055147             109 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Synechococcus elongatus].
ACCESSION   WP_011055147
VERSION     WP_011055147.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus elongatus
  ORGANISM  Synechococcus elongatus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Synechococcus elongatus"
                     /db_xref="taxon:32046"
     Protein         1..109
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12127
     Region          1..101
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mnrqtlqqlp ppllafcqkw kvselslfgs ilrddfrpds dvdvlvsfep kapwtildlv
       61 lmeselaglv krpadliekr aieeslnpir kaeilstavs iyppraeaa
//
LOCUS       WP_011055983             920 aa            linear   BCT 20-JAN-2025
DEFINITION  AAA family ATPase [Thermosynechococcus vestitus].
ACCESSION   WP_011055983
VERSION     WP_011055983.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus vestitus
  ORGANISM  Thermosynechococcus vestitus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
REFERENCE   1  (residues 1 to 920)
  AUTHORS   Liu,Y., Sung,S., Kim,Y., Li,F., Gwon,G., Jo,A., Kim,A.K., Kim,T.,
            Song,O.K., Lee,S.E. and Cho,Y.
  TITLE     ATP-dependent DNA binding, unwinding, and resection by the
            Mre11/Rad50 complex
  JOURNAL   EMBO J 35 (7), 743-758 (2016)
   PUBMED   26717941
REFERENCE   2  (residues 1 to 920)
  AUTHORS   Chen,Z., Luong,T.T. and Lee,C.Y.
  TITLE     The sbcDC locus mediates repression of type 5 capsule production as
            part of the SOS response in Staphylococcus aureus
  JOURNAL   J Bacteriol 189 (20), 7343-7350 (2007)
   PUBMED   17704228
REFERENCE   3  (residues 1 to 920)
  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   4  (residues 1 to 920)
  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
REFERENCE   5  (residues 1 to 920)
  AUTHORS   Hopfner,K.P., Karcher,A., Craig,L., Woo,T.T., Carney,J.P. and
            Tainer,J.A.
  TITLE     Structural biochemistry and interaction architecture of the DNA
            double-strand break repair Mre11 nuclease and Rad50-ATPase
  JOURNAL   Cell 105 (4), 473-485 (2001)
   PUBMED   11371344
REFERENCE   6  (residues 1 to 920)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..920
                     /organism="Thermosynechococcus vestitus"
                     /db_xref="taxon:146786"
     Protein         1..920
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=104145
     Region          1..916
                     /region_name="PRK03918"
                     /note="DNA double-strand break repair ATPase Rad50"
                     /db_xref="CDD:235175"
ORIGIN      
        1 meiqrltlkn fkthrdrtfe fmpgvnvicg engagktslf eaiawvlfda rsgygsgfhk
       61 aiirrgtqra eaivqfisaa dgrsyivrrn tqtgysivdp qvgelglplr edvhawlqeh
      121 lgirsafplr dlfeqiigip qgmmtadflk ppaqrrqife pilqvsdyrq afdnalalvn
      181 fsqeqvasle rqlalqnqel atrsqyeqqa talaaelerd rqrceelrqe cqalaakkqe
      241 yeaavetlnr lqqtcerlea qlrqqeelcr drqrqltaar esqarcqqlq sdydryrqqe
      301 acyqeleqql reratlehki rtleeqqqkl atelariesq rqaiatiasq laalepqiad
      361 adaldaeiap levryqqaqq adqelrhlkq qaatlqtrle eidqqvqale qqrpiaatls
      421 akqaqreqlq aqlnhaaaah alaatldpil ntaqrqaavs dalvtaaitg ltaaqqfslv
      481 aaaiqeglga lqqlqqnyhw lldqltalrh tltdpaalpa lnqrleelea eialaaaaer
      541 sllraqalee ercrlqtelr qlgdrqqale plsqeladle grveklrqer anlgqphaqr
      601 qllleqqaaa pqleadyerl cseraslqar ltplyrerhh yatlearrqq lsdelargrs
      661 sydtylqhqq qaaqvetyea alraatqean alkgdlakaq aeykaqaqgv dlaalaavrd
      721 ryeslereyq rclgaipeke kqyqnclatl qhlddvaaak ettlqhlaaa rnhhhlieta
      781 rnifrrsgpr vseaylhtvs aeadrllrel lnrpdvalqw tsdyeiqvne ggywrpfksl
      841 sggeqmcaal avrlallrvl vntdiaffde pttnmdqvrr qqlaeslsnl ksfhqlfvis
      901 hdetfealte htihlersll
//
LOCUS       WP_011056853             150 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Thermosynechococcus vestitus].
ACCESSION   WP_011056853
VERSION     WP_011056853.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus vestitus
  ORGANISM  Thermosynechococcus vestitus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Thermosynechococcus vestitus"
                     /db_xref="taxon:146786"
     Protein         1..150
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15374
     Region          15..137
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mktelkakfl qhllakkken egftliellv vviiigilaa ialpsmlnqa akarlssaks
       61 aigainraqq ayrlentqfa pnvttlklgv stpdgyttpa itanggnday vqtsaddpqg
      121 tgvtgcvtva ngittstvit gnsatapncs
//
LOCUS       WP_011057322             385 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Thermosynechococcus vestitus].
ACCESSION   WP_011057322
VERSION     WP_011057322.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus vestitus
  ORGANISM  Thermosynechococcus vestitus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Thermosynechococcus vestitus"
                     /db_xref="taxon:146786"
     Protein         1..385
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=44249
     Region          79..>371
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 msngvswgpd nphplsrmkt elvwegkyde ygnrrpvklp tlplplqrie tideprdrek
       61 aqqlsifnea afhqqahrdd frnmliwgdn klvmaalleq frgkidliyi dppfdvgadf
      121 tmqvqigeeg eavqkeqsil eavayrdtwg kgtdsylhmm yerltlmrel lsergsiyvh
      181 cdwrmnaflr qvlddifgrd rflnhiiway ktggipenvg fskkhddili ytksdtpvfn
      241 qllqksyvpt lpepttisgk qlgvqrdevc elcgvgrpgq kyrnvimrdv wddiqsifrn
      301 dqqttgfdtq kpeallerii kassnegdlv adffcgsgtt lavaeklgrr wigvdlgrya
      361 ihttrkrliq vqrelhaadq pyrsi
//
LOCUS       WP_011058130             133 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Thermosynechococcus vestitus].
ACCESSION   WP_011058130
VERSION     WP_011058130.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus vestitus
  ORGANISM  Thermosynechococcus vestitus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Thermosynechococcus vestitus"
                     /db_xref="taxon:146786"
     Protein         1..133
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=14999
     Region          10..110
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(10..11,29..30,38,41,43..44,46,49..50,52,60,65,72)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(29,60..61,63,90)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mkmdtgaltf qqkiywlvkq iplgrvatyg qiaalcgwpr hgryvgyaly rvapnsdipw
       61 hrvvnaqgki syapqrrgtd elqrwrlaae giiftagdri nlrryqwqpp atvyqqliwp
      121 egaatdsaka kvg
//
LOCUS       WP_011058173             415 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Thermosynechococcus vestitus].
ACCESSION   WP_011058173
VERSION     WP_011058173.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus vestitus
  ORGANISM  Thermosynechococcus vestitus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Thermosynechococcus vestitus"
                     /db_xref="taxon:146786"
     Protein         1..415
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44226
     Region          4..410
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mitvlvlnag ssslkaslyr lapeigatav rppaplwqgl ldwgqnptva rlkvttanqh
       61 yeanlthpeg giaglrdwlk slldtltsgq tkllenlaei tiighrvvhg gsryqapvrv
      121 daqvkaaise lseyaplhnp anllgmelma dicpqtpqva vfdtafhaql pavartyaip
      181 yelttagiqr ygfhgishqy vseraatllq rplaelhlit chlgngcslt avkggvsvet
      241 tmgftptagv mmgtrcgdid pgillyllrr gwtvaeldrl vnrqsgllgv sgvsndlrqi
      301 laaidqgnpq aqlaydcfiy slqrgiasll palgrldglv ftagigenap gvrrdicrgl
      361 gwlgieldst anekgqgdrn ialptapvsv lvvqtqedwa iaracgqlls lpiss
//
LOCUS       WP_011058506             830 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas protegens].
ACCESSION   WP_011058506
VERSION     WP_011058506.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas protegens
  ORGANISM  Pseudomonas protegens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 830)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 830)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 830)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..830
                     /organism="Pseudomonas protegens"
                     /db_xref="taxon:380021"
     Protein         1..830
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90830
     Region          72..122
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          101..830
                     /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 mtlrdtrpss pcarplcqai raallcssig lgtvapqvla aasavdaprh sysvapgnlg
       61 dalnqfarqa gitlsttpal tqgrqspglq gdysipqgln qllrgsglea vsqdggsyvl
      121 rplpqgsalt lpatevkgfa lgnalgsmeg ynathsqiat ktstallets qsvsvvtreq
      181 iddqgaqtva qtmrytpgvl tnpygathry dyvamrgfnd gsvdniyldg lksmgdsgty
      241 ssmqvdpyfl ervdilkgps svlygrsspg glvaltskkp lyepyhqiqa tvgtqgkqgl
      301 gfdfsgpldd dkhiayrlig ltdksdtqfd hakekrfals ptlsidfsed tsltlqaylq
      361 ndpdggyhgg mpangtlnqr ngqrisehff egepgvdgyk rdqqsfgyqf ehrfndtfta
      421 rqnfryldsk vkldqvyayg wtnatsndln ryysgggekl hsfivdnmlq aefltgdvkh
      481 tlllgadyqr rktvvdwdqg tlqpinafnp vygnstinyy shtsylrrle qtgvylqdli
      541 eldkwrfslg lrqdwvetsd enrlaeaqrp lgteisdkrt kltgragaly lfdnglapyv
      601 sysesfnpns yadsagnplp ptdgtqwevg lkyqppgtdn lftaslfrid qenlasklpq
      661 enfyravgav rsqgleleah mqltdnlkll gsytftdiqy sksmtstlss atnlienkgn
      721 sptqaprqma slwadykfds atldglrlgg gvryvgyswa daentmkvpa ytlfdasigy
      781 dlgklglkgv dvrlnannlt nesyvascas lsycylgeer nvaatvsyqf
//
LOCUS       WP_011059611             809 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pseudomonas protegens].
ACCESSION   WP_011059611
VERSION     WP_011059611.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas protegens
  ORGANISM  Pseudomonas protegens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 809)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 809)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 809)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..809
                     /organism="Pseudomonas protegens"
                     /db_xref="taxon:380021"
     Protein         1..809
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=88472
     Region          31..809
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 maspafshfl prfgvaaava salslagcqs wntqdtlppt sgvqplkgla qnvsvrrnav
       61 gvpliesssf hdalftlgyv hasdrigqmv tlhllaqgrl aemsgadale vdrlmrainl
      121 kksadelyka ssprikrffe vyargvnayl fryrdklppd laaqgytpey wkaedsalif
      181 cllnfgqsan lqeeinalvl aqkvgsdklp wltpsypdep lplaeadklk glnltvpgln
      241 evsrainrla qlnslgtrgg snlaiapqrs rtgrsllaad shlqawyytq irapkyqaag
      301 asiaglpail qgfngkvaws mssvegdnqd lfleklkrqg nalyyqnngk wqpvtvrnet
      361 yfvkgqrpir eavyetrhgp llnsalgaal gngfglalqt pelkddktld affdlsraqn
      421 vekasdasre iraialnmvf adasnigwqv tgrfpnrreg egllpspgwd grydwdgyad
      481 pmlhpydqdp pqgwiatanq rvisqgygmq lsnswhaper aermaglass gkqdnrslia
      541 lqydqstlfa aklkkmfeap gmaqplkqai ealpdterak areaysrlla fdgkvsagsa
      601 daalyelflq esakqifldk lgpessdawq afvangnlsy saqadhllgq edspfwddsr
      661 taqkedkpai larslaaais sgeqllgadr kawqwgklhs yqwtnangrq irgplqaggd
      721 hntinsaayr wgqdfaitdt palrlivdfs lseplmglns sgqsgnpvsp nyangidgwl
      781 kaqylslpmq pqnfersygk trltlvpgk
//
LOCUS       WP_011060005             759 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Pseudomonas protegens].
ACCESSION   WP_011060005
VERSION     WP_011060005.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas protegens
  ORGANISM  Pseudomonas protegens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 759)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 759)
  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   3  (residues 1 to 759)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Pseudomonas protegens"
                     /db_xref="taxon:380021"
     Protein         1..759
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=79824
     Region          6..758
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msfgadeeil qdflveagei leqlseqlve lesrpddadl lnaifrgfht vkggagflql
       61 nelvecchia envfdilrkg errvdselmd vvlealdavn gmfsqvrert eitaatpell
      121 aalarlaepa gaepaapave evvepvaepv aeespagdit dnefelllds lnaakaeaea
      181 apaaapaaqg epasdeitda efeslldqlh gkgqfapdav apaaasatsg aagagdeitd
      241 defealldql hgkgnfavea ldsavaaapa apaaaapsaa aagsdlitdh efeslldelh
      301 gkgkfsetpg aakpaaasaa paaaataava kpaakkpepk aeapkaaaap aaaparaaaa
      361 appaekpase aettvrvdta rldeimnmvg elvlvrnrlv rlglnsgdea mskavsnldv
      421 vtadlqtavm ktrmqpikkv fgrfprlvrd larqlkkein lelvgeetdl dknlvealad
      481 plvhlvrnav dhgiespeer easgksrggk vvlaaeqegd hillsisddg kgmdpnvlra
      541 iavkrgvmdk daadrlsdte cynlifapgf stkteisdvs grgvgmdvvk tkisqlngsi
      601 niystkgqgs kivikvpltl aimptlmvml gnqafafplv nvneifhldl srtnvvdgqe
      661 vvivrdkalp lfylkrwlvs saaheeqreg hvvilsvgtq rigfvvdqlv gqeevvikpl
      721 gkmlqgtpgm sgatitgdgr ialildvpsm lkryaarri
//
LOCUS       WP_011060690             823 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas protegens].
ACCESSION   WP_011060690
VERSION     WP_011060690.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas protegens
  ORGANISM  Pseudomonas protegens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 823)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 823)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 823)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..823
                     /organism="Pseudomonas protegens"
                     /db_xref="taxon:380021"
     Protein         1..823
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90534
     Region          74..124
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          104..823
                     /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 mqiipisygt smhlptltpa rsilalaicl acnpvmavep ttatdnqata tysfaiarqs
       61 lanaldqlst qsglqiaysa alaqgiesag vsgrmsaeqa lgkllagtgl gfernganav
      121 lltrlpqssq aveleatqiv snqlgtvteg sgsytpgtia tatrmvltpr qtpqsitvvt
      181 rqhmedfgln nvddvmrhtp gitvsaydtd rtnyyargfs innfqydgip stvrnvaysa
      241 gntlsdmaiy drvevlkgat glltgagslg atinlvrkkp taqfqghasl gmgswdnyrs
      301 eldvsgplte tgnvrgrava ayqdkqsfld hysrktstyy gilefdlspd tlltvggdyq
      361 dnipkgssws gtfplinatg ghnsmsrsyn ngatwsgweq ytrtafamle hdlgdgwvtk
      421 lqldhkinsy haelgsiqfd epqtdgtakv naqkytgdtt sdsadlylsg pfnlfgrehe
      481 lvlggsians rwtgkgywsp dfpggkgnvv dfynwhgkie rpiwglpaqr tddtvrqtgt
      541 ymttrlnlmd dlnlflggrv vnyhltgltp sykesgrfvp yvgavydldd hfsvyasytd
      601 ifmpqeswnk dkdskllnpd egqnyelglk geffegrlns slayfevhet nrsvpddayn
      661 nqsptpdnya fkgakavtkg yeleisgels pgwqvqagyt hkivrddegd kistfepqdq
      721 vnlytsyklk gdldkltvgg glrwqsegwy svynaprkin edisqeaywl vdlmtryqit
      781 qnlsatlnvn nifdksyytn vgfynsaayg eprnfmlstr wdf
//
LOCUS       WP_011061765             806 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas protegens].
ACCESSION   WP_011061765
VERSION     WP_011061765.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas protegens
  ORGANISM  Pseudomonas protegens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 806)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 806)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 806)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..806
                     /organism="Pseudomonas protegens"
                     /db_xref="taxon:380021"
     Protein         1..806
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88204
     Region          67..109
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          92..806
                     /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 mhirltplaa tlrpviigls vastslplla aetgaavtdh qqrdyaiapg nldqvlgifg
       61 qqsasmiaid anlsagkrst glngrfsvae glqrllkplg lqavaegagy rviqasgger
      121 velgattvtt nqlgtvtegs ssytpgtiat atrlvltpre tpqsisvvtr qamddfglns
      181 idevmrhtpg itvatydsdr tsyysrgfai qnfqydgipi lqdaqyssgh tltdtviydr
      241 veilkgatgl ltgaggpggt inmvrkkpta efaghidlga gswdnyrsqv dvsgpltdsg
      301 nvrgrmvaay qdkksfldhy qrqtsvyygi lefdlspdtl ltvgadyqdn dpkgsswsgs
      361 sslydskgna istsrsynng aswsrwsqyt rtafttlehs fangwvakaq ynhqingyna
      421 plgslmspna etgiaslltr kytgetvsds gdlyatgpfd llgrehqlvv gasisnshwk
      481 grdftsatnh nnfydyfnwd ghspkpdwgr itkkndettr qsagymtarf slnddlslll
      541 gsrvnnyevs gtsrtkdtgk vipyagvvyd lgqnfsvyas yteiylpqdd yrdrndkvlk
      601 pdegtnyevg lkgeffdgrl nsslayfevh eenrpvddla ynanpttpgl dyaskgiksk
      661 akgyeaevsg elapgwqlqa gythkiirdq sgakvstwep edqvnlytsy kltgsldklt
      721 lgsgvrwqgt gwkilsnygk gteekfaqap ywlvdlmary qitenvsatl nvnnlfdkky
      781 ftnigfynss yygdprnvml strwnf
//
LOCUS       WP_011042240             174 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Colwellia
            psychrerythraea].
ACCESSION   WP_011042240
VERSION     WP_011042240.1
KEYWORDS    RefSeq.
SOURCE      Colwellia psychrerythraea
  ORGANISM  Colwellia psychrerythraea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Colwelliaceae; Colwellia.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Colwellia psychrerythraea"
                     /db_xref="taxon:28229"
     Protein         1..174
                     /product="TRAP transporter small permease subunit"
                     /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=19595
     Region          1..162
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mqfilklfkk iidavgslcs iimilmvlnv fydvvsryff ndvsigmqel ewhlfaamfm
       61 fgigytlked ghvrvdvfyd rmsehsqaii nilgaiffal pitllvlyyg sdyaleafqm
      121 gegspdpggl pyrwivrsii pfssaflllc ilyvtlknis llnppsqskq gqps
//
LOCUS       WP_011061981             345 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_011061981
VERSION     WP_011061981.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 345)
  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 345)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..345
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38244
     Region          31..214
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          259..339
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqikaadahd qlalvspfll qtladvaeak gvsaerlcrg lgftlddlqd ptlrisyrqa
       61 vamieralaa lpqqglglwv gsrnvlgtlg llghalslcr tlgdafelgi rhqhtsgtiv
      121 sadvgrqgee ffvelqcrlp ygevqifaae effaslliyg ralvsadfqa lrvefmhaap
      181 ayaelytrll gphvqfgclq armviearwl qaplpnhhpv alrqalklle lesaqvhqkm
      241 dliqaveral srdlragshi eqvagdlnms grtlrrrlte hgltfealle rvrqartlnl
      301 lgnpelsier iteevgysdv rsfrrafkrw tglspsafre eaalh
//
LOCUS       WP_011062529             404 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Pseudomonas
            protegens].
ACCESSION   WP_011062529
VERSION     WP_011062529.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas protegens
  ORGANISM  Pseudomonas protegens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 404)
  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 404)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Pseudomonas protegens"
                     /db_xref="taxon:380021"
     Protein         1..404
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46047
     Region          2..404
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mpalpsfslk qarrlalaaq gfggrqppas ikasrlnqqi erlgllqids vnalvrahyl
       61 plfsrlgsyp qqlldqaaws qgrqrtlfey wgheasllpm smyplmrwrm qrarqgqgiy
      121 sqlarfgqer qatlrrvlaa veqqgalgag slstreerag pwwdwseekh alewlfaage
      181 vtvsgrrgfe rlydlpervi paailqqmpl eeaqaqrrll lqaagalgva tekdlrdyfr
      241 ldpgdsrarl aelcesgell gcevqgwkqs ayclpearvp rkveasalls pfdsliwers
      301 rterlfdfry rleiytpehk rvygyyvlpf lhneriaarv dlraeraqgr lavhavheep
      361 fglddegvra lalqlrkmad wlgleqiqfn cqrdgarrlr evlg
//
LOCUS       WP_011063540             133 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Pseudomonas protegens].
ACCESSION   WP_011063540
VERSION     WP_011063540.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas protegens
  ORGANISM  Pseudomonas protegens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Pseudomonas protegens"
                     /db_xref="taxon:380021"
     Protein         1..133
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14153
     Region          1..131
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mrrsnqgftl ieimiviaii glvltlslps iteyvkkphr seiavllteq aqqlerhfsk
       61 agvysnapdl sagneyysia atltdtgfsl tatpkddglm aadkcgsfsi dqtgatrisg
      121 qaegltakdc wgl
//
LOCUS       WP_011063881             809 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas protegens].
ACCESSION   WP_011063881
VERSION     WP_011063881.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas protegens
  ORGANISM  Pseudomonas protegens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 809)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 809)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 809)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..809
                     /organism="Pseudomonas protegens"
                     /db_xref="taxon:380021"
     Protein         1..809
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87904
     Region          61..111
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          92..809
                     /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 msrpldtllr psllavaial caplaspalm aaeqstsvra ynlsaaplas tlnqiasqag
       61 lalslnpsla agktsapvkg qfdapgalre alrgtglqle hssagtyslv atpegvvalp
      121 qtnitgqqag esawgpvdgy latrtaagtk tdtslveapr sisvatrqqm edrnvqnldd
      181 avrympgivs asygsdtryd wmrvrgfept qfldglplpr gvyanpkaet wnldrlallr
      241 gpassvygqt ppgglldmvs rrpsadtsha vqiqygsdny rqinfastgk iddegqflyg
      301 lsgvvrdagt qvdhidnkry niapsltwni dtdtkltllt qftrddtgat sqfmpiqgtk
      361 iksplgdvsh hknlgdpdye fydrtyyalg yafehrlndv wqfrqnlryt kselsfqqlt
      421 vgsyayspad aagnisrtst nvdedigqfa vdnnfqadft tgdishtvll gldhqrtdts
      481 ylsiygnggt tnifnpvygq sivrpsrada yydydqktiq tglyvqdqma ldnwrltlgg
      541 redwvhqgtt ylnkkdvtnt drsknfsgna alsyvfdsgv vpyisyaesf qpasnasvsp
      601 tesykptegk qwelgvkyqp pgsntllsaa vydltqknvl vtsigagges itnqtgevkv
      661 kgleleavsd vtenlkviaa ytlaksevqk giykgnrlql mpnqqaslwt dytwhsgvld
      721 gfgigagary tgntygdqan twlgkadayt vfdaavhydl grldnslkga slklnatnlf
      781 dkdylstcdg sycyfgdqrs vvasatyqw
//
LOCUS       WP_011063970             295 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Pseudomonas].
ACCESSION   WP_011063970
VERSION     WP_011063970.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            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="formate/nitrite transporter family protein"
                     /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=32237
     Region          24..277
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mdaqkdgktp glsaqeqhev dhnqppraav lheiirtqgd qelersvaal wwsalaaglt
       61 mglslmgmgl lnsrlpdgea fkviasfgyc agflavilar qqlftentlt avlpvmskps
      121 lnnfgrllrl wgvvlvgnlc gtllvayvml hlpifdgktd qafleigrkv mendraqmfa
      181 kgiisgwmia tmvwmipsme saklwiiili tylmalgdft hivvgsaevs ylvfagelpw
      241 rdfwmvfagp tlagniiggs fifalishaq vrsesgkpnr nadrapapdp rqikk
//
LOCUS       WP_011064092             806 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Pseudomonas protegens].
ACCESSION   WP_011064092
VERSION     WP_011064092.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas protegens
  ORGANISM  Pseudomonas protegens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 806)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 806)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 806)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..806
                     /organism="Pseudomonas protegens"
                     /db_xref="taxon:380021"
     Protein         1..806
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=89281
     Region          25..800
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mkrsltvvav lilallagla gylyskqptr qgqvelnglq gsvtvryder gvphiraene
       61 adlyralgyv haqdrlfqme vlrrlsrgel aevlgpklvd tdklfrslri reradsyiag
      121 ldhqspawka leayldginq yqdshaspie fdvlgihkrp ftaedtvsva gfmaysfama
      181 frteplltyi rdelgndylk vfdldwqpkg vlakgktqps aplatvdwqg lgriarlsqq
      241 aleeaglpqf egsnawvvsg srtksgrall agdphirysl psvwyeaqls apgfelyghh
      301 qalvpfaflg hnldfgwslt mfqnddldli aekvnpensn qvwfhdkwvd litseqqiav
      361 kgqapvtltl rqsphgpiin dmlgttvgka piamwwgfle tpnpildgfy qlnradtlak
      421 vraaaakvha pglnivwana kgdigwwaaa llpkrpagak pafildgsts ladkegfypf
      481 sanpqeenpa rgyivsanfq pvsptgmeip gyynladrgq qldrqlsdks qkwdlentqk
      541 lqlgtttayg prllapllpv lrevvsdpee lklveqlakw qgdyplests atlfnqflfn
      601 ladatfhekl gdayfdaliq arvvdaalpr laadpdspww dnrttpqres radtvklawr
      661 asidhlrltl ganpaqwrwg qahtlthghp lgmqkpldrl fnvgpldapg shevpnnlta
      721 kigpapwsvv ygpstrriid fadpahslti npvgqsgvlf dkhyddqaea yiegvyqqah
      781 fsdeevtant rstlkllpar prvpap
//
LOCUS       WP_011066201             221 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Oceanobacillus iheyensis].
ACCESSION   WP_011066201
VERSION     WP_011066201.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus iheyensis
  ORGANISM  Oceanobacillus iheyensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 221)
  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   3  (residues 1 to 221)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Oceanobacillus iheyensis"
                     /db_xref="taxon:182710"
     Protein         1..221
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25836
     Region          15..219
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mleigmkiql emknsdnskt diylctiide tednyiinyp vhketlkttf fnigtyfsav
       61 yvgeddaiyr fptkitsrkk akipslyitk peveqwkriq rreyvrvdas idvavhsvlh
      121 qfdpfttttl disgggvaii tpkevelvlh tlvdiwlple ikyqnkihha yaqaeivtir
      181 elnirknvvs lqfhsitqkd rqeiirycfd kerekrlker n
//
LOCUS       WP_011066837             672 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Oceanobacillus iheyensis].
ACCESSION   WP_011066837
VERSION     WP_011066837.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus iheyensis
  ORGANISM  Oceanobacillus iheyensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 672)
  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 672)
  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 672)
  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 672)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Oceanobacillus iheyensis"
                     /db_xref="taxon:182710"
     Protein         1..672
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=72160
     Region          15..663
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mskkqqkskk dgqgnstqdi lekfdsesrv rnitnkkial lvtllailys lyhlyvtvnp
       61 ipallqrsih msfgialifl iypsfkkqyr gkipyydwll ftlsiasaly lmleynalmt
      121 trggipnmad ilfailtvll vleaarrvtg wilpilalif laypffshni wvpdmlmtrp
      181 fdlgdifgql ylkteglfst aigasvqfif lfilfgafla ksgmgqlfnd lamalagskq
      241 ggpakvavis sgfmgsinga avanvvgtga ftiplmkrig ysknfsgave asasiggqil
      301 ppimgasafi maettgiayg tialaalipa vlyflgvimq vhfragrrnl kgipkadlpr
      361 vkevlkergh lllpivglii flymgvpvgf aalytiglti viaalrktsr mgikdifkal
      421 edgarqslav mvacavvgii igvvnltsfg tvmtsaitsf gagslfltlf ltmiasiilg
      481 mglpsipayi itatmtapal aeygvpvlva hlfvfyfgif anitppvala afagagisgg
      541 dpmrtgftal rlslagflip ymfvynpaml fidpsglavn atefpfppii dvalitvtai
      601 igiigfgaal egffkmelqw mvrlilgigs llliipegft diigiiivml ifgwktiqyk
      661 kqetvsstks as
//
LOCUS       WP_011067428             336 aa            linear   BCT 20-JAN-2025
DEFINITION  acyltransferase family protein [Oceanobacillus iheyensis].
ACCESSION   WP_011067428
VERSION     WP_011067428.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus iheyensis
  ORGANISM  Oceanobacillus iheyensis
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Oceanobacillus iheyensis"
                     /db_xref="taxon:182710"
     Protein         1..336
                     /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=38251
     Region          1..270
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mernaffdna kvlliflvvf ghmiqpftse yagintlylw iytfhmpafi llagffakgs
       61 gnagyvwkla kkliipylif qilytiyyfy igkpdwqtgv fhphwslwfl fslfswhill
      121 ivfkkisply sislavligv vvgyfgeigh tfslsrtfvf fpfflvgywv tekqmmsvkr
      181 navkvvslav mtvlaiaiyy mpefnsgwll asksygdlgm eqyggiarll vyataavmvv
      241 svlawvpkrn fgwltqlgtr tlyvyllhgf ivqflrqhei lsvnnmldfi gvagisamiv
      301 illsskpvlt vsqpliegkm siirsiinnq rtrths
//
LOCUS       WP_011068741             397 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Bifidobacterium longum].
ACCESSION   WP_011068741
VERSION     WP_011068741.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium longum
  ORGANISM  Bifidobacterium longum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 397)
  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 397)
  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
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 397)
  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   5  (residues 1 to 397)
  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   6  (residues 1 to 397)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 397)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 397)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Bifidobacterium longum"
                     /db_xref="taxon:216816"
     Protein         1..397
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43675
     Region          20..68
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Site            39..53
                     /site_type="active"
                     /note="putative DNA binding helix [active]"
                     /db_xref="CDD:133389"
     Region          76..363
                     /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 mrampstavk ahnrsamaqy lyghshvtkq elerelglsl ptitqnlhal eddglirkge
       61 lqdstggrka qnyefnpdhr taigvvmrsn elrlcainly gnviekrnda lpyrntnvyy
      121 qriggiinnf aadvekkhgk vlgvsfaiqg ilspdattii fgtimgntgl tletisqsvh
      181 ypcmmihdsd asamaelwfd stltdavcvy lerrpggavi aggklyqgpn qcngaiehmt
      241 lvpggrecyc gqrgcmdtyc spetlpedye sipgffsvle qgerhhrerm dewldyvaqa
      301 ivnarsiiag dvivggeaaq hledsdiedl ktrviarspf gtdhfnlrks ycaedqniig
      361 aalrfaenyl dgicgaaerg rksrastksd ntstmev
//
LOCUS       WP_011070477             435 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Shewanella
            oneidensis].
ACCESSION   WP_011070477
VERSION     WP_011070477.1
KEYWORDS    RefSeq.
SOURCE      Shewanella oneidensis
  ORGANISM  Shewanella oneidensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Shewanella oneidensis"
                     /db_xref="taxon:70863"
     Protein         1..435
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48323
     Region          3..424
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mranrigyvy snkrfagell efntlegyey sftyaasyia sglpqigykl pithepyrrn
       61 ylppffanlm segwvrrhqa riarldqddk fglllgngae ligpvsvfte yrgdnisaai
      121 eviavpmksl kgyqidfprc efnevamesl ggvsisgvqp kmfltyaegn pktltnavgm
      181 gpyivkpspn dfpelaenef mvmqlckavg fnvaehhlvp fscgqlayvt arfdldretg
      241 rrhefiedla salnvapgnk ssdtlsyeka ikeayqlsgg hvqllkdgfl qvlmayivgn
      301 ndlhlknisl srasdsnras gytpiydmvs vapyrqydns gelsiwlles evergfstss
      361 yehygyytgh dfitfaeaig lgeragkvlm ndlgkkvaka rdkvianapg seqlkqiise
      421 ritarlstlt rpalr
//
LOCUS       WP_011072184             702 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Shewanella oneidensis].
ACCESSION   WP_011072184
VERSION     WP_011072184.1
KEYWORDS    RefSeq.
SOURCE      Shewanella oneidensis
  ORGANISM  Shewanella oneidensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 702)
  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   3  (residues 1 to 702)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Shewanella oneidensis"
                     /db_xref="taxon:70863"
     Protein         1..702
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76891
     Region          3..702
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msinmaefhq vffeeshehl enmeqlliai nlqspdpeel ntifraahsi kggsgifgft
       61 alssvthvme nlldkvrkgt felssgiidl llktvdtlsh ilslyreeep idwqqvefak
      121 nqlvaalngd pflttspeai patptkteit qtavvvsdas hqddigfgff eddveltlai
      181 enqdfgffde aftakeisve dinktlldsq lvtntepddd lgfgffeslt pesvdseina
      241 lvhiqankai aaieplskpv nspsvpkipr ytgntaestk vapadpvdps pvlnksvasg
      301 tkstptaatk kgntstqdat lrvetskidt lvnlagelvi tqsmltlign eisgelgerl
      361 ktalvelern tremqeavms vrmlpvsfvf nrfhrlvrdl sdqlgknvnl vieggnteid
      421 kgmieklvdp lthlvrnsld hgiekpevrr llgkaeiaql slrasqrggn iviavhddga
      481 glhrekilqk arennmsvtd nmpdkqiwql ifaagfstak eitdvsgrgv gmdvvrrnie
      541 alggridids vagqgatfei qlpltlaivd gmsvsvgkqi yilplvhiie siqphteqlk
      601 ylaqerlirv reeylpllnl hqlmeitpfa kcpeegivvl lesnnkrfgl cvdalvgqqq
      661 vvikslekhy rripgvsgat imgdgsvali ldveslaqqi kn
//
LOCUS       WP_011073357             130 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Shewanella oneidensis].
ACCESSION   WP_011073357
VERSION     WP_011073357.1
KEYWORDS    RefSeq.
SOURCE      Shewanella oneidensis
  ORGANISM  Shewanella oneidensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Shewanella oneidensis"
                     /db_xref="taxon:70863"
     Protein         1..130
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=13969
     Region          1..129
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mkikdkgftl ievmivvvii gilsaiayps ytryvaqstr aeglsalmkl anlqeqyyld
       61 nrkyatdltk iinadpyite ngnysvtssg tssftlkava kgvqasrdss cspltitdtg
      121 akgpsaecwk
//
LOCUS       WP_011073057             455 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Shewanella
            oneidensis].
ACCESSION   WP_011073057
VERSION     WP_011073057.1
KEYWORDS    RefSeq.
SOURCE      Shewanella oneidensis
  ORGANISM  Shewanella oneidensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 455)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 455)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 455)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Shewanella oneidensis"
                     /db_xref="taxon:70863"
     Protein         1..455
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=50701
     Region          29..415
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mqiltvqmni agewrdvavv gfyapekgtg gpcvlnydie hvtsyfhqfa qtavsvslpv
       61 dniplrsphw hrfledimpa gssrdywvkr lglqdmpnle rdfqllkygt iapignlrik
      121 esvpekakks lpvtfsiadv selqidfiey aqsrgaaagg asgaggaapk llvrlneqqg
      181 vwidtfqddp rnldqpylvk fprgkttlds dilraeyhfy heltqlgfet isvesmklie
      241 vergpslwlp rfdygveaga mvsygmesvy ailgeptakp llhadvirrl laefnkkeny
      301 gntrtpldve aglegksgie afvvewvrrd llniafgnsd nhgrntsfik hgnrvqlapi
      361 ydfapmkady emitrtftwg egmelggvyn fpaiaehlsd llspndlmsa lnetavrllg
      421 lelrlrqrgv pesilahsgi gfatlearmq qwgll
//
LOCUS       WP_011074249             354 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Shewanella
            oneidensis].
ACCESSION   WP_011074249
VERSION     WP_011074249.1
KEYWORDS    RefSeq.
SOURCE      Shewanella oneidensis
  ORGANISM  Shewanella oneidensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Shewanella oneidensis"
                     /db_xref="taxon:70863"
     Protein         1..354
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39382
     Region          1..350
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msihiqqvnk hfgnfvavds vnleiktgel tallgpsgsg kttllriiag leqadsgivk
       61 fngedittqh vsergvgfvf qhyalfkhmt vfenvayglt vrprktrpsk aeiaekvhsl
      121 lklvqldwta drypsqlsgg qrqrialara lavepkvlll depfgaldak vraelrrwlr
      181 rlhdeinvtt vfvthdqeea levadkivvm nkgrieqqgt peevydtpsn pfvyeflgnv
      241 nlfharvkhg hstignihip spehaggeeq qglayvrphe ievltqpten aikvnldlvt
      301 ivgpvarlev lteideqlih velskvqfkq lgiskgdnaw iqpryskvfl gegi
//
LOCUS       WP_011074357              96 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Shewanella oneidensis].
ACCESSION   WP_011074357
VERSION     WP_011074357.1
KEYWORDS    RefSeq.
SOURCE      Shewanella oneidensis
  ORGANISM  Shewanella oneidensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Shewanella oneidensis"
                     /db_xref="taxon:70863"
     Protein         1..96
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10167
     Region          1..96
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mrpsavlalk rsviretasr frvtnprvfg svldgtdldg sdldllvdal pgatlfdlgg
       61 lqdelesllg lqvdlltpgd lppkfraqvl aearpv
//
LOCUS       WP_011074572             301 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Streptococcus mutans].
ACCESSION   WP_011074572
VERSION     WP_011074572.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus mutans
  ORGANISM  Streptococcus mutans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 301)
  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 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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Streptococcus mutans"
                     /db_xref="taxon:1309"
     Protein         1..301
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35917
     Region          41..298
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <193..300
                     /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 mermkafltd enfkheinfd ndllpykiyq ttiangypda lfhwhpelei syiyegtaqy
       61 hidydyfnsq tddiilvrpn gmhsihpikn kmqkaqtllf hldlvgysll dqislrylqp
      121 lqnstfklvp cikpdmlgyq diknclfaif diyqrqgrhf elllkaklqe liyllyfhqy
      181 vlrkhsddmy rknekireli dyihqhyqek lfiisladii gyskthfmtv fkqhtgtsct
      241 dfiiqfrlsk acdllvnsik pilevasevg ftnlsnfnrq fkryyqitps qyrkqfkktq
      301 k
//
LOCUS       WP_011078144             100 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Vibrio vulnificus].
ACCESSION   WP_011078144
VERSION     WP_011078144.1
KEYWORDS    RefSeq.
SOURCE      Vibrio vulnificus
  ORGANISM  Vibrio vulnificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 100)
  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   2  (residues 1 to 100)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Vibrio vulnificus"
                     /db_xref="taxon:672"
     Protein         1..100
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10736
     Region          39..99
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkqvitllam lmafsfpsvs fadsatkaad kyegieisvn intataeeia mmlkgvgikk
       61 aqqivdfrea ngpfktvdel aqvkgigkst ieknqsrikl
//
LOCUS       WP_011080066             443 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Vibrio
            vulnificus].
ACCESSION   WP_011080066
VERSION     WP_011080066.1
KEYWORDS    RefSeq.
SOURCE      Vibrio vulnificus
  ORGANISM  Vibrio vulnificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 443)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 443)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Vibrio vulnificus"
                     /db_xref="taxon:672"
     Protein         1..443
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=50222
     Region          4..440
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mvmevitity qddlvgavsf dtekglgsfe ydpsfvkkgv elspikmpls nriyrfpeld
       61 fntfkglpgl iadslpddfg navlnawvas qgrspsditp lqrlqytgkr gmgaleyapa
      121 tklrslnasq qveiqslvsi aqeildsrgn fevelkqngq ddreammsll svgmsaggar
      181 pkavlafned ftqvrsgqtn vpsgfthylm kfdgvsehnk nqetfgdplg ygamefvyhl
      241 mankcgvdmm pcrllhegnr rhfitqrfdr iknskvhvqt lnglahidyk kpgsfsyael
      301 fgiarqlkls avdaeqlfkr mtfniiarnh ddhsknfafm lkqdrlkkdk wslapaydla
      361 ysykpgskwv nshwmslngk rdnftrsdfy sleklspifn krkiddiidt tiehvstwrq
      421 laeewdvpkt lideiqenlr ldi
//
LOCUS       WP_011081067             377 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Vibrio vulnificus].
ACCESSION   WP_011081067
VERSION     WP_011081067.1
KEYWORDS    RefSeq.
SOURCE      Vibrio vulnificus
  ORGANISM  Vibrio vulnificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Vibrio vulnificus"
                     /db_xref="taxon:672"
     Protein         1..377
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=42563
     Region          1..270
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          267..353
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkfihtsdwh lgrqfhnvsl lddqrvvldq lvnyirnhpv davvvagdif drsvpptaai
       61 ellgktidei cgeldtpmil ipgnhdgaar lgfgasqmkp sglhiisqfs qmiepvvlks
      121 eragevafyg mpysdpeqvr dafgvlvsny deahrvlvde irqhfdpkqr qvllshcfvd
      181 gaqsseserp lsiggsdrvs yehfsifdyv alghlhqpqk rveehirysg slmkysfseq
      241 fqkkgfmlve ldengfvcae hialdaphdm rviegemndi leqgkqdpny qdyllvrlhd
      301 khailnpmek lravypnvlh lekpgmlmnv eqglsqakla rsevdmfrdf faqaqdnpls
      361 etqdaaicql iqqltks
//
LOCUS       WP_011081184             275 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Vibrio vulnificus].
ACCESSION   WP_011081184
VERSION     WP_011081184.1
KEYWORDS    RefSeq.
SOURCE      Vibrio vulnificus
  ORGANISM  Vibrio vulnificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 275)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Vibrio vulnificus"
                     /db_xref="taxon:672"
     Protein         1..275
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=31957
     Region          25..259
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mqlitqsdye qyirqkddgd yimllnnltf ssvfqpifnq lmqligfeal lriqdekqnf
       61 irpdrffadp nhsdeyilsv eflsraihir nfskhytakg vklflnvmpn slitmtkdle
      121 yvdrsllfrr lkqlgmapsd vtfevieelc yqnddlreav kvlrskgfhf aiddfgaghs
      181 dekraveltp dlikidrgyl lsycagqqee llhalnlaqr igarvivegv eeeeqyqamr
      241 elglefyqgy hfgrpekidy waaqpislav dddhr
//
LOCUS       WP_011081191             292 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio vulnificus].
ACCESSION   WP_011081191
VERSION     WP_011081191.1
KEYWORDS    RefSeq.
SOURCE      Vibrio vulnificus
  ORGANISM  Vibrio vulnificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 292)
  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 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 292)
  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   4  (residues 1 to 292)
  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 292)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Vibrio vulnificus"
                     /db_xref="taxon:672"
     Protein         1..292
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32700
     Region          28..180
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          210..290
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 metlaelmqr yvdvkglekl eeiiptdipg vrfyrssrgn prhpfvyqsg iivlgqgykn
       61 ihigdhavcy gaddylvvgv pmpleceafa dddkpllgis vdvpmvllqq mvqklekhgy
      121 qnicsgkees cglksvkmea smlnackrlm rglcdplete vlgqslleev vyrallspkg
      181 yvlfelahae gnysriaqvl dkvhqdysep ltvqdlaska nmsisafhta frsvtlespi
      241 qyikkvrlnk ardliklegk rvndaarlvg ynstsqfsre ykrhfnetpk sa
//
LOCUS       WP_011081203             267 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Vibrio].
ACCESSION   WP_011081203
VERSION     WP_011081203.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 267)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..267
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=30765
     Region          30..257
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mntltaekln eyifseqggq fvsrykemtl rsvfqpiykk dltvvgleal vriqcddgsi
       61 irpdhffhsd eispidklnv erlsrimhir nfaqssyrdk klflnvlpha verlaleels
      121 yhfllktire vdlcpeqivm elieikvnce qelqcatrsl skngfwwaid dfgiaastqe
      181 rtrnilpnii kldrsllqry eegdtnlllc alafaremes ltviegiete qqlslmklln
      241 ldmyqgyfla mpqsleeepa fslasfg
//
LOCUS       WP_011081880             609 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Vibrio vulnificus].
ACCESSION   WP_011081880
VERSION     WP_011081880.1
KEYWORDS    RefSeq.
SOURCE      Vibrio vulnificus
  ORGANISM  Vibrio vulnificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 609)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 609)
  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 609)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Vibrio vulnificus"
                     /db_xref="taxon:672"
     Protein         1..609
                     /product="M4 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=65747
     Region          11..605
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mkhnqrhrlg lmiaavmcsl pvtaaemvsv sdsavleqal svqarslapv engfeavkti
       61 qlpngktkvr yqqtylglpv fdtavvateg rsglsnvhgt maqglaadlp svsvnldqqq
      121 aialgklrhq aqhanakaln tenetaqlmv rldannkaql vylvsffvae eepsrpfmfi
      181 dansgeilqv wdglnhaqag gtgpggnskt gryefgtdyp sfvidkvgtt ctmensvvkt
      241 vdlqnrtsgs taysyscpga snyndhkavn gaysplndah yfgkvvydmy kdwmntaplt
      301 fkltmrvhys snyenafwdg samtfgdgas tfyplvdinv sahevshgft eqnsgliysn
      361 msggmneafs diageaaefy mkgsvdwivg adifksnggl ryfdqpskdg rsidhasqyy
      421 dglnvhhssg vynrafylla nktgwnvrkg feiftlanql ywtanstfda gacgvvkaaq
      481 dmgynsndva eafnqvgvna scgvtppsgn vlknntpvsn ltgnkgsevf ytftvdrnat
      541 aivsisggsg dadlylkags kpttsswdcr pyrygnnesc svsaapgtty hvmikgysny
      601 ngvtlklqy
//
LOCUS       WP_011081890             706 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Vibrio vulnificus].
ACCESSION   WP_011081890
VERSION     WP_011081890.1
KEYWORDS    RefSeq.
SOURCE      Vibrio vulnificus
  ORGANISM  Vibrio vulnificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 706)
  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 706)
  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 706)
  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 706)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Vibrio vulnificus"
                     /db_xref="taxon:672"
     Protein         1..706
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=75461
     Region          13..692
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 msdslqqqlq qfelptrtdf pwvtaaitgi gvvlsllhiw fntlstlpel wisathfagf
       61 alicllwypa haslkrsria lavdvligia alacliyipf aedalyqrgv kfvasdwvvs
      121 itailiaiei irrtmgwfip vliviclsyv vwwgkwaggi fhfpglsmet llyrsffsse
      181 gmfgsisris wtfvfmfilf gaflvksgvg dyiinvsraa agkiiggpgf iavlgsglmg
      241 svsgssvant vstgvisipl mqkagfpsrf aagveaaast ggqlmppvmg agafimasyt
      301 qipyvdivav sfvpaliyfl svaffvriea krsgvqkitt sdeslgkvll sgwhnliplv
      361 vlvtllvqgf tptyaaglsi lsvvvaswfs kdhkmgpkei iealaqgakn mattavllvg
      421 iglvinvist tgigntfslm ingwsqgdll imlvlialas lvlgmglpvt aayivlgtls
      481 apalyqliae nqllslmsag qlpeqakaif mlaapdkldl lnapmaieta kemlalvpvd
      541 fketllqqsl gieavglall aahliifwls qdsnvtppvc ltafaaatia ktppmrtglt
      601 awkiakglyl vplliaytgl vswdvttvlm tgffaifgty aligalegyl egqinwllrl
      661 alaasgalmv whdvplwlrv asliifavif vysgrqyqaq qaaavs
//
LOCUS       WP_011083795             739 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate--CoA ligase family protein [Bradyrhizobium].
ACCESSION   WP_011083795
VERSION     WP_011083795.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium
  ORGANISM  Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 739)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 739)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Bradyrhizobium"
                     /db_xref="taxon:374"
     Protein         1..739
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=77629
     Region          28..737
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mearvsaafs sprpwspspd asdivkgiha mlhphnivlv gatdkpgnya eriwnnlvky
       61 gfegglypvn akretiwgvp cykdfaalpe kpdhvlvlvp arfavqvird aaaagarsat
      121 ivtsgfselq ddesqqlaae lqaairetgl avtgpnclgn lsageklftn iddrivtmeq
      181 gavaiagqsg aivmairqal edrgvgvgym vttgneagle tpdlmryfae dpsvkvivvy
      241 legvrntkaf rdackaaraa skpvialklg aseggraaam ahtgalagsi etfdaiatre
      301 gvirvgglde liettecfvh aavpngdrla avtlsggkrg mlidafyaeg lnfaplsphv
      361 sselarmlgp gsivgnplda gfaavvdpsv ymksiklmid dpdidiviid aelpkaphel
      421 rernlrivde masraskpvi yisamsigft eftkslrksl phlavmqgmd ravtaiksll
      481 ayaklrkevp divssskpaa ravlekalts angaaldeva skkllkaygi ptskeataqt
      541 aaeavkiakq igfpvvakvv saeilhksdi ggvvlnlsna aevkkafadi tarvkrlkgk
      601 prldgiliaq qvkadlelvv gasldaemgp vvlfgtggid ielmkdvala gapldeaear
      661 lligrtkagi kmrgyrgkpa lheasavkal vglsnliada gdriasidin pflintrtgv
      721 avdalivlnn aaakraagh
//
LOCUS       WP_011084120             702 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter permease [Bradyrhizobium].
ACCESSION   WP_011084120
VERSION     WP_011084120.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium
  ORGANISM  Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 702)
  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 702)
  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 702)
  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 702)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Bradyrhizobium"
                     /db_xref="taxon:374"
     Protein         1..702
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=74528
     Region          28..697
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mlqaegseap ikvefdnfeh gfpegfgpgw wgrlaywigi afatfqlyva afnylpsqvv
       61 rgvhvgflvl ltfglianft arsdvgralg wviggagffc glyqwifyad liardgdptr
      121 ldlavgtlla vlifegtrrl mgaalplmcg acllywffgq ylpsplnhrg ydfdqivthl
      181 sfgtegfygv piyvsatyif lfilfgsfle ragmiqlftd vslglfgrtr ggpakvavfa
      241 sgmmgtisgs gvanvvtvgq ftiplmikfg yrrafaagve atasmggqim ppvmgavafi
      301 maetlgvqys eivkaaaipa ilyfasafwm vhleagkhgl vgmkrseips awkalvtrwy
      361 lvlplaalvy mlfegftply agsmglaltv tlilgasita gassmvirti fwvglalvva
      421 alsrdglqiv pvasvvagli vitafirggf kalrecrdal aesaksaitv gmacaivgvi
      481 igmmsqtgvg tifggwvigl gekslflali mtmllsillg tgiptiptyi itaalaapal
      541 aklgvplias hmfafyygim adlsppvala alaaapiake npdkigweam rialagyvip
      601 fvfvyspalm lqagdpmaak lgfygavala tfkalvaigl fgmvaigflf trltfverlv
      661 algaafcllg dfpfsdtagf vlsaalalwq wrqrppavve av
//
LOCUS       WP_011084459             268 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: EAL domain-containing protein [Bradyrhizobium].
ACCESSION   WP_011084459
VERSION     WP_011084459.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium
  ORGANISM  Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 268)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Bradyrhizobium"
                     /db_xref="taxon:374"
     Protein         1..268
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=29592
     Region          12..244
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mplepapspa vdvpealkas slelwyqqkl hlrtlvpsga ealirmrhpa wgvvppayfi
       61 pdesdphfha lsefviarai edwryllgqi gpvdlsinlp isfladdaav relcyripdh
      121 aafaglliei dsaevidnld laidvarrvr lhnigisidn vgakwpsllg lpnfpfvqlk
      181 vdhqyvtgca dqrlkqtvcr rivelahdsg aqviaqgget radflaahem dfdqvqgylf
      241 gkpmgvkkfa rsrthfseke pivlthga
//
LOCUS       WP_011085304             398 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Bradyrhizobium].
ACCESSION   WP_011085304
VERSION     WP_011085304.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium
  ORGANISM  Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Bradyrhizobium"
                     /db_xref="taxon:374"
     Protein         1..398
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42533
     Region          6..393
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mpapeavlvl nsgsssikfg lfeisaaepa llckglldeh earprlvvkg pagedlfekr
       61 rdeadadggh lfadalafid drfgqdslra vghrivhggp dhsgpveltd ditaklealt
      121 plaplhqprc lapvrtlsai rraltqiacf dtafhhglap pasrfaiprr yeergvrryg
      181 fhglsfeyva grlagiapql vakrtviahl gngaslcalr ngrsvdttmg ltpldglvmg
      241 trsgtidpgv llylqqhegm svedvqhlly hesgllgvsg msadmrtlla sreaaardai
      301 dlftfraaqe iammattlqg ldclvftggi gehaseirsa igerlawlgv ridaaanseg
      361 rerigtgdsa vdifiiptne eiaiarhcaa llrerhaa
//
LOCUS       WP_011085389             124 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein
            [Bradyrhizobium].
ACCESSION   WP_011085389
VERSION     WP_011085389.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium
  ORGANISM  Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Bradyrhizobium"
                     /db_xref="taxon:374"
     Protein         1..124
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=13455
     Region          16..92
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mlnqreldrs emgrligsdr vegtsvygad rnkigsierv midkisgkvs yavlgfggfl
       61 gvgndhyplp wqslkydtdl ggyvtgitak elqgapkyge qsdwnwgdda avrginsyyg
      121 vpfa
//
LOCUS       WP_011085837              98 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein
            [Bradyrhizobium].
ACCESSION   WP_011085837
VERSION     WP_011085837.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium
  ORGANISM  Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Bradyrhizobium"
                     /db_xref="taxon:374"
     Protein         1..98
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10474
     Region          1..97
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mtrdeiiaai rknadaikak gvsklaivgs radadyrpds didvlvevep easfsllnli
       61 dveqiiedat glqaqatvrr sasphsaqqi addileif
//
LOCUS       WP_011086968             315 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Bradyrhizobium].
ACCESSION   WP_011086968
VERSION     WP_011086968.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium
  ORGANISM  Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (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   2  (residues 1 to 315)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Bradyrhizobium"
                     /db_xref="taxon:374"
     Protein         1..315
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35384
     Region          232..311
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mtsdddaptl apkifrfsdv defrnairgl nfeftpfvrr iaaeqiilql pgcdvnvtra
       61 fprvvdaeli adctavgfam ddldvpirfn gaqrdravvv igsggaaynt ieevqrqias
      121 vvfrpevknr gwpetrsnfk ifetstlaln gvrnvvrevv aaasepidpt eaplkaaamk
      181 eslfgavdav fanlvsarwt vrpnderqfk ifqdiralls gdlaqpiyse eiarelglsv
      241 rtlhdvvrry rgmslhrylr lrrlwlvrqr llagadsvka valafgfwhl sdfsrsyrdr
      301 fgeapsetle rgrrr
//
LOCUS       WP_011088421             372 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Bradyrhizobium].
ACCESSION   WP_011088421
VERSION     WP_011088421.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium
  ORGANISM  Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 372)
  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 372)
  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   3  (residues 1 to 372)
  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   4  (residues 1 to 372)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 372)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Bradyrhizobium"
                     /db_xref="taxon:374"
     Protein         1..372
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39743
     Region          27..358
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(100..102,123..124,173,225,249)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkslkligla fgasialssa afaqdvtiav agpmtgtesa fgrqmkngae mavadintag
       61 gingkklaln veddacdpkq arsiaekiag akipfvaghy cssssipase ayadgnvlqi
      121 tpastnplft erklwnvarv cgrddqqgli aaqyiaknyk gkniailndk ttygkglade
      181 tkkalnkagi tekmyesynk gdkdfnaivs rlkrdnidlv yvggyhqesg lilrqmrdqg
      241 lktvlmagda ladkeyasit gpagegtlft fgpdprnkpt akkivdafka knidpegytl
      301 ytyaamqvws qaakkagttd akkvmeamka gkwdtvigpi eydakgdikq idyvvykwda
      361 kggyaeikgn gt
//
LOCUS       WP_011090378             118 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: PRC-barrel domain-containing protein
            [Bradyrhizobium].
ACCESSION   WP_011090378
VERSION     WP_011090378.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium
  ORGANISM  Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Bradyrhizobium"
                     /db_xref="taxon:374"
     Protein         1..118
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=12897
     Region          10..88
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 meterretgt ligsdkvegt avygagdqki gsiervmidk vsgqvsyavl gfggflgigd
       61 dhyplpwqsl kydtnlggyr tnlsadrlqg aphygndndw nwddptrara vndyysgf
//
LOCUS       WP_011090540             363 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [Bradyrhizobium].
ACCESSION   WP_011090540
VERSION     WP_011090540.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium
  ORGANISM  Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 363)
  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 363)
  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 363)
  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 363)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Bradyrhizobium"
                     /db_xref="taxon:374"
     Protein         1..363
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39869
     Region          1..355
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkrrdflkvt gaglaastav aapaiaqsap evkwrlaasw pkaldtlygg ceyfckrvae
       61 vtdnkfqiqp faageivpgl qvldavsngt vemgntalyy ywgknpaftf gtslpfglnt
      121 rahiswllfg ggtellngll keyntvgipt gstgaqmggw frkeiksmed fkglkfrvgg
      181 fagtiiakvg gvpqqiaggd iypalekgti daaewvgpyd deklgfvkva kfyyypgwwe
      241 gtgqghnimn ldkwnalpkh yqaaiemasr dtftwvtgky dyvnppalkr llvagailkp
      301 fpqevleacy aaaneiyadl sktnphfakm ytslsafrne slawmqvael sydsfmmrmr
      361 trt
//
LOCUS       WP_011090647             743 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CHASE2 domain-containing protein [Bradyrhizobium].
ACCESSION   WP_011090647
VERSION     WP_011090647.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium
  ORGANISM  Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 743)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Bradyrhizobium"
                     /db_xref="taxon:374"
     Protein         1..743
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=82424
     Region          23..659
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mkrlkilrrw farklglarl mclallvvfa garlwdpppi qelrlrtfdm fqlidprhkt
       61 arpvtivdid dkslarlgqw pwprtriadl iqnltsngav aigfdvvfse adrlnpdlva
      121 sqmrylddat raklrelptn dqiladaikr srvvlgetgq raisseidke lpftgvatvg
      181 edgaerflfe fpgllrnvpv iekvaagrgl fsikterdgl irrvpmimra qgmvmpslsl
      241 eilrvitgtp tllvrtdktg vrgvrlkgve iptdrngqlw vhyarqdpsi yvsaadvldn
      301 tvppakiagk lvlvgtsavg lndikttpvs stmpgveiha qvlesvlsga visqpnyalg
      361 veliaalvig llviiftpnl gpvrlvlaga mfaailvgvs wffyaqyryl idftypllst
      421 taiyltlifa sfvreqrqrv qirgmfaqym spvlveqlaq speklvlgge eremtimfsd
      481 vrgfttises ykhdpqglit lmnrfltplt dviidqkgyi dkymgdaima fwnaplddae
      541 hevnaceaai qmleridavn kereeeaadg ghvyiplnvg iglntgigvv gnmgsdlkkn
      601 ysvlgdsvnl asrlegqske ygfpiivgsr talaakdkfa ileldfimvk gktepeviya
      661 vagredvmhs gsfqrlrnvt iemlgcyrnr dwqgaldaie rgrrsedadt leklfklyei
      721 rikefqlnpp aegwngayal ltk
//
LOCUS       WP_011091649             193 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Buchnera aphidicola].
ACCESSION   WP_011091649
VERSION     WP_011091649.1
KEYWORDS    RefSeq.
SOURCE      Buchnera aphidicola
  ORGANISM  Buchnera aphidicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Buchnera.
REFERENCE   1  (residues 1 to 193)
  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 193)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 193)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Buchnera aphidicola"
                     /db_xref="taxon:9"
     Protein         1..193
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22719
     Region          <70..191
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Site            order(80..81,84..85,87,114,117..118,121..122,124..125,148,
                     150..151,154..155,158)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          80..108
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          113..142
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          147..173
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 miknsyinek lnfyqksflt cmlliviviv yffsknyldk pknsyvhtkm mtfltnsnel
       61 nisknliwtk ktisgnlmsl klakvyvinn qlekalkile ksknnsvdln ffnlisfkia
      121 qiyfqknnik kaittikdil gdswdsirnn figdvyfkld nqkravtlwk rsiiqnkkie
      181 fekiiqmkin nyn
//
LOCUS       WP_011094113             251 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Pectobacterium atrosepticum].
ACCESSION   WP_011094113
VERSION     WP_011094113.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium atrosepticum
  ORGANISM  Pectobacterium atrosepticum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  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   3  (residues 1 to 251)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Pectobacterium atrosepticum"
                     /db_xref="taxon:29471"
     Protein         1..251
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28316
     Region          34..245
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mkavnenlke qfvkrnklai catlrelkkn dtslmvhhsh gqfiskildv vpdnnlfvfd
       61 lggierensr alyagalsfi aepagakvef naeiaktvny dglpafsaqi pellyliqrr
      121 tyfrintplw ppltcrgelp ddsvftftik dlslgglsly tdrdttgllt egdiiksvem
      181 dladhgffcv dlqfvgqamv kivdnkgelk ltqrlsfkfp slnaaqerdl qqvifelekl
      241 qnekkkrfqe l
//
LOCUS       WP_011095052             246 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Pectobacterium atrosepticum].
ACCESSION   WP_011095052
VERSION     WP_011095052.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium atrosepticum
  ORGANISM  Pectobacterium atrosepticum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 246)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Pectobacterium atrosepticum"
                     /db_xref="taxon:29471"
     Protein         1..246
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=27979
     Region          14..239
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mntttlnidg eilrltaefq piihlpknki fryealarfy nsegaltptq qtidkiekcq
       61 aidkvtdfmf dvvcqviknk nsmtisfnls hllfnntlyl eslyqkclsn nvspqnieie
      121 isekttrqql idgipflnqa kkygfmisld dfgagnlqid slslfnfdti kidrsiidgi
      181 gkeetksqkl kvllnklipl gvniicegve katdlnrlnk yhpigiqgyi fyrpltfsql
      241 rllegf
//
LOCUS       WP_011099431             580 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Clostridium tetani].
ACCESSION   WP_011099431
VERSION     WP_011099431.1
KEYWORDS    RefSeq.
SOURCE      Clostridium tetani
  ORGANISM  Clostridium tetani
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 580)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 580)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Clostridium tetani"
                     /db_xref="taxon:1513"
     Protein         1..580
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=65744
     Region          2..559
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 minrrlinlv gdskvwiflt vlmkwisllf niinimfian yleftylygv dsrkglitlg
       61 ifiisilira icnymsvkfs skcsqnarit lrntiyekli nlginynekv stsetiqvai
      121 dgveqleiyf grylpqffys vlapltlfvt lgfisikvvl illicvplip isialimkia
      181 kkifakywgi yvnlgdtfle nlqglttlki ynmdedrntk mneeaenfrk itmkvlsmql
      241 nsisvmdlia fggsaigmil tlkelaqgri smagaftiil lsseffiplr llgsffhvam
      301 ngisasqkif niidtpleqy ktkeikdfns lsvefknvnf syeedrkiln sinlninsgk
      361 italvgpsgc gkstisslim gfnknyqgki lingnelrei deeqlkrkin ivthnsyift
      421 gtieenlkmg resasieemy ealrkvnlyd fvmsldnklk seikegganl sggqrqrlal
      481 arallydsei yifdeatsni dveseneimd viyeigkekt illishrlyn vknadciyvl
      541 sqgeikecgn hkelmnkkgi yftlveeqne leklgadyca
//
LOCUS       WP_011099633             101 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Clostridium tetani].
ACCESSION   WP_011099633
VERSION     WP_011099633.1
KEYWORDS    RefSeq.
SOURCE      Clostridium tetani
  ORGANISM  Clostridium tetani
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Clostridium tetani"
                     /db_xref="taxon:1513"
     Protein         1..101
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11562
     Region          4..94
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mlddklktql ekifakypqv ekvvlfgsra rgdnkynsdi dlcifgeels hltlakitfy
       61 iedldtclmf dilafneltk kdliknilne gvviyrgkev e
//
LOCUS       WP_011099924             798 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Clostridium tetani].
ACCESSION   WP_011099924
VERSION     WP_011099924.1
KEYWORDS    RefSeq.
SOURCE      Clostridium tetani
  ORGANISM  Clostridium tetani
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 798)
  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   3  (residues 1 to 798)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Clostridium tetani"
                     /db_xref="taxon:1513"
     Protein         1..798
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=90551
     Region          1..>138
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          173..250
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
     Region          293..370
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
     Region          350..798
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdtsqymsmf leeamenlqt lndsllqleq epedsdklne ifrvahtlkg msatmgfnei
       61 aelthkmedv lsefrdgelk vtenvvtvlf kcldtleqmv nniaddidee isiegiisel
      121 qdikkssekg dikekaieeh kdkialnsds dlnlneydkn imkqaknkgy ntyiikvils
      181 entllksara flifksledv geivksepsa ediesenfdf einlmyvske nekeiykils
      241 giseveevml hkleeekiie eskehtasnl dldlneydin vvkqaedkgf dsyaikvvln
      301 entllksara flifknleds geivksipsv edierenfdf einlmyisnr akeeiyeils
      361 niseveqvmv dnvnvekere kiikaeekvv aikekvqqek skvdvksvqn nkprgkkehq
      421 fkkqhqsvrv dlgrldkfmn mvselvinrt rleqisqnyk ltelnetleq varttsdlqd
      481 lvmkirmlpl divfnrfprl irdlsveldk emeliikgqd teldrtvide igeplihlir
      541 naadhgiept eerikkgknp vgkikllayq egtkavikve ddgggidvqk vrakanrldi
      601 ntegmtdndi rnlifmqgfs tnekvtdisg rgvgmdvvkt kiaslggsve viseenkgss
      661 fiirlpltlq iiqallvkvg eetmaislgy idrvidfked likktnnkev iiynenvipl
      721 irlskrlnle esnskkkyiv ivkvgeknig lvvdsllgqq eivikplgkt lqglkeyiga
      781 tilgdglvtl ildvsslv
//
LOCUS       WP_011100327             192 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Clostridium tetani].
ACCESSION   WP_011100327
VERSION     WP_011100327.1
KEYWORDS    RefSeq.
SOURCE      Clostridium tetani
  ORGANISM  Clostridium tetani
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 192)
  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 192)
  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   3  (residues 1 to 192)
  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   4  (residues 1 to 192)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 192)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Clostridium tetani"
                     /db_xref="taxon:1513"
     Protein         1..192
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21521
     Region          4..191
                     /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"
ORIGIN      
        1 mikkiviadd epitrmdmre mleeegynvv aeasdgfdai elakkhspdl iimdikmpll
       61 dglsaakiil keelagevil lsayndktfi ekakeagvig ylvkpidnks littievsls
      121 rckefkevkk nvkvlekkle srkiiekakg kimqklnise edaythirni smkkrvsmea
      181 vaqiiimseg ei
//
LOCUS       WP_011100567             126 aa            linear   BCT 20-JAN-2025
DEFINITION  zinc ribbon domain-containing protein [Clostridium tetani].
ACCESSION   WP_011100567
VERSION     WP_011100567.1
KEYWORDS    RefSeq.
SOURCE      Clostridium tetani
  ORGANISM  Clostridium tetani
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 126)
  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 12181465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Clostridium tetani"
                     /db_xref="taxon:1513"
     Protein         1..126
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14695
     Region          23..122
                     /region_name="zinc_ribbon_15"
                     /note="zinc-ribbon family; pfam17032"
                     /db_xref="CDD:465334"
ORIGIN      
        1 mffigifgid erkkeikvir nlvckacgni tvyklikvnk vfhfffipif twnkryylms
       61 eccnsiflis celgkalenn ehvdikdedl eqinsytntn ericsncsnv vqsnfkycph
      121 cgermn
//
LOCUS       WP_011101393             203 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Lactiplantibacillus].
ACCESSION   WP_011101393
VERSION     WP_011101393.1
KEYWORDS    RefSeq.
SOURCE      Lactiplantibacillus
  ORGANISM  Lactiplantibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 203)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Lactiplantibacillus"
                     /db_xref="taxon:2767842"
     Protein         1..203
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=22712
     Region          81..202
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(147..148,152,176..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkisvhqliw vtigaislti ftgfghlfar hhqaiasnrp itkvshsatk vttpvpetvd
       61 whkpslsrpy pklakyddin iqvsikkqrv ylknhdqtly tmlastgkhg sdtpkghfei
      121 qaergqhffn tqsgeganyw vsfkdhgiyl fhsvpvdand qyivkeaqql gkvanshgci
      181 rltiadakwl yenisthtpv vvs
//
LOCUS       WP_011101425              81 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Lactobacillaceae].
ACCESSION   WP_011101425
VERSION     WP_011101425.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillaceae
  ORGANISM  Lactobacillaceae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales.
REFERENCE   1  (residues 1 to 81)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 81)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 81)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 81)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Lactobacillaceae"
                     /db_xref="taxon:33958"
     Protein         1..81
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8414
     Region          4..81
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 meltiklfam laeqigptvt vtvstpataa mvkpalsqrt palkavinna riavnqefia
       61 ddrqvlqstd eialippvsg g
//
LOCUS       WP_011101462             393 aa            linear   BCT 20-JAN-2025
DEFINITION  exonuclease SbcCD subunit D [Lactiplantibacillus plantarum].
ACCESSION   WP_011101462
VERSION     WP_011101462.1
KEYWORDS    RefSeq.
SOURCE      Lactiplantibacillus plantarum
  ORGANISM  Lactiplantibacillus plantarum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactiplantibacillus.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Lactiplantibacillus plantarum"
                     /db_xref="taxon:1590"
     Protein         1..393
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44257
     Region          1..282
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          277..366
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mkllhtadwh igrtlngysl ldeqeaafkq iltialaekv dgiviagdiy dravpstdav
       61 tsldhmlqai niehhlpiya iagnhdgakr lnygrewlay nnfhintlla eaftpietpt
      121 aqifmlpffd pidarvyyqq qglpekqvka ihtihdamqr vvsdlvttfd pekrhllith
      181 ftvtpkandd leltsettsk vgglatlttd lfadfdyvml ghihtrlasp dkdriryags
      241 pvkfnvkean pkfhgkgvei vtitptaith efkpiqpqtd lvtlrapwet lldpnfyqqq
      301 plkqawfait vqefdrskhl nvraqleqiy gtiveldyes nhqataisgp knmnelspda
      361 ivgqffhait gnqlsttqqq lvdqifvnlr ked
//
LOCUS       WP_011105775             194 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Vibrio
            parahaemolyticus].
ACCESSION   WP_011105775
VERSION     WP_011105775.1
KEYWORDS    RefSeq.
SOURCE      Vibrio parahaemolyticus
  ORGANISM  Vibrio parahaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 194)
  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 194)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Vibrio parahaemolyticus"
                     /db_xref="taxon:670"
     Protein         1..194
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21707
     Region          42..101
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msgycstvll vsfkvhkels fmsrnqfsit kqiieanlkk shgltvaeqs vlvtlssyfg
       61 krgnsntysc fpsqdriaeq vgctrptvnn alqklerlrf irssyrgtnt sklytwlgip
      121 tleeeeteel sptnergdtv ssesqtgnds dtensdalas stvnavqlqr eqhqatsdww
      181 ndfeeelevs espf
//
LOCUS       WP_011106323             128 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Vibrio
            parahaemolyticus].
ACCESSION   WP_011106323
VERSION     WP_011106323.1
KEYWORDS    RefSeq.
SOURCE      Vibrio parahaemolyticus
  ORGANISM  Vibrio parahaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 128)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 128)
  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 128)
  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 128)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Vibrio parahaemolyticus"
                     /db_xref="taxon:670"
     Protein         1..128
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14644
     Region          30..123
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(53,72..73,91,94,102..103,115,120)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 msdqatlsvl ptltsdcqdc ghsssadhvl tldkytqsvt iqsqpkktdi qltpiqfell
       61 rtliqhqdkv ltkpflyqtv lqrpftehdr aldmhisrmr krliaegmpp dqiqtihrkg
      121 ylfksinr
//
LOCUS       WP_011107149              99 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein
            [Bacteroidales].
ACCESSION   WP_011107149
VERSION     WP_011107149.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidales
  ORGANISM  Bacteroidales
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Bacteroidales"
                     /db_xref="taxon:171549"
     Protein         1..99
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11553
     Region          2..97
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mklienniqk iidlckkhkv hklfvfgsil tnrfndnsdi dlvvdfnkae vsdyfdnyfd
       61 fkyalenlfg revdlleeqt iknpylkknv datktliyg
//
LOCUS       WP_011108011             348 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Bacteroides].
ACCESSION   WP_011108011
VERSION     WP_011108011.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 348)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..348
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=39686
     Region          213..346
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mncidymnki sfgisiafcv lcsctsrtgq kssdetlqvd slaqdtiaet vaepvvkkit
       61 peeiqitkel lydkytledt ypykdttrsf qwekikeqla lleniqiqps qwailqnykn
      121 rngeaplvkn fkrnaygrva dtlgveryqs vplylltdtv tperygqdge ltrfiedgen
      181 fvkaepifte gewmipkkyv kvigdtvvfn kaifvdrhnq nitalertek gkwvvrsmnp
      241 sttglhrppy aqetplgmfv lqekkvkmif lkdgsketgg yapyasrftd gayihgvpvn
      301 eprktqieys wslgttprsh mcvrnatsha kfifdwapvn etiifvle
//
LOCUS       WP_011108237             265 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Bacteroides
            thetaiotaomicron].
ACCESSION   WP_011108237
VERSION     WP_011108237.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides thetaiotaomicron
  ORGANISM  Bacteroides thetaiotaomicron
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Bacteroides thetaiotaomicron"
                     /db_xref="taxon:818"
     Protein         1..265
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30181
     Region          19..127
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          191..265
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mvkskvifed eeqveikypc felkdiveyy feiytpnnsi tpfslvalpn anilvsiyis
       61 dssqtfkvhr ehgiidtsgd kisgslteai tvihapgthe fsikfkpgvl ysclskdist
      121 lvdnhlslqk ylnqkvidel klkssfaerv qfvenwllsn mkifssdfkl ntvikaiyhi
      181 nnnrnyklnt vskevgvsnp tlnryfkevl gispkqcfka lrfktalkny rangsydlyd
      241 elgytdfshf vkeaknlant tpsel
//
LOCUS       WP_011108532             686 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Bacteroides thetaiotaomicron].
ACCESSION   WP_011108532
VERSION     WP_011108532.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides thetaiotaomicron
  ORGANISM  Bacteroides thetaiotaomicron
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Bacteroides thetaiotaomicron"
                     /db_xref="taxon:818"
     Protein         1..686
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73986
     Region          4..686
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mittqllrpe sivvvgasnn vhkpggailk nlinggyqge lravnpkete vqgvpafadv
       61 kelpdtdlav lavpavmcpd ivetlasekq trafiilsag fgeethegal leerilesvn
      121 kygasligpn ciglmniwhh svfsqpipnl nskgvdliss sgatavfile savtkglqfn
      181 svwsvgnakq igvedvlqfm denfdlekds rikllyiesi hnpdrllfha sslirkgcki
      241 aaikagsses gsraasshtg aiassdsave alfrkagivr cfsreelttv gciftlpelk
      301 gknfaiitha ggpgvmltda lskgglnvpk legelaeelk aqlfpgasvg npidilatgt
      361 pdhlricidy ceekldnida ilaifgtpgl vtmfemydvl hekmqtchkp ifpvlpsint
      421 agaevaafla kghvnfsdev tlgtalsriv napkpavpei elfgvdvpri rriidsipen
      481 gyiephyvqa llhaagislv deyvsnkkee vvdfarrcgf pvvakvvgpv hksdvggvvl
      541 nikgeqhlal efdrmmqipd akaimvqpml kgtelfigak yeekfghvvl cglggifvev
      601 lkdvssglap lsyeeaysmi rslraykiiq gtrgqkgvne dkfaeiivrl stllrfatei
      661 kemdinplla tekaviavda ririek
//
LOCUS       WP_011110687             817 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: Lon protease family protein [Nitrosomonas].
ACCESSION   WP_011110687
VERSION     WP_011110687.1
KEYWORDS    RefSeq.
SOURCE      Nitrosomonas
  ORGANISM  Nitrosomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae.
REFERENCE   1  (residues 1 to 817)
  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 817)
  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 817)
  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   4  (residues 1 to 817)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Nitrosomonas"
                     /db_xref="taxon:914"
     Protein         1..817
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /function="InterPro IPR001092 COGs COG1067"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=91539
     Region          71..805
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mpitrlepca lgltidpdsl efpdtsalid qpldwigqer arqatyfgle mehpdynlfv
       61 lgetgsgrss llrqamaeva arkpaprdlc ymynfdvper plalhlpagk gswlrqqlaq
      121 svshllqeip erlsgddfkv etshiekrfk leetryfeel ntfaeslcfa lrresgrlvf
      181 tlldesgkpl teeeilalpk drraaldqde qvlrseiasy lqkirvleqs rdkelaalcw
      241 gwiepllgqv lnvvlegldq sfsdharlkn hldnikhdil enldlfqltd lseeknpedl
      301 kqlferyrin vvvdnrdlls apvvidenps fksligsigy qsvegvlvtd ftriragsll
      361 rahggflmlh lddllvdafl wekfcrllrn hllqieepwa vnvsapvvpi epeavkvdvr
      421 ivligsreqy yaiqeenpel arrfrvkvdf aaaftasiqa yralsvfiah icqqsclphf
      481 sreavasvlr tchraaedqk rlsanfshte mlvvesarqc ktrgnlvvea rdvttarrar
      541 ilrhnypdqc aqeaiadgdv vitvhderig qinglsliem gdhsfgipsr itahtfaged
      601 gllnierevg msgpihdkgv filqsflsal fhhnaplafn asivfeqeyy gvegdsasca
      661 elyallsals glpfrqgiav tgainqygem lpiggineki egffrvcata gldgtqgvli
      721 pdrncrhlml ddevvdavsk gvfhiyaish mreglellsg lpagisagtd lqeiinypqd
      781 tvlgyaqktl rvyrmacqqp sqrtktlhkr sgehidk
//
LOCUS       WP_011110798             214 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Nitrosomonas].
ACCESSION   WP_011110798
VERSION     WP_011110798.1
KEYWORDS    RefSeq.
SOURCE      Nitrosomonas
  ORGANISM  Nitrosomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae.
REFERENCE   1  (residues 1 to 214)
  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 214)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 214)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Nitrosomonas"
                     /db_xref="taxon:914"
     Protein         1..214
                     /product="YfgM family protein"
                     /function="InterPro IPR001687 COGs COG2976"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23257
     Region          3..209
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
ORIGIN      
        1 msaynfeeqe kieglkswwa angttmlfai avfaatvagn rlwnhykaeq aqqaadlyav
       61 lqqqvekgse lvkitdaahl ltegfpgsgy asraaliaar aagqagndqv ardmlqwald
      121 haeepeikdm arlrlasvlv deskydqalk lldaqhaasf tglyadlrgd alaaagktde
      181 araayqkald slnaqgayrn vvqmkldvlr eqrq
//
LOCUS       WP_011111877             759 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CHASE2 domain-containing protein [Nitrosomonas].
ACCESSION   WP_011111877
VERSION     WP_011111877.1
KEYWORDS    RefSeq.
SOURCE      Nitrosomonas
  ORGANISM  Nitrosomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae.
REFERENCE   1  (residues 1 to 759)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 759)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Nitrosomonas"
                     /db_xref="taxon:914"
     Protein         1..759
                     /product="CHASE2 domain-containing protein"
                     /EC_number="4.6.1.-"
                     /function="InterPro IPR001054 COGs COG2114"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016849 - phosphorus-oxygen lyase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=83605
     Region          8..704
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mklwrwrfal avfigllgaa vylspqgtai eeqfglywlf hlrgertapa dvvviavdqa
       61 sathlelplk pslwsralha rlidrlveag arvvvfdlvf drpgsdarhd kqfaaalkha
      121 gnvvlverld feetrfpgma adgsythilr eytgkilpii adaarahapf plqksswvsy
      181 ywtfrpggsd mptlpslllq lssaevyehf ltllagidpa lirqlpasvn eadvenlvld
      241 lrnlfmqkpv laekllqksa egenldtaqq rilralidly ggsevrylnf ygpprtirti
      301 pyhllldegg gqpetageld lagktifvgf saetvsgqdk vrddyqtvfs lpdgltlsgv
      361 eiaatafanl legesihpaa pvngalilll lgtgvcllcf viparntmvh tlgmalagil
      421 sfcaygsasv wlfgqwqlwi plaiplmvql pvgvigivtl lyfeadrerr riealfgghr
      481 pepvvrdmvr gagpihtegq lvygaclatd aekytalaea mdprqlaalm hayyeclfep
      541 veryqgkvsd vigdamlaiw aagsadplvr eraclacldi isaierfnhq ggygrpplpt
      601 rlglhfgemv lgnigarqhy eyravgdivn tanriqgvnk hlgtrllvse evvnglndll
      661 lrplgrfllp gksqpvnlfe lvarqsgsna aqrqlcaaye qalhvcqtgn rvdalhrfem
      721 iherfpedgp trfmltycre prlfpvreag eliisiqsk
//
LOCUS       WP_011112298             139 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Nitrosomonas].
ACCESSION   WP_011112298
VERSION     WP_011112298.1
KEYWORDS    RefSeq.
SOURCE      Nitrosomonas
  ORGANISM  Nitrosomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Nitrosomonas"
                     /db_xref="taxon:914"
     Protein         1..139
                     /product="type IV pilin protein"
                     /function="InterPro IPR001082:IPR001120 COGs COG2165"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15099
     Region          3..137
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 msrtrtytgn sgftlievmv vvaivgilaa iaypsyqehv rranraearg illemaqlle
       61 rnyteannye nfvlpvsqsp rtgtarytvq fsadtltrnt ytleavpegs magdacgtlt
      121 ltqtgvrgsd gvvaecwqr
//
LOCUS       WP_011112823             431 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: amidohydrolase family protein [Nitrosomonas].
ACCESSION   WP_011112823
VERSION     WP_011112823.1
KEYWORDS    RefSeq.
SOURCE      Nitrosomonas
  ORGANISM  Nitrosomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae.
REFERENCE   1  (residues 1 to 431)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Nitrosomonas"
                     /db_xref="taxon:914"
     Protein         1..431
                     /product="amidohydrolase family protein"
                     /EC_number="3.5.-.-"
                     /function="COGs COG1228"
                     /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=45963
     Region          44..425
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mriqnftdtl snrmrhmccf cvavitglcf saqvyaqetg ktgpsslllh aarvfdgnem
       61 hsglsvlvkd griarvgprh sfrtgdasad idlgdatllp gfielhahla fqkvpadivl
      121 rhgvttlrdv ggpvhppygg egslrvltsg riitaphgyp ivtmgardla ipvaseaear
      181 eavrhlvgeg aviikialep gseagapwss hhdhahhdaa htasavthhh ahaashdqsa
      241 wpmlpepivk avvdeahrhq rkvsahvaep sgvqvalnag vdewahmpcn pipepllkqa
      301 raqnvtiigt ldtlskcsgi ahntmvwtel ggellygtei ahpdipwgid aqelmylmhl
      361 gkmklldalg aatakagryl gipmlgtiqp gapadliair gnpeqqlkrl eypdlvisgg
      421 hivvnhfssl p
//
LOCUS       WP_011113136             289 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AfsR/SARP family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_011113136
VERSION     WP_011113136.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            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="AfsR/SARP family transcriptional regulator"
                     /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=31482
     Region          3..255
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mniqvlgala aqvngmsitp tapkprqvla llalhaghmv pvaalteelw genpprsart
       61 tlqtyvlqlr dligaalarr adggavsakd vlvtlpggyr ldtrdglldf referragag
      121 yramdagdhe daarrlreal slwhgaalad vqaggqiame vrrleearlc aldqrieadl
      181 rlgrhrells eltvlvnryr mheslhgqfm valyrsgrrg ealsvyrrlh tamvrelgle
      241 pspalgrlqr silsahpepa atgpvdvpag hpardlhraq trhlaghal
//
LOCUS       WP_011115020             144 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Helicobacter hepaticus].
ACCESSION   WP_011115020
VERSION     WP_011115020.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter hepaticus
  ORGANISM  Helicobacter hepaticus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Helicobacter hepaticus"
                     /db_xref="taxon:32025"
     Protein         1..144
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16051
     Region          6..144
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mveyyeyglv glfficfias tlyplgseaf vigfvafgfe plkvwiiasv gntlgslsty
       61 ylayyggepf itrffpkakd kiailaprvr vygfiyaflv fmpfvgdifa lvlgiirysq
      121 ilsilgiafg kmlryavlll pfvl
//
LOCUS       WP_011113156             276 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AfsR/SARP family transcriptional regulator
            [Streptomyces].
ACCESSION   WP_011113156
VERSION     WP_011113156.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Novakova,R., Rehakova,A., Kutas,P., Feckova,L. and Kormanec,J.
  TITLE     The role of two SARP family transcriptional regulators in
            regulation of the auricin gene cluster in Streptomyces aureofaciens
            CCM 3239
  JOURNAL   Microbiology (Reading) 157 (Pt 6), 1629-1639 (2011)
   PUBMED   21393365
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Tanaka,A., Takano,Y., Ohnishi,Y. and Horinouchi,S.
  TITLE     AfsR recruits RNA polymerase to the afsS promoter: a model for
            transcriptional activation by SARPs
  JOURNAL   J Mol Biol 369 (2), 322-333 (2007)
   PUBMED   17434533
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Umeyama,T., Lee,P.C., Ueda,K. and Horinouchi,S.
  TITLE     An AfsK/AfsR system involved in the response of aerial mycelium
            formation to glucose in Streptomyces griseus
  JOURNAL   Microbiology (Reading) 145 (Pt 9), 2281-2292 (1999)
   PUBMED   10517581
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Horinouchi,S., Kito,M., Nishiyama,M., Furuya,K., Hong,S.K.,
            Miyake,K. and Beppu,T.
  TITLE     Primary structure of AfsR, a global regulatory protein for
            secondary metabolite formation in Streptomyces coelicolor A3(2)
  JOURNAL   Gene 95 (1), 49-56 (1990)
   PUBMED   2253887
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..276
                     /product="AfsR/SARP family transcriptional regulator"
                     /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=30682
     Region          1..254
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
ORIGIN      
        1 mdidvlgtla vkendvsvtp rapkprqvla llalhadqvv piaslidelw gdrpprsart
       61 tlqtyilqlr emiakaleqd pqdapprtpk dvlatapggy vlhtfggtsd vreferlagl
      121 gyramdaadf praarelgea lalwtdsalc dvqagpqlem qarrleetrl caldqriead
      181 lrlgrhrell gelsvlvsry rthenlhaqf mlalhrsgrr sealdvyhrl rstlvretgl
      241 epsagvrrlq qsmlmahpep vaaqpvaere rlhrvg
//
LOCUS       WP_011116850             222 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Streptomyces violaceoruber].
ACCESSION   WP_011116850
VERSION     WP_011116850.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces violaceoruber
  ORGANISM  Streptomyces violaceoruber
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            violaceoruber group.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Streptomyces violaceoruber"
                     /db_xref="taxon:1935"
     Protein         1..222
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=23786
     Region          <104..207
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mrilatvaat aaavaalitp ahadgplgvk gdtltlplad aitalpvaee sragyqrsaf
       61 khwvdadkdg cntrsevlka eavvapeqgt rcklsggqwy saysntyvns asaldldhlv
      121 plaegwdsga sawtakerea yandlgddrs liavtaatnr skadqdpaew lppyepyhcq
      181 yltdwiatkl rwqltvdqae rdtltqatts cpnlpvevtl ar
//
LOCUS       WP_011117877             753 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Rhodopirellula
            baltica].
ACCESSION   WP_011117877
VERSION     WP_011117877.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula baltica
  ORGANISM  Rhodopirellula baltica
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 753)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 753)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Rhodopirellula baltica"
                     /db_xref="taxon:265606"
     Protein         1..753
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /function="nitrogen and sulphur utilization"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=83773
     Region          59..747
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 msisikdnrn dagktfqlpt llqrrtgpmt relvlrpgdh glgmthdsma adttttatcg
       61 fcatgcglrl hlkdgeaigl tpetaypvnl gmacpkgwea lrvldspera tlpllrdetg
      121 klspiewdda fskfcdgmkq vqsehgpesi aflstgqiac eemaflgala rfgmdirhcd
      181 gntrqcmata vtaykesfgf dsppytyddf eqsdclvfig anpcvghpim wervlrnphn
      241 peiividprr tetaaaatqh lqlrpkndla llyaitneli lrdfvehdfv qnhtqgfeel
      301 rqhvsqydla tvceeaglav edvsaaveai grgravslww tmgvnqsyqg trtaqaiini
      361 alitgnigrp gtgansitgq cnamgsrlws nttnlfghhs fteesdrrkv aealnipvek
      421 ipsttswkyd riiegirnge ikglwvvatn pahswidqgd vrelfdqldf lvvqdmyktt
      481 etcshadlil psagwgekeg tfinserryg llkkvrhapg qaladfqifr giahrwgvge
      541 mfaewtspea vfqimqrasr gqpsdisgie gyeqidrcgg iqwpwsadha sggfepeqqr
      601 rlfadgrffh edrrarlivd dvspmpepag edypivlltg rgtvsqwhtq trtrqspllr
      661 slypnqpyve mhprdaaeld vehgdlvrvr srrghadata clthsvqpgq vfmpmhyect
      721 nqltlshfdp hsgqpsykdc avriepvlts dhd
//
LOCUS       WP_011119018             222 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Rhodopirellula baltica].
ACCESSION   WP_011119018
VERSION     WP_011119018.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula baltica
  ORGANISM  Rhodopirellula baltica
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Rhodopirellula baltica"
                     /db_xref="taxon:265606"
     Protein         1..222
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /function="biosynthesis of vitamins, cofactors, and
                     prosthetic groups"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=24207
     Region          8..221
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 msdatkrrrr ivlamtgasg apiavrllqv mrrdpsvevh ltispsgaav lhqemglqln
       61 lrspdlnall acvpqwasep apefdeigpt gderlhyhqh ddymtpiasg sfltdamvlc
      121 pcsgstlsgi arsaasnlvq raaevhlkeh rklvvvpret pmsvlqienm qrlaaagavl
      181 lpampgwyhd vkriedlvdf vvarildqig ldngliqrwk da
//
LOCUS       WP_011121747             259 aa            linear   BCT 20-JAN-2025
DEFINITION  hydroxypyruvate isomerase family protein [Rhodopirellula baltica].
ACCESSION   WP_011121747
VERSION     WP_011121747.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula baltica
  ORGANISM  Rhodopirellula baltica
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 259)
  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 259)
  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 11466508
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Rhodopirellula baltica"
                     /db_xref="taxon:265606"
     Protein         1..259
                     /product="hydroxypyruvate isomerase family protein"
                     /EC_number="5.3.1.-"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28098
     Region          24..257
                     /region_name="Hyi"
                     /note="Hydroxypyruvate/dehydroerythronate isomerase,
                     Hyi/OtnI family [Carbohydrate transport and metabolism];
                     COG3622"
                     /db_xref="CDD:442840"
ORIGIN      
        1 mnsparlkas vcvdavlenl stvdamklva dcgypafefw kwwdkdldsi nqareelqlq
       61 vaavctkfvs lvdpdvraey laglkesiaa agslncpvli sqvgdarpgv draeqrdcli
      121 aglkeaapml edsgvvlaie plnelidhag yylvrsdeaf siiqevdspn vkvtfdiyhq
      181 qiseghvian ltqnvdaiah fhaagnpgrh eldrgelhyp sifaaiadtg ysghvgleyw
      241 pvneaaaglr eaaswikkv
//
LOCUS       WP_011127299             244 aa            linear   BCT 20-JAN-2025
DEFINITION  3-deoxy-manno-octulosonate cytidylyltransferase [Parasynechococcus
            marenigrum].
ACCESSION   WP_011127299
VERSION     WP_011127299.1
KEYWORDS    RefSeq.
SOURCE      Parasynechococcus marenigrum
  ORGANISM  Parasynechococcus marenigrum
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Prochlorococcaceae; Parasynechococcus.
REFERENCE   1  (residues 1 to 244)
  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 244)
  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 10793788
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Parasynechococcus marenigrum"
                     /db_xref="taxon:2881428"
     Protein         1..244
                     /product="3-deoxy-manno-octulosonate cytidylyltransferase"
                     /EC_number="2.7.7.38"
                     /GO_function="GO:0008690 - 3-deoxy-manno-octulosonate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0009103 - lipopolysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0033468 -
                     CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27549
     Region          1..240
                     /region_name="PRK13368"
                     /note="3-deoxy-manno-octulosonate cytidylyltransferase;
                     Provisional"
                     /db_xref="CDD:184007"
     Site            order(8..10,49,76,96,98)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133010"
     Site            order(137,143..145,151..152,154..160,170,196..197,
                     200..202,209..212)
                     /site_type="active"
                     /note="oligomer interface [active]"
                     /db_xref="CDD:133010"
ORIGIN      
        1 mkvcvvipar ysssrfpgkp lvnllykpmi iwvadiaara vgiehvyvat ddtriadavt
       61 sygykfiets phaltgtdrv aeaskqidyd iyinvqgdep tidhleilkc iqlkkenfdc
      121 vvngyctist nsnpssknip kvvkteknrl vymsrslvpg fkdlnimpke ylkqvciygf
      181 sfeelqlfsn ygrkslleqs edieilrfld lgkqvlmyqc akeslavdvp sdiqivedyl
      241 qpnk
//
LOCUS       WP_011128106             215 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Parasynechococcus marenigrum].
ACCESSION   WP_011128106
VERSION     WP_011128106.1
KEYWORDS    RefSeq.
SOURCE      Parasynechococcus marenigrum
  ORGANISM  Parasynechococcus marenigrum
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Prochlorococcaceae; Parasynechococcus.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Parasynechococcus marenigrum"
                     /db_xref="taxon:2881428"
     Protein         1..215
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22922
     Region          21..211
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mshplrsvla dvgpdscpgs fnfhchtics dgslepleli rqaserglsh lavtdhhsar
       61 afqpmadwlq aqrdagavvp tlwtgmeisc llkgclvhvl algfepghaa lepynrgdsv
      121 vgealradav vkaihtaggl avlahparyr lghdvlidea arlgfdggea wydydmqtvw
      181 apspmiceai drqlanlgll rtcgtdshgi dlggr
//
LOCUS       WP_011128542             112 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Parasynechococcus marenigrum].
ACCESSION   WP_011128542
VERSION     WP_011128542.1
KEYWORDS    RefSeq.
SOURCE      Parasynechococcus marenigrum
  ORGANISM  Parasynechococcus marenigrum
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Prochlorococcaceae; Parasynechococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Parasynechococcus marenigrum"
                     /db_xref="taxon:2881428"
     Protein         1..112
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12378
     Region          6..107
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(7..8,26..27,35,38,40..41,43,46..47,49,57,62,71)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(26,57..58,60,87)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mgdrisfdss vwdavsriph grlatygqia dligaygcar qvgwalrrlp lpsnvpwhrv
       61 vnaqgrisms lsregsdwiq relllaegvp vdeegrlplk erlwrpdams gs
//
LOCUS       WP_011129648             133 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Prochlorococcus marinus].
ACCESSION   WP_011129648
VERSION     WP_011129648.1
KEYWORDS    RefSeq.
SOURCE      Prochlorococcus marinus
  ORGANISM  Prochlorococcus marinus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Prochlorococcaceae; Prochlorococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Prochlorococcus marinus"
                     /db_xref="taxon:1219"
     Protein         1..133
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=14696
     Region          1..105
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(6..7,25..26,34,37,39..40,42,45..46,48,56,61,70)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(25,56..57,59,86)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mgqasfdlrv wdavslipfg qlatygqiae migaygcarq vgwamrrlpl pskvpwhrvv
       61 nakgmismsl sregsdwmqr qmliaegilv daeghlplrr hlwrpqlsde gllpgmaqeg
      121 vssgrfisvq dnh
//
LOCUS       WP_011131244             257 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Prochlorococcus marinus].
ACCESSION   WP_011131244
VERSION     WP_011131244.1
KEYWORDS    RefSeq.
SOURCE      Prochlorococcus marinus
  ORGANISM  Prochlorococcus marinus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Prochlorococcaceae; Prochlorococcus.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Prochlorococcus marinus"
                     /db_xref="taxon:1219"
     Protein         1..257
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27023
     Region          19..256
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mlvdgnyykk ggsteielgg taggwwkfae fdrieitgdl elagdlrvla inyfqlsagd
       61 sfvitrvdgd ldgqydglne gdsvgsfesd nsgilelfit ykggdgndie lytesvsgvl
      121 peslreprii gsaaddsltg tsadevifgg sgddvllggg gdnqvtggng ddrlyggfgd
      181 dilkgdrgad tyrlsrgndv iiafslaend risvadgvdl sfkqvgddll itadgihttl
      241 kdvdkgefla advidfi
//
LOCUS       WP_011130090             312 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Prochlorococcus marinus].
ACCESSION   WP_011130090
VERSION     WP_011130090.1
KEYWORDS    RefSeq.
SOURCE      Prochlorococcus marinus
  ORGANISM  Prochlorococcus marinus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Prochlorococcaceae; Prochlorococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Prochlorococcus marinus"
                     /db_xref="taxon:1219"
     Protein         1..312
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=35611
     Region          117..303
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 masdylttli msirsktkrf liiiifsisg liiftrytkn sipddqskln qslqsrlerl
       61 vqvseednqk sndlpstsqq kppralswss plskqcsdid qglkkrlnhr qqqlaterny
      121 vvidssnygk ryrwdlygrr vdptpsvvil hettdsyqsa lyafkdyhrk dedqvsyhtl
      181 itldgqiidv vdplnrayga gnsaflgewv vtnprfkgsv nnfalhlsle tpwdgrngyl
      241 nhsgysdkqy dslalvladw mdrfnippen itthqhvdla gersdprsfd wsnlqrrlaa
      301 igylcvssnp sd
//
LOCUS       WP_011133612             489 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Chromobacterium violaceum].
ACCESSION   WP_011133612
VERSION     WP_011133612.1
KEYWORDS    RefSeq.
SOURCE      Chromobacterium violaceum
  ORGANISM  Chromobacterium violaceum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Chromobacterium.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 489)
  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 489)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Chromobacterium violaceum"
                     /db_xref="taxon:536"
     Protein         1..489
                     /product="M4 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=52845
     Region          12..489
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mrkeqlmlrg lvlsalavfs satmaaerid lekqgkaqan sasaftgvsq gdlkalrstq
       61 fasgkvvtry qqyyqgvpvw gegvveekpa aalksvqgkl sghyiagiqa dlasakptls
      121 saqvlsqaka lkangnptyn dkaelvvrln ernvaqlvyl vsfvvdgkep srphliidan
      181 sgqvlkqweg lnhaeangpg gnaktgqyyy gkdygplivt sdckmdsgnv atvnlnggts
      241 gstpykfacp tntykainga ysplndahyf gnvvfnlykd wfnlkpitqk llmkvhysrn
      301 yenafwdgta mtfgdgyntf yplvsldvsa hevshgfteq nsglvysgqs ggineafsdm
      361 ageaaeyymk gkndflvgae ifkktgalry fadptkdgqs ignakdyyng ldvhyssgvy
      421 nkafyliats pnwntrkafe vfvdanrlyw nanatynsaa cgvvkaadar gynsadvtka
      481 faavgvtcq
//
LOCUS       WP_011134038             135 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Chromobacterium violaceum].
ACCESSION   WP_011134038
VERSION     WP_011134038.1
KEYWORDS    RefSeq.
SOURCE      Chromobacterium violaceum
  ORGANISM  Chromobacterium violaceum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Chromobacterium.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Chromobacterium violaceum"
                     /db_xref="taxon:536"
     Protein         1..135
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14106
     Region          1..133
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mrgvtlvelm itlavvailg tiaypmytgy aqrsrrsdaw qalttaqaqm eqcysqyfay
       61 nnaactvtta spngyyqvqi assttasayt ltatpvssgl qaadtscgsf svgstgirsa
      121 qnaqgadtss tcwph
//
LOCUS       WP_011136438             348 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Chromobacterium violaceum].
ACCESSION   WP_011136438
VERSION     WP_011136438.1
KEYWORDS    RefSeq.
SOURCE      Chromobacterium violaceum
  ORGANISM  Chromobacterium violaceum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Chromobacterium.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Chromobacterium violaceum"
                     /db_xref="taxon:536"
     Protein         1..348
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=37765
     Region          89..321
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 mrlgrklgvw lsrravgaga apvyalavaa calpalfllw rlgaasfdpp dwrgwaiase
       61 igllaalvga mlagwlrrga glrgaggwei segmrsqaff ahyqpivtgt rgecvgvevl
      121 arwrhpvrgn vradlfipea veaglivplt ryllkrvcde lrkvalppdf mvgvniageh
      181 lalpelvqdc remvdmlrak qatlvleise qvplseasga lgvirrlkre gvklalddfg
      241 sgyadvaylr rwgfdylkve kglvstlewd alrgggrdgv lssgepgvrv ivkgvetsgq
      301 qsdlsgkgfe llqgfyfgkp mtlnhfrqwl ysgiiqdrst agvrprds
//
LOCUS       WP_011137292             383 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Chromobacterium violaceum].
ACCESSION   WP_011137292
VERSION     WP_011137292.1
KEYWORDS    RefSeq.
SOURCE      Chromobacterium violaceum
  ORGANISM  Chromobacterium violaceum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Chromobacterium.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 383)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Chromobacterium violaceum"
                     /db_xref="taxon:536"
     Protein         1..383
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=41049
     Region          6..383
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mnrcllaina gsatlkfraf spdgrtllar gmvdrfgske arlrladakg qalaerdlad
       61 aahaaalaav lnsladqgle aqalvhrvvh ggsrfrepvr idaevraald dyialaplhq
      121 pvslevvdaf seldprlpqi acfdtafhat qptvatrfgi arhwhdegvr rygfhglsya
      181 aisrrlpelg lahgkvvvch lgsgasacai esgksvassm gfsavdglmm gsrpgyidpe
      241 vilywqeheg mgvkdvrrel yknsgllgvs gvsadmrell asdlpearea velfcyraar
      301 eaaslaaamr gldglvftag igehsaevra rilqqlswlg fdldhaanla harrltaags
      361 rlpayvlptd eegemarqaa rll
//
LOCUS       WP_011137378             105 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Chromobacterium violaceum].
ACCESSION   WP_011137378
VERSION     WP_011137378.1
KEYWORDS    RefSeq.
SOURCE      Chromobacterium violaceum
  ORGANISM  Chromobacterium violaceum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Chromobacterium.
REFERENCE   1  (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   2  (residues 1 to 105)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Chromobacterium violaceum"
                     /db_xref="taxon:536"
     Protein         1..105
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10679
     Region          20..81
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkklfavfaa llllcnvawa avnlntatpq qlealkgigp akakaivdyr tkngpfktvd
       61 dlkkvsgigd ktleslrkev tvggaavpaa kpaaakpaaa kpaak
//
LOCUS       WP_011137755             155 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Chromobacterium violaceum].
ACCESSION   WP_011137755
VERSION     WP_011137755.1
KEYWORDS    RefSeq.
SOURCE      Chromobacterium violaceum
  ORGANISM  Chromobacterium violaceum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Chromobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Chromobacterium violaceum"
                     /db_xref="taxon:536"
     Protein         1..155
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=16031
     Region          1..131
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkkqrkqqgf tlielmivva ivgilaaiai payqdytkra rvseglalad aaktavteyy
       61 atnnawasgt apfnttygla asitgnsvss invlangvvq iaynstvsng alvdlvptvs
      121 agsvqwycty tgsgttaias asqlsanwvp stcrq
//
LOCUS       WP_011138319             167 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Wolinella succinogenes].
ACCESSION   WP_011138319
VERSION     WP_011138319.1
KEYWORDS    RefSeq.
SOURCE      Wolinella succinogenes
  ORGANISM  Wolinella succinogenes
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Wolinella.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Wolinella succinogenes"
                     /db_xref="taxon:844"
     Protein         1..167
                     /product="TRAP transporter small permease subunit"
                     /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=19193
     Region          1..164
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mekisyacdk ltqwmgkasa flafalvflv lydalsrylf kmgsvslqel ewhlfalmfl
       61 lgipyalkhd khvrldlfyq hyskrskrvl wilcnllfvl pfcafviwhg ydfalmsylq
      121 nessdsgglp yrfliksapl lafflvalqa lsevikasil lrkessc
//
LOCUS       WP_011138342              76 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Wolinella succinogenes].
ACCESSION   WP_011138342
VERSION     WP_011138342.1
KEYWORDS    RefSeq.
SOURCE      Wolinella succinogenes
  ORGANISM  Wolinella succinogenes
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Wolinella.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 76)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 76)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 76)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Wolinella succinogenes"
                     /db_xref="taxon:844"
     Protein         1..76
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8458
     Region          2..76
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mritvrlfaq yregffkeev refplettvq evieslgirv dlypigimvl ngrhasleti
       61 lhegdvlglf pkvggg
//
LOCUS       WP_011138716             522 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Wolinella succinogenes].
ACCESSION   WP_011138716
VERSION     WP_011138716.1
KEYWORDS    RefSeq.
SOURCE      Wolinella succinogenes
  ORGANISM  Wolinella succinogenes
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Wolinella.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 522)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Wolinella succinogenes"
                     /db_xref="taxon:844"
     Protein         1..522
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=59697
     Region          <120..513
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 menlrilfvq fssssltipl qvdfpllvvt dsfekalewc eesafevvvi egesgesllp
       61 flrgvrqrss ltrflflsph pfpsmlseia qagiegffhe ipdpfrvrqa lsliaktffr
      121 sadhakeksr liqaiakedd rvmmlievdh ldnyhtvfsl afidailqev gdflehykpd
      181 gseifsisee kyailmeden tfraedfati lnvlildrki yvkkqevdvs fsvgvakgrg
      241 etllskayaa lrkakesgrk hvvlaeddee frffqrenlr wmrgvrhale edrivpyyqp
      301 iinnatgkie kyeclarlid hevvvppaif lqsarqiglm snvtfaiink sltlfqnndm
      361 elsiniaeed irdakiiryl lnrcerygid psrivieile ditfgrnnks lehmrylhqe
      421 gfkiaiddfg fensnfgrli dmevdyikid gsfvknmetd drsykivdsi akfcksigak
      481 siaeyvhsqg vqervlalgi dysqgyffgk atpkplegds li
//
LOCUS       WP_011142863             299 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Gloeobacter violaceus].
ACCESSION   WP_011142863
VERSION     WP_011142863.1
KEYWORDS    RefSeq.
SOURCE      Gloeobacter violaceus
  ORGANISM  Gloeobacter violaceus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Gloeobacterales; Gloeobacteraceae; Gloeobacter.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Gloeobacter violaceus"
                     /db_xref="taxon:33072"
     Protein         1..299
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32714
     Region          18..258
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 metaapsptv lvnararlge gpcwhqptrs lywvdiynhr ihhydpdtgt drffdagevv
       61 gcvapagenr lilarrhdla fldiidstvt plldveaprp gvrfndgkcd aagrfwfgsm
      121 dpaggegrly rydpdgalhl metgifvsng lgwspdnrtf yltdssqqti yaydfdfesg
      181 rivnrrpcvd lsgapffpdg ltvdregclw samwdgwcvi rfapdghell rlplpvqrpt
      241 cctfggadlg tlyitsasvg lseaqieksf hsgdvfsvqg lavglpthgf agshnvksl
//
LOCUS       WP_011141570             692 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Gloeobacter
            violaceus].
ACCESSION   WP_011141570
VERSION     WP_011141570.1
KEYWORDS    RefSeq.
SOURCE      Gloeobacter violaceus
  ORGANISM  Gloeobacter violaceus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Gloeobacterales; Gloeobacteraceae; Gloeobacter.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 692)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Gloeobacter violaceus"
                     /db_xref="taxon:33072"
     Protein         1..692
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=75402
     Region          4..691
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 mptdtlaktl cpycgvgcgl evtadarvrg drahpstlgm vcvkgatvle sigkdrllyp
       61 mvrarldepf rqasweeala lvvgrlraas peslcfygsg qfvtedyyva qklfkgclgs
      121 nhidansrlc mssavsgylq slgsdgppac yddldltdca flvgtntaec hpvlfnrllk
      181 hrkqdlnsrl vvvdpratpt akaadlhlai rpgsdidlfn giahlilqwd radqrfigah
      241 tqgfaamaev vrhyppeava rrcgittaal elaarlwvns arvlslwsmg inqsiegtak
      301 vralinlhll taqigrpgsg pfsltgqpna mggreaggls qllpgyrsva dpdhrrqvee
      361 hwqlpsgsia arpgrtawem iealeagave vfwiaatnpa vslpdlertk aallrspftv
      421 yqdcyyptet aryahvllpa tqwsektgtm tnserrvtlc pafhpppgea rddwqifaev
      481 grrlgfaeqf afadaaavfa efaaltrgrp cemtgishar leregplqwp cpagsagtar
      541 lytdwrfatp dararfaach arglaeppdp eypfvlingr lyghwhtltr tgriekllnl
      601 ypepfieihp rdagklglge gdwvevrsrr gairlparlt lavapgtvfv pmhwgalwae
      661 aaevnalthp esdpisgqpe vkscavqlsa lp
//
LOCUS       WP_011137940             309 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Chromobacterium violaceum].
ACCESSION   WP_011137940
VERSION     WP_011137940.1
KEYWORDS    RefSeq.
SOURCE      Chromobacterium violaceum
  ORGANISM  Chromobacterium violaceum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Chromobacterium.
REFERENCE   1  (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   2  (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   3  (residues 1 to 309)
  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   4  (residues 1 to 309)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Chromobacterium violaceum"
                     /db_xref="taxon:536"
     Protein         1..309
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=33335
     Region          1..309
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mieianvska fhgapavsdl sltvadgefa vlvgtsgsgk stmlkmlnrl lapdsgeiri
       61 agrdiraqpp eqlrrhigya iqsvglfphw tveqniaavp qllkwprpri qarvdellal
      121 lrlpdglrrr yphqlsggqq qrvgvarala adpdlllmde pfgaldpvtr anlqqelari
      181 hrlsgktiil vthdideall lgqriavmdq griqqqgspr dillhpandf vrgffqpdea
      241 gvrllglqrv aermrpgera agpplradat lrealsafiv qgaaalpvid aagaevgalr
      301 fedllgaaa
//
LOCUS       WP_011143163             445 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Gloeobacter violaceus].
ACCESSION   WP_011143163
VERSION     WP_011143163.1
KEYWORDS    RefSeq.
SOURCE      Gloeobacter violaceus
  ORGANISM  Gloeobacter violaceus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Gloeobacterales; Gloeobacteraceae; Gloeobacter.
REFERENCE   1  (residues 1 to 445)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Gloeobacter violaceus"
                     /db_xref="taxon:33072"
     Protein         1..445
                     /product="amidohydrolase family protein"
                     /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=49021
     Region          28..426
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mdkavlpwgr wllgpllglv lasgpvaaqg pdqnyafvgg rwfngrgfek ktvyavggrf
       61 tferpakvds tvdlqnryvv ppfgeahthr lsdpreveag iadylrdgif yakipndipl
      121 ssaaarerln rpdsvdavya hggltatggh pmrlyaflaq skyieitepk kldgqayhvv
      181 dseadlerkw pqilagkpdf iktyllysee fnkrkddkry fgakgldprl lgrivekahr
      241 aglqvvthie taadfrsava agvdeiahlp gywfgppewp mppaafeltr edaqlarrnn
      301 vavvtttlvt dglvkdkaqa eqiqavqkrn lrllkeagvp lvigsdafga tslqealkln
      361 tlgsfdrlel lkslcestpq nifprrkigv iaegyeasfl vleadplvdf gnvkkiarrf
      421 kqgrwvelsa aggekrseaa pshah
//
LOCUS       WP_011141164             113 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Gloeobacter violaceus].
ACCESSION   WP_011141164
VERSION     WP_011141164.1
KEYWORDS    RefSeq.
SOURCE      Gloeobacter violaceus
  ORGANISM  Gloeobacter violaceus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Gloeobacterales; Gloeobacteraceae; Gloeobacter.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Gloeobacter violaceus"
                     /db_xref="taxon:33072"
     Protein         1..113
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12771
     Region          18..113
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mngelrsist edtsliprrq gvleclrchw peiqsygvkt iavfgstard earpdsdvdl
       61 lvefeadarv tfyqfcdlqd ylesilrirv dlgtfdslrp rtaakilkea vyv
//
LOCUS       WP_011147652             455 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: replicative DNA helicase [Photorhabdus].
ACCESSION   WP_011147652
VERSION     WP_011147652.1
KEYWORDS    RefSeq.
SOURCE      Photorhabdus
  ORGANISM  Photorhabdus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Photorhabdus"
                     /db_xref="taxon:29487"
     Protein         1..455
                     /product="replicative DNA helicase"
                     /EC_number="3.6.4.12"
                     /function="Unknown"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=50540
     Region          4..425
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mnelnlesav isgllsggat qdaydvfatl seeafsssfl rrvyveikkq afssslidpi
       61 fiaeamsedg ntlanilels kspvwnanlk gyankvseyw yvrrvtavin agqqalletk
      121 nhtqaqhvit gfmstmgeli rdtgnlapvh iktliegyid ilgrrnlged srgmimtgie
      181 pfdsltggfn ptdliliggr pgmgktelal cmiegmtrng gavllfsmem aaqqiteriv
      241 agsaqlsvsk lrrgefyded warisnaise lidrdihild aselsaeqic aisethkrry
      301 pnlkgifvdy lglierpkae rndlaiaqis ralkglakrl htpvtalsql srdvdkrpih
      361 qrrpvaadlr dsgsleqdad riiftyrdvv ynplsparny aeiildknrh getgtifqef
      421 knghylptdq ivaaeicrtq qqakqkerry adkaf
//
LOCUS       WP_011148003             124 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Photorhabdus].
ACCESSION   WP_011148003
VERSION     WP_011148003.1
KEYWORDS    RefSeq.
SOURCE      Photorhabdus
  ORGANISM  Photorhabdus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
REFERENCE   1  (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   2  (residues 1 to 124)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Photorhabdus"
                     /db_xref="taxon:29487"
     Protein         1..124
                     /product="ComEA family DNA-binding protein"
                     /function="Unknown"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13181
     Region          53..123
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mkksgilsvl lagllyacgg qfaiaaeqvk dkvakaastt shsspekqlq qqdalkveek
       61 gkvnintasa eelaralngi gvkkaqgive yrekhgafta veqlqevqgi gpvfiernrs
      121 klsy
//
LOCUS       WP_011147654             250 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Photorhabdus].
ACCESSION   WP_011147654
VERSION     WP_011147654.1
KEYWORDS    RefSeq.
SOURCE      Photorhabdus
  ORGANISM  Photorhabdus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
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   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 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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Photorhabdus"
                     /db_xref="taxon:29487"
     Protein         1..250
                     /product="helix-turn-helix domain-containing protein"
                     /function="Unknown"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=27605
     Region          20..67
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msmslmvkam sikvgnplrk lvlikladna ndqgecwpsv ayiaeqceis ersvqnhikq
       61 lvkdgivcva erktqnglnq snvyflnldk sshgysenva pygaslapsg ansagvsgag
      121 daprtshpfe pvtepktplt prkgkreklk fdpitakpkn vsdevwadwv tfrleikkpl
      181 tetmckqqek kladctnpds victsiangw qglfpeksqn ikpkftqnth tsyegityep
      241 qdsywsenid
//
LOCUS       WP_011149420             360 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Vibrio vulnificus].
ACCESSION   WP_011149420
VERSION     WP_011149420.1
KEYWORDS    RefSeq.
SOURCE      Vibrio vulnificus
  ORGANISM  Vibrio vulnificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 360)
  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 360)
  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 360)
  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 360)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Vibrio vulnificus"
                     /db_xref="taxon:672"
     Protein         1..360
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40386
     Region          8..356
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mptikpnrsf lkraiiasta llsfslfaae evhrlklaet wgpntpilgd asknmaklae
       61 emsngrlqir idsankhkap lgvfdmvksg qydlghsssy ywkgkvpntl yfssmpfgmi
      121 tteqyawfyy gggmelmqkv yaphnllsfp ggnsdiqmgg wfkkeinsve dlkglkmrip
      181 gfagevlarv gakptniapg elytslergt idalewvgpa fdlrmgfhki apyyytawhe
      241 pgsetqflvn kktwerlpkd lqviletafr vaafdmynqa idananswat mqseypdikv
      301 rdfppvvlqa mrqatnelle eeaakdplak eiitsqenyl kkvrawtais skayldtnpq
//
LOCUS       WP_011151815             342 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Vibrio].
ACCESSION   WP_011151815
VERSION     WP_011151815.1
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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..342
                     /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=38697
     Region          1..277
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mstrtewvdy akaigiilvv fghvnrgiyd agfglpesih svvdsviysf hmplffflsg
       61 lfcmesfrkr ggtgvlkaki dtliypyllw sllqgsievg lsnytngsts fsdliqilwa
      121 praqfwflyv lfaifcvmav yfsmvkrrqv ellfvlsvll ylfrgslpes yllnliainl
      181 vyfvlgivfa enmsrneewl rpqtsllacl lifivlqwlf hfnlgyrhyd kgvmtltiat
      241 iaialvicls itlskvkvgw lqviglysmq iylmhiltgs garimmskif hvdstlihlv
      301 vgtsagvvlp ivltkvierv niqylfsapv cdfifrskkk al
//
LOCUS       WP_011150907             741 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Vibrio].
ACCESSION   WP_011150907
VERSION     WP_011150907.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 741)
  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   3  (residues 1 to 741)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..741
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=78918
     Region          6..740
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msydldedil qdflieagei lellseqlve lennpedrdl lnaifrgfht vkggagflsl
       61 telvetchga envfdvlrng qrsvspslmd tmlrsldtvn hqfkavqdre pleaadpell
      121 delhrlcrpe sedevaapva eevvvaepep eiipepvvea papassaiss vdeitqdefe
      181 klldelhgkg aapsakaaap aaptppsvsa svdsgditdd efeklldelh gagkspsasd
      241 fqatpppepa kpaakapsag dsdlmtdeef eklldelhgs gkgptleeld fatkpasanv
      301 apapepakpa apvapkpaaa paparaevka pavqeakapa aqqaakkpqa eatvrvdtst
      361 ldtimnmvge lvlvrnrlls lglnsndeem akavanldvv tadlqgavmk trmqpikkvf
      421 grfprvvrdl arnlqkdivl emrgeetdld knlvealadp lihlvrnsvd hgiempddra
      481 kagksrtgkv ilsasqegdh ielaiiddgg gmdpdklrgi avkrgmmded aagrlsdkec
      541 fnlifapgfs skekisdisg rgvgmdvvkt aintlngsid idselgkgtk itikvpltla
      601 ilptlmvgva ghpfalplas vneifhldls rtnvvdgqlt iivrekaipl fylqnwlapk
      661 sgkaqlrkgh ghvvivqigs qrvgfvvdtl igqeevvikp ldnllqgtpg magatitsdg
      721 hialildvpd llkqyaaasr l
//
LOCUS       WP_011151902             608 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Vibrio vulnificus].
ACCESSION   WP_011151902
VERSION     WP_011151902.1
KEYWORDS    RefSeq.
SOURCE      Vibrio vulnificus
  ORGANISM  Vibrio vulnificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 608)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 608)
  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 608)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Vibrio vulnificus"
                     /db_xref="taxon:672"
     Protein         1..608
                     /product="M4 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=64770
     Region          29..603
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mkcavlrsyg gnkmdftlea fmtfkttiia tcllaaapls maangpnahp spslkglqak
       61 nfvlpdnatl vkrfalghsg metqrfqqhf qnaivfggei slitaasgdv vavigrrydh
      121 llssnsvklk aeaakgivmm kigghgrwtt nlfinpsngl ffyivenqra dsrwhywida
      181 etgevlnayd glttgsgtgv hgdskdlsgl ttfnrgnfem vsangrlsty daggrsrlpg
      241 dlatdsddqw vepghtspgq aamvdahffa nvtdsyflsv lqfnwlnhys qgmvstahvk
      301 rnynnaywng yqmaygdgdg isfinlsgdl dvvghelshg ltdatsdliy qnesgalnea
      361 fsdimgtnie fyygsgnwti geditpnsng irnmadpged gdpshynery tgtgdnggvh
      421 insgiinhwy yllvnggqns dgqfasgtdv agigldaatq ivyngftslp pnadfclara
      481 atdavagths anvldawdev gvssdlcagg gdgggsgtgg ditisnvssr vikgvkfqis
      541 wdtdvasste vtfsccgtyv kneqvtshsy nfngskgvay eyyitskvyd sagnvassat
      601 agpfihqn
//
LOCUS       WP_011152057             292 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Vibrio vulnificus].
ACCESSION   WP_011152057
VERSION     WP_011152057.1
KEYWORDS    RefSeq.
SOURCE      Vibrio vulnificus
  ORGANISM  Vibrio vulnificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 292)
  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 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 292)
  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   4  (residues 1 to 292)
  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 292)
  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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Vibrio vulnificus"
                     /db_xref="taxon:672"
     Protein         1..292
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32566
     Region          28..180
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          210..290
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 meslaelmqq yvevkgfetl egiaetdipg vwfyrssqgn arqpfvyqsg iivlgqgskn
       61 ihigdhpvry gaddylvvgv pmpleceafa dddkpllgis vdvpmvllqq mvqklekhgy
      121 qnicsgkees cglksvkmea smlnackrlm rglcdplete vlgqslleev vyrallspkg
      181 yvlfelahae gnysriaqvl dkvhqdysep ltvqdlaska nmsisafhta frsvtlespi
      241 qyikkvrlnk ardliklegk rvndaarlvg ynstsqfsre ykrhfnetpk sa
//
LOCUS       WP_011153776              96 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [unclassified
            Synechocystis].
ACCESSION   WP_011153776
VERSION     WP_011153776.1
KEYWORDS    RefSeq.
SOURCE      unclassified Synechocystis
  ORGANISM  unclassified Synechocystis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Merismopediaceae; Synechocystis.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="unclassified Synechocystis"
                     /db_xref="taxon:2640012"
     Protein         1..96
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10649
     Region          1..96
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mkrqsvlqll sqskadlqar fgvtrlalfg stardeagph sdvdilvgfd gpatshryfg
       61 vqfyledllg cavdlvteka lrpelhpyve reriyv
//
LOCUS       WP_011154274             818 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Cupriavidus
            necator].
ACCESSION   WP_011154274
VERSION     WP_011154274.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus necator (Ralstonia eutropha)
  ORGANISM  Cupriavidus necator
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 818)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 818)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..818
                     /organism="Cupriavidus necator"
                     /db_xref="taxon:106590"
     Protein         1..818
                     /product="VirB4 family type IV secretion system protein"
                     /function="conjugative mating pair formation and DNA
                     transfer"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=92262
     Region          246..802
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mlklkrrpla eivpwltslt pelilnkdgs llatyefrgv dadsadasdi tsardqldqa
       61 crsfdnrita wwrlshrrtt gfidgefsna adarlnalnr thmttgryfr nthalsiayt
      121 pesgiakffe kigyhmtvgg rsvygaivea akdtvlsrsa fafdmekmra dtrrfeamld
      181 afaggiprik ptrltmqdsy aalhqvanps vpprrirypv tlldthltes evtvgaerll
      241 fesahgkrya avvavkewms fqeaaldsll qvdaeldici myrfldtara tayiekvrrf
      301 ykmaavnlrs mmkqyvskee sendegreel akeaghalkr ltaegvqhgf anisviiyad
      361 sesecedavs evvgaltnag fgairekanl mpawnstlpg rwdkqrrlqf vetpavsdia
      421 pvrsvlegpt fnawlsektg aevppltclp trhrtiqrvd mhqrggnghl fvigpigagk
      481 svflnflvsq gdrhkarrir fdkdrstrip tllsggtfid vtgkfqtgtp vnplslladp
      541 anftyvtewl tlaledddft lspqqvqdlf eavklvagyp rerwtlssls tmlhadlrar
      601 lqiwlkggqy ghffdhaeda favsdnlcie mgelfqkyer aavlftdyaf hrisqsmdgi
      661 rytiieveec gfffqnerfy rryedwitti rklngaiwsa tqslrqiarv anfeilkeni
      721 anwvylpngq aktspelykd kfgltddqvq liseavpnrd yllitntqtr mlqtafsdem
      781 vamlrsdgva qsicdkhhas ggpdwqdryv remlaraa
//
LOCUS       WP_011155710             688 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Rhodopseudomonas palustris].
ACCESSION   WP_011155710
VERSION     WP_011155710.1
KEYWORDS    RefSeq.
SOURCE      Rhodopseudomonas palustris
  ORGANISM  Rhodopseudomonas palustris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Rhodopseudomonas.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 688)
  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   3  (residues 1 to 688)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Rhodopseudomonas palustris"
                     /db_xref="taxon:1076"
     Protein         1..688
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /function="InterPro
                     IPR002545:IPR002570:IPR003594:IPR004105:IPR004358:IPR00546
                     7 COGs COG0643"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=74260
     Region          8..683
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mttidpaavf rqeaaelfev leaalldlgq npddrelvds afralhtikg sgamfgfdkv
       61 atfthefeta fervrkgeik ptqdlvsval aakdfirali etpdeadaii geailadlsr
      121 fvspteavea pvsspaqepa papvserrqv gwhlrfefds qilrngsnpl dllddlsklg
      181 scfampltdg ipfldelvpe dcylkwdvsl hsdcdkaaid dvfmfvqdem qlsleplfeg
      241 etpqpvpvle lpdvsilppe ppqaaeetkp apqaataapa aptverrsge prraddrgia
      301 tvrvqaerld elmdrvgelv iaqarltqla asgndisikl iaeeierlas slrdttmgar
      361 mvpigslfgr frrlvhdlsr dlgkpvefit sgedteldkt miecladplv hlirnaidhg
      421 ieapaarvaa gkpeqgriel aavhagaqvl vtvkdngggl ntarirakae eqgliapgvt
      481 asdqeihqfl fhpgfstaqt vsalsgrgvg mdvvkrtien mrgsidlstv pgdgttvtlr
      541 lpltlaiieg llirvgsgry iiplsaveec veltaeders rsrnflnvrg nlvpflrlrq
      601 ifdadgepdq hqktiiistg etrvglvadq iignhqtvik slsklhsdvt mfsgatilgd
      661 gtaalildvv qlvglaqaqs ekqmseaa
//
LOCUS       WP_011155775             132 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Rhodopseudomonas palustris].
ACCESSION   WP_011155775
VERSION     WP_011155775.1
KEYWORDS    RefSeq.
SOURCE      Rhodopseudomonas palustris
  ORGANISM  Rhodopseudomonas palustris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Rhodopseudomonas.
REFERENCE   1  (residues 1 to 132)
  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   2  (residues 1 to 132)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Rhodopseudomonas palustris"
                     /db_xref="taxon:1076"
     Protein         1..132
                     /product="ComEA family DNA-binding protein"
                     /function="COGs COG1031"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13615
     Region          61..128
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mgtstfrrlt laplaaaval gllasapama qapqpatppt aksdkmappp kaetpkaetk
       61 aaapaksekt elldinsata eqldalpgvg kaysaaiikg rpykgkdelv qkkivpqkty
      121 dgikdkiiak qk
//
LOCUS       WP_011156332             787 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Rhodopseudomonas
            palustris].
ACCESSION   WP_011156332
VERSION     WP_011156332.1
KEYWORDS    RefSeq.
SOURCE      Rhodopseudomonas palustris
  ORGANISM  Rhodopseudomonas palustris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Rhodopseudomonas.
REFERENCE   1  (residues 1 to 787)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..787
                     /organism="Rhodopseudomonas palustris"
                     /db_xref="taxon:1076"
     Protein         1..787
                     /product="TonB-dependent receptor family protein"
                     /function="InterPro IPR000531 COGs COG1629"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=84608
     Region          108..787
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mradahpdtr sligktlaag qrrplrtitl aalltsssql cfaqsatpga titldtivve
       61 qrreavrapa rqrsvvrraa paatpnaapa astvqtvdlv rerfnvlagg valvsqkdmp
      121 nagnptlant lsgvpgliiq nflgandqpr iqmrgsaqqn paergvlvly nglpinradg
      181 syivgfanpr qaeaievyrg ymanrlgatv lsgainfisp tgssqpgvqm svsggsfgqi
      241 nssaqigtkk dnvdaflqfd ttrrdgfrdy nssdrtslna nvgialsenv ktrfflgytd
      301 lgfdvagpin kdalfanprq tatgptvvng vainpgpnav rdkprrdasq fmignrttat
      361 fdahlidial gytytddtfr fpissgvrst kggdftglvr yaynpadall plfettaqys
      421 vgsadrdyyl nqsgmtgaqf gsnrldaqtl slfaganvpv wqqwtvspai syayatrdnd
      481 drytaaarpt iaynpakptv llpngsvptq dngyarsysg wnpslalsyr pdatqtffia
      541 gshsfeppth ddliatingt pnsspgrptp pspnlkaaaf atpnlsaqta vtveggwrgr
      601 adrfswdvvt yyswidnell nlrdvtgasi gainadrtth fgielgagvr ftdklsgrla
      661 ytyqdfrfvn dplrgnnklg gavphliyaq lqlqatdawm vqgavrwspa svpvdnmntl
      721 yadpyavvdl rseyrinktf rvfgeitnlf nktyaatslv vdqarpdqaa flpgdgrgfy
      781 agikasf
//
LOCUS       WP_011156428             133 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Rhodopseudomonas
            palustris].
ACCESSION   WP_011156428
VERSION     WP_011156428.1
KEYWORDS    RefSeq.
SOURCE      Rhodopseudomonas palustris
  ORGANISM  Rhodopseudomonas palustris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Rhodopseudomonas.
REFERENCE   1  (residues 1 to 133)
  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 133)
  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   3  (residues 1 to 133)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Rhodopseudomonas palustris"
                     /db_xref="taxon:1076"
     Protein         1..133
                     /product="endonuclease domain-containing protein"
                     /function="COGs COG2852"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14809
     Region          9..109
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 masatarglr krltpqearl waglrelklr gyhfrrrapi gcyvvdfvcl saklvidadg
       61 eqqampahfa adrqrgvvlr rqgfrvlhfw nsdidryfeg vmqtvldalp ppsvrpnvsr
      121 tghsihegag esg
//
LOCUS       WP_011156465             200 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Rhodopseudomonas palustris].
ACCESSION   WP_011156465
VERSION     WP_011156465.1
KEYWORDS    RefSeq.
SOURCE      Rhodopseudomonas palustris
  ORGANISM  Rhodopseudomonas palustris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Rhodopseudomonas.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Rhodopseudomonas palustris"
                     /db_xref="taxon:1076"
     Protein         1..200
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /function="COGs COG0163"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21346
     Region          4..192
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mstqhrivvg isgasgaavg lrvvellasv dcevhlvvsk aarrtiayev gpnaldhaad
       61 lvhrfhkied vgaciasgsf rtsgmivapc sirtlsaiah gdldnllvra advqlkerrr
      121 lvlmlretpl hlghirsmaq ateigaivap lspafyqrpr sisemvdhma lraigllgln
      181 dlelsapews ddtpptcpkp
//
LOCUS       WP_011157530             363 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Rhodopseudomonas
            palustris].
ACCESSION   WP_011157530
VERSION     WP_011157530.1
KEYWORDS    RefSeq.
SOURCE      Rhodopseudomonas palustris
  ORGANISM  Rhodopseudomonas palustris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Rhodopseudomonas.
REFERENCE   1  (residues 1 to 363)
  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 363)
  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 363)
  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 363)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Rhodopseudomonas palustris"
                     /db_xref="taxon:1076"
     Protein         1..363
                     /product="TRAP transporter substrate-binding protein"
                     /function="InterPro IPR004682:IPR006311 COGs COG1638"
                     /GO_component="GO:0005886 - plasma 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=39990
     Region          1..355
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkrrdflkvs atgaaaaaav aspaiaqssp evkwrltssf pksldtiygg aeylakqvae
       61 mtdnkfqiqv faagevvpgl qaldatsngt vemchtvsyy yvgkdptfav fasvpfglna
      121 rqqnswlyqg ggnelanefy kkyglvgfpc gntctqmggw frkeiktvad msglkmrigg
      181 iagqvlqkvg vvpqqiaggd iypalekgti daaewvgpyd deklgfqkva kyyyypgfwe
      241 ggptvhaftn lekfnqlpkn yqailanaav ntntwmnary dmlnptalkr lvaggtqlrp
      301 fsneildacl katnelwgei saknpdfkka idamqtyrsd qylwwqvaey tfdsfmirsr
      361 trg
//
LOCUS       WP_011157667             462 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Rhodopseudomonas palustris].
ACCESSION   WP_011157667
VERSION     WP_011157667.1
KEYWORDS    RefSeq.
SOURCE      Rhodopseudomonas palustris
  ORGANISM  Rhodopseudomonas palustris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Rhodopseudomonas.
REFERENCE   1  (residues 1 to 462)
  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 462)
  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 462)
  AUTHORS   ter Beek,J., 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 462)
  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 462)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Rhodopseudomonas palustris"
                     /db_xref="taxon:1076"
     Protein         1..462
                     /product="CmpA/NrtA family ABC transporter
                     substrate-binding protein"
                     /function="InterPro IPR006311 COGs COG0715"
                     /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=50539
     Region          102..341
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mstfdnpfdp nrrlhtagcs cgghateaeh aaeqaaalqs avtqgeekrf egavasavmr
       61 amfpqdasrr aflksvgaat alaavsqffp lqtatdvfas ggplektdlk vgfipitcat
      121 piimahpmgf yakyglnvev iktagwavir dktlnkeyda ahmlspmpla itmgvgsnpi
      181 pytmpaveni ngqaitlamk hkdrrnpkdw kgfkfavpfd ysmhnyllry ylaehgldpd
      241 vdvqiravpp pemvanlrad nidgylapdp mnqravydgv gfihiltkei wdghpccafa
      301 askefvttmp ntygallksi ieatayahkp enrkeiaqai spanylnqpa ivleqiltgt
      361 yadglgnvvk qpnridfdpf pwqsfaiwim tqmkrwgqik gdvdyktiae qvylatdtak
      421 lmkeaglaap dttsrsfsvm gkpfdgsnpd qylasfkikk as
//
LOCUS       WP_011157854             330 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Rhodopseudomonas palustris].
ACCESSION   WP_011157854
VERSION     WP_011157854.1
KEYWORDS    RefSeq.
SOURCE      Rhodopseudomonas palustris
  ORGANISM  Rhodopseudomonas palustris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Rhodopseudomonas.
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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
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
REFERENCE   5  (residues 1 to 330)
  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   6  (residues 1 to 330)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Rhodopseudomonas palustris"
                     /db_xref="taxon:1076"
     Protein         1..330
                     /product="AraC family transcriptional regulator"
                     /function="InterPro IPR000005 COGs COG2207"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36595
     Region          14..197
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          88..329
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 merrtiaplf veevadclrr agvapgpafa aaglpevvre rvsaaqfgal wlavaaamdd
       61 effglggrpm rpgsftllch avlnastlrq alnralrflk valddpygel rvegglariv
      121 lhdktaprsa fayrtfwivv hgiacwlvgr rlplrrvdfa cgppavaady rsffgapvrf
      181 gqpqsalafd asyldlrttr teralkeflr lapanilvry rhdatltaai rttlrakppt
      241 awpnfetlak qmkipastlr rrlraegqty qtikdeirra lairwlaene kpvgdiaadl
      301 gfaepsafhr afrkwmarsp gafrretrag
//
LOCUS       WP_011159246             386 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Rhodopseudomonas palustris].
ACCESSION   WP_011159246
VERSION     WP_011159246.1
KEYWORDS    RefSeq.
SOURCE      Rhodopseudomonas palustris
  ORGANISM  Rhodopseudomonas palustris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Rhodopseudomonas.
REFERENCE   1  (residues 1 to 386)
  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 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   3  (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   4  (residues 1 to 386)
  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 386)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Rhodopseudomonas palustris"
                     /db_xref="taxon:1076"
     Protein         1..386
                     /product="CmpA/NrtA family ABC transporter
                     substrate-binding protein"
                     /function="COGs COG0715"
                     /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=40922
     Region          2..261
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mserlrigfi plvdaaaliv aadkgfcaae gldvelvrei swanvrdkfn iglfdaahll
       61 aplavasslg ighvkvpvis gfglgvngna itvspdlhaa ivamadgdva dplvsgrala
      121 rvvaerrakg qepltfgmtf pfsshnydlr fwmgaggvdp dedvrlvvlp ppfmveslas
      181 khldgfcvga pwnsvaidlg igtilhftse lfqraaekml tvranwaaqh pevlkalira
      241 haraadyied vanrdevcal ltapgrieva pelirrtldg rlkvaadgtl rtsdryllvg
      301 rgaaarpdpv qgawnyaqmv rwgqaplsad llaaakavfr pdlydaavgt apalpsapad
      361 gigectgapf dpddiagyla rmtirr
//
LOCUS       WP_011160098             398 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Rhodopseudomonas palustris].
ACCESSION   WP_011160098
VERSION     WP_011160098.1
KEYWORDS    RefSeq.
SOURCE      Rhodopseudomonas palustris
  ORGANISM  Rhodopseudomonas palustris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Rhodopseudomonas.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Rhodopseudomonas palustris"
                     /db_xref="taxon:1076"
     Protein         1..398
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /function="InterPro IPR000890:IPR004372 COGs COG0282"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42532
     Region          3..394
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msdvllvlna gsssikfaly eahteptadh liceggigsl ghrphfkvvn sdgstrydty
       61 lpegtshdda mavligwiet tfpehrlsav ghrvvhggal fdgpvdvtpe viaqlrafdr
      121 laplhqphnv saiealaklh pslpqiacfd tafhhrlpev atafalprel teqgvrrygf
      181 hglsyeyiag rlpdvagqav adgrvvvahl gagasmcaml rcrsiattmg ftaldglmmg
      241 srcgeldpgv vlylleeksm tareiedlly resgllgvsg isddmrtlla sddphaceai
      301 elfvyriare lgslaaalgg ldalvftggi gehaseirrr vceqaawlgv tldpdanasl
      361 sgagrisapd skvsawaipt dedlmiarhv wrladggr
//
LOCUS       WP_011161641             152 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Lactobacillus johnsonii].
ACCESSION   WP_011161641
VERSION     WP_011161641.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus johnsonii
  ORGANISM  Lactobacillus johnsonii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Lactobacillus johnsonii"
                     /db_xref="taxon:33959"
     Protein         1..152
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16745
     Region          2..150
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 maattednyq lllkqaqalv egendwiant anisallfns lnnvnfagvy ryenqelilg
       61 pfqgkpacvh iqigkgvcgt aakekqtqiv knvhefaghi acdsesnsei vvpifkangd
      121 lwgvfdfdst klanfdeldq kylekiskvf kf
//
LOCUS       WP_011161804             402 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Lactobacillus johnsonii].
ACCESSION   WP_011161804
VERSION     WP_011161804.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus johnsonii
  ORGANISM  Lactobacillus johnsonii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Lactobacillus johnsonii"
                     /db_xref="taxon:33959"
     Protein         1..402
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44210
     Region          2..396
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkkvlavnsg sssfkyklfs ldneeviasg madrvglpgs vftmtladgs qhdeqsdian
       61 qeeavqklls wlkeynvids lediagvghr vvaggeeftd stvitednlw kiynmsdyap
      121 lhnpaeadgi yafmkvlpnv pevavfdtsf hqsldpvqyl ysvpykyyek frarkygahg
      181 tsaryvsrrt adllnkpved lkmvlchlgs gasvtaikdg ksfdtsmgfs pvagitmstr
      241 sgdvdpsllq fimkkgnits fnevikmlnt esgllglsgi spdmrdieka ikngdkqaql
      301 tkdifinriv ryigaymtem ggldvlvfta gigehdasvr kqimdgltwl gleydeeank
      361 anhesvittp nskitamivp tneelmiard vvrlakldkl nk
//
LOCUS       WP_011162073             160 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Lactobacillus johnsonii].
ACCESSION   WP_011162073
VERSION     WP_011162073.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus johnsonii
  ORGANISM  Lactobacillus johnsonii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Lactobacillus johnsonii"
                     /db_xref="taxon:33959"
     Protein         1..160
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17954
     Region          1..152
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mnaifereav rkytdekide ekiqklinaf qaspcamhqt dvmelsvits pellkkiedn
       61 tnnscynapl ifmintkkds qfgerdasva aenvmveaad lglgsvyvmg gvfalnkfpe
      121 lqkelgmdeg yeptvlvpig ypadkeqved rrnrykvvrk
//
LOCUS       WP_011163148             578 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Bdellovibrio bacteriovorus].
ACCESSION   WP_011163148
VERSION     WP_011163148.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriovorus
  ORGANISM  Bdellovibrio bacteriovorus
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 578)
  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   3  (residues 1 to 578)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Bdellovibrio bacteriovorus"
                     /db_xref="taxon:959"
     Protein         1..578
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /function="Chemotaxis protein histidine kinase and related
                     kinases"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=64679
     Region          19..566
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msdenkpqds qevdlsafid feqveevsra ffeeskeile dldnlilkle nnpedqdqvn
       61 vlfrkihtik gsvgavpggq llgslshefe alltrikres rpvtkncidl flkssrilkv
      121 laqslrdkre vypeelseai eiisaygvfe fgdesspran rpaasravss sddegvwlsv
      181 kqmnellrls gellvlknff qmmnqtvnfr vqpevferrq sdfaqnlgki sdqfqsqvqs
      241 vrkekagdsl sglpllvrqa stelnksvhl eftgsdllid kglgkdlyec lvhlvrnsid
      301 hgiedqfera vqgkptigll nlevleknga vhvifkddgk gldrerilqr aiknalvtee
      361 aaksladeqi ykfifhagfs tkekvttisg rgvgmdivls tverykgriq idnnpgagat
      421 fhleipipqh imvesallca wshfqlavpl tsvahitscd elqvttvdhl rycqfsgmtv
      481 pllnyseiln lrtsvsdevv rnssavfirm keavfallvd ridaqtdlvv ksfgtmigeq
      541 kgfkgisila dekvtyivdp ekmmalmmfd qqkheeaa
//
LOCUS       WP_011164986             281 aa            linear   BCT 20-JAN-2025
DEFINITION  HNH endonuclease family protein [Bdellovibrio bacteriovorus].
ACCESSION   WP_011164986
VERSION     WP_011164986.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriovorus
  ORGANISM  Bdellovibrio bacteriovorus
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Wu,C.C., Lin,J.L.J. and Yuan,H.S.
  TITLE     Structures, Mechanisms, and Functions of His-Me Finger Nucleases
  JOURNAL   Trends Biochem Sci 45 (11), 935-946 (2020)
   PUBMED   32807610
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Jablonska,J., Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Systematic classification of the His-Me finger superfamily
  JOURNAL   Nucleic Acids Res 45 (20), 11479-11494 (2017)
   PUBMED   29040665
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10539890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Bdellovibrio bacteriovorus"
                     /db_xref="taxon:959"
     Protein         1..281
                     /product="HNH endonuclease family protein"
                     /calculated_mol_wt=32312
     Region          <140..235
                     /region_name="DUF1524"
                     /note="Protein of unknown function (DUF1524); pfam07510"
                     /db_xref="CDD:462188"
ORIGIN      
        1 mkktllvmml vatsgtskal aeenlanprf ddyytvresi sspaenftgp wdaaqnllqq
       61 neefftelrt rfyslvrfdh htdgygnvge rynrakhfgg wlndhrdedc yntrakvlmr
      121 dsevpvgfas ngctvstgqw qdpygdrqys rasdiqidhf vplknayisg ahkwsrtkrc
      181 lysnylgnef hllsvfgken asksdktpeg ymppnpgyrc qylvqwlkvk miwslgltpp
      241 ekdtvlrlas enrcdlndfv ysegdlqnqr rfmnenmalc e
//
LOCUS       WP_011165846             165 aa            linear   BCT 20-JAN-2025
DEFINITION  GAF domain-containing protein [Bdellovibrio bacteriovorus].
ACCESSION   WP_011165846
VERSION     WP_011165846.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio bacteriovorus
  ORGANISM  Bdellovibrio bacteriovorus
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Bdellovibrio bacteriovorus"
                     /db_xref="taxon:959"
     Protein         1..165
                     /product="GAF domain-containing protein"
                     /function="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18156
     Region          10..160
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mqqhtsinys dktkfykelh seaeglaeke wfvnlanfsa llkqhlpein wvgfyllhnn
       61 elllssfqgl pactriaigk gvcgtaaktl qtqlvadvdq fpghivcdaa skseivvpli
      121 hngkllgvld vdapvlnrfd sedqkglqgl vqilisktvw pdrfa
//
LOCUS       WP_011166301             304 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Mycoplasma mycoides].
ACCESSION   WP_011166301
VERSION     WP_011166301.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasma mycoides
  ORGANISM  Mycoplasma mycoides
            Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Mycoplasmataceae;
            Mycoplasma.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Mycoplasma mycoides"
                     /db_xref="taxon:2102"
     Protein         1..304
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35523
     Region          4..288
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mitnetkpil lidgyhllhk gyygtlkrti vsknkdgivi naiysfvani lkfvqsdryh
       61 svivafdfde ncwrkelyse ykakrkptpi dlipqlqiar dfltsanisw yekynyegdd
      121 vigsicrian klgydvcilt ndkdiyqlvn nktsiitnis kkekikiiks eqvyehflcq
      181 pnqvadikai lgdqsdnikg vkyikrkqae slinkyenve nildhineln eplktiisen
      241 kqliidnkki tkiltnvklg rinfkptkit yyrlirflke qemyafirpi rkylertnkk
      301 tvnk
//
LOCUS       WP_011166955             249 aa            linear   BCT 20-JAN-2025
DEFINITION  phosphonate ABC transporter ATP-binding protein [Mycoplasma
            mycoides].
ACCESSION   WP_011166955
VERSION     WP_011166955.1
KEYWORDS    RefSeq.
SOURCE      Mycoplasma mycoides
  ORGANISM  Mycoplasma mycoides
            Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Mycoplasmataceae;
            Mycoplasma.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Manav,M.C., Sofos,N., Hove-Jensen,B. and Brodersen,D.E.
  TITLE     The Abc of Phosphonate Breakdown: A Mechanism for Bacterial
            Survival
  JOURNAL   Bioessays 40 (11), e1800091 (2018)
   PUBMED   30198068
REFERENCE   2  (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   3  (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   4  (residues 1 to 249)
  AUTHORS   Kononova,S.V. and Nesmeyanova,M.A.
  TITLE     Phosphonates and their degradation by microorganisms
  JOURNAL   Biochemistry (Mosc) 67 (2), 184-195 (2002)
   PUBMED   11952414
REFERENCE   5  (residues 1 to 249)
  AUTHORS   Wanner,B.L.
  TITLE     Genes for phosphonate biodegradation in Escherichia coli
  JOURNAL   SAAS Bull Biochem Biotechnol 5, 1-6 (1992)
   PUBMED   1368181
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466534
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Mycoplasma mycoides"
                     /db_xref="taxon:2102"
     Protein         1..249
                     /product="phosphonate ABC transporter ATP-binding protein"
                     /EC_number="7.3.2.2"
                     /EC_number="7.6.2.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015416 - ABC-type phosphonate
                     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=28705
     Region          3..244
                     /region_name="PhnC"
                     /note="ABC-type phosphate/phosphonate transport system,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG3638"
                     /db_xref="CDD:442855"
ORIGIN      
        1 mnkvielkei svqynnksdl ilkdinldif qgelvaiigp sgvgkstlfk iiinslrpvk
       61 gqakvfdkdi lkfnkkqkrl fiskigfltq tpnliytdnv ynniirstsk yknnfykffs
      121 iltrkqkiai fekldelnil dkaffkvsel sggqqqrvei akllikdvel iladeptsnl
      181 dkktsievlk vlkniskqnk tilvnihdls lvkryfdrvi ainnkqivfd kktkdikqwq
      241 ldriiksrs
//
LOCUS       WP_011167322             326 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Pseudomonas].
ACCESSION   WP_011167322
VERSION     WP_011167322.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   ter Beek,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 11438136
            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="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=36646
     Region          1..321
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msievrnvsk nfnafkalnn isldiqsgel vallgpsgcg kttllriiag letpddgsiv
       61 fhgedvsghd vrdrnvgfvf qhyalfrhmt vfdnvafglr mkpkrerpne triaekvhel
      121 lnmvqldwla drypeqlsgg qrqrialara lavepkvlll depfgaldak vrkelrrwla
      181 rlhedinlts vfvthdqeea mevadrivvm nkgvieqigs pgevyenpsn dfvyhflgds
      241 nrlslgeegh llfrphevsl shqeiedhha aevrdirplg attrvtlkve gqselieaev
      301 vkdhdslvgl akgetlffkp kvwqkl
//
LOCUS       WP_011168773             355 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_011168773
VERSION     WP_011168773.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 355)
  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 355)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 355)
  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   4  (residues 1 to 355)
  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 355)
  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 12117701
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40104
     Region          30..214
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          257..339
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkliadplfs easappqvsr mllqyaterg vdaewlcrgl gfapddlkkp gyllshrqsn
       61 llvrrtitvl gddglglsvg erqtavswgi vglgmqaspt lgealdlair yqkhagallr
      121 hrmelhegrc ltymvpqffd pdvisfylee afasamaiar hltghhdmlp srieleypep
      181 ahrqryseif rcpvvfagah nliefdalwl diplltrddf vaaevaelld sanwedkgts
      241 dlvetvqrei rkrlcappsl ndfaqqlnig ertlrrrlde agqsyqgvid slrrtralsl
      301 lshretklid vatetgfsdi rdfrrafkrw tgvtpreary eiqqfrkdiq glsts
//
LOCUS       WP_011168295             801 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [Pseudomonas].
ACCESSION   WP_011168295
VERSION     WP_011168295.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 801)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 801)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 801)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            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="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87626
     Region          60..110
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          90..801
                     /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 mptpfsrlrt grvktlglrl gglvlalafq gealaeefdf dipaqplnsa lkelgrqgdl
       61 qilynpddvn gkfsgpvhgr ltpeqavadl lkqagvthnl eadtltlgsa asahpmnlgp
      121 vaikgdpfgi ttegsgsyat tgvsinktsq slretpqsvt vmtrqlmndk nlngldevma
      181 qtpgitfsqr nfgshvfssr gfaledesyt idgvagqgys vtgwmtpdte iydrvevlrg
      241 aaglligagn pggavnlvrk rptalpqfsi ttragswdqy rvdldgsskl ndsgsvrgrf
      301 vtsyedrgyf idglkktapl lygiletdls edttltlglr hqsadthgys ifglprysng
      361 kaidlprsts laqdwnrhqt rtdevfsele trfdenwsgt lsathsdgaf dqkvayakga
      421 idpatqsgsr lvrtlfrsdt lqsdgfdshl dgrfdafglt hqltiggnws eqkrdsryat
      481 vnsnrpldif npdhdaiaep arpawrstdy sdkrygvysn lrlsltesls lvmggrvswy
      541 dyqsqsagvt traqeenqvt pfvgviydln rdwswyasht diflpqsgyr tasgafldpa
      601 igashetgik gelfdkrlnv sfalfyvkqk dvaveddana gqclsndayg tcyvngdirr
      661 skgidmeisg eplpglqtla gytfnltrgs dgksisaetp rhmlrlsssy nlpgtwrrlt
      721 vgggvsaqsg ysehestqpi dnpgratwda raswkidehw svalngnnll drkyykatgd
      781 idrgnyygdp rnyvltlrgd f
//
LOCUS       WP_011169694             271 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: formate/nitrite transporter family protein
            [Pseudomonas].
ACCESSION   WP_011169694
VERSION     WP_011169694.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..271
                     /product="formate/nitrite transporter family protein"
                     /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=28210
     Region          5..251
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 mslntpqqia eiavesgvkk ahlglsslmi lgflagafia lgflldihvs tmiphewasl
       61 gnllgavvfp vglilvvlag gelltgnmms lpmalfagri glgqlvrnwv lvtlanliga
      121 lfvaycfghv vgltegpfma ktvaianakm gasfeqafis gigcnwlvcl avwlsyaskd
      181 vigkvvgmwf pvmafvaigf qhivanmfvi paaifagals waqfgdnfvp vflgnavgga
      241 vfvglayhla ffnaaarpae lsrasgaqap e
//
LOCUS       WP_011172720             100 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nucleotidyltransferase family protein [Thermus].
ACCESSION   WP_011172720
VERSION     WP_011172720.1
KEYWORDS    RefSeq.
SOURCE      Thermus
  ORGANISM  Thermus
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Thermus"
                     /db_xref="taxon:270"
     Protein         1..100
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11092
     Region          <25..97
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 matsldrdke avlralrpyl egtgtrlflf gsfargegrq asdldlalls pvplkdlmpl
       61 lrealeeapv vrrvdlvdla eaepafrerv lregvlwaef
//
LOCUS       WP_011173226             657 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Thermus thermophilus].
ACCESSION   WP_011173226
VERSION     WP_011173226.1
KEYWORDS    RefSeq.
SOURCE      Thermus thermophilus
  ORGANISM  Thermus thermophilus
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Thermus.
REFERENCE   1  (residues 1 to 657)
  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 657)
  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 657)
  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 657)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..657
                     /organism="Thermus thermophilus"
                     /db_xref="taxon:274"
     Protein         1..657
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=69375
     Region          3..657
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mdkdaallve eselggrrpk gwsrhllfgl gvawslfqlw atelgtldpl rlravhlafa
       61 lalaflaypg krgpkdrvpl ldwalallga lgalyvvwdy ygitqlrggi psdrdvvmgt
      121 ltllvlfvas wrvvgpalpi iasvfilyal tgpkglipyt lpswlqlhag sqwgqlmgql
      181 yttaegiwgv plgvsatfvf lfvlfgalle kagaghffiq aayallghfr ggpakaavva
      241 saltgvvsgs svsntvttgt ftiplmkrvg yppekagave vasssngqlm ppvmgaaafi
      301 maeflnipys qlilialvpa llayatlfvt vhlealalgl kgvprselpp lapvlrsglh
      361 yllplaylly alvglrltpe raalntvflm allillqeaw rawrsgagvg fglleggrll
      421 legleagarg mvgialatas agvivgivtm tgigfgltdi verlsggnll lvlllaqlts
      481 lllgmglptt anyivmaslv vpvilnlaek agyavppvaa hmfafyfgim adstppvala
      541 ayaasaiars dfwktavqgf vyelrtalla ymfffnpkll llgvgsvaeg vlivatafag
      601 mvafsaalvg ffhkrttlwe rgllllaaft lvvpglatdl lglgllglvy lvqrvrk
//
LOCUS       WP_011173927             188 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UbiX family flavin prenyltransferase [Thermus].
ACCESSION   WP_011173927
VERSION     WP_011173927.1
KEYWORDS    RefSeq.
SOURCE      Thermus
  ORGANISM  Thermus
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Thermus"
                     /db_xref="taxon:270"
     Protein         1..188
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20181
     Region          6..187
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mdapfrvvvg vsgasgmpya ldllealkdl aevhlvlsqg akrvlweemg lspkdlhala
       61 hrvykdqdlg apiasgsfpt rgmvvvpcsa ttlakvatgl adtlltraay vhlkerrplv
      121 lvlretplpl ptlramvqaa eagatilpas pgfyhrpkei rdllgfvtqr ildhlglpgk
      181 raprwget
//
LOCUS       WP_011175066             199 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Candidatus Protochlamydia amoebophila].
ACCESSION   WP_011175066
VERSION     WP_011175066.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Protochlamydia amoebophila
  ORGANISM  Candidatus Protochlamydia amoebophila
            Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia;
            Parachlamydiales; Parachlamydiaceae; Candidatus Protochlamydia.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Candidatus Protochlamydia amoebophila"
                     /db_xref="taxon:362787"
     Protein         1..199
                     /product="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=22474
     Region          19..187
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mkkptnlsii rplfaqssft aeevkqfgvs aahlgyyikk glikrlgrgi yqsadyqgsp
       61 enfrwedlie avnsvpngvi clisalaihd iteeiprehw iaiphttsic rgakvrivrf
      121 rnmelgktel dlggvripif nrertiidsf rllsretaik alkmalfqkg tmrldlkklq
      181 syakklrfni apylitatt
//
LOCUS       WP_011179267             286 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Bartonella quintana].
ACCESSION   WP_011179267
VERSION     WP_011179267.1
KEYWORDS    RefSeq.
SOURCE      Bartonella quintana
  ORGANISM  Bartonella quintana
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Bartonella quintana"
                     /db_xref="taxon:803"
     Protein         1..286
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32451
     Region          5..278
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 minflpysln ilratdrdry isvlfapkkk rralaalyaf naevvrvres vhdpligeir
       61 lrwwydsiah semqksesnp ilndlfmait lfnlpktafl rycdakildl yhnpiatlhd
      121 lklycgetas iilqlscqil dpdaaqdftd ayeqggiaqg lsgvlrllsf mqsryqyylp
      181 sdilkavgvn reelesdris neqkchiiet mvalsqdhyt rfyehfsalp ktlkpaflpl
      241 aiipaslqka vqlgaavfqe satlpllhry wfitkaaisg nlpkil
//
LOCUS       WP_011179800             202 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Bartonella quintana].
ACCESSION   WP_011179800
VERSION     WP_011179800.1
KEYWORDS    RefSeq.
SOURCE      Bartonella quintana
  ORGANISM  Bartonella quintana
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Bartonella quintana"
                     /db_xref="taxon:803"
     Protein         1..202
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22899
     Region          2..166
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 milnrlklwt islanrrtap hwlgfiafme ssvfpipvdv lyipialvhp kkvyryafia
       61 tacsvlggif gwfignfayd slakpilefy grienfqalq ngvtlqflvi llalsgflhl
      121 ppikivtila gvmdmhlglf vltcifarga rfyllawlir rfgrqamnfl arhlqwiali
      181 gcimllliyg tftafvkkyl ll
//
LOCUS       WP_011181237             202 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Bartonella henselae].
ACCESSION   WP_011181237
VERSION     WP_011181237.1
KEYWORDS    RefSeq.
SOURCE      Bartonella henselae
  ORGANISM  Bartonella henselae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Bartonella henselae"
                     /db_xref="taxon:38323"
     Protein         1..202
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22905
     Region          2..166
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 milnklklwt islanrrtas ywlgfiafie ssffpipvdv lylpmalvhp kkayryafia
       61 tvcsvlggvs gwfighfayd tlakpilefy gkvesfqtlk nsatlkflvi llitsgflhl
      121 pplkittlla gvmgvhlglf iltcifarga rfyllawlik hfgrqamhfl arhfkwivli
      181 gcvtlflvyg ifitfvnkyl lf
//
LOCUS       WP_011181789             279 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: aminoglycoside phosphotransferase family protein
            [Bacillus cereus group].
ACCESSION   WP_011181789
VERSION     WP_011181789.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus group
  ORGANISM  Bacillus cereus group
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 279)
  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   2  (residues 1 to 279)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Bacillus cereus group"
                     /db_xref="taxon:86661"
     Protein         1..279
                     /product="aminoglycoside 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=32235
     Region          22..216
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mdisiiaaql vkenvishfp nsikvlnggt tstvylldgk yvvklneaev ireeahflsf
       61 yegntlfskl lykepfhayi vysflegsts ceqghkrstl rtlvkevink yeivsdvdvw
      121 grkespvqsw neflttnvve ahknvrpyms deeyrkvlkl anrdaginqp fllhgdlgfh
      181 nfifqgnmlh gvidplpvlg dpiydliyaf cstpedvtke tidyamkqcv fhkkerdlye
      241 eiviglylri dtclrhhpkd ledylvawry wmdevevtl
//
LOCUS       WP_011182952             317 aa            linear   BCT 20-JAN-2025
DEFINITION  5'-3' exonuclease [Mesoplasma florum].
ACCESSION   WP_011182952
VERSION     WP_011182952.1
KEYWORDS    RefSeq.
SOURCE      Mesoplasma florum
  ORGANISM  Mesoplasma florum
            Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Entomoplasmatales;
            Entomoplasmataceae; Mesoplasma.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Senissar,M., Manav,M.C. and Brodersen,D.E.
  TITLE     Structural conservation of the PIN domain active site across all
            domains of life
  JOURNAL   Protein Sci 26 (8), 1474-1492 (2017)
   PUBMED   28508407
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415718
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Mesoplasma florum"
                     /db_xref="taxon:2151"
     Protein         1..317
                     /product="5'-3' exonuclease"
                     /EC_number="3.1.11.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008409 - 5'-3' exonuclease activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36859
     Region          5..260
                     /region_name="ExoIX"
                     /note="5'-3' exonuclease Xni/ExoIX (flap endonuclease)
                     [Replication, recombination and repair]; COG0258"
                     /db_xref="CDD:440028"
ORIGIN      
        1 mntlnekrti liidgyhllh kgyygtlkrk klatnregvp inaiytfvak inqlvkknny
       61 ysiivtldmd egcwrrelyp eykakrketp edlvpqkqii refltaanip wyempryead
      121 diigtinria lkldydvhil sndkdifqlv gerttvitns skddehilid hekvvekfgc
      181 hpsqvadika lmgdpsdnik gvrylhyaqa idllnkygni dnifehidei nkniskrlne
      241 skeliltnkk ittiqdrlpi grvnlkpirv nwyglskflk kqkmwayvad vekmasesrn
      301 knskvnkikn ehiskek
//
LOCUS       WP_011184891             587 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Streptococcus
            pyogenes].
ACCESSION   WP_011184891
VERSION     WP_011184891.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus pyogenes
  ORGANISM  Streptococcus pyogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 587)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Streptococcus pyogenes"
                     /db_xref="taxon:1314"
     Protein         1..587
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=65669
     Region          24..569
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mmetedtisr gkrkrllkrl reriapkryl lyvsaflswl qfvmrmisfy liaktfstfi
       61 lghaialgrl aglllllnvv gfvlailgkq lqgiasqfar dslkqsffea fidldgqfda
      121 hasdadiltl asqgidsldt yygyylslsm rtkwncttim ilvfliypla glvflgvlpl
      181 iplsivamqk rskqimshyw ssymdvgnlf mddlkglntl ysyqatgrye qefsgkaeqf
      241 rkatmsllgf qlqavgymda vmylgiglsg flavqalatg qlsffnflff lliatefftp
      301 ireqgygmhl vmmntkmadr ifsfldsvpa rkdnksktai nfnqidiqni slayekktvl
      361 sgvtmtltkg qltaiagvsg qgktslaqll lkrqsattgh ilfdgldsdn lsqetinqqv
      421 lyvsdqstll nrsiydnlrl aanlskkeil dwidqhglls finwlpdgld tivgengnll
      481 spgqkqqvic arallskrsl yifdeatssl daeneriidn litrlaktai vivithkmsr
      541 lkganqvlfl ntgqpaclgk pcdlyrdqpt yrhlvdtqar leasiyg
//
LOCUS       WP_011185361             397 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Leifsonia xyli].
ACCESSION   WP_011185361
VERSION     WP_011185361.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia xyli
  ORGANISM  Leifsonia xyli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Leifsonia xyli"
                     /db_xref="taxon:1575"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=41525
     Region          2..395
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msavlvvnsg ssslkyqlid akseealatg liervgegeg rirhrgpggs aeytlvipdh
       61 taaframlaa fgtdgsslve hpldavghrv vhggkrffep tivtplvean iddladlapl
      121 hnpanldgir aarqafpavp hvavfdtafh qtlepaayty aidaalaeeh rvrrygfhgt
      181 shkyvsgava ellgrplgel kqivlhlgng asacavdggr sidtsmgmtp leglvmgtrs
      241 gdidpavlfh lsrraglgid eldellnrrs gllgltghgd mrdvrrvaes gdavarlald
      301 tvahrlkhyi gaytallggl daltftagvg endpdlraaa ckglgvlgiq ldpernaars
      361 pgarivsadg spvtvlvvpt neeleiarqa lqavaag
//
LOCUS       WP_011185983             201 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Leifsonia xyli].
ACCESSION   WP_011185983
VERSION     WP_011185983.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia xyli
  ORGANISM  Leifsonia xyli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 201)
  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 201)
  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   3  (residues 1 to 201)
  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   4  (residues 1 to 201)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 201)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 201)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Leifsonia xyli"
                     /db_xref="taxon:1575"
     Protein         1..201
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21971
     Region          13..201
                     /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"
ORIGIN      
        1 mtdqettpta phrvvvaede slirldivei lsdngfevvg eagdgetava latelrpdlv
       61 imdvklpqld gisaaerlsk dqiapvvllt afsqrelver aseagalayv vkpftpndll
      121 paieialarh qqilalaaev tdmvqrfetr klvdrakgll nekmglsepd afrwiqkasm
      181 drrltmhdva qaiieqlapk k
//
LOCUS       WP_011186450             403 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Leifsonia xyli].
ACCESSION   WP_011186450
VERSION     WP_011186450.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia xyli
  ORGANISM  Leifsonia xyli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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 403)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Leifsonia xyli"
                     /db_xref="taxon:1575"
     Protein         1..403
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45494
     Region          18..402
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 madhlspaaa rrialaaqgf grprpatvga rqlnalidri nllqidsvnv fershylpaf
       61 arlgaydrsl ldrltfdarg phteywahea afirkedwpl fewrmrfnrd rygkaggwfd
      121 snretvdwlr relaasgpla aseiehdant rtgpwwgwsa vkraletlfl mgevaiagrt
      181 rfqrryalve evlpasvlkr svseedavre lirrsavahg vgtvrdfady yrirtapara
      241 airdleesge llpvcvpgwe sngrplpawi hrgarrprrv etaallspfd pvvwrrdral
      301 rmfgfhyrie iytpapkrvy gyyslpllld dalvgrvdlk sdrqngvlrv qsawtettgp
      361 ygiverlvpl lattarwqgl dgvevaarar gdlapalasa vrh
//
LOCUS       WP_011186067             297 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Leifsonia xyli].
ACCESSION   WP_011186067
VERSION     WP_011186067.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia xyli
  ORGANISM  Leifsonia xyli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
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
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Leifsonia xyli"
                     /db_xref="taxon:1575"
     Protein         1..297
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=31601
     Region          1..250
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 miefrsvtkr fpdgtvavdd fslvvpsrri tvlvgssgsg kttilrminr mvdptsgtve
       61 idgegverlk pvqlrrsigy vmqnsgllph rkvvdniatv plllgerrma araralelme
      121 tvglerslad rypaqlsggq qqrvgvargl aadpnillmd epfgavdpiv redlqnellr
      181 lqrdlgktvv fvthdideaf rlgdqvvifq kggivaqrga paeilaspad efvasffgad
      241 rgkrvlrier tpagsvlvds egraagvlsg ldpsaagetr aaavpvagaa aqgedst
//
LOCUS       WP_011187762             651 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Desulfotalea psychrophila].
ACCESSION   WP_011187762
VERSION     WP_011187762.1
KEYWORDS    RefSeq.
SOURCE      Desulfotalea psychrophila
  ORGANISM  Desulfotalea psychrophila
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfocapsaceae; Desulfotalea.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 651)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Desulfotalea psychrophila"
                     /db_xref="taxon:84980"
     Protein         1..651
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=72544
     Region          79..648
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mtlyrqlvif tlilfvllfs aiwveklqst rsflltqmes haqdtatsls lslspivaeg
       61 diptvetmmn avfdggyyrv isfkdmegav iterllkitl egvpqwfidl vpiqapsaea
      121 lvmagwtqag vlyveshpgy ayramwdaav kmslyfllag slvlllggfg lrlllkplkr
      181 velqaeaicr rdfriqeklp ktkelrqvvq smnrmtnqvr emfsgqvkia erfrrnaysd
      241 qltglgnrry itgqvearle sggesmhgal lmlqldnlqk vneldgfaag dellkkvadi
      301 ikqetkmlnd valarltggd faifiseiss vavydlaeki sqkvtrlave nashsdniah
      361 iggvvyeetp tlpkllaead nalqaarqqg pnkwlvnfls sgaddlikgk swwketlenv
      421 lergeiilfr qpvmnstdqn rvqhqellsr iamdsgeivs agvfvplaer lqlvsrldkv
      481 vlekvfaqke kmadlhtiav nvspssldds afvdwvlael gqlqdksihi ifefpefgav
      541 qyldvvkdfa rkiqklghgi gldhfgqsfs nfgylkslrp eyvkidraft keldadngds
      601 effigalcgv ahsldirvia egveraeqvd llvelnvdal qgylfgepkh v
//
LOCUS       WP_011187804             405 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Desulfotalea psychrophila].
ACCESSION   WP_011187804
VERSION     WP_011187804.1
KEYWORDS    RefSeq.
SOURCE      Desulfotalea psychrophila
  ORGANISM  Desulfotalea psychrophila
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfocapsaceae; Desulfotalea.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 405)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Desulfotalea psychrophila"
                     /db_xref="taxon:84980"
     Protein         1..405
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43998
     Region          1..404
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkiliinsgs ssikfqlidm sdesvlasgl verigetdtt ekninctfhp gtdkkhkiei
       61 cqtvadhrqg mlaaiellgd keqavmsdls eidavghriv hggetmyqpv vvdekviaei
      121 taaiplaplh npghldgikv aqelftevph vtvfdtaffq tipphahiya lpyelytkhr
      181 irrygahgts hkfvtnecak llekpveecn litvhlgngs smsaveggka idtsmgvtpl
      241 eglvmgtrsg didpaimafl nrnlgmsiee idhmlnkesg lkgicgmndm rdihaaadag
      301 nelaelavgi qtyrirkyig symaalgqvd aivftagige nddivraksl eklenlgvil
      361 dkklnaqrsk epfcistpes kiqvwviptn eelaiaretk avvna
//
LOCUS       WP_011188430             327 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Desulfotalea
            psychrophila].
ACCESSION   WP_011188430
VERSION     WP_011188430.1
KEYWORDS    RefSeq.
SOURCE      Desulfotalea psychrophila
  ORGANISM  Desulfotalea psychrophila
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfocapsaceae; Desulfotalea.
REFERENCE   1  (residues 1 to 327)
  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 327)
  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 327)
  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 327)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Desulfotalea psychrophila"
                     /db_xref="taxon:84980"
     Protein         1..327
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=36475
     Region          3..325
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mdkiirsilc avcvmmfact avsaktikir fghdqietsp hhkaalylkk lieegsngdi
       61 evtvypnqll gsgiqmvemv qagaiemiav ptskiqvisp ifqildlpfl fpskeelyne
      121 iygdfgkalf atlknnnvvg ltywgmgfkq ltgnfpihqp sdykgkkirv mpspvireqf
      181 kalgaspvpv dfhelynalq qgvvdgqenp lvgiatmkly evqkymtlsn haflaygmvi
      241 nknlmdrlta dqqklikdsa kksasyqldl lekrdqdfld tikaggvevs elsseqsaqf
      301 qnamtpvytw ftknvkngrk ylemigk
//
LOCUS       WP_011188606             373 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Desulfotalea psychrophila].
ACCESSION   WP_011188606
VERSION     WP_011188606.1
KEYWORDS    RefSeq.
SOURCE      Desulfotalea psychrophila
  ORGANISM  Desulfotalea psychrophila
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfocapsaceae; Desulfotalea.
REFERENCE   1  (residues 1 to 373)
  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 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   3  (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   4  (residues 1 to 373)
  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 373)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Desulfotalea psychrophila"
                     /db_xref="taxon:84980"
     Protein         1..373
                     /product="CmpA/NrtA family 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=40450
     Region          27..302
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mhrnlkrkiq aviiamvvtl amgnvyaaka pniymgyilt thhsplmvaa drgkelnptg
       61 pylasmvakq kyrliaadgk tlavinlivs kngsetstlf amnrldlgla sstafmsgid
      121 kgtkvkiicp lhvdgmsmvf pmeskinsyq dlataikask tpykigyhsp tsaprvvfeg
      181 alhragfkis enpndveadi lmvdlkstan lipallskqv dswvgpaphp vvaeykkvgh
      241 igldsrdlpp lgawtdfpcc vmgaseqaik eqpeivqama dimtaataws nnnkketaki
      301 ssrwigvpaa aiekstiiyt ttpsqnwlkg egifltmlng mhkfkgklkd mdlakaapll
      361 ydfsfnkkal dqe
//
LOCUS       WP_011188693             142 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Desulfotalea psychrophila].
ACCESSION   WP_011188693
VERSION     WP_011188693.1
KEYWORDS    RefSeq.
SOURCE      Desulfotalea psychrophila
  ORGANISM  Desulfotalea psychrophila
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
            Desulfobulbales; Desulfocapsaceae; Desulfotalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Desulfotalea psychrophila"
                     /db_xref="taxon:84980"
     Protein         1..142
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14754
     Region          6..142
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkkalknqqg ftlielmivv aiigilaava ipqyqnytkr akvteglnma gaaktavsey
       61 yqsqnvlpts laeagistvd tdivkslgig asgvitvtfk apvlldativ ltpslsttga
      121 gltwtctntg tdmdnyvpan cr
//
LOCUS       WP_011190501             385 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Rickettsia typhi].
ACCESSION   WP_011190501
VERSION     WP_011190501.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia typhi
  ORGANISM  Rickettsia typhi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; typhus
            group.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Rickettsia typhi"
                     /db_xref="taxon:785"
     Protein         1..385
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43250
     Region          3..385
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mkdviliana gssslkisif giqnkkvkdk iynifleknn nkilfyinqk qesaisikdn
       61 aiemminlfe ewwtkqsaln liatghrivh ggknfnkpvi vnekiikelr vliplsplhq
      121 pynlqvldlf fqkykdishi icfdtsfhyt nppitkafgl pkqyydkgim rygfhglsyq
      181 yvsshfkeit medlptktii ahlgsgsslc aiknglslts smgfsvldgv mmatrtgnld
      241 pgvvlylinh ekmtmkeite llykksgllg isgessdmrt litnnshdsk favelfvyri
      301 vleigkliaa legidciift agigqnsavi remisgklsw lgikidygkn qknehristk
      361 gskvkvfvvp tneeliiaee vmkfl
//
LOCUS       WP_011190539             215 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Rickettsia typhi].
ACCESSION   WP_011190539
VERSION     WP_011190539.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia typhi
  ORGANISM  Rickettsia typhi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; typhus
            group.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Rickettsia typhi"
                     /db_xref="taxon:785"
     Protein         1..215
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24011
     Region          134..211
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 minnilclic isgiyfgyqy yqnskpviti ypddippkir psiiennqit svysniynli
       61 akdtniqtvk llpdpekpii idssnqsqnd ktfdgmsnlm pliesnnkna tdlniiklak
      121 giknkvgnaq ncrshtsykv qlgsvkseae ameegakikk kfpkilqnvv ittkkvkydd
      181 gkfyylilag eysslnqaqa vckklahnqq scvlk
//
LOCUS       WP_011190653             207 aa            linear   BCT 20-JAN-2025
DEFINITION  MJ0042-type zinc finger domain-containing protein [Rickettsia
            typhi].
ACCESSION   WP_011190653
VERSION     WP_011190653.1
KEYWORDS    RefSeq.
SOURCE      Rickettsia typhi
  ORGANISM  Rickettsia typhi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; typhus
            group.
REFERENCE   1  (residues 1 to 207)
  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 10020205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Rickettsia typhi"
                     /db_xref="taxon:785"
     Protein         1..207
                     /product="MJ0042-type zinc finger domain-containing
                     protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24114
     Region          1..38
                     /region_name="MJ0042_CXXC"
                     /note="MJ0042 family finger-like domain; TIGR02098"
                     /db_xref="CDD:131153"
ORIGIN      
        1 myitcpncnt qfivtsnqig ingrrvkcsk ckhlwyqkld ynnsklndfk dkintetvtt
       61 ptknhyntnv pvilprkkey kifpilwssf iifclvilli dsfkflgkyd qlkieainlg
      121 eyhhmngmki fyklsnesdy litnplikvr vidsnnhtld eyasitklrt kihakqaiyl
      181 elnidkipvn akyiditicn rlgllfk
//
LOCUS       WP_011191985             312 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Yersinia pseudotuberculosis].
ACCESSION   WP_011191985
VERSION     WP_011191985.1
KEYWORDS    RefSeq.
SOURCE      Yersinia pseudotuberculosis
  ORGANISM  Yersinia pseudotuberculosis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
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
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Yersinia pseudotuberculosis"
                     /db_xref="taxon:633"
     Protein         1..312
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=35011
     Region          1..308
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 miqfhqvsky fagkravdnl slqiskgeft vligtsgsgk sttlkminrl iehdegkirf
       61 ageeirnykp edlrrrmgya iqsiglfphw tverniatvp qllkwpkdri rqrvvellel
      121 lhldpqqfch ryphqlsggq qqrvgvaral avdpevllmd epfgaldpvt rsalqleitr
      181 ihqlsgrtiv lvthdideal sladrivlmd egrviqqgtp lemlaqpand fvrdffgrsd
      241 lgikllslgr veqrvrcget lagqpilgtt slrealslfv srqtdklpva nehgqplgvl
      301 yfadlvanke rv
//
LOCUS       WP_011193131             496 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Yersinia pseudotuberculosis].
ACCESSION   WP_011193131
VERSION     WP_011193131.1
KEYWORDS    RefSeq.
SOURCE      Yersinia pseudotuberculosis
  ORGANISM  Yersinia pseudotuberculosis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Yersinia pseudotuberculosis"
                     /db_xref="taxon:633"
     Protein         1..496
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54401
     Region          1..496
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mqniikihpl dnvavalqdl aaderiesge fsvklaqpvv rghkfaltai epgqmivkyg
       61 lpighaltli qpgehihsqn aktnlsdlde yeyqpefssl ppqmadrdvq iyrrpkgevg
      121 irnelwiipt vgcvngiarq iqqrflketq daegidgvyl fshpfgcsql gqdhentrtm
      181 lqnmvrhpna gavlviglgc ennqvdvfqt tlgkvdeerv rfmvcqqhdd eveaglehlh
      241 alyqvmrhdr repgqlselk fglecggsdg lsgitanpll grfsdyvian dgtsvltevp
      301 emfgaerilm srcrdeatfe ktvsmvndfk qyfiahdqpi yenpspgnka ggittleeks
      361 lgctqkagqs qvvdvlkyge rlqrpglnll sapgndavat salagagchm vlfstgrgtp
      421 yggfvptvkl atnselaakk phwidfdagk lihgtsmdtl lnefvdlive iangkparne
      481 vndfrelaif ksgvtl
//
LOCUS       WP_011194204             822 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Symbiobacterium thermophilum].
ACCESSION   WP_011194204
VERSION     WP_011194204.1
KEYWORDS    RefSeq.
SOURCE      Symbiobacterium thermophilum
  ORGANISM  Symbiobacterium thermophilum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Symbiobacteriaceae; Symbiobacterium.
REFERENCE   1  (residues 1 to 822)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 822)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 822)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..822
                     /organism="Symbiobacterium thermophilum"
                     /db_xref="taxon:2734"
     Protein         1..822
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=90391
     Region          33..798
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 msvvvqrrtr rvtrwigyta ltlvvlllla vaggyavarr slprasgelv lpglrapvtv
       61 yrdewgvphi eaqnehdlym aqgyvvaqdr lfqmdltrra aagrlaeviw psqletdkff
      121 ralnlrraae asvqsygpwa relleayaag vnafiaeaka qnrlpvefll lgyepepwsp
      181 vdsaligkim aydlggnfea evyrlqlrnq vgpeladqlm pvypedgitm iryrggegae
      241 eprpgasava garppgssld ltgllallrv pdegrgsnnw vvagsgtrtg kpllandphl
      301 gartpsiwye qhlvvpgmin aygvmfpgap givigqneri awgvtntnpd vqdlyierrn
      361 pdnpyqfeym grwedalvhr eligvkgqdp vpfevvitrh gpiisevvgd pdnrpeeala
      421 lkwtahmatp eleavllfpk arnweefrea lrsfhvptqn fvyadvdgti ayrtgglvpi
      481 rrsgdgllpv pgwtdeyewv gfipfdqmpe avnppegyiv tannkvidda ypyfltysws
      541 qpyramriae mieaklgdlt addmqamqvd yanlhartll pvllpavera gvtgtaatav
      601 ellkswdmvd sadqpqplif hlwwseltrm lyeplmgeel yrrmadkgnv tdmallaaae
      661 grpngwieaa ggldklaads lqaavdrava lqgsdpgrws wgryhrlqpp hpvgaaatpl
      721 gwllnptsyp iggsgvtvga msfggdgmvr tfapwrqvvd ladptgnsrs ivtpgqsghf
      781 lsphyddqsa mhsrgelitr nfhgyrtgra lrllpdqaga gg
//
LOCUS       WP_011195014             118 aa            linear   BCT 20-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein
            [Symbiobacterium thermophilum].
ACCESSION   WP_011195014
VERSION     WP_011195014.1
KEYWORDS    RefSeq.
SOURCE      Symbiobacterium thermophilum
  ORGANISM  Symbiobacterium thermophilum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Symbiobacteriaceae; Symbiobacterium.
REFERENCE   1  (residues 1 to 118)
  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 118)
  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 11517917
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Symbiobacterium thermophilum"
                     /db_xref="taxon:2734"
     Protein         1..118
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=12993
     Region          10..53
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
     Region          <74..118
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
ORIGIN      
        1 mpqcppgsfs ytvrpgdnfw tlawrfgttp qaiaranpgv nswslrigqt lcipgwspwv
       61 tppqgrcpqg wepyriqpgd tlgsiawerq ttvanllrvn pvnpnnlrig qiicvpar
//
LOCUS       WP_011195667             710 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Symbiobacterium thermophilum].
ACCESSION   WP_011195667
VERSION     WP_011195667.1
KEYWORDS    RefSeq.
SOURCE      Symbiobacterium thermophilum
  ORGANISM  Symbiobacterium thermophilum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Symbiobacteriaceae; Symbiobacterium.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 710)
  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   3  (residues 1 to 710)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Symbiobacterium thermophilum"
                     /db_xref="taxon:2734"
     Protein         1..710
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76188
     Region          14..704
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          173..244
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 mgsgfdisae dirvfldeae ellqtmeagi lrlesdagdp dpeviqdifr aahtlkgssa
       61 tlghqrmael thamenvldr lrkgkasvtt plvdtlfhcl dalklfkdei atgepaqvnt
      121 delmrelaal egasapaapa qaapsadgve fppltaqqqa kvdeartkgl nvyqarleia
      181 pdaampavra fqallavgdi geivlsvptq eqvendqvgs dmkllfvtre slqkvqdvlr
      241 evpemavrtl aayepvsaaa psgptpagev aaaamapaap kagpvpagdn gagngggalr
      301 tprggmrtvr vdvevldnlm ntvgelvier trlqqvlsrl everegdels qtmssalaql
      361 grltgnlqee iqrarmipve nlfrkfprmv rdiaqkfgke infimrgeet eldrsvieei
      421 gdplmhllrn avdhgieppe vrvaagkpaa gtvileafhe enhiiisvrd dgrgvdpeki
      481 rasavrkgil seeaarrlsd peainliwsp gfstadkvsd vsgrgvgldv vqkniering
      541 sveirstvgq gtefrvklpl tlaiiralqv ellgtiycip lgsvvetdri pvseiqtvrq
      601 revvvkrgev ipllrlaeaf elqrpegaee pdeifvviva vmgrqiglvv dsligegdvv
      661 ikplgrfige ipgisgatim gdgdvaiild vsslvnsvqd eagrlemvah
//
LOCUS       WP_011195773             403 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Symbiobacterium
            thermophilum].
ACCESSION   WP_011195773
VERSION     WP_011195773.1
KEYWORDS    RefSeq.
SOURCE      Symbiobacterium thermophilum
  ORGANISM  Symbiobacterium thermophilum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Symbiobacteriaceae; Symbiobacterium.
REFERENCE   1  (residues 1 to 403)
  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 403)
  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
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 403)
  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   5  (residues 1 to 403)
  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   6  (residues 1 to 403)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 403)
  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 12122468
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Symbiobacterium thermophilum"
                     /db_xref="taxon:2734"
     Protein         1..403
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43089
     Region          15..56
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
     Region          75..394
                     /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 mlvgpelira inkqrvlrlv rsagamsrad laertgltrp tvsavvaell eegwveeigt
       61 gessggrppi llrfnprarw vigaelgagh vravladlag nvfhrfkqrv esrdplievd
      121 qleravryll dqtprygppt pvagvgigit gvidpeegvw rysphyqvrd lpvapmlqer
      181 lslpvwiend aramawgers fgaaqgvdnl afirvgvglg agiiidgrly ggahqgagei
      241 ghimvkergl rcrcgsdgcl etvgsaiaia rravqrmaqg eetlirelcg gdpskviatt
      301 vieaadagdr vaqeilseag rflgigigam inllnpamvi igggtsragd ylieplrqaa
      361 lertlpalre rvkivrtelg edagplggaa lvieelfrtp tlk
//
LOCUS       WP_011196300            1200 aa            linear   BCT 20-JAN-2025
DEFINITION  AAA family ATPase [Symbiobacterium thermophilum].
ACCESSION   WP_011196300
VERSION     WP_011196300.1
KEYWORDS    RefSeq.
SOURCE      Symbiobacterium thermophilum
  ORGANISM  Symbiobacterium thermophilum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Symbiobacteriaceae; Symbiobacterium.
REFERENCE   1  (residues 1 to 1200)
  AUTHORS   Liu,Y., Sung,S., Kim,Y., Li,F., Gwon,G., Jo,A., Kim,A.K., Kim,T.,
            Song,O.K., Lee,S.E. and Cho,Y.
  TITLE     ATP-dependent DNA binding, unwinding, and resection by the
            Mre11/Rad50 complex
  JOURNAL   EMBO J 35 (7), 743-758 (2016)
   PUBMED   26717941
REFERENCE   2  (residues 1 to 1200)
  AUTHORS   Chen,Z., Luong,T.T. and Lee,C.Y.
  TITLE     The sbcDC locus mediates repression of type 5 capsule production as
            part of the SOS response in Staphylococcus aureus
  JOURNAL   J Bacteriol 189 (20), 7343-7350 (2007)
   PUBMED   17704228
REFERENCE   3  (residues 1 to 1200)
  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   4  (residues 1 to 1200)
  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
REFERENCE   5  (residues 1 to 1200)
  AUTHORS   Hopfner,K.P., Karcher,A., Craig,L., Woo,T.T., Carney,J.P. and
            Tainer,J.A.
  TITLE     Structural biochemistry and interaction architecture of the DNA
            double-strand break repair Mre11 nuclease and Rad50-ATPase
  JOURNAL   Cell 105 (4), 473-485 (2001)
   PUBMED   11371344
REFERENCE   6  (residues 1 to 1200)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1200
                     /organism="Symbiobacterium thermophilum"
                     /db_xref="taxon:2734"
     Protein         1..1200
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=133791
     Region          1..1190
                     /region_name="sbcc"
                     /note="exonuclease SbcC; TIGR00618"
                     /db_xref="CDD:129705"
     Region          1..>157
                     /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            35..42
                     /site_type="other"
                     /note="Walker A/P-loop"
                     /db_xref="CDD:213246"
     Site            146..149
                     /site_type="other"
                     /note="Q-loop/lid"
                     /db_xref="CDD:213246"
ORIGIN      
        1 mrpirlafag lqsyrepqei dfrelmgagl fgifgptgag kstildaitl alygrvertr
       61 gtmgimnlne nrlwvkftfa lggteyrver syrrekdtps irseharlvr vlpegdevla
      121 drerevtqqv tdllgleidd ftravvlpqg qfaeflkltg skrtemlqri falsqygdvl
      181 nerlkrrkea verqldavag eqrglgdasa eavsaaeeal rqvtaalaea erqladtesr
      241 fkewervwql qqelagitde larweaqaqa vdaaraelda arradavrph ltardqaaaa
      301 aaraeraval aeqavrdaea evaraaqaya eartnrmeqa paltrrqadl qraveledrl
      361 eearrqagev eeqvaalrek hdavvrqige aekraaalra retglqeeia rlevspeern
      421 ritdaqrald rlreaerall qaeqrvrqre qeleharraa eqaealrlea errlqevesa
      481 lqrleteppa deadlraqea wlgrageqir tvaglaaqya qrqaeadarr reweeaaari
      541 eqalleeaqq qqaveaaeqe reavraavaa arrrahaaal aqaltpgepc pvcgsrehpq
      601 pavvgeavnl eaeearleqa earlraagsa lgraqertaa areqaesarr rqaeaerale
      661 earlaleaar erlpaawrsl agpqleeala reaaeheera rrfagwreqv aalqqareer
      721 tralfaaagd arerqaavah aeqaladara eadarrsaaa ecaaqfdavr ddldaagvea
      781 alrrirdade rvadlrrsla evrtgqqele srlgalrtee krcadelqea rvrhaqavqr
      841 yeevadqwrr lsggeparpq ltavesrltr laqeeeqaaa akeraerahg qaeaaraaav
      901 relevahrhv aeaeaalaea ltvagfesae aargalrlaa rqaaldeeir rhdqegerlk
      961 grqaaleqql agrsisaeew rawvdrleqa rrsaaerree raramqvrdd llakqrrwqe
     1021 leeqrlglaa rldhldelqk vlrgnafvnf iaqeqmarva adasrrlrql trdrytleaa
     1081 pdgsflvrde tnggtlrsvn tlsggetfla slslalalsa qiqlhghypl efffldegfg
     1141 tldpelldvv istlerlhfd rlnvgvishv aelrnrlhrr vivepaepgg rgsrlrlera
//
LOCUS       WP_011198883             282 aa            linear   BCT 20-JAN-2025
DEFINITION  aminoglycoside phosphotransferase family protein [Bacillus cereus].
ACCESSION   WP_011198883
VERSION     WP_011198883.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 282)
  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   2  (residues 1 to 282)
  AUTHORS   Kim,C. and Mobashery,S.
  TITLE     Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and
            manifestation of antibiotic resistance
  JOURNAL   Bioorg Chem 33 (3), 149-158 (2005)
   PUBMED   15888308
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12025366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         1..282
                     /product="aminoglycoside 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=32585
     Region          22..221
                     /region_name="APH"
                     /note="Phosphotransferase enzyme family; pfam01636"
                     /db_xref="CDD:426359"
ORIGIN      
        1 mdisviaaql vkekvisyyp nsikvlnggt tstvylldee yvvklneaev ireeaiflsf
       61 yerntlfanl lykeplhtyi vysflegsts cgrghkritl stlvkevink yeivsridgw
      121 gwkespvqsw safltknvme ayenvrryis eeeyrtvlkl anspnrgtgi nqpfllhgdl
      181 gfhnfifqgn elhgvidplp vlgdpiydli yafcstpedl tketidyamk qcvfhkkdrn
      241 lyeeivigly lridtclrhh pkdledylva wrywmgevev tl
//
LOCUS       WP_011206365             424 aa            linear   BCT 20-JAN-2025
DEFINITION  VirB4 family type IV secretion system protein [Mesomycoplasma
            hyopneumoniae].
ACCESSION   WP_011206365
VERSION     WP_011206365.1
KEYWORDS    RefSeq.
SOURCE      Mesomycoplasma hyopneumoniae (Mycoplasma hyopneumoniae)
  ORGANISM  Mesomycoplasma hyopneumoniae
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mesomycoplasma.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Wallden,K., Williams,R., Yan,J., Lian,P.W., Wang,L.,
            Thalassinos,K., Orlova,E.V. and Waksman,G.
  TITLE     Structure of the VirB4 ATPase, alone and bound to the core complex
            of a type IV secretion system
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), 11348-11353 (2012)
   PUBMED   22745169
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Rabel,C., Grahn,A.M., Lurz,R. and Lanka,E.
  TITLE     The VirB4 family of proposed traffic nucleoside triphosphatases:
            common motifs in plasmid RP4 TrbE are essential for conjugation and
            phage adsorption
  JOURNAL   J Bacteriol 185 (3), 1045-1058 (2003)
   PUBMED   12533481
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Mesomycoplasma hyopneumoniae"
                     /db_xref="taxon:2099"
     Protein         1..424
                     /product="VirB4 family type IV secretion system protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=48369
     Region          <1..405
                     /region_name="VirB4"
                     /note="Type IV secretory pathway, VirB4 component
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3451"
                     /db_xref="CDD:442674"
ORIGIN      
        1 mptnniawgf pftlrdfndn nynalglnyy dntplffdqf yqkgtrknsn lfilgtsgsg
       61 kttltkklit ynislgnsvi vldpqneywk igqklnanii hlnssgislf nplqirkvfs
      121 pgtddfilns dlialnlskl etffqivfpn isnnsliaii scikklyeen gffeleqdit
      181 klenkeypii sdlieiikkt efsylsemek qsiianfess fdkssilgrm fngksntkdi
      241 nakfsifnvs almnlekrvy qaafflvltf iqgqisdfyh kidkkiiliv deghkfides
      301 nlfalnflfd saktirkyng slmittqnpg dfaitgeaar kseaiiencq ysiffnlksn
      361 dinkinnlyk nvgglseeek sfinlaqige flltvnsvdr fklkayfndi ekkyffdkgd
      421 ranv
//
LOCUS       WP_011208023             267 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Nocardia farcinica].
ACCESSION   WP_011208023
VERSION     WP_011208023.1
KEYWORDS    RefSeq.
SOURCE      Nocardia farcinica
  ORGANISM  Nocardia farcinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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   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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Nocardia farcinica"
                     /db_xref="taxon:37329"
     Protein         1..267
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29423
     Region          18..69
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msiraiswvl yqaevddhgd frllvaladr asddgtgafp svdflakrmr rtprsvqrgl
       61 rklmedgwir lgdqqlvahy radrrptvyd lvmdrtrgda dvtpplngat psvtppnsne
      121 atsyvtplhp hevtpdvtph pargdihgth gvtsdvtqtv psllrnetvq esgapsalgt
      181 pdddepkrkr pairlpadwa ptdahresal nagvdvavea ykfrlhaaeq drrcvswnaa
      241 fsrwlmnarp trpvtsgvse sgrlwqd
//
LOCUS       WP_011209335             218 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Nocardia farcinica].
ACCESSION   WP_011209335
VERSION     WP_011209335.1
KEYWORDS    RefSeq.
SOURCE      Nocardia farcinica
  ORGANISM  Nocardia farcinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Nocardia farcinica"
                     /db_xref="taxon:37329"
     Protein         1..218
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24069
     Region          10..213
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mpieldlnpd ellsttrtvr krldlerevp lavvreclel avqapsgsnr qgwhwvvvtd
       61 aekrrrlgel yrrgfaeyra apeylgtkat gdpavdatrr rvadsaeyla ekmgevpvll
      121 vpclwgrvdn vsgaasashw gslfpavwsf claararglg tawttlhlky ereaaevlgi
      181 pfekvsqgal ipvaytkgtd fkpaarvdma rivhvdsw
//
LOCUS       WP_011211322             278 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Nocardia].
ACCESSION   WP_011211322
VERSION     WP_011211322.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 278)
  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 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   3  (residues 1 to 278)
  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   4  (residues 1 to 278)
  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 278)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..278
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30096
     Region          35..265
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          184..265
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mepttevvta rpapalagfi dhytgyrmtg yapglhrglp srhltfivai gptidvveqt
       61 drtqspgdyr cvlsglqasa aaiahnghqe gvgieltplg crvlfglpag alwnttleca
      121 eiagpaadel werlqgpasw rerfavcdev ltrlacpdrl vvpelawawr avvdsggavh
      181 vgalaerigw srqhltrrfa tefglgpkla aritrferar rmlertpsfv tiaqvaaacg
      241 yydqahlnrd faelagcspt twlaqevpsv qdentarg
//
LOCUS       WP_011211329             394 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: exonuclease SbcCD subunit D [Nocardia].
ACCESSION   WP_011211329
VERSION     WP_011211329.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Liu,S., Tian,L.F., Liu,Y.P., An,X.M., Tang,Q., Yan,X.X. and
            Liang,D.C.
  TITLE     Structural basis for DNA recognition and nuclease processing by the
            Mre11 homologue SbcD in double-strand breaks repair
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 299-309 (2014)
   PUBMED   24531464
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Connelly,J.C., Kirkham,L.A. and Leach,D.R.
  TITLE     The SbcCD nuclease of Escherichia coli is a structural maintenance
            of chromosomes (SMC) family protein that cleaves hairpin DNA
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7969-7974 (1998)
   PUBMED   9653124
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..394
                     /product="exonuclease SbcCD subunit D"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0004529 - DNA exonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=41919
     Region          1..268
                     /region_name="SbcD"
                     /note="DNA repair exonuclease SbcCD nuclease subunit
                     [Replication, recombination and repair]; COG0420"
                     /db_xref="CDD:440189"
     Region          260..355
                     /region_name="SbcD_C"
                     /note="Type 5 capsule protein repressor C-terminal domain;
                     pfam12320"
                     /db_xref="CDD:463533"
ORIGIN      
        1 mrllhtsdwh vgrtfhgvdl lvdqarslaa iaelvaeesv dvvvvpgdvy drsipsadai
       61 avctrgleai raagavivat sgnhdsparl gagasfaaag glylrtrlae adrpivlrdd
      121 agevafygip ylepevvrge lgvprarsha evldvvmdrv radlagrpgv rsvvlahafv
      181 vggaatgser sisvggvetv plsafdgvdy valghlhspq tlsasvrysg splpysfgea
      241 shrkavwiid ldesgvaevr rrdlpvvrgl srltgtleel lsdpahedav ahyvsatltd
      301 tarpidamrr lrnrfphavh vewvrpdads vlhyrervrg rddaevarsf ltdvrgepst
      361 aelrwleral aagvtepega avlagsdaae elsa
//
LOCUS       WP_011211833             188 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: LytR C-terminal domain-containing protein [Nocardia].
ACCESSION   WP_011211833
VERSION     WP_011211833.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 188)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..188
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=18159
     Region          100..186
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mnypnptsgg pplralamvl ialaivfagl gamsmsssds dgeesaaptt tsaaapaatt
       61 tttaapatta tttvastppp ppppepqvaa ppapavdrav pvrvlnnslv aglanrtanq
      121 laangwtnvt agnyaagtla kttvyygnsa aereaalaia qelgavaepk sagvgdgsag
      181 viviltgn
//
LOCUS       WP_011213823             224 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Legionella].
ACCESSION   WP_011213823
VERSION     WP_011213823.1
KEYWORDS    RefSeq.
SOURCE      Legionella
  ORGANISM  Legionella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae.
REFERENCE   1  (residues 1 to 224)
  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 224)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 224)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Legionella"
                     /db_xref="taxon:445"
     Protein         1..224
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=25635
     Region          1..207
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Region          92..121
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(94..95,98..99,101,128,131..132,135..136,138..139,
                     161,164..165,168..169,172)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          126..155
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          160..188
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msvymteeeq leiikkwwkr ygnmitifls ivlliiagyr ymnwhndkik qqasiayenm
       61 miafsnqnik svrsyaneli knynhtvyad iahmtlakiy vsknkleqar nelkavases
      121 qmtplrqiak iriarllaad kaytnalnel savedeaylp vinelkgdiy sakgqyqdam
      181 nayrlaidev rtngmgnlfl emktnelaik tqsmitddkk vkaa
//
LOCUS       WP_011213860             162 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Legionella pneumophila].
ACCESSION   WP_011213860
VERSION     WP_011213860.1
KEYWORDS    RefSeq.
SOURCE      Legionella pneumophila
  ORGANISM  Legionella pneumophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 162)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Legionella pneumophila"
                     /db_xref="taxon:446"
     Protein         1..162
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=18051
     Region          29..161
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cl49639"
                     /db_xref="CDD:483979"
     Site            order(105,119,122,135..138,140)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mvknskfifi sikkqemscf ekdhlianya issgkngvge kinsgctprg whkihsilgi
       61 dlpinsvmva rewtgeiyse slatqfperd wiltrilqld glepgrnkge dvdtlhryiy
      121 ihgtpdttql gipgshgcir lnndaviela awatkntlvy iq
//
LOCUS       WP_011214167             137 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Legionella pneumophila].
ACCESSION   WP_011214167
VERSION     WP_011214167.1
KEYWORDS    RefSeq.
SOURCE      Legionella pneumophila
  ORGANISM  Legionella pneumophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Legionella pneumophila"
                     /db_xref="taxon:446"
     Protein         1..137
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14363
     Region          1..136
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mrtkgftlie lmivaailgi lvaiampayq dytirarvve glemasaakl avvetslidn
       61 tlpanqadtg ytspaptinv asiaignqgi ititytanag ngtitmvptl datnriltwd
      121 ctggtlisky rpaycrp
//
LOCUS       WP_011214487             362 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Legionella pneumophila].
ACCESSION   WP_011214487
VERSION     WP_011214487.1
KEYWORDS    RefSeq.
SOURCE      Legionella pneumophila
  ORGANISM  Legionella pneumophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 362)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Legionella pneumophila"
                     /db_xref="taxon:446"
     Protein         1..362
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=41279
     Region          <112..357
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mpcekcdsvt tyhlsgtyql lilpprghcy skllnhlten nfdinkrdsg iiellftaer
       61 aqdighaler cysqaeleds kavllpidia drnvervlnh thslkkivgl clsqwlvgli
      121 enqglstfcq pilhnttlkp ygfecllrgk qdnnilpssd lfgaakssdm lflldkkari
      181 chienmskid iadkkifinf nptaiydplf cltttnqslk ktsikpaqiv fevtesdevk
      241 dkkhllkiid yyrnqgycva lddlgsgyss lnlltelqpd yvkldqelis qihtnefkqi
      301 ilekiceman klkikiiceg ietedelqii knyaidfyqg flfekpmpye kipdyiktst
      361 qk
//
LOCUS       WP_011214579             218 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Legionella pneumophila].
ACCESSION   WP_011214579
VERSION     WP_011214579.1
KEYWORDS    RefSeq.
SOURCE      Legionella pneumophila
  ORGANISM  Legionella pneumophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Legionella pneumophila"
                     /db_xref="taxon:446"
     Protein         1..218
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=24703
     Region          60..207
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mkiiisllfa fisasghafs cydpqtiiqk piqfdkkria ltreyqlthy gidsesieie
       61 pkmivlhwtc ipsldttfri fnppalpsss prrnelpgdl nvsshflvdr dgtiyqlmpe
      121 twmarhvigl nhyaigieni ggvdskddlt eeqakanafl vcylkekypq ikhvighney
      181 lqykgtalwl ekdpnyqtdk tdpgptfvkk vkqliaap
//
LOCUS       WP_011214632             137 aa            linear   BCT 20-JAN-2025
DEFINITION  acyl carrier protein [Legionella pneumophila].
ACCESSION   WP_011214632
VERSION     WP_011214632.1
KEYWORDS    RefSeq.
SOURCE      Legionella pneumophila
  ORGANISM  Legionella pneumophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 137)
  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 137)
  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 137)
  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   4  (residues 1 to 137)
  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 10011594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Legionella pneumophila"
                     /db_xref="taxon:446"
     Protein         1..137
                     /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=15183
     Region          4..>64
                     /region_name="acpP"
                     /note="acyl carrier protein; Provisional; PRK00982"
                     /db_xref="CDD:179197"
ORIGIN      
        1 mnvaevypkv reiiadvlvi deeevslnss liedlgaesi dfldlvfqle kefkikiprg
       61 qleknargdl aedefekggi lttpglqalk nylsevpadr fkenmkvnei pvlftvetfc
      121 klvisaiaqq qatetva
//
LOCUS       WP_011215679             225 aa            linear   BCT 20-JAN-2025
DEFINITION  murein L,D-transpeptidase catalytic domain family protein
            [Legionella pneumophila].
ACCESSION   WP_011215679
VERSION     WP_011215679.1
KEYWORDS    RefSeq.
SOURCE      Legionella pneumophila
  ORGANISM  Legionella pneumophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 225)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Legionella pneumophila"
                     /db_xref="taxon:446"
     Protein         1..225
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=24867
     Region          43..210
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mntlftlist vlltsnitss aplfakpgtd intqlqhlsh kapqlnkkvl klaltaykna
       61 skrgavkkpv ltvidyslps nkqrmwvfdl rnerllynty vahgknsgvn varsfsnres
      121 skqsslgtyi tkntyighkg yslnlqgldr gfndnaynrr vvihgawyve pefikkagra
      181 glswgcpaia qtlakpvint ikngsvvfay ypdkkflshs gylva
//
LOCUS       WP_011215876             137 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Legionella pneumophila].
ACCESSION   WP_011215876
VERSION     WP_011215876.1
KEYWORDS    RefSeq.
SOURCE      Legionella pneumophila
  ORGANISM  Legionella pneumophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Legionella pneumophila"
                     /db_xref="taxon:446"
     Protein         1..137
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14471
     Region          1..136
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mrtkgftlie lmivatilgv llaiafpayh dytirvrvae glekasfakl avaekilidn
       61 ilpanqadtg ytspaptinv asiaignqgi ititytanag ngtitmvptl datgriltwd
      121 ctggtlisky rpaycrp
//
LOCUS       WP_011215980             335 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Legionella pneumophila].
ACCESSION   WP_011215980
VERSION     WP_011215980.1
KEYWORDS    RefSeq.
SOURCE      Legionella pneumophila
  ORGANISM  Legionella pneumophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 335)
  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 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   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 335)
  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   5  (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   6  (residues 1 to 335)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Legionella pneumophila"
                     /db_xref="taxon:446"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38823
     Region          24..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          <184..332
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mdlviaanyl stlekcleqf ginhflekig fdlirvhdpd ayltqdefnq vimeayklsn
       61 cpelglvfgq nlsivnhgfl gyaamssptf gtaiqtvlsy lntrtnllsl elrqfnnens
      121 ayikllphtk emvlsrfite lavahlikmr nfliscndpl lkielnydep pyakyyqtif
      181 qtkivfntea trvwfkaeel nypihfaddv syqlakrqlq elekkmslke dmaskiksil
      241 inqnlnhasm deiasrlcmt srtlrrhlqr ldvtyqelld evreqkaktf llnnnismte
      301 isfllgfqdt snfskafkrw tgitpteyre khevq
//
LOCUS       WP_011216034             624 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Legionella pneumophila].
ACCESSION   WP_011216034
VERSION     WP_011216034.1
KEYWORDS    RefSeq.
SOURCE      Legionella pneumophila
  ORGANISM  Legionella pneumophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 624)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 624)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 624)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 624)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 624)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 624)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..624
                     /organism="Legionella pneumophila"
                     /db_xref="taxon:446"
     Protein         1..624
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=70635
     Region          8..620
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mnesltekrn elslsfaalg vvfgdigtsp lyafgqviky fpindyniyg ilslifwsli
       61 iivsikylvi vfradndgeg giialagvir qkikkpggwl lfitlvgigl iigdgmltpa
      121 isilsavegl eslspnlaky vlpvtliilf flfkmqsigt gkigvyfapv mlvwfitigi
      181 lgflqiiqnp kvlmainpyy ainffmihqy salfilggvf lvmtggealf adlghfgkka
      241 irtgwfaval palllcyfgq gafvlmhted ikypffslsp dwflpvmiil atlatiiasq
      301 aiisaafsil kqasllnlip rlkivftskf ekgevylpli nfilalgtcs lvvifksssn
      361 ladaygiavn ldmlittvlv giiayrcwsw hafkilifll iliielaffa gnipklltgg
      421 wipvliaflg fvvmytwhcg feklrelhhr dalmdafiid elnqnkisrq pgmglyiidp
      481 ydyegesllh hlrlnriffe nmvfvsikie nkpyipiedk felikkaegf ylifihygft
      541 eninlpneld emfkrvylpf diiknkliyf ieivfvemtg erqkhmylwq khffslmirn
      601 avpdiqfyql pynntiaigt yyqf
//
LOCUS       WP_011217520             203 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Photobacterium].
ACCESSION   WP_011217520
VERSION     WP_011217520.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium
  ORGANISM  Photobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 203)
  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 203)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 203)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Photobacterium"
                     /db_xref="taxon:657"
     Protein         1..203
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=22119
     Region          1..201
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Region          91..117
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(93..94,97..98,100,127,130..131,134..135,137..138,
                     160,163..164,167..168,171)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          122..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 mevyeteeqq vealkswwke ngkavvlgav iglgglygwr yyqgevqttk eltsdaysqv
       61 mttldsgsen avadvqafis anessqysvl aalqlaktqv elsdldgaik qltwaisqtk
      121 dqailplaqt rlariyaeqq kfdealaeld kvtatswqsk iaelrgdill lkgdviaark
      181 ayisaqqlga spalqmkldd laq
//
LOCUS       WP_011218136             361 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Photobacterium
            profundum].
ACCESSION   WP_011218136
VERSION     WP_011218136.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium profundum
  ORGANISM  Photobacterium profundum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 361)
  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 361)
  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 361)
  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 361)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Photobacterium profundum"
                     /db_xref="taxon:74109"
     Protein         1..361
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39174
     Region          1..357
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mqlkdvikkl alittvasvl ftplivqaas aeykwkmvtt wpknfpglgt gandlanlin
       61 emsngriqvk vygakelvga levfdavsrg taemghgaay ywkgkvpagq ffaavpfglt
      121 aqemngwiys ggglalwqea yapfgiipmp ggntgvqmgg wfnkeiktld dlkglkmrip
      181 glggevlkra ggtpvllpgg eifpalqsga idatewvgpy ndmafglyka akyyyypgwh
      241 epgttleali nkkafdklpk dlqaivlnat kvansnmlae ytarnnaalq slvtdhkvkl
      301 lpypaevlsq lktlsdevva eeaqkdemsk kvyasyiafr dqavdwhavs eqaylnarnp
      361 e
//
LOCUS       WP_011227339             251 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Streptococcus thermophilus].
ACCESSION   WP_011227339
VERSION     WP_011227339.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thermophilus
  ORGANISM  Streptococcus thermophilus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
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
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Streptococcus thermophilus"
                     /db_xref="taxon:1308"
     Protein         1..251
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=28210
     Region          5..>239
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mteiikfdhv tkrygdkivi dnlnfsiktg efitilgtsg sgktttlkmi nrliepssga
       61 vifdgsqidq ldeitlrrri gyvvqqiglf phqiveenia ivpkllnwdk ktikarvsel
      121 lsliklpydq yakrypnels ggqqqrvgva ralaadpsvt lfdepfgaid aitrselqee
      181 lltihktypn ktfvfithdi yeafklgtrv mimdegkiaq fdtpeailkk pandfvkrlp
      241 dtaknqeslw g
//
LOCUS       WP_011227767             180 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit [Thermus].
ACCESSION   WP_011227767
VERSION     WP_011227767.1
KEYWORDS    RefSeq.
SOURCE      Thermus
  ORGANISM  Thermus
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae.
REFERENCE   1  (residues 1 to 180)
  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 180)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 180)
  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   4  (residues 1 to 180)
  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   5  (residues 1 to 180)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Thermus"
                     /db_xref="taxon:270"
     Protein         1..180
                     /product="TRAP transporter small permease subunit"
                     /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=19848
     Region          3..170
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mrallalsra idalsegvgr iivwlvlavs llsagnalmr yafryssnay leaqwylfsl
       61 ifllggayal khnahvridl vygrlskrtq awidlvgtll flipmslgvi ylswdwvana
      121 vairemspdv gglprwpiki alpvgfalla lqglselikr lafltghlpd wtpgeeeevv
//
LOCUS       WP_011227769             359 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein [Thermus].
ACCESSION   WP_011227769
VERSION     WP_011227769.1
KEYWORDS    RefSeq.
SOURCE      Thermus
  ORGANISM  Thermus
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae.
REFERENCE   1  (residues 1 to 359)
  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 359)
  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 359)
  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 359)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Thermus"
                     /db_xref="taxon:270"
     Protein         1..359
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40198
     Region          1..354
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkrrdflkra gigvaasaaf gpvfaqgspt vrwrmassfp ksldtiygaa evladrvsal
       61 tggrfqirvy qageivpglq vmdavqqgtv eaghtasyyy vgkaqvlafd tsvpfgltar
      121 qqnawmyhgg gielfrpifa dfniiqfpgg ntgvqmggwf rkevrsladl kglkmripgp
      181 ggqvmsrlgv vpqvlaggdi ypalergtid atewvgpydd eklgfykvak yyyypgwhep
      241 gpmlsfyvnl qewrklpkey qqafevaaae anqwmmakyd rvnppalqrl lragvrlrkw
      301 pneimqaaqk aafewfeeea akdatyrkvy tawkafreeq yrwfavaelg yaqfafpgv
//
LOCUS       WP_011228602             387 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Thermus].
ACCESSION   WP_011228602
VERSION     WP_011228602.1
KEYWORDS    RefSeq.
SOURCE      Thermus
  ORGANISM  Thermus
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae.
REFERENCE   1  (residues 1 to 387)
  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 387)
  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   3  (residues 1 to 387)
  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   4  (residues 1 to 387)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 387)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 387)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 387)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Thermus"
                     /db_xref="taxon:270"
     Protein         1..387
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41533
     Region          25..365
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(99..101,122..123,172,223,247)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mrkigflvag vaalglalaq snvikiatms plsgpqaalg eqiklgaela veeakerfka
       61 lgfelvlvpy ddqanpdvgv ananrmindp dilglvgtln sgvaipasev larvnlvmvs
      121 pantnpvvtd rklpnvnriv grddvqgpaa aefvyndlkl rrvfvihdkt aygqglaeef
      181 rkrfealggr vvafigteeq snfvpiinqi raqnpqlvyf ggiysqigpf tkqlrerglr
      241 mplmsgdgld sseferlags qnakgayytt vagpvsafpq akalaerfka kygkdiegfg
      301 iyaydaarvi laalenaika nggkkptraq vaqevrkvkl egitgtiefd skgdiqkaky
      361 fvmqvagtgn wadnklikvi evaapqk
//
LOCUS       WP_011230912             478 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase [Geobacillus].
ACCESSION   WP_011230912
VERSION     WP_011230912.1
KEYWORDS    RefSeq.
SOURCE      Geobacillus
  ORGANISM  Geobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Geobacillus"
                     /db_xref="taxon:129337"
     Protein         1..478
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=53994
     Region          51..>470
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 manvggrrkp aadarleaik klfpeavvdg gidwellkkv fggherqeay eftwpgkaea
       61 rrlaelpasg vlrpdqaask qwettnnwyi egdnlealkl lrtshagtiq miyidppynt
      121 gkvltykdnw rkgkavvpsg iqeearahag wlnmmyprlw varellaetg aifisiddte
      181 qanlrkmcde ifgernfvat fiwqrafspv nmnkfasrnh dfilcyakni drlawyglpr
      241 hpeadgryan pdndprgpwt sgdlsvgppi pekiyeivtp sgrvvsppng ycwrvtkerf
      301 aelaadnriw fgkdgngvpr lkrflsevks tvtpltiwth devshsqeak kelkelfggl
      361 avmdypkpvk liqrmvaltt rdddlildff sgsattahav mqqnaedggr rsflmvqlpe
      421 plaetsaayr agfrticdig rerirragek ivretgktel digfrvfrle kkskqpar
//
LOCUS       WP_011233572             430 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: amidohydrolase family protein [Idiomarina].
ACCESSION   WP_011233572
VERSION     WP_011233572.1
KEYWORDS    RefSeq.
SOURCE      Idiomarina
  ORGANISM  Idiomarina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae.
REFERENCE   1  (residues 1 to 430)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Idiomarina"
                     /db_xref="taxon:135575"
     Protein         1..430
                     /product="amidohydrolase family protein"
                     /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=47114
     Region          28..422
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mkikivaalf vaaialiils lptprqesae nsnsfilgpv kifdgetisk aayvevldgy
       61 ikdlhmeqpd sqlrkvdgqn rwlvpglida hvhtwgdale qslergvttv idmfghpnfl
      121 rqhqpqratt kfsrkadifg agllitapng hgtqygievs tlskpqeaek likqrinags
      181 dfikivytrn gsayahapsi seqglqaair aahkqnylav vhiadhdsal daveagadgl
      241 vhsffdqpvs dellallkin gvfviptmtv yegmlrgsin deillnnetl kisasakstl
      301 nrnfpnsgrf pehfytnlli ntkrmhntgi pilagsdapn pntahgwsll velllfqeag
      361 mpteailksa tskpadafsl adrgriregm kadflllqks pykdlktile plrvwkngyl
      421 vsskdsarnh
//
LOCUS       WP_011235311             441 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Idiomarina
            loihiensis].
ACCESSION   WP_011235311
VERSION     WP_011235311.1
KEYWORDS    RefSeq.
SOURCE      Idiomarina loihiensis
  ORGANISM  Idiomarina loihiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Idiomarina.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 441)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Idiomarina loihiensis"
                     /db_xref="taxon:135577"
     Protein         1..441
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=50134
     Region          3..436
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mintievryk gepvgalsyn kgdtaarfey lsefveknip lapltmpaek griysfpgln
       61 wdtfrglpgm ladslpddfg navlnqwvaq qpdrteplsp lerlqytger gmgaleyhpa
      121 rknqtnaknk dieleslmrl aqevldarkg frqrthfdda adkemmqall avgtsaggar
      181 pkavlafnkd fsqvrsgqgl vpegfehyll kfdgvkerdp sqqtfgdplg ygameyvyyl
      241 matkagihmm pchlldegnr rhfvtkrfdr ignekkhiqt ltaikhvnyh digafsyeel
      301 fqvarqlrlp radavdlfrr mvfnhvatnh ddhsknfgfm ledkewrlsp aydvafsykp
      361 gnpwveqhwm slngkrsght radfyaladv qlpkverkei daiiddvvna vsqwrelate
      421 hevpkaltds ieghlrlkdf a
//
LOCUS       WP_011235867             144 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Aromatoleum aromaticum].
ACCESSION   WP_011235867
VERSION     WP_011235867.1
KEYWORDS    RefSeq.
SOURCE      Aromatoleum aromaticum
  ORGANISM  Aromatoleum aromaticum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Rhodocyclaceae; Aromatoleum.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Aromatoleum aromaticum"
                     /db_xref="taxon:551760"
     Protein         1..144
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14279
     Region          1..139
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkkvqqgftl ielmivvaii gilaavalpa yqdytiraqv selmsltdga kvavaetfqs
       61 tgalpasdaa agyggavgky tasvaigpsg vitstggvda ndaiaaetit ltpkadatgv
      121 lvwacagsvd akyrpstcra aaae
//
LOCUS       WP_011237057             727 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Aromatoleum aromaticum].
ACCESSION   WP_011237057
VERSION     WP_011237057.1
KEYWORDS    RefSeq.
SOURCE      Aromatoleum aromaticum
  ORGANISM  Aromatoleum aromaticum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Rhodocyclaceae; Aromatoleum.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 727)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Aromatoleum aromaticum"
                     /db_xref="taxon:551760"
     Protein         1..727
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76943
     Region          10..716
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 melapplprt splhdflapg siaiigastd ptkrgykamv glikdgypga iypinpkvdn
       61 vlgvrtyatl ddipgpvdla lictpaatvp glvadcgrkg vkgaailasg fretgpagar
      121 leqqvlaaar eggvrligpn tsgmfnlhkk vnllalanvk pgnigfisqs gnmllslvle
      181 aehnghvgfs tyvgpgnqtd igfndylryl gedpdtrvat fyvegfrdgq rflhnareit
      241 avkpvvvyks gateqgkkaa sshtgalags yamtvdllrq vgvsvvqhsn eilpvaeglg
      301 llqhapgkrv avvsdgggqa tiasdriiea glelaelgea tkkrlgaill pqaspvnpvd
      361 vagssdanpa lladclaiva dddnvdavfl vgmfggyhir faedllggem rgaesmiela
      421 rridkpvvvy slyapvkppa lrrlheaglp vytsieyavr vlaalgergv ylqdaanqap
      481 lpammpndat laifaaaqae arnlfefeak tllrahgvdv paealvrnvd eldevaarfg
      541 drplvmkvvs kdilhksdag gvklnlhgra alreafdqii gschaykpaa dikgvlitpm
      601 arkgieviig vsrdpifgpv lmfglggifv eiledvafra iplsryaars mveqirarri
      661 lqgargeaav dkealvdlll kvssivaayp qlaeldlnpv ilyedgyaiv darvivnqtv
      721 lnpkdea
//
LOCUS       WP_011236397             202 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Aromatoleum aromaticum].
ACCESSION   WP_011236397
VERSION     WP_011236397.1
KEYWORDS    RefSeq.
SOURCE      Aromatoleum aromaticum
  ORGANISM  Aromatoleum aromaticum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Rhodocyclaceae; Aromatoleum.
REFERENCE   1  (residues 1 to 202)
  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 202)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 202)
  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   4  (residues 1 to 202)
  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   5  (residues 1 to 202)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Aromatoleum aromaticum"
                     /db_xref="taxon:551760"
     Protein         1..202
                     /product="TRAP transporter small permease subunit"
                     /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=21689
     Region          4..171
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mgtllklshl idafsrfigk siiwlvlaat lisaanavar kafsigsnaf leiqwylfaa
       61 vfmlgagyaf lqnahvridv iankmssrmr nyvdvfgiiv fllplcyfmi sfswpvvhga
      121 yvsgemssna gglirwpvya lvpvgfallg lqavselikr vafltgrgpd plataghdet
      181 knhihaavgd tseanaages qk
//
LOCUS       WP_011237623             371 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Aromatoleum aromaticum].
ACCESSION   WP_011237623
VERSION     WP_011237623.1
KEYWORDS    RefSeq.
SOURCE      Aromatoleum aromaticum
  ORGANISM  Aromatoleum aromaticum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Rhodocyclaceae; Aromatoleum.
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   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   3  (residues 1 to 371)
  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   4  (residues 1 to 371)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 371)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 371)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Aromatoleum aromaticum"
                     /db_xref="taxon:551760"
     Protein         1..371
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39037
     Region          26..363
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(102..104,125..126,175,227,251)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkrsvvalav lglglslaha qetvvrlgsv apltgtishl gkdnengarl aiedanakgv
       61 tidgkkvrfe llgeddqadp rtgttvaqrl vdadvkgvvg hlnsgttipa sriynqagvp
      121 mvspsatnpt ltrqgypgvf rtiandvqqg gmlgkfivgs lgaktiaiid drtaygqgla
      181 detekavkaa ggkvvareft tdkatdfnai ltkirgvkpd aiffggmdaq agpmlrqlkq
      241 lgieakfvtg dggcspemik lagdainatt ycsmpglaid kmpggpefrt rykarfntdv
      301 qiyspyayda ataiiramqa adsaepskyl palkksnfqg vigtvafddk gdikegavtm
      361 yqyrngawsp m
//
LOCUS       WP_011238709             137 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Aromatoleum aromaticum].
ACCESSION   WP_011238709
VERSION     WP_011238709.1
KEYWORDS    RefSeq.
SOURCE      Aromatoleum aromaticum
  ORGANISM  Aromatoleum aromaticum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Rhodocyclaceae; Aromatoleum.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Aromatoleum aromaticum"
                     /db_xref="taxon:551760"
     Protein         1..137
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14030
     Region          1..135
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mksrtggftl ielmiavavv ailaaiavps ymesirksrr sdattslaki qlaqetyrln
       61 nnsygtlaal glgatstegy ytiaitegti sttgytatan aisgksqasd sdctaitmtv
      121 tgggntvsnt patcwsk
//
LOCUS       WP_011238890             806 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Aromatoleum aromaticum].
ACCESSION   WP_011238890
VERSION     WP_011238890.1
KEYWORDS    RefSeq.
SOURCE      Aromatoleum aromaticum
  ORGANISM  Aromatoleum aromaticum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Rhodocyclaceae; Aromatoleum.
REFERENCE   1  (residues 1 to 806)
  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 806)
  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 806)
  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   4  (residues 1 to 806)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..806
                     /organism="Aromatoleum aromaticum"
                     /db_xref="taxon:551760"
     Protein         1..806
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=87952
     Region          60..796
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 madfeplpad rlrvvcapdv fefdstaglp dlpgglgqar aedalrfgla mrqpgyhvfv
       61 lgesgtgrhv avqrvlrefa dqgevprdlc ylhnfddplr prllnlpagr gamlradmqa
      121 firelrpaid aaldsdtyss rseslqeahk sreeaalrel gqacaaegis llrtpegfvf
      181 apirdgetms pegfealqqp erdaieakvg awserltdll eqfpgwrkel heamkraard
      241 alapavshlm rglreryadl eqvgsflsai saelldsgde waggeneeda sedeartrfh
      301 ryqinllvdh sathgapvvy ednpnfvnli griehvaqmg tlvthfnlir agalhracgg
      361 yliidverll gqpfawdglk rvlrgreiri eppaeaqgwt sivtlepepv pcdikvvlig
      421 drelffllte hdpdfpelfk vgadfdddlp rtaenvvrya hllatlarsa dllpldrsgi
      481 agmvehgari aedggrltlq trlladvmre adyharnakl tiigraqvdl avasrarrya
      541 ryservleam vegttlists gercgqingl vivdlagerf ghpvritata rlgegdvidi
      601 ereielggal hskgvlilsa flasryarhq plslsaslvf eqsyvpvegd saslaelcal
      661 lsalaqlpir qsfgvtgsvn qlgevqvigg vnekvegffd lcaicgltge qgvvipsasv
      721 rhlmlrndvv eaarngqfhi ysvatvdeam tvltglaagt pdakgvlpke sinqrvasal
      781 atmtaakhaf aegpgrthrh rrrsdh
//
LOCUS       WP_011239266             713 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Aromatoleum aromaticum].
ACCESSION   WP_011239266
VERSION     WP_011239266.1
KEYWORDS    RefSeq.
SOURCE      Aromatoleum aromaticum
  ORGANISM  Aromatoleum aromaticum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Rhodocyclaceae; Aromatoleum.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Aromatoleum aromaticum"
                     /db_xref="taxon:551760"
     Protein         1..713
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=76770
     Region          23..711
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mnrlsstsgd naprshprci vlallagvga apvfaaeaap vlnpvvvtgs rveaesfdlp
       61 fsvdvvdmar vragnlgvna sealtgipgl vvqnrqnyaq dlqisirgfg arsafgvrgv
      121 kliadgipas npdgqgqaat fnldvaerie vlrgpfstiy gnhaggviql fsrdpkgtps
      181 vrggalagsw gttrigvgse gekdgvgyll dasrfdtdgy rdhsaatreq afaklnfapd
      241 adsrltltas glrqpdtedp lgltwatyrr dpratesvak tfdtrkridh lqggatyerr
      301 fgddrlqlva yagqrsvtqy qsipagpqan prhsggvidf drdfhgvgar wigrrelgpg
      361 kltftagidv drseddrqgf enfigttlgv kgrlrrdemd tvtsidpyvq taweqgawqw
      421 taglrhsrvk fdvdddylan gddsgaltfr ettpalgvvy klspalnfyg saargfetpt
      481 mtelaysgag gaagfnfgle patstqlelg vkafvgdntr lnaaifqvrt dnelvvesss
      541 ggrtvfknag ttlrrgvela ldsefspnwr arlsvtrlqa iydetfvtgs gtaaktiadg
      601 rrlpgipals ayaelewipv ggiaaaleal yrskmyvedt nteraapaha lanlrftaeq
      661 ksgpwtfnem lrldnlfdre hvasvivgdg ngrfyepgpe rswyagvras yrf
//
LOCUS       WP_011239019             200 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Aromatoleum aromaticum].
ACCESSION   WP_011239019
VERSION     WP_011239019.1
KEYWORDS    RefSeq.
SOURCE      Aromatoleum aromaticum
  ORGANISM  Aromatoleum aromaticum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Rhodocyclaceae; Aromatoleum.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Aromatoleum aromaticum"
                     /db_xref="taxon:551760"
     Protein         1..200
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21789
     Region          1..187
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mrrliigisg asgaiygira lqaladvqev ethlvlspsa krtiieetdw tvekvealad
       61 vvhthrdiga aissgsfrta gmliapcsik tlsglvasyn dnlltraadv clkerrrlvl
      121 lvretplhlg hiemlaqatr ygavvlppvp afynrpqtid divnqsvgka ldqfeiphhl
      181 fkrwkepvae eaatklkvav
//
LOCUS       WP_011239755             290 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Aromatoleum aromaticum].
ACCESSION   WP_011239755
VERSION     WP_011239755.1
KEYWORDS    RefSeq.
SOURCE      Aromatoleum aromaticum
  ORGANISM  Aromatoleum aromaticum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Rhodocyclaceae; Aromatoleum.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Aromatoleum aromaticum"
                     /db_xref="taxon:551760"
     Protein         1..290
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=31652
     Region          63..120
                     /region_name="YlmC"
                     /note="Sporulation protein YlmC, YlmC/YmxH family,
                     contains PRC-barrel domain [General function prediction
                     only]; COG1873"
                     /db_xref="CDD:441477"
     Region          176..253
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mnmnartkrk liaalaatav glpaymghaa eerpappats treappaaap daataaqsrv
       61 araskligae vknpvgeklg eikdlvvdvr nqtahyavls fggiagiadk lfaypvsmlr
      121 wgpgkdelil diqrsrleaa pgfgpgnwpd wgvdsyrrsv deyfktdrpt algpnpqlmq
      181 asklldvkve drekrnagei kdlvvsladg tvpyavldld kawsaddkli plplssfefs
      241 tddekvmlke sregfdtsrg fdekhwpdmn dpalrrdmnk spgereqdrk
//
LOCUS       WP_011239699             149 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Aromatoleum aromaticum].
ACCESSION   WP_011239699
VERSION     WP_011239699.1
KEYWORDS    RefSeq.
SOURCE      Aromatoleum aromaticum
  ORGANISM  Aromatoleum aromaticum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Rhodocyclaceae; Aromatoleum.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Aromatoleum aromaticum"
                     /db_xref="taxon:551760"
     Protein         1..149
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=15947
     Region          32..111
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 masinppgtt ttttqhadiv gsgnedrsgp gpqvmaastl egddvvnrag edlgnikevm
       61 idvqsgrvay avlstggflg lgrklfaipw galtldtdrk cfildvdaer lknapgfdkd
      121 hwpsmadttw aseihayygq qnywqppsh
//
LOCUS       WP_011241948             737 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Ruegeria pomeroyi].
ACCESSION   WP_011241948
VERSION     WP_011241948.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria pomeroyi (Silicibacter pomeroyi)
  ORGANISM  Ruegeria pomeroyi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 737)
  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 737)
  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 737)
  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 737)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Ruegeria pomeroyi"
                     /db_xref="taxon:89184"
     Protein         1..737
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=78115
     Region          13..734
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mtdatsqktd tltaeelaai eekydesaat rpvspgfarf lkvvalsfat yhyltagfal
       61 ptdhwhmgwh lsglfiltya lfpairtrgt ydlktglmhy ggvpyldill mglgvasaly
      121 lgfawrgvpw lgieeqtfrm gnpngydmlf gsilivlvld iarrtlgwvl paiicvfmay
      181 alfgpvfpgi lqhpgvkirt fvssmyfpqe gifgvtlwvv stivfhfvlf gviaqrtglg
      241 qlfidnatil agrytggpak vsvvssaffg tisgssvant vstgaltipn mkrlgypghf
      301 aggveaaasa ggqitppimg aaafimaefl evpyttivia aifpallhyv gvfsvvhlma
      361 rrlnlqglsk emlprlgavw regwanmvpl vgllvvlfsg ytpymsafcg islaivtgma
      421 rrsapvtlay paafiafvvw kctgggfdlp msallvaltl lgslnpqeri rlpqmaetfe
      481 tgvkyalavg aaaaavgivv gvinttgvgf rvgfmvtqsa gelgaslhsl lsfgrfelfs
      541 vtditlfisl ifiavacilm gagipttaly imlvsvaqpa laqlgvppia shmfvlyygv
      601 vaeitppvct sayaaaaian snpfrtgisa ftlglgkiva pmafvyapvl livsqtgfdl
      661 wtfsytatsc ilgviclsva vvgywlapmg alfrvllama glvfiapslq adliaaliaa
      721 pavlsqivlr rrtteag
//
LOCUS       WP_011242018             211 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Ruegeria pomeroyi].
ACCESSION   WP_011242018
VERSION     WP_011242018.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria pomeroyi (Silicibacter pomeroyi)
  ORGANISM  Ruegeria pomeroyi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 211)
  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 211)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 211)
  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   4  (residues 1 to 211)
  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   5  (residues 1 to 211)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Ruegeria pomeroyi"
                     /db_xref="taxon:89184"
     Protein         1..211
                     /product="TRAP transporter small permease subunit"
                     /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=22559
     Region          13..178
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 maghasvlqd gsalsrldra llrlerglal isglavfslm llavvsvggr namnaplpgy
       61 vdwieqampl iafmgiafvq regghirmdl vigqlkgral wlfelisvll ilglmmllvw
      121 gswahflraf dmgaplwsrd ssidigiplw pskllapvaf svlclrlglq vwgygrafvl
      181 gleapvavpl iqdvaaqaaa eaeqlaghdn g
//
LOCUS       WP_011242891             126 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Synechococcus elongatus].
ACCESSION   WP_011242891
VERSION     WP_011242891.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus elongatus
  ORGANISM  Synechococcus elongatus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Synechococcus elongatus"
                     /db_xref="taxon:32046"
     Protein         1..126
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=13692
     Region          2..105
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(4,22..23,31,34,36..37,39,42..43,45,55,60,69)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(22,55..56,58,85)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mntydqiyav vrqipvgcva tygqvatlag lpgkprvvgy alyrvapglt dsipwhrvvn
       61 argavsmsal rhgsdylqrh lleaegiefd pqgrlslhry rwqpdfaspq sgecplgsis
      121 npdnds
//
LOCUS       WP_011242580             610 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Synechococcus elongatus].
ACCESSION   WP_011242580
VERSION     WP_011242580.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus elongatus
  ORGANISM  Synechococcus elongatus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 610)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Synechococcus elongatus"
                     /db_xref="taxon:32046"
     Protein         1..610
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=61502
     Region          <48..196
                     /region_name="myxo_dep_M36"
                     /note="myxosortase-dependent M36 family metallopeptidase;
                     NF038112"
                     /db_xref="CDD:468355"
     Region          146..396
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          297..540
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mapfnfsaft fvklfsrlfn fnskpiaqsq tqnltenagl fngqliasdp ngdpitflla
       61 pnqvapagft lnsngsysfd qddtsydslg lgdtqviaid yvvkdsrgav sqtrtlsinl
      121 agtndaptit agpvvdansi tftaedidsd tltarvgttn lmpgtvnngs pttstitald
      181 talfgelnvf dgtdsvgvgl fvgigtigad tltaigtnpa vlygfegddr ltgadqddti
      241 lggdgndtii eisgnnlieg nnnndsivgg tdsdringga gadtilggdg adtidgglgn
      301 dsifgdsgnd nirgfgdsnt ilggsgndti egtiagsnsi dggenddvit eigfgstllg
      361 glgndsilgf sastinggdg sdtinvefgn ntidggmgnd sieiainpsf tisgsgntvs
      421 gsngndtiia ingsnliegn ndndsivggt dsdtinggtg adtltgglgs dtfsfaatgd
      481 giaatsgeng svtfgngfdy itdfesidsi ivgtdgftiq ssvgtafidg dgnyvivsvg
      541 misdifaiag vltdttfesr dpgmgdsfte lllfkasnam mgdvitattt petliiggsa
      601 ldmlqpyscc
//
LOCUS       WP_011244212             615 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Synechococcus elongatus].
ACCESSION   WP_011244212
VERSION     WP_011244212.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus elongatus
  ORGANISM  Synechococcus elongatus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 615)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 615)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Synechococcus elongatus"
                     /db_xref="taxon:32046"
     Protein         1..615
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=65861
     Region          39..611
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 maiarrlgws lptalagaia laglllspla ispltqpgrw ldavllsaaf rlrgpqapdp
       61 aiaivvided slrlgdlfta aelearppla dlqdwpwprr iyalalqrlr aagarrvifd
      121 ivfatptrfg pdddrrfada iaqagssvtl ageleqvdrs aglsqaslaq piyehpfgla
      181 nliagadgsl qaipgqdwlq pwqilqardr pplsnlasaa lgqappplsl ginysgpegt
      241 yprwpfwalf dpelwqgplq qgavfrdrdv ligasasslg drhatpfads magveiqana
      301 iatlrsqrgl rslpqvwlsl llilvallqi wgvqrcpspl skalwtlgit savllacfia
      361 flqtwlvspt alllvpllag igdsansawq vqrerrslrr alalrvspal lgtilaqrda
      421 vanqlgghnc eavilfsdlr gftqlssqid stvlvallnr yfeamaqpil aaqglidkfv
      481 gdaimaefgl plsrgtviea qaaiqaalam rrslarlrae lvaeglpplf hgiglnfgtv
      541 vagnlgaper leytvigdav niaarleslt ktlgydiiis qalyeqvqeq vevmplglqq
      601 lrwaiaagvh lcclg
//
LOCUS       WP_011245303             497 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Shouchella clausii].
ACCESSION   WP_011245303
VERSION     WP_011245303.1
KEYWORDS    RefSeq.
SOURCE      Shouchella clausii
  ORGANISM  Shouchella clausii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Shouchella.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Shouchella clausii"
                     /db_xref="taxon:79880"
     Protein         1..497
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=54413
     Region          3..497
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 msnaffqvhp tdnvivslkd lqkdqriqfk eehiplsrdv psghkiaird iavgedivky
       61 gfpigkaskp iqkgdwvhtd nvvtklsgtl eyqyqhksqp frvresattf dgywrkngea
      121 girneiwiin tvgcinktae ilakmgneaf qeegidgiyh fphplgcsql gddlhntqki
      181 lgrlvehpna aavlvlglgc ennfiesfkq vlseideerv kflavqdved eleegldllg
      241 slvsyaktfk kepiplsklk vglkcggsdg fsgitanpmv gafsdmlisa ggttiltevp
      301 emfgaetilm ervtdkkvfn dlvdvvngfk eyflkynqpv yenpspgnkk ggittleeks
      361 lgcvqkggfa pvvdvlpygs kvtkqglniv qgpgndlvsv tnlaaagahi vlfttgrgtp
      421 fggpvptvki stntalfekk knwidynagq liqgssmddv kedfftyllq vasgekktkn
      481 eqygfkeiai fkdgvtl
//
LOCUS       WP_011246594             171 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: L,D-transpeptidase [Shouchella].
ACCESSION   WP_011246594
VERSION     WP_011246594.1
KEYWORDS    RefSeq.
SOURCE      Shouchella
  ORGANISM  Shouchella
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 171)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Shouchella"
                     /db_xref="taxon:2893057"
     Protein         1..171
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=18649
     Region          32..154
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
     Site            order(107,111,114,127..130,132)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mkwsflcifl vmslqplqmp gdtdweveka svivnvrtnt lalieanhia eihpvatgkk
       61 gdetplgqft vlvkveqpyy rkknipggda rnplgsrwig fdalgtagrt yglhgtnrpg
      121 sigysasagc irlanptier lyqkidigsk ifivnehrsf qaiakeagli n
//
LOCUS       WP_011246805             280 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Shouchella].
ACCESSION   WP_011246805
VERSION     WP_011246805.1
KEYWORDS    RefSeq.
SOURCE      Shouchella
  ORGANISM  Shouchella
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 280)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (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   5  (residues 1 to 280)
  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   6  (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 12204073
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Shouchella"
                     /db_xref="taxon:2893057"
     Protein         1..280
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31831
     Region          18..96
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
     Region          122..279
                     /region_name="YdeE"
                     /note="Predicted transcriptional regulator YdeE, contains
                     AraC-type DNA-binding domain [Transcription]; COG3708"
                     /db_xref="CDD:442922"
ORIGIN      
        1 mldsieyien hldnelllde iaavacmsrf hfqrmfrmlt gyavseyirn rritvaaqel
       61 vhskskvidv amkygyespe sftkafrrih gispsdakkh sqslkaypki sfqiqlkgdv
      121 emdykivekd aftvvgksir tttiggennr kiaafwnesn rnglskqlak ncgplgllgi
      181 cidfdkqqen ltyliaaekn sdqipvdwet rqipaatwai fpvhgampna mpkvwerifs
      241 ewfpatgyeh sggpemevyv sdadpyskdy yseiwvpvkk
//
LOCUS       WP_011248389             280 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Shouchella clausii].
ACCESSION   WP_011248389
VERSION     WP_011248389.1
KEYWORDS    RefSeq.
SOURCE      Shouchella clausii
  ORGANISM  Shouchella clausii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Shouchella.
REFERENCE   1  (residues 1 to 280)
  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   2  (residues 1 to 280)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Shouchella clausii"
                     /db_xref="taxon:79880"
     Protein         1..280
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31140
     Region          <61..>189
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          211..274
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mntlfllfll ltffglilgl ikpalvrfpt rkrvfaygip afiitaflfg ntlpaetaqs
       61 aqldrsqaki etleaslqdk etemeeltva leeaeeslke seeqlellqa eegdvdgsfe
      121 eqleeaklew eeefreqiee eleeritaei sedyedklaa lddkikekeq tieekettis
      181 kleeevasas tnngnetatt etetaqsses astdscgpgt vkinsasese lqaiyeigpd
      241 raaqiiqlrp fssyndmkri kgigdaraea ienqgivcfd
//
LOCUS       WP_011251637             423 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Gluconobacter oxydans].
ACCESSION   WP_011251637
VERSION     WP_011251637.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter oxydans
  ORGANISM  Gluconobacter oxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 423)
  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 423)
  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 423)
  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 12807598
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Gluconobacter oxydans"
                     /db_xref="taxon:442"
     Protein         1..423
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43568
     Region          14..84
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          <174..289
                     /region_name="PRK10856"
                     /note="cytoskeleton protein RodZ"
                     /db_xref="CDD:236776"
     Region          268..335
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 msppssnrpf sqpsdqpsvg tvlrarreel gwrledvaew lrirpkllaa leaddlsklp
       61 gvayavgflr tyahamqlda dalverfrrd trgavtrkpe lvfpqpesdr glpvgvlvga
      121 glvvvvaayv gwyrftehdn paqrqvpava elmpgaatpa mtspqvasvm pgraptpeph
      181 apvtassvpa tpapavaptq napapdvsaa psvaqstpst vapsvaplas dddseplpag
      241 eaapsqqaga igqpatdlpp avpegavvlr alapvwtqvr drdghvlmsr vmqpgeswqg
      301 dpagapfrms fgnaggivlt tagatsaplg kegqvrrnve vtadairsga fgsgialpvq
      361 pnapvpvpga taapstvapa pvpprvppvs vprkapaape vsaddlnarq lehqpleqss
      421 psh
//
LOCUS       WP_011252829             459 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Gluconobacter oxydans].
ACCESSION   WP_011252829
VERSION     WP_011252829.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter oxydans
  ORGANISM  Gluconobacter oxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 459)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Gluconobacter oxydans"
                     /db_xref="taxon:442"
     Protein         1..459
                     /product="amidohydrolase family protein"
                     /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=48875
     Region          22..451
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mtirsafaal llatpaalsa gsamaepvaf eharlidgtg alaqpdatvv idngtiisvg
       61 ipapaevrhv dltgktlmpa lisdhvhvgl vkgtgasrdn ytranilaal kqysdygvlt
      121 vtalglnrsp lfdtlrqeqh dgrnpgadly gvdqgigapd gvppaamvkg vgpdqvfrpt
      181 tpeetrkdvd qmiaehtdlv klwvddfrnd vpdgktypml ppaiyqavid eahqhgtrva
      241 vhihdlavak aivaskadil ahgvrdqpvd hdliaamlrq gtwyiatldl deanylyaeq
      301 pellsnpfvl agidpalrre ftdpkwraet makpltkash yalsvnqknl avlyragvkv
      361 gfgtdsgaap trvpgfaehr elyltvqagl spvqaislat gnaaallhls drgviapgrr
      421 adllvvngna denigavdqi dqvwqrgtlv shgpvrskn
//
LOCUS       WP_011253078             682 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Gluconobacter oxydans].
ACCESSION   WP_011253078
VERSION     WP_011253078.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter oxydans
  ORGANISM  Gluconobacter oxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 682)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 682)
  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   3  (residues 1 to 682)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Gluconobacter oxydans"
                     /db_xref="taxon:442"
     Protein         1..682
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76198
     Region          8..677
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mstedftddm dairliffde cdeqltllee eltaledepe ngekintifr cvhsikggaa
       61 afgmedlvrf shlfesvldr frsgelsvna esirvflkck dalsdivsdf knggstyeva
      121 peitadlehy lgsdasepep aseevrtedi fgmsfapvki eidapseqqf sivltvspef
      181 yergddirni lmaleglgqi kvqvdsdavp lladispgqs yltwqilltt eksresidei
      241 fdwcgddlqa vitsvpeeae qtkipsapva eektdppvrk gterkdsatv rvdiqridkl
      301 vdligelvin qgaiqsqmrr nkvpgdsflg svvtaqeqli helqenvitm raypiktvfq
      361 klgrvvreta rltekqvrlv legedtevdr sileklsdpl thmvrnaidh giespevraq
      421 agkdpegllr lrafqrsgri iveiqddgag ldpdriyeka vekkiiekgq rldreeiysl
      481 ifepgfstva evtdvsgrgv gmdvvkqslq qingrifiss skgkgtifsi slpftlsvie
      541 giifksegqd fvvpinnvsd tiifdnskaf higegkygyp yrdgylsviy asdlldvpsd
      601 kknqkicfvi eneneekmaf ivdkiidqsr fvvknledny rkiacfstat ilgdgnvafi
      661 ldveflfgel lkkresslee rv
//
LOCUS       WP_011253119             675 aa            linear   BCT 20-JAN-2025
DEFINITION  potassium transporter Kup [Gluconobacter oxydans].
ACCESSION   WP_011253119
VERSION     WP_011253119.1
KEYWORDS    RefSeq.
SOURCE      Gluconobacter oxydans
  ORGANISM  Gluconobacter oxydans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Gluconobacter.
REFERENCE   1  (residues 1 to 675)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 675)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 675)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 675)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 675)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 675)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..675
                     /organism="Gluconobacter oxydans"
                     /db_xref="taxon:442"
     Protein         1..675
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=73335
     Region          56..675
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mepampehdg dhasnpphgv gipndsagiv qtieqarseg htheigggee gsgherpagm
       61 gallavlgvv ygdigtsply alqssvsivs spkapaqpwe imglasltfw almlivtiky
      121 vilimradhd geggiialms laqrvcksqh frwlfglvgi agtclffgds iitpaisvls
      181 avegietsvp sashiiipla mvvlvalfsv qvlgtgkigk afgpimvcwf svlailgikg
      241 iflyphilla lsptfalefi vlhgylsfia lgsvvlsvtg aealyadmgh fgrapirkaw
      301 lffvlpsltl nyfgqaalli rdphalsnpf yllvphwaqi pmlvlatfat viasqagisg
      361 sfslcrqliq lgylprtrim htnaseeaqi ylpslnwila fgalvlvlaf rtssalaaay
      421 giavtgtflc tcvlamvvfr rvfkwksatv aivfgfffiv dsiffsanvl kipdggwvpl
      481 aigiistiim ttwkrgrsli aarqqadsmp mgsflarlpq srtirvpgla vfltanpdiv
      541 pnsllhnlkh nkvlhdhilf vtvenldqpe aerghraivq elapnihrvi vrygfmempn
      601 lprallelna lgvafdaiqa syftshelvv rsrvpkmqlw rmwiflfllr naastteflr
      661 ippdrvvefg vriai
//
LOCUS       WP_011257362             309 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SPOR domain-containing protein [Xanthomonas].
ACCESSION   WP_011257362
VERSION     WP_011257362.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..309
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30603
     Region          200..265
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 myvralivvl ivlnagvalw walqpppapp pappqptgva rlellptlpg vggaalpgaa
       61 aatgsasaae sestasatpa ipatpastpv saavpaptpa avvstststp asttsasava
      121 aetphaaaep svttktaakp adsvaatatk pspttpspap ercaslgpfv aradadaala
      181 rvrgqasras vredkdagvs tfrvmlpnvg draaaqalvk riaaagmgdy yviaqgednt
      241 valgqyqsre raerrqaslv gagfpaqlvp sgsgqsrwwi dvrssaatsa lqgaagaarq
      301 rsldcaalr
//
LOCUS       WP_011257508             283 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Pseudomonadota].
ACCESSION   WP_011257508
VERSION     WP_011257508.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonadota (proteobacteria)
  ORGANISM  Pseudomonadota
            Bacteria; Pseudomonadati.
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   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 283)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Pseudomonadota"
                     /db_xref="taxon:1224"
     Protein         1..283
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30906
     Region          12..66
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msikamnwaw eqrlppnskl ilmaladsad eigkcwprvr liaekccase rtvqrvlkel
       61 eergflhier rfrgdggqss nayylclesp pvnlsspslt psdklspggd aavtppvtrq
      121 tsqgdrtvsp hepptrtink sslqlpakvi htpppspvpg eaekgacgal vwpsrlnere
      181 rsaiasmvsg ldandaqmll delagvmatq siktsperwf ravldrfhqg rfapsaglaa
      241 kekrlriqst paetpvqtas pevirhhler iqtmlgrkga tve
//
LOCUS       WP_011257760             117 aa            linear   BCT 20-JAN-2025
DEFINITION  PilZ domain-containing protein [Xanthomonas oryzae].
ACCESSION   WP_011257760
VERSION     WP_011257760.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (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   3  (residues 1 to 117)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 117)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..117
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12311
     Region          1..117
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 msamnarqgi lslalkdkpa lysaympfvk gggifvptpk rymlgdevfv lltlpdsser
       61 lpvagkviwt tpagaqgnrp agigvqfpdg pegeavrnki etllagltts dkpthtm
//
LOCUS       WP_011258433             635 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: potassium transporter Kup [Xanthomonas].
ACCESSION   WP_011258433
VERSION     WP_011258433.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 635)
  AUTHORS   Surovtseva,Y.V., Shakirov,E.V., Vespa,L., Osbun,N., Song,X. and
            Shippen,D.E.
  TITLE     Arabidopsis POT1 associates with the telomerase RNP and is required
            for telomere maintenance
  JOURNAL   EMBO J 26 (15), 3653-3661 (2007)
   PUBMED   17627276
REFERENCE   2  (residues 1 to 635)
  AUTHORS   Trchounian,A. and Kobayashi,H.
  TITLE     Kup is the major K+ uptake system in Escherichia coli upon
            hyper-osmotic stress at a low pH
  JOURNAL   FEBS Lett 447 (2-3), 144-148 (1999)
   PUBMED   10214935
REFERENCE   3  (residues 1 to 635)
  AUTHORS   Quintero,F.J. and Blatt,M.R.
  TITLE     A new family of K+ transporters from Arabidopsis that are conserved
            across phyla
  JOURNAL   FEBS Lett 415 (2), 206-211 (1997)
   PUBMED   9350997
REFERENCE   4  (residues 1 to 635)
  AUTHORS   Banuelos,M.A., Klein,R.D., Alexander-Bowman,S.J. and
            Rodriguez-Navarro,A.
  TITLE     A potassium transporter of the yeast Schwanniomyces occidentalis
            homologous to the Kup system of Escherichia coli has a high
            concentrative capacity
  JOURNAL   EMBO J 14 (13), 3021-3027 (1995)
   PUBMED   7621817
REFERENCE   5  (residues 1 to 635)
  AUTHORS   Schleyer,M. and Bakker,E.P.
  TITLE     Nucleotide sequence and 3'-end deletion studies indicate that the
            K(+)-uptake protein kup from Escherichia coli is composed of a
            hydrophobic core linked to a large and partially essential
            hydrophilic C terminus
  JOURNAL   J Bacteriol 175 (21), 6925-6931 (1993)
   PUBMED   8226635
REFERENCE   6  (residues 1 to 635)
  AUTHORS   Bossemeyer,D., Schlosser,A. and Bakker,E.P.
  TITLE     Specific cesium transport via the Escherichia coli Kup (TrkD) K+
            uptake system
  JOURNAL   J Bacteriol 171 (4), 2219-2221 (1989)
   PUBMED   2649491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..635
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..635
                     /product="potassium transporter Kup"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=68739
     Region          6..635
                     /region_name="Kup"
                     /note="K+ uptake protein Kup [Inorganic ion transport and
                     metabolism]; COG3158"
                     /db_xref="CDD:442392"
ORIGIN      
        1 mshtptpaag sghasansqt alvigaigvv fgdigtsply tlkeafsphy gltpdhdtvl
       61 gilslvfwal mlvvtlkyvt vimradndge ggimaltala qrtlpggsrs myvvgilgif
      121 gaslffgdgv itpaisvlsa veglqvaapk leafvvpitl vvlgmlflaq rfgtervgka
      181 fgpitlvwff algaigvynm arapevlhal npwwgvlffv ehnwhavfvl gavvlavtgg
      241 ealyadmghf gakairrswq fvvlpmltlt ylgqgalvlr dpsavsnpfy eavpewalyp
      301 mivlataatv iasqalitga ysvasqamql gyiprmhirh tshstigqiy vpavnwclll
      361 avavavvgfg dstslatayg vsvtgtmlit tvlmviyara nprvpapllw lfalvflavd
      421 caffyaniik fldgawfpll lglilftlmr twrrgrkllh deirkdgikl dtflpglmla
      481 ppvrvpgtav fltadpmvvp halmhnlkhn kvlhernvfl tvetlqgpya aagkrlkiea
      541 igdefyrvhv rfgfmetpdv plalmrscdq ggiyfdpmdt tyfasretiv asanrgmpiw
      601 rdklfalmhr naapatgffr ipgnrlvelg aqvei
//
LOCUS       WP_011259488             303 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Xanthomonas].
ACCESSION   WP_011259488
VERSION     WP_011259488.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..303
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33332
     Region          20..268
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mvstsehtav lavdsrcthg egvlwcarre alywvdisek rlwrhhpasa qsrhwtlpdr
       61 pgciglmddg rvlvalakai givdpdtiee dvlpfeklad veadnpltrs ndgradrngn
      121 fvfgtmdehd tkaargamyq fslthglral plpgvsipns icfspdgrtl yycdsarpqi
      181 lccdydaqta qtsntrvftt ldrddaepdg siidaeghlw naqwrawrvv ryrpdgsver
      241 ivqlpvkhpt csafggaald rlhvissrld hsaeelartp eagslywcdl pvaglpeslv
      301 asa
//
LOCUS       WP_011259697             358 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Xanthomonas].
ACCESSION   WP_011259697
VERSION     WP_011259697.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..358
                     /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=38716
     Region          22..301
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mtselspthg arvhssadar ptrdwqidaa kavaialvvl ghasgmppay klfaysfhvp
       61 lffvlsgwvg erfgqraltg atvaklgrtl lvpylaffmv ayalwllsaa mdghaghpqt
      121 rplwhpltgl lwangsrlyv lpalwflpal fvtmlayial rarlsaaava aisltlalaw
      181 agwfpslqlr lplaldvlpv alffiaiggw lsrfaealrs lgaqvwalal lplaavwwwl
      241 agwngqvdvn nlqcgqsaav fmlvsllgta mtfcvayfir gmrwvqwigt ntllilctht
      301 lvflvatsvv artgliarsa igtlawalgl safaitmsvp mravlvrgap wmlglkrk
//
LOCUS       WP_011262232             294 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Aliivibrio].
ACCESSION   WP_011262232
VERSION     WP_011262232.1
KEYWORDS    RefSeq.
SOURCE      Aliivibrio
  ORGANISM  Aliivibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 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   4  (residues 1 to 294)
  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 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 12071874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Aliivibrio"
                     /db_xref="taxon:511678"
     Protein         1..294
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32646
     Region          27..182
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          211..290
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkslgelmqs yadhcgfndl egiketaipg vwfyrsskgn qrqpfvyqsg iivlgkghkn
       61 iyignqpvhy gpddylvvgv pmpleceafp engepllgls idvdsallhr lvneleeakf
      121 qpciqtssdg fgltsvkman dmlesckrlm aalhtdldtk mlgealltei vyrvltgpeg
      181 hvlfnlahhd sqyarvakam nkmhqsyans ltvqnlaeea nmsvsafhsa frkitlespl
      241 qylkkvrlnk akeliqlegk rvndaahlvg ytstsqfsre fkrhfnvtpk gcla
//
LOCUS       WP_011262355             225 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Aliivibrio fischeri].
ACCESSION   WP_011262355
VERSION     WP_011262355.1
KEYWORDS    RefSeq.
SOURCE      Aliivibrio fischeri (Vibrio fischeri)
  ORGANISM  Aliivibrio fischeri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Aliivibrio.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 225)
  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   3  (residues 1 to 225)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Aliivibrio fischeri"
                     /db_xref="taxon:668"
     Protein         1..225
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24903
     Region          24..215
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mtsvslstdq nvlnkmdigs rviievtcpn gqsaqansql igfkkghyvf ieypsspple
       61 fnkiylegad vtfraitntt hcdviafktt ihsviyrpme miclhapssi tmkpirthrr
      121 ieskfscnls vneqnltgvm rdfsfggcai alpsklspds llnkkialti eieslepisv
      181 rgeiknidvk esqskigvmf dtdgisesel qtlhhqcvlk gwdkq
//
LOCUS       WP_011262865             298 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Aliivibrio fischeri].
ACCESSION   WP_011262865
VERSION     WP_011262865.1
KEYWORDS    RefSeq.
SOURCE      Aliivibrio fischeri (Vibrio fischeri)
  ORGANISM  Aliivibrio fischeri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Aliivibrio.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Aliivibrio fischeri"
                     /db_xref="taxon:668"
     Protein         1..298
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33281
     Region          83..151
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mtqlikitki slgvlssvlv mthayandas nddvvkkesa ltsicfskaa hsdaknvlld
       61 acpigdglwg nqqpklekgk sefwiqcgvf nqdltkekvn hiqkkvdasi nfklegeakr
      121 cligpyqdft taqkqlrslq sdrlfkhaal revnlallpq veepiesape avsepepdpi
      181 tirkqtkinn ihfvvpftdd ssegfymens lpwlratslh aqeicqqidm dlvtkeqwqi
      241 lldstimtkd kwpvllpywg adnlglfkdg aarklkntsm lnvmctkkve devvgnpi
//
LOCUS       WP_011263190             375 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Aliivibrio
            fischeri].
ACCESSION   WP_011263190
VERSION     WP_011263190.1
KEYWORDS    RefSeq.
SOURCE      Aliivibrio fischeri (Vibrio fischeri)
  ORGANISM  Aliivibrio fischeri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Aliivibrio.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 375)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 375)
  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 375)
  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 375)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Aliivibrio fischeri"
                     /db_xref="taxon:668"
     Protein         1..375
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43621
     Region          12..99
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(33,52..53,70,73,81..82,92,97)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mnkkeivktq nltidysslt vvinstkeei kislneanll fllyshpnri ytkdeiytqc
       61 wedgsvansv vtqtisllrk kflthnisii dtiknkgyks gdrllakpik kfyflffsvl
      121 ilvslflifp ifkqvapnsi tqnlnkvsdn iymlstskpi ditklniqpn ylyflhlged
      181 klslsqclfi ehkcndvtnk iifletnedn vetlinqnlt sdleqdnnpi iqkdsdqdgn
      241 fnlhtnvqft snddkdyiaf atynfyfnlq edksydldms inisetgyng kytyfsdfka
      301 qfdkdtlisn vinedeqssl iqhghiedqt klkmfpktfk ndnkynylhf yiidkgfslt
      361 yseqqdisfi vkefy
//
LOCUS       WP_011263693             257 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Aliivibrio fischeri].
ACCESSION   WP_011263693
VERSION     WP_011263693.1
KEYWORDS    RefSeq.
SOURCE      Aliivibrio fischeri (Vibrio fischeri)
  ORGANISM  Aliivibrio fischeri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Aliivibrio.
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
REFERENCE   2  (residues 1 to 257)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Aliivibrio fischeri"
                     /db_xref="taxon:668"
     Protein         1..257
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29692
     Region          177..256
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mvslinsfkl qftevshtie qpfvlyfsgf sgiikdeeik ksgrnclilv neieknsiyd
       61 vvmkktifin ntpliytagy dvkikpqsqv ilidlsffek lgvpsfksgl ithihsrlir
      121 lllesicssv kptyellalv nligvdhykt nlndnlnkik dkieecysce efnldmlckk
      181 thmsrrkiqy iladsntsfl eilnnlridk liyfmqkepk tsigvliyrv gfkhqstanr
      241 lfkkyknvsi refkksi
//
LOCUS       WP_011266092             170 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Mammaliicoccus sciuri].
ACCESSION   WP_011266092
VERSION     WP_011266092.1
KEYWORDS    RefSeq.
SOURCE      Mammaliicoccus sciuri
  ORGANISM  Mammaliicoccus sciuri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Mammaliicoccus.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Mammaliicoccus sciuri"
                     /db_xref="taxon:1296"
     Protein         1..170
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18663
     Region          51..170
                     /region_name="COG3942"
                     /note="Surface antigen [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443142"
ORIGIN      
        1 mgsniqgeni lnikkiatyt vlstlvltgf tnidtgvknf tqheakaaai dkyprpikta
       61 qpnyhwknnc twyvhnkrnq tkrylpssft haknwlseak kagfktgktp lagailqtsk
      121 gggglghvaf vekvnangsi kiseynynvs lgygtrtltk aqaatynyiy
//
LOCUS       WP_011266629             705 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Pseudomonas].
ACCESSION   WP_011266629
VERSION     WP_011266629.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 705)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 705)
  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   3  (residues 1 to 705)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..705
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..705
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76103
     Region          3..695
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msinldqaqq tfivearell qameesllql esepgdldai gavfraahti kgsaglfglt
       61 pivsfthive dvldrlregs vsvnaeliav llksgdhmle lidvvasrge qlqqpalere
      121 aalrqalqvf qapasasaad iasaqvvsdd eqsadvlwhi slrfgvdvfr ngmdplsflr
      181 ylntlgqmvq vttltdsipt veawdpesch lgfeidfrsa aghaainevf dfvredcave
      241 itpldetpdh veptgtelvs qpehspvvas gellgdqrav prtpatatat ataverpssg
      301 seqknkdgry vrvnadklde linlvgelvi asagasllak scdndplqea sstvsglveq
      361 ildgalhlrm ipigdtfnrf rrvvrdvsqe lgkdidliin gaeteldktv vekigdplmh
      421 llrnsmdhgi esaearraag kpakghlsln ayhdsgsivi eiaddgagln rerildkaqq
      481 rglvaagasl tdqeiynlif epgfstaeav tnlsgrgvgm dvvkrnitll rgtvdldsqp
      541 gqgtivrirl pltlaiingf lvgidqstyv ipldmvqeci eldehnrqlt rdsgyldlrg
      601 evlplvylrd hfnhegpaar rqnvvvvrya ehkaglvvdd llgefqtvik plgklfgalr
      661 gisgstilgs gavalildip allnqivhme arstqapqfl lptsr
//
LOCUS       WP_011267348             803 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pseudomonas syringae].
ACCESSION   WP_011267348
VERSION     WP_011267348.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 803)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 803)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 803)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..803
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87234
     Region          62..112
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          92..803
                     /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 mqssssrlrt grvktlglrl ggvglvlals vqgqalaeef efdipaqtls salkelgrqc
       61 dlqilynpdd lngklsspvh grltpeqvva dllkkanvah sledntltlg aaasahtmnl
      121 gpvaikgdsf gittegsgsy aatgvsinkt aqslretpqs vtvmtrqvmd dknltgldev
      181 maqtpgitfs qrnfgshvfs srgfaledes yiidgvagqg ysvtgwmtpd meiydrvevl
      241 rgaaglliga gnpggavnlv rkrptalpql sittragswd syrvdldgss klndsgsirg
      301 rfvtsyedrg yftdglqkta pllygiletd lsedttltlg vrhqnadtqg fsifglprys
      361 ngkaidlprs tslaqdwnrh qtrtdevfse letrfddnws gtlsathsdg afdqkvayaq
      421 gaidpatqsg srlvrtlfrs ddihsngida hldgrfdafg lshqltvggn gseqkresry
      481 atvnanqpla ifspdhdaia epprpawsst dysdkrygvy snlrlsltes lslvmggrvs
      541 sydyqttsag vtrraqednq vtpfagviyd lnrdwswyas ytdiflpqsa yrtasgtlld
      601 paigashetg ikgelfdkrl nvslalfyvk qkdvavedda nagqcvsnda ygtcylngdi
      661 rrskgidmei sgeplpglqt lagytfnitr gsdgqsisae tprhmlrlts sytlpgawrr
      721 ltigggvsaq sgysehestq pidnagraiw darvawkide hwtvalngnn lldrkyykat
      781 gdidrgnyyg dprnyvltlr gdf
//
LOCUS       WP_011267438             403 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Pseudomonas syringae].
ACCESSION   WP_011267438
VERSION     WP_011267438.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 403)
  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 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   3  (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   4  (residues 1 to 403)
  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 403)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..403
                     /product="CmpA/NrtA family 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=43940
     Region          16..267
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mnertgnald wvagsdapem nsldvgfmal tdcaplvvaa tqgfaqpygl slnlerqtsw
       61 aglrdrlvsg rlqaahslyg liyavelgis ggpatdmail mglnqngqci nlsrelqqag
      121 vitpealdkh ahqsgskltf aqtfptgnha mwlyywlasq gihplddvts vvvpptqmaq
      181 hlqagridgf cvgepwgasa vqqqlgftma tsqsiwpdhp gkvlgctref veqnpntara
      241 limavleasr fieendhnrr staqllsgad yldtsvdcie prllgqysdg lgnhwqdpha
      301 vsfhtqgqvn ypwlsdgmwf mtqfrrwgll redpdylava srvqqldlyr qaasalgidv
      361 paatlrssql idgrvwdgsd pagyarsfkl hsladdvpam asr
//
LOCUS       WP_011268433             758 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Pseudomonas syringae].
ACCESSION   WP_011268433
VERSION     WP_011268433.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 758)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 758)
  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   3  (residues 1 to 758)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..758
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..758
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=80116
     Region          6..757
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msfgadeeil qdflveagei leqlseqlve lesrpddadl lnaifrgfht vkggagflql
       61 helvecchia envfdilrkg errvdselmd vvlealdtvn smfgqvrert dvtpatpell
      121 aalarlaepq sadeavapep epvvevqaaa pvaepaagde itddefeqll dslhgsspvs
      181 aapaqtpaaa aaapagdeit dqefeslldq lhgkgkfaad aatapapapv aqgsaapasd
      241 eitddefeal ldqlhgkgsf dgavaapvaa apvavaakap aaaaasdeit dhefesllde
      301 lhgkgkfepe aivakapapa aaaaappppp pvakpapapa akaepakpaa apaaarapap
      361 sgekpvatea ettvrvdtar ldeimnmvge lvlvrnrlvr lglnsgdeam skavsnldvv
      421 tadlqtavmk trmqpikkvf grfprlvrdl arqlkkeinl elvgeetdld knlvealadp
      481 lvhlvrnavd hgietpeere atgksrggrv ilsaeqegdh illsisddgk gmdpnvlrsi
      541 avkrgvmdkd aadrlsdtdc ynlifapgfs tkteisdvsg rgvgmdvvkt kisqlngsin
      601 iystkgqgsk ivikvpltla imptlmvmlg nqafafplvn vneifhlnls ttnvvdgqev
      661 vivrdkalpl fylkrwlvss aaheeqregh vviltvgtqr igfvvdqlvg qeevvikplg
      721 kmlqgtpgms gatitgdgri alildvpsml kryaarri
//
LOCUS       WP_011268830             118 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MGMT family protein [Pseudomonas].
ACCESSION   WP_011268830
VERSION     WP_011268830.1
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 10790320
            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="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=12649
     Region          15..117
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(21,39..40,48,51,53..54,56,59..60,62,70,75,82)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(39,70..71,73,99)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mtdpdltlpy pagqspnear rtalyltmaq ipegkvvayg qlaelaglgr aarwvgrtls
       61 qlpdgsslpw hrvlgaggrl slppgsvsgd eqrarlraeg vtivnnrvdm qrhgwrpl
//
LOCUS       WP_011270159            3064 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Pseudomonas aeruginosa].
ACCESSION   WP_011270159
VERSION     WP_011270159.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 3064)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 3064)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 3064)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..3064
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..3064
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=318192
     Region          301..499
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          1012..1227
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          1182..1445
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          <1519..1676
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          1549..3062
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 mdnvlgekvm smptieqivs rylfnqdtpp anlkdeslir aegaigdpvf vdmnefmtvg
       61 ggrfagverf nfvrnflgah ddvyapmgga klppgvytle difeaygiap enrklavsqy
      121 ysgvfdsdfa erayvfgsge yqinsdalfy vnedgsreiv dicvepvsdn fdydgegvla
      181 qitnsltegh idpsgigrqv piiftgsvtd kqsftsedwy aldiknravg laettnkaai
      241 atsapyftal faavlgrlai ndiitfedae grfvvydgrd vnhsgvvdpy klknftelvm
      301 ssgsaviagn gndtlygtny sndelyggkg ndyldgrega drmlggagdd iyvvddegdv
      361 vieqagegvd lvrssvthtl genvenlrlt gegnidgsgn sldneitgns gnnfirgggg
      421 edtiyggggd dtilggvekv nlygesgndd lyggdgddyl sggigndyis ggdghdimdg
      481 gegrdtllgg agydtyfadm hdvieddpeg rgqvflgkqr ltggtrkesd pentyrdnrg
      541 nvyvlsgstl tvnggltiln ydkdkstlri vlsdeeeede tpdtgpaenr tspividldg
      601 dgietldiga syfdldgdgl semtgwvspd dgllvhdrng dgrisngtel fgnhsilsng
      661 qtaengfqal aeydnngdgv idaqdasysv lqvwrdlngn gisdigelqs ladagvlsis
      721 tgytnsahtd shghqhrqig tvmlangtas taadvwfkvd sarrvnsgdi eltpdiyfla
      781 nakgfgkvhd lhqamaldpe lktlltqyvs atnaasrdal ldnliyrwag aegvdpysrd
      841 pkkvyghvmd arqlvtlenl vgrpymgvwc wgeydpnphg qaapilvaey lefkrftaaq
      901 ilaqtdyaee lgiiksafgs dangitvdws slqgtletly angqldriag vigiltdlgt
      961 yspnyrtkrd aafqavaaan ldlapffdfs tkigttvgdt lsgintgsvf yglggddrly
     1021 gqagndsyhf arghgndtil drggldqvvf gegigqgdlt fsrnattvwi hvknadgsds
     1081 gslridnffd fdgtvdfgav ellvfadgss lnlaqildil tassitegnd lvfgtiagdt
     1141 idalagndsi hglagddqls ggagddvlmg ddgndtligg igndsliggr gsdtylfeig
     1201 hgndvidnaa qsagtkldrv vfgqgidpat vsversgshl vihtsasdsi rltnyfsgea
     1261 vngtavdeiv fhdgtvwaia dikgmvlqag egndviqgya sddllsgleg ndqlygnagn
     1321 dtllggdghd tldggtgndv llgdtgndvl rggegddyld ggdgndtldg gsgddtligg
     1381 agndylsgga grdtlqggdg ndtllggagd dflaggkgnd rldggtgtns ylfargdgqd
     1441 vivdayegvv tiylsdlpld tlvfrrngts levafpdspd dklslsaffr deiplsgirl
     1501 rygegletli epaqlrlltl egteaadlih ayssddliea lggddvvhag agndsiyggd
     1561 gsdrlyagsg ndlidggtgd dlidagegdd vlhggsgndt llggagadvl dggtgddrle
     1621 ggsgddlyrf avgwgndfii dstgsdsvqf tgvaptdlll rrdgvdlvvl nqttgdqlri
     1681 qgqfsylagv agataieqfv fdggttwdye aiklkalegt tqhdtiygha dddtvnagag
     1741 ndlvygqdgn deihggegad tlyggngndl lvggteddll dgglgddslh ggagndtlqa
     1801 gggddvldgg tgndrlegga gndqyhftag wgsdliidsa gsdsvqftgv apadlllrrd
     1861 gvdlvvlnqt tgdqlriqgq fsslagvaga kaieqfvfdg gttwdyeaik lkalegtgqd
     1921 diiyghaddd lvtaqagndl vygqdgndei hggdgadtly ggdgddlldg gtgddqldgg
     1981 wgndtlqgge ghdlligggg fdelyggagn dtlqghglld ggdgddlleg sgellggvgn
     2041 dtllgqgfdt lrggagddvl etysnawdqg snileggtgn dtlygsfgdd tyifnlgdgh
     2101 dllierrpge aysniepstd tlsfgagiaa gdlgfvrrgn dliiehangs dsitvqnwfq
     2161 eptdhfkleh flfadgsels qadvenrviw qgtsgvdsfi gyrdlgdhir lgdgddkawg
     2221 ragndlihge ggndylegea gndtlfggsg ndqldggagd dllvggtgdd kyiyapggga
     2281 dvidnsgggy dgvfftngig qdrltfgrdg ddllilvdgd taqsvrvldh flggdkaisf
     2341 vqpsggyllt aerighivaa qgvagdfeal iegtaageql agydgrdllr glagndtlfg
     2401 mggddriegg dgndylsggn gqhngsgndl liggagndil agedgddtli ggagddayyy
     2461 ranggvdivd nsgggfdgvf fldvprsrls fhrdgddlvi lvdsdlgqqv rvtnhflgsd
     2521 yaidyvqpdg gnylttaqia aqltalpdgs ggeepgepge pgeptdpdnp ggpgeppvag
     2581 vggddllvgt agndillgga gndtlngaag ndtliggsgd dtyvytagqd vieeiggadt
     2641 lvfaggitfn qvasglmksg ndlilrvngs tanqvtlkdf flggdnlvet iafetggqlt
     2701 aeqifgafgl avptpaaafd dtiqgstgdd aaldgtagnd llqggnggdv lfgdagndrl
     2761 eggngddtld ggtgndtlvg grgddtyifa agggqdvidn sgggadtlhf egisfnqvas
     2821 glmksgndlv lnvsggsdkv tirnwflggd yvvdtitfas ggqitaaqlf gafglsnpdp
     2881 vgspvyqnlp derafgtvlt gragdqiilg ssdddlidgg agndtlrgna gndyliggag
     2941 sdtyvfavgd gqdvinnlsn tpdtdtdvls iegivredlw lsrngddlvi dvtgsedsit
     3001 vqdwyansaq qldviqaggs slyanqvdsl vnamaafgap aggelnltqt qrdqlnvvia
     3061 anwq
//
LOCUS       WP_011272084             157 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YqaA family protein [Haemophilus].
ACCESSION   WP_011272084
VERSION     WP_011272084.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus
  ORGANISM  Haemophilus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Haemophilus"
                     /db_xref="taxon:724"
     Protein         1..157
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17361
     Region          16..151
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mdifsffsad fwqanslcfm fisaflsatv lpgnsevifv alavpklmlg slfnadilal
       61 iliatagnsl gslttygigr wmpkfdpkny rtlwainqlr rygaivllls wlpvvgdlfc
      121 aiagwlrlnf vtsslfiflg kmvryvallf lstpfll
//
LOCUS       WP_011272155             581 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein/permease [Haemophilus
            influenzae].
ACCESSION   WP_011272155
VERSION     WP_011272155.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus influenzae
  ORGANISM  Haemophilus influenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Robinson,H.C. and Poole,R.K.
  TITLE     A bacterial glutathione transporter (Escherichia coli CydDC)
            exports reductant to the periplasm
  JOURNAL   J Biol Chem 280 (37), 32254-32261 (2005)
   PUBMED   16040611
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Cruz-Ramos,H., Cook,G.M., Wu,G., Cleeter,M.W. and Poole,R.K.
  TITLE     Membrane topology and mutational analysis of Escherichia coli
            CydDC, an ABC-type cysteine exporter required for cytochrome
            assembly
  JOURNAL   Microbiology (Reading) 150 (Pt 10), 3415-3427 (2004)
   PUBMED   15470119
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Pittman,M.S., Corker,H., Wu,G., Binet,M.B., Moir,A.J. and
            Poole,R.K.
  TITLE     Cysteine is exported from the Escherichia coli cytoplasm by CydDC,
            an ATP-binding cassette-type transporter required for cytochrome
            assembly
  JOURNAL   J Biol Chem 277 (51), 49841-49849 (2002)
   PUBMED   12393891
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471988
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Haemophilus influenzae"
                     /db_xref="taxon:727"
     Protein         1..581
                     /product="ABC transporter ATP-binding protein/permease"
                     /EC_number="7.4.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042883 - cysteine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=64340
     Region          3..560
                     /region_name="CydD"
                     /note="ABC-type transport system involved in cytochrome bd
                     biosynthesis, ATPase and permease components [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG4988"
                     /db_xref="CDD:444012"
ORIGIN      
        1 mmidkrlint vadskkwigv tvlwnwvalv ggiisavvfs yilqaayfhk lsllsavilg
       61 ivliaalalr afagkksvqa syfastkvkh elrsliyrkl asmplnqvnq qstssiiqva
      121 segveqleiy fgrylpqlfy sllapltlfv fliffsfkta villicvpli pmsiiavnki
      181 akkllakyws iyvglgssfl dnlqglitlk iyqddgykak amdkeaehfr kitmkvltmq
      241 lnsvslmdll ayggaaigil tallqfqnaq lsvlgvilfi llsseffipl rllgsffhva
      301 mngkaasdki ftlldtpvet qqsavdfeak nnvqveikdl hfsyseeksa itgldlsilp
      361 nqltvfvgks gcgkstlvsl lmgfnqaqqg eilfngqnal nidrtsfyqk vslvshssyv
      421 fkgslrenmt makidatdeq iyacleqvnl aqfvrenggl dmqllsrgan lsggqiqrla
      481 larallhnae lyifdeatsn idveseeiil qfiqqfkqqk tivmishrla navnadcinv
      541 ldqgklieqg theslmakqg ayaemfqqqk dleqirevan a
//
LOCUS       WP_011272607             252 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Haemophilus
            influenzae].
ACCESSION   WP_011272607
VERSION     WP_011272607.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus influenzae
  ORGANISM  Haemophilus influenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
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
REFERENCE   2  (residues 1 to 252)
  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 252)
  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 10617438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Haemophilus influenzae"
                     /db_xref="taxon:727"
     Protein         1..252
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28269
     Region          16..67
                     /region_name="HTH_36"
                     /note="Helix-turn-helix domain; pfam13730"
                     /db_xref="CDD:463970"
ORIGIN      
        1 msmrlmvqam nckvgnpark lvllkladna nddgicfpsy qyiadkcemt rrsainhiey
       61 likmglvskk erknkdgsis nlyflhleqg senfalgsen islgsenfal ggsenisprt
      121 shslepvnep kkttqkseae mlleqfgitg qlakdfiahr kakkgvinqt qlnrlqkqad
      181 kagisiceav eiciernwqg fnaswdwrde klrpnsphlg qshrnkpkfd dtqtgwsagm
      241 nfivdgtqwq ip
//
LOCUS       WP_011272980             231 aa            linear   BCT 20-JAN-2025
DEFINITION  LytR C-terminal domain-containing protein [Corynebacterium
            jeikeium].
ACCESSION   WP_011272980
VERSION     WP_011272980.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium jeikeium
  ORGANISM  Corynebacterium jeikeium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 231)
  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 10598501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Corynebacterium jeikeium"
                     /db_xref="taxon:38289"
     Protein         1..231
                     /product="LytR C-terminal domain-containing protein"
                     /calculated_mol_wt=24524
     Region          128..210
                     /region_name="LytR_C"
                     /note="LytR cell envelope-related transcriptional
                     attenuator; pfam13399"
                     /db_xref="CDD:463868"
ORIGIN      
        1 mtepnrprha ldddtdnenl glplrglami liavavllig wgvfslsgnd sdeseqasqt
       61 qqaqqsqgqq gqqpsasneq dkgtatddae qpkpedgrdt pegdrtdagr egdtaaaegg
      121 vkkedtyvav lnnspiagla gdvankmrdq qwnktgvgnl pdesgvfpts vvlyskgnda
      181 erqlaeqlak dlgiqarerd eatdraiegv emlegerpag vvvvttndmp r
//
LOCUS       WP_011273989             357 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sulfate/molybdate ABC transporter ATP-binding protein
            [Corynebacterium].
ACCESSION   WP_011273989
VERSION     WP_011273989.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..357
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /function="ABC-type sulfate/molybdate transport systems
                     ATPase component"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38221
     Region          20..351
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mteatellef dvsipsrkfd iafelpmgrv lgiigpngag kstiagalag tvvptsgris
       61 vrdrvltdta tgtyvpihqr kvgllaqdpl lfphlsvidn ltfapksqgs pdaqkvaehw
      121 lrklelepls hrkphelsgg qaqrvalgra fagspdilcl depfraldit vaadmrally
      181 pllhkmtvll ithdvldimy laddvavieh grlvrlgttd dviekpldkf tarfsgtnii
      241 kgrsignetl rsgsgeilvt gkpghkipag qraiasfrpt avsiltdhtd enmrnqwpat
      301 ikgleqgagt itvicdvkgd siraeispas aaqlslvtgn aiivavkaqe ielypah
//
LOCUS       WP_011274749             263 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CHAP domain-containing protein [Staphylococcus].
ACCESSION   WP_011274749
VERSION     WP_011274749.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus
  ORGANISM  Staphylococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Staphylococcus"
                     /db_xref="taxon:1279"
     Protein         1..263
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27424
     Region          160..262
                     /region_name="COG3942"
                     /note="Surface antigen [Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443142"
ORIGIN      
        1 mkkiatatia tagiatfgla hqdadaaenn ngynpndpys ysytytidqq gnyhyewqgn
       61 wspsqaqqgg qqntgnqavn ntqsnnnyny nynnnqsnqn tqsytannna ggglgasyst
      121 sdrnvkvttq napttqstss nassssssea lagkssggsn lytagqctyy vydkvggkig
      181 stwgnannwa taaaadgytv nntpkagavm qtsqgayghv ayvesvnddg svkvsemnyn
      241 ggpgvvssrt isagqagsyn yis
//
LOCUS       WP_011274345             193 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Corynebacterium jeikeium].
ACCESSION   WP_011274345
VERSION     WP_011274345.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium jeikeium
  ORGANISM  Corynebacterium jeikeium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Corynebacterium jeikeium"
                     /db_xref="taxon:38289"
     Protein         1..193
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /function="Nitroreductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20695
     Region          5..183
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mtltvteais nrratrkykn qaipvevlnr vvdnaleaps afnaqmrdlv viqdeavkqa
       61 ifdasgqqqf ldapvvfvvv grsevvpeda eevlgaelte kvrgfngsas aaklreigir
      121 damlvagfll laaqeqglat spttgwneeg vkkaiglegr gdrsialvva agyadeepvh
      181 pgraenrrvd nhy
//
LOCUS       WP_011279548             145 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Psychrobacter arcticus].
ACCESSION   WP_011279548
VERSION     WP_011279548.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter arcticus
  ORGANISM  Psychrobacter arcticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Psychrobacter arcticus"
                     /db_xref="taxon:334543"
     Protein         1..145
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15661
     Region          1..127
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mintinqkpn gftlielmiv vaiigilaai aypsyqryii ktkrtdmmse mhniaaeiqs
       61 rklaqgsfan vvttdltgny prqgtalytv aaapspltnt wtitaepkss tqmngdgnlt
      121 lnyqgvkcri vnsvstcgtg ddwnn
//
LOCUS       WP_011280029             694 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Psychrobacter arcticus].
ACCESSION   WP_011280029
VERSION     WP_011280029.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter arcticus
  ORGANISM  Psychrobacter arcticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 694)
  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 694)
  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 694)
  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 694)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Psychrobacter arcticus"
                     /db_xref="taxon:334543"
     Protein         1..694
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=73840
     Region          52..687
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 mnsqvtdhns astmssedan lskhpdlhvd tdvdddddvd psvtqailek ydresitrhi
       61 tqgpvkyiia aicifysifh lyitfnpmps llqrsvhvgv gfaliflifp askkssrkkv
      121 awydwiwfll sfsgmayliy eyqeivtsrg gmansvdvif siitvicvle gsrritgwil
      181 pilasiflly pfishldfmp nrlltrpydf gdifgqlflk teglysvaig asvtfiflfi
      241 lfgaflarsg mgqlfndlal alagdkkggp akvavissgf mgsingsals nvvstgafti
      301 plmkkvgyhk dfagaveasa svggqilppi mgasafimae ttglpystia laallpaily
      361 ylgviaqvhf ragrrdlkgm akeslpqvke vlkarghmll pivfliylli qnvpvgyaaa
      421 ytigftvvis mlrketrmgf kdilgaledg arqslavmaa cavvgiiigv vsltsfgtvm
      481 tssivtlgag sllltliltm lasmvlgmgl psipayiita tmaapalagf dipilsahmf
      541 vfyfgvfani tppvclaafa gagisggdpm ttgylslkla lagfivpfmf iynpamlmid
      601 ptdlavtaka fplppvidiv iavvtsvigv iglsaalegy fksdmnvvtr lilalgalll
      661 iypglitgvi ggvivlgiaa fnikgskapt alsv
//
LOCUS       WP_011280584             115 aa            linear   BCT 20-JAN-2025
DEFINITION  PilZ domain-containing protein [Psychrobacter arcticus].
ACCESSION   WP_011280584
VERSION     WP_011280584.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter arcticus
  ORGANISM  Psychrobacter arcticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 115)
  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   3  (residues 1 to 115)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Psychrobacter arcticus"
                     /db_xref="taxon:334543"
     Protein         1..115
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12465
     Region          2..115
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 mampgrggil tchienidml yasylsfvts galfvpsdrv qklgdevfia vtlpnsserl
       61 pmngkviwvn sktqssrpvg favqmgtdit glriknever lltgkidslq atytm
//
LOCUS       WP_011280723             473 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Psychrobacter arcticus].
ACCESSION   WP_011280723
VERSION     WP_011280723.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter arcticus
  ORGANISM  Psychrobacter arcticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 473)
  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 11465564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Psychrobacter arcticus"
                     /db_xref="taxon:334543"
     Protein         1..473
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=51372
     Region          <206..257
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          347..471
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 myqkfakhpn yahnslissh hkyanmmkik plitaisiav vsisaiaapa dstrtlpvrs
       61 adslpsiakk vslnvqenrs ssvnssatvk lnankakpad rmtqlidakq daevkasvtv
      121 sadnmtveel trkdeqsdsd disegqavsa pssatadsaa dtsiksitnv dgkkhttlnl
      181 snyakqvnga twtpnmkvns amtikmqall dwnhaspgai dggwgmnskk alinfqtmqg
      241 lpangkmdqk twnalnknit ankpvlvtyt iteddvntnf atmptgseak skmkglyyqd
      301 ikemfgerfh mdvryldkln knkqykvget itvlntrapl kqrinrvvan kadktlyayn
      361 ddklvatypt tvgsdstpsp qgtfkivnkv kmpwykatvg egtdkkvhml ppgpnspvgv
      421 vwmglskpsy glhgspkpeg isrqasagcv rltnwdvlev yaniengatv elk
//
LOCUS       WP_011280893             173 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Psychrobacter arcticus].
ACCESSION   WP_011280893
VERSION     WP_011280893.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter arcticus
  ORGANISM  Psychrobacter arcticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 173)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Psychrobacter arcticus"
                     /db_xref="taxon:334543"
     Protein         1..173
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=18854
     Region          11..163
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cl49639"
                     /db_xref="CDD:483979"
     Site            order(108,126,129,142..145,147)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mtynenlmtq ivisiaqqtl tvykrqkvia qypvstakng mgsqqdsgct plgkhviaek
       61 igagmlsnav figrvptget ynselgashp erdwilsril wlsgleegvn kgsnsqggcd
      121 tyqryiyihg tpdsepmgip lshgcvrmrn qdiielfeqv dvdkgtpvni iaq
//
LOCUS       WP_011280942             697 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Psychrobacter arcticus].
ACCESSION   WP_011280942
VERSION     WP_011280942.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter arcticus
  ORGANISM  Psychrobacter arcticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 697)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 697)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 697)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Psychrobacter arcticus"
                     /db_xref="taxon:334543"
     Protein         1..697
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /function="dual function sensor, contains a PAS-like
                     sensory box to regulate the diguanylate cyclase and
                     phosphodiesterase A domains"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=77423
     Region          123..687
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mrtqsllkll vidadqlyae rlvhllgsyy dsvnlgfldd kdellkslrq swdvlvfgqa
       61 ydmkftdvva iiqeqnidlp lvclinkdta gnahneeglp sivngtmvka lyaeqemavi
      121 maicllqenl hsrqqlktlq svlseaeqra nvliknsksa vayidqgihi fandpylqlf
      181 gfeamndiig ipvidliagg dnvkavkqfl rqfdkgnrkd vefnfesrrt dgstfeaklq
      241 lavatlegep vtqiiiqqnn snsmevakrl aeaerkdslt gidnrhsfee qltalyeqar
      301 kgaltaally vqldnigkir sslglqgids tvkqvantld elvvdghvsr fsdtaftilv
      361 enqttatlek laeqigmsis nmlievdkrt tsttasiaiv kiekntpepr vlleramdai
      421 nqimietsnh ggryhlydas ehansddhal aeslvdaitn nrfellfqpi ydinndrsdf
      481 fevflqlpla danntiltpd qfmavakshq llekidrwvl inackrinev rkthpearll
      541 vqmtnaslvd kklpsvasql inaiggkaga ltlqfnekdi sdyltvakfq ftalsqincq
      601 lginnfgssi ksvelanfvh pdvvrlahny vegidaaenl etvksiivrt nesnvdvlmp
      661 yiedaatmsv awsvgvrylq gnylevpsnt ikvsnes
//
LOCUS       WP_011281003             242 aa            linear   BCT 20-JAN-2025
DEFINITION  CHAP domain-containing protein [Psychrobacter arcticus].
ACCESSION   WP_011281003
VERSION     WP_011281003.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter arcticus
  ORGANISM  Psychrobacter arcticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Bateman,A. and Rawlings,N.D.
  TITLE     The CHAP domain: a large family of amidases including GSP amidase
            and peptidoglycan hydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 234-237 (2003)
   PUBMED   12765834
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Rigden,D.J., Jedrzejas,M.J. and Galperin,M.Y.
  TITLE     Amidase domains from bacterial and phage autolysins define a family
            of gamma-D,L-glutamate-specific amidohydrolases
  JOURNAL   Trends Biochem Sci 28 (5), 230-234 (2003)
   PUBMED   12765833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Psychrobacter arcticus"
                     /db_xref="taxon:334543"
     Protein         1..242
                     /product="CHAP domain-containing protein"
                     /GO_function="GO:0004040 - amidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26313
     Region          127..207
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
ORIGIN      
        1 mkqallilsv lgmgvaqtsg aaettfqsnn tlshtitnit tsanygssrn iystnsgayv
       61 ssndeisqai dnlsahakqk eyqlasltnr lsyeqrqqkv ssvpdrysap aiaaanasrv
      121 alssstgyca ryvrkalqsa gyeftpnpsa yqyasrgtls qagftkisnn mqpqvgdviv
      181 ydrssnrphg hiqifdgndw vsdfrqnsis pysgvyaytt wrdskyvdda sdrgiylama
      241 dk
//
LOCUS       WP_011281934             293 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Candidatus Pelagibacter
            communis].
ACCESSION   WP_011281934
VERSION     WP_011281934.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Pelagibacter communis
  ORGANISM  Candidatus Pelagibacter communis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Candidatus Pelagibacterales; Candidatus Pelagibacteraceae;
            Candidatus Pelagibacter.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Candidatus Pelagibacter communis"
                     /db_xref="taxon:198252"
     Protein         1..293
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33552
     Region          18..258
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mniitskpkv iwnsktilge gtlwvpshns iyfvdikkkk iftlnvktnk rriikinkei
       61 gflahikkdi filglqselr ivnlknketi rsipieedkp lnrindgkid pegrlwfgtm
      121 dnlernikng slycldkkln ihkvdtkyyi tngpafinse nflhtdsrsk tiykirinkk
      181 hkiikktkfl kfskidgspd gmtidskknv wichyggaci svynsrgkki hkielpakni
      241 tnctfgglsn neiyistalk gmtkneikky klsgsffkik tnvkgiksks fki
//
LOCUS       WP_011282286             169 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Candidatus Pelagibacter
            communis].
ACCESSION   WP_011282286
VERSION     WP_011282286.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Pelagibacter communis
  ORGANISM  Candidatus Pelagibacter communis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Candidatus Pelagibacterales; Candidatus Pelagibacteraceae;
            Candidatus Pelagibacter.
REFERENCE   1  (residues 1 to 169)
  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 169)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 169)
  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   4  (residues 1 to 169)
  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   5  (residues 1 to 169)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Candidatus Pelagibacter communis"
                     /db_xref="taxon:198252"
     Protein         1..169
                     /product="TRAP transporter small permease subunit"
                     /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=19471
     Region          8..166
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mpkifsiyvn iidnicvkvg rfvmygvffm mfllilsfvt rniinyplmw iiemaqftlt
       61 ayyllgggys mitddhvrmd lfygklsakg kakmdvftsi flifflvvll ygsisslqyt
      121 leykqklfta wapylwpiks lmllgillml lqafsmlikd iakikgiki
//
LOCUS       WP_011284151             575 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Mesomycoplasma hyopneumoniae].
ACCESSION   WP_011284151
VERSION     WP_011284151.1
KEYWORDS    RefSeq.
SOURCE      Mesomycoplasma hyopneumoniae (Mycoplasma hyopneumoniae)
  ORGANISM  Mesomycoplasma hyopneumoniae
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Mesomycoplasma.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Mesomycoplasma hyopneumoniae"
                     /db_xref="taxon:2099"
     Protein         1..575
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=67162
     Region          95..566
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mnkkkellkd hlkeleqisk sslnenqkel iklnleilkn ndkisiddfe qiwrflkqrv
       61 atgfvfdeap einnqsiail ekdeklsfss skmkdnlqns liigenydvl knligverer
      121 eredsnfdli yidppyntqk tsddgnnltd dqitadkfiy rdkfsrtgwl nllnerlkla
      181 rqllkedgvi fvsiddneqa ylkvlmdeif geenfvanmv wrksaqgthk dvevdnlntv
      241 neyivtyakd kskfkfdyvk hsqekldeiy kfrdknfeky gayklqplvn swngawyrsg
      301 qdyeleapdg tnfkiwqnid kpqsasysws kptfdkaknl gliefkknkq dywvvhkkey
      361 qyakfdtkeg vlktvargvp ftnmivanqn nlesdiytse garelnsifn skefdypkpv
      421 rlikylikml sskknirvld ffagsgttgq avlelnkedn gtrtftlvtn nennigqnvt
      481 yerlyrinkg qgtkgqkdfe wikkneafdt slnvfwskty ntsllnndit nqelkdkfkk
      541 llkefgiykn kskvndsvlk tlsslrsyke eneek
//
LOCUS       WP_011291241             246 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Thermobifida].
ACCESSION   WP_011291241
VERSION     WP_011291241.1
KEYWORDS    RefSeq.
SOURCE      Thermobifida
  ORGANISM  Thermobifida
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 246)
  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 246)
  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 246)
  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 11444466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Thermobifida"
                     /db_xref="taxon:83677"
     Protein         1..246
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=25793
     Region          <29..81
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          168..228
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 mrqecsneeq dqsaapvgre laaararrgy tlrqlseltr ipesvlhawe hgdtacgpae
       61 ryraqvrtlc avldldpaal lcrgdpgqap vrrrtapsrg gqwgwaavvi aaaltlavla
      121 wpgrpftpdh peafpaagqs pagspsapdp assaapavpp tagqvtlrvt ahrptwvsvt
      181 dgtdmlftgv laagqtrdwt adevihlrla daggvhlwvn ghaygvpgad gevthltyta
      241 qsgspr
//
LOCUS       WP_011293159             102 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: MoaD/ThiS family protein [Thermobifida].
ACCESSION   WP_011293159
VERSION     WP_011293159.1
KEYWORDS    RefSeq.
SOURCE      Thermobifida
  ORGANISM  Thermobifida
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 102)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 102)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Thermobifida"
                     /db_xref="taxon:83677"
     Protein         1..102
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=10894
     Region          21..102
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mrsgkiasee ykdnpltscg tvrywaaaka aagrheetft astlsdlleq vrqkyegnaa
       61 mlavlarssf lvnatpvgvr phhevvlepg wivevlppfa gg
//
LOCUS       WP_011292347             389 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ROK family transcriptional regulator [Thermobifida].
ACCESSION   WP_011292347
VERSION     WP_011292347.1
KEYWORDS    RefSeq.
SOURCE      Thermobifida
  ORGANISM  Thermobifida
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae.
REFERENCE   1  (residues 1 to 389)
  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 389)
  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
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 389)
  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   5  (residues 1 to 389)
  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   6  (residues 1 to 389)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 389)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 389)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Thermobifida"
                     /db_xref="taxon:83677"
     Protein         1..389
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40532
     Region          19..73
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          84..386
                     /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 mttdaqvtpg sqaalrqanr erviaalrrg gtltqaeiar atglsaasvs nivrdlramg
       61 vvsvretssn grraravtlq rppgvlvaid fthsrltval gntdgrvlqe esiaydvsed
      121 pvrgvrravw ltetlltqar vdrsmvlgva aaipgpvdpa tgligditsm phwagfnpga
      181 elqerlglpv svdndanlca laeltegaar glehvvyvkv ahgvgagvil ggrlfrgmng
      241 nageighigl dergqvcrcg nrgcletlvg tpylldmlpq qgrvkhgasl vdlleaaqeg
      301 dpgcrriiae agaalgrgva vvvnmvnpqm vivggeiaea gellldpmrr amelgalgna
      361 ltglrlvtge lgeraalrga lqvvldstf
//
LOCUS       WP_011296466             659 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: sensor histidine kinase [Cupriavidus].
ACCESSION   WP_011296466
VERSION     WP_011296466.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20493667
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     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=70722
     Region          56..245
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          350..644
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mphsddflav hdpaaaqaah epgsenrrww gfavalaagl vllcaltwlv svqrglatlq
       61 estatradry aatlestldr yeflpalvsl hpfvrgllqa pddparvaaa nhylaevnrr
      121 shasatyvia tngialaasn agepgsfvgt dyrfrpyfqi asrgemgrfy aigitsdepg
      181 yyiaqpvesg gkvigvtvvk lnlewfqrag ggsaeplmvs ddhgviflss vpawqyrtlg
      241 plpaelhdel gktrqyhdrd vtplpleplt spvtewlasr aldpgarlvr vradgpnpdg
      301 seradrylel grkvgpaewt mqvmapldpv lanarnatva aalayacicl llvnwrqrrq
      361 rardmlysrr lleaaydele rrveartadl mainekleee vaertraese lraaqdelvq
      421 asklaalgqm aagithelnq plaalrtfsd ntrvllergq laaaegnlsa iadltermgk
      481 itgqlklfag karpprrsvl vsaaiehvla llaprltgvt lhvdglhalp niavradelk
      541 leqvllnlig naldaiasaa paqgridvsv sadasavtiq vrdngtgisp edlprlfepf
      601 fttketgqgl glglaisssi vrefggqlsa anadgggavf tivltrapvd agagvtqth
//
LOCUS       WP_011296294             258 aa            linear   BCT 20-JAN-2025
DEFINITION  SPOR domain-containing protein [Cupriavidus necator].
ACCESSION   WP_011296294
VERSION     WP_011296294.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus necator (Ralstonia eutropha)
  ORGANISM  Cupriavidus necator
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Cupriavidus necator"
                     /db_xref="taxon:106590"
     Protein         1..258
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28374
     Region          45..>122
                     /region_name="PRK09169"
                     /note="hypothetical protein; Validated"
                     /db_xref="CDD:236394"
     Region          143..209
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 mfrldppdqp rwlsislpll llanvvllaa vlgvfgpdpl sgwsgtprep arlrqqvrte
       61 rmelqpaqpn rpasgavpep qargagpagk vlaaatkrva vaasedqcve iggfsaqavr
      121 raaedlsggs wqveqferre qvrwwihlpa qptrenlerk laelrrrnvt dysvvtsgsa
      181 eaesftvslg lfrereraeh ymetlrgqgv rtavladaph pftrqwlrvr gaddaararl
      241 ndmrqrygae tllacgaa
//
LOCUS       WP_011296520             437 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Cupriavidus].
ACCESSION   WP_011296520
VERSION     WP_011296520.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 437)
  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 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   3  (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   4  (residues 1 to 437)
  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 437)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..437
                     /product="CmpA/NrtA family 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=47172
     Region          61..311
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mpsrlriakp lpaavdttla apdaapassg rrralasiag asvmtlvdpl vragawaags
       61 dapekpevri gfipltdcas vvmaaalgfd kkygikitps keaswagvrd klvngeldaa
      121 hvlygliygv qlgiggpkkd mavlmslnhn gqaitlsskl aekgakdgas lkalmskekr
      181 eytfaqtfpt gthamwlyyw laanginpmq dakaitvppp qmvanmrvgn mdgfcvgepw
      241 garaiadkig ftvettqaiw kdhpektlgt taefvqkypn taramvaavl easkfidasa
      301 snrrktaeti aaksyvntdm diildrmlgr ysnglgktwd dpdsmkfyqd gsanfpflsd
      361 gmwfltqhkr wgllkehpdy lgvakqvnri diykqaataa qvplpksdfr taklidgvvw
      421 datrdpkaya dgfkika
//
LOCUS       WP_011296616             192 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Cupriavidus necator].
ACCESSION   WP_011296616
VERSION     WP_011296616.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus necator (Ralstonia eutropha)
  ORGANISM  Cupriavidus necator
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Cupriavidus necator"
                     /db_xref="taxon:106590"
     Protein         1..192
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22091
     Region          1..180
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 meaffdwlfe tvalpkvglp aifvvslvsa tllplgsepa vfgyiklnpd mfwpavlvat
       61 lgntaggaid wwlgyaakla lvryrkrrqm reheqehreh rrhvrkptkp kldaryfhwm
      121 krlgpptlll swlpavgdpl ctlagwlrls fwpslaymai gkflrylamt asllwipdsf
      181 whniaqmlrs wf
//
LOCUS       WP_011298004             829 aa            linear   BCT 20-JAN-2025
DEFINITION  penicillin acylase family protein [Cupriavidus necator].
ACCESSION   WP_011298004
VERSION     WP_011298004.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus necator (Ralstonia eutropha)
  ORGANISM  Cupriavidus necator
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 829)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 829)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 829)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..829
                     /organism="Cupriavidus necator"
                     /db_xref="taxon:106590"
     Protein         1..829
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=91871
     Region          24..820
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 mrwfrrlawl vivlllvsaa alaggyiwyr qasqpqtagt lslqglqgrv tivrdrnavp
       61 hiraasrldg yyamgfvhaq drlwqmqmnk rivagrlaei lgpkaldtdk flrtlgvrrn
      121 aeaiyaqlep dtraalqaya agvnayidqr kgplppefll lqtrpehwep adtlgwqtmm
      181 awdlggnwtq etlrmalsqv lptarisell apypgerpvr tldygtlyrh laplasalar
      241 vgdmappsyv egmgsnnwvv sgahtqsgkp mlandphlgl qapalwyfah lqapgldvag
      301 atlpgaplvv lghnariawg ftntapdvqd lylerlqpgs tdnyqtpdgw aafvtraeti
      361 hvkgaadval tvretrhgpv isdvsepvan aasplgaryv vafqwtalra ddrtfqaglk
      421 lnvatdwasf tqalrdfhsp qqnmvyadvd gnigfiapgr iplrradndl kgltpapgwd
      481 arydwngfip fehlpraynp pngiivtanq rivgtdypyf itsewtvpyr yqrirsllda
      541 tprhtfesfg aiqkdvvsla vrdilpllla spvasdksrp grerelfdal rkwdgtmdat
      601 saeplvvsaw lrelsrrlfe dkvgeplfqr mweqrnvhqp mlnilrnpag pgslgsfwcd
      661 klgttehesc aaavadawtl aiadlsqryg dnagkwrwgk ahaarsehkp fgkqpylsgf
      721 fnlrvptggd tytvnvgrnn lrdeqapfes thaaslraly dlsdldasrf mdstgqsgnp
      781 vspnyrdwtg kwaaveyitm agkqepvrep fdtlvlepak vregavrgk
//
LOCUS       WP_011296813             407 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate/propionate family kinase [Cupriavidus].
ACCESSION   WP_011296813
VERSION     WP_011296813.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..407
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42883
     Region          7..402
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 msathpvvlv vnagsssvkv svytvpeaah dnadinpvls ahgqiesigv aprlrasmad
       61 ghvvadesfp vaqvadhdaa frlirlvlsv glrdnppvai ghrvvhggsd faqavriddd
      121 visrlealip laplhqphnl tairavrkaa pdllqvacfd tafhaghdml aqlialpyey
      181 yergirrygf hglsyeyiar rlgqvapdva agrvivahlg ngaslcamrd grsvestmgl
      241 taldgmpmgt rcgsidpgav lwlaqqgmta daiqtmlyga sglkglsgvs sdmrallase
      301 eprarlavdf yayraaqeig klavtlggld tlvftagiga nsppvraric ahltdlfgis
      361 ldnaanndns qrvssdasrv pvlvlptdee gmialstari lresgkl
//
LOCUS       WP_011296973             163 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV pilin protein [Cupriavidus].
ACCESSION   WP_011296973
VERSION     WP_011296973.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            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="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=17602
     Region          15..161
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mnartlahrg stglcrtrrl aqgmtlmelm avvailgila aiaipnytey vrrgyradar
       61 gmmteaaqvl erfrsvngry nqdvggnafa lpaglrtspr dstrvrynvs ivansltans
      121 yllqavpvda tdacgtytld qagtrlntvg anpaaylqnc wer
//
LOCUS       WP_011296881             180 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Cupriavidus].
ACCESSION   WP_011296881
VERSION     WP_011296881.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 180)
  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 180)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 180)
  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   4  (residues 1 to 180)
  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   5  (residues 1 to 180)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..180
                     /product="TRAP transporter small permease subunit"
                     /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=20494
     Region          4..167
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mnyllglsrq idrlnqhtgr lanimillsc lisagnallr ygfnlsdnwp lelqwymfai
       61 avmfgasytf qrnehvrvdl fygnvseraq hwidifgivv fllpscilft wlswdslflp
      121 swrileqsgn sgglprypik lvvpvgfall alqgvselik rfaalkglvr ieskyerpvq
//
LOCUS       WP_011297793             443 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [Cupriavidus].
ACCESSION   WP_011297793
VERSION     WP_011297793.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 443)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 443)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            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="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48294
     Region          8..428
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 msfelhpryl evhlhgrlcg flceaggntr fvptdeyrgd nerytlslsi tlpteigrea
       61 tsavfdnafh paiyntggel ppyfagllpe gelrkrlest rtnpedkddf gvlasagndl
      121 pgaivvkpad vralpgyvrt ygvtggadnl eiavvegate gaasvsgvqn klalstmrkg
      181 erytlptkgk vsdiiaklpa knddsqvfne yvsmhlaaaa gvniapiqvl pmssidvpdl
      241 adlmgkglhy laverfdraa dggllhaedg cqmlgrmpnr kyakreeyir llaalyrlsp
      301 kgfenvrqff lrqavntlig nsdahlknfs viyrdrklpe lspaydivcv aalpnftsyg
      361 qnvaideiqr ketmdlyedi adkagiprri ataavkeavs mahahwpgll ekmgasqalr
      421 dviaerlenl plakvgrptr kga
//
LOCUS       WP_011298070             699 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acetate--CoA ligase family protein [Cupriavidus].
ACCESSION   WP_011298070
VERSION     WP_011298070.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 699)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..699
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=71675
     Region          6..680
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mteifhalfa pasvavigas dnpnkvggrp ihymrhfgya gevfpvnpgr ttiqgyrayp
       61 tlhdigrtpe aaviavsgda tleqvrlcad agvkaavima sgfaetgeag rrrqqqlvda
      121 anaggmrlvg pnaqgtanfa sgavlnfstm fmevtpqdgp iaiisqsgaa svmpyallrq
      181 aglgvrylva tgndadldac amtaavaadp eirlilvyle sitdpaalar aaalarsrga
      241 sivavkagss qhgaraaash tgalvgndaa idaflarhgi wrardigelv ravplylqgr
      301 apgqgrtvvm shsgavgvms adlaerhglp laalqsstld rlgailpefg tagnpldmta
      361 almgkgdmfp rvldtlgadp qadmlmvgip vagpgydvea lardaaafss rfgkplvasa
      421 pqqnvrdafv rhgvptfvte adavaalaqy agharlagva aepevepqag wpalqpldgt
      481 glqdearslt llgeagvpvv pyrccanade avaafaalgg gavvvkgcaa evphksehgl
      541 vhlrladapa vaqaaedcla alrslgvasp rvvvaamvrg rhefalgvsv dslfgplvmi
      601 geggtllelr kdvvtllapf tmadvkaaca rlrlaplfng yrdipvldld alaasavalg
      661 nwalrhrgtl ksvdinplmv maagdgvvav davvelqga
//
LOCUS       WP_011299952             700 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Cupriavidus necator].
ACCESSION   WP_011299952
VERSION     WP_011299952.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus necator (Ralstonia eutropha)
  ORGANISM  Cupriavidus necator
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 700)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Cupriavidus necator"
                     /db_xref="taxon:106590"
     Protein         1..700
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72529
     Region          10..700
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mnttptaipd cllnprsvai igasdeptri ggrpissmla kgyagrimpv npnrstvqgl
       61 ptyasvadlp evpdvaiiav paqhalqavk alaergtkaa ilftagfaev seegaamqae
      121 mvaiarrggm rllgpntlgm vnmhngfvgs fstfsslgvs rpgrvgivsq sgaygshlvs
      181 sameagvyps sivmtgnead lnvsdivrlf aadpmtdvia vyaegisdgp glvdalkaah
      241 aagkpvvmmk vgrsevggaa arshtasiag ddavvsavld elgvvrvrtt eemldilrla
      301 srrvfpadnt lgvvtisgga gviisdaaed lgipmpempa aaqarmlekl picaprnpvd
      361 vtaqfindtt lvtpfteamm geggygtlla ffsyaasyht vadtllqqla dvrkrypdrl
      421 yvmvgrgdpt vlaryeeagf tvfgdpsrav aaiaamgrfg ralagkttap apqvpavtlp
      481 satpteaeak allaeagips aperacadee aavraareig fplvlkilsp dilhkseigg
      541 vllnvnsega vregfallle rahkavpdar iegvlvakql vggvecimgi nrdpvfgpia
      601 mfglggvfve ilkdvvfhrc pfgpdvaeem irsikgapll lgargrpvtd ipalartlsq
      661 lsafavaagp rlqsidlnpv lampegqgay avdavievge
//
LOCUS       WP_011299827             725 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate--CoA ligase family protein [Cupriavidus necator].
ACCESSION   WP_011299827
VERSION     WP_011299827.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus necator (Ralstonia eutropha)
  ORGANISM  Cupriavidus necator
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 725)
  AUTHORS   Hegg,E.L.
  TITLE     Unraveling the structure and mechanism of acetyl-coenzyme A
            synthase
  JOURNAL   Acc Chem Res 37 (10), 775-783 (2004)
   PUBMED   15491124
REFERENCE   2  (residues 1 to 725)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437147
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..725
                     /organism="Cupriavidus necator"
                     /db_xref="taxon:106590"
     Protein         1..725
                     /product="acetate--CoA ligase family protein"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043758 - acetate-CoA ligase
                     (ADP-forming) activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=74976
     Region          3..724
                     /region_name="PatZN"
                     /note="Acyl-CoA synthetase (NDP forming) [Energy
                     production and conversion]; COG1042"
                     /db_xref="CDD:440664"
ORIGIN      
        1 mvdlnsllyp rsiavigast qpdkvggmpi rllrelgyag riypvnasaa evqglpaygs
       61 lsdigepvdl aiiavpasas qdvmaqlagn gtraavvfts gfaeaggagv qmqerlarsa
      121 qqagitllgp nclgamnlre rvfatfspia lsgtppvgev glvsqsgafg ayafalarea
      181 glglshwvtt gneaglqvad viewlahdpn trvilayieg crdgarlrra laaaraagkp
      241 vvvtkvgtte agarsaqsht aslagedavy qavfeaygvh rahtleeffr lgyvlsrgrr
      301 patwqrtsgg dadvgtplgi vtvsggvgim madraeelgl plppmpddaa aalrtaipfa
      361 stanpidvtg qivaqprvfm daiadvarsg aygsvavfla gganaprfwp elqqaigals
      421 eaadaaplmv sglvdddkra wleargclvf repghaveav atlaraaale dargddaieg
      481 qaqsdpqddl lrdippaata lseyeamrll aeagvpvaph dlardaeeav riaerlgypv
      541 vvklcsreil hksdvggval nlanaqavrd afgrmaqava glrtdkgtpv aldgvlvarm
      601 vrgwgevmvg vrrdpvfglv alagiggtav eifrqtacgl aplsreqara mlhasrvaal
      661 ceghrghpqv dlnaaaqvla svsqlaaelg drldtieinp fivtapglva adavvtlrad
      721 shgal
//
LOCUS       WP_011299974             352 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Cupriavidus].
ACCESSION   WP_011299974
VERSION     WP_011299974.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 352)
  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 352)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 352)
  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   4  (residues 1 to 352)
  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 352)
  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 12117701
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..352
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38733
     Region          21..202
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          246..328
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msrlvrsatl srytevarsv gldplrilae vglprtclda gdnlvsanav crllemsaad
       61 sdaedfglrm gegrqlsvlg plgmavrdsp tlrdalgamv ryitlhseal flgveerega
      121 lvirvslive hagstrqade mvvvslyrml qeligpgwra rriclsheap rslashlrvf
      181 gravdfgcdf ngivcelkdm dampraarpe laqyahayld slsaratlsm tenvrrmvls
      241 llpsgncsve rvasqlgvdr rtvhrkllqe gasfssilde vratlalqyl rhlerpvsyv
      301 avllgfsmqs afsrwfrdhf gcspsawrse gmqparpvpr qpllaaspeq rm
//
LOCUS       WP_011298711             112 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ComEA family DNA-binding protein [Cupriavidus].
ACCESSION   WP_011298711
VERSION     WP_011298711.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (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   2  (residues 1 to 112)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..112
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10992
     Region          18..84
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mfkalfkrgc laaaiwmalt gaamaavdvn tadataltsv kgigpatakn iidertkhgp
       61 yksaadlaer vsgvgaksva rmqeggltig akaapaaaap agaaaaqrsa kr
//
LOCUS       WP_011300365             698 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor family protein [Cupriavidus].
ACCESSION   WP_011300365
VERSION     WP_011300365.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 698)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..698
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..698
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=76119
     Region          34..698
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mkgarhwrra aalpaaaltg aaiaqtapvt gpepvtlptv tatakaegsl tvpgvarqre
       61 slyqsagsvg fvdaesyant yasnlrdvlk dapgvyvqer ygqelrlsvr gsgiargfht
      121 rgleilqdgv ptnfadgsgd fyqidpigln aaevykggng laygsttlgg ainfttptaf
      181 tteapnqvrv dggsfgtvra agqasrqign fdfmanlsvd hsegyrdher gqyeqlnanf
      241 gyrfsptvet rfyvgayvvd qllpgtlslq dalnnptkas asalagdqar ntrterlanv
      301 ttvkldsgql dfstwvihkn lyhpifqvid qdywtygfap rytgtqtigg mrnqliagar
      361 ffggnndarq yvnvsgdrga qtlnsrqday nyeayfedrl yvmptvavma gakayynqrr
      421 ytdygglpan pvpksddtty sgvnpkfgvl wepakdiqaf aditrsadvp dfsdlnqtis
      481 tttqfvplsa qhgwtlelgt rgrrerlgwd ltlyrslvrd qllqyttnpn vpaatfnanr
      541 ttlqgvelgv sadllqnvat tadkvtlsql wnysdfrfdn dpqygnnria gvpehvlrtt
      601 laysqasglr iagtidwvpt gayvdyantl kvpsyvlfgv qasydfkqgl tvfldarnlg
      661 nkryvsdfst vtdartanta vfypgtgral yagvrykf
//
LOCUS       WP_011301408             384 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: UxaA family hydrolase [Cupriavidus].
ACCESSION   WP_011301408
VERSION     WP_011301408.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..384
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=40106
     Region          <1..384
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mattflgypr engavgvrnw vavvsvmdnc npvtrtiart vggcipvttl fvrgqfgadl
       61 dfafeqlagl grnpniasvl lvglepsste evarriqaag kpvervhlqp ngtvdciaeg
      121 trkaarlsla asrarrvpcp vsslvigvec ggsdttsgls cnpvigrmad mviaeggtvi
      181 isetsefiga dhlfaeraad grvreafvta vrnmenlais rgvdmredqp spdnkrgglt
      241 tveekalgam akagstplvg vlrygeaprk pglhfmdapa aavenltala aggcqltffg
      301 tgvgnpigsm vaptvkvcgn vntlqtmadn idfdvsgvlq hgekisdlge qlyayamdia
      361 sgtqltsevl dvretaisrf alsl
//
LOCUS       WP_011300762             708 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Cupriavidus necator].
ACCESSION   WP_011300762
VERSION     WP_011300762.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus necator (Ralstonia eutropha)
  ORGANISM  Cupriavidus necator
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Cupriavidus necator"
                     /db_xref="taxon:106590"
     Protein         1..708
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=77309
     Region          20..708
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mkssrcgnep aapqialrat alavsllcma plafaqkvda qsgesgnveq vldtvqvtgn
       61 wlgtglqnsv ktfpgartvv geeqieqsga ssisdvmrri pgvqstdnsg tsgsaislni
      121 gvrgltgrys prstvlldgi pmavapygqp qvsfapvslg nidsidvvrs ggavrygpqn
      181 vggiinfntr piptspgitg dasireniyt egggsntqyn afvgttldsg lglavlysgm
      241 tgrewrkgsd ddvndlavkf aydinntsqv ygkvsyydvr srtpggltva qynadpfqnt
      301 rpndywsgnr tafdlgyvnt isgnqefeir tffnesyrqs tlqqsatvia hqprnyttfg
      361 ieprytqrla lgptthditv gyryirergd dnafnqnprt gvvgptttfd natdahavyi
      421 ddriavgnwr ivpgvrfehi dttrqqrgtt tqfdsmnnka lpsinvsylv nnawtvftdy
      481 stsfgpvqnt qlnsqtpsnp lqpevartfe vgtrwtdnri kaeltafkik fdnqiqqvpg
      541 lfpatfqnig atdhdgveta idytfdrasv lgglnvyany tytraiqksg atagmdvpfy
      601 srntdtigar ynwrnwtfna stthqsaqys dlantvaesa dgsvgripgf rtwnlqamft
      661 vpqwkrtdit iginnlfdkr yytrttdsna grlvgaprmv yiqaragf
//
LOCUS       WP_011301335             345 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter substrate-binding protein
            [Cupriavidus].
ACCESSION   WP_011301335
VERSION     WP_011301335.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 345)
  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 345)
  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 345)
  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 345)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..345
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=37636
     Region          18..343
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 msgfnngrrl alkqgialva asaasglmih tparaagqty nyklgialda thpttvnlta
       61 aaaeiarasn grlnirvfpn sqlgsdtdmv sqvrsgaidl vstagliwgt lvpaasisgi
      121 gfafpsyehv wkamdgdlga hirgafakvn lmplpkiwdh gfrqvtssnr qintpqdlsg
      181 fkirvplspa ltsmfkafga apaginmaet ytalqtkivd gqenpltilg tqrlyevqky
      241 csltshvwdg fwlvanlrtw nalpedlrql aattfdtyav kqrqavdaln trlreelkgr
      301 gmvfnqpdvk vfrdylskag fyrdwqkkfp aetwalleqy sgkla
//
LOCUS       WP_011301773             380 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Cupriavidus].
ACCESSION   WP_011301773
VERSION     WP_011301773.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 380)
  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 380)
  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   3  (residues 1 to 380)
  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   4  (residues 1 to 380)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 380)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 380)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..380
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40204
     Region          30..366
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(106..108,128..129,178,230,254)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mkrhllgmaa laalglafad saiaqvqevr lgfaapmtgn qaqygkdmqn gvtlaledfn
       61 atrpringqe vrfvlvsedd qadpkagsvv aqklvdggik gmlghfnsgt sipasgvysr
      121 agipqiamat apeytrqgfk ttfrmmtsdt qqgsevgayv vnklgakria ivddrtaygq
      181 gladefekaa kaaggtivrr eftndkavdf kavltnlkhq spdvvfygga eaqsaplarq
      241 mrelgmksvl vsgemskten fiklagnaad gtlcslaglp ldqmpggagy kqryekrfsg
      301 pvqtyspyay dgamammkam vqanssdpqk ylaslaasat pgvtarqiay dargdlkegg
      361 itiykvvsgk wqpveslagk
//
LOCUS       WP_011303454             334 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Staphylococcus].
ACCESSION   WP_011303454
VERSION     WP_011303454.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus
  ORGANISM  Staphylococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Staphylococcus"
                     /db_xref="taxon:1279"
     Protein         1..334
                     /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=39105
     Region          1..275
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 msqlkerdyf fdnaramlif lvvfghllqp yteaskhlss lyltiysfhm pgflfisgyf
       61 akkagqagyl ekvskkllip yviffgffsf yyyltgkeds vkfdpfdpvf alwflltlff
      121 fhvilvivkd ykpyyvlpia iiislfagys snidnylsfs rtimffpify lgylftnkhi
      181 qtlknkklvp isiiilivfy vtytyhpina drllgdspym slegkqdlys pikrlllyfi
      241 ilitlfsfln lipekekfyt yigrrtmyvy llhglvigvi rgfgiypfkd svsiltyvyl
      301 llfttiivya lstrfvskwt npiinlqsps kfke
//
LOCUS       WP_011311234             675 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Thiobacillus
            denitrificans].
ACCESSION   WP_011311234
VERSION     WP_011311234.1
KEYWORDS    RefSeq.
SOURCE      Thiobacillus denitrificans
  ORGANISM  Thiobacillus denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Thiobacillaceae; Thiobacillus.
REFERENCE   1  (residues 1 to 675)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..675
                     /organism="Thiobacillus denitrificans"
                     /db_xref="taxon:36861"
     Protein         1..675
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=74288
     Region          3..674
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mkkkllavli plafsahaqe teqleavsvs adwlgaatpe aakkhpgart vvteqelaes
       61 gartvedalr tvpgvrvlde sgtgilpnig vrglsplrse qvlvlvdgmp itlapygqtg
      121 lslfpltlna veaidvargg vavhygpnnv ggvinfvtkr iprkpaftak etlsiassgn
      181 llsdtylrag gfvserlglq aqanliegea erdhsstsvq nlmldadwfl tdsanlragl
      241 qyyktendmp galtpasyea dreqstrpld rfdgdtlrgh vtysqafang aelswanfah
      301 rsnrqfffgn ssnadtpstn emssprefwv ygseprltfd idagvkqkis lgarylreev
      361 dyvvdsrtla tnayavtrdw rfendavaay lsdtfflldd rlkvtpgvrh etvdlyyrnn
      421 ltgaetrdtt kdwlpgidig yqasdavflf anyhkslrpv qftqitfggd ldaeraenye
      481 agirvaptan vdtsltafrf dfdnklefvs qavgfrnlge arhqgveaev awrpaavrgl
      541 elktaytyvd teqrsgqfeg nelplaphhq lnlqgnyrsg dwnwnlngly qsasfsdgan
      601 tvdenatgsv gripaysvwn aqvtrdfrwn gtkmkaalal nnlfdrdyyf rgvdfsqgrm
      661 papgraallt lqmdm
//
LOCUS       WP_011311188             810 aa            linear   BCT 20-JAN-2025
DEFINITION  Lon protease family protein [Thiobacillus denitrificans].
ACCESSION   WP_011311188
VERSION     WP_011311188.1
KEYWORDS    RefSeq.
SOURCE      Thiobacillus denitrificans
  ORGANISM  Thiobacillus denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Thiobacillaceae; Thiobacillus.
REFERENCE   1  (residues 1 to 810)
  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 810)
  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 810)
  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   4  (residues 1 to 810)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Thiobacillus denitrificans"
                     /db_xref="taxon:36861"
     Protein         1..810
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88021
     Region          1..805
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mtidtlppsa lrltidpasl gfadtselqd ealpwigqar aeaaatfglg mgapdynlfv
       61 lgevgsgrss llrqamhaaa atrrvppdlc ylhnfdaper plalrlpagq gralrqqlad
      121 airtlqsdip qrlqgpdyka ererieqawk devarhyadl tafaearsfs lhreggrmvf
      181 tltgkkgqal tedevlalpk arriaveeae qelraeisry ieqtqplera mnealarsrr
      241 qfvkplvare lqairselkk qikdaaklna wldaleqdll dnlevfdgde gddgdeqapa
      301 tpasvvaryr vnlvvdnggl agapvvvedn pvhrtlfgsi eyqseadvlm tdfsrirags
      361 llqahggflm lhlrdvladp lvwerlrrfl rsgrlqieep gvslaplatm slapepvdve
      421 vkivlvgsre qyyalqdaap efmrhfrakv dfadsflard etrrasaifv ahacrqhglp
      481 hfspaavarl leeshreadd qaresaifaa tealvlesaa icrargpglv laedvevalv
      541 araarhdype qrlresiadg dvlialrgaa sgqinaltqv dlgdarfglp vrvsartyag
      601 edgvlniare velsgpvhdk gvfilqsyla alfghlapls ldasiifeqq yqgvegdsas
      661 caefyalvsa lsgvtfsqgi avtgalnqhg evlpvggine kiegwfrvce tagldgrqgv
      721 liparnrrhl mlapavvaav aagrfhvhta ehvldglall sglaageada aghyphdsvl
      781 graeaalraf reacekarah rpearrsgrr
//
LOCUS       WP_011311448             577 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: site-specific DNA-methyltransferase [Pseudomonadota].
ACCESSION   WP_011311448
VERSION     WP_011311448.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonadota (proteobacteria)
  ORGANISM  Pseudomonadota
            Bacteria; Pseudomonadati.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Pseudomonadota"
                     /db_xref="taxon:1224"
     Protein         1..577
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=65218
     Region          7..508
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mskqkleltw igkekrpkle prilledpek syhakhrvsd ndifdnrlif gdnllalkal
       61 eqefsgkvkc vfidppyntg safaqyddgl ehsiwlglvr drleiirrll sddgslwisi
      121 ddneahylkv lcdeifgrkc fvtsfiwkkv dspndnkgal spdheyilcy vknpdsiyfr
      181 pkqdesilna yrqpdaesdr pyrdrllkkn gknslridrp smyfpikgpd gvdvypihdd
      241 gqearwamgk kgvdeliakg elvwkqresg gvlrwvpytr eyapdaptrp wptiwsdlht
      301 trqtkahqrs vlegvqafet pkpedlvsri lsistnpgdw vldsfagsgt tgaaahkmgr
      361 rwimveleet chthiiprlr kvidgedkgg vtealswhgg ggfryyrlap slivndrwgn
      421 pvinpeynaa qlaealakle gfnyapseth wwqhghsser dfiyvttqnl saeqlqalad
      481 evgpersllv ccaafhgvta akaaerwpnl tlkkipkmvl archwgrddy slnvtnlpma
      541 eieksepapp gnsfkntksr kaalanagqg glfgene
//
LOCUS       WP_011312109             255 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Thiobacillus denitrificans].
ACCESSION   WP_011312109
VERSION     WP_011312109.1
KEYWORDS    RefSeq.
SOURCE      Thiobacillus denitrificans
  ORGANISM  Thiobacillus denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Thiobacillaceae; Thiobacillus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  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   3  (residues 1 to 255)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Thiobacillus denitrificans"
                     /db_xref="taxon:36861"
     Protein         1..255
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28097
     Region          44..254
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 msssppqhdl ghcdgddfla rytlhsraei lfqlralqkr kvlvnldlse srqiivtsvl
       61 avneadntvv ldsargdaln nelmsgkgae fvaqldgvsi sfsigavslc eyeklpalri
      121 pvptslirlq rrehfrvplp ianpvkcivp spweeskeqi tthlvdigcg gvaltdigar
      181 lgtesgrllr gcrlllpetd vvvttleirn saqirlqngs fqtrlgckfv dlpndmaahl
      241 qrfvmniera rrnrl
//
LOCUS       WP_011312469             309 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Thiobacillus denitrificans].
ACCESSION   WP_011312469
VERSION     WP_011312469.1
KEYWORDS    RefSeq.
SOURCE      Thiobacillus denitrificans
  ORGANISM  Thiobacillus denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Thiobacillaceae; Thiobacillus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  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   3  (residues 1 to 309)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Thiobacillus denitrificans"
                     /db_xref="taxon:36861"
     Protein         1..309
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33015
     Region          123..307
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mdnprsirvh aselevgrpl swavydengv lllnkgmapa teaqiiamlq rgvfrqpgsg
       61 vgagaagsks aippmglgps edesktrltg dpipfddlam qpgevlqlhp alevvaadvp
      121 avligylkdr aivvatpmvs gkpllvkdgt lfniktfsgt slynfrtrvl ashshpmphl
      181 hleyprlvcq tkirkalral tdlpatllnp asgdsrdvvl kdlsvggaki vlpepvtcak
      241 gdpfvvgfri kigddleeai radavmcsae srtgkettvh tmsvqfkelp kstslaimal
      301 vyrlqlrkg
//
LOCUS       WP_011312784             423 aa            linear   BCT 20-JAN-2025
DEFINITION  CmpA/NrtA family ABC transporter substrate-binding protein
            [Thiobacillus denitrificans].
ACCESSION   WP_011312784
VERSION     WP_011312784.1
KEYWORDS    RefSeq.
SOURCE      Thiobacillus denitrificans
  ORGANISM  Thiobacillus denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Thiobacillaceae; Thiobacillus.
REFERENCE   1  (residues 1 to 423)
  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 423)
  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 423)
  AUTHORS   ter Beek,J., 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 423)
  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 423)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Thiobacillus denitrificans"
                     /db_xref="taxon:36861"
     Protein         1..423
                     /product="CmpA/NrtA family 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=45836
     Region          49..298
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mtdsqdksri qdpskrdfik qgarlsaaaa lmalvppgvr sgawaagsda pekaalkigf
       61 ipltdcasvv vaavkgfdkk ygltitpske aswaavrdkl vngeldaahv lygliygvql
      121 giggpkkdma vlatinnngq aitlsnqlra kgvsggasla klvkaeprey tfaqtfptgt
      181 hamwlyywla aygidpfrdv knivvpppqm vanmrvgnmd gfcvgepwga rairdrigft
      241 avttqeiwkd hpekvlgtta efverypnta ramvaailda skyiddlknr aevakliaak
      301 syvntdvasi egrmrgqydn gigrkwvdan smkffaggqv gfpylsdgmw fltqhkrwgl
      361 lkthpdylav artvnridvy kdaaaltktp lpssdmrask lidgvvwdgs npqayadgfr
      421 ika
//
LOCUS       WP_011314507             362 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Nitrobacter
            winogradskyi].
ACCESSION   WP_011314507
VERSION     WP_011314507.1
KEYWORDS    RefSeq.
SOURCE      Nitrobacter winogradskyi
  ORGANISM  Nitrobacter winogradskyi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Nitrobacter.
REFERENCE   1  (residues 1 to 362)
  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 362)
  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 362)
  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 362)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Nitrobacter winogradskyi"
                     /db_xref="taxon:913"
     Protein         1..362
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=39725
     Region          1..354
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkrrdflkgs aagaavsava spaiaqsape ikwrmtssfp ksldtiygta avfakqvaem
       61 tdnkfqiqlf aagevvpalq aldatanntv emshtasyyy vgkdptfaif asvpfglnar
      121 qqnswlfqgg gneladeffk kfgvvglpcg ntgtqmggwf rkeiktvadl sglkmriggi
      181 agqvlqkvgv ipqqlaggdv ypslekgtid aaewvgpydd eklglqkvak yyyypgfweg
      241 gptlhafcnl ekwntlpkty qailvnaant antwmtaryd mqnptalkrl vaggtqlrpf
      301 shdvldaclk atnelwgeis annadfkkvi damqayrsde ylwwqvaeyt ydtfmirsrt
      361 rg
//
LOCUS       WP_011315316             410 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Nitrobacter
            winogradskyi].
ACCESSION   WP_011315316
VERSION     WP_011315316.1
KEYWORDS    RefSeq.
SOURCE      Nitrobacter winogradskyi
  ORGANISM  Nitrobacter winogradskyi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Nitrobacter.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Nitrobacter winogradskyi"
                     /db_xref="taxon:913"
     Protein         1..410
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=45064
     Region          15..399
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mtessaqvvl gesltpigql rftqtgprqf stfsydpawi kdpraftlqp dmpfeggpfh
       61 asaqpgnprd alagafsdaa pdswgrrlle raygkglsef eyltlsddtc rqgalrfldd
      121 qgkvitgksv eavprlldlq aitaiaraye qgkdisaedm qalagaggsg ggrpkanvrd
      181 ehvlwlakft sihdqhpieq ievatltlak acgirtpevr leladtpfpv aliqrfdrrg
      241 saripyisar talgktgtel gsyteivdfm rtaasdpkad fqelyrrlif tilvsnkddh
      301 lknhgflyvg sgrwrlspvf dvnpapdrnp hletaimegg shdrsiklal daceffeipe
      361 adarrtirta aqrisdgwrd afrqvgvtga rvrdyepafi neqtdiglal
//
LOCUS       WP_011315580             270 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Nitrobacter winogradskyi].
ACCESSION   WP_011315580
VERSION     WP_011315580.1
KEYWORDS    RefSeq.
SOURCE      Nitrobacter winogradskyi
  ORGANISM  Nitrobacter winogradskyi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Nitrobacter.
REFERENCE   1  (residues 1 to 270)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Nitrobacter winogradskyi"
                     /db_xref="taxon:913"
     Protein         1..270
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=29668
     Region          26..138
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cd16913"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mrrflvpvag lillaaggva dakvsilvdk dnqrmtvsvn gveryqwpvs sgnpsyetpn
       61 gkfqafrmea dhfskefdda pmphsifftk aghaihgtls egslgvpvsh gcvrisrana
      121 stlfslvkqe gvlnttvtlt gssrvalarn prgkrktdva grdpgpayqs ydaagnpvdl
      181 tprqiapgwq pqayvrgadg ymypadgrsn dprypdprsy rrhygaqnvp pqqhsyygdr
      241 neygyaqpyq pqvyapqpyr prglfsdfdd
//
LOCUS       WP_011315738             114 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Nitrobacter winogradskyi].
ACCESSION   WP_011315738
VERSION     WP_011315738.1
KEYWORDS    RefSeq.
SOURCE      Nitrobacter winogradskyi
  ORGANISM  Nitrobacter winogradskyi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Nitrobacter.
REFERENCE   1  (residues 1 to 114)
  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 114)
  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   3  (residues 1 to 114)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Nitrobacter winogradskyi"
                     /db_xref="taxon:913"
     Protein         1..114
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=12931
     Region          15..112
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mrgpkpnvtg farhlrisqt qaeaklwsri rarqidgrkf vrqvpvgpyf cdfvcreqkl
       61 vvevdggqha dsqgdhirdr yltmngyrvl rfwnndvlgn iegvvsviha elig
//
LOCUS       WP_011315640             137 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Nitrobacter winogradskyi].
ACCESSION   WP_011315640
VERSION     WP_011315640.1
KEYWORDS    RefSeq.
SOURCE      Nitrobacter winogradskyi
  ORGANISM  Nitrobacter winogradskyi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Nitrobacter.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Nitrobacter winogradskyi"
                     /db_xref="taxon:913"
     Protein         1..137
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=14784
     Region          18..76
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 mamegnsesl igsdkesgka vygaedkkig siervmidks sgepayavls vggflgvgde
       61 hypvpwrllr ydseldgyrs disgnrlkgy pksvfgssgs elfdwtarra eldsyydnid
      121 tvttkegaes pltrnsg
//
LOCUS       WP_011317739             184 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter small permease subunit
            [Nostocaceae].
ACCESSION   WP_011317739
VERSION     WP_011317739.1
KEYWORDS    RefSeq.
SOURCE      Nostocaceae
  ORGANISM  Nostocaceae
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales.
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   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (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   4  (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   5  (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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Nostocaceae"
                     /db_xref="taxon:1162"
     Protein         1..184
                     /product="TRAP transporter small permease subunit"
                     /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=20884
     Region          4..177
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mekllkisri idaftervgr ytswlvlvmv ilgvwnvvgr ylgrisgnnl tsnayieaqw
       61 yifdvifflg aaytlkhneh vrvdifysnw qrrrkaiadf lgtifflipf siivifvswd
      121 tivaswqige lspdpgglpr ypikamiivg fvlliiqgis qaiknlaiiq grlepqeenh
      181 dagl
//
LOCUS       WP_011317875             458 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Nostocaceae].
ACCESSION   WP_011317875
VERSION     WP_011317875.1
KEYWORDS    RefSeq.
SOURCE      Nostocaceae
  ORGANISM  Nostocaceae
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales.
REFERENCE   1  (residues 1 to 458)
  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 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   3  (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   4  (residues 1 to 458)
  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 458)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Nostocaceae"
                     /db_xref="taxon:1162"
     Protein         1..458
                     /product="CmpA/NrtA family 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=50252
     Region          56..316
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mteffnqfsr rkfivtagas agavflkgcl gnppettggt qsaptaqpaa nvsaeqapev
       61 ttvklgyipi vesapliiak ekgffakygl tnvelskqas wgsardnvei gsagggidgg
      121 qwqmpmphli teglitkgnq kipmyvlcql ithgngiaia nkhqgkgisl klegakslfs
      181 qlksstpfta aftfphvnqd lwirywlaag gidpdadvkl ltvpaaqtva nmktgtmdaf
      241 stgdpwpfrl vndkigymaa ltaeiwknhp eeylamradw vdkypkatka llkgimeaqq
      301 wldnfdnrke aaqilagrny fnlnnpeila dpyvgkydmg dgrkiddksm aayywkdekg
      361 svsypykshd lwfitenvrw gflpkdylan gaakakelid kvnrediwke aakeagiaaa
      421 diptstsrgv eeffdgtkfd pekpdeylks lkikkvsv
//
LOCUS       WP_011320338             589 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: calcium-binding protein [Nostocaceae].
ACCESSION   WP_011320338
VERSION     WP_011320338.1
KEYWORDS    RefSeq.
SOURCE      Nostocaceae
  ORGANISM  Nostocaceae
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 589)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 589)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Nostocaceae"
                     /db_xref="taxon:1162"
     Protein         1..589
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=61119
     Region          <6..181
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          172..421
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mtiicgtnsn dylyggdesd tikgfagydy lygglgddyl yggldndkly gglgndklyg
       61 gegndnlnge egnnslygea gddtldagns tgnnlldgge gndeiyvyss sgdntlkgga
      121 gndildvrfs ygknildggs gndqlyarys qgnnslrggs gddylgvdls agnnildggd
      181 gndildisyq wkgknivsgg ngndifyayg vqgsntlngg sgndsfyiss pdantvvhpl
      241 atqtvdggtg ydylcidyss aiagitssfn tttkqglita dtnqirykni eqlkiigtay
      301 ddiivggnsd diidggsggn dtlnggagnd ilsirgnsrn nntvyggagn dslyandtag
      361 tnlldggdgn dylsatnnys yffnasqtli ggagddtldv sgsygnnfly ggagndslya
      421 dysvgphtld ggdgddylsa kgsssrfiin thildggagn dildvgsara knkliggggn
      481 diligglned tfvfknyneg idriynfdhl driqicavgf ggglspdsls agqftlgtva
      541 ttndqrfiyd tsngalyfdq dgngsgfhqv qiaqlygvps lsvsnfvvv
//
LOCUS       WP_011321361             735 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CHASE2 domain-containing protein [Nostocaceae].
ACCESSION   WP_011321361
VERSION     WP_011321361.1
KEYWORDS    RefSeq.
SOURCE      Nostocaceae
  ORGANISM  Nostocaceae
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales.
REFERENCE   1  (residues 1 to 735)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 735)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..735
                     /organism="Nostocaceae"
                     /db_xref="taxon:1162"
     Protein         1..735
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=80743
     Region          45..649
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 miwaklkplf wqwrgvifav pnmtilvigl rltgllqlle laaldqffll rspeppdtri
       61 viveineadv rkqtqwpmsd aamatvldti kqqqpraigl diyrdlpvnp gheilvklfa
      121 stpnligvqk lsdtrdssav naspilkenn qvgsndlpld gdgkirrgll yvdvnedevl
      181 esfalklall ylkpekitek paannpdylq lnrgvfpife andggyirad arsyqillny
      241 rgriqqfttv tltqvqqkqi ppdlmrgkvv ligataeslk difytpyssn lftppermag
      301 vtihanlvsq ilsaaldsrp qiqtlpetge wllilawsii gaslcwqqrs skrqkivvav
      361 gvplmsgavi agsflafvag wwipvvpsll afggsaiavt lyiaqsagem rknlgryltd
      421 evlaniletp sglklggerr kvtllfsdlr gfsamseqls peqvvqilnl ylgvmtdvin
      481 qykgtinefi gdgifimfga picrpddsqr aiacaiamqq amqqvnaqtr qmnlpqlemg
      541 igintgevva gnigsqkraq ytvigshvnl aarietytvg gqilisantr qdaktdlqia
      601 gqmqiepkgi kepitiyeis giggaynlsl pedkdvmvkl kspvpveyqv lqgkqavgev
      661 frgelvsvse kkallhsphp veklanlklk llhepelata diyakvmkqs dadlfiirft
      721 nippqaiasl nslhq
//
LOCUS       WP_011321209             440 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: CmpA/NrtA family ABC transporter substrate-binding
            protein [Nostocaceae].
ACCESSION   WP_011321209
VERSION     WP_011321209.1
KEYWORDS    RefSeq.
SOURCE      Nostocaceae
  ORGANISM  Nostocaceae
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales.
REFERENCE   1  (residues 1 to 440)
  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 440)
  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 440)
  AUTHORS   ter Beek,J., 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 440)
  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 440)
  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 10596738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Nostocaceae"
                     /db_xref="taxon:1162"
     Protein         1..440
                     /product="CmpA/NrtA family 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=48306
     Region          58..310
                     /region_name="NMT1_2"
                     /note="NMT1-like family; pfam13379"
                     /db_xref="CDD:463863"
ORIGIN      
        1 mthvsrrkfl fttgaaaaas ilahgctsng sqsattgeqa psaapaanvs aanapkvett
       61 kaklgfiplt daapliiake kgffakygmt dvevikqksw pvtrdnlkig ssgggidgah
      121 ilspmpylmt ikdkvpmyil arlntngqai svaekykdln inlesknlkd vaakakadkk
      181 awkagitfpg gthdlwmryw laagginpdq dvvlepvppp qmvanmkvgt vdsfcvgepw
      241 naqlvnqklg ysalvtgelw kdhpekaftm rqdwvdqnpn aaqailmail eaqqwcdkae
      301 nkeemckica drkylnvaaa diverakgni dygdgrkeen fayrmkfwad nasypykshd
      361 iwfltedirw gylpkdtkvq divnqvnked lwkkaakaig vadaeipass srgvetffdg
      421 vkfdpekpee ylnslkikkv
//
LOCUS       WP_011321420             221 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: nitroreductase family protein [Nostocaceae].
ACCESSION   WP_011321420
VERSION     WP_011321420.1
KEYWORDS    RefSeq.
SOURCE      Nostocaceae
  ORGANISM  Nostocaceae
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Nostocaceae"
                     /db_xref="taxon:1162"
     Protein         1..221
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23713
     Region          15..210
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mstitqiqpl dvpsaivqrr siktfktdpi apellkqlvd ltvaapssfn iqdwriilvq
       61 deaqkaalsa aswnqkqiie apvtfvfaad ssvgegdltp vfetalatga wnegtvnyfk
      121 naipqfqagl gdkrreyaik daiiaathlv laaeslglst cfmngwiedq vkevigaadn
      181 pdlaiavlvp vgyaaeprln pgrlplsnnv svdridnpyv g
//
LOCUS       WP_011327163             431 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system HipA family toxin
            [Pseudoalteromonas].
ACCESSION   WP_011327163
VERSION     WP_011327163.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 431)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 431)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..431
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /function="5.2 : From other organisms"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47981
     Region          22..418
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mvfkpinkle vkrtlsdste llvgvlaqnr qgvyfqfdqn yldqysnlsp fslsfnrdvq
       61 lapksphngl hgvfsdclpd gwgsllqdrv frqnnimpnf vtamdrlsfv ghsamgalsf
      121 tpeanynips eeepglaelg qqaqaifdgq tetvlsalva agssggarpk aqvyfpehni
      181 eecrtqpkig ddawlikfts knlslgheeg lceavylela dkaklspper llvnapegtg
      241 akqwlalkrf drfklpsnkm grkqmhsacg lldadfrapt ldyedlikas rvlckspaag
      301 qlqfrraifn lfscnqddhs knwaflqeds gewnlapfyd vtfsphpfne hatsfagygk
      361 nppikaiqkl asaagyanwk qvqiiiseia divfsfkdta ktfevnkqti qlieqqldnt
      421 yrinkqlcgs l
//
LOCUS       WP_011327722             807 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: Lon protease family protein [Pseudoalteromonas].
ACCESSION   WP_011327722
VERSION     WP_011327722.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 807)
  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 807)
  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 807)
  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   4  (residues 1 to 807)
  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 11437488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..807
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..807
                     /product="Lon protease family protein"
                     /EC_number="3.4.21.-"
                     /function="2.2.3.1 : Degradation of proteins, peptides,
                     and glycopeptides"
                     /GO_function="GO:0004176 - ATP-dependent peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89690
     Region          69..801
                     /region_name="LonB"
                     /note="Predicted ATP-dependent protease [Posttranslational
                     modification, protein turnover, chaperones]; COG1067"
                     /db_xref="CDD:440686"
ORIGIN      
        1 mtkkllplpv sklapsists hvhtcmsnpy pehftfigqq raqsaldfsl gmdlpgynvy
       61 vmgeaahgrf tlvkdklkeh akgrvtpnew lyvnnyddhr epialfmqag qskkladdid
      121 afidevldtf paafdnpayq rkkksidref ndaydgaita veiaaleqsv alieekgvvg
      181 fapliggkql sdnefshled elretfferi ekledtliea lielprwkre steklrnlkk
      241 staeqatkpl lkdlehkyas higvlrylkd irveiidavl ewlddegese enkedfdrkg
      301 mltdffapni lvefkegdaa pvvyepnptf gnifgkveya tsqgslitsy rsiqagalhr
      361 anggylmmda ekvmanpqvw dglklslkth qikndlpyqd svvgssftlr pqlipldvki
      421 illgsrelyy tigeydeefa elfriladfd yylpssdklq yqfitkvtdy cehvlkcttt
      481 eaamvrllkf syrqaehhnk lsarfadvle lvaeasyyak qdkltvidah hideaiegkq
      541 yrtgqisenm lsdikeghtl iatqgqaigk vngltvlhig dtsfgtpari tatvyagadg
      601 vldvereael gkaihskgvm lltgylgnky aqhfsltlsa niaieqsygy idgdsaslae
      661 lcalisaits lplsqsialt gsinqhgdvq aiggvnekie gffklckmrg ltgeegviip
      721 ksnqvnlvld eeilnavelg kfniyavetv dqalnllmdl eagdlvdghy pensvnglal
      781 arlkdiadiv ngdsedekda epeeekn
//
LOCUS       WP_011329774             206 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YfgM family protein [Pseudoalteromonas].
ACCESSION   WP_011329774
VERSION     WP_011329774.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 206)
  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 206)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 206)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..206
                     /product="YfgM family protein"
                     /function="5.2 : From other organisms"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=21872
     Region          1..199
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Region          120..149
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          154..182
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdiysteeqq aeaikrffre nglslalgvi vglgglygwk aynqnqitta eqasdayttl
       61 vsgesvlssa dtfisenkdt nyatlaafva akdaveandl daaseklswi vsnvkndelk
      121 aiaitrlarv qiaqqqydea ltslnaslpd afsanvaelk gdiytkqgdk kqaraayqaa
      181 vdaggltsnp llqiklddla vtspaa
//
LOCUS       WP_011330721             123 aa            linear   BCT 20-JAN-2025
DEFINITION  PilZ domain-containing protein [Nitrosococcus oceani].
ACCESSION   WP_011330721
VERSION     WP_011330721.1
KEYWORDS    RefSeq.
SOURCE      Nitrosococcus oceani
  ORGANISM  Nitrosococcus oceani
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Nitrosococcus.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 123)
  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   3  (residues 1 to 123)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 123)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007091
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Nitrosococcus oceani"
                     /db_xref="taxon:1229"
     Protein         1..123
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13353
     Region          8..123
                     /region_name="PilZ"
                     /note="Type IV pilus assembly protein PilZ [Cell motility,
                     Extracellular structures]; COG3215"
                     /db_xref="CDD:442448"
ORIGIN      
        1 msipnqssss lpprqgilsl sikdinalyh ayipftrngg lfiptnrnyc igdevfmllt
       61 lmeevekvpv agkvvwitpr gaqsnraagi giqfndings aarnkietyl agmlksekst
      121 htm
//
LOCUS       WP_011331703             265 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: type IV toxin-antitoxin system AbiEi family antitoxin
            domain-containing protein [Rhodococcus].
ACCESSION   WP_011331703
VERSION     WP_011331703.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Hampton,H.G., Jackson,S.A., Fagerlund,R.D., Vogel,A.I.M., Dy,R.L.,
            Blower,T.R. and Fineran,P.C.
  TITLE     AbiEi Binds Cooperatively to the Type IV abiE Toxin-Antitoxin
            Operator Via a Positively-Charged Surface and Causes DNA Bending
            and Negative Autoregulation
  JOURNAL   J Mol Biol 430 (8), 1141-1156 (2018)
   PUBMED   29518409
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Dy,R.L., Przybilski,R., Semeijn,K., Salmond,G.P. and Fineran,P.C.
  TITLE     A widespread bacteriophage abortive infection system functions
            through a Type IV toxin-antitoxin mechanism
  JOURNAL   Nucleic Acids Res 42 (7), 4590-4605 (2014)
   PUBMED   24465005
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475017
            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="type IV toxin-antitoxin system AbiEi family
                     antitoxin domain-containing protein"
                     /calculated_mol_wt=28437
     Region          19..191
                     /region_name="AbiEi"
                     /note="Abortive phage infection protein AbiEi, antitoxin
                     conponent of an AbiEi-AbiEii TA system [Defense
                     mechanisms]; COG5340"
                     /db_xref="CDD:444124"
ORIGIN      
        1 mkgddrflal adlaqdqwgm ftsaqaaesg vsaqhlkrla drfiltrirh gvyrltgtpi
       61 hptdhvraqw laldptrsat erigsadprg vashrtaadl rqlgdidadi aeftvprrrn
      121 trsdgvrfhv atldpthwsl ldglpvttta rtivdlassr tdgghlagvv wdalrtdqvs
      181 rgqleselrp faylygaplg dgagliaali ddvaasdlrs aptdtrasrq eeaagevghg
      241 pgvlnilrdp alpaalralr kqgiv
//
LOCUS       WP_011332772             816 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: penicillin acylase family protein [Pseudomonas].
ACCESSION   WP_011332772
VERSION     WP_011332772.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 816)
  AUTHORS   Mukherji,R., Varshney,N.K., Panigrahi,P., Suresh,C.G. and
            Prabhune,A.
  TITLE     A new role for penicillin acylases: degradation of acyl homoserine
            lactone quorum sensing signals by Kluyvera citrophila penicillin G
            acylase
  JOURNAL   Enzyme Microb Technol 56, 1-7 (2014)
   PUBMED   24564895
REFERENCE   2  (residues 1 to 816)
  AUTHORS   Verhaert,R.M., Riemens,A.M., van der Laan,J.M., van Duin,J. and
            Quax,W.J.
  TITLE     Molecular cloning and analysis of the gene encoding the
            thermostable penicillin G acylase from Alcaligenes faecalis
  JOURNAL   Appl Environ Microbiol 63 (9), 3412-3418 (1997)
   PUBMED   9292993
REFERENCE   3  (residues 1 to 816)
  AUTHORS   Duggleby,H.J., Tolley,S.P., Hill,C.P., Dodson,E.J., Dodson,G. and
            Moody,P.C.
  TITLE     Penicillin acylase has a single-amino-acid catalytic centre
  JOURNAL   Nature 373 (6511), 264-268 (1995)
   PUBMED   7816145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457167
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..816
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..816
                     /product="penicillin acylase family protein"
                     /EC_number="3.5.1.-"
                     /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=88895
     Region          12..816
                     /region_name="PvdQ"
                     /note="Acyl-homoserine lactone (AHL) acylase PvdQ
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2366"
                     /db_xref="CDD:441933"
ORIGIN      
        1 maspalshfl prfgvaaava gvlsltgcqt wnaqdtlppt sgvqplkgla qnvsvrrnam
       61 gmpliesnsf hdalfalgyv hasdrinqmv tlrllaqgrl aemsgssmld adrymravnl
      121 kksagelyka ssprlkrffe vyargvnayl fryadklpgd lassgykpey wkpedsalif
      181 cllnfsqsan lpeeiaslvl aqtvtndkla wltpsapden lplaeadklq giklngqipg
      241 ltelsnaseq laalnllgtq ssnnwaiapq rsrsgkslla sdshgplaap slwsfvqira
      301 pkyqaagvtv aglpmvlggf ngkvawslts vlgdnqdlfl ekirrqgssl tyevngkwqp
      361 vavrnetyfv kgqrpireav yetrhgalln stqaaaqgtg fglalqtpsf tddksldaff
      421 dlsraqnver asdatreira ialnlvfada snigwqvtgr fpnrregegl lpspgwegry
      481 dwdgyadpml hpydqdpaqg wlgtanqrvi phgygmqlsn swaaperger laelagsgkh
      541 dsrsviamqy dqtttfaakl kkmfeapgma qplkqaidal peaerskare aytrlmafdg
      601 klsptsadaa iyelflqesm kqifldelgp qnspawkafi angdlsyaaq adhllgreds
      661 pfwddartpq kedkpailar slaaaisagd sqlggdrraw qwgklhryew knangqsvrg
      721 piaaggdhtt lntaafawgq dfnttrapsm rfivdfgqse plmgqngtgq sgnpvspnyl
      781 ngidpwlkgq yiglpmqpqn fdrvygktrl tltpgk
//
LOCUS       WP_011334549             343 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_011334549
VERSION     WP_011334549.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 343)
  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 343)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 343)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 343)
  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   5  (residues 1 to 343)
  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   6  (residues 1 to 343)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..343
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38288
     Region          31..211
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          138..339
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mnvkvqdptf elalvspfll qtlaevaank gvepqslcrg lgfdfddlqd paqrisyrqa
       61 vamiqralka lpnqglglwv gaqnvlgtlg llghvlslck tlrdafeigv rhqhtsggiv
      121 vssvdvvgdq vyvdvecrlp faevqvfave effasllvyg ralvgetfkp iavefmhaap
      181 dyldeyrrll gpevrfgclh nrmlidvqwl dvnlpnhhsl alrqavklle leaaqvhqkl
      241 dliqaverai ardlsrgshi ekiaadlnms srtlrrrlte hsltfealle qvrqartmsl
      301 lanpdmpier iteevgysdv rsfrrafkrw tgkspsawrs asi
//
LOCUS       WP_011334749             237 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: murein L,D-transpeptidase catalytic domain family
            protein [Pseudomonas].
ACCESSION   WP_011334749
VERSION     WP_011334749.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 237)
  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 10614777
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..237
                     /product="murein L,D-transpeptidase catalytic domain
                     family protein"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=26126
     Region          41..208
                     /region_name="YkuD_2"
                     /note="L,D-transpeptidase catalytic domain; pfam13645"
                     /db_xref="CDD:463944"
ORIGIN      
        1 mltflrrlll tatalgvlts pafaagtssp vlytslahaa pelnpqalkg alnamqcain
       61 ngakqsrhla iidysqpste rrlwifdltr kklvlrdlva hgsnsgenfa trfsnregsf
      121 qsslglfrtq esyqgthgys lrmdglepgi ndmardraiv ihaadyvnpf wskrtgrlgr
      181 sqgcpavrpq vakrvidslk ngqfmfswyp dqqwlksspy lncqpqqias ilsthas
//
LOCUS       WP_011335426             291 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Pseudomonas
            fluorescens].
ACCESSION   WP_011335426
VERSION     WP_011335426.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas fluorescens
  ORGANISM  Pseudomonas fluorescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Pseudomonas fluorescens"
                     /db_xref="taxon:294"
     Protein         1..291
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31794
     Region          13..262
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mtwtavtehr aqlgegpfwd altqalywvd iagrqalrli gqnvqiwqmp ehvsafipca
       61 sgdalvtlss gvyrldldsp gleprltlfc iadpqpgnra nearcdgqgr lwlgtmqnni
      121 geqgedlpii rrsgglfrid pdkrvtpllr glgipntllw sddgttllfg dsldstlyry
      181 fihtdgnldt aqpwysadqh ggpdgsamda egyvwnarwd gscllrltpd gqidrrielp
      241 isrptscvfg gtdlktlyit saksplnhpl dgavlslqvd vagklctrfa g
//
LOCUS       WP_011334282             338 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Pseudomonas fluorescens].
ACCESSION   WP_011334282
VERSION     WP_011334282.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas fluorescens
  ORGANISM  Pseudomonas fluorescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 338)
  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   5  (residues 1 to 338)
  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   6  (residues 1 to 338)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Pseudomonas fluorescens"
                     /db_xref="taxon:294"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38003
     Region          23..204
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          103..330
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msekdtiaiq lvreallqsc apgvateevl skvgidpall stddarvpas qyarlwrlla
       61 rrgddeffgm dprklksgsl eflcrsamaq pnlaaglssg lnflslmler lpaqlvhqqs
      121 laeivlledd peprraftyf tywmivhgva cwlagrripi laielrcpap dfcddyrvmf
      181 senlrfdrpr trmifaadvl dlpikrsaee lkrflahapa nilvkyrdpd slasrikqdl
      241 rqlsadhwpe tdalaqqlcm sastlrrrla eegqtyqglk dsvrkelait wlaepsisfa
      301 eiatrlgfad assfykafrk wsgtnpghyr slilneav
//
LOCUS       WP_011335691             309 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Pseudomonas].
ACCESSION   WP_011335691
VERSION     WP_011335691.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 309)
  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 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   3  (residues 1 to 309)
  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   4  (residues 1 to 309)
  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 309)
  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 12071874
            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="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34439
     Region          39..191
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          219..298
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtsfdrfqgp pdadmekqra elaaiirrnt sedgsyatav gslfmsrhtq shdfapvlaq
       61 palcimaqgr kevrladeff nydplnylvv svsmplsgrv vnvspeepil avrldidpae
      121 italiadagp mgvptrptgr glyvekidsa mldavlrlar lldapkdiam laplirreil
      181 yrllrspqgh rlyeiaians qshrisqaik wlngnfeqpl riddlakevn lsvstlhhrf
      241 kamtamsplq yqkqlrlqea rrlmlaegle asaagyrvgy espsqfsrey srlfgapplr
      301 dlarlrlsv
//
LOCUS       WP_011320551             458 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ATP-grasp domain-containing protein [Nostocaceae].
ACCESSION   WP_011320551
VERSION     WP_011320551.1
KEYWORDS    RefSeq.
SOURCE      Nostocaceae
  ORGANISM  Nostocaceae
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Ogasawara,Y. and Dairi,T.
  TITLE     Biosynthesis of Oligopeptides Using ATP-Grasp Enzymes
  JOURNAL   Chemistry 23 (45), 10714-10724 (2017)
   PUBMED   28488371
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Fawaz,M.V., Topper,M.E. and Firestine,S.M.
  TITLE     The ATP-grasp enzymes
  JOURNAL   Bioorg Chem 39 (5-6), 185-191 (2011)
   PUBMED   21920581
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Galperin,M.Y. and Koonin,E.V.
  TITLE     A diverse superfamily of enzymes with ATP-dependent
            carboxylate-amine/thiol ligase activity
  JOURNAL   Protein Sci 6 (12), 2639-2643 (1997)
   PUBMED   9416615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10792831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Nostocaceae"
                     /db_xref="taxon:1162"
     Protein         1..458
                     /product="ATP-grasp domain-containing protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=51731
     Region          60..455
                     /region_name="PRK06849"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:235876"
ORIGIN      
        1 maqslplssa patpslpsqt kiaaiiqnic tlallllalp inativfisl lvfrpqkvka
       61 anpqtilisg gkmtkalqla rsfhaaghrv vlvethkywl tghrfsqavd kfytvpapqd
      121 npqayiqalv divkqenidv yipvtspvgs yydslakpel shycevfhfd aditqmlddk
      181 faltqkarsl glsvpksfki tspeqvinfd fsgetrkyil ksipydsvrr ldltklpcat
      241 peetaafvrs lpitpekpwi mqefipgkef cthstvrnge lrlhcccess afqvnyenvn
      301 npqitewvqh fvkelkltgq isfdfiqaed gtvyaiecnp rthsaittfy dhpqvaeayl
      361 sqapttetiq plttskptyw tyhevwrltg irsftqlqrw lgniwrgtda iyqpddplpf
      421 lmvhhwqipl lllnnlrrlk gwtridfnig klvelggd
//
LOCUS       WP_011336852             654 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Cereibacter sphaeroides].
ACCESSION   WP_011336852
VERSION     WP_011336852.1
KEYWORDS    RefSeq.
SOURCE      Cereibacter sphaeroides
  ORGANISM  Cereibacter sphaeroides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Cereibacter.
REFERENCE   1  (residues 1 to 654)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 654)
  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   3  (residues 1 to 654)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..654
                     /organism="Cereibacter sphaeroides"
                     /db_xref="taxon:1063"
     Protein         1..654
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /function="Essential for chemotaxis and phototaxis in
                     strain WS8N. Autophosphorylates and phosphotransfers to
                     CheY1, CheY2, CheY3, CheY4, CheY5, CheY6, CheB1 and
                     CheB2."
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=69268
     Region          1..652
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mmdddmmavf rqeatdlies lerglldlsd spedrdlina vfrdlhtikg sgamfgfadm
       61 aafvhafesa fdllrsgkav vtpeiirlal sardeiigfl adepdpdgrr pailsaleaa
      121 vggsgvatap avaaaaappa drlwfrltgn alalgarpdl llaelrelga tdiradlsav
      181 ppldaldpev cmigwsmsfp nrvtreaidn vflfnevelr leaapatapa aapvpaapvs
      241 aaaappppaa prkaadeatg adkagatmrv aaerldhlmd rvgelviada rllqlaqqsr
      301 dpalmaaaee isrlaaglrd ttmrirmvpv rsmvgrfrrl ihglsemvgk pvsfvvlgee
      361 teldktvieq ladpivhmlr nsvdhgleap adraaagkpa egritleaeq sgaevviris
      421 ddgrglnrdr irakavangi igpdailtes amnalilepg fstaeaitei sgrgvgmdvv
      481 kktieglrgs ievqsvegrg ttftlrlplt laiiegllve vagerfsipl aavqeivelp
      541 pdrreedgsa dfldvrdrlv plvrlrrifs spgtpdefqt vvivragetr agavvdriig
      601 tnqivikqms rlhsgirafs gatilgdgtv alildvphla gvgqgvedrr gaaa
//
LOCUS       WP_011337488             686 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Cereibacter sphaeroides].
ACCESSION   WP_011337488
VERSION     WP_011337488.1
KEYWORDS    RefSeq.
SOURCE      Cereibacter sphaeroides
  ORGANISM  Cereibacter sphaeroides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Cereibacter.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 686)
  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   3  (residues 1 to 686)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Cereibacter sphaeroides"
                     /db_xref="taxon:1063"
     Protein         1..686
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /function="Autophosphorylates and phosphotransfers to
                     CheY1, CheY2 and CheY5 (from WS8N)"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=74096
     Region          1..667
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdqsdirsaf fvecedlmea lnegldried mlddghddet vnavfravhs ikggagafkl
       61 dalvrfahqf ettldalrag rvsadpplla llhkaadrls dllqaartgs etatidpddl
      121 vaqlaqaage eeageadaed lgfvpmpldl dlpaaapdeg qsgcysidfs ptralyacgn
      181 dtsilfrvls dlgrmevrld rsrlpdfdal dwqeswldwh ltletdepeh qidevfefve
      241 dlcrleirpm ameaprtdpd pepdpepdpp asgpaaakks paedhrtssp ratvrveldr
      301 vdrlinivge lvinqamlsq cvqdegvppr spvrnrlddf rnlareiqes vmairaqaik
      361 plfqrmsria reaseiaqkq irlvtegest evdktvierl adplthmirn avdhgiepad
      421 rrlhlgkppv glitltaahr sgrvlieikd dggginrprv leiargkglv apdaqlteee
      481 idgllfmpgf stasvvsdls grgvgmdvvk saieslggri tiasdpgvgt tftislpltl
      541 avldgmvvdv ggqtmvvpva aivetlrprp adihilgsgd qvvairgslv pivdcgsifg
      601 frapvrsyee svlllvetar qklcalvvdt ihdqrqvvik glengygrip gvaaatilgd
      661 grialiiape eavdigtsgg tfsmef
//
LOCUS       WP_011337954             399 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Cereibacter sphaeroides].
ACCESSION   WP_011337954
VERSION     WP_011337954.1
KEYWORDS    RefSeq.
SOURCE      Cereibacter sphaeroides
  ORGANISM  Cereibacter sphaeroides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Cereibacter.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 399)
  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   3  (residues 1 to 399)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Cereibacter sphaeroides"
                     /db_xref="taxon:1063"
     Protein         1..399
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /function="Essential for chemotaxis and phototaxis in
                     strain WS8N"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42526
     Region          <2..399
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msapveagpd ggllrvssek igrlmdlvge lslsvaetvh spdleglelp afdgavhrlr
       61 mivrevqdaa telrlvpvee vfkrlrrmvr elerqtgkki emvfegaeta idklvadqly
      121 dpllhvvrns adhgleppee rraagkpetg rivlaaaqag sevrisvsdd grglsrpkil
      181 krarerglfg pdeepepatl wkvifepgfs taeavtnlsg rgvgmdvlna tmtalrgrig
      241 vdsrdgqgse vslhipvsla fldciilrlg arlyalpida vseivqpkpc dlmgvgaagg
      301 semlrlrghw ipvcrlerfy geapsavppp agqvlavvst atglialpvd evldrqqvvm
      361 kpltgrlaqv raswgcallg tgevalvldg nrlaaggaa
//
LOCUS       WP_011338645             407 aa            linear   BCT 20-JAN-2025
DEFINITION  ROK family transcriptional regulator [Cereibacter sphaeroides].
ACCESSION   WP_011338645
VERSION     WP_011338645.1
KEYWORDS    RefSeq.
SOURCE      Cereibacter sphaeroides
  ORGANISM  Cereibacter sphaeroides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Cereibacter.
REFERENCE   1  (residues 1 to 407)
  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 407)
  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
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 407)
  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   5  (residues 1 to 407)
  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   6  (residues 1 to 407)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Titgemeyer,F., Reizer,J., Reizer,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationships between sugar kinases and
            transcriptional repressors in bacteria
  JOURNAL   Microbiology (Reading) 140 (Pt 9), 2349-2354 (1994)
   PUBMED   7952186
REFERENCE   8  (residues 1 to 407)
  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 18624027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Cereibacter sphaeroides"
                     /db_xref="taxon:1063"
     Protein         1..407
                     /product="ROK 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:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43447
     Region          29..>75
                     /region_name="COG2512"
                     /note="Predicted transcriptional regulator, contains CW
                     (cell wall-binding) repeats and an HTH domain [General
                     function prediction only]"
                     /db_xref="CDD:442002"
     Region          94..379
                     /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 mrqgqetaer sggaepglrg snqsgmrahn erlvlslvrr egalaksdia rmtglsaqtv
       61 svimrelerd gllrrgepir grigqpsvpm slapegayfl glkigrrsae lvlidflgrp
      121 vasrrrlypy ptpdavvaft aetlprlmes lspesrtrvg glgiampfql wnwvsyvgap
      181 qaemdawrtr diqselaalt glpvhvrnda taacgaelvf gsgarpkdfl yfyfayfigg
      241 glvlnghlfa grtgnaagvg pmpvpgrdgq mrrllnvasm svlaealeqa gepsaalwed
      301 pgrwevsgpi leewlegaaa glasailsaa alvemetvvi dgwmppaira divrrthaal
      361 hrldlsgiep pliregtvga qaralgaaai plsqrylvea mgagqes
//
LOCUS       WP_011338726             280 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Cereibacter sphaeroides].
ACCESSION   WP_011338726
VERSION     WP_011338726.1
KEYWORDS    RefSeq.
SOURCE      Cereibacter sphaeroides
  ORGANISM  Cereibacter sphaeroides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Cereibacter.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Cereibacter sphaeroides"
                     /db_xref="taxon:1063"
     Protein         1..280
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26927
     Region          <1..195
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 matipggafs dfifgtsgnd yvlsgagndt vsgasgddli rgglgddlln ggsgadrlfg
       61 eegddqllgg tgddmldggi gndtlsggag qdllfggagd dllaggagdd tmeggsgnda
      121 llggagndal dggegddtls gdagddllsg glgddrldgg dgndvlsggg gddlflggag
      181 ddqidggagd dviytgegnd lvtfsgggdv imdfsegdml qisgslegvt lasaedvagy
      241 aldlgdagtl idfgqgdsvl lqgvsyddva adpsryfsiv
//
LOCUS       WP_011339920              74 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Syntrophotalea carbinolica].
ACCESSION   WP_011339920
VERSION     WP_011339920.1
KEYWORDS    RefSeq.
SOURCE      Syntrophotalea carbinolica
  ORGANISM  Syntrophotalea carbinolica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Desulfuromonadales; Syntrophotaleaceae;
            Syntrophotalea.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 74)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 74)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 74)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Syntrophotalea carbinolica"
                     /db_xref="taxon:19"
     Protein         1..74
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=7951
     Region          2..74
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mtifvklfag frenrfkvak revkddctia dvleqlgike pelgvalidg rhvtsdqvlh
       61 agvtislfpk vggg
//
LOCUS       WP_011341157             197 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Syntrophotalea carbinolica].
ACCESSION   WP_011341157
VERSION     WP_011341157.1
KEYWORDS    RefSeq.
SOURCE      Syntrophotalea carbinolica
  ORGANISM  Syntrophotalea carbinolica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Desulfuromonadales; Syntrophotaleaceae;
            Syntrophotalea.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Syntrophotalea carbinolica"
                     /db_xref="taxon:19"
     Protein         1..197
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22175
     Region          3..167
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 mklirrlydw vlrwadtsyg mpalfllafa essffpippd vllmalalgk prasyrfaai
       61 asvgsilgga lgyaiglgfw dvlgdffysy vpmfseqgfi evqrlfetyd fwvvftagft
      121 pipykiitig agvfhinfam fmvasllsrs lrfflisglv fhfgetvrif iekyfnyltf
      181 avmilgiggf vfvshft
//
LOCUS       WP_011341843             187 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Syntrophotalea
            carbinolica].
ACCESSION   WP_011341843
VERSION     WP_011341843.1
KEYWORDS    RefSeq.
SOURCE      Syntrophotalea carbinolica
  ORGANISM  Syntrophotalea carbinolica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Desulfuromonadales; Syntrophotaleaceae;
            Syntrophotalea.
REFERENCE   1  (residues 1 to 187)
  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 187)
  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   3  (residues 1 to 187)
  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   4  (residues 1 to 187)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 187)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 187)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Syntrophotalea carbinolica"
                     /db_xref="taxon:19"
     Protein         1..187
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21023
     Region          1..187
                     /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"
ORIGIN      
        1 mksvlvvddk peirrrvaea likygftdil eaengqqaid maqahkplli lmdyvmpvmd
       61 gitaaekisk kcptpivllt tradhetiek arlagisnyv vepfredqlf pavdlaihhf
      121 ievtslrqev aklkdtlesr kiiekakgal iqqgmseqda yrkiqrmamn krktlkevae
      181 ailltle
//
LOCUS       WP_011342805             364 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Syntrophotalea
            carbinolica].
ACCESSION   WP_011342805
VERSION     WP_011342805.1
KEYWORDS    RefSeq.
SOURCE      Syntrophotalea carbinolica
  ORGANISM  Syntrophotalea carbinolica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Desulfuromonadales; Syntrophotaleaceae;
            Syntrophotalea.
REFERENCE   1  (residues 1 to 364)
  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 364)
  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 364)
  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 364)
  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 10772470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Syntrophotalea carbinolica"
                     /db_xref="taxon:19"
     Protein         1..364
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=40504
     Region          84..364
                     /region_name="DctP"
                     /note="TRAP-type C4-dicarboxylate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1638"
                     /db_xref="CDD:441245"
ORIGIN      
        1 mkktvmmavl ilsvvfcglt gcqkeqdpsq qepsapekaa aakkdplvgw qpqfdpssaq
       61 ytyllsnldh ptiegvavgy hirdkvwers ggrlyvdyrp lsqlgqekgv lsklklgavq
      121 gvlcssvaaa nisdtlgivn lpfvidsadk leqfrndpel fdefrnsalr qglmvvdits
      181 ygsygwatnt pvrtlaearq vnfriaqapv ntdfyrawgm kftvmpwgdv pqalqtgvid
      241 gldhtptvcn ithkfevary ftrvdyaqgl fihlmnkawl erlpedlrri lleviaeesa
      301 aarqrarvqq qeqiaaaeav gvqffelaae draelirlse pvyatwgaki gaeylakvrq
      361 rlar
//
LOCUS       WP_011343935             215 aa            linear   BCT 20-JAN-2025
DEFINITION  flagellar brake protein [Carboxydothermus hydrogenoformans].
ACCESSION   WP_011343935
VERSION     WP_011343935.1
KEYWORDS    RefSeq.
SOURCE      Carboxydothermus hydrogenoformans
  ORGANISM  Carboxydothermus hydrogenoformans
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Carboxydothermus.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Galperin,M.Y. and Chou,S.H.
  TITLE     Structural Conservation and Diversity of PilZ-Related Domains
  JOURNAL   J Bacteriol 202 (4), e00664-19 (2020)
   PUBMED   31740493
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 215)
  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   3  (residues 1 to 215)
  AUTHORS   Benach,J., Swaminathan,S.S., Tamayo,R., Handelman,S.K.,
            Folta-Stogniew,E., Ramos,J.E., Forouhar,F., Neely,H.,
            Seetharaman,J., Camilli,A. and Hunt,J.F.
  TITLE     The structural basis of cyclic diguanylate signal transduction by
            PilZ domains
  JOURNAL   EMBO J 26 (24), 5153-5166 (2007)
   PUBMED   18034161
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Ryjenkov,D.A., Simm,R., Romling,U. and Gomelsky,M.
  TITLE     The PilZ domain is a receptor for the second messenger c-di-GMP:
            the PilZ domain protein YcgR controls motility in enterobacteria
  JOURNAL   J Biol Chem 281 (41), 30310-30314 (2006)
   PUBMED   16920715
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Carboxydothermus hydrogenoformans"
                     /db_xref="taxon:129958"
     Protein         1..215
                     /product="flagellar brake protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25190
     Region          8..210
                     /region_name="YcgR"
                     /note="Cyclic di-GMP-binding flagellar brake protein
                     FlgZ/YcgR, contains PilZNR(YcgR) and PilZ domains [Cell
                     motility]; COG5581"
                     /db_xref="CDD:444320"
ORIGIN      
        1 mlqeflklel ypnpavkksf paqvqevkek tflilgpfdr gtllflypaq evlieyvaee
       61 cryqfstrvv rrlqkpffgy elllpapdei qriqlrryvr vkkvldvfya lvkkdeelnw
      121 kkgksvdisi ggiklatnep lsvdacvklr fyielkgnvv efvldglvkr eekkenhvyh
      181 ygiefvnisr qeqdtlfayl fqemqksrrm ladgk
//
LOCUS       WP_011344166             385 aa            linear   BCT 20-JAN-2025
DEFINITION  UxaA family hydrolase [Carboxydothermus hydrogenoformans].
ACCESSION   WP_011344166
VERSION     WP_011344166.1
KEYWORDS    RefSeq.
SOURCE      Carboxydothermus hydrogenoformans
  ORGANISM  Carboxydothermus hydrogenoformans
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Carboxydothermus.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Iyer,L.M. and Aravind,L.
  TITLE     The emergence of catalytic and structural diversity within the
            beta-clip fold
  JOURNAL   Proteins 55 (4), 977-991 (2004)
   PUBMED   15146494
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Hubbard,B.K., Koch,M., Palmer,D.R., Babbitt,P.C. and Gerlt,J.A.
  TITLE     Evolution of enzymatic activities in the enolase superfamily:
            characterization of the (D)-glucarate/galactarate catabolic pathway
            in Escherichia coli
  JOURNAL   Biochemistry 37 (41), 14369-14375 (1998)
   PUBMED   9772162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Carboxydothermus hydrogenoformans"
                     /db_xref="taxon:129958"
     Protein         1..385
                     /product="UxaA family hydrolase"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=40615
     Region          <1..381
                     /region_name="UxaA"
                     /note="Altronate dehydratase [Carbohydrate transport and
                     metabolism]; COG2721"
                     /db_xref="CDD:442034"
ORIGIN      
        1 mkikgfvrpd gkvgirnhvl iipssvcase vamriashvn gavalanqhg ccqigadlel
       61 vtktliglgk npnvaavlvv glgcegvpte kvadeisktg kkveyiiiqd cggtlkaeei
      121 gtrlarqmaq evsllkreev ditnlilave cggsdttsgl asnpvagyvs dklielggts
      181 mfsetteiig aehllakrav skevaqklle ivrrceekak tmgvdmrggq ptpgnieggi
      241 stieekslgc iykggtkpvq gvleyaeapt gkglyimdtp gqdiesitgm taggaqlvif
      301 ttgrgtptgs piapvikita npdtfkkmed nidfnagtii lgdetireag erlfsemiev
      361 cngkltkaea lkhrefgiyk listf
//
LOCUS       WP_011345402              99 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Carboxydothermus
            hydrogenoformans].
ACCESSION   WP_011345402
VERSION     WP_011345402.1
KEYWORDS    RefSeq.
SOURCE      Carboxydothermus hydrogenoformans
  ORGANISM  Carboxydothermus hydrogenoformans
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Carboxydothermus.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Carboxydothermus hydrogenoformans"
                     /db_xref="taxon:129958"
     Protein         1..99
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11261
     Region          3..96
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 medknfilnk llenknllkt ynvskiglfg sfvrneasqt sdidllidfd epvtifqfve
       61 lknaleelfk rkvdlgtfda ikpvimenil reaiiiegl
//
LOCUS       WP_011347003             191 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Xanthomonas].
ACCESSION   WP_011347003
VERSION     WP_011347003.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..191
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=21668
     Region          23..186
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 msdavlpspp ityaplsyes rlarraltqi dmvvihctel pdmamareyg ervlydsgtg
       61 nsghyyldrn gsiqqyvale rvahhvrghn phtlgielvn rgryphwlds ryqqmtepyp
      121 eaqiaalitl lqwlqqqlps vrriaghqal dttqeaandd parkirrkld pgplfpwpri
      181 eaavswshtp r
//
LOCUS       WP_011347258             552 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheA [Xanthomonas].
ACCESSION   WP_011347258
VERSION     WP_011347258.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 552)
  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   3  (residues 1 to 552)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..552
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=59255
     Region          6..547
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msavpddiaa dfiveaqeil drlgeqlvsl eqapeeadql navfrgfhtl kggagflaik
       61 pmvelchaae etlgmarsgq avlqahhfda aqqsldylqa mldamgsgea vphapatlia
      121 qfdaksappa vkaapqaaaa kpvaaahgdd ahapapkaag kgaaktgaea eqtvrvdtkr
      181 ldaivnlige lvlsrnrlkt lrtrlrdeel dravstldia tarlqtavmr trmqpvskvf
      241 arfpkvardv artlskevel eligaeteld rnlvealadp lvhlvrnaid hgiespalre
      301 atgkprsghv rlsaqqegdy vsieiqddga gidperlrei arnkglidae aaarlstdec
      361 lhlifmpgfs tkvevtdisg rgvgmdvvqs rirelsgqiq iqselgrgsr fmirvpltla
      421 ilptllvqag eavyalplar vvevlhapqt slgwfdgrav ldrrshtlpl idlrrwlgvp
      481 aeqpplltvv llqagetrfg lvvdqvrgre evvikplpra lrglpgyaga tligdgrmal
      541 ildvdglrss dh
//
LOCUS       WP_011348339             142 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: pilin [Xanthomonas].
ACCESSION   WP_011348339
VERSION     WP_011348339.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            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 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..142
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14212
     Region          2..141
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mkkqngftli elmivvaiia ilaaialpay qdytvrgrvs eamvaasaak tvvaenaang
       61 salnsgwtap tatnnvasva vaaatgnitv tttdkagggt iifaptanga altsgtvptd
      121 riswdckggt lvakyrpaec rt
//
LOCUS       WP_011347919             135 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Xanthomonas euvesicatoria].
ACCESSION   WP_011347919
VERSION     WP_011347919.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas euvesicatoria
  ORGANISM  Xanthomonas euvesicatoria
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Xanthomonas euvesicatoria"
                     /db_xref="taxon:456327"
     Protein         1..135
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=14473
     Region          8..135
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mtrtvaqmrg ftlielmivv avvailsaia ypsytehvrk srraqakvdl veygqlaerf
       61 htvqntyigf slpstvspre ggtaayslal sqqtqsgyvi tatpgaaqva dkcgtlsidq
      121 asrktnskgl qsdcw
//
LOCUS       WP_011349343             339 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia lata].
ACCESSION   WP_011349343
VERSION     WP_011349343.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia lata
  ORGANISM  Burkholderia lata
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 339)
  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 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 339)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 339)
  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   5  (residues 1 to 339)
  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   6  (residues 1 to 339)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia lata"
                     /db_xref="taxon:482957"
     Protein         1..339
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37149
     Region          22..197
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          88..331
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mgpqmispdf vddalaclrr qglptepvlr taglpaavre pvtpqqygrl wlaiagaldd
       61 effglaarpm rhgsftllch avlhagtlek alrralqflr vvldephgel vvadgqaqiv
      121 ltqtgapypa fayrtfwlil lgvacwligr riplqridfa cpspdqrsdy hqffgvpvhf
      181 drpdsrlafn aaylalptir seqalktflr gapgnllvry rhdtgwvakt raqlktlpaa
      241 ewpdfdtlav rlgttpatlr rrlrsegqsf aaikdelrga laqsllrgda lsvaeiaael
      301 gftepsafhr afrkwtgtsp gafrrdvhaa egepgvasg
//
LOCUS       WP_011350790             198 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Burkholderia lata].
ACCESSION   WP_011350790
VERSION     WP_011350790.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia lata
  ORGANISM  Burkholderia lata
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia lata"
                     /db_xref="taxon:482957"
     Protein         1..198
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21107
     Region          8..193
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 maspsapprr livaitgatg aiygvrlldl lraaggveth llisnagwln iqhelklska
       61 dvenradvvh svrdvgatia sgsfatggmv iapcsmktla svahglsdnl itraadvtlk
      121 errrlvlmvr etpfnlahlr nmtavtemgg ivfpplpafy ampktieelv dqtvtrvldl
      181 falnaplttp wagirhvq
//
LOCUS       WP_011350533             379 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Burkholderia].
ACCESSION   WP_011350533
VERSION     WP_011350533.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 379)
  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 379)
  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   3  (residues 1 to 379)
  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   4  (residues 1 to 379)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 379)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 379)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 379)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..379
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40064
     Region          29..365
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(105..107,127..128,177,229,253)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mqhtmkklag atfvavmsla gtahaddvki gyagpmtgaq ahygkdmqng ivlaiedfna
       61 tnpkiggkpv kfaldtqddq adprtgttva qklvddgikg mlghfnsgtt ipasriyana
      121 gipqiamata peytqqgykt tfrmmtsdtq qgsvagtfas kdlgmkkiai vddrtaygqg
      181 ladqfekaak aggasivdre ftndkavdfk ailtklkaqk pdlvyyggad sqaapmvkqm
      241 ktlgitaplm sgemvktptf lkiagnaadg tiaslaglpl eempggktya dkykkrfged
      301 vqtyspyayd gamalfnamk kadstdpaky lpllaktdma gvtsthvayd akgdlknggi
      361 tmykvekgew kplksiggk
//
LOCUS       WP_011344606              77 aa            linear   BCT 20-JAN-2025
DEFINITION  MoaD/ThiS family protein [Carboxydothermus hydrogenoformans].
ACCESSION   WP_011344606
VERSION     WP_011344606.1
KEYWORDS    RefSeq.
SOURCE      Carboxydothermus hydrogenoformans
  ORGANISM  Carboxydothermus hydrogenoformans
            Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
            Thermoanaerobacteraceae; Carboxydothermus.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Xu,X., Wang,T., Niu,Y., Liang,K. and Yang,Y.
  TITLE     The ubiquitin-like modification by ThiS and ThiF in Escherichia
            coli
  JOURNAL   Int J Biol Macromol 141, 351-357 (2019)
   PUBMED   31442507
REFERENCE   2  (residues 1 to 77)
  AUTHORS   Vierstra,R.D.
  TITLE     The expanding universe of ubiquitin and ubiquitin-like modifiers
  JOURNAL   Plant Physiol 160 (1), 2-14 (2012)
   PUBMED   22693286
REFERENCE   3  (residues 1 to 77)
  AUTHORS   Burroughs,A.M., Iyer,L.M. and Aravind,L.
  TITLE     The natural history of ubiquitin and ubiquitin-related domains
  JOURNAL   Front Biosci (Landmark Ed) 17 (4), 1433-1460 (2012)
   PUBMED   22201813
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 77)
  AUTHORS   Hochstrasser,M.
  TITLE     Origin and function of ubiquitin-like proteins
  JOURNAL   Nature 458 (7237), 422-429 (2009)
   PUBMED   19325621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Carboxydothermus hydrogenoformans"
                     /db_xref="taxon:129958"
     Protein         1..77
                     /product="MoaD/ThiS family protein"
                     /calculated_mol_wt=8656
     Region          2..77
                     /region_name="MoaD"
                     /note="Molybdopterin synthase sulfur carrier subunit MoaD
                     [Coenzyme transport and metabolism]; COG1977"
                     /db_xref="CDD:441580"
ORIGIN      
        1 mqvkvkllgi lsftypafsk fryveiekge tvrdlqerlg lsvnevhfis vngkmveedy
       61 vlsdkdevif fpnvsgg
//
LOCUS       WP_011349851             565 aa            linear   BCT 20-JAN-2025
DEFINITION  M4 family metallopeptidase [Burkholderia lata].
ACCESSION   WP_011349851
VERSION     WP_011349851.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia lata
  ORGANISM  Burkholderia lata
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Adekoya,O.A. and Sylte,I.
  TITLE     The thermolysin family (M4) of enzymes: therapeutic and
            biotechnological potential
  JOURNAL   Chem Biol Drug Des 73 (1), 7-16 (2009)
   PUBMED   19152630
REFERENCE   2  (residues 1 to 565)
  AUTHORS   Khan,M.T. and Sylte,I.
  TITLE     Determinants for psychrophilic and thermophilic features of
            metallopeptidases of the M4 family
  JOURNAL   In Silico Biol 9 (3), 105-124 (2009)
   PUBMED   19795569
REFERENCE   3  (residues 1 to 565)
  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 565)
  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 11461404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Burkholderia lata"
                     /db_xref="taxon:482957"
     Protein         1..565
                     /product="M4 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=59719
     Region          1..565
                     /region_name="LasB"
                     /note="Zn-dependent metalloprotease (Neutral protease B)
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3227"
                     /db_xref="CDD:442460"
ORIGIN      
        1 mkklsrllsi saitvaslsa faqagdpsat vdkalqliqq npsafslavg gaartlkfag
       61 pqasapadgd qfqvrdvivd pdgtehvrfd rfyaglpvig gdvvvhsskg qlkqasvtql
      121 apinlagnig kvgdrsvirn apdvgaarvk riaaarfnsd vrrvddaelv vfardvtptl
      181 ayavrvygka tdahgdavly yvdarngtvl daqdliktaa atgtgrslyy gnltlttdqt
      241 gtnayrmldp srgsgsvydg rgltsddveq atdlpiftss tnvwgnnttt drqtvaadid
      301 yglaltwdyy ktmhnrngif ndgrgvksya hvvfntgsgt tganaawlns hvmvygdgqp
      361 gtslpkpvvs vdvaghemsh gvteatanln ysgdagglne stsdifgtlv kyyannpndp
      421 gnyvigarvv sgglrkmykq dldgrsfscy psggfswsnp rhdphftsgv gnrlfyllae
      481 gptvpstdtg ltkaqlvcng dttfsgvgre kagkiwyrtl tvylnanssy pnarrasiqa
      541 andlygansa estavaraws avgvn
//
LOCUS       WP_011352143             329 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Burkholderia lata].
ACCESSION   WP_011352143
VERSION     WP_011352143.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia lata
  ORGANISM  Burkholderia lata
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 329)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Burkholderia lata"
                     /db_xref="taxon:482957"
     Protein         1..329
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35555
     Region          2..329
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 migvssiawa fpetmltaqa ygsrvgltee qvlaktgirr rfllerdqce lplardafak
       61 lqaqtgfgdg didllvyvtq npgrsmphsa aqllgmlsyq ghpaafdvsl gcsafpyvls
      121 lcrgmleaqn wnravivtnd pysrlltldq pktaaifgda atatllerdr ggaicvgdfg
      181 tdggewralh tpqwrdarrt shllddtpvp eadahsvrmn gaklasyfsk rvpesmtkcl
      241 asngvqpsdv divvlhqasr pmlellierl pfgvntevpv llqdggntts ssiplalgri
      301 mqeralagrk vlltgfgvgl swgslllef
//
LOCUS       WP_011353663             300 aa            linear   BCT 20-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Burkholderia lata].
ACCESSION   WP_011353663
VERSION     WP_011353663.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia lata
  ORGANISM  Burkholderia lata
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Chakraborti,S. and Bahnson,B.J.
  TITLE     Crystal structure of human senescence marker protein 30: insights
            linking structural, enzymatic, and physiological functions
  JOURNAL   Biochemistry 49 (16), 3436-3444 (2010)
   PUBMED   20329768
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Chen,C.N., Chin,K.H., Wang,A.H. and Chou,S.H.
  TITLE     The first crystal structure of gluconolactonase important in the
            glucose secondary metabolic pathways
  JOURNAL   J Mol Biol 384 (3), 604-614 (2008)
   PUBMED   18848569
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Tanaka,Y., Morikawa,K., Ohki,Y., Yao,M., Tsumoto,K., Watanabe,N.,
            Ohta,T. and Tanaka,I.
  TITLE     Structural and mutational analyses of Drp35 from Staphylococcus
            aureus: a possible mechanism for its lactonase activity
  JOURNAL   J Biol Chem 282 (8), 5770-5780 (2007)
   PUBMED   17166853
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12093833
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia lata"
                     /db_xref="taxon:482957"
     Protein         1..300
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32104
     Region          20..262
                     /region_name="SGL"
                     /note="SMP-30/Gluconolactonase/LRE-like region; pfam08450"
                     /db_xref="CDD:462480"
ORIGIN      
        1 mqqthpagqa tlladsrntl gegatwcdrt halywvdieg aqlwrcradg sdltpwampe
       61 rlacfalthd pdvllvglat hlaffdlrsg aftrivdvep elptrlndgr cdpfgalvfg
      121 mkdegseppq avggfyrlna dltlerlalp paaiansiaf spdgsklyfc dslvreifvc
      181 dyraggdvan vrpfarltdp dgdpdgsmid rdgglwnaqw ggrrvvrygp dgvetdrvav
      241 ptaqpsctal dgegrlyvts ariglsddal agdphaggvf vaqtrhagma tarfagtprg
//
LOCUS       WP_011354944             198 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Burkholderia lata].
ACCESSION   WP_011354944
VERSION     WP_011354944.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia lata
  ORGANISM  Burkholderia lata
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 198)
  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 198)
  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   3  (residues 1 to 198)
  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   4  (residues 1 to 198)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 198)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia lata"
                     /db_xref="taxon:482957"
     Protein         1..198
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=21548
     Region          9..195
                     /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"
ORIGIN      
        1 mstpassarl rvllvtdtdk pigdlgdala tlgyemlndv atparlpaav eeqhpdvvii
       61 dtdspsrdtl eqlavmhata prpvlmfshd snqsliraav gagvsaylve glsaerlapi
      121 levalarfsh ddalrrrlad verelaerkl idrakrllmd qrklsehday aalrkramdq
      181 glrivdvarq lldaspqs
//
LOCUS       WP_011354467             132 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [Burkholderia].
ACCESSION   WP_011354467
VERSION     WP_011354467.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (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   2  (residues 1 to 132)
  AUTHORS   Kenney,L.J.
  TITLE     Structure/function relationships in OmpR and other winged-helix
            transcription factors
  JOURNAL   Curr Opin Microbiol 5 (2), 135-141 (2002)
   PUBMED   11934608
REFERENCE   3  (residues 1 to 132)
  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 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   5  (residues 1 to 132)
  AUTHORS   Martinez-Hackert,E. and Stock,A.M.
  TITLE     Structural relationships in the OmpR family of winged-helix
            transcription factors
  JOURNAL   J Mol Biol 269 (3), 301-312 (1997)
   PUBMED   9199401
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10086760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..132
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15088
     Region          11..100
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(30,49..50,68,71,79..80,92,97)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mdckylyidn ikinfvrrti eidnkiidvt prefdvvefl ldnmnkivpr qaiqeavwgr
       61 elgvssrtld thisrirskl qldhdknlri ipiyavgyrl vlfgaamthv erhdaapilr
      121 vapqavmaad ya
//
LOCUS       WP_011351670             858 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia lata].
ACCESSION   WP_011351670
VERSION     WP_011351670.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia lata
  ORGANISM  Burkholderia lata
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 858)
  AUTHORS   Krewulak,K.D. and Vogel,H.J.
  TITLE     TonB or not TonB: is that the question?
  JOURNAL   Biochem Cell Biol 89 (2), 87-97 (2011)
   PUBMED   21455261
REFERENCE   2  (residues 1 to 858)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
REFERENCE   3  (residues 1 to 858)
  AUTHORS   Moeck,G.S. and Coulton,J.W.
  TITLE     TonB-dependent iron acquisition: mechanisms of siderophore-mediated
            active transport
  JOURNAL   Mol Microbiol 28 (4), 675-681 (1998)
   PUBMED   9643536
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12223540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..858
                     /organism="Burkholderia lata"
                     /db_xref="taxon:482957"
     Protein         1..858
                     /product="TonB-dependent siderophore receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=92385
     Region          107..158
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          136..858
                     /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 mgsesstgps stdlpimvsi rltyrrrpap arhlprasrp aapaapgrla rrlagavlvs
       61 allplpalad tdtdaapaaq raprrafdip agpleaalnr fgrdagilla fpaeltaglt
      121 sggvqgrfdi dgafdrllag tglvalrqpa ggytlkradg slarpaaagv aagaelpain
      181 vrtsalraes yrapkeagvl rsdiplldta qavnivpaqv lrdqrprnld dalgnvsgit
      241 qgntlagtqd timkrgfggn rdgsimqngm plvqgrafna avdsvevlkg ptsllyglmd
      301 pggvvnvvtk qpqlkrynai slgastfghg knggsatfds tgpvgdsrla yrlivdqsne
      361 qywrnfgeyr qtfvapslaw ygrdtqvavs yqyrkfhspf drgtaldprt napldiparr
      421 ridepfnnmd geshlaqvsv dhqfnadwsa hfgysynret ydanqlrttg vdpvkgtmtr
      481 sndathgsls tdsygigyvn gklmlggmqh dvqvgfdtey rriyrkdmlr qavktpfnyl
      541 npvygllpps stvsasdsdq tdtlhdasaf vqdtihltdk wivsgglryi tynqvagrgr
      601 pfvantdlsg skwlpragvv ykwtdtfsly gsysqslkps ssiapmtgyi idgatppeea
      661 tawevggkld lpggvtgtla lfnidkknvl vsqyndatkl tdwrtsgkar srgieldvsg
      721 kigervnvia syayidaktt edplyagnql wnvarhtasl aavydfgtvv ggddlrigad
      781 vryvgarpgd sansftlpsy vladafatyd trigkqklsf qlnvknlfnr tyypssanry
      841 fvaigdarqv sllttlqf
//
LOCUS       WP_011355263             373 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter
            substrate-binding protein [Burkholderia].
ACCESSION   WP_011355263
VERSION     WP_011355263.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 373)
  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 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   3  (residues 1 to 373)
  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   4  (residues 1 to 373)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 373)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 373)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..373
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38550
     Region          28..363
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(103..105,125..126,175,227,251)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mrhlvtalsv alaagaltsa haqevvmigh sapltgpqaa ngkdnengar lavdelnkag
       61 ikvagkavtf klvsdddqad pkagvqvaqn lvdkgvvavl gpynsgvaip asrvystagv
      121 pmlpvasnpa ltkqgfknif rigasdeqlg gtmatfaakt lnaktaavid drtaygqgva
      181 eqfmnvakan gikivdqeyt sssatdflgi ltkikasnpd viflggyaaq gapmakqmkq
      241 rglrakllgg dgicsadmgk vagdaasivy caqggvalek taagreflkk yhdtyhtdpq
      301 vygvnyydgm klladamvka gtttdkakli aqlaksdykg vagtysfdan gdlkgapttv
      361 yvirnglpep yak
//
LOCUS       WP_011356269             383 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Burkholderia lata].
ACCESSION   WP_011356269
VERSION     WP_011356269.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia lata
  ORGANISM  Burkholderia lata
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 383)
  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 383)
  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   3  (residues 1 to 383)
  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   4  (residues 1 to 383)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 383)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 383)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 383)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Burkholderia lata"
                     /db_xref="taxon:482957"
     Protein         1..383
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39923
     Region          33..369
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(109..111,132..133,182,234,258)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mtfrirslsg valtaailal qtgaahaqet vvkvgvagpl tgggaaygkd iengvrmavd
       61 eanaahttvg gkpvkfvvas qddqsdprtg vqaaqqlada qvavvighfn sgttlpaski
      121 yakagipmit psatnpditr aglgtvyrvi atdtqnagna gayaasvtka kriaiiddrt
      181 afgqgeadef eksvkanggt ivareftndk avdfsaqltk ikstnadlvf fggldaqaam
      241 lvkrmrqlgi raqflagggv mnanfiklag naaegasvwe ygqplsrlak gkqfetkfkq
      301 kygidmlaya pfaydatwia inamqkanst kpadfngalk gtrydgitgt iaftntgdlk
      361 npsstlyevk naawqpvttk sad
//
LOCUS       WP_011356295             700 aa            linear   BCT 20-JAN-2025
DEFINITION  TonB-dependent receptor family protein [Burkholderia lata].
ACCESSION   WP_011356295
VERSION     WP_011356295.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia lata
  ORGANISM  Burkholderia lata
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Burkholderia lata"
                     /db_xref="taxon:482957"
     Protein         1..700
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=75976
     Region          16..700
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 mftstriaaa lsgaisvlfa saacaqgada paastlpain vnatrvpdsl tskstgslkr
       61 tleqtvgsvg fvdadsyrnt yaftlrdvlk dvpgvfvenr ygqelrlsir gsgiarsyht
      121 rgleilqdgi ptnladgsgd yyqidplalq avqvykggng laygastlgg aidfitptah
      181 tadapnilrv eggsygtvrt saqisrvlgp ldflanfsvn hadgyrdhsk gqyeqfnanv
      241 gyrfsptvet rfyvgvyvvd qllpgtlsls dalnnptkaa pnamsgdqar ntrterianr
      301 ttvkldsgel qfdtwaihks lyhpifqald qdgwtygfap rytghltlgg mrndlivgar
      361 ffggrtqanq yvnvngnkga qtldstqtaf nyeayvenrl ffvptvalmt gvkvlhsvre
      421 yidngglprs pnykstnasy sgvnpklgll wqpdantqay vditrsqdvp dftdltqtfs
      481 nttrftplaa qhawtiefgt rgsrervswd vtayrslvrd qllqyttnpd vpastfnank
      541 tvlqgieaga svellrnvtg rgagdkvtls giwnlndfrf kndpqygnnr iagvplnvlr
      601 atlgyarpsg fhiaatldwv psgawaddan tlrvpsytll glqagydfrn glslfvdarn
      661 ltnkryvsdi stvadartan taifypgegr svfagmryaf
//
LOCUS       WP_011353329             441 aa            linear   BCT 20-JAN-2025
DEFINITION  type II toxin-antitoxin system HipA family toxin [Burkholderia
            lata].
ACCESSION   WP_011353329
VERSION     WP_011353329.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia lata
  ORGANISM  Burkholderia lata
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Wen,Y., Behiels,E., Felix,J., Elegheert,J., Vergauwen,B.,
            Devreese,B. and Savvides,S.N.
  TITLE     The bacterial antitoxin HipB establishes a ternary complex with
            operator DNA and phosphorylated toxin HipA to regulate bacterial
            persistence
  JOURNAL   Nucleic Acids Res 42 (15), 10134-10147 (2014)
   PUBMED   25056321
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Germain,E., Castro-Roa,D., Zenkin,N. and Gerdes,K.
  TITLE     Molecular mechanism of bacterial persistence by HipA
  JOURNAL   Mol Cell 52 (2), 248-254 (2013)
   PUBMED   24095282
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Kaspy,I., Rotem,E., Weiss,N., Ronin,I., Balaban,N.Q. and Glaser,G.
  TITLE     HipA-mediated antibiotic persistence via phosphorylation of the
            glutamyl-tRNA-synthetase
  JOURNAL   Nat Commun 4, 3001 (2013)
   PUBMED   24343429
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Schumacher,M.A., Piro,K.M., Xu,W., Hansen,S., Lewis,K. and
            Brennan,R.G.
  TITLE     Molecular mechanisms of HipA-mediated multidrug tolerance and its
            neutralization by HipB
  JOURNAL   Science 323 (5912), 396-401 (2009)
   PUBMED   19150849
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Jayaraman,R.
  TITLE     Bacterial persistence: some new insights into an old phenomenon
  JOURNAL   J Biosci 33 (5), 795-805 (2008)
   PUBMED   19179767
REFERENCE   6  (residues 1 to 441)
  AUTHORS   Black,D.S., Kelly,A.J., Mardis,M.J. and Moyed,H.S.
  TITLE     Structure and organization of hip, an operon that affects lethality
            due to inhibition of peptidoglycan or DNA synthesis
  JOURNAL   J Bacteriol 173 (18), 5732-5739 (1991)
   PUBMED   1715862
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia lata"
                     /db_xref="taxon:482957"
     Protein         1..441
                     /product="type II toxin-antitoxin system HipA family
                     toxin"
                     /EC_number="2.7.11.1"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=49365
     Region          11..420
                     /region_name="HipA"
                     /note="Serine/threonine protein kinase HipA, toxin
                     component of the HipAB toxin-antitoxin module [Signal
                     transduction mechanisms]; COG3550"
                     /db_xref="CDD:442771"
ORIGIN      
        1 mngkaikpdv sealdlhigt sglpvghlly vsqgrrelsq fvyderwlth pdhfeispdl
       61 plhagyqtrr apravdsvfh faladtepda wgrrvidrah aklrrtqpdl rplneldylc
      121 avddfsrvga lrlcrsgryl rteedgrrtt ppfieleria datraleagt dtaadlrylq
      181 gkgtslggmr pkctvldeng rlaigkfpsi gdtinvtrae vlalrlarta gidaagarcv
      241 mvgetpvali drfdrtgddl ripylsaasm lqasrddeha yteivdamrq hgarplddar
      301 elwrrlvfnl litntddhlq nlgflydgnr rwrlapafdv npmpgklres ktwltedtgp
      361 idsigmllda cghfsltreq aldvlgvvfd avqswrrigq ladigltvre lddledafeh
      421 pqteqarryl grpvrrgtge r
//
LOCUS       WP_011356600             339 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Burkholderia].
ACCESSION   WP_011356600
VERSION     WP_011356600.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 339)
  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 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 339)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 339)
  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   5  (residues 1 to 339)
  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   6  (residues 1 to 339)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..339
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37687
     Region          28..211
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          91..334
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mddtdrytta nlpvhllrcl aetskelgid ptrlclglgf dvadlsnpsc rislrqastm
       61 irraldmapg ralglelgts etiasiglvg yamltsptlk daisvgmelq rhtgplmrfe
      121 visdartlsi ratnvflepd ieaflveeaf gsfmkigrsl vgpafqpkvv dlsypppaya
      181 eqytrvfpcp vrfeqeqnlf scdaalgnrp iathdplahr qaleflqdal ppepegtefl
      241 esierimrrd lrhapslaei aaqlcmsert lrrrladqgv syqtvidtir rkraftllsn
      301 prlsiedvah evgfsdahnf rrafkrwtgh gpregqrpa
//
LOCUS       WP_011357218             197 aa            linear   BCT 20-JAN-2025
DEFINITION  nitroreductase family protein [Pelodictyon luteolum].
ACCESSION   WP_011357218
VERSION     WP_011357218.1
KEYWORDS    RefSeq.
SOURCE      Pelodictyon luteolum (Chlorobium luteolum)
  ORGANISM  Pelodictyon luteolum
            Bacteria; Pseudomonadati; Chlorobiota; Chlorobiia; Chlorobiales;
            Chlorobiaceae; Chlorobium/Pelodictyon group; Pelodictyon.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Akiva,E., Copp,J.N., Tokuriki,N. and Babbitt,P.C.
  TITLE     Evolutionary and molecular foundations of multiple contemporary
            functions of the nitroreductase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 114 (45), E9549-E9558 (2017)
   PUBMED   29078300
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Somerville,C.C., Nishino,S.F. and Spain,J.C.
  TITLE     Purification and characterization of nitrobenzene nitroreductase
            from Pseudomonas pseudoalcaligenes JS45
  JOURNAL   J Bacteriol 177 (13), 3837-3842 (1995)
   PUBMED   7601851
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Pelodictyon luteolum"
                     /db_xref="taxon:1100"
     Protein         1..197
                     /product="nitroreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21342
     Region          4..157
                     /region_name="NfnB"
                     /note="Nitroreductase [Energy production and conversion];
                     COG0778"
                     /db_xref="CDD:440541"
ORIGIN      
        1 mmqfrdlvvr srsirrfdes vavqdgvlrd lvelacyvps pknlqplkfi arsgpdcsra
       61 lfpllswagy ladwpgpeag erptayivml gdtsitsdfs idsgiaaevi mlgaasiglg
      121 gciiasidrp alqsllhipd ryqilqvlal gkpvetvvid qigdgdpvry yrdpngihhv
      181 pkrtpgdill dfsddpg
//
LOCUS       WP_011358087             311 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Pelodictyon luteolum].
ACCESSION   WP_011358087
VERSION     WP_011358087.1
KEYWORDS    RefSeq.
SOURCE      Pelodictyon luteolum (Chlorobium luteolum)
  ORGANISM  Pelodictyon luteolum
            Bacteria; Pseudomonadati; Chlorobiota; Chlorobiia; Chlorobiales;
            Chlorobiaceae; Chlorobium/Pelodictyon group; Pelodictyon.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Pelodictyon luteolum"
                     /db_xref="taxon:1100"
     Protein         1..311
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36037
     Region          21..306
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 mhhdndreti aikaaggstp ldsayrycre iakhhaktfy latlflpkpq qkpifaiyal
       61 lrtvddlvdn aqdqleaghi trtdinrmle ewmeklqncy qgkhggdpim mawhdtllrc
      121 nipielplel iegvamdief npfqtfdely vycykvasvv glmtseifgy sdrralqhai
      181 dlgiamqltn ilrdvgedid rgriyipled lerfgysree fmqktmnerf kklmqfqier
      241 arnyylsade gipmlekrsr favavssvny gnilnaieen gydvftkray rsfiqkisti
      301 phvwlktrnt q
//
LOCUS       WP_011358284             357 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Pelodictyon
            luteolum].
ACCESSION   WP_011358284
VERSION     WP_011358284.1
KEYWORDS    RefSeq.
SOURCE      Pelodictyon luteolum (Chlorobium luteolum)
  ORGANISM  Pelodictyon luteolum
            Bacteria; Pseudomonadati; Chlorobiota; Chlorobiia; Chlorobiales;
            Chlorobiaceae; Chlorobium/Pelodictyon group; Pelodictyon.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Pelodictyon luteolum"
                     /db_xref="taxon:1100"
     Protein         1..357
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=39954
     Region          1..351
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msieiknvtk kypgytaldd itlkvqtgel iallgpsgcg kttllriiag letpdagsvl
       61 lgdrdttnlq preknvgfvf qhyalfrrld vfenvafgln vrpsgsrpsk seirdrveyl
      121 lklvqmdwam krypsqlsgg qrqrvalara lavnpkvlll depfsaldak vrqelrrwlr
      181 klhydihvts ifvthdqeea leladrivvi nkgrieqqgs pqevydhpan afvynflgnv
      241 nvfhgrvreg kilvgeklle agpasgihea fdgqafirph eigisrirss gndlsgfird
      301 irlmggqigl aletkafdqp ieaeitreaw hnlqlskgde vfitldrlkv fsgdyei
//
LOCUS       WP_011359897             308 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Synechococcus sp. CC9902].
ACCESSION   WP_011359897
VERSION     WP_011359897.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus sp. CC9902
  ORGANISM  Synechococcus sp. CC9902
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Synechococcus sp. CC9902"
                     /db_xref="taxon:316279"
     Protein         1..308
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=33700
     Region          138..303
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mvqnflnrcr eqpfsflrrh qktalsavai gsvglvglgw llidgrmlsf agdrpsllel
       61 ldqvaedkga rskpsplgsv pvaplsrswr splarqcssi dkgirsrlls lqkrsgswrt
      121 fvpidptnfg krftedafgr rldgsprviv lhetvysvss avntfqtphp idedqvsyht
      181 lisrdgrvld lvdplmrayg agysaflgew aitnkrlkgs vnnfalhlsl etpsngangr
      241 sghsgysseq ydalalvlag wmdafnlppt svtthrhvdi ggeradprsf dwsalqvrla
      301 amgdlcvp
//
LOCUS       WP_011364331             215 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Synechococcus sp. CC9605].
ACCESSION   WP_011364331
VERSION     WP_011364331.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus sp. CC9605
  ORGANISM  Synechococcus sp. CC9605
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Synechococcus sp. CC9605"
                     /db_xref="taxon:110662"
     Protein         1..215
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23278
     Region          22..211
                     /region_name="YciV"
                     /note="5'-3' exoribonuclease TrpH/YciV (RNase AM),
                     contains PHP domain [Nucleotide transport and metabolism];
                     COG0613"
                     /db_xref="CDD:440378"
ORIGIN      
        1 mthplktvle qvgpsscptt hnfhchtvcs dgslepieli wqaterglkh lavtdhhssh
       61 ahreiqawld qqrasgvevp tvwsgmeisa llkgclvhvl algfelnhpa lqpynrgdav
      121 vgeplraeav vnaihaaggl avlahparyr lghdvlidea arlgfdggea wydyemqptw
      181 saspliceai drqlsnlgll rtcgtdthgi dlcgr
//
LOCUS       WP_011366407             374 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Oleidesulfovibrio alaskensis].
ACCESSION   WP_011366407
VERSION     WP_011366407.1
KEYWORDS    RefSeq.
SOURCE      Oleidesulfovibrio alaskensis
  ORGANISM  Oleidesulfovibrio alaskensis
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Oleidesulfovibrio.
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   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   3  (residues 1 to 374)
  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   4  (residues 1 to 374)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 374)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 374)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 374)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Oleidesulfovibrio alaskensis"
                     /db_xref="taxon:58180"
     Protein         1..374
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39772
     Region          28..364
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(101..103,124..125,173,225,249)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 msrkmtafvl gvvatvlmag tamagtvkig lmcpltgswa segqdmrniv lmlaeqtnaq
       61 ggingdmvei vveddagdpk taalaaqrls tmgvsavigs ygsaiteasq aiydemdivq
      121 vatgstairl tekglplffr tcprddeqgr vaaavlkekg ykkiailhdn tsyakglaee
      181 tltllksagt evvfydaltp nerdysailt klkaagpdai fftgyypeag mllrqkqemk
      241 wdvpmmggda tnnldlvkia gksaagflfi spptlqdlpd kqakdfaaay karygtmpas
      301 vwsvlagdaf ialkaaitga gstdpqdiaa ymkkdlkdlp gltgslsfne kgdrvgdlyr
      361 lyrvdengnf vlqp
//
LOCUS       WP_011368853             105 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Oleidesulfovibrio alaskensis].
ACCESSION   WP_011368853
VERSION     WP_011368853.1
KEYWORDS    RefSeq.
SOURCE      Oleidesulfovibrio alaskensis
  ORGANISM  Oleidesulfovibrio alaskensis
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Oleidesulfovibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Oleidesulfovibrio alaskensis"
                     /db_xref="taxon:58180"
     Protein         1..105
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11654
     Region          1..101
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(6..7,25..26,34,37,39..40,42,45..46,48,56,61,68)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Site            order(25,56..57,59,84)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mertqftvev irqiksipag yvstygmiaa magnpraarq varvlhscsa rdalpwyrvi
       61 naggnislpr gggyerqkal lqregivfde tdrvdlqrfm wtmpa
//
LOCUS       WP_011371671             123 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Sulfurimonas denitrificans].
ACCESSION   WP_011371671
VERSION     WP_011371671.1
KEYWORDS    RefSeq.
SOURCE      Sulfurimonas denitrificans
  ORGANISM  Sulfurimonas denitrificans
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurimonadaceae; Sulfurimonas.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Sulfurimonas denitrificans"
                     /db_xref="taxon:39766"
     Protein         1..123
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=13595
     Region          2..123
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 maatilpfss eisfvaales gmsvknamff assgnilaii lnyslgylly ektktkllss
       61 kigrvsykyg hsygyvallf swlpiigdpl tlvagvlrln fiyfilisas lrvlryyflt
      121 lml
//
LOCUS       WP_011372349             270 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Sulfurimonas
            denitrificans].
ACCESSION   WP_011372349
VERSION     WP_011372349.1
KEYWORDS    RefSeq.
SOURCE      Sulfurimonas denitrificans
  ORGANISM  Sulfurimonas denitrificans
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurimonadaceae; Sulfurimonas.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Sulfurimonas denitrificans"
                     /db_xref="taxon:39766"
     Protein         1..270
                     /product="formate/nitrite transporter family protein"
                     /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=29265
     Region          2..266
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msylvpsefv tkmidagesk vymstkdtii rafmagaila lsaafaitva mqsgsalvga
       61 mlfpvgfiml ylmgfdlltg vfvlvplall dkrkgvtikq vlrnwglvfl gnfagailva
      121 fmisfiltyg ysidagalge kigsigeert lgykehgisg wftifirgml cnwmvsmgvv
      181 gamistnvsg kaiamwmpim lfffmgfehs vvnmflfpfs mimggdftva dyiiwneipt
      241 vfgnliggla ftgltlyath vktgakreld
//
LOCUS       WP_011372559             738 aa            linear   BCT 20-JAN-2025
DEFINITION  CHASE2 domain-containing protein [Sulfurimonas denitrificans].
ACCESSION   WP_011372559
VERSION     WP_011372559.1
KEYWORDS    RefSeq.
SOURCE      Sulfurimonas denitrificans
  ORGANISM  Sulfurimonas denitrificans
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurimonadaceae; Sulfurimonas.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Zhulin,I.B., Nikolskaya,A.N. and Galperin,M.Y.
  TITLE     Common extracellular sensory domains in transmembrane receptors for
            diverse signal transduction pathways in bacteria and archaea
  JOURNAL   J Bacteriol 185 (1), 285-294 (2003)
   PUBMED   12486065
REFERENCE   2  (residues 1 to 738)
  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 10008393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Sulfurimonas denitrificans"
                     /db_xref="taxon:39766"
     Protein         1..738
                     /product="CHASE2 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:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=82235
     Region          8..661
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mkkslaqlfv alliafmstl aymytsefyl pfenkikdlm fkargeivgd keiiiidide
       61 kslkelgqwp wsrdvvskll qnlaeyevgi vgldivfaep dnsspkkvfq klglstqgvv
      121 dydallaeti aqtptivgyv falsndgiap esspksnaii veqnrpksss lvkpyrtiln
      181 ieaiqesays sgyfntipdn dgvvrsiplv meydgilyps lslemvriml dekkitivyd
      241 dngashvelg etmiptdffa rmqinyrgkq nsyryisavd vynktedash iagkiallgt
      301 saaglmdlrs tpfdsvfagv evhanaidni inadfiakpi wsvgvdmasf silalltfai
      361 lllpsavlsf islvfinaii igvhyyfmvy egailhtfll lvsvnalfvl gqainyflei
      421 rqkemikgkf askvssavmd dllsvegdif agkereisif fsdvrgftnl seamgdprsl
      481 ihlmnaymdp mtdivikskg tvdkfigdai maywnapnev enhadvavsa aldqlhalre
      541 lneqirlnpe fknavlmsdk kgipiidigi gintgvaivg emgsssrsdy tvigdpinlg
      601 srleslckyy ssklnisnft keqlkgsyif rfldlvtvkg ksvpieiwqi hdyddaletp
      661 lynvtkeele eelkiyhhai alykdtkfse aleifetlda nenktnktiy siyierchhy
      721 iemppinfng vfehtskg
//
LOCUS       WP_011372604             691 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Sulfurimonas denitrificans].
ACCESSION   WP_011372604
VERSION     WP_011372604.1
KEYWORDS    RefSeq.
SOURCE      Sulfurimonas denitrificans
  ORGANISM  Sulfurimonas denitrificans
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurimonadaceae; Sulfurimonas.
REFERENCE   1  (residues 1 to 691)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 691)
  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   3  (residues 1 to 691)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..691
                     /organism="Sulfurimonas denitrificans"
                     /db_xref="taxon:39766"
     Protein         1..691
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=78289
     Region          5..680
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mnkhdrvmqi flneckeile eiapkllnle dtpndknlin difrgihtlk gnansfgfvk
       61 lgefvhhfed llsiyrkdes vldssevdlf irsfdivgsv feyeedgvdg yptnyyeile
      121 eikkalnike nskesfeeiv sassfahvaq esvivkkmve htqynlkdig dkkiyeikle
      181 ldsdiylrgy nhqiffrlle slgtllysny iideniptle efntehsyvk slyiyllsds
      241 demdildvfe fiaqehevsl svvdlkelet lqekeskeee sqsqetlyvq ngskehksva
      301 kssirvesak ldelfdsige lviaqsyisq nekirsindn elnqylemls kstriiqskv
      361 mslrmipird tflkmkrvvr dvsvktskei elilsgedte idktmvdkls eplihllrns
      421 vdhgieesah drvalgkeec gniylsaahk gssfvieird dgrgidtqki lqkaiekgfa
      481 kegasytqde iinflfcagf stansitdis grgvgldavr qsieelrgkv tveselgvgt
      541 ifriilpltl aiidgltirv dnemlivptl svvesfspii kdihyvkgeg efinyrgeil
      601 pivrlnrllg lnksktefen stficidher gryiiqvdel lgrqqvviks lgvlsnnvke
      661 isgaailgtg qialilnteg vrdhldfeys a
//
LOCUS       WP_011372984             378 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Sulfurimonas denitrificans].
ACCESSION   WP_011372984
VERSION     WP_011372984.1
KEYWORDS    RefSeq.
SOURCE      Sulfurimonas denitrificans
  ORGANISM  Sulfurimonas denitrificans
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurimonadaceae; Sulfurimonas.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Sulfurimonas denitrificans"
                     /db_xref="taxon:39766"
     Protein         1..378
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=43072
     Region          57..>352
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 malslieelp kivkegraea arilerinsg nalalqtnel vlpskdvsgl frgempssde
       61 sewknrliyg dnilvmqgll agdatsgles mrgkidliyi dppfdskady rtkitlpnin
      121 lsqkptvieq fayadtwkdg tvsylkmiyp rlvlmrells ekgsiyvhid whvghyvkil
      181 lddifgkgkf rneiiwhyst lgrpkdkfaq khdqifvygk sddaffntee akipysddyi
      241 eshfrdiddn gkkcrkrfda gkwriyypde gmipndvwdi pyensmsker vsyatqkpva
      301 lmeriiksst ikgqliadff ggsgttavva erlnrqwiss digkpsimvq rkvstphhkh
      361 rfsacnvskr egyislit
//
LOCUS       WP_011373630             280 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Sulfurimonas
            denitrificans].
ACCESSION   WP_011373630
VERSION     WP_011373630.1
KEYWORDS    RefSeq.
SOURCE      Sulfurimonas denitrificans
  ORGANISM  Sulfurimonas denitrificans
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Sulfurimonadaceae; Sulfurimonas.
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   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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Sulfurimonas denitrificans"
                     /db_xref="taxon:39766"
     Protein         1..280
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32919
     Region          184..260
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 miydvfpsai elkdvvrqyv vvtslegiek llflpngcnf iifnrgfdgy ikiynedkrf
       61 hipknysisi knnkikkfkl ydkslassvk lplimaeltp igfyklfnrd atilnkcfle
      121 iqeniideyf sqlythecve aelkylndal drlqkscnnt rmciqdvmdk iiniyrfevs
      181 vkhlleefsc srsklerefk rnigftpknf iyiskfcktv layieddcgf nemeylysdy
      241 shmnsvfkkf fgaspsvvfe dvtnnkilly qmqraqkhsi
//
LOCUS       WP_011374290             196 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Latilactobacillus sakei].
ACCESSION   WP_011374290
VERSION     WP_011374290.1
KEYWORDS    RefSeq.
SOURCE      Latilactobacillus sakei
  ORGANISM  Latilactobacillus sakei
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Latilactobacillus.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Latilactobacillus sakei"
                     /db_xref="taxon:1599"
     Protein         1..196
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /function="2.5 Metabolism of coenzymes and prosthetic
                     groups"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21442
     Region          1..188
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mrkivvgisg asgtiygirl lealhqvpdv ethlvmsrwa kenlaiektg ytekqvvala
       61 dfvhpeqnmg atiasgsfkh dgmvivptsm ktlasiatgl genliaraad vtlkerrpli
      121 ivprespfnq ihlenmlkla qmgvaivppi pafynqpqti ddivnhtvmk lldqlhietn
      181 lgprweglan arqnar
//
LOCUS       WP_011374484              86 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: zinc ribbon domain-containing protein
            [Latilactobacillus].
ACCESSION   WP_011374484
VERSION     WP_011374484.1
KEYWORDS    RefSeq.
SOURCE      Latilactobacillus
  ORGANISM  Latilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
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 10577258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Latilactobacillus"
                     /db_xref="taxon:2767885"
     Protein         1..86
                     /product="zinc ribbon domain-containing protein"
                     /function="5 Proteins of unknown function that are similar
                     to other proteins"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=9857
     Region          4..86
                     /region_name="Zn_ribbon_2"
                     /note="Putative zinc ribbon domain; pfam12674"
                     /db_xref="CDD:463667"
ORIGIN      
        1 mekfcqscgm plspanqgre qdgtkstqyc qlcyidgqwt eptitfeqml akgiaglrad
       61 qttgqlkkwf liksypmmlk kmrrwq
//
LOCUS       WP_011375360             394 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Latilactobacillus sakei].
ACCESSION   WP_011375360
VERSION     WP_011375360.1
KEYWORDS    RefSeq.
SOURCE      Latilactobacillus sakei
  ORGANISM  Latilactobacillus sakei
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Latilactobacillus.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Latilactobacillus sakei"
                     /db_xref="taxon:1599"
     Protein         1..394
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /function="2.1 Metabolism of carbohydrates and related
                     molecules"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42516
     Region          3..394
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mnnilvinag ssslkwqlfq qtdlslvasg lmermntpea rftfkfngqk eqvaianlty
       61 edgvirllkq lqdnaiidsp sdivavghrv vagattfeks tlitadnlat lkaldkyapl
      121 hnpvqvdcie tlmhilpnsv pevavfdsqf yldmpdatsf yglpyedsqk yqirkygehg
      181 ishgyilqet aaflnqpvae lklitlhlgg gssitasqng kpvdtsmgft pleglpmgtr
      241 agsldaaivp flmnelnksa deiitllnte sgilgvsgvs admrdiqssl atnpraklay
      301 dmfitsaakf igsyyvelgg anvitftagi gendakmrad vcdrlavlgv kidperneqg
      361 hsarqistdd saikvlmipt neelaiakqv kalv
//
LOCUS       WP_011374646             127 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ribonuclease HI family protein [Latilactobacillus].
ACCESSION   WP_011374646
VERSION     WP_011374646.1
KEYWORDS    RefSeq.
SOURCE      Latilactobacillus
  ORGANISM  Latilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Kanaya,S.
  TITLE     Ribonuclease H
  JOURNAL   FEBS J 276 (6), 1481 (2009)
   PUBMED   19228198
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Tadokoro,T. and Kanaya,S.
  TITLE     Ribonuclease H: molecular diversities, substrate binding domains,
            and catalytic mechanism of the prokaryotic enzymes
  JOURNAL   FEBS J 276 (6), 1482-1493 (2009)
   PUBMED   19228197
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Malik,H.S.
  TITLE     Ribonuclease H evolution in retrotransposable elements
  JOURNAL   Cytogenet Genome Res 110 (1-4), 392-401 (2005)
   PUBMED   16093691
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Ohtani,N., Haruki,M., Morikawa,M. and Kanaya,S.
  TITLE     Molecular diversities of RNases H
  JOURNAL   J Biosci Bioeng 88 (1), 12-19 (1999)
   PUBMED   16232566
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Crouch,R.J.
  TITLE     Ribonuclease H: from discovery to 3D structure
  JOURNAL   New Biol 2 (9), 771-777 (1990)
   PUBMED   2177653
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10174584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Latilactobacillus"
                     /db_xref="taxon:2767885"
     Protein         1..127
                     /product="ribonuclease HI family protein"
                     /EC_number="3.-.-.-"
                     /function="3.6 RNA restriction and modification"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004523 - RNA-DNA hybrid ribonuclease
                     activity [Evidence IEA]"
                     /GO_process="GO:0043137 - DNA replication, removal of RNA
                     primer [Evidence IEA]"
                     /calculated_mol_wt=14044
     Region          2..126
                     /region_name="RNase_HI_like"
                     /note="RNAse HI family that includes archaeal, some
                     bacterial as well as plant RNase HI; cd09279"
                     /db_xref="CDD:260011"
     Site            order(7..10,40..42,45,71,108,122)
                     /site_type="other"
                     /note="RNA/DNA hybrid binding site [nucleotide binding]"
                     /db_xref="CDD:260011"
ORIGIN      
        1 miklytdaat lgnpgpsaag ilivtakkqy qfsiplppvd nhiaefmavq lglekiatla
       61 ltesllqinv dskivcqsle kqyakhyqqy vdqiialeqp yslvlhqwlp drqnkgahhl
      121 aqqalkk
//
LOCUS       WP_011377961             610 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Synechococcus elongatus].
ACCESSION   WP_011377961
VERSION     WP_011377961.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus elongatus
  ORGANISM  Synechococcus elongatus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 610)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Synechococcus elongatus"
                     /db_xref="taxon:32046"
     Protein         1..610
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=61543
     Region          <48..196
                     /region_name="myxo_dep_M36"
                     /note="myxosortase-dependent M36 family metallopeptidase;
                     NF038112"
                     /db_xref="CDD:468355"
     Region          146..396
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
     Region          297..540
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mapfnfsaft fvklfsrlfn fnskpiaqsq tqnltenagl fngqliasdp ngdpitflla
       61 pnqvapagft lnsngsysfd qddtsydslg lgdtqviaid yvvkdsrgav sqtrtltinl
      121 agtndaptit agpvvdansi tftaedidsd tltarvgttn lmpgtvnngs pttstitald
      181 talfgelnvf dgtdsvgvgl fvgigtigad tltaigtnpa vlygfegddr ltgadqddti
      241 lggdgndtii eingnnlieg nnnndsivgg tdsdringga gadtilggdg adtidgglgn
      301 dsifgdsgnd nirgfgdsnt ilggsgndti egtiagsnsi dggenddvit eigfgstllg
      361 glgndsilgf sastinggdg sdtinvefgn ntidggmgnd sieiainpsf tisgsgntvs
      421 gsngndtiia ingsnliegn ndndsivggt dsdtinggtg adtltgglgs dtfsfaatgd
      481 giaatsgeng svtfgngfdy itdfesidsi ivgtdgftiq ssvgtafidg dgnyvivsvg
      541 misdifaiag vltdttfesr dpgmgdsfte lllfkasnam mgdvitattt petliiggsa
      601 ldmlqpyscc
//
LOCUS       WP_011378306             393 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Synechococcus elongatus].
ACCESSION   WP_011378306
VERSION     WP_011378306.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus elongatus
  ORGANISM  Synechococcus elongatus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Synechococcus elongatus"
                     /db_xref="taxon:32046"
     Protein         1..393
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=42432
     Region          1..387
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mqlltfnags ssyklsgfei ttaaeqtdpv wqvqidwktd raatltqpgq pvqmldssdr
       61 rawleialet lpdrsaiaav vhrvvhggqq qapavvtpel katiaaaanl aplhnplnla
      121 gieqmeqlfg lampqiavfd tafhqqmpva aaiyggpyhw weqgyrrygf hgishqylae
      181 rcaqlsdrsl snlqlvtahl gngcslaair nghsvdtsmg fspleglvmg srsgtvdpgl
      241 llhllqqpdc spsqlstvln qqsgllglsg rsndvralai aadagdqrsq lalaafthsl
      301 rrhlgamlas ltrldalvfa ggigenyrsl wpavcehfag mpirldpeam avagdrrist
      361 pdsaitvwvi hsredwqmvq lalpllrspq sfn
//
LOCUS       WP_011379562             171 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Nitrosospira multiformis].
ACCESSION   WP_011379562
VERSION     WP_011379562.1
KEYWORDS    RefSeq.
SOURCE      Nitrosospira multiformis
  ORGANISM  Nitrosospira multiformis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosospira.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Nitrosospira multiformis"
                     /db_xref="taxon:1231"
     Protein         1..171
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=19008
     Region          24..103
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 maytdrdtyg myknygkegk gpgprlmgad tligedvynt rdedlgdike imldmnngki
       61 ayavlsfggl mgmgdklfav pwgaltldte nkrfildvdk erldsapgfd kddwpdmadt
      121 swqntinsyy gtktytessr tkqptdtpdt pyeqtpytti qssgmdsgrv k
//
LOCUS       WP_011379865             360 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein [Nitrosospira
            multiformis].
ACCESSION   WP_011379865
VERSION     WP_011379865.1
KEYWORDS    RefSeq.
SOURCE      Nitrosospira multiformis
  ORGANISM  Nitrosospira multiformis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosospira.
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 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Nitrosospira multiformis"
                     /db_xref="taxon:1231"
     Protein         1..360
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=40629
     Region          1..357
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 msieirnlsk qfgtfsalrd vslevksgel lallgpsgsg kttllrviag leaadtgqvl
       61 fqgedatdqh vrerqvgfvf qhyalfrnmt ifenvafglr vrpkkfrpst aeiqqrvhel
      121 lklvqldwla dryphqlsgg qrqrialara lavepkvlll depfgaldak vrkelrswlr
      181 rlhdemhits vfvthdqeea levadrvvvm negrieqigt pdevyehpas pfvykflgkv
      241 nlfhgrlhrg rawiggieid apehteaeel sgvayvrphd ihvdkvdhal ngegaiaahv
      301 shilsvgpvv rlqlvrddgk dkelieveis rerfrelqlt rgdqvfikps rfdlfpaqih
//
LOCUS       WP_011380847             140 aa            linear   BCT 20-JAN-2025
DEFINITION  PRC-barrel domain-containing protein [Nitrosospira multiformis].
ACCESSION   WP_011380847
VERSION     WP_011380847.1
KEYWORDS    RefSeq.
SOURCE      Nitrosospira multiformis
  ORGANISM  Nitrosospira multiformis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosospira.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The PRC-barrel: a widespread, conserved domain shared by
            photosynthetic reaction center subunits and proteins of RNA
            metabolism
  JOURNAL   Genome Biol 3 (11), RESEARCH0061 (2002)
   PUBMED   12429060
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10525995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Nitrosospira multiformis"
                     /db_xref="taxon:1231"
     Protein         1..140
                     /product="PRC-barrel domain-containing protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_process="GO:0019684 - photosynthesis, light reaction
                     [Evidence IEA]"
                     /calculated_mol_wt=15756
     Region          34..107
                     /region_name="PRC"
                     /note="PRC-barrel domain; pfam05239"
                     /db_xref="CDD:398765"
ORIGIN      
        1 msmsyeryey nihgldkivd gtnpmprfmg atwpigedvy nnkgeklgdi kevmldveeg
       61 rvayavlsfg gflgvgdklf avpwnaltlk lealdkrfil dvekerlesa pgfdkgnwpd
      121 madeswntri hayydnqkgg
//
LOCUS       WP_011381088              99 aa            linear   BCT 20-JAN-2025
DEFINITION  ComEA family DNA-binding protein [Nitrosospira multiformis].
ACCESSION   WP_011381088
VERSION     WP_011381088.1
KEYWORDS    RefSeq.
SOURCE      Nitrosospira multiformis
  ORGANISM  Nitrosospira multiformis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosospira.
REFERENCE   1  (residues 1 to 99)
  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   2  (residues 1 to 99)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446237
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Nitrosospira multiformis"
                     /db_xref="taxon:1231"
     Protein         1..99
                     /product="ComEA family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10436
     Region          10..74
                     /region_name="ComEA"
                     /note="DNA uptake protein ComE or related DNA-binding
                     protein [Replication, recombination and repair]; COG1555"
                     /db_xref="CDD:441164"
ORIGIN      
        1 mgklliiisa plifagsvha avnintatqq elqtlngits akaraiieyr skagkfrtae
       61 dltkvdginp ryldmkqlyk dvsvagptvl kvgakpagk
//
LOCUS       WP_011381668             448 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Nitrosospira
            multiformis].
ACCESSION   WP_011381668
VERSION     WP_011381668.1
KEYWORDS    RefSeq.
SOURCE      Nitrosospira multiformis
  ORGANISM  Nitrosospira multiformis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosospira.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 448)
  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 448)
  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 448)
  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 12807598
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Nitrosospira multiformis"
                     /db_xref="taxon:1231"
     Protein         1..448
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46284
     Region          20..87
                     /region_name="RodZ"
                     /note="Cytoskeletal protein RodZ, contains Xre-like HTH
                     and DUF4115 domains [Cell cycle control, cell division,
                     chromosome partitioning]; COG1426"
                     /db_xref="CDD:441035"
     Region          23..437
                     /region_name="PRK10856"
                     /note="cytoskeleton protein RodZ"
                     /db_xref="CDD:236776"
     Region          373..433
                     /region_name="DUF4115"
                     /note="Domain of unknown function (DUF4115); pfam13464"
                     /db_xref="CDD:433229"
ORIGIN      
        1 meapessdie qheepkktge qvgqvlraar lergldiedv arqlrfaarq vtaleedeyd
       61 klaggpflrg fvrnyakllq ldeapllkll eqsvppptth vgrppseeip fpsgqeylkr
      121 nvvlgggivl aitllgyaiy sgdkasvanq pdmamesekd tgqptlsfpf psqappaevp
      181 esqapapsal vpdmasqrep giaaleetap sadtgreqdt vasapkdaaa gsgaeasage
      241 pltlplappp avqtaptapa vpggepanvp vapkppqvtv apkpsegpvt skpsgsavtp
      301 kppqvavapk plegpvtsqp sesavtskpp qvavapkpse gaatskpses avtpkppqva
      361 atpkpppaka girltfages wvqvkdgngk lllsrvnppg seqvlrgkpp yslmignpgq
      421 vklvynskpv dlsifaklpg gmahlvlq
//
LOCUS       WP_011383301             226 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Paramagnetospirillum
            magneticum].
ACCESSION   WP_011383301
VERSION     WP_011383301.1
KEYWORDS    RefSeq.
SOURCE      Paramagnetospirillum magneticum
  ORGANISM  Paramagnetospirillum magneticum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Magnetospirillaceae; Paramagnetospirillum.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Paramagnetospirillum magneticum"
                     /db_xref="taxon:84159"
     Protein         1..226
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=24843
     Region          6..156
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mtiisrpspn feprpagaiv dtlvlhytgm esgeaalarl cdaqakvsah yvieedgrvf
       61 alvpedmraw hagasswrge pdvnsrsigi elvnpghefg yrafpgaqie slirlcrgil
      121 erhpiparnv vghsdvaptr kedpgelfpw adlaerhgig lwpcgeptpl ppehvllsgl
      181 ahvgydihdp katltafqrh frpwkvdglv deesvgrlrs llrivr
//
LOCUS       WP_011384258             297 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Paramagnetospirillum magneticum].
ACCESSION   WP_011384258
VERSION     WP_011384258.1
KEYWORDS    RefSeq.
SOURCE      Paramagnetospirillum magneticum
  ORGANISM  Paramagnetospirillum magneticum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Magnetospirillaceae; Paramagnetospirillum.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 297)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Paramagnetospirillum magneticum"
                     /db_xref="taxon:84159"
     Protein         1..297
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=32765
     Region          51..274
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
ORIGIN      
        1 msfmtnkdgs aiqfeqliah feersgaspl lehcvhfeda gavgrygdls lrsafqplfl
       61 adsmraaahe allrvdddrq rsispeqafr ipktperivh fdrlcrtiha infaaqagpd
      121 avlylnvdgr hllnvqggth gtffeallgh cglrpgqvvl eilesrindf grlteaiaay
      181 lqrgfgiaid dfgcrnsnfd rlwrlspdiv kldrslivqs tanprarkil pklveiihdl
      241 garvvcegie tvsqhslavd agvdmlqgyl yarpaerlqh rptspmagta arhppgf
//
LOCUS       WP_011384935             397 aa            linear   BCT 20-JAN-2025
DEFINITION  acetate/propionate family kinase [Paramagnetospirillum magneticum].
ACCESSION   WP_011384935
VERSION     WP_011384935.1
KEYWORDS    RefSeq.
SOURCE      Paramagnetospirillum magneticum
  ORGANISM  Paramagnetospirillum magneticum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Magnetospirillaceae; Paramagnetospirillum.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Chittori,S., Savithri,H.S. and Murthy,M.R.
  TITLE     Structural and mechanistic investigations on Salmonella typhimurium
            acetate kinase (AckA): identification of a putative ligand binding
            pocket at the dimeric interface
  JOURNAL   BMC Struct Biol 12, 24 (2012)
   PUBMED   23031654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Ingram-Smith,C., Martin,S.R. and Smith,K.S.
  TITLE     Acetate kinase: not just a bacterial enzyme
  JOURNAL   Trends Microbiol 14 (6), 249-253 (2006)
   PUBMED   16678422
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Hesslinger,C., Fairhurst,S.A. and Sawers,G.
  TITLE     Novel keto acid formate-lyase and propionate kinase enzymes are
            components of an anaerobic pathway in Escherichia coli that
            degrades L-threonine to propionate
  JOURNAL   Mol Microbiol 27 (2), 477-492 (1998)
   PUBMED   9484901
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S.
  TITLE     Identification and characterization of the ackA (acetate kinase
            A)-pta (phosphotransacetylase) operon and complementation analysis
            of acetate utilization by an ackA-pta deletion mutant of
            Escherichia coli
  JOURNAL   J Biochem 116 (4), 916-922 (1994)
   PUBMED   7883769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Paramagnetospirillum magneticum"
                     /db_xref="taxon:84159"
     Protein         1..397
                     /product="acetate/propionate family kinase"
                     /EC_number="2.7.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016774 - phosphotransferase activity,
                     carboxyl group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006082 - organic acid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43127
     Region          5..393
                     /region_name="AckA"
                     /note="Acetate kinase [Energy production and conversion];
                     COG0282"
                     /db_xref="CDD:440051"
ORIGIN      
        1 mregilvina gsssikfsly isngdekpll sckgqvegin vaphfiaksp hggvlneqrw
       61 pdqpnmshea lfkymiewie aqlgdaelka aghrvvhggs qysqpllvnd elmeelekli
      121 plaplhqphn lapiraltkv hpgltqvacf dtafhrsnpw taqsfalprk itgegvkryg
      181 fhglsyefia rqmrqlspaa argkvvvchl gsgasmcaid ggksvastmg ftavdglpmg
      241 trtgtmdagv ilyllqqkgm tpkeiedlly kqsgllgvsg vsndmrille ssephaaeav
      301 elfvyrisre lgslaaamgg ldalvftagi gerspqirer vcahaewlgv emdqeanqrd
      361 sllisaadsp vsvwviptde emmiakhtre llrslrd
//
LOCUS       WP_011384963             187 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter small permease subunit [Paramagnetospirillum
            magneticum].
ACCESSION   WP_011384963
VERSION     WP_011384963.1
KEYWORDS    RefSeq.
SOURCE      Paramagnetospirillum magneticum
  ORGANISM  Paramagnetospirillum magneticum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Magnetospirillaceae; Paramagnetospirillum.
REFERENCE   1  (residues 1 to 187)
  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 187)
  AUTHORS   Fischer,M., Zhang,Q.Y., Hubbard,R.E. and Thomas,G.H.
  TITLE     Caught in a TRAP: substrate-binding proteins in secondary transport
  JOURNAL   Trends Microbiol 18 (10), 471-478 (2010)
   PUBMED   20656493
REFERENCE   3  (residues 1 to 187)
  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   4  (residues 1 to 187)
  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   5  (residues 1 to 187)
  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 10008692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Paramagnetospirillum magneticum"
                     /db_xref="taxon:84159"
     Protein         1..187
                     /product="TRAP transporter small permease subunit"
                     /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=20850
     Region          4..172
                     /region_name="FcbT2"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, small permease component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4665"
                     /db_xref="CDD:443702"
ORIGIN      
        1 mkpllalssl idrinewvgr svywlillmv ivssgnatir yifsnssnaw levqwylfaa
       61 vfllcagytl lknehiridv iagrlprrtq iwidilgtlv flfpmallil tlswpmfmks
      121 ftmmemssda gglirwpvkl llpvgfsllm lqgvselikk iailtgdlad pgdhghhhht
      181 sadgeaa
//
LOCUS       WP_011387994             939 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Rhodospirillum rubrum].
ACCESSION   WP_011387994
VERSION     WP_011387994.1
KEYWORDS    RefSeq.
SOURCE      Rhodospirillum rubrum
  ORGANISM  Rhodospirillum rubrum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Rhodospirillaceae; Rhodospirillum.
REFERENCE   1  (residues 1 to 939)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..939
                     /organism="Rhodospirillum rubrum"
                     /db_xref="taxon:1085"
     Protein         1..939
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=105466
     Region          88..578
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 makeigvetl thkdakrvni ptaelqsvmq eevkspirva ydrrnrdldp qlvwrgkder
       61 dwselivqap plyiqekihp kvliddlkre srarakemvg atvdlfadfn glpdkeaate
      121 fyqhhanwtn rmilgdslsv maslaeregl rgkvqciyfd ppygikfnsn fqwsttsrdv
      181 kdgnkdhitr epeqvrafrd twrdgihtyl sylrdrltva rdlltdsgsi fvqigdenvh
      241 rvrmlmdevf gdenfisqis tktsggstge yisnvvdfil wysksrsyik frklnkskei
      301 geagsekytr irfdnlhsra ltpeerlsts svpcdgrvyr qdnmtsqsvg rdkgegaasw
      361 fpviisgsei kpslrvrwkt nqtgmdrllk aerleltgns isyvrfiddf sgiplsnswd
      421 diggiqsrld pkvyvvqtpt tviqrcilma sdpgdlvldp tcgsgstafv aeqwgrrwit
      481 idtsrvslal ararimgary pyylladsrd gqvkegqvtr tlpkdtpthg dirqgfvyer
      541 vphvmlsnia snseidviwd kaqetleplr tqlnaaldkt whdweiprea dkgwsaaaka
      601 lhaqwwdari rrqkeidasi aakaefeyly dkpyedkakv rvagpftves lsphrvlavd
      661 qndelvdllq aaegkgasks ldasdfaqmv ldnlksagvq qahkedriaf taltgwpgkf
      721 icakgvfreg dkdrsagivi gpefgtvsrl dlvtaareag dagfdvliac afnfdahsae
      781 fdklgairil karmnpdlhm ggdlkstgag nlfvvfgepd idiiitaddk vrvkikgvdi
      841 fhpstgeies ggpdtiavwf idtdyneesf fvrhayflga ddpykalktt lkaeidreaw
      901 dslnrdisrp fdkpksgria vkvinhlgde vmkvfsvdv
//
LOCUS       WP_011389349             540 aa            linear   BCT 20-JAN-2025
DEFINITION  EAL domain-containing protein [Rhodospirillum rubrum].
ACCESSION   WP_011389349
VERSION     WP_011389349.1
KEYWORDS    RefSeq.
SOURCE      Rhodospirillum rubrum
  ORGANISM  Rhodospirillum rubrum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Rhodospirillaceae; Rhodospirillum.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Chou,S.H. and Galperin,M.Y.
  TITLE     Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms
  JOURNAL   J Bacteriol 198 (1), 32-46 (2016)
   PUBMED   26055114
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Schirmer,T. and Jenal,U.
  TITLE     Structural and mechanistic determinants of c-di-GMP signalling
  JOURNAL   Nat Rev Microbiol 7 (10), 724-735 (2009)
   PUBMED   19756011
REFERENCE   3  (residues 1 to 540)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Rhodospirillum rubrum"
                     /db_xref="taxon:1085"
     Protein         1..540
                     /product="EAL domain-containing protein"
                     /EC_number="3.1.4.52"
                     /GO_function="GO:0071111 - cyclic-guanylate-specific
                     phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=58621
     Region          1..510
                     /region_name="EAL"
                     /note="EAL domain, c-di-GMP-specific phosphodiesterase
                     class I (or its enzymatically inactive variant) [Signal
                     transduction mechanisms]; COG2200"
                     /db_xref="CDD:441802"
ORIGIN      
        1 mqidsrdriv faagpfeafi drrqddlrge evatlmvped rvlmgqclkl vrrkgrasge
       61 vvrlyrprga plsmdfagyt ldqqsfialr ltshrgygar dgiprdpqsg llppqafsel
      121 asgkikqsqe tgqdfgvtvi dlpglgglcd rlpspgalgl lrsvgaslra cafddnsate
      181 iaqgryglvh dgaadlealr hdlseivrqh dpdgeegrve tsaidlegid qidegdlakg
      241 liyainqcqr adgaaislrm lstsipqlvh qginevalfr rvvanrsfdi vlqpivslst
      301 gdihhyealc rfdssrpdls pyraitfaee tglihdfdla maekvlgwls gkprnsdayr
      361 vavnisgfsi gvdsyvkgll dllraepwtk gkmlfeites skmtdldsan sfigslrdsg
      421 yqvclddfga gaasfqylsa levdvvkidg savrnamrgp kglaflsalt elcrrlgvtt
      481 iaemidtkes ldfvrscgcd fvqgylfgrp sadlksfqpl pnlgllrgsp drlrgragls
//
LOCUS       WP_011389512             282 aa            linear   BCT 20-JAN-2025
DEFINITION  phytoene/squalene synthase family protein [Rhodospirillum rubrum].
ACCESSION   WP_011389512
VERSION     WP_011389512.1
KEYWORDS    RefSeq.
SOURCE      Rhodospirillum rubrum
  ORGANISM  Rhodospirillum rubrum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Rhodospirillaceae; Rhodospirillum.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Lin,F.Y., Liu,Y.L., Li,K., Cao,R., Zhu,W., Axelson,J., Pang,R. and
            Oldfield,E.
  TITLE     Head-to-head prenyl tranferases: anti-infective drug targets
  JOURNAL   J Med Chem 55 (9), 4367-4372 (2012)
   PUBMED   22486710
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Lin,F.Y., Liu,C.I., Liu,Y.L., Zhang,Y., Wang,K., Jeng,W.Y.,
            Ko,T.P., Cao,R., Wang,A.H. and Oldfield,E.
  TITLE     Mechanism of action and inhibition of dehydrosqualene synthase
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21337-21342 (2010)
   PUBMED   21098670
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Liang,P.H., Ko,T.P. and Wang,A.H.
  TITLE     Structure, mechanism and function of prenyltransferases
  JOURNAL   Eur J Biochem 269 (14), 3339-3354 (2002)
   PUBMED   12135472
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Rhodospirillum rubrum"
                     /db_xref="taxon:1085"
     Protein         1..282
                     /product="phytoene/squalene synthase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30221
     Region          4..258
                     /region_name="ERG9"
                     /note="Phytoene/squalene synthetase [Lipid transport and
                     metabolism]; COG1562"
                     /db_xref="CDD:441170"
ORIGIN      
        1 maqaedlspl agavrdfdpn rfqtalfapa eqrenlmaly afnveiaria etvsealige
       61 mrlqwwhdlc egafsgavia rghpvgeame rliaggrldr ptlsaaiaar rldlaaepfa
      121 tpadlrgyae dtagglsrma aallgadpst iaaaghvgta wgllgvvrtl cpmaaqgrly
      181 lpsqladerg vtredlsapp vteaakalcl dlvgevedll aearalrrri drrhlspfll
      241 aplarpylal lrqsggdpad pglwtivrrp fslfwtgirg ri
//
LOCUS       WP_011389806             203 aa            linear   BCT 20-JAN-2025
DEFINITION  UbiX family flavin prenyltransferase [Rhodospirillum rubrum].
ACCESSION   WP_011389806
VERSION     WP_011389806.1
KEYWORDS    RefSeq.
SOURCE      Rhodospirillum rubrum
  ORGANISM  Rhodospirillum rubrum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Rhodospirillaceae; Rhodospirillum.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   White,M.D., Payne,K.A., Fisher,K., Marshall,S.A., Parker,D.,
            Rattray,N.J., Trivedi,D.K., Goodacre,R., Rigby,S.E., Scrutton,N.S.,
            Hay,S. and Leys,D.
  TITLE     UbiX is a flavin prenyltransferase required for bacterial
            ubiquinone biosynthesis
  JOURNAL   Nature 522 (7557), 502-506 (2015)
   PUBMED   26083743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Rhodospirillum rubrum"
                     /db_xref="taxon:1085"
     Protein         1..203
                     /product="UbiX family flavin prenyltransferase"
                     /EC_number="2.5.1.129"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0106141 - flavin prenyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21958
     Region          1..188
                     /region_name="UbiX"
                     /note="Flavin prenyltransferase UbiX [Coenzyme transport
                     and metabolism]; COG0163"
                     /db_xref="CDD:439933"
ORIGIN      
        1 mkrlivgisg asgvlygira lealrrlpdi eshlilspaa grtiveetdl gidqvtalad
       61 vvhshrdiga alasgsfrtl gmliapcsik tlsgivtcyd dnlmvraadv clkerrrlvl
      121 mvretplhag hidlmarata hgaiimppvp afyhrpktle dmvdhtvgra ldlfgidntl
      181 tkrwkdtppe qtalneapst qkl
//
LOCUS       WP_011389943              96 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Rhodospirillum rubrum].
ACCESSION   WP_011389943
VERSION     WP_011389943.1
KEYWORDS    RefSeq.
SOURCE      Rhodospirillum rubrum
  ORGANISM  Rhodospirillum rubrum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Rhodospirillaceae; Rhodospirillum.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Rhodospirillum rubrum"
                     /db_xref="taxon:1085"
     Protein         1..96
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10131
     Region          1..96
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mkpsvalelk rvavrecvgr srasnprvfg svlhgtdreg sdldllvdal pgttlfdlgg
       61 lqadledllg ipvdlrtpad lsgkfrshvl aeaqpl
//
LOCUS       WP_011390020             370 aa            linear   BCT 20-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter substrate-binding protein
            [Rhodospirillum rubrum].
ACCESSION   WP_011390020
VERSION     WP_011390020.1
KEYWORDS    RefSeq.
SOURCE      Rhodospirillum rubrum
  ORGANISM  Rhodospirillum rubrum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Rhodospirillaceae; Rhodospirillum.
REFERENCE   1  (residues 1 to 370)
  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 370)
  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   3  (residues 1 to 370)
  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   4  (residues 1 to 370)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   5  (residues 1 to 370)
  AUTHORS   Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L.
  TITLE     X-ray structures of the leucine-binding protein illustrate
            conformational changes and the basis of ligand specificity
  JOURNAL   J Biol Chem 279 (10), 8747-8752 (2004)
   PUBMED   14672931
REFERENCE   6  (residues 1 to 370)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   7  (residues 1 to 370)
  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 10156937
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Rhodospirillum rubrum"
                     /db_xref="taxon:1085"
     Protein         1..370
                     /product="branched-chain amino acid ABC transporter
                     substrate-binding protein"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - 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]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38404
     Region          29..360
                     /region_name="PBP1_ABC_LIVBP-like"
                     /note="type 1 periplasmic ligand-binding domain of ABC
                     (Atpase Binding Cassette)-type active transport systems
                     involved in the transport of all three branched chain
                     aliphatic amino acids (leucine, isoleucine and valine);
                     cd06342"
                     /db_xref="CDD:380565"
     Site            order(101..103,124..125,174,226,250)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380565"
ORIGIN      
        1 mrtlhkavfs vtvsalaisp lpaladipvg lalgltgqia aigeqsrrga eaaiaafnka
       61 gglkgetitl qveddacdpk qgvavankfv sagveavigh mctgptmaas tvyseeeipm
      121 vtasatgpdl tergltnvfr atgrddqqgt iagkmiaerf adqttaivhd kqaygrglae
      181 eakkamnaag keealfaaiv pgeqdfsali srlkqagvkv vyyggyyndl gqivrqsraq
      241 gldavfvggd glsssefwai tgeagegtlf tftpdastnp aakeaveafk adgkgdadnf
      301 ayyyyaaaqv ltqamakags adpeavtkal rdntfetvag pmdfdakgdl tapafvfyqw
      361 sagkpkpaaf
//
LOCUS       WP_011391150             356 aa            linear   BCT 20-JAN-2025
DEFINITION  sulfate/molybdate ABC transporter ATP-binding protein
            [Rhodospirillum rubrum].
ACCESSION   WP_011391150
VERSION     WP_011391150.1
KEYWORDS    RefSeq.
SOURCE      Rhodospirillum rubrum
  ORGANISM  Rhodospirillum rubrum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Rhodospirillaceae; Rhodospirillum.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Rhodospirillum rubrum"
                     /db_xref="taxon:1085"
     Protein         1..356
                     /product="sulfate/molybdate ABC transporter ATP-binding
                     protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015419 - ABC-type sulfate 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=38802
     Region          1..356
                     /region_name="CysA"
                     /note="ABC-type sulfate/molybdate transport systems,
                     ATPase component [Inorganic ion transport and metabolism];
                     COG1118"
                     /db_xref="CDD:440735"
ORIGIN      
        1 mridienirk tfrhgtaaal agvdlavasg elvallgpsg sgkttllrii aglefpdggr
       61 vlfdgedasa lpvrdrhvgf vfqqyalfrh mtvlenvafg lrvrprgtrp sdgeidrrvr
      121 dlltlvqleg legrypaqls ggqrqrvala ralaiepgvl lldepfgald arvrkdlrrw
      181 lrdlhdrtgh ttvfvthdqe ealeladrvv vfsqgrieqa gspvevydrp atpfvydflg
      241 svnrlpvevr dghvwlegha qplangqavd stglftlyar phdlgiadqt lpagdalpgi
      301 vaavrqagav vrldvrvagl dhlvevevsa gderwrawkt gspvalvpar fdlfpr
//
LOCUS       WP_011392263             685 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Neomoorella thermoacetica].
ACCESSION   WP_011392263
VERSION     WP_011392263.1
KEYWORDS    RefSeq.
SOURCE      Neomoorella thermoacetica (Moorella thermoacetica)
  ORGANISM  Neomoorella thermoacetica
            Bacteria; Bacillati; Bacillota; Clostridia; Neomoorellales;
            Neomoorellaceae; Neomoorella.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 685)
  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   3  (residues 1 to 685)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Neomoorella thermoacetica"
                     /db_xref="taxon:1525"
     Protein         1..685
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=74545
     Region          5..684
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
     Region          165..244
                     /region_name="P2"
                     /note="P2 response regulator binding domain; pfam07194"
                     /db_xref="CDD:462116"
ORIGIN      
        1 msdldmsqyl gifldeaeeq lqqldeavvq leqtpddqel lntifraaht lkgssasmgf
       61 nrlatlthrm esvldslrqg klavsreiid illasvdtlr alkdsiaagk geegdvnevv
      121 arleavlagp aapvankava naeltlddie qnviraaevk gfrayeirvq leagcqmksa
      181 raylvfnnlk elgeiiksvp htqdleaekf ddtftlafvs redadtlanv vksvseikdv
      241 lvrpivleed qpaaaragta pgkpgveaag gkngttapag ehhvnqtvrv dvqrlenlmn
      301 lvgelvidrt rltevgnglk nrlgneelle tleevslhig ritsdlqeei mkarmfpidq
      361 vfnrfprmvr dlarkagkei dfiiegrete ldrtvieeig dplihllrna idhgieepev
      421 rlrqgkprhg tvrlkafhqe nqivitvedd gagmdaekik akaiarglis pesaarlsrr
      481 ealdliflpg lstsdkvtdv sgrgvgmdiv rnhiekingt idirttpgkg tcftiklplt
      541 lainrsllvh vdgrvyafpl anvveiidvt pdsiqhvhrq qvvvvrgrvl pliylgqalg
      601 lgtpipaadt yavvivglae kqvgfivddl igeqeiviks lgnfigkipg iagatimgdg
      661 svalildvrs lmnfvgeead relas
//
LOCUS       WP_011392809             208 aa            linear   BCT 20-JAN-2025
DEFINITION  ANTAR domain-containing response regulator [Neomoorella
            thermoacetica].
ACCESSION   WP_011392809
VERSION     WP_011392809.1
KEYWORDS    RefSeq.
SOURCE      Neomoorella thermoacetica (Moorella thermoacetica)
  ORGANISM  Neomoorella thermoacetica
            Bacteria; Bacillati; Bacillota; Clostridia; Neomoorellales;
            Neomoorellaceae; Neomoorella.
REFERENCE   1  (residues 1 to 208)
  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 208)
  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   3  (residues 1 to 208)
  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   4  (residues 1 to 208)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 208)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 208)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Neomoorella thermoacetica"
                     /db_xref="taxon:1525"
     Protein         1..208
                     /product="ANTAR domain-containing response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=23105
     Region          1..194
                     /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"
ORIGIN      
        1 mqqakifiac adpsarqnlk ymlvregyli ageapdgsqa lrmirtlqpn lvildsdlqg
       61 tnalevarvi dedrvapiil lasswhrnli irtrdfpvfa ylikpvqest lipaveaala
      121 nyrrvtrleq eisklketla srkvverakg ilmdtmglte aeayrrlqrq smdrcvpmkt
      181 iaeaiivahe lqqgghkakn dsgnsgra
//
LOCUS       WP_011392526             359 aa            linear   BCT 20-JAN-2025
DEFINITION  GerAB/ArcD/ProY family transporter [Neomoorella thermoacetica].
ACCESSION   WP_011392526
VERSION     WP_011392526.1
KEYWORDS    RefSeq.
SOURCE      Neomoorella thermoacetica (Moorella thermoacetica)
  ORGANISM  Neomoorella thermoacetica
            Bacteria; Bacillati; Bacillota; Clostridia; Neomoorellales;
            Neomoorellaceae; Neomoorella.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Artzi,L., Alon,A., Brock,K.P., Green,A.G., Tam,A.,
            Ramirez-Guadiana,F.H., Marks,D., Kruse,A. and Rudner,D.Z.
  TITLE     Dormant spores sense amino acids through the B subunits of their
            germination receptors
  JOURNAL   Nat Commun 12 (1), 6842 (2021)
   PUBMED   34824238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Moir,A., Corfe,B.M. and Behravan,J.
  TITLE     Spore germination
  JOURNAL   Cell Mol Life Sci 59 (3), 403-409 (2002)
   PUBMED   11964118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Neomoorella thermoacetica"
                     /db_xref="taxon:1525"
     Protein         1..359
                     /product="GerAB/ArcD/ProY family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=39847
     Region          2..357
                     /region_name="GerAB"
                     /note="Spore germination receptor GerABC, GerB subunit
                     (amino acid transporter) [Cell cycle control, cell
                     division, chromosome partitioning]; COG5902"
                     /db_xref="CDD:444604"
ORIGIN      
        1 mrerigtnea tflivaamie vgtlkgarni vekvgvdtwl vspletifsl gaiylltalv
       61 mkfpdldlvg fsrrlvgkwl awllglivlv ywvgltaevg rvtadtikss llshtpdavv
      121 lssyllvaay lagkglepla rasiiivift lpitlllfal viprihldnf lpilphgpwp
      181 viklalwris naeemslfli lvpflkeprr awraasygfl tvmavvitii ttcqgvlgvd
      241 qlkytlipgl tvtqlaefag afierislif isvwiilvfp tasallwass yllgrllnlk
      301 dykmlafyql pvvyylawrp gnpfevksff fflqplglvv lvgipsllyl valfrcrar
//
LOCUS       WP_011392816             112 aa            linear   BCT 20-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Neomoorella
            thermoacetica].
ACCESSION   WP_011392816
VERSION     WP_011392816.1
KEYWORDS    RefSeq.
SOURCE      Neomoorella thermoacetica (Moorella thermoacetica)
  ORGANISM  Neomoorella thermoacetica
            Bacteria; Bacillati; Bacillota; Clostridia; Neomoorellales;
            Neomoorellaceae; Neomoorella.
REFERENCE   1  (residues 1 to 112)
  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 112)
  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 15193204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Neomoorella thermoacetica"
                     /db_xref="taxon:1525"
     Protein         1..112
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=12167
     Region          <3..112
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          70..110
                     /region_name="LysM"
                     /note="Lysin motif; smart00257"
                     /db_xref="CDD:197609"
ORIGIN      
        1 mgqkqvpcps grywrveagd tlyfialrvg ttvaelerln pgvnpynlqi gqvlclpdeq
       61 pcpsgvywqv apgdtlysia ratgttvekl lelnphinpy nlqvgqnicl pg
//
LOCUS       WP_011393801             114 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Neomoorella thermoacetica].
ACCESSION   WP_011393801
VERSION     WP_011393801.1
KEYWORDS    RefSeq.
SOURCE      Neomoorella thermoacetica (Moorella thermoacetica)
  ORGANISM  Neomoorella thermoacetica
            Bacteria; Bacillati; Bacillota; Clostridia; Neomoorellales;
            Neomoorellaceae; Neomoorella.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Neomoorella thermoacetica"
                     /db_xref="taxon:1525"
     Protein         1..114
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12992
     Region          23..114
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mtqefarlkr lldikreeel dkrralawqk arevasflrd vygvqqvily gslargdfqk
       61 msdidlyirg fegpywqmla ragrlaapfd vsivcaedal pslqeevare gvel
//
LOCUS       WP_011393409             744 aa            linear   BCT 20-JAN-2025
DEFINITION  molybdopterin oxidoreductase family protein [Neomoorella
            thermoacetica].
ACCESSION   WP_011393409
VERSION     WP_011393409.1
KEYWORDS    RefSeq.
SOURCE      Neomoorella thermoacetica (Moorella thermoacetica)
  ORGANISM  Neomoorella thermoacetica
            Bacteria; Bacillati; Bacillota; Clostridia; Neomoorellales;
            Neomoorellaceae; Neomoorella.
REFERENCE   1  (residues 1 to 744)
  AUTHORS   Allen,A.E., Booth,M.G., Frischer,M.E., Verity,P.G., Zehr,J.P. and
            Zani,S.
  TITLE     Diversity and detection of nitrate assimilation genes in marine
            bacteria
  JOURNAL   Appl Environ Microbiol 67 (11), 5343-5348 (2001)
   PUBMED   11679368
REFERENCE   2  (residues 1 to 744)
  AUTHORS   Boyington,J.C., Gladyshev,V.N., Khangulov,S.V., Stadtman,T.C. and
            Sun,P.D.
  TITLE     Crystal structure of formate dehydrogenase H: catalysis involving
            Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
  JOURNAL   Science 275 (5304), 1305-1308 (1997)
   PUBMED   9036855
REFERENCE   3  (residues 1 to 744)
  AUTHORS   Shuber,A.P., Orr,E.C., Recny,M.A., Schendel,P.F., May,H.D.,
            Schauer,N.L. and Ferry,J.G.
  TITLE     Cloning, expression, and nucleotide sequence of the formate
            dehydrogenase genes from Methanobacterium formicicum
  JOURNAL   J Biol Chem 261 (28), 12942-12947 (1986)
   PUBMED   3531194
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Neomoorella thermoacetica"
                     /db_xref="taxon:1525"
     Protein         1..744
                     /product="molybdopterin oxidoreductase family protein"
                     /EC_number="1.17.-.-"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=81328
     Region          18..730
                     /region_name="YjgC"
                     /note="Predicted molibdopterin-dependent oxidoreductase
                     YjgC [General function prediction only]; COG3383"
                     /db_xref="CDD:442610"
ORIGIN      
        1 maeleegivs lfqdrkgtav drwvattcgy cgtgcglylg ikddravavk adteaavnkg
       61 hlclkglyew ktlhhperak vplcrrgrem hpvtwekale etaerlrqal aaggpeavgi
      121 yhggqltlee yyaihklakg vlgtpnidan trlcmastvs gytrsfgvda ppgcyedldv
      181 srlvfifgan paemhpqlwq rilrnrklng arimvadprl tlparvadlr lrlrcgsnip
      241 llyglinili kedmldrdfi rratagfedl araaaafppe rvadltgvpa adivaaarlf
      301 grspsavtvf cqgvnqtsqa vdavtlinsl hlitgkigrp gsapfsltgq asalsmreig
      361 gggslpgfrn penpehrrqv adywgipeer lprrvndinr mlelidtgrl kvlwvigtnp
      421 avslpdlgfs rrqlekvfli vqdifypmet aafadiflpg agwgektgvv tnserrlnlv
      481 rravappgea rddlaivssv arylgagglf awqgpenafr elreltrgrp ndmtgvdyal
      541 lehlggvqwp cpeggrgtpr lytdgvfptr aeeaqgygef nhpegrarlw avpyapppev
      601 pdgefpfwln tgriiehyht rtrtkripel qalvpgayve inphdaarlk isegevvrvv
      661 srrgwievpa rltdvvapge vfvpfhfgdl dpgeggrqqa anhltgrnvd plsgqplakt
      721 gacrierqea gsmgqegqge ncsg
//
LOCUS       WP_011394442             695 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Hahella chejuensis].
ACCESSION   WP_011394442
VERSION     WP_011394442.1
KEYWORDS    RefSeq.
SOURCE      Hahella chejuensis
  ORGANISM  Hahella chejuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Hahellaceae; Hahella.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 695)
  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   3  (residues 1 to 695)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Hahella chejuensis"
                     /db_xref="taxon:158327"
     Protein         1..695
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=76146
     Region          3..683
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 msmdlsrfhd vffeesfeav ntieasllev dldapdpesi niifraahsi kggsatfgfs
       61 qvaaythvme nlldevragk rrltqpivdv llesvdamrl llssakasen ipeeeftqhk
      121 skleaisqdq aslttsnaaf tdsgaapaae sfdaddgvsg wrvvftphke mmqrgndplr
      181 larevaalae gdaeiecdls alpdwehfep lnsylgwtvr lrrpvdkaqi ddafawvede
      241 cdmaivpipk aqsapsqqam etlaepsapv deqaqasdkg aspaakqnkp amvaesqsir
      301 vdlekvdali nmvgelvitq smlnmlsede alqgmekllq gltqlkrqtr alqegvmqir
      361 mlpisfcfnr fprmvrdlsr qlgkdielml sgentevdkt viekitdplv hlvrnsvdhg
      421 iespadrtak gkpehgsvyl rayhqvgniv ieveddgkgl dpqvllskak rkgliagdai
      481 lseaqifeli flpgfstkee asdlsgrgvg mdvvkrnvqs lggsiqvese lnrrtrftir
      541 lpltlaimdg qlislgeely viplvtiies lqpdpsminr vagthetikl rgaylpvlrl
      601 sealdaaqne skkskpltdg iivivehesr rfglfvdell sqqqiviksl eenyrmipgv
      661 saatilgdgr valildvsgl sqlqkdsevs yadag
//
LOCUS       WP_011394156             355 aa            linear   BCT 20-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Hahella chejuensis].
ACCESSION   WP_011394156
VERSION     WP_011394156.1
KEYWORDS    RefSeq.
SOURCE      Hahella chejuensis
  ORGANISM  Hahella chejuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Hahellaceae; Hahella.
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   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   4  (residues 1 to 355)
  AUTHORS   Schwiebert,E.M.
  TITLE     ABC transporter-facilitated ATP conductive transport
  JOURNAL   Am J Physiol 276 (1), C1-C8 (1999)
   PUBMED   9886914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Hahella chejuensis"
                     /db_xref="taxon:158327"
     Protein         1..355
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.-"
                     /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=39032
     Region          1..353
                     /region_name="OpuBA"
                     /note="ABC-type proline/glycine betaine transport system,
                     ATPase component [Amino acid transport and metabolism];
                     COG1125"
                     /db_xref="CDD:440742"
ORIGIN      
        1 mirldnvsmq ygehyavrnl sldiasgdfc vlvgtsgcgk sttlkminrl aehskgrili
       61 nnqeiasfei ntlrrrigya iqsiglfphw nvakniavvp rllkwepqri qnrvnellel
      121 faldpaifae kmphelsggq aqrvgvaral aadpdillmd epfgaldpit reslqeemlr
      181 iqsqikktiv fvthdieeal klatrivvmd agqivqydtp enilhrpanp fveniigsqd
      241 rglkaasckq vreimrpdpp riqgvappcq gagrlwavdg anapvrllqa tvdgdasyrw
      301 reidvtpdmg lqaedsvkla iskmlwrkvg alpvlspdga llaevrmadl vggca
//
LOCUS       WP_011394899             695 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter permease [Hahella chejuensis].
ACCESSION   WP_011394899
VERSION     WP_011394899.1
KEYWORDS    RefSeq.
SOURCE      Hahella chejuensis
  ORGANISM  Hahella chejuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Hahellaceae; Hahella.
REFERENCE   1  (residues 1 to 695)
  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 695)
  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 695)
  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 695)
  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 11468699
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Hahella chejuensis"
                     /db_xref="taxon:158327"
     Protein         1..695
                     /product="TRAP transporter permease"
                     /GO_component="GO:0005886 - plasma 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=74419
     Region          15..686
                     /region_name="COG4666"
                     /note="TRAP-type uncharacterized transport system, fused
                     permease components [General function prediction only]"
                     /db_xref="CDD:443703"
ORIGIN      
        1 msqsatewsq lrdsrvffya avvvslihiv inmtgwisgf wpnvihfigf awlcvgwyva
       61 rdaskklklf nyslaaatta atlwlffsed tiyergfhlt wadwmagcvv vlasleltrr
      121 magwliptli iialgyvaww gqylpgvfrf sglsletimf rslfgddgmf gsiatisssf
      181 vmmfilfgaf lvrsgagdfi idlakrsagk mhggpgliav iasgltgtis gsavantast
      241 gvitiplmkk agysprfsag veaaastggq lmppimgaga fvmanytqip ytdivvvsfl
      301 pallyfltia afvrlqakke glkpieegsp eplsvlmkrg gysflipivl liglliwgls
      361 ptyaagfail aviaaswltp nrmgftaicd alalgaknmv mtalllisvg llvnvvattg
      421 igntfsfmiv qwaggqlwia illialaslv lgmglpvtaa yimvatiaap alqqlilqnq
      481 lvdllvagql petarvtlqf magvtdvdls qpipydqaaa lvggisrdil ptlldvaiap
      541 emitlallsa hmiifwlsqd snvtppvclt aftaaaiakt spmaaglsaw slakalyivp
      601 flfaytpfls gdwgealqif vfsafglyaf aavfvgwlgq alnpvmrllv fvaallllwp
      661 lslwwhlggl gmlialrlln rtrrssgdap riqtq
//
LOCUS       WP_011395736             261 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Hahella chejuensis].
ACCESSION   WP_011395736
VERSION     WP_011395736.1
KEYWORDS    RefSeq.
SOURCE      Hahella chejuensis
  ORGANISM  Hahella chejuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Hahellaceae; Hahella.
REFERENCE   1  (residues 1 to 261)
  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 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   3  (residues 1 to 261)
  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   4  (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   5  (residues 1 to 261)
  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 12820790
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Hahella chejuensis"
                     /db_xref="taxon:158327"
     Protein         1..261
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30047
     Region          15..258
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <155..254
                     /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 mlqanvislp qnvnrhkhth yqlvlgltgt aeidmcglaa rldvshaciv ptetfhdfyg
       61 rprnhvlvid ldqdypafld shhpdydlln pmferpqlvt ldrglqqltq vsiqeiqwaq
      121 ddralrhhla csiirclsrr ispsvkrqks pvldmhridq fiykhlheri cisdlagsic
      181 vserhfhelf kqatnqtphq yvirarldya krlmletnls iaeisqkcgf ssqsaltncm
      241 rkhdgltpkq vqkrsqqsdr m
//
LOCUS       WP_011396535             160 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase [Hahella chejuensis].
ACCESSION   WP_011396535
VERSION     WP_011396535.1
KEYWORDS    RefSeq.
SOURCE      Hahella chejuensis
  ORGANISM  Hahella chejuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Hahellaceae; Hahella.
REFERENCE   1  (residues 1 to 160)
  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 13014342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Hahella chejuensis"
                     /db_xref="taxon:158327"
     Protein         1..160
                     /product="L,D-transpeptidase"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=17468
     Region          5..158
                     /region_name="YkuD_like"
                     /note="L,D-transpeptidases/carboxypeptidases similar to
                     Bacillus YkuD; cl49639"
                     /db_xref="CDD:483979"
     Site            order(102,116,119,132..135,137)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341130"
ORIGIN      
        1 mslsivisvp sqtltlldag etveafsvst akagvgerng sgqtprgqhi irakigaqap
       61 lnavfrgrrw tgeiysqala etyperdwil trilwlsgtq kgfnrggdvd tmrryiylhg
      121 tpdsepmgep qshgcirmrn qdiirlfdrv apgtsvlieg
//
LOCUS       WP_011396832             273 aa            linear   BCT 20-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Hahella chejuensis].
ACCESSION   WP_011396832
VERSION     WP_011396832.1
KEYWORDS    RefSeq.
SOURCE      Hahella chejuensis
  ORGANISM  Hahella chejuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Hahellaceae; Hahella.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 273)
  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 12122938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Hahella chejuensis"
                     /db_xref="taxon:158327"
     Protein         1..273
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30766
     Region          6..101
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          186..261
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mitwkhqped afvsryiecy wflrkdqddi ahdspklnpc peahliiapp eqpytyglce
       61 relsgkgthl klpntssmtl hqaepfailg vkfkpgalys ianglaaidd visppgflae
      121 mpdllredvl knaadnavtv grnldawfka hsdciredrh srlardalal lattkasele
      181 tglyrslrav qrafvrvtgl tpkqyqimvr ldelllylyq qntesmswad vaaifgftdq
      241 phliryfkkl igdtphayrq aknltidayg dfd
//
LOCUS       WP_011397058             297 aa            linear   BCT 20-JAN-2025
DEFINITION  calcium-binding protein [Hahella chejuensis].
ACCESSION   WP_011397058
VERSION     WP_011397058.1
KEYWORDS    RefSeq.
SOURCE      Hahella chejuensis
  ORGANISM  Hahella chejuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Hahellaceae; Hahella.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Motlova,L., Klimova,N., Fiser,R., Sebo,P. and Bumba,L.
  TITLE     Continuous Assembly of beta-Roll Structures Is Implicated in the
            Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
  JOURNAL   J Mol Biol 432 (20), 5696-5710 (2020)
   PUBMED   32860773
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Bumba,L., Masin,J., Macek,P., Wald,T., Motlova,L., Bibova,I.,
            Klimova,N., Bednarova,L., Veverka,V., Kachala,M., Svergun,D.I.,
            Barinka,C. and Sebo,P.
  TITLE     Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets
            Translocation of RTX Proteins through Type I Secretion Ducts
  JOURNAL   Mol Cell 62 (1), 47-62 (2016)
   PUBMED   27058787
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Coote,J.G.
  TITLE     Structural and functional relationships among the RTX toxin
            determinants of gram-negative bacteria
  JOURNAL   FEMS Microbiol Rev 8 (2), 137-161 (1992)
   PUBMED   1558765
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458495
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Hahella chejuensis"
                     /db_xref="taxon:158327"
     Protein         1..297
                     /product="calcium-binding protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31394
     Region          <18..183
                     /region_name="COG2931"
                     /note="Ca2+-binding protein, RTX toxin-related [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442175"
ORIGIN      
        1 mnlsktwmat avslalfgga slaqadivig ndlnstegan aainqlysan rgsngggdqs
       61 lqfgdqiygt esndiliggl gidvlfgydg ddiiiggted fnsfnrdraf ggkgndifvw
      121 tpgdgndffd ggegqdilvi gligesqdnd gntdlapffn vsppgtpgsq dfdgifinpd
      181 vglpelrieq tpgfcrildk stegmselnl dhlvqfilrg pannfdeaia adpnidpdtl
      241 dtglrisvhl kntefvvcps rsgdeievyd isqtppvrvt lddlpptaat ssarlar
//
LOCUS       WP_011397665             349 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Hahella chejuensis].
ACCESSION   WP_011397665
VERSION     WP_011397665.1
KEYWORDS    RefSeq.
SOURCE      Hahella chejuensis
  ORGANISM  Hahella chejuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Hahellaceae; Hahella.
REFERENCE   1  (residues 1 to 349)
  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 349)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 349)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 349)
  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   5  (residues 1 to 349)
  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   6  (residues 1 to 349)
  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 11677366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Hahella chejuensis"
                     /db_xref="taxon:158327"
     Protein         1..349
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39558
     Region          44..224
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          109..347
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mnaiskeleq gfftqsvigd qpypsyelrn ilacleewgd aefvesvlkq vgldwerlwe
       61 epsmpthrll qtldlvrery atpglggaig qsytlaslge igvqvaacrt lgealvlver
      121 nydqlgvvmd ksltlqgdqv vvrhynvsgl nhetldflme iciaafftva revagfdfpl
      181 ryvsftrepp tdqkiyrlvf gdplrfsqpf iewafdvrll eapvrvrlpd sapmqeqpty
      241 lqftawdets lvqrisdmly arrgfpelpe iagrlnmspr tlrrrlatag inyqrllnri
      301 rcqqaiallq eeelavddia dqlgfteaan frhafkkwlg lppgavrsv
//
LOCUS       WP_011398383             106 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Hahella chejuensis].
ACCESSION   WP_011398383
VERSION     WP_011398383.1
KEYWORDS    RefSeq.
SOURCE      Hahella chejuensis
  ORGANISM  Hahella chejuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Hahellaceae; Hahella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Hahella chejuensis"
                     /db_xref="taxon:158327"
     Protein         1..106
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=11714
     Region          5..106
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(28,59..60,62,88)
                     /site_type="active"
                     /db_xref="CDD:119438"
     Site            order(28..29,37,40,42..43,45,48..49,51,59,64,73)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mselsqqekl qaiwfvvsqi ppgkvatygq vailaglpgl sryvgyamkq lpegssipwh
       61 rvinsqgkis fppkskaffr qqsvlthegi evhngrialk rfqwap
//
LOCUS       WP_011399015             157 aa            linear   BCT 20-JAN-2025
DEFINITION  pilin [Hahella chejuensis].
ACCESSION   WP_011399015
VERSION     WP_011399015.1
KEYWORDS    RefSeq.
SOURCE      Hahella chejuensis
  ORGANISM  Hahella chejuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Hahellaceae; Hahella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Hahella chejuensis"
                     /db_xref="taxon:158327"
     Protein         1..157
                     /product="pilin"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=16013
     Region          1..127
                     /region_name="PilA"
                     /note="Type IV pilus assembly protein, major pilin PilA
                     [Cell motility, Extracellular structures]; COG4969"
                     /db_xref="CDD:443995"
ORIGIN      
        1 mksiqkgftl ielmivvaii gilaavaipa yqdyiarsqv seavsltsav kgsmaeafqn
       61 tavrpglgev gavtsgkyva gmtvveittn rwavvatmkt agvnaniaga tfatatydgg
      121 qhwtcgsvav endgataftg asdnttvnnq ylpssck
//
LOCUS       WP_011400189             150 aa            linear   BCT 20-JAN-2025
DEFINITION  YqaA family protein [Hahella chejuensis].
ACCESSION   WP_011400189
VERSION     WP_011400189.1
KEYWORDS    RefSeq.
SOURCE      Hahella chejuensis
  ORGANISM  Hahella chejuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Hahellaceae; Hahella.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Inadome,H., Noda,Y., Kamimura,Y., Adachi,H. and Yoda,K.
  TITLE     Tvp38, Tvp23, Tvp18 and Tvp15: novel membrane proteins in the
            Tlg2-containing Golgi/endosome compartments of Saccharomyces
            cerevisiae
  JOURNAL   Exp Cell Res 313 (4), 688-697 (2007)
   PUBMED   17178117
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441035
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Hahella chejuensis"
                     /db_xref="taxon:158327"
     Protein         1..150
                     /product="YqaA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17117
     Region          3..140
                     /region_name="YqaA"
                     /note="Uncharacterized membrane protein YqaA, VTT domain
                     [Function unknown]; COG1238"
                     /db_xref="CDD:440851"
ORIGIN      
        1 meayfslffi aflaatlvpa yseimlagll atgydpallw vfatvgntlg svvnwalgry
       61 llhfkdrrwf pfkeknlgpa qrwfqrygvw sllmawaplf gdaltfiagl mrirlpifvf
      121 ltfagkgary aiivglfdqf etyflntdwf
//
LOCUS       WP_011400473             327 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Hahella chejuensis].
ACCESSION   WP_011400473
VERSION     WP_011400473.1
KEYWORDS    RefSeq.
SOURCE      Hahella chejuensis
  ORGANISM  Hahella chejuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Hahellaceae; Hahella.
REFERENCE   1  (residues 1 to 327)
  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 327)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 327)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 327)
  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   5  (residues 1 to 327)
  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   6  (residues 1 to 327)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Hahella chejuensis"
                     /db_xref="taxon:158327"
     Protein         1..327
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37118
     Region          17..199
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          79..325
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mrghyvavli dllvergvdr aeflkdcqlq edelnadtli dqrrleqvtr laaervqetg
       61 igllvgrrln vnthgalgya amasasyeqa lqllvkyyrv qapkayfelr trdgyyelac
      121 essftlperp wvttefliss iytsteflls grmqgveihl syaepphlel yreifqapvr
      181 frqtftgili pfsvarqplp sadpmaaslf tkrcesiqhd erdeqlprrv kemlyagage
      241 fpsqtelasr lhmsvstlhr klaeqgaayk allaevkkel alqhlrdsrl tvdeiaqllg
      301 fsdasnfrra fvgwtgetps efrkrsl
//
LOCUS       WP_011401435             368 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Burkholderia
            thailandensis].
ACCESSION   WP_011401435
VERSION     WP_011401435.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia thailandensis
  ORGANISM  Burkholderia thailandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 368)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Burkholderia thailandensis"
                     /db_xref="taxon:57975"
     Protein         1..368
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40327
     Region          4..331
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 msynvrmasl acnlpsrllr nddaafddve pipsewwqfw giesryvidp hageselama
       61 ertarqalar agvdageldl vlfnitspfv taddgarrfa prlsrtlrer lgarsaldad
      121 vemecasfvl qmqlatnlik qgrvkralvc ssermsavvd ytskssttfg dgaaaavlva
      181 dahdphgadw lnavyrsdat hydlatmqwr yprpaadrdd aerqaerfga yftlkpeaqe
      241 qiarfmpeai pdiverllrk tglraddida mvfhqpsdil vrawaqrlgl spdqyvirla
      301 dcaclvsaav plalyeslrr gvvkpgsqvv iagagagwgf gaqlwrwget vvtdaaptve
      361 aaesehaa
//
LOCUS       WP_011402046             150 aa            linear   BCT 20-JAN-2025
DEFINITION  type IV pilin protein [Burkholderia thailandensis].
ACCESSION   WP_011402046
VERSION     WP_011402046.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia thailandensis
  ORGANISM  Burkholderia thailandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Giltner,C.L., Habash,M. and Burrows,L.L.
  TITLE     Pseudomonas aeruginosa minor pilins are incorporated into type IV
            pili
  JOURNAL   J Mol Biol 398 (3), 444-461 (2010)
   PUBMED   20338182
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Russell,M.A. and Darzins,A.
  TITLE     The pilE gene product of Pseudomonas aeruginosa, required for pilus
            biogenesis, shares amino acid sequence identity with the N-termini
            of type 4 prepilin proteins
  JOURNAL   Mol Microbiol 13 (6), 973-985 (1994)
   PUBMED   7854130
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Burkholderia thailandensis"
                     /db_xref="taxon:57975"
     Protein         1..150
                     /product="type IV pilin protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=15540
     Region          6..113
                     /region_name="PilE"
                     /note="Type IV pilus assembly protein PilE [Cell motility,
                     Extracellular structures]; COG4968"
                     /db_xref="CDD:443994"
ORIGIN      
        1 mscierssrl rgftlievvv alaivavlaa favpsyrshv ergnrltaia alyraaqyvd
       61 afgdappaal pdgmnrapds grvvyvlrit lddarggyal easpaadgam qgdrcgvyvl
      121 hadgtrgnra aggaafdegv lgadvcwras
//
LOCUS       WP_011402621             339 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia thailandensis].
ACCESSION   WP_011402621
VERSION     WP_011402621.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia thailandensis
  ORGANISM  Burkholderia thailandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 339)
  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 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 339)
  AUTHORS   Schleif,R.
  TITLE     AraC protein: a love-hate relationship
  JOURNAL   Bioessays 25 (3), 274-282 (2003)
   PUBMED   12596232
REFERENCE   4  (residues 1 to 339)
  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   5  (residues 1 to 339)
  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   6  (residues 1 to 339)
  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 12117664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia thailandensis"
                     /db_xref="taxon:57975"
     Protein         1..339
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37964
     Region          33..216
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          108..337
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkpvamavtr taaqrpaplh tifitlevmk riglsretll egtgispsdv erpnamvtha
       61 qemvlfanal katgnsaigl higneipvta yglrahamlv sptlgdamrl afehpllgis
      121 yfrmkllidg evariivggy tyrhdllvin tdmcftairr qmidliggsp nftrigfayp
      181 kpshadsysd yfsclvifds einflefdas ilmtklpfah pieyevarka cekrefelah
      241 wmptdlvgql lclmyenpis qdvfefadrl gmslrslqrk lkdmgtsfsa lqdlvrqdia
      301 skyrtekhyt akeiaarlgy knasafsram rrwskvsvd
//
LOCUS       WP_011403413              95 aa            linear   BCT 20-JAN-2025
DEFINITION  nucleotidyltransferase family protein [Salinibacter ruber].
ACCESSION   WP_011403413
VERSION     WP_011403413.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     DNA polymerase beta-like nucleotidyltransferase superfamily:
            identification of three new families, classification and
            evolutionary history
  JOURNAL   Nucleic Acids Res 27 (7), 1609-1618 (1999)
   PUBMED   10075991
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..95
                     /product="nucleotidyltransferase family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10625
     Region          3..94
                     /region_name="MJ0435"
                     /note="Predicted nucleotidyltransferase MJ0435 [General
                     function prediction only]; COG1669"
                     /db_xref="CDD:441275"
ORIGIN      
        1 mtkvarehrt eilqlarehg aydvrlfgsv argedrpdsd ldllvrmedg rslldhvalk
       61 qdledllgrd vdvvteaslh pglrdrvlre avslq
//
LOCUS       WP_011403302             274 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: YaaA family protein [Salinibacter].
ACCESSION   WP_011403302
VERSION     WP_011403302.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter
  ORGANISM  Salinibacter
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Prahlad,J., Yuan,Y., Lin,J., Chang,C.W., Iwata-Reuyl,D., Liu,Y., de
            Crecy-Lagard,V. and Wilson,M.A.
  TITLE     The DUF328 family member YaaA is a DNA-binding protein with a novel
            fold
  JOURNAL   J Biol Chem 295 (41), 14236-14247 (2020)
   PUBMED   32796037
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Liu,Y., Bauer,S.C. and Imlay,J.A.
  TITLE     The YaaA protein of the Escherichia coli OxyR regulon lessens
            hydrogen peroxide toxicity by diminishing the amount of
            intracellular unincorporated iron
  JOURNAL   J Bacteriol 193 (9), 2186-2196 (2011)
   PUBMED   21378183
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006857
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Salinibacter"
                     /db_xref="taxon:146918"
     Protein         1..274
                     /product="YaaA family protein"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=31258
     Region          6..270
                     /region_name="YaaA"
                     /note="DNA-binding protein YaaA associated with the
                     oxidative stress response [Replication, recombination and
                     repair]; COG3022"
                     /db_xref="CDD:442258"
ORIGIN      
        1 mpdltvllsp adqkqpggnp fapdmfdyrt sgtfnyfddl npdrrelidt lqavvdeede
       61 ealgevfgve gyeleeairv ndeiydaplm saldrfspgv myaamdfanl ptgaqrrlle
      121 ngvilsglfg llrpddlipn yqlgmeaslp dvgpvadywr piispmlnes ledrwvwdll
      181 pevhrnawtd ehtytarvev qfervedger vpitgedlev qrgqfvnfiv qetaeemedl
      241 rewseeesde ltfdedasty dedtktweiv mvqd
//
LOCUS       WP_011407169             712 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor family protein [Xanthomonas].
ACCESSION   WP_011407169
VERSION     WP_011407169.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Yue,W.W., Grizot,S. and Buchanan,S.K.
  TITLE     Structural evidence for iron-free citrate and ferric citrate
            binding to the TonB-dependent outer membrane transporter FecA
  JOURNAL   J Mol Biol 332 (2), 353-368 (2003)
   PUBMED   12948487
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..712
                     /product="TonB-dependent receptor family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015343 - siderophore-iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0038023 - signaling receptor activity
                     [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=77228
     Region          22..710
                     /region_name="FecA"
                     /note="Outer membrane receptor for Fe3+-dicitrate
                     [Inorganic ion transport and metabolism]; COG4772"
                     /db_xref="CDD:443804"
ORIGIN      
        1 msrltvlaaa cglfatsatp pvlaadpapp astpiqrlpa vqvdaarvrg vddfdlpasf
       61 tvvsadddnr rgaqvselld gipglvardr qnyaqdtqls irgfgarstf gvrgvrllvd
      121 gipasmpdgq gqlshfnvlg aervevlrgp fsalygnssg gvlqlwsadg apndpwrlra
      181 tygsnatvdv gtqllgqqga vhynlaanhf etdgvrdhsr akrdsvnakl gfdlaegsrl
      241 dlvlnyldap daqdplgltr aqfnadpaha tsvatqfntr ksvrqsqaga iftqqfdnqa
      301 lrlmaydgqr sveqflaipl avqrnplhsg gvidldsnye gadarwawqg ealgrplqlt
      361 vgtnvdrqrq hrtgyenfvg dilgvkgalr rnqrdevqnv dqfaqlwwqw serwsallgv
      421 rhsdvrfasd dhytvgrnpd dsgqreysat tpvagivfra dedlrfyasl grgfetptfn
      481 elgyrsdgga glaldlgaat srnvevgskw raqsgaavef alfradtdde lavasntngr
      541 styrniratr rqgaelswhq pigatqqlql aytfvdatvr dgyltcassg catptvpvan
      601 garlpgvprq qlfarwqwqp aqwrfaaesv asgatvvndl aterapgdal vnleasrrwt
      661 ttlgalrtfa rvdnvldrqy vgsvivndgn gryyepgpdr tytvglqwdf gg
//
LOCUS       WP_011407408             306 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: SPOR domain-containing protein [Xanthomonas].
ACCESSION   WP_011407408
VERSION     WP_011407408.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..306
                     /product="SPOR domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30325
     Region          197..262
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 myvralivvl ivlnagvalw walqpppapp pappqptgva rlellptlpg vggaaltgaa
       61 aatgsasaae sestasatpa tpastpvsaa vpaptpaavv stststpast tsasavaaet
      121 phaaaepsvt tktaakpads vaatatkpsp ttpspaperc aslgpfvara dadaalarvr
      181 gqasrasvre dkdagvstfr vmlpnvgdra aaqalvkria aagmgdyyvi aqgedntval
      241 gqyqsrerae rrqaslvgag fpaqlvpsgs gqsrwwidvr ssaatsalqg aagaarqrsl
      301 dcaalr
//
LOCUS       WP_011407596             160 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [Xanthomonas].
ACCESSION   WP_011407596
VERSION     WP_011407596.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Hurley,J.H.
  TITLE     GAF domains: cyclic nucleotides come full circle
  JOURNAL   Sci STKE 2003 (164), PE1 (2003)
   PUBMED   12518043
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005003
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..160
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16882
     Region          8..160
                     /region_name="MsrC"
                     /note="GAF domain-containing protein, putative
                     methionine-R-sulfoxide reductase [Defense mechanisms,
                     Signal transduction mechanisms]; COG1956"
                     /db_xref="CDD:441559"
ORIGIN      
        1 mfatssltgs kpeqyaqlta qaqalvhgep drianaanla alifhslpsl nwagfyfydg
       61 relvvgpfqg lpacvripld kgvcgaaast rqsqriadvd afpghiacds asrselvipl
      121 vkgdtligvl dldspeldrf daddqrglea iaqlfvdala
//
LOCUS       WP_011409040             358 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: acyltransferase family protein [Xanthomonas].
ACCESSION   WP_011409040
VERSION     WP_011409040.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            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 10007593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..358
                     /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=38726
     Region          22..301
                     /region_name="NolL"
                     /note="Fucose 4-O-acetylase or related acetyltransferase
                     [Carbohydrate transport and metabolism]; COG3594"
                     /db_xref="CDD:442813"
ORIGIN      
        1 mtselspthg arvhssadar ptrdwqidaa kavaialvvl ghasgmppay klfaysfhvp
       61 lffvlsgwvg erfgqraltg atvaklgrtl lvpylaffmv ayalwllsaa mdghaghpqt
      121 rplwhpltgl lwangsrlyv lpalwflpal fvtmlayial rarlsaaava aisltlalaw
      181 agwfpslqlr lplaldvlpv alffiaiggw lsrfaealrs lgaqvwalal lplaavwwwl
      241 agwngqvdvn nlqfgqsaav fllvsllgta mtfcvayfir gmrwvqwigt ntllilctht
      301 lvflvatsvv artgliarsa igtpawalgl safaitmsvp mravlvrgap wmlglkrk
//
LOCUS       WP_011408613             191 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Xanthomonas].
ACCESSION   WP_011408613
VERSION     WP_011408613.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas
  ORGANISM  Xanthomonas
            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 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Xanthomonas"
                     /db_xref="taxon:338"
     Protein         1..191
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=21406
     Region          1..186
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 msdavlpspp ityaplsyes rlttraltqi dmvvihctel pdmamareyg ervlydsgtg
       61 nsghyyldrn gsiqqyvale rvahhvrghn lhtlgielvn rgryphwlds rhqemtepyp
      121 eaqiaalisl lqwlqqqlps vrriaghqal dttqqaasda parniqrkld pgplfpwpri
      181 eaavswshtp g
//
LOCUS       WP_011409081             135 aa            linear   BCT 20-JAN-2025
DEFINITION  MGMT family protein [Xanthomonas oryzae].
ACCESSION   WP_011409081
VERSION     WP_011409081.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..135
                     /product="MGMT family protein"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /calculated_mol_wt=14156
     Site            order(32,50..51,59,62,64..65,67,70..71,73,80,85,94)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:119438"
     Region          34..135
                     /region_name="Atl1"
                     /note="Alkylated DNA nucleotide flippase Atl1,
                     participates in nucleotide excision repair, Ada-like
                     DNA-binding domain [Transcription]; COG3695"
                     /db_xref="CDD:442910"
     Site            order(50,80..81,83,109)
                     /site_type="active"
                     /db_xref="CDD:119438"
ORIGIN      
        1 mskspqpttr psaspaarag skgqslsgeq arlrilevir aipvgevagy gdvaqraglp
       61 ararlvarvl ggnddpqlpw hrvlrsdgri afpggsagyr eqcqrlraeg vqvaqgrvrr
      121 asaaqrldaa vwgps
//
LOCUS       WP_011409549             268 aa            linear   BCT 20-JAN-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase [Xanthomonas oryzae].
ACCESSION   WP_011409549
VERSION     WP_011409549.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..268
                     /product="N-acetylmuramoyl-L-alanine amidase"
                     /EC_number="3.5.1.28"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine
                     amidase activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=29096
     Region          37..184
                     /region_name="AmpD"
                     /note="N-acetyl-anhydromuramyl-L-alanine amidase AmpD
                     [Cell wall/membrane/envelope biogenesis]; COG3023"
                     /db_xref="CDD:442259"
ORIGIN      
        1 mlpsfpfsss awlraavclv alslgacaha pernplarwv pspnndmrrp ilivlhfteq
       61 hsvqqsvstl rgrnsggwvs ahyligkdgq ryqlvsdaqr awhggagrwg titdinsasi
      121 gieldndgse pfapaqidsl lvllddlcnr lriprtqivg hedvaptrrn dpgplfpwkr
      181 laeagfgrwp aadapaapas fdpwqalami gysiddpaat lqafhhhyrg hsattldaed
      241 lrilsaltkg artssprpal epiegdnr
//
LOCUS       WP_011412461             498 aa            linear   BCT 20-JAN-2025
DEFINITION  replicative DNA helicase [Aster yellows witches'-broom
            phytoplasma].
ACCESSION   WP_011412461
VERSION     WP_011412461.1
KEYWORDS    RefSeq.
SOURCE      Aster yellows witches'-broom phytoplasma
  ORGANISM  Aster yellows witches'-broom phytoplasma
            Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Acholeplasmatales;
            Acholeplasmataceae; Candidatus Phytoplasma; 16SrI (Aster yellows
            group).
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Aster yellows witches'-broom phytoplasma"
                     /db_xref="taxon:229545"
     Protein         1..498
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=58608
     Region          22..486
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mltneqkalk qlinyieqgq weklnlycqi inpknllnpk ntkiftalky lflekqtshp
       61 wdklttkpii ikelltylqt hfpqdnftld slnylnddfn nqnnnhvldn lkhtytqekl
      121 fqqlikiisp tyenqdpyhk nlyyqeifdk lrnfissiph kndkthftln qmaslhpeff
      181 dtdnqskqki qeeyyrlset fkglnqstkg fkkgqiitig gytglgkttf vynllldiak
      241 tkhkeishyp hilvfsyemt leenlnrlla hqtqipldvi ldknfedani tplkytermk
      301 iakqffanin lsfsydkskn idyvidlvyr fylekqaeii vidhlqitkt tnhlendrla
      361 ideimtklkk laielnivii ilsqfsrdty snyqgkspei talkgsggie tnsdivlmms
      421 efkpklskdk ekpiniynst leelysdynd nenqkiievc ikknrsgtkk tliyhfemtt
      481 qtfqeigyvl pykietyy
//
LOCUS       WP_011411715             260 aa            linear   BCT 20-JAN-2025
DEFINITION  formate/nitrite transporter family protein [Sodalis glossinidius].
ACCESSION   WP_011411715
VERSION     WP_011411715.1
KEYWORDS    RefSeq.
SOURCE      Sodalis glossinidius
  ORGANISM  Sodalis glossinidius
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Bruguierivoracaceae; Sodalis.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Helmstetter,F., Arnold,P., Hoger,B., Petersen,L.M. and Beitz,E.
  TITLE     Formate-nitrite transporters carrying nonprotonatable amide amino
            acids instead of a central histidine maintain pH-dependent
            transport
  JOURNAL   J Biol Chem 294 (2), 623-631 (2019)
   PUBMED   30455351
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Wiechert,M. and Beitz,E.
  TITLE     Formate-nitrite transporters: Monoacids ride the dielectric slide
  JOURNAL   Channels (Austin) 11 (5), 365-367 (2017)
   PUBMED   28494190
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Mukherjee,M., Vajpai,M. and Sankararamakrishnan,R.
  TITLE     Anion-selective Formate/nitrite transporters: taxonomic
            distribution, phylogenetic analysis and subfamily-specific
            conservation pattern in prokaryotes
  JOURNAL   BMC Genomics 18 (1), 560 (2017)
   PUBMED   28738779
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Lu,W., Du,J., Schwarzer,N.J., Wacker,T., Andrade,S.L. and Einsle,O.
  TITLE     The formate/nitrite transporter family of anion channels
  JOURNAL   Biol Chem 394 (6), 715-727 (2013)
   PUBMED   23380538
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Sodalis glossinidius"
                     /db_xref="taxon:63612"
     Protein         1..260
                     /product="formate/nitrite transporter family protein"
                     /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=27622
     Region          2..252
                     /region_name="FocA"
                     /note="Formate/nitrite transporter FocA, FNT family
                     [Inorganic ion transport and metabolism]; COG2116"
                     /db_xref="CDD:441719"
ORIGIN      
        1 msfyspkeva aiamhtgvtk sqaslpvlvv lgimagafia lgflldihvv ssmppawgsf
       61 gvflgasvfp vglvltvlag gelltgnmmt lpmalfsrqi gvlalirnwf wvtlanfigs
      121 lmiawffghi lgmtegafla ktvaianaki sadfthafis aigcnwlvsl avwlayaakd
      181 magkilgiwf pimafvdlgf qhvvanmfvi paaifagqat whdyfinfpp vflgnavggg
      241 ifvaliyfia yrplggksha
//
LOCUS       WP_011412502             498 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: replicative DNA helicase [16SrI (Aster yellows
            group)].
ACCESSION   WP_011412502
VERSION     WP_011412502.1
KEYWORDS    RefSeq.
SOURCE      16SrI (Aster yellows group)
  ORGANISM  16SrI (Aster yellows group)
            Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Acholeplasmatales;
            Acholeplasmataceae; Candidatus Phytoplasma.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Egelman,E.H.
  TITLE     Bacterial helicases
  JOURNAL   J Struct Biol 124 (2-3), 123-128 (1998)
   PUBMED   10049800
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416751
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="16SrI (Aster yellows group)"
                     /db_xref="taxon:3042590"
     Protein         1..498
                     /product="replicative DNA helicase"
                     /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:0006269 - DNA replication, synthesis of
                     primer [Evidence IEA]"
                     /calculated_mol_wt=58526
     Region          22..486
                     /region_name="DnaB"
                     /note="Replicative DNA helicase [Replication,
                     recombination and repair]; COG0305"
                     /db_xref="CDD:440074"
ORIGIN      
        1 mltneqkalk qlinyieqgq weklnlycqi inpktlldpq nkkifttlky lflekqtthp
       61 wdkiksqtdi ikelltylqt nfqqdnftke slsflnndfs kennldfldn lkhtytqekl
      121 fqqllkiisp sfetqdpytk nlyyqeifdk lrnfissiph kndkthftln qmaslhteff
      181 atdnqakqki qeeyyrlsei fkglnqstkg fkksqiitig gytglgkttf vynllldiak
      241 tkhqesscyp hilvfsyemt meenlsrlla hqtqipldvi ldknledsni tpqqytermk
      301 qakqffvnin lsfsydkskn idyiidlvyr lylekqveii vidhlqitka snhlendrla
      361 ideimtklkq lamelniiii ilsqfsrdty snyqgkspei talkgsggie tnsdivlmms
      421 efrpklakdq ekplniynst lnqlylesdd nenqkiievc ikknrsgnkk tliyhfemst
      481 qtfqeigyvl pykietyy
//
LOCUS       WP_011413694             517 aa            linear   BCT 20-JAN-2025
DEFINITION  amidohydrolase family protein [Erythrobacter litoralis].
ACCESSION   WP_011413694
VERSION     WP_011413694.1
KEYWORDS    RefSeq.
SOURCE      Erythrobacter litoralis
  ORGANISM  Erythrobacter litoralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Erythrobacter/Porphyrobacter
            group; Erythrobacter.
REFERENCE   1  (residues 1 to 517)
  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 11440812
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Erythrobacter litoralis"
                     /db_xref="taxon:39960"
     Protein         1..517
                     /product="amidohydrolase family protein"
                     /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=56472
     Region          40..498
                     /region_name="HutI"
                     /note="Imidazolonepropionase or related amidohydrolase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG1228"
                     /db_xref="CDD:440841"
ORIGIN      
        1 mrilksicla mlaalaapaf aqgmervpdr pvgegqgpyg sllikgatmi dgsgappegp
       61 vdilvegnri ariargganl sadrtidatg mfvmpgmvdv hghngdpdka pqpsygfklw
      121 lahgvtsvrg vgfgfgpddp sldqkrrsaa ntitaprlfa ytvpggswts gavqtpaqgr
      181 awtrwakaqg ydgikffnse dpatlaaild eaeqqglgtv ahlgqrgvaq vnarkavelg
      241 ldgithfygh mesllddrst pdypadynyl deqsrfawva rleaqavepg sekwdeyidf
      301 lvengvtlsp tfniyaasrd vmrartlewh erytlpslmn fyepsltnhg syyhdwtsed
      361 eaawkrfyak wfaltrdfkn kggrvtagsd pgyiyqtwgf ayvaelemlr eagltpmevi
      421 qaatingare iydpkgsapp fgmiregmla dlaivdgnpl enlkvlygtg hrrlnretnq
      481 letvggvrwt ikdgivfdar alladvaqmv eaqkaar
//
LOCUS       WP_011413978             425 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Erythrobacter litoralis].
ACCESSION   WP_011413978
VERSION     WP_011413978.1
KEYWORDS    RefSeq.
SOURCE      Erythrobacter litoralis
  ORGANISM  Erythrobacter litoralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Erythrobacter/Porphyrobacter
            group; Erythrobacter.
REFERENCE   1  (residues 1 to 425)
  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 11465564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Erythrobacter litoralis"
                     /db_xref="taxon:39960"
     Protein         1..425
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /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=44990
     Region          <86..138
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          296..423
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mrvallatls tfalvacgps aesgdsseqq taaaetndyg yetysddnla dtmasnddry
       61 mdesgsdags edatptdlpd seerpimqaq vvldragfgp gvidgkmgms tenallgfqe
      121 andletsgkl ddatkealkd weripatrvv tiptswsdat ysdipddtaa kakmerlgyr
      181 sldervaerf httvdvlkrl npngkpagsq tgtgsqgnsg aegaddrsss atpsstssst
      241 ggasktsegf fragqqirvp nigadriapg sledtdwqrt laslgvgteq pevdrivvsk
      301 sedtlkaykg dtlvamftvs sgssefplpl gewdivgeay nppysydpev lgqgegetyt
      361 lppgpngmvg vvwidlskeh ygihgtpepe tigraqssgc vrltnwdaar lsqmvstdta
      421 vefva
//
LOCUS       WP_011414313             144 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Erythrobacter litoralis].
ACCESSION   WP_011414313
VERSION     WP_011414313.1
KEYWORDS    RefSeq.
SOURCE      Erythrobacter litoralis
  ORGANISM  Erythrobacter litoralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Erythrobacter/Porphyrobacter
            group; Erythrobacter.
REFERENCE   1  (residues 1 to 144)
  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 144)
  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   3  (residues 1 to 144)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Erythrobacter litoralis"
                     /db_xref="taxon:39960"
     Protein         1..144
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=16259
     Region          15..117
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mitgtrdsvk larkmrsemt lpegklwiel rkrpggykfr rqhpagqfvl dfycaaarla
       61 ievdgqahdc eavvdrdkrr sawlrdrgia mtriparlil qdieavvtrl veicdarrve
      121 lkrkaraplh hpadgpppqi geeg
//
LOCUS       WP_011415231             119 aa            linear   BCT 20-JAN-2025
DEFINITION  endonuclease domain-containing protein [Erythrobacter litoralis].
ACCESSION   WP_011415231
VERSION     WP_011415231.1
KEYWORDS    RefSeq.
SOURCE      Erythrobacter litoralis
  ORGANISM  Erythrobacter litoralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Erythrobacter/Porphyrobacter
            group; Erythrobacter.
REFERENCE   1  (residues 1 to 119)
  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 119)
  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   3  (residues 1 to 119)
  AUTHORS   Kinch,L.N., Ginalski,K., Rychlewski,L. and Grishin,N.V.
  TITLE     Identification of novel restriction endonuclease-like fold families
            among hypothetical proteins
  JOURNAL   Nucleic Acids Res 33 (11), 3598-3605 (2005)
   PUBMED   15972856
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789861
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Erythrobacter litoralis"
                     /db_xref="taxon:39960"
     Protein         1..119
                     /product="endonuclease domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=13747
     Region          15..115
                     /region_name="YcjD"
                     /note="Very-short-patch-repair endonuclease [Replication,
                     recombination and repair]; COG2852"
                     /db_xref="CDD:442100"
ORIGIN      
        1 mptwnprntk rarklrntat paeqrlwqhl srsqpgakfs rqmpvgpwya dflcrelklv
       61 ieldgfshdv qpdrderrda dlrelgyhvl hftnadvmnn tegvviaiqr kiadlrglk
//
LOCUS       WP_011417103             735 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Syntrophus aciditrophicus].
ACCESSION   WP_011417103
VERSION     WP_011417103.1
KEYWORDS    RefSeq.
SOURCE      Syntrophus aciditrophicus
  ORGANISM  Syntrophus aciditrophicus
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Syntrophia;
            Syntrophales; Syntrophaceae; Syntrophus.
REFERENCE   1  (residues 1 to 735)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 735)
  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   3  (residues 1 to 735)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..735
                     /organism="Syntrophus aciditrophicus"
                     /db_xref="taxon:316277"
     Protein         1..735
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=81832
     Region          149..734
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mnyetllksi dcmasdflfl dsgdmdvptt gkflnhlenv arealnlnim piqevgrgln
       61 sileciilds iedkeaailt feqgiallqe ivnveknqgk yqgdirgyle riafvtgtsi
      121 sssdkeivde vqaskekita agaseefliq desllrdfia egmeyveeie vnilnlennp
      181 enrdyinaif rpfhsikgva sflnlekire lshnieslld karngehsvt pplidvvldg
      241 adalksmisr lkealegkke npldvdlsal emrihninkg ieqepsvkkl geiliddgvl
      301 seqmleeglk akennpekrl getlikerav tpkqvsqalr kqaeqitdms tirvdtrkld
      361 dlidmvgelv itqsmvqqni snqengnkdl arnvsqlfri tsnlqkvsts lrmipikqtf
      421 qrmarlardv sknvgkavvv emegedteld rnmvdeiynp lvhmirnsvd hgletpeerv
      481 rcgkpekgli qlkayhrggn fvieisddgr glnrekilkk aiqnhlvnsv egltdqeiyr
      541 miflpgfsta ekvtdvsgrg vgmdvvrqti eklrgkieie sipgkgttfi trfpltmaii
      601 dgmivkvgke rfilpttair qvlrptresh nhivgqgetv nvmgrlmplv rvydlfdiep
      661 ekvdpwdaiv ivvdgasrsk cllvdqiigk aevvikslge glkdidgisg gaimgdgqig
      721 liidpeglfe lsehc
//
LOCUS       WP_011417516             225 aa            linear   BCT 20-JAN-2025
DEFINITION  YfgM family protein [Syntrophus aciditrophicus].
ACCESSION   WP_011417516
VERSION     WP_011417516.1
KEYWORDS    RefSeq.
SOURCE      Syntrophus aciditrophicus
  ORGANISM  Syntrophus aciditrophicus
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Syntrophia;
            Syntrophales; Syntrophaceae; Syntrophus.
REFERENCE   1  (residues 1 to 225)
  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 225)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 225)
  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 11459477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Syntrophus aciditrophicus"
                     /db_xref="taxon:316277"
     Protein         1..225
                     /product="YfgM family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0044877 - protein-containing complex
                     binding [Evidence IEA]"
                     /calculated_mol_wt=26080
     Region          50..224
                     /region_name="YfgM"
                     /note="Putative negative regulator of RcsB-dependent
                     stress response, UPF0070 family [Signal transduction
                     mechanisms]; COG2976"
                     /db_xref="CDD:442215"
     Site            order(107..108,111..112,114,142,145..146,149..150,
                     152..153,179,182..183,186..187,190)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          107..135
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          140..170
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          175..206
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mtkkailgei ekpdyfqrfi anisqfyvln krkvltiaav vilvlmivvg wftykyynek
       61 kaweeyaeie ktavlqesav nsdilikkyr dlsskfsgsq asqlsdyrlg nlyfknndid
      121 saiksyekfi anasdenefk vlsysslayc yeskkdyqka lkalqqaekv eagkyfgtfl
      181 yrdmgrlyek mqnrsealkf yrkaleqsid ptvtlfikrk iatls
//
LOCUS       WP_011417541             643 aa            linear   BCT 20-JAN-2025
DEFINITION  site-specific DNA-methyltransferase [Syntrophus aciditrophicus].
ACCESSION   WP_011417541
VERSION     WP_011417541.1
KEYWORDS    RefSeq.
SOURCE      Syntrophus aciditrophicus
  ORGANISM  Syntrophus aciditrophicus
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Syntrophia;
            Syntrophales; Syntrophaceae; Syntrophus.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Cheng,X. and Roberts,R.J.
  TITLE     AdoMet-dependent methylation, DNA methyltransferases and base
            flipping
  JOURNAL   Nucleic Acids Res 29 (18), 3784-3795 (2001)
   PUBMED   11557810
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Syntrophus aciditrophicus"
                     /db_xref="taxon:316277"
     Protein         1..643
                     /product="site-specific DNA-methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006306 - obsolete DNA methylation
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=73126
     Region          64..580
                     /region_name="Mod"
                     /note="Adenine specific DNA methylase Mod [Replication,
                     recombination and repair]; COG2189"
                     /db_xref="CDD:441792"
ORIGIN      
        1 mmekmkmhsp nltqeniari lemfpgcvte aqgqdgklkl avdfdllrqe lsesivegpq
       61 eryhlnwpgk realltanap iaktlrpcre esvdfdttkn lfiegdnlea lkllqetylg
      121 kvkmiyvdpp yntgndfiye ddfsensdef lkrsnqkdee gnrliantea ngrfhsdwls
      181 miyprlklar nllrddgvif isiddnevtn lqracdeifg ganfvaqlti ivkpegrryg
      241 ffakthdyil vycknheyas mneilvegle hphsddqggf tlkglrnrnv qafnstnrpn
      301 lrypffvdkq npdangffkv stipldrfvk veastvdglk svwrwskeks ekekdslvay
      361 egndgeirif qkerklsqma ktvlsdkeii snkgtrelqv llgkgifdfp kpvaliklit
      421 tigsdehsli ldffsgsatt ahaviqlnae dggnrkfimv qlpepcdeks eafkagykti
      481 aeiskerirr agrktlegec hedwnkdigf rvlkidssnm advyytpdai eqgqlkiftd
      541 niksdrkped llfqvlldwg vdlslpirke tiqgktvffv nqppydlvac fdtgvnedlv
      601 kelarfeplr vvfrdtgfvs dgvkinveqi fkqmspgtdv ksi
//
LOCUS       WP_011419066             331 aa            linear   BCT 20-JAN-2025
DEFINITION  3-oxoacyl-ACP synthase III family protein [Anaeromyxobacter
            dehalogenans].
ACCESSION   WP_011419066
VERSION     WP_011419066.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter dehalogenans
  ORGANISM  Anaeromyxobacter dehalogenans
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Lai,C.Y. and Cronan,J.E.
  TITLE     Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential
            for bacterial fatty acid synthesis
  JOURNAL   J Biol Chem 278 (51), 51494-51503 (2003)
   PUBMED   14523010
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Rock,C.O. and Jackowski,S.
  TITLE     Forty years of bacterial fatty acid synthesis
  JOURNAL   Biochem Biophys Res Commun 292 (5), 1155-1166 (2002)
   PUBMED   11969206
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Abbadi,A., Brummel,M., Schutt,B.S., Slabaugh,M.B., Schuch,R. and
            Spener,F.
  TITLE     Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein)
            synthase III from Cuphea wrightii embryo, a fatty acid synthase
            type II condensing enzyme
  JOURNAL   Biochem J 345 Pt 1 (Pt 1), 153-160 (2000)
   PUBMED   10600651
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Qiu,X., Janson,C.A., Konstantinidis,A.K., Nwagwu,S., Silverman,C.,
            Smith,W.W., Khandekar,S., Lonsdale,J. and Abdel-Meguid,S.S.
  TITLE     Crystal structure of beta-ketoacyl-acyl carrier protein synthase
            III. A key condensing enzyme in bacterial fatty acid biosynthesis
  JOURNAL   J Biol Chem 274 (51), 36465-36471 (1999)
   PUBMED   10593943
REFERENCE   5  (residues 1 to 331)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Anaeromyxobacter dehalogenans"
                     /db_xref="taxon:161493"
     Protein         1..331
                     /product="3-oxoacyl-ACP synthase III family protein"
                     /EC_number="2.3.1.-"
                     /EC_number="2.3.1.180"
                     /GO_function="GO:0004315 -
                     3-oxoacyl-[acyl-carrier-protein] synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35967
     Region          2..331
                     /region_name="FabH"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase III
                     [Lipid transport and metabolism]; COG0332"
                     /db_xref="CDD:440101"
ORIGIN      
        1 mpraaivalg thvpdrvvtn eeltrhmett dawiqertgi qerrwvregt gnsdlaleat
       61 kkaldkagwk ptdieaivya slspdhmfpg dgcflnaklg ipgvpaidir nqctgflygl
      121 svadawirtg myrrillvgs evhstgldvt trgrdvavif gdgagaalle atddpgrgvl
      181 schlhadgrf ardlftdapg siyhprvqpr mledasifph megqkvfkha vvrmpevlke
      241 afdkngvgpq dlkvlvphqa nlriaqmvqr slglrddqvf nniqrygntt aasiplalae
      301 aveargvvrg dlvglcafga gftwasalvr w
//
LOCUS       WP_011421634             283 aa            linear   BCT 20-JAN-2025
DEFINITION  PHP domain-containing protein [Anaeromyxobacter dehalogenans].
ACCESSION   WP_011421634
VERSION     WP_011421634.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter dehalogenans
  ORGANISM  Anaeromyxobacter dehalogenans
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Phosphoesterase domains associated with DNA polymerases of diverse
            origins
  JOURNAL   Nucleic Acids Res 26 (16), 3746-3752 (1998)
   PUBMED   9685491
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427581
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Anaeromyxobacter dehalogenans"
                     /db_xref="taxon:161493"
     Protein         1..283
                     /product="PHP domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30744
     Region          14..256
                     /region_name="nside_bi_sphtase"
                     /note="3',5'-nucleoside bisphosphate phosphatase;
                     NF041577"
                     /db_xref="CDD:469462"
ORIGIN      
        1 mgepaagqgv ngkidlhshs kasdgqypag evaerasaag vgvwalcdhd tvagmddaaa
       61 aaarlglrlv pgielsafle rreihllghf vdpahprlra fedflalrrr ermqrivekl
      121 galglrlqve diekwsggkt igrphvaral velgavatvk eafdaylgeg kpayvqryrl
      181 eadeavrlvr aaggtttvah pgvsklerwd lerlrqagve glevyhvdhn psvrekylri
      241 aealdlvpta gsdfhgeava pdrhlgdvsm pehelqrlea rrp
//
LOCUS       WP_011421944             387 aa            linear   BCT 20-JAN-2025
DEFINITION  TRAP transporter substrate-binding protein [Anaeromyxobacter
            dehalogenans].
ACCESSION   WP_011421944
VERSION     WP_011421944.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter dehalogenans
  ORGANISM  Anaeromyxobacter dehalogenans
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 387)
  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 387)
  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 387)
  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 387)
  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 10008687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Anaeromyxobacter dehalogenans"
                     /db_xref="taxon:161493"
     Protein         1..387
                     /product="TRAP transporter substrate-binding protein"
                     /GO_component="GO:0005886 - plasma 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=42679
     Region          17..379
                     /region_name="FcbT1"
                     /note="TRAP-type mannitol/chloroaromatic compound
                     transport system, periplasmic component [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG4663"
                     /db_xref="CDD:443700"
ORIGIN      
        1 mkkttsrsqp dtapkasrrs flkkaalgaa gvaagaaapt ihvaqapitl rfqstwpqkd
       61 ifhefaldya kkvnemsggr lkievlaags vvkafdllda vskgtldggh gvvaywygkn
      121 talalwgsgp afgmdpnmvl awhhygggrq lleeiyrsln ldvvslmygp mptqplgwfk
      181 qkpiakpddm kglkfrtvgl sidifnglga avnalpgaei vpamdrglld aaefnnassd
      241 rvlgfpdvsk icmlqsfhqc seqfeilfng krfqalpadl ksiisiaaqa asadmswkai
      301 dryssdyfem rdkqgvkfys trpeilkrql eiwdqvmekr aaenptfkkv lesqrrfaqr
      361 aarwqndtnv dfkmaynhff ggkkkat
//
LOCUS       WP_011422870             282 aa            linear   BCT 20-JAN-2025
DEFINITION  AraC family transcriptional regulator [Anaeromyxobacter
            dehalogenans].
ACCESSION   WP_011422870
VERSION     WP_011422870.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter dehalogenans
  ORGANISM  Anaeromyxobacter dehalogenans
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
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   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   4  (residues 1 to 282)
  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 282)
  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 11454538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Anaeromyxobacter dehalogenans"
                     /db_xref="taxon:161493"
     Protein         1..282
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_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          33..253
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          177..253
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mrlptipihp dapglplwpp llaargpggr stahahhgvh vvlalggdlr vragdagawv
       61 raagivtapd aphaidaags eilivfvdpe seagramrga tagslrtlga aerdaladgv
      121 tpmeimgpgg aawtsrvvea lggervrspr avhprvrrll rvlqamppgg daslealarq
      181 vglspgrlmh vftesigvpl rpylawlrlq raaaaavsgr plgeaahaag fadaahmsrt
      241 frrmlgvtps elrpaahsra ahargrscaa srqarakppv rt
//
LOCUS       WP_011424004             760 aa            linear   BCT 20-JAN-2025
DEFINITION  chemotaxis protein CheA [Rhizobium etli].
ACCESSION   WP_011424004
VERSION     WP_011424004.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium etli
  ORGANISM  Rhizobium etli
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 760)
  AUTHORS   Muok,A.R., Briegel,A. and Crane,B.R.
  TITLE     Regulation of the chemotaxis histidine kinase CheA: A structural
            perspective
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (1), 183030 (2020)
   PUBMED   31374212
REFERENCE   2  (residues 1 to 760)
  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   3  (residues 1 to 760)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..760
                     /organism="Rhizobium etli"
                     /db_xref="taxon:29449"
     Protein         1..760
                     /product="chemotaxis protein CheA"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=80663
     Region          1..749
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mdmneikeif fqeceeqlae lesgllkmnd gdrdpetvna vfravhsikg gagafglddl
       61 vafahvfett ldcvrsnkle ptqdvlkvml ksadvladlt naardggsvd esrsrglvke
      121 lealangelp spsaeppapk aaakaapaap apaakptdds gfqpipfsfd dfgdedgaet
      181 glpayeitfk prhelyskgn datlllrdls rlgemtiycn mdelpgleel dpeaayffwn
      241 itiktdkged airtvfefae wdcdltvkpv eeasagvtgn eelpmvpvpf dlsildetda
      301 aeavsaarse dtaaavaaae tasnvtqmaa aaarvekkes aaaaaaaana aaqnnaagag
      361 qtirvdldrv drlinlvgel vinqamlsqs viendttgts sinmgleelq qltreiqdsv
      421 mairaqpvkp vfqrmsrivr eiadmtgksi rlitegente vdktvidkla eplthmirna
      481 vdhgietpek raaagknteg tvrltakhrs grilieladd gaginrekvr qkaidndlip
      541 adanlsdeei dnliflpgfs tadkisdisg rgvgmdvvkr siqalggrin itskpghgsv
      601 ftmslpltla vldgmvvtva gqtlvvplta ivetlqpeaa aihsfganhr lisirnsfcp
      661 lvdvgrilnf ratqanpveg vallvesegg gqralmvdai qgqrqvviks leanythvpg
      721 iaaatilgdg rvalildvda vvgasrghsl kaemslaavg
//
LOCUS       WP_011424278             396 aa            linear   BCT 20-JAN-2025
DEFINITION  winged helix-turn-helix domain-containing protein [Rhizobium etli].
ACCESSION   WP_011424278
VERSION     WP_011424278.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium etli
  ORGANISM  Rhizobium etli
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 396)
  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 396)
  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 10007089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Rhizobium etli"
                     /db_xref="taxon:29449"
     Protein         1..396
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46013
     Region          1..395
                     /region_name="YcaQ"
                     /note="DNA glycosylase YcaQ, repair of DNA interstrand
                     crosslinks [Replication, recombination and repair];
                     COG3214"
                     /db_xref="CDD:442447"
ORIGIN      
        1 mtnllsnsda rrvflakqgl sappnraltk agllqlihdl gfvqvdsiqt verahhqilf
       61 srnqtyrreh lkallekera lfehwthdas ilpsaffvyw khkfrhqekv lverwrkwrg
      121 egfeaafeet yervrrdgam lardvkadgh vsggwwnwhp nktaleyfwh tgkfaiagrs
      181 nfqkiydlte rvipaefrep evsredfvdw acrsaltrlg fathgeiaaf wnlvspeeak
      241 awvsahrdel tevliepatg dkpraswafa dffsaldshp dapprirvls pfdpmirdrn
      301 rterlfgffy rievfvpepk reygyyvfpl legdrligri dmkadrkkst ldvkrlwlep
      361 gvkpsagrle kleaelerva rfagvekvvl legwrg
//
LOCUS       WP_011424507             244 aa            linear   BCT 20-JAN-2025
DEFINITION  L,D-transpeptidase family protein [Rhizobium etli].
ACCESSION   WP_011424507
VERSION     WP_011424507.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium etli
  ORGANISM  Rhizobium etli
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Magnet,S., Arbeloa,A., Mainardi,J.L., Hugonnet,J.E., Fourgeaud,M.,
            Dubost,L., Marie,A., Delfosse,V., Mayer,C., Rice,L.B. and Arthur,M.
  TITLE     Specificity of L,D-transpeptidases from gram-positive bacteria
            producing different peptidoglycan chemotypes
  JOURNAL   J Biol Chem 282 (18), 13151-13159 (2007)
   PUBMED   17311917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12106649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Rhizobium etli"
                     /db_xref="taxon:29449"
     Protein         1..244
                     /product="L,D-transpeptidase family protein"
                     /EC_number="2.3.2.-"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=26672
     Region          6..30
                     /region_name="TAT_signal"
                     /note="TAT (twin-arginine translocation) pathway signal
                     sequence; pfam10518"
                     /db_xref="CDD:463131"
     Region          106..242
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mssdrhlsrr sflslsalta asaltgcass antvtsgdts iiyrspgrlf qspaassvps
       61 gpelavmygp iedggflipa vpyeqidpry yrqrvldptg qppgtivvdt psrflylvqa
      121 dgmamrygvg igregfawqg sgviqwrqkw prwkppnemv arqpelvkys ienggmepgl
      181 knplgaraly ifsngedtly rlhgnpdwrs igkavssgcv rllnqdiidl ydrvptkapi
      241 vvwq
//
LOCUS       WP_011425077             195 aa            linear   BCT 20-JAN-2025
DEFINITION  MULTISPECIES: ANTAR domain-containing response regulator
            [Rhizobium].
ACCESSION   WP_011425077
VERSION     WP_011425077.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 195)
  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 195)
  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   3  (residues 1 to 195)
  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   4  (residues 1 to 195)
  AUTHORS   Varughese,K.I.
  TITLE     Molecular recognition of bacterial phosphorelay proteins
  JOURNAL   Curr Opin Microbiol 5 (2), 142-148 (2002)
   PUBMED   11934609
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Shu,C.J. and Zhulin,I.B.
  TITLE     ANTAR: an RNA-binding domain in transcription antitermination
            regulatory proteins
  JOURNAL   Trends Biochem Sci 27 (1), 3-5 (2002)
   PUBMED   11796212
REFERENCE   6  (residues 1 to 195)
  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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
    